HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   14-APR-08   3CTU              
OBSLTE     27-OCT-09 3CTU      3K6E                                             
TITLE     CRYSTAL STRUCTURE OF CBS DOMAIN PROTEIN FROM STREPTOCOCCUS            
TITLE    2 PNEUMONIAE TIGR4                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CBS DOMAIN PROTEIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE TIGR4;                 
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 ATCC: BAA-334;                                                       
SOURCE   6 GENE: SP_1878;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) DERIVATIVE;                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    CBS DOMAIN PROTEIN, SP1878, STREPTOCOCCUS PNEUMONIAE TIGR4,           
KEYWDS   2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,            
KEYWDS   3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN                
KEYWDS   4 FUNCTION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,M.ZHOU,J.ABDULLAH,A.JOACHIMIAK,MIDWEST CENTER FOR             
AUTHOR   2 STRUCTURAL GENOMICS (MCSG)                                           
REVDAT   3   27-OCT-09 3CTU    1       OBSLTE                                   
REVDAT   2   24-FEB-09 3CTU    1       VERSN                                    
REVDAT   1   29-APR-08 3CTU    0                                                
JRNL        AUTH   C.CHANG,M.ZHOU,J.ABDULLAH,A.JOACHIMIAK                       
JRNL        TITL   CRYSTAL STRUCTURE OF CBS DOMAIN PROTEIN FROM                 
JRNL        TITL 2 STREPTOCOCCUS PNEUMONIAE TIGR4.                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 10820                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 520                             
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) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 669                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 42                           
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2292                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 77.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.50000                                              
REMARK   3    B22 (A**2) : -4.31000                                             
REMARK   3    B33 (A**2) : -2.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.981         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.382         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.367         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.002        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2350 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3201 ; 2.002 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   304 ; 0.691 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;12.204 ;25.700       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   403 ; 5.514 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 8.153 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   397 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1719 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1265 ; 0.318 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1711 ; 0.338 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   161 ; 0.244 ; 0.500       
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):    37 ; 0.433 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.249 ; 0.500       
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):  1528 ; 0.864 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2422 ; 1.463 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   892 ; 0.744 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   774 ; 1.223 ; 3.000       
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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -1        A    22                          
REMARK   3    RESIDUE RANGE :   A   123        A   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5620  47.7352  82.5458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2883 T22:  -0.1069                                     
REMARK   3      T33:  -0.2360 T12:  -0.0510                                     
REMARK   3      T13:   0.0368 T23:   0.0614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4332 L22:  13.3601                                     
REMARK   3      L33:   7.1614 L12:   0.9195                                     
REMARK   3      L13:  -1.2210 L23:  -8.0174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1107 S12:  -0.5563 S13:  -0.0604                       
REMARK   3      S21:   2.0191 S22:  -0.1917 S23:  -0.5433                       
REMARK   3      S31:  -1.3273 S32:   0.3627 S33:   0.3024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    23        A    92                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6887  64.9664  59.5155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0731 T22:  -0.1352                                     
REMARK   3      T33:   0.0582 T12:   0.0250                                     
REMARK   3      T13:   0.0283 T23:   0.0960                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5265 L22:   6.9751                                     
REMARK   3      L33:   8.7559 L12:  -0.6199                                     
REMARK   3      L13:   0.9983 L23:  -1.5405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2435 S12:   0.0043 S13:  -0.1163                       
REMARK   3      S21:   0.5088 S22:   0.1986 S23:   0.4312                       
REMARK   3      S31:  -0.6659 S32:  -0.3845 S33:  -0.4421                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    93        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8466  53.1808  77.0656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0958 T22:  -0.1618                                     
REMARK   3      T33:   0.0934 T12:   0.1362                                     
REMARK   3      T13:   0.3280 T23:   0.2606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5828 L22:  14.4512                                     
REMARK   3      L33:   6.3375 L12:  -0.1368                                     
REMARK   3      L13:   2.7955 L23:  -8.5148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0328 S12:  -0.4394 S13:  -0.2881                       
REMARK   3      S21:   1.4757 S22:   1.2351 S23:   2.2998                       
REMARK   3      S31:  -0.9377 S32:  -0.8556 S33:  -1.2023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -1        B    22                          
REMARK   3    RESIDUE RANGE :   B   123        B   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1410  35.3496  72.3682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0950 T22:  -0.1259                                     
REMARK   3      T33:   0.0029 T12:  -0.1087                                     
REMARK   3      T13:  -0.0673 T23:   0.1049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8652 L22:  13.0940                                     
REMARK   3      L33:  21.2109 L12:   1.0281                                     
REMARK   3      L13: -10.5892 L23:  -7.0547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3791 S12:  -0.0650 S13:  -0.1217                       
REMARK   3      S21:  -0.3032 S22:  -0.4884 S23:  -0.3978                       
REMARK   3      S31:   0.8460 S32:  -0.2925 S33:   0.8675                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    23        B    92                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7594  51.5655  50.0868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1374 T22:  -0.0404                                     
REMARK   3      T33:  -0.1350 T12:  -0.0601                                     
REMARK   3      T13:   0.0158 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2471 L22:  11.1810                                     
REMARK   3      L33:   9.2246 L12:   1.1805                                     
REMARK   3      L13:  -3.4279 L23:  -3.4869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3456 S12:   0.0308 S13:  -0.0584                       
REMARK   3      S21:  -0.5864 S22:   0.2763 S23:   0.2145                       
REMARK   3      S31:   0.7480 S32:  -0.3595 S33:   0.0693                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    93        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.6686  39.4966  66.7423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1183 T22:  -0.1686                                     
REMARK   3      T33:  -0.0523 T12:   0.0858                                     
REMARK   3      T13:   0.1414 T23:   0.2130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.7254 L22:   3.9749                                     
REMARK   3      L33:  16.1905 L12:  -0.5341                                     
REMARK   3      L13:  -6.2650 L23:  -2.2207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2306 S12:   0.1524 S13:   0.1799                       
REMARK   3      S21:  -1.0016 S22:  -0.4892 S23:  -1.0535                       
REMARK   3      S31:   0.6634 S32:   0.8453 S33:   0.2586                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED IN            
REMARK   3  PHASING. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS          
REMARK   4                                                                      
REMARK   4 3CTU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047201.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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) : 0.97933                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19974                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.5200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.230                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M NA/K PHOSPHATE, PH 5.6, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.60950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.80100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.58750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.80100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.60950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.58750            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    54                                                      
REMARK 465     PHE A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     LYS A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     TYR A   148                                                      
REMARK 465     GLU A   149                                                      
REMARK 465     ILE A   150                                                      
REMARK 465     ARG A   151                                                      
REMARK 465     CYS A   152                                                      
REMARK 465     GLN A   153                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ARG B   151                                                      
REMARK 465     CYS B   152                                                      
REMARK 465     GLN B   153                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A  44    OG1  CG2                                            
REMARK 470     TYR A  45    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A  50    CG1  CG2                                            
REMARK 470     VAL A  51    CG1  CG2                                            
REMARK 470     THR A  52    OG1  CG2                                            
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     ASP A  92    CG   OD1  OD2                                       
REMARK 470     ASP A 119    CG   OD1  OD2                                       
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 123    CG1  CG2  CD1                                       
REMARK 470     GLN A 125    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 133    CG1  CG2  CD1                                       
REMARK 470     ASN B  -1    CG   OD1  ND2                                       
REMARK 470     THR B  44    OG1  CG2                                            
REMARK 470     GLU B  78    CG   CD   OE1  OE2                                  
REMARK 470     SER B 145    OG                                                  
REMARK 470     GLU B 147    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 149    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 150    CG1  CG2  CD1                                       
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    ILE B   123     OE1  GLN B   125              1.95            
REMARK 500   NZ   LYS B    90     O    ASP B    92              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN B 125   CD    GLN B 125   OE1     0.374                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 109   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  -1       62.19   -106.88                                   
REMARK 500    GLU A  14      -30.75    -38.81                                   
REMARK 500    THR A  16       46.11    -93.75                                   
REMARK 500    LYS A  22      -29.41    -28.28                                   
REMARK 500    LEU A  24      118.15   -165.79                                   
REMARK 500    ASP A  29       -1.76    -47.98                                   
REMARK 500    ASN A  32      157.12    -48.21                                   
REMARK 500    ASP A  74       70.27     56.11                                   
REMARK 500    VAL A  86      -37.10    -34.13                                   
REMARK 500    ALA A 120       -8.75    -54.06                                   
REMARK 500    ILE A 133       14.33    -67.53                                   
REMARK 500    GLU B  14      -46.08    -28.15                                   
REMARK 500    GLU B  78      -34.94    -36.73                                   
REMARK 500    PRO B  98        6.40    -64.52                                   
REMARK 500    ALA B 120       16.85    -61.67                                   
REMARK 500    ASN B 138       -8.86    -59.30                                   
REMARK 500    TYR B 148        2.92    -66.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 154                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 154                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC80633   RELATED DB: TARGETDB                          
DBREF  3CTU A    1   153  UNP    Q9EUQ9   Q9EUQ9_STRPN     1    153             
