HEADER    ISOMERASE                               20-JUL-09   3IDD              
TITLE     COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE FROM                     
TITLE    2 THERMOPLASMA ACIDOPHILUM DSM 1728                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT                        
COMPND   3 PHOSPHOGLYCERATE MUTASE;                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: PHOSPHOGLYCEROMUTASE, BPG-INDEPENDENT PGAM, APGAM,          
COMPND   6 COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE;                        
COMPND   7 EC: 5.4.2.1;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;                       
SOURCE   3 ORGANISM_TAXID: 2303;                                                
SOURCE   4 GENE: APGM, TA0413;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG19                                   
KEYWDS    PHOSPHOGLYCERATE MUTASE, STRUCTURAL GENOMICS, PSI-2, PROTEIN          
KEYWDS   2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL                  
KEYWDS   3 GENOMICS, MCSG, GLYCOLYSIS, ISOMERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.JOACHIMIAK,N.E.C.DUKE,N.MARSHALL,K.BUCK,MIDWEST CENTER FOR          
AUTHOR   2 STRUCTURAL GENOMICS (MCSG)                                           
REVDAT   1   06-OCT-09 3IDD    0                                                
JRNL        AUTH   A.JOACHIMIAK,N.E.C.DUKE,N.MARSHALL,K.BUCK                    
JRNL        TITL   COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE FROM            
JRNL        TITL 2 THERMOPLASMA ACIDOPHILUM DSM 1728                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18474                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 995                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1378                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.4690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5585                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 84                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.66000                                              
REMARK   3    B22 (A**2) : -2.08000                                             
REMARK   3    B33 (A**2) : 0.42000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.492         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.379         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.386        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.833                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5689 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7688 ; 1.610 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   715 ; 6.774 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   257 ;34.569 ;23.268       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   977 ;23.704 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;20.855 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   848 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4334 ; 0.007 ; 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):  3597 ; 0.730 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5786 ; 1.430 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2092 ; 2.071 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1902 ; 3.610 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3IDD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054270.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924, 0.97948                   
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL SI(111)             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22991                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 74.330                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09800                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20 M NACL, 0.10 M PHOSPHATE            
REMARK 280  CITRATE, PH 4.2, 10% PEG 3000, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       44.30250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.37200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.30250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.37200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: DIMER PRESENT IN ASYMMETRIC UNIT OF CELL                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     MSE A     2                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     ILE A    54                                                      
REMARK 465     ARG A    55                                                      
REMARK 465     CYS A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     THR A   270                                                      
REMARK 465     VAL A   271                                                      
REMARK 465     GLY A   272                                                      
REMARK 465     ALA A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     VAL A   301                                                      
REMARK 465     ALA A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     GLY A   306                                                      
REMARK 465     THR A   342                                                      
REMARK 465     PRO A   343                                                      
REMARK 465     CYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     PHE A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     HIS A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     ARG A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     ASP A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     PHE A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     SER A   404                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ILE B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     PRO B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     ILE B    54                                                      
REMARK 465     ARG B    55                                                      
REMARK 465     CYS B    56                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     SER B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     THR B   268                                                      
REMARK 465     GLY B   269                                                      
REMARK 465     THR B   270                                                      
REMARK 465     VAL B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     THR B   299                                                      
REMARK 465     ASP B   300                                                      
REMARK 465     VAL B   301                                                      
REMARK 465     ALA B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     ASP B   305                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     SER B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     PRO B   343                                                      
REMARK 465     CYS B   344                                                      
REMARK 465     SER B   345                                                      
REMARK 465     PHE B   346                                                      
REMARK 465     LYS B   347                                                      
REMARK 465     ASP B   348                                                      
REMARK 465     HIS B   349                                                      
REMARK 465     SER B   350                                                      
REMARK 465     GLY B   351                                                      
REMARK 465     ARG B   398                                                      
REMARK 465     SER B   399                                                      
REMARK 465     ASP B   400                                                      
REMARK 465     LYS B   401                                                      
REMARK 465     PHE B   402                                                      
REMARK 465     GLY B   403                                                      
REMARK 465     SER B   404                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    MSE B   158     O    PRO B   176              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  15     -156.84   -108.24                                   
REMARK 500    ARG A  16      108.50     58.84                                   
REMARK 500    ASP A  59       -7.66    -52.37                                   
REMARK 500    LEU A  66        8.17    -68.84                                   
REMARK 500    TYR A  73       31.01     39.24                                   
REMARK 500    ASP A 105       79.95     34.37                                   
REMARK 500    GLU A 143     -137.70     53.71                                   
REMARK 500    HIS A 165       -9.55     78.50                                   
REMARK 500    ASP A 178      136.22    170.72                                   
REMARK 500    PRO A 179      -30.57    -31.26                                   
REMARK 500    GLU A 207        3.72    -67.62                                   
REMARK 500    PRO A 228     -168.20    -77.24                                   
REMARK 500    ILE A 230       97.15     33.01                                   
REMARK 500    SER A 232      160.73    -43.08                                   
REMARK 500    SER A 247      109.71     97.54                                   
REMARK 500    ASN A 274       48.05    -88.93                                   
REMARK 500    SER A 288       -0.02   -140.25                                   
REMARK 500    LEU A 395       -9.29   -154.73                                   
REMARK 500    ASP B  15      175.83     64.64                                   
REMARK 500    GLN B  22       50.88     71.60                                   
REMARK 500    PHE B  31       99.02    -67.74                                   
REMARK 500    LYS B  71      -24.53     96.90                                   
REMARK 500    LEU B  85       54.29   -103.75                                   
REMARK 500    GLU B 143     -121.89     49.16                                   
REMARK 500    ASP B 154       10.17     58.51                                   
REMARK 500    HIS B 165       -0.45     71.82                                   
REMARK 500    THR B 177      -60.47     90.26                                   
REMARK 500    ILE B 230       97.36     25.99                                   
REMARK 500    SER B 232      156.58    -36.39                                   
REMARK 500    SER B 247      119.33    136.44                                   
REMARK 500    ASP B 263      -64.19    -93.84                                   
REMARK 500    ILE B 296      -88.11    -77.61                                   
REMARK 500    LYS B 297      -98.25   -139.73                                   
REMARK 500    SER B 385      -42.90    -22.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A   73     TYR A   74                  148.88                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     THR A  60        24.2      L          L   OUTSIDE RANGE          
REMARK 500     TYR A  73        23.3      L          L   OUTSIDE RANGE          
REMARK 500     GLU A 280        24.1      L          L   OUTSIDE RANGE          
REMARK 500     HIS A 340        24.0      L          L   OUTSIDE RANGE          
REMARK 500     ILE B 296        24.3      L          L   OUTSIDE RANGE          
REMARK 500     LYS B 297        24.7      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC64091   RELATED DB: TARGETDB                          
DBREF  3IDD A    1   404  UNP    Q9HL27   APGM_THEAC       1    404             
DBREF  3IDD B    1   404  UNP    Q9HL27   APGM_THEAC       1    404             
SEQADV 3IDD SER A   -2  UNP  Q9HL27              EXPRESSION TAG                 
SEQADV 3IDD ASN A   -1  UNP  Q9HL27              EXPRESSION TAG                 
SEQADV 3IDD ALA A    0  UNP  Q9HL27              EXPRESSION TAG                 
SEQADV 3IDD SER B   -2  UNP  Q9HL27              EXPRESSION TAG                 
SEQADV 3IDD ASN B   -1  UNP  Q9HL27              EXPRESSION TAG                 
SEQADV 3IDD ALA B    0  UNP  Q9HL27              EXPRESSION TAG                 
SEQRES   1 A  407  SER ASN ALA MSE MSE LYS SER ILE ILE LEU ILE VAL LEU          
SEQRES   2 A  407  ASP GLY LEU GLY ASP ARG PRO GLY SER ASP LEU GLN ASN          
SEQRES   3 A  407  ARG THR PRO LEU GLN ALA ALA PHE ARG PRO ASN LEU ASN          
SEQRES   4 A  407  TRP LEU ALA SER HIS GLY ILE ASN GLY ILE MSE HIS PRO          
SEQRES   5 A  407  ILE SER PRO GLY ILE ARG CYS GLY SER ASP THR SER HIS          
SEQRES   6 A  407  MSE SER LEU LEU GLY TYR ASP PRO LYS VAL TYR TYR PRO          
SEQRES   7 A  407  GLY ARG GLY PRO PHE GLU ALA LEU GLY LEU GLY MSE ASP          
SEQRES   8 A  407  ILE ARG PRO GLY ASP LEU ALA PHE ARG ALA ASN PHE ALA          
SEQRES   9 A  407  THR ASN ARG ASP GLY VAL ILE VAL ASP ARG ARG ALA GLY          
SEQRES  10 A  407  ARG GLU ASN LYS GLY ASN GLU GLU LEU ALA ASP ALA ILE          
SEQRES  11 A  407  SER LEU ASP MSE GLY GLU TYR SER PHE ARG VAL LYS SER          
SEQRES  12 A  407  GLY VAL GLU HIS ARG ALA ALA LEU VAL VAL SER GLY PRO          
SEQRES  13 A  407  ASP LEU SER ASP MSE ILE GLY ASP SER ASP PRO HIS ARG          
SEQRES  14 A  407  GLU GLY LEU PRO PRO GLU LYS ILE ARG PRO THR ASP PRO          
SEQRES  15 A  407  SER GLY ASP ARG THR ALA GLU VAL MSE ASN ALA TYR LEU          
SEQRES  16 A  407  GLU GLU ALA ARG ARG ILE LEU SER ASP HIS ARG VAL ASN          
SEQRES  17 A  407  LYS GLU ARG VAL LYS ASN GLY ARG LEU PRO GLY ASN GLU          
SEQRES  18 A  407  LEU LEU VAL ARG SER ALA GLY LYS VAL PRO ALA ILE PRO          
SEQRES  19 A  407  SER PHE THR GLU LYS ASN ARG MSE LYS GLY ALA CYS VAL          
SEQRES  20 A  407  VAL GLY SER PRO TRP LEU LYS GLY LEU CYS ARG LEU LEU          
SEQRES  21 A  407  ARG MSE ASP VAL PHE ASP VAL PRO GLY ALA THR GLY THR          
SEQRES  22 A  407  VAL GLY SER ASN TYR ARG GLY LYS ILE GLU LYS ALA VAL          
SEQRES  23 A  407  ASP LEU THR SER SER HIS ASP PHE VAL LEU VAL ASN ILE          
SEQRES  24 A  407  LYS ALA THR ASP VAL ALA GLY HIS ASP GLY ASN TYR PRO          
SEQRES  25 A  407  LEU LYS ARG ASP VAL ILE GLU ASP ILE ASP ARG ALA MSE          
SEQRES  26 A  407  GLU PRO LEU LYS SER ILE GLY ASP HIS ALA VAL ILE CYS          
SEQRES  27 A  407  VAL THR GLY ASP HIS SER THR PRO CYS SER PHE LYS ASP          
SEQRES  28 A  407  HIS SER GLY ASP PRO VAL PRO ILE VAL PHE TYR THR ASP          
SEQRES  29 A  407  GLY VAL MSE ASN ASP GLY VAL HIS LEU PHE ASP GLU LEU          
SEQRES  30 A  407  SER SER ALA SER GLY SER LEU ARG ILE THR SER TYR ASN          
SEQRES  31 A  407  VAL MSE ASP ILE LEU MSE GLN LEU ALA GLY ARG SER ASP          
SEQRES  32 A  407  LYS PHE GLY SER                                              
SEQRES   1 B  407  SER ASN ALA MSE MSE LYS SER ILE ILE LEU ILE VAL LEU          
SEQRES   2 B  407  ASP GLY LEU GLY ASP ARG PRO GLY SER ASP LEU GLN ASN          
SEQRES   3 B  407  ARG THR PRO LEU GLN ALA ALA PHE ARG PRO ASN LEU ASN          
SEQRES   4 B  407  TRP LEU ALA SER HIS GLY ILE ASN GLY ILE MSE HIS PRO          
SEQRES   5 B  407  ILE SER PRO GLY ILE ARG CYS GLY SER ASP THR SER HIS          
SEQRES   6 B  407  MSE SER LEU LEU GLY TYR ASP PRO LYS VAL TYR TYR PRO          
SEQRES   7 B  407  GLY ARG GLY PRO PHE GLU ALA LEU GLY LEU GLY MSE ASP          
SEQRES   8 B  407  ILE ARG PRO GLY ASP LEU ALA PHE ARG ALA ASN PHE ALA          
SEQRES   9 B  407  THR ASN ARG ASP GLY VAL ILE VAL ASP ARG ARG ALA GLY          
SEQRES  10 B  407  ARG GLU ASN LYS GLY ASN GLU GLU LEU ALA ASP ALA ILE          
SEQRES  11 B  407  SER LEU ASP MSE GLY GLU TYR SER PHE ARG VAL LYS SER          
SEQRES  12 B  407  GLY VAL GLU HIS ARG ALA ALA LEU VAL VAL SER GLY PRO          
SEQRES  13 B  407  ASP LEU SER ASP MSE ILE GLY ASP SER ASP PRO HIS ARG          
SEQRES  14 B  407  GLU GLY LEU PRO PRO GLU LYS ILE ARG PRO THR ASP PRO          
SEQRES  15 B  407  SER GLY ASP ARG THR ALA GLU VAL MSE ASN ALA TYR LEU          
SEQRES  16 B  407  GLU GLU ALA ARG ARG ILE LEU SER ASP HIS ARG VAL ASN          
SEQRES  17 B  407  LYS GLU ARG VAL LYS ASN GLY ARG LEU PRO GLY ASN GLU          
SEQRES  18 B  407  LEU LEU VAL ARG SER ALA GLY LYS VAL PRO ALA ILE PRO          
SEQRES  19 B  407  SER PHE THR GLU LYS ASN ARG MSE LYS GLY ALA CYS VAL          
SEQRES  20 B  407  VAL GLY SER PRO TRP LEU LYS GLY LEU CYS ARG LEU LEU          
SEQRES  21 B  407  ARG MSE ASP VAL PHE ASP VAL PRO GLY ALA THR GLY THR          
SEQRES  22 B  407  VAL GLY SER ASN TYR ARG GLY LYS ILE GLU LYS ALA VAL          
SEQRES  23 B  407  ASP LEU THR SER SER HIS ASP PHE VAL LEU VAL ASN ILE          
SEQRES  24 B  407  LYS ALA THR ASP VAL ALA GLY HIS ASP GLY ASN TYR PRO          
SEQRES  25 B  407  LEU LYS ARG ASP VAL ILE GLU ASP ILE ASP ARG ALA MSE          
SEQRES  26 B  407  GLU PRO LEU LYS SER ILE GLY ASP HIS ALA VAL ILE CYS          
SEQRES  27 B  407  VAL THR GLY ASP HIS SER THR PRO CYS SER PHE LYS ASP          
SEQRES  28 B  407  HIS SER GLY ASP PRO VAL PRO ILE VAL PHE TYR THR ASP          
SEQRES  29 B  407  GLY VAL MSE ASN ASP GLY VAL HIS LEU PHE ASP GLU LEU          
SEQRES  30 B  407  SER SER ALA SER GLY SER LEU ARG ILE THR SER TYR ASN          
SEQRES  31 B  407  VAL MSE ASP ILE LEU MSE GLN LEU ALA GLY ARG SER ASP          
SEQRES  32 B  407  LYS PHE GLY SER                                              
MODRES 3IDD MSE A   47  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A   63  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A   87  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  131  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  188  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  239  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  259  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  322  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  364  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  389  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE A  393  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B    2  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B   47  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B   63  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B   87  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  131  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  158  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  188  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  239  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  259  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  322  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  364  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  389  MET  SELENOMETHIONINE                                   
MODRES 3IDD MSE B  393  MET  SELENOMETHIONINE                                   
HET    MSE  A  47       8                                                       
HET    MSE  A  63       8                                                       
HET    MSE  A  87       8                                                       
HET    MSE  A 131       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 188       8                                                       
HET    MSE  A 239       8                                                       
HET    MSE  A 259       8                                                       
HET    MSE  A 322       8                                                       
HET    MSE  A 364       8                                                       
HET    MSE  A 389       8                                                       
HET    MSE  A 393       8                                                       
HET    MSE  B   2       8                                                       
HET    MSE  B  47       8                                                       
HET    MSE  B  63       8                                                       
HET    MSE  B  87       8                                                       
HET    MSE  B 131       8                                                       
HET    MSE  B 158       8                                                       
HET    MSE  B 188       8                                                       
HET    MSE  B 239       8                                                       
HET    MSE  B 259       8                                                       
HET    MSE  B 322       8                                                       
HET    MSE  B 364       8                                                       
HET    MSE  B 389       8                                                       
HET    MSE  B 393       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    25(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *84(H2 O)                                                     
HELIX    1   1 GLY A   18  GLN A   22  5                                   5    
HELIX    2   2 THR A   25  ALA A   30  1                                   6    
HELIX    3   3 ARG A   32  HIS A   41  1                                  10    
HELIX    4   4 SER A   61  LEU A   66  1                                   6    
HELIX    5   5 GLY A   76  LEU A   85  1                                  10    
HELIX    6   6 ARG A  112  GLU A  116  5                                   5    
HELIX    7   7 GLY A  119  ILE A  127  1                                   9    
HELIX    8   8 ASP A  178  SER A  180  5                                   3    
HELIX    9   9 GLY A  181  HIS A  202  1                                  22    
HELIX   10  10 HIS A  202  LYS A  210  1                                   9    
HELIX   11  11 SER A  232  ARG A  238  1                                   7    
HELIX   12  12 SER A  247  LEU A  257  1                                  11    
HELIX   13  13 ASN A  274  LEU A  285  1                                  12    
HELIX   14  14 THR A  286  SER A  288  5                                   3    
HELIX   15  15 ASN A  307  MSE A  322  1                                  16    
HELIX   16  16 GLU A  323  ILE A  328  5                                   6    
HELIX   17  17 LEU A  374  GLY A  379  5                                   6    
HELIX   18  18 ASN A  387  GLN A  394  1                                   8    
HELIX   19  19 THR B   25  ALA B   30  1                                   6    
HELIX   20  20 ARG B   32  HIS B   41  1                                  10    
HELIX   21  21 THR B   60  LEU B   66  1                                   7    
HELIX   22  22 GLY B   76  LEU B   85  1                                  10    
HELIX   23  23 ARG B  112  GLU B  116  5                                   5    
HELIX   24  24 GLY B  119  ILE B  127  1                                   9    
HELIX   25  25 ASP B  178  SER B  180  5                                   3    
HELIX   26  26 GLY B  181  HIS B  202  1                                  22    
HELIX   27  27 HIS B  202  ASN B  211  1                                  10    
HELIX   28  28 SER B  232  ARG B  238  1                                   7    
HELIX   29  29 SER B  247  LEU B  257  1                                  11    
HELIX   30  30 ASN B  274  LEU B  285  1                                  12    
HELIX   31  31 ASN B  307  ALA B  321  1                                  15    
HELIX   32  32 MSE B  322  ILE B  328  5                                   7    
HELIX   33  33 LEU B  374  GLY B  379  5                                   6    
HELIX   34  34 TYR B  386  GLY B  397  1                                  12    
SHEET    1   A 8 ASP A 260  PHE A 262  0                                        
SHEET    2   A 8 GLY A 241  VAL A 244  1  N  CYS A 243   O  PHE A 262           
SHEET    3   A 8 PHE A 291  ILE A 296  1  O  LEU A 293   N  VAL A 244           
SHEET    4   A 8 SER A   4  ASP A  11  1  N  LEU A   7   O  VAL A 294           
SHEET    5   A 8 ALA A 332  ASP A 339  1  O  THR A 337   N  LEU A  10           
SHEET    6   A 8 VAL A 354  TYR A 359 -1  O  TYR A 359   N  ILE A 334           
SHEET    7   A 8 ILE A  43  HIS A  48 -1  N  ILE A  43   O  PHE A 358           
SHEET    8   A 8 LEU A 381  THR A 384  1  O  ILE A 383   N  HIS A  48           
SHEET    1   B 5 VAL A 107  ASP A 110  0                                        
SHEET    2   B 5 LEU A  94  ARG A 104 -1  N  THR A 102   O  ASP A 110           
SHEET    3   B 5 ARG A 145  SER A 151 -1  O  VAL A 150   N  LEU A  94           
SHEET    4   B 5 SER A 135  SER A 140 -1  N  ARG A 137   O  VAL A 149           
SHEET    5   B 5 LEU A 129  ASP A 130 -1  N  LEU A 129   O  PHE A 136           
SHEET    1   C 3 VAL A 107  ASP A 110  0                                        
SHEET    2   C 3 LEU A  94  ARG A 104 -1  N  THR A 102   O  ASP A 110           
SHEET    3   C 3 GLU A 218  LYS A 226 -1  O  LEU A 220   N  ASN A  99           
SHEET    1   D 8 ASP B 260  PHE B 262  0                                        
SHEET    2   D 8 GLY B 241  VAL B 244  1  N  CYS B 243   O  ASP B 260           
SHEET    3   D 8 PHE B 291  ASN B 295  1  O  LEU B 293   N  VAL B 244           
SHEET    4   D 8 SER B   4  LEU B  10  1  N  ILE B   5   O  VAL B 292           
SHEET    5   D 8 ALA B 332  GLY B 338  1  O  THR B 337   N  LEU B  10           
SHEET    6   D 8 VAL B 354  TYR B 359 -1  O  TYR B 359   N  ILE B 334           
SHEET    7   D 8 ILE B  43  HIS B  48 -1  N  MSE B  47   O  VAL B 354           
SHEET    8   D 8 LEU B 381  THR B 384  1  O  LEU B 381   N  ASN B  44           
SHEET    1   E 5 VAL B 107  ASP B 110  0                                        
SHEET    2   E 5 LEU B  94  ARG B 104 -1  N  THR B 102   O  ASP B 110           
SHEET    3   E 5 ARG B 145  SER B 151 -1  O  LEU B 148   N  PHE B  96           
SHEET    4   E 5 TYR B 134  SER B 140 -1  N  LYS B 139   O  ALA B 147           
SHEET    5   E 5 LEU B 129  MSE B 131 -1  N  LEU B 129   O  PHE B 136           
SHEET    1   F 3 VAL B 107  ASP B 110  0                                        
SHEET    2   F 3 LEU B  94  ARG B 104 -1  N  THR B 102   O  ASP B 110           
SHEET    3   F 3 GLU B 218  LYS B 226 -1  O  GLY B 225   N  ALA B  95           
SSBOND   1 CYS A  243    CYS A  254                          1555   1555  2.06  
SSBOND   2 CYS B  243    CYS B  254                          1555   1555  2.05  
LINK         C   ILE A  46                 N   MSE A  47     1555   1555  1.33  
LINK         C   MSE A  47                 N   HIS A  48     1555   1555  1.33  
LINK         C   HIS A  62                 N   MSE A  63     1555   1555  1.32  
LINK         C   MSE A  63                 N   SER A  64     1555   1555  1.33  
LINK         C   GLY A  86                 N   MSE A  87     1555   1555  1.33  
LINK         C   MSE A  87                 N   ASP A  88     1555   1555  1.33  
LINK         C   ASP A 130                 N   MSE A 131     1555   1555  1.33  
LINK         C   MSE A 131                 N   GLY A 132     1555   1555  1.34  
LINK         C   ASP A 157                 N   MSE A 158     1555   1555  1.33  
LINK         C   MSE A 158                 N   ILE A 159     1555   1555  1.34  
LINK         C   VAL A 187                 N   MSE A 188     1555   1555  1.34  
LINK         C   MSE A 188                 N   ASN A 189     1555   1555  1.33  
LINK         C   ARG A 238                 N   MSE A 239     1555   1555  1.33  
LINK         C   MSE A 239                 N   LYS A 240     1555   1555  1.32  
LINK         C   ARG A 258                 N   MSE A 259     1555   1555  1.33  
LINK         C   MSE A 259                 N   ASP A 260     1555   1555  1.32  
LINK         C   ALA A 321                 N   MSE A 322     1555   1555  1.32  
LINK         C   MSE A 322                 N   GLU A 323     1555   1555  1.33  
LINK         C   VAL A 363                 N   MSE A 364     1555   1555  1.35  
LINK         C   MSE A 364                 N   ASN A 365     1555   1555  1.34  
LINK         C   VAL A 388                 N   MSE A 389     1555   1555  1.34  
LINK         C   MSE A 389                 N   ASP A 390     1555   1555  1.33  
LINK         C   LEU A 392                 N   MSE A 393     1555   1555  1.33  
LINK         C   MSE A 393                 N   GLN A 394     1555   1555  1.33  
LINK         C   MSE B   2                 N   LYS B   3     1555   1555  1.33  
LINK         C   ILE B  46                 N   MSE B  47     1555   1555  1.32  
LINK         C   MSE B  47                 N   HIS B  48     1555   1555  1.34  
LINK         C   HIS B  62                 N   MSE B  63     1555   1555  1.33  
LINK         C   MSE B  63                 N   SER B  64     1555   1555  1.34  
LINK         C   GLY B  86                 N   MSE B  87     1555   1555  1.33  
LINK         C   MSE B  87                 N   ASP B  88     1555   1555  1.33  
LINK         C   ASP B 130                 N   MSE B 131     1555   1555  1.33  
LINK         C   MSE B 131                 N   GLY B 132     1555   1555  1.32  
LINK         C   ASP B 157                 N   MSE B 158     1555   1555  1.33  
LINK         C   MSE B 158                 N   ILE B 159     1555   1555  1.33  
LINK         C   VAL B 187                 N   MSE B 188     1555   1555  1.33  
LINK         C   MSE B 188                 N   ASN B 189     1555   1555  1.33  
LINK         C   ARG B 238                 N   MSE B 239     1555   1555  1.33  
LINK         C   MSE B 239                 N   LYS B 240     1555   1555  1.33  
LINK         C   ARG B 258                 N   MSE B 259     1555   1555  1.32  
LINK         C   MSE B 259                 N   ASP B 260     1555   1555  1.33  
LINK         C   ALA B 321                 N   MSE B 322     1555   1555  1.32  
LINK         C   MSE B 322                 N   GLU B 323     1555   1555  1.33  
LINK         C   VAL B 363                 N   MSE B 364     1555   1555  1.32  
LINK         C   MSE B 364                 N   ASN B 365     1555   1555  1.33  
LINK         C   VAL B 388                 N   MSE B 389     1555   1555  1.33  
LINK         C   MSE B 389                 N   ASP B 390     1555   1555  1.34  
LINK         C   LEU B 392                 N   MSE B 393     1555   1555  1.33  
LINK         C   MSE B 393                 N   GLN B 394     1555   1555  1.33  
CRYST1   88.605  136.744   63.289  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011286  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015801        0.00000                         
ATOM      1  N   LYS A   3       6.284  49.933 -20.564  1.00 26.79           N  
ATOM      2  CA  LYS A   3       7.034  51.220 -20.373  1.00 26.83           C  
ATOM      3  C   LYS A   3       8.409  50.979 -19.768  1.00 26.41           C  
ATOM      4  O   LYS A   3       8.520  50.333 -18.728  1.00 26.60           O  
ATOM      5  CB  LYS A   3       6.282  52.153 -19.437  1.00 27.08           C  
ATOM      6  CG  LYS A   3       5.454  53.255 -20.068  1.00 28.30           C  
ATOM      7  CD  LYS A   3       4.708  53.989 -18.918  1.00 31.02           C  
ATOM      8  CE  LYS A   3       3.484  54.840 -19.341  1.00 30.97           C  
ATOM      9  NZ  LYS A   3       2.655  55.254 -18.150  1.00 28.41           N  
ATOM     10  N   SER A   4       9.446  51.528 -20.404  1.00 25.69           N  
ATOM     11  CA  SER A   4      10.824  51.402 -19.930  1.00 25.16           C  
ATOM     12  C   SER A   4      11.084  52.306 -18.739  1.00 24.41           C  
ATOM     13  O   SER A   4      10.236  53.108 -18.368  1.00 24.54           O  
ATOM     14  CB  SER A   4      11.811  51.757 -21.037  1.00 25.51           C  
ATOM     15  OG  SER A   4      11.756  50.834 -22.113  1.00 27.55           O  
ATOM     16  N   ILE A   5      12.270  52.180 -18.147  1.00 23.38           N  
ATOM     17  CA  ILE A   5      12.622  52.934 -16.969  1.00 22.21           C  
ATOM     18  C   ILE A   5      13.985  53.511 -17.183  1.00 21.69           C  
ATOM     19  O   ILE A   5      14.888  52.800 -17.559  1.00 22.37           O  
ATOM     20  CB  ILE A   5      12.662  52.033 -15.729  1.00 22.35           C  
ATOM     21  CG1 ILE A   5      11.259  51.518 -15.386  1.00 22.17           C  
ATOM     22  CG2 ILE A   5      13.229  52.783 -14.529  1.00 22.17           C  
ATOM     23  CD1 ILE A   5      11.252  50.162 -14.674  1.00 20.61           C  
ATOM     24  N   ILE A   6      14.133  54.803 -16.953  1.00 20.89           N  
ATOM     25  CA  ILE A   6      15.445  55.403 -16.882  1.00 20.78           C  
ATOM     26  C   ILE A   6      15.648  55.920 -15.468  1.00 20.45           C  
ATOM     27  O   ILE A   6      14.905  56.776 -15.008  1.00 21.27           O  
ATOM     28  CB  ILE A   6      15.567  56.568 -17.855  1.00 20.95           C  
ATOM     29  CG1 ILE A   6      15.192  56.125 -19.261  1.00 22.38           C  
ATOM     30  CG2 ILE A   6      16.983  57.107 -17.876  1.00 21.52           C  
ATOM     31  CD1 ILE A   6      15.545  57.147 -20.308  1.00 24.78           C  
ATOM     32  N   LEU A   7      16.639  55.395 -14.771  1.00 19.99           N  
ATOM     33  CA  LEU A   7      16.924  55.818 -13.408  1.00 19.85           C  
ATOM     34  C   LEU A   7      18.222  56.627 -13.401  1.00 19.89           C  
ATOM     35  O   LEU A   7      19.302  56.107 -13.732  1.00 19.77           O  
ATOM     36  CB  LEU A   7      17.007  54.599 -12.477  1.00 19.98           C  
ATOM     37  CG  LEU A   7      17.560  54.781 -11.065  1.00 20.62           C  
ATOM     38  CD1 LEU A   7      16.621  55.589 -10.218  1.00 20.93           C  
ATOM     39  CD2 LEU A   7      17.806  53.444 -10.418  1.00 20.90           C  
ATOM     40  N   ILE A   8      18.103  57.905 -13.047  1.00 19.59           N  
ATOM     41  CA  ILE A   8      19.221  58.829 -13.116  1.00 19.48           C  
ATOM     42  C   ILE A   8      19.700  59.119 -11.723  1.00 20.07           C  
ATOM     43  O   ILE A   8      18.954  59.655 -10.924  1.00 19.91           O  
ATOM     44  CB  ILE A   8      18.806  60.140 -13.770  1.00 18.96           C  
ATOM     45  CG1 ILE A   8      17.823  59.853 -14.907  1.00 19.36           C  
ATOM     46  CG2 ILE A   8      20.027  60.926 -14.211  1.00 18.04           C  
ATOM     47  CD1 ILE A   8      18.067  60.591 -16.186  1.00 17.74           C  
ATOM     48  N   VAL A   9      20.942  58.753 -11.432  1.00 21.26           N  
ATOM     49  CA  VAL A   9      21.521  58.995 -10.123  1.00 22.77           C  
ATOM     50  C   VAL A   9      22.504  60.145 -10.227  1.00 24.51           C  
ATOM     51  O   VAL A   9      23.525  60.036 -10.892  1.00 24.59           O  
ATOM     52  CB  VAL A   9      22.244  57.754  -9.587  1.00 22.61           C  
ATOM     53  CG1 VAL A   9      22.765  58.004  -8.202  1.00 22.07           C  
ATOM     54  CG2 VAL A   9      21.325  56.581  -9.571  1.00 22.38           C  
ATOM     55  N   LEU A  10      22.170  61.260  -9.594  1.00 26.91           N  
ATOM     56  CA  LEU A  10      23.056  62.404  -9.535  1.00 29.41           C  
ATOM     57  C   LEU A  10      24.059  62.101  -8.449  1.00 31.73           C  
ATOM     58  O   LEU A  10      23.749  62.198  -7.278  1.00 31.69           O  
ATOM     59  CB  LEU A  10      22.264  63.679  -9.223  1.00 29.06           C  
ATOM     60  CG  LEU A  10      21.795  64.553 -10.400  1.00 28.58           C  
ATOM     61  CD1 LEU A  10      21.936  63.844 -11.736  1.00 28.34           C  
ATOM     62  CD2 LEU A  10      20.385  65.114 -10.220  1.00 25.83           C  
ATOM     63  N   ASP A  11      25.260  61.705  -8.844  1.00 35.25           N  
ATOM     64  CA  ASP A  11      26.244  61.189  -7.892  1.00 38.88           C  
ATOM     65  C   ASP A  11      27.070  62.317  -7.294  1.00 40.82           C  
ATOM     66  O   ASP A  11      27.693  63.104  -8.024  1.00 41.12           O  
ATOM     67  CB  ASP A  11      27.153  60.140  -8.558  1.00 39.36           C  
ATOM     68  CG  ASP A  11      27.749  59.131  -7.558  1.00 41.68           C  
ATOM     69  OD1 ASP A  11      28.199  58.043  -8.022  1.00 43.04           O  
ATOM     70  OD2 ASP A  11      27.777  59.419  -6.325  1.00 44.64           O  
ATOM     71  N   GLY A  12      27.079  62.374  -5.963  1.00 43.06           N  
ATOM     72  CA  GLY A  12      27.730  63.460  -5.238  1.00 45.96           C  
ATOM     73  C   GLY A  12      26.855  64.685  -5.365  1.00 48.09           C  
ATOM     74  O   GLY A  12      27.200  65.637  -6.064  1.00 48.49           O  
ATOM     75  N   LEU A  13      25.700  64.652  -4.709  1.00 50.14           N  
ATOM     76  CA  LEU A  13      24.759  65.759  -4.806  1.00 52.10           C  
ATOM     77  C   LEU A  13      24.958  66.799  -3.706  1.00 53.20           C  
ATOM     78  O   LEU A  13      24.371  66.686  -2.620  1.00 53.20           O  
ATOM     79  CB  LEU A  13      23.316  65.255  -4.820  1.00 52.36           C  
ATOM     80  CG  LEU A  13      22.302  66.276  -5.349  1.00 53.29           C  
ATOM     81  CD1 LEU A  13      22.895  67.106  -6.507  1.00 53.48           C  
ATOM     82  CD2 LEU A  13      21.021  65.558  -5.785  1.00 53.58           C  
ATOM     83  N   GLY A  14      25.784  67.806  -4.016  1.00 54.53           N  
ATOM     84  CA  GLY A  14      26.063  68.940  -3.127  1.00 55.70           C  
ATOM     85  C   GLY A  14      24.815  69.422  -2.402  1.00 56.63           C  
ATOM     86  O   GLY A  14      23.937  70.066  -3.014  1.00 57.15           O  
ATOM     87  N   ASP A  15      24.711  69.038  -1.124  1.00 56.67           N  
ATOM     88  CA  ASP A  15      23.759  69.619  -0.177  1.00 56.64           C  
ATOM     89  C   ASP A  15      24.507  70.496   0.848  1.00 56.22           C  
ATOM     90  O   ASP A  15      25.622  70.980   0.568  1.00 56.38           O  
ATOM     91  CB  ASP A  15      22.850  68.551   0.476  1.00 57.13           C  
ATOM     92  CG  ASP A  15      23.625  67.359   1.068  1.00 58.79           C  
ATOM     93  OD1 ASP A  15      22.962  66.349   1.409  1.00 59.87           O  
ATOM     94  OD2 ASP A  15      24.875  67.412   1.195  1.00 59.88           O  
ATOM     95  N   ARG A  16      23.900  70.702   2.016  1.00 55.43           N  
ATOM     96  CA  ARG A  16      24.398  71.652   3.020  1.00 54.94           C  
ATOM     97  C   ARG A  16      24.480  73.087   2.446  1.00 53.69           C  
ATOM     98  O   ARG A  16      25.331  73.373   1.594  1.00 53.56           O  
ATOM     99  CB  ARG A  16      25.731  71.159   3.649  1.00 55.38           C  
ATOM    100  CG  ARG A  16      25.759  71.102   5.216  1.00 57.67           C  
ATOM    101  CD  ARG A  16      24.537  70.315   5.874  1.00 61.03           C  
ATOM    102  NE  ARG A  16      23.293  71.114   5.950  1.00 62.43           N  
ATOM    103  CZ  ARG A  16      22.662  71.516   7.066  1.00 63.79           C  
ATOM    104  NH1 ARG A  16      23.109  71.178   8.281  1.00 63.89           N  
ATOM    105  NH2 ARG A  16      21.553  72.261   6.961  1.00 63.66           N  
ATOM    106  N   PRO A  17      23.572  73.987   2.896  1.00 52.60           N  
ATOM    107  CA  PRO A  17      23.488  75.358   2.404  1.00 51.97           C  
ATOM    108  C   PRO A  17      24.801  76.095   2.567  1.00 51.48           C  
ATOM    109  O   PRO A  17      25.626  75.699   3.391  1.00 51.77           O  
ATOM    110  CB  PRO A  17      22.444  75.999   3.323  1.00 51.88           C  
ATOM    111  CG  PRO A  17      21.649  74.911   3.810  1.00 52.02           C  
ATOM    112  CD  PRO A  17      22.575  73.751   3.952  1.00 52.56           C  
ATOM    113  N   GLY A  18      24.987  77.157   1.788  1.00 50.94           N  
ATOM    114  CA  GLY A  18      26.210  77.965   1.826  1.00 50.01           C  
ATOM    115  C   GLY A  18      25.845  79.421   1.698  1.00 49.25           C  
ATOM    116  O   GLY A  18      24.987  79.767   0.896  1.00 48.86           O  
ATOM    117  N   SER A  19      26.480  80.272   2.503  1.00 48.78           N  
ATOM    118  CA  SER A  19      26.186  81.711   2.481  1.00 48.24           C  
ATOM    119  C   SER A  19      26.439  82.291   1.093  1.00 47.56           C  
ATOM    120  O   SER A  19      25.738  83.203   0.658  1.00 47.36           O  
ATOM    121  CB  SER A  19      27.024  82.457   3.520  1.00 48.41           C  
ATOM    122  OG  SER A  19      28.397  82.143   3.352  1.00 49.38           O  
ATOM    123  N   ASP A  20      27.439  81.735   0.410  1.00 46.81           N  
ATOM    124  CA  ASP A  20      27.836  82.148  -0.935  1.00 46.05           C  
ATOM    125  C   ASP A  20      26.684  82.125  -1.932  1.00 45.17           C  
ATOM    126  O   ASP A  20      26.604  82.971  -2.836  1.00 45.03           O  
ATOM    127  CB  ASP A  20      28.978  81.256  -1.447  1.00 46.37           C  
ATOM    128  CG  ASP A  20      30.341  81.610  -0.837  1.00 46.86           C  
ATOM    129  OD1 ASP A  20      31.324  80.955  -1.238  1.00 47.33           O  
ATOM    130  OD2 ASP A  20      30.438  82.526   0.023  1.00 47.29           O  
ATOM    131  N   LEU A  21      25.799  81.150  -1.758  1.00 44.30           N  
ATOM    132  CA  LEU A  21      24.596  81.030  -2.585  1.00 43.37           C  
ATOM    133  C   LEU A  21      23.372  81.629  -1.887  1.00 42.71           C  
ATOM    134  O   LEU A  21      22.240  81.267  -2.188  1.00 42.60           O  
ATOM    135  CB  LEU A  21      24.358  79.566  -2.991  1.00 43.09           C  
ATOM    136  CG  LEU A  21      25.512  78.838  -3.704  1.00 43.64           C  
ATOM    137  CD1 LEU A  21      25.127  77.414  -4.044  1.00 43.30           C  
ATOM    138  CD2 LEU A  21      26.003  79.569  -4.970  1.00 44.02           C  
ATOM    139  N   GLN A  22      23.620  82.566  -0.973  1.00 42.21           N  
ATOM    140  CA  GLN A  22      22.575  83.199  -0.168  1.00 41.82           C  
ATOM    141  C   GLN A  22      21.763  82.173   0.619  1.00 41.14           C  
ATOM    142  O   GLN A  22      20.533  82.147   0.529  1.00 41.19           O  
ATOM    143  CB  GLN A  22      21.674  84.085  -1.031  1.00 41.96           C  
ATOM    144  CG  GLN A  22      22.401  85.287  -1.586  1.00 42.86           C  
ATOM    145  CD  GLN A  22      21.917  85.683  -2.959  1.00 44.18           C  
ATOM    146  OE1 GLN A  22      21.272  86.725  -3.131  1.00 44.72           O  
ATOM    147  NE2 GLN A  22      22.234  84.858  -3.955  1.00 43.93           N  
ATOM    148  N   ASN A  23      22.482  81.345   1.385  1.00 40.16           N  
ATOM    149  CA  ASN A  23      21.910  80.312   2.248  1.00 39.49           C  
ATOM    150  C   ASN A  23      20.981  79.333   1.528  1.00 38.25           C  
ATOM    151  O   ASN A  23      19.850  79.073   1.956  1.00 38.49           O  
ATOM    152  CB  ASN A  23      21.243  80.936   3.476  1.00 40.21           C  
ATOM    153  CG  ASN A  23      22.109  80.836   4.707  1.00 42.12           C  
ATOM    154  OD1 ASN A  23      21.654  80.356   5.757  1.00 43.56           O  
ATOM    155  ND2 ASN A  23      23.379  81.261   4.585  1.00 42.97           N  
ATOM    156  N   ARG A  24      21.491  78.801   0.423  1.00 36.41           N  
ATOM    157  CA  ARG A  24      20.792  77.851  -0.421  1.00 34.12           C  
ATOM    158  C   ARG A  24      21.822  76.839  -0.830  1.00 32.97           C  
ATOM    159  O   ARG A  24      23.019  77.060  -0.688  1.00 32.42           O  
ATOM    160  CB  ARG A  24      20.212  78.533  -1.660  1.00 33.62           C  
ATOM    161  CG  ARG A  24      19.098  79.537  -1.352  1.00 33.82           C  
ATOM    162  CD  ARG A  24      18.662  80.294  -2.587  1.00 33.24           C  
ATOM    163  NE  ARG A  24      19.791  80.989  -3.187  1.00 32.82           N  
ATOM    164  CZ  ARG A  24      19.763  81.619  -4.352  1.00 33.12           C  
ATOM    165  NH1 ARG A  24      18.655  81.651  -5.071  1.00 34.53           N  
ATOM    166  NH2 ARG A  24      20.855  82.220  -4.797  1.00 33.12           N  
ATOM    167  N   THR A  25      21.338  75.716  -1.327  1.00 31.90           N  
ATOM    168  CA  THR A  25      22.176  74.655  -1.829  1.00 30.70           C  
ATOM    169  C   THR A  25      22.534  74.898  -3.281  1.00 29.16           C  
ATOM    170  O   THR A  25      21.821  75.624  -3.977  1.00 28.39           O  
ATOM    171  CB  THR A  25      21.389  73.365  -1.774  1.00 31.10           C  
ATOM    172  OG1 THR A  25      20.960  73.155  -0.429  1.00 32.18           O  
ATOM    173  CG2 THR A  25      22.238  72.189  -2.216  1.00 31.70           C  
ATOM    174  N   PRO A  26      23.634  74.278  -3.751  1.00 28.16           N  
ATOM    175  CA  PRO A  26      23.817  74.203  -5.182  1.00 27.51           C  
ATOM    176  C   PRO A  26      22.523  73.864  -5.901  1.00 27.19           C  
ATOM    177  O   PRO A  26      22.128  74.599  -6.802  1.00 27.23           O  
ATOM    178  CB  PRO A  26      24.860  73.118  -5.327  1.00 27.07           C  
ATOM    179  CG  PRO A  26      25.761  73.381  -4.173  1.00 26.97           C  
ATOM    180  CD  PRO A  26      24.845  73.820  -3.044  1.00 28.03           C  
ATOM    181  N   LEU A  27      21.836  72.807  -5.486  1.00 26.89           N  
ATOM    182  CA  LEU A  27      20.618  72.399  -6.179  1.00 26.52           C  
ATOM    183  C   LEU A  27      19.597  73.519  -6.103  1.00 26.47           C  
ATOM    184  O   LEU A  27      19.025  73.924  -7.108  1.00 26.94           O  
ATOM    185  CB  LEU A  27      20.065  71.139  -5.548  1.00 26.70           C  
ATOM    186  CG  LEU A  27      19.182  70.148  -6.295  1.00 27.20           C  
ATOM    187  CD1 LEU A  27      19.641  69.873  -7.732  1.00 27.67           C  
ATOM    188  CD2 LEU A  27      19.232  68.875  -5.480  1.00 26.76           C  
ATOM    189  N   GLN A  28      19.398  74.065  -4.913  1.00 26.04           N  
ATOM    190  CA  GLN A  28      18.443  75.160  -4.761  1.00 25.05           C  
ATOM    191  C   GLN A  28      18.776  76.420  -5.564  1.00 24.12           C  
ATOM    192  O   GLN A  28      17.886  77.157  -5.936  1.00 24.24           O  
ATOM    193  CB  GLN A  28      18.309  75.551  -3.300  1.00 25.41           C  
ATOM    194  CG  GLN A  28      17.769  74.518  -2.367  1.00 24.67           C  
ATOM    195  CD  GLN A  28      17.500  75.152  -1.028  1.00 25.60           C  
ATOM    196  OE1 GLN A  28      18.390  75.252  -0.193  1.00 27.15           O  
ATOM    197  NE2 GLN A  28      16.281  75.630  -0.833  1.00 24.90           N  
ATOM    198  N   ALA A  29      20.041  76.710  -5.802  1.00 23.42           N  
ATOM    199  CA  ALA A  29      20.337  77.930  -6.557  1.00 23.13           C  
ATOM    200  C   ALA A  29      20.326  77.700  -8.085  1.00 22.97           C  
ATOM    201  O   ALA A  29      20.068  78.628  -8.853  1.00 23.21           O  
ATOM    202  CB  ALA A  29      21.637  78.565  -6.095  1.00 22.58           C  
ATOM    203  N   ALA A  30      20.558  76.461  -8.514  1.00 22.32           N  
ATOM    204  CA  ALA A  30      20.686  76.153  -9.927  1.00 21.95           C  
ATOM    205  C   ALA A  30      19.408  76.387 -10.724  1.00 22.03           C  
ATOM    206  O   ALA A  30      18.314  75.976 -10.331  1.00 21.95           O  
ATOM    207  CB  ALA A  30      21.164  74.758 -10.114  1.00 21.92           C  
ATOM    208  N   PHE A  31      19.579  77.062 -11.854  1.00 21.96           N  
ATOM    209  CA  PHE A  31      18.535  77.250 -12.841  1.00 21.67           C  
ATOM    210  C   PHE A  31      18.232  75.842 -13.403  1.00 21.97           C  
ATOM    211  O   PHE A  31      19.053  75.240 -14.121  1.00 22.12           O  
ATOM    212  CB  PHE A  31      19.027  78.266 -13.882  1.00 20.98           C  
ATOM    213  CG  PHE A  31      18.084  78.517 -14.995  1.00 20.69           C  
ATOM    214  CD1 PHE A  31      16.842  79.094 -14.763  1.00 22.37           C  
ATOM    215  CD2 PHE A  31      18.443  78.188 -16.306  1.00 22.40           C  
ATOM    216  CE1 PHE A  31      15.927  79.329 -15.837  1.00 23.61           C  
ATOM    217  CE2 PHE A  31      17.552  78.410 -17.390  1.00 22.90           C  
ATOM    218  CZ  PHE A  31      16.293  78.988 -17.155  1.00 23.59           C  
ATOM    219  N   ARG A  32      17.043  75.341 -13.049  1.00 21.77           N  
ATOM    220  CA  ARG A  32      16.681  73.909 -13.099  1.00 21.08           C  
ATOM    221  C   ARG A  32      15.401  73.597 -13.876  1.00 20.94           C  
ATOM    222  O   ARG A  32      14.645  72.697 -13.496  1.00 20.89           O  
ATOM    223  CB  ARG A  32      16.404  73.478 -11.666  1.00 20.78           C  
ATOM    224  CG  ARG A  32      17.470  72.694 -11.030  1.00 20.25           C  
ATOM    225  CD  ARG A  32      17.527  72.828  -9.488  1.00 19.35           C  
ATOM    226  NE  ARG A  32      16.278  73.105  -8.771  1.00 18.49           N  
ATOM    227  CZ  ARG A  32      16.042  74.216  -8.081  1.00 17.93           C  
ATOM    228  NH1 ARG A  32      16.944  75.189  -8.031  1.00 17.93           N  
ATOM    229  NH2 ARG A  32      14.893  74.362  -7.455  1.00 18.25           N  
ATOM    230  N   PRO A  33      15.124  74.326 -14.959  1.00 21.08           N  
ATOM    231  CA  PRO A  33      13.765  74.134 -15.497  1.00 21.35           C  
ATOM    232  C   PRO A  33      13.367  72.672 -15.835  1.00 21.36           C  
ATOM    233  O   PRO A  33      12.205  72.307 -15.663  1.00 21.03           O  
ATOM    234  CB  PRO A  33      13.737  75.036 -16.743  1.00 21.14           C  
ATOM    235  CG  PRO A  33      15.164  75.300 -17.083  1.00 20.90           C  
ATOM    236  CD  PRO A  33      15.927  75.246 -15.784  1.00 21.01           C  
ATOM    237  N   ASN A  34      14.310  71.850 -16.286  1.00 21.48           N  
ATOM    238  CA  ASN A  34      13.963  70.486 -16.674  1.00 22.20           C  
ATOM    239  C   ASN A  34      13.692  69.597 -15.463  1.00 22.75           C  
ATOM    240  O   ASN A  34      12.655  68.919 -15.398  1.00 22.65           O  
ATOM    241  CB  ASN A  34      14.998  69.894 -17.628  1.00 21.92           C  
ATOM    242  CG  ASN A  34      15.048  70.636 -18.981  1.00 23.85           C  
ATOM    243  OD1 ASN A  34      14.044  71.220 -19.437  1.00 25.59           O  
ATOM    244  ND2 ASN A  34      16.225  70.627 -19.621  1.00 23.67           N  
ATOM    245  N   LEU A  35      14.597  69.622 -14.489  1.00 23.25           N  
ATOM    246  CA  LEU A  35      14.349  68.951 -13.225  1.00 23.82           C  
ATOM    247  C   LEU A  35      13.045  69.452 -12.632  1.00 24.31           C  
ATOM    248  O   LEU A  35      12.215  68.647 -12.181  1.00 23.90           O  
ATOM    249  CB  LEU A  35      15.482  69.215 -12.243  1.00 23.99           C  
ATOM    250  CG  LEU A  35      16.535  68.148 -11.945  1.00 24.33           C  
ATOM    251  CD1 LEU A  35      16.477  66.953 -12.879  1.00 23.82           C  
ATOM    252  CD2 LEU A  35      17.913  68.780 -11.952  1.00 23.10           C  
ATOM    253  N   ASN A  36      12.843  70.773 -12.658  1.00 24.55           N  
ATOM    254  CA  ASN A  36      11.654  71.314 -12.023  1.00 25.53           C  
ATOM    255  C   ASN A  36      10.414  70.847 -12.733  1.00 26.28           C  
ATOM    256  O   ASN A  36       9.408  70.536 -12.089  1.00 25.75           O  
ATOM    257  CB  ASN A  36      11.697  72.829 -11.907  1.00 25.28           C  
ATOM    258  CG  ASN A  36      12.630  73.302 -10.800  1.00 26.20           C  
ATOM    259  OD1 ASN A  36      12.800  72.638  -9.767  1.00 27.04           O  
ATOM    260  ND2 ASN A  36      13.250  74.450 -11.017  1.00 25.53           N  
ATOM    261  N   TRP A  37      10.517  70.756 -14.062  1.00 27.53           N  
ATOM    262  CA  TRP A  37       9.414  70.306 -14.912  1.00 28.72           C  
ATOM    263  C   TRP A  37       8.957  68.919 -14.457  1.00 28.50           C  
ATOM    264  O   TRP A  37       7.763  68.661 -14.278  1.00 28.35           O  
ATOM    265  CB  TRP A  37       9.851  70.292 -16.377  1.00 29.40           C  
ATOM    266  CG  TRP A  37       8.739  70.081 -17.370  1.00 33.37           C  
ATOM    267  CD1 TRP A  37       8.050  71.048 -18.047  1.00 35.94           C  
ATOM    268  CD2 TRP A  37       8.204  68.821 -17.815  1.00 37.57           C  
ATOM    269  NE1 TRP A  37       7.112  70.474 -18.884  1.00 38.40           N  
ATOM    270  CE2 TRP A  37       7.178  69.111 -18.758  1.00 39.02           C  
ATOM    271  CE3 TRP A  37       8.479  67.476 -17.503  1.00 38.42           C  
ATOM    272  CZ2 TRP A  37       6.423  68.102 -19.390  1.00 40.29           C  
ATOM    273  CZ3 TRP A  37       7.729  66.463 -18.142  1.00 40.01           C  
ATOM    274  CH2 TRP A  37       6.720  66.784 -19.074  1.00 40.51           C  
ATOM    275  N   LEU A  38       9.930  68.043 -14.235  1.00 28.27           N  
ATOM    276  CA  LEU A  38       9.656  66.699 -13.765  1.00 27.72           C  
ATOM    277  C   LEU A  38       8.989  66.710 -12.408  1.00 27.78           C  
ATOM    278  O   LEU A  38       8.028  65.984 -12.197  1.00 27.83           O  
ATOM    279  CB  LEU A  38      10.935  65.864 -13.734  1.00 27.43           C  
ATOM    280  CG  LEU A  38      11.508  65.593 -15.127  1.00 26.06           C  
ATOM    281  CD1 LEU A  38      12.974  65.206 -15.035  1.00 25.23           C  
ATOM    282  CD2 LEU A  38      10.701  64.537 -15.856  1.00 23.77           C  
ATOM    283  N   ALA A  39       9.469  67.541 -11.496  1.00 27.93           N  
ATOM    284  CA  ALA A  39       8.829  67.618 -10.190  1.00 28.70           C  
ATOM    285  C   ALA A  39       7.374  68.073 -10.304  1.00 29.32           C  
ATOM    286  O   ALA A  39       6.487  67.544  -9.644  1.00 29.15           O  
ATOM    287  CB  ALA A  39       9.606  68.522  -9.269  1.00 28.83           C  
ATOM    288  N   SER A  40       7.134  69.053 -11.164  1.00 30.71           N  
ATOM    289  CA  SER A  40       5.784  69.541 -11.396  1.00 31.53           C  
ATOM    290  C   SER A  40       4.912  68.423 -11.908  1.00 31.92           C  
ATOM    291  O   SER A  40       3.859  68.166 -11.337  1.00 32.33           O  
ATOM    292  CB  SER A  40       5.788  70.684 -12.385  1.00 31.37           C  
ATOM    293  OG  SER A  40       6.547  71.733 -11.843  1.00 32.88           O  
ATOM    294  N   HIS A  41       5.365  67.736 -12.953  1.00 31.80           N  
ATOM    295  CA  HIS A  41       4.569  66.670 -13.543  1.00 31.82           C  
ATOM    296  C   HIS A  41       4.698  65.268 -12.909  1.00 30.87           C  
ATOM    297  O   HIS A  41       4.404  64.278 -13.576  1.00 31.18           O  
ATOM    298  CB  HIS A  41       4.798  66.621 -15.060  1.00 32.53           C  
ATOM    299  CG  HIS A  41       4.464  67.902 -15.772  1.00 35.52           C  
ATOM    300  ND1 HIS A  41       3.168  68.357 -15.936  1.00 37.76           N  
ATOM    301  CD2 HIS A  41       5.259  68.815 -16.379  1.00 37.37           C  
ATOM    302  CE1 HIS A  41       3.183  69.493 -16.611  1.00 38.16           C  
ATOM    303  NE2 HIS A  41       4.440  69.792 -16.893  1.00 38.41           N  
ATOM    304  N   GLY A  42       5.065  65.172 -11.630  1.00 30.09           N  
ATOM    305  CA  GLY A  42       5.353  63.858 -11.026  1.00 29.44           C  
ATOM    306  C   GLY A  42       5.261  63.705  -9.522  1.00 29.06           C  
ATOM    307  O   GLY A  42       4.764  64.582  -8.832  1.00 29.37           O  
ATOM    308  N   ILE A  43       5.720  62.574  -9.004  1.00 28.54           N  
ATOM    309  CA  ILE A  43       5.703  62.360  -7.558  1.00 28.42           C  
ATOM    310  C   ILE A  43       7.076  62.667  -6.997  1.00 27.80           C  
ATOM    311  O   ILE A  43       8.075  62.396  -7.634  1.00 27.49           O  
ATOM    312  CB  ILE A  43       5.307  60.913  -7.151  1.00 28.83           C  
ATOM    313  CG1 ILE A  43       4.016  60.478  -7.804  1.00 29.15           C  
ATOM    314  CG2 ILE A  43       5.108  60.796  -5.666  1.00 29.87           C  
ATOM    315  CD1 ILE A  43       4.281  59.498  -8.883  1.00 32.29           C  
ATOM    316  N   ASN A  44       7.115  63.221  -5.793  1.00 27.52           N  
ATOM    317  CA  ASN A  44       8.340  63.752  -5.228  1.00 27.71           C  
ATOM    318  C   ASN A  44       8.479  63.353  -3.772  1.00 28.67           C  
ATOM    319  O   ASN A  44       7.484  63.061  -3.088  1.00 29.35           O  
ATOM    320  CB  ASN A  44       8.358  65.281  -5.352  1.00 27.19           C  
ATOM    321  CG  ASN A  44       8.142  65.752  -6.776  1.00 26.55           C  
ATOM    322  OD1 ASN A  44       9.071  65.796  -7.563  1.00 26.15           O  
ATOM    323  ND2 ASN A  44       6.908  66.083  -7.116  1.00 24.94           N  
ATOM    324  N   GLY A  45       9.712  63.328  -3.290  1.00 29.10           N  
ATOM    325  CA  GLY A  45       9.931  63.086  -1.894  1.00 29.96           C  
ATOM    326  C   GLY A  45      11.397  63.013  -1.559  1.00 30.92           C  
ATOM    327  O   GLY A  45      12.236  63.662  -2.191  1.00 30.32           O  
ATOM    328  N   ILE A  46      11.676  62.194  -0.554  1.00 31.89           N  
ATOM    329  CA  ILE A  46      12.984  62.062   0.021  1.00 33.29           C  
ATOM    330  C   ILE A  46      13.277  60.581   0.127  1.00 34.81           C  
ATOM    331  O   ILE A  46      12.466  59.823   0.656  1.00 35.04           O  
ATOM    332  CB  ILE A  46      13.015  62.668   1.433  1.00 32.80           C  
ATOM    333  CG1 ILE A  46      12.746  64.178   1.388  1.00 32.58           C  
ATOM    334  CG2 ILE A  46      14.306  62.313   2.141  1.00 31.43           C  
ATOM    335  CD1 ILE A  46      13.666  64.993   0.487  1.00 32.72           C  
HETATM  336  N   MSE A  47      14.440  60.176  -0.365  1.00 36.61           N  
HETATM  337  CA  MSE A  47      14.851  58.790  -0.280  1.00 38.55           C  
HETATM  338  C   MSE A  47      16.013  58.662   0.677  1.00 40.22           C  
HETATM  339  O   MSE A  47      16.918  59.470   0.638  1.00 40.03           O  
HETATM  340  CB  MSE A  47      15.237  58.282  -1.655  1.00 38.32           C  
HETATM  341  CG  MSE A  47      15.542  56.818  -1.696  1.00 37.36           C  
HETATM  342 SE   MSE A  47      17.065  56.564  -2.833  1.00 37.45          SE  
HETATM  343  CE  MSE A  47      18.427  56.411  -1.490  1.00 34.27           C  
ATOM    344  N   HIS A  48      15.965  57.659   1.546  1.00 43.20           N  
ATOM    345  CA  HIS A  48      17.007  57.437   2.539  1.00 46.75           C  
ATOM    346  C   HIS A  48      17.804  56.237   2.084  1.00 48.59           C  
ATOM    347  O   HIS A  48      17.271  55.132   2.050  1.00 48.95           O  
ATOM    348  CB  HIS A  48      16.405  57.212   3.932  1.00 47.00           C  
ATOM    349  CG  HIS A  48      15.660  58.406   4.462  1.00 50.84           C  
ATOM    350  ND1 HIS A  48      14.341  58.675   4.133  1.00 53.23           N  
ATOM    351  CD2 HIS A  48      16.053  59.416   5.281  1.00 53.03           C  
ATOM    352  CE1 HIS A  48      13.955  59.793   4.730  1.00 53.33           C  
ATOM    353  NE2 HIS A  48      14.974  60.262   5.432  1.00 53.61           N  
ATOM    354  N   PRO A  49      19.072  56.453   1.685  1.00 50.63           N  
ATOM    355  CA  PRO A  49      19.914  55.358   1.191  1.00 52.53           C  
ATOM    356  C   PRO A  49      20.141  54.354   2.305  1.00 54.40           C  
ATOM    357  O   PRO A  49      20.086  54.729   3.479  1.00 54.70           O  
ATOM    358  CB  PRO A  49      21.222  56.059   0.792  1.00 52.37           C  
ATOM    359  CG  PRO A  49      20.843  57.513   0.629  1.00 51.65           C  
ATOM    360  CD  PRO A  49      19.789  57.738   1.670  1.00 50.72           C  
ATOM    361  N   ILE A  50      20.390  53.099   1.946  1.00 56.63           N  
ATOM    362  CA  ILE A  50      20.227  51.993   2.906  1.00 58.88           C  
ATOM    363  C   ILE A  50      21.136  52.010   4.159  1.00 60.46           C  
ATOM    364  O   ILE A  50      22.309  52.416   4.088  1.00 60.60           O  
ATOM    365  CB  ILE A  50      20.153  50.593   2.184  1.00 58.70           C  
ATOM    366  CG1 ILE A  50      18.692  50.243   1.871  1.00 58.47           C  
ATOM    367  CG2 ILE A  50      20.804  49.471   2.996  1.00 58.79           C  
ATOM    368  CD1 ILE A  50      17.694  50.652   2.962  1.00 57.94           C  
ATOM    369  N   SER A  51      20.541  51.592   5.288  1.00 62.22           N  
ATOM    370  CA  SER A  51      21.159  51.536   6.632  1.00 63.84           C  
ATOM    371  C   SER A  51      22.512  50.760   6.712  1.00 64.93           C  
ATOM    372  O   SER A  51      22.869  50.032   5.776  1.00 65.14           O  
ATOM    373  CB  SER A  51      20.144  50.944   7.632  1.00 63.98           C  
ATOM    374  OG  SER A  51      18.823  51.388   7.359  1.00 63.81           O  
ATOM    375  N   PRO A  52      23.272  50.918   7.829  1.00 65.83           N  
ATOM    376  CA  PRO A  52      24.611  50.281   7.896  1.00 66.21           C  
ATOM    377  C   PRO A  52      24.595  48.809   8.338  1.00 66.10           C  
ATOM    378  O   PRO A  52      25.632  48.141   8.303  1.00 65.83           O  
ATOM    379  CB  PRO A  52      25.381  51.158   8.918  1.00 66.51           C  
ATOM    380  CG  PRO A  52      24.431  52.328   9.276  1.00 66.34           C  
ATOM    381  CD  PRO A  52      23.045  51.819   8.977  1.00 65.76           C  
ATOM    382  N   SER A  58      31.078  50.544   2.591  1.00 68.17           N  
ATOM    383  CA  SER A  58      29.735  51.028   2.226  1.00 68.31           C  
ATOM    384  C   SER A  58      29.793  51.933   0.975  1.00 68.29           C  
ATOM    385  O   SER A  58      28.918  52.794   0.752  1.00 68.45           O  
ATOM    386  CB  SER A  58      29.063  51.751   3.422  1.00 68.48           C  
ATOM    387  OG  SER A  58      27.651  51.885   3.258  1.00 67.52           O  
ATOM    388  N   ASP A  59      30.826  51.709   0.158  1.00 67.76           N  
ATOM    389  CA  ASP A  59      31.116  52.519  -1.045  1.00 67.04           C  
ATOM    390  C   ASP A  59      29.940  52.687  -2.023  1.00 65.81           C  
ATOM    391  O   ASP A  59      30.033  53.462  -2.991  1.00 65.97           O  
ATOM    392  CB  ASP A  59      32.368  51.979  -1.778  1.00 67.53           C  
ATOM    393  CG  ASP A  59      32.740  50.551  -1.341  1.00 68.82           C  
ATOM    394  OD1 ASP A  59      33.853  50.385  -0.778  1.00 70.23           O  
ATOM    395  OD2 ASP A  59      31.919  49.611  -1.532  1.00 69.23           O  
ATOM    396  N   THR A  60      28.841  51.967  -1.776  1.00 64.00           N  
ATOM    397  CA  THR A  60      27.682  52.109  -2.643  1.00 62.04           C  
ATOM    398  C   THR A  60      26.264  51.858  -2.111  1.00 60.03           C  
ATOM    399  O   THR A  60      25.994  50.975  -1.273  1.00 59.33           O  
ATOM    400  CB  THR A  60      27.884  51.393  -4.006  1.00 62.42           C  
ATOM    401  OG1 THR A  60      27.381  52.245  -5.046  1.00 63.17           O  
ATOM    402  CG2 THR A  60      27.186  50.021  -4.039  1.00 62.53           C  
ATOM    403  N   SER A  61      25.391  52.694  -2.669  1.00 57.50           N  
ATOM    404  CA  SER A  61      23.957  52.593  -2.599  1.00 54.81           C  
ATOM    405  C   SER A  61      23.402  52.278  -3.998  1.00 52.58           C  
ATOM    406  O   SER A  61      22.198  52.115  -4.164  1.00 52.19           O  
ATOM    407  CB  SER A  61      23.409  53.923  -2.083  1.00 54.98           C  
ATOM    408  OG  SER A  61      22.043  54.104  -2.406  1.00 56.32           O  
ATOM    409  N   HIS A  62      24.286  52.195  -4.995  1.00 49.88           N  
ATOM    410  CA  HIS A  62      23.907  51.843  -6.362  1.00 47.43           C  
ATOM    411  C   HIS A  62      23.436  50.409  -6.432  1.00 46.22           C  
ATOM    412  O   HIS A  62      22.529  50.066  -7.185  1.00 45.94           O  
ATOM    413  CB  HIS A  62      25.091  51.995  -7.297  1.00 47.24           C  
ATOM    414  CG  HIS A  62      25.442  53.412  -7.595  1.00 46.97           C  
ATOM    415  ND1 HIS A  62      26.068  54.230  -6.681  1.00 47.09           N  
ATOM    416  CD2 HIS A  62      25.254  54.159  -8.706  1.00 46.83           C  
ATOM    417  CE1 HIS A  62      26.248  55.423  -7.216  1.00 47.17           C  
ATOM    418  NE2 HIS A  62      25.766  55.405  -8.446  1.00 47.52           N  
HETATM  419  N   MSE A  63      24.074  49.571  -5.639  1.00 44.67           N  
HETATM  420  CA  MSE A  63      23.724  48.182  -5.566  1.00 43.46           C  
HETATM  421  C   MSE A  63      22.245  47.996  -5.172  1.00 41.83           C  
HETATM  422  O   MSE A  63      21.489  47.323  -5.876  1.00 41.80           O  
HETATM  423  CB  MSE A  63      24.675  47.503  -4.593  1.00 44.08           C  
HETATM  424  CG  MSE A  63      24.423  46.048  -4.363  1.00 46.81           C  
HETATM  425 SE   MSE A  63      26.125  45.126  -4.351  1.00 53.12          SE  
HETATM  426  CE  MSE A  63      25.886  44.271  -6.073  1.00 51.55           C  
ATOM    427  N   SER A  64      21.815  48.607  -4.077  1.00 39.58           N  
ATOM    428  CA  SER A  64      20.416  48.475  -3.671  1.00 37.93           C  
ATOM    429  C   SER A  64      19.387  49.132  -4.606  1.00 36.28           C  
ATOM    430  O   SER A  64      18.215  48.783  -4.559  1.00 36.16           O  
ATOM    431  CB  SER A  64      20.216  48.961  -2.239  1.00 38.22           C  
ATOM    432  OG  SER A  64      21.115  50.013  -1.952  1.00 39.95           O  
ATOM    433  N   LEU A  65      19.812  50.075  -5.446  1.00 34.28           N  
ATOM    434  CA  LEU A  65      18.916  50.652  -6.441  1.00 32.11           C  
ATOM    435  C   LEU A  65      18.630  49.629  -7.548  1.00 31.75           C  
ATOM    436  O   LEU A  65      17.494  49.449  -7.976  1.00 31.62           O  
ATOM    437  CB  LEU A  65      19.465  51.966  -6.991  1.00 31.11           C  
ATOM    438  CG  LEU A  65      19.284  53.177  -6.076  1.00 29.63           C  
ATOM    439  CD1 LEU A  65      20.207  54.316  -6.466  1.00 27.93           C  
ATOM    440  CD2 LEU A  65      17.857  53.651  -6.022  1.00 26.08           C  
ATOM    441  N   LEU A  66      19.661  48.930  -7.987  1.00 31.07           N  
ATOM    442  CA  LEU A  66      19.460  47.841  -8.904  1.00 30.35           C  
ATOM    443  C   LEU A  66      18.741  46.674  -8.215  1.00 30.83           C  
ATOM    444  O   LEU A  66      18.628  45.600  -8.800  1.00 31.24           O  
ATOM    445  CB  LEU A  66      20.798  47.390  -9.464  1.00 29.90           C  
ATOM    446  CG  LEU A  66      21.646  48.481 -10.115  1.00 28.80           C  
ATOM    447  CD1 LEU A  66      23.106  48.225  -9.808  1.00 28.97           C  
ATOM    448  CD2 LEU A  66      21.439  48.540 -11.611  1.00 25.91           C  
ATOM    449  N   GLY A  67      18.264  46.864  -6.983  1.00 30.42           N  
ATOM    450  CA  GLY A  67      17.429  45.861  -6.344  1.00 30.60           C  
ATOM    451  C   GLY A  67      18.142  44.735  -5.613  1.00 31.53           C  
ATOM    452  O   GLY A  67      17.549  43.677  -5.356  1.00 31.86           O  
ATOM    453  N   TYR A  68      19.408  44.953  -5.257  1.00 31.96           N  
ATOM    454  CA  TYR A  68      20.177  43.992  -4.466  1.00 31.92           C  
ATOM    455  C   TYR A  68      20.388  44.488  -3.052  1.00 33.55           C  
ATOM    456  O   TYR A  68      20.941  45.559  -2.862  1.00 34.09           O  
ATOM    457  CB  TYR A  68      21.533  43.787  -5.097  1.00 30.70           C  
ATOM    458  CG  TYR A  68      21.468  43.104  -6.426  1.00 28.48           C  
ATOM    459  CD1 TYR A  68      21.235  43.822  -7.580  1.00 27.82           C  
ATOM    460  CD2 TYR A  68      21.659  41.743  -6.534  1.00 25.49           C  
ATOM    461  CE1 TYR A  68      21.184  43.201  -8.811  1.00 27.65           C  
ATOM    462  CE2 TYR A  68      21.608  41.108  -7.752  1.00 26.27           C  
ATOM    463  CZ  TYR A  68      21.369  41.838  -8.901  1.00 27.11           C  
ATOM    464  OH  TYR A  68      21.320  41.212 -10.142  1.00 25.24           O  
ATOM    465  N   ASP A  69      19.961  43.717  -2.056  1.00 35.40           N  
ATOM    466  CA  ASP A  69      20.279  44.028  -0.654  1.00 37.13           C  
ATOM    467  C   ASP A  69      21.802  43.933  -0.411  1.00 37.92           C  
ATOM    468  O   ASP A  69      22.354  42.851  -0.437  1.00 37.86           O  
ATOM    469  CB  ASP A  69      19.510  43.068   0.263  1.00 37.43           C  
ATOM    470  CG  ASP A  69      19.870  43.215   1.751  1.00 39.22           C  
ATOM    471  OD1 ASP A  69      20.581  44.178   2.151  1.00 40.45           O  
ATOM    472  OD2 ASP A  69      19.412  42.342   2.531  1.00 40.44           O  
ATOM    473  N   PRO A  70      22.476  45.065  -0.145  1.00 38.97           N  
ATOM    474  CA  PRO A  70      23.937  45.026  -0.060  1.00 40.11           C  
ATOM    475  C   PRO A  70      24.469  44.264   1.142  1.00 41.21           C  
ATOM    476  O   PRO A  70      25.650  43.940   1.177  1.00 41.61           O  
ATOM    477  CB  PRO A  70      24.339  46.509   0.047  1.00 40.23           C  
ATOM    478  CG  PRO A  70      23.062  47.311  -0.130  1.00 39.34           C  
ATOM    479  CD  PRO A  70      21.950  46.380   0.255  1.00 39.20           C  
ATOM    480  N   LYS A  71      23.618  43.987   2.121  1.00 42.66           N  
ATOM    481  CA  LYS A  71      24.004  43.108   3.214  1.00 44.17           C  
ATOM    482  C   LYS A  71      24.486  41.775   2.646  1.00 44.76           C  
ATOM    483  O   LYS A  71      25.648  41.431   2.811  1.00 45.38           O  
ATOM    484  CB  LYS A  71      22.857  42.917   4.209  1.00 44.46           C  
ATOM    485  CG  LYS A  71      22.956  43.823   5.420  1.00 45.98           C  
ATOM    486  CD  LYS A  71      21.581  44.314   5.890  1.00 48.16           C  
ATOM    487  CE  LYS A  71      21.745  45.397   6.958  1.00 48.44           C  
ATOM    488  NZ  LYS A  71      20.851  46.559   6.706  1.00 49.17           N  
ATOM    489  N   VAL A  72      23.603  41.041   1.968  1.00 45.57           N  
ATOM    490  CA  VAL A  72      23.990  39.825   1.228  1.00 45.98           C  
ATOM    491  C   VAL A  72      24.477  40.240  -0.162  1.00 46.75           C  
ATOM    492  O   VAL A  72      24.211  41.351  -0.616  1.00 47.18           O  
ATOM    493  CB  VAL A  72      22.849  38.742   1.206  1.00 45.66           C  
ATOM    494  CG1 VAL A  72      21.495  39.369   0.972  1.00 45.19           C  
ATOM    495  CG2 VAL A  72      23.132  37.623   0.211  1.00 44.74           C  
ATOM    496  N   TYR A  73      25.218  39.366  -0.824  1.00 47.51           N  
ATOM    497  CA  TYR A  73      25.907  39.711  -2.090  1.00 48.42           C  
ATOM    498  C   TYR A  73      26.569  41.112  -2.253  1.00 48.59           C  
ATOM    499  O   TYR A  73      26.674  41.641  -3.364  1.00 48.61           O  
ATOM    500  CB  TYR A  73      25.119  39.291  -3.355  1.00 48.46           C  
ATOM    501  CG  TYR A  73      23.630  39.368  -3.264  1.00 48.54           C  
ATOM    502  CD1 TYR A  73      22.995  40.578  -3.021  1.00 48.11           C  
ATOM    503  CD2 TYR A  73      22.846  38.222  -3.460  1.00 49.56           C  
ATOM    504  CE1 TYR A  73      21.604  40.654  -2.930  1.00 50.08           C  
ATOM    505  CE2 TYR A  73      21.448  38.281  -3.383  1.00 50.18           C  
ATOM    506  CZ  TYR A  73      20.834  39.508  -3.115  1.00 50.68           C  
ATOM    507  OH  TYR A  73      19.460  39.608  -3.027  1.00 51.88           O  
ATOM    508  N   TYR A  74      27.052  41.687  -1.159  1.00 48.87           N  
ATOM    509  CA  TYR A  74      28.201  42.552  -1.315  1.00 49.36           C  
ATOM    510  C   TYR A  74      29.337  41.615  -1.750  1.00 48.72           C  
ATOM    511  O   TYR A  74      29.549  40.568  -1.111  1.00 48.70           O  
ATOM    512  CB  TYR A  74      28.576  43.281  -0.028  1.00 49.99           C  
ATOM    513  CG  TYR A  74      29.897  44.010  -0.164  1.00 52.26           C  
ATOM    514  CD1 TYR A  74      31.003  43.648   0.612  1.00 54.15           C  
ATOM    515  CD2 TYR A  74      30.050  45.047  -1.100  1.00 54.45           C  
ATOM    516  CE1 TYR A  74      32.223  44.319   0.475  1.00 55.76           C  
ATOM    517  CE2 TYR A  74      31.269  45.718  -1.252  1.00 55.42           C  
ATOM    518  CZ  TYR A  74      32.345  45.345  -0.464  1.00 55.60           C  
ATOM    519  OH  TYR A  74      33.540  45.996  -0.607  1.00 55.81           O  
ATOM    520  N   PRO A  75      30.044  41.964  -2.849  1.00 48.09           N  
ATOM    521  CA  PRO A  75      31.074  41.089  -3.445  1.00 46.97           C  
ATOM    522  C   PRO A  75      32.286  40.806  -2.542  1.00 45.73           C  
ATOM    523  O   PRO A  75      32.804  39.688  -2.576  1.00 45.84           O  
ATOM    524  CB  PRO A  75      31.504  41.859  -4.697  1.00 47.21           C  
ATOM    525  CG  PRO A  75      31.160  43.320  -4.385  1.00 47.84           C  
ATOM    526  CD  PRO A  75      29.868  43.205  -3.633  1.00 48.21           C  
ATOM    527  N   GLY A  76      32.721  41.790  -1.746  1.00 44.10           N  
ATOM    528  CA  GLY A  76      33.878  41.631  -0.845  1.00 42.10           C  
ATOM    529  C   GLY A  76      35.041  42.530  -1.243  1.00 40.96           C  
ATOM    530  O   GLY A  76      35.248  42.780  -2.422  1.00 40.94           O  
ATOM    531  N   ARG A  77      35.811  43.012  -0.272  1.00 39.79           N  
ATOM    532  CA  ARG A  77      36.958  43.894  -0.555  1.00 39.09           C  
ATOM    533  C   ARG A  77      37.955  43.390  -1.596  1.00 37.57           C  
ATOM    534  O   ARG A  77      38.512  44.191  -2.336  1.00 37.73           O  
ATOM    535  CB  ARG A  77      37.710  44.331   0.722  1.00 39.58           C  
ATOM    536  CG  ARG A  77      37.704  43.330   1.878  1.00 43.29           C  
ATOM    537  CD  ARG A  77      38.673  43.733   3.017  1.00 48.44           C  
ATOM    538  NE  ARG A  77      38.394  45.048   3.604  1.00 50.48           N  
ATOM    539  CZ  ARG A  77      39.234  45.716   4.401  1.00 51.91           C  
ATOM    540  NH1 ARG A  77      40.418  45.196   4.719  1.00 52.48           N  
ATOM    541  NH2 ARG A  77      38.892  46.911   4.880  1.00 51.49           N  
ATOM    542  N   GLY A  78      38.194  42.084  -1.650  1.00 35.98           N  
ATOM    543  CA  GLY A  78      39.048  41.518  -2.689  1.00 33.95           C  
ATOM    544  C   GLY A  78      38.456  41.787  -4.056  1.00 32.96           C  
ATOM    545  O   GLY A  78      39.015  42.536  -4.850  1.00 32.51           O  
ATOM    546  N   PRO A  79      37.288  41.201  -4.328  1.00 32.53           N  
ATOM    547  CA  PRO A  79      36.580  41.373  -5.599  1.00 32.37           C  
ATOM    548  C   PRO A  79      36.383  42.827  -6.017  1.00 32.18           C  
ATOM    549  O   PRO A  79      36.500  43.172  -7.206  1.00 32.07           O  
ATOM    550  CB  PRO A  79      35.231  40.720  -5.317  1.00 32.50           C  
ATOM    551  CG  PRO A  79      35.561  39.643  -4.323  1.00 32.21           C  
ATOM    552  CD  PRO A  79      36.624  40.215  -3.453  1.00 32.21           C  
ATOM    553  N   PHE A  80      36.090  43.664  -5.034  1.00 32.03           N  
ATOM    554  CA  PHE A  80      35.850  45.081  -5.262  1.00 32.47           C  
ATOM    555  C   PHE A  80      37.086  45.849  -5.742  1.00 31.66           C  
ATOM    556  O   PHE A  80      36.992  46.699  -6.624  1.00 31.47           O  
ATOM    557  CB  PHE A  80      35.279  45.712  -3.991  1.00 33.36           C  
ATOM    558  CG  PHE A  80      34.789  47.102  -4.188  1.00 36.19           C  
ATOM    559  CD1 PHE A  80      35.579  48.198  -3.774  1.00 38.37           C  
ATOM    560  CD2 PHE A  80      33.550  47.330  -4.811  1.00 37.77           C  
ATOM    561  CE1 PHE A  80      35.132  49.514  -3.971  1.00 40.03           C  
ATOM    562  CE2 PHE A  80      33.087  48.634  -5.014  1.00 39.79           C  
ATOM    563  CZ  PHE A  80      33.879  49.737  -4.596  1.00 40.82           C  
ATOM    564  N   GLU A  81      38.237  45.554  -5.157  1.00 31.01           N  
ATOM    565  CA  GLU A  81      39.473  46.111  -5.651  1.00 30.99           C  
ATOM    566  C   GLU A  81      39.623  45.769  -7.123  1.00 30.10           C  
ATOM    567  O   GLU A  81      39.893  46.652  -7.939  1.00 29.83           O  
ATOM    568  CB  GLU A  81      40.659  45.547  -4.884  1.00 31.60           C  
ATOM    569  CG  GLU A  81      41.998  46.128  -5.307  1.00 34.16           C  
ATOM    570  CD  GLU A  81      42.432  47.306  -4.441  1.00 39.56           C  
ATOM    571  OE1 GLU A  81      43.636  47.664  -4.520  1.00 41.81           O  
ATOM    572  OE2 GLU A  81      41.589  47.864  -3.680  1.00 40.09           O  
ATOM    573  N   ALA A  82      39.434  44.487  -7.445  1.00 29.07           N  
ATOM    574  CA  ALA A  82      39.614  43.987  -8.798  1.00 28.41           C  
ATOM    575  C   ALA A  82      38.647  44.676  -9.696  1.00 28.31           C  
ATOM    576  O   ALA A  82      39.000  45.078 -10.810  1.00 27.89           O  
ATOM    577  CB  ALA A  82      39.377  42.512  -8.862  1.00 28.37           C  
ATOM    578  N   LEU A  83      37.420  44.799  -9.194  1.00 28.17           N  
ATOM    579  CA  LEU A  83      36.355  45.480  -9.893  1.00 28.34           C  
ATOM    580  C   LEU A  83      36.714  46.929 -10.228  1.00 28.91           C  
ATOM    581  O   LEU A  83      36.391  47.415 -11.324  1.00 29.15           O  
ATOM    582  CB  LEU A  83      35.125  45.443  -9.034  1.00 27.91           C  
ATOM    583  CG  LEU A  83      33.881  44.910  -9.703  1.00 27.14           C  
ATOM    584  CD1 LEU A  83      34.211  43.999 -10.865  1.00 26.56           C  
ATOM    585  CD2 LEU A  83      33.171  44.162  -8.614  1.00 25.11           C  
ATOM    586  N   GLY A  84      37.406  47.597  -9.296  1.00 29.12           N  
ATOM    587  CA  GLY A  84      37.874  48.973  -9.489  1.00 29.36           C  
ATOM    588  C   GLY A  84      39.086  49.139 -10.405  1.00 29.64           C  
ATOM    589  O   GLY A  84      39.399  50.246 -10.855  1.00 29.76           O  
ATOM    590  N   LEU A  85      39.794  48.053 -10.679  1.00 29.61           N  
ATOM    591  CA  LEU A  85      40.845  48.121 -11.682  1.00 29.72           C  
ATOM    592  C   LEU A  85      40.362  47.761 -13.107  1.00 29.97           C  
ATOM    593  O   LEU A  85      41.158  47.684 -14.043  1.00 29.73           O  
ATOM    594  CB  LEU A  85      42.034  47.284 -11.252  1.00 29.63           C  
ATOM    595  CG  LEU A  85      43.205  47.980 -10.550  1.00 30.06           C  
ATOM    596  CD1 LEU A  85      42.860  49.289  -9.817  1.00 31.02           C  
ATOM    597  CD2 LEU A  85      43.820  46.975  -9.598  1.00 29.82           C  
ATOM    598  N   GLY A  86      39.053  47.571 -13.261  1.00 30.10           N  
ATOM    599  CA  GLY A  86      38.467  47.249 -14.545  1.00 30.51           C  
ATOM    600  C   GLY A  86      38.637  45.781 -14.886  1.00 31.36           C  
ATOM    601  O   GLY A  86      38.726  45.409 -16.067  1.00 32.16           O  
HETATM  602  N   MSE A  87      38.683  44.922 -13.871  1.00 31.49           N  
HETATM  603  CA  MSE A  87      38.741  43.487 -14.128  1.00 31.47           C  
HETATM  604  C   MSE A  87      37.343  42.887 -14.067  1.00 31.77           C  
HETATM  605  O   MSE A  87      36.565  43.185 -13.157  1.00 32.01           O  
HETATM  606  CB  MSE A  87      39.666  42.786 -13.139  1.00 31.36           C  
HETATM  607  CG  MSE A  87      41.084  43.246 -13.189  1.00 31.22           C  
HETATM  608 SE   MSE A  87      42.049  42.497 -11.714  1.00 30.53          SE  
HETATM  609  CE  MSE A  87      42.427  40.821 -12.573  1.00 30.79           C  
ATOM    610  N   ASP A  88      37.025  42.061 -15.054  1.00 32.25           N  
ATOM    611  CA  ASP A  88      35.770  41.328 -15.064  1.00 32.86           C  
ATOM    612  C   ASP A  88      35.892  40.185 -14.087  1.00 32.06           C  
ATOM    613  O   ASP A  88      36.874  39.439 -14.110  1.00 31.76           O  
ATOM    614  CB  ASP A  88      35.504  40.708 -16.444  1.00 34.20           C  
ATOM    615  CG  ASP A  88      35.297  41.742 -17.547  1.00 36.25           C  
ATOM    616  OD1 ASP A  88      35.553  42.953 -17.331  1.00 38.14           O  
ATOM    617  OD2 ASP A  88      34.873  41.307 -18.646  1.00 38.97           O  
ATOM    618  N   ILE A  89      34.898  40.040 -13.227  1.00 31.26           N  
ATOM    619  CA  ILE A  89      34.831  38.857 -12.388  1.00 30.27           C  
ATOM    620  C   ILE A  89      33.489  38.195 -12.600  1.00 30.05           C  
ATOM    621  O   ILE A  89      32.514  38.821 -13.027  1.00 29.73           O  
ATOM    622  CB  ILE A  89      35.083  39.146 -10.883  1.00 30.08           C  
ATOM    623  CG1 ILE A  89      34.058  40.148 -10.355  1.00 30.25           C  
ATOM    624  CG2 ILE A  89      36.501  39.663 -10.662  1.00 28.47           C  
ATOM    625  CD1 ILE A  89      34.029  40.243  -8.876  1.00 30.61           C  
ATOM    626  N   ARG A  90      33.467  36.911 -12.308  1.00 29.69           N  
ATOM    627  CA  ARG A  90      32.302  36.101 -12.475  1.00 29.44           C  
ATOM    628  C   ARG A  90      32.127  35.337 -11.162  1.00 28.70           C  
ATOM    629  O   ARG A  90      33.052  35.270 -10.366  1.00 27.77           O  
ATOM    630  CB  ARG A  90      32.506  35.177 -13.680  1.00 29.82           C  
ATOM    631  CG  ARG A  90      32.333  35.863 -15.047  1.00 32.53           C  
ATOM    632  CD  ARG A  90      33.145  35.234 -16.217  1.00 38.22           C  
ATOM    633  NE  ARG A  90      33.628  33.876 -15.950  1.00 42.63           N  
ATOM    634  CZ  ARG A  90      34.908  33.550 -15.726  1.00 45.57           C  
ATOM    635  NH1 ARG A  90      35.875  34.476 -15.768  1.00 46.56           N  
ATOM    636  NH2 ARG A  90      35.229  32.285 -15.465  1.00 45.96           N  
ATOM    637  N   PRO A  91      30.923  34.804 -10.907  1.00 28.78           N  
ATOM    638  CA  PRO A  91      30.695  33.981  -9.712  1.00 28.91           C  
ATOM    639  C   PRO A  91      31.648  32.794  -9.588  1.00 29.01           C  
ATOM    640  O   PRO A  91      31.948  32.115 -10.583  1.00 29.35           O  
ATOM    641  CB  PRO A  91      29.266  33.508  -9.911  1.00 28.73           C  
ATOM    642  CG  PRO A  91      28.628  34.688 -10.583  1.00 28.98           C  
ATOM    643  CD  PRO A  91      29.650  35.200 -11.540  1.00 28.64           C  
ATOM    644  N   GLY A  92      32.157  32.567  -8.383  1.00 28.63           N  
ATOM    645  CA  GLY A  92      33.089  31.463  -8.170  1.00 28.53           C  
ATOM    646  C   GLY A  92      34.576  31.786  -8.229  1.00 28.46           C  
ATOM    647  O   GLY A  92      35.406  30.968  -7.839  1.00 28.74           O  
ATOM    648  N   ASP A  93      34.934  32.968  -8.713  1.00 28.13           N  
ATOM    649  CA  ASP A  93      36.335  33.371  -8.710  1.00 27.61           C  
ATOM    650  C   ASP A  93      36.808  33.799  -7.345  1.00 26.34           C  
ATOM    651  O   ASP A  93      36.012  34.124  -6.463  1.00 26.49           O  
ATOM    652  CB  ASP A  93      36.571  34.516  -9.684  1.00 28.54           C  
ATOM    653  CG  ASP A  93      36.187  34.166 -11.105  1.00 30.64           C  
ATOM    654  OD1 ASP A  93      36.314  35.068 -11.981  1.00 31.67           O  
ATOM    655  OD2 ASP A  93      35.762  32.998 -11.337  1.00 35.26           O  
ATOM    656  N   LEU A  94      38.117  33.794  -7.179  1.00 25.11           N  
ATOM    657  CA  LEU A  94      38.715  34.254  -5.947  1.00 24.26           C  
ATOM    658  C   LEU A  94      39.411  35.548  -6.244  1.00 23.89           C  
ATOM    659  O   LEU A  94      40.073  35.674  -7.286  1.00 24.33           O  
ATOM    660  CB  LEU A  94      39.748  33.258  -5.439  1.00 23.99           C  
ATOM    661  CG  LEU A  94      39.659  32.839  -3.973  1.00 22.89           C  
ATOM    662  CD1 LEU A  94      41.040  32.722  -3.436  1.00 22.64           C  
ATOM    663  CD2 LEU A  94      38.882  33.797  -3.123  1.00 20.81           C  
ATOM    664  N   ALA A  95      39.287  36.517  -5.350  1.00 22.86           N  
ATOM    665  CA  ALA A  95      39.965  37.771  -5.618  1.00 22.31           C  
ATOM    666  C   ALA A  95      40.736  38.279  -4.429  1.00 21.78           C  
ATOM    667  O   ALA A  95      40.308  38.136  -3.295  1.00 21.83           O  
ATOM    668  CB  ALA A  95      38.998  38.798  -6.122  1.00 22.33           C  
ATOM    669  N   PHE A  96      41.894  38.857  -4.703  1.00 21.27           N  
ATOM    670  CA  PHE A  96      42.756  39.353  -3.651  1.00 20.94           C  
ATOM    671  C   PHE A  96      43.059  40.818  -3.917  1.00 21.38           C  
ATOM    672  O   PHE A  96      43.081  41.236  -5.073  1.00 21.37           O  
ATOM    673  CB  PHE A  96      44.078  38.608  -3.652  1.00 20.13           C  
ATOM    674  CG  PHE A  96      43.972  37.142  -3.376  1.00 18.78           C  
ATOM    675  CD1 PHE A  96      43.610  36.257  -4.360  1.00 18.21           C  
ATOM    676  CD2 PHE A  96      44.322  36.630  -2.144  1.00 18.71           C  
ATOM    677  CE1 PHE A  96      43.569  34.890  -4.106  1.00 17.14           C  
ATOM    678  CE2 PHE A  96      44.278  35.265  -1.897  1.00 17.12           C  
ATOM    679  CZ  PHE A  96      43.897  34.404  -2.878  1.00 15.75           C  
ATOM    680  N   ARG A  97      43.281  41.597  -2.856  1.00 21.69           N  
ATOM    681  CA  ARG A  97      44.046  42.823  -2.994  1.00 22.12           C  
ATOM    682  C   ARG A  97      45.476  42.338  -3.043  1.00 21.11           C  
ATOM    683  O   ARG A  97      45.785  41.259  -2.507  1.00 20.68           O  
ATOM    684  CB  ARG A  97      43.852  43.763  -1.814  1.00 23.23           C  
ATOM    685  CG  ARG A  97      42.400  44.102  -1.512  1.00 27.62           C  
ATOM    686  CD  ARG A  97      42.266  44.832  -0.160  1.00 35.14           C  
ATOM    687  NE  ARG A  97      42.286  46.285  -0.318  1.00 41.23           N  
ATOM    688  CZ  ARG A  97      41.222  47.086  -0.199  1.00 44.32           C  
ATOM    689  NH1 ARG A  97      40.012  46.600   0.096  1.00 44.89           N  
ATOM    690  NH2 ARG A  97      41.374  48.397  -0.372  1.00 45.89           N  
ATOM    691  N   ALA A  98      46.333  43.102  -3.714  1.00 20.30           N  
ATOM    692  CA  ALA A  98      47.719  42.689  -3.922  1.00 20.00           C  
ATOM    693  C   ALA A  98      48.631  43.878  -3.921  1.00 19.91           C  
ATOM    694  O   ALA A  98      48.197  44.983  -4.225  1.00 20.01           O  
ATOM    695  CB  ALA A  98      47.876  41.937  -5.219  1.00 19.94           C  
ATOM    696  N   ASN A  99      49.892  43.639  -3.570  1.00 19.56           N  
ATOM    697  CA  ASN A  99      50.926  44.637  -3.677  1.00 19.92           C  
ATOM    698  C   ASN A  99      52.144  44.053  -4.366  1.00 20.44           C  
ATOM    699  O   ASN A  99      52.608  42.957  -4.032  1.00 20.67           O  
ATOM    700  CB  ASN A  99      51.408  45.087  -2.296  1.00 20.10           C  
ATOM    701  CG  ASN A  99      50.355  45.815  -1.469  1.00 20.29           C  
ATOM    702  OD1 ASN A  99      49.172  45.989  -1.852  1.00 19.58           O  
ATOM    703  ND2 ASN A  99      50.797  46.239  -0.285  1.00 19.59           N  
ATOM    704  N   PHE A 100      52.716  44.799  -5.292  1.00 20.91           N  
ATOM    705  CA  PHE A 100      54.049  44.451  -5.735  1.00 21.38           C  
ATOM    706  C   PHE A 100      54.989  44.828  -4.626  1.00 22.13           C  
ATOM    707  O   PHE A 100      54.919  45.945  -4.131  1.00 22.35           O  
ATOM    708  CB  PHE A 100      54.402  45.191  -7.012  1.00 21.10           C  
ATOM    709  CG  PHE A 100      53.694  44.676  -8.198  1.00 19.11           C  
ATOM    710  CD1 PHE A 100      52.577  45.336  -8.689  1.00 20.01           C  
ATOM    711  CD2 PHE A 100      54.111  43.504  -8.802  1.00 17.26           C  
ATOM    712  CE1 PHE A 100      51.890  44.844  -9.798  1.00 19.51           C  
ATOM    713  CE2 PHE A 100      53.444  42.999  -9.888  1.00 18.28           C  
ATOM    714  CZ  PHE A 100      52.328  43.677 -10.398  1.00 18.72           C  
ATOM    715  N   ALA A 101      55.838  43.889  -4.221  1.00 23.07           N  
ATOM    716  CA  ALA A 101      56.788  44.109  -3.138  1.00 23.78           C  
ATOM    717  C   ALA A 101      58.218  43.626  -3.435  1.00 25.07           C  
ATOM    718  O   ALA A 101      58.458  42.800  -4.328  1.00 24.91           O  
ATOM    719  CB  ALA A 101      56.274  43.488  -1.891  1.00 23.10           C  
ATOM    720  N   THR A 102      59.161  44.155  -2.664  1.00 26.79           N  
ATOM    721  CA  THR A 102      60.572  43.813  -2.782  1.00 28.83           C  
ATOM    722  C   THR A 102      60.869  42.757  -1.745  1.00 30.30           C  
ATOM    723  O   THR A 102      60.405  42.861  -0.599  1.00 31.30           O  
ATOM    724  CB  THR A 102      61.470  45.063  -2.557  1.00 29.01           C  
ATOM    725  OG1 THR A 102      61.059  46.109  -3.450  1.00 29.82           O  
ATOM    726  CG2 THR A 102      62.946  44.763  -2.809  1.00 28.36           C  
ATOM    727  N   ASN A 103      61.630  41.742  -2.150  1.00 31.71           N  
ATOM    728  CA  ASN A 103      61.921  40.559  -1.332  1.00 32.90           C  
ATOM    729  C   ASN A 103      63.388  40.252  -1.604  1.00 34.14           C  
ATOM    730  O   ASN A 103      63.727  39.665  -2.637  1.00 34.19           O  
ATOM    731  CB  ASN A 103      60.967  39.403  -1.747  1.00 32.73           C  
ATOM    732  CG  ASN A 103      61.256  38.054  -1.052  1.00 31.80           C  
ATOM    733  OD1 ASN A 103      62.369  37.766  -0.608  1.00 31.90           O  
ATOM    734  ND2 ASN A 103      60.235  37.207  -1.002  1.00 29.04           N  
ATOM    735  N   ARG A 104      64.263  40.713  -0.715  1.00 35.77           N  
ATOM    736  CA  ARG A 104      65.687  40.433  -0.861  1.00 37.49           C  
ATOM    737  C   ARG A 104      65.973  39.267   0.023  1.00 37.95           C  
ATOM    738  O   ARG A 104      65.801  39.352   1.252  1.00 38.33           O  
ATOM    739  CB  ARG A 104      66.574  41.611  -0.466  1.00 37.78           C  
ATOM    740  CG  ARG A 104      66.487  42.802  -1.399  1.00 40.66           C  
ATOM    741  CD  ARG A 104      67.709  43.715  -1.233  1.00 46.18           C  
ATOM    742  NE  ARG A 104      67.351  45.139  -1.143  1.00 50.04           N  
ATOM    743  CZ  ARG A 104      67.202  45.820   0.000  1.00 52.50           C  
ATOM    744  NH1 ARG A 104      66.877  47.113  -0.036  1.00 53.06           N  
ATOM    745  NH2 ARG A 104      67.376  45.220   1.186  1.00 53.78           N  
ATOM    746  N   ASP A 105      66.402  38.184  -0.627  1.00 38.64           N  
ATOM    747  CA  ASP A 105      66.627  36.855  -0.009  1.00 39.02           C  
ATOM    748  C   ASP A 105      65.647  36.481   1.134  1.00 38.12           C  
ATOM    749  O   ASP A 105      65.941  36.636   2.323  1.00 37.92           O  
ATOM    750  CB  ASP A 105      68.127  36.606   0.330  1.00 39.61           C  
ATOM    751  CG  ASP A 105      68.769  37.745   1.171  1.00 41.34           C  
ATOM    752  OD1 ASP A 105      68.510  37.829   2.407  1.00 43.32           O  
ATOM    753  OD2 ASP A 105      69.561  38.533   0.600  1.00 41.27           O  
ATOM    754  N   GLY A 106      64.457  36.037   0.732  1.00 37.42           N  
ATOM    755  CA  GLY A 106      63.464  35.483   1.656  1.00 36.06           C  
ATOM    756  C   GLY A 106      62.784  36.437   2.626  1.00 34.85           C  
ATOM    757  O   GLY A 106      61.904  36.019   3.369  1.00 35.13           O  
ATOM    758  N   VAL A 107      63.173  37.705   2.636  1.00 33.38           N  
ATOM    759  CA  VAL A 107      62.569  38.659   3.571  1.00 32.41           C  
ATOM    760  C   VAL A 107      61.914  39.838   2.822  1.00 31.57           C  
ATOM    761  O   VAL A 107      62.486  40.365   1.855  1.00 31.82           O  
ATOM    762  CB  VAL A 107      63.612  39.170   4.640  1.00 32.59           C  
ATOM    763  CG1 VAL A 107      62.998  40.210   5.584  1.00 32.17           C  
ATOM    764  CG2 VAL A 107      64.217  38.002   5.435  1.00 32.11           C  
ATOM    765  N   ILE A 108      60.715  40.232   3.262  1.00 30.23           N  
ATOM    766  CA  ILE A 108      60.039  41.427   2.723  1.00 29.08           C  
ATOM    767  C   ILE A 108      60.636  42.708   3.303  1.00 28.52           C  
ATOM    768  O   ILE A 108      60.457  43.026   4.483  1.00 27.89           O  
ATOM    769  CB  ILE A 108      58.488  41.435   2.918  1.00 28.62           C  
ATOM    770  CG1 ILE A 108      57.854  40.145   2.403  1.00 27.85           C  
ATOM    771  CG2 ILE A 108      57.880  42.654   2.248  1.00 27.39           C  
ATOM    772  CD1 ILE A 108      58.330  39.684   1.036  1.00 27.12           C  
ATOM    773  N   VAL A 109      61.319  43.434   2.428  1.00 28.01           N  
ATOM    774  CA  VAL A 109      62.118  44.582   2.783  1.00 27.63           C  
ATOM    775  C   VAL A 109      61.332  45.861   2.564  1.00 27.87           C  
ATOM    776  O   VAL A 109      61.468  46.806   3.340  1.00 27.86           O  
ATOM    777  CB  VAL A 109      63.418  44.537   1.993  1.00 27.59           C  
ATOM    778  CG1 VAL A 109      63.732  45.848   1.319  1.00 27.57           C  
ATOM    779  CG2 VAL A 109      64.532  44.041   2.894  1.00 27.46           C  
ATOM    780  N   ASP A 110      60.469  45.869   1.548  1.00 28.03           N  
ATOM    781  CA  ASP A 110      59.564  46.996   1.307  1.00 28.38           C  
ATOM    782  C   ASP A 110      58.246  46.483   0.770  1.00 27.99           C  
ATOM    783  O   ASP A 110      58.206  46.008  -0.359  1.00 28.60           O  
ATOM    784  CB  ASP A 110      60.189  47.939   0.269  1.00 29.05           C  
ATOM    785  CG  ASP A 110      59.432  49.252   0.117  1.00 29.41           C  
ATOM    786  OD1 ASP A 110      58.200  49.234  -0.115  1.00 30.18           O  
ATOM    787  OD2 ASP A 110      60.095  50.310   0.211  1.00 31.18           O  
ATOM    788  N   ARG A 111      57.166  46.614   1.531  1.00 27.28           N  
ATOM    789  CA  ARG A 111      55.892  45.981   1.144  1.00 26.82           C  
ATOM    790  C   ARG A 111      55.203  46.637  -0.027  1.00 26.73           C  
ATOM    791  O   ARG A 111      54.047  46.333  -0.307  1.00 26.82           O  
ATOM    792  CB  ARG A 111      54.895  46.003   2.301  1.00 27.04           C  
ATOM    793  CG  ARG A 111      54.975  44.857   3.266  1.00 25.71           C  
ATOM    794  CD  ARG A 111      54.004  45.083   4.387  1.00 25.50           C  
ATOM    795  NE  ARG A 111      52.613  44.948   3.952  1.00 27.27           N  
ATOM    796  CZ  ARG A 111      51.766  45.956   3.719  1.00 26.34           C  
ATOM    797  NH1 ARG A 111      52.148  47.218   3.864  1.00 24.43           N  
ATOM    798  NH2 ARG A 111      50.523  45.689   3.334  1.00 25.32           N  
ATOM    799  N   ARG A 112      55.896  47.544  -0.700  1.00 26.77           N  
ATOM    800  CA  ARG A 112      55.298  48.320  -1.769  1.00 26.71           C  
ATOM    801  C   ARG A 112      56.248  48.514  -2.948  1.00 26.75           C  
ATOM    802  O   ARG A 112      55.926  49.247  -3.883  1.00 27.14           O  
ATOM    803  CB  ARG A 112      54.862  49.687  -1.244  1.00 26.61           C  
ATOM    804  CG  ARG A 112      53.614  49.707  -0.397  1.00 27.79           C  
ATOM    805  CD  ARG A 112      53.447  51.059   0.281  1.00 30.00           C  
ATOM    806  NE  ARG A 112      52.874  50.904   1.614  1.00 34.10           N  
ATOM    807  CZ  ARG A 112      51.569  50.959   1.875  1.00 37.48           C  
ATOM    808  NH1 ARG A 112      50.687  51.195   0.905  1.00 39.50           N  
ATOM    809  NH2 ARG A 112      51.134  50.796   3.114  1.00 37.43           N  
ATOM    810  N   ALA A 113      57.412  47.869  -2.928  1.00 26.63           N  
ATOM    811  CA  ALA A 113      58.449  48.151  -3.943  1.00 26.80           C  
ATOM    812  C   ALA A 113      58.647  49.672  -4.115  1.00 27.15           C  
ATOM    813  O   ALA A 113      58.761  50.182  -5.226  1.00 27.48           O  
ATOM    814  CB  ALA A 113      58.113  47.484  -5.267  1.00 26.14           C  
ATOM    815  N   GLY A 114      58.658  50.386  -2.990  1.00 27.50           N  
ATOM    816  CA  GLY A 114      58.865  51.819  -2.963  1.00 27.92           C  
ATOM    817  C   GLY A 114      57.786  52.655  -3.627  1.00 28.50           C  
ATOM    818  O   GLY A 114      57.949  53.858  -3.772  1.00 28.73           O  
ATOM    819  N   ARG A 115      56.681  52.031  -4.020  1.00 28.87           N  
ATOM    820  CA  ARG A 115      55.646  52.690  -4.824  1.00 29.29           C  
ATOM    821  C   ARG A 115      56.118  52.959  -6.274  1.00 29.82           C  
ATOM    822  O   ARG A 115      55.566  53.804  -6.977  1.00 29.97           O  
ATOM    823  CB  ARG A 115      55.123  53.959  -4.129  1.00 29.16           C  
ATOM    824  CG  ARG A 115      54.517  53.714  -2.751  1.00 29.71           C  
ATOM    825  CD  ARG A 115      54.050  55.003  -2.053  1.00 31.30           C  
ATOM    826  NE  ARG A 115      54.456  55.002  -0.640  1.00 33.46           N  
ATOM    827  CZ  ARG A 115      53.680  54.670   0.395  1.00 34.99           C  
ATOM    828  NH1 ARG A 115      52.405  54.316   0.226  1.00 34.32           N  
ATOM    829  NH2 ARG A 115      54.188  54.689   1.623  1.00 35.90           N  
ATOM    830  N   GLU A 116      57.134  52.232  -6.733  1.00 30.42           N  
ATOM    831  CA  GLU A 116      57.537  52.331  -8.130  1.00 31.35           C  
ATOM    832  C   GLU A 116      56.355  51.887  -8.956  1.00 31.49           C  
ATOM    833  O   GLU A 116      55.746  50.883  -8.628  1.00 31.81           O  
ATOM    834  CB  GLU A 116      58.716  51.406  -8.424  1.00 31.48           C  
ATOM    835  CG  GLU A 116      60.022  51.760  -7.703  1.00 33.99           C  
ATOM    836  CD  GLU A 116      60.683  53.041  -8.223  1.00 36.77           C  
ATOM    837  OE1 GLU A 116      60.536  53.332  -9.428  1.00 38.34           O  
ATOM    838  OE2 GLU A 116      61.349  53.751  -7.425  1.00 37.14           O  
ATOM    839  N   ASN A 117      55.996  52.627 -10.003  1.00 32.06           N  
ATOM    840  CA  ASN A 117      54.963  52.108 -10.918  1.00 32.44           C  
ATOM    841  C   ASN A 117      55.472  51.661 -12.277  1.00 31.91           C  
ATOM    842  O   ASN A 117      54.852  50.830 -12.918  1.00 31.42           O  
ATOM    843  CB  ASN A 117      53.740  53.037 -11.079  1.00 32.97           C  
ATOM    844  CG  ASN A 117      52.584  52.352 -11.849  1.00 34.33           C  
ATOM    845  OD1 ASN A 117      52.589  52.299 -13.082  1.00 35.33           O  
ATOM    846  ND2 ASN A 117      51.609  51.811 -11.116  1.00 34.97           N  
ATOM    847  N   LYS A 118      56.606  52.209 -12.693  1.00 32.01           N  
ATOM    848  CA  LYS A 118      57.089  52.059 -14.053  1.00 32.25           C  
ATOM    849  C   LYS A 118      57.407  50.598 -14.429  1.00 32.05           C  
ATOM    850  O   LYS A 118      58.335  49.981 -13.899  1.00 32.22           O  
ATOM    851  CB  LYS A 118      58.292  52.979 -14.244  1.00 32.87           C  
ATOM    852  CG  LYS A 118      58.339  53.694 -15.581  1.00 35.37           C  
ATOM    853  CD  LYS A 118      59.074  52.847 -16.631  1.00 40.19           C  
ATOM    854  CE  LYS A 118      58.934  53.452 -18.023  1.00 44.14           C  
ATOM    855  NZ  LYS A 118      59.709  54.737 -18.114  1.00 46.91           N  
ATOM    856  N   GLY A 119      56.620  50.041 -15.337  1.00 31.73           N  
ATOM    857  CA  GLY A 119      56.821  48.671 -15.766  1.00 31.76           C  
ATOM    858  C   GLY A 119      55.975  47.663 -15.007  1.00 32.22           C  
ATOM    859  O   GLY A 119      56.072  46.451 -15.256  1.00 32.47           O  
ATOM    860  N   ASN A 120      55.150  48.132 -14.075  1.00 31.99           N  
ATOM    861  CA  ASN A 120      54.352  47.205 -13.290  1.00 32.39           C  
ATOM    862  C   ASN A 120      53.371  46.441 -14.162  1.00 32.39           C  
ATOM    863  O   ASN A 120      53.258  45.228 -14.052  1.00 32.68           O  
ATOM    864  CB  ASN A 120      53.576  47.897 -12.163  1.00 32.72           C  
ATOM    865  CG  ASN A 120      54.423  48.191 -10.929  1.00 32.93           C  
ATOM    866  OD1 ASN A 120      55.614  47.884 -10.849  1.00 31.35           O  
ATOM    867  ND2 ASN A 120      53.784  48.803  -9.952  1.00 34.89           N  
ATOM    868  N   GLU A 121      52.665  47.139 -15.034  1.00 32.24           N  
ATOM    869  CA  GLU A 121      51.671  46.476 -15.876  1.00 32.68           C  
ATOM    870  C   GLU A 121      52.245  45.289 -16.692  1.00 31.58           C  
ATOM    871  O   GLU A 121      51.532  44.334 -17.000  1.00 31.59           O  
ATOM    872  CB  GLU A 121      51.006  47.493 -16.793  1.00 33.20           C  
ATOM    873  CG  GLU A 121      52.016  48.343 -17.542  1.00 37.52           C  
ATOM    874  CD  GLU A 121      51.377  49.146 -18.663  1.00 43.71           C  
ATOM    875  OE1 GLU A 121      50.419  48.628 -19.314  1.00 45.96           O  
ATOM    876  OE2 GLU A 121      51.848  50.294 -18.894  1.00 45.12           O  
ATOM    877  N   GLU A 122      53.532  45.346 -17.014  1.00 30.30           N  
ATOM    878  CA  GLU A 122      54.189  44.268 -17.723  1.00 29.39           C  
ATOM    879  C   GLU A 122      54.511  43.130 -16.784  1.00 28.12           C  
ATOM    880  O   GLU A 122      54.460  41.961 -17.178  1.00 27.99           O  
ATOM    881  CB  GLU A 122      55.465  44.773 -18.376  1.00 30.11           C  
ATOM    882  CG  GLU A 122      55.240  45.932 -19.322  1.00 33.23           C  
ATOM    883  CD  GLU A 122      56.524  46.666 -19.639  1.00 39.14           C  
ATOM    884  OE1 GLU A 122      56.464  47.926 -19.741  1.00 41.34           O  
ATOM    885  OE2 GLU A 122      57.584  45.982 -19.780  1.00 41.25           O  
ATOM    886  N   LEU A 123      54.857  43.477 -15.545  1.00 26.67           N  
ATOM    887  CA  LEU A 123      55.008  42.498 -14.483  1.00 25.26           C  
ATOM    888  C   LEU A 123      53.663  41.848 -14.183  1.00 25.00           C  
ATOM    889  O   LEU A 123      53.558  40.638 -14.061  1.00 24.84           O  
ATOM    890  CB  LEU A 123      55.539  43.156 -13.223  1.00 24.86           C  
ATOM    891  CG  LEU A 123      56.926  43.786 -13.192  1.00 23.52           C  
ATOM    892  CD1 LEU A 123      57.139  44.405 -11.815  1.00 20.16           C  
ATOM    893  CD2 LEU A 123      58.004  42.760 -13.508  1.00 20.72           C  
ATOM    894  N   ALA A 124      52.626  42.665 -14.074  1.00 24.79           N  
ATOM    895  CA  ALA A 124      51.288  42.157 -13.881  1.00 24.51           C  
ATOM    896  C   ALA A 124      51.001  41.123 -14.945  1.00 24.84           C  
ATOM    897  O   ALA A 124      50.493  40.044 -14.621  1.00 24.97           O  
ATOM    898  CB  ALA A 124      50.288  43.266 -13.937  1.00 24.00           C  
ATOM    899  N   ASP A 125      51.345  41.432 -16.202  1.00 24.91           N  
ATOM    900  CA  ASP A 125      51.045  40.516 -17.324  1.00 25.31           C  
ATOM    901  C   ASP A 125      51.789  39.201 -17.193  1.00 24.59           C  
ATOM    902  O   ASP A 125      51.208  38.146 -17.372  1.00 25.03           O  
ATOM    903  CB  ASP A 125      51.362  41.122 -18.702  1.00 25.79           C  
ATOM    904  CG  ASP A 125      50.384  42.243 -19.123  1.00 28.54           C  
ATOM    905  OD1 ASP A 125      49.195  42.245 -18.704  1.00 30.12           O  
ATOM    906  OD2 ASP A 125      50.829  43.130 -19.900  1.00 30.69           O  
ATOM    907  N   ALA A 126      53.073  39.275 -16.872  1.00 23.72           N  
ATOM    908  CA  ALA A 126      53.931  38.107 -16.888  1.00 22.78           C  
ATOM    909  C   ALA A 126      53.502  37.063 -15.865  1.00 22.67           C  
ATOM    910  O   ALA A 126      53.879  35.894 -15.977  1.00 22.87           O  
ATOM    911  CB  ALA A 126      55.351  38.518 -16.646  1.00 22.35           C  
ATOM    912  N   ILE A 127      52.734  37.477 -14.858  1.00 22.02           N  
ATOM    913  CA  ILE A 127      52.260  36.534 -13.858  1.00 21.42           C  
ATOM    914  C   ILE A 127      50.767  36.308 -13.975  1.00 22.38           C  
ATOM    915  O   ILE A 127      50.156  35.736 -13.075  1.00 22.21           O  
ATOM    916  CB  ILE A 127      52.629  36.936 -12.450  1.00 20.74           C  
ATOM    917  CG1 ILE A 127      52.236  38.382 -12.180  1.00 19.76           C  
ATOM    918  CG2 ILE A 127      54.098  36.745 -12.260  1.00 20.64           C  
ATOM    919  CD1 ILE A 127      51.881  38.665 -10.785  1.00 16.11           C  
ATOM    920  N   SER A 128      50.195  36.764 -15.090  1.00 23.23           N  
ATOM    921  CA  SER A 128      48.856  36.400 -15.476  1.00 24.56           C  
ATOM    922  C   SER A 128      48.918  35.200 -16.418  1.00 25.95           C  
ATOM    923  O   SER A 128      49.468  35.291 -17.519  1.00 25.95           O  
ATOM    924  CB  SER A 128      48.161  37.585 -16.119  1.00 24.25           C  
ATOM    925  OG  SER A 128      47.930  38.591 -15.145  1.00 25.81           O  
ATOM    926  N   LEU A 129      48.365  34.063 -15.985  1.00 27.67           N  
ATOM    927  CA  LEU A 129      48.570  32.827 -16.710  1.00 29.19           C  
ATOM    928  C   LEU A 129      47.667  31.700 -16.313  1.00 30.79           C  
ATOM    929  O   LEU A 129      47.244  31.620 -15.182  1.00 31.10           O  
ATOM    930  CB  LEU A 129      50.014  32.364 -16.538  1.00 29.43           C  
ATOM    931  CG  LEU A 129      50.695  32.508 -15.183  1.00 28.45           C  
ATOM    932  CD1 LEU A 129      50.362  31.339 -14.302  1.00 29.13           C  
ATOM    933  CD2 LEU A 129      52.174  32.578 -15.412  1.00 27.20           C  
ATOM    934  N   ASP A 130      47.415  30.820 -17.280  1.00 33.10           N  
ATOM    935  CA  ASP A 130      46.686  29.571 -17.116  1.00 34.95           C  
ATOM    936  C   ASP A 130      47.660  28.508 -16.701  1.00 36.61           C  
ATOM    937  O   ASP A 130      48.631  28.246 -17.405  1.00 37.18           O  
ATOM    938  CB  ASP A 130      46.131  29.106 -18.450  1.00 34.71           C  
ATOM    939  CG  ASP A 130      44.721  29.549 -18.690  1.00 35.43           C  
ATOM    940  OD1 ASP A 130      44.510  30.754 -18.935  1.00 35.26           O  
ATOM    941  OD2 ASP A 130      43.815  28.681 -18.660  1.00 37.14           O  
HETATM  942  N   MSE A 131      47.386  27.870 -15.573  1.00 38.59           N  
HETATM  943  CA  MSE A 131      48.152  26.720 -15.130  1.00 40.28           C  
HETATM  944  C   MSE A 131      47.215  25.494 -15.117  1.00 40.32           C  
HETATM  945  O   MSE A 131      46.996  24.865 -14.061  1.00 40.80           O  
HETATM  946  CB  MSE A 131      48.692  27.000 -13.748  1.00 40.92           C  
HETATM  947  CG  MSE A 131      50.164  26.910 -13.601  1.00 44.66           C  
HETATM  948 SE   MSE A 131      50.383  27.490 -11.763  1.00 57.83          SE  
HETATM  949  CE  MSE A 131      49.117  26.259 -10.850  1.00 52.44           C  
ATOM    950  N   GLY A 132      46.658  25.183 -16.296  1.00 39.88           N  
ATOM    951  CA  GLY A 132      45.712  24.085 -16.469  1.00 39.27           C  
ATOM    952  C   GLY A 132      44.280  24.420 -16.093  1.00 38.86           C  
ATOM    953  O   GLY A 132      43.591  25.158 -16.807  1.00 39.02           O  
ATOM    954  N   GLU A 133      43.834  23.884 -14.960  1.00 38.18           N  
ATOM    955  CA  GLU A 133      42.422  23.976 -14.572  1.00 37.76           C  
ATOM    956  C   GLU A 133      42.128  25.265 -13.779  1.00 36.65           C  
ATOM    957  O   GLU A 133      40.973  25.552 -13.440  1.00 36.62           O  
ATOM    958  CB  GLU A 133      41.965  22.677 -13.841  1.00 38.12           C  
ATOM    959  CG  GLU A 133      41.969  22.721 -12.288  1.00 40.51           C  
ATOM    960  CD  GLU A 133      42.149  21.352 -11.591  1.00 43.20           C  
ATOM    961  OE1 GLU A 133      43.144  20.652 -11.898  1.00 43.21           O  
ATOM    962  OE2 GLU A 133      41.318  21.004 -10.701  1.00 43.82           O  
ATOM    963  N   TYR A 134      43.180  26.035 -13.505  1.00 35.35           N  
ATOM    964  CA  TYR A 134      43.068  27.280 -12.758  1.00 34.21           C  
ATOM    965  C   TYR A 134      43.645  28.409 -13.557  1.00 33.48           C  
ATOM    966  O   TYR A 134      44.690  28.254 -14.176  1.00 33.46           O  
ATOM    967  CB  TYR A 134      43.846  27.200 -11.453  1.00 34.04           C  
ATOM    968  CG  TYR A 134      43.304  26.201 -10.479  1.00 34.05           C  
ATOM    969  CD1 TYR A 134      42.177  26.494  -9.694  1.00 33.86           C  
ATOM    970  CD2 TYR A 134      43.918  24.959 -10.323  1.00 33.80           C  
ATOM    971  CE1 TYR A 134      41.669  25.554  -8.789  1.00 33.16           C  
ATOM    972  CE2 TYR A 134      43.419  24.019  -9.423  1.00 32.95           C  
ATOM    973  CZ  TYR A 134      42.302  24.328  -8.668  1.00 32.81           C  
ATOM    974  OH  TYR A 134      41.834  23.402  -7.792  1.00 33.72           O  
ATOM    975  N   SER A 135      42.986  29.557 -13.521  1.00 32.56           N  
ATOM    976  CA  SER A 135      43.500  30.718 -14.217  1.00 31.88           C  
ATOM    977  C   SER A 135      43.737  31.917 -13.343  1.00 31.01           C  
ATOM    978  O   SER A 135      42.913  32.248 -12.493  1.00 31.20           O  
ATOM    979  CB  SER A 135      42.595  31.087 -15.359  1.00 32.02           C  
ATOM    980  OG  SER A 135      43.182  30.539 -16.510  1.00 34.20           O  
ATOM    981  N   PHE A 136      44.867  32.571 -13.583  1.00 29.90           N  
ATOM    982  CA  PHE A 136      45.335  33.670 -12.765  1.00 29.03           C  
ATOM    983  C   PHE A 136      45.486  34.930 -13.578  1.00 28.94           C  
ATOM    984  O   PHE A 136      46.180  34.942 -14.589  1.00 28.72           O  
ATOM    985  CB  PHE A 136      46.670  33.310 -12.141  1.00 28.75           C  
ATOM    986  CG  PHE A 136      46.625  32.077 -11.325  1.00 27.58           C  
ATOM    987  CD1 PHE A 136      46.810  30.836 -11.918  1.00 27.70           C  
ATOM    988  CD2 PHE A 136      46.386  32.146  -9.970  1.00 26.93           C  
ATOM    989  CE1 PHE A 136      46.763  29.663 -11.173  1.00 27.55           C  
ATOM    990  CE2 PHE A 136      46.327  30.985  -9.208  1.00 28.73           C  
ATOM    991  CZ  PHE A 136      46.525  29.733  -9.810  1.00 28.37           C  
ATOM    992  N   ARG A 137      44.827  35.991 -13.125  1.00 29.14           N  
ATOM    993  CA  ARG A 137      44.913  37.301 -13.773  1.00 29.63           C  
ATOM    994  C   ARG A 137      45.246  38.402 -12.767  1.00 29.08           C  
ATOM    995  O   ARG A 137      44.519  38.630 -11.805  1.00 28.66           O  
ATOM    996  CB  ARG A 137      43.627  37.627 -14.533  1.00 29.79           C  
ATOM    997  CG  ARG A 137      43.440  36.844 -15.820  1.00 32.29           C  
ATOM    998  CD  ARG A 137      42.087  37.165 -16.448  1.00 37.95           C  
ATOM    999  NE  ARG A 137      40.946  36.686 -15.649  1.00 41.64           N  
ATOM   1000  CZ  ARG A 137      39.822  37.375 -15.412  1.00 42.79           C  
ATOM   1001  NH1 ARG A 137      38.861  36.832 -14.671  1.00 42.60           N  
ATOM   1002  NH2 ARG A 137      39.655  38.609 -15.898  1.00 45.19           N  
ATOM   1003  N   VAL A 138      46.376  39.054 -12.995  1.00 29.01           N  
ATOM   1004  CA  VAL A 138      46.791  40.175 -12.188  1.00 29.07           C  
ATOM   1005  C   VAL A 138      46.765  41.421 -13.050  1.00 29.32           C  
ATOM   1006  O   VAL A 138      47.310  41.421 -14.157  1.00 29.39           O  
ATOM   1007  CB  VAL A 138      48.221  39.980 -11.680  1.00 29.29           C  
ATOM   1008  CG1 VAL A 138      48.727  41.262 -11.011  1.00 28.03           C  
ATOM   1009  CG2 VAL A 138      48.305  38.757 -10.744  1.00 28.79           C  
ATOM   1010  N   LYS A 139      46.118  42.467 -12.551  1.00 29.51           N  
ATOM   1011  CA  LYS A 139      46.158  43.787 -13.178  1.00 30.08           C  
ATOM   1012  C   LYS A 139      46.750  44.774 -12.190  1.00 29.83           C  
ATOM   1013  O   LYS A 139      46.524  44.658 -10.994  1.00 30.08           O  
ATOM   1014  CB  LYS A 139      44.754  44.237 -13.569  1.00 30.53           C  
ATOM   1015  CG  LYS A 139      44.692  45.498 -14.426  1.00 32.36           C  
ATOM   1016  CD  LYS A 139      43.328  45.597 -15.100  1.00 34.79           C  
ATOM   1017  CE  LYS A 139      43.144  46.917 -15.845  1.00 35.01           C  
ATOM   1018  NZ  LYS A 139      43.617  46.834 -17.246  1.00 36.27           N  
ATOM   1019  N   SER A 140      47.499  45.749 -12.690  1.00 29.88           N  
ATOM   1020  CA  SER A 140      48.150  46.746 -11.838  1.00 29.47           C  
ATOM   1021  C   SER A 140      47.477  48.127 -11.864  1.00 29.48           C  
ATOM   1022  O   SER A 140      46.920  48.545 -12.884  1.00 29.24           O  
ATOM   1023  CB  SER A 140      49.594  46.879 -12.262  1.00 29.35           C  
ATOM   1024  OG  SER A 140      50.018  48.219 -12.176  1.00 30.77           O  
ATOM   1025  N   GLY A 141      47.555  48.840 -10.740  1.00 29.71           N  
ATOM   1026  CA  GLY A 141      46.934  50.164 -10.594  1.00 29.80           C  
ATOM   1027  C   GLY A 141      47.924  51.287 -10.376  1.00 29.88           C  
ATOM   1028  O   GLY A 141      48.983  51.325 -11.008  1.00 30.05           O  
ATOM   1029  N   VAL A 142      47.571  52.217  -9.493  1.00 30.21           N  
ATOM   1030  CA  VAL A 142      48.485  53.293  -9.105  1.00 30.28           C  
ATOM   1031  C   VAL A 142      49.522  52.733  -8.107  1.00 30.46           C  
ATOM   1032  O   VAL A 142      49.182  51.986  -7.167  1.00 30.16           O  
ATOM   1033  CB  VAL A 142      47.728  54.535  -8.535  1.00 30.22           C  
ATOM   1034  CG1 VAL A 142      46.559  54.915  -9.433  1.00 30.14           C  
ATOM   1035  CG2 VAL A 142      47.200  54.283  -7.112  1.00 30.99           C  
ATOM   1036  N   GLU A 143      50.785  53.089  -8.336  1.00 30.49           N  
ATOM   1037  CA  GLU A 143      51.914  52.649  -7.509  1.00 30.32           C  
ATOM   1038  C   GLU A 143      51.944  51.120  -7.385  1.00 29.94           C  
ATOM   1039  O   GLU A 143      51.721  50.428  -8.367  1.00 30.64           O  
ATOM   1040  CB  GLU A 143      51.912  53.366  -6.152  1.00 30.55           C  
ATOM   1041  CG  GLU A 143      52.093  54.876  -6.253  1.00 31.59           C  
ATOM   1042  CD  GLU A 143      51.662  55.617  -4.992  1.00 35.42           C  
ATOM   1043  OE1 GLU A 143      50.677  55.196  -4.343  1.00 37.93           O  
ATOM   1044  OE2 GLU A 143      52.305  56.630  -4.645  1.00 36.65           O  
ATOM   1045  N   HIS A 144      52.211  50.602  -6.191  1.00 29.37           N  
ATOM   1046  CA  HIS A 144      52.314  49.158  -5.916  1.00 28.60           C  
ATOM   1047  C   HIS A 144      50.966  48.412  -6.041  1.00 28.09           C  
ATOM   1048  O   HIS A 144      50.903  47.195  -5.936  1.00 28.06           O  
ATOM   1049  CB  HIS A 144      52.771  49.027  -4.474  1.00 28.21           C  
ATOM   1050  CG  HIS A 144      51.861  49.744  -3.555  1.00 27.53           C  
ATOM   1051  ND1 HIS A 144      50.866  49.098  -2.856  1.00 27.77           N  
ATOM   1052  CD2 HIS A 144      51.678  51.067  -3.347  1.00 27.04           C  
ATOM   1053  CE1 HIS A 144      50.148  49.989  -2.197  1.00 28.65           C  
ATOM   1054  NE2 HIS A 144      50.625  51.191  -2.474  1.00 29.74           N  
ATOM   1055  N   ARG A 145      49.886  49.148  -6.218  1.00 27.76           N  
ATOM   1056  CA  ARG A 145      48.556  48.574  -6.082  1.00 27.59           C  
ATOM   1057  C   ARG A 145      48.215  47.611  -7.216  1.00 26.71           C  
ATOM   1058  O   ARG A 145      48.461  47.916  -8.379  1.00 27.15           O  
ATOM   1059  CB  ARG A 145      47.495  49.677  -5.911  1.00 27.97           C  
ATOM   1060  CG  ARG A 145      47.240  50.030  -4.443  1.00 29.57           C  
ATOM   1061  CD  ARG A 145      46.264  51.188  -4.266  1.00 32.20           C  
ATOM   1062  NE  ARG A 145      46.995  52.452  -4.167  1.00 36.15           N  
ATOM   1063  CZ  ARG A 145      47.116  53.202  -3.069  1.00 36.00           C  
ATOM   1064  NH1 ARG A 145      46.522  52.860  -1.924  1.00 36.81           N  
ATOM   1065  NH2 ARG A 145      47.822  54.323  -3.136  1.00 35.85           N  
ATOM   1066  N   ALA A 146      47.689  46.442  -6.841  1.00 25.49           N  
ATOM   1067  CA  ALA A 146      47.358  45.354  -7.749  1.00 24.10           C  
ATOM   1068  C   ALA A 146      46.192  44.532  -7.216  1.00 23.50           C  
ATOM   1069  O   ALA A 146      45.851  44.611  -6.035  1.00 23.08           O  
ATOM   1070  CB  ALA A 146      48.555  44.466  -7.930  1.00 23.99           C  
ATOM   1071  N   ALA A 147      45.576  43.751  -8.098  1.00 23.00           N  
ATOM   1072  CA  ALA A 147      44.660  42.684  -7.671  1.00 22.77           C  
ATOM   1073  C   ALA A 147      44.844  41.384  -8.468  1.00 22.52           C  
ATOM   1074  O   ALA A 147      45.119  41.392  -9.666  1.00 22.24           O  
ATOM   1075  CB  ALA A 147      43.216  43.136  -7.715  1.00 22.56           C  
ATOM   1076  N   LEU A 148      44.713  40.269  -7.762  1.00 22.30           N  
ATOM   1077  CA  LEU A 148      44.704  38.962  -8.376  1.00 22.07           C  
ATOM   1078  C   LEU A 148      43.297  38.355  -8.383  1.00 21.72           C  
ATOM   1079  O   LEU A 148      42.610  38.321  -7.354  1.00 21.41           O  
ATOM   1080  CB  LEU A 148      45.668  38.058  -7.630  1.00 21.98           C  
ATOM   1081  CG  LEU A 148      45.524  36.571  -7.879  1.00 22.08           C  
ATOM   1082  CD1 LEU A 148      45.910  36.256  -9.308  1.00 24.02           C  
ATOM   1083  CD2 LEU A 148      46.431  35.850  -6.920  1.00 23.62           C  
ATOM   1084  N   VAL A 149      42.866  37.898  -9.554  1.00 21.51           N  
ATOM   1085  CA  VAL A 149      41.615  37.142  -9.668  1.00 21.55           C  
ATOM   1086  C   VAL A 149      41.999  35.746 -10.140  1.00 21.97           C  
ATOM   1087  O   VAL A 149      42.827  35.602 -11.036  1.00 22.14           O  
ATOM   1088  CB  VAL A 149      40.593  37.775 -10.661  1.00 21.12           C  
ATOM   1089  CG1 VAL A 149      39.285  37.050 -10.569  1.00 20.47           C  
ATOM   1090  CG2 VAL A 149      40.368  39.244 -10.375  1.00 20.45           C  
ATOM   1091  N   VAL A 150      41.432  34.717  -9.522  1.00 22.41           N  
ATOM   1092  CA  VAL A 150      41.749  33.340  -9.922  1.00 22.85           C  
ATOM   1093  C   VAL A 150      40.457  32.556 -10.144  1.00 23.74           C  
ATOM   1094  O   VAL A 150      39.488  32.700  -9.387  1.00 23.76           O  
ATOM   1095  CB  VAL A 150      42.829  32.671  -8.994  1.00 22.61           C  
ATOM   1096  CG1 VAL A 150      42.913  33.379  -7.655  1.00 22.40           C  
ATOM   1097  CG2 VAL A 150      42.637  31.183  -8.835  1.00 21.70           C  
ATOM   1098  N   SER A 151      40.435  31.796 -11.238  1.00 24.52           N  
ATOM   1099  CA  SER A 151      39.233  31.132 -11.711  1.00 25.57           C  
ATOM   1100  C   SER A 151      39.472  29.658 -11.662  1.00 26.47           C  
ATOM   1101  O   SER A 151      40.582  29.198 -11.942  1.00 27.41           O  
ATOM   1102  CB  SER A 151      38.958  31.524 -13.147  1.00 25.24           C  
ATOM   1103  OG  SER A 151      38.614  32.881 -13.200  1.00 26.22           O  
ATOM   1104  N   GLY A 152      38.441  28.904 -11.323  1.00 27.27           N  
ATOM   1105  CA  GLY A 152      38.579  27.460 -11.267  1.00 28.53           C  
ATOM   1106  C   GLY A 152      37.420  26.801 -10.577  1.00 29.69           C  
ATOM   1107  O   GLY A 152      36.426  27.451 -10.223  1.00 29.74           O  
ATOM   1108  N   PRO A 153      37.526  25.495 -10.390  1.00 30.67           N  
ATOM   1109  CA  PRO A 153      36.473  24.714  -9.751  1.00 31.68           C  
ATOM   1110  C   PRO A 153      36.621  24.662  -8.221  1.00 32.76           C  
ATOM   1111  O   PRO A 153      37.676  24.272  -7.686  1.00 33.20           O  
ATOM   1112  CB  PRO A 153      36.651  23.340 -10.376  1.00 31.35           C  
ATOM   1113  CG  PRO A 153      38.154  23.250 -10.626  1.00 31.68           C  
ATOM   1114  CD  PRO A 153      38.614  24.660 -10.916  1.00 31.20           C  
ATOM   1115  N   ASP A 154      35.570  25.072  -7.527  1.00 33.65           N  
ATOM   1116  CA  ASP A 154      35.570  25.088  -6.067  1.00 35.14           C  
ATOM   1117  C   ASP A 154      36.776  25.782  -5.391  1.00 34.50           C  
ATOM   1118  O   ASP A 154      37.519  25.195  -4.604  1.00 34.57           O  
ATOM   1119  CB  ASP A 154      35.339  23.674  -5.502  1.00 36.13           C  
ATOM   1120  CG  ASP A 154      34.867  23.697  -4.016  1.00 41.04           C  
ATOM   1121  OD1 ASP A 154      33.963  22.876  -3.681  1.00 44.81           O  
ATOM   1122  OD2 ASP A 154      35.387  24.536  -3.192  1.00 44.45           O  
ATOM   1123  N   LEU A 155      36.956  27.050  -5.696  1.00 34.13           N  
ATOM   1124  CA  LEU A 155      37.826  27.857  -4.889  1.00 33.72           C  
ATOM   1125  C   LEU A 155      37.175  28.103  -3.523  1.00 33.56           C  
ATOM   1126  O   LEU A 155      35.953  28.069  -3.376  1.00 33.40           O  
ATOM   1127  CB  LEU A 155      38.104  29.186  -5.586  1.00 33.64           C  
ATOM   1128  CG  LEU A 155      39.189  29.251  -6.659  1.00 33.27           C  
ATOM   1129  CD1 LEU A 155      40.204  28.133  -6.516  1.00 33.15           C  
ATOM   1130  CD2 LEU A 155      38.571  29.244  -8.012  1.00 32.81           C  
ATOM   1131  N   SER A 156      38.010  28.357  -2.529  1.00 33.33           N  
ATOM   1132  CA  SER A 156      37.538  28.765  -1.219  1.00 33.29           C  
ATOM   1133  C   SER A 156      38.243  30.053  -0.769  1.00 32.99           C  
ATOM   1134  O   SER A 156      39.418  30.259  -1.070  1.00 32.91           O  
ATOM   1135  CB  SER A 156      37.810  27.644  -0.220  1.00 33.10           C  
ATOM   1136  OG  SER A 156      37.175  27.901   1.021  1.00 34.32           O  
ATOM   1137  N   ASP A 157      37.547  30.928  -0.054  1.00 32.72           N  
ATOM   1138  CA  ASP A 157      38.257  32.042   0.574  1.00 32.79           C  
ATOM   1139  C   ASP A 157      38.588  31.748   2.032  1.00 32.62           C  
ATOM   1140  O   ASP A 157      39.064  32.620   2.755  1.00 32.45           O  
ATOM   1141  CB  ASP A 157      37.538  33.384   0.406  1.00 32.80           C  
ATOM   1142  CG  ASP A 157      36.236  33.459   1.168  1.00 34.20           C  
ATOM   1143  OD1 ASP A 157      35.592  34.522   1.114  1.00 35.49           O  
ATOM   1144  OD2 ASP A 157      35.843  32.472   1.824  1.00 37.21           O  
HETATM 1145  N   MSE A 158      38.367  30.503   2.446  1.00 32.46           N  
HETATM 1146  CA  MSE A 158      38.744  30.075   3.783  1.00 32.70           C  
HETATM 1147  C   MSE A 158      40.254  29.862   3.884  1.00 31.93           C  
HETATM 1148  O   MSE A 158      40.726  28.786   4.286  1.00 31.75           O  
HETATM 1149  CB  MSE A 158      37.966  28.831   4.196  1.00 33.37           C  
HETATM 1150  CG  MSE A 158      36.477  29.070   4.339  1.00 36.88           C  
HETATM 1151 SE   MSE A 158      36.065  30.388   5.725  1.00 45.31          SE  
HETATM 1152  CE  MSE A 158      34.299  29.652   6.192  1.00 42.59           C  
ATOM   1153  N   ILE A 159      40.990  30.920   3.524  1.00 30.88           N  
ATOM   1154  CA  ILE A 159      42.453  30.949   3.527  1.00 29.73           C  
ATOM   1155  C   ILE A 159      42.991  32.291   4.064  1.00 29.43           C  
ATOM   1156  O   ILE A 159      42.295  33.305   4.059  1.00 29.42           O  
ATOM   1157  CB  ILE A 159      43.005  30.703   2.115  1.00 29.56           C  
ATOM   1158  CG1 ILE A 159      42.265  31.567   1.090  1.00 28.59           C  
ATOM   1159  CG2 ILE A 159      42.861  29.236   1.738  1.00 29.68           C  
ATOM   1160  CD1 ILE A 159      43.100  31.930  -0.111  1.00 27.26           C  
ATOM   1161  N   GLY A 160      44.236  32.299   4.521  1.00 28.80           N  
ATOM   1162  CA  GLY A 160      44.845  33.519   5.023  1.00 27.91           C  
ATOM   1163  C   GLY A 160      45.561  34.338   3.967  1.00 27.75           C  
ATOM   1164  O   GLY A 160      45.225  34.301   2.783  1.00 28.16           O  
ATOM   1165  N   ASP A 161      46.561  35.089   4.399  1.00 27.29           N  
ATOM   1166  CA  ASP A 161      47.187  36.057   3.538  1.00 26.68           C  
ATOM   1167  C   ASP A 161      48.629  35.701   3.272  1.00 26.31           C  
ATOM   1168  O   ASP A 161      49.282  35.060   4.066  1.00 25.54           O  
ATOM   1169  CB  ASP A 161      47.107  37.445   4.172  1.00 26.98           C  
ATOM   1170  CG  ASP A 161      45.658  37.947   4.362  1.00 27.57           C  
ATOM   1171  OD1 ASP A 161      44.711  37.369   3.775  1.00 28.41           O  
ATOM   1172  OD2 ASP A 161      45.472  38.946   5.102  1.00 27.94           O  
ATOM   1173  N   SER A 162      49.113  36.117   2.121  1.00 26.40           N  
ATOM   1174  CA  SER A 162      50.510  36.013   1.828  1.00 26.81           C  
ATOM   1175  C   SER A 162      51.223  37.244   2.429  1.00 27.28           C  
ATOM   1176  O   SER A 162      52.406  37.190   2.766  1.00 27.36           O  
ATOM   1177  CB  SER A 162      50.689  35.798   0.319  1.00 26.58           C  
ATOM   1178  OG  SER A 162      51.493  36.756  -0.334  1.00 27.73           O  
ATOM   1179  N   ASP A 163      50.477  38.326   2.636  1.00 27.77           N  
ATOM   1180  CA  ASP A 163      51.024  39.568   3.198  1.00 28.40           C  
ATOM   1181  C   ASP A 163      51.237  39.481   4.720  1.00 28.92           C  
ATOM   1182  O   ASP A 163      50.304  39.146   5.472  1.00 29.50           O  
ATOM   1183  CB  ASP A 163      50.092  40.744   2.854  1.00 28.48           C  
ATOM   1184  CG  ASP A 163      50.783  42.097   2.937  1.00 28.58           C  
ATOM   1185  OD1 ASP A 163      51.669  42.280   3.782  1.00 28.03           O  
ATOM   1186  OD2 ASP A 163      50.431  42.995   2.147  1.00 30.97           O  
ATOM   1187  N   PRO A 164      52.456  39.795   5.192  1.00 29.06           N  
ATOM   1188  CA  PRO A 164      52.699  39.775   6.631  1.00 29.42           C  
ATOM   1189  C   PRO A 164      52.421  41.121   7.333  1.00 30.25           C  
ATOM   1190  O   PRO A 164      52.511  41.219   8.549  1.00 30.22           O  
ATOM   1191  CB  PRO A 164      54.167  39.375   6.721  1.00 29.17           C  
ATOM   1192  CG  PRO A 164      54.766  39.745   5.394  1.00 29.32           C  
ATOM   1193  CD  PRO A 164      53.672  40.132   4.440  1.00 28.89           C  
ATOM   1194  N   HIS A 165      52.087  42.143   6.554  1.00 31.46           N  
ATOM   1195  CA  HIS A 165      51.604  43.437   7.040  1.00 32.89           C  