DBREF  3CTU B    1   153  UNP    Q9EUQ9   Q9EUQ9_STRPN     1    153             
SEQADV 3CTU SER A   -2  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQADV 3CTU ASN A   -1  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQADV 3CTU ALA A    0  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQADV 3CTU SER B   -2  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQADV 3CTU ASN B   -1  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQADV 3CTU ALA B    0  UNP  Q9EUQ9              EXPRESSION TAG                 
SEQRES   1 A  156  SER ASN ALA MSE ILE ALA LYS GLU PHE GLU THR PHE LEU          
SEQRES   2 A  156  LEU GLY GLN GLU GLU THR PHE LEU THR PRO ALA LYS ASN          
SEQRES   3 A  156  LEU ALA VAL LEU ILE ASP THR HIS ASN ALA ASP HIS ALA          
SEQRES   4 A  156  THR LEU LEU LEU SER GLN MSE THR TYR THR ARG VAL PRO          
SEQRES   5 A  156  VAL VAL THR ASP GLU LYS GLN PHE VAL GLY THR ILE GLY          
SEQRES   6 A  156  LEU ARG ASP ILE MSE ALA TYR GLN MSE GLU HIS ASP LEU          
SEQRES   7 A  156  SER GLN GLU ILE MSE ALA ASP THR ASP ILE VAL HIS MSE          
SEQRES   8 A  156  THR LYS THR ASP VAL ALA VAL VAL SER PRO ASP PHE THR          
SEQRES   9 A  156  ILE THR GLU VAL LEU HIS LYS LEU VAL ASP GLU SER PHE          
SEQRES  10 A  156  LEU PRO VAL VAL ASP ALA GLU GLY ILE PHE GLN GLY ILE          
SEQRES  11 A  156  ILE THR ARG LYS SER ILE LEU LYS ALA VAL ASN ALA LEU          
SEQRES  12 A  156  LEU HIS ASP PHE SER LYS GLU TYR GLU ILE ARG CYS GLN          
SEQRES   1 B  156  SER ASN ALA MSE ILE ALA LYS GLU PHE GLU THR PHE LEU          
SEQRES   2 B  156  LEU GLY GLN GLU GLU THR PHE LEU THR PRO ALA LYS ASN          
SEQRES   3 B  156  LEU ALA VAL LEU ILE ASP THR HIS ASN ALA ASP HIS ALA          
SEQRES   4 B  156  THR LEU LEU LEU SER GLN MSE THR TYR THR ARG VAL PRO          
SEQRES   5 B  156  VAL VAL THR ASP GLU LYS GLN PHE VAL GLY THR ILE GLY          
SEQRES   6 B  156  LEU ARG ASP ILE MSE ALA TYR GLN MSE GLU HIS ASP LEU          
SEQRES   7 B  156  SER GLN GLU ILE MSE ALA ASP THR ASP ILE VAL HIS MSE          
SEQRES   8 B  156  THR LYS THR ASP VAL ALA VAL VAL SER PRO ASP PHE THR          
SEQRES   9 B  156  ILE THR GLU VAL LEU HIS LYS LEU VAL ASP GLU SER PHE          
SEQRES  10 B  156  LEU PRO VAL VAL ASP ALA GLU GLY ILE PHE GLN GLY ILE          
SEQRES  11 B  156  ILE THR ARG LYS SER ILE LEU LYS ALA VAL ASN ALA LEU          
SEQRES  12 B  156  LEU HIS ASP PHE SER LYS GLU TYR GLU ILE ARG CYS GLN          
MODRES 3CTU MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE A   43  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE A   67  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE A   71  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE A   80  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B   43  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B   67  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B   71  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B   80  MET  SELENOMETHIONINE                                   
MODRES 3CTU MSE B   88  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  43       8                                                       
HET    MSE  A  67       8                                                       
HET    MSE  A  71       8                                                       
HET    MSE  A  80       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  43       8                                                       
HET    MSE  B  67       8                                                       
HET    MSE  B  71       8                                                       
HET    MSE  B  80       8                                                       
HET    MSE  B  88       8                                                       
HET    PO4  B 154       5                                                       
HET    GOL  A 154       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GOL GLYCEROL                                                         
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *18(H2 O)                                                     
HELIX    1   1 ASN A   -1  GLY A   12  1                                  14    
HELIX    2   2 GLN A   13  THR A   16  5                                   4    
HELIX    3   3 LYS A   22  LEU A   24  5                                   3    
HELIX    4   4 ASN A   32  SER A   41  1                                  10    
HELIX    5   5 LEU A   63  ASP A   74  1                                  12    
HELIX    6   6 SER A   76  ALA A   81  1                                   6    
HELIX    7   7 ASP A   82  THR A   83  5                                   2    
HELIX    8   8 ASP A   84  THR A   89  5                                   6    
HELIX    9   9 THR A  101  LEU A  109  1                                   9    
HELIX   10  10 LYS A  131  LEU A  141  1                                  11    
HELIX   11  11 ALA B    0  GLY B   12  1                                  13    
HELIX   12  12 GLN B   13  PHE B   17  1                                   5    
HELIX   13  13 LYS B   22  LEU B   24  5                                   3    
HELIX   14  14 ASN B   32  SER B   41  1                                  10    
HELIX   15  15 GLY B   62  ASP B   74  1                                  13    
HELIX   16  16 SER B   76  ALA B   81  1                                   6    
HELIX   17  17 ASP B   82  THR B   83  5                                   2    
HELIX   18  18 ASP B   84  THR B   89  5                                   6    
HELIX   19  19 THR B  101  GLU B  112  1                                  12    
HELIX   20  20 ARG B  130  HIS B  142  1                                  13    
HELIX   21  21 LYS B  146  ILE B  150  5                                   5    
SHEET    1   A 3 LEU A  18  PRO A  20  0                                        
SHEET    2   A 3 PHE A 124  THR A 129 -1  O  ILE A 127   N  THR A  19           
SHEET    3   A 3 PHE A 114  VAL A 118 -1  N  LEU A 115   O  ILE A 128           
SHEET    1   B 3 LEU A  27  ILE A  28  0                                        
SHEET    2   B 3 ARG A  47  VAL A  51  1  O  VAL A  51   N  LEU A  27           
SHEET    3   B 3 PHE A  57  GLY A  62 -1  O  ILE A  61   N  VAL A  48           
SHEET    1   C 3 LEU B  18  PRO B  20  0                                        
SHEET    2   C 3 PHE B 124  THR B 129 -1  O  ILE B 127   N  THR B  19           
SHEET    3   C 3 PHE B 114  VAL B 118 -1  N  LEU B 115   O  ILE B 128           
SHEET    1   D 3 LEU B  27  ILE B  28  0                                        
SHEET    2   D 3 VAL B  48  VAL B  51  1  O  VAL B  51   N  LEU B  27           
SHEET    3   D 3 PHE B  57  ILE B  61 -1  O  GLY B  59   N  VAL B  50           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   ILE A   2     1555   1555  1.33  
LINK         C   GLN A  42                 N   MSE A  43     1555   1555  1.33  
LINK         C   ILE A  66                 N   MSE A  67     1555   1555  1.32  
LINK         C   MSE A  67                 N   ALA A  68     1555   1555  1.32  
LINK         C   GLN A  70                 N   MSE A  71     1555   1555  1.33  
LINK         C   MSE A  71                 N   GLU A  72     1555   1555  1.33  
LINK         C   ILE A  79                 N   MSE A  80     1555   1555  1.32  
LINK         C   MSE A  80                 N   ALA A  81     1555   1555  1.32  
LINK         C   HIS A  87                 N   MSE A  88     1555   1555  1.32  
LINK         C   MSE A  88                 N   THR A  89     1555   1555  1.32  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   ILE B   2     1555   1555  1.32  
LINK         C   GLN B  42                 N   MSE B  43     1555   1555  1.32  
LINK         C   ILE B  66                 N   MSE B  67     1555   1555  1.34  
LINK         C   MSE B  67                 N   ALA B  68     1555   1555  1.32  
LINK         C   GLN B  70                 N   MSE B  71     1555   1555  1.32  
LINK         C   MSE B  71                 N   GLU B  72     1555   1555  1.32  
LINK         C   ILE B  79                 N   MSE B  80     1555   1555  1.33  
LINK         C   MSE B  80                 N   ALA B  81     1555   1555  1.33  
LINK         C   HIS B  87                 N   MSE B  88     1555   1555  1.33  
LINK         C   MSE B  88                 N   THR B  89     1555   1555  1.32  
LINK         C   MSE A  43                 N   THR A  44     1555   1555  1.33  
LINK         C   MSE B  43                 N   THR B  44     1555   1555  1.32  
SITE     1 AC1  3 LYS A 131  ASP B 111  ARG B 130                               
SITE     1 AC2  7 LEU A  27  ILE A  28  HIS A  31  ASN A  32                    
SITE     2 AC2  7 HIS A  35  ALA A  36  THR B 101                               
CRYST1   55.219   85.175   91.602  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018110  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011741  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010917        0.00000                         
ATOM      1  N   SER A  -2      10.516  26.852  83.198  1.00 97.35           N  
ATOM      2  CA  SER A  -2      11.819  26.752  82.456  1.00 97.00           C  
ATOM      3  C   SER A  -2      13.061  27.139  83.329  1.00 96.64           C  
ATOM      4  O   SER A  -2      13.322  26.529  84.377  1.00 95.85           O  
ATOM      5  CB  SER A  -2      11.721  27.494  81.079  1.00 96.62           C  
ATOM      6  OG  SER A  -2      11.330  28.864  81.180  1.00 95.24           O  
ATOM      7  N   ASN A  -1      13.839  28.109  82.855  1.00 96.13           N  
ATOM      8  CA  ASN A  -1      15.019  28.602  83.559  1.00 94.51           C  
ATOM      9  C   ASN A  -1      14.600  29.979  84.089  1.00 93.65           C  
ATOM     10  O   ASN A  -1      15.112  31.040  83.727  1.00 92.25           O  
ATOM     11  CB  ASN A  -1      16.283  28.577  82.675  1.00 94.16           C  
ATOM     12  CG  ASN A  -1      16.125  29.352  81.360  1.00 92.84           C  
ATOM     13  OD1 ASN A  -1      15.099  29.961  81.096  1.00 92.76           O  
ATOM     14  ND2 ASN A  -1      17.149  29.305  80.531  1.00 92.00           N  
ATOM     15  N   ALA A   0      13.590  29.908  84.946  1.00 93.27           N  
ATOM     16  CA  ALA A   0      13.018  31.072  85.573  1.00 92.63           C  
ATOM     17  C   ALA A   0      13.920  31.613  86.664  1.00 91.94           C  
ATOM     18  O   ALA A   0      13.891  32.806  86.958  1.00 92.41           O  
ATOM     19  CB  ALA A   0      11.645  30.732  86.137  1.00 92.25           C  
HETATM   20  N   MSE A   1      14.749  30.751  87.242  1.00 90.93           N  
HETATM   21  CA  MSE A   1      15.629  31.208  88.304  1.00 89.89           C  
HETATM   22  C   MSE A   1      16.644  32.235  87.799  1.00 89.60           C  
HETATM   23  O   MSE A   1      16.902  33.240  88.468  1.00 89.46           O  
HETATM   24  CB  MSE A   1      16.329  30.050  89.007  1.00 89.15           C  
HETATM   25  CG  MSE A   1      17.090  30.538  90.218  1.00 88.87           C  
HETATM   26 SE   MSE A   1      15.857  31.336  91.539  0.50 87.61          SE  
HETATM   27  CE  MSE A   1      17.178  31.931  92.822  1.00 88.67           C  
ATOM     28  N   ILE A   2      17.213  32.009  86.621  1.00 89.33           N  
ATOM     29  CA  ILE A   2      18.180  32.980  86.120  1.00 88.99           C  
ATOM     30  C   ILE A   2      17.474  34.270  85.673  1.00 88.83           C  
ATOM     31  O   ILE A   2      18.022  35.362  85.820  1.00 88.90           O  
ATOM     32  CB  ILE A   2      19.104  32.415  85.008  1.00 88.92           C  
ATOM     33  CG1 ILE A   2      20.160  33.448  84.622  1.00 88.91           C  
ATOM     34  CG2 ILE A   2      18.307  31.979  83.792  1.00 88.73           C  
ATOM     35  CD1 ILE A   2      21.048  33.881  85.778  1.00 89.10           C  
ATOM     36  N   ALA A   3      16.250  34.146  85.159  1.00 88.27           N  
ATOM     37  CA  ALA A   3      15.506  35.316  84.711  1.00 87.67           C  
ATOM     38  C   ALA A   3      15.222  36.247  85.876  1.00 87.80           C  
ATOM     39  O   ALA A   3      15.076  37.447  85.698  1.00 88.24           O  
ATOM     40  CB  ALA A   3      14.219  34.907  84.052  1.00 87.40           C  
ATOM     41  N   LYS A   4      15.164  35.703  87.080  1.00 87.86           N  
ATOM     42  CA  LYS A   4      14.888  36.541  88.223  1.00 87.82           C  
ATOM     43  C   LYS A   4      16.219  37.111  88.679  1.00 87.48           C  
ATOM     44  O   LYS A   4      16.320  38.288  88.962  1.00 86.91           O  
ATOM     45  CB  LYS A   4      14.082  35.762  89.268  1.00 88.04           C  
ATOM     46  CG  LYS A   4      13.528  36.563  90.444  1.00 89.31           C  
ATOM     47  CD  LYS A   4      14.473  37.060  91.526  1.00 90.25           C  
ATOM     48  CE  LYS A   4      15.036  35.869  92.318  1.00 91.09           C  
ATOM     49  NZ  LYS A   4      15.886  36.257  93.482  1.00 90.95           N  
ATOM     50  N   GLU A   5      17.259  36.293  88.689  1.00 87.80           N  
ATOM     51  CA  GLU A   5      18.570  36.775  89.095  1.00 88.69           C  
ATOM     52  C   GLU A   5      19.018  37.923  88.180  1.00 88.47           C  
ATOM     53  O   GLU A   5      19.704  38.844  88.604  1.00 88.23           O  
ATOM     54  CB  GLU A   5      19.579  35.639  89.012  1.00 88.61           C  
ATOM     55  CG  GLU A   5      19.267  34.496  89.946  1.00 89.93           C  
ATOM     56  CD  GLU A   5      20.209  33.296  89.781  1.00 90.51           C  
ATOM     57  OE1 GLU A   5      20.120  32.350  90.598  1.00 91.53           O  
ATOM     58  OE2 GLU A   5      21.031  33.281  88.836  1.00 91.22           O  
ATOM     59  N   PHE A   6      18.604  37.871  86.922  1.00 88.88           N  
ATOM     60  CA  PHE A   6      18.965  38.891  85.943  1.00 88.97           C  
ATOM     61  C   PHE A   6      18.184  40.178  86.121  1.00 89.21           C  
ATOM     62  O   PHE A   6      18.727  41.272  85.983  1.00 89.28           O  
ATOM     63  CB  PHE A   6      18.823  38.306  84.535  1.00 89.61           C  
ATOM     64  CG  PHE A   6      19.144  39.266  83.415  1.00 90.26           C  
ATOM     65  CD1 PHE A   6      20.460  39.606  83.124  1.00 90.50           C  
ATOM     66  CD2 PHE A   6      18.148  39.708  82.555  1.00 90.24           C  
ATOM     67  CE1 PHE A   6      20.762  40.465  82.064  1.00 90.40           C  
ATOM     68  CE2 PHE A   6      18.445  40.547  81.482  1.00 89.88           C  