ATOM   1196  C   HIS A 165      52.642  44.406   7.574  1.00 33.57           C  
ATOM   1197  O   HIS A 165      52.324  45.572   7.818  1.00 33.85           O  
ATOM   1198  CB  HIS A 165      50.444  43.277   8.006  1.00 33.02           C  
ATOM   1199  CG  HIS A 165      49.213  42.734   7.356  1.00 36.27           C  
ATOM   1200  ND1 HIS A 165      49.052  41.393   7.064  1.00 38.49           N  
ATOM   1201  CD2 HIS A 165      48.084  43.353   6.922  1.00 39.31           C  
ATOM   1202  CE1 HIS A 165      47.872  41.206   6.494  1.00 40.23           C  
ATOM   1203  NE2 HIS A 165      47.262  42.379   6.397  1.00 41.18           N  
ATOM   1204  N   ARG A 166      53.876  43.939   7.742  1.00 34.31           N  
ATOM   1205  CA  ARG A 166      54.996  44.836   8.021  1.00 35.04           C  
ATOM   1206  C   ARG A 166      56.273  44.343   7.376  1.00 35.23           C  
ATOM   1207  O   ARG A 166      56.421  43.149   7.125  1.00 35.18           O  
ATOM   1208  CB  ARG A 166      55.215  45.025   9.518  1.00 35.48           C  
ATOM   1209  CG  ARG A 166      55.150  43.766  10.385  1.00 37.59           C  
ATOM   1210  CD  ARG A 166      53.795  43.616  11.147  1.00 41.52           C  
ATOM   1211  NE  ARG A 166      53.371  44.733  12.028  1.00 44.89           N  
ATOM   1212  CZ  ARG A 166      54.145  45.668  12.620  1.00 46.63           C  
ATOM   1213  NH1 ARG A 166      55.483  45.690  12.485  1.00 47.12           N  
ATOM   1214  NH2 ARG A 166      53.561  46.601  13.384  1.00 45.84           N  
ATOM   1215  N   GLU A 167      57.192  45.268   7.107  1.00 35.39           N  
ATOM   1216  CA  GLU A 167      58.516  44.930   6.580  1.00 36.06           C  
ATOM   1217  C   GLU A 167      59.305  44.196   7.665  1.00 35.60           C  
ATOM   1218  O   GLU A 167      59.021  44.351   8.851  1.00 36.33           O  
ATOM   1219  CB  GLU A 167      59.230  46.210   6.170  1.00 36.19           C  
ATOM   1220  CG  GLU A 167      58.270  47.373   6.192  1.00 40.68           C  
ATOM   1221  CD  GLU A 167      58.291  48.202   4.916  1.00 46.77           C  
ATOM   1222  OE1 GLU A 167      57.324  48.079   4.092  1.00 46.29           O  
ATOM   1223  OE2 GLU A 167      59.279  48.980   4.758  1.00 48.88           O  
ATOM   1224  N   GLY A 168      60.278  43.381   7.279  1.00 34.98           N  
ATOM   1225  CA  GLY A 168      61.065  42.655   8.267  1.00 34.16           C  
ATOM   1226  C   GLY A 168      60.702  41.189   8.434  1.00 33.74           C  
ATOM   1227  O   GLY A 168      61.513  40.404   8.928  1.00 34.01           O  
ATOM   1228  N   LEU A 169      59.491  40.817   8.032  1.00 32.82           N  
ATOM   1229  CA  LEU A 169      59.066  39.423   8.024  1.00 32.13           C  
ATOM   1230  C   LEU A 169      59.109  38.773   6.633  1.00 32.04           C  
ATOM   1231  O   LEU A 169      59.066  39.478   5.631  1.00 31.87           O  
ATOM   1232  CB  LEU A 169      57.647  39.356   8.552  1.00 32.01           C  
ATOM   1233  CG  LEU A 169      57.537  39.609  10.042  1.00 31.57           C  
ATOM   1234  CD1 LEU A 169      56.073  39.782  10.406  1.00 29.67           C  
ATOM   1235  CD2 LEU A 169      58.199  38.456  10.805  1.00 29.63           C  
ATOM   1236  N   PRO A 170      59.174  37.422   6.561  1.00 32.08           N  
ATOM   1237  CA  PRO A 170      58.994  36.695   5.286  1.00 32.20           C  
ATOM   1238  C   PRO A 170      57.552  36.704   4.741  1.00 32.74           C  
ATOM   1239  O   PRO A 170      56.598  36.962   5.498  1.00 33.16           O  
ATOM   1240  CB  PRO A 170      59.373  35.260   5.653  1.00 31.60           C  
ATOM   1241  CG  PRO A 170      59.068  35.160   7.071  1.00 31.68           C  
ATOM   1242  CD  PRO A 170      59.467  36.484   7.658  1.00 32.08           C  
ATOM   1243  N   PRO A 171      57.381  36.412   3.437  1.00 33.20           N  
ATOM   1244  CA  PRO A 171      56.019  36.205   2.941  1.00 33.60           C  
ATOM   1245  C   PRO A 171      55.405  34.943   3.572  1.00 34.19           C  
ATOM   1246  O   PRO A 171      56.103  33.945   3.770  1.00 34.16           O  
ATOM   1247  CB  PRO A 171      56.221  36.026   1.443  1.00 33.33           C  
ATOM   1248  CG  PRO A 171      57.628  35.485   1.328  1.00 33.67           C  
ATOM   1249  CD  PRO A 171      58.395  36.178   2.391  1.00 33.15           C  
ATOM   1250  N   GLU A 172      54.123  35.017   3.913  1.00 34.97           N  
ATOM   1251  CA  GLU A 172      53.415  33.930   4.550  1.00 36.05           C  
ATOM   1252  C   GLU A 172      53.036  32.926   3.510  1.00 36.37           C  
ATOM   1253  O   GLU A 172      52.601  33.301   2.425  1.00 37.02           O  
ATOM   1254  CB  GLU A 172      52.133  34.444   5.180  1.00 36.32           C  
ATOM   1255  CG  GLU A 172      52.325  35.239   6.467  1.00 40.29           C  
ATOM   1256  CD  GLU A 172      52.108  34.411   7.752  1.00 45.42           C  
ATOM   1257  OE1 GLU A 172      52.553  33.220   7.841  1.00 46.49           O  
ATOM   1258  OE2 GLU A 172      51.487  34.983   8.688  1.00 47.68           O  
ATOM   1259  N   LYS A 173      53.215  31.651   3.830  1.00 36.56           N  
ATOM   1260  CA  LYS A 173      52.603  30.586   3.077  1.00 36.80           C  
ATOM   1261  C   LYS A 173      51.110  30.692   3.375  1.00 36.76           C  
ATOM   1262  O   LYS A 173      50.734  31.127   4.467  1.00 36.90           O  
ATOM   1263  CB  LYS A 173      53.140  29.271   3.597  1.00 37.18           C  
ATOM   1264  CG  LYS A 173      53.005  28.121   2.650  1.00 39.77           C  
ATOM   1265  CD  LYS A 173      52.810  26.802   3.398  1.00 44.53           C  
ATOM   1266  CE  LYS A 173      53.806  26.641   4.551  1.00 47.14           C  
ATOM   1267  NZ  LYS A 173      54.183  25.209   4.734  1.00 49.86           N  
ATOM   1268  N   ILE A 174      50.253  30.335   2.421  1.00 36.79           N  
ATOM   1269  CA  ILE A 174      48.804  30.457   2.624  1.00 36.61           C  
ATOM   1270  C   ILE A 174      48.341  29.226   3.376  1.00 36.98           C  
ATOM   1271  O   ILE A 174      48.680  28.120   2.991  1.00 37.33           O  
ATOM   1272  CB  ILE A 174      47.992  30.614   1.292  1.00 36.37           C  
ATOM   1273  CG1 ILE A 174      48.563  31.712   0.370  1.00 36.22           C  
ATOM   1274  CG2 ILE A 174      46.536  30.920   1.586  1.00 36.43           C  
ATOM   1275  CD1 ILE A 174      48.146  33.162   0.685  1.00 34.19           C  
ATOM   1276  N   ARG A 175      47.601  29.429   4.469  1.00 37.72           N  
ATOM   1277  CA  ARG A 175      47.061  28.347   5.300  1.00 38.04           C  
ATOM   1278  C   ARG A 175      45.576  28.374   5.106  1.00 37.42           C  
ATOM   1279  O   ARG A 175      45.004  29.453   4.988  1.00 37.54           O  
ATOM   1280  CB  ARG A 175      47.317  28.587   6.796  1.00 38.61           C  
ATOM   1281  CG  ARG A 175      48.694  29.153   7.177  1.00 42.42           C  
ATOM   1282  CD  ARG A 175      49.797  28.082   7.229  1.00 48.88           C  
ATOM   1283  NE  ARG A 175      51.093  28.666   6.863  1.00 55.19           N  
ATOM   1284  CZ  ARG A 175      52.198  28.683   7.619  1.00 57.96           C  
ATOM   1285  NH1 ARG A 175      52.222  28.117   8.822  1.00 58.50           N  
ATOM   1286  NH2 ARG A 175      53.307  29.257   7.149  1.00 59.20           N  
ATOM   1287  N   PRO A 176      44.935  27.197   5.081  1.00 36.93           N  
ATOM   1288  CA  PRO A 176      43.476  27.083   5.099  1.00 36.49           C  
ATOM   1289  C   PRO A 176      42.928  27.398   6.490  1.00 36.58           C  
ATOM   1290  O   PRO A 176      43.482  26.926   7.474  1.00 36.78           O  
ATOM   1291  CB  PRO A 176      43.252  25.617   4.788  1.00 36.27           C  
ATOM   1292  CG  PRO A 176      44.489  24.938   5.294  1.00 36.53           C  
ATOM   1293  CD  PRO A 176      45.595  25.883   5.001  1.00 36.83           C  
ATOM   1294  N   THR A 177      41.862  28.187   6.585  1.00 36.48           N  
ATOM   1295  CA  THR A 177      41.290  28.518   7.889  1.00 36.40           C  
ATOM   1296  C   THR A 177      40.152  27.562   8.231  1.00 36.84           C  
ATOM   1297  O   THR A 177      39.361  27.799   9.136  1.00 36.85           O  
ATOM   1298  CB  THR A 177      40.799  29.983   7.959  1.00 36.38           C  
ATOM   1299  OG1 THR A 177      39.851  30.235   6.911  1.00 36.07           O  
ATOM   1300  CG2 THR A 177      41.974  30.961   7.856  1.00 36.08           C  
ATOM   1301  N   ASP A 178      40.099  26.457   7.506  1.00 37.41           N  
ATOM   1302  CA  ASP A 178      39.009  25.501   7.600  1.00 38.05           C  
ATOM   1303  C   ASP A 178      39.212  24.509   6.443  1.00 37.46           C  
ATOM   1304  O   ASP A 178      39.539  24.929   5.340  1.00 37.26           O  
ATOM   1305  CB  ASP A 178      37.650  26.241   7.567  1.00 38.44           C  
ATOM   1306  CG  ASP A 178      36.688  25.716   6.487  1.00 41.53           C  
ATOM   1307  OD1 ASP A 178      36.170  26.549   5.695  1.00 42.77           O  
ATOM   1308  OD2 ASP A 178      36.428  24.485   6.436  1.00 44.97           O  
ATOM   1309  N   PRO A 179      39.050  23.192   6.708  1.00 37.12           N  
ATOM   1310  CA  PRO A 179      39.174  22.041   5.787  1.00 36.62           C  
ATOM   1311  C   PRO A 179      38.804  22.268   4.317  1.00 35.74           C  
ATOM   1312  O   PRO A 179      39.369  21.612   3.449  1.00 35.78           O  
ATOM   1313  CB  PRO A 179      38.214  20.996   6.387  1.00 36.74           C  
ATOM   1314  CG  PRO A 179      37.907  21.489   7.813  1.00 37.52           C  
ATOM   1315  CD  PRO A 179      38.754  22.722   8.069  1.00 37.23           C  
ATOM   1316  N   SER A 180      37.868  23.168   4.040  1.00 34.78           N  
ATOM   1317  CA  SER A 180      37.407  23.377   2.669  1.00 34.04           C  
ATOM   1318  C   SER A 180      38.303  24.314   1.849  1.00 33.01           C  
ATOM   1319  O   SER A 180      38.012  24.583   0.689  1.00 33.03           O  
ATOM   1320  CB  SER A 180      35.976  23.907   2.669  1.00 34.27           C  
ATOM   1321  OG  SER A 180      35.978  25.266   3.072  1.00 35.36           O  
ATOM   1322  N   GLY A 181      39.365  24.827   2.458  1.00 31.72           N  
ATOM   1323  CA  GLY A 181      40.322  25.671   1.758  1.00 30.56           C  
ATOM   1324  C   GLY A 181      41.678  25.018   1.582  1.00 30.04           C  
ATOM   1325  O   GLY A 181      42.639  25.659   1.170  1.00 29.74           O  
ATOM   1326  N   ASP A 182      41.763  23.736   1.910  1.00 29.65           N  
ATOM   1327  CA  ASP A 182      43.018  23.027   1.796  1.00 29.38           C  
ATOM   1328  C   ASP A 182      43.440  22.928   0.336  1.00 28.11           C  
ATOM   1329  O   ASP A 182      44.609  23.140   0.029  1.00 28.02           O  
ATOM   1330  CB  ASP A 182      42.956  21.662   2.491  1.00 30.15           C  
ATOM   1331  CG  ASP A 182      42.826  21.796   4.008  1.00 33.63           C  
ATOM   1332  OD1 ASP A 182      41.698  22.020   4.504  1.00 36.63           O  
ATOM   1333  OD2 ASP A 182      43.856  21.700   4.723  1.00 38.05           O  
ATOM   1334  N   ARG A 183      42.494  22.666  -0.565  1.00 26.60           N  
ATOM   1335  CA  ARG A 183      42.811  22.670  -1.994  1.00 25.28           C  
ATOM   1336  C   ARG A 183      43.276  24.051  -2.517  1.00 25.15           C  
ATOM   1337  O   ARG A 183      44.321  24.144  -3.189  1.00 24.38           O  
ATOM   1338  CB  ARG A 183      41.662  22.096  -2.816  1.00 24.62           C  
ATOM   1339  CG  ARG A 183      41.908  22.058  -4.310  1.00 24.43           C  
ATOM   1340  CD  ARG A 183      43.092  21.150  -4.737  1.00 24.16           C  
ATOM   1341  NE  ARG A 183      43.183  21.015  -6.197  1.00 23.19           N  
ATOM   1342  CZ  ARG A 183      44.172  20.404  -6.850  1.00 25.42           C  
ATOM   1343  NH1 ARG A 183      45.200  19.855  -6.201  1.00 25.92           N  
ATOM   1344  NH2 ARG A 183      44.142  20.350  -8.172  1.00 27.22           N  
ATOM   1345  N   THR A 184      42.529  25.110  -2.179  1.00 24.86           N  
ATOM   1346  CA  THR A 184      42.867  26.461  -2.615  1.00 24.80           C  
ATOM   1347  C   THR A 184      44.242  26.875  -2.126  1.00 25.08           C  
ATOM   1348  O   THR A 184      44.990  27.513  -2.858  1.00 25.50           O  
ATOM   1349  CB  THR A 184      41.848  27.524  -2.141  1.00 24.95           C  
ATOM   1350  OG1 THR A 184      40.543  27.243  -2.669  1.00 25.04           O  
ATOM   1351  CG2 THR A 184      42.270  28.932  -2.592  1.00 24.50           C  
ATOM   1352  N   ALA A 185      44.579  26.520  -0.892  1.00 25.56           N  
ATOM   1353  CA  ALA A 185      45.883  26.879  -0.341  1.00 26.03           C  
ATOM   1354  C   ALA A 185      47.011  26.158  -1.090  1.00 26.74           C  
ATOM   1355  O   ALA A 185      48.004  26.785  -1.448  1.00 27.05           O  
ATOM   1356  CB  ALA A 185      45.938  26.612   1.134  1.00 25.33           C  
ATOM   1357  N   GLU A 186      46.840  24.863  -1.374  1.00 27.34           N  
ATOM   1358  CA  GLU A 186      47.827  24.125  -2.165  1.00 27.80           C  
ATOM   1359  C   GLU A 186      48.073  24.824  -3.516  1.00 26.89           C  
ATOM   1360  O   GLU A 186      49.220  24.967  -3.931  1.00 27.11           O  
ATOM   1361  CB  GLU A 186      47.428  22.648  -2.355  1.00 28.31           C  
ATOM   1362  CG  GLU A 186      48.617  21.692  -2.741  1.00 33.65           C  
ATOM   1363  CD  GLU A 186      48.198  20.300  -3.384  1.00 41.03           C  
ATOM   1364  OE1 GLU A 186      47.013  19.841  -3.254  1.00 42.67           O  
ATOM   1365  OE2 GLU A 186      49.087  19.658  -4.027  1.00 42.91           O  
ATOM   1366  N   VAL A 187      47.006  25.267  -4.180  1.00 25.89           N  
ATOM   1367  CA  VAL A 187      47.096  25.910  -5.491  1.00 24.93           C  
ATOM   1368  C   VAL A 187      47.788  27.263  -5.422  1.00 24.80           C  
ATOM   1369  O   VAL A 187      48.678  27.554  -6.238  1.00 24.52           O  
ATOM   1370  CB  VAL A 187      45.706  26.119  -6.089  1.00 24.94           C  
ATOM   1371  CG1 VAL A 187      45.782  26.872  -7.428  1.00 24.21           C  
ATOM   1372  CG2 VAL A 187      45.034  24.781  -6.264  1.00 25.04           C  
HETATM 1373  N   MSE A 188      47.374  28.071  -4.441  1.00 24.18           N  
HETATM 1374  CA  MSE A 188      47.884  29.427  -4.244  1.00 23.80           C  
HETATM 1375  C   MSE A 188      49.371  29.487  -3.947  1.00 23.21           C  
HETATM 1376  O   MSE A 188      50.069  30.370  -4.454  1.00 23.87           O  
HETATM 1377  CB  MSE A 188      47.142  30.129  -3.105  1.00 24.59           C  
HETATM 1378  CG  MSE A 188      45.793  30.662  -3.469  1.00 25.70           C  
HETATM 1379 SE   MSE A 188      45.976  31.797  -5.005  1.00 31.39          SE  
HETATM 1380  CE  MSE A 188      44.144  31.634  -5.545  1.00 29.66           C  
ATOM   1381  N   ASN A 189      49.851  28.570  -3.111  1.00 21.79           N  
ATOM   1382  CA  ASN A 189      51.243  28.582  -2.688  1.00 20.50           C  
ATOM   1383  C   ASN A 189      52.181  28.269  -3.829  1.00 19.68           C  
ATOM   1384  O   ASN A 189      53.308  28.772  -3.878  1.00 19.08           O  
ATOM   1385  CB  ASN A 189      51.466  27.601  -1.539  1.00 20.56           C  
ATOM   1386  CG  ASN A 189      50.980  28.140  -0.214  1.00 20.36           C  
ATOM   1387  OD1 ASN A 189      50.923  29.348  -0.010  1.00 20.64           O  
ATOM   1388  ND2 ASN A 189      50.637  27.245   0.699  1.00 19.90           N  
ATOM   1389  N   ALA A 190      51.696  27.435  -4.739  1.00 18.95           N  
ATOM   1390  CA  ALA A 190      52.496  26.976  -5.849  1.00 19.21           C  
ATOM   1391  C   ALA A 190      52.529  28.082  -6.889  1.00 19.22           C  
ATOM   1392  O   ALA A 190      53.568  28.357  -7.519  1.00 18.90           O  
ATOM   1393  CB  ALA A 190      51.908  25.697  -6.438  1.00 19.18           C  
ATOM   1394  N   TYR A 191      51.383  28.734  -7.045  1.00 18.97           N  
ATOM   1395  CA  TYR A 191      51.297  29.855  -7.945  1.00 18.62           C  
ATOM   1396  C   TYR A 191      52.202  30.999  -7.466  1.00 19.68           C  
ATOM   1397  O   TYR A 191      52.978  31.556  -8.243  1.00 19.57           O  
ATOM   1398  CB  TYR A 191      49.855  30.306  -8.126  1.00 17.43           C  
ATOM   1399  CG  TYR A 191      49.782  31.677  -8.699  1.00 15.28           C  
ATOM   1400  CD1 TYR A 191      50.091  31.900 -10.024  1.00 11.78           C  
ATOM   1401  CD2 TYR A 191      49.449  32.763  -7.904  1.00 13.39           C  
ATOM   1402  CE1 TYR A 191      50.065  33.145 -10.544  1.00 11.11           C  
ATOM   1403  CE2 TYR A 191      49.402  34.028  -8.422  1.00 11.94           C  
ATOM   1404  CZ  TYR A 191      49.718  34.218  -9.747  1.00 12.13           C  
ATOM   1405  OH  TYR A 191      49.675  35.483 -10.296  1.00 11.09           O  
ATOM   1406  N   LEU A 192      52.122  31.337  -6.184  1.00 20.98           N  
ATOM   1407  CA  LEU A 192      52.949  32.420  -5.661  1.00 22.26           C  
ATOM   1408  C   LEU A 192      54.441  32.154  -5.781  1.00 23.75           C  
ATOM   1409  O   LEU A 192      55.221  33.088  -5.946  1.00 24.20           O  
ATOM   1410  CB  LEU A 192      52.590  32.734  -4.222  1.00 21.74           C  
ATOM   1411  CG  LEU A 192      51.190  33.303  -4.033  1.00 20.42           C  
ATOM   1412  CD1 LEU A 192      50.950  33.544  -2.563  1.00 19.82           C  
ATOM   1413  CD2 LEU A 192      51.013  34.570  -4.814  1.00 18.01           C  
ATOM   1414  N   GLU A 193      54.827  30.884  -5.691  1.00 25.68           N  
ATOM   1415  CA  GLU A 193      56.213  30.473  -5.884  1.00 27.47           C  
ATOM   1416  C   GLU A 193      56.573  30.577  -7.355  1.00 27.87           C  
ATOM   1417  O   GLU A 193      57.634  31.073  -7.717  1.00 27.80           O  
ATOM   1418  CB  GLU A 193      56.447  29.045  -5.374  1.00 27.80           C  
ATOM   1419  CG  GLU A 193      57.885  28.545  -5.588  1.00 31.32           C  
ATOM   1420  CD  GLU A 193      58.970  29.484  -4.991  1.00 37.51           C  
ATOM   1421  OE1 GLU A 193      59.968  29.778  -5.722  1.00 37.86           O  
ATOM   1422  OE2 GLU A 193      58.829  29.923  -3.799  1.00 39.75           O  
ATOM   1423  N   GLU A 194      55.675  30.116  -8.211  1.00 28.72           N  
ATOM   1424  CA  GLU A 194      55.881  30.307  -9.623  1.00 29.61           C  
ATOM   1425  C   GLU A 194      56.015  31.801  -9.919  1.00 29.33           C  
ATOM   1426  O   GLU A 194      56.942  32.198 -10.602  1.00 29.85           O  
ATOM   1427  CB  GLU A 194      54.751  29.685 -10.433  1.00 29.86           C  
ATOM   1428  CG  GLU A 194      55.089  29.569 -11.908  1.00 33.70           C  
ATOM   1429  CD  GLU A 194      54.053  28.784 -12.704  1.00 39.14           C  
ATOM   1430  OE1 GLU A 194      53.925  29.054 -13.931  1.00 41.25           O  
ATOM   1431  OE2 GLU A 194      53.379  27.898 -12.110  1.00 40.19           O  
ATOM   1432  N   ALA A 195      55.110  32.618  -9.382  1.00 29.04           N  
ATOM   1433  CA  ALA A 195      55.096  34.050  -9.653  1.00 28.88           C  
ATOM   1434  C   ALA A 195      56.403  34.743  -9.250  1.00 29.09           C  
ATOM   1435  O   ALA A 195      56.972  35.522 -10.014  1.00 28.76           O  
ATOM   1436  CB  ALA A 195      53.920  34.697  -8.979  1.00 28.14           C  
ATOM   1437  N   ARG A 196      56.898  34.443  -8.059  1.00 29.91           N  
ATOM   1438  CA  ARG A 196      58.088  35.137  -7.565  1.00 30.53           C  
ATOM   1439  C   ARG A 196      59.319  34.764  -8.372  1.00 30.66           C  
ATOM   1440  O   ARG A 196      60.267  35.522  -8.403  1.00 30.74           O  
ATOM   1441  CB  ARG A 196      58.283  34.997  -6.035  1.00 30.20           C  
ATOM   1442  CG  ARG A 196      58.905  33.694  -5.548  1.00 31.95           C  
ATOM   1443  CD  ARG A 196      58.846  33.576  -4.009  1.00 33.35           C  
ATOM   1444  NE  ARG A 196      57.557  33.049  -3.558  1.00 34.96           N  
ATOM   1445  CZ  ARG A 196      56.863  33.538  -2.530  1.00 35.57           C  
ATOM   1446  NH1 ARG A 196      57.336  34.564  -1.846  1.00 35.30           N  
ATOM   1447  NH2 ARG A 196      55.684  33.020  -2.198  1.00 35.51           N  
ATOM   1448  N   ARG A 197      59.283  33.624  -9.053  1.00 31.26           N  
ATOM   1449  CA  ARG A 197      60.370  33.251  -9.952  1.00 32.26           C  
ATOM   1450  C   ARG A 197      60.272  34.016 -11.283  1.00 32.07           C  
ATOM   1451  O   ARG A 197      61.291  34.492 -11.803  1.00 32.49           O  
ATOM   1452  CB  ARG A 197      60.407  31.745 -10.195  1.00 32.73           C  
ATOM   1453  CG  ARG A 197      61.778  31.202 -10.637  1.00 37.11           C  
ATOM   1454  CD  ARG A 197      61.681  30.165 -11.781  1.00 43.72           C  
ATOM   1455  NE  ARG A 197      60.386  29.454 -11.796  1.00 50.02           N  
ATOM   1456  CZ  ARG A 197      59.485  29.481 -12.792  1.00 51.57           C  
ATOM   1457  NH1 ARG A 197      59.719  30.160 -13.916  1.00 51.47           N  
ATOM   1458  NH2 ARG A 197      58.343  28.802 -12.670  1.00 52.15           N  
ATOM   1459  N   ILE A 198      59.065  34.144 -11.833  1.00 31.46           N  
ATOM   1460  CA  ILE A 198      58.881  34.965 -13.019  1.00 31.23           C  
ATOM   1461  C   ILE A 198      59.331  36.416 -12.746  1.00 31.73           C  
ATOM   1462  O   ILE A 198      60.338  36.871 -13.305  1.00 32.03           O  
ATOM   1463  CB  ILE A 198      57.456  34.864 -13.580  1.00 31.03           C  
ATOM   1464  CG1 ILE A 198      57.310  33.511 -14.287  1.00 31.28           C  
ATOM   1465  CG2 ILE A 198      57.186  36.019 -14.581  1.00 29.93           C  
ATOM   1466  CD1 ILE A 198      55.941  32.892 -14.261  1.00 30.69           C  
ATOM   1467  N   LEU A 199      58.618  37.109 -11.858  1.00 31.64           N  
ATOM   1468  CA  LEU A 199      59.005  38.429 -11.384  1.00 31.52           C  
ATOM   1469  C   LEU A 199      60.512  38.612 -11.266  1.00 32.02           C  
ATOM   1470  O   LEU A 199      61.094  39.469 -11.925  1.00 32.16           O  
ATOM   1471  CB  LEU A 199      58.356  38.695 -10.033  1.00 31.18           C  
ATOM   1472  CG  LEU A 199      57.131  39.606  -9.938  1.00 30.58           C  
ATOM   1473  CD1 LEU A 199      56.475  39.860 -11.276  1.00 28.26           C  
ATOM   1474  CD2 LEU A 199      56.115  39.038  -8.938  1.00 29.89           C  
ATOM   1475  N   SER A 200      61.154  37.788 -10.453  1.00 32.55           N  
ATOM   1476  CA  SER A 200      62.553  38.032 -10.125  1.00 33.46           C  
ATOM   1477  C   SER A 200      63.461  38.062 -11.337  1.00 34.17           C  
ATOM   1478  O   SER A 200      64.516  38.677 -11.294  1.00 34.46           O  
ATOM   1479  CB  SER A 200      63.056  37.033  -9.085  1.00 33.49           C  
ATOM   1480  OG  SER A 200      62.497  37.345  -7.815  1.00 33.17           O  
ATOM   1481  N   ASP A 201      63.021  37.431 -12.423  1.00 35.11           N  
ATOM   1482  CA  ASP A 201      63.810  37.328 -13.650  1.00 35.69           C  
ATOM   1483  C   ASP A 201      63.401  38.266 -14.750  1.00 35.34           C  
ATOM   1484  O   ASP A 201      64.041  38.299 -15.797  1.00 35.59           O  
ATOM   1485  CB  ASP A 201      63.726  35.921 -14.205  1.00 36.56           C  
ATOM   1486  CG  ASP A 201      64.999  35.162 -14.003  1.00 39.03           C  
ATOM   1487  OD1 ASP A 201      65.016  34.313 -13.069  1.00 41.32           O  
ATOM   1488  OD2 ASP A 201      65.978  35.444 -14.758  1.00 40.41           O  
ATOM   1489  N   HIS A 202      62.329  39.014 -14.529  1.00 34.95           N  
ATOM   1490  CA  HIS A 202      61.824  39.912 -15.543  1.00 34.25           C  
ATOM   1491  C   HIS A 202      62.779  41.035 -15.880  1.00 34.87           C  
ATOM   1492  O   HIS A 202      63.600  41.441 -15.052  1.00 34.73           O  
ATOM   1493  CB  HIS A 202      60.543  40.518 -15.081  1.00 33.40           C  
ATOM   1494  CG  HIS A 202      59.683  40.966 -16.204  1.00 32.20           C  
ATOM   1495  ND1 HIS A 202      59.784  42.221 -16.759  1.00 31.72           N  
ATOM   1496  CD2 HIS A 202      58.723  40.319 -16.899  1.00 30.33           C  
ATOM   1497  CE1 HIS A 202      58.897  42.342 -17.729  1.00 30.68           C  
ATOM   1498  NE2 HIS A 202      58.239  41.202 -17.831  1.00 31.65           N  
ATOM   1499  N   ARG A 203      62.655  41.552 -17.101  1.00 35.54           N  
ATOM   1500  CA  ARG A 203      63.523  42.636 -17.536  1.00 36.06           C  
ATOM   1501  C   ARG A 203      63.311  43.930 -16.734  1.00 35.67           C  
ATOM   1502  O   ARG A 203      64.296  44.631 -16.436  1.00 36.08           O  
ATOM   1503  CB  ARG A 203      63.515  42.862 -19.072  1.00 36.58           C  
ATOM   1504  CG  ARG A 203      62.213  42.557 -19.841  1.00 39.82           C  
ATOM   1505  CD  ARG A 203      61.249  43.771 -19.913  1.00 44.98           C  
ATOM   1506  NE  ARG A 203      61.573  44.761 -20.945  1.00 47.91           N  
ATOM   1507  CZ  ARG A 203      62.252  45.897 -20.742  1.00 51.01           C  
ATOM   1508  NH1 ARG A 203      62.716  46.222 -19.529  1.00 51.41           N  
ATOM   1509  NH2 ARG A 203      62.480  46.720 -21.770  1.00 51.37           N  
ATOM   1510  N   VAL A 204      62.069  44.235 -16.346  1.00 34.83           N  
ATOM   1511  CA  VAL A 204      61.833  45.491 -15.619  1.00 34.19           C  
ATOM   1512  C   VAL A 204      62.404  45.524 -14.200  1.00 34.38           C  
ATOM   1513  O   VAL A 204      62.841  46.588 -13.742  1.00 34.21           O  
ATOM   1514  CB  VAL A 204      60.381  46.068 -15.728  1.00 33.78           C  
ATOM   1515  CG1 VAL A 204      59.544  45.290 -16.672  1.00 33.80           C  
ATOM   1516  CG2 VAL A 204      59.720  46.192 -14.390  1.00 32.91           C  
ATOM   1517  N   ASN A 205      62.441  44.361 -13.544  1.00 34.47           N  
ATOM   1518  CA  ASN A 205      63.106  44.224 -12.251  1.00 35.07           C  
ATOM   1519  C   ASN A 205      64.613  44.142 -12.356  1.00 35.72           C  
ATOM   1520  O   ASN A 205      65.309  44.586 -11.453  1.00 35.90           O  
ATOM   1521  CB  ASN A 205      62.582  43.030 -11.447  1.00 35.08           C  
ATOM   1522  CG  ASN A 205      61.236  43.299 -10.830  1.00 34.80           C  
ATOM   1523  OD1 ASN A 205      60.905  44.444 -10.576  1.00 35.93           O  
ATOM   1524  ND2 ASN A 205      60.439  42.251 -10.606  1.00 33.53           N  
ATOM   1525  N   LYS A 206      65.126  43.565 -13.437  1.00 36.65           N  
ATOM   1526  CA  LYS A 206      66.573  43.578 -13.659  1.00 37.72           C  
ATOM   1527  C   LYS A 206      67.040  45.010 -13.938  1.00 37.83           C  
ATOM   1528  O   LYS A 206      67.994  45.485 -13.320  1.00 37.10           O  
ATOM   1529  CB  LYS A 206      66.970  42.631 -14.790  1.00 38.08           C  
ATOM   1530  CG  LYS A 206      66.847  41.152 -14.441  1.00 40.17           C  
ATOM   1531  CD  LYS A 206      67.465  40.237 -15.523  1.00 44.05           C  
ATOM   1532  CE  LYS A 206      66.903  40.498 -16.940  1.00 45.76           C  
ATOM   1533  NZ  LYS A 206      67.234  39.357 -17.861  1.00 47.50           N  
ATOM   1534  N   GLU A 207      66.333  45.692 -14.844  1.00 38.45           N  
ATOM   1535  CA  GLU A 207      66.572  47.119 -15.131  1.00 39.67           C  
ATOM   1536  C   GLU A 207      66.199  48.054 -13.954  1.00 39.21           C  
ATOM   1537  O   GLU A 207      66.285  49.289 -14.068  1.00 39.41           O  
ATOM   1538  CB  GLU A 207      65.901  47.562 -16.460  1.00 40.08           C  
ATOM   1539  CG  GLU A 207      66.853  47.587 -17.714  1.00 43.99           C  
ATOM   1540  CD  GLU A 207      67.570  48.962 -17.949  1.00 49.22           C  
ATOM   1541  OE1 GLU A 207      68.830  49.008 -18.001  1.00 49.95           O  
ATOM   1542  OE2 GLU A 207      66.874  50.003 -18.087  1.00 51.09           O  
ATOM   1543  N   ARG A 208      65.793  47.464 -12.829  1.00 38.50           N  
ATOM   1544  CA  ARG A 208      65.595  48.224 -11.605  1.00 37.48           C  
ATOM   1545  C   ARG A 208      66.787  48.095 -10.677  1.00 37.90           C  
ATOM   1546  O   ARG A 208      67.329  49.111 -10.242  1.00 38.09           O  
ATOM   1547  CB  ARG A 208      64.325  47.813 -10.896  1.00 36.77           C  
ATOM   1548  CG  ARG A 208      63.149  48.569 -11.368  1.00 33.63           C  
ATOM   1549  CD  ARG A 208      61.974  48.173 -10.572  1.00 27.99           C  
ATOM   1550  NE  ARG A 208      60.763  48.659 -11.192  1.00 26.97           N  
ATOM   1551  CZ  ARG A 208      59.549  48.563 -10.659  1.00 27.79           C  
ATOM   1552  NH1 ARG A 208      59.360  48.005  -9.466  1.00 28.67           N  
ATOM   1553  NH2 ARG A 208      58.511  49.041 -11.319  1.00 27.44           N  
ATOM   1554  N   VAL A 209      67.202  46.862 -10.379  1.00 37.80           N  
ATOM   1555  CA  VAL A 209      68.398  46.659  -9.558  1.00 38.25           C  
ATOM   1556  C   VAL A 209      69.586  47.315 -10.242  1.00 38.40           C  
ATOM   1557  O   VAL A 209      70.423  47.926  -9.583  1.00 38.76           O  
ATOM   1558  CB  VAL A 209      68.711  45.149  -9.193  1.00 38.25           C  
ATOM   1559  CG1 VAL A 209      67.490  44.455  -8.585  1.00 37.39           C  
ATOM   1560  CG2 VAL A 209      69.260  44.352 -10.392  1.00 38.92           C  
ATOM   1561  N   LYS A 210      69.620  47.216 -11.569  1.00 38.74           N  
ATOM   1562  CA  LYS A 210      70.654  47.837 -12.397  1.00 39.07           C  
ATOM   1563  C   LYS A 210      70.674  49.333 -12.128  1.00 38.59           C  
ATOM   1564  O   LYS A 210      71.728  49.907 -11.844  1.00 38.48           O  
ATOM   1565  CB  LYS A 210      70.349  47.580 -13.878  1.00 39.62           C  
ATOM   1566  CG  LYS A 210      71.523  47.710 -14.855  1.00 41.58           C  
ATOM   1567  CD  LYS A 210      71.090  47.400 -16.321  1.00 44.56           C  
ATOM   1568  CE  LYS A 210      70.741  45.894 -16.552  1.00 45.54           C  
ATOM   1569  NZ  LYS A 210      69.568  45.682 -17.478  1.00 44.44           N  
ATOM   1570  N   ASN A 211      69.491  49.944 -12.194  1.00 37.96           N  
ATOM   1571  CA  ASN A 211      69.342  51.376 -12.033  1.00 37.80           C  
ATOM   1572  C   ASN A 211      69.134  51.857 -10.579  1.00 37.62           C  
ATOM   1573  O   ASN A 211      68.567  52.927 -10.346  1.00 37.63           O  
ATOM   1574  CB  ASN A 211      68.229  51.860 -12.963  1.00 37.55           C  
ATOM   1575  CG  ASN A 211      68.620  51.759 -14.426  1.00 39.04           C  
ATOM   1576  OD1 ASN A 211      69.808  51.784 -14.760  1.00 39.72           O  
ATOM   1577  ND2 ASN A 211      67.627  51.636 -15.313  1.00 39.70           N  
ATOM   1578  N   GLY A 212      69.608  51.065  -9.614  1.00 37.45           N  
ATOM   1579  CA  GLY A 212      69.419  51.330  -8.176  1.00 37.04           C  
ATOM   1580  C   GLY A 212      67.979  51.495  -7.660  1.00 36.70           C  
ATOM   1581  O   GLY A 212      67.754  52.110  -6.620  1.00 36.86           O  
ATOM   1582  N   ARG A 213      66.997  50.957  -8.374  1.00 36.02           N  
ATOM   1583  CA  ARG A 213      65.606  51.030  -7.922  1.00 35.19           C  
ATOM   1584  C   ARG A 213      65.131  49.753  -7.186  1.00 33.76           C  
ATOM   1585  O   ARG A 213      65.842  48.735  -7.139  1.00 33.72           O  
ATOM   1586  CB  ARG A 213      64.677  51.372  -9.096  1.00 35.99           C  
ATOM   1587  CG  ARG A 213      65.046  52.661  -9.860  1.00 37.88           C  
ATOM   1588  CD  ARG A 213      63.986  52.980 -10.936  1.00 40.53           C  
ATOM   1589  NE  ARG A 213      64.273  54.101 -11.856  1.00 42.03           N  
ATOM   1590  CZ  ARG A 213      65.283  54.970 -11.785  1.00 42.79           C  
ATOM   1591  NH1 ARG A 213      66.200  54.909 -10.820  1.00 43.04           N  
ATOM   1592  NH2 ARG A 213      65.376  55.918 -12.711  1.00 43.91           N  
ATOM   1593  N   LEU A 214      63.936  49.834  -6.593  1.00 32.02           N  
ATOM   1594  CA  LEU A 214      63.323  48.728  -5.831  1.00 29.60           C  
ATOM   1595  C   LEU A 214      62.543  47.717  -6.727  1.00 28.09           C  
ATOM   1596  O   LEU A 214      61.528  48.072  -7.343  1.00 27.91           O  
ATOM   1597  CB  LEU A 214      62.448  49.307  -4.708  1.00 29.02           C  
ATOM   1598  CG  LEU A 214      62.859  49.082  -3.239  1.00 29.44           C  
ATOM   1599  CD1 LEU A 214      64.265  48.479  -3.048  1.00 29.05           C  
ATOM   1600  CD2 LEU A 214      62.667  50.312  -2.338  1.00 29.10           C  
ATOM   1601  N   PRO A 215      63.019  46.456  -6.818  1.00 26.35           N  
ATOM   1602  CA  PRO A 215      62.310  45.549  -7.703  1.00 25.22           C  
ATOM   1603  C   PRO A 215      61.008  45.057  -7.090  1.00 24.44           C  
ATOM   1604  O   PRO A 215      60.932  44.842  -5.883  1.00 24.12           O  
ATOM   1605  CB  PRO A 215      63.294  44.398  -7.869  1.00 25.04           C  
ATOM   1606  CG  PRO A 215      64.055  44.372  -6.628  1.00 24.59           C  
ATOM   1607  CD  PRO A 215      64.204  45.810  -6.222  1.00 26.34           C  
ATOM   1608  N   GLY A 216      59.985  44.906  -7.922  1.00 23.62           N  
ATOM   1609  CA  GLY A 216      58.716  44.358  -7.485  1.00 23.07           C  
ATOM   1610  C   GLY A 216      58.724  42.889  -7.802  1.00 22.94           C  
ATOM   1611  O   GLY A 216      58.083  42.472  -8.751  1.00 23.01           O  
ATOM   1612  N   ASN A 217      59.459  42.111  -7.002  1.00 22.81           N  
ATOM   1613  CA  ASN A 217      59.752  40.706  -7.294  1.00 22.38           C  
ATOM   1614  C   ASN A 217      58.855  39.712  -6.570  1.00 22.12           C  
ATOM   1615  O   ASN A 217      59.082  38.513  -6.617  1.00 22.03           O  
ATOM   1616  CB  ASN A 217      61.227  40.407  -6.976  1.00 22.45           C  
ATOM   1617  CG  ASN A 217      61.535  40.504  -5.506  1.00 22.88           C  
ATOM   1618  OD1 ASN A 217      60.679  40.884  -4.702  1.00 23.89           O  
ATOM   1619  ND2 ASN A 217      62.764  40.168  -5.139  1.00 22.39           N  
ATOM   1620  N   GLU A 218      57.841  40.230  -5.889  1.00 22.11           N  
ATOM   1621  CA  GLU A 218      56.985  39.441  -5.019  1.00 21.40           C  
ATOM   1622  C   GLU A 218      55.565  39.947  -5.178  1.00 20.60           C  
ATOM   1623  O   GLU A 218      55.317  41.150  -5.122  1.00 20.65           O  
ATOM   1624  CB  GLU A 218      57.446  39.656  -3.573  1.00 21.93           C  
ATOM   1625  CG  GLU A 218      56.588  39.004  -2.487  1.00 23.70           C  
ATOM   1626  CD  GLU A 218      56.616  37.476  -2.524  1.00 25.10           C  
ATOM   1627  OE1 GLU A 218      57.702  36.908  -2.778  1.00 25.68           O  
ATOM   1628  OE2 GLU A 218      55.550  36.849  -2.286  1.00 26.27           O  
ATOM   1629  N   LEU A 219      54.618  39.054  -5.381  1.00 19.47           N  
ATOM   1630  CA  LEU A 219      53.244  39.490  -5.271  1.00 18.94           C  
ATOM   1631  C   LEU A 219      52.719  39.164  -3.864  1.00 19.27           C  
ATOM   1632  O   LEU A 219      52.674  37.984  -3.454  1.00 20.01           O  
ATOM   1633  CB  LEU A 219      52.373  38.883  -6.374  1.00 18.17           C  
ATOM   1634  CG  LEU A 219      51.054  39.638  -6.580  1.00 17.44           C  
ATOM   1635  CD1 LEU A 219      51.247  41.064  -7.139  1.00 15.10           C  
ATOM   1636  CD2 LEU A 219      50.117  38.839  -7.455  1.00 16.33           C  
ATOM   1637  N   LEU A 220      52.369  40.198  -3.106  1.00 18.69           N  
ATOM   1638  CA  LEU A 220      51.790  39.974  -1.789  1.00 18.88           C  
ATOM   1639  C   LEU A 220      50.286  40.031  -1.888  1.00 19.17           C  
ATOM   1640  O   LEU A 220      49.730  41.055  -2.267  1.00 19.68           O  
ATOM   1641  CB  LEU A 220      52.311  40.977  -0.746  1.00 18.51           C  
ATOM   1642  CG  LEU A 220      53.788  40.838  -0.347  1.00 18.02           C  
ATOM   1643  CD1 LEU A 220      54.195  41.827   0.756  1.00 14.52           C  
ATOM   1644  CD2 LEU A 220      54.130  39.394   0.033  1.00 17.56           C  
ATOM   1645  N   VAL A 221      49.623  38.938  -1.544  1.00 19.51           N  
ATOM   1646  CA  VAL A 221      48.171  38.901  -1.632  1.00 20.39           C  
ATOM   1647  C   VAL A 221      47.536  38.941  -0.252  1.00 21.41           C  
ATOM   1648  O   VAL A 221      48.133  38.511   0.728  1.00 21.90           O  
ATOM   1649  CB  VAL A 221      47.669  37.664  -2.413  1.00 20.15           C  
ATOM   1650  CG1 VAL A 221      48.351  37.572  -3.799  1.00 20.76           C  
ATOM   1651  CG2 VAL A 221      47.871  36.390  -1.620  1.00 18.94           C  
ATOM   1652  N   ARG A 222      46.320  39.456  -0.177  1.00 22.62           N  
ATOM   1653  CA  ARG A 222      45.582  39.503   1.086  1.00 23.66           C  
ATOM   1654  C   ARG A 222      44.106  39.615   0.794  1.00 24.01           C  
ATOM   1655  O   ARG A 222      43.728  39.843  -0.352  1.00 24.54           O  
ATOM   1656  CB  ARG A 222      46.050  40.684   1.954  1.00 23.75           C  
ATOM   1657  CG  ARG A 222      45.745  42.053   1.368  1.00 24.61           C  
ATOM   1658  CD  ARG A 222      46.550  43.172   2.020  1.00 24.91           C  
ATOM   1659  NE  ARG A 222      45.911  44.443   1.703  1.00 26.58           N  
ATOM   1660  CZ  ARG A 222      46.336  45.307   0.784  1.00 28.87           C  
ATOM   1661  NH1 ARG A 222      47.448  45.081   0.085  1.00 28.95           N  
ATOM   1662  NH2 ARG A 222      45.645  46.422   0.577  1.00 29.58           N  
ATOM   1663  N   SER A 223      43.291  39.452   1.831  1.00 24.59           N  
ATOM   1664  CA  SER A 223      41.840  39.666   1.778  1.00 25.33           C  
ATOM   1665  C   SER A 223      41.152  38.786   0.755  1.00 25.69           C  
ATOM   1666  O   SER A 223      40.235  39.231   0.055  1.00 26.23           O  
ATOM   1667  CB  SER A 223      41.513  41.140   1.497  1.00 25.31           C  
ATOM   1668  OG  SER A 223      41.952  41.987   2.554  1.00 27.20           O  
ATOM   1669  N   ALA A 224      41.586  37.537   0.650  1.00 25.90           N  
ATOM   1670  CA  ALA A 224      40.980  36.648  -0.316  1.00 25.84           C  
ATOM   1671  C   ALA A 224      39.466  36.647  -0.121  1.00 26.28           C  
ATOM   1672  O   ALA A 224      38.984  36.428   0.986  1.00 26.51           O  
ATOM   1673  CB  ALA A 224      41.529  35.286  -0.153  1.00 25.97           C  
ATOM   1674  N   GLY A 225      38.725  36.927  -1.193  1.00 26.64           N  
ATOM   1675  CA  GLY A 225      37.260  36.952  -1.156  1.00 27.11           C  
ATOM   1676  C   GLY A 225      36.650  36.281  -2.367  1.00 27.60           C  
ATOM   1677  O   GLY A 225      37.056  36.560  -3.504  1.00 28.09           O  
ATOM   1678  N   LYS A 226      35.692  35.385  -2.139  1.00 27.92           N  
ATOM   1679  CA  LYS A 226      35.087  34.614  -3.229  1.00 28.48           C  
ATOM   1680  C   LYS A 226      33.757  35.215  -3.698  1.00 28.83           C  
ATOM   1681  O   LYS A 226      32.793  35.326  -2.926  1.00 28.74           O  
ATOM   1682  CB  LYS A 226      34.874  33.160  -2.806  1.00 28.62           C  
ATOM   1683  CG  LYS A 226      34.231  32.301  -3.906  1.00 29.69           C  
ATOM   1684  CD  LYS A 226      33.997  30.869  -3.482  1.00 30.52           C  
ATOM   1685  CE  LYS A 226      33.322  30.089  -4.589  1.00 31.44           C  
ATOM   1686  NZ  LYS A 226      33.202  28.640  -4.234  1.00 32.61           N  
ATOM   1687  N   VAL A 227      33.693  35.592  -4.969  1.00 28.99           N  
ATOM   1688  CA  VAL A 227      32.495  36.266  -5.451  1.00 29.24           C  
ATOM   1689  C   VAL A 227      31.338  35.273  -5.442  1.00 29.65           C  
ATOM   1690  O   VAL A 227      31.439  34.208  -6.044  1.00 30.39           O  
ATOM   1691  CB  VAL A 227      32.722  37.041  -6.810  1.00 28.99           C  
ATOM   1692  CG1 VAL A 227      34.055  36.712  -7.435  1.00 27.47           C  
ATOM   1693  CG2 VAL A 227      31.579  36.844  -7.782  1.00 29.42           C  
ATOM   1694  N   PRO A 228      30.244  35.609  -4.740  1.00 30.02           N  
ATOM   1695  CA  PRO A 228      29.175  34.653  -4.467  1.00 30.34           C  
ATOM   1696  C   PRO A 228      28.293  34.444  -5.684  1.00 30.60           C  
ATOM   1697  O   PRO A 228      28.648  34.886  -6.779  1.00 31.06           O  
ATOM   1698  CB  PRO A 228      28.389  35.325  -3.343  1.00 30.20           C  
ATOM   1699  CG  PRO A 228      28.590  36.792  -3.558  1.00 30.57           C  
ATOM   1700  CD  PRO A 228      29.825  36.983  -4.418  1.00 30.36           C  
ATOM   1701  N   ALA A 229      27.151  33.788  -5.493  1.00 30.97           N  
ATOM   1702  CA  ALA A 229      26.260  33.405  -6.612  1.00 30.89           C  
ATOM   1703  C   ALA A 229      25.607  34.566  -7.406  1.00 30.17           C  
ATOM   1704  O   ALA A 229      25.520  34.497  -8.631  1.00 30.75           O  
ATOM   1705  CB  ALA A 229      25.204  32.428  -6.133  1.00 31.56           C  
ATOM   1706  N   ILE A 230      25.155  35.604  -6.711  1.00 28.63           N  
ATOM   1707  CA  ILE A 230      24.606  36.834  -7.331  1.00 26.98           C  
ATOM   1708  C   ILE A 230      23.840  36.690  -8.673  1.00 25.47           C  
ATOM   1709  O   ILE A 230      24.428  36.623  -9.760  1.00 25.31           O  
ATOM   1710  CB  ILE A 230      25.641  37.990  -7.351  1.00 27.03           C  
ATOM   1711  CG1 ILE A 230      24.929  39.323  -7.098  1.00 27.08           C  
ATOM   1712  CG2 ILE A 230      26.436  38.002  -8.647  1.00 26.92           C  
ATOM   1713  CD1 ILE A 230      25.852  40.478  -6.635  1.00 28.01           C  
ATOM   1714  N   PRO A 231      22.513  36.630  -8.585  1.00 23.84           N  
ATOM   1715  CA  PRO A 231      21.655  36.549  -9.727  1.00 23.20           C  
ATOM   1716  C   PRO A 231      21.967  37.621 -10.775  1.00 23.17           C  
ATOM   1717  O   PRO A 231      22.450  38.695 -10.412  1.00 22.66           O  
ATOM   1718  CB  PRO A 231      20.289  36.844  -9.118  1.00 23.23           C  
ATOM   1719  CG  PRO A 231      20.371  36.381  -7.760  1.00 22.10           C  
ATOM   1720  CD  PRO A 231      21.763  36.527  -7.324  1.00 23.34           C  
ATOM   1721  N   SER A 232      21.668  37.318 -12.053  1.00 23.25           N  
ATOM   1722  CA  SER A 232      21.507  38.304 -13.148  1.00 22.82           C  
ATOM   1723  C   SER A 232      20.706  39.494 -12.662  1.00 22.53           C  
ATOM   1724  O   SER A 232      19.969  39.395 -11.677  1.00 22.70           O  
ATOM   1725  CB  SER A 232      20.641  37.750 -14.285  1.00 22.83           C  
ATOM   1726  OG  SER A 232      21.150  36.592 -14.884  1.00 24.54           O  
ATOM   1727  N   PHE A 233      20.817  40.603 -13.379  1.00 21.68           N  
ATOM   1728  CA  PHE A 233      19.862  41.656 -13.237  1.00 21.47           C  
ATOM   1729  C   PHE A 233      18.481  41.104 -13.653  1.00 21.95           C  
ATOM   1730  O   PHE A 233      17.467  41.356 -12.973  1.00 21.82           O  
ATOM   1731  CB  PHE A 233      20.259  42.888 -14.072  1.00 21.15           C  
ATOM   1732  CG  PHE A 233      19.323  44.045 -13.901  1.00 20.41           C  
ATOM   1733  CD1 PHE A 233      19.478  44.924 -12.849  1.00 19.32           C  
ATOM   1734  CD2 PHE A 233      18.241  44.211 -14.753  1.00 19.42           C  
ATOM   1735  CE1 PHE A 233      18.590  45.961 -12.667  1.00 19.47           C  
ATOM   1736  CE2 PHE A 233      17.368  45.247 -14.587  1.00 19.11           C  
ATOM   1737  CZ  PHE A 233      17.538  46.128 -13.536  1.00 19.01           C  
ATOM   1738  N   THR A 234      18.448  40.344 -14.757  1.00 22.21           N  
ATOM   1739  CA  THR A 234      17.207  39.758 -15.255  1.00 22.34           C  
ATOM   1740  C   THR A 234      16.703  38.749 -14.231  1.00 22.84           C  
ATOM   1741  O   THR A 234      15.501  38.670 -13.945  1.00 22.63           O  
ATOM   1742  CB  THR A 234      17.402  39.082 -16.607  1.00 22.19           C  
ATOM   1743  OG1 THR A 234      18.007  40.001 -17.518  1.00 22.56           O  
ATOM   1744  CG2 THR A 234      16.063  38.629 -17.190  1.00 22.80           C  
ATOM   1745  N   GLU A 235      17.636  38.007 -13.648  1.00 23.17           N  
ATOM   1746  CA  GLU A 235      17.285  37.080 -12.582  1.00 23.50           C  
ATOM   1747  C   GLU A 235      16.687  37.731 -11.349  1.00 23.06           C  
ATOM   1748  O   GLU A 235      15.807  37.149 -10.740  1.00 23.32           O  
ATOM   1749  CB  GLU A 235      18.467  36.188 -12.188  1.00 23.87           C  
ATOM   1750  CG  GLU A 235      18.466  34.821 -12.880  1.00 24.85           C  
ATOM   1751  CD  GLU A 235      19.866  34.251 -13.037  1.00 28.10           C  
ATOM   1752  OE1 GLU A 235      19.989  33.130 -13.580  1.00 30.70           O  
ATOM   1753  OE2 GLU A 235      20.848  34.915 -12.630  1.00 27.47           O  
ATOM   1754  N   LYS A 236      17.150  38.920 -10.981  1.00 22.43           N  
ATOM   1755  CA  LYS A 236      16.687  39.542  -9.753  1.00 22.40           C  
ATOM   1756  C   LYS A 236      15.416  40.334  -9.987  1.00 22.89           C  
ATOM   1757  O   LYS A 236      14.525  40.366  -9.152  1.00 22.98           O  
ATOM   1758  CB  LYS A 236      17.749  40.476  -9.200  1.00 22.41           C  
ATOM   1759  CG  LYS A 236      17.504  40.978  -7.777  1.00 22.72           C  
ATOM   1760  CD  LYS A 236      18.331  40.187  -6.768  1.00 22.99           C  
ATOM   1761  CE  LYS A 236      17.466  39.476  -5.786  1.00 23.77           C  
ATOM   1762  NZ  LYS A 236      16.913  40.491  -4.858  1.00 25.56           N  
ATOM   1763  N   ASN A 237      15.330  40.970 -11.139  1.00 23.20           N  
ATOM   1764  CA  ASN A 237      14.315  41.967 -11.334  1.00 23.23           C  
ATOM   1765  C   ASN A 237      13.366  41.653 -12.419  1.00 23.62           C  
ATOM   1766  O   ASN A 237      12.348  42.324 -12.546  1.00 23.28           O  
ATOM   1767  CB  ASN A 237      14.977  43.277 -11.650  1.00 23.29           C  
ATOM   1768  CG  ASN A 237      15.731  43.782 -10.512  1.00 22.49           C  
ATOM   1769  OD1 ASN A 237      15.164  43.991  -9.455  1.00 23.29           O  
ATOM   1770  ND2 ASN A 237      17.034  43.948 -10.684  1.00 23.66           N  
ATOM   1771  N   ARG A 238      13.720  40.652 -13.215  1.00 24.46           N  
ATOM   1772  CA  ARG A 238      12.837  40.139 -14.241  1.00 25.75           C  
ATOM   1773  C   ARG A 238      12.648  41.203 -15.305  1.00 25.83           C  
ATOM   1774  O   ARG A 238      11.525  41.505 -15.688  1.00 26.21           O  
ATOM   1775  CB  ARG A 238      11.485  39.699 -13.627  1.00 25.97           C  
ATOM   1776  CG  ARG A 238      11.628  38.757 -12.413  1.00 28.81           C  
ATOM   1777  CD  ARG A 238      10.517  37.697 -12.323  1.00 32.92           C  
ATOM   1778  NE  ARG A 238       9.417  38.054 -11.423  1.00 35.50           N  
ATOM   1779  CZ  ARG A 238       8.393  38.851 -11.735  1.00 36.93           C  
ATOM   1780  NH1 ARG A 238       8.298  39.405 -12.930  1.00 37.70           N  
ATOM   1781  NH2 ARG A 238       7.446  39.093 -10.844  1.00 38.29           N  
HETATM 1782  N   MSE A 239      13.758  41.808 -15.726  1.00 26.31           N  
HETATM 1783  CA  MSE A 239      13.816  42.732 -16.882  1.00 26.78           C  
HETATM 1784  C   MSE A 239      15.226  42.792 -17.461  1.00 26.05           C  
HETATM 1785  O   MSE A 239      16.187  42.276 -16.884  1.00 26.04           O  
HETATM 1786  CB  MSE A 239      13.390  44.163 -16.545  1.00 27.39           C  
HETATM 1787  CG  MSE A 239      12.910  44.406 -15.132  1.00 31.56           C  
HETATM 1788 SE   MSE A 239      12.660  46.307 -14.728  1.00 39.91          SE  
HETATM 1789  CE  MSE A 239      10.811  46.484 -15.392  1.00 34.43           C  
ATOM   1790  N   LYS A 240      15.342  43.434 -18.610  1.00 25.41           N  
ATOM   1791  CA  LYS A 240      16.614  43.571 -19.272  1.00 24.75           C  
ATOM   1792  C   LYS A 240      17.120  44.959 -18.949  1.00 24.01           C  
ATOM   1793  O   LYS A 240      16.431  45.940 -19.176  1.00 24.03           O  
ATOM   1794  CB  LYS A 240      16.404  43.401 -20.774  1.00 24.96           C  
ATOM   1795  CG  LYS A 240      17.621  43.041 -21.582  1.00 25.82           C  
ATOM   1796  CD  LYS A 240      17.201  42.885 -23.028  1.00 28.81           C  
ATOM   1797  CE  LYS A 240      18.326  43.215 -23.996  1.00 31.13           C  
ATOM   1798  NZ  LYS A 240      17.730  43.723 -25.267  1.00 32.94           N  
ATOM   1799  N   GLY A 241      18.324  45.046 -18.410  1.00 23.68           N  
ATOM   1800  CA  GLY A 241      18.902  46.344 -18.039  1.00 22.78           C  
ATOM   1801  C   GLY A 241      20.175  46.737 -18.774  1.00 22.11           C  
ATOM   1802  O   GLY A 241      20.914  45.877 -19.260  1.00 20.70           O  
ATOM   1803  N   ALA A 242      20.391  48.052 -18.868  1.00 22.25           N  
ATOM   1804  CA  ALA A 242      21.690  48.610 -19.236  1.00 23.17           C  
ATOM   1805  C   ALA A 242      22.132  49.743 -18.300  1.00 23.91           C  
ATOM   1806  O   ALA A 242      21.302  50.381 -17.655  1.00 23.89           O  
ATOM   1807  CB  ALA A 242      21.691  49.071 -20.668  1.00 22.97           C  
ATOM   1808  N   CYS A 243      23.444  49.964 -18.228  1.00 24.94           N  
ATOM   1809  CA  CYS A 243      24.043  51.059 -17.470  1.00 26.39           C  
ATOM   1810  C   CYS A 243      24.716  51.992 -18.460  1.00 25.66           C  
ATOM   1811  O   CYS A 243      25.529  51.555 -19.273  1.00 25.74           O  
ATOM   1812  CB  CYS A 243      25.101  50.552 -16.468  1.00 26.55           C  
ATOM   1813  SG  CYS A 243      24.566  49.060 -15.579  1.00 35.39           S  
ATOM   1814  N   VAL A 244      24.370  53.269 -18.404  1.00 25.04           N  
ATOM   1815  CA  VAL A 244      25.238  54.287 -18.949  1.00 24.81           C  
ATOM   1816  C   VAL A 244      26.030  54.876 -17.783  1.00 25.39           C  
ATOM   1817  O   VAL A 244      25.565  55.761 -17.030  1.00 25.19           O  
ATOM   1818  CB  VAL A 244      24.491  55.380 -19.734  1.00 24.85           C  
ATOM   1819  CG1 VAL A 244      25.480  56.401 -20.299  1.00 23.72           C  
ATOM   1820  CG2 VAL A 244      23.632  54.770 -20.853  1.00 24.18           C  
ATOM   1821  N   VAL A 245      27.230  54.347 -17.619  1.00 25.71           N  
ATOM   1822  CA  VAL A 245      28.101  54.803 -16.573  1.00 26.49           C  
ATOM   1823  C   VAL A 245      29.491  54.853 -17.160  1.00 27.39           C  
ATOM   1824  O   VAL A 245      29.790  54.137 -18.111  1.00 27.86           O  
ATOM   1825  CB  VAL A 245      28.042  53.865 -15.323  1.00 26.48           C  
ATOM   1826  CG1 VAL A 245      26.610  53.596 -14.902  1.00 25.33           C  
ATOM   1827  CG2 VAL A 245      28.733  52.554 -15.573  1.00 26.13           C  
ATOM   1828  N   GLY A 246      30.316  55.749 -16.638  1.00 28.29           N  
ATOM   1829  CA  GLY A 246      31.766  55.697 -16.838  1.00 29.30           C  
ATOM   1830  C   GLY A 246      32.183  55.285 -15.457  1.00 30.19           C  
ATOM   1831  O   GLY A 246      31.318  55.216 -14.584  1.00 31.06           O  
ATOM   1832  N   SER A 247      33.455  55.009 -15.215  1.00 30.37           N  
ATOM   1833  CA  SER A 247      33.855  54.565 -13.872  1.00 31.35           C  
ATOM   1834  C   SER A 247      33.966  53.062 -13.790  1.00 31.78           C  
ATOM   1835  O   SER A 247      32.958  52.355 -13.782  1.00 32.09           O  
ATOM   1836  CB  SER A 247      32.891  55.043 -12.767  1.00 31.34           C  
ATOM   1837  OG  SER A 247      32.608  54.000 -11.836  1.00 31.56           O  
ATOM   1838  N   PRO A 248      35.199  52.577 -13.672  1.00 31.99           N  
ATOM   1839  CA  PRO A 248      35.527  51.169 -13.707  1.00 31.92           C  
ATOM   1840  C   PRO A 248      34.704  50.314 -12.737  1.00 31.86           C  
ATOM   1841  O   PRO A 248      34.140  49.296 -13.147  1.00 31.52           O  
ATOM   1842  CB  PRO A 248      37.022  51.153 -13.352  1.00 31.87           C  
ATOM   1843  CG  PRO A 248      37.258  52.473 -12.661  1.00 32.57           C  
ATOM   1844  CD  PRO A 248      36.384  53.409 -13.412  1.00 32.01           C  
ATOM   1845  N   TRP A 249      34.627  50.700 -11.475  1.00 32.15           N  
ATOM   1846  CA  TRP A 249      33.954  49.828 -10.540  1.00 33.23           C  
ATOM   1847  C   TRP A 249      32.494  49.598 -10.962  1.00 32.71           C  
ATOM   1848  O   TRP A 249      32.001  48.462 -11.001  1.00 32.51           O  
ATOM   1849  CB  TRP A 249      34.056  50.348  -9.105  1.00 34.08           C  
ATOM   1850  CG  TRP A 249      32.752  50.252  -8.361  1.00 38.88           C  
ATOM   1851  CD1 TRP A 249      32.098  49.106  -7.950  1.00 41.93           C  
ATOM   1852  CD2 TRP A 249      31.917  51.348  -7.974  1.00 43.98           C  
ATOM   1853  NE1 TRP A 249      30.914  49.434  -7.322  1.00 43.89           N  
ATOM   1854  CE2 TRP A 249      30.779  50.800  -7.321  1.00 44.59           C  
ATOM   1855  CE3 TRP A 249      32.024  52.747  -8.103  1.00 47.02           C  
ATOM   1856  CZ2 TRP A 249      29.756  51.601  -6.800  1.00 46.47           C  
ATOM   1857  CZ3 TRP A 249      30.993  53.552  -7.581  1.00 49.26           C  
ATOM   1858  CH2 TRP A 249      29.876  52.968  -6.934  1.00 48.56           C  
ATOM   1859  N   LEU A 250      31.804  50.677 -11.293  1.00 32.03           N  
ATOM   1860  CA  LEU A 250      30.398  50.563 -11.592  1.00 31.32           C  
ATOM   1861  C   LEU A 250      30.133  49.761 -12.868  1.00 30.64           C  
ATOM   1862  O   LEU A 250      29.236  48.938 -12.883  1.00 30.34           O  
ATOM   1863  CB  LEU A 250      29.772  51.952 -11.653  1.00 31.86           C  
ATOM   1864  CG  LEU A 250      28.266  52.006 -11.464  1.00 31.42           C  
ATOM   1865  CD1 LEU A 250      27.876  51.223 -10.232  1.00 31.64           C  
ATOM   1866  CD2 LEU A 250      27.846  53.456 -11.339  1.00 32.23           C  
ATOM   1867  N   LYS A 251      30.917  50.007 -13.920  1.00 30.16           N  
ATOM   1868  CA  LYS A 251      30.869  49.210 -15.156  1.00 29.93           C  
ATOM   1869  C   LYS A 251      31.088  47.736 -14.874  1.00 29.86           C  
ATOM   1870  O   LYS A 251      30.376  46.903 -15.422  1.00 30.37           O  
ATOM   1871  CB  LYS A 251      31.938  49.646 -16.162  1.00 29.78           C  
ATOM   1872  CG  LYS A 251      31.688  50.962 -16.837  1.00 29.97           C  
ATOM   1873  CD  LYS A 251      32.960  51.534 -17.452  1.00 30.90           C  
ATOM   1874  CE  LYS A 251      33.193  51.071 -18.874  1.00 30.97           C  
ATOM   1875  NZ  LYS A 251      34.540  51.499 -19.332  1.00 30.81           N  
ATOM   1876  N   GLY A 252      32.078  47.422 -14.037  1.00 29.46           N  
ATOM   1877  CA  GLY A 252      32.421  46.034 -13.713  1.00 29.62           C  
ATOM   1878  C   GLY A 252      31.312  45.292 -12.972  1.00 29.68           C  
ATOM   1879  O   GLY A 252      31.040  44.105 -13.238  1.00 29.49           O  
ATOM   1880  N   LEU A 253      30.678  46.002 -12.042  1.00 29.52           N  
ATOM   1881  CA  LEU A 253      29.531  45.493 -11.311  1.00 29.50           C  
ATOM   1882  C   LEU A 253      28.382  45.251 -12.249  1.00 29.37           C  
ATOM   1883  O   LEU A 253      27.673  44.253 -12.124  1.00 29.39           O  
ATOM   1884  CB  LEU A 253      29.110  46.487 -10.233  1.00 29.89           C  
ATOM   1885  CG  LEU A 253      27.710  46.417  -9.630  1.00 29.62           C  
ATOM   1886  CD1 LEU A 253      27.543  45.158  -8.832  1.00 27.79           C  
ATOM   1887  CD2 LEU A 253      27.527  47.638  -8.744  1.00 30.92           C  
ATOM   1888  N   CYS A 254      28.195  46.168 -13.188  1.00 29.47           N  
ATOM   1889  CA  CYS A 254      27.120  46.021 -14.165  1.00 30.06           C  
ATOM   1890  C   CYS A 254      27.317  44.794 -15.045  1.00 29.85           C  
ATOM   1891  O   CYS A 254      26.346  44.093 -15.339  1.00 29.95           O  
ATOM   1892  CB  CYS A 254      26.939  47.282 -15.002  1.00 30.11           C  
ATOM   1893  SG  CYS A 254      25.972  48.559 -14.163  1.00 31.79           S  
ATOM   1894  N   ARG A 255      28.566  44.530 -15.431  1.00 29.44           N  
ATOM   1895  CA  ARG A 255      28.919  43.291 -16.124  1.00 29.61           C  
ATOM   1896  C   ARG A 255      28.780  42.041 -15.244  1.00 29.36           C  
ATOM   1897  O   ARG A 255      28.491  40.947 -15.734  1.00 28.42           O  
ATOM   1898  CB  ARG A 255      30.327  43.383 -16.684  1.00 29.57           C  
ATOM   1899  CG  ARG A 255      30.438  44.381 -17.799  1.00 31.12           C  
ATOM   1900  CD  ARG A 255      31.403  43.923 -18.866  1.00 34.33           C  
ATOM   1901  NE  ARG A 255      31.578  44.951 -19.882  1.00 37.93           N  
ATOM   1902  CZ  ARG A 255      32.364  46.026 -19.745  1.00 40.53           C  
ATOM   1903  NH1 ARG A 255      33.074  46.223 -18.626  1.00 40.97           N  
ATOM   1904  NH2 ARG A 255      32.452  46.907 -20.739  1.00 40.79           N  
ATOM   1905  N   LEU A 256      29.004  42.224 -13.945  1.00 29.83           N  
ATOM   1906  CA  LEU A 256      28.788  41.181 -12.942  1.00 29.90           C  
ATOM   1907  C   LEU A 256      27.346  40.720 -12.996  1.00 30.15           C  
ATOM   1908  O   LEU A 256      27.077  39.519 -13.109  1.00 30.42           O  
ATOM   1909  CB  LEU A 256      29.066  41.720 -11.544  1.00 29.49           C  
ATOM   1910  CG  LEU A 256      29.709  40.774 -10.545  1.00 29.78           C  
ATOM   1911  CD1 LEU A 256      29.151  41.009  -9.157  1.00 29.71           C  
ATOM   1912  CD2 LEU A 256      29.506  39.326 -10.966  1.00 31.41           C  
ATOM   1913  N   LEU A 257      26.434  41.696 -12.916  1.00 30.07           N  
ATOM   1914  CA  LEU A 257      24.999  41.474 -12.906  1.00 29.42           C  
ATOM   1915  C   LEU A 257      24.522  41.097 -14.296  1.00 30.11           C  
ATOM   1916  O   LEU A 257      23.362  40.775 -14.490  1.00 30.44           O  
ATOM   1917  CB  LEU A 257      24.307  42.752 -12.443  1.00 29.30           C  
ATOM   1918  CG  LEU A 257      23.987  43.144 -10.985  1.00 27.73           C  
ATOM   1919  CD1 LEU A 257      24.787  42.422  -9.924  1.00 27.29           C  
ATOM   1920  CD2 LEU A 257      24.144  44.630 -10.804  1.00 25.30           C  
ATOM   1921  N   ARG A 258      25.429  41.138 -15.265  1.00 30.98           N  
ATOM   1922  CA  ARG A 258      25.170  40.695 -16.644  1.00 31.87           C  
ATOM   1923  C   ARG A 258      24.258  41.626 -17.428  1.00 32.11           C  
ATOM   1924  O   ARG A 258      23.583  41.199 -18.350  1.00 32.44           O  
ATOM   1925  CB  ARG A 258      24.678  39.242 -16.694  1.00 32.00           C  
ATOM   1926  CG  ARG A 258      25.690  38.249 -16.151  1.00 34.47           C  
ATOM   1927  CD  ARG A 258      25.614  36.921 -16.890  1.00 42.20           C  
ATOM   1928  NE  ARG A 258      24.795  35.910 -16.193  1.00 46.33           N  
ATOM   1929  CZ  ARG A 258      24.138  34.913 -16.794  1.00 46.94           C  
ATOM   1930  NH1 ARG A 258      24.172  34.794 -18.123  1.00 47.13           N  
ATOM   1931  NH2 ARG A 258      23.426  34.050 -16.065  1.00 46.95           N  
HETATM 1932  N   MSE A 259      24.253  42.903 -17.058  1.00 32.89           N  
HETATM 1933  CA  MSE A 259      23.551  43.952 -17.802  1.00 33.29           C  
HETATM 1934  C   MSE A 259      24.475  44.443 -18.889  1.00 33.48           C  
HETATM 1935  O   MSE A 259      25.678  44.283 -18.779  1.00 33.88           O  
HETATM 1936  CB  MSE A 259      23.228  45.126 -16.881  1.00 33.31           C  
HETATM 1937  CG  MSE A 259      22.939  44.739 -15.445  1.00 33.50           C  
HETATM 1938 SE   MSE A 259      22.657  46.309 -14.330  1.00 36.55          SE  
HETATM 1939  CE  MSE A 259      21.035  47.049 -15.122  1.00 35.41           C  
ATOM   1940  N   ASP A 260      23.934  45.040 -19.934  1.00 33.97           N  
ATOM   1941  CA  ASP A 260      24.772  45.594 -20.974  1.00 35.02           C  
ATOM   1942  C   ASP A 260      25.379  46.898 -20.479  1.00 35.43           C  
ATOM   1943  O   ASP A 260      24.671  47.737 -19.952  1.00 35.54           O  
ATOM   1944  CB  ASP A 260      23.945  45.874 -22.218  1.00 35.56           C  
ATOM   1945  CG  ASP A 260      23.319  44.629 -22.804  1.00 37.00           C  
ATOM   1946  OD1 ASP A 260      24.083  43.686 -23.130  1.00 39.56           O  
ATOM   1947  OD2 ASP A 260      22.072  44.612 -22.958  1.00 36.91           O  
ATOM   1948  N   VAL A 261      26.683  47.074 -20.647  1.00 36.05           N  
ATOM   1949  CA  VAL A 261      27.332  48.301 -20.210  1.00 36.74           C  
ATOM   1950  C   VAL A 261      27.640  49.193 -21.400  1.00 37.92           C  
ATOM   1951  O   VAL A 261      28.096  48.711 -22.426  1.00 38.57           O  
ATOM   1952  CB  VAL A 261      28.608  48.008 -19.455  1.00 36.39           C  
ATOM   1953  CG1 VAL A 261      29.335  49.271 -19.176  1.00 36.04           C  
ATOM   1954  CG2 VAL A 261      28.285  47.327 -18.155  1.00 36.46           C  
ATOM   1955  N   PHE A 262      27.379  50.492 -21.257  1.00 39.01           N  
ATOM   1956  CA  PHE A 262      27.578  51.473 -22.312  1.00 39.72           C  
ATOM   1957  C   PHE A 262      28.284  52.684 -21.736  1.00 41.20           C  
ATOM   1958  O   PHE A 262      27.802  53.272 -20.758  1.00 41.38           O  
ATOM   1959  CB  PHE A 262      26.224  51.923 -22.819  1.00 39.34           C  
ATOM   1960  CG  PHE A 262      25.558  50.939 -23.704  1.00 38.78           C  
ATOM   1961  CD1 PHE A 262      24.784  49.927 -23.172  1.00 37.63           C  
ATOM   1962  CD2 PHE A 262      25.702  51.025 -25.085  1.00 39.60           C  
ATOM   1963  CE1 PHE A 262      24.161  49.001 -23.985  1.00 38.19           C  
ATOM   1964  CE2 PHE A 262      25.082  50.092 -25.921  1.00 40.41           C  
ATOM   1965  CZ  PHE A 262      24.302  49.071 -25.361  1.00 39.46           C  
ATOM   1966  N   ASP A 263      29.417  53.079 -22.312  1.00 42.66           N  
ATOM   1967  CA  ASP A 263      30.084  54.278 -21.785  1.00 44.25           C  
ATOM   1968  C   ASP A 263      30.316  55.390 -22.809  1.00 44.94           C  
ATOM   1969  O   ASP A 263      31.278  55.353 -23.576  1.00 45.27           O  
ATOM   1970  CB  ASP A 263      31.384  53.934 -21.025  1.00 44.41           C  
ATOM   1971  CG  ASP A 263      31.977  55.147 -20.278  1.00 44.53           C  
ATOM   1972  OD1 ASP A 263      31.213  56.051 -19.853  1.00 44.11           O  
ATOM   1973  OD2 ASP A 263      33.214  55.185 -20.111  1.00 44.49           O  
ATOM   1974  N   VAL A 264      29.448  56.395 -22.789  1.00 45.94           N  
ATOM   1975  CA  VAL A 264      29.622  57.556 -23.656  1.00 47.24           C  
ATOM   1976  C   VAL A 264      30.756  58.411 -23.078  1.00 48.36           C  
ATOM   1977  O   VAL A 264      30.746  58.704 -21.880  1.00 48.75           O  
ATOM   1978  CB  VAL A 264      28.329  58.424 -23.775  1.00 47.00           C  
ATOM   1979  CG1 VAL A 264      28.424  59.364 -24.973  1.00 46.71           C  
ATOM   1980  CG2 VAL A 264      27.097  57.560 -23.893  1.00 46.38           C  
ATOM   1981  N   PRO A 265      31.764  58.765 -23.908  1.00 49.23           N  
ATOM   1982  CA  PRO A 265      32.741  59.720 -23.391  1.00 49.42           C  
ATOM   1983  C   PRO A 265      32.959  60.870 -24.386  1.00 49.35           C  
ATOM   1984  O   PRO A 265      32.668  62.020 -24.067  1.00 49.18           O  
ATOM   1985  CB  PRO A 265      34.003  58.851 -23.257  1.00 49.47           C  
ATOM   1986  CG  PRO A 265      33.757  57.626 -24.331  1.00 50.04           C  
ATOM   1987  CD  PRO A 265      32.379  57.927 -24.956  1.00 49.38           C  
ATOM   1988  N   SER A 273      32.266  65.236 -18.977  1.00 42.40           N  
ATOM   1989  CA  SER A 273      31.206  66.226 -19.131  1.00 42.52           C  
ATOM   1990  C   SER A 273      30.306  65.997 -20.365  1.00 42.06           C  
ATOM   1991  O   SER A 273      29.698  66.944 -20.888  1.00 42.27           O  
ATOM   1992  CB  SER A 273      31.797  67.652 -19.133  1.00 42.72           C  
ATOM   1993  OG  SER A 273      30.911  68.583 -19.751  1.00 43.72           O  
ATOM   1994  N   ASN A 274      30.198  64.758 -20.833  1.00 41.19           N  
ATOM   1995  CA  ASN A 274      29.239  64.512 -21.901  1.00 40.67           C  
ATOM   1996  C   ASN A 274      27.844  64.162 -21.321  1.00 39.78           C  
ATOM   1997  O   ASN A 274      27.214  63.191 -21.759  1.00 40.13           O  
ATOM   1998  CB  ASN A 274      29.759  63.457 -22.906  1.00 41.01           C  
ATOM   1999  CG  ASN A 274      29.164  63.627 -24.339  1.00 42.24           C  
ATOM   2000  OD1 ASN A 274      29.641  63.002 -25.295  1.00 42.23           O  
ATOM   2001  ND2 ASN A 274      28.133  64.470 -24.480  1.00 43.04           N  
ATOM   2002  N   TYR A 275      27.360  64.957 -20.355  1.00 37.97           N  
ATOM   2003  CA  TYR A 275      26.042  64.731 -19.762  1.00 36.36           C  
ATOM   2004  C   TYR A 275      24.975  64.561 -20.827  1.00 35.48           C  
ATOM   2005  O   TYR A 275      24.246  63.586 -20.813  1.00 34.73           O  
ATOM   2006  CB  TYR A 275      25.622  65.879 -18.852  1.00 36.28           C  
ATOM   2007  CG  TYR A 275      26.578  66.261 -17.735  1.00 36.99           C  
ATOM   2008  CD1 TYR A 275      27.213  65.298 -16.931  1.00 36.68           C  
ATOM   2009  CD2 TYR A 275      26.810  67.606 -17.451  1.00 37.88           C  
ATOM   2010  CE1 TYR A 275      28.078  65.679 -15.902  1.00 36.24           C  
ATOM   2011  CE2 TYR A 275      27.669  67.993 -16.433  1.00 38.03           C  
ATOM   2012  CZ  TYR A 275      28.299  67.035 -15.663  1.00 37.70           C  
ATOM   2013  OH  TYR A 275      29.137  67.482 -14.660  1.00 37.41           O  
ATOM   2014  N   ARG A 276      24.898  65.521 -21.752  1.00 35.12           N  
ATOM   2015  CA  ARG A 276      23.944  65.483 -22.870  1.00 34.56           C  
ATOM   2016  C   ARG A 276      23.930  64.128 -23.548  1.00 33.62           C  
ATOM   2017  O   ARG A 276      22.870  63.532 -23.731  1.00 33.49           O  
ATOM   2018  CB  ARG A 276      24.254  66.561 -23.922  1.00 34.96           C  
ATOM   2019  CG  ARG A 276      23.021  67.370 -24.276  1.00 37.36           C  
ATOM   2020  CD  ARG A 276      22.717  67.516 -25.759  1.00 40.38           C  
ATOM   2021  NE  ARG A 276      21.293  67.219 -25.996  1.00 44.82           N  
ATOM   2022  CZ  ARG A 276      20.247  67.985 -25.641  1.00 45.84           C  
ATOM   2023  NH1 ARG A 276      20.419  69.164 -25.030  1.00 44.21           N  
ATOM   2024  NH2 ARG A 276      19.004  67.565 -25.915  1.00 45.21           N  
ATOM   2025  N   GLY A 277      25.123  63.661 -23.903  1.00 32.59           N  
ATOM   2026  CA  GLY A 277      25.313  62.426 -24.630  1.00 31.92           C  
ATOM   2027  C   GLY A 277      24.945  61.189 -23.840  1.00 31.50           C  
ATOM   2028  O   GLY A 277      24.311  60.266 -24.385  1.00 31.97           O  
ATOM   2029  N   LYS A 278      25.336  61.154 -22.565  1.00 30.56           N  
ATOM   2030  CA  LYS A 278      24.943  60.059 -21.688  1.00 29.89           C  
ATOM   2031  C   LYS A 278      23.439  60.072 -21.528  1.00 29.68           C  
ATOM   2032  O   LYS A 278      22.794  59.035 -21.655  1.00 30.16           O  
ATOM   2033  CB  LYS A 278      25.614  60.144 -20.329  1.00 29.57           C  
ATOM   2034  CG  LYS A 278      27.096  60.195 -20.402  1.00 30.05           C  
ATOM   2035  CD  LYS A 278      27.716  60.386 -19.046  1.00 31.69           C  
ATOM   2036  CE  LYS A 278      27.828  59.081 -18.280  1.00 32.29           C  
ATOM   2037  NZ  LYS A 278      28.786  59.261 -17.158  1.00 34.06           N  
ATOM   2038  N   ILE A 279      22.875  61.246 -21.287  1.00 29.32           N  
ATOM   2039  CA  ILE A 279      21.445  61.340 -21.169  1.00 29.43           C  
ATOM   2040  C   ILE A 279      20.781  60.826 -22.439  1.00 30.10           C  
ATOM   2041  O   ILE A 279      19.936  59.922 -22.356  1.00 30.30           O  
ATOM   2042  CB  ILE A 279      20.951  62.744 -20.757  1.00 29.05           C  
ATOM   2043  CG1 ILE A 279      21.288  63.006 -19.290  1.00 28.61           C  
ATOM   2044  CG2 ILE A 279      19.453  62.854 -20.900  1.00 28.66           C  
ATOM   2045  CD1 ILE A 279      20.675  62.021 -18.292  1.00 26.54           C  
ATOM   2046  N   GLU A 280      21.163  61.333 -23.611  1.00 30.46           N  
ATOM   2047  CA  GLU A 280      20.475  60.848 -24.806  1.00 31.09           C  
ATOM   2048  C   GLU A 280      20.804  59.419 -25.275  1.00 31.16           C  
ATOM   2049  O   GLU A 280      20.004  58.834 -26.001  1.00 31.12           O  
ATOM   2050  CB  GLU A 280      20.406  61.856 -25.942  1.00 31.10           C  
ATOM   2051  CG  GLU A 280      21.695  62.355 -26.498  1.00 33.97           C  
ATOM   2052  CD  GLU A 280      21.461  63.652 -27.290  1.00 38.53           C  
ATOM   2053  OE1 GLU A 280      22.300  64.588 -27.221  1.00 40.17           O  
ATOM   2054  OE2 GLU A 280      20.412  63.742 -27.972  1.00 39.22           O  
ATOM   2055  N   LYS A 281      21.931  58.847 -24.838  1.00 31.31           N  
ATOM   2056  CA  LYS A 281      22.164  57.405 -25.035  1.00 31.14           C  
ATOM   2057  C   LYS A 281      21.199  56.576 -24.209  1.00 30.77           C  
ATOM   2058  O   LYS A 281      20.604  55.635 -24.712  1.00 30.78           O  
ATOM   2059  CB  LYS A 281      23.585  56.998 -24.678  1.00 31.58           C  
ATOM   2060  CG  LYS A 281      23.902  55.524 -24.985  1.00 32.94           C  
ATOM   2061  CD  LYS A 281      23.782  55.234 -26.484  1.00 36.30           C  
ATOM   2062  CE  LYS A 281      23.784  53.737 -26.793  1.00 38.08           C  
ATOM   2063  NZ  LYS A 281      23.724  53.495 -28.261  1.00 39.64           N  
ATOM   2064  N   ALA A 282      21.060  56.921 -22.932  1.00 30.35           N  
ATOM   2065  CA  ALA A 282      20.037  56.331 -22.089  1.00 29.97           C  
ATOM   2066  C   ALA A 282      18.647  56.334 -22.764  1.00 30.11           C  
ATOM   2067  O   ALA A 282      17.914  55.362 -22.671  1.00 29.93           O  
ATOM   2068  CB  ALA A 282      19.988  57.051 -20.764  1.00 29.65           C  
ATOM   2069  N   VAL A 283      18.291  57.423 -23.447  1.00 30.48           N  
ATOM   2070  CA  VAL A 283      16.960  57.562 -24.045  1.00 30.41           C  
ATOM   2071  C   VAL A 283      16.822  56.633 -25.250  1.00 31.09           C  
ATOM   2072  O   VAL A 283      15.762  56.033 -25.475  1.00 31.49           O  
ATOM   2073  CB  VAL A 283      16.659  59.039 -24.420  1.00 30.45           C  
ATOM   2074  CG1 VAL A 283      15.472  59.162 -25.383  1.00 29.02           C  
ATOM   2075  CG2 VAL A 283      16.431  59.854 -23.166  1.00 29.35           C  
ATOM   2076  N   ASP A 284      17.912  56.487 -25.995  1.00 31.27           N  
ATOM   2077  CA  ASP A 284      17.953  55.594 -27.154  1.00 31.88           C  
ATOM   2078  C   ASP A 284      17.913  54.119 -26.748  1.00 30.73           C  
ATOM   2079  O   ASP A 284      17.397  53.278 -27.478  1.00 30.81           O  
ATOM   2080  CB  ASP A 284      19.152  55.954 -28.053  1.00 32.64           C  
ATOM   2081  CG  ASP A 284      19.117  57.469 -28.497  1.00 37.59           C  
ATOM   2082  OD1 ASP A 284      20.176  58.180 -28.480  1.00 39.58           O  
ATOM   2083  OD2 ASP A 284      17.994  57.962 -28.826  1.00 42.70           O  
ATOM   2084  N   LEU A 285      18.414  53.830 -25.558  1.00 29.21           N  
ATOM   2085  CA  LEU A 285      18.407  52.499 -25.031  1.00 28.10           C  
ATOM   2086  C   LEU A 285      17.042  52.069 -24.534  1.00 28.06           C  
ATOM   2087  O   LEU A 285      16.826  50.885 -24.276  1.00 27.66           O  
ATOM   2088  CB  LEU A 285      19.400  52.407 -23.890  1.00 28.11           C  
ATOM   2089  CG  LEU A 285      20.886  52.389 -24.223  1.00 27.98           C  
ATOM   2090  CD1 LEU A 285      21.699  52.425 -22.948  1.00 28.41           C  
ATOM   2091  CD2 LEU A 285      21.238  51.148 -25.015  1.00 29.17           C  
ATOM   2092  N   THR A 286      16.110  53.006 -24.392  1.00 28.16           N  
ATOM   2093  CA  THR A 286      14.804  52.633 -23.849  1.00 28.77           C  
ATOM   2094  C   THR A 286      13.958  51.922 -24.885  1.00 29.06           C  
ATOM   2095  O   THR A 286      12.866  51.461 -24.591  1.00 29.66           O  
ATOM   2096  CB  THR A 286      14.003  53.821 -23.245  1.00 28.64           C  
ATOM   2097  OG1 THR A 286      13.315  54.546 -24.272  1.00 30.22           O  
ATOM   2098  CG2 THR A 286      14.888  54.751 -22.482  1.00 28.60           C  
ATOM   2099  N   SER A 287      14.476  51.843 -26.100  1.00 29.63           N  
ATOM   2100  CA  SER A 287      13.778  51.244 -27.229  1.00 30.35           C  
ATOM   2101  C   SER A 287      14.001  49.753 -27.221  1.00 30.27           C  
ATOM   2102  O   SER A 287      13.289  49.015 -27.922  1.00 30.98           O  
ATOM   2103  CB  SER A 287      14.319  51.791 -28.567  1.00 30.92           C  
ATOM   2104  OG  SER A 287      14.145  53.204 -28.701  1.00 33.20           O  
ATOM   2105  N   SER A 288      14.997  49.317 -26.440  1.00 29.60           N  
ATOM   2106  CA  SER A 288      15.451  47.926 -26.430  1.00 28.41           C  
ATOM   2107  C   SER A 288      15.795  47.380 -25.050  1.00 27.86           C  
ATOM   2108  O   SER A 288      16.210  46.227 -24.947  1.00 27.92           O  
ATOM   2109  CB  SER A 288      16.660  47.777 -27.340  1.00 28.20           C  
ATOM   2110  OG  SER A 288      17.697  48.611 -26.880  1.00 28.18           O  
ATOM   2111  N   HIS A 289      15.654  48.200 -24.008  1.00 27.10           N  
ATOM   2112  CA  HIS A 289      15.892  47.762 -22.636  1.00 26.50           C  
ATOM   2113  C   HIS A 289      14.786  48.273 -21.749  1.00 26.53           C  
ATOM   2114  O   HIS A 289      14.358  49.405 -21.922  1.00 27.24           O  
ATOM   2115  CB  HIS A 289      17.213  48.306 -22.143  1.00 26.26           C  
ATOM   2116  CG  HIS A 289      18.401  47.714 -22.830  1.00 26.38           C  
ATOM   2117  ND1 HIS A 289      18.608  47.822 -24.187  1.00 26.53           N  
ATOM   2118  CD2 HIS A 289      19.454  47.015 -22.344  1.00 26.76           C  
ATOM   2119  CE1 HIS A 289      19.734  47.213 -24.509  1.00 26.93           C  
ATOM   2120  NE2 HIS A 289      20.271  46.720 -23.407  1.00 26.98           N  
ATOM   2121  N   ASP A 290      14.316  47.463 -20.803  1.00 25.97           N  
ATOM   2122  CA  ASP A 290      13.243  47.900 -19.920  1.00 25.91           C  
ATOM   2123  C   ASP A 290      13.735  48.775 -18.789  1.00 25.54           C  
ATOM   2124  O   ASP A 290      12.938  49.475 -18.173  1.00 26.57           O  
ATOM   2125  CB  ASP A 290      12.520  46.729 -19.275  1.00 26.81           C  
ATOM   2126  CG  ASP A 290      12.352  45.551 -20.199  1.00 29.36           C  
ATOM   2127  OD1 ASP A 290      12.324  44.412 -19.666  1.00 30.40           O  
ATOM   2128  OD2 ASP A 290      12.259  45.757 -21.441  1.00 34.53           O  
ATOM   2129  N   PHE A 291      15.026  48.706 -18.479  1.00 24.25           N  
ATOM   2130  CA  PHE A 291      15.603  49.488 -17.405  1.00 23.15           C  
ATOM   2131  C   PHE A 291      16.958  49.988 -17.847  1.00 22.97           C  
ATOM   2132  O   PHE A 291      17.758  49.241 -18.429  1.00 23.36           O  
ATOM   2133  CB  PHE A 291      15.737  48.634 -16.141  1.00 23.29           C  
ATOM   2134  CG  PHE A 291      16.417  49.327 -14.994  1.00 22.66           C  
ATOM   2135  CD1 PHE A 291      15.666  49.949 -13.999  1.00 23.42           C  
ATOM   2136  CD2 PHE A 291      17.808  49.337 -14.892  1.00 22.00           C  
ATOM   2137  CE1 PHE A 291      16.294  50.598 -12.922  1.00 23.24           C  
ATOM   2138  CE2 PHE A 291      18.453  49.973 -13.825  1.00 22.16           C  
ATOM   2139  CZ  PHE A 291      17.691  50.609 -12.834  1.00 22.61           C  
ATOM   2140  N   VAL A 292      17.217  51.257 -17.575  1.00 21.93           N  
ATOM   2141  CA  VAL A 292      18.479  51.856 -17.911  1.00 21.13           C  
ATOM   2142  C   VAL A 292      18.933  52.671 -16.695  1.00 21.76           C  
ATOM   2143  O   VAL A 292      18.246  53.606 -16.254  1.00 21.65           O  
ATOM   2144  CB  VAL A 292      18.359  52.762 -19.147  1.00 20.85           C  
ATOM   2145  CG1 VAL A 292      19.665  53.479 -19.421  1.00 19.60           C  
ATOM   2146  CG2 VAL A 292      17.946  51.969 -20.367  1.00 20.35           C  
ATOM   2147  N   LEU A 293      20.081  52.306 -16.143  1.00 21.44           N  
ATOM   2148  CA  LEU A 293      20.663  53.087 -15.097  1.00 22.06           C  
ATOM   2149  C   LEU A 293      21.623  54.133 -15.698  1.00 23.05           C  
ATOM   2150  O   LEU A 293      22.399  53.809 -16.592  1.00 23.60           O  
ATOM   2151  CB  LEU A 293      21.392  52.167 -14.147  1.00 21.59           C  
ATOM   2152  CG  LEU A 293      22.279  52.910 -13.167  1.00 21.63           C  
ATOM   2153  CD1 LEU A 293      21.532  53.145 -11.877  1.00 21.74           C  
ATOM   2154  CD2 LEU A 293      23.496  52.082 -12.922  1.00 22.88           C  
ATOM   2155  N   VAL A 294      21.549  55.385 -15.243  1.00 23.65           N  
ATOM   2156  CA  VAL A 294      22.490  56.415 -15.691  1.00 24.19           C  
ATOM   2157  C   VAL A 294      23.127  57.067 -14.488  1.00 24.92           C  
ATOM   2158  O   VAL A 294      22.430  57.600 -13.619  1.00 24.97           O  
ATOM   2159  CB  VAL A 294      21.826  57.552 -16.508  1.00 24.06           C  
ATOM   2160  CG1 VAL A 294      22.875  58.316 -17.273  1.00 23.36           C  
ATOM   2161  CG2 VAL A 294      20.824  57.022 -17.470  1.00 23.81           C  
ATOM   2162  N   ASN A 295      24.451  57.056 -14.448  1.00 25.71           N  
ATOM   2163  CA  ASN A 295      25.163  57.642 -13.323  1.00 26.77           C  
ATOM   2164  C   ASN A 295      25.933  58.876 -13.754  1.00 27.63           C  
ATOM   2165  O   ASN A 295      26.761  58.800 -14.652  1.00 28.26           O  
ATOM   2166  CB  ASN A 295      26.113  56.626 -12.714  1.00 26.62           C  
ATOM   2167  CG  ASN A 295      26.651  57.067 -11.391  1.00 27.13           C  
ATOM   2168  OD1 ASN A 295      25.918  57.176 -10.405  1.00 26.17           O  
ATOM   2169  ND2 ASN A 295      27.951  57.325 -11.351  1.00 28.83           N  
ATOM   2170  N   ILE A 296      25.650  60.011 -13.122  1.00 28.61           N  
ATOM   2171  CA  ILE A 296      26.283  61.269 -13.469  1.00 29.48           C  
ATOM   2172  C   ILE A 296      27.187  61.679 -12.323  1.00 30.58           C  
ATOM   2173  O   ILE A 296      26.767  61.689 -11.171  1.00 30.07           O  
ATOM   2174  CB  ILE A 296      25.258  62.379 -13.644  1.00 29.45           C  
ATOM   2175  CG1 ILE A 296      24.095  61.979 -14.573  1.00 29.09           C  
ATOM   2176  CG2 ILE A 296      25.941  63.648 -14.080  1.00 30.39           C  
ATOM   2177  CD1 ILE A 296      24.469  61.699 -16.014  1.00 29.32           C  
ATOM   2178  N   LYS A 297      28.432  62.009 -12.656  1.00 32.45           N  
ATOM   2179  CA  LYS A 297      29.432  62.442 -11.683  1.00 34.00           C  
ATOM   2180  C   LYS A 297      29.975  63.818 -12.052  1.00 34.73           C  
ATOM   2181  O   LYS A 297      30.042  64.717 -11.200  1.00 35.99           O  
ATOM   2182  CB  LYS A 297      30.582  61.441 -11.602  1.00 34.30           C  
ATOM   2183  CG  LYS A 297      30.384  60.353 -10.565  1.00 36.74           C  
ATOM   2184  CD  LYS A 297      31.623  59.466 -10.411  1.00 40.85           C  
ATOM   2185  CE  LYS A 297      31.790  58.500 -11.604  1.00 45.02           C  
ATOM   2186  NZ  LYS A 297      33.214  58.021 -11.737  1.00 47.39           N  
ATOM   2187  N   ASN A 307      34.311  74.859  -5.072  1.00 43.23           N  
ATOM   2188  CA  ASN A 307      33.568  75.939  -4.439  1.00 43.74           C  
ATOM   2189  C   ASN A 307      32.109  75.898  -4.876  1.00 43.82           C  
ATOM   2190  O   ASN A 307      31.765  75.132  -5.782  1.00 44.39           O  
ATOM   2191  CB  ASN A 307      34.205  77.313  -4.744  1.00 43.90           C  
ATOM   2192  CG  ASN A 307      33.774  77.912  -6.120  1.00 44.61           C  
ATOM   2193  OD1 ASN A 307      32.723  77.574  -6.681  1.00 45.22           O  
ATOM   2194  ND2 ASN A 307      34.587  78.833  -6.637  1.00 44.49           N  
ATOM   2195  N   TYR A 308      31.274  76.752  -4.279  1.00 43.46           N  
ATOM   2196  CA  TYR A 308      29.812  76.673  -4.436  1.00 43.08           C  
ATOM   2197  C   TYR A 308      29.197  77.075  -5.792  1.00 42.18           C  
ATOM   2198  O   TYR A 308      28.528  76.254  -6.403  1.00 41.84           O  
ATOM   2199  CB  TYR A 308      29.092  77.343  -3.254  1.00 43.61           C  
ATOM   2200  CG  TYR A 308      28.851  76.398  -2.115  1.00 45.08           C  
ATOM   2201  CD1 TYR A 308      29.900  75.964  -1.304  1.00 48.01           C  
ATOM   2202  CD2 TYR A 308      27.574  75.924  -1.854  1.00 47.71           C  
ATOM   2203  CE1 TYR A 308      29.674  75.071  -0.248  1.00 50.40           C  
ATOM   2204  CE2 TYR A 308      27.328  75.029  -0.809  1.00 50.21           C  
ATOM   2205  CZ  TYR A 308      28.381  74.604  -0.009  1.00 50.96           C  
ATOM   2206  OH  TYR A 308      28.126  73.722   1.022  1.00 51.29           O  
ATOM   2207  N   PRO A 309      29.406  78.328  -6.260  1.00 41.63           N  
ATOM   2208  CA  PRO A 309      28.893  78.693  -7.604  1.00 41.00           C  
ATOM   2209  C   PRO A 309      29.292  77.744  -8.755  1.00 40.80           C  
ATOM   2210  O   PRO A 309      28.529  77.615  -9.711  1.00 40.83           O  
ATOM   2211  CB  PRO A 309      29.479  80.085  -7.850  1.00 40.79           C  
ATOM   2212  CG  PRO A 309      30.474  80.313  -6.731  1.00 41.02           C  
ATOM   2213  CD  PRO A 309      30.028  79.483  -5.587  1.00 41.00           C  
ATOM   2214  N   LEU A 310      30.462  77.097  -8.674  1.00 40.40           N  
ATOM   2215  CA  LEU A 310      30.881  76.108  -9.688  1.00 39.67           C  
ATOM   2216  C   LEU A 310      30.028  74.851  -9.647  1.00 39.03           C  
ATOM   2217  O   LEU A 310      29.736  74.254 -10.694  1.00 39.50           O  
ATOM   2218  CB  LEU A 310      32.350  75.705  -9.519  1.00 39.81           C  
ATOM   2219  CG  LEU A 310      33.427  76.545 -10.208  1.00 40.96           C  
ATOM   2220  CD1 LEU A 310      34.783  75.863 -10.043  1.00 41.99           C  
ATOM   2221  CD2 LEU A 310      33.097  76.765 -11.696  1.00 41.83           C  
ATOM   2222  N   LYS A 311      29.654  74.444  -8.435  1.00 37.74           N  
ATOM   2223  CA  LYS A 311      28.824  73.269  -8.231  1.00 36.58           C  
ATOM   2224  C   LYS A 311      27.440  73.552  -8.773  1.00 35.46           C  
ATOM   2225  O   LYS A 311      26.843  72.711  -9.438  1.00 35.67           O  
ATOM   2226  CB  LYS A 311      28.774  72.890  -6.753  1.00 36.77           C  
ATOM   2227  CG  LYS A 311      30.039  72.191  -6.260  1.00 37.86           C  
ATOM   2228  CD  LYS A 311      29.967  71.975  -4.754  1.00 41.51           C  
ATOM   2229  CE  LYS A 311      30.778  70.766  -4.284  1.00 43.81           C  
ATOM   2230  NZ  LYS A 311      31.096  70.885  -2.823  1.00 45.10           N  
ATOM   2231  N   ARG A 312      26.961  74.759  -8.501  1.00 34.10           N  
ATOM   2232  CA  ARG A 312      25.743  75.313  -9.080  1.00 32.96           C  
ATOM   2233  C   ARG A 312      25.770  75.235 -10.600  1.00 32.85           C  
ATOM   2234  O   ARG A 312      24.801  74.815 -11.221  1.00 32.76           O  
ATOM   2235  CB  ARG A 312      25.647  76.787  -8.702  1.00 32.64           C  
ATOM   2236  CG  ARG A 312      24.280  77.306  -8.451  1.00 30.99           C  
ATOM   2237  CD  ARG A 312      23.959  78.489  -9.326  1.00 28.70           C  
ATOM   2238  NE  ARG A 312      25.129  79.048  -9.975  1.00 27.46           N  
ATOM   2239  CZ  ARG A 312      25.682  80.218  -9.667  1.00 28.32           C  
ATOM   2240  NH1 ARG A 312      25.178  80.976  -8.702  1.00 27.75           N  
ATOM   2241  NH2 ARG A 312      26.755  80.630 -10.335  1.00 28.26           N  
ATOM   2242  N   ASP A 313      26.883  75.657 -11.192  1.00 32.64           N  
ATOM   2243  CA  ASP A 313      26.976  75.792 -12.629  1.00 32.60           C  
ATOM   2244  C   ASP A 313      27.060  74.436 -13.285  1.00 32.40           C  
ATOM   2245  O   ASP A 313      26.635  74.287 -14.446  1.00 33.06           O  
ATOM   2246  CB  ASP A 313      28.161  76.662 -13.026  1.00 33.02           C  
ATOM   2247  CG  ASP A 313      27.872  78.166 -12.870  1.00 34.97           C  
ATOM   2248  OD1 ASP A 313      26.673  78.542 -12.699  1.00 36.17           O  
ATOM   2249  OD2 ASP A 313      28.852  78.967 -12.930  1.00 34.80           O  
ATOM   2250  N   VAL A 314      27.589  73.448 -12.556  1.00 31.39           N  
ATOM   2251  CA  VAL A 314      27.514  72.037 -13.001  1.00 30.00           C  
ATOM   2252  C   VAL A 314      26.065  71.511 -13.002  1.00 29.27           C  
ATOM   2253  O   VAL A 314      25.579  71.055 -14.037  1.00 29.41           O  
ATOM   2254  CB  VAL A 314      28.460  71.109 -12.220  1.00 29.58           C  
ATOM   2255  CG1 VAL A 314      27.966  69.698 -12.252  1.00 28.91           C  
ATOM   2256  CG2 VAL A 314      29.820  71.159 -12.833  1.00 29.73           C  
ATOM   2257  N   ILE A 315      25.371  71.603 -11.869  1.00 27.86           N  
ATOM   2258  CA  ILE A 315      23.950  71.263 -11.833  1.00 26.89           C  
ATOM   2259  C   ILE A 315      23.175  71.922 -12.979  1.00 26.60           C  
ATOM   2260  O   ILE A 315      22.317  71.296 -13.590  1.00 26.77           O  
ATOM   2261  CB  ILE A 315      23.313  71.539 -10.456  1.00 26.62           C  
ATOM   2262  CG1 ILE A 315      24.069  70.724  -9.400  1.00 27.07           C  
ATOM   2263  CG2 ILE A 315      21.839  71.170 -10.459  1.00 25.41           C  
ATOM   2264  CD1 ILE A 315      23.467  70.714  -8.019  1.00 27.92           C  
ATOM   2265  N   GLU A 316      23.503  73.160 -13.316  1.00 26.28           N  
ATOM   2266  CA  GLU A 316      22.830  73.799 -14.431  1.00 26.08           C  
ATOM   2267  C   GLU A 316      23.159  73.119 -15.745  1.00 26.29           C  
ATOM   2268  O   GLU A 316      22.299  73.029 -16.613  1.00 26.37           O  
ATOM   2269  CB  GLU A 316      23.119  75.285 -14.474  1.00 25.48           C  
ATOM   2270  CG  GLU A 316      22.349  75.994 -13.406  1.00 26.08           C  
ATOM   2271  CD  GLU A 316      22.679  77.450 -13.302  1.00 27.43           C  
ATOM   2272  OE1 GLU A 316      21.992  78.149 -12.513  1.00 26.27           O  
ATOM   2273  OE2 GLU A 316      23.622  77.897 -14.003  1.00 28.50           O  
ATOM   2274  N   ASP A 317      24.385  72.617 -15.870  1.00 26.35           N  
ATOM   2275  CA  ASP A 317      24.823  71.951 -17.082  1.00 27.00           C  
ATOM   2276  C   ASP A 317      24.148  70.584 -17.232  1.00 26.96           C  
ATOM   2277  O   ASP A 317      23.865  70.111 -18.344  1.00 27.17           O  
ATOM   2278  CB  ASP A 317      26.337  71.802 -17.054  1.00 27.72           C  
ATOM   2279  CG  ASP A 317      26.920  71.422 -18.407  1.00 30.81           C  
ATOM   2280  OD1 ASP A 317      28.060  70.882 -18.436  1.00 34.06           O  
ATOM   2281  OD2 ASP A 317      26.247  71.652 -19.441  1.00 34.08           O  
ATOM   2282  N   ILE A 318      23.894  69.951 -16.095  1.00 26.58           N  
ATOM   2283  CA  ILE A 318      23.221  68.673 -16.053  1.00 25.68           C  
ATOM   2284  C   ILE A 318      21.784  68.897 -16.482  1.00 26.19           C  
ATOM   2285  O   ILE A 318      21.222  68.121 -17.253  1.00 26.98           O  
ATOM   2286  CB  ILE A 318      23.328  68.043 -14.636  1.00 25.27           C  
ATOM   2287  CG1 ILE A 318      24.682  67.339 -14.491  1.00 23.26           C  
ATOM   2288  CG2 ILE A 318      22.155  67.117 -14.343  1.00 23.92           C  
ATOM   2289  CD1 ILE A 318      25.143  67.120 -13.079  1.00 21.17           C  
ATOM   2290  N   ASP A 319      21.191  69.985 -16.012  1.00 26.31           N  
ATOM   2291  CA  ASP A 319      19.776  70.194 -16.249  1.00 26.15           C  
ATOM   2292  C   ASP A 319      19.491  70.377 -17.720  1.00 26.53           C  
ATOM   2293  O   ASP A 319      18.409  70.051 -18.175  1.00 26.22           O  
ATOM   2294  CB  ASP A 319      19.268  71.396 -15.486  1.00 25.75           C  
ATOM   2295  CG  ASP A 319      17.784  71.445 -15.463  1.00 26.08           C  
ATOM   2296  OD1 ASP A 319      17.192  70.551 -14.818  1.00 27.12           O  
ATOM   2297  OD2 ASP A 319      17.208  72.348 -16.107  1.00 25.82           O  
ATOM   2298  N   ARG A 320      20.460  70.911 -18.460  1.00 27.15           N  
ATOM   2299  CA  ARG A 320      20.244  71.165 -19.864  1.00 28.37           C  
ATOM   2300  C   ARG A 320      20.134  69.841 -20.603  1.00 29.17           C  
ATOM   2301  O   ARG A 320      19.230  69.646 -21.428  1.00 28.76           O  
ATOM   2302  CB  ARG A 320      21.355  72.023 -20.438  1.00 28.45           C  
ATOM   2303  CG  ARG A 320      21.158  73.505 -20.203  1.00 29.19           C  
ATOM   2304  CD  ARG A 320      22.328  74.299 -20.784  1.00 29.21           C  
ATOM   2305  NE  ARG A 320      23.000  75.065 -19.733  1.00 29.25           N  
ATOM   2306  CZ  ARG A 320      24.249  74.846 -19.329  1.00 28.66           C  
ATOM   2307  NH1 ARG A 320      24.984  73.904 -19.889  1.00 27.99           N  
ATOM   2308  NH2 ARG A 320      24.774  75.584 -18.369  1.00 29.69           N  
ATOM   2309  N   ALA A 321      21.044  68.930 -20.245  1.00 30.07           N  
ATOM   2310  CA  ALA A 321      21.110  67.575 -20.766  1.00 30.53           C  
ATOM   2311  C   ALA A 321      19.802  66.786 -20.612  1.00 31.43           C  
ATOM   2312  O   ALA A 321      19.554  65.828 -21.358  1.00 31.84           O  
ATOM   2313  CB  ALA A 321      22.214  66.857 -20.094  1.00 30.22           C  
HETATM 2314  N   MSE A 322      18.955  67.178 -19.673  1.00 31.76           N  
HETATM 2315  CA  MSE A 322      17.731  66.435 -19.481  1.00 32.52           C  
HETATM 2316  C   MSE A 322      16.517  66.893 -20.263  1.00 32.74           C  
HETATM 2317  O   MSE A 322      15.401  66.446 -20.001  1.00 32.72           O  
HETATM 2318  CB  MSE A 322      17.435  66.352 -18.019  1.00 32.86           C  
HETATM 2319  CG  MSE A 322      18.275  65.302 -17.452  1.00 34.89           C  
HETATM 2320 SE   MSE A 322      18.195  65.484 -15.585  1.00 42.64          SE  
HETATM 2321  CE  MSE A 322      19.839  64.496 -15.192  1.00 38.29           C  
ATOM   2322  N   GLU A 323      16.745  67.766 -21.236  1.00 33.34           N  
ATOM   2323  CA  GLU A 323      15.710  68.209 -22.170  1.00 34.04           C  
ATOM   2324  C   GLU A 323      14.942  67.062 -22.889  1.00 33.75           C  
ATOM   2325  O   GLU A 323      13.718  67.108 -23.001  1.00 34.17           O  
ATOM   2326  CB  GLU A 323      16.334  69.146 -23.199  1.00 34.51           C  
ATOM   2327  CG  GLU A 323      15.445  70.302 -23.637  1.00 37.78           C  
ATOM   2328  CD  GLU A 323      15.623  70.641 -25.114  1.00 42.62           C  
ATOM   2329  OE1 GLU A 323      16.272  69.841 -25.851  1.00 43.84           O  
ATOM   2330  OE2 GLU A 323      15.091  71.701 -25.541  1.00 45.05           O  
ATOM   2331  N   PRO A 324      15.641  66.030 -23.380  1.00 33.26           N  
ATOM   2332  CA  PRO A 324      14.798  65.043 -24.030  1.00 33.09           C  
ATOM   2333  C   PRO A 324      13.769  64.402 -23.112  1.00 33.05           C  
ATOM   2334  O   PRO A 324      12.665  64.111 -23.561  1.00 33.48           O  
ATOM   2335  CB  PRO A 324      15.786  63.995 -24.545  1.00 32.98           C  
ATOM   2336  CG  PRO A 324      17.138  64.452 -24.141  1.00 33.24           C  
ATOM   2337  CD  PRO A 324      17.062  65.857 -23.715  1.00 33.41           C  
ATOM   2338  N   LEU A 325      14.105  64.216 -21.839  1.00 32.78           N  
ATOM   2339  CA  LEU A 325      13.271  63.446 -20.928  1.00 32.33           C  
ATOM   2340  C   LEU A 325      11.871  63.976 -20.874  1.00 32.99           C  
ATOM   2341  O   LEU A 325      10.929  63.212 -20.767  1.00 33.92           O  
ATOM   2342  CB  LEU A 325      13.860  63.460 -19.538  1.00 32.01           C  
ATOM   2343  CG  LEU A 325      14.886  62.407 -19.117  1.00 31.35           C  
ATOM   2344  CD1 LEU A 325      15.755  61.860 -20.245  1.00 29.91           C  
ATOM   2345  CD2 LEU A 325      15.754  62.979 -18.012  1.00 29.59           C  
ATOM   2346  N   LYS A 326      11.729  65.289 -20.963  1.00 33.66           N  
ATOM   2347  CA  LYS A 326      10.417  65.950 -21.018  1.00 34.47           C  
ATOM   2348  C   LYS A 326       9.341  65.299 -21.904  1.00 34.70           C  
ATOM   2349  O   LYS A 326       8.149  65.457 -21.635  1.00 35.22           O  
ATOM   2350  CB  LYS A 326      10.588  67.391 -21.494  1.00 34.57           C  
ATOM   2351  CG  LYS A 326      10.594  68.430 -20.401  1.00 35.36           C  
ATOM   2352  CD  LYS A 326      10.268  69.794 -21.004  1.00 38.06           C  
ATOM   2353  CE  LYS A 326      11.511  70.575 -21.444  1.00 38.34           C  
ATOM   2354  NZ  LYS A 326      12.711  69.711 -21.649  1.00 39.16           N  
ATOM   2355  N   SER A 327       9.752  64.589 -22.952  1.00 34.55           N  
ATOM   2356  CA  SER A 327       8.818  64.150 -23.986  1.00 34.55           C  
ATOM   2357  C   SER A 327       8.810  62.646 -24.241  1.00 34.32           C  
ATOM   2358  O   SER A 327       8.314  62.180 -25.263  1.00 34.03           O  
ATOM   2359  CB  SER A 327       9.101  64.904 -25.296  1.00 34.87           C  
ATOM   2360  OG  SER A 327      10.470  64.815 -25.652  1.00 35.18           O  
ATOM   2361  N   ILE A 328       9.347  61.869 -23.322  1.00 34.22           N  
ATOM   2362  CA  ILE A 328       9.313  60.443 -23.544  1.00 34.44           C  
ATOM   2363  C   ILE A 328       8.525  59.690 -22.493  1.00 34.95           C  
ATOM   2364  O   ILE A 328       8.711  58.486 -22.319  1.00 35.22           O  
ATOM   2365  CB  ILE A 328      10.713  59.859 -23.713  1.00 34.39           C  
ATOM   2366  CG1 ILE A 328      11.495  59.925 -22.398  1.00 34.65           C  
ATOM   2367  CG2 ILE A 328      11.432  60.565 -24.855  1.00 33.64           C  
ATOM   2368  CD1 ILE A 328      12.883  59.287 -22.486  1.00 34.11           C  
ATOM   2369  N   GLY A 329       7.613  60.390 -21.826  1.00 35.33           N  
ATOM   2370  CA  GLY A 329       6.841  59.804 -20.738  1.00 36.05           C  
ATOM   2371  C   GLY A 329       5.694  58.922 -21.194  1.00 36.79           C  
ATOM   2372  O   GLY A 329       5.114  58.179 -20.392  1.00 36.99           O  
ATOM   2373  N   ASP A 330       5.358  59.029 -22.478  1.00 37.38           N  
ATOM   2374  CA  ASP A 330       4.302  58.247 -23.118  1.00 37.88           C  
ATOM   2375  C   ASP A 330       4.700  56.778 -23.126  1.00 37.60           C  
ATOM   2376  O   ASP A 330       3.854  55.898 -23.012  1.00 37.76           O  
ATOM   2377  CB  ASP A 330       4.058  58.746 -24.557  1.00 38.45           C  
ATOM   2378  CG  ASP A 330       5.376  58.926 -25.372  1.00 40.87           C  
ATOM   2379  OD1 ASP A 330       6.208  59.799 -24.998  1.00 43.10           O  
ATOM   2380  OD2 ASP A 330       5.582  58.206 -26.392  1.00 42.98           O  
ATOM   2381  N   HIS A 331       6.005  56.531 -23.242  1.00 37.26           N  
ATOM   2382  CA  HIS A 331       6.546  55.178 -23.286  1.00 36.46           C  
ATOM   2383  C   HIS A 331       7.704  54.925 -22.295  1.00 35.19           C  
ATOM   2384  O   HIS A 331       8.336  53.874 -22.355  1.00 35.53           O  
ATOM   2385  CB  HIS A 331       6.973  54.833 -24.711  1.00 37.03           C  
ATOM   2386  CG  HIS A 331       8.228  55.526 -25.161  1.00 39.84           C  
ATOM   2387  ND1 HIS A 331       8.230  56.508 -26.131  1.00 43.39           N  
ATOM   2388  CD2 HIS A 331       9.525  55.365 -24.791  1.00 42.47           C  
ATOM   2389  CE1 HIS A 331       9.471  56.926 -26.334  1.00 43.39           C  
ATOM   2390  NE2 HIS A 331      10.275  56.251 -25.531  1.00 42.97           N  
ATOM   2391  N   ALA A 332       7.991  55.859 -21.388  1.00 33.16           N  
ATOM   2392  CA  ALA A 332       8.991  55.586 -20.350  1.00 31.06           C  
ATOM   2393  C   ALA A 332       8.637  56.120 -18.986  1.00 29.57           C  
ATOM   2394  O   ALA A 332       7.724  56.915 -18.847  1.00 29.46           O  
ATOM   2395  CB  ALA A 332      10.358  56.083 -20.762  1.00 31.18           C  
ATOM   2396  N   VAL A 333       9.386  55.671 -17.987  1.00 27.77           N  
ATOM   2397  CA  VAL A 333       9.266  56.164 -16.632  1.00 26.36           C  
ATOM   2398  C   VAL A 333      10.618  56.768 -16.247  1.00 25.72           C  
ATOM   2399  O   VAL A 333      11.658  56.094 -16.369  1.00 25.79           O  
ATOM   2400  CB  VAL A 333       8.917  55.038 -15.665  1.00 26.19           C  
ATOM   2401  CG1 VAL A 333       8.594  55.586 -14.320  1.00 26.59           C  
ATOM   2402  CG2 VAL A 333       7.731  54.275 -16.156  1.00 27.13           C  
ATOM   2403  N   ILE A 334      10.613  58.033 -15.811  1.00 24.05           N  
ATOM   2404  CA  ILE A 334      11.842  58.728 -15.448  1.00 22.43           C  
ATOM   2405  C   ILE A 334      11.909  58.866 -13.943  1.00 22.17           C  
ATOM   2406  O   ILE A 334      10.942  59.268 -13.319  1.00 21.71           O  
ATOM   2407  CB  ILE A 334      11.876  60.134 -16.061  1.00 22.61           C  
ATOM   2408  CG1 ILE A 334      11.599  60.096 -17.579  1.00 21.98           C  
ATOM   2409  CG2 ILE A 334      13.166  60.906 -15.672  1.00 20.99           C  
ATOM   2410  CD1 ILE A 334      12.538  59.232 -18.425  1.00 21.76           C  
ATOM   2411  N   CYS A 335      13.050  58.509 -13.361  1.00 21.86           N  
ATOM   2412  CA  CYS A 335      13.299  58.701 -11.938  1.00 21.38           C  
ATOM   2413  C   CYS A 335      14.624  59.389 -11.794  1.00 21.08           C  
ATOM   2414  O   CYS A 335      15.545  59.099 -12.544  1.00 20.41           O  
ATOM   2415  CB  CYS A 335      13.357  57.372 -11.206  1.00 21.55           C  
ATOM   2416  SG  CYS A 335      13.935  57.506  -9.488  1.00 23.51           S  
ATOM   2417  N   VAL A 336      14.717  60.313 -10.841  1.00 21.62           N  
ATOM   2418  CA  VAL A 336      15.966  61.034 -10.604  1.00 21.89           C  
ATOM   2419  C   VAL A 336      16.228  61.131  -9.126  1.00 23.21           C  
ATOM   2420  O   VAL A 336      15.394  61.650  -8.391  1.00 23.62           O  
ATOM   2421  CB  VAL A 336      15.964  62.461 -11.201  1.00 21.19           C  
ATOM   2422  CG1 VAL A 336      17.290  63.135 -10.942  1.00 20.25           C  
ATOM   2423  CG2 VAL A 336      15.687  62.448 -12.691  1.00 19.43           C  
ATOM   2424  N   THR A 337      17.382  60.628  -8.691  1.00 24.85           N  
ATOM   2425  CA  THR A 337      17.831  60.779  -7.288  1.00 26.51           C  
ATOM   2426  C   THR A 337      19.285  61.197  -7.196  1.00 27.65           C  
ATOM   2427  O   THR A 337      19.989  61.302  -8.189  1.00 27.45           O  
ATOM   2428  CB  THR A 337      17.784  59.463  -6.487  1.00 26.29           C  
ATOM   2429  OG1 THR A 337      17.089  58.457  -7.224  1.00 27.61           O  
ATOM   2430  CG2 THR A 337      17.131  59.677  -5.162  1.00 25.17           C  
ATOM   2431  N   GLY A 338      19.728  61.395  -5.969  1.00 29.51           N  
ATOM   2432  CA  GLY A 338      21.123  61.568  -5.677  1.00 32.13           C  
ATOM   2433  C   GLY A 338      21.655  60.420  -4.855  1.00 34.01           C  
ATOM   2434  O   GLY A 338      20.946  59.476  -4.553  1.00 33.97           O  
ATOM   2435  N   ASP A 339      22.916  60.538  -4.476  1.00 36.53           N  
ATOM   2436  CA  ASP A 339      23.665  59.493  -3.820  1.00 39.12           C  
ATOM   2437  C   ASP A 339      24.817  60.234  -3.180  1.00 40.54           C  
ATOM   2438  O   ASP A 339      25.049  61.392  -3.513  1.00 40.49           O  
ATOM   2439  CB  ASP A 339      24.174  58.543  -4.887  1.00 39.29           C  
ATOM   2440  CG  ASP A 339      24.896  57.348  -4.321  1.00 41.74           C  
ATOM   2441  OD1 ASP A 339      24.318  56.234  -4.395  1.00 43.91           O  
ATOM   2442  OD2 ASP A 339      26.038  57.517  -3.821  1.00 43.34           O  
ATOM   2443  N   HIS A 340      25.549  59.596  -2.270  1.00 43.11           N  
ATOM   2444  CA  HIS A 340      26.713  60.282  -1.678  1.00 45.39           C  
ATOM   2445  C   HIS A 340      28.111  59.641  -1.753  1.00 46.38           C  
ATOM   2446  O   HIS A 340      28.270  58.413  -1.777  1.00 46.43           O  
ATOM   2447  CB  HIS A 340      26.396  60.848  -0.292  1.00 45.77           C  
ATOM   2448  CG  HIS A 340      25.700  62.174  -0.345  1.00 47.23           C  
ATOM   2449  ND1 HIS A 340      24.418  62.366   0.130  1.00 47.87           N  
ATOM   2450  CD2 HIS A 340      26.104  63.371  -0.839  1.00 48.40           C  
ATOM   2451  CE1 HIS A 340      24.067  63.626  -0.056  1.00 48.66           C  
ATOM   2452  NE2 HIS A 340      25.072  64.256  -0.645  1.00 49.63           N  
ATOM   2453  N   SER A 341      29.103  60.536  -1.731  1.00 47.89           N  
ATOM   2454  CA  SER A 341      30.451  60.340  -2.302  1.00 48.98           C  
ATOM   2455  C   SER A 341      31.582  60.281  -1.249  1.00 49.02           C  
ATOM   2456  O   SER A 341      32.484  61.138  -1.215  1.00 48.95           O  
ATOM   2457  CB  SER A 341      30.708  61.489  -3.303  1.00 49.22           C  
ATOM   2458  OG  SER A 341      31.960  61.376  -3.960  1.00 50.45           O  
ATOM   2459  N   ASP A 352      21.995  61.752   5.715  1.00 31.37           N  
ATOM   2460  CA  ASP A 352      22.267  62.174   4.337  1.00 31.30           C  
ATOM   2461  C   ASP A 352      21.183  61.735   3.284  1.00 29.85           C  
ATOM   2462  O   ASP A 352      21.499  61.076   2.280  1.00 30.59           O  
ATOM   2463  CB  ASP A 352      23.693  61.734   3.942  1.00 31.76           C  
ATOM   2464  CG  ASP A 352      23.902  60.197   4.038  1.00 34.64           C  
ATOM   2465  OD1 ASP A 352      25.094  59.769   3.946  1.00 37.77           O  
ATOM   2466  OD2 ASP A 352      22.897  59.428   4.200  1.00 33.37           O  
ATOM   2467  N   PRO A 353      19.902  62.104   3.502  1.00 27.98           N  
ATOM   2468  CA  PRO A 353      18.902  61.723   2.507  1.00 26.03           C  
ATOM   2469  C   PRO A 353      18.795  62.710   1.361  1.00 24.17           C  
ATOM   2470  O   PRO A 353      19.014  63.915   1.548  1.00 24.34           O  
ATOM   2471  CB  PRO A 353      17.614  61.725   3.311  1.00 26.30           C  
ATOM   2472  CG  PRO A 353      17.837  62.735   4.362  1.00 26.60           C  
ATOM   2473  CD  PRO A 353      19.279  62.691   4.703  1.00 27.47           C  
ATOM   2474  N   VAL A 354      18.412  62.194   0.198  1.00 21.77           N  
ATOM   2475  CA  VAL A 354      18.418  62.934  -1.070  1.00 19.20           C  
ATOM   2476  C   VAL A 354      17.012  63.171  -1.640  1.00 18.44           C  
ATOM   2477  O   VAL A 354      16.058  62.523  -1.210  1.00 17.98           O  
ATOM   2478  CB  VAL A 354      19.252  62.180  -2.133  1.00 18.93           C  
ATOM   2479  CG1 VAL A 354      20.721  62.264  -1.807  1.00 18.00           C  
ATOM   2480  CG2 VAL A 354      18.795  60.717  -2.273  1.00 17.95           C  
ATOM   2481  N   PRO A 355      16.870  64.106  -2.605  1.00 17.80           N  
ATOM   2482  CA  PRO A 355      15.578  64.253  -3.260  1.00 17.56           C  
ATOM   2483  C   PRO A 355      15.399  63.228  -4.343  1.00 17.55           C  
ATOM   2484  O   PRO A 355      16.381  62.799  -4.951  1.00 18.06           O  
ATOM   2485  CB  PRO A 355      15.653  65.641  -3.895  1.00 16.98           C  
ATOM   2486  CG  PRO A 355      16.759  66.289  -3.262  1.00 17.09           C  
ATOM   2487  CD  PRO A 355      17.736  65.250  -2.908  1.00 17.64           C  
ATOM   2488  N   ILE A 356      14.148  62.851  -4.590  1.00 17.65           N  
ATOM   2489  CA  ILE A 356      13.812  61.917  -5.656  1.00 17.70           C  
ATOM   2490  C   ILE A 356      12.539  62.377  -6.334  1.00 18.01           C  
ATOM   2491  O   ILE A 356      11.635  62.838  -5.653  1.00 18.70           O  
ATOM   2492  CB  ILE A 356      13.663  60.485  -5.099  1.00 17.75           C  
ATOM   2493  CG1 ILE A 356      13.565  59.467  -6.233  1.00 17.42           C  
ATOM   2494  CG2 ILE A 356      12.526  60.402  -4.066  1.00 17.04           C  
ATOM   2495  CD1 ILE A 356      14.094  58.131  -5.829  1.00 17.63           C  
ATOM   2496  N   VAL A 357      12.486  62.285  -7.660  1.00 18.26           N  
ATOM   2497  CA  VAL A 357      11.290  62.584  -8.435  1.00 18.90           C  
ATOM   2498  C   VAL A 357      11.023  61.429  -9.395  1.00 19.88           C  
ATOM   2499  O   VAL A 357      11.971  60.950 -10.029  1.00 20.65           O  
ATOM   2500  CB  VAL A 357      11.466  63.852  -9.275  1.00 19.00           C  
ATOM   2501  CG1 VAL A 357      12.470  63.639 -10.391  1.00 18.75           C  
ATOM   2502  CG2 VAL A 357      10.165  64.229  -9.904  1.00 19.78           C  
ATOM   2503  N   PHE A 358       9.761  60.985  -9.499  1.00 20.20           N  
ATOM   2504  CA  PHE A 358       9.336  59.958 -10.469  1.00 20.70           C  
ATOM   2505  C   PHE A 358       8.356  60.540 -11.473  1.00 21.25           C  
ATOM   2506  O   PHE A 358       7.287  61.009 -11.101  1.00 21.23           O  
ATOM   2507  CB  PHE A 358       8.631  58.770  -9.787  1.00 20.68           C  
ATOM   2508  CG  PHE A 358       9.475  58.010  -8.831  1.00 20.80           C  
ATOM   2509  CD1 PHE A 358       9.492  58.341  -7.495  1.00 22.70           C  
ATOM   2510  CD2 PHE A 358      10.239  56.945  -9.260  1.00 22.27           C  
ATOM   2511  CE1 PHE A 358      10.282  57.626  -6.599  1.00 24.44           C  
ATOM   2512  CE2 PHE A 358      11.028  56.210  -8.375  1.00 22.38           C  
ATOM   2513  CZ  PHE A 358      11.054  56.550  -7.049  1.00 23.31           C  
ATOM   2514  N   TYR A 359       8.690  60.482 -12.750  1.00 22.75           N  
ATOM   2515  CA  TYR A 359       7.761  60.923 -13.784  1.00 24.50           C  
ATOM   2516  C   TYR A 359       7.471  59.877 -14.881  1.00 25.96           C  
ATOM   2517  O   TYR A 359       8.357  59.100 -15.274  1.00 26.15           O  
ATOM   2518  CB  TYR A 359       8.230  62.230 -14.422  1.00 24.06           C  
ATOM   2519  CG  TYR A 359       7.456  62.565 -15.674  1.00 24.99           C  
ATOM   2520  CD1 TYR A 359       6.141  63.053 -15.598  1.00 24.37           C  
ATOM   2521  CD2 TYR A 359       8.017  62.365 -16.928  1.00 24.96           C  
ATOM   2522  CE1 TYR A 359       5.420  63.339 -16.726  1.00 24.82           C  
ATOM   2523  CE2 TYR A 359       7.312  62.666 -18.068  1.00 27.27           C  
ATOM   2524  CZ  TYR A 359       6.005  63.143 -17.966  1.00 27.29           C  
ATOM   2525  OH  TYR A 359       5.299  63.425 -19.120  1.00 27.71           O  
ATOM   2526  N   THR A 360       6.207  59.873 -15.328  1.00 27.74           N  
ATOM   2527  CA  THR A 360       5.711  59.215 -16.558  1.00 28.84           C  
ATOM   2528  C   THR A 360       4.396  59.898 -16.999  1.00 30.44           C  
ATOM   2529  O   THR A 360       3.966  60.843 -16.359  1.00 30.43           O  
ATOM   2530  CB  THR A 360       5.509  57.681 -16.382  1.00 28.33           C  
ATOM   2531  OG1 THR A 360       5.336  57.085 -17.671  1.00 27.43           O  
ATOM   2532  CG2 THR A 360       4.295  57.384 -15.527  1.00 26.67           C  
ATOM   2533  N   ASP A 361       3.753  59.443 -18.075  1.00 32.51           N  
ATOM   2534  CA  ASP A 361       2.468  60.045 -18.470  1.00 34.46           C  
ATOM   2535  C   ASP A 361       1.309  59.670 -17.567  1.00 35.00           C  
ATOM   2536  O   ASP A 361       1.130  58.510 -17.215  1.00 35.01           O  
ATOM   2537  CB  ASP A 361       2.113  59.763 -19.930  1.00 35.21           C  
ATOM   2538  CG  ASP A 361       2.518  60.903 -20.846  1.00 37.37           C  
ATOM   2539  OD1 ASP A 361       1.625  61.556 -21.444  1.00 38.88           O  
ATOM   2540  OD2 ASP A 361       3.736  61.172 -20.930  1.00 39.43           O  
ATOM   2541  N   GLY A 362       0.530  60.679 -17.200  1.00 36.08           N  
ATOM   2542  CA  GLY A 362      -0.613  60.514 -16.306  1.00 37.33           C  
ATOM   2543  C   GLY A 362      -0.264  59.946 -14.952  1.00 38.25           C  
ATOM   2544  O   GLY A 362      -0.921  59.038 -14.483  1.00 38.55           O  
ATOM   2545  N   VAL A 363       0.766  60.477 -14.306  1.00 39.62           N  
ATOM   2546  CA  VAL A 363       1.194  59.912 -13.023  1.00 40.90           C  
ATOM   2547  C   VAL A 363       0.253  60.343 -11.889  1.00 41.88           C  
ATOM   2548  O   VAL A 363      -0.104  59.514 -11.030  1.00 41.51           O  
ATOM   2549  CB  VAL A 363       2.691  60.238 -12.658  1.00 40.81           C  
ATOM   2550  CG1 VAL A 363       3.398  60.984 -13.767  1.00 41.08           C  
ATOM   2551  CG2 VAL A 363       2.801  61.030 -11.383  1.00 40.71           C  
HETATM 2552  N   MSE A 364      -0.154  61.625 -11.918  1.00 42.96           N  
HETATM 2553  CA  MSE A 364      -0.854  62.296 -10.793  1.00 44.43           C  
HETATM 2554  C   MSE A 364       0.113  63.144  -9.904  1.00 43.03           C  
HETATM 2555  O   MSE A 364       0.548  62.696  -8.820  1.00 42.31           O  
HETATM 2556  CB  MSE A 364      -1.678  61.293  -9.918  1.00 46.02           C  
HETATM 2557  CG  MSE A 364      -2.921  60.573 -10.587  1.00 51.51           C  
HETATM 2558 SE   MSE A 364      -4.577  61.602 -11.061  1.00 63.96          SE  
HETATM 2559  CE  MSE A 364      -5.876  60.365 -10.199  1.00 60.61           C  
ATOM   2560  N   ASN A 365       0.428  64.358 -10.374  1.00 41.74           N  
ATOM   2561  CA  ASN A 365       1.311  65.281  -9.659  1.00 40.90           C  
ATOM   2562  C   ASN A 365       0.866  65.495  -8.225  1.00 39.94           C  
ATOM   2563  O   ASN A 365      -0.246  65.952  -8.004  1.00 40.44           O  
ATOM   2564  CB  ASN A 365       1.363  66.640 -10.367  1.00 41.05           C  
ATOM   2565  CG  ASN A 365       2.205  67.705  -9.595  1.00 41.91           C  
ATOM   2566  OD1 ASN A 365       1.906  68.903  -9.659  1.00 43.97           O  
ATOM   2567  ND2 ASN A 365       3.265  67.271  -8.906  1.00 41.22           N  
ATOM   2568  N   ASP A 366       1.738  65.196  -7.265  1.00 38.29           N  
ATOM   2569  CA  ASP A 366       1.430  65.361  -5.843  1.00 36.88           C  
ATOM   2570  C   ASP A 366       1.699  66.758  -5.253  1.00 35.68           C  
ATOM   2571  O   ASP A 366       1.794  66.899  -4.041  1.00 35.12           O  
ATOM   2572  CB  ASP A 366       2.185  64.318  -5.025  1.00 37.21           C  
ATOM   2573  CG  ASP A 366       3.699  64.566  -4.991  1.00 37.96           C  
ATOM   2574  OD1 ASP A 366       4.381  63.831  -4.244  1.00 39.49           O  
ATOM   2575  OD2 ASP A 366       4.210  65.479  -5.690  1.00 37.87           O  
ATOM   2576  N   GLY A 367       1.841  67.777  -6.099  1.00 34.61           N  
ATOM   2577  CA  GLY A 367       1.879  69.169  -5.624  1.00 33.70           C  
ATOM   2578  C   GLY A 367       3.224  69.870  -5.444  1.00 33.31           C  
ATOM   2579  O   GLY A 367       3.293  71.090  -5.410  1.00 32.92           O  
ATOM   2580  N   VAL A 368       4.304  69.108  -5.298  1.00 32.98           N  
ATOM   2581  CA  VAL A 368       5.649  69.698  -5.253  1.00 31.93           C  
ATOM   2582  C   VAL A 368       5.950  70.279  -6.631  1.00 31.91           C  
ATOM   2583  O   VAL A 368       5.541  69.692  -7.651  1.00 32.13           O  
ATOM   2584  CB  VAL A 368       6.694  68.648  -4.862  1.00 31.32           C  
ATOM   2585  CG1 VAL A 368       8.051  69.244  -4.821  1.00 30.04           C  
ATOM   2586  CG2 VAL A 368       6.346  68.087  -3.520  1.00 31.54           C  
ATOM   2587  N   HIS A 369       6.631  71.426  -6.673  1.00 31.20           N  
ATOM   2588  CA  HIS A 369       6.904  72.049  -7.957  1.00 30.88           C  
ATOM   2589  C   HIS A 369       8.369  72.199  -8.257  1.00 30.22           C  
ATOM   2590  O   HIS A 369       8.740  72.384  -9.414  1.00 31.09           O  
ATOM   2591  CB  HIS A 369       6.187  73.384  -8.084  1.00 31.19           C  
ATOM   2592  CG  HIS A 369       4.701  73.292  -7.889  1.00 33.67           C  
ATOM   2593  ND1 HIS A 369       4.054  73.838  -6.793  1.00 34.67           N  
ATOM   2594  CD2 HIS A 369       3.735  72.716  -8.652  1.00 34.48           C  
ATOM   2595  CE1 HIS A 369       2.755  73.616  -6.900  1.00 35.52           C  
ATOM   2596  NE2 HIS A 369       2.537  72.931  -8.014  1.00 35.77           N  
ATOM   2597  N   LEU A 370       9.211  72.137  -7.233  1.00 29.17           N  
ATOM   2598  CA  LEU A 370      10.658  72.237  -7.454  1.00 27.87           C  
ATOM   2599  C   LEU A 370      11.454  70.997  -6.990  1.00 27.40           C  
ATOM   2600  O   LEU A 370      11.084  70.320  -6.015  1.00 26.91           O  
ATOM   2601  CB  LEU A 370      11.218  73.508  -6.807  1.00 27.75           C  
ATOM   2602  CG  LEU A 370      10.358  74.766  -6.852  1.00 26.63           C  
ATOM   2603  CD1 LEU A 370      10.843  75.790  -5.828  1.00 26.10           C  
ATOM   2604  CD2 LEU A 370      10.357  75.318  -8.238  1.00 24.93           C  
ATOM   2605  N   PHE A 371      12.545  70.703  -7.702  1.00 26.32           N  
ATOM   2606  CA  PHE A 371      13.440  69.628  -7.297  1.00 25.09           C  
ATOM   2607  C   PHE A 371      14.596  70.176  -6.479  1.00 25.32           C  
ATOM   2608  O   PHE A 371      15.523  70.758  -7.022  1.00 25.65           O  
ATOM   2609  CB  PHE A 371      13.983  68.884  -8.516  1.00 24.24           C  
ATOM   2610  CG  PHE A 371      14.737  67.629  -8.180  1.00 21.31           C  
ATOM   2611  CD1 PHE A 371      14.070  66.499  -7.718  1.00 21.03           C  
ATOM   2612  CD2 PHE A 371      16.101  67.561  -8.354  1.00 18.83           C  
ATOM   2613  CE1 PHE A 371      14.768  65.319  -7.414  1.00 20.15           C  
ATOM   2614  CE2 PHE A 371      16.806  66.395  -8.070  1.00 18.35           C  
ATOM   2615  CZ  PHE A 371      16.140  65.270  -7.599  1.00 19.07           C  
ATOM   2616  N   ASP A 372      14.549  69.995  -5.170  1.00 25.25           N  
ATOM   2617  CA  ASP A 372      15.719  70.267  -4.349  1.00 25.23           C  
ATOM   2618  C   ASP A 372      15.485  69.644  -3.003  1.00 25.14           C  
ATOM   2619  O   ASP A 372      14.375  69.204  -2.716  1.00 25.06           O  
ATOM   2620  CB  ASP A 372      15.964  71.758  -4.207  1.00 25.36           C  
ATOM   2621  CG  ASP A 372      14.753  72.484  -3.743  1.00 26.89           C  
ATOM   2622  OD1 ASP A 372      14.405  72.349  -2.550  1.00 29.81           O  
ATOM   2623  OD2 ASP A 372      14.130  73.181  -4.571  1.00 28.87           O  
ATOM   2624  N   GLU A 373      16.516  69.613  -2.169  1.00 24.95           N  
ATOM   2625  CA  GLU A 373      16.414  68.858  -0.940  1.00 25.46           C  
ATOM   2626  C   GLU A 373      15.471  69.505   0.058  1.00 25.51           C  
ATOM   2627  O   GLU A 373      15.076  68.894   1.061  1.00 25.82           O  
ATOM   2628  CB  GLU A 373      17.788  68.527  -0.342  1.00 25.91           C  
ATOM   2629  CG  GLU A 373      18.805  69.673  -0.279  1.00 26.94           C  
ATOM   2630  CD  GLU A 373      19.424  70.030  -1.626  1.00 25.94           C  
ATOM   2631  OE1 GLU A 373      20.362  69.334  -2.075  1.00 25.30           O  
ATOM   2632  OE2 GLU A 373      18.980  71.037  -2.205  1.00 26.12           O  
ATOM   2633  N   LEU A 374      15.062  70.731  -0.240  1.00 25.31           N  
ATOM   2634  CA  LEU A 374      14.130  71.391   0.634  1.00 24.95           C  
ATOM   2635  C   LEU A 374      12.698  71.224   0.179  1.00 24.79           C  
ATOM   2636  O   LEU A 374      11.879  70.710   0.929  1.00 24.28           O  
ATOM   2637  CB  LEU A 374      14.503  72.850   0.820  1.00 25.23           C  
ATOM   2638  CG  LEU A 374      14.200  73.291   2.251  1.00 25.73           C  
ATOM   2639  CD1 LEU A 374      15.374  74.089   2.783  1.00 26.01           C  
ATOM   2640  CD2 LEU A 374      12.864  74.078   2.288  1.00 27.47           C  
ATOM   2641  N   SER A 375      12.393  71.623  -1.051  1.00 24.94           N  
ATOM   2642  CA  SER A 375      11.007  71.594  -1.490  1.00 25.33           C  
ATOM   2643  C   SER A 375      10.505  70.212  -1.838  1.00 25.66           C  
ATOM   2644  O   SER A 375       9.306  69.999  -1.902  1.00 26.01           O  
ATOM   2645  CB  SER A 375      10.707  72.601  -2.603  1.00 25.39           C  
ATOM   2646  OG  SER A 375      11.878  73.076  -3.216  1.00 26.02           O  
ATOM   2647  N   SER A 376      11.417  69.270  -2.028  1.00 26.42           N  
ATOM   2648  CA  SER A 376      11.041  67.882  -2.271  1.00 26.54           C  
ATOM   2649  C   SER A 376      10.536  67.176  -1.000  1.00 26.97           C  
ATOM   2650  O   SER A 376       9.893  66.135  -1.087  1.00 26.93           O  
ATOM   2651  CB  SER A 376      12.178  67.123  -2.975  1.00 26.88           C  
ATOM   2652  OG  SER A 376      12.351  67.578  -4.333  1.00 26.21           O  
ATOM   2653  N   ALA A 377      10.772  67.778   0.165  1.00 27.51           N  
ATOM   2654  CA  ALA A 377      10.261  67.267   1.445  1.00 27.97           C  
ATOM   2655  C   ALA A 377       8.766  67.426   1.578  1.00 28.66           C  
ATOM   2656  O   ALA A 377       8.131  66.793   2.408  1.00 29.05           O  
ATOM   2657  CB  ALA A 377      10.932  67.962   2.588  1.00 27.80           C  
ATOM   2658  N   SER A 378       8.196  68.288   0.763  1.00 29.66           N  
ATOM   2659  CA  SER A 378       6.779  68.530   0.845  1.00 30.77           C  
ATOM   2660  C   SER A 378       6.020  67.448   0.150  1.00 31.66           C  
ATOM   2661  O   SER A 378       4.830  67.286   0.404  1.00 32.65           O  
ATOM   2662  CB  SER A 378       6.434  69.874   0.241  1.00 30.63           C  
ATOM   2663  OG  SER A 378       6.863  70.861   1.151  1.00 30.99           O  
ATOM   2664  N   GLY A 379       6.709  66.697  -0.709  1.00 32.25           N  
ATOM   2665  CA  GLY A 379       6.103  65.576  -1.445  1.00 32.77           C  
ATOM   2666  C   GLY A 379       5.564  64.429  -0.596  1.00 33.07           C  
ATOM   2667  O   GLY A 379       5.804  64.366   0.622  1.00 32.67           O  
ATOM   2668  N   SER A 380       4.844  63.523  -1.258  1.00 33.59           N  
ATOM   2669  CA  SER A 380       4.211  62.369  -0.603  1.00 34.37           C  
ATOM   2670  C   SER A 380       5.189  61.287  -0.179  1.00 34.67           C  
ATOM   2671  O   SER A 380       5.025  60.695   0.885  1.00 35.53           O  
ATOM   2672  CB  SER A 380       3.124  61.757  -1.487  1.00 34.32           C  
ATOM   2673  OG  SER A 380       3.406  61.947  -2.865  1.00 34.97           O  
ATOM   2674  N   LEU A 381       6.221  61.066  -0.992  1.00 34.81           N  
ATOM   2675  CA  LEU A 381       7.152  59.936  -0.838  1.00 34.33           C  
ATOM   2676  C   LEU A 381       8.153  60.023   0.315  1.00 34.08           C  
ATOM   2677  O   LEU A 381       8.846  61.020   0.454  1.00 34.41           O  
ATOM   2678  CB  LEU A 381       7.902  59.729  -2.155  1.00 34.01           C  
ATOM   2679  CG  LEU A 381       7.303  58.770  -3.189  1.00 34.06           C  
ATOM   2680  CD1 LEU A 381       5.764  58.716  -3.244  1.00 33.98           C  
ATOM   2681  CD2 LEU A 381       7.872  59.073  -4.546  1.00 32.95           C  
ATOM   2682  N   ARG A 382       8.227  58.965   1.121  1.00 33.92           N  
ATOM   2683  CA  ARG A 382       9.264  58.804   2.145  1.00 34.23           C  
ATOM   2684  C   ARG A 382       9.781  57.373   2.116  1.00 33.91           C  
ATOM   2685  O   ARG A 382       9.186  56.471   2.710  1.00 34.62           O  
ATOM   2686  CB  ARG A 382       8.749  59.144   3.551  1.00 34.52           C  
ATOM   2687  CG  ARG A 382       8.479  60.632   3.809  1.00 36.60           C  
ATOM   2688  CD  ARG A 382       9.739  61.498   3.697  1.00 40.32           C  
ATOM   2689  NE  ARG A 382       9.542  62.808   4.319  1.00 43.84           N  
ATOM   2690  CZ  ARG A 382       8.971  63.866   3.738  1.00 45.63           C  
ATOM   2691  NH1 ARG A 382       8.524  63.810   2.477  1.00 46.44           N  
ATOM   2692  NH2 ARG A 382       8.842  64.997   4.428  1.00 45.97           N  
ATOM   2693  N   ILE A 383      10.897  57.164   1.434  1.00 32.97           N  
ATOM   2694  CA  ILE A 383      11.273  55.825   1.055  1.00 32.10           C  
ATOM   2695  C   ILE A 383      12.767  55.566   1.158  1.00 32.05           C  
ATOM   2696  O   ILE A 383      13.549  56.451   1.439  1.00 32.15           O  
ATOM   2697  CB  ILE A 383      10.814  55.533  -0.377  1.00 32.12           C  
ATOM   2698  CG1 ILE A 383      11.589  56.408  -1.355  1.00 31.22           C  
ATOM   2699  CG2 ILE A 383       9.298  55.733  -0.522  1.00 31.73           C  
ATOM   2700  CD1 ILE A 383      11.668  55.840  -2.718  1.00 31.02           C  
ATOM   2701  N   THR A 384      13.159  54.331   0.921  1.00 31.95           N  
ATOM   2702  CA  THR A 384      14.539  53.947   1.033  1.00 32.29           C  
ATOM   2703  C   THR A 384      14.935  53.459  -0.347  1.00 32.09           C  
ATOM   2704  O   THR A 384      14.078  53.323  -1.208  1.00 31.65           O  
ATOM   2705  CB  THR A 384      14.681  52.821   2.057  1.00 32.83           C  
ATOM   2706  OG1 THR A 384      15.001  51.589   1.388  1.00 33.57           O  
ATOM   2707  CG2 THR A 384      13.359  52.652   2.868  1.00 32.77           C  
ATOM   2708  N   SER A 385      16.213  53.179  -0.571  1.00 32.27           N  
ATOM   2709  CA  SER A 385      16.632  52.755  -1.898  1.00 33.13           C  
ATOM   2710  C   SER A 385      15.961  51.459  -2.281  1.00 33.84           C  
ATOM   2711  O   SER A 385      15.837  51.153  -3.463  1.00 33.78           O  
ATOM   2712  CB  SER A 385      18.144  52.601  -1.995  1.00 33.09           C  
ATOM   2713  OG  SER A 385      18.566  51.370  -1.438  1.00 34.82           O  
ATOM   2714  N   TYR A 386      15.528  50.701  -1.274  1.00 35.08           N  
ATOM   2715  CA  TYR A 386      14.892  49.412  -1.506  1.00 36.33           C  
ATOM   2716  C   TYR A 386      13.639  49.589  -2.325  1.00 35.63           C  
ATOM   2717  O   TYR A 386      13.399  48.820  -3.252  1.00 36.07           O  
ATOM   2718  CB  TYR A 386      14.529  48.689  -0.201  1.00 37.58           C  
ATOM   2719  CG  TYR A 386      13.623  47.495  -0.465  1.00 42.47           C  
ATOM   2720  CD1 TYR A 386      14.157  46.195  -0.591  1.00 47.18           C  
ATOM   2721  CD2 TYR A 386      12.236  47.669  -0.640  1.00 45.69           C  
ATOM   2722  CE1 TYR A 386      13.322  45.085  -0.875  1.00 50.36           C  
ATOM   2723  CE2 TYR A 386      11.389  46.581  -0.927  1.00 49.33           C  
ATOM   2724  CZ  TYR A 386      11.927  45.280  -1.043  1.00 51.66           C  
ATOM   2725  OH  TYR A 386      11.077  44.191  -1.318  1.00 52.68           O  
ATOM   2726  N   ASN A 387      12.862  50.612  -1.981  1.00 34.83           N  
ATOM   2727  CA  ASN A 387      11.514  50.791  -2.492  1.00 34.30           C  
ATOM   2728  C   ASN A 387      11.454  51.226  -3.924  1.00 34.46           C  
ATOM   2729  O   ASN A 387      10.378  51.205  -4.519  1.00 34.75           O  
ATOM   2730  CB  ASN A 387      10.770  51.829  -1.663  1.00 34.37           C  
ATOM   2731  CG  ASN A 387      10.404  51.324  -0.297  1.00 34.00           C  
ATOM   2732  OD1 ASN A 387       9.902  50.213  -0.172  1.00 37.12           O  
ATOM   2733  ND2 ASN A 387      10.651  52.127   0.739  1.00 31.21           N  
ATOM   2734  N   VAL A 388      12.595  51.624  -4.479  1.00 34.52           N  
ATOM   2735  CA  VAL A 388      12.616  52.276  -5.783  1.00 34.47           C  
ATOM   2736  C   VAL A 388      12.177  51.383  -6.927  1.00 35.40           C  
ATOM   2737  O   VAL A 388      11.379  51.824  -7.733  1.00 35.53           O  
ATOM   2738  CB  VAL A 388      13.956  52.957  -6.081  1.00 33.98           C  
ATOM   2739  CG1 VAL A 388      13.871  53.755  -7.356  1.00 32.33           C  
ATOM   2740  CG2 VAL A 388      14.306  53.869  -4.956  1.00 33.09           C  
HETATM 2741  N   MSE A 389      12.666  50.140  -6.992  1.00 36.83           N  
HETATM 2742  CA  MSE A 389      12.243  49.184  -8.052  1.00 38.27           C  
HETATM 2743  C   MSE A 389      10.725  49.058  -8.122  1.00 39.23           C  
HETATM 2744  O   MSE A 389      10.133  49.084  -9.195  1.00 39.28           O  
HETATM 2745  CB  MSE A 389      12.853  47.782  -7.865  1.00 38.32           C  
HETATM 2746  CG  MSE A 389      14.160  47.525  -8.603  1.00 38.65           C  
HETATM 2747 SE   MSE A 389      14.235  48.324 -10.390  1.00 42.20          SE  
HETATM 2748  CE  MSE A 389      16.137  48.022 -10.697  1.00 40.48           C  
ATOM   2749  N   ASP A 390      10.116  48.931  -6.950  1.00 40.69           N  
ATOM   2750  CA  ASP A 390       8.677  48.828  -6.795  1.00 42.06           C  
ATOM   2751  C   ASP A 390       7.920  50.000  -7.419  1.00 42.84           C  
ATOM   2752  O   ASP A 390       7.035  49.814  -8.256  1.00 43.09           O  
ATOM   2753  CB  ASP A 390       8.353  48.731  -5.311  1.00 42.35           C  
ATOM   2754  CG  ASP A 390       8.779  47.417  -4.724  1.00 43.80           C  
ATOM   2755  OD1 ASP A 390       9.902  47.351  -4.169  1.00 45.95           O  
ATOM   2756  OD2 ASP A 390       8.005  46.441  -4.850  1.00 45.14           O  
ATOM   2757  N   ILE A 391       8.277  51.206  -7.005  1.00 43.45           N  
ATOM   2758  CA  ILE A 391       7.624  52.398  -7.484  1.00 44.06           C  
ATOM   2759  C   ILE A 391       7.779  52.482  -8.985  1.00 45.10           C  
ATOM   2760  O   ILE A 391       6.850  52.858  -9.678  1.00 45.03           O  
ATOM   2761  CB  ILE A 391       8.213  53.626  -6.797  1.00 43.90           C  
ATOM   2762  CG1 ILE A 391       8.163  53.404  -5.278  1.00 43.52           C  
ATOM   2763  CG2 ILE A 391       7.496  54.884  -7.260  1.00 43.99           C  
ATOM   2764  CD1 ILE A 391       8.340  54.616  -4.401  1.00 43.44           C  
ATOM   2765  N   LEU A 392       8.946  52.095  -9.486  1.00 46.65           N  
ATOM   2766  CA  LEU A 392       9.209  52.147 -10.908  1.00 48.33           C  
ATOM   2767  C   LEU A 392       8.353  51.147 -11.657  1.00 49.99           C  
ATOM   2768  O   LEU A 392       7.516  51.536 -12.464  1.00 50.00           O  
ATOM   2769  CB  LEU A 392      10.693  51.930 -11.198  1.00 48.16           C  
ATOM   2770  CG  LEU A 392      11.588  53.119 -10.837  1.00 47.72           C  
ATOM   2771  CD1 LEU A 392      13.020  52.689 -10.762  1.00 46.86           C  