ATOM     69  CZ  PHE A   6      19.751  40.923  81.239  1.00 90.02           C  
ATOM     70  N   GLU A   7      16.907  40.043  86.438  1.00 89.37           N  
ATOM     71  CA  GLU A   7      16.059  41.193  86.643  1.00 89.65           C  
ATOM     72  C   GLU A   7      16.678  41.930  87.818  1.00 88.98           C  
ATOM     73  O   GLU A   7      16.997  43.106  87.724  1.00 88.99           O  
ATOM     74  CB  GLU A   7      14.655  40.720  86.998  1.00 90.18           C  
ATOM     75  CG  GLU A   7      13.581  41.794  87.170  1.00 91.07           C  
ATOM     76  CD  GLU A   7      12.229  41.185  87.600  1.00 91.94           C  
ATOM     77  OE1 GLU A   7      11.240  41.940  87.733  1.00 92.47           O  
ATOM     78  OE2 GLU A   7      12.155  39.943  87.827  1.00 93.59           O  
ATOM     79  N   THR A   8      16.876  41.217  88.924  1.00 89.11           N  
ATOM     80  CA  THR A   8      17.463  41.810  90.119  1.00 88.57           C  
ATOM     81  C   THR A   8      18.676  42.615  89.739  1.00 88.34           C  
ATOM     82  O   THR A   8      18.718  43.813  89.980  1.00 88.49           O  
ATOM     83  CB  THR A   8      17.846  40.766  91.177  1.00 88.55           C  
ATOM     84  OG1 THR A   8      16.662  40.115  91.642  1.00 88.58           O  
ATOM     85  CG2 THR A   8      18.484  41.444  92.363  1.00 88.86           C  
ATOM     86  N   PHE A   9      19.647  41.969  89.109  1.00 88.39           N  
ATOM     87  CA  PHE A   9      20.858  42.672  88.704  1.00 88.67           C  
ATOM     88  C   PHE A   9      20.523  43.948  87.916  1.00 89.50           C  
ATOM     89  O   PHE A   9      21.117  44.989  88.163  1.00 90.25           O  
ATOM     90  CB  PHE A   9      21.827  41.755  87.945  1.00 87.92           C  
ATOM     91  CG  PHE A   9      23.124  42.413  87.580  1.00 87.43           C  
ATOM     92  CD1 PHE A   9      24.186  42.413  88.476  1.00 87.16           C  
ATOM     93  CD2 PHE A   9      23.293  43.019  86.341  1.00 87.49           C  
ATOM     94  CE1 PHE A   9      25.396  43.018  88.162  1.00 87.14           C  
ATOM     95  CE2 PHE A   9      24.504  43.629  86.011  1.00 87.75           C  
ATOM     96  CZ  PHE A   9      25.562  43.625  86.931  1.00 87.66           C  
ATOM     97  N   LEU A  10      19.576  43.891  86.984  1.00 90.12           N  
ATOM     98  CA  LEU A  10      19.234  45.100  86.225  1.00 90.54           C  
ATOM     99  C   LEU A  10      18.711  46.266  87.039  1.00 91.48           C  
ATOM    100  O   LEU A  10      19.149  47.384  86.801  1.00 91.94           O  
ATOM    101  CB  LEU A  10      18.319  44.822  85.038  1.00 90.46           C  
ATOM    102  CG  LEU A  10      18.982  44.026  83.932  1.00 90.48           C  
ATOM    103  CD1 LEU A  10      17.999  43.748  82.831  1.00 90.69           C  
ATOM    104  CD2 LEU A  10      20.149  44.854  83.413  1.00 90.21           C  
ATOM    105  N   LEU A  11      17.776  46.053  87.967  1.00 92.43           N  
ATOM    106  CA  LEU A  11      17.305  47.205  88.735  1.00 93.41           C  
ATOM    107  C   LEU A  11      18.497  47.839  89.429  1.00 94.54           C  
ATOM    108  O   LEU A  11      18.401  48.939  89.967  1.00 95.03           O  
ATOM    109  CB  LEU A  11      16.150  46.924  89.709  1.00 93.28           C  
ATOM    110  CG  LEU A  11      14.783  46.484  89.174  1.00 93.31           C  
ATOM    111  CD1 LEU A  11      14.895  45.166  88.454  1.00 93.31           C  
ATOM    112  CD2 LEU A  11      13.762  46.368  90.295  1.00 93.24           C  
ATOM    113  N   GLY A  12      19.625  47.136  89.386  1.00 95.84           N  
ATOM    114  CA  GLY A  12      20.862  47.604  89.989  1.00 97.80           C  
ATOM    115  C   GLY A  12      21.315  48.863  89.270  1.00 99.69           C  
ATOM    116  O   GLY A  12      21.936  49.730  89.881  1.00 99.92           O  
ATOM    117  N   GLN A  13      21.014  48.956  87.968  1.00101.54           N  
ATOM    118  CA  GLN A  13      21.378  50.125  87.136  1.00103.37           C  
ATOM    119  C   GLN A  13      20.202  50.934  86.609  1.00104.52           C  
ATOM    120  O   GLN A  13      20.411  51.939  85.937  1.00104.75           O  
ATOM    121  CB  GLN A  13      22.309  49.788  85.954  1.00103.81           C  
ATOM    122  CG  GLN A  13      23.699  49.329  86.325  1.00104.62           C  
ATOM    123  CD  GLN A  13      23.694  48.057  87.114  1.00105.44           C  
ATOM    124  OE1 GLN A  13      22.719  47.302  87.079  1.00105.93           O  
ATOM    125  NE2 GLN A  13      24.803  47.778  87.801  1.00105.71           N  
ATOM    126  N   GLU A  14      18.979  50.499  86.908  1.00106.05           N  
ATOM    127  CA  GLU A  14      17.764  51.192  86.455  1.00107.56           C  
ATOM    128  C   GLU A  14      17.963  52.710  86.525  1.00107.77           C  
ATOM    129  O   GLU A  14      17.418  53.479  85.721  1.00107.67           O  
ATOM    130  CB  GLU A  14      16.574  50.771  87.319  1.00107.76           C  
ATOM    131  CG  GLU A  14      15.239  51.350  86.893  1.00108.61           C  
ATOM    132  CD  GLU A  14      14.105  50.906  87.802  1.00109.11           C  
ATOM    133  OE1 GLU A  14      14.389  50.315  88.868  1.00109.93           O  
ATOM    134  OE2 GLU A  14      12.928  51.172  87.471  1.00109.89           O  
ATOM    135  N   GLU A  15      18.786  53.102  87.492  1.00108.04           N  
ATOM    136  CA  GLU A  15      19.145  54.476  87.783  1.00108.00           C  
ATOM    137  C   GLU A  15      19.976  55.054  86.636  1.00107.23           C  
ATOM    138  O   GLU A  15      19.659  56.109  86.073  1.00107.13           O  
ATOM    139  CB  GLU A  15      20.036  54.454  89.026  1.00109.05           C  
ATOM    140  CG  GLU A  15      19.455  53.670  90.218  1.00110.29           C  
ATOM    141  CD  GLU A  15      18.146  54.218  90.765  1.00111.07           C  
ATOM    142  OE1 GLU A  15      17.489  53.489  91.541  1.00111.44           O  
ATOM    143  OE2 GLU A  15      17.761  55.354  90.410  1.00111.60           O  
ATOM    144  N   THR A  16      21.033  54.322  86.284  1.00106.17           N  
ATOM    145  CA  THR A  16      21.963  54.719  85.217  1.00104.66           C  
ATOM    146  C   THR A  16      21.761  54.212  83.775  1.00102.96           C  
ATOM    147  O   THR A  16      22.703  53.732  83.142  1.00102.42           O  
ATOM    148  CB  THR A  16      23.428  54.462  85.640  1.00105.09           C  
ATOM    149  OG1 THR A  16      23.623  53.057  85.862  1.00105.36           O  
ATOM    150  CG2 THR A  16      23.770  55.257  86.919  1.00104.92           C  
ATOM    151  N   PHE A  17      20.532  54.277  83.279  1.00101.27           N  
ATOM    152  CA  PHE A  17      20.250  53.859  81.914  1.00 99.28           C  
ATOM    153  C   PHE A  17      19.818  55.110  81.169  1.00 98.09           C  
ATOM    154  O   PHE A  17      19.959  55.211  79.946  1.00 98.52           O  
ATOM    155  CB  PHE A  17      19.112  52.862  81.776  1.00 99.20           C  
ATOM    156  CG  PHE A  17      19.348  51.544  82.416  1.00 99.23           C  
ATOM    157  CD1 PHE A  17      20.215  50.634  81.836  1.00 99.43           C  
ATOM    158  CD2 PHE A  17      18.560  51.124  83.453  1.00 99.31           C  
ATOM    159  CE1 PHE A  17      20.405  49.383  82.375  1.00 98.95           C  
ATOM    160  CE2 PHE A  17      18.731  49.863  83.985  1.00 99.50           C  
ATOM    161  CZ  PHE A  17      19.660  48.994  83.442  1.00 99.22           C  
ATOM    162  N   LEU A  18      19.265  56.055  81.923  1.00 96.08           N  
ATOM    163  CA  LEU A  18      18.798  57.297  81.355  1.00 94.02           C  
ATOM    164  C   LEU A  18      19.930  58.185  80.858  1.00 92.62           C  
ATOM    165  O   LEU A  18      20.896  58.443  81.575  1.00 92.22           O  
ATOM    166  CB  LEU A  18      17.942  58.066  82.368  1.00 93.97           C  
ATOM    167  CG  LEU A  18      17.377  59.423  81.913  1.00 93.94           C  
ATOM    168  CD1 LEU A  18      16.496  59.270  80.696  1.00 94.14           C  
ATOM    169  CD2 LEU A  18      16.589  60.098  83.011  1.00 94.04           C  
ATOM    170  N   THR A  19      19.824  58.598  79.600  1.00 90.80           N  
ATOM    171  CA  THR A  19      20.808  59.469  79.010  1.00 89.45           C  
ATOM    172  C   THR A  19      20.114  60.810  79.133  1.00 89.32           C  
ATOM    173  O   THR A  19      19.038  61.023  78.562  1.00 88.87           O  
ATOM    174  CB  THR A  19      21.148  59.123  77.569  1.00 88.99           C  
ATOM    175  OG1 THR A  19      21.787  57.849  77.538  1.00 88.73           O  
ATOM    176  CG2 THR A  19      22.123  60.129  77.009  1.00 88.73           C  
ATOM    177  N   PRO A  20      20.713  61.706  79.925  1.00 89.27           N  
ATOM    178  CA  PRO A  20      20.154  63.010  80.144  1.00 89.07           C  
ATOM    179  C   PRO A  20      20.029  63.778  78.861  1.00 89.29           C  
ATOM    180  O   PRO A  20      20.978  63.852  78.069  1.00 88.87           O  
ATOM    181  CB  PRO A  20      21.194  63.692  81.038  1.00 89.12           C  
ATOM    182  CG  PRO A  20      21.942  62.593  81.673  1.00 89.08           C  
ATOM    183  CD  PRO A  20      21.989  61.530  80.637  1.00 89.29           C  
ATOM    184  N   ALA A  21      18.842  64.327  78.655  1.00 89.47           N  
ATOM    185  CA  ALA A  21      18.591  65.108  77.480  1.00 89.60           C  
ATOM    186  C   ALA A  21      19.527  66.305  77.636  1.00 89.81           C  
ATOM    187  O   ALA A  21      20.245  66.669  76.710  1.00 89.00           O  
ATOM    188  CB  ALA A  21      17.141  65.566  77.459  1.00 88.83           C  
ATOM    189  N   LYS A  22      19.547  66.856  78.854  1.00 91.30           N  
ATOM    190  CA  LYS A  22      20.369  68.028  79.226  1.00 92.38           C  
ATOM    191  C   LYS A  22      21.641  68.145  78.400  1.00 92.45           C  
ATOM    192  O   LYS A  22      22.133  69.253  78.157  1.00 93.16           O  
ATOM    193  CB  LYS A  22      20.728  68.052  80.732  1.00 92.51           C  
ATOM    194  CG  LYS A  22      19.549  68.072  81.689  1.00 92.76           C  
ATOM    195  CD  LYS A  22      18.724  66.811  81.497  1.00 93.29           C  
ATOM    196  CE  LYS A  22      17.524  66.740  82.425  1.00 93.73           C  
ATOM    197  NZ  LYS A  22      16.733  65.483  82.194  1.00 93.57           N  
ATOM    198  N   ASN A  23      22.159  67.008  77.953  1.00 91.80           N  
ATOM    199  CA  ASN A  23      23.369  67.022  77.168  1.00 91.27           C  
ATOM    200  C   ASN A  23      23.228  65.835  76.195  1.00 90.59           C  
ATOM    201  O   ASN A  23      23.753  64.730  76.425  1.00 90.92           O  
ATOM    202  CB  ASN A  23      24.552  66.890  78.139  1.00 91.63           C  
ATOM    203  CG  ASN A  23      25.890  67.102  77.476  1.00 91.74           C  
ATOM    204  OD1 ASN A  23      25.965  67.445  76.292  1.00 91.90           O  
ATOM    205  ND2 ASN A  23      26.960  66.954  78.253  1.00 91.47           N  
ATOM    206  N   LEU A  24      22.483  66.088  75.114  1.00 88.93           N  
ATOM    207  CA  LEU A  24      22.206  65.108  74.083  1.00 87.16           C  
ATOM    208  C   LEU A  24      21.647  65.850  72.878  1.00 86.27           C  
ATOM    209  O   LEU A  24      20.576  66.445  72.972  1.00 86.59           O  
ATOM    210  CB  LEU A  24      21.125  64.180  74.619  1.00 87.48           C  
ATOM    211  CG  LEU A  24      20.559  63.027  73.795  1.00 87.54           C  
ATOM    212  CD1 LEU A  24      21.647  62.044  73.439  1.00 87.62           C  
ATOM    213  CD2 LEU A  24      19.484  62.335  74.605  1.00 87.65           C  
ATOM    214  N   ALA A  25      22.338  65.789  71.741  1.00 84.83           N  
ATOM    215  CA  ALA A  25      21.912  66.475  70.507  1.00 83.28           C  
ATOM    216  C   ALA A  25      20.580  66.032  69.890  1.00 82.70           C  
ATOM    217  O   ALA A  25      20.401  64.853  69.597  1.00 82.58           O  
ATOM    218  CB  ALA A  25      23.030  66.393  69.466  1.00 83.11           C  
ATOM    219  N   VAL A  26      19.667  66.981  69.661  1.00 82.36           N  
ATOM    220  CA  VAL A  26      18.346  66.681  69.066  1.00 82.26           C  
ATOM    221  C   VAL A  26      17.965  67.613  67.890  1.00 82.49           C  
ATOM    222  O   VAL A  26      18.718  68.525  67.558  1.00 82.59           O  
ATOM    223  CB  VAL A  26      17.233  66.769  70.112  1.00 81.95           C  
ATOM    224  CG1 VAL A  26      17.505  65.801  71.238  1.00 81.71           C  
ATOM    225  CG2 VAL A  26      17.139  68.173  70.654  1.00 81.59           C  
ATOM    226  N   LEU A  27      16.804  67.375  67.262  1.00 82.51           N  
ATOM    227  CA  LEU A  27      16.323  68.199  66.125  1.00 82.16           C  
ATOM    228  C   LEU A  27      14.928  68.725  66.366  1.00 83.33           C  
ATOM    229  O   LEU A  27      14.140  68.060  67.035  1.00 84.60           O  
ATOM    230  CB  LEU A  27      16.287  67.404  64.831  1.00 80.51           C  
ATOM    231  CG  LEU A  27      17.630  66.880  64.392  1.00 80.02           C  
ATOM    232  CD1 LEU A  27      17.498  66.152  63.108  1.00 80.26           C  
ATOM    233  CD2 LEU A  27      18.530  68.048  64.205  1.00 81.09           C  
ATOM    234  N   ILE A  28      14.612  69.895  65.804  1.00 84.01           N  
ATOM    235  CA  ILE A  28      13.284  70.509  65.967  1.00 84.72           C  
ATOM    236  C   ILE A  28      12.397  70.198  64.776  1.00 84.60           C  
ATOM    237  O   ILE A  28      12.778  70.459  63.633  1.00 85.07           O  
ATOM    238  CB  ILE A  28      13.367  72.038  66.057  1.00 85.86           C  
ATOM    239  CG1 ILE A  28      14.365  72.477  67.137  1.00 86.66           C  
ATOM    240  CG2 ILE A  28      11.972  72.643  66.258  1.00 86.03           C  
ATOM    241  CD1 ILE A  28      15.802  72.026  66.875  1.00 87.48           C  
ATOM    242  N   ASP A  29      11.199  69.688  65.042  1.00 84.32           N  
ATOM    243  CA  ASP A  29      10.248  69.332  63.976  1.00 84.47           C  
ATOM    244  C   ASP A  29      10.002  70.360  62.877  1.00 83.83           C  
ATOM    245  O   ASP A  29       9.239  70.097  61.953  1.00 84.39           O  
ATOM    246  CB  ASP A  29       8.912  68.936  64.581  1.00 85.42           C  
ATOM    247  CG  ASP A  29       8.336  70.034  65.433  1.00 86.68           C  
ATOM    248  OD1 ASP A  29       7.205  69.872  65.948  1.00 87.51           O  
ATOM    249  OD2 ASP A  29       9.026  71.068  65.593  1.00 87.12           O  
ATOM    250  N   THR A  30      10.626  71.526  62.958  1.00 82.69           N  