ATOM   2772  CD2 LEU A 392      11.427  54.234 -11.836  1.00 47.48           C  
HETATM 2773  N   MSE A 393       8.535  49.863 -11.367  1.00 52.24           N  
HETATM 2774  CA  MSE A 393       7.854  48.828 -12.135  1.00 54.68           C  
HETATM 2775  C   MSE A 393       6.349  48.799 -11.899  1.00 54.96           C  
HETATM 2776  O   MSE A 393       5.593  48.413 -12.791  1.00 55.47           O  
HETATM 2777  CB  MSE A 393       8.504  47.438 -11.967  1.00 55.87           C  
HETATM 2778  CG  MSE A 393       8.180  46.686 -10.686  1.00 60.10           C  
HETATM 2779 SE   MSE A 393       7.585  44.849 -11.094  1.00 71.73          SE  
HETATM 2780  CE  MSE A 393       5.608  45.107 -11.184  1.00 66.85           C  
ATOM   2781  N   GLN A 394       5.910  49.226 -10.722  1.00 55.43           N  
ATOM   2782  CA  GLN A 394       4.477  49.294 -10.435  1.00 56.07           C  
ATOM   2783  C   GLN A 394       3.916  50.648 -10.814  1.00 55.48           C  
ATOM   2784  O   GLN A 394       3.048  51.190 -10.134  1.00 55.48           O  
ATOM   2785  CB  GLN A 394       4.200  48.977  -8.962  1.00 56.86           C  
ATOM   2786  CG  GLN A 394       4.210  47.467  -8.619  1.00 60.06           C  
ATOM   2787  CD  GLN A 394       4.568  47.183  -7.148  1.00 64.14           C  
ATOM   2788  OE1 GLN A 394       4.168  47.931  -6.237  1.00 65.79           O  
ATOM   2789  NE2 GLN A 394       5.331  46.097  -6.916  1.00 64.28           N  
ATOM   2790  N   LEU A 395       4.429  51.175 -11.917  1.00 55.36           N  
ATOM   2791  CA  LEU A 395       4.117  52.507 -12.406  1.00 55.36           C  
ATOM   2792  C   LEU A 395       4.352  52.506 -13.898  1.00 55.76           C  
ATOM   2793  O   LEU A 395       4.022  53.459 -14.594  1.00 55.62           O  
ATOM   2794  CB  LEU A 395       5.031  53.542 -11.750  1.00 55.01           C  
ATOM   2795  CG  LEU A 395       4.678  55.028 -11.863  1.00 54.35           C  
ATOM   2796  CD1 LEU A 395       5.231  55.833 -10.701  1.00 52.27           C  
ATOM   2797  CD2 LEU A 395       5.226  55.563 -13.144  1.00 54.04           C  
ATOM   2798  N   ALA A 396       4.948  51.422 -14.378  1.00 56.46           N  
ATOM   2799  CA  ALA A 396       5.173  51.225 -15.797  1.00 56.94           C  
ATOM   2800  C   ALA A 396       4.133  50.259 -16.367  1.00 57.43           C  
ATOM   2801  O   ALA A 396       4.173  49.934 -17.558  1.00 57.52           O  
ATOM   2802  CB  ALA A 396       6.578  50.720 -16.039  1.00 56.80           C  
ATOM   2803  N   GLY A 397       3.206  49.814 -15.509  1.00 58.00           N  
ATOM   2804  CA  GLY A 397       2.074  48.960 -15.914  1.00 58.50           C  
ATOM   2805  C   GLY A 397       2.165  47.486 -15.509  1.00 58.86           C  
ATOM   2806  O   GLY A 397       1.223  46.722 -15.772  1.00 58.76           O  
TER    2807      GLY A 397                                                      
HETATM 2808  N   MSE B   2      38.728  23.439 -25.197  1.00 44.10           N  
HETATM 2809  CA  MSE B   2      39.100  24.102 -26.490  1.00 44.40           C  
HETATM 2810  C   MSE B   2      39.549  25.567 -26.265  1.00 42.27           C  
HETATM 2811  O   MSE B   2      39.030  26.260 -25.380  1.00 42.18           O  
HETATM 2812  CB  MSE B   2      37.956  23.991 -27.536  1.00 45.72           C  
HETATM 2813  CG  MSE B   2      36.979  25.204 -27.628  1.00 52.63           C  
HETATM 2814 SE   MSE B   2      36.392  25.841 -29.458  1.00 69.02          SE  
HETATM 2815  CE  MSE B   2      36.108  27.751 -29.021  1.00 64.20           C  
ATOM   2816  N   LYS B   3      40.509  26.026 -27.070  1.00 39.70           N  
ATOM   2817  CA  LYS B   3      41.134  27.336 -26.880  1.00 36.80           C  
ATOM   2818  C   LYS B   3      40.284  28.526 -27.341  1.00 35.20           C  
ATOM   2819  O   LYS B   3      39.312  28.382 -28.079  1.00 34.74           O  
ATOM   2820  CB  LYS B   3      42.489  27.385 -27.575  1.00 36.59           C  
ATOM   2821  CG  LYS B   3      43.430  26.271 -27.235  1.00 35.56           C  
ATOM   2822  CD  LYS B   3      44.858  26.621 -27.686  1.00 35.39           C  
ATOM   2823  CE  LYS B   3      45.640  25.370 -28.110  1.00 34.09           C  
ATOM   2824  NZ  LYS B   3      47.014  25.631 -28.589  1.00 31.66           N  
ATOM   2825  N   SER B   4      40.665  29.706 -26.874  1.00 33.44           N  
ATOM   2826  CA  SER B   4      40.046  30.954 -27.305  1.00 32.12           C  
ATOM   2827  C   SER B   4      40.860  31.588 -28.429  1.00 30.70           C  
ATOM   2828  O   SER B   4      42.006  31.177 -28.688  1.00 30.49           O  
ATOM   2829  CB  SER B   4      39.932  31.924 -26.140  1.00 32.13           C  
ATOM   2830  OG  SER B   4      41.079  31.821 -25.321  1.00 33.94           O  
ATOM   2831  N   ILE B   5      40.268  32.584 -29.092  1.00 28.44           N  
ATOM   2832  CA  ILE B   5      40.887  33.210 -30.256  1.00 26.19           C  
ATOM   2833  C   ILE B   5      41.000  34.720 -30.101  1.00 25.14           C  
ATOM   2834  O   ILE B   5      40.087  35.376 -29.618  1.00 24.72           O  
ATOM   2835  CB  ILE B   5      40.085  32.904 -31.536  1.00 26.50           C  
ATOM   2836  CG1 ILE B   5      39.864  31.394 -31.702  1.00 24.53           C  
ATOM   2837  CG2 ILE B   5      40.732  33.551 -32.766  1.00 25.84           C  
ATOM   2838  CD1 ILE B   5      38.701  31.070 -32.621  1.00 22.12           C  
ATOM   2839  N   ILE B   6      42.140  35.254 -30.514  1.00 23.95           N  
ATOM   2840  CA  ILE B   6      42.352  36.676 -30.559  1.00 22.98           C  
ATOM   2841  C   ILE B   6      42.775  37.058 -31.967  1.00 22.70           C  
ATOM   2842  O   ILE B   6      43.862  36.717 -32.411  1.00 22.30           O  
ATOM   2843  CB  ILE B   6      43.407  37.097 -29.553  1.00 23.09           C  
ATOM   2844  CG1 ILE B   6      43.027  36.549 -28.167  1.00 23.04           C  
ATOM   2845  CG2 ILE B   6      43.567  38.626 -29.558  1.00 23.28           C  
ATOM   2846  CD1 ILE B   6      43.920  37.003 -27.004  1.00 23.51           C  
ATOM   2847  N   LEU B   7      41.880  37.751 -32.666  1.00 22.52           N  
ATOM   2848  CA  LEU B   7      42.127  38.265 -33.990  1.00 22.46           C  
ATOM   2849  C   LEU B   7      42.365  39.764 -33.911  1.00 23.10           C  
ATOM   2850  O   LEU B   7      41.469  40.535 -33.624  1.00 23.77           O  
ATOM   2851  CB  LEU B   7      40.939  37.939 -34.900  1.00 22.24           C  
ATOM   2852  CG  LEU B   7      40.927  38.509 -36.331  1.00 21.68           C  
ATOM   2853  CD1 LEU B   7      42.222  38.281 -37.075  1.00 20.07           C  
ATOM   2854  CD2 LEU B   7      39.760  37.992 -37.131  1.00 20.73           C  
ATOM   2855  N   ILE B   8      43.588  40.172 -34.172  1.00 24.04           N  
ATOM   2856  CA  ILE B   8      43.979  41.566 -34.106  1.00 25.26           C  
ATOM   2857  C   ILE B   8      44.162  42.105 -35.509  1.00 26.23           C  
ATOM   2858  O   ILE B   8      45.090  41.686 -36.213  1.00 26.13           O  
ATOM   2859  CB  ILE B   8      45.311  41.693 -33.364  1.00 25.02           C  
ATOM   2860  CG1 ILE B   8      45.125  41.240 -31.929  1.00 25.72           C  
ATOM   2861  CG2 ILE B   8      45.814  43.110 -33.388  1.00 25.18           C  
ATOM   2862  CD1 ILE B   8      46.309  40.583 -31.359  1.00 27.33           C  
ATOM   2863  N   VAL B   9      43.287  43.031 -35.905  1.00 27.52           N  
ATOM   2864  CA  VAL B   9      43.374  43.697 -37.222  1.00 28.78           C  
ATOM   2865  C   VAL B   9      44.112  45.045 -37.170  1.00 30.06           C  
ATOM   2866  O   VAL B   9      43.634  45.991 -36.561  1.00 30.71           O  
ATOM   2867  CB  VAL B   9      41.973  43.948 -37.831  1.00 28.27           C  
ATOM   2868  CG1 VAL B   9      42.099  44.440 -39.251  1.00 27.77           C  
ATOM   2869  CG2 VAL B   9      41.153  42.706 -37.786  1.00 27.28           C  
ATOM   2870  N   LEU B  10      45.257  45.142 -37.822  1.00 31.81           N  
ATOM   2871  CA  LEU B  10      45.967  46.410 -37.906  1.00 34.22           C  
ATOM   2872  C   LEU B  10      45.537  47.237 -39.127  1.00 36.33           C  
ATOM   2873  O   LEU B  10      45.885  46.892 -40.252  1.00 36.40           O  
ATOM   2874  CB  LEU B  10      47.469  46.154 -37.975  1.00 33.71           C  
ATOM   2875  CG  LEU B  10      48.082  45.319 -36.866  1.00 33.26           C  
ATOM   2876  CD1 LEU B  10      49.549  45.151 -37.135  1.00 32.28           C  
ATOM   2877  CD2 LEU B  10      47.860  45.972 -35.502  1.00 33.59           C  
ATOM   2878  N   ASP B  11      44.800  48.328 -38.919  1.00 39.04           N  
ATOM   2879  CA  ASP B  11      44.395  49.194 -40.047  1.00 41.76           C  
ATOM   2880  C   ASP B  11      45.563  49.960 -40.620  1.00 43.03           C  
ATOM   2881  O   ASP B  11      46.508  50.280 -39.903  1.00 43.31           O  
ATOM   2882  CB  ASP B  11      43.310  50.177 -39.630  1.00 42.02           C  
ATOM   2883  CG  ASP B  11      42.087  49.478 -39.089  1.00 43.88           C  
ATOM   2884  OD1 ASP B  11      40.978  49.707 -39.635  1.00 46.07           O  
ATOM   2885  OD2 ASP B  11      42.251  48.678 -38.133  1.00 43.54           O  
ATOM   2886  N   GLY B  12      45.506  50.236 -41.916  1.00 44.77           N  
ATOM   2887  CA  GLY B  12      46.543  51.038 -42.558  1.00 47.29           C  
ATOM   2888  C   GLY B  12      47.724  50.265 -43.127  1.00 49.03           C  
ATOM   2889  O   GLY B  12      48.304  50.691 -44.143  1.00 49.14           O  
ATOM   2890  N   LEU B  13      48.069  49.135 -42.494  1.00 50.47           N  
ATOM   2891  CA  LEU B  13      49.243  48.322 -42.885  1.00 52.04           C  
ATOM   2892  C   LEU B  13      49.199  47.742 -44.281  1.00 53.10           C  
ATOM   2893  O   LEU B  13      48.150  47.726 -44.930  1.00 53.71           O  
ATOM   2894  CB  LEU B  13      49.550  47.217 -41.889  1.00 52.09           C  
ATOM   2895  CG  LEU B  13      50.290  47.737 -40.660  1.00 52.73           C  
ATOM   2896  CD1 LEU B  13      51.223  46.644 -40.163  1.00 52.35           C  
ATOM   2897  CD2 LEU B  13      51.019  49.079 -40.931  1.00 52.52           C  
ATOM   2898  N   GLY B  14      50.350  47.238 -44.719  1.00 54.19           N  
ATOM   2899  CA  GLY B  14      50.675  47.223 -46.148  1.00 55.22           C  
ATOM   2900  C   GLY B  14      51.538  48.466 -46.358  1.00 55.84           C  
ATOM   2901  O   GLY B  14      52.675  48.503 -45.868  1.00 56.08           O  
ATOM   2902  N   ASP B  15      50.988  49.502 -47.010  1.00 55.90           N  
ATOM   2903  CA  ASP B  15      51.758  50.709 -47.418  1.00 56.01           C  
ATOM   2904  C   ASP B  15      52.834  50.340 -48.458  1.00 55.76           C  
ATOM   2905  O   ASP B  15      53.007  49.164 -48.808  1.00 55.72           O  
ATOM   2906  CB  ASP B  15      52.383  51.464 -46.218  1.00 56.24           C  
ATOM   2907  CG  ASP B  15      51.358  51.820 -45.126  1.00 57.17           C  
ATOM   2908  OD1 ASP B  15      51.614  51.517 -43.930  1.00 57.71           O  
ATOM   2909  OD2 ASP B  15      50.301  52.401 -45.461  1.00 57.69           O  
ATOM   2910  N   ARG B  16      53.540  51.335 -48.974  1.00 55.33           N  
ATOM   2911  CA  ARG B  16      54.520  51.066 -50.016  1.00 55.03           C  
ATOM   2912  C   ARG B  16      55.907  51.540 -49.606  1.00 53.93           C  
ATOM   2913  O   ARG B  16      56.027  52.250 -48.606  1.00 54.15           O  
ATOM   2914  CB  ARG B  16      54.059  51.660 -51.342  1.00 55.64           C  
ATOM   2915  CG  ARG B  16      53.364  50.626 -52.197  1.00 58.62           C  
ATOM   2916  CD  ARG B  16      52.644  51.220 -53.407  1.00 63.20           C  
ATOM   2917  NE  ARG B  16      52.778  50.343 -54.581  1.00 67.71           N  
ATOM   2918  CZ  ARG B  16      52.220  49.132 -54.727  1.00 69.13           C  
ATOM   2919  NH1 ARG B  16      51.465  48.601 -53.764  1.00 69.57           N  
ATOM   2920  NH2 ARG B  16      52.427  48.439 -55.848  1.00 69.08           N  
ATOM   2921  N   PRO B  17      56.966  51.119 -50.334  1.00 52.75           N  
ATOM   2922  CA  PRO B  17      58.283  51.604 -49.894  1.00 52.05           C  
ATOM   2923  C   PRO B  17      58.499  53.101 -50.183  1.00 51.39           C  
ATOM   2924  O   PRO B  17      57.869  53.659 -51.078  1.00 51.28           O  
ATOM   2925  CB  PRO B  17      59.273  50.722 -50.671  1.00 51.86           C  
ATOM   2926  CG  PRO B  17      58.468  49.550 -51.130  1.00 51.90           C  
ATOM   2927  CD  PRO B  17      57.087  50.063 -51.354  1.00 52.38           C  
ATOM   2928  N   GLY B  18      59.341  53.745 -49.384  1.00 50.60           N  
ATOM   2929  CA  GLY B  18      59.754  55.109 -49.641  1.00 49.51           C  
ATOM   2930  C   GLY B  18      61.256  55.151 -49.511  1.00 48.87           C  
ATOM   2931  O   GLY B  18      61.838  54.377 -48.742  1.00 48.64           O  
ATOM   2932  N   SER B  19      61.895  56.048 -50.259  1.00 48.15           N  
ATOM   2933  CA  SER B  19      63.347  56.241 -50.133  1.00 47.38           C  
ATOM   2934  C   SER B  19      63.692  56.879 -48.775  1.00 46.82           C  
ATOM   2935  O   SER B  19      64.860  56.970 -48.377  1.00 46.85           O  
ATOM   2936  CB  SER B  19      63.924  57.043 -51.318  1.00 47.32           C  
ATOM   2937  OG  SER B  19      63.124  58.166 -51.641  1.00 47.17           O  
ATOM   2938  N   ASP B  20      62.653  57.308 -48.072  1.00 45.99           N  
ATOM   2939  CA  ASP B  20      62.789  57.839 -46.736  1.00 45.39           C  
ATOM   2940  C   ASP B  20      63.226  56.756 -45.732  1.00 44.24           C  
ATOM   2941  O   ASP B  20      64.033  57.022 -44.831  1.00 44.07           O  
ATOM   2942  CB  ASP B  20      61.463  58.485 -46.305  1.00 46.18           C  
ATOM   2943  CG  ASP B  20      61.394  60.002 -46.601  1.00 48.06           C  
ATOM   2944  OD1 ASP B  20      62.434  60.641 -46.929  1.00 50.22           O  
ATOM   2945  OD2 ASP B  20      60.272  60.553 -46.487  1.00 49.64           O  
ATOM   2946  N   LEU B  21      62.693  55.545 -45.885  1.00 42.86           N  
ATOM   2947  CA  LEU B  21      63.056  54.434 -45.012  1.00 41.80           C  
ATOM   2948  C   LEU B  21      64.053  53.524 -45.755  1.00 41.91           C  
ATOM   2949  O   LEU B  21      64.292  52.361 -45.371  1.00 42.04           O  
ATOM   2950  CB  LEU B  21      61.807  53.677 -44.537  1.00 41.12           C  
ATOM   2951  CG  LEU B  21      60.699  54.463 -43.825  1.00 39.17           C  
ATOM   2952  CD1 LEU B  21      59.404  53.749 -43.945  1.00 37.15           C  
ATOM   2953  CD2 LEU B  21      61.004  54.701 -42.367  1.00 37.47           C  
ATOM   2954  N   GLN B  22      64.633  54.090 -46.819  1.00 41.38           N  
ATOM   2955  CA  GLN B  22      65.641  53.440 -47.672  1.00 40.70           C  
ATOM   2956  C   GLN B  22      65.015  52.350 -48.524  1.00 40.03           C  
ATOM   2957  O   GLN B  22      65.498  51.216 -48.576  1.00 40.06           O  
ATOM   2958  CB  GLN B  22      66.842  52.945 -46.856  1.00 40.73           C  
ATOM   2959  CG  GLN B  22      67.489  54.050 -46.032  1.00 40.89           C  
ATOM   2960  CD  GLN B  22      68.616  53.552 -45.161  1.00 42.05           C  
ATOM   2961  OE1 GLN B  22      69.579  52.971 -45.661  1.00 42.26           O  
ATOM   2962  NE2 GLN B  22      68.512  53.785 -43.844  1.00 42.13           N  
ATOM   2963  N   ASN B  23      63.936  52.733 -49.202  1.00 39.11           N  
ATOM   2964  CA  ASN B  23      63.124  51.831 -50.041  1.00 38.51           C  
ATOM   2965  C   ASN B  23      62.692  50.539 -49.398  1.00 37.09           C  
ATOM   2966  O   ASN B  23      62.968  49.450 -49.894  1.00 37.31           O  
ATOM   2967  CB  ASN B  23      63.697  51.667 -51.449  1.00 38.68           C  
ATOM   2968  CG  ASN B  23      63.361  52.865 -52.303  1.00 40.84           C  
ATOM   2969  OD1 ASN B  23      62.167  53.177 -52.508  1.00 41.81           O  
ATOM   2970  ND2 ASN B  23      64.391  53.604 -52.736  1.00 41.42           N  
ATOM   2971  N   ARG B  24      62.003  50.721 -48.275  1.00 35.23           N  
ATOM   2972  CA  ARG B  24      61.428  49.677 -47.464  1.00 33.18           C  
ATOM   2973  C   ARG B  24      60.128  50.275 -46.977  1.00 31.77           C  
ATOM   2974  O   ARG B  24      60.002  51.492 -46.923  1.00 31.04           O  
ATOM   2975  CB  ARG B  24      62.312  49.427 -46.245  1.00 33.41           C  
ATOM   2976  CG  ARG B  24      63.717  48.962 -46.516  1.00 32.37           C  
ATOM   2977  CD  ARG B  24      64.364  48.555 -45.209  1.00 32.76           C  
ATOM   2978  NE  ARG B  24      64.685  49.715 -44.375  1.00 33.79           N  
ATOM   2979  CZ  ARG B  24      65.477  49.683 -43.305  1.00 33.26           C  
ATOM   2980  NH1 ARG B  24      66.044  48.549 -42.918  1.00 35.08           N  
ATOM   2981  NH2 ARG B  24      65.723  50.791 -42.629  1.00 31.90           N  
ATOM   2982  N   THR B  25      59.168  49.432 -46.600  1.00 30.24           N  
ATOM   2983  CA  THR B  25      57.896  49.925 -46.047  1.00 28.51           C  
ATOM   2984  C   THR B  25      58.115  50.300 -44.591  1.00 27.12           C  
ATOM   2985  O   THR B  25      59.137  49.942 -44.022  1.00 26.86           O  
ATOM   2986  CB  THR B  25      56.780  48.864 -46.113  1.00 28.53           C  
ATOM   2987  OG1 THR B  25      57.125  47.777 -45.253  1.00 30.20           O  
ATOM   2988  CG2 THR B  25      56.542  48.357 -47.548  1.00 26.69           C  
ATOM   2989  N   PRO B  26      57.159  51.020 -43.978  1.00 26.05           N  
ATOM   2990  CA  PRO B  26      57.265  51.279 -42.536  1.00 25.07           C  
ATOM   2991  C   PRO B  26      57.410  49.993 -41.727  1.00 23.99           C  
ATOM   2992  O   PRO B  26      58.155  49.941 -40.767  1.00 23.25           O  
ATOM   2993  CB  PRO B  26      55.934  51.969 -42.211  1.00 24.92           C  
ATOM   2994  CG  PRO B  26      55.569  52.668 -43.458  1.00 25.33           C  
ATOM   2995  CD  PRO B  26      56.043  51.775 -44.584  1.00 26.14           C  
ATOM   2996  N   LEU B  27      56.711  48.958 -42.165  1.00 23.65           N  
ATOM   2997  CA  LEU B  27      56.673  47.684 -41.497  1.00 22.88           C  
ATOM   2998  C   LEU B  27      57.998  46.958 -41.520  1.00 22.70           C  
ATOM   2999  O   LEU B  27      58.353  46.339 -40.523  1.00 23.04           O  
ATOM   3000  CB  LEU B  27      55.626  46.814 -42.143  1.00 22.94           C  
ATOM   3001  CG  LEU B  27      55.090  45.663 -41.321  1.00 23.69           C  
ATOM   3002  CD1 LEU B  27      54.933  46.055 -39.867  1.00 22.14           C  
ATOM   3003  CD2 LEU B  27      53.765  45.216 -41.935  1.00 23.49           C  
ATOM   3004  N   GLN B  28      58.734  47.003 -42.630  1.00 22.10           N  
ATOM   3005  CA  GLN B  28      60.037  46.318 -42.654  1.00 21.71           C  
ATOM   3006  C   GLN B  28      61.114  47.164 -41.991  1.00 21.04           C  
ATOM   3007  O   GLN B  28      62.189  46.673 -41.645  1.00 20.84           O  
ATOM   3008  CB  GLN B  28      60.488  45.940 -44.067  1.00 21.96           C  
ATOM   3009  CG  GLN B  28      59.402  45.778 -45.127  1.00 22.96           C  
ATOM   3010  CD  GLN B  28      59.923  46.124 -46.531  1.00 25.54           C  
ATOM   3011  OE1 GLN B  28      59.462  47.091 -47.167  1.00 26.15           O  
ATOM   3012  NE2 GLN B  28      60.919  45.357 -47.003  1.00 22.60           N  
ATOM   3013  N   ALA B  29      60.839  48.453 -41.840  1.00 20.57           N  
ATOM   3014  CA  ALA B  29      61.800  49.340 -41.205  1.00 19.95           C  
ATOM   3015  C   ALA B  29      61.683  49.232 -39.697  1.00 19.46           C  
ATOM   3016  O   ALA B  29      62.668  49.339 -38.995  1.00 19.00           O  
ATOM   3017  CB  ALA B  29      61.603  50.764 -41.653  1.00 19.48           C  
ATOM   3018  N   ALA B  30      60.474  48.990 -39.217  1.00 19.52           N  
ATOM   3019  CA  ALA B  30      60.183  48.998 -37.788  1.00 20.29           C  
ATOM   3020  C   ALA B  30      60.890  47.898 -36.958  1.00 20.82           C  
ATOM   3021  O   ALA B  30      60.931  46.727 -37.343  1.00 21.08           O  
ATOM   3022  CB  ALA B  30      58.680  48.951 -37.576  1.00 20.07           C  
ATOM   3023  N   PHE B  31      61.456  48.299 -35.825  1.00 21.02           N  
ATOM   3024  CA  PHE B  31      61.978  47.354 -34.833  1.00 21.40           C  
ATOM   3025  C   PHE B  31      60.775  46.616 -34.239  1.00 21.31           C  
ATOM   3026  O   PHE B  31      60.096  47.159 -33.359  1.00 21.40           O  
ATOM   3027  CB  PHE B  31      62.744  48.114 -33.732  1.00 21.11           C  
ATOM   3028  CG  PHE B  31      63.305  47.239 -32.663  1.00 20.88           C  
ATOM   3029  CD1 PHE B  31      64.344  46.332 -32.946  1.00 21.22           C  
ATOM   3030  CD2 PHE B  31      62.816  47.321 -31.344  1.00 20.59           C  
ATOM   3031  CE1 PHE B  31      64.886  45.494 -31.914  1.00 20.43           C  
ATOM   3032  CE2 PHE B  31      63.355  46.504 -30.298  1.00 18.24           C  
ATOM   3033  CZ  PHE B  31      64.385  45.587 -30.591  1.00 19.31           C  
ATOM   3034  N   ARG B  32      60.510  45.401 -34.731  1.00 20.99           N  
ATOM   3035  CA  ARG B  32      59.262  44.688 -34.421  1.00 20.72           C  
ATOM   3036  C   ARG B  32      59.474  43.276 -33.873  1.00 20.62           C  
ATOM   3037  O   ARG B  32      58.960  42.317 -34.450  1.00 21.86           O  
ATOM   3038  CB  ARG B  32      58.369  44.619 -35.671  1.00 20.58           C  
ATOM   3039  CG  ARG B  32      58.995  43.868 -36.833  1.00 20.52           C  
ATOM   3040  CD  ARG B  32      58.298  44.223 -38.111  1.00 22.84           C  
ATOM   3041  NE  ARG B  32      58.782  43.468 -39.269  1.00 22.41           N  
ATOM   3042  CZ  ARG B  32      59.924  43.709 -39.907  1.00 23.34           C  
ATOM   3043  NH1 ARG B  32      60.742  44.682 -39.514  1.00 21.75           N  
ATOM   3044  NH2 ARG B  32      60.253  42.962 -40.948  1.00 24.89           N  
ATOM   3045  N   PRO B  33      60.197  43.125 -32.749  1.00 20.10           N  
ATOM   3046  CA  PRO B  33      60.596  41.774 -32.388  1.00 19.21           C  
ATOM   3047  C   PRO B  33      59.446  40.862 -31.928  1.00 18.48           C  
ATOM   3048  O   PRO B  33      59.552  39.651 -32.083  1.00 19.19           O  
ATOM   3049  CB  PRO B  33      61.613  42.004 -31.273  1.00 19.33           C  
ATOM   3050  CG  PRO B  33      61.147  43.267 -30.606  1.00 20.31           C  
ATOM   3051  CD  PRO B  33      60.618  44.109 -31.731  1.00 20.52           C  
ATOM   3052  N   ASN B  34      58.355  41.412 -31.409  1.00 17.17           N  
ATOM   3053  CA  ASN B  34      57.255  40.564 -30.948  1.00 16.38           C  
ATOM   3054  C   ASN B  34      56.397  39.992 -32.062  1.00 15.77           C  
ATOM   3055  O   ASN B  34      56.001  38.848 -32.030  1.00 15.98           O  
ATOM   3056  CB  ASN B  34      56.374  41.314 -29.952  1.00 16.57           C  
ATOM   3057  CG  ASN B  34      57.043  41.512 -28.606  1.00 15.74           C  
ATOM   3058  OD1 ASN B  34      57.991  40.830 -28.247  1.00 15.19           O  
ATOM   3059  ND2 ASN B  34      56.540  42.456 -27.860  1.00 17.14           N  
ATOM   3060  N   LEU B  35      56.079  40.830 -33.026  1.00 15.65           N  
ATOM   3061  CA  LEU B  35      55.459  40.436 -34.274  1.00 15.21           C  
ATOM   3062  C   LEU B  35      56.369  39.440 -35.046  1.00 15.31           C  
ATOM   3063  O   LEU B  35      55.888  38.482 -35.657  1.00 13.66           O  
ATOM   3064  CB  LEU B  35      55.245  41.719 -35.072  1.00 14.89           C  
ATOM   3065  CG  LEU B  35      53.896  42.293 -35.485  1.00 15.87           C  
ATOM   3066  CD1 LEU B  35      52.695  41.848 -34.631  1.00 17.36           C  
ATOM   3067  CD2 LEU B  35      54.013  43.801 -35.473  1.00 16.60           C  
ATOM   3068  N   ASN B  36      57.687  39.661 -35.006  1.00 15.97           N  
ATOM   3069  CA  ASN B  36      58.624  38.755 -35.687  1.00 17.34           C  
ATOM   3070  C   ASN B  36      58.676  37.396 -35.019  1.00 17.91           C  
ATOM   3071  O   ASN B  36      58.705  36.362 -35.686  1.00 18.63           O  
ATOM   3072  CB  ASN B  36      60.030  39.326 -35.711  1.00 17.33           C  
ATOM   3073  CG  ASN B  36      60.199  40.391 -36.738  1.00 17.84           C  
ATOM   3074  OD1 ASN B  36      59.421  40.488 -37.677  1.00 19.19           O  
ATOM   3075  ND2 ASN B  36      61.238  41.199 -36.581  1.00 18.72           N  
ATOM   3076  N   TRP B  37      58.704  37.419 -33.693  1.00 17.63           N  
ATOM   3077  CA  TRP B  37      58.597  36.224 -32.917  1.00 17.29           C  
ATOM   3078  C   TRP B  37      57.328  35.468 -33.323  1.00 17.45           C  
ATOM   3079  O   TRP B  37      57.397  34.279 -33.637  1.00 17.70           O  
ATOM   3080  CB  TRP B  37      58.569  36.592 -31.437  1.00 17.54           C  
ATOM   3081  CG  TRP B  37      58.677  35.441 -30.533  1.00 16.53           C  
ATOM   3082  CD1 TRP B  37      59.801  34.970 -29.956  1.00 15.46           C  
ATOM   3083  CD2 TRP B  37      57.612  34.587 -30.115  1.00 16.50           C  
ATOM   3084  NE1 TRP B  37      59.511  33.872 -29.187  1.00 17.26           N  
ATOM   3085  CE2 TRP B  37      58.172  33.610 -29.272  1.00 17.33           C  
ATOM   3086  CE3 TRP B  37      56.240  34.550 -30.376  1.00 15.35           C  
ATOM   3087  CZ2 TRP B  37      57.409  32.593 -28.689  1.00 18.66           C  
ATOM   3088  CZ3 TRP B  37      55.469  33.557 -29.779  1.00 17.28           C  
ATOM   3089  CH2 TRP B  37      56.053  32.588 -28.944  1.00 18.14           C  
ATOM   3090  N   LEU B  38      56.180  36.142 -33.334  1.00 16.97           N  
ATOM   3091  CA  LEU B  38      54.946  35.485 -33.718  1.00 17.26           C  
ATOM   3092  C   LEU B  38      55.134  34.767 -35.036  1.00 17.84           C  
ATOM   3093  O   LEU B  38      54.726  33.614 -35.207  1.00 17.86           O  
ATOM   3094  CB  LEU B  38      53.807  36.483 -33.810  1.00 17.16           C  
ATOM   3095  CG  LEU B  38      52.739  36.580 -32.700  1.00 18.34           C  
ATOM   3096  CD1 LEU B  38      53.013  35.736 -31.467  1.00 17.29           C  
ATOM   3097  CD2 LEU B  38      52.543  38.026 -32.286  1.00 17.79           C  
ATOM   3098  N   ALA B  39      55.807  35.433 -35.959  1.00 18.63           N  
ATOM   3099  CA  ALA B  39      55.982  34.879 -37.288  1.00 19.28           C  
ATOM   3100  C   ALA B  39      56.819  33.619 -37.250  1.00 19.70           C  
ATOM   3101  O   ALA B  39      56.404  32.582 -37.801  1.00 19.79           O  
ATOM   3102  CB  ALA B  39      56.616  35.887 -38.200  1.00 19.57           C  
ATOM   3103  N   SER B  40      57.987  33.717 -36.596  1.00 19.62           N  
ATOM   3104  CA  SER B  40      58.957  32.622 -36.542  1.00 19.36           C  
ATOM   3105  C   SER B  40      58.397  31.419 -35.840  1.00 19.35           C  
ATOM   3106  O   SER B  40      58.853  30.334 -36.103  1.00 20.08           O  
ATOM   3107  CB  SER B  40      60.246  33.018 -35.829  1.00 19.17           C  
ATOM   3108  OG  SER B  40      60.227  34.370 -35.439  1.00 20.12           O  
ATOM   3109  N   HIS B  41      57.430  31.600 -34.940  1.00 19.55           N  
ATOM   3110  CA  HIS B  41      56.826  30.466 -34.223  1.00 19.59           C  
ATOM   3111  C   HIS B  41      55.462  30.095 -34.750  1.00 19.70           C  
ATOM   3112  O   HIS B  41      54.764  29.293 -34.140  1.00 20.47           O  
ATOM   3113  CB  HIS B  41      56.790  30.706 -32.705  1.00 19.55           C  
ATOM   3114  CG  HIS B  41      58.156  30.777 -32.092  1.00 20.62           C  
ATOM   3115  ND1 HIS B  41      58.781  31.971 -31.797  1.00 21.40           N  
ATOM   3116  CD2 HIS B  41      59.048  29.802 -31.793  1.00 20.63           C  
ATOM   3117  CE1 HIS B  41      59.990  31.727 -31.323  1.00 21.00           C  
ATOM   3118  NE2 HIS B  41      60.175  30.418 -31.306  1.00 21.26           N  
ATOM   3119  N   GLY B  42      55.088  30.655 -35.896  1.00 19.66           N  
ATOM   3120  CA  GLY B  42      53.767  30.397 -36.455  1.00 19.73           C  
ATOM   3121  C   GLY B  42      53.675  30.117 -37.946  1.00 19.85           C  
ATOM   3122  O   GLY B  42      54.679  29.876 -38.637  1.00 18.69           O  
ATOM   3123  N   ILE B  43      52.444  30.131 -38.441  1.00 20.39           N  
ATOM   3124  CA  ILE B  43      52.258  30.026 -39.877  1.00 21.50           C  
ATOM   3125  C   ILE B  43      51.983  31.404 -40.484  1.00 22.56           C  
ATOM   3126  O   ILE B  43      51.454  32.304 -39.821  1.00 22.78           O  
ATOM   3127  CB  ILE B  43      51.279  28.887 -40.309  1.00 21.36           C  
ATOM   3128  CG1 ILE B  43      49.863  29.135 -39.836  1.00 21.47           C  
ATOM   3129  CG2 ILE B  43      51.740  27.555 -39.750  1.00 19.88           C  
ATOM   3130  CD1 ILE B  43      48.968  27.971 -40.119  1.00 20.72           C  
ATOM   3131  N   ASN B  44      52.420  31.565 -41.727  1.00 23.65           N  
ATOM   3132  CA  ASN B  44      52.563  32.859 -42.359  1.00 24.74           C  
ATOM   3133  C   ASN B  44      51.994  32.859 -43.760  1.00 26.19           C  
ATOM   3134  O   ASN B  44      51.851  31.807 -44.391  1.00 26.45           O  
ATOM   3135  CB  ASN B  44      54.034  33.215 -42.423  1.00 24.33           C  
ATOM   3136  CG  ASN B  44      54.596  33.465 -41.090  1.00 23.53           C  
ATOM   3137  OD1 ASN B  44      54.348  34.505 -40.511  1.00 26.15           O  
ATOM   3138  ND2 ASN B  44      55.328  32.509 -40.563  1.00 22.90           N  
ATOM   3139  N   GLY B  45      51.673  34.045 -44.249  1.00 27.50           N  
ATOM   3140  CA  GLY B  45      51.019  34.142 -45.519  1.00 29.31           C  
ATOM   3141  C   GLY B  45      50.536  35.536 -45.812  1.00 30.79           C  
ATOM   3142  O   GLY B  45      50.835  36.486 -45.078  1.00 30.59           O  
ATOM   3143  N   ILE B  46      49.782  35.620 -46.902  1.00 32.23           N  
ATOM   3144  CA  ILE B  46      49.305  36.845 -47.478  1.00 34.27           C  
ATOM   3145  C   ILE B  46      47.814  36.660 -47.595  1.00 36.05           C  
ATOM   3146  O   ILE B  46      47.361  35.675 -48.159  1.00 36.52           O  
ATOM   3147  CB  ILE B  46      49.925  37.046 -48.894  1.00 33.95           C  
ATOM   3148  CG1 ILE B  46      51.443  37.162 -48.816  1.00 33.78           C  
ATOM   3149  CG2 ILE B  46      49.368  38.267 -49.588  1.00 34.18           C  
ATOM   3150  CD1 ILE B  46      51.951  38.250 -47.866  1.00 34.63           C  
HETATM 3151  N   MSE B  47      47.055  37.595 -47.045  1.00 38.80           N  
HETATM 3152  CA  MSE B  47      45.600  37.591 -47.163  1.00 41.86           C  
HETATM 3153  C   MSE B  47      45.135  38.822 -47.957  1.00 43.37           C  
HETATM 3154  O   MSE B  47      45.817  39.849 -47.960  1.00 43.36           O  
HETATM 3155  CB  MSE B  47      44.964  37.586 -45.774  1.00 41.97           C  
HETATM 3156  CG  MSE B  47      43.457  37.498 -45.782  1.00 44.46           C  
HETATM 3157 SE   MSE B  47      42.643  38.879 -44.664  1.00 51.95          SE  
HETATM 3158  CE  MSE B  47      42.657  40.402 -45.884  1.00 49.58           C  
ATOM   3159  N   HIS B  48      43.982  38.701 -48.629  1.00 45.72           N  
ATOM   3160  CA  HIS B  48      43.331  39.801 -49.388  1.00 47.54           C  
ATOM   3161  C   HIS B  48      41.810  39.628 -49.431  1.00 48.51           C  
ATOM   3162  O   HIS B  48      41.311  38.521 -49.268  1.00 48.54           O  
ATOM   3163  CB  HIS B  48      43.855  39.847 -50.818  1.00 47.84           C  
ATOM   3164  CG  HIS B  48      43.800  38.527 -51.509  1.00 48.94           C  
ATOM   3165  ND1 HIS B  48      42.733  38.142 -52.292  1.00 51.21           N  
ATOM   3166  CD2 HIS B  48      44.670  37.489 -51.517  1.00 50.78           C  
ATOM   3167  CE1 HIS B  48      42.955  36.927 -52.764  1.00 52.26           C  
ATOM   3168  NE2 HIS B  48      44.122  36.507 -52.305  1.00 52.62           N  
ATOM   3169  N   PRO B  49      41.063  40.728 -49.613  1.00 49.79           N  
ATOM   3170  CA  PRO B  49      39.608  40.560 -49.862  1.00 50.40           C  
ATOM   3171  C   PRO B  49      39.204  40.431 -51.346  1.00 50.58           C  
ATOM   3172  O   PRO B  49      38.135  39.870 -51.652  1.00 50.59           O  
ATOM   3173  CB  PRO B  49      38.987  41.814 -49.212  1.00 50.78           C  
ATOM   3174  CG  PRO B  49      40.110  42.365 -48.267  1.00 50.55           C  
ATOM   3175  CD  PRO B  49      41.377  42.040 -49.009  1.00 50.03           C  
ATOM   3176  N   THR B  60      33.695  46.499 -46.564  1.00 53.40           N  
ATOM   3177  CA  THR B  60      34.014  46.071 -45.205  1.00 53.30           C  
ATOM   3178  C   THR B  60      34.738  44.715 -45.207  1.00 52.94           C  
ATOM   3179  O   THR B  60      34.133  43.664 -45.506  1.00 52.99           O  
ATOM   3180  CB  THR B  60      32.739  46.049 -44.291  1.00 53.56           C  
ATOM   3181  OG1 THR B  60      32.168  47.366 -44.234  1.00 54.57           O  
ATOM   3182  CG2 THR B  60      33.060  45.588 -42.867  1.00 52.96           C  
ATOM   3183  N   SER B  61      36.037  44.769 -44.888  1.00 51.92           N  
ATOM   3184  CA  SER B  61      36.865  43.585 -44.698  1.00 50.91           C  
ATOM   3185  C   SER B  61      36.649  43.018 -43.303  1.00 50.22           C  
ATOM   3186  O   SER B  61      36.857  41.823 -43.069  1.00 50.20           O  
ATOM   3187  CB  SER B  61      38.343  43.931 -44.859  1.00 51.11           C  
ATOM   3188  OG  SER B  61      38.855  44.526 -43.672  1.00 51.58           O  
ATOM   3189  N   HIS B  62      36.250  43.885 -42.371  1.00 49.16           N  
ATOM   3190  CA  HIS B  62      36.055  43.488 -40.979  1.00 47.95           C  
ATOM   3191  C   HIS B  62      34.897  42.531 -40.822  1.00 47.44           C  
ATOM   3192  O   HIS B  62      34.913  41.674 -39.941  1.00 47.33           O  
ATOM   3193  CB  HIS B  62      35.821  44.703 -40.093  1.00 47.92           C  
ATOM   3194  CG  HIS B  62      37.042  45.529 -39.878  1.00 47.62           C  
ATOM   3195  ND1 HIS B  62      37.486  46.451 -40.801  1.00 48.74           N  
ATOM   3196  CD2 HIS B  62      37.919  45.568 -38.850  1.00 46.98           C  
ATOM   3197  CE1 HIS B  62      38.584  47.027 -40.346  1.00 48.20           C  
ATOM   3198  NE2 HIS B  62      38.872  46.502 -39.169  1.00 47.61           N  
HETATM 3199  N   MSE B  63      33.893  42.672 -41.678  1.00 46.65           N  
HETATM 3200  CA  MSE B  63      32.735  41.820 -41.583  1.00 46.16           C  
HETATM 3201  C   MSE B  63      33.005  40.391 -42.062  1.00 45.54           C  
HETATM 3202  O   MSE B  63      32.450  39.446 -41.492  1.00 45.70           O  
HETATM 3203  CB  MSE B  63      31.559  42.431 -42.325  1.00 46.75           C  
HETATM 3204  CG  MSE B  63      30.248  41.695 -42.106  1.00 48.10           C  
HETATM 3205 SE   MSE B  63      28.673  42.764 -42.505  1.00 52.24          SE  
HETATM 3206  CE  MSE B  63      29.340  43.761 -44.075  1.00 47.40           C  
ATOM   3207  N   SER B  64      33.837  40.222 -43.096  1.00 44.46           N  
ATOM   3208  CA  SER B  64      34.150  38.873 -43.588  1.00 43.52           C  
ATOM   3209  C   SER B  64      35.011  38.178 -42.562  1.00 42.68           C  
ATOM   3210  O   SER B  64      34.752  37.026 -42.212  1.00 42.82           O  
ATOM   3211  CB  SER B  64      34.872  38.871 -44.935  1.00 43.54           C  
ATOM   3212  OG  SER B  64      34.767  40.121 -45.587  1.00 45.25           O  
ATOM   3213  N   LEU B  65      36.021  38.889 -42.065  1.00 41.32           N  
ATOM   3214  CA  LEU B  65      36.856  38.374 -41.000  1.00 40.10           C  
ATOM   3215  C   LEU B  65      35.999  37.741 -39.910  1.00 39.61           C  
ATOM   3216  O   LEU B  65      36.319  36.669 -39.411  1.00 39.93           O  
ATOM   3217  CB  LEU B  65      37.754  39.476 -40.436  1.00 39.90           C  
ATOM   3218  CG  LEU B  65      38.964  39.856 -41.304  1.00 39.55           C  
ATOM   3219  CD1 LEU B  65      39.787  41.001 -40.721  1.00 37.75           C  
ATOM   3220  CD2 LEU B  65      39.860  38.657 -41.560  1.00 38.65           C  
ATOM   3221  N   LEU B  66      34.884  38.378 -39.580  1.00 38.73           N  
ATOM   3222  CA  LEU B  66      33.993  37.856 -38.567  1.00 38.36           C  
ATOM   3223  C   LEU B  66      33.092  36.733 -39.065  1.00 38.71           C  
ATOM   3224  O   LEU B  66      32.171  36.318 -38.366  1.00 38.00           O  
ATOM   3225  CB  LEU B  66      33.154  38.990 -37.999  1.00 38.22           C  
ATOM   3226  CG  LEU B  66      33.912  40.064 -37.234  1.00 37.54           C  
ATOM   3227  CD1 LEU B  66      33.048  41.281 -37.086  1.00 37.11           C  
ATOM   3228  CD2 LEU B  66      34.299  39.548 -35.880  1.00 38.10           C  
ATOM   3229  N   GLY B  67      33.349  36.257 -40.279  1.00 39.72           N  
ATOM   3230  CA  GLY B  67      32.639  35.105 -40.850  1.00 41.32           C  
ATOM   3231  C   GLY B  67      31.253  35.352 -41.437  1.00 42.47           C  
ATOM   3232  O   GLY B  67      30.379  34.472 -41.392  1.00 42.63           O  
ATOM   3233  N   TYR B  68      31.048  36.544 -41.993  1.00 43.40           N  
ATOM   3234  CA  TYR B  68      29.764  36.920 -42.594  1.00 43.84           C  
ATOM   3235  C   TYR B  68      30.044  37.395 -44.001  1.00 44.99           C  
ATOM   3236  O   TYR B  68      30.659  38.437 -44.180  1.00 44.95           O  
ATOM   3237  CB  TYR B  68      29.132  38.085 -41.824  1.00 43.24           C  
ATOM   3238  CG  TYR B  68      28.549  37.768 -40.475  1.00 40.07           C  
ATOM   3239  CD1 TYR B  68      29.354  37.667 -39.350  1.00 37.48           C  
ATOM   3240  CD2 TYR B  68      27.186  37.623 -40.323  1.00 38.36           C  
ATOM   3241  CE1 TYR B  68      28.817  37.395 -38.105  1.00 36.70           C  
ATOM   3242  CE2 TYR B  68      26.629  37.337 -39.091  1.00 38.71           C  
ATOM   3243  CZ  TYR B  68      27.447  37.228 -37.980  1.00 38.05           C  
ATOM   3244  OH  TYR B  68      26.876  36.945 -36.755  1.00 37.42           O  
ATOM   3245  N   ASP B  69      29.613  36.641 -45.002  1.00 46.83           N  
ATOM   3246  CA  ASP B  69      29.790  37.074 -46.396  1.00 48.66           C  
ATOM   3247  C   ASP B  69      29.127  38.444 -46.632  1.00 49.30           C  
ATOM   3248  O   ASP B  69      27.896  38.565 -46.545  1.00 49.05           O  
ATOM   3249  CB  ASP B  69      29.259  36.015 -47.384  1.00 48.86           C  
ATOM   3250  CG  ASP B  69      29.491  36.393 -48.864  1.00 51.11           C  
ATOM   3251  OD1 ASP B  69      28.748  35.880 -49.740  1.00 53.42           O  
ATOM   3252  OD2 ASP B  69      30.414  37.189 -49.164  1.00 52.82           O  
ATOM   3253  N   PRO B  70      29.948  39.480 -46.913  1.00 50.20           N  
ATOM   3254  CA  PRO B  70      29.384  40.778 -47.266  1.00 51.29           C  
ATOM   3255  C   PRO B  70      28.707  40.633 -48.619  1.00 52.52           C  
ATOM   3256  O   PRO B  70      29.231  39.921 -49.492  1.00 53.20           O  
ATOM   3257  CB  PRO B  70      30.617  41.672 -47.395  1.00 50.94           C  
ATOM   3258  CG  PRO B  70      31.675  40.754 -47.853  1.00 50.37           C  
ATOM   3259  CD  PRO B  70      31.405  39.449 -47.134  1.00 50.23           C  
ATOM   3260  N   LYS B  71      27.557  41.277 -48.788  1.00 53.27           N  
ATOM   3261  CA  LYS B  71      26.787  41.192 -50.035  1.00 54.38           C  
ATOM   3262  C   LYS B  71      25.683  40.150 -49.927  1.00 54.49           C  
ATOM   3263  O   LYS B  71      24.681  40.235 -50.639  1.00 54.62           O  
ATOM   3264  CB  LYS B  71      27.671  41.032 -51.311  1.00 54.78           C  
ATOM   3265  CG  LYS B  71      27.888  39.606 -51.858  1.00 55.90           C  
ATOM   3266  CD  LYS B  71      29.079  39.566 -52.826  1.00 57.96           C  
ATOM   3267  CE  LYS B  71      29.114  38.257 -53.622  1.00 59.88           C  
ATOM   3268  NZ  LYS B  71      29.019  37.045 -52.728  1.00 61.11           N  
ATOM   3269  N   VAL B  72      25.847  39.171 -49.045  1.00 54.60           N  
ATOM   3270  CA  VAL B  72      24.645  38.556 -48.496  1.00 55.06           C  
ATOM   3271  C   VAL B  72      24.246  39.346 -47.251  1.00 55.38           C  
ATOM   3272  O   VAL B  72      23.061  39.618 -47.027  1.00 55.38           O  
ATOM   3273  CB  VAL B  72      24.698  36.983 -48.301  1.00 55.00           C  
ATOM   3274  CG1 VAL B  72      26.095  36.429 -48.394  1.00 55.11           C  
ATOM   3275  CG2 VAL B  72      23.984  36.526 -47.016  1.00 54.60           C  
ATOM   3276  N   TYR B  73      25.244  39.783 -46.490  1.00 55.77           N  
ATOM   3277  CA  TYR B  73      24.971  40.423 -45.207  1.00 56.19           C  
ATOM   3278  C   TYR B  73      25.210  41.937 -45.106  1.00 56.21           C  
ATOM   3279  O   TYR B  73      24.699  42.565 -44.164  1.00 56.37           O  
ATOM   3280  CB  TYR B  73      25.676  39.672 -44.070  1.00 56.22           C  
ATOM   3281  CG  TYR B  73      25.040  38.342 -43.718  1.00 56.74           C  
ATOM   3282  CD1 TYR B  73      25.718  37.136 -43.942  1.00 57.87           C  
ATOM   3283  CD2 TYR B  73      23.767  38.286 -43.154  1.00 57.14           C  
ATOM   3284  CE1 TYR B  73      25.136  35.896 -43.608  1.00 58.52           C  
ATOM   3285  CE2 TYR B  73      23.169  37.063 -42.829  1.00 58.38           C  
ATOM   3286  CZ  TYR B  73      23.856  35.868 -43.049  1.00 58.88           C  
ATOM   3287  OH  TYR B  73      23.258  34.663 -42.716  1.00 58.71           O  
ATOM   3288  N   TYR B  74      25.955  42.522 -46.052  1.00 55.98           N  
ATOM   3289  CA  TYR B  74      26.219  43.976 -46.050  1.00 55.96           C  
ATOM   3290  C   TYR B  74      24.918  44.734 -45.824  1.00 54.94           C  
ATOM   3291  O   TYR B  74      23.962  44.544 -46.571  1.00 55.32           O  
ATOM   3292  CB  TYR B  74      26.875  44.437 -47.364  1.00 56.60           C  
ATOM   3293  CG  TYR B  74      27.233  45.925 -47.421  1.00 59.39           C  
ATOM   3294  CD1 TYR B  74      27.886  46.560 -46.345  1.00 62.10           C  
ATOM   3295  CD2 TYR B  74      26.950  46.697 -48.566  1.00 62.00           C  
ATOM   3296  CE1 TYR B  74      28.223  47.942 -46.388  1.00 63.33           C  
ATOM   3297  CE2 TYR B  74      27.290  48.083 -48.626  1.00 63.17           C  
ATOM   3298  CZ  TYR B  74      27.927  48.692 -47.529  1.00 63.66           C  
ATOM   3299  OH  TYR B  74      28.269  50.032 -47.567  1.00 63.48           O  
ATOM   3300  N   PRO B  75      24.864  45.589 -44.790  1.00 53.90           N  
ATOM   3301  CA  PRO B  75      23.551  46.157 -44.472  1.00 52.93           C  
ATOM   3302  C   PRO B  75      23.107  47.315 -45.398  1.00 52.03           C  
ATOM   3303  O   PRO B  75      21.911  47.603 -45.480  1.00 52.12           O  
ATOM   3304  CB  PRO B  75      23.717  46.604 -43.020  1.00 52.87           C  
ATOM   3305  CG  PRO B  75      25.189  46.932 -42.901  1.00 53.35           C  
ATOM   3306  CD  PRO B  75      25.931  46.115 -43.918  1.00 53.70           C  
ATOM   3307  N   GLY B  76      24.047  47.951 -46.100  1.00 51.01           N  
ATOM   3308  CA  GLY B  76      23.720  49.027 -47.048  1.00 49.67           C  
ATOM   3309  C   GLY B  76      24.017  50.411 -46.488  1.00 48.70           C  
ATOM   3310  O   GLY B  76      24.087  50.587 -45.268  1.00 48.82           O  
ATOM   3311  N   ARG B  77      24.173  51.399 -47.371  1.00 47.47           N  
ATOM   3312  CA  ARG B  77      24.675  52.722 -46.961  1.00 46.43           C  
ATOM   3313  C   ARG B  77      23.789  53.435 -45.920  1.00 45.06           C  
ATOM   3314  O   ARG B  77      24.301  54.013 -44.967  1.00 44.72           O  
ATOM   3315  CB  ARG B  77      25.056  53.614 -48.176  1.00 46.79           C  
ATOM   3316  CG  ARG B  77      23.898  54.163 -49.001  1.00 48.75           C  
ATOM   3317  CD  ARG B  77      24.078  53.928 -50.511  1.00 52.73           C  
ATOM   3318  NE  ARG B  77      22.775  53.896 -51.197  1.00 54.77           N  
ATOM   3319  CZ  ARG B  77      21.989  52.817 -51.336  1.00 55.80           C  
ATOM   3320  NH1 ARG B  77      22.346  51.617 -50.854  1.00 54.75           N  
ATOM   3321  NH2 ARG B  77      20.830  52.938 -51.983  1.00 56.79           N  
ATOM   3322  N   GLY B  78      22.474  53.357 -46.085  1.00 43.54           N  
ATOM   3323  CA  GLY B  78      21.573  53.919 -45.107  1.00 41.97           C  
ATOM   3324  C   GLY B  78      21.985  53.495 -43.713  1.00 41.19           C  
ATOM   3325  O   GLY B  78      22.485  54.310 -42.937  1.00 40.86           O  
ATOM   3326  N   PRO B  79      21.801  52.203 -43.391  1.00 40.64           N  
ATOM   3327  CA  PRO B  79      22.076  51.678 -42.061  1.00 40.21           C  
ATOM   3328  C   PRO B  79      23.503  51.919 -41.651  1.00 39.96           C  
ATOM   3329  O   PRO B  79      23.776  52.179 -40.492  1.00 39.26           O  
ATOM   3330  CB  PRO B  79      21.833  50.189 -42.231  1.00 40.07           C  
ATOM   3331  CG  PRO B  79      20.863  50.105 -43.304  1.00 40.01           C  
ATOM   3332  CD  PRO B  79      21.248  51.162 -44.267  1.00 40.40           C  
ATOM   3333  N   PHE B  80      24.403  51.855 -42.612  1.00 40.32           N  
ATOM   3334  CA  PHE B  80      25.795  52.170 -42.351  1.00 41.46           C  
ATOM   3335  C   PHE B  80      26.002  53.562 -41.709  1.00 41.17           C  
ATOM   3336  O   PHE B  80      26.758  53.690 -40.742  1.00 41.08           O  
ATOM   3337  CB  PHE B  80      26.609  52.028 -43.639  1.00 42.19           C  
ATOM   3338  CG  PHE B  80      28.083  52.081 -43.426  1.00 45.01           C  
ATOM   3339  CD1 PHE B  80      28.800  53.269 -43.700  1.00 47.56           C  
ATOM   3340  CD2 PHE B  80      28.766  50.958 -42.936  1.00 47.30           C  
ATOM   3341  CE1 PHE B  80      30.197  53.346 -43.492  1.00 47.85           C  
ATOM   3342  CE2 PHE B  80      30.157  51.011 -42.726  1.00 49.34           C  
ATOM   3343  CZ  PHE B  80      30.877  52.216 -43.007  1.00 49.13           C  
ATOM   3344  N   GLU B  81      25.332  54.589 -42.241  1.00 40.73           N  
ATOM   3345  CA  GLU B  81      25.421  55.936 -41.694  1.00 40.56           C  
ATOM   3346  C   GLU B  81      24.978  55.914 -40.239  1.00 40.08           C  
ATOM   3347  O   GLU B  81      25.676  56.398 -39.337  1.00 39.52           O  
ATOM   3348  CB  GLU B  81      24.531  56.880 -42.487  1.00 40.76           C  
ATOM   3349  CG  GLU B  81      24.811  58.359 -42.292  1.00 43.11           C  
ATOM   3350  CD  GLU B  81      25.730  58.917 -43.357  1.00 47.65           C  
ATOM   3351  OE1 GLU B  81      25.513  60.071 -43.805  1.00 50.20           O  
ATOM   3352  OE2 GLU B  81      26.666  58.194 -43.759  1.00 48.35           O  
ATOM   3353  N   ALA B  82      23.809  55.325 -40.033  1.00 39.77           N  
ATOM   3354  CA  ALA B  82      23.237  55.154 -38.720  1.00 39.84           C  
ATOM   3355  C   ALA B  82      24.214  54.519 -37.749  1.00 39.98           C  
ATOM   3356  O   ALA B  82      24.266  54.913 -36.596  1.00 40.25           O  
ATOM   3357  CB  ALA B  82      21.995  54.327 -38.814  1.00 39.99           C  
ATOM   3358  N   LEU B  83      24.977  53.533 -38.215  1.00 40.24           N  
ATOM   3359  CA  LEU B  83      26.070  52.933 -37.427  1.00 40.08           C  
ATOM   3360  C   LEU B  83      27.157  53.955 -37.129  1.00 40.29           C  
ATOM   3361  O   LEU B  83      27.635  54.053 -35.994  1.00 40.17           O  
ATOM   3362  CB  LEU B  83      26.684  51.731 -38.159  1.00 39.60           C  
ATOM   3363  CG  LEU B  83      26.267  50.309 -37.774  1.00 37.72           C  
ATOM   3364  CD1 LEU B  83      24.877  50.265 -37.207  1.00 34.13           C  
ATOM   3365  CD2 LEU B  83      26.409  49.382 -38.988  1.00 35.73           C  
ATOM   3366  N   GLY B  84      27.525  54.717 -38.156  1.00 40.58           N  
ATOM   3367  CA  GLY B  84      28.537  55.756 -38.033  1.00 41.00           C  
ATOM   3368  C   GLY B  84      28.191  56.788 -36.986  1.00 41.27           C  
ATOM   3369  O   GLY B  84      29.077  57.359 -36.373  1.00 41.33           O  
ATOM   3370  N   LEU B  85      26.903  57.011 -36.762  1.00 41.72           N  
ATOM   3371  CA  LEU B  85      26.465  58.049 -35.841  1.00 42.26           C  
ATOM   3372  C   LEU B  85      25.986  57.498 -34.492  1.00 42.72           C  
ATOM   3373  O   LEU B  85      24.873  57.810 -34.056  1.00 43.18           O  
ATOM   3374  CB  LEU B  85      25.344  58.881 -36.488  1.00 42.17           C  
ATOM   3375  CG  LEU B  85      25.583  60.057 -37.455  1.00 42.08           C  
ATOM   3376  CD1 LEU B  85      26.983  60.649 -37.365  1.00 42.51           C  
ATOM   3377  CD2 LEU B  85      25.231  59.724 -38.901  1.00 43.00           C  
ATOM   3378  N   GLY B  86      26.812  56.705 -33.813  1.00 42.92           N  
ATOM   3379  CA  GLY B  86      26.339  55.984 -32.621  1.00 43.33           C  
ATOM   3380  C   GLY B  86      25.230  55.084 -33.117  1.00 43.51           C  
ATOM   3381  O   GLY B  86      25.390  54.457 -34.150  1.00 44.41           O  
HETATM 3382  N   MSE B  87      24.105  55.019 -32.414  1.00 43.66           N  
HETATM 3383  CA  MSE B  87      22.859  54.490 -33.007  1.00 43.76           C  
HETATM 3384  C   MSE B  87      22.852  52.982 -33.250  1.00 44.57           C  
HETATM 3385  O   MSE B  87      23.726  52.424 -33.940  1.00 44.46           O  
HETATM 3386  CB  MSE B  87      22.550  55.212 -34.317  1.00 43.12           C  
HETATM 3387  CG  MSE B  87      21.141  55.734 -34.433  1.00 42.05           C  
HETATM 3388 SE   MSE B  87      20.924  56.953 -35.952  1.00 37.17          SE  
HETATM 3389  CE  MSE B  87      19.023  57.186 -35.754  1.00 38.02           C  
ATOM   3390  N   ASP B  88      21.844  52.324 -32.686  1.00 45.41           N  
ATOM   3391  CA  ASP B  88      21.746  50.881 -32.785  1.00 46.12           C  
ATOM   3392  C   ASP B  88      20.557  50.451 -33.625  1.00 46.22           C  
ATOM   3393  O   ASP B  88      19.411  50.621 -33.214  1.00 46.62           O  
ATOM   3394  CB  ASP B  88      21.696  50.245 -31.384  1.00 46.58           C  
ATOM   3395  CG  ASP B  88      23.051  50.322 -30.652  1.00 47.79           C  
ATOM   3396  OD1 ASP B  88      24.109  49.998 -31.261  1.00 48.51           O  
ATOM   3397  OD2 ASP B  88      23.053  50.702 -29.458  1.00 49.01           O  
ATOM   3398  N   ILE B  89      20.837  49.891 -34.798  1.00 45.97           N  
ATOM   3399  CA  ILE B  89      19.785  49.308 -35.628  1.00 45.89           C  
ATOM   3400  C   ILE B  89      19.666  47.788 -35.387  1.00 45.62           C  
ATOM   3401  O   ILE B  89      20.482  47.211 -34.668  1.00 45.83           O  
ATOM   3402  CB  ILE B  89      19.995  49.647 -37.128  1.00 45.85           C  
ATOM   3403  CG1 ILE B  89      20.878  48.621 -37.825  1.00 45.77           C  
ATOM   3404  CG2 ILE B  89      20.621  51.013 -37.272  1.00 46.37           C  
ATOM   3405  CD1 ILE B  89      22.336  48.920 -37.769  1.00 45.70           C  
ATOM   3406  N   ARG B  90      18.651  47.160 -35.981  1.00 45.04           N  
ATOM   3407  CA  ARG B  90      18.372  45.723 -35.821  1.00 44.64           C  
ATOM   3408  C   ARG B  90      17.835  45.139 -37.145  1.00 43.94           C  
ATOM   3409  O   ARG B  90      17.204  45.860 -37.911  1.00 44.54           O  
ATOM   3410  CB  ARG B  90      17.340  45.517 -34.708  1.00 44.79           C  
ATOM   3411  CG  ARG B  90      17.817  45.862 -33.297  1.00 45.80           C  
ATOM   3412  CD  ARG B  90      18.376  44.629 -32.607  1.00 49.43           C  
ATOM   3413  NE  ARG B  90      19.748  44.300 -33.027  1.00 52.59           N  
ATOM   3414  CZ  ARG B  90      20.228  43.062 -33.207  1.00 53.72           C  
ATOM   3415  NH1 ARG B  90      19.449  41.991 -33.038  1.00 53.99           N  
ATOM   3416  NH2 ARG B  90      21.495  42.895 -33.579  1.00 52.93           N  
ATOM   3417  N   PRO B  91      18.074  43.844 -37.435  1.00 42.82           N  
ATOM   3418  CA  PRO B  91      17.520  43.321 -38.687  1.00 41.93           C  
ATOM   3419  C   PRO B  91      16.031  43.626 -38.829  1.00 40.98           C  
ATOM   3420  O   PRO B  91      15.284  43.516 -37.852  1.00 40.87           O  
ATOM   3421  CB  PRO B  91      17.728  41.813 -38.560  1.00 42.00           C  
ATOM   3422  CG  PRO B  91      18.060  41.581 -37.116  1.00 42.69           C  
ATOM   3423  CD  PRO B  91      18.780  42.800 -36.686  1.00 42.67           C  
ATOM   3424  N   GLY B  92      15.621  44.036 -40.030  1.00 39.95           N  
ATOM   3425  CA  GLY B  92      14.220  44.379 -40.324  1.00 38.50           C  
ATOM   3426  C   GLY B  92      13.908  45.867 -40.212  1.00 37.57           C  
ATOM   3427  O   GLY B  92      12.829  46.310 -40.636  1.00 37.52           O  
ATOM   3428  N   ASP B  93      14.847  46.621 -39.621  1.00 36.28           N  
ATOM   3429  CA  ASP B  93      14.785  48.079 -39.511  1.00 34.69           C  
ATOM   3430  C   ASP B  93      15.184  48.724 -40.815  1.00 33.59           C  
ATOM   3431  O   ASP B  93      16.017  48.188 -41.549  1.00 34.14           O  
ATOM   3432  CB  ASP B  93      15.710  48.577 -38.417  1.00 34.70           C  
ATOM   3433  CG  ASP B  93      15.157  48.338 -37.028  1.00 37.09           C  
ATOM   3434  OD1 ASP B  93      15.878  48.642 -36.045  1.00 39.25           O  
ATOM   3435  OD2 ASP B  93      14.008  47.840 -36.902  1.00 40.04           O  
ATOM   3436  N   LEU B  94      14.578  49.876 -41.095  1.00 32.06           N  
ATOM   3437  CA  LEU B  94      14.759  50.624 -42.343  1.00 30.54           C  
ATOM   3438  C   LEU B  94      15.590  51.846 -42.086  1.00 29.52           C  
ATOM   3439  O   LEU B  94      15.212  52.666 -41.269  1.00 30.21           O  
ATOM   3440  CB  LEU B  94      13.400  51.090 -42.854  1.00 30.19           C  
ATOM   3441  CG  LEU B  94      13.384  51.659 -44.265  1.00 29.93           C  
ATOM   3442  CD1 LEU B  94      13.653  50.581 -45.299  1.00 29.53           C  
ATOM   3443  CD2 LEU B  94      12.063  52.322 -44.540  1.00 28.38           C  
ATOM   3444  N   ALA B  95      16.713  51.994 -42.766  1.00 28.55           N  
ATOM   3445  CA  ALA B  95      17.570  53.161 -42.497  1.00 27.74           C  
ATOM   3446  C   ALA B  95      17.740  54.160 -43.656  1.00 27.07           C  
ATOM   3447  O   ALA B  95      17.854  53.775 -44.843  1.00 26.62           O  
ATOM   3448  CB  ALA B  95      18.916  52.730 -41.959  1.00 27.48           C  
ATOM   3449  N   PHE B  96      17.753  55.440 -43.292  1.00 25.86           N  
ATOM   3450  CA  PHE B  96      17.964  56.495 -44.250  1.00 25.19           C  
ATOM   3451  C   PHE B  96      19.174  57.331 -43.882  1.00 25.42           C  
ATOM   3452  O   PHE B  96      19.403  57.595 -42.694  1.00 25.61           O  
ATOM   3453  CB  PHE B  96      16.786  57.439 -44.220  1.00 24.95           C  
ATOM   3454  CG  PHE B  96      15.500  56.858 -44.702  1.00 24.00           C  
ATOM   3455  CD1 PHE B  96      14.653  56.184 -43.828  1.00 23.81           C  
ATOM   3456  CD2 PHE B  96      15.095  57.048 -46.007  1.00 22.86           C  
ATOM   3457  CE1 PHE B  96      13.437  55.689 -44.260  1.00 22.84           C  
ATOM   3458  CE2 PHE B  96      13.880  56.540 -46.447  1.00 22.97           C  
ATOM   3459  CZ  PHE B  96      13.054  55.867 -45.573  1.00 22.35           C  
ATOM   3460  N   ARG B  97      19.927  57.777 -44.884  1.00 25.18           N  
ATOM   3461  CA  ARG B  97      20.797  58.924 -44.694  1.00 25.65           C  
ATOM   3462  C   ARG B  97      19.911  60.150 -44.680  1.00 24.68           C  
ATOM   3463  O   ARG B  97      18.950  60.204 -45.433  1.00 24.93           O  
ATOM   3464  CB  ARG B  97      21.770  59.051 -45.856  1.00 26.72           C  
ATOM   3465  CG  ARG B  97      22.750  57.904 -45.956  1.00 31.04           C  
ATOM   3466  CD  ARG B  97      23.581  57.957 -47.236  1.00 37.47           C  
ATOM   3467  NE  ARG B  97      24.809  58.733 -47.058  1.00 42.91           N  
ATOM   3468  CZ  ARG B  97      26.010  58.377 -47.519  1.00 44.82           C  
ATOM   3469  NH1 ARG B  97      26.187  57.224 -48.176  1.00 45.10           N  
ATOM   3470  NH2 ARG B  97      27.048  59.176 -47.299  1.00 45.52           N  
ATOM   3471  N   ALA B  98      20.240  61.141 -43.857  1.00 24.16           N  
ATOM   3472  CA  ALA B  98      19.447  62.388 -43.757  1.00 23.78           C  
ATOM   3473  C   ALA B  98      20.283  63.683 -43.739  1.00 23.60           C  
ATOM   3474  O   ALA B  98      21.441  63.673 -43.309  1.00 23.62           O  
ATOM   3475  CB  ALA B  98      18.533  62.344 -42.530  1.00 23.37           C  
ATOM   3476  N   ASN B  99      19.674  64.776 -44.227  1.00 23.23           N  
ATOM   3477  CA  ASN B  99      20.164  66.153 -44.117  1.00 22.42           C  
ATOM   3478  C   ASN B  99      19.133  66.956 -43.359  1.00 22.65           C  
ATOM   3479  O   ASN B  99      17.941  66.818 -43.604  1.00 22.74           O  
ATOM   3480  CB  ASN B  99      20.274  66.809 -45.492  1.00 22.30           C  
ATOM   3481  CG  ASN B  99      21.438  66.283 -46.326  1.00 23.55           C  
ATOM   3482  OD1 ASN B  99      22.277  65.537 -45.842  1.00 25.55           O  
ATOM   3483  ND2 ASN B  99      21.492  66.686 -47.596  1.00 23.40           N  
ATOM   3484  N   PHE B 100      19.574  67.793 -42.432  1.00 23.28           N  
ATOM   3485  CA  PHE B 100      18.751  68.896 -41.941  1.00 23.83           C  
ATOM   3486  C   PHE B 100      18.806  70.043 -42.969  1.00 24.57           C  
ATOM   3487  O   PHE B 100      19.886  70.568 -43.250  1.00 24.20           O  
ATOM   3488  CB  PHE B 100      19.278  69.381 -40.587  1.00 23.82           C  
ATOM   3489  CG  PHE B 100      18.735  68.627 -39.417  1.00 23.02           C  
ATOM   3490  CD1 PHE B 100      19.461  67.588 -38.843  1.00 23.87           C  
ATOM   3491  CD2 PHE B 100      17.498  68.961 -38.876  1.00 21.12           C  
ATOM   3492  CE1 PHE B 100      18.941  66.879 -37.763  1.00 22.53           C  
ATOM   3493  CE2 PHE B 100      16.974  68.265 -37.799  1.00 20.25           C  
ATOM   3494  CZ  PHE B 100      17.686  67.227 -37.242  1.00 20.73           C  
ATOM   3495  N   ALA B 101      17.657  70.425 -43.534  1.00 25.60           N  
ATOM   3496  CA  ALA B 101      17.640  71.397 -44.644  1.00 26.66           C  
ATOM   3497  C   ALA B 101      16.592  72.490 -44.476  1.00 27.54           C  
ATOM   3498  O   ALA B 101      15.767  72.433 -43.576  1.00 27.69           O  
ATOM   3499  CB  ALA B 101      17.457  70.682 -45.963  1.00 26.18           C  
ATOM   3500  N   THR B 102      16.635  73.486 -45.349  1.00 29.01           N  
ATOM   3501  CA  THR B 102      15.739  74.632 -45.253  1.00 30.97           C  
ATOM   3502  C   THR B 102      14.646  74.615 -46.288  1.00 32.23           C  
ATOM   3503  O   THR B 102      14.871  74.364 -47.470  1.00 32.71           O  
ATOM   3504  CB  THR B 102      16.483  75.935 -45.465  1.00 30.96           C  
ATOM   3505  OG1 THR B 102      17.742  75.874 -44.785  1.00 32.72           O  
ATOM   3506  CG2 THR B 102      15.653  77.121 -44.954  1.00 31.16           C  
ATOM   3507  N   ASN B 103      13.463  74.974 -45.845  1.00 33.84           N  
ATOM   3508  CA  ASN B 103      12.295  74.821 -46.644  1.00 35.69           C  
ATOM   3509  C   ASN B 103      11.433  76.027 -46.365  1.00 36.97           C  
ATOM   3510  O   ASN B 103      10.606  75.993 -45.442  1.00 37.80           O  
ATOM   3511  CB  ASN B 103      11.622  73.542 -46.166  1.00 36.07           C  
ATOM   3512  CG  ASN B 103      10.289  73.274 -46.811  1.00 37.09           C  
ATOM   3513  OD1 ASN B 103       9.974  73.774 -47.888  1.00 39.02           O  
ATOM   3514  ND2 ASN B 103       9.491  72.451 -46.142  1.00 38.56           N  
ATOM   3515  N   ARG B 104      11.637  77.109 -47.116  1.00 37.83           N  
ATOM   3516  CA  ARG B 104      10.803  78.282 -46.918  1.00 38.83           C  
ATOM   3517  C   ARG B 104       9.744  78.281 -47.990  1.00 38.55           C  
ATOM   3518  O   ARG B 104      10.049  78.068 -49.160  1.00 38.80           O  
ATOM   3519  CB  ARG B 104      11.618  79.585 -46.854  1.00 39.21           C  
ATOM   3520  CG  ARG B 104      11.916  80.241 -48.180  1.00 42.43           C  
ATOM   3521  CD  ARG B 104      12.665  81.563 -47.995  1.00 49.84           C  
ATOM   3522  NE  ARG B 104      14.116  81.382 -47.802  1.00 54.81           N  
ATOM   3523  CZ  ARG B 104      14.915  82.221 -47.128  1.00 56.85           C  
ATOM   3524  NH1 ARG B 104      16.223  81.954 -47.017  1.00 56.62           N  
ATOM   3525  NH2 ARG B 104      14.414  83.320 -46.551  1.00 56.96           N  
ATOM   3526  N   ASP B 105       8.498  78.466 -47.558  1.00 38.72           N  
ATOM   3527  CA  ASP B 105       7.294  78.471 -48.424  1.00 38.64           C  
ATOM   3528  C   ASP B 105       7.170  77.269 -49.378  1.00 38.17           C  
ATOM   3529  O   ASP B 105       6.771  77.415 -50.537  1.00 38.64           O  
ATOM   3530  CB  ASP B 105       7.145  79.811 -49.177  1.00 39.11           C  
ATOM   3531  CG  ASP B 105       6.774  81.002 -48.237  1.00 40.21           C  
ATOM   3532  OD1 ASP B 105       5.883  80.871 -47.357  1.00 40.69           O  
ATOM   3533  OD2 ASP B 105       7.376  82.088 -48.390  1.00 40.79           O  
ATOM   3534  N   GLY B 106       7.522  76.085 -48.876  1.00 37.36           N  
ATOM   3535  CA  GLY B 106       7.398  74.833 -49.622  1.00 35.86           C  
ATOM   3536  C   GLY B 106       8.441  74.509 -50.683  1.00 34.89           C  
ATOM   3537  O   GLY B 106       8.164  73.711 -51.578  1.00 35.69           O  
ATOM   3538  N   VAL B 107       9.628  75.106 -50.608  1.00 33.36           N  
ATOM   3539  CA  VAL B 107      10.702  74.796 -51.555  1.00 32.27           C  
ATOM   3540  C   VAL B 107      11.987  74.588 -50.788  1.00 32.01           C  
ATOM   3541  O   VAL B 107      12.300  75.347 -49.874  1.00 32.21           O  
ATOM   3542  CB  VAL B 107      10.955  75.952 -52.576  1.00 32.27           C  
ATOM   3543  CG1 VAL B 107      12.223  75.711 -53.373  1.00 30.82           C  
ATOM   3544  CG2 VAL B 107       9.788  76.129 -53.517  1.00 32.29           C  
ATOM   3545  N   ILE B 108      12.753  73.575 -51.167  1.00 31.48           N  
ATOM   3546  CA  ILE B 108      14.073  73.386 -50.562  1.00 30.81           C  
ATOM   3547  C   ILE B 108      15.022  74.476 -51.041  1.00 30.43           C  
ATOM   3548  O   ILE B 108      15.471  74.481 -52.188  1.00 30.58           O  
ATOM   3549  CB  ILE B 108      14.648  71.957 -50.795  1.00 30.55           C  
ATOM   3550  CG1 ILE B 108      13.683  70.902 -50.263  1.00 30.45           C  
ATOM   3551  CG2 ILE B 108      15.962  71.780 -50.096  1.00 30.13           C  
ATOM   3552  CD1 ILE B 108      13.037  71.269 -48.940  1.00 30.66           C  
ATOM   3553  N   VAL B 109      15.313  75.403 -50.142  1.00 30.00           N  
ATOM   3554  CA  VAL B 109      16.163  76.549 -50.453  1.00 29.63           C  
ATOM   3555  C   VAL B 109      17.653  76.254 -50.238  1.00 29.44           C  
ATOM   3556  O   VAL B 109      18.515  76.798 -50.927  1.00 29.44           O  
ATOM   3557  CB  VAL B 109      15.691  77.777 -49.661  1.00 29.26           C  
ATOM   3558  CG1 VAL B 109      16.728  78.833 -49.654  1.00 30.11           C  
ATOM   3559  CG2 VAL B 109      14.433  78.321 -50.290  1.00 28.96           C  
ATOM   3560  N   ASP B 110      17.943  75.374 -49.290  1.00 29.36           N  
ATOM   3561  CA  ASP B 110      19.292  74.954 -48.995  1.00 29.58           C  
ATOM   3562  C   ASP B 110      19.153  73.531 -48.478  1.00 30.00           C  
ATOM   3563  O   ASP B 110      18.641  73.316 -47.374  1.00 31.03           O  
ATOM   3564  CB  ASP B 110      19.863  75.862 -47.907  1.00 29.39           C  
ATOM   3565  CG  ASP B 110      21.376  75.788 -47.798  1.00 30.35           C  
ATOM   3566  OD1 ASP B 110      21.898  74.694 -47.466  1.00 30.78           O  
ATOM   3567  OD2 ASP B 110      22.045  76.841 -48.017  1.00 31.13           O  
ATOM   3568  N   ARG B 111      19.583  72.545 -49.259  1.00 30.03           N  
ATOM   3569  CA  ARG B 111      19.506  71.140 -48.808  1.00 29.72           C  
ATOM   3570  C   ARG B 111      20.323  70.865 -47.531  1.00 29.49           C  
ATOM   3571  O   ARG B 111      20.236  69.774 -46.966  1.00 29.65           O  
ATOM   3572  CB  ARG B 111      19.918  70.155 -49.923  1.00 29.63           C  
ATOM   3573  CG  ARG B 111      18.946  70.027 -51.133  1.00 29.25           C  
ATOM   3574  CD  ARG B 111      19.385  68.917 -52.117  1.00 29.13           C  
ATOM   3575  NE  ARG B 111      20.830  68.664 -52.038  1.00 31.48           N  
ATOM   3576  CZ  ARG B 111      21.409  67.571 -51.528  1.00 31.43           C  
ATOM   3577  NH1 ARG B 111      20.682  66.563 -51.066  1.00 32.33           N  
ATOM   3578  NH2 ARG B 111      22.733  67.480 -51.485  1.00 30.23           N  
ATOM   3579  N   ARG B 112      21.093  71.849 -47.070  1.00 28.95           N  
ATOM   3580  CA  ARG B 112      21.970  71.642 -45.929  1.00 28.86           C  
ATOM   3581  C   ARG B 112      21.756  72.572 -44.720  1.00 29.02           C  
ATOM   3582  O   ARG B 112      22.489  72.479 -43.729  1.00 28.41           O  
ATOM   3583  CB  ARG B 112      23.415  71.733 -46.390  1.00 29.13           C  
ATOM   3584  CG  ARG B 112      23.892  70.537 -47.154  1.00 29.63           C  
ATOM   3585  CD  ARG B 112      25.316  70.726 -47.649  1.00 32.48           C  
ATOM   3586  NE  ARG B 112      25.632  69.723 -48.668  1.00 36.66           N  
ATOM   3587  CZ  ARG B 112      25.378  69.849 -49.976  1.00 37.27           C  
ATOM   3588  NH1 ARG B 112      24.821  70.956 -50.467  1.00 36.00           N  
ATOM   3589  NH2 ARG B 112      25.689  68.855 -50.802  1.00 37.72           N  
ATOM   3590  N   ALA B 113      20.760  73.462 -44.793  1.00 29.47           N  
ATOM   3591  CA  ALA B 113      20.559  74.520 -43.768  1.00 29.59           C  
ATOM   3592  C   ALA B 113      21.846  75.311 -43.441  1.00 29.71           C  
ATOM   3593  O   ALA B 113      22.223  75.471 -42.280  1.00 29.65           O  
ATOM   3594  CB  ALA B 113      19.928  73.939 -42.500  1.00 29.56           C  
ATOM   3595  N   GLY B 114      22.524  75.780 -44.486  1.00 29.87           N  
ATOM   3596  CA  GLY B 114      23.785  76.476 -44.340  1.00 30.35           C  
ATOM   3597  C   GLY B 114      24.913  75.649 -43.747  1.00 30.87           C  
ATOM   3598  O   GLY B 114      26.015  76.153 -43.569  1.00 30.76           O  
ATOM   3599  N   ARG B 115      24.660  74.369 -43.479  1.00 31.57           N  
ATOM   3600  CA  ARG B 115      25.603  73.509 -42.762  1.00 32.02           C  
ATOM   3601  C   ARG B 115      25.750  73.949 -41.300  1.00 32.79           C  
ATOM   3602  O   ARG B 115      26.793  73.726 -40.683  1.00 32.64           O  
ATOM   3603  CB  ARG B 115      26.975  73.486 -43.429  1.00 31.81           C  
ATOM   3604  CG  ARG B 115      27.019  72.973 -44.831  1.00 32.26           C  
ATOM   3605  CD  ARG B 115      28.450  73.078 -45.330  1.00 35.05           C  
ATOM   3606  NE  ARG B 115      28.882  71.917 -46.107  1.00 37.91           N  
ATOM   3607  CZ  ARG B 115      28.727  71.784 -47.428  1.00 40.70           C  
ATOM   3608  NH1 ARG B 115      28.143  72.734 -48.161  1.00 40.04           N  
ATOM   3609  NH2 ARG B 115      29.149  70.675 -48.020  1.00 43.14           N  
ATOM   3610  N   GLU B 116      24.703  74.578 -40.762  1.00 33.82           N  
ATOM   3611  CA  GLU B 116      24.629  74.942 -39.351  1.00 34.98           C  
ATOM   3612  C   GLU B 116      24.633  73.709 -38.448  1.00 35.67           C  
ATOM   3613  O   GLU B 116      24.060  72.685 -38.812  1.00 35.81           O  
ATOM   3614  CB  GLU B 116      23.356  75.747 -39.095  1.00 35.01           C  
ATOM   3615  CG  GLU B 116      23.279  77.092 -39.837  1.00 36.22           C  
ATOM   3616  CD  GLU B 116      24.164  78.199 -39.235  1.00 37.29           C  
ATOM   3617  OE1 GLU B 116      24.608  78.063 -38.065  1.00 37.06           O  
ATOM   3618  OE2 GLU B 116      24.404  79.213 -39.942  1.00 36.76           O  
ATOM   3619  N   ASN B 117      25.265  73.816 -37.274  1.00 36.68           N  
ATOM   3620  CA  ASN B 117      25.347  72.688 -36.333  1.00 37.64           C  
ATOM   3621  C   ASN B 117      24.671  72.866 -34.966  1.00 37.71           C  
ATOM   3622  O   ASN B 117      24.149  71.897 -34.401  1.00 37.87           O  
ATOM   3623  CB  ASN B 117      26.794  72.233 -36.123  1.00 37.95           C  
ATOM   3624  CG  ASN B 117      26.913  70.713 -35.954  1.00 39.98           C  
ATOM   3625  OD1 ASN B 117      27.847  70.106 -36.481  1.00 43.96           O  
ATOM   3626  ND2 ASN B 117      25.968  70.093 -35.240  1.00 39.63           N  
ATOM   3627  N   LYS B 118      24.699  74.084 -34.430  1.00 37.66           N  
ATOM   3628  CA  LYS B 118      24.111  74.362 -33.116  1.00 37.68           C  
ATOM   3629  C   LYS B 118      22.646  73.958 -33.103  1.00 36.43           C  
ATOM   3630  O   LYS B 118      21.880  74.340 -33.972  1.00 36.04           O  
ATOM   3631  CB  LYS B 118      24.219  75.855 -32.778  1.00 38.57           C  
ATOM   3632  CG  LYS B 118      24.420  76.179 -31.304  1.00 41.26           C  
ATOM   3633  CD  LYS B 118      25.906  76.138 -30.978  1.00 45.92           C  
ATOM   3634  CE  LYS B 118      26.302  77.277 -30.032  1.00 49.24           C  
ATOM   3635  NZ  LYS B 118      27.631  77.884 -30.433  1.00 50.20           N  
ATOM   3636  N   GLY B 119      22.264  73.179 -32.113  1.00 35.62           N  
ATOM   3637  CA  GLY B 119      20.863  72.831 -31.930  1.00 35.12           C  
ATOM   3638  C   GLY B 119      20.474  71.578 -32.668  1.00 34.80           C  
ATOM   3639  O   GLY B 119      19.505  70.908 -32.307  1.00 34.30           O  
ATOM   3640  N   ASN B 120      21.242  71.257 -33.704  1.00 34.73           N  
ATOM   3641  CA  ASN B 120      20.992  70.066 -34.494  1.00 34.80           C  
ATOM   3642  C   ASN B 120      20.708  68.857 -33.625  1.00 35.18           C  
ATOM   3643  O   ASN B 120      19.913  67.982 -33.990  1.00 34.54           O  
ATOM   3644  CB  ASN B 120      22.152  69.794 -35.437  1.00 34.52           C  
ATOM   3645  CG  ASN B 120      21.970  70.452 -36.776  1.00 33.60           C  
ATOM   3646  OD1 ASN B 120      21.069  71.260 -36.973  1.00 33.28           O  
ATOM   3647  ND2 ASN B 120      22.824  70.101 -37.714  1.00 34.07           N  
ATOM   3648  N   GLU B 121      21.348  68.838 -32.460  1.00 36.03           N  
ATOM   3649  CA  GLU B 121      21.143  67.764 -31.514  1.00 37.01           C  
ATOM   3650  C   GLU B 121      19.756  67.743 -30.865  1.00 36.48           C  
ATOM   3651  O   GLU B 121      19.151  66.676 -30.706  1.00 36.47           O  
ATOM   3652  CB  GLU B 121      22.278  67.688 -30.493  1.00 37.55           C  
ATOM   3653  CG  GLU B 121      23.252  66.589 -30.874  1.00 42.38           C  
ATOM   3654  CD  GLU B 121      22.535  65.360 -31.513  1.00 49.70           C  
ATOM   3655  OE1 GLU B 121      21.517  64.859 -30.940  1.00 52.07           O  
ATOM   3656  OE2 GLU B 121      22.985  64.893 -32.595  1.00 51.75           O  
ATOM   3657  N   GLU B 122      19.238  68.916 -30.521  1.00 35.81           N  
ATOM   3658  CA  GLU B 122      17.923  68.966 -29.907  1.00 35.46           C  
ATOM   3659  C   GLU B 122      16.842  68.704 -30.942  1.00 34.59           C  
ATOM   3660  O   GLU B 122      15.793  68.143 -30.617  1.00 34.62           O  
ATOM   3661  CB  GLU B 122      17.685  70.295 -29.194  1.00 35.79           C  
ATOM   3662  CG  GLU B 122      18.804  70.701 -28.227  1.00 37.98           C  
ATOM   3663  CD  GLU B 122      18.586  72.093 -27.630  1.00 41.23           C  
ATOM   3664  OE1 GLU B 122      19.549  72.896 -27.613  1.00 40.46           O  
ATOM   3665  OE2 GLU B 122      17.442  72.393 -27.199  1.00 44.27           O  
ATOM   3666  N   LEU B 123      17.109  69.108 -32.184  1.00 33.68           N  
ATOM   3667  CA  LEU B 123      16.194  68.875 -33.294  1.00 32.30           C  
ATOM   3668  C   LEU B 123      16.105  67.391 -33.607  1.00 31.99           C  
ATOM   3669  O   LEU B 123      15.013  66.883 -33.820  1.00 31.76           O  
ATOM   3670  CB  LEU B 123      16.629  69.652 -34.523  1.00 32.10           C  
ATOM   3671  CG  LEU B 123      16.821  71.159 -34.376  1.00 31.45           C  
ATOM   3672  CD1 LEU B 123      17.685  71.657 -35.510  1.00 30.22           C  
ATOM   3673  CD2 LEU B 123      15.495  71.894 -34.359  1.00 31.42           C  
ATOM   3674  N   ALA B 124      17.243  66.695 -33.614  1.00 31.60           N  
ATOM   3675  CA  ALA B 124      17.243  65.243 -33.728  1.00 31.35           C  
ATOM   3676  C   ALA B 124      16.320  64.621 -32.683  1.00 31.97           C  
ATOM   3677  O   ALA B 124      15.381  63.910 -33.045  1.00 32.40           O  
ATOM   3678  CB  ALA B 124      18.614  64.708 -33.598  1.00 31.02           C  
ATOM   3679  N   ASP B 125      16.561  64.907 -31.399  1.00 32.26           N  
ATOM   3680  CA  ASP B 125      15.677  64.443 -30.314  1.00 32.45           C  
ATOM   3681  C   ASP B 125      14.216  64.790 -30.552  1.00 31.87           C  
ATOM   3682  O   ASP B 125      13.361  63.922 -30.513  1.00 32.17           O  
ATOM   3683  CB  ASP B 125      16.100  65.006 -28.947  1.00 33.08           C  
ATOM   3684  CG  ASP B 125      17.493  64.528 -28.501  1.00 35.60           C  
ATOM   3685  OD1 ASP B 125      18.022  63.549 -29.091  1.00 38.16           O  
ATOM   3686  OD2 ASP B 125      18.060  65.143 -27.556  1.00 37.70           O  
ATOM   3687  N   ALA B 126      13.932  66.059 -30.801  1.00 31.29           N  
ATOM   3688  CA  ALA B 126      12.566  66.520 -30.923  1.00 30.95           C  
ATOM   3689  C   ALA B 126      11.772  65.781 -31.984  1.00 31.26           C  
ATOM   3690  O   ALA B 126      10.552  65.738 -31.917  1.00 31.74           O  
ATOM   3691  CB  ALA B 126      12.550  67.982 -31.204  1.00 31.05           C  
ATOM   3692  N   ILE B 127      12.457  65.213 -32.976  1.00 31.63           N  
ATOM   3693  CA  ILE B 127      11.790  64.459 -34.054  1.00 31.24           C  
ATOM   3694  C   ILE B 127      12.122  62.971 -33.993  1.00 31.68           C  
ATOM   3695  O   ILE B 127      11.889  62.222 -34.945  1.00 31.27           O  
ATOM   3696  CB  ILE B 127      12.016  65.059 -35.483  1.00 30.85           C  
ATOM   3697  CG1 ILE B 127      13.482  64.987 -35.921  1.00 30.19           C  
ATOM   3698  CG2 ILE B 127      11.527  66.474 -35.528  1.00 30.57           C  
ATOM   3699  CD1 ILE B 127      13.704  65.147 -37.441  1.00 27.25           C  
ATOM   3700  N   SER B 128      12.670  62.558 -32.854  1.00 32.41           N  
ATOM   3701  CA  SER B 128      12.779  61.147 -32.527  1.00 33.28           C  
ATOM   3702  C   SER B 128      11.543  60.758 -31.728  1.00 34.14           C  
ATOM   3703  O   SER B 128      11.363  61.201 -30.606  1.00 34.75           O  
ATOM   3704  CB  SER B 128      14.061  60.864 -31.751  1.00 32.86           C  
ATOM   3705  OG  SER B 128      15.201  61.020 -32.582  1.00 32.69           O  
ATOM   3706  N   LEU B 129      10.671  59.954 -32.315  1.00 35.26           N  
ATOM   3707  CA  LEU B 129       9.382  59.703 -31.700  1.00 36.51           C  
ATOM   3708  C   LEU B 129       8.744  58.412 -32.152  1.00 37.46           C  
ATOM   3709  O   LEU B 129       9.262  57.696 -33.009  1.00 37.21           O  
ATOM   3710  CB  LEU B 129       8.427  60.860 -32.001  1.00 36.46           C  
ATOM   3711  CG  LEU B 129       8.309  61.243 -33.479  1.00 36.35           C  
ATOM   3712  CD1 LEU B 129       7.181  60.483 -34.168  1.00 36.34           C  
ATOM   3713  CD2 LEU B 129       8.094  62.732 -33.591  1.00 36.21           C  
ATOM   3714  N   ASP B 130       7.595  58.137 -31.558  1.00 38.69           N  
ATOM   3715  CA  ASP B 130       6.821  56.986 -31.919  1.00 40.32           C  
ATOM   3716  C   ASP B 130       5.499  57.499 -32.427  1.00 40.96           C  
ATOM   3717  O   ASP B 130       5.020  58.527 -31.965  1.00 41.55           O  
ATOM   3718  CB  ASP B 130       6.626  56.076 -30.701  1.00 40.69           C  
ATOM   3719  CG  ASP B 130       7.905  55.290 -30.324  1.00 42.55           C  
ATOM   3720  OD1 ASP B 130       9.045  55.679 -30.718  1.00 44.03           O  
ATOM   3721  OD2 ASP B 130       7.756  54.271 -29.610  1.00 43.76           O  
HETATM 3722  N   MSE B 131       4.942  56.816 -33.420  1.00 41.76           N  
HETATM 3723  CA  MSE B 131       3.587  57.085 -33.899  1.00 42.60           C  
HETATM 3724  C   MSE B 131       3.055  55.786 -34.486  1.00 42.53           C  
HETATM 3725  O   MSE B 131       3.750  55.099 -35.231  1.00 42.85           O  
HETATM 3726  CB  MSE B 131       3.518  58.286 -34.884  1.00 43.01           C  
HETATM 3727  CG  MSE B 131       4.072  58.084 -36.303  1.00 43.91           C  
HETATM 3728 SE   MSE B 131       4.479  59.766 -37.286  1.00 49.77          SE  
HETATM 3729  CE  MSE B 131       2.739  60.381 -37.926  1.00 46.17           C  
ATOM   3730  N   GLY B 132       1.837  55.428 -34.111  1.00 42.37           N  
ATOM   3731  CA  GLY B 132       1.316  54.107 -34.427  1.00 41.94           C  
ATOM   3732  C   GLY B 132       2.233  52.998 -33.939  1.00 41.46           C  
ATOM   3733  O   GLY B 132       2.813  53.073 -32.858  1.00 41.25           O  
ATOM   3734  N   GLU B 133       2.363  51.976 -34.772  1.00 41.38           N  
ATOM   3735  CA  GLU B 133       3.180  50.796 -34.504  1.00 41.34           C  
ATOM   3736  C   GLU B 133       4.647  51.086 -34.769  1.00 40.68           C  
ATOM   3737  O   GLU B 133       5.512  50.190 -34.703  1.00 40.79           O  
ATOM   3738  CB  GLU B 133       2.732  49.667 -35.431  1.00 41.69           C  
ATOM   3739  CG  GLU B 133       1.411  49.028 -35.050  1.00 44.69           C  
ATOM   3740  CD  GLU B 133       1.604  47.857 -34.086  1.00 48.76           C  
ATOM   3741  OE1 GLU B 133       1.959  48.086 -32.890  1.00 48.61           O  
ATOM   3742  OE2 GLU B 133       1.410  46.700 -34.546  1.00 50.79           O  
ATOM   3743  N   TYR B 134       4.920  52.349 -35.080  1.00 39.74           N  
ATOM   3744  CA  TYR B 134       6.198  52.722 -35.654  1.00 38.26           C  
ATOM   3745  C   TYR B 134       7.039  53.512 -34.717  1.00 37.56           C  
ATOM   3746  O   TYR B 134       6.516  54.197 -33.829  1.00 37.28           O  
ATOM   3747  CB  TYR B 134       5.987  53.487 -36.952  1.00 38.07           C  
ATOM   3748  CG  TYR B 134       5.486  52.574 -38.003  1.00 36.55           C  
ATOM   3749  CD1 TYR B 134       6.371  51.756 -38.704  1.00 36.45           C  
ATOM   3750  CD2 TYR B 134       4.128  52.475 -38.264  1.00 34.90           C  
ATOM   3751  CE1 TYR B 134       5.920  50.885 -39.660  1.00 36.05           C  
ATOM   3752  CE2 TYR B 134       3.661  51.610 -39.222  1.00 35.53           C  
ATOM   3753  CZ  TYR B 134       4.565  50.819 -39.912  1.00 36.20           C  
ATOM   3754  OH  TYR B 134       4.114  49.953 -40.857  1.00 38.80           O  
ATOM   3755  N   SER B 135       8.346  53.412 -34.952  1.00 36.42           N  
ATOM   3756  CA  SER B 135       9.344  54.080 -34.144  1.00 35.62           C  
ATOM   3757  C   SER B 135      10.405  54.826 -35.007  1.00 34.60           C  
ATOM   3758  O   SER B 135      11.010  54.255 -35.925  1.00 34.97           O  
ATOM   3759  CB  SER B 135       9.909  53.058 -33.145  1.00 35.57           C  
ATOM   3760  OG  SER B 135      11.314  52.968 -33.187  1.00 37.12           O  
ATOM   3761  N   PHE B 136      10.598  56.116 -34.731  1.00 33.14           N  
ATOM   3762  CA  PHE B 136      11.515  56.945 -35.517  1.00 31.58           C  
ATOM   3763  C   PHE B 136      12.670  57.489 -34.693  1.00 30.93           C  
ATOM   3764  O   PHE B 136      12.474  58.162 -33.701  1.00 30.30           O  
ATOM   3765  CB  PHE B 136      10.751  58.079 -36.182  1.00 31.10           C  
ATOM   3766  CG  PHE B 136       9.615  57.609 -37.010  1.00 30.70           C  
ATOM   3767  CD1 PHE B 136       8.369  57.371 -36.437  1.00 31.06           C  
ATOM   3768  CD2 PHE B 136       9.781  57.361 -38.365  1.00 30.50           C  
ATOM   3769  CE1 PHE B 136       7.294  56.916 -37.212  1.00 29.74           C  
ATOM   3770  CE2 PHE B 136       8.716  56.902 -39.139  1.00 29.28           C  
ATOM   3771  CZ  PHE B 136       7.472  56.688 -38.562  1.00 28.83           C  
ATOM   3772  N   ARG B 137      13.880  57.177 -35.122  1.00 30.70           N  
ATOM   3773  CA  ARG B 137      15.086  57.565 -34.408  1.00 30.66           C  
ATOM   3774  C   ARG B 137      15.871  58.483 -35.327  1.00 30.03           C  
ATOM   3775  O   ARG B 137      16.159  58.107 -36.458  1.00 29.72           O  
ATOM   3776  CB  ARG B 137      15.930  56.319 -34.043  1.00 31.02           C  
ATOM   3777  CG  ARG B 137      15.827  55.789 -32.605  1.00 32.36           C  
ATOM   3778  CD  ARG B 137      14.647  56.396 -31.840  1.00 35.94           C  
ATOM   3779  NE  ARG B 137      14.078  55.466 -30.874  1.00 38.19           N  
ATOM   3780  CZ  ARG B 137      12.785  55.407 -30.550  1.00 39.91           C  
ATOM   3781  NH1 ARG B 137      12.369  54.508 -29.667  1.00 40.78           N  
ATOM   3782  NH2 ARG B 137      11.895  56.226 -31.102  1.00 40.16           N  
ATOM   3783  N   VAL B 138      16.182  59.689 -34.861  1.00 29.54           N  
ATOM   3784  CA  VAL B 138      17.069  60.557 -35.589  1.00 29.55           C  
ATOM   3785  C   VAL B 138      18.245  60.920 -34.703  1.00 30.44           C  
ATOM   3786  O   VAL B 138      18.078  61.203 -33.518  1.00 30.78           O  
ATOM   3787  CB  VAL B 138      16.395  61.835 -36.121  1.00 29.36           C  
ATOM   3788  CG1 VAL B 138      17.368  62.593 -37.012  1.00 28.79           C  
ATOM   3789  CG2 VAL B 138      15.156  61.513 -36.937  1.00 28.96           C  
ATOM   3790  N   LYS B 139      19.437  60.900 -35.292  1.00 31.09           N  
ATOM   3791  CA  LYS B 139      20.651  61.326 -34.619  1.00 31.60           C  
ATOM   3792  C   LYS B 139      21.463  62.166 -35.606  1.00 31.35           C  
ATOM   3793  O   LYS B 139      21.450  61.913 -36.811  1.00 31.22           O  
ATOM   3794  CB  LYS B 139      21.447  60.111 -34.137  1.00 32.03           C  
ATOM   3795  CG  LYS B 139      22.047  60.228 -32.735  1.00 34.38           C  
ATOM   3796  CD  LYS B 139      23.504  60.704 -32.771  1.00 38.25           C  
ATOM   3797  CE  LYS B 139      24.215  60.433 -31.442  1.00 40.67           C  
ATOM   3798  NZ  LYS B 139      23.550  61.173 -30.308  1.00 43.07           N  
ATOM   3799  N   SER B 140      22.156  63.171 -35.083  1.00 31.23           N  
ATOM   3800  CA  SER B 140      22.823  64.158 -35.903  1.00 30.90           C  
ATOM   3801  C   SER B 140      24.308  64.056 -35.805  1.00 30.45           C  
ATOM   3802  O   SER B 140      24.856  63.864 -34.733  1.00 30.46           O  
ATOM   3803  CB  SER B 140      22.441  65.557 -35.453  1.00 31.02           C  
ATOM   3804  OG  SER B 140      23.623  66.342 -35.355  1.00 32.43           O  
ATOM   3805  N   GLY B 141      24.964  64.261 -36.927  1.00 30.47           N  
ATOM   3806  CA  GLY B 141      26.407  64.210 -36.964  1.00 30.97           C  
ATOM   3807  C   GLY B 141      27.035  65.565 -37.166  1.00 31.23           C  
ATOM   3808  O   GLY B 141      26.632  66.563 -36.537  1.00 31.79           O  
ATOM   3809  N   VAL B 142      28.029  65.576 -38.049  1.00 31.13           N  
ATOM   3810  CA  VAL B 142      28.804  66.757 -38.403  1.00 30.75           C  
ATOM   3811  C   VAL B 142      27.970  67.633 -39.333  1.00 30.97           C  
ATOM   3812  O   VAL B 142      27.264  67.122 -40.219  1.00 30.92           O  
ATOM   3813  CB  VAL B 142      30.112  66.332 -39.103  1.00 30.50           C  
ATOM   3814  CG1 VAL B 142      30.798  67.509 -39.749  1.00 30.42           C  
ATOM   3815  CG2 VAL B 142      31.037  65.612 -38.127  1.00 29.31           C  
ATOM   3816  N   GLU B 143      28.043  68.945 -39.120  1.00 30.71           N  
ATOM   3817  CA  GLU B 143      27.300  69.889 -39.925  1.00 30.87           C  
ATOM   3818  C   GLU B 143      25.824  69.489 -40.049  1.00 30.76           C  
ATOM   3819  O   GLU B 143      25.135  69.332 -39.050  1.00 31.49           O  
ATOM   3820  CB  GLU B 143      27.927  70.002 -41.304  1.00 31.16           C  
ATOM   3821  CG  GLU B 143      29.394  70.289 -41.302  1.00 33.21           C  
ATOM   3822  CD  GLU B 143      29.928  70.473 -42.706  1.00 37.47           C  
ATOM   3823  OE1 GLU B 143      29.698  71.552 -43.286  1.00 39.58           O  
ATOM   3824  OE2 GLU B 143      30.573  69.539 -43.241  1.00 39.58           O  
ATOM   3825  N   HIS B 144      25.361  69.304 -41.278  1.00 30.34           N  
ATOM   3826  CA  HIS B 144      23.956  69.021 -41.595  1.00 30.10           C  
ATOM   3827  C   HIS B 144      23.639  67.533 -41.603  1.00 29.85           C  
ATOM   3828  O   HIS B 144      22.487  67.151 -41.745  1.00 30.03           O  
ATOM   3829  CB  HIS B 144      23.705  69.492 -43.007  1.00 30.06           C  
ATOM   3830  CG  HIS B 144      24.680  68.921 -43.970  1.00 29.64           C  
ATOM   3831  ND1 HIS B 144      24.337  67.949 -44.880  1.00 31.14           N  
ATOM   3832  CD2 HIS B 144      26.015  69.095 -44.086  1.00 29.33           C  
ATOM   3833  CE1 HIS B 144      25.410  67.595 -45.567  1.00 32.00           C  
ATOM   3834  NE2 HIS B 144      26.443  68.271 -45.098  1.00 31.92           N  
ATOM   3835  N   ARG B 145      24.669  66.701 -41.503  1.00 29.35           N  
ATOM   3836  CA  ARG B 145      24.512  65.260 -41.610  1.00 28.81           C  
ATOM   3837  C   ARG B 145      23.689  64.688 -40.467  1.00 27.86           C  
ATOM   3838  O   ARG B 145      23.691  65.218 -39.364  1.00 28.49           O  
ATOM   3839  CB  ARG B 145      25.881  64.596 -41.653  1.00 29.07           C  
ATOM   3840  CG  ARG B 145      26.593  64.783 -42.971  1.00 30.79           C  
ATOM   3841  CD  ARG B 145      28.075  64.395 -42.905  1.00 35.20           C  
ATOM   3842  NE  ARG B 145      28.762  64.873 -44.102  1.00 38.45           N  
ATOM   3843  CZ  ARG B 145      29.297  66.087 -44.222  1.00 40.39           C  
ATOM   3844  NH1 ARG B 145      29.262  66.955 -43.205  1.00 41.02           N  
ATOM   3845  NH2 ARG B 145      29.878  66.432 -45.362  1.00 41.36           N  
ATOM   3846  N   ALA B 146      22.981  63.609 -40.749  1.00 26.71           N  
ATOM   3847  CA  ALA B 146      22.087  62.962 -39.792  1.00 25.51           C  
ATOM   3848  C   ALA B 146      21.658  61.587 -40.329  1.00 24.72           C  
ATOM   3849  O   ALA B 146      21.874  61.263 -41.495  1.00 24.10           O  
ATOM   3850  CB  ALA B 146      20.865  63.843 -39.520  1.00 25.24           C  
ATOM   3851  N   ALA B 147      21.064  60.776 -39.470  1.00 24.22           N  
ATOM   3852  CA  ALA B 147      20.558  59.484 -39.898  1.00 23.89           C  
ATOM   3853  C   ALA B 147      19.219  59.211 -39.248  1.00 23.48           C  
ATOM   3854  O   ALA B 147      18.991  59.603 -38.107  1.00 22.97           O  
ATOM   3855  CB  ALA B 147      21.545  58.394 -39.561  1.00 23.94           C  
ATOM   3856  N   LEU B 148      18.346  58.555 -40.000  1.00 23.30           N  
ATOM   3857  CA  LEU B 148      17.038  58.138 -39.514  1.00 23.64           C  
ATOM   3858  C   LEU B 148      16.878  56.621 -39.647  1.00 24.16           C  
ATOM   3859  O   LEU B 148      17.165  56.013 -40.705  1.00 24.03           O  
ATOM   3860  CB  LEU B 148      15.902  58.859 -40.257  1.00 23.33           C  
ATOM   3861  CG  LEU B 148      14.476  58.318 -40.074  1.00 23.15           C  
ATOM   3862  CD1 LEU B 148      13.755  59.029 -38.955  1.00 22.22           C  
ATOM   3863  CD2 LEU B 148      13.686  58.456 -41.339  1.00 24.22           C  
ATOM   3864  N   VAL B 149      16.411  56.026 -38.555  1.00 24.81           N  
ATOM   3865  CA  VAL B 149      16.167  54.593 -38.467  1.00 25.11           C  
ATOM   3866  C   VAL B 149      14.711  54.418 -38.104  1.00 25.52           C  
ATOM   3867  O   VAL B 149      14.245  54.958 -37.102  1.00 25.53           O  
ATOM   3868  CB  VAL B 149      17.083  53.936 -37.400  1.00 25.02           C  
ATOM   3869  CG1 VAL B 149      16.777  52.474 -37.267  1.00 25.60           C  
ATOM   3870  CG2 VAL B 149      18.559  54.109 -37.767  1.00 23.65           C  
ATOM   3871  N   VAL B 150      13.986  53.689 -38.934  1.00 26.15           N  
ATOM   3872  CA  VAL B 150      12.583  53.418 -38.657  1.00 27.74           C  
ATOM   3873  C   VAL B 150      12.437  51.941 -38.287  1.00 28.75           C  
ATOM   3874  O   VAL B 150      13.156  51.102 -38.814  1.00 29.26           O  
ATOM   3875  CB  VAL B 150      11.723  53.737 -39.886  1.00 27.77           C  
ATOM   3876  CG1 VAL B 150      10.245  53.586 -39.572  1.00 27.49           C  
ATOM   3877  CG2 VAL B 150      12.019  55.149 -40.372  1.00 28.45           C  
ATOM   3878  N   SER B 151      11.540  51.610 -37.370  1.00 29.77           N  
ATOM   3879  CA  SER B 151      11.211  50.199 -37.126  1.00 31.16           C  
ATOM   3880  C   SER B 151       9.714  50.038 -36.887  1.00 32.08           C  
ATOM   3881  O   SER B 151       9.051  50.954 -36.379  1.00 33.30           O  
ATOM   3882  CB  SER B 151      12.029  49.606 -35.975  1.00 31.10           C  
ATOM   3883  OG  SER B 151      11.637  50.147 -34.727  1.00 32.11           O  
ATOM   3884  N   GLY B 152       9.182  48.883 -37.269  1.00 32.76           N  
ATOM   3885  CA  GLY B 152       7.743  48.635 -37.231  1.00 33.62           C  
ATOM   3886  C   GLY B 152       7.378  47.591 -38.277  1.00 34.53           C  
ATOM   3887  O   GLY B 152       8.258  47.071 -38.980  1.00 34.39           O  
ATOM   3888  N   PRO B 153       6.080  47.271 -38.393  1.00 35.04           N  
ATOM   3889  CA  PRO B 153       5.652  46.258 -39.360  1.00 35.85           C  
ATOM   3890  C   PRO B 153       5.911  46.625 -40.850  1.00 36.86           C  
ATOM   3891  O   PRO B 153       6.114  47.804 -41.198  1.00 36.61           O  
ATOM   3892  CB  PRO B 153       4.150  46.120 -39.077  1.00 35.85           C  
ATOM   3893  CG  PRO B 153       3.759  47.443 -38.419  1.00 35.27           C  
ATOM   3894  CD  PRO B 153       4.955  47.838 -37.624  1.00 34.90           C  
ATOM   3895  N   ASP B 154       5.951  45.595 -41.697  1.00 37.90           N  
ATOM   3896  CA  ASP B 154       5.919  45.739 -43.162  1.00 39.25           C  
ATOM   3897  C   ASP B 154       7.018  46.572 -43.835  1.00 38.78           C  
ATOM   3898  O   ASP B 154       6.883  46.865 -45.019  1.00 39.32           O  
ATOM   3899  CB  ASP B 154       4.545  46.297 -43.643  1.00 40.06           C  
ATOM   3900  CG  ASP B 154       3.389  45.270 -43.559  1.00 42.45           C  
ATOM   3901  OD1 ASP B 154       2.218  45.678 -43.775  1.00 44.78           O  
ATOM   3902  OD2 ASP B 154       3.633  44.069 -43.294  1.00 46.32           O  
ATOM   3903  N   LEU B 155       8.073  46.969 -43.126  1.00 37.97           N  
ATOM   3904  CA  LEU B 155       9.066  47.894 -43.713  1.00 37.19           C  
ATOM   3905  C   LEU B 155       9.745  47.396 -45.023  1.00 36.94           C  
ATOM   3906  O   LEU B 155      10.239  46.270 -45.091  1.00 36.86           O  
ATOM   3907  CB  LEU B 155      10.124  48.294 -42.679  1.00 36.91           C  
ATOM   3908  CG  LEU B 155       9.731  49.042 -41.397  1.00 36.69           C  
ATOM   3909  CD1 LEU B 155      10.978  49.484 -40.690  1.00 35.87           C  
ATOM   3910  CD2 LEU B 155       8.859  50.243 -41.651  1.00 36.77           C  
ATOM   3911  N   SER B 156       9.750  48.241 -46.058  1.00 36.29           N  
ATOM   3912  CA  SER B 156      10.396  47.916 -47.335  1.00 35.70           C  
ATOM   3913  C   SER B 156      11.321  49.049 -47.749  1.00 35.24           C  
ATOM   3914  O   SER B 156      10.987  50.220 -47.537  1.00 35.12           O  
ATOM   3915  CB  SER B 156       9.341  47.680 -48.425  1.00 35.93           C  
ATOM   3916  OG  SER B 156       9.903  47.129 -49.608  1.00 35.63           O  
ATOM   3917  N   ASP B 157      12.482  48.707 -48.320  1.00 34.72           N  
ATOM   3918  CA  ASP B 157      13.413  49.731 -48.829  1.00 34.19           C  
ATOM   3919  C   ASP B 157      13.158  50.061 -50.294  1.00 33.52           C  
ATOM   3920  O   ASP B 157      13.903  50.805 -50.929  1.00 32.83           O  
ATOM   3921  CB  ASP B 157      14.892  49.394 -48.541  1.00 34.31           C  
ATOM   3922  CG  ASP B 157      15.390  48.141 -49.262  1.00 35.24           C  
ATOM   3923  OD1 ASP B 157      14.658  47.570 -50.104  1.00 35.49           O  
ATOM   3924  OD2 ASP B 157      16.545  47.731 -48.974  1.00 35.63           O  
HETATM 3925  N   MSE B 158      12.079  49.491 -50.813  1.00 33.29           N  
HETATM 3926  CA  MSE B 158      11.651  49.746 -52.169  1.00 33.25           C  
HETATM 3927  C   MSE B 158      10.848  51.009 -52.133  1.00 32.34           C  
HETATM 3928  O   MSE B 158       9.645  50.955 -52.258  1.00 32.05           O  
HETATM 3929  CB  MSE B 158      10.774  48.600 -52.674  1.00 33.71           C  
HETATM 3930  CG  MSE B 158      11.506  47.299 -52.846  1.00 36.23           C  
HETATM 3931 SE   MSE B 158      12.662  47.403 -54.402  1.00 45.13          SE  
HETATM 3932  CE  MSE B 158      13.564  45.659 -54.192  1.00 44.22           C  
ATOM   3933  N   ILE B 159      11.510  52.139 -51.904  1.00 31.71           N  
ATOM   3934  CA  ILE B 159      10.867  53.447 -51.928  1.00 30.60           C  
ATOM   3935  C   ILE B 159      11.818  54.465 -52.504  1.00 30.81           C  
ATOM   3936  O   ILE B 159      13.024  54.229 -52.556  1.00 30.58           O  
ATOM   3937  CB  ILE B 159      10.456  53.920 -50.540  1.00 30.25           C  
ATOM   3938  CG1 ILE B 159      11.513  53.557 -49.509  1.00 29.46           C  
ATOM   3939  CG2 ILE B 159       9.108  53.346 -50.164  1.00 30.18           C  
ATOM   3940  CD1 ILE B 159      11.255  54.162 -48.180  1.00 28.89           C  
ATOM   3941  N   GLY B 160      11.267  55.598 -52.938  1.00 31.06           N  
ATOM   3942  CA  GLY B 160      12.059  56.722 -53.440  1.00 31.07           C  
ATOM   3943  C   GLY B 160      12.616  57.609 -52.343  1.00 30.94           C  
ATOM   3944  O   GLY B 160      12.460  57.317 -51.155  1.00 31.33           O  
ATOM   3945  N   ASP B 161      13.260  58.700 -52.751  1.00 30.89           N  
ATOM   3946  CA  ASP B 161      13.901  59.647 -51.838  1.00 30.64           C  
ATOM   3947  C   ASP B 161      12.975  60.826 -51.504  1.00 30.69           C  
ATOM   3948  O   ASP B 161      12.084  61.174 -52.276  1.00 30.86           O  
ATOM   3949  CB  ASP B 161      15.219  60.167 -52.448  1.00 30.53           C  
ATOM   3950  CG  ASP B 161      16.340  59.103 -52.491  1.00 31.31           C  
ATOM   3951  OD1 ASP B 161      16.376  58.184 -51.651  1.00 33.20           O  
ATOM   3952  OD2 ASP B 161      17.226  59.195 -53.363  1.00 32.50           O  
ATOM   3953  N   SER B 162      13.186  61.435 -50.342  1.00 31.01           N  
ATOM   3954  CA  SER B 162      12.501  62.680 -49.976  1.00 30.97           C  
ATOM   3955  C   SER B 162      13.272  63.858 -50.565  1.00 30.82           C  
ATOM   3956  O   SER B 162      12.694  64.840 -51.009  1.00 30.65           O  
ATOM   3957  CB  SER B 162      12.461  62.806 -48.455  1.00 31.06           C  
ATOM   3958  OG  SER B 162      11.564  63.806 -48.032  1.00 31.54           O  
ATOM   3959  N   ASP B 163      14.592  63.720 -50.550  1.00 30.73           N  
ATOM   3960  CA  ASP B 163      15.544  64.698 -51.021  1.00 30.62           C  
ATOM   3961  C   ASP B 163      15.405  64.942 -52.514  1.00 30.69           C  
ATOM   3962  O   ASP B 163      15.600  64.032 -53.301  1.00 31.17           O  
ATOM   3963  CB  ASP B 163      16.935  64.142 -50.727  1.00 30.59           C  
ATOM   3964  CG  ASP B 163      18.006  65.205 -50.717  1.00 31.11           C  
ATOM   3965  OD1 ASP B 163      17.905  66.190 -51.473  1.00 31.50           O  
ATOM   3966  OD2 ASP B 163      18.979  65.048 -49.957  1.00 32.13           O  
ATOM   3967  N   PRO B 164      15.110  66.183 -52.923  1.00 30.89           N  
ATOM   3968  CA  PRO B 164      14.908  66.428 -54.348  1.00 31.16           C  
ATOM   3969  C   PRO B 164      16.222  66.468 -55.093  1.00 31.50           C  
ATOM   3970  O   PRO B 164      16.242  66.567 -56.312  1.00 31.90           O  
ATOM   3971  CB  PRO B 164      14.262  67.820 -54.387  1.00 30.95           C  
ATOM   3972  CG  PRO B 164      14.094  68.250 -52.975  1.00 30.91           C  
ATOM   3973  CD  PRO B 164      15.030  67.431 -52.152  1.00 30.91           C  
ATOM   3974  N   HIS B 165      17.309  66.416 -54.344  1.00 31.91           N  
ATOM   3975  CA  HIS B 165      18.665  66.481 -54.884  1.00 32.36           C  
ATOM   3976  C   HIS B 165      19.177  67.828 -55.435  1.00 32.61           C  
ATOM   3977  O   HIS B 165      20.339  67.938 -55.834  1.00 32.33           O  
ATOM   3978  CB  HIS B 165      18.925  65.317 -55.815  1.00 31.96           C  
ATOM   3979  CG  HIS B 165      19.029  64.016 -55.090  1.00 32.48           C  
ATOM   3980  ND1 HIS B 165      17.926  63.251 -54.778  1.00 32.98           N  
ATOM   3981  CD2 HIS B 165      20.101  63.358 -54.588  1.00 33.06           C  
ATOM   3982  CE1 HIS B 165      18.317  62.159 -54.144  1.00 33.18           C  
ATOM   3983  NE2 HIS B 165      19.631  62.199 -54.013  1.00 33.43           N  
ATOM   3984  N   ARG B 166      18.342  68.860 -55.394  1.00 33.23           N  
ATOM   3985  CA  ARG B 166      18.819  70.200 -55.682  1.00 33.66           C  
ATOM   3986  C   ARG B 166      17.917  71.252 -55.111  1.00 33.90           C  
ATOM   3987  O   ARG B 166      16.747  70.995 -54.842  1.00 34.30           O  
ATOM   3988  CB  ARG B 166      18.962  70.404 -57.180  1.00 33.91           C  
ATOM   3989  CG  ARG B 166      17.672  70.504 -57.949  1.00 34.78           C  
ATOM   3990  CD  ARG B 166      17.869  69.983 -59.377  1.00 37.90           C  
ATOM   3991  NE  ARG B 166      19.002  70.595 -60.080  1.00 39.30           N  
ATOM   3992  CZ  ARG B 166      20.125  69.966 -60.431  1.00 40.04           C  
ATOM   3993  NH1 ARG B 166      20.315  68.678 -60.160  1.00 40.24           N  
ATOM   3994  NH2 ARG B 166      21.067  70.639 -61.068  1.00 40.23           N  
ATOM   3995  N   GLU B 167      18.475  72.446 -54.936  1.00 34.31           N  
ATOM   3996  CA  GLU B 167      17.734  73.622 -54.459  1.00 34.27           C  
ATOM   3997  C   GLU B 167      16.674  73.962 -55.496  1.00 33.61           C  
ATOM   3998  O   GLU B 167      16.886  73.762 -56.682  1.00 33.94           O  
ATOM   3999  CB  GLU B 167      18.696  74.806 -54.274  1.00 34.70           C  
ATOM   4000  CG  GLU B 167      19.505  74.852 -52.947  1.00 37.26           C  
ATOM   4001  CD  GLU B 167      20.564  73.751 -52.786  1.00 41.97           C  
ATOM   4002  OE1 GLU B 167      21.191  73.364 -53.804  1.00 45.19           O  
ATOM   4003  OE2 GLU B 167      20.789  73.279 -51.634  1.00 42.23           O  
ATOM   4004  N   GLY B 168      15.525  74.447 -55.066  1.00 33.08           N  
ATOM   4005  CA  GLY B 168      14.519  74.875 -56.022  1.00 32.51           C  
ATOM   4006  C   GLY B 168      13.273  74.011 -56.090  1.00 32.52           C  
ATOM   4007  O   GLY B 168      12.219  74.475 -56.563  1.00 33.15           O  
ATOM   4008  N   LEU B 169      13.371  72.767 -55.615  1.00 31.55           N  
ATOM   4009  CA  LEU B 169      12.233  71.842 -55.636  1.00 30.51           C  
ATOM   4010  C   LEU B 169      11.550  71.676 -54.272  1.00 30.37           C  
ATOM   4011  O   LEU B 169      12.183  71.870 -53.229  1.00 30.03           O  
ATOM   4012  CB  LEU B 169      12.695  70.484 -56.159  1.00 30.28           C  
ATOM   4013  CG  LEU B 169      13.187  70.585 -57.590  1.00 29.34           C  
ATOM   4014  CD1 LEU B 169      13.979  69.367 -58.021  1.00 28.22           C  
ATOM   4015  CD2 LEU B 169      11.986  70.849 -58.501  1.00 29.40           C  
ATOM   4016  N   PRO B 170      10.252  71.315 -54.264  1.00 30.21           N  
ATOM   4017  CA  PRO B 170       9.723  70.986 -52.960  1.00 30.39           C  
ATOM   4018  C   PRO B 170      10.317  69.642 -52.513  1.00 31.00           C  
ATOM   4019  O   PRO B 170      10.927  68.930 -53.333  1.00 31.28           O  
ATOM   4020  CB  PRO B 170       8.231  70.860 -53.222  1.00 29.97           C  
ATOM   4021  CG  PRO B 170       8.158  70.371 -54.591  1.00 29.89           C  
ATOM   4022  CD  PRO B 170       9.271  71.046 -55.328  1.00 29.94           C  
ATOM   4023  N   PRO B 171      10.174  69.302 -51.222  1.00 31.14           N  
ATOM   4024  CA  PRO B 171      10.518  67.945 -50.791  1.00 31.38           C  
ATOM   4025  C   PRO B 171       9.637  66.954 -51.532  1.00 31.84           C  
ATOM   4026  O   PRO B 171       8.426  67.166 -51.600  1.00 31.75           O  
ATOM   4027  CB  PRO B 171      10.135  67.927 -49.317  1.00 30.98           C  
ATOM   4028  CG  PRO B 171       9.928  69.331 -48.933  1.00 31.65           C  
ATOM   4029  CD  PRO B 171       9.673  70.146 -50.129  1.00 30.93           C  
ATOM   4030  N   GLU B 172      10.213  65.892 -52.090  1.00 32.55           N  
ATOM   4031  CA  GLU B 172       9.385  64.885 -52.765  1.00 33.59           C  
ATOM   4032  C   GLU B 172       8.638  64.012 -51.797  1.00 33.85           C  
ATOM   4033  O   GLU B 172       9.141  63.658 -50.727  1.00 34.22           O  
ATOM   4034  CB  GLU B 172      10.190  64.022 -53.713  1.00 33.73           C  
ATOM   4035  CG  GLU B 172      10.931  64.858 -54.718  1.00 36.62           C  
ATOM   4036  CD  GLU B 172      11.024  64.222 -56.082  1.00 41.10           C  
ATOM   4037  OE1 GLU B 172      10.764  62.992 -56.214  1.00 43.32           O  
ATOM   4038  OE2 GLU B 172      11.373  64.972 -57.030  1.00 42.77           O  
ATOM   4039  N   LYS B 173       7.408  63.697 -52.167  1.00 34.34           N  
ATOM   4040  CA  LYS B 173       6.654  62.671 -51.482  1.00 34.81           C  
ATOM   4041  C   LYS B 173       7.354  61.345 -51.745  1.00 34.88           C  
ATOM   4042  O   LYS B 173       7.773  61.091 -52.866  1.00 35.41           O  
ATOM   4043  CB  LYS B 173       5.241  62.631 -52.048  1.00 34.88           C  
ATOM   4044  CG  LYS B 173       4.269  63.379 -51.207  1.00 35.31           C  
ATOM   4045  CD  LYS B 173       3.538  64.425 -51.989  1.00 37.12           C  
ATOM   4046  CE  LYS B 173       3.570  65.752 -51.206  1.00 38.60           C  
ATOM   4047  NZ  LYS B 173       3.681  65.550 -49.718  1.00 36.99           N  
ATOM   4048  N   ILE B 174       7.515  60.517 -50.727  1.00 34.58           N  
ATOM   4049  CA  ILE B 174       8.032  59.174 -50.954  1.00 34.76           C  
ATOM   4050  C   ILE B 174       7.088  58.378 -51.866  1.00 34.94           C  
ATOM   4051  O   ILE B 174       5.886  58.382 -51.645  1.00 35.32           O  
ATOM   4052  CB  ILE B 174       8.197  58.404 -49.619  1.00 34.70           C  
ATOM   4053  CG1 ILE B 174       8.914  59.270 -48.570  1.00 34.11           C  
ATOM   4054  CG2 ILE B 174       8.901  57.062 -49.848  1.00 33.91           C  
ATOM   4055  CD1 ILE B 174      10.325  59.730 -48.955  1.00 33.12           C  
ATOM   4056  N   ARG B 175       7.633  57.705 -52.878  1.00 35.22           N  
ATOM   4057  CA  ARG B 175       6.860  56.783 -53.722  1.00 35.82           C  
ATOM   4058  C   ARG B 175       7.340  55.323 -53.688  1.00 35.68           C  
ATOM   4059  O   ARG B 175       8.511  55.057 -53.463  1.00 35.72           O  
ATOM   4060  CB  ARG B 175       6.815  57.287 -55.157  1.00 36.22           C  
ATOM   4061  CG  ARG B 175       5.647  58.217 -55.405  1.00 39.40           C  
ATOM   4062  CD  ARG B 175       5.841  59.036 -56.660  1.00 44.65           C  
ATOM   4063  NE  ARG B 175       5.423  60.417 -56.432  1.00 50.78           N  
ATOM   4064  CZ  ARG B 175       5.116  61.292 -57.393  1.00 54.73           C  
ATOM   4065  NH1 ARG B 175       5.167  60.928 -58.677  1.00 56.87           N  
ATOM   4066  NH2 ARG B 175       4.743  62.534 -57.070  1.00 55.11           N  
ATOM   4067  N   PRO B 176       6.423  54.372 -53.905  1.00 35.96           N  
ATOM   4068  CA  PRO B 176       6.664  52.929 -53.945  1.00 36.13           C  
ATOM   4069  C   PRO B 176       7.898  52.353 -54.673  1.00 36.44           C  
ATOM   4070  O   PRO B 176       8.671  51.682 -54.013  1.00 37.41           O  
ATOM   4071  CB  PRO B 176       5.374  52.385 -54.529  1.00 36.14           C  
ATOM   4072  CG  PRO B 176       4.353  53.270 -53.928  1.00 36.65           C  
ATOM   4073  CD  PRO B 176       4.982  54.647 -53.780  1.00 36.11           C  
ATOM   4074  N   THR B 177       8.110  52.546 -55.974  1.00 36.09           N  
ATOM   4075  CA  THR B 177       9.239  51.837 -56.645  1.00 35.79           C  
ATOM   4076  C   THR B 177       8.762  50.504 -57.185  1.00 35.84           C  
ATOM   4077  O   THR B 177       8.848  50.259 -58.397  1.00 36.31           O  
ATOM   4078  CB  THR B 177      10.465  51.620 -55.699  1.00 35.50           C  
ATOM   4079  OG1 THR B 177      11.173  52.848 -55.580  1.00 36.32           O  
ATOM   4080  CG2 THR B 177      11.435  50.552 -56.195  1.00 35.61           C  
ATOM   4081  N   ASP B 178       8.288  49.653 -56.269  1.00 35.54           N  
ATOM   4082  CA  ASP B 178       7.484  48.461 -56.566  1.00 35.25           C  
ATOM   4083  C   ASP B 178       6.437  48.314 -55.444  1.00 34.65           C  
ATOM   4084  O   ASP B 178       6.554  48.958 -54.395  1.00 34.39           O  
ATOM   4085  CB  ASP B 178       8.360  47.208 -56.708  1.00 35.26           C  
ATOM   4086  CG  ASP B 178       8.731  46.581 -55.366  1.00 37.33           C  
ATOM   4087  OD1 ASP B 178       7.907  46.594 -54.423  1.00 39.25           O  
ATOM   4088  OD2 ASP B 178       9.851  46.038 -55.252  1.00 39.49           O  
ATOM   4089  N   PRO B 179       5.418  47.462 -55.648  1.00 34.16           N  
ATOM   4090  CA  PRO B 179       4.237  47.474 -54.761  1.00 33.67           C  
ATOM   4091  C   PRO B 179       4.446  46.938 -53.353  1.00 32.96           C  
ATOM   4092  O   PRO B 179       3.511  46.953 -52.549  1.00 32.88           O  
ATOM   4093  CB  PRO B 179       3.212  46.613 -55.508  1.00 33.76           C  
ATOM   4094  CG  PRO B 179       3.766  46.450 -56.907  1.00 34.22           C  
ATOM   4095  CD  PRO B 179       5.247  46.541 -56.784  1.00 34.24           C  
ATOM   4096  N   SER B 180       5.649  46.473 -53.056  1.00 32.20           N  
ATOM   4097  CA  SER B 180       5.953  46.050 -51.706  1.00 31.81           C  
ATOM   4098  C   SER B 180       6.228  47.274 -50.830  1.00 32.15           C  
ATOM   4099  O   SER B 180       6.261  47.185 -49.593  1.00 32.55           O  
ATOM   4100  CB  SER B 180       7.115  45.045 -51.678  1.00 31.30           C  
ATOM   4101  OG  SER B 180       8.362  45.689 -51.733  1.00 29.75           O  
ATOM   4102  N   GLY B 181       6.398  48.424 -51.469  1.00 31.86           N  
ATOM   4103  CA  GLY B 181       6.753  49.621 -50.735  1.00 31.92           C  
ATOM   4104  C   GLY B 181       5.566  50.460 -50.320  1.00 31.99           C  
ATOM   4105  O   GLY B 181       5.720  51.426 -49.584  1.00 31.61           O  
ATOM   4106  N   ASP B 182       4.382  50.087 -50.783  1.00 32.32           N  
ATOM   4107  CA  ASP B 182       3.193  50.927 -50.622  1.00 32.94           C  
ATOM   4108  C   ASP B 182       2.927  51.414 -49.199  1.00 32.56           C  
ATOM   4109  O   ASP B 182       2.569  52.571 -48.990  1.00 33.11           O  
ATOM   4110  CB  ASP B 182       1.968  50.221 -51.194  1.00 33.36           C  
ATOM   4111  CG  ASP B 182       1.866  50.371 -52.719  1.00 36.23           C  
ATOM   4112  OD1 ASP B 182       0.784  50.804 -53.183  1.00 39.21           O  
ATOM   4113  OD2 ASP B 182       2.855  50.079 -53.456  1.00 38.09           O  
ATOM   4114  N   ARG B 183       3.135  50.537 -48.231  1.00 31.94           N  
ATOM   4115  CA  ARG B 183       2.927  50.844 -46.840  1.00 31.30           C  
ATOM   4116  C   ARG B 183       3.986  51.824 -46.287  1.00 31.44           C  
ATOM   4117  O   ARG B 183       3.652  52.881 -45.729  1.00 31.19           O  
ATOM   4118  CB  ARG B 183       2.950  49.533 -46.077  1.00 31.47           C  
ATOM   4119  CG  ARG B 183       2.424  49.633 -44.701  1.00 32.31           C  
ATOM   4120  CD  ARG B 183       0.982  49.993 -44.747  1.00 35.61           C  
ATOM   4121  NE  ARG B 183       0.651  50.906 -43.675  1.00 38.74           N  
ATOM   4122  CZ  ARG B 183      -0.560  51.399 -43.478  1.00 41.89           C  
ATOM   4123  NH1 ARG B 183      -1.557  51.050 -44.300  1.00 42.24           N  
ATOM   4124  NH2 ARG B 183      -0.766  52.243 -42.461  1.00 43.28           N  
ATOM   4125  N   THR B 184       5.258  51.460 -46.433  1.00 31.08           N  
ATOM   4126  CA  THR B 184       6.376  52.312 -46.035  1.00 31.33           C  
ATOM   4127  C   THR B 184       6.205  53.781 -46.484  1.00 31.47           C  
ATOM   4128  O   THR B 184       6.287  54.695 -45.673  1.00 31.35           O  
ATOM   4129  CB  THR B 184       7.724  51.734 -46.566  1.00 31.77           C  
ATOM   4130  OG1 THR B 184       7.864  50.349 -46.182  1.00 31.81           O  
ATOM   4131  CG2 THR B 184       8.916  52.549 -46.062  1.00 30.94           C  
ATOM   4132  N   ALA B 185       5.963  53.983 -47.775  1.00 31.70           N  
ATOM   4133  CA  ALA B 185       5.643  55.287 -48.335  1.00 32.15           C  
ATOM   4134  C   ALA B 185       4.528  56.022 -47.592  1.00 32.64           C  
ATOM   4135  O   ALA B 185       4.716  57.163 -47.193  1.00 32.71           O  
ATOM   4136  CB  ALA B 185       5.286  55.158 -49.811  1.00 32.05           C  
ATOM   4137  N   GLU B 186       3.368  55.392 -47.419  1.00 33.21           N  
ATOM   4138  CA  GLU B 186       2.251  56.051 -46.721  1.00 34.21           C  
ATOM   4139  C   GLU B 186       2.685  56.491 -45.310  1.00 33.49           C  
ATOM   4140  O   GLU B 186       2.350  57.587 -44.857  1.00 33.14           O  
ATOM   4141  CB  GLU B 186       1.032  55.116 -46.645  1.00 35.03           C  
ATOM   4142  CG  GLU B 186      -0.323  55.761 -46.995  1.00 39.67           C  
ATOM   4143  CD  GLU B 186      -1.525  55.076 -46.282  1.00 46.24           C  
ATOM   4144  OE1 GLU B 186      -2.368  54.441 -46.979  1.00 48.13           O  
ATOM   4145  OE2 GLU B 186      -1.627  55.180 -45.023  1.00 47.37           O  
ATOM   4146  N   VAL B 187       3.457  55.623 -44.651  1.00 33.11           N  
ATOM   4147  CA  VAL B 187       3.951  55.818 -43.289  1.00 32.34           C  
ATOM   4148  C   VAL B 187       5.031  56.887 -43.250  1.00 32.45           C  
ATOM   4149  O   VAL B 187       5.028  57.750 -42.373  1.00 32.54           O  
ATOM   4150  CB  VAL B 187       4.490  54.481 -42.716  1.00 32.24           C  
ATOM   4151  CG1 VAL B 187       5.477  54.695 -41.597  1.00 30.62           C  
ATOM   4152  CG2 VAL B 187       3.338  53.600 -42.245  1.00 32.38           C  
HETATM 4153  N   MSE B 188       5.942  56.831 -44.215  1.00 32.41           N  
HETATM 4154  CA  MSE B 188       7.037  57.780 -44.293  1.00 32.18           C  
HETATM 4155  C   MSE B 188       6.584  59.206 -44.656  1.00 32.40           C  
HETATM 4156  O   MSE B 188       7.132  60.175 -44.139  1.00 33.61           O  
HETATM 4157  CB  MSE B 188       8.118  57.277 -45.241  1.00 32.01           C  
HETATM 4158  CG  MSE B 188       9.505  57.678 -44.812  1.00 32.97           C  
HETATM 4159 SE   MSE B 188      10.140  56.594 -43.343  1.00 32.76          SE  
HETATM 4160  CE  MSE B 188       8.592  56.710 -42.215  1.00 33.68           C  
ATOM   4161  N   ASN B 189       5.580  59.362 -45.509  1.00 31.69           N  
ATOM   4162  CA  ASN B 189       5.106  60.702 -45.805  1.00 31.27           C  
ATOM   4163  C   ASN B 189       4.433  61.317 -44.582  1.00 31.01           C  
ATOM   4164  O   ASN B 189       4.426  62.531 -44.389  1.00 31.66           O  
ATOM   4165  CB  ASN B 189       4.181  60.697 -47.022  1.00 31.22           C  
ATOM   4166  CG  ASN B 189       4.906  60.292 -48.302  1.00 32.22           C  
ATOM   4167  OD1 ASN B 189       6.088  60.587 -48.488  1.00 33.47           O  
ATOM   4168  ND2 ASN B 189       4.199  59.611 -49.186  1.00 32.64           N  
ATOM   4169  N   ALA B 190       3.882  60.467 -43.740  1.00 30.33           N  
ATOM   4170  CA  ALA B 190       3.150  60.945 -42.606  1.00 29.55           C  
ATOM   4171  C   ALA B 190       4.149  61.271 -41.515  1.00 29.16           C  
ATOM   4172  O   ALA B 190       3.909  62.164 -40.703  1.00 29.72           O  
ATOM   4173  CB  ALA B 190       2.124  59.904 -42.150  1.00 29.65           C  
ATOM   4174  N   TYR B 191       5.281  60.584 -41.500  1.00 28.04           N  
ATOM   4175  CA  TYR B 191       6.298  60.952 -40.543  1.00 27.74           C  
ATOM   4176  C   TYR B 191       6.973  62.238 -40.949  1.00 28.17           C  
ATOM   4177  O   TYR B 191       7.197  63.114 -40.118  1.00 28.09           O  
ATOM   4178  CB  TYR B 191       7.346  59.867 -40.355  1.00 27.43           C  
ATOM   4179  CG  TYR B 191       8.552  60.357 -39.597  1.00 26.73           C  
ATOM   4180  CD1 TYR B 191       8.464  60.669 -38.238  1.00 26.05           C  
ATOM   4181  CD2 TYR B 191       9.775  60.537 -40.233  1.00 26.47           C  
ATOM   4182  CE1 TYR B 191       9.562  61.135 -37.526  1.00 25.15           C  
ATOM   4183  CE2 TYR B 191      10.889  61.013 -39.526  1.00 26.19           C  
ATOM   4184  CZ  TYR B 191      10.777  61.305 -38.166  1.00 25.26           C  
ATOM   4185  OH  TYR B 191      11.871  61.766 -37.443  1.00 23.31           O  
ATOM   4186  N   LEU B 192       7.311  62.357 -42.223  1.00 28.80           N  
ATOM   4187  CA  LEU B 192       7.979  63.566 -42.702  1.00 29.79           C  
ATOM   4188  C   LEU B 192       7.196  64.875 -42.446  1.00 30.65           C  
ATOM   4189  O   LEU B 192       7.786  65.908 -42.098  1.00 30.03           O  
ATOM   4190  CB  LEU B 192       8.358  63.408 -44.170  1.00 29.45           C  
ATOM   4191  CG  LEU B 192       9.814  63.015 -44.457  1.00 29.03           C  
ATOM   4192  CD1 LEU B 192      10.585  62.499 -43.241  1.00 26.56           C  
ATOM   4193  CD2 LEU B 192       9.878  62.032 -45.629  1.00 28.11           C  
ATOM   4194  N   GLU B 193       5.873  64.809 -42.613  1.00 31.97           N  
ATOM   4195  CA  GLU B 193       4.985  65.919 -42.278  1.00 33.44           C  
ATOM   4196  C   GLU B 193       5.102  66.208 -40.815  1.00 33.51           C  
ATOM   4197  O   GLU B 193       5.353  67.321 -40.429  1.00 33.28           O  
ATOM   4198  CB  GLU B 193       3.522  65.608 -42.626  1.00 33.46           C  
ATOM   4199  CG  GLU B 193       3.116  66.065 -44.011  1.00 36.35           C  
ATOM   4200  CD  GLU B 193       3.132  67.595 -44.166  1.00 40.14           C  
ATOM   4201  OE1 GLU B 193       2.432  68.281 -43.373  1.00 41.08           O  
ATOM   4202  OE2 GLU B 193       3.834  68.102 -45.087  1.00 40.25           O  
ATOM   4203  N   GLU B 194       4.926  65.183 -40.002  1.00 34.67           N  
ATOM   4204  CA  GLU B 194       4.992  65.352 -38.571  1.00 36.35           C  
ATOM   4205  C   GLU B 194       6.295  66.097 -38.193  1.00 36.85           C  
ATOM   4206  O   GLU B 194       6.243  67.151 -37.538  1.00 37.19           O  
ATOM   4207  CB  GLU B 194       4.858  63.991 -37.877  1.00 36.58           C  
ATOM   4208  CG  GLU B 194       4.995  64.011 -36.364  1.00 39.73           C  
ATOM   4209  CD  GLU B 194       3.792  64.624 -35.662  1.00 44.94           C  
ATOM   4210  OE1 GLU B 194       3.981  65.260 -34.594  1.00 46.71           O  
ATOM   4211  OE2 GLU B 194       2.660  64.470 -36.184  1.00 46.69           O  
ATOM   4212  N   ALA B 195       7.445  65.576 -38.640  1.00 36.96           N  
ATOM   4213  CA  ALA B 195       8.740  66.176 -38.332  1.00 36.82           C  
ATOM   4214  C   ALA B 195       8.812  67.597 -38.855  1.00 37.05           C  
ATOM   4215  O   ALA B 195       9.462  68.444 -38.250  1.00 37.45           O  
ATOM   4216  CB  ALA B 195       9.853  65.353 -38.905  1.00 36.55           C  
ATOM   4217  N   ARG B 196       8.124  67.837 -39.969  1.00 37.18           N  
ATOM   4218  CA  ARG B 196       8.069  69.132 -40.623  1.00 37.37           C  
ATOM   4219  C   ARG B 196       7.549  70.230 -39.701  1.00 38.17           C  
ATOM   4220  O   ARG B 196       8.158  71.305 -39.614  1.00 38.59           O  
ATOM   4221  CB  ARG B 196       7.138  69.056 -41.819  1.00 37.03           C  
ATOM   4222  CG  ARG B 196       7.291  70.183 -42.759  1.00 35.81           C  
ATOM   4223  CD  ARG B 196       7.983  69.655 -43.945  1.00 33.59           C  
ATOM   4224  NE  ARG B 196       7.047  68.886 -44.745  1.00 32.55           N  
ATOM   4225  CZ  ARG B 196       7.345  67.814 -45.468  1.00 31.51           C  
ATOM   4226  NH1 ARG B 196       8.571  67.322 -45.508  1.00 30.23           N  
ATOM   4227  NH2 ARG B 196       6.385  67.225 -46.150  1.00 32.79           N  
ATOM   4228  N   ARG B 197       6.418  69.979 -39.045  1.00 38.18           N  
ATOM   4229  CA  ARG B 197       5.869  70.963 -38.141  1.00 39.24           C  
ATOM   4230  C   ARG B 197       6.737  71.145 -36.888  1.00 38.85           C  
ATOM   4231  O   ARG B 197       7.110  72.269 -36.539  1.00 39.02           O  
ATOM   4232  CB  ARG B 197       4.404  70.666 -37.803  1.00 40.06           C  
ATOM   4233  CG  ARG B 197       4.108  69.586 -36.713  1.00 44.19           C  
ATOM   4234  CD  ARG B 197       2.579  69.405 -36.497  1.00 49.64           C  
ATOM   4235  NE  ARG B 197       1.875  69.863 -37.698  1.00 54.59           N  
ATOM   4236  CZ  ARG B 197       1.662  69.134 -38.797  1.00 56.90           C  
ATOM   4237  NH1 ARG B 197       2.048  67.855 -38.858  1.00 57.36           N  
ATOM   4238  NH2 ARG B 197       1.034  69.688 -39.835  1.00 57.22           N  
ATOM   4239  N   ILE B 198       7.079  70.036 -36.238  1.00 38.46           N  
ATOM   4240  CA  ILE B 198       7.911  70.061 -35.047  1.00 38.04           C  
ATOM   4241  C   ILE B 198       9.184  70.849 -35.318  1.00 38.06           C  
ATOM   4242  O   ILE B 198       9.519  71.785 -34.578  1.00 38.23           O  
ATOM   4243  CB  ILE B 198       8.263  68.646 -34.566  1.00 37.92           C  
ATOM   4244  CG1 ILE B 198       7.017  67.948 -34.034  1.00 37.89           C  
ATOM   4245  CG2 ILE B 198       9.343  68.691 -33.484  1.00 37.71           C  
ATOM   4246  CD1 ILE B 198       7.249  66.500 -33.681  1.00 38.58           C  
ATOM   4247  N   LEU B 199       9.885  70.479 -36.384  1.00 37.60           N  
ATOM   4248  CA  LEU B 199      11.095  71.183 -36.731  1.00 37.28           C  
ATOM   4249  C   LEU B 199      10.801  72.681 -36.870  1.00 37.82           C  
ATOM   4250  O   LEU B 199      11.485  73.507 -36.264  1.00 37.72           O  
ATOM   4251  CB  LEU B 199      11.703  70.597 -38.003  1.00 36.85           C  
ATOM   4252  CG  LEU B 199      13.018  69.826 -37.924  1.00 34.38           C  
ATOM   4253  CD1 LEU B 199      13.098  69.072 -36.666  1.00 33.51           C  
ATOM   4254  CD2 LEU B 199      13.155  68.897 -39.093  1.00 31.53           C  
ATOM   4255  N   SER B 200       9.751  73.013 -37.619  1.00 38.38           N  
ATOM   4256  CA  SER B 200       9.415  74.409 -37.938  1.00 38.97           C  
ATOM   4257  C   SER B 200       9.087  75.213 -36.705  1.00 39.52           C  
ATOM   4258  O   SER B 200       9.190  76.446 -36.707  1.00 39.81           O  
ATOM   4259  CB  SER B 200       8.220  74.483 -38.884  1.00 38.77           C  
ATOM   4260  OG  SER B 200       8.655  74.446 -40.220  1.00 38.97           O  
ATOM   4261  N   ASP B 201       8.699  74.513 -35.652  1.00 39.79           N  
ATOM   4262  CA  ASP B 201       8.169  75.175 -34.485  1.00 40.32           C  
ATOM   4263  C   ASP B 201       9.144  75.233 -33.324  1.00 39.78           C  
ATOM   4264  O   ASP B 201       8.888  75.926 -32.339  1.00 39.74           O  
ATOM   4265  CB  ASP B 201       6.894  74.468 -34.039  1.00 41.12           C  
ATOM   4266  CG  ASP B 201       5.791  75.441 -33.701  1.00 43.45           C  
ATOM   4267  OD1 ASP B 201       4.611  75.013 -33.747  1.00 44.83           O  
ATOM   4268  OD2 ASP B 201       6.111  76.632 -33.417  1.00 45.86           O  
ATOM   4269  N   HIS B 202      10.246  74.497 -33.449  1.00 39.27           N  
ATOM   4270  CA  HIS B 202      11.228  74.357 -32.389  1.00 38.88           C  
ATOM   4271  C   HIS B 202      11.976  75.650 -32.128  1.00 39.15           C  
ATOM   4272  O   HIS B 202      12.285  76.383 -33.064  1.00 39.08           O  
ATOM   4273  CB  HIS B 202      12.213  73.279 -32.768  1.00 38.40           C  
ATOM   4274  CG  HIS B 202      12.891  72.653 -31.598  1.00 37.93           C  
ATOM   4275  ND1 HIS B 202      13.983  73.221 -30.982  1.00 37.77           N  
ATOM   4276  CD2 HIS B 202      12.645  71.496 -30.940  1.00 37.22           C  
ATOM   4277  CE1 HIS B 202      14.386  72.438 -29.997  1.00 37.99           C  
ATOM   4278  NE2 HIS B 202      13.590  71.384 -29.951  1.00 38.33           N  
ATOM   4279  N   ARG B 203      12.277  75.924 -30.858  1.00 39.64           N  
ATOM   4280  CA  ARG B 203      12.941  77.191 -30.491  1.00 40.17           C  
ATOM   4281  C   ARG B 203      14.321  77.360 -31.134  1.00 39.49           C  
ATOM   4282  O   ARG B 203      14.705  78.480 -31.472  1.00 39.40           O  
ATOM   4283  CB  ARG B 203      13.029  77.408 -28.971  1.00 40.60           C  
ATOM   4284  CG  ARG B 203      13.794  76.318 -28.229  1.00 43.66           C  
ATOM   4285  CD  ARG B 203      14.779  76.906 -27.226  1.00 48.86           C  
ATOM   4286  NE  ARG B 203      15.821  75.940 -26.830  1.00 53.06           N  
ATOM   4287  CZ  ARG B 203      17.138  76.086 -27.032  1.00 54.31           C  
ATOM   4288  NH1 ARG B 203      17.629  77.168 -27.636  1.00 54.23           N  
ATOM   4289  NH2 ARG B 203      17.975  75.137 -26.618  1.00 55.08           N  
ATOM   4290  N   VAL B 204      15.053  76.260 -31.316  1.00 38.60           N  
ATOM   4291  CA  VAL B 204      16.358  76.341 -31.955  1.00 37.93           C  
ATOM   4292  C   VAL B 204      16.225  77.023 -33.309  1.00 37.76           C  
ATOM   4293  O   VAL B 204      17.067  77.834 -33.677  1.00 37.87           O  
ATOM   4294  CB  VAL B 204      17.038  74.966 -32.098  1.00 37.95           C  
ATOM   4295  CG1 VAL B 204      18.286  75.050 -32.975  1.00 37.02           C  
ATOM   4296  CG2 VAL B 204      17.403  74.411 -30.725  1.00 38.02           C  
ATOM   4297  N   ASN B 205      15.151  76.719 -34.030  1.00 37.54           N  
ATOM   4298  CA  ASN B 205      14.940  77.299 -35.346  1.00 37.47           C  
ATOM   4299  C   ASN B 205      14.337  78.704 -35.312  1.00 37.81           C  
ATOM   4300  O   ASN B 205      14.643  79.527 -36.174  1.00 37.87           O  
ATOM   4301  CB  ASN B 205      14.123  76.367 -36.241  1.00 37.05           C  
ATOM   4302  CG  ASN B 205      14.962  75.272 -36.872  1.00 37.09           C  
ATOM   4303  OD1 ASN B 205      16.179  75.396 -37.033  1.00 35.28           O  
ATOM   4304  ND2 ASN B 205      14.306  74.183 -37.236  1.00 38.46           N  
ATOM   4305  N   LYS B 206      13.485  78.985 -34.325  1.00 38.30           N  
ATOM   4306  CA  LYS B 206      12.951  80.335 -34.160  1.00 38.72           C  
ATOM   4307  C   LYS B 206      14.091  81.248 -33.739  1.00 39.11           C  
ATOM   4308  O   LYS B 206      14.139  82.404 -34.141  1.00 39.56           O  
ATOM   4309  CB  LYS B 206      11.809  80.368 -33.152  1.00 38.54           C  
ATOM   4310  CG  LYS B 206      10.516  79.813 -33.719  1.00 40.10           C  
ATOM   4311  CD  LYS B 206       9.289  80.054 -32.824  1.00 43.22           C  
ATOM   4312  CE  LYS B 206       8.751  81.495 -32.952  1.00 44.13           C  
ATOM   4313  NZ  LYS B 206       7.336  81.597 -32.502  1.00 44.40           N  
ATOM   4314  N   GLU B 207      15.014  80.705 -32.947  1.00 39.34           N  
ATOM   4315  CA  GLU B 207      16.278  81.352 -32.647  1.00 39.61           C  
ATOM   4316  C   GLU B 207      17.043  81.693 -33.903  1.00 39.21           C  
ATOM   4317  O   GLU B 207      17.508  82.818 -34.055  1.00 39.45           O  
ATOM   4318  CB  GLU B 207      17.142  80.462 -31.752  1.00 40.05           C  
ATOM   4319  CG  GLU B 207      17.029  80.805 -30.283  1.00 42.70           C  
ATOM   4320  CD  GLU B 207      17.598  82.188 -29.989  1.00 46.66           C  
ATOM   4321  OE1 GLU B 207      16.796  83.141 -29.740  1.00 47.44           O  
ATOM   4322  OE2 GLU B 207      18.849  82.316 -30.046  1.00 46.97           O  
ATOM   4323  N   ARG B 208      17.164  80.725 -34.803  1.00 38.91           N  
ATOM   4324  CA  ARG B 208      17.922  80.913 -36.026  1.00 38.92           C  
ATOM   4325  C   ARG B 208      17.394  82.034 -36.931  1.00 39.22           C  
ATOM   4326  O   ARG B 208      18.190  82.829 -37.423  1.00 39.28           O  
ATOM   4327  CB  ARG B 208      18.046  79.606 -36.811  1.00 38.72           C  
ATOM   4328  CG  ARG B 208      19.152  78.678 -36.308  1.00 38.76           C  
ATOM   4329  CD  ARG B 208      19.259  77.465 -37.215  1.00 36.85           C  
ATOM   4330  NE  ARG B 208      20.165  76.432 -36.720  1.00 35.05           N  
ATOM   4331  CZ  ARG B 208      20.366  75.264 -37.328  1.00 34.88           C  
ATOM   4332  NH1 ARG B 208      19.730  74.969 -38.458  1.00 35.32           N  
ATOM   4333  NH2 ARG B 208      21.206  74.384 -36.810  1.00 34.49           N  
ATOM   4334  N   VAL B 209      16.083  82.107 -37.160  1.00 39.28           N  
ATOM   4335  CA  VAL B 209      15.568  83.104 -38.099  1.00 39.94           C  
ATOM   4336  C   VAL B 209      15.889  84.513 -37.593  1.00 40.50           C  
ATOM   4337  O   VAL B 209      16.353  85.367 -38.364  1.00 40.30           O  
ATOM   4338  CB  VAL B 209      14.049  82.957 -38.394  1.00 40.07           C  
ATOM   4339  CG1 VAL B 209      13.633  83.919 -39.506  1.00 40.12           C  
ATOM   4340  CG2 VAL B 209      13.694  81.529 -38.806  1.00 39.83           C  
ATOM   4341  N   LYS B 210      15.669  84.722 -36.290  1.00 41.07           N  
ATOM   4342  CA  LYS B 210      15.920  86.002 -35.618  1.00 41.50           C  
ATOM   4343  C   LYS B 210      17.358  86.439 -35.779  1.00 41.31           C  
ATOM   4344  O   LYS B 210      17.626  87.562 -36.203  1.00 41.78           O  
ATOM   4345  CB  LYS B 210      15.570  85.941 -34.121  1.00 41.97           C  
ATOM   4346  CG  LYS B 210      14.070  85.690 -33.778  1.00 44.11           C  
ATOM   4347  CD  LYS B 210      13.090  86.667 -34.490  1.00 47.33           C  
ATOM   4348  CE  LYS B 210      12.554  86.104 -35.831  1.00 48.09           C  