ATOM    251  CA  THR A  30      10.397  72.511  61.916  1.00 82.05           C  
ATOM    252  C   THR A  30      11.595  72.755  61.000  1.00 81.06           C  
ATOM    253  O   THR A  30      11.408  72.915  59.800  1.00 81.24           O  
ATOM    254  CB  THR A  30       9.840  73.843  62.460  1.00 82.51           C  
ATOM    255  OG1 THR A  30      10.793  74.432  63.355  1.00 83.19           O  
ATOM    256  CG2 THR A  30       8.506  73.611  63.175  1.00 82.20           C  
ATOM    257  N   HIS A  31      12.816  72.795  61.523  1.00 79.47           N  
ATOM    258  CA  HIS A  31      13.937  73.031  60.616  0.50 77.75           C  
ATOM    259  C   HIS A  31      13.895  72.061  59.445  1.00 76.77           C  
ATOM    260  O   HIS A  31      13.653  70.878  59.621  1.00 76.50           O  
ATOM    261  CB  HIS A  31      15.255  73.181  61.356  0.50 77.32           C  
ATOM    262  CG  HIS A  31      15.269  74.381  62.249  0.50 76.90           C  
ATOM    263  ND1 HIS A  31      14.805  74.352  63.546  0.50 76.56           N  
ATOM    264  CD2 HIS A  31      15.637  75.662  62.011  0.50 76.86           C  
ATOM    265  CE1 HIS A  31      14.915  75.554  64.078  0.50 76.38           C  
ATOM    266  NE2 HIS A  31      15.420  76.367  63.169  0.50 76.69           N  
ATOM    267  N   ASN A  32      14.073  72.613  58.247  1.00 76.12           N  
ATOM    268  CA  ASN A  32      14.034  71.876  56.978  1.00 75.16           C  
ATOM    269  C   ASN A  32      14.845  70.596  56.903  1.00 74.43           C  
ATOM    270  O   ASN A  32      15.821  70.411  57.622  1.00 73.33           O  
ATOM    271  CB  ASN A  32      14.379  72.806  55.808  1.00 75.36           C  
ATOM    272  CG  ASN A  32      15.821  73.223  55.807  1.00 75.23           C  
ATOM    273  OD1 ASN A  32      16.696  72.400  56.014  1.00 75.90           O  
ATOM    274  ND2 ASN A  32      16.085  74.459  55.433  1.00 75.64           N  
ATOM    275  N   ALA A  33      14.440  69.734  55.982  1.00 74.50           N  
ATOM    276  CA  ALA A  33      15.095  68.449  55.780  1.00 74.90           C  
ATOM    277  C   ALA A  33      16.482  68.502  55.149  1.00 75.65           C  
ATOM    278  O   ALA A  33      17.326  67.652  55.436  1.00 76.03           O  
ATOM    279  CB  ALA A  33      14.188  67.517  54.980  1.00 73.88           C  
ATOM    280  N   ASP A  34      16.734  69.481  54.289  1.00 76.52           N  
ATOM    281  CA  ASP A  34      18.041  69.539  53.678  1.00 76.81           C  
ATOM    282  C   ASP A  34      19.079  69.806  54.758  1.00 76.25           C  
ATOM    283  O   ASP A  34      20.156  69.212  54.786  1.00 76.47           O  
ATOM    284  CB  ASP A  34      18.102  70.621  52.631  1.00 78.17           C  
ATOM    285  CG  ASP A  34      19.440  70.653  51.926  1.00 79.62           C  
ATOM    286  OD1 ASP A  34      20.249  69.721  52.171  1.00 80.22           O  
ATOM    287  OD2 ASP A  34      19.674  71.582  51.109  1.00 80.13           O  
ATOM    288  N   HIS A  35      18.742  70.708  55.657  1.00 75.43           N  
ATOM    289  CA  HIS A  35      19.634  71.042  56.723  1.00 74.08           C  
ATOM    290  C   HIS A  35      19.779  69.856  57.660  1.00 73.27           C  
ATOM    291  O   HIS A  35      20.874  69.398  57.911  1.00 73.39           O  
ATOM    292  CB  HIS A  35      19.109  72.250  57.462  1.00 74.61           C  
ATOM    293  CG  HIS A  35      19.963  72.651  58.608  1.00 75.85           C  
ATOM    294  ND1 HIS A  35      21.032  73.511  58.470  1.00 76.03           N  
ATOM    295  CD2 HIS A  35      19.913  72.305  59.917  1.00 76.07           C  
ATOM    296  CE1 HIS A  35      21.601  73.681  59.651  1.00 76.63           C  
ATOM    297  NE2 HIS A  35      20.943  72.960  60.545  1.00 76.49           N  
ATOM    298  N   ALA A  36      18.676  69.329  58.167  1.00 72.36           N  
ATOM    299  CA  ALA A  36      18.769  68.195  59.072  1.00 71.09           C  
ATOM    300  C   ALA A  36      19.657  67.101  58.498  1.00 71.19           C  
ATOM    301  O   ALA A  36      20.477  66.510  59.198  1.00 71.76           O  
ATOM    302  CB  ALA A  36      17.413  67.652  59.368  1.00 70.19           C  
ATOM    303  N   THR A  37      19.496  66.833  57.213  1.00 71.04           N  
ATOM    304  CA  THR A  37      20.287  65.799  56.563  1.00 70.89           C  
ATOM    305  C   THR A  37      21.782  66.084  56.750  1.00 69.90           C  
ATOM    306  O   THR A  37      22.592  65.195  57.032  1.00 68.29           O  
ATOM    307  CB  THR A  37      19.858  65.635  55.089  1.00 70.86           C  
ATOM    308  OG1 THR A  37      20.696  64.675  54.447  1.00 70.92           O  
ATOM    309  CG2 THR A  37      20.006  66.916  54.382  1.00 71.50           C  
ATOM    310  N   LEU A  38      22.110  67.353  56.621  1.00 69.77           N  
ATOM    311  CA  LEU A  38      23.466  67.820  56.775  1.00 71.08           C  
ATOM    312  C   LEU A  38      24.012  67.623  58.189  1.00 70.95           C  
ATOM    313  O   LEU A  38      25.205  67.407  58.371  1.00 70.46           O  
ATOM    314  CB  LEU A  38      23.542  69.293  56.379  1.00 71.49           C  
ATOM    315  CG  LEU A  38      24.891  69.960  56.607  1.00 72.33           C  
ATOM    316  CD1 LEU A  38      26.052  69.126  56.015  1.00 72.81           C  
ATOM    317  CD2 LEU A  38      24.862  71.413  56.083  1.00 72.15           C  
ATOM    318  N   LEU A  39      23.147  67.707  59.192  1.00 71.49           N  
ATOM    319  CA  LEU A  39      23.605  67.528  60.563  1.00 71.62           C  
ATOM    320  C   LEU A  39      23.733  66.060  60.868  1.00 71.65           C  
ATOM    321  O   LEU A  39      24.700  65.629  61.473  1.00 71.52           O  
ATOM    322  CB  LEU A  39      22.712  68.241  61.580  1.00 71.16           C  
ATOM    323  CG  LEU A  39      22.645  69.764  61.500  1.00 71.45           C  
ATOM    324  CD1 LEU A  39      22.215  70.240  60.137  1.00 71.51           C  
ATOM    325  CD2 LEU A  39      21.713  70.319  62.564  1.00 71.81           C  
ATOM    326  N   LEU A  40      22.759  65.282  60.443  1.00 72.61           N  
ATOM    327  CA  LEU A  40      22.828  63.861  60.695  1.00 74.28           C  
ATOM    328  C   LEU A  40      24.014  63.206  59.978  1.00 75.23           C  
ATOM    329  O   LEU A  40      24.476  62.134  60.376  1.00 75.62           O  
ATOM    330  CB  LEU A  40      21.532  63.185  60.287  1.00 74.37           C  
ATOM    331  CG  LEU A  40      20.307  63.588  61.082  1.00 74.85           C  
ATOM    332  CD1 LEU A  40      19.148  62.863  60.521  1.00 75.57           C  
ATOM    333  CD2 LEU A  40      20.493  63.196  62.530  1.00 75.17           C  
ATOM    334  N   SER A  41      24.514  63.841  58.924  1.00 75.76           N  
ATOM    335  CA  SER A  41      25.638  63.262  58.212  1.00 76.30           C  
ATOM    336  C   SER A  41      26.965  63.491  58.960  1.00 76.97           C  
ATOM    337  O   SER A  41      28.021  63.025  58.540  1.00 76.85           O  
ATOM    338  CB  SER A  41      25.674  63.741  56.748  1.00 75.95           C  
ATOM    339  OG  SER A  41      25.800  65.147  56.644  1.00 76.41           O  
ATOM    340  N   GLN A  42      26.909  64.186  60.089  1.00 78.42           N  
ATOM    341  CA  GLN A  42      28.129  64.440  60.848  1.00 79.89           C  
ATOM    342  C   GLN A  42      27.969  64.089  62.335  1.00 79.55           C  
ATOM    343  O   GLN A  42      28.947  64.107  63.076  1.00 79.74           O  
ATOM    344  CB  GLN A  42      28.647  65.878  60.611  1.00 81.23           C  
ATOM    345  CG  GLN A  42      27.705  66.983  61.088  1.00 84.01           C  
ATOM    346  CD  GLN A  42      27.535  67.063  62.635  1.00 85.79           C  
ATOM    347  OE1 GLN A  42      26.426  67.340  63.133  1.00 86.35           O  
ATOM    348  NE2 GLN A  42      28.617  66.762  63.388  1.00 85.96           N  
HETATM  349  N   MSE A  43      26.747  63.771  62.759  1.00 79.33           N  
HETATM  350  CA  MSE A  43      26.474  63.407  64.151  1.00 80.12           C  
HETATM  351  C   MSE A  43      26.847  61.966  64.436  1.00 79.98           C  
HETATM  352  O   MSE A  43      26.661  61.101  63.589  1.00 80.01           O  
HETATM  353  CB  MSE A  43      25.003  63.578  64.458  1.00 80.43           C  
HETATM  354  CG  MSE A  43      24.566  64.993  64.375  1.00 81.43           C  
HETATM  355 SE   MSE A  43      22.641  65.179  64.621  0.50 81.60          SE  
HETATM  356  CE  MSE A  43      22.562  67.139  64.593  1.00 81.01           C  
ATOM    357  N   THR A  44      27.356  61.707  65.638  1.00 79.97           N  
ATOM    358  CA  THR A  44      27.752  60.355  66.027  1.00 79.98           C  
ATOM    359  C   THR A  44      26.586  59.336  66.012  1.00 80.14           C  
ATOM    360  O   THR A  44      26.716  58.264  65.433  1.00 79.65           O  
ATOM    361  CB  THR A  44      28.464  60.374  67.393  1.00 79.15           C  
ATOM    362  N   TYR A  45      25.451  59.676  66.626  1.00 80.48           N  
ATOM    363  CA  TYR A  45      24.301  58.764  66.667  1.00 80.89           C  
ATOM    364  C   TYR A  45      23.624  58.603  65.299  1.00 80.78           C  
ATOM    365  O   TYR A  45      23.676  59.510  64.481  1.00 80.46           O  
ATOM    366  CB  TYR A  45      23.303  59.211  67.740  1.00 81.14           C  
ATOM    367  N   THR A  46      22.992  57.452  65.056  1.00 80.97           N  
ATOM    368  CA  THR A  46      22.319  57.197  63.767  1.00 81.31           C  
ATOM    369  C   THR A  46      20.875  57.691  63.691  1.00 80.41           C  
ATOM    370  O   THR A  46      20.332  57.833  62.597  1.00 80.74           O  
ATOM    371  CB  THR A  46      22.317  55.695  63.370  1.00 82.28           C  
ATOM    372  OG1 THR A  46      21.494  54.934  64.277  1.00 82.78           O  
ATOM    373  CG2 THR A  46      23.751  55.142  63.304  1.00 82.54           C  
ATOM    374  N   ARG A  47      20.229  57.869  64.840  1.00 79.45           N  
ATOM    375  CA  ARG A  47      18.843  58.359  64.884  1.00 78.47           C  
ATOM    376  C   ARG A  47      18.790  59.339  66.023  1.00 76.54           C  
ATOM    377  O   ARG A  47      19.529  59.192  66.980  1.00 76.63           O  
ATOM    378  CB  ARG A  47      17.811  57.262  65.132  1.00 79.87           C  
ATOM    379  CG  ARG A  47      17.784  56.169  64.081  1.00 82.45           C  
ATOM    380  CD  ARG A  47      16.650  55.176  64.338  1.00 83.70           C  
ATOM    381  NE  ARG A  47      15.379  55.893  64.312  1.00 85.08           N  
ATOM    382  CZ  ARG A  47      14.670  56.106  63.207  1.00 85.84           C  
ATOM    383  NH1 ARG A  47      15.108  55.650  62.033  1.00 86.62           N  
ATOM    384  NH2 ARG A  47      13.527  56.776  63.278  1.00 86.00           N  
ATOM    385  N   VAL A  48      17.948  60.357  65.926  1.00 74.33           N  
ATOM    386  CA  VAL A  48      17.875  61.314  67.002  1.00 72.17           C  
ATOM    387  C   VAL A  48      16.455  61.724  67.275  1.00 71.72           C  
ATOM    388  O   VAL A  48      15.572  61.632  66.414  1.00 71.29           O  
ATOM    389  CB  VAL A  48      18.662  62.608  66.701  1.00 71.97           C  
ATOM    390  CG1 VAL A  48      20.114  62.294  66.409  1.00 72.29           C  
ATOM    391  CG2 VAL A  48      18.072  63.339  65.542  1.00 71.61           C  
ATOM    392  N   PRO A  49      16.228  62.180  68.497  1.00 71.61           N  
ATOM    393  CA  PRO A  49      14.916  62.629  68.914  1.00 72.14           C  
ATOM    394  C   PRO A  49      14.559  63.945  68.248  1.00 72.95           C  
ATOM    395  O   PRO A  49      15.441  64.747  67.941  1.00 72.59           O  
ATOM    396  CB  PRO A  49      15.086  62.876  70.416  1.00 71.77           C  
ATOM    397  CG  PRO A  49      16.440  62.357  70.791  1.00 71.02           C  
ATOM    398  CD  PRO A  49      17.241  62.258  69.562  1.00 70.94           C  
ATOM    399  N   VAL A  50      13.277  64.146  67.993  1.00 74.54           N  
ATOM    400  CA  VAL A  50      12.826  65.377  67.383  1.00 76.51           C  
ATOM    401  C   VAL A  50      11.980  66.026  68.480  1.00 78.50           C  
ATOM    402  O   VAL A  50      11.031  65.413  68.974  1.00 79.24           O  
ATOM    403  CB  VAL A  50      12.014  65.111  66.125  1.00 75.47           C  
ATOM    404  N   VAL A  51      12.359  67.226  68.919  1.00 80.73           N  
ATOM    405  CA  VAL A  51      11.618  67.941  69.970  1.00 82.52           C  
ATOM    406  C   VAL A  51      10.827  69.092  69.332  1.00 83.92           C  
ATOM    407  O   VAL A  51      11.321  69.725  68.394  1.00 84.26           O  
ATOM    408  CB  VAL A  51      12.563  68.448  71.051  1.00 82.12           C  
ATOM    409  N   THR A  52       9.602  69.333  69.822  1.00 85.29           N  
ATOM    410  CA  THR A  52       8.709  70.400  69.307  1.00 86.28           C  
ATOM    411  C   THR A  52       8.981  71.745  69.922  1.00 87.31           C  
ATOM    412  O   THR A  52       9.379  72.674  69.214  1.00 88.02           O  
ATOM    413  CB  THR A  52       7.232  70.043  69.505  1.00 86.12           C  
ATOM    414  N   ASP A  53       8.718  71.843  71.229  1.00 88.30           N  
ATOM    415  CA  ASP A  53       8.918  73.062  72.029  1.00 89.05           C  
ATOM    416  C   ASP A  53       7.591  73.693  72.433  1.00 88.69           C  
ATOM    417  O   ASP A  53       6.926  73.217  73.347  1.00 88.23           O  
ATOM    418  CB  ASP A  53       9.781  74.093  71.289  1.00 90.11           C  
ATOM    419  CG  ASP A  53      11.159  73.537  70.873  1.00 91.03           C  
ATOM    420  OD1 ASP A  53      11.443  72.318  71.064  1.00 90.71           O  
ATOM    421  OD2 ASP A  53      11.943  74.335  70.306  1.00 91.31           O  
ATOM    422  N   LYS A  55      10.038  72.199  75.094  1.00 73.01           N  
ATOM    423  CA  LYS A  55      10.623  71.071  74.367  1.00 73.78           C  
ATOM    424  C   LYS A  55       9.746  69.799  74.351  1.00 73.82           C  
ATOM    425  O   LYS A  55      10.061  68.787  74.999  1.00 73.70           O  
ATOM    426  CB  LYS A  55      12.047  70.761  74.876  1.00 73.51           C  
ATOM    427  N   GLN A  56       8.636  69.875  73.622  1.00 73.56           N  
ATOM    428  CA  GLN A  56       7.721  68.754  73.498  1.00 73.36           C  
ATOM    429  C   GLN A  56       8.330  67.632  72.697  1.00 73.83           C  
ATOM    430  O   GLN A  56       9.080  67.873  71.750  1.00 73.67           O  
ATOM    431  CB  GLN A  56       6.414  69.201  72.844  1.00 72.89           C  