ATOM   4349  NZ  LYS B 210      12.228  87.170 -36.841  1.00 47.46           N  
ATOM   4350  N   ASN B 211      18.286  85.548 -35.461  1.00 40.69           N  
ATOM   4351  CA  ASN B 211      19.702  85.868 -35.599  1.00 40.13           C  
ATOM   4352  C   ASN B 211      20.223  85.848 -37.042  1.00 39.30           C  
ATOM   4353  O   ASN B 211      21.431  85.932 -37.255  1.00 39.36           O  
ATOM   4354  CB  ASN B 211      20.528  84.946 -34.708  1.00 40.46           C  
ATOM   4355  CG  ASN B 211      20.013  84.898 -33.281  1.00 42.16           C  
ATOM   4356  OD1 ASN B 211      19.147  85.692 -32.883  1.00 44.91           O  
ATOM   4357  ND2 ASN B 211      20.539  83.963 -32.500  1.00 42.95           N  
ATOM   4358  N   GLY B 212      19.313  85.739 -38.017  1.00 38.56           N  
ATOM   4359  CA  GLY B 212      19.654  85.716 -39.452  1.00 37.48           C  
ATOM   4360  C   GLY B 212      20.334  84.472 -40.029  1.00 36.93           C  
ATOM   4361  O   GLY B 212      20.961  84.550 -41.088  1.00 37.05           O  
ATOM   4362  N   ARG B 213      20.206  83.333 -39.340  1.00 36.16           N  
ATOM   4363  CA  ARG B 213      20.714  82.023 -39.792  1.00 35.01           C  
ATOM   4364  C   ARG B 213      19.626  81.216 -40.510  1.00 33.85           C  
ATOM   4365  O   ARG B 213      18.428  81.479 -40.309  1.00 33.48           O  
ATOM   4366  CB  ARG B 213      21.144  81.188 -38.588  1.00 35.49           C  
ATOM   4367  CG  ARG B 213      21.804  81.928 -37.458  1.00 36.65           C  
ATOM   4368  CD  ARG B 213      23.256  81.538 -37.397  1.00 39.11           C  
ATOM   4369  NE  ARG B 213      23.820  81.671 -36.058  1.00 41.12           N  
ATOM   4370  CZ  ARG B 213      24.339  82.794 -35.561  1.00 42.70           C  
ATOM   4371  NH1 ARG B 213      24.367  83.912 -36.294  1.00 42.81           N  
ATOM   4372  NH2 ARG B 213      24.834  82.797 -34.324  1.00 42.96           N  
ATOM   4373  N   LEU B 214      20.035  80.219 -41.305  1.00 32.35           N  
ATOM   4374  CA  LEU B 214      19.089  79.287 -41.948  1.00 31.11           C  
ATOM   4375  C   LEU B 214      18.611  78.169 -41.018  1.00 30.58           C  
ATOM   4376  O   LEU B 214      19.439  77.437 -40.445  1.00 30.77           O  
ATOM   4377  CB  LEU B 214      19.706  78.643 -43.172  1.00 30.76           C  
ATOM   4378  CG  LEU B 214      19.824  79.557 -44.370  1.00 30.39           C  
ATOM   4379  CD1 LEU B 214      20.818  78.960 -45.376  1.00 29.17           C  
ATOM   4380  CD2 LEU B 214      18.457  79.831 -44.969  1.00 28.65           C  
ATOM   4381  N   PRO B 215      17.280  78.015 -40.874  1.00 29.41           N  
ATOM   4382  CA  PRO B 215      16.787  76.966 -39.997  1.00 28.70           C  
ATOM   4383  C   PRO B 215      16.852  75.625 -40.698  1.00 28.37           C  
ATOM   4384  O   PRO B 215      16.890  75.581 -41.927  1.00 28.36           O  
ATOM   4385  CB  PRO B 215      15.339  77.364 -39.755  1.00 28.68           C  
ATOM   4386  CG  PRO B 215      14.947  78.179 -40.960  1.00 28.58           C  
ATOM   4387  CD  PRO B 215      16.192  78.775 -41.521  1.00 29.32           C  
ATOM   4388  N   GLY B 216      16.905  74.542 -39.927  1.00 27.92           N  
ATOM   4389  CA  GLY B 216      16.780  73.202 -40.485  1.00 26.74           C  
ATOM   4390  C   GLY B 216      15.380  72.743 -40.163  1.00 26.21           C  
ATOM   4391  O   GLY B 216      15.153  72.188 -39.094  1.00 26.06           O  
ATOM   4392  N   ASN B 217      14.439  73.010 -41.065  1.00 25.57           N  
ATOM   4393  CA  ASN B 217      13.029  72.725 -40.825  1.00 25.34           C  
ATOM   4394  C   ASN B 217      12.507  71.669 -41.782  1.00 25.31           C  
ATOM   4395  O   ASN B 217      11.296  71.525 -42.015  1.00 25.83           O  
ATOM   4396  CB  ASN B 217      12.200  73.996 -40.956  1.00 25.34           C  
ATOM   4397  CG  ASN B 217      12.384  74.659 -42.287  1.00 25.62           C  
ATOM   4398  OD1 ASN B 217      13.258  74.274 -43.067  1.00 26.87           O  
ATOM   4399  ND2 ASN B 217      11.573  75.668 -42.563  1.00 26.06           N  
ATOM   4400  N   GLU B 218      13.441  70.942 -42.360  1.00 24.95           N  
ATOM   4401  CA  GLU B 218      13.113  69.781 -43.145  1.00 25.00           C  
ATOM   4402  C   GLU B 218      14.137  68.757 -42.776  1.00 24.44           C  
ATOM   4403  O   GLU B 218      15.337  69.077 -42.741  1.00 24.58           O  
ATOM   4404  CB  GLU B 218      13.279  70.055 -44.637  1.00 25.47           C  
ATOM   4405  CG  GLU B 218      12.016  70.355 -45.396  1.00 27.26           C  
ATOM   4406  CD  GLU B 218      11.047  69.200 -45.489  1.00 30.15           C  
ATOM   4407  OE1 GLU B 218      11.446  68.010 -45.489  1.00 31.09           O  
ATOM   4408  OE2 GLU B 218       9.844  69.504 -45.579  1.00 32.14           O  
ATOM   4409  N   LEU B 219      13.673  67.546 -42.487  1.00 23.28           N  
ATOM   4410  CA  LEU B 219      14.534  66.393 -42.575  1.00 22.52           C  
ATOM   4411  C   LEU B 219      14.351  65.781 -43.942  1.00 21.70           C  
ATOM   4412  O   LEU B 219      13.341  65.164 -44.254  1.00 21.49           O  
ATOM   4413  CB  LEU B 219      14.242  65.369 -41.487  1.00 22.82           C  
ATOM   4414  CG  LEU B 219      15.360  64.334 -41.383  1.00 22.08           C  
ATOM   4415  CD1 LEU B 219      16.451  64.902 -40.510  1.00 22.04           C  
ATOM   4416  CD2 LEU B 219      14.826  63.078 -40.791  1.00 20.77           C  
ATOM   4417  N   LEU B 220      15.341  65.990 -44.769  1.00 21.26           N  
ATOM   4418  CA  LEU B 220      15.350  65.414 -46.089  1.00 21.31           C  
ATOM   4419  C   LEU B 220      15.978  63.990 -46.066  1.00 21.69           C  
ATOM   4420  O   LEU B 220      17.197  63.831 -45.804  1.00 21.61           O  
ATOM   4421  CB  LEU B 220      16.122  66.363 -47.018  1.00 20.93           C  
ATOM   4422  CG  LEU B 220      15.367  67.206 -48.046  1.00 19.59           C  
ATOM   4423  CD1 LEU B 220      14.184  67.900 -47.463  1.00 19.75           C  
ATOM   4424  CD2 LEU B 220      16.311  68.203 -48.648  1.00 19.96           C  
ATOM   4425  N   VAL B 221      15.175  62.957 -46.333  1.00 21.39           N  
ATOM   4426  CA  VAL B 221      15.732  61.589 -46.333  1.00 21.60           C  
ATOM   4427  C   VAL B 221      16.036  60.991 -47.711  1.00 21.96           C  
ATOM   4428  O   VAL B 221      15.360  61.274 -48.707  1.00 21.07           O  
ATOM   4429  CB  VAL B 221      14.874  60.624 -45.515  1.00 21.43           C  
ATOM   4430  CG1 VAL B 221      14.696  61.160 -44.111  1.00 20.99           C  
ATOM   4431  CG2 VAL B 221      13.536  60.421 -46.165  1.00 21.71           C  
ATOM   4432  N   ARG B 222      17.080  60.179 -47.757  1.00 23.10           N  
ATOM   4433  CA  ARG B 222      17.443  59.471 -48.995  1.00 24.99           C  
ATOM   4434  C   ARG B 222      18.102  58.095 -48.740  1.00 25.83           C  
ATOM   4435  O   ARG B 222      18.397  57.740 -47.581  1.00 26.22           O  
ATOM   4436  CB  ARG B 222      18.347  60.348 -49.874  1.00 24.87           C  
ATOM   4437  CG  ARG B 222      19.797  60.365 -49.421  1.00 26.52           C  
ATOM   4438  CD  ARG B 222      20.642  61.424 -50.100  1.00 29.08           C  
ATOM   4439  NE  ARG B 222      21.972  61.461 -49.492  1.00 31.38           N  
ATOM   4440  CZ  ARG B 222      22.318  62.221 -48.452  1.00 32.95           C  
ATOM   4441  NH1 ARG B 222      21.445  63.050 -47.870  1.00 33.59           N  
ATOM   4442  NH2 ARG B 222      23.554  62.149 -47.990  1.00 32.98           N  
ATOM   4443  N   SER B 223      18.332  57.338 -49.821  1.00 26.63           N  
ATOM   4444  CA  SER B 223      19.050  56.053 -49.763  1.00 27.66           C  
ATOM   4445  C   SER B 223      18.502  55.068 -48.713  1.00 27.97           C  
ATOM   4446  O   SER B 223      19.238  54.575 -47.877  1.00 27.91           O  
ATOM   4447  CB  SER B 223      20.551  56.285 -49.532  1.00 27.76           C  
ATOM   4448  OG  SER B 223      21.113  57.107 -50.551  1.00 29.72           O  
ATOM   4449  N   ALA B 224      17.205  54.794 -48.763  1.00 28.74           N  
ATOM   4450  CA  ALA B 224      16.577  53.842 -47.867  1.00 29.45           C  
ATOM   4451  C   ALA B 224      17.200  52.461 -48.030  1.00 30.41           C  
ATOM   4452  O   ALA B 224      17.401  51.986 -49.149  1.00 30.51           O  
ATOM   4453  CB  ALA B 224      15.097  53.779 -48.145  1.00 29.32           C  
ATOM   4454  N   GLY B 225      17.509  51.822 -46.909  1.00 31.27           N  
ATOM   4455  CA  GLY B 225      18.089  50.488 -46.927  1.00 32.04           C  
ATOM   4456  C   GLY B 225      17.543  49.706 -45.760  1.00 32.92           C  
ATOM   4457  O   GLY B 225      17.453  50.222 -44.647  1.00 32.44           O  
ATOM   4458  N   LYS B 226      17.159  48.461 -46.018  1.00 34.21           N  
ATOM   4459  CA  LYS B 226      16.585  47.613 -44.977  1.00 35.36           C  
ATOM   4460  C   LYS B 226      17.662  46.730 -44.384  1.00 36.10           C  
ATOM   4461  O   LYS B 226      18.430  46.123 -45.118  1.00 35.82           O  
ATOM   4462  CB  LYS B 226      15.486  46.728 -45.562  1.00 35.27           C  
ATOM   4463  CG  LYS B 226      14.515  46.165 -44.513  1.00 34.97           C  
ATOM   4464  CD  LYS B 226      13.996  44.793 -44.930  1.00 32.90           C  
ATOM   4465  CE  LYS B 226      13.034  44.221 -43.919  1.00 32.06           C  
ATOM   4466  NZ  LYS B 226      11.673  44.560 -44.299  1.00 30.78           N  
ATOM   4467  N   VAL B 227      17.708  46.647 -43.060  1.00 37.40           N  
ATOM   4468  CA  VAL B 227      18.662  45.756 -42.401  1.00 39.19           C  
ATOM   4469  C   VAL B 227      18.213  44.294 -42.557  1.00 40.77           C  
ATOM   4470  O   VAL B 227      17.101  43.930 -42.155  1.00 40.99           O  
ATOM   4471  CB  VAL B 227      18.870  46.120 -40.926  1.00 39.01           C  
ATOM   4472  CG1 VAL B 227      20.081  45.399 -40.369  1.00 37.94           C  
ATOM   4473  CG2 VAL B 227      19.053  47.621 -40.798  1.00 38.86           C  
ATOM   4474  N   PRO B 228      19.068  43.453 -43.170  1.00 42.12           N  
ATOM   4475  CA  PRO B 228      18.605  42.091 -43.468  1.00 43.19           C  
ATOM   4476  C   PRO B 228      18.707  41.095 -42.280  1.00 44.33           C  
ATOM   4477  O   PRO B 228      18.824  41.515 -41.114  1.00 44.22           O  
ATOM   4478  CB  PRO B 228      19.476  41.664 -44.673  1.00 43.15           C  
ATOM   4479  CG  PRO B 228      20.451  42.824 -44.932  1.00 42.62           C  
ATOM   4480  CD  PRO B 228      20.403  43.726 -43.737  1.00 42.08           C  
ATOM   4481  N   ALA B 229      18.654  39.797 -42.609  1.00 45.28           N  
ATOM   4482  CA  ALA B 229      18.551  38.689 -41.651  1.00 45.64           C  
ATOM   4483  C   ALA B 229      19.528  38.794 -40.501  1.00 45.91           C  
ATOM   4484  O   ALA B 229      19.123  38.737 -39.339  1.00 45.95           O  
ATOM   4485  CB  ALA B 229      18.743  37.356 -42.372  1.00 45.75           C  
ATOM   4486  N   ILE B 230      20.803  38.956 -40.856  1.00 46.32           N  
ATOM   4487  CA  ILE B 230      21.958  38.908 -39.934  1.00 46.92           C  
ATOM   4488  C   ILE B 230      21.808  38.086 -38.640  1.00 46.81           C  
ATOM   4489  O   ILE B 230      21.267  38.578 -37.649  1.00 46.99           O  
ATOM   4490  CB  ILE B 230      22.501  40.311 -39.602  1.00 47.07           C  
ATOM   4491  CG1 ILE B 230      23.375  40.851 -40.743  1.00 48.16           C  
ATOM   4492  CG2 ILE B 230      23.381  40.244 -38.384  1.00 48.21           C  
ATOM   4493  CD1 ILE B 230      22.658  41.748 -41.761  1.00 48.45           C  
ATOM   4494  N   PRO B 231      22.303  36.828 -38.646  1.00 46.97           N  
ATOM   4495  CA  PRO B 231      22.335  36.009 -37.436  1.00 46.72           C  
ATOM   4496  C   PRO B 231      23.334  36.547 -36.427  1.00 46.42           C  
ATOM   4497  O   PRO B 231      24.409  37.020 -36.812  1.00 45.96           O  
ATOM   4498  CB  PRO B 231      22.829  34.645 -37.943  1.00 46.68           C  
ATOM   4499  CG  PRO B 231      22.538  34.640 -39.392  1.00 46.92           C  
ATOM   4500  CD  PRO B 231      22.748  36.054 -39.820  1.00 47.03           C  
ATOM   4501  N   SER B 232      22.950  36.459 -35.154  1.00 46.07           N  
ATOM   4502  CA  SER B 232      23.815  36.650 -33.998  1.00 45.83           C  
ATOM   4503  C   SER B 232      25.201  36.105 -34.250  1.00 45.84           C  
ATOM   4504  O   SER B 232      25.374  35.235 -35.078  1.00 45.91           O  
ATOM   4505  CB  SER B 232      23.220  35.868 -32.845  1.00 45.62           C  
ATOM   4506  OG  SER B 232      23.276  36.595 -31.647  1.00 46.76           O  
ATOM   4507  N   PHE B 233      26.199  36.598 -33.535  1.00 46.45           N  
ATOM   4508  CA  PHE B 233      27.520  35.996 -33.640  1.00 47.07           C  
ATOM   4509  C   PHE B 233      27.444  34.542 -33.207  1.00 48.03           C  
ATOM   4510  O   PHE B 233      27.910  33.662 -33.933  1.00 48.29           O  
ATOM   4511  CB  PHE B 233      28.565  36.744 -32.816  1.00 46.77           C  
ATOM   4512  CG  PHE B 233      29.967  36.225 -33.002  1.00 45.74           C  
ATOM   4513  CD1 PHE B 233      30.716  36.589 -34.111  1.00 45.00           C  
ATOM   4514  CD2 PHE B 233      30.540  35.375 -32.065  1.00 45.27           C  
ATOM   4515  CE1 PHE B 233      32.022  36.115 -34.288  1.00 45.04           C  
ATOM   4516  CE2 PHE B 233      31.838  34.892 -32.238  1.00 45.03           C  
ATOM   4517  CZ  PHE B 233      32.585  35.268 -33.348  1.00 44.45           C  
ATOM   4518  N   THR B 234      26.843  34.302 -32.040  1.00 49.04           N  
ATOM   4519  CA  THR B 234      26.608  32.945 -31.522  1.00 50.33           C  
ATOM   4520  C   THR B 234      25.863  32.039 -32.519  1.00 51.13           C  
ATOM   4521  O   THR B 234      26.395  31.012 -32.958  1.00 51.05           O  
ATOM   4522  CB  THR B 234      25.838  32.983 -30.196  1.00 50.26           C  
ATOM   4523  OG1 THR B 234      26.575  33.760 -29.250  1.00 50.28           O  
ATOM   4524  CG2 THR B 234      25.641  31.578 -29.651  1.00 50.41           C  
ATOM   4525  N   GLU B 235      24.638  32.417 -32.874  1.00 52.04           N  
ATOM   4526  CA  GLU B 235      23.952  31.761 -33.981  1.00 53.24           C  
ATOM   4527  C   GLU B 235      24.956  31.387 -35.123  1.00 53.44           C  
ATOM   4528  O   GLU B 235      25.106  30.207 -35.454  1.00 53.58           O  
ATOM   4529  CB  GLU B 235      22.764  32.616 -34.487  1.00 53.42           C  
ATOM   4530  CG  GLU B 235      21.623  32.844 -33.448  1.00 55.16           C  
ATOM   4531  CD  GLU B 235      20.545  33.878 -33.886  1.00 57.42           C  
ATOM   4532  OE1 GLU B 235      19.640  34.177 -33.067  1.00 57.38           O  
ATOM   4533  OE2 GLU B 235      20.596  34.394 -35.033  1.00 58.06           O  
ATOM   4534  N   LYS B 236      25.676  32.371 -35.673  1.00 53.43           N  
ATOM   4535  CA  LYS B 236      26.533  32.145 -36.847  1.00 53.41           C  
ATOM   4536  C   LYS B 236      27.747  31.248 -36.593  1.00 53.29           C  
ATOM   4537  O   LYS B 236      28.029  30.361 -37.391  1.00 53.14           O  
ATOM   4538  CB  LYS B 236      26.972  33.483 -37.471  1.00 53.48           C  
ATOM   4539  CG  LYS B 236      27.968  33.391 -38.650  1.00 54.11           C  
ATOM   4540  CD  LYS B 236      27.594  32.328 -39.698  1.00 56.10           C  
ATOM   4541  CE  LYS B 236      26.485  32.794 -40.626  1.00 57.39           C  
ATOM   4542  NZ  LYS B 236      26.964  33.940 -41.439  1.00 58.87           N  
ATOM   4543  N   ASN B 237      28.450  31.487 -35.490  1.00 53.37           N  
ATOM   4544  CA  ASN B 237      29.756  30.871 -35.228  1.00 53.51           C  
ATOM   4545  C   ASN B 237      29.816  30.003 -33.956  1.00 53.59           C  
ATOM   4546  O   ASN B 237      30.885  29.529 -33.570  1.00 53.41           O  
ATOM   4547  CB  ASN B 237      30.829  31.965 -35.150  1.00 53.69           C  
ATOM   4548  CG  ASN B 237      31.133  32.611 -36.510  1.00 54.59           C  
ATOM   4549  OD1 ASN B 237      31.443  33.809 -36.591  1.00 53.22           O  
ATOM   4550  ND2 ASN B 237      31.059  31.814 -37.581  1.00 55.96           N  
ATOM   4551  N   ARG B 238      28.657  29.784 -33.332  1.00 53.62           N  
ATOM   4552  CA  ARG B 238      28.539  29.149 -32.005  1.00 53.59           C  
ATOM   4553  C   ARG B 238      29.746  29.334 -31.090  1.00 52.69           C  
ATOM   4554  O   ARG B 238      30.456  28.395 -30.761  1.00 52.86           O  
ATOM   4555  CB  ARG B 238      28.072  27.683 -32.097  1.00 54.22           C  
ATOM   4556  CG  ARG B 238      28.732  26.858 -33.178  1.00 56.25           C  
ATOM   4557  CD  ARG B 238      27.913  25.611 -33.500  1.00 60.46           C  
ATOM   4558  NE  ARG B 238      27.695  25.440 -34.940  1.00 64.02           N  
ATOM   4559  CZ  ARG B 238      28.546  25.802 -35.908  1.00 66.08           C  
ATOM   4560  NH1 ARG B 238      29.734  26.347 -35.630  1.00 66.29           N  
ATOM   4561  NH2 ARG B 238      28.210  25.597 -37.177  1.00 66.64           N  
HETATM 4562  N   MSE B 239      29.953  30.585 -30.699  1.00 51.89           N  
HETATM 4563  CA  MSE B 239      31.013  31.010 -29.791  1.00 51.14           C  
HETATM 4564  C   MSE B 239      30.553  32.272 -29.058  1.00 50.09           C  
HETATM 4565  O   MSE B 239      29.506  32.837 -29.382  1.00 50.15           O  
HETATM 4566  CB  MSE B 239      32.281  31.333 -30.574  1.00 51.40           C  
HETATM 4567  CG  MSE B 239      33.103  30.143 -31.018  1.00 53.50           C  
HETATM 4568 SE   MSE B 239      34.807  30.724 -31.824  1.00 60.41          SE  
HETATM 4569  CE  MSE B 239      34.188  31.625 -33.469  1.00 55.94           C  
ATOM   4570  N   LYS B 240      31.337  32.727 -28.086  1.00 48.72           N  
ATOM   4571  CA  LYS B 240      31.045  33.985 -27.408  1.00 47.50           C  
ATOM   4572  C   LYS B 240      32.019  35.079 -27.858  1.00 45.91           C  
ATOM   4573  O   LYS B 240      33.235  34.920 -27.727  1.00 45.59           O  
ATOM   4574  CB  LYS B 240      31.093  33.787 -25.892  1.00 48.10           C  
ATOM   4575  CG  LYS B 240      30.080  34.632 -25.102  1.00 49.49           C  
ATOM   4576  CD  LYS B 240      29.813  34.031 -23.706  1.00 52.23           C  
ATOM   4577  CE  LYS B 240      28.916  32.766 -23.771  1.00 53.07           C  
ATOM   4578  NZ  LYS B 240      28.826  32.033 -22.466  1.00 52.86           N  
ATOM   4579  N   GLY B 241      31.482  36.185 -28.380  1.00 44.26           N  
ATOM   4580  CA  GLY B 241      32.313  37.229 -29.002  1.00 42.28           C  
ATOM   4581  C   GLY B 241      32.438  38.590 -28.325  1.00 40.76           C  
ATOM   4582  O   GLY B 241      31.456  39.159 -27.879  1.00 40.80           O  
ATOM   4583  N   ALA B 242      33.660  39.108 -28.269  1.00 39.27           N  
ATOM   4584  CA  ALA B 242      33.934  40.431 -27.753  1.00 38.08           C  
ATOM   4585  C   ALA B 242      34.795  41.233 -28.730  1.00 37.82           C  
ATOM   4586  O   ALA B 242      35.628  40.690 -29.444  1.00 37.46           O  
ATOM   4587  CB  ALA B 242      34.607  40.338 -26.435  1.00 37.51           C  
ATOM   4588  N   CYS B 243      34.565  42.539 -28.755  1.00 37.64           N  
ATOM   4589  CA  CYS B 243      35.317  43.456 -29.582  1.00 37.46           C  
ATOM   4590  C   CYS B 243      35.991  44.445 -28.671  1.00 37.08           C  
ATOM   4591  O   CYS B 243      35.346  45.075 -27.847  1.00 37.17           O  
ATOM   4592  CB  CYS B 243      34.384  44.196 -30.531  1.00 37.43           C  
ATOM   4593  SG  CYS B 243      33.365  43.083 -31.569  1.00 40.83           S  
ATOM   4594  N   VAL B 244      37.304  44.545 -28.769  1.00 36.86           N  
ATOM   4595  CA  VAL B 244      37.994  45.661 -28.169  1.00 36.42           C  
ATOM   4596  C   VAL B 244      38.188  46.599 -29.336  1.00 37.00           C  
ATOM   4597  O   VAL B 244      39.173  46.515 -30.064  1.00 37.33           O  
ATOM   4598  CB  VAL B 244      39.324  45.266 -27.549  1.00 35.86           C  
ATOM   4599  CG1 VAL B 244      40.017  46.481 -27.002  1.00 35.80           C  
ATOM   4600  CG2 VAL B 244      39.100  44.277 -26.449  1.00 35.77           C  
ATOM   4601  N   VAL B 245      37.203  47.461 -29.539  1.00 37.55           N  
ATOM   4602  CA  VAL B 245      37.156  48.307 -30.708  1.00 38.29           C  
ATOM   4603  C   VAL B 245      36.809  49.742 -30.305  1.00 39.07           C  
ATOM   4604  O   VAL B 245      35.890  49.973 -29.516  1.00 38.99           O  
ATOM   4605  CB  VAL B 245      36.131  47.769 -31.726  1.00 37.99           C  
ATOM   4606  CG1 VAL B 245      35.924  48.749 -32.819  1.00 39.07           C  
ATOM   4607  CG2 VAL B 245      36.614  46.486 -32.340  1.00 38.47           C  
ATOM   4608  N   GLY B 246      37.569  50.703 -30.825  1.00 39.82           N  
ATOM   4609  CA  GLY B 246      37.191  52.109 -30.721  1.00 40.76           C  
ATOM   4610  C   GLY B 246      36.924  52.615 -32.122  1.00 41.59           C  
ATOM   4611  O   GLY B 246      37.745  52.398 -33.026  1.00 42.40           O  
ATOM   4612  N   SER B 247      35.792  53.284 -32.322  1.00 41.47           N  
ATOM   4613  CA  SER B 247      35.347  53.665 -33.669  1.00 41.62           C  
ATOM   4614  C   SER B 247      33.869  53.372 -33.749  1.00 41.97           C  
ATOM   4615  O   SER B 247      33.447  52.225 -33.611  1.00 42.33           O  
ATOM   4616  CB  SER B 247      36.098  52.909 -34.783  1.00 41.48           C  
ATOM   4617  OG  SER B 247      35.205  52.247 -35.673  1.00 40.88           O  
ATOM   4618  N   PRO B 248      33.067  54.408 -33.991  1.00 42.18           N  
ATOM   4619  CA  PRO B 248      31.652  54.188 -33.743  1.00 41.89           C  
ATOM   4620  C   PRO B 248      31.046  53.091 -34.615  1.00 41.35           C  
ATOM   4621  O   PRO B 248      30.137  52.398 -34.152  1.00 41.02           O  
ATOM   4622  CB  PRO B 248      31.025  55.574 -34.007  1.00 41.76           C  
ATOM   4623  CG  PRO B 248      32.190  56.551 -33.829  1.00 42.26           C  
ATOM   4624  CD  PRO B 248      33.351  55.795 -34.414  1.00 42.30           C  
ATOM   4625  N   TRP B 249      31.540  52.913 -35.841  1.00 41.15           N  
ATOM   4626  CA  TRP B 249      30.887  51.944 -36.736  1.00 41.59           C  
ATOM   4627  C   TRP B 249      31.237  50.490 -36.415  1.00 40.78           C  
ATOM   4628  O   TRP B 249      30.388  49.607 -36.503  1.00 40.38           O  
ATOM   4629  CB  TRP B 249      31.089  52.270 -38.214  1.00 41.84           C  
ATOM   4630  CG  TRP B 249      32.408  51.894 -38.722  1.00 45.62           C  
ATOM   4631  CD1 TRP B 249      33.569  52.612 -38.595  1.00 49.61           C  
ATOM   4632  CD2 TRP B 249      32.746  50.708 -39.456  1.00 49.09           C  
ATOM   4633  NE1 TRP B 249      34.617  51.944 -39.207  1.00 51.04           N  
ATOM   4634  CE2 TRP B 249      34.141  50.776 -39.748  1.00 50.97           C  
ATOM   4635  CE3 TRP B 249      32.015  49.600 -39.902  1.00 50.18           C  
ATOM   4636  CZ2 TRP B 249      34.819  49.768 -40.463  1.00 51.63           C  
ATOM   4637  CZ3 TRP B 249      32.689  48.600 -40.619  1.00 52.13           C  
ATOM   4638  CH2 TRP B 249      34.082  48.697 -40.893  1.00 52.10           C  
ATOM   4639  N   LEU B 250      32.477  50.247 -36.010  1.00 40.41           N  
ATOM   4640  CA  LEU B 250      32.854  48.917 -35.564  1.00 40.11           C  
ATOM   4641  C   LEU B 250      32.202  48.557 -34.247  1.00 39.90           C  
ATOM   4642  O   LEU B 250      31.739  47.437 -34.059  1.00 40.05           O  
ATOM   4643  CB  LEU B 250      34.359  48.789 -35.461  1.00 40.13           C  
ATOM   4644  CG  LEU B 250      34.945  47.945 -36.580  1.00 40.55           C  
ATOM   4645  CD1 LEU B 250      36.456  48.044 -36.542  1.00 41.84           C  
ATOM   4646  CD2 LEU B 250      34.486  46.508 -36.414  1.00 40.99           C  
ATOM   4647  N   LYS B 251      32.175  49.517 -33.332  1.00 39.67           N  
ATOM   4648  CA  LYS B 251      31.454  49.369 -32.084  1.00 39.46           C  
ATOM   4649  C   LYS B 251      30.014  49.033 -32.459  1.00 39.17           C  
ATOM   4650  O   LYS B 251      29.451  48.043 -31.980  1.00 39.07           O  
ATOM   4651  CB  LYS B 251      31.577  50.667 -31.284  1.00 39.50           C  
ATOM   4652  CG  LYS B 251      31.035  50.648 -29.878  1.00 39.68           C  
ATOM   4653  CD  LYS B 251      30.757  52.089 -29.369  1.00 41.25           C  
ATOM   4654  CE  LYS B 251      31.903  52.690 -28.546  1.00 40.77           C  
ATOM   4655  NZ  LYS B 251      33.145  52.829 -29.336  1.00 40.45           N  
ATOM   4656  N   GLY B 252      29.470  49.827 -33.381  1.00 39.08           N  
ATOM   4657  CA  GLY B 252      28.106  49.677 -33.894  1.00 39.42           C  
ATOM   4658  C   GLY B 252      27.759  48.350 -34.563  1.00 39.60           C  
ATOM   4659  O   GLY B 252      26.687  47.780 -34.304  1.00 39.68           O  
ATOM   4660  N   LEU B 253      28.653  47.872 -35.433  1.00 39.51           N  
ATOM   4661  CA  LEU B 253      28.523  46.569 -36.080  1.00 39.19           C  
ATOM   4662  C   LEU B 253      28.633  45.404 -35.074  1.00 39.85           C  
ATOM   4663  O   LEU B 253      27.816  44.463 -35.092  1.00 40.55           O  
ATOM   4664  CB  LEU B 253      29.579  46.428 -37.172  1.00 38.68           C  
ATOM   4665  CG  LEU B 253      29.813  45.028 -37.722  1.00 37.30           C  
ATOM   4666  CD1 LEU B 253      28.507  44.365 -38.106  1.00 34.61           C  
ATOM   4667  CD2 LEU B 253      30.729  45.127 -38.909  1.00 37.27           C  
ATOM   4668  N   CYS B 254      29.639  45.460 -34.207  1.00 39.59           N  
ATOM   4669  CA  CYS B 254      29.791  44.455 -33.176  1.00 39.35           C  
ATOM   4670  C   CYS B 254      28.512  44.268 -32.360  1.00 38.94           C  
ATOM   4671  O   CYS B 254      28.103  43.127 -32.137  1.00 39.05           O  
ATOM   4672  CB  CYS B 254      30.972  44.786 -32.278  1.00 39.66           C  
ATOM   4673  SG  CYS B 254      32.558  44.313 -32.997  1.00 41.15           S  
ATOM   4674  N   ARG B 255      27.878  45.369 -31.938  1.00 38.14           N  
ATOM   4675  CA  ARG B 255      26.573  45.292 -31.253  1.00 37.58           C  
ATOM   4676  C   ARG B 255      25.431  44.753 -32.142  1.00 37.05           C  
ATOM   4677  O   ARG B 255      24.506  44.111 -31.638  1.00 37.07           O  
ATOM   4678  CB  ARG B 255      26.182  46.634 -30.630  1.00 37.61           C  
ATOM   4679  CG  ARG B 255      26.810  46.884 -29.264  1.00 38.99           C  
ATOM   4680  CD  ARG B 255      26.870  48.373 -28.977  1.00 40.64           C  
ATOM   4681  NE  ARG B 255      27.626  48.704 -27.766  1.00 41.59           N  
ATOM   4682  CZ  ARG B 255      28.206  49.890 -27.538  1.00 42.26           C  
ATOM   4683  NH1 ARG B 255      28.138  50.867 -28.442  1.00 41.81           N  
ATOM   4684  NH2 ARG B 255      28.877  50.098 -26.410  1.00 42.15           N  
ATOM   4685  N   LEU B 256      25.492  45.002 -33.450  1.00 36.10           N  
ATOM   4686  CA  LEU B 256      24.520  44.425 -34.351  1.00 35.73           C  
ATOM   4687  C   LEU B 256      24.618  42.902 -34.266  1.00 36.07           C  
ATOM   4688  O   LEU B 256      23.601  42.219 -34.127  1.00 36.13           O  
ATOM   4689  CB  LEU B 256      24.728  44.904 -35.788  1.00 35.57           C  
ATOM   4690  CG  LEU B 256      23.825  44.274 -36.854  1.00 34.91           C  
ATOM   4691  CD1 LEU B 256      22.404  44.668 -36.584  1.00 35.22           C  
ATOM   4692  CD2 LEU B 256      24.213  44.665 -38.269  1.00 33.59           C  
ATOM   4693  N   LEU B 257      25.841  42.376 -34.310  1.00 35.82           N  
ATOM   4694  CA  LEU B 257      26.049  40.929 -34.209  1.00 35.71           C  
ATOM   4695  C   LEU B 257      26.003  40.398 -32.760  1.00 36.13           C  
ATOM   4696  O   LEU B 257      26.237  39.213 -32.524  1.00 36.05           O  
ATOM   4697  CB  LEU B 257      27.364  40.531 -34.888  1.00 35.33           C  
ATOM   4698  CG  LEU B 257      27.775  41.192 -36.207  1.00 34.33           C  
ATOM   4699  CD1 LEU B 257      29.228  40.917 -36.518  1.00 32.73           C  
ATOM   4700  CD2 LEU B 257      26.914  40.742 -37.355  1.00 33.93           C  
ATOM   4701  N   ARG B 258      25.693  41.280 -31.807  1.00 36.75           N  
ATOM   4702  CA  ARG B 258      25.600  40.974 -30.357  1.00 37.48           C  
ATOM   4703  C   ARG B 258      26.862  40.537 -29.626  1.00 37.66           C  
ATOM   4704  O   ARG B 258      26.781  39.781 -28.675  1.00 37.86           O  
ATOM   4705  CB  ARG B 258      24.488  39.979 -30.039  1.00 37.58           C  
ATOM   4706  CG  ARG B 258      23.143  40.546 -30.216  1.00 39.13           C  
ATOM   4707  CD  ARG B 258      22.126  39.895 -29.313  1.00 42.16           C  
ATOM   4708  NE  ARG B 258      20.793  40.299 -29.744  1.00 44.56           N  
ATOM   4709  CZ  ARG B 258      20.355  41.559 -29.760  1.00 45.22           C  
ATOM   4710  NH1 ARG B 258      21.143  42.556 -29.351  1.00 45.41           N  
ATOM   4711  NH2 ARG B 258      19.127  41.823 -30.198  1.00 45.15           N  
HETATM 4712  N   MSE B 259      28.013  41.034 -30.040  1.00 38.14           N  
HETATM 4713  CA  MSE B 259      29.247  40.815 -29.301  1.00 38.77           C  
HETATM 4714  C   MSE B 259      29.464  41.943 -28.286  1.00 39.75           C  
HETATM 4715  O   MSE B 259      29.215  43.113 -28.595  1.00 40.54           O  
HETATM 4716  CB  MSE B 259      30.380  40.787 -30.301  1.00 38.53           C  
HETATM 4717  CG  MSE B 259      29.989  40.016 -31.542  1.00 38.54           C  
HETATM 4718 SE   MSE B 259      31.193  40.247 -33.018  1.00 39.42          SE  
HETATM 4719  CE  MSE B 259      32.820  39.425 -32.281  1.00 38.52           C  
ATOM   4720  N   ASP B 260      29.918  41.626 -27.077  1.00 40.44           N  
ATOM   4721  CA  ASP B 260      30.151  42.690 -26.098  1.00 41.36           C  
ATOM   4722  C   ASP B 260      31.279  43.573 -26.579  1.00 41.79           C  
ATOM   4723  O   ASP B 260      32.237  43.090 -27.185  1.00 41.20           O  
ATOM   4724  CB  ASP B 260      30.503  42.160 -24.709  1.00 41.71           C  
ATOM   4725  CG  ASP B 260      29.756  40.902 -24.349  1.00 42.65           C  
ATOM   4726  OD1 ASP B 260      30.159  40.251 -23.362  1.00 44.39           O  
ATOM   4727  OD2 ASP B 260      28.787  40.546 -25.052  1.00 44.08           O  
ATOM   4728  N   VAL B 261      31.162  44.870 -26.294  1.00 42.75           N  
ATOM   4729  CA  VAL B 261      32.174  45.844 -26.707  1.00 43.44           C  
ATOM   4730  C   VAL B 261      32.826  46.522 -25.522  1.00 44.16           C  
ATOM   4731  O   VAL B 261      32.184  46.794 -24.509  1.00 43.87           O  
ATOM   4732  CB  VAL B 261      31.610  46.902 -27.659  1.00 43.18           C  
ATOM   4733  CG1 VAL B 261      31.099  46.247 -28.951  1.00 43.10           C  
ATOM   4734  CG2 VAL B 261      30.514  47.659 -26.974  1.00 43.52           C  
ATOM   4735  N   PHE B 262      34.119  46.765 -25.662  1.00 45.59           N  
ATOM   4736  CA  PHE B 262      34.909  47.411 -24.642  1.00 47.73           C  
ATOM   4737  C   PHE B 262      35.724  48.463 -25.376  1.00 49.78           C  
ATOM   4738  O   PHE B 262      36.243  48.178 -26.458  1.00 50.02           O  
ATOM   4739  CB  PHE B 262      35.817  46.382 -23.959  1.00 47.34           C  
ATOM   4740  CG  PHE B 262      35.068  45.221 -23.342  1.00 46.94           C  
ATOM   4741  CD1 PHE B 262      34.472  44.245 -24.144  1.00 45.54           C  
ATOM   4742  CD2 PHE B 262      34.956  45.103 -21.964  1.00 45.77           C  
ATOM   4743  CE1 PHE B 262      33.769  43.195 -23.586  1.00 43.97           C  
ATOM   4744  CE2 PHE B 262      34.264  44.047 -21.408  1.00 44.45           C  
ATOM   4745  CZ  PHE B 262      33.664  43.097 -22.224  1.00 44.60           C  
ATOM   4746  N   ASP B 263      35.831  49.678 -24.832  1.00 52.29           N  
ATOM   4747  CA  ASP B 263      36.587  50.710 -25.552  1.00 54.68           C  
ATOM   4748  C   ASP B 263      38.066  50.807 -25.124  1.00 55.94           C  
ATOM   4749  O   ASP B 263      38.956  50.522 -25.932  1.00 56.32           O  
ATOM   4750  CB  ASP B 263      35.860  52.074 -25.564  1.00 54.95           C  
ATOM   4751  CG  ASP B 263      35.987  52.811 -26.925  1.00 55.46           C  
ATOM   4752  OD1 ASP B 263      37.106  52.869 -27.484  1.00 55.89           O  
ATOM   4753  OD2 ASP B 263      34.972  53.346 -27.429  1.00 55.46           O  
ATOM   4754  N   VAL B 264      38.317  51.178 -23.867  1.00 57.60           N  
ATOM   4755  CA  VAL B 264      39.673  51.457 -23.372  1.00 59.41           C  
ATOM   4756  C   VAL B 264      40.376  52.539 -24.207  1.00 60.83           C  
ATOM   4757  O   VAL B 264      41.308  52.217 -24.942  1.00 60.77           O  
ATOM   4758  CB  VAL B 264      40.568  50.186 -23.403  1.00 59.35           C  
ATOM   4759  CG1 VAL B 264      41.783  50.347 -22.492  1.00 59.61           C  
ATOM   4760  CG2 VAL B 264      39.779  48.955 -23.013  1.00 59.85           C  
ATOM   4761  N   PRO B 265      39.928  53.817 -24.130  1.00 62.45           N  
ATOM   4762  CA  PRO B 265      40.658  54.851 -24.894  1.00 63.49           C  
ATOM   4763  C   PRO B 265      41.791  55.484 -24.060  1.00 64.60           C  
ATOM   4764  O   PRO B 265      42.175  54.908 -23.038  1.00 64.81           O  
ATOM   4765  CB  PRO B 265      39.559  55.873 -25.264  1.00 63.37           C  
ATOM   4766  CG  PRO B 265      38.256  55.363 -24.606  1.00 62.99           C  
ATOM   4767  CD  PRO B 265      38.684  54.364 -23.554  1.00 62.69           C  
ATOM   4768  N   GLY B 266      42.328  56.633 -24.492  1.00 65.81           N  
ATOM   4769  CA  GLY B 266      43.423  57.318 -23.761  1.00 67.12           C  
ATOM   4770  C   GLY B 266      43.296  58.834 -23.522  1.00 67.97           C  
ATOM   4771  O   GLY B 266      42.629  59.545 -24.299  1.00 68.14           O  
ATOM   4772  N   ALA B 267      43.942  59.316 -22.443  1.00 68.42           N  
ATOM   4773  CA  ALA B 267      44.043  60.759 -22.098  1.00 68.71           C  
ATOM   4774  C   ALA B 267      45.497  61.282 -22.100  1.00 68.70           C  
ATOM   4775  O   ALA B 267      46.142  61.409 -23.156  1.00 68.56           O  
ATOM   4776  CB  ALA B 267      43.362  61.053 -20.734  1.00 68.69           C  
ATOM   4777  N   SER B 273      49.396  56.649 -28.035  1.00 45.96           N  
ATOM   4778  CA  SER B 273      48.069  56.027 -27.943  1.00 45.83           C  
ATOM   4779  C   SER B 273      48.090  54.725 -27.131  1.00 45.35           C  
ATOM   4780  O   SER B 273      49.169  54.152 -26.871  1.00 45.48           O  
ATOM   4781  CB  SER B 273      47.458  55.783 -29.340  1.00 46.18           C  
ATOM   4782  OG  SER B 273      46.128  55.265 -29.251  1.00 46.13           O  
ATOM   4783  N   ASN B 274      46.886  54.271 -26.762  1.00 44.22           N  
ATOM   4784  CA  ASN B 274      46.699  53.153 -25.841  1.00 42.96           C  
ATOM   4785  C   ASN B 274      46.584  51.778 -26.507  1.00 41.14           C  
ATOM   4786  O   ASN B 274      45.531  51.149 -26.503  1.00 40.65           O  
ATOM   4787  CB  ASN B 274      45.502  53.422 -24.922  1.00 43.62           C  
ATOM   4788  CG  ASN B 274      45.505  52.526 -23.674  1.00 46.06           C  
ATOM   4789  OD1 ASN B 274      46.572  52.100 -23.184  1.00 48.18           O  
ATOM   4790  ND2 ASN B 274      44.308  52.229 -23.159  1.00 47.35           N  
ATOM   4791  N   TYR B 275      47.696  51.314 -27.058  1.00 39.27           N  
ATOM   4792  CA  TYR B 275      47.762  50.002 -27.667  1.00 37.31           C  
ATOM   4793  C   TYR B 275      47.858  48.908 -26.622  1.00 36.13           C  
ATOM   4794  O   TYR B 275      47.091  47.951 -26.670  1.00 35.37           O  
ATOM   4795  CB  TYR B 275      48.931  49.944 -28.626  1.00 37.22           C  
ATOM   4796  CG  TYR B 275      48.802  50.930 -29.749  1.00 36.47           C  
ATOM   4797  CD1 TYR B 275      49.865  51.750 -30.100  1.00 36.75           C  
ATOM   4798  CD2 TYR B 275      47.613  51.059 -30.450  1.00 36.44           C  
ATOM   4799  CE1 TYR B 275      49.757  52.669 -31.134  1.00 35.51           C  
ATOM   4800  CE2 TYR B 275      47.491  51.967 -31.490  1.00 36.84           C  
ATOM   4801  CZ  TYR B 275      48.575  52.768 -31.823  1.00 36.27           C  
ATOM   4802  OH  TYR B 275      48.463  53.675 -32.850  1.00 38.19           O  
ATOM   4803  N   ARG B 276      48.789  49.080 -25.678  1.00 35.15           N  
ATOM   4804  CA  ARG B 276      48.940  48.228 -24.479  1.00 34.38           C  
ATOM   4805  C   ARG B 276      47.637  47.813 -23.816  1.00 33.38           C  
ATOM   4806  O   ARG B 276      47.389  46.633 -23.597  1.00 33.27           O  
ATOM   4807  CB  ARG B 276      49.806  48.913 -23.427  1.00 34.44           C  
ATOM   4808  CG  ARG B 276      51.169  48.308 -23.310  1.00 36.58           C  
ATOM   4809  CD  ARG B 276      52.054  48.999 -22.261  1.00 40.56           C  
ATOM   4810  NE  ARG B 276      53.414  49.216 -22.786  1.00 43.29           N  
ATOM   4811  CZ  ARG B 276      54.323  48.259 -23.011  1.00 43.50           C  
ATOM   4812  NH1 ARG B 276      54.060  46.971 -22.748  1.00 42.92           N  
ATOM   4813  NH2 ARG B 276      55.507  48.601 -23.509  1.00 43.50           N  
ATOM   4814  N   GLY B 277      46.819  48.796 -23.493  1.00 32.26           N  
ATOM   4815  CA  GLY B 277      45.545  48.539 -22.873  1.00 31.65           C  
ATOM   4816  C   GLY B 277      44.607  47.705 -23.722  1.00 31.08           C  
ATOM   4817  O   GLY B 277      43.968  46.775 -23.206  1.00 31.50           O  
ATOM   4818  N   LYS B 278      44.518  48.021 -25.012  1.00 30.24           N  
ATOM   4819  CA  LYS B 278      43.685  47.235 -25.913  1.00 29.74           C  
ATOM   4820  C   LYS B 278      44.190  45.776 -26.024  1.00 29.42           C  
ATOM   4821  O   LYS B 278      43.410  44.832 -26.048  1.00 28.71           O  
ATOM   4822  CB  LYS B 278      43.580  47.895 -27.284  1.00 30.00           C  
ATOM   4823  CG  LYS B 278      43.080  49.357 -27.294  1.00 31.30           C  
ATOM   4824  CD  LYS B 278      42.199  49.602 -28.518  1.00 33.69           C  
ATOM   4825  CE  LYS B 278      42.373  50.986 -29.099  1.00 34.69           C  
ATOM   4826  NZ  LYS B 278      42.034  50.949 -30.564  1.00 35.25           N  
ATOM   4827  N   ILE B 279      45.497  45.578 -26.045  1.00 29.19           N  
ATOM   4828  CA  ILE B 279      45.963  44.226 -26.096  1.00 29.39           C  
ATOM   4829  C   ILE B 279      45.751  43.535 -24.757  1.00 29.89           C  
ATOM   4830  O   ILE B 279      45.372  42.363 -24.717  1.00 30.25           O  
ATOM   4831  CB  ILE B 279      47.423  44.112 -26.579  1.00 29.47           C  
ATOM   4832  CG1 ILE B 279      47.545  44.549 -28.038  1.00 28.57           C  
ATOM   4833  CG2 ILE B 279      47.914  42.674 -26.494  1.00 29.19           C  
ATOM   4834  CD1 ILE B 279      46.539  43.921 -28.959  1.00 28.72           C  
ATOM   4835  N   GLU B 280      45.974  44.242 -23.658  1.00 30.13           N  
ATOM   4836  CA  GLU B 280      45.936  43.581 -22.365  1.00 30.43           C  
ATOM   4837  C   GLU B 280      44.535  43.187 -22.016  1.00 30.40           C  
ATOM   4838  O   GLU B 280      44.315  42.104 -21.446  1.00 30.43           O  
ATOM   4839  CB  GLU B 280      46.507  44.461 -21.286  1.00 30.66           C  
ATOM   4840  CG  GLU B 280      47.968  44.201 -21.024  1.00 33.25           C  
ATOM   4841  CD  GLU B 280      48.550  45.206 -20.037  1.00 37.47           C  
ATOM   4842  OE1 GLU B 280      49.799  45.363 -19.993  1.00 39.54           O  
ATOM   4843  OE2 GLU B 280      47.755  45.860 -19.320  1.00 37.18           O  
ATOM   4844  N   LYS B 281      43.603  44.073 -22.368  1.00 30.19           N  
ATOM   4845  CA  LYS B 281      42.177  43.836 -22.206  1.00 30.53           C  
ATOM   4846  C   LYS B 281      41.686  42.673 -23.061  1.00 30.53           C  
ATOM   4847  O   LYS B 281      40.819  41.912 -22.645  1.00 30.38           O  
ATOM   4848  CB  LYS B 281      41.402  45.076 -22.610  1.00 30.54           C  
ATOM   4849  CG  LYS B 281      39.897  44.906 -22.578  1.00 31.98           C  
ATOM   4850  CD  LYS B 281      39.298  45.397 -21.238  1.00 33.04           C  
ATOM   4851  CE  LYS B 281      38.851  44.256 -20.349  1.00 33.44           C  
ATOM   4852  NZ  LYS B 281      37.610  44.607 -19.574  1.00 34.44           N  
ATOM   4853  N   ALA B 282      42.221  42.566 -24.275  1.00 30.87           N  
ATOM   4854  CA  ALA B 282      41.789  41.550 -25.205  1.00 30.82           C  
ATOM   4855  C   ALA B 282      42.264  40.212 -24.680  1.00 31.38           C  
ATOM   4856  O   ALA B 282      41.565  39.211 -24.816  1.00 31.31           O  
ATOM   4857  CB  ALA B 282      42.326  41.824 -26.575  1.00 30.73           C  
ATOM   4858  N   VAL B 283      43.439  40.205 -24.053  1.00 31.90           N  
ATOM   4859  CA  VAL B 283      43.919  39.020 -23.342  1.00 32.59           C  
ATOM   4860  C   VAL B 283      43.027  38.680 -22.137  1.00 33.66           C  
ATOM   4861  O   VAL B 283      42.758  37.510 -21.895  1.00 34.27           O  
ATOM   4862  CB  VAL B 283      45.417  39.127 -22.939  1.00 32.05           C  
ATOM   4863  CG1 VAL B 283      45.802  38.019 -22.020  1.00 30.98           C  
ATOM   4864  CG2 VAL B 283      46.288  39.052 -24.170  1.00 32.17           C  
ATOM   4865  N   ASP B 284      42.559  39.680 -21.392  1.00 34.73           N  
ATOM   4866  CA  ASP B 284      41.677  39.403 -20.249  1.00 36.12           C  
ATOM   4867  C   ASP B 284      40.405  38.673 -20.648  1.00 35.88           C  
ATOM   4868  O   ASP B 284      40.008  37.688 -20.004  1.00 35.85           O  
ATOM   4869  CB  ASP B 284      41.293  40.679 -19.500  1.00 36.96           C  
ATOM   4870  CG  ASP B 284      42.253  40.999 -18.363  1.00 40.96           C  
ATOM   4871  OD1 ASP B 284      42.677  42.183 -18.266  1.00 45.38           O  
ATOM   4872  OD2 ASP B 284      42.589  40.073 -17.571  1.00 43.89           O  
ATOM   4873  N   LEU B 285      39.777  39.163 -21.708  1.00 35.44           N  
ATOM   4874  CA  LEU B 285      38.523  38.622 -22.170  1.00 35.55           C  
ATOM   4875  C   LEU B 285      38.648  37.176 -22.677  1.00 35.88           C  
ATOM   4876  O   LEU B 285      37.649  36.479 -22.865  1.00 36.13           O  
ATOM   4877  CB  LEU B 285      37.970  39.521 -23.252  1.00 35.48           C  
ATOM   4878  CG  LEU B 285      37.871  41.004 -22.913  1.00 35.81           C  
ATOM   4879  CD1 LEU B 285      37.717  41.793 -24.210  1.00 35.72           C  
ATOM   4880  CD2 LEU B 285      36.729  41.296 -21.946  1.00 34.85           C  
ATOM   4881  N   THR B 286      39.883  36.727 -22.880  1.00 36.12           N  
ATOM   4882  CA  THR B 286      40.188  35.335 -23.194  1.00 35.89           C  
ATOM   4883  C   THR B 286      39.671  34.391 -22.132  1.00 36.08           C  
ATOM   4884  O   THR B 286      39.260  33.278 -22.452  1.00 36.52           O  
ATOM   4885  CB  THR B 286      41.676  35.162 -23.365  1.00 35.60           C  
ATOM   4886  OG1 THR B 286      41.943  35.219 -24.759  1.00 36.48           O  
ATOM   4887  CG2 THR B 286      42.188  33.843 -22.794  1.00 35.59           C  
ATOM   4888  N   SER B 287      39.683  34.853 -20.881  1.00 35.95           N  
ATOM   4889  CA  SER B 287      39.111  34.120 -19.755  1.00 35.58           C  
ATOM   4890  C   SER B 287      37.618  33.844 -19.923  1.00 34.88           C  
ATOM   4891  O   SER B 287      37.178  32.729 -19.644  1.00 35.11           O  
ATOM   4892  CB  SER B 287      39.371  34.870 -18.432  1.00 36.06           C  
ATOM   4893  OG  SER B 287      38.610  34.327 -17.357  1.00 36.93           O  
ATOM   4894  N   SER B 288      36.854  34.837 -20.383  1.00 33.75           N  
ATOM   4895  CA  SER B 288      35.388  34.738 -20.391  1.00 32.93           C  
ATOM   4896  C   SER B 288      34.733  34.670 -21.773  1.00 32.32           C  
ATOM   4897  O   SER B 288      33.512  34.545 -21.867  1.00 32.24           O  
ATOM   4898  CB  SER B 288      34.788  35.911 -19.624  1.00 33.25           C  
ATOM   4899  OG  SER B 288      35.099  37.141 -20.269  1.00 33.54           O  
ATOM   4900  N   HIS B 289      35.533  34.774 -22.836  1.00 31.56           N  
ATOM   4901  CA  HIS B 289      35.018  34.747 -24.214  1.00 30.80           C  
ATOM   4902  C   HIS B 289      35.824  33.824 -25.143  1.00 30.32           C  
ATOM   4903  O   HIS B 289      37.025  33.624 -24.957  1.00 29.90           O  
ATOM   4904  CB  HIS B 289      34.999  36.160 -24.806  1.00 30.59           C  
ATOM   4905  CG  HIS B 289      34.068  37.112 -24.115  1.00 31.25           C  
ATOM   4906  ND1 HIS B 289      34.392  37.752 -22.936  1.00 31.61           N  
ATOM   4907  CD2 HIS B 289      32.834  37.560 -24.456  1.00 31.79           C  
ATOM   4908  CE1 HIS B 289      33.395  38.546 -22.579  1.00 32.91           C  
ATOM   4909  NE2 HIS B 289      32.434  38.441 -23.480  1.00 32.11           N  
ATOM   4910  N   ASP B 290      35.168  33.283 -26.161  1.00 29.78           N  
ATOM   4911  CA  ASP B 290      35.856  32.403 -27.109  1.00 29.50           C  
ATOM   4912  C   ASP B 290      36.642  33.112 -28.215  1.00 28.35           C  
ATOM   4913  O   ASP B 290      37.548  32.519 -28.809  1.00 27.89           O  
ATOM   4914  CB  ASP B 290      34.851  31.477 -27.772  1.00 30.18           C  
ATOM   4915  CG  ASP B 290      34.200  30.538 -26.799  1.00 33.05           C  
ATOM   4916  OD1 ASP B 290      32.953  30.608 -26.641  1.00 35.44           O  
ATOM   4917  OD2 ASP B 290      34.944  29.722 -26.202  1.00 37.53           O  
ATOM   4918  N   PHE B 291      36.268  34.356 -28.503  1.00 27.12           N  
ATOM   4919  CA  PHE B 291      36.737  35.070 -29.680  1.00 26.23           C  
ATOM   4920  C   PHE B 291      36.740  36.553 -29.419  1.00 25.72           C  
ATOM   4921  O   PHE B 291      35.716  37.142 -29.098  1.00 25.53           O  
ATOM   4922  CB  PHE B 291      35.827  34.799 -30.874  1.00 26.28           C  
ATOM   4923  CG  PHE B 291      36.246  35.507 -32.135  1.00 27.07           C  
ATOM   4924  CD1 PHE B 291      37.043  34.860 -33.076  1.00 27.78           C  
ATOM   4925  CD2 PHE B 291      35.839  36.813 -32.383  1.00 27.68           C  
ATOM   4926  CE1 PHE B 291      37.433  35.505 -34.237  1.00 28.47           C  
ATOM   4927  CE2 PHE B 291      36.227  37.477 -33.534  1.00 27.87           C  
ATOM   4928  CZ  PHE B 291      37.028  36.821 -34.471  1.00 28.99           C  
ATOM   4929  N   VAL B 292      37.895  37.160 -29.600  1.00 25.18           N  
ATOM   4930  CA  VAL B 292      38.072  38.557 -29.317  1.00 24.52           C  
ATOM   4931  C   VAL B 292      38.715  39.226 -30.517  1.00 24.91           C  
ATOM   4932  O   VAL B 292      39.869  38.963 -30.837  1.00 25.19           O  
ATOM   4933  CB  VAL B 292      38.946  38.726 -28.074  1.00 24.23           C  
ATOM   4934  CG1 VAL B 292      39.590  40.088 -28.034  1.00 23.60           C  
ATOM   4935  CG2 VAL B 292      38.118  38.486 -26.827  1.00 24.01           C  
ATOM   4936  N   LEU B 293      37.953  40.067 -31.201  1.00 25.22           N  
ATOM   4937  CA  LEU B 293      38.496  40.933 -32.223  1.00 25.54           C  
ATOM   4938  C   LEU B 293      38.985  42.234 -31.581  1.00 26.00           C  
ATOM   4939  O   LEU B 293      38.226  42.900 -30.871  1.00 25.92           O  
ATOM   4940  CB  LEU B 293      37.406  41.235 -33.246  1.00 25.77           C  
ATOM   4941  CG  LEU B 293      37.677  42.372 -34.233  1.00 25.90           C  
ATOM   4942  CD1 LEU B 293      38.530  41.857 -35.359  1.00 24.05           C  
ATOM   4943  CD2 LEU B 293      36.358  42.886 -34.752  1.00 25.49           C  
ATOM   4944  N   VAL B 294      40.241  42.593 -31.808  1.00 26.45           N  
ATOM   4945  CA  VAL B 294      40.744  43.874 -31.316  1.00 27.47           C  
ATOM   4946  C   VAL B 294      41.281  44.664 -32.480  1.00 28.29           C  
ATOM   4947  O   VAL B 294      42.156  44.200 -33.214  1.00 28.87           O  
ATOM   4948  CB  VAL B 294      41.806  43.737 -30.191  1.00 27.54           C  
ATOM   4949  CG1 VAL B 294      42.506  42.400 -30.260  1.00 27.61           C  
ATOM   4950  CG2 VAL B 294      42.812  44.902 -30.234  1.00 26.93           C  
ATOM   4951  N   ASN B 295      40.738  45.856 -32.662  1.00 29.02           N  
ATOM   4952  CA  ASN B 295      41.032  46.608 -33.856  1.00 29.97           C  
ATOM   4953  C   ASN B 295      41.929  47.755 -33.556  1.00 30.51           C  
ATOM   4954  O   ASN B 295      41.633  48.540 -32.678  1.00 30.44           O  
ATOM   4955  CB  ASN B 295      39.756  47.117 -34.501  1.00 30.07           C  
ATOM   4956  CG  ASN B 295      40.012  47.691 -35.861  1.00 30.09           C  
ATOM   4957  OD1 ASN B 295      40.577  47.016 -36.723  1.00 28.95           O  
ATOM   4958  ND2 ASN B 295      39.634  48.957 -36.061  1.00 30.05           N  
ATOM   4959  N   ILE B 296      43.007  47.874 -34.309  1.00 31.95           N  
ATOM   4960  CA  ILE B 296      44.047  48.785 -33.920  1.00 34.15           C  
ATOM   4961  C   ILE B 296      43.820  50.282 -34.182  1.00 35.93           C  
ATOM   4962  O   ILE B 296      43.336  50.960 -33.243  1.00 37.48           O  
ATOM   4963  CB  ILE B 296      45.436  48.304 -34.298  1.00 34.24           C  
ATOM   4964  CG1 ILE B 296      46.361  48.514 -33.105  1.00 34.30           C  
ATOM   4965  CG2 ILE B 296      45.932  48.986 -35.567  1.00 35.29           C  
ATOM   4966  CD1 ILE B 296      45.897  47.745 -31.849  1.00 33.82           C  
ATOM   4967  N   LYS B 297      44.169  50.838 -35.357  1.00 36.50           N  
ATOM   4968  CA  LYS B 297      44.081  52.314 -35.486  1.00 37.54           C  
ATOM   4969  C   LYS B 297      43.551  52.908 -36.797  1.00 39.02           C  
ATOM   4970  O   LYS B 297      42.320  52.982 -36.985  1.00 39.09           O  
ATOM   4971  CB  LYS B 297      45.364  53.048 -35.001  1.00 37.21           C  
ATOM   4972  CG  LYS B 297      46.742  52.502 -35.452  1.00 36.18           C  
ATOM   4973  CD  LYS B 297      46.971  52.460 -36.972  1.00 34.02           C  
ATOM   4974  CE  LYS B 297      48.455  52.640 -37.352  1.00 33.97           C  
ATOM   4975  NZ  LYS B 297      49.133  51.502 -38.050  1.00 30.88           N  
ATOM   4976  N   ALA B 298      44.501  53.319 -37.662  1.00 40.44           N  
ATOM   4977  CA  ALA B 298      44.357  54.134 -38.915  1.00 41.46           C  
ATOM   4978  C   ALA B 298      44.774  55.614 -38.746  1.00 42.01           C  
ATOM   4979  O   ALA B 298      45.958  55.921 -38.518  1.00 42.70           O  
ATOM   4980  CB  ALA B 298      42.949  53.998 -39.603  1.00 41.49           C  
ATOM   4981  N   ASN B 307      53.576  60.833 -43.223  1.00 42.96           N  
ATOM   4982  CA  ASN B 307      55.008  60.914 -42.940  1.00 43.02           C  
ATOM   4983  C   ASN B 307      55.567  59.538 -42.555  1.00 42.65           C  
ATOM   4984  O   ASN B 307      55.069  58.890 -41.627  1.00 42.46           O  
ATOM   4985  CB  ASN B 307      55.284  61.973 -41.844  1.00 43.33           C  
ATOM   4986  CG  ASN B 307      56.753  61.982 -41.354  1.00 43.48           C  
ATOM   4987  OD1 ASN B 307      57.230  61.017 -40.751  1.00 43.64           O  
ATOM   4988  ND2 ASN B 307      57.450  63.094 -41.584  1.00 43.24           N  
ATOM   4989  N   TYR B 308      56.615  59.108 -43.250  1.00 42.15           N  
ATOM   4990  CA  TYR B 308      57.091  57.728 -43.107  1.00 41.64           C  
ATOM   4991  C   TYR B 308      57.744  57.348 -41.778  1.00 40.16           C  
ATOM   4992  O   TYR B 308      57.276  56.423 -41.130  1.00 40.00           O  
ATOM   4993  CB  TYR B 308      57.895  57.273 -44.332  1.00 42.39           C  
ATOM   4994  CG  TYR B 308      57.011  56.606 -45.377  1.00 45.37           C  
ATOM   4995  CD1 TYR B 308      55.773  57.161 -45.737  1.00 48.04           C  
ATOM   4996  CD2 TYR B 308      57.404  55.416 -46.004  1.00 47.79           C  
ATOM   4997  CE1 TYR B 308      54.951  56.541 -46.695  1.00 49.79           C  
ATOM   4998  CE2 TYR B 308      56.587  54.792 -46.964  1.00 48.62           C  
ATOM   4999  CZ  TYR B 308      55.365  55.359 -47.299  1.00 48.98           C  
ATOM   5000  OH  TYR B 308      54.555  54.760 -48.231  1.00 48.81           O  
ATOM   5001  N   PRO B 309      58.794  58.067 -41.350  1.00 39.19           N  
ATOM   5002  CA  PRO B 309      59.368  57.816 -40.015  1.00 38.38           C  
ATOM   5003  C   PRO B 309      58.344  57.654 -38.884  1.00 37.41           C  
ATOM   5004  O   PRO B 309      58.488  56.769 -38.042  1.00 37.18           O  
ATOM   5005  CB  PRO B 309      60.217  59.058 -39.776  1.00 38.43           C  
ATOM   5006  CG  PRO B 309      60.676  59.425 -41.143  1.00 38.55           C  
ATOM   5007  CD  PRO B 309      59.527  59.135 -42.057  1.00 39.00           C  
ATOM   5008  N   LEU B 310      57.317  58.495 -38.879  1.00 36.58           N  
ATOM   5009  CA  LEU B 310      56.238  58.381 -37.912  1.00 35.76           C  
ATOM   5010  C   LEU B 310      55.439  57.093 -38.037  1.00 35.00           C  
ATOM   5011  O   LEU B 310      55.221  56.413 -37.038  1.00 35.19           O  
ATOM   5012  CB  LEU B 310      55.319  59.600 -37.980  1.00 35.78           C  
ATOM   5013  CG  LEU B 310      55.406  60.562 -36.780  1.00 36.79           C  
ATOM   5014  CD1 LEU B 310      56.805  61.248 -36.572  1.00 34.40           C  
ATOM   5015  CD2 LEU B 310      54.261  61.588 -36.857  1.00 37.24           C  
ATOM   5016  N   LYS B 311      55.020  56.750 -39.254  1.00 34.17           N  
ATOM   5017  CA  LYS B 311      54.288  55.499 -39.499  1.00 33.24           C  
ATOM   5018  C   LYS B 311      55.060  54.299 -38.965  1.00 32.02           C  
ATOM   5019  O   LYS B 311      54.463  53.363 -38.431  1.00 31.60           O  
ATOM   5020  CB  LYS B 311      54.003  55.302 -40.983  1.00 33.48           C  
ATOM   5021  CG  LYS B 311      52.994  56.284 -41.567  1.00 35.25           C  
ATOM   5022  CD  LYS B 311      52.098  55.595 -42.603  1.00 39.58           C  
ATOM   5023  CE  LYS B 311      51.536  56.572 -43.643  1.00 41.60           C  
ATOM   5024  NZ  LYS B 311      52.433  56.690 -44.831  1.00 41.59           N  
ATOM   5025  N   ARG B 312      56.385  54.367 -39.109  1.00 30.52           N  
ATOM   5026  CA  ARG B 312      57.328  53.392 -38.598  1.00 29.14           C  
ATOM   5027  C   ARG B 312      57.245  53.310 -37.092  1.00 29.07           C  
ATOM   5028  O   ARG B 312      56.944  52.249 -36.547  1.00 29.23           O  
ATOM   5029  CB  ARG B 312      58.740  53.802 -38.977  1.00 28.93           C  
ATOM   5030  CG  ARG B 312      59.740  52.677 -39.066  1.00 28.31           C  
ATOM   5031  CD  ARG B 312      61.036  52.912 -38.257  1.00 27.87           C  
ATOM   5032  NE  ARG B 312      61.187  54.270 -37.716  1.00 28.23           N  
ATOM   5033  CZ  ARG B 312      61.977  55.216 -38.220  1.00 26.64           C  
ATOM   5034  NH1 ARG B 312      62.715  54.981 -39.295  1.00 25.98           N  
ATOM   5035  NH2 ARG B 312      62.033  56.402 -37.637  1.00 26.50           N  
ATOM   5036  N   ASP B 313      57.505  54.431 -36.415  1.00 28.77           N  
ATOM   5037  CA  ASP B 313      57.542  54.465 -34.934  1.00 28.31           C  
ATOM   5038  C   ASP B 313      56.211  54.009 -34.295  1.00 27.74           C  
ATOM   5039  O   ASP B 313      56.200  53.349 -33.239  1.00 27.12           O  
ATOM   5040  CB  ASP B 313      58.012  55.844 -34.402  1.00 28.34           C  
ATOM   5041  CG  ASP B 313      59.461  56.226 -34.864  1.00 29.78           C  
ATOM   5042  OD1 ASP B 313      60.287  55.340 -35.229  1.00 31.02           O  
ATOM   5043  OD2 ASP B 313      59.782  57.440 -34.869  1.00 30.71           O  
ATOM   5044  N   VAL B 314      55.101  54.336 -34.963  1.00 27.36           N  
ATOM   5045  CA  VAL B 314      53.778  53.842 -34.576  1.00 26.98           C  
ATOM   5046  C   VAL B 314      53.732  52.310 -34.601  1.00 27.23           C  
ATOM   5047  O   VAL B 314      53.217  51.692 -33.672  1.00 27.68           O  
ATOM   5048  CB  VAL B 314      52.678  54.402 -35.474  1.00 26.71           C  
ATOM   5049  CG1 VAL B 314      51.380  53.680 -35.220  1.00 26.56           C  
ATOM   5050  CG2 VAL B 314      52.506  55.885 -35.246  1.00 26.78           C  
ATOM   5051  N   ILE B 315      54.286  51.691 -35.647  1.00 26.93           N  
ATOM   5052  CA  ILE B 315      54.389  50.236 -35.663  1.00 26.18           C  
ATOM   5053  C   ILE B 315      55.251  49.768 -34.500  1.00 26.16           C  
ATOM   5054  O   ILE B 315      54.836  48.880 -33.776  1.00 26.33           O  
ATOM   5055  CB  ILE B 315      54.838  49.657 -37.026  1.00 25.91           C  
ATOM   5056  CG1 ILE B 315      53.714  49.828 -38.041  1.00 25.65           C  
ATOM   5057  CG2 ILE B 315      55.075  48.178 -36.910  1.00 24.85           C  
ATOM   5058  CD1 ILE B 315      54.147  49.745 -39.488  1.00 26.45           C  
ATOM   5059  N   GLU B 316      56.407  50.397 -34.287  1.00 26.39           N  
ATOM   5060  CA  GLU B 316      57.313  50.025 -33.179  1.00 26.93           C  
ATOM   5061  C   GLU B 316      56.625  50.078 -31.819  1.00 27.18           C  
ATOM   5062  O   GLU B 316      56.898  49.237 -30.958  1.00 27.21           O  
ATOM   5063  CB  GLU B 316      58.583  50.875 -33.158  1.00 26.70           C  
ATOM   5064  CG  GLU B 316      59.333  50.917 -34.480  1.00 28.50           C  
ATOM   5065  CD  GLU B 316      60.802  51.342 -34.348  1.00 31.37           C  
ATOM   5066  OE1 GLU B 316      61.573  51.079 -35.307  1.00 31.33           O  
ATOM   5067  OE2 GLU B 316      61.187  51.932 -33.302  1.00 31.62           O  
ATOM   5068  N   ASP B 317      55.746  51.069 -31.641  1.00 27.72           N  
ATOM   5069  CA  ASP B 317      54.820  51.133 -30.498  1.00 28.33           C  
ATOM   5070  C   ASP B 317      53.913  49.912 -30.476  1.00 27.98           C  
ATOM   5071  O   ASP B 317      53.920  49.139 -29.510  1.00 28.27           O  
ATOM   5072  CB  ASP B 317      53.956  52.420 -30.533  1.00 28.91           C  
ATOM   5073  CG  ASP B 317      53.430  52.837 -29.142  1.00 29.97           C  
ATOM   5074  OD1 ASP B 317      52.237  53.200 -29.033  1.00 32.36           O  
ATOM   5075  OD2 ASP B 317      54.204  52.812 -28.153  1.00 31.27           O  
ATOM   5076  N   ILE B 318      53.144  49.736 -31.547  1.00 27.45           N  
ATOM   5077  CA  ILE B 318      52.229  48.614 -31.635  1.00 27.05           C  
ATOM   5078  C   ILE B 318      52.932  47.293 -31.256  1.00 27.47           C  
ATOM   5079  O   ILE B 318      52.385  46.484 -30.514  1.00 27.26           O  
ATOM   5080  CB  ILE B 318      51.548  48.550 -33.009  1.00 26.67           C  
ATOM   5081  CG1 ILE B 318      50.694  49.799 -33.238  1.00 25.74           C  
ATOM   5082  CG2 ILE B 318      50.657  47.331 -33.108  1.00 26.55           C  
ATOM   5083  CD1 ILE B 318      50.221  49.982 -34.662  1.00 23.14           C  
ATOM   5084  N   ASP B 319      54.158  47.097 -31.728  1.00 28.20           N  
ATOM   5085  CA  ASP B 319      54.865  45.855 -31.470  1.00 29.03           C  
ATOM   5086  C   ASP B 319      55.171  45.674 -29.988  1.00 29.51           C  
ATOM   5087  O   ASP B 319      55.162  44.554 -29.487  1.00 29.44           O  
ATOM   5088  CB  ASP B 319      56.155  45.763 -32.277  1.00 29.05           C  
ATOM   5089  CG  ASP B 319      56.815  44.379 -32.167  1.00 31.46           C  
ATOM   5090  OD1 ASP B 319      57.731  44.187 -31.319  1.00 33.91           O  
ATOM   5091  OD2 ASP B 319      56.406  43.469 -32.925  1.00 33.42           O  
ATOM   5092  N   ARG B 320      55.457  46.766 -29.285  1.00 30.33           N  
ATOM   5093  CA  ARG B 320      55.810  46.666 -27.868  1.00 30.95           C  
ATOM   5094  C   ARG B 320      54.598  46.261 -27.053  1.00 31.12           C  
ATOM   5095  O   ARG B 320      54.722  45.572 -26.036  1.00 31.20           O  
ATOM   5096  CB  ARG B 320      56.400  47.973 -27.343  1.00 31.08           C  
ATOM   5097  CG  ARG B 320      57.906  47.938 -27.057  1.00 31.64           C  
ATOM   5098  CD  ARG B 320      58.575  49.243 -27.475  1.00 32.03           C  
ATOM   5099  NE  ARG B 320      57.624  50.369 -27.525  1.00 32.22           N  
ATOM   5100  CZ  ARG B 320      57.803  51.481 -28.246  1.00 31.46           C  
ATOM   5101  NH1 ARG B 320      58.910  51.640 -28.978  1.00 30.05           N  
ATOM   5102  NH2 ARG B 320      56.880  52.440 -28.234  1.00 29.65           N  
ATOM   5103  N   ALA B 321      53.428  46.669 -27.530  1.00 31.29           N  
ATOM   5104  CA  ALA B 321      52.183  46.373 -26.852  1.00 31.68           C  
ATOM   5105  C   ALA B 321      51.766  44.938 -27.057  1.00 31.89           C  
ATOM   5106  O   ALA B 321      50.718  44.515 -26.604  1.00 31.89           O  
ATOM   5107  CB  ALA B 321      51.107  47.296 -27.350  1.00 32.02           C  
HETATM 5108  N   MSE B 322      52.604  44.184 -27.734  1.00 32.63           N  
HETATM 5109  CA  MSE B 322      52.226  42.871 -28.184  1.00 33.62           C  
HETATM 5110  C   MSE B 322      52.946  41.769 -27.409  1.00 33.69           C  
HETATM 5111  O   MSE B 322      52.812  40.597 -27.738  1.00 33.87           O  
HETATM 5112  CB  MSE B 322      52.551  42.785 -29.655  1.00 33.94           C  
HETATM 5113  CG  MSE B 322      51.629  41.958 -30.449  1.00 36.74           C  
HETATM 5114 SE   MSE B 322      51.004  43.070 -31.896  1.00 45.18          SE  
HETATM 5115  CE  MSE B 322      49.115  43.171 -31.377  1.00 38.03           C  
ATOM   5116  N   GLU B 323      53.696  42.156 -26.376  1.00 33.72           N  
ATOM   5117  CA  GLU B 323      54.505  41.230 -25.571  1.00 33.88           C  
ATOM   5118  C   GLU B 323      53.650  40.178 -24.837  1.00 33.05           C  
ATOM   5119  O   GLU B 323      54.020  38.999 -24.804  1.00 32.89           O  
ATOM   5120  CB  GLU B 323      55.420  42.024 -24.623  1.00 34.39           C  
ATOM   5121  CG  GLU B 323      56.308  41.229 -23.671  1.00 37.22           C  
ATOM   5122  CD  GLU B 323      57.061  42.152 -22.683  1.00 43.39           C  
ATOM   5123  OE1 GLU B 323      58.196  41.796 -22.276  1.00 44.67           O  
ATOM   5124  OE2 GLU B 323      56.531  43.245 -22.308  1.00 44.60           O  
ATOM   5125  N   PRO B 324      52.493  40.586 -24.279  1.00 32.39           N  
ATOM   5126  CA  PRO B 324      51.553  39.628 -23.718  1.00 31.76           C  
ATOM   5127  C   PRO B 324      51.376  38.401 -24.596  1.00 31.51           C  
ATOM   5128  O   PRO B 324      51.491  37.281 -24.096  1.00 32.33           O  
ATOM   5129  CB  PRO B 324      50.237  40.404 -23.674  1.00 31.39           C  
ATOM   5130  CG  PRO B 324      50.551  41.780 -24.134  1.00 31.91           C  
ATOM   5131  CD  PRO B 324      52.015  41.957 -24.071  1.00 32.12           C  
ATOM   5132  N   LEU B 325      51.138  38.604 -25.889  1.00 30.78           N  
ATOM   5133  CA  LEU B 325      50.779  37.512 -26.804  1.00 29.95           C  
ATOM   5134  C   LEU B 325      51.701  36.278 -26.895  1.00 29.96           C  
ATOM   5135  O   LEU B 325      51.223  35.178 -27.181  1.00 29.99           O  
ATOM   5136  CB  LEU B 325      50.534  38.059 -28.205  1.00 29.75           C  
ATOM   5137  CG  LEU B 325      49.237  38.794 -28.552  1.00 29.76           C  
ATOM   5138  CD1 LEU B 325      48.069  38.375 -27.663  1.00 29.49           C  
ATOM   5139  CD2 LEU B 325      49.443  40.277 -28.487  1.00 30.23           C  
ATOM   5140  N   LYS B 326      53.005  36.435 -26.676  1.00 29.98           N  
ATOM   5141  CA  LYS B 326      53.928  35.296 -26.879  1.00 30.08           C  
ATOM   5142  C   LYS B 326      53.725  34.134 -25.891  1.00 30.18           C  
ATOM   5143  O   LYS B 326      54.287  33.062 -26.071  1.00 30.63           O  
ATOM   5144  CB  LYS B 326      55.413  35.709 -26.855  1.00 29.83           C  
ATOM   5145  CG  LYS B 326      55.744  37.118 -27.276  1.00 29.98           C  
ATOM   5146  CD  LYS B 326      57.257  37.286 -27.456  1.00 31.79           C  
ATOM   5147  CE  LYS B 326      58.070  37.058 -26.180  1.00 32.01           C  
ATOM   5148  NZ  LYS B 326      58.497  38.320 -25.514  1.00 32.14           N  
ATOM   5149  N   SER B 327      52.924  34.325 -24.858  1.00 30.28           N  
ATOM   5150  CA  SER B 327      52.886  33.332 -23.794  1.00 30.66           C  
ATOM   5151  C   SER B 327      51.534  32.688 -23.606  1.00 30.58           C  
ATOM   5152  O   SER B 327      51.416  31.771 -22.800  1.00 31.07           O  
ATOM   5153  CB  SER B 327      53.326  33.962 -22.479  1.00 30.49           C  
ATOM   5154  OG  SER B 327      54.104  35.102 -22.775  1.00 32.10           O  
ATOM   5155  N   ILE B 328      50.518  33.154 -24.324  1.00 30.06           N  
ATOM   5156  CA  ILE B 328      49.176  32.591 -24.169  1.00 29.99           C  
ATOM   5157  C   ILE B 328      48.870  31.481 -25.182  1.00 30.15           C  
ATOM   5158  O   ILE B 328      47.720  31.093 -25.380  1.00 29.88           O  
ATOM   5159  CB  ILE B 328      48.109  33.689 -24.199  1.00 29.99           C  
ATOM   5160  CG1 ILE B 328      48.317  34.588 -25.414  1.00 28.96           C  
ATOM   5161  CG2 ILE B 328      48.184  34.495 -22.914  1.00 29.71           C  
ATOM   5162  CD1 ILE B 328      47.322  35.667 -25.502  1.00 28.81           C  
ATOM   5163  N   GLY B 329      49.932  30.960 -25.785  1.00 30.51           N  
ATOM   5164  CA  GLY B 329      49.838  30.039 -26.893  1.00 31.32           C  
ATOM   5165  C   GLY B 329      49.221  28.726 -26.506  1.00 32.06           C  
ATOM   5166  O   GLY B 329      48.639  28.037 -27.346  1.00 32.08           O  
ATOM   5167  N   ASP B 330      49.343  28.392 -25.228  1.00 32.76           N  
ATOM   5168  CA  ASP B 330      48.796  27.163 -24.681  1.00 33.81           C  
ATOM   5169  C   ASP B 330      47.277  27.231 -24.503  1.00 33.43           C  
ATOM   5170  O   ASP B 330      46.613  26.200 -24.390  1.00 33.49           O  
ATOM   5171  CB  ASP B 330      49.473  26.830 -23.346  1.00 34.70           C  
ATOM   5172  CG  ASP B 330      49.270  27.937 -22.286  1.00 38.23           C  
ATOM   5173  OD1 ASP B 330      49.589  29.128 -22.576  1.00 41.02           O  
ATOM   5174  OD2 ASP B 330      48.800  27.612 -21.164  1.00 39.82           O  
ATOM   5175  N   HIS B 331      46.717  28.438 -24.493  1.00 33.55           N  
ATOM   5176  CA  HIS B 331      45.272  28.594 -24.211  1.00 33.31           C  
ATOM   5177  C   HIS B 331      44.467  29.486 -25.147  1.00 32.19           C  
ATOM   5178  O   HIS B 331      43.233  29.576 -25.028  1.00 31.99           O  
ATOM   5179  CB  HIS B 331      45.040  28.938 -22.740  1.00 33.68           C  
ATOM   5180  CG  HIS B 331      45.217  27.751 -21.846  1.00 36.45           C  
ATOM   5181  ND1 HIS B 331      44.459  26.606 -21.980  1.00 38.58           N  
ATOM   5182  CD2 HIS B 331      46.105  27.501 -20.854  1.00 38.43           C  
ATOM   5183  CE1 HIS B 331      44.846  25.718 -21.079  1.00 39.61           C  
ATOM   5184  NE2 HIS B 331      45.842  26.237 -20.382  1.00 39.67           N  
ATOM   5185  N   ALA B 332      45.162  30.111 -26.093  1.00 30.90           N  
ATOM   5186  CA  ALA B 332      44.499  30.891 -27.137  1.00 29.65           C  
ATOM   5187  C   ALA B 332      45.208  30.730 -28.475  1.00 28.42           C  
ATOM   5188  O   ALA B 332      46.393  30.383 -28.516  1.00 28.55           O  
ATOM   5189  CB  ALA B 332      44.415  32.370 -26.737  1.00 29.55           C  
ATOM   5190  N   VAL B 333      44.475  30.970 -29.559  1.00 26.43           N  
ATOM   5191  CA  VAL B 333      45.074  31.119 -30.880  1.00 24.87           C  
ATOM   5192  C   VAL B 333      45.152  32.587 -31.205  1.00 23.66           C  
ATOM   5193  O   VAL B 333      44.206  33.309 -30.971  1.00 23.45           O  
ATOM   5194  CB  VAL B 333      44.237  30.422 -31.944  1.00 24.83           C  
ATOM   5195  CG1 VAL B 333      44.868  30.582 -33.302  1.00 24.94           C  
ATOM   5196  CG2 VAL B 333      44.108  28.963 -31.603  1.00 25.07           C  
ATOM   5197  N   ILE B 334      46.283  33.033 -31.726  1.00 22.94           N  
ATOM   5198  CA  ILE B 334      46.468  34.453 -32.055  1.00 22.29           C  
ATOM   5199  C   ILE B 334      46.646  34.689 -33.555  1.00 21.90           C  
ATOM   5200  O   ILE B 334      47.583  34.156 -34.162  1.00 21.35           O  
ATOM   5201  CB  ILE B 334      47.683  35.075 -31.304  1.00 22.08           C  
ATOM   5202  CG1 ILE B 334      47.380  35.207 -29.833  1.00 21.77           C  
ATOM   5203  CG2 ILE B 334      48.057  36.464 -31.851  1.00 21.76           C  
ATOM   5204  CD1 ILE B 334      48.189  34.302 -29.040  1.00 24.93           C  
ATOM   5205  N   CYS B 335      45.762  35.502 -34.134  1.00 21.48           N  
ATOM   5206  CA  CYS B 335      45.965  35.997 -35.492  1.00 21.61           C  
ATOM   5207  C   CYS B 335      46.260  37.484 -35.540  1.00 21.04           C  
ATOM   5208  O   CYS B 335      45.528  38.261 -34.978  1.00 21.19           O  
ATOM   5209  CB  CYS B 335      44.753  35.724 -36.354  1.00 21.67           C  
ATOM   5210  SG  CYS B 335      45.051  36.218 -38.052  1.00 24.47           S  
ATOM   5211  N   VAL B 336      47.322  37.876 -36.227  1.00 20.76           N  
ATOM   5212  CA  VAL B 336      47.544  39.278 -36.543  1.00 20.52           C  
ATOM   5213  C   VAL B 336      47.444  39.438 -38.046  1.00 21.42           C  
ATOM   5214  O   VAL B 336      47.939  38.609 -38.790  1.00 21.68           O  
ATOM   5215  CB  VAL B 336      48.914  39.735 -36.102  1.00 19.92           C  
ATOM   5216  CG1 VAL B 336      49.096  41.237 -36.337  1.00 17.47           C  
ATOM   5217  CG2 VAL B 336      49.121  39.362 -34.658  1.00 20.21           C  
ATOM   5218  N   THR B 337      46.803  40.509 -38.489  1.00 22.44           N  
ATOM   5219  CA  THR B 337      46.648  40.774 -39.908  1.00 23.51           C  
ATOM   5220  C   THR B 337      46.421  42.248 -40.141  1.00 24.95           C  
ATOM   5221  O   THR B 337      45.959  42.947 -39.270  1.00 25.33           O  
ATOM   5222  CB  THR B 337      45.457  40.024 -40.499  1.00 23.22           C  
ATOM   5223  OG1 THR B 337      45.381  40.300 -41.897  1.00 22.15           O  
ATOM   5224  CG2 THR B 337      44.172  40.462 -39.830  1.00 22.53           C  
ATOM   5225  N   GLY B 338      46.732  42.715 -41.338  1.00 26.82           N  
ATOM   5226  CA  GLY B 338      46.561  44.113 -41.661  1.00 28.61           C  
ATOM   5227  C   GLY B 338      45.235  44.288 -42.353  1.00 30.03           C  
ATOM   5228  O   GLY B 338      44.544  43.300 -42.600  1.00 30.15           O  
ATOM   5229  N   ASP B 339      44.896  45.554 -42.641  1.00 31.76           N  
ATOM   5230  CA  ASP B 339      43.767  45.981 -43.503  1.00 32.98           C  
ATOM   5231  C   ASP B 339      43.874  47.481 -43.888  1.00 32.79           C  
ATOM   5232  O   ASP B 339      43.821  47.858 -45.074  1.00 33.04           O  
ATOM   5233  CB  ASP B 339      42.422  45.664 -42.832  1.00 33.56           C  
ATOM   5234  CG  ASP B 339      41.301  46.591 -43.289  1.00 36.93           C  
ATOM   5235  OD1 ASP B 339      40.518  47.055 -42.412  1.00 38.46           O  
ATOM   5236  OD2 ASP B 339      41.208  46.862 -44.521  1.00 40.93           O  
ATOM   5237  N   ASP B 352      46.716  46.439 -51.727  1.00 36.58           N  
ATOM   5238  CA  ASP B 352      45.780  45.322 -51.776  1.00 36.87           C  
ATOM   5239  C   ASP B 352      45.919  44.193 -50.755  1.00 36.28           C  
ATOM   5240  O   ASP B 352      45.080  44.021 -49.898  1.00 37.18           O  
ATOM   5241  CB  ASP B 352      45.822  44.698 -53.144  1.00 20.00           C  
ATOM   5242  CG  ASP B 352      44.487  44.251 -53.590  1.00 20.00           C  
ATOM   5243  OD1 ASP B 352      43.515  44.911 -53.167  1.00 20.00           O  
ATOM   5244  OD2 ASP B 352      44.418  43.253 -54.337  1.00 20.00           O  
ATOM   5245  N   PRO B 353      46.967  43.402 -50.892  1.00 34.86           N  
ATOM   5246  CA  PRO B 353      47.195  42.231 -50.073  1.00 33.36           C  
ATOM   5247  C   PRO B 353      48.041  42.507 -48.891  1.00 31.84           C  
ATOM   5248  O   PRO B 353      48.999  43.222 -48.953  1.00 31.78           O  
ATOM   5249  CB  PRO B 353      48.014  41.375 -50.983  1.00 33.55           C  
ATOM   5250  CG  PRO B 353      47.580  41.692 -52.240  1.00 34.91           C  
ATOM   5251  CD  PRO B 353      47.228  43.096 -52.288  1.00 35.14           C  
ATOM   5252  N   VAL B 354      47.689  41.885 -47.798  1.00 30.13           N  
ATOM   5253  CA  VAL B 354      48.290  42.197 -46.500  1.00 28.43           C  
ATOM   5254  C   VAL B 354      48.876  40.952 -45.845  1.00 26.72           C  
ATOM   5255  O   VAL B 354      48.380  39.855 -46.078  1.00 26.60           O  
ATOM   5256  CB  VAL B 354      47.244  42.835 -45.527  1.00 28.67           C  
ATOM   5257  CG1 VAL B 354      46.680  44.153 -46.085  1.00 28.69           C  
ATOM   5258  CG2 VAL B 354      46.122  41.868 -45.210  1.00 28.53           C  
ATOM   5259  N   PRO B 355      49.923  41.117 -45.018  1.00 25.13           N  
ATOM   5260  CA  PRO B 355      50.479  39.976 -44.290  1.00 24.10           C  
ATOM   5261  C   PRO B 355      49.506  39.414 -43.268  1.00 23.18           C  
ATOM   5262  O   PRO B 355      48.649  40.139 -42.747  1.00 23.13           O  
ATOM   5263  CB  PRO B 355      51.699  40.564 -43.569  1.00 23.96           C  
ATOM   5264  CG  PRO B 355      52.028  41.777 -44.322  1.00 24.94           C  
ATOM   5265  CD  PRO B 355      50.709  42.335 -44.788  1.00 25.07           C  
ATOM   5266  N   ILE B 356      49.631  38.120 -43.004  1.00 22.17           N  
ATOM   5267  CA  ILE B 356      48.864  37.476 -41.950  1.00 21.06           C  
ATOM   5268  C   ILE B 356      49.716  36.441 -41.224  1.00 21.32           C  
ATOM   5269  O   ILE B 356      50.561  35.764 -41.842  1.00 22.02           O  
ATOM   5270  CB  ILE B 356      47.553  36.871 -42.484  1.00 20.74           C  
ATOM   5271  CG1 ILE B 356      46.656  36.482 -41.315  1.00 19.09           C  
ATOM   5272  CG2 ILE B 356      47.823  35.709 -43.456  1.00 19.14           C  
ATOM   5273  CD1 ILE B 356      45.288  36.129 -41.726  1.00 17.96           C  
ATOM   5274  N   VAL B 357      49.522  36.338 -39.912  1.00 20.86           N  
ATOM   5275  CA  VAL B 357      50.289  35.390 -39.102  1.00 20.66           C  
ATOM   5276  C   VAL B 357      49.410  34.701 -38.067  1.00 20.80           C  
ATOM   5277  O   VAL B 357      48.579  35.343 -37.428  1.00 20.82           O  
ATOM   5278  CB  VAL B 357      51.487  36.057 -38.451  1.00 20.32           C  
ATOM   5279  CG1 VAL B 357      51.030  37.210 -37.610  1.00 19.87           C  
ATOM   5280  CG2 VAL B 357      52.320  35.049 -37.665  1.00 20.46           C  
ATOM   5281  N   PHE B 358      49.579  33.384 -37.957  1.00 20.96           N  
ATOM   5282  CA  PHE B 358      48.815  32.557 -37.040  1.00 21.40           C  
ATOM   5283  C   PHE B 358      49.758  31.909 -36.039  1.00 22.29           C  
ATOM   5284  O   PHE B 358      50.734  31.261 -36.421  1.00 22.40           O  
ATOM   5285  CB  PHE B 358      48.046  31.474 -37.790  1.00 20.86           C  
ATOM   5286  CG  PHE B 358      46.932  31.989 -38.638  1.00 19.41           C  
ATOM   5287  CD1 PHE B 358      47.146  32.296 -39.983  1.00 18.51           C  
ATOM   5288  CD2 PHE B 358      45.661  32.171 -38.104  1.00 17.30           C  
ATOM   5289  CE1 PHE B 358      46.100  32.773 -40.788  1.00 17.48           C  
ATOM   5290  CE2 PHE B 358      44.602  32.647 -38.903  1.00 16.11           C  
ATOM   5291  CZ  PHE B 358      44.814  32.935 -40.242  1.00 15.76           C  
ATOM   5292  N   TYR B 359      49.472  32.111 -34.760  1.00 23.54           N  
ATOM   5293  CA  TYR B 359      50.222  31.456 -33.712  1.00 25.12           C  
ATOM   5294  C   TYR B 359      49.341  30.866 -32.629  1.00 26.12           C  
ATOM   5295  O   TYR B 359      48.499  31.533 -32.040  1.00 25.93           O  
ATOM   5296  CB  TYR B 359      51.240  32.380 -33.060  1.00 25.28           C  
ATOM   5297  CG  TYR B 359      51.915  31.707 -31.899  1.00 26.54           C  
ATOM   5298  CD1 TYR B 359      52.603  30.507 -32.076  1.00 29.91           C  
ATOM   5299  CD2 TYR B 359      51.853  32.235 -30.638  1.00 27.55           C  
ATOM   5300  CE1 TYR B 359      53.211  29.868 -31.026  1.00 30.38           C  
ATOM   5301  CE2 TYR B 359      52.474  31.611 -29.576  1.00 29.99           C  
ATOM   5302  CZ  TYR B 359      53.148  30.425 -29.777  1.00 31.04           C  
ATOM   5303  OH  TYR B 359      53.758  29.780 -28.728  1.00 33.59           O  
ATOM   5304  N   THR B 360      49.540  29.578 -32.418  1.00 27.78           N  
ATOM   5305  CA  THR B 360      49.184  28.927 -31.179  1.00 29.54           C  
ATOM   5306  C   THR B 360      50.214  27.840 -30.917  1.00 30.11           C  
ATOM   5307  O   THR B 360      51.111  27.622 -31.725  1.00 30.07           O  
ATOM   5308  CB  THR B 360      47.754  28.376 -31.177  1.00 29.67           C  
ATOM   5309  OG1 THR B 360      47.444  27.892 -29.860  1.00 31.65           O  
ATOM   5310  CG2 THR B 360      47.589  27.260 -32.193  1.00 30.03           C  
ATOM   5311  N   ASP B 361      50.111  27.186 -29.773  1.00 31.57           N  
ATOM   5312  CA  ASP B 361      51.150  26.253 -29.373  1.00 33.03           C  
ATOM   5313  C   ASP B 361      50.959  24.978 -30.139  1.00 32.57           C  
ATOM   5314  O   ASP B 361      49.828  24.599 -30.460  1.00 32.29           O  
ATOM   5315  CB  ASP B 361      51.148  25.999 -27.863  1.00 34.02           C  
ATOM   5316  CG  ASP B 361      51.472  24.539 -27.515  1.00 37.91           C  
ATOM   5317  OD1 ASP B 361      52.660  24.130 -27.665  1.00 42.13           O  
ATOM   5318  OD2 ASP B 361      50.532  23.798 -27.103  1.00 40.89           O  
ATOM   5319  N   GLY B 362      52.089  24.349 -30.449  1.00 32.90           N  
ATOM   5320  CA  GLY B 362      52.125  23.123 -31.237  1.00 33.11           C  
ATOM   5321  C   GLY B 362      51.970  23.378 -32.722  1.00 33.27           C  
ATOM   5322  O   GLY B 362      51.754  22.429 -33.491  1.00 34.24           O  
ATOM   5323  N   VAL B 363      52.061  24.643 -33.138  1.00 32.56           N  
ATOM   5324  CA  VAL B 363      51.988  24.964 -34.557  1.00 32.56           C  
ATOM   5325  C   VAL B 363      53.367  24.814 -35.193  1.00 32.62           C  
ATOM   5326  O   VAL B 363      54.372  25.211 -34.622  1.00 32.14           O  
ATOM   5327  CB  VAL B 363      51.353  26.358 -34.834  1.00 32.52           C  
ATOM   5328  CG1 VAL B 363      51.844  26.949 -36.135  1.00 31.98           C  
ATOM   5329  CG2 VAL B 363      49.848  26.242 -34.912  1.00 32.74           C  
HETATM 5330  N   MSE B 364      53.403  24.231 -36.380  1.00 32.91           N  
HETATM 5331  CA  MSE B 364      54.654  24.075 -37.073  1.00 33.60           C  
HETATM 5332  C   MSE B 364      55.017  25.304 -37.913  1.00 32.28           C  
HETATM 5333  O   MSE B 364      54.240  25.733 -38.764  1.00 31.96           O  
HETATM 5334  CB  MSE B 364      54.596  22.809 -37.909  1.00 35.07           C  
HETATM 5335  CG  MSE B 364      55.031  21.572 -37.130  1.00 40.51           C  
HETATM 5336 SE   MSE B 364      55.729  20.258 -38.372  1.00 55.36          SE  
HETATM 5337  CE  MSE B 364      53.998  19.829 -39.235  1.00 50.72           C  
ATOM   5338  N   ASN B 365      56.200  25.865 -37.666  1.00 31.07           N  
ATOM   5339  CA  ASN B 365      56.658  27.045 -38.404  1.00 30.14           C  
ATOM   5340  C   ASN B 365      56.926  26.819 -39.898  1.00 29.75           C  
ATOM   5341  O   ASN B 365      57.563  25.859 -40.314  1.00 29.51           O  
ATOM   5342  CB  ASN B 365      57.864  27.714 -37.730  1.00 29.90           C  
ATOM   5343  CG  ASN B 365      58.458  28.858 -38.565  1.00 29.18           C  
ATOM   5344  OD1 ASN B 365      59.638  28.844 -38.872  1.00 29.18           O  
ATOM   5345  ND2 ASN B 365      57.644  29.846 -38.918  1.00 28.75           N  
ATOM   5346  N   ASP B 366      56.376  27.756 -40.653  1.00 29.63           N  
ATOM   5347  CA  ASP B 366      56.396  27.925 -42.081  1.00 29.53           C  
ATOM   5348  C   ASP B 366      57.796  27.957 -42.671  1.00 29.15           C  
ATOM   5349  O   ASP B 366      58.017  27.544 -43.810  1.00 28.56           O  
ATOM   5350  CB  ASP B 366      55.837  29.337 -42.281  1.00 30.28           C  
ATOM   5351  CG  ASP B 366      54.685  29.386 -43.229  1.00 32.89           C  
ATOM   5352  OD1 ASP B 366      54.771  28.782 -44.311  1.00 37.32           O  
ATOM   5353  OD2 ASP B 366      53.689  30.057 -42.908  1.00 35.35           O  
ATOM   5354  N   GLY B 367      58.732  28.500 -41.893  1.00 28.84           N  
ATOM   5355  CA  GLY B 367      60.037  28.910 -42.396  1.00 28.22           C  
ATOM   5356  C   GLY B 367      60.206  30.425 -42.537  1.00 28.03           C  
ATOM   5357  O   GLY B 367      61.295  30.892 -42.901  1.00 28.10           O  
ATOM   5358  N   VAL B 368      59.142  31.191 -42.263  1.00 27.33           N  
ATOM   5359  CA  VAL B 368      59.204  32.647 -42.344  1.00 26.76           C  
ATOM   5360  C   VAL B 368      59.590  33.186 -40.980  1.00 26.80           C  
ATOM   5361  O   VAL B 368      59.164  32.663 -39.956  1.00 26.75           O  
ATOM   5362  CB  VAL B 368      57.883  33.253 -42.819  1.00 26.63           C  
ATOM   5363  CG1 VAL B 368      57.873  34.749 -42.607  1.00 26.40           C  
ATOM   5364  CG2 VAL B 368      57.671  32.944 -44.279  1.00 26.20           C  
ATOM   5365  N   HIS B 369      60.415  34.221 -40.974  1.00 26.81           N  
ATOM   5366  CA  HIS B 369      61.022  34.689 -39.738  1.00 27.06           C  
ATOM   5367  C   HIS B 369      60.675  36.115 -39.365  1.00 26.21           C  
ATOM   5368  O   HIS B 369      60.758  36.484 -38.193  1.00 26.62           O  
ATOM   5369  CB  HIS B 369      62.540  34.512 -39.796  1.00 27.64           C  
ATOM   5370  CG  HIS B 369      62.974  33.084 -39.751  1.00 30.88           C  
ATOM   5371  ND1 HIS B 369      63.902  32.559 -40.625  1.00 33.88           N  
ATOM   5372  CD2 HIS B 369      62.585  32.059 -38.950  1.00 33.06           C  
ATOM   5373  CE1 HIS B 369      64.083  31.277 -40.351  1.00 34.77           C  
ATOM   5374  NE2 HIS B 369      63.289  30.948 -39.345  1.00 34.60           N  
ATOM   5375  N   LEU B 370      60.313  36.922 -40.358  1.00 25.33           N  
ATOM   5376  CA  LEU B 370      59.887  38.282 -40.105  1.00 24.45           C  
ATOM   5377  C   LEU B 370      58.482  38.476 -40.619  1.00 24.11           C  
ATOM   5378  O   LEU B 370      58.001  37.718 -41.480  1.00 23.99           O  
ATOM   5379  CB  LEU B 370      60.864  39.314 -40.699  1.00 24.64           C  
ATOM   5380  CG  LEU B 370      62.365  39.020 -40.512  1.00 24.62           C  
ATOM   5381  CD1 LEU B 370      62.945  38.662 -41.842  1.00 26.76           C  
ATOM   5382  CD2 LEU B 370      63.141  40.158 -39.937  1.00 23.93           C  
ATOM   5383  N   PHE B 371      57.825  39.493 -40.074  1.00 23.49           N  
ATOM   5384  CA  PHE B 371      56.461  39.830 -40.430  1.00 22.67           C  
ATOM   5385  C   PHE B 371      56.435  41.169 -41.168  1.00 23.03           C  
ATOM   5386  O   PHE B 371      56.611  42.230 -40.569  1.00 23.04           O  
ATOM   5387  CB  PHE B 371      55.650  39.905 -39.161  1.00 21.70           C  
ATOM   5388  CG  PHE B 371      54.273  40.396 -39.356  1.00 20.92           C  
ATOM   5389  CD1 PHE B 371      53.272  39.536 -39.803  1.00 20.70           C  
ATOM   5390  CD2 PHE B 371      53.950  41.701 -39.062  1.00 20.17           C  
ATOM   5391  CE1 PHE B 371      51.968  39.969 -39.979  1.00 19.47           C  
ATOM   5392  CE2 PHE B 371      52.645  42.148 -39.233  1.00 20.31           C  
ATOM   5393  CZ  PHE B 371      51.653  41.279 -39.698  1.00 19.67           C  
ATOM   5394  N   ASP B 372      56.244  41.101 -42.478  1.00 23.48           N  
ATOM   5395  CA  ASP B 372      56.125  42.287 -43.338  1.00 24.04           C  
ATOM   5396  C   ASP B 372      55.726  41.893 -44.752  1.00 24.59           C  
ATOM   5397  O   ASP B 372      55.627  40.717 -45.058  1.00 25.26           O  
ATOM   5398  CB  ASP B 372      57.432  43.040 -43.400  1.00 23.75           C  
ATOM   5399  CG  ASP B 372      58.470  42.287 -44.128  1.00 23.04           C  
ATOM   5400  OD1 ASP B 372      58.335  42.086 -45.346  1.00 22.75           O  
ATOM   5401  OD2 ASP B 372      59.429  41.873 -43.476  1.00 24.50           O  
ATOM   5402  N   GLU B 373      55.555  42.872 -45.627  1.00 25.40           N  
ATOM   5403  CA  GLU B 373      54.918  42.636 -46.926  1.00 26.68           C  
ATOM   5404  C   GLU B 373      55.695  41.671 -47.854  1.00 27.07           C  
ATOM   5405  O   GLU B 373      55.087  40.849 -48.552  1.00 27.05           O  
ATOM   5406  CB  GLU B 373      54.580  43.964 -47.633  1.00 26.82           C  
ATOM   5407  CG  GLU B 373      53.825  44.990 -46.782  1.00 27.16           C  
ATOM   5408  CD  GLU B 373      54.765  45.769 -45.857  1.00 29.15           C  
ATOM   5409  OE1 GLU B 373      55.974  45.449 -45.840  1.00 29.57           O  
ATOM   5410  OE2 GLU B 373      54.311  46.707 -45.158  1.00 29.75           O  
ATOM   5411  N   LEU B 374      57.024  41.785 -47.837  1.00 27.62           N  
ATOM   5412  CA  LEU B 374      57.933  40.918 -48.591  1.00 27.85           C  
ATOM   5413  C   LEU B 374      58.166  39.582 -47.930  1.00 27.84           C  
ATOM   5414  O   LEU B 374      57.957  38.538 -48.540  1.00 28.13           O  
ATOM   5415  CB  LEU B 374      59.299  41.571 -48.715  1.00 27.97           C  
ATOM   5416  CG  LEU B 374      59.667  42.271 -50.011  1.00 29.69           C  
ATOM   5417  CD1 LEU B 374      58.517  43.172 -50.535  1.00 30.67           C  
ATOM   5418  CD2 LEU B 374      60.979  43.072 -49.773  1.00 31.50           C  
ATOM   5419  N   SER B 375      58.649  39.594 -46.696  1.00 27.33           N  
ATOM   5420  CA  SER B 375      59.097  38.340 -46.147  1.00 27.42           C  
ATOM   5421  C   SER B 375      57.918  37.411 -45.928  1.00 26.94           C  
ATOM   5422  O   SER B 375      58.048  36.195 -46.095  1.00 26.53           O  
ATOM   5423  CB  SER B 375      59.940  38.530 -44.893  1.00 27.55           C  
ATOM   5424  OG  SER B 375      59.204  39.220 -43.919  1.00 29.46           O  
ATOM   5425  N   SER B 376      56.760  37.984 -45.619  1.00 26.81           N  
ATOM   5426  CA  SER B 376      55.563  37.171 -45.400  1.00 27.09           C  
ATOM   5427  C   SER B 376      54.963  36.567 -46.694  1.00 27.26           C  
ATOM   5428  O   SER B 376      54.151  35.637 -46.645  1.00 27.25           O  
ATOM   5429  CB  SER B 376      54.532  37.929 -44.560  1.00 27.22           C  
ATOM   5430  OG  SER B 376      54.981  38.066 -43.207  1.00 27.99           O  
ATOM   5431  N   ALA B 377      55.409  37.052 -47.849  1.00 27.33           N  
ATOM   5432  CA  ALA B 377      54.968  36.500 -49.122  1.00 27.09           C  
ATOM   5433  C   ALA B 377      55.609  35.151 -49.430  1.00 27.17           C  
ATOM   5434  O   ALA B 377      55.281  34.508 -50.434  1.00 26.98           O  
ATOM   5435  CB  ALA B 377      55.231  37.456 -50.209  1.00 26.95           C  
ATOM   5436  N   SER B 378      56.520  34.733 -48.561  1.00 27.08           N  
ATOM   5437  CA  SER B 378      57.076  33.399 -48.626  1.00 27.28           C  
ATOM   5438  C   SER B 378      56.306  32.467 -47.730  1.00 27.20           C  
ATOM   5439  O   SER B 378      56.701  31.329 -47.529  1.00 27.52           O  
ATOM   5440  CB  SER B 378      58.527  33.406 -48.182  1.00 27.44           C  
ATOM   5441  OG  SER B 378      59.366  33.901 -49.207  1.00 29.20           O  
ATOM   5442  N   GLY B 379      55.212  32.949 -47.171  1.00 27.44           N  
ATOM   5443  CA  GLY B 379      54.398  32.114 -46.302  1.00 28.02           C  
ATOM   5444  C   GLY B 379      53.631  31.027 -47.044  1.00 28.47           C  
ATOM   5445  O   GLY B 379      53.339  31.161 -48.242  1.00 28.30           O  
ATOM   5446  N   SER B 380      53.286  29.961 -46.318  1.00 28.90           N  
ATOM   5447  CA  SER B 380      52.540  28.830 -46.878  1.00 29.13           C  
ATOM   5448  C   SER B 380      51.104  29.185 -47.143  1.00 29.16           C  
ATOM   5449  O   SER B 380      50.427  28.478 -47.856  1.00 29.29           O  
ATOM   5450  CB  SER B 380      52.565  27.634 -45.928  1.00 29.18           C  
ATOM   5451  OG  SER B 380      51.628  27.797 -44.877  1.00 29.46           O  
ATOM   5452  N   LEU B 381      50.647  30.270 -46.541  1.00 29.75           N  
ATOM   5453  CA  LEU B 381      49.253  30.666 -46.601  1.00 30.44           C  
ATOM   5454  C   LEU B 381      48.983  31.683 -47.692  1.00 31.07           C  
ATOM   5455  O   LEU B 381      49.687  32.673 -47.845  1.00 31.22           O  
ATOM   5456  CB  LEU B 381      48.796  31.198 -45.234  1.00 30.24           C  
ATOM   5457  CG  LEU B 381      48.019  30.283 -44.268  1.00 30.06           C  
ATOM   5458  CD1 LEU B 381      48.258  28.771 -44.495  1.00 29.78           C  
ATOM   5459  CD2 LEU B 381      48.323  30.658 -42.831  1.00 27.26           C  
ATOM   5460  N   ARG B 382      47.959  31.395 -48.471  1.00 32.44           N  
ATOM   5461  CA  ARG B 382      47.408  32.330 -49.445  1.00 33.63           C  
ATOM   5462  C   ARG B 382      45.898  32.308 -49.269  1.00 33.80           C  
ATOM   5463  O   ARG B 382      45.213  31.392 -49.728  1.00 33.60           O  
ATOM   5464  CB  ARG B 382      47.784  31.935 -50.872  1.00 33.63           C  
ATOM   5465  CG  ARG B 382      48.789  32.858 -51.487  1.00 35.35           C  
ATOM   5466  CD  ARG B 382      50.078  32.166 -51.738  1.00 39.44           C  
ATOM   5467  NE  ARG B 382      51.078  33.111 -52.212  1.00 43.37           N  
ATOM   5468  CZ  ARG B 382      51.912  33.776 -51.418  1.00 45.59           C  
ATOM   5469  NH1 ARG B 382      51.878  33.590 -50.097  1.00 47.19           N  
ATOM   5470  NH2 ARG B 382      52.794  34.619 -51.944  1.00 45.43           N  
ATOM   5471  N   ILE B 383      45.379  33.297 -48.567  1.00 34.20           N  
ATOM   5472  CA  ILE B 383      44.019  33.177 -48.121  1.00 35.25           C  
ATOM   5473  C   ILE B 383      43.192  34.402 -48.401  1.00 35.95           C  
ATOM   5474  O   ILE B 383      43.662  35.379 -48.988  1.00 35.53           O  
ATOM   5475  CB  ILE B 383      43.928  32.772 -46.619  1.00 35.29           C  
ATOM   5476  CG1 ILE B 383      44.664  33.774 -45.733  1.00 35.07           C  
ATOM   5477  CG2 ILE B 383      44.479  31.349 -46.405  1.00 36.38           C  
ATOM   5478  CD1 ILE B 383      44.562  33.488 -44.255  1.00 35.26           C  
ATOM   5479  N   THR B 384      41.950  34.311 -47.946  1.00 37.31           N  
ATOM   5480  CA  THR B 384      40.910  35.276 -48.204  1.00 38.59           C  
ATOM   5481  C   THR B 384      40.230  35.607 -46.882  1.00 39.63           C  
ATOM   5482  O   THR B 384      40.094  34.730 -46.041  1.00 39.93           O  
ATOM   5483  CB  THR B 384      39.919  34.671 -49.231  1.00 38.51           C  
ATOM   5484  OG1 THR B 384      40.391  34.948 -50.557  1.00 37.86           O  
ATOM   5485  CG2 THR B 384      38.488  35.194 -49.062  1.00 38.69           C  
ATOM   5486  N   SER B 385      39.838  36.873 -46.700  1.00 41.00           N  
ATOM   5487  CA  SER B 385      38.999  37.329 -45.583  1.00 41.99           C  
ATOM   5488  C   SER B 385      38.191  36.195 -44.992  1.00 42.86           C  
ATOM   5489  O   SER B 385      38.092  36.078 -43.781  1.00 43.20           O  
ATOM   5490  CB  SER B 385      38.006  38.394 -46.056  1.00 41.92           C  
ATOM   5491  OG  SER B 385      38.639  39.551 -46.569  1.00 42.93           O  
ATOM   5492  N   TYR B 386      37.626  35.364 -45.864  1.00 44.14           N  
ATOM   5493  CA  TYR B 386      36.690  34.305 -45.485  1.00 45.58           C  
ATOM   5494  C   TYR B 386      37.318  33.052 -44.866  1.00 45.33           C  
ATOM   5495  O   TYR B 386      36.688  32.380 -44.047  1.00 45.99           O  
ATOM   5496  CB  TYR B 386      35.806  33.910 -46.684  1.00 46.50           C  
ATOM   5497  CG  TYR B 386      34.372  33.701 -46.283  1.00 49.88           C  
ATOM   5498  CD1 TYR B 386      33.554  34.803 -45.993  1.00 52.93           C  
ATOM   5499  CD2 TYR B 386      33.830  32.409 -46.153  1.00 53.26           C  
ATOM   5500  CE1 TYR B 386      32.217  34.636 -45.587  1.00 55.48           C  
ATOM   5501  CE2 TYR B 386      32.478  32.223 -45.748  1.00 55.62           C  
ATOM   5502  CZ  TYR B 386      31.681  33.351 -45.468  1.00 56.48           C  
ATOM   5503  OH  TYR B 386      30.361  33.223 -45.068  1.00 57.42           O  
ATOM   5504  N   ASN B 387      38.541  32.723 -45.259  1.00 45.09           N  
ATOM   5505  CA  ASN B 387      39.206  31.535 -44.720  1.00 44.91           C  
ATOM   5506  C   ASN B 387      39.761  31.770 -43.325  1.00 44.09           C  
ATOM   5507  O   ASN B 387      40.102  30.820 -42.616  1.00 44.17           O  
ATOM   5508  CB  ASN B 387      40.334  31.044 -45.638  1.00 45.32           C  
ATOM   5509  CG  ASN B 387      39.951  31.059 -47.103  1.00 46.40           C  
ATOM   5510  OD1 ASN B 387      40.430  31.905 -47.870  1.00 47.19           O  
ATOM   5511  ND2 ASN B 387      39.080  30.131 -47.502  1.00 47.63           N  
ATOM   5512  N   VAL B 388      39.852  33.034 -42.938  1.00 43.25           N  
ATOM   5513  CA  VAL B 388      40.470  33.395 -41.672  1.00 42.68           C  
ATOM   5514  C   VAL B 388      39.722  32.731 -40.528  1.00 42.92           C  
ATOM   5515  O   VAL B 388      40.322  31.999 -39.741  1.00 42.38           O  
ATOM   5516  CB  VAL B 388      40.573  34.924 -41.505  1.00 42.26           C  
ATOM   5517  CG1 VAL B 388      41.042  35.297 -40.115  1.00 40.94           C  
ATOM   5518  CG2 VAL B 388      41.514  35.485 -42.545  1.00 41.72           C  
HETATM 5519  N   MSE B 389      38.409  32.937 -40.483  1.00 43.56           N  
HETATM 5520  CA  MSE B 389      37.579  32.357 -39.427  1.00 44.49           C  
HETATM 5521  C   MSE B 389      37.621  30.824 -39.353  1.00 44.26           C  
HETATM 5522  O   MSE B 389      37.547  30.278 -38.260  1.00 44.16           O  
HETATM 5523  CB  MSE B 389      36.137  32.868 -39.508  1.00 45.09           C  
HETATM 5524  CG  MSE B 389      35.298  32.519 -38.285  1.00 47.49           C  
HETATM 5525 SE   MSE B 389      36.020  33.248 -36.605  1.00 53.92          SE  
HETATM 5526  CE  MSE B 389      34.789  34.748 -36.418  1.00 53.42           C  
ATOM   5527  N   ASP B 390      37.752  30.142 -40.497  1.00 44.37           N  
ATOM   5528  CA  ASP B 390      37.932  28.670 -40.533  1.00 44.30           C  
ATOM   5529  C   ASP B 390      39.282  28.226 -39.962  1.00 43.45           C  
ATOM   5530  O   ASP B 390      39.331  27.411 -39.035  1.00 43.66           O  
ATOM   5531  CB  ASP B 390      37.780  28.103 -41.958  1.00 45.02           C  
ATOM   5532  CG  ASP B 390      36.361  28.240 -42.511  1.00 47.29           C  
ATOM   5533  OD1 ASP B 390      36.229  28.496 -43.735  1.00 49.34           O  
ATOM   5534  OD2 ASP B 390      35.384  28.099 -41.731  1.00 49.44           O  
ATOM   5535  N   ILE B 391      40.373  28.751 -40.515  1.00 42.16           N  
ATOM   5536  CA  ILE B 391      41.699  28.439 -40.006  1.00 41.14           C  
ATOM   5537  C   ILE B 391      41.744  28.715 -38.510  1.00 41.24           C  
ATOM   5538  O   ILE B 391      42.347  27.966 -37.755  1.00 40.99           O  
ATOM   5539  CB  ILE B 391      42.781  29.248 -40.734  1.00 40.81           C  
ATOM   5540  CG1 ILE B 391      42.962  28.723 -42.153  1.00 39.66           C  
ATOM   5541  CG2 ILE B 391      44.101  29.192 -39.990  1.00 40.03           C  
ATOM   5542  CD1 ILE B 391      43.545  29.722 -43.100  1.00 38.54           C  
ATOM   5543  N   LEU B 392      41.083  29.784 -38.084  1.00 41.48           N  
ATOM   5544  CA  LEU B 392      41.014  30.095 -36.665  1.00 41.94           C  
ATOM   5545  C   LEU B 392      40.275  29.045 -35.856  1.00 42.78           C  
ATOM   5546  O   LEU B 392      40.743  28.653 -34.789  1.00 42.92           O  
ATOM   5547  CB  LEU B 392      40.434  31.485 -36.409  1.00 41.43           C  
ATOM   5548  CG  LEU B 392      41.453  32.610 -36.581  1.00 40.21           C  
ATOM   5549  CD1 LEU B 392      40.814  33.935 -36.222  1.00 39.27           C  
ATOM   5550  CD2 LEU B 392      42.714  32.377 -35.763  1.00 37.78           C  
HETATM 5551  N   MSE B 393      39.143  28.561 -36.359  1.00 43.74           N  
HETATM 5552  CA  MSE B 393      38.422  27.510 -35.640  1.00 44.71           C  
HETATM 5553  C   MSE B 393      39.177  26.190 -35.593  1.00 44.01           C  
HETATM 5554  O   MSE B 393      39.029  25.444 -34.633  1.00 43.94           O  
HETATM 5555  CB  MSE B 393      36.988  27.335 -36.148  1.00 45.59           C  
HETATM 5556  CG  MSE B 393      35.941  27.932 -35.190  1.00 49.80           C  
HETATM 5557 SE   MSE B 393      34.442  28.895 -36.065  1.00 59.75          SE  
HETATM 5558  CE  MSE B 393      33.860  27.500 -37.367  1.00 56.67           C  
ATOM   5559  N   GLN B 394      40.004  25.914 -36.598  1.00 43.53           N  
ATOM   5560  CA  GLN B 394      40.754  24.655 -36.605  1.00 43.52           C  
ATOM   5561  C   GLN B 394      41.979  24.652 -35.713  1.00 42.52           C  
ATOM   5562  O   GLN B 394      42.239  23.672 -35.021  1.00 42.42           O  
ATOM   5563  CB  GLN B 394      41.105  24.176 -38.019  1.00 44.16           C  
ATOM   5564  CG  GLN B 394      40.462  22.818 -38.366  1.00 46.95           C  
ATOM   5565  CD  GLN B 394      40.645  22.405 -39.830  1.00 51.42           C  
ATOM   5566  OE1 GLN B 394      40.443  21.232 -40.194  1.00 53.24           O  
ATOM   5567  NE2 GLN B 394      41.013  23.367 -40.679  1.00 52.10           N  
ATOM   5568  N   LEU B 395      42.727  25.746 -35.727  1.00 41.69           N  
ATOM   5569  CA  LEU B 395      43.861  25.904 -34.823  1.00 40.87           C  
ATOM   5570  C   LEU B 395      43.412  25.852 -33.357  1.00 40.84           C  
ATOM   5571  O   LEU B 395      44.187  25.497 -32.465  1.00 40.47           O  
ATOM   5572  CB  LEU B 395      44.571  27.218 -35.123  1.00 40.50           C  
ATOM   5573  CG  LEU B 395      45.776  27.208 -36.055  1.00 39.38           C  
ATOM   5574  CD1 LEU B 395      45.793  25.987 -36.920  1.00 38.42           C  
ATOM   5575  CD2 LEU B 395      45.734  28.433 -36.906  1.00 38.01           C  
ATOM   5576  N   ALA B 396      42.149  26.196 -33.132  1.00 40.89           N  
ATOM   5577  CA  ALA B 396      41.578  26.237 -31.810  1.00 41.13           C  
ATOM   5578  C   ALA B 396      41.134  24.856 -31.363  1.00 41.51           C  
ATOM   5579  O   ALA B 396      41.202  24.543 -30.178  1.00 41.70           O  
ATOM   5580  CB  ALA B 396      40.431  27.197 -31.792  1.00 40.97           C  
ATOM   5581  N   GLY B 397      40.706  24.031 -32.317  1.00 41.94           N  
ATOM   5582  CA  GLY B 397      40.196  22.691 -32.033  1.00 42.53           C  
ATOM   5583  C   GLY B 397      38.871  22.794 -31.301  1.00 43.00           C  
ATOM   5584  O   GLY B 397      37.820  22.302 -31.719  1.00 43.24           O  
TER    5585      GLY B 397                                                      
HETATM 5586  O   HOH A 405      23.777  83.295  -5.031  1.00 28.86           O  
HETATM 5587  O   HOH A 406      20.237  75.241 -16.505  1.00 38.79           O  
HETATM 5588  O   HOH A 407      10.543  74.096 -14.686  1.00 14.50           O  
HETATM 5589  O   HOH A 408      55.599  48.856  -6.807  1.00 37.03           O  
HETATM 5590  O   HOH A 409      47.779  43.316 -16.860  1.00 23.50           O  
HETATM 5591  O   HOH A 410      44.655  51.849  -7.488  1.00 20.92           O  
HETATM 5592  O   HOH A 411      54.807  36.013   8.254  1.00 31.14           O  
HETATM 5593  O   HOH A 412      48.281  32.565   5.102  1.00 28.83           O  
HETATM 5594  O   HOH A 413      20.139  38.390 -18.950  1.00 25.37           O  
HETATM 5595  O   HOH A 414      19.360  42.452 -18.269  1.00 22.34           O  
HETATM 5596  O   HOH A 415      21.291  42.456 -20.728  1.00 36.58           O  
HETATM 5597  O   HOH A 416       6.708  63.256 -21.553  1.00 27.62           O  
HETATM 5598  O   HOH A 417      45.514  32.163 -21.893  1.00 19.57           O  
HETATM 5599  O   HOH A 418       4.931  71.479 -20.501  1.00 20.93           O  
HETATM 5600  O   HOH A 419      40.257  49.628  -7.423  1.00 21.53           O  
HETATM 5601  O   HOH A 420      31.518  39.462 -15.708  1.00 24.70           O  
HETATM 5602  O   HOH A 421      32.246  31.515 -13.912  1.00 36.23           O  
HETATM 5603  O   HOH A 422      54.553  48.547   5.607  1.00 38.54           O  
HETATM 5604  O   HOH A 423      49.281  48.632   0.970  1.00 22.94           O  
HETATM 5605  O   HOH A 424      50.410  54.923  -1.561  1.00 22.53           O  
HETATM 5606  O   HOH A 425      34.938  28.414  -7.406  1.00 15.56           O  
HETATM 5607  O   HOH A 426      35.193  30.133   0.256  1.00 26.35           O  
HETATM 5608  O   HOH A 427      55.508  26.654  -7.830  1.00 23.79           O  
HETATM 5609  O   HOH A 428      68.188  48.169  -5.985  1.00 31.69           O  
HETATM 5610  O   HOH A 429      54.861  36.581  -5.210  1.00 18.64           O  
HETATM 5611  O   HOH A 430      43.898  41.412   5.186  1.00 21.82           O  
HETATM 5612  O   HOH A 431       8.699  44.093 -15.435  1.00 34.73           O  
HETATM 5613  O   HOH A 432      24.977  37.520 -12.223  1.00 23.34           O  
HETATM 5614  O   HOH A 433      27.911  45.250 -23.413  1.00 23.69           O  
HETATM 5615  O   HOH A 434      30.958  69.862 -15.691  1.00 27.53           O  
HETATM 5616  O   HOH A 435      24.448  69.752 -21.020  1.00 27.97           O  
HETATM 5617  O   HOH A 436      14.253  67.667 -27.529  1.00 43.84           O  
HETATM 5618  O   HOH A 437       9.782  71.688   1.948  1.00 46.13           O  
HETATM 5619  O   HOH A 438      46.024  46.747  -3.732  1.00 29.83           O  
HETATM 5620  O   HOH A 439      36.237  36.262 -14.425  1.00 37.95           O  
HETATM 5621  O   HOH A 440      49.643  54.128   1.625  1.00 38.77           O  
HETATM 5622  O   HOH A 441      47.867  50.787   0.286  1.00 23.95           O  
HETATM 5623  O   HOH A 442      42.863  33.679 -18.422  1.00 35.56           O  
HETATM 5624  O   HOH A 443      34.315  27.139   1.089  1.00 24.54           O  
HETATM 5625  O   HOH A 444      61.084  50.011 -13.590  1.00 25.00           O  
HETATM 5626  O   HOH A 445      26.122  32.770 -10.765  1.00 28.94           O  
HETATM 5627  O   HOH A 446      25.410  34.994 -12.804  1.00 29.22           O  
HETATM 5628  O   HOH A 447      29.874  56.852 -13.765  1.00  2.00           O  
HETATM 5629  O   HOH A 448      32.412  42.096 -14.215  1.00 29.92           O  
HETATM 5630  O   HOH A 449      16.550  60.772 -28.511  1.00 39.21           O  
HETATM 5631  O   HOH A 450      25.290  76.943 -16.431  1.00 16.88           O  
HETATM 5632  O   HOH A 451      15.035  49.380  -5.713  1.00 28.66           O  
HETATM 5633  O   HOH A 452       5.953  45.529 -15.202  1.00 26.60           O  
HETATM 5634  O   HOH A 453      43.426  49.672  -6.334  1.00 20.85           O  
HETATM 5635  O   HOH A 454      13.403  62.931 -26.119  1.00 24.11           O  
HETATM 5636  O   HOH B 405      37.679  31.406 -23.783  1.00 36.53           O  
HETATM 5637  O   HOH B 406      65.041  51.190 -39.090  1.00 29.18           O  
HETATM 5638  O   HOH B 407      62.781  43.680 -35.712  1.00 17.38           O  
HETATM 5639  O   HOH B 408      23.757  66.371 -49.159  1.00 27.20           O  
HETATM 5640  O   HOH B 409      23.773  73.238 -49.198  1.00 19.12           O  
HETATM 5641  O   HOH B 410      15.057  56.131 -50.513  1.00 18.43           O  
HETATM 5642  O   HOH B 411      18.787  73.621 -59.872  1.00 44.18           O  
HETATM 5643  O   HOH B 412       3.039  50.034 -56.458  1.00 33.07           O  
HETATM 5644  O   HOH B 413      38.584  50.630 -34.051  1.00  2.00           O  
HETATM 5645  O   HOH B 414      67.625  49.617 -48.175  1.00 35.69           O  
HETATM 5646  O   HOH B 415      24.093  62.126 -43.999  1.00 21.98           O  
HETATM 5647  O   HOH B 416      18.348  81.552 -48.944  1.00 32.03           O  
HETATM 5648  O   HOH B 417      10.924  79.943 -51.239  1.00 36.18           O  
HETATM 5649  O   HOH B 418      14.657  63.734 -57.313  1.00 29.68           O  
HETATM 5650  O   HOH B 419       6.785  64.606 -54.841  1.00 42.13           O  
HETATM 5651  O   HOH B 420       5.944  66.975 -53.787  1.00 43.36           O  
HETATM 5652  O   HOH B 421       9.697  48.109 -59.748  1.00 13.04           O  
HETATM 5653  O   HOH B 422       9.200  71.989 -31.686  1.00 21.70           O  
HETATM 5654  O   HOH B 423      10.946  66.767 -43.143  1.00 15.14           O  
HETATM 5655  O   HOH B 424      23.238  58.871 -50.397  1.00 22.33           O  
HETATM 5656  O   HOH B 425      43.847  53.139 -27.846  1.00 31.87           O  
HETATM 5657  O   HOH B 426      50.148  56.195 -32.015  1.00 26.21           O  
HETATM 5658  O   HOH B 427      37.651  37.407 -18.119  1.00 35.75           O  
HETATM 5659  O   HOH B 428      52.029  50.548 -26.110  1.00 25.12           O  
HETATM 5660  O   HOH B 429      61.040  42.256 -45.710  1.00 20.84           O  
HETATM 5661  O   HOH B 430      54.341  49.231 -43.946  1.00 40.67           O  
HETATM 5662  O   HOH B 431      58.767  57.887 -48.387  1.00 43.44           O  
HETATM 5663  O   HOH B 432      59.994  39.593 -28.090  1.00 38.87           O  
HETATM 5664  O   HOH B 433      25.225  76.688 -36.153  1.00 33.66           O  
HETATM 5665  O   HOH B 434      22.619  79.720 -42.137  1.00 44.17           O  
HETATM 5666  O   HOH B 435       6.025  48.795 -47.549  1.00 20.56           O  
HETATM 5667  O   HOH B 436      19.079  63.311 -47.745  1.00 23.48           O  
HETATM 5668  O   HOH B 437      52.114  45.019 -21.527  1.00 18.75           O  
HETATM 5669  O   HOH B 438      17.211  82.622 -42.187  1.00 35.02           O  
CONECT  330  336                                                                
CONECT  336  330  337                                                           
CONECT  337  336  338  340                                                      
CONECT  338  337  339  344                                                      
CONECT  339  338                                                                
CONECT  340  337  341                                                           
CONECT  341  340  342                                                           
CONECT  342  341  343                                                           
CONECT  343  342                                                                
CONECT  344  338                                                                
CONECT  411  419                                                                
CONECT  419  411  420                                                           
CONECT  420  419  421  423                                                      
CONECT  421  420  422  427                                                      
CONECT  422  421                                                                
CONECT  423  420  424                                                           
CONECT  424  423  425                                                           
CONECT  425  424  426                                                           
CONECT  426  425                                                                
CONECT  427  421                                                                
CONECT  600  602                                                                
CONECT  602  600  603                                                           
CONECT  603  602  604  606                                                      
CONECT  604  603  605  610                                                      
CONECT  605  604                                                                
CONECT  606  603  607                                                           
CONECT  607  606  608                                                           
CONECT  608  607  609                                                           
CONECT  609  608                                                                
CONECT  610  604                                                                
CONECT  936  942                                                                
CONECT  942  936  943                                                           
CONECT  943  942  944  946                                                      
CONECT  944  943  945  950                                                      
CONECT  945  944                                                                
CONECT  946  943  947                                                           
CONECT  947  946  948                                                           
CONECT  948  947  949                                                           
CONECT  949  948                                                                
CONECT  950  944                                                                
CONECT 1139 1145                                                                
CONECT 1145 1139 1146                                                           
CONECT 1146 1145 1147 1149                                                      
CONECT 1147 1146 1148 1153                                                      
CONECT 1148 1147                                                                
CONECT 1149 1146 1150                                                           
CONECT 1150 1149 1151                                                           
CONECT 1151 1150 1152                                                           
CONECT 1152 1151                                                                
CONECT 1153 1147                                                                
CONECT 1368 1373                                                                
CONECT 1373 1368 1374                                                           
CONECT 1374 1373 1375 1377                                                      
CONECT 1375 1374 1376 1381                                                      
CONECT 1376 1375                                                                
CONECT 1377 1374 1378                                                           
CONECT 1378 1377 1379                                                           
CONECT 1379 1378 1380                                                           
CONECT 1380 1379                                                                
CONECT 1381 1375                                                                
CONECT 1773 1782                                                                
CONECT 1782 1773 1783                                                           
CONECT 1783 1782 1784 1786                                                      
CONECT 1784 1783 1785 1790                                                      
CONECT 1785 1784                                                                
CONECT 1786 1783 1787                                                           
CONECT 1787 1786 1788                                                           
CONECT 1788 1787 1789                                                           
CONECT 1789 1788                                                                
CONECT 1790 1784                                                                
CONECT 1813 1893                                                                
CONECT 1893 1813                                                                
CONECT 1923 1932                                                                
CONECT 1932 1923 1933                                                           
CONECT 1933 1932 1934 1936                                                      
CONECT 1934 1933 1935 1940                                                      
CONECT 1935 1934                                                                
CONECT 1936 1933 1937                                                           
CONECT 1937 1936 1938                                                           
CONECT 1938 1937 1939                                                           
CONECT 1939 1938                                                                
CONECT 1940 1934                                                                
CONECT 2311 2314                                                                
CONECT 2314 2311 2315                                                           
CONECT 2315 2314 2316 2318                                                      
CONECT 2316 2315 2317 2322                                                      
CONECT 2317 2316                                                                
CONECT 2318 2315 2319                                                           
CONECT 2319 2318 2320                                                           
CONECT 2320 2319 2321                                                           
CONECT 2321 2320                                                                
CONECT 2322 2316                                                                
CONECT 2547 2552                                                                
CONECT 2552 2547 2553                                                           
CONECT 2553 2552 2554 2556                                                      
CONECT 2554 2553 2555 2560                                                      
CONECT 2555 2554                                                                
CONECT 2556 2553 2557                                                           
CONECT 2557 2556 2558                                                           
CONECT 2558 2557 2559                                                           
CONECT 2559 2558                                                                
CONECT 2560 2554                                                                
CONECT 2736 2741                                                                
CONECT 2741 2736 2742                                                           
CONECT 2742 2741 2743 2745                                                      
CONECT 2743 2742 2744 2749                                                      
CONECT 2744 2743                                                                
CONECT 2745 2742 2746                                                           
CONECT 2746 2745 2747                                                           
CONECT 2747 2746 2748                                                           
CONECT 2748 2747                                                                
CONECT 2749 2743                                                                
CONECT 2767 2773                                                                
CONECT 2773 2767 2774                                                           
CONECT 2774 2773 2775 2777                                                      
CONECT 2775 2774 2776 2781                                                      
CONECT 2776 2775                                                                
CONECT 2777 2774 2778                                                           
CONECT 2778 2777 2779                                                           
CONECT 2779 2778 2780                                                           
CONECT 2780 2779                                                                
CONECT 2781 2775                                                                
CONECT 2808 2809                                                                
CONECT 2809 2808 2810 2812                                                      
CONECT 2810 2809 2811 2816                                                      
CONECT 2811 2810                                                                
CONECT 2812 2809 2813                                                           
CONECT 2813 2812 2814                                                           
CONECT 2814 2813 2815                                                           
CONECT 2815 2814                                                                
CONECT 2816 2810                                                                
CONECT 3145 3151                                                                
CONECT 3151 3145 3152                                                           
CONECT 3152 3151 3153 3155                                                      
CONECT 3153 3152 3154 3159                                                      
CONECT 3154 3153                                                                
CONECT 3155 3152 3156                                                           
CONECT 3156 3155 3157                                                           
CONECT 3157 3156 3158                                                           
CONECT 3158 3157                                                                
CONECT 3159 3153                                                                
CONECT 3191 3199                                                                
CONECT 3199 3191 3200                                                           
CONECT 3200 3199 3201 3203                                                      
CONECT 3201 3200 3202 3207                                                      
CONECT 3202 3201                                                                
CONECT 3203 3200 3204                                                           
CONECT 3204 3203 3205                                                           
CONECT 3205 3204 3206                                                           
CONECT 3206 3205                                                                
CONECT 3207 3201                                                                
CONECT 3380 3382                                                                
CONECT 3382 3380 3383                                                           
CONECT 3383 3382 3384 3386                                                      
CONECT 3384 3383 3385 3390                                                      
CONECT 3385 3384                                                                
CONECT 3386 3383 3387                                                           
CONECT 3387 3386 3388                                                           
CONECT 3388 3387 3389                                                           
CONECT 3389 3388                                                                
CONECT 3390 3384                                                                
CONECT 3716 3722                                                                
CONECT 3722 3716 3723                                                           
CONECT 3723 3722 3724 3726                                                      
CONECT 3724 3723 3725 3730                                                      
CONECT 3725 3724                                                                
CONECT 3726 3723 3727                                                           
CONECT 3727 3726 3728                                                           
CONECT 3728 3727 3729                                                           
CONECT 3729 3728                                                                
CONECT 3730 3724                                                                
CONECT 3919 3925                                                                
CONECT 3925 3919 3926                                                           
CONECT 3926 3925 3927 3929                                                      
CONECT 3927 3926 3928 3933                                                      
CONECT 3928 3927                                                                
CONECT 3929 3926 3930                                                           
CONECT 3930 3929 3931                                                           
CONECT 3931 3930 3932                                                           
CONECT 3932 3931                                                                
CONECT 3933 3927                                                                
CONECT 4148 4153                                                                
CONECT 4153 4148 4154                                                           
CONECT 4154 4153 4155 4157                                                      
CONECT 4155 4154 4156 4161                                                      
CONECT 4156 4155                                                                
CONECT 4157 4154 4158                                                           
CONECT 4158 4157 4159                                                           
CONECT 4159 4158 4160                                                           
CONECT 4160 4159                                                                
CONECT 4161 4155                                                                
CONECT 4553 4562                                                                
CONECT 4562 4553 4563                                                           
CONECT 4563 4562 4564 4566                                                      
CONECT 4564 4563 4565 4570                                                      
CONECT 4565 4564                                                                
CONECT 4566 4563 4567                                                           
CONECT 4567 4566 4568                                                           
CONECT 4568 4567 4569                                                           
CONECT 4569 4568                                                                
CONECT 4570 4564                                                                
CONECT 4593 4673                                                                
CONECT 4673 4593                                                                
CONECT 4703 4712                                                                
CONECT 4712 4703 4713                                                           
CONECT 4713 4712 4714 4716                                                      
CONECT 4714 4713 4715 4720                                                      
CONECT 4715 4714                                                                
CONECT 4716 4713 4717                                                           
CONECT 4717 4716 4718                                                           
CONECT 4718 4717 4719                                                           
CONECT 4719 4718                                                                
CONECT 4720 4714                                                                
CONECT 5105 5108                                                                
CONECT 5108 5105 5109                                                           
CONECT 5109 5108 5110 5112                                                      
CONECT 5110 5109 5111 5116                                                      
CONECT 5111 5110                                                                
CONECT 5112 5109 5113                                                           
CONECT 5113 5112 5114                                                           
CONECT 5114 5113 5115                                                           
CONECT 5115 5114                                                                
CONECT 5116 5110                                                                
CONECT 5325 5330                                                                
CONECT 5330 5325 5331                                                           
CONECT 5331 5330 5332 5334                                                      
CONECT 5332 5331 5333 5338                                                      
CONECT 5333 5332                                                                
CONECT 5334 5331 5335                                                           
CONECT 5335 5334 5336                                                           
CONECT 5336 5335 5337                                                           
CONECT 5337 5336                                                                
CONECT 5338 5332                                                                
CONECT 5514 5519                                                                
CONECT 5519 5514 5520                                                           
CONECT 5520 5519 5521 5523                                                      
CONECT 5521 5520 5522 5527                                                      
CONECT 5522 5521                                                                
CONECT 5523 5520 5524                                                           
CONECT 5524 5523 5525                                                           
CONECT 5525 5524 5526                                                           
CONECT 5526 5525                                                                
CONECT 5527 5521                                                                
CONECT 5545 5551                                                                
CONECT 5551 5545 5552                                                           
CONECT 5552 5551 5553 5555                                                      
CONECT 5553 5552 5554 5559                                                      
CONECT 5554 5553                                                                
CONECT 5555 5552 5556                                                           
CONECT 5556 5555 5557                                                           
CONECT 5557 5556 5558                                                           
CONECT 5558 5557                                                                
CONECT 5559 5553                                                                
MASTER      425    0   25   34   32    0    0    6 5667    2  253   64          
END                                                                             