ATOM    432  CG  GLN A  56       5.644  70.120  73.722  1.00 72.33           C  
ATOM    433  CD  GLN A  56       5.204  69.399  74.975  1.00 72.12           C  
ATOM    434  OE1 GLN A  56       5.012  70.004  76.018  1.00 72.19           O  
ATOM    435  NE2 GLN A  56       5.116  68.081  74.893  1.00 72.14           N  
ATOM    436  N   PHE A  57       8.063  66.398  73.111  1.00 74.58           N  
ATOM    437  CA  PHE A  57       8.598  65.268  72.374  1.00 74.79           C  
ATOM    438  C   PHE A  57       7.733  65.112  71.131  1.00 74.43           C  
ATOM    439  O   PHE A  57       6.503  65.205  71.211  1.00 74.74           O  
ATOM    440  CB  PHE A  57       8.639  63.971  73.191  1.00 75.22           C  
ATOM    441  CG  PHE A  57       9.073  62.778  72.374  1.00 75.72           C  
ATOM    442  CD1 PHE A  57      10.421  62.506  72.168  1.00 75.67           C  
ATOM    443  CD2 PHE A  57       8.121  61.938  71.789  1.00 75.63           C  
ATOM    444  CE1 PHE A  57      10.811  61.420  71.395  1.00 75.63           C  
ATOM    445  CE2 PHE A  57       8.503  60.857  71.017  1.00 75.41           C  
ATOM    446  CZ  PHE A  57       9.849  60.596  70.821  1.00 75.63           C  
ATOM    447  N   VAL A  58       8.371  64.900  69.983  1.00 73.37           N  
ATOM    448  CA  VAL A  58       7.625  64.743  68.747  1.00 72.40           C  
ATOM    449  C   VAL A  58       7.747  63.320  68.245  1.00 71.56           C  
ATOM    450  O   VAL A  58       6.744  62.647  68.046  1.00 71.65           O  
ATOM    451  CB  VAL A  58       8.121  65.701  67.642  1.00 72.52           C  
ATOM    452  CG1 VAL A  58       7.289  65.517  66.381  1.00 72.57           C  
ATOM    453  CG2 VAL A  58       8.030  67.133  68.101  1.00 72.03           C  
ATOM    454  N   GLY A  59       8.982  62.873  68.043  1.00 70.57           N  
ATOM    455  CA  GLY A  59       9.250  61.528  67.558  1.00 69.87           C  
ATOM    456  C   GLY A  59      10.740  61.287  67.407  1.00 69.45           C  
ATOM    457  O   GLY A  59      11.534  61.719  68.248  1.00 69.32           O  
ATOM    458  N   THR A  60      11.119  60.600  66.329  1.00 68.56           N  
ATOM    459  CA  THR A  60      12.522  60.290  66.053  1.00 67.45           C  
ATOM    460  C   THR A  60      12.767  60.279  64.545  1.00 66.58           C  
ATOM    461  O   THR A  60      11.849  59.974  63.798  1.00 66.18           O  
ATOM    462  CB  THR A  60      12.940  58.936  66.678  1.00 67.46           C  
ATOM    463  OG1 THR A  60      14.299  58.694  66.354  1.00 69.19           O  
ATOM    464  CG2 THR A  60      12.145  57.776  66.133  1.00 66.69           C  
ATOM    465  N   ILE A  61      13.968  60.632  64.079  1.00 65.79           N  
ATOM    466  CA  ILE A  61      14.204  60.621  62.632  1.00 66.63           C  
ATOM    467  C   ILE A  61      15.660  60.232  62.545  1.00 67.53           C  
ATOM    468  O   ILE A  61      16.410  60.369  63.517  1.00 67.43           O  
ATOM    469  CB  ILE A  61      14.202  62.054  61.926  1.00 66.40           C  
ATOM    470  CG1 ILE A  61      13.436  63.153  62.642  1.00 68.16           C  
ATOM    471  CG2 ILE A  61      14.043  62.030  60.425  1.00 65.28           C  
ATOM    472  CD1 ILE A  61      14.069  63.582  64.012  1.00 69.16           C  
ATOM    473  N   GLY A  62      16.066  59.749  61.377  1.00 68.05           N  
ATOM    474  CA  GLY A  62      17.443  59.344  61.127  1.00 68.10           C  
ATOM    475  C   GLY A  62      17.549  59.460  59.619  1.00 67.90           C  
ATOM    476  O   GLY A  62      16.528  59.707  58.956  1.00 67.40           O  
ATOM    477  N   LEU A  63      18.755  59.318  59.070  1.00 66.68           N  
ATOM    478  CA  LEU A  63      18.916  59.404  57.615  1.00 66.43           C  
ATOM    479  C   LEU A  63      17.976  58.471  56.863  1.00 67.83           C  
ATOM    480  O   LEU A  63      17.357  58.857  55.880  1.00 68.85           O  
ATOM    481  CB  LEU A  63      20.356  59.154  57.192  1.00 64.08           C  
ATOM    482  CG  LEU A  63      21.362  60.212  57.615  1.00 62.10           C  
ATOM    483  CD1 LEU A  63      22.759  59.759  57.325  1.00 61.05           C  
ATOM    484  CD2 LEU A  63      21.036  61.533  56.916  1.00 61.28           C  
ATOM    485  N   ARG A  64      17.870  57.243  57.331  1.00 69.60           N  
ATOM    486  CA  ARG A  64      17.007  56.269  56.714  1.00 71.35           C  
ATOM    487  C   ARG A  64      15.657  56.936  56.391  1.00 71.11           C  
ATOM    488  O   ARG A  64      15.171  56.882  55.264  1.00 69.85           O  
ATOM    489  CB  ARG A  64      16.815  55.148  57.715  1.00 73.78           C  
ATOM    490  CG  ARG A  64      15.949  54.009  57.284  1.00 77.10           C  
ATOM    491  CD  ARG A  64      15.761  53.073  58.501  1.00 79.90           C  
ATOM    492  NE  ARG A  64      14.833  51.980  58.219  1.00 81.85           N  
ATOM    493  CZ  ARG A  64      13.503  52.126  58.268  1.00 83.08           C  
ATOM    494  NH1 ARG A  64      12.974  53.339  58.487  1.00 83.69           N  
ATOM    495  NH2 ARG A  64      12.697  51.094  58.011  1.00 83.22           N  
ATOM    496  N   ASP A  65      15.064  57.588  57.383  1.00 71.59           N  
ATOM    497  CA  ASP A  65      13.780  58.261  57.199  1.00 72.25           C  
ATOM    498  C   ASP A  65      13.808  59.357  56.169  1.00 71.65           C  
ATOM    499  O   ASP A  65      12.880  59.514  55.379  1.00 71.43           O  
ATOM    500  CB  ASP A  65      13.336  58.905  58.505  1.00 74.14           C  
ATOM    501  CG  ASP A  65      13.056  57.900  59.587  1.00 76.38           C  
ATOM    502  OD1 ASP A  65      13.088  58.327  60.763  1.00 77.58           O  
ATOM    503  OD2 ASP A  65      12.840  56.693  59.279  1.00 77.27           O  
ATOM    504  N   ILE A  66      14.860  60.153  56.221  1.00 70.82           N  
ATOM    505  CA  ILE A  66      15.004  61.249  55.301  1.00 70.11           C  
ATOM    506  C   ILE A  66      15.282  60.763  53.909  1.00 69.48           C  
ATOM    507  O   ILE A  66      14.530  61.071  53.002  1.00 70.67           O  
ATOM    508  CB  ILE A  66      16.036  62.247  55.801  1.00 70.90           C  
ATOM    509  CG1 ILE A  66      15.503  62.877  57.089  1.00 71.01           C  
ATOM    510  CG2 ILE A  66      16.240  63.360  54.813  1.00 71.18           C  
ATOM    511  CD1 ILE A  66      16.412  63.889  57.708  1.00 70.90           C  
HETATM  512  N   MSE A  67      16.330  59.982  53.715  1.00 68.18           N  
HETATM  513  CA  MSE A  67      16.586  59.512  52.366  1.00 66.86           C  
HETATM  514  C   MSE A  67      15.425  58.705  51.842  1.00 65.65           C  
HETATM  515  O   MSE A  67      15.244  58.618  50.652  1.00 66.32           O  
HETATM  516  CB  MSE A  67      17.819  58.635  52.287  1.00 67.19           C  
HETATM  517  CG  MSE A  67      19.097  59.285  52.774  1.00 68.18           C  
HETATM  518 SE   MSE A  67      19.504  60.948  51.893  0.50 67.94          SE  
HETATM  519  CE  MSE A  67      18.054  62.044  52.527  1.00 67.08           C  
ATOM    520  N   ALA A  68      14.649  58.085  52.715  1.00 64.56           N  
ATOM    521  CA  ALA A  68      13.527  57.293  52.236  1.00 64.44           C  
ATOM    522  C   ALA A  68      12.522  58.206  51.582  1.00 63.48           C  
ATOM    523  O   ALA A  68      12.086  58.006  50.452  1.00 63.09           O  
ATOM    524  CB  ALA A  68      12.878  56.535  53.373  1.00 64.99           C  
ATOM    525  N   TYR A  69      12.172  59.229  52.324  1.00 62.83           N  
ATOM    526  CA  TYR A  69      11.225  60.215  51.878  1.00 62.75           C  
ATOM    527  C   TYR A  69      11.661  60.834  50.565  1.00 62.75           C  
ATOM    528  O   TYR A  69      10.893  60.906  49.609  1.00 63.23           O  
ATOM    529  CB  TYR A  69      11.149  61.291  52.944  1.00 61.63           C  
ATOM    530  CG  TYR A  69      10.216  62.398  52.635  1.00 61.17           C  
ATOM    531  CD1 TYR A  69       8.880  62.330  52.997  1.00 60.81           C  
ATOM    532  CD2 TYR A  69      10.680  63.535  52.006  1.00 61.39           C  
ATOM    533  CE1 TYR A  69       8.030  63.369  52.722  1.00 61.02           C  
ATOM    534  CE2 TYR A  69       9.853  64.578  51.725  1.00 61.16           C  
ATOM    535  CZ  TYR A  69       8.528  64.500  52.083  1.00 61.37           C  
ATOM    536  OH  TYR A  69       7.724  65.579  51.781  1.00 61.50           O  
ATOM    537  N   GLN A  70      12.912  61.257  50.524  1.00 62.42           N  
ATOM    538  CA  GLN A  70      13.454  61.873  49.350  1.00 62.82           C  
ATOM    539  C   GLN A  70      13.543  60.961  48.133  1.00 63.10           C  
ATOM    540  O   GLN A  70      13.250  61.404  47.029  1.00 63.14           O  
ATOM    541  CB  GLN A  70      14.798  62.470  49.677  1.00 63.55           C  
ATOM    542  CG  GLN A  70      15.404  63.190  48.538  1.00 65.29           C  
ATOM    543  CD  GLN A  70      16.705  63.788  48.935  1.00 66.86           C  
ATOM    544  OE1 GLN A  70      17.209  63.505  50.019  1.00 68.32           O  
ATOM    545  NE2 GLN A  70      17.282  64.607  48.063  1.00 67.70           N  
HETATM  546  N   MSE A  71      13.933  59.702  48.313  1.00 63.03           N  
HETATM  547  CA  MSE A  71      14.029  58.786  47.189  1.00 64.12           C  
HETATM  548  C   MSE A  71      12.656  58.335  46.734  1.00 64.54           C  
HETATM  549  O   MSE A  71      12.364  58.305  45.544  1.00 63.93           O  
HETATM  550  CB  MSE A  71      14.757  57.522  47.588  1.00 65.81           C  
HETATM  551  CG  MSE A  71      16.162  57.687  48.093  1.00 68.07           C  
HETATM  552 SE   MSE A  71      17.384  58.476  46.820  0.50 69.69          SE  
HETATM  553  CE  MSE A  71      17.336  57.189  45.387  1.00 68.68           C  
ATOM    554  N   GLU A  72      11.832  57.944  47.702  1.00 65.70           N  
ATOM    555  CA  GLU A  72      10.469  57.470  47.449  1.00 67.44           C  
ATOM    556  C   GLU A  72       9.649  58.483  46.731  1.00 65.76           C  
ATOM    557  O   GLU A  72       8.723  58.138  46.004  1.00 66.38           O  
ATOM    558  CB  GLU A  72       9.739  57.175  48.751  1.00 68.67           C  
ATOM    559  CG  GLU A  72      10.350  56.075  49.597  1.00 71.26           C  
ATOM    560  CD  GLU A  72       9.591  55.869  50.912  1.00 71.60           C  
ATOM    561  OE1 GLU A  72       9.906  54.878  51.645  1.00 72.43           O  
ATOM    562  OE2 GLU A  72       8.676  56.700  51.186  1.00 72.93           O  
ATOM    563  N   HIS A  73       9.951  59.744  46.976  1.00 64.09           N  
ATOM    564  CA  HIS A  73       9.210  60.786  46.326  1.00 62.50           C  
ATOM    565  C   HIS A  73      10.021  61.411  45.202  1.00 62.34           C  
ATOM    566  O   HIS A  73       9.475  62.146  44.402  1.00 62.43           O  
ATOM    567  CB  HIS A  73       8.687  61.782  47.344  1.00 61.74           C  
ATOM    568  CG  HIS A  73       7.796  61.155  48.374  1.00 61.30           C  
ATOM    569  ND1 HIS A  73       6.450  60.944  48.164  1.00 61.33           N  
ATOM    570  CD2 HIS A  73       8.053  60.710  49.626  1.00 61.08           C  
ATOM    571  CE1 HIS A  73       5.920  60.380  49.235  1.00 61.27           C  
ATOM    572  NE2 HIS A  73       6.872  60.232  50.139  1.00 61.05           N  
ATOM    573  N   ASP A  74      11.316  61.099  45.137  1.00 62.49           N  
ATOM    574  CA  ASP A  74      12.188  61.625  44.092  1.00 62.35           C  
ATOM    575  C   ASP A  74      12.132  63.143  44.107  1.00 61.74           C  
ATOM    576  O   ASP A  74      11.602  63.755  43.200  1.00 62.24           O  
ATOM    577  CB  ASP A  74      11.667  61.100  42.754  1.00 63.63           C  
ATOM    578  CG  ASP A  74      12.513  61.534  41.559  1.00 64.75           C  
ATOM    579  OD1 ASP A  74      13.738  61.802  41.720  1.00 64.64           O  
ATOM    580  OD2 ASP A  74      11.939  61.534  40.435  1.00 65.43           O  
ATOM    581  N   LEU A  75      12.699  63.751  45.135  1.00 62.29           N  
ATOM    582  CA  LEU A  75      12.706  65.207  45.294  1.00 62.08           C  
ATOM    583  C   LEU A  75      14.100  65.816  45.298  1.00 63.69           C  
ATOM    584  O   LEU A  75      15.034  65.300  45.905  1.00 63.06           O  
ATOM    585  CB  LEU A  75      12.059  65.528  46.631  1.00 60.52           C  
ATOM    586  CG  LEU A  75      10.620  65.086  46.873  1.00 59.24           C  
ATOM    587  CD1 LEU A  75      10.256  65.141  48.336  1.00 58.50           C  
ATOM    588  CD2 LEU A  75       9.664  65.856  45.979  1.00 58.39           C  
ATOM    589  N   SER A  76      14.219  66.947  44.629  1.00 66.22           N  
ATOM    590  CA  SER A  76      15.473  67.669  44.529  1.00 67.94           C  
ATOM    591  C   SER A  76      15.902  68.297  45.853  1.00 69.30           C  
ATOM    592  O   SER A  76      15.068  68.497  46.739  1.00 69.69           O  
ATOM    593  CB  SER A  76      15.251  68.782  43.527  1.00 68.23           C  
ATOM    594  OG  SER A  76      14.170  69.600  43.952  1.00 68.35           O  
ATOM    595  N   GLN A  77      17.194  68.611  45.987  1.00 70.70           N  
ATOM    596  CA  GLN A  77      17.703  69.235  47.213  1.00 71.80           C  
ATOM    597  C   GLN A  77      16.920  70.483  47.552  1.00 71.10           C  
ATOM    598  O   GLN A  77      16.669  70.788  48.703  1.00 70.38           O  
ATOM    599  CB  GLN A  77      19.200  69.552  47.106  1.00 73.88           C  
ATOM    600  CG  GLN A  77      20.062  68.310  47.051  1.00 77.16           C  
ATOM    601  CD  GLN A  77      19.950  67.465  48.348  1.00 79.59           C  
ATOM    602  OE1 GLN A  77      19.418  67.924  49.378  1.00 80.73           O  
ATOM    603  NE2 GLN A  77      20.492  66.241  48.311  1.00 80.70           N  
ATOM    604  N   GLU A  78      16.518  71.185  46.512  1.00 71.58           N  
ATOM    605  CA  GLU A  78      15.761  72.408  46.628  1.00 71.96           C  
ATOM    606  C   GLU A  78      14.424  72.181  47.313  1.00 71.38           C  
ATOM    607  O   GLU A  78      14.089  72.853  48.279  1.00 71.94           O  
ATOM    608  CB  GLU A  78      15.565  72.962  45.230  1.00 73.51           C  
ATOM    609  CG  GLU A  78      14.818  74.246  45.131  1.00 75.75           C  
ATOM    610  CD  GLU A  78      14.731  74.702  43.681  1.00 77.41           C  
ATOM    611  OE1 GLU A  78      15.262  73.972  42.798  1.00 78.16           O  
ATOM    612  OE2 GLU A  78      14.146  75.782  43.421  1.00 78.01           O  
ATOM    613  N   ILE A  79      13.656  71.227  46.818  1.00 70.55           N  
ATOM    614  CA  ILE A  79      12.357  70.935  47.403  1.00 69.53           C  
ATOM    615  C   ILE A  79      12.482  70.337  48.779  1.00 69.04           C  
ATOM    616  O   ILE A  79      11.602  70.489  49.630  1.00 68.57           O  
ATOM    617  CB  ILE A  79      11.560  69.954  46.512  1.00 69.08           C  
ATOM    618  CG1 ILE A  79      11.200  70.637  45.187  1.00 68.64           C  
ATOM    619  CG2 ILE A  79      10.285  69.535  47.196  1.00 68.55           C  
ATOM    620  CD1 ILE A  79      10.452  69.765  44.209  1.00 68.23           C  
HETATM  621  N   MSE A  80      13.623  69.714  49.015  1.00 69.03           N  
HETATM  622  CA  MSE A  80      13.885  69.055  50.281  1.00 68.31           C  
HETATM  623  C   MSE A  80      14.280  70.129  51.301  1.00 67.84           C  
HETATM  624  O   MSE A  80      14.072  69.990  52.493  1.00 67.83           O  
HETATM  625  CB  MSE A  80      15.015  68.076  50.028  1.00 68.13           C  
HETATM  626  CG  MSE A  80      15.163  66.975  51.017  1.00 69.30           C  
HETATM  627 SE   MSE A  80      13.542  65.873  50.852  0.50 68.39          SE  
HETATM  628  CE  MSE A  80      13.612  65.447  48.995  1.00 70.04           C  
ATOM    629  N   ALA A  81      14.819  71.234  50.814  1.00 67.93           N  
ATOM    630  CA  ALA A  81      15.233  72.318  51.694  1.00 67.95           C  
ATOM    631  C   ALA A  81      14.068  73.236  52.054  1.00 68.34           C  
ATOM    632  O   ALA A  81      14.243  74.278  52.700  1.00 67.37           O  
ATOM    633  CB  ALA A  81      16.331  73.112  51.033  1.00 67.11           C  
ATOM    634  N   ASP A  82      12.872  72.837  51.648  1.00 69.15           N  
ATOM    635  CA  ASP A  82      11.701  73.632  51.917  1.00 69.68           C  
ATOM    636  C   ASP A  82      10.673  72.684  52.472  1.00 69.83           C  
ATOM    637  O   ASP A  82       9.477  72.934  52.388  1.00 70.10           O  
ATOM    638  CB  ASP A  82      11.194  74.226  50.599  1.00 70.41           C  
ATOM    639  CG  ASP A  82      10.014  75.162  50.788  1.00 71.31           C  
ATOM    640  OD1 ASP A  82       9.808  75.626  51.927  1.00 71.92           O  
ATOM    641  OD2 ASP A  82       9.324  75.488  49.793  1.00 71.82           O  
ATOM    642  N   THR A  83      11.149  71.584  53.037  1.00 70.09           N  
ATOM    643  CA  THR A  83      10.269  70.577  53.606  1.00 70.48           C  
ATOM    644  C   THR A  83      10.582  70.306  55.078  1.00 72.15           C  
ATOM    645  O   THR A  83      11.706  69.909  55.405  1.00 73.20           O  
ATOM    646  CB  THR A  83      10.376  69.245  52.787  1.00 69.61           C  
ATOM    647  OG1 THR A  83       9.944  69.467  51.445  1.00 69.42           O  
ATOM    648  CG2 THR A  83       9.516  68.166  53.358  1.00 69.57           C  
ATOM    649  N   ASP A  84       9.611  70.542  55.967  1.00 73.57           N  
ATOM    650  CA  ASP A  84       9.795  70.295  57.413  1.00 74.89           C  
ATOM    651  C   ASP A  84       9.977  68.826  57.685  1.00 75.09           C  
ATOM    652  O   ASP A  84       9.282  67.988  57.113  1.00 75.60           O  
ATOM    653  CB  ASP A  84       8.595  70.734  58.264  1.00 75.53           C  
ATOM    654  CG  ASP A  84       8.372  72.213  58.252  1.00 76.14           C  
ATOM    655  OD1 ASP A  84       7.455  72.665  58.970  1.00 76.62           O  
ATOM    656  OD2 ASP A  84       9.127  72.924  57.556  1.00 76.84           O  
ATOM    657  N   ILE A  85      10.862  68.510  58.610  1.00 75.36           N  
ATOM    658  CA  ILE A  85      11.084  67.121  58.913  1.00 76.12           C  
ATOM    659  C   ILE A  85       9.858  66.434  59.468  1.00 76.78           C  
ATOM    660  O   ILE A  85       9.569  65.303  59.125  1.00 76.96           O  
ATOM    661  CB  ILE A  85      12.274  66.951  59.809  1.00 76.15           C  
ATOM    662  CG1 ILE A  85      12.076  67.764  61.085  1.00 76.84           C  
ATOM    663  CG2 ILE A  85      13.500  67.458  59.094  1.00 75.39           C  
ATOM    664  CD1 ILE A  85      13.259  67.654  62.053  1.00 77.05           C  
ATOM    665  N   VAL A  86       9.097  67.125  60.285  1.00 78.39           N  
ATOM    666  CA  VAL A  86       7.922  66.497  60.833  1.00 80.56           C  
ATOM    667  C   VAL A  86       7.251  65.511  59.862  1.00 82.20           C  
ATOM    668  O   VAL A  86       6.783  64.459  60.269  1.00 81.66           O  
ATOM    669  CB  VAL A  86       6.921  67.544  61.260  1.00 80.81           C  
ATOM    670  CG1 VAL A  86       6.585  68.444  60.072  1.00 80.80           C  
ATOM    671  CG2 VAL A  86       5.672  66.877  61.846  1.00 81.07           C  
ATOM    672  N   HIS A  87       7.235  65.822  58.575  1.00 85.14           N  
ATOM    673  CA  HIS A  87       6.595  64.927  57.601  1.00 88.56           C  
ATOM    674  C   HIS A  87       7.314  63.639  57.311  1.00 89.58           C  
ATOM    675  O   HIS A  87       6.915  62.896  56.412  1.00 89.88           O  
ATOM    676  CB  HIS A  87       6.417  65.640  56.265  1.00 90.24           C  
ATOM    677  CG  HIS A  87       5.561  66.853  56.354  1.00 92.20           C  
ATOM    678  ND1 HIS A  87       6.073  68.101  56.640  1.00 92.89           N  
ATOM    679  CD2 HIS A  87       4.223  67.010  56.223  1.00 92.76           C  
ATOM    680  CE1 HIS A  87       5.087  68.980  56.671  1.00 93.08           C  
ATOM    681  NE2 HIS A  87       3.955  68.345  56.415  1.00 93.37           N  
HETATM  682  N   MSE A  88       8.349  63.348  58.074  1.00 90.70           N  
HETATM  683  CA  MSE A  88       9.091  62.134  57.820  1.00 92.17           C  
HETATM  684  C   MSE A  88       9.725  61.626  59.094  1.00 89.99           C  
HETATM  685  O   MSE A  88      10.585  60.762  59.083  1.00 89.83           O  
HETATM  686  CB  MSE A  88      10.103  62.490  56.753  1.00 92.86           C  
HETATM  687  CG  MSE A  88      11.047  63.556  57.208  1.00 94.54           C  
HETATM  688 SE   MSE A  88      12.017  64.341  55.716  1.00 97.29          SE  
HETATM  689  CE  MSE A  88      10.460  65.132  54.825  1.00 96.03           C  
ATOM    690  N   THR A  89       9.275  62.196  60.194  1.00 88.55           N  
ATOM    691  CA  THR A  89       9.744  61.836  61.494  1.00 87.55           C  
ATOM    692  C   THR A  89       8.892  60.653  61.874  1.00 87.67           C  
ATOM    693  O   THR A  89       7.675  60.710  61.764  1.00 87.45           O  
ATOM    694  CB  THR A  89       9.504  62.973  62.471  1.00 86.96           C  
ATOM    695  OG1 THR A  89      10.267  64.099  62.044  1.00 86.42           O  
ATOM    696  CG2 THR A  89       9.947  62.599  63.856  1.00 86.99           C  
ATOM    697  N   LYS A  90       9.524  59.567  62.291  1.00 88.30           N  
ATOM    698  CA  LYS A  90       8.767  58.397  62.672  1.00 88.76           C  
ATOM    699  C   LYS A  90       8.262  58.765  64.065  1.00 88.87           C  
ATOM    700  O   LYS A  90       9.025  59.181  64.937  1.00 88.17           O  
ATOM    701  CB  LYS A  90       9.644  57.136  62.602  1.00 88.78           C  
ATOM    702  CG  LYS A  90       8.911  55.801  62.784  1.00 89.04           C  
ATOM    703  CD  LYS A  90       9.868  54.630  62.537  1.00 89.10           C  
ATOM    704  CE  LYS A  90       9.170  53.278  62.605  1.00 89.39           C  
ATOM    705  NZ  LYS A  90       8.543  53.004  63.936  1.00 89.63           N  
ATOM    706  N   THR A  91       6.954  58.703  64.246  1.00 89.78           N  
ATOM    707  CA  THR A  91       6.386  59.048  65.536  1.00 90.89           C  
ATOM    708  C   THR A  91       5.635  57.880  66.117  1.00 91.33           C  
ATOM    709  O   THR A  91       5.321  57.864  67.307  1.00 91.44           O  
ATOM    710  CB  THR A  91       5.443  60.236  65.427  1.00 91.24           C  
ATOM    711  OG1 THR A  91       4.394  59.904  64.517  1.00 91.68           O  
ATOM    712  CG2 THR A  91       6.181  61.467  64.905  1.00 91.55           C  
ATOM    713  N   ASP A  92       5.326  56.906  65.271  1.00 92.00           N  
ATOM    714  CA  ASP A  92       4.619  55.733  65.741  1.00 92.86           C  
ATOM    715  C   ASP A  92       5.669  54.916  66.506  1.00 93.31           C  
ATOM    716  O   ASP A  92       5.906  53.742  66.191  1.00 93.91           O  
ATOM    717  CB  ASP A  92       4.059  54.945  64.560  1.00 92.91           C  
ATOM    718  N   VAL A  93       6.299  55.541  67.508  1.00 93.04           N  
ATOM    719  CA  VAL A  93       7.334  54.870  68.297  1.00 93.08           C  
ATOM    720  C   VAL A  93       7.055  54.681  69.775  1.00 93.04           C  
ATOM    721  O   VAL A  93       6.239  55.377  70.364  1.00 93.17           O  
ATOM    722  CB  VAL A  93       8.697  55.604  68.209  1.00 93.22           C  
ATOM    723  CG1 VAL A  93       9.225  55.587  66.780  1.00 93.31           C  
ATOM    724  CG2 VAL A  93       8.584  57.029  68.757  1.00 93.11           C  
ATOM    725  N   ALA A  94       7.785  53.734  70.359  1.00 93.01           N  
ATOM    726  CA  ALA A  94       7.683  53.398  71.763  1.00 92.64           C  
ATOM    727  C   ALA A  94       8.158  54.580  72.601  1.00 92.62           C  
ATOM    728  O   ALA A  94       8.763  55.507  72.073  1.00 93.37           O  
ATOM    729  CB  ALA A  94       8.525  52.195  72.036  1.00 92.73           C  
ATOM    730  N   VAL A  95       7.893  54.548  73.904  1.00 92.41           N  
ATOM    731  CA  VAL A  95       8.301  55.637  74.797  1.00 92.26           C  
ATOM    732  C   VAL A  95       7.971  55.290  76.257  1.00 91.97           C  
ATOM    733  O   VAL A  95       7.073  54.485  76.513  1.00 92.19           O  
ATOM    734  CB  VAL A  95       7.586  56.945  74.405  1.00 92.21           C  
ATOM    735  CG1 VAL A  95       6.076  56.744  74.469  1.00 92.14           C  
ATOM    736  CG2 VAL A  95       8.018  58.083  75.298  1.00 92.17           C  
ATOM    737  N   VAL A  96       8.690  55.887  77.209  1.00 91.66           N  
ATOM    738  CA  VAL A  96       8.443  55.613  78.631  1.00 91.41           C  
ATOM    739  C   VAL A  96       8.428  56.861  79.482  1.00 91.62           C  
ATOM    740  O   VAL A  96       8.955  57.919  79.077  1.00 92.16           O  
ATOM    741  CB  VAL A  96       9.516  54.709  79.245  1.00 91.31           C  
ATOM    742  CG1 VAL A  96       9.517  53.357  78.559  1.00 91.56           C  
ATOM    743  CG2 VAL A  96      10.886  55.371  79.160  1.00 91.14           C  
ATOM    744  N   SER A  97       7.831  56.726  80.667  1.00 90.83           N  
ATOM    745  CA  SER A  97       7.739  57.825  81.605  1.00 90.57           C  
ATOM    746  C   SER A  97       9.039  57.802  82.373  1.00 90.25           C  
ATOM    747  O   SER A  97       9.744  56.783  82.349  1.00 89.58           O  
ATOM    748  CB  SER A  97       6.567  57.624  82.556  1.00 90.96           C  
ATOM    749  OG  SER A  97       6.722  56.423  83.293  1.00 91.60           O  
ATOM    750  N   PRO A  98       9.381  58.923  83.038  1.00 90.36           N  
ATOM    751  CA  PRO A  98      10.623  58.923  83.784  1.00 90.79           C  
ATOM    752  C   PRO A  98      10.591  57.749  84.734  1.00 91.51           C  
ATOM    753  O   PRO A  98      11.646  57.273  85.149  1.00 92.27           O  
ATOM    754  CB  PRO A  98      10.593  60.259  84.517  1.00 90.52           C  
ATOM    755  CG  PRO A  98       9.800  61.125  83.615  1.00 90.44           C  
ATOM    756  CD  PRO A  98       8.688  60.220  83.144  1.00 90.44           C  
ATOM    757  N   ASP A  99       9.384  57.283  85.065  1.00 91.86           N  
ATOM    758  CA  ASP A  99       9.217  56.132  85.959  1.00 91.97           C  
ATOM    759  C   ASP A  99       8.942  54.913  85.095  1.00 91.62           C  
ATOM    760  O   ASP A  99       7.794  54.506  84.916  1.00 91.89           O  
ATOM    761  CB  ASP A  99       8.076  56.309  86.962  1.00 92.36           C  
ATOM    762  CG  ASP A  99       8.297  57.468  87.899  1.00 92.94           C  
ATOM    763  OD1 ASP A  99       9.228  58.263  87.660  1.00 93.60           O  
ATOM    764  OD2 ASP A  99       7.525  57.597  88.871  1.00 93.00           O  
ATOM    765  N   PHE A 100      10.013  54.343  84.563  1.00 90.88           N  
ATOM    766  CA  PHE A 100       9.948  53.175  83.708  1.00 90.34           C  
ATOM    767  C   PHE A 100      10.379  51.933  84.459  1.00 90.14           C  
ATOM    768  O   PHE A 100      11.323  51.978  85.244  1.00 90.36           O  
ATOM    769  CB  PHE A 100      10.908  53.400  82.566  1.00 90.07           C  
ATOM    770  CG  PHE A 100      12.297  53.697  83.031  1.00 90.36           C  
ATOM    771  CD1 PHE A 100      12.681  55.002  83.293  1.00 90.54           C  
ATOM    772  CD2 PHE A 100      13.217  52.681  83.239  1.00 90.60           C  
ATOM    773  CE1 PHE A 100      13.967  55.289  83.738  1.00 90.66           C  
ATOM    774  CE2 PHE A 100      14.512  52.962  83.687  1.00 90.52           C  
ATOM    775  CZ  PHE A 100      14.885  54.263  83.934  1.00 90.32           C  
ATOM    776  N   THR A 101       9.689  50.822  84.233  1.00 89.63           N  
ATOM    777  CA  THR A 101      10.054  49.588  84.910  1.00 88.94           C  
ATOM    778  C   THR A 101      11.153  48.975  84.056  1.00 87.76           C  
ATOM    779  O   THR A 101      11.692  49.631  83.185  1.00 87.53           O  
ATOM    780  CB  THR A 101       8.865  48.618  85.064  1.00 89.21           C  
ATOM    781  OG1 THR A 101       8.402  48.190  83.777  1.00 89.39           O  
ATOM    782  CG2 THR A 101       7.736  49.283  85.832  1.00 89.00           C  
ATOM    783  N   ILE A 102      11.496  47.724  84.276  1.00 86.94           N  
ATOM    784  CA  ILE A 102      12.543  47.175  83.452  1.00 86.16           C  
ATOM    785  C   ILE A 102      11.943  46.464  82.251  1.00 85.79           C  
ATOM    786  O   ILE A 102      12.384  46.695  81.128  1.00 85.24           O  
ATOM    787  CB  ILE A 102      13.483  46.292  84.255  1.00 86.27           C  
ATOM    788  CG1 ILE A 102      13.988  47.082  85.458  1.00 86.67           C  
ATOM    789  CG2 ILE A 102      14.619  45.830  83.396  1.00 85.67           C  
ATOM    790  CD1 ILE A 102      14.682  48.366  85.061  1.00 86.99           C  
ATOM    791  N   THR A 103      10.921  45.634  82.486  1.00 85.50           N  
ATOM    792  CA  THR A 103      10.239  44.881  81.416  1.00 85.26           C  
ATOM    793  C   THR A 103       9.904  45.757  80.206  1.00 85.82           C  
ATOM    794  O   THR A 103      10.203  45.401  79.063  1.00 86.35           O  
ATOM    795  CB  THR A 103       8.935  44.235  81.898  1.00 84.76           C  
ATOM    796  OG1 THR A 103       9.218  43.339  82.972  1.00 84.57           O  
ATOM    797  CG2 THR A 103       8.266  43.459  80.762  1.00 84.38           C  
ATOM    798  N   GLU A 104       9.260  46.890  80.453  1.00 85.42           N  
ATOM    799  CA  GLU A 104       8.913  47.780  79.377  1.00 85.14           C  
ATOM    800  C   GLU A 104      10.152  48.053  78.545  1.00 85.24           C  
ATOM    801  O   GLU A 104      10.140  47.924  77.320  1.00 85.78           O  
ATOM    802  CB  GLU A 104       8.502  49.119  79.946  1.00 85.51           C  
ATOM    803  CG  GLU A 104       7.336  49.108  80.855  1.00 86.17           C  
ATOM    804  CD  GLU A 104       7.051  50.495  81.387  1.00 86.56           C  
ATOM    805  OE1 GLU A 104       6.084  50.644  82.183  1.00 87.01           O  
ATOM    806  OE2 GLU A 104       7.805  51.431  81.016  1.00 86.08           O  
ATOM    807  N   VAL A 105      11.221  48.448  79.231  1.00 84.58           N  
ATOM    808  CA  VAL A 105      12.501  48.770  78.596  1.00 83.83           C  
ATOM    809  C   VAL A 105      13.063  47.677  77.689  1.00 83.53           C  
ATOM    810  O   VAL A 105      13.192  47.866  76.478  1.00 83.97           O  
ATOM    811  CB  VAL A 105      13.554  49.156  79.649  1.00 83.34           C  
ATOM    812  CG1 VAL A 105      14.860  49.479  78.987  1.00 82.65           C  
ATOM    813  CG2 VAL A 105      13.074  50.351  80.444  1.00 83.02           C  
ATOM    814  N   LEU A 106      13.411  46.542  78.266  1.00 82.75           N  
ATOM    815  CA  LEU A 106      13.947  45.471  77.462  1.00 83.38           C  
ATOM    816  C   LEU A 106      12.970  45.138  76.343  1.00 83.75           C  
ATOM    817  O   LEU A 106      13.361  44.843  75.223  1.00 83.98           O  
ATOM    818  CB  LEU A 106      14.236  44.233  78.322  1.00 83.56           C  
ATOM    819  CG  LEU A 106      15.276  44.365  79.438  1.00 83.35           C  
ATOM    820  CD1 LEU A 106      16.649  44.615  78.881  1.00 83.14           C  
ATOM    821  CD2 LEU A 106      14.900  45.466  80.408  1.00 83.71           C  
ATOM    822  N   HIS A 107      11.688  45.193  76.644  1.00 84.61           N  
ATOM    823  CA  HIS A 107      10.698  44.889  75.640  1.00 85.84           C  
ATOM    824  C   HIS A 107      10.679  45.915  74.520  1.00 86.29           C  
ATOM    825  O   HIS A 107      10.854  45.583  73.352  1.00 86.80           O  
ATOM    826  CB  HIS A 107       9.328  44.810  76.285  1.00 87.05           C  
ATOM    827  CG  HIS A 107       8.217  44.583  75.312  1.00 88.22           C  
ATOM    828  ND1 HIS A 107       7.805  43.324  74.928  1.00 88.93           N  
ATOM    829  CD2 HIS A 107       7.413  45.458  74.662  1.00 88.54           C  
ATOM    830  CE1 HIS A 107       6.801  43.433  74.076  1.00 89.01           C  
ATOM    831  NE2 HIS A 107       6.545  44.717  73.896  1.00 89.20           N  
ATOM    832  N   LYS A 108      10.467  47.171  74.877  1.00 86.11           N  
ATOM    833  CA  LYS A 108      10.424  48.212  73.876  1.00 86.24           C  
ATOM    834  C   LYS A 108      11.727  48.324  73.099  1.00 85.94           C  
ATOM    835  O   LYS A 108      11.690  48.604  71.900  1.00 85.73           O  
ATOM    836  CB  LYS A 108       9.942  49.528  74.493  1.00 86.62           C  
ATOM    837  CG  LYS A 108       8.533  49.365  75.064  1.00 86.92           C  
ATOM    838  CD  LYS A 108       7.977  50.594  75.752  1.00 87.27           C  
ATOM    839  CE  LYS A 108       6.582  50.292  76.317  1.00 87.57           C  
ATOM    840  NZ  LYS A 108       5.978  51.440  77.055  1.00 87.78           N  
ATOM    841  N   LEU A 109      12.861  48.088  73.763  1.00 85.70           N  
ATOM    842  CA  LEU A 109      14.151  48.171  73.073  1.00 86.88           C  
ATOM    843  C   LEU A 109      14.374  47.132  71.982  1.00 88.29           C  
ATOM    844  O   LEU A 109      15.426  47.118  71.344  1.00 88.60           O  
ATOM    845  CB  LEU A 109      15.370  48.224  74.006  1.00 86.08           C  
ATOM    846  CG  LEU A 109      15.751  49.389  74.916  1.00 85.52           C  
ATOM    847  CD1 LEU A 109      16.932  49.000  75.752  1.00 85.26           C  
ATOM    848  CD2 LEU A 109      16.075  50.648  74.126  1.00 85.10           C  
ATOM    849  N   VAL A 110      13.404  46.258  71.764  1.00 89.75           N  
ATOM    850  CA  VAL A 110      13.572  45.258  70.722  1.00 90.99           C  
ATOM    851  C   VAL A 110      13.286  45.889  69.367  1.00 91.75           C  
ATOM    852  O   VAL A 110      13.920  45.540  68.376  1.00 92.55           O  
ATOM    853  CB  VAL A 110      12.648  44.043  70.895  1.00 91.11           C  
ATOM    854  CG1 VAL A 110      12.850  43.075  69.758  1.00 91.42           C  
ATOM    855  CG2 VAL A 110      12.932  43.355  72.193  1.00 91.57           C  
ATOM    856  N   ASP A 111      12.357  46.840  69.319  1.00 91.92           N  
ATOM    857  CA  ASP A 111      12.035  47.469  68.048  1.00 92.15           C  
ATOM    858  C   ASP A 111      12.832  48.708  67.729  1.00 92.03           C  
ATOM    859  O   ASP A 111      13.061  49.036  66.566  1.00 92.15           O  
ATOM    860  CB  ASP A 111      10.540  47.741  67.956  1.00 92.92           C  
ATOM    861  CG  ASP A 111       9.722  46.463  68.022  1.00 93.75           C  
ATOM    862  OD1 ASP A 111      10.322  45.385  68.229  1.00 93.93           O  
ATOM    863  OD2 ASP A 111       8.483  46.527  67.869  1.00 94.11           O  
ATOM    864  N   GLU A 112      13.289  49.390  68.758  1.00 91.47           N  
ATOM    865  CA  GLU A 112      14.047  50.585  68.518  1.00 91.18           C  
ATOM    866  C   GLU A 112      15.378  50.615  69.270  1.00 90.44           C  
ATOM    867  O   GLU A 112      15.476  50.114  70.383  1.00 90.07           O  
ATOM    868  CB  GLU A 112      13.183  51.756  68.915  1.00 91.80           C  
ATOM    869  CG  GLU A 112      12.763  51.667  70.352  1.00 93.20           C  
ATOM    870  CD  GLU A 112      11.935  52.852  70.790  1.00 94.55           C  
ATOM    871  OE1 GLU A 112      11.664  53.746  69.952  1.00 95.07           O  
ATOM    872  OE2 GLU A 112      11.565  52.902  71.983  1.00 95.59           O  
ATOM    873  N   SER A 113      16.388  51.213  68.641  1.00 89.74           N  
ATOM    874  CA  SER A 113      17.733  51.338  69.198  1.00 89.52           C  
ATOM    875  C   SER A 113      17.792  52.107  70.510  1.00 89.55           C  
ATOM    876  O   SER A 113      18.692  51.912  71.323  1.00 89.57           O  
ATOM    877  CB  SER A 113      18.669  51.968  68.176  1.00 89.88           C  
ATOM    878  OG  SER A 113      18.196  53.247  67.785  1.00 90.36           O  
ATOM    879  N   PHE A 114      16.863  53.016  70.721  1.00 90.20           N  
ATOM    880  CA  PHE A 114      16.889  53.748  71.983  1.00 90.75           C  
ATOM    881  C   PHE A 114      15.483  54.097  72.444  1.00 90.51           C  
ATOM    882  O   PHE A 114      14.572  54.304  71.652  1.00 90.31           O  
ATOM    883  CB  PHE A 114      17.791  54.984  71.974  1.00 91.55           C  
ATOM    884  CG  PHE A 114      17.369  56.053  71.013  1.00 91.70           C  
ATOM    885  CD1 PHE A 114      16.361  56.945  71.356  1.00 92.12           C  
ATOM    886  CD2 PHE A 114      18.041  56.239  69.826  1.00 92.07           C  
ATOM    887  CE1 PHE A 114      15.980  57.945  70.501  1.00 91.82           C  
ATOM    888  CE2 PHE A 114      17.675  57.251  68.958  1.00 91.93           C  
ATOM    889  CZ  PHE A 114      16.645  58.103  69.298  1.00 91.98           C  
ATOM    890  N   LEU A 115      15.330  54.205  73.744  1.00 90.70           N  
ATOM    891  CA  LEU A 115      14.042  54.507  74.315  1.00 90.68           C  
ATOM    892  C   LEU A 115      13.894  55.921  74.907  1.00 89.67           C  
ATOM    893  O   LEU A 115      14.487  56.257  75.942  1.00 88.91           O  
ATOM    894  CB  LEU A 115      13.755  53.404  75.323  1.00 91.93           C  
ATOM    895  CG  LEU A 115      12.465  53.459  76.097  1.00 93.24           C  
ATOM    896  CD1 LEU A 115      11.298  53.501  75.138  1.00 93.76           C  
ATOM    897  CD2 LEU A 115      12.445  52.227  76.967  1.00 93.92           C  
ATOM    898  N   PRO A 116      13.074  56.746  74.238  1.00 88.92           N  
ATOM    899  CA  PRO A 116      12.771  58.136  74.584  1.00 88.49           C  
ATOM    900  C   PRO A 116      12.084  58.264  75.929  1.00 87.91           C  
ATOM    901  O   PRO A 116      11.057  57.635  76.157  1.00 87.75           O  
ATOM    902  CB  PRO A 116      11.809  58.578  73.465  1.00 88.42           C  
ATOM    903  CG  PRO A 116      12.009  57.592  72.356  1.00 88.14           C  
ATOM    904  CD  PRO A 116      12.343  56.303  73.041  1.00 88.47           C  
ATOM    905  N   VAL A 117      12.654  59.065  76.818  1.00 87.55           N  
ATOM    906  CA  VAL A 117      12.065  59.252  78.133  1.00 87.64           C  
ATOM    907  C   VAL A 117      11.438  60.640  78.163  1.00 87.85           C  
ATOM    908  O   VAL A 117      12.143  61.651  78.112  1.00 87.38           O  
ATOM    909  CB  VAL A 117      13.121  59.156  79.223  1.00 87.56           C  
ATOM    910  CG1 VAL A 117      12.491  59.356  80.580  1.00 87.36           C  
ATOM    911  CG2 VAL A 117      13.800  57.820  79.157  1.00 87.68           C  
ATOM    912  N   VAL A 118      10.113  60.690  78.245  1.00 88.06           N  
ATOM    913  CA  VAL A 118       9.431  61.975  78.268  1.00 88.47           C  
ATOM    914  C   VAL A 118       8.658  62.187  79.572  1.00 88.44           C  
ATOM    915  O   VAL A 118       7.987  61.272  80.066  1.00 88.56           O  
ATOM    916  CB  VAL A 118       8.489  62.141  77.036  1.00 88.67           C  
ATOM    917  CG1 VAL A 118       9.273  61.925  75.770  1.00 88.65           C  
ATOM    918  CG2 VAL A 118       7.370  61.133  77.058  1.00 88.88           C  
ATOM    919  N   ASP A 119       8.764  63.394  80.129  1.00 87.91           N  
ATOM    920  CA  ASP A 119       8.077  63.734  81.372  1.00 87.27           C  
ATOM    921  C   ASP A 119       6.557  63.735  81.209  1.00 86.84           C  
ATOM    922  O   ASP A 119       6.027  63.872  80.107  1.00 86.24           O  
ATOM    923  CB  ASP A 119       8.553  65.086  81.889  1.00 87.35           C  
ATOM    924  N   ALA A 120       5.864  63.595  82.333  1.00 86.94           N  
ATOM    925  CA  ALA A 120       4.399  63.573  82.364  1.00 86.75           C  
ATOM    926  C   ALA A 120       3.727  64.781  81.695  1.00 86.34           C  
ATOM    927  O   ALA A 120       2.505  64.807  81.533  1.00 86.15           O  
ATOM    928  CB  ALA A 120       3.903  63.414  83.800  1.00 86.68           C  
ATOM    929  N   GLU A 121       4.514  65.787  81.327  1.00 85.84           N  
ATOM    930  CA  GLU A 121       3.954  66.964  80.678  1.00 85.27           C  
ATOM    931  C   GLU A 121       4.450  67.042  79.229  1.00 84.96           C  
ATOM    932  O   GLU A 121       4.555  68.122  78.650  1.00 85.15           O  
ATOM    933  CB  GLU A 121       4.276  68.240  81.456  1.00 84.98           C  
ATOM    934  N   GLY A 122       4.777  65.885  78.656  1.00 84.14           N  
ATOM    935  CA  GLY A 122       5.249  65.812  77.276  1.00 83.32           C  
ATOM    936  C   GLY A 122       6.666  66.251  76.954  1.00 82.97           C  
ATOM    937  O   GLY A 122       7.160  65.981  75.852  1.00 82.88           O  
ATOM    938  N   ILE A 123       7.328  66.915  77.900  1.00 82.49           N  
ATOM    939  CA  ILE A 123       8.703  67.387  77.689  1.00 81.93           C  
ATOM    940  C   ILE A 123       9.793  66.294  77.752  1.00 81.73           C  
ATOM    941  O   ILE A 123      10.026  65.652  78.787  1.00 81.79           O  
ATOM    942  CB  ILE A 123       9.032  68.540  78.634  1.00 81.52           C  
ATOM    943  N   PHE A 124      10.447  66.101  76.612  1.00 81.16           N  
ATOM    944  CA  PHE A 124      11.517  65.132  76.450  1.00 80.51           C  
ATOM    945  C   PHE A 124      12.618  65.276  77.500  1.00 80.20           C  
ATOM    946  O   PHE A 124      13.323  66.276  77.511  1.00 80.43           O  
ATOM    947  CB  PHE A 124      12.109  65.310  75.053  1.00 80.27           C  
ATOM    948  CG  PHE A 124      13.297  64.455  74.796  1.00 80.24           C  
ATOM    949  CD1 PHE A 124      13.149  63.160  74.345  1.00 80.13           C  
ATOM    950  CD2 PHE A 124      14.572  64.951  74.998  1.00 80.21           C  
ATOM    951  CE1 PHE A 124      14.251  62.359  74.120  1.00 80.23           C  
ATOM    952  CE2 PHE A 124      15.680  64.162  74.763  1.00 80.43           C  
ATOM    953  CZ  PHE A 124      15.519  62.860  74.326  1.00 80.41           C  
ATOM    954  N   GLN A 125      12.799  64.269  78.352  1.00 79.76           N  
ATOM    955  CA  GLN A 125      13.834  64.343  79.391  1.00 79.57           C  
ATOM    956  C   GLN A 125      15.101  63.485  79.177  1.00 79.43           C  
ATOM    957  O   GLN A 125      16.030  63.532  79.985  1.00 80.17           O  
ATOM    958  CB  GLN A 125      13.217  64.096  80.794  1.00 79.30           C  
ATOM    959  N   GLY A 126      15.156  62.712  78.099  1.00 78.71           N  
ATOM    960  CA  GLY A 126      16.330  61.883  77.844  1.00 77.98           C  
ATOM    961  C   GLY A 126      15.990  60.606  77.102  1.00 78.22           C  
ATOM    962  O   GLY A 126      14.956  60.523  76.436  1.00 78.18           O  
ATOM    963  N   ILE A 127      16.864  59.608  77.208  1.00 78.01           N  
ATOM    964  CA  ILE A 127      16.653  58.316  76.539  1.00 77.96           C  
ATOM    965  C   ILE A 127      17.424  57.172  77.192  1.00 78.69           C  
ATOM    966  O   ILE A 127      18.310  57.380  78.025  1.00 79.62           O  
ATOM    967  CB  ILE A 127      17.096  58.341  75.079  1.00 76.83           C  
ATOM    968  CG1 ILE A 127      18.599  58.650  75.022  1.00 76.55           C  
ATOM    969  CG2 ILE A 127      16.303  59.352  74.321  1.00 76.55           C  
ATOM    970  CD1 ILE A 127      19.223  58.683  73.646  1.00 75.28           C  
ATOM    971  N   ILE A 128      17.090  55.957  76.792  1.00 78.33           N  
ATOM    972  CA  ILE A 128      17.735  54.774  77.319  1.00 77.88           C  
ATOM    973  C   ILE A 128      18.185  54.082  76.073  1.00 78.25           C  
ATOM    974  O   ILE A 128      17.379  53.870  75.175  1.00 79.10           O  
ATOM    975  CB  ILE A 128      16.737  53.925  78.045  1.00 77.33           C  
ATOM    976  CG1 ILE A 128      16.130  54.730  79.194  1.00 77.06           C  
ATOM    977  CG2 ILE A 128      17.417  52.698  78.562  1.00 77.49           C  
ATOM    978  CD1 ILE A 128      15.086  53.994  79.971  1.00 76.66           C  
ATOM    979  N   THR A 129      19.447  53.689  75.992  1.00 78.01           N  
ATOM    980  CA  THR A 129      19.870  53.052  74.754  1.00 77.58           C  
ATOM    981  C   THR A 129      20.147  51.571  74.790  1.00 77.89           C  
ATOM    982  O   THR A 129      20.375  51.010  75.867  1.00 76.20           O  
ATOM    983  CB  THR A 129      21.202  53.691  74.257  1.00 77.22           C  
ATOM    984  OG1 THR A 129      22.272  53.392  75.173  1.00 77.26           O  
ATOM    985  CG2 THR A 129      21.066  55.190  74.078  1.00 76.40           C  
ATOM    986  N   ARG A 130      20.090  50.937  73.607  1.00 78.55           N  
ATOM    987  CA  ARG A 130      20.399  49.521  73.545  1.00 79.66           C  
ATOM    988  C   ARG A 130      21.812  49.341  74.124  1.00 79.68           C  
ATOM    989  O   ARG A 130      22.049  48.436  74.915  1.00 79.85           O  
ATOM    990  CB  ARG A 130      20.181  48.805  72.186  1.00 79.60           C  
ATOM    991  CG  ARG A 130      18.701  48.553  71.812  1.00 80.90           C  
ATOM    992  CD  ARG A 130      18.562  47.491  70.653  1.00 81.69           C  
ATOM    993  NE  ARG A 130      18.919  47.877  69.297  1.00 84.06           N  
ATOM    994  CZ  ARG A 130      18.026  48.134  68.340  1.00 84.68           C  
ATOM    995  NH1 ARG A 130      16.739  47.883  68.547  1.00 85.08           N  
ATOM    996  NH2 ARG A 130      18.430  48.502  67.131  1.00 85.42           N  
ATOM    997  N   LYS A 131      22.722  50.249  73.787  1.00 79.94           N  
ATOM    998  CA  LYS A 131      24.082  50.182  74.296  1.00 80.83           C  
ATOM    999  C   LYS A 131      24.142  50.181  75.842  1.00 81.83           C  
ATOM   1000  O   LYS A 131      24.945  49.452  76.451  1.00 81.52           O  
ATOM   1001  CB  LYS A 131      24.877  51.376  73.789  1.00 80.66           C  
ATOM   1002  CG  LYS A 131      26.307  51.433  74.302  1.00 80.63           C  
ATOM   1003  CD  LYS A 131      26.992  52.669  73.781  1.00 81.84           C  
ATOM   1004  CE  LYS A 131      28.420  52.817  74.293  1.00 82.50           C  
ATOM   1005  NZ  LYS A 131      29.076  54.054  73.729  1.00 82.99           N  
ATOM   1006  N   SER A 132      23.308  51.015  76.467  1.00 82.52           N  
ATOM   1007  CA  SER A 132      23.264  51.120  77.930  1.00 82.63           C  
ATOM   1008  C   SER A 132      22.913  49.786  78.541  1.00 82.15           C  
ATOM   1009  O   SER A 132      23.721  49.179  79.220  1.00 81.83           O  
ATOM   1010  CB  SER A 132      22.237  52.169  78.384  1.00 83.46           C  
ATOM   1011  OG  SER A 132      22.510  53.476  77.862  1.00 84.58           O  
ATOM   1012  N   ILE A 133      21.700  49.322  78.274  1.00 82.86           N  
ATOM   1013  CA  ILE A 133      21.223  48.034  78.810  1.00 83.43           C  
ATOM   1014  C   ILE A 133      21.983  46.854  78.208  1.00 83.43           C  
ATOM   1015  O   ILE A 133      21.564  45.703  78.345  1.00 83.50           O  
ATOM   1016  CB  ILE A 133      19.676  47.861  78.599  1.00 81.87           C  
ATOM   1017  N   LEU A 134      23.107  47.135  77.558  1.00 82.49           N  
ATOM   1018  CA  LEU A 134      23.862  46.067  76.958  1.00 81.61           C  
ATOM   1019  C   LEU A 134      25.181  46.054  77.711  1.00 81.24           C  
ATOM   1020  O   LEU A 134      25.838  45.021  77.814  1.00 80.49           O  
ATOM   1021  CB  LEU A 134      24.030  46.352  75.463  1.00 81.95           C  
ATOM   1022  CG  LEU A 134      24.532  45.327  74.441  1.00 82.10           C  
ATOM   1023  CD1 LEU A 134      25.949  44.810  74.683  1.00 82.61           C  
ATOM   1024  CD2 LEU A 134      23.538  44.180  74.433  1.00 82.10           C  
ATOM   1025  N   LYS A 135      25.565  47.211  78.252  1.00 81.30           N  
ATOM   1026  CA  LYS A 135      26.808  47.286  79.000  1.00 80.71           C  
ATOM   1027  C   LYS A 135      26.475  46.581  80.295  1.00 79.79           C  
ATOM   1028  O   LYS A 135      27.331  45.937  80.886  1.00 79.31           O  
ATOM   1029  CB  LYS A 135      27.222  48.700  79.396  1.00 81.00           C  
ATOM   1030  CG  LYS A 135      27.381  49.788  78.343  1.00 81.34           C  
ATOM   1031  CD  LYS A 135      27.929  51.041  79.102  1.00 81.67           C  
ATOM   1032  CE  LYS A 135      28.002  52.380  78.321  1.00 81.96           C  
ATOM   1033  NZ  LYS A 135      26.646  52.958  77.921  1.00 82.00           N  
ATOM   1034  N   ALA A 136      25.228  46.730  80.745  1.00 79.59           N  
ATOM   1035  CA  ALA A 136      24.777  46.093  81.997  1.00 79.95           C  
ATOM   1036  C   ALA A 136      24.923  44.586  81.867  1.00 79.82           C  
ATOM   1037  O   ALA A 136      25.525  43.913  82.715  1.00 79.87           O  
ATOM   1038  CB  ALA A 136      23.332  46.460  82.328  1.00 79.71           C  
ATOM   1039  N   VAL A 137      24.354  44.070  80.788  1.00 79.30           N  
ATOM   1040  CA  VAL A 137      24.417  42.666  80.505  1.00 78.39           C  
ATOM   1041  C   VAL A 137      25.861  42.227  80.585  1.00 78.62           C  
ATOM   1042  O   VAL A 137      26.219  41.313  81.309  1.00 79.18           O  
ATOM   1043  CB  VAL A 137      23.940  42.411  79.083  1.00 77.67           C  
ATOM   1044  CG1 VAL A 137      24.279  41.010  78.637  1.00 77.14           C  
ATOM   1045  CG2 VAL A 137      22.460  42.764  78.945  1.00 77.16           C  
ATOM   1046  N   ASN A 138      26.711  42.932  79.875  1.00 78.94           N  
ATOM   1047  CA  ASN A 138      28.097  42.578  79.876  1.00 79.68           C  
ATOM   1048  C   ASN A 138      28.738  42.600  81.266  1.00 80.94           C  
ATOM   1049  O   ASN A 138      29.448  41.666  81.630  1.00 81.10           O  
ATOM   1050  CB  ASN A 138      28.824  43.450  78.879  1.00 78.91           C  
ATOM   1051  CG  ASN A 138      30.211  43.029  78.684  1.00 78.38           C  
ATOM   1052  OD1 ASN A 138      30.816  43.367  77.683  1.00 78.96           O  
ATOM   1053  ND2 ASN A 138      30.706  42.192  79.571  1.00 78.40           N  
ATOM   1054  N   ALA A 139      28.459  43.634  82.053  1.00 82.46           N  
ATOM   1055  CA  ALA A 139      29.023  43.745  83.403  1.00 84.08           C  
ATOM   1056  C   ALA A 139      28.564  42.609  84.338  1.00 85.51           C  
ATOM   1057  O   ALA A 139      29.039  42.466  85.486  1.00 86.08           O  
ATOM   1058  CB  ALA A 139      28.698  45.094  84.002  1.00 84.11           C  
ATOM   1059  N   LEU A 140      27.633  41.805  83.843  1.00 86.09           N  
ATOM   1060  CA  LEU A 140      27.126  40.696  84.611  1.00 86.70           C  
ATOM   1061  C   LEU A 140      28.073  39.519  84.455  1.00 87.89           C  
ATOM   1062  O   LEU A 140      28.256  38.750  85.381  1.00 88.25           O  
ATOM   1063  CB  LEU A 140      25.739  40.310  84.125  1.00 86.10           C  
ATOM   1064  CG  LEU A 140      25.108  39.127  84.842  1.00 85.79           C  
ATOM   1065  CD1 LEU A 140      25.004  39.426  86.298  1.00 85.99           C  
ATOM   1066  CD2 LEU A 140      23.743  38.871  84.281  1.00 86.13           C  
ATOM   1067  N   LEU A 141      28.679  39.380  83.280  1.00 89.50           N  
ATOM   1068  CA  LEU A 141      29.607  38.277  83.040  1.00 91.23           C  
ATOM   1069  C   LEU A 141      30.949  38.466  83.739  1.00 92.81           C  
ATOM   1070  O   LEU A 141      31.834  37.623  83.638  1.00 93.12           O  
ATOM   1071  CB  LEU A 141      29.813  38.026  81.545  1.00 90.87           C  
ATOM   1072  CG  LEU A 141      28.624  37.619  80.674  1.00 90.30           C  
ATOM   1073  CD1 LEU A 141      29.097  37.457  79.246  1.00 90.33           C  
ATOM   1074  CD2 LEU A 141      28.013  36.324  81.158  1.00 90.12           C  
ATOM   1075  N   HIS A 142      31.099  39.587  84.431  1.00 95.00           N  
ATOM   1076  CA  HIS A 142      32.324  39.890  85.159  1.00 97.34           C  
ATOM   1077  C   HIS A 142      31.864  40.411  86.503  1.00 98.28           C  
ATOM   1078  O   HIS A 142      31.632  41.616  86.668  1.00 98.87           O  
ATOM   1079  CB  HIS A 142      33.157  40.927  84.424  1.00 98.22           C  
ATOM   1080  CG  HIS A 142      33.586  40.487  83.062  1.00 99.18           C  
ATOM   1081  ND1 HIS A 142      34.760  39.799  82.839  1.00 99.84           N  
ATOM   1082  CD2 HIS A 142      32.992  40.622  81.853  1.00 99.32           C  
ATOM   1083  CE1 HIS A 142      34.878  39.543  81.548  1.00 99.94           C  
ATOM   1084  NE2 HIS A 142      33.818  40.031  80.928  1.00 99.74           N  
ATOM   1085  N   ASP A 143      31.720  39.492  87.456  1.00 98.60           N  
ATOM   1086  CA  ASP A 143      31.265  39.847  88.786  1.00 98.66           C  
ATOM   1087  C   ASP A 143      31.600  38.716  89.758  1.00 98.71           C  
ATOM   1088  O   ASP A 143      32.740  38.589  90.210  1.00 98.75           O  
ATOM   1089  CB  ASP A 143      29.746  40.071  88.710  1.00 98.70           C  
ATOM   1090  CG  ASP A 143      29.138  40.504  90.024  1.00 98.58           C  
ATOM   1091  OD1 ASP A 143      27.903  40.719  90.054  1.00 98.07           O  
ATOM   1092  OD2 ASP A 143      29.888  40.637  91.016  1.00 98.72           O  
TER    1093      ASP A 143                                                      
ATOM   1094  N   ASN B  -1      27.853  33.222  93.643  1.00 61.36           N  
ATOM   1095  CA  ASN B  -1      29.181  32.998  93.017  1.00 61.43           C  
ATOM   1096  C   ASN B  -1      29.086  33.276  91.514  1.00 61.81           C  
ATOM   1097  O   ASN B  -1      28.022  33.684  91.019  1.00 61.98           O  
ATOM   1098  CB  ASN B  -1      29.650  31.573  93.281  1.00 61.10           C  
ATOM   1099  N   ALA B   0      30.194  33.063  90.795  1.00 61.72           N  
ATOM   1100  CA  ALA B   0      30.244  33.285  89.344  1.00 60.75           C  
ATOM   1101  C   ALA B   0      29.280  32.361  88.617  1.00 60.30           C  
ATOM   1102  O   ALA B   0      29.204  32.393  87.396  1.00 61.12           O  
ATOM   1103  CB  ALA B   0      31.655  33.114  88.805  1.00 60.71           C  
HETATM 1104  N   MSE B   1      28.580  31.513  89.367  1.00 59.43           N  
HETATM 1105  CA  MSE B   1      27.613  30.596  88.795  1.00 58.83           C  
HETATM 1106  C   MSE B   1      26.607  31.408  88.039  1.00 57.67           C  
HETATM 1107  O   MSE B   1      26.241  31.061  86.933  1.00 58.15           O  
HETATM 1108  CB  MSE B   1      26.901  29.794  89.877  1.00 60.85           C  
HETATM 1109  CG  MSE B   1      27.783  28.780  90.570  1.00 62.59           C  
HETATM 1110 SE   MSE B   1      28.232  27.558  89.117  0.50 64.16          SE  
HETATM 1111  CE  MSE B   1      26.432  26.945  88.696  1.00 63.88           C  
ATOM   1112  N   ILE B   2      26.159  32.499  88.640  1.00 55.90           N  
ATOM   1113  CA  ILE B   2      25.191  33.365  88.001  1.00 54.20           C  
ATOM   1114  C   ILE B   2      25.675  33.729  86.605  1.00 53.50           C  
ATOM   1115  O   ILE B   2      24.909  33.688  85.631  1.00 52.72           O  
ATOM   1116  CB  ILE B   2      24.990  34.628  88.821  1.00 54.20           C  
ATOM   1117  CG1 ILE B   2      24.561  34.236  90.240  1.00 54.21           C  
ATOM   1118  CG2 ILE B   2      23.984  35.542  88.135  1.00 53.80           C  
ATOM   1119  CD1 ILE B   2      24.323  35.392  91.162  1.00 54.52           C  
ATOM   1120  N   ALA B   3      26.960  34.054  86.509  1.00 52.65           N  
ATOM   1121  CA  ALA B   3      27.556  34.420  85.233  1.00 52.43           C  
ATOM   1122  C   ALA B   3      27.651  33.211  84.318  1.00 52.28           C  
ATOM   1123  O   ALA B   3      27.446  33.327  83.106  1.00 52.22           O  
ATOM   1124  CB  ALA B   3      28.920  35.042  85.437  1.00 52.72           C  
ATOM   1125  N   LYS B   4      27.972  32.051  84.890  1.00 52.05           N  
ATOM   1126  CA  LYS B   4      28.080  30.839  84.081  1.00 51.85           C  
ATOM   1127  C   LYS B   4      26.664  30.466  83.625  1.00 52.00           C  
ATOM   1128  O   LYS B   4      26.451  30.149  82.459  1.00 51.21           O  
ATOM   1129  CB  LYS B   4      28.849  29.726  84.807  1.00 51.28           C  
ATOM   1130  CG  LYS B   4      30.258  30.194  85.210  1.00 51.67           C  
ATOM   1131  CD  LYS B   4      31.167  29.140  85.917  1.00 51.48           C  
ATOM   1132  CE  LYS B   4      31.485  27.973  84.986  1.00 51.05           C  
ATOM   1133  NZ  LYS B   4      32.377  26.955  85.561  1.00 49.75           N  
ATOM   1134  N   GLU B   5      25.698  30.536  84.539  1.00 53.00           N  
ATOM   1135  CA AGLU B   5      24.316  30.217  84.225  0.50 53.54           C  
ATOM   1136  CA BGLU B   5      24.311  30.217  84.205  0.50 53.73           C  
ATOM   1137  C   GLU B   5      23.846  31.167  83.136  1.00 54.05           C  
ATOM   1138  O   GLU B   5      23.096  30.791  82.239  1.00 54.58           O  
ATOM   1139  CB AGLU B   5      23.427  30.391  85.465  0.50 53.39           C  
ATOM   1140  CB BGLU B   5      23.373  30.364  85.406  0.50 53.80           C  
ATOM   1141  CG AGLU B   5      23.809  29.509  86.659  0.50 53.42           C  
ATOM   1142  CG BGLU B   5      23.510  29.373  86.560  0.50 54.22           C  
ATOM   1143  CD AGLU B   5      22.927  29.714  87.898  0.50 53.39           C  
ATOM   1144  CD BGLU B   5      23.125  27.937  86.196  0.50 54.29           C  
ATOM   1145  OE1AGLU B   5      21.978  30.529  87.862  0.50 53.43           O  
ATOM   1146  OE1BGLU B   5      22.894  27.624  85.008  0.50 54.48           O  
ATOM   1147  OE2AGLU B   5      23.194  29.050  88.920  0.50 53.07           O  
ATOM   1148  OE2BGLU B   5      23.044  27.112  87.124  0.50 54.49           O  
ATOM   1149  N   PHE B   6      24.300  32.401  83.210  1.00 54.70           N  
ATOM   1150  CA  PHE B   6      23.860  33.340  82.191  1.00 56.49           C  
ATOM   1151  C   PHE B   6      24.505  33.038  80.835  1.00 56.06           C  
ATOM   1152  O   PHE B   6      23.811  32.945  79.825  1.00 56.06           O  
ATOM   1153  CB  PHE B   6      24.015  34.794  82.672  1.00 57.90           C  
ATOM   1154  CG  PHE B   6      23.369  35.791  81.779  1.00 58.30           C  
ATOM   1155  CD1 PHE B   6      21.979  35.902  81.773  1.00 59.00           C  
ATOM   1156  CD2 PHE B   6      24.113  36.693  81.046  1.00 59.27           C  
ATOM   1157  CE1 PHE B   6      21.321  36.828  80.969  1.00 59.67           C  
ATOM   1158  CE2 PHE B   6      23.481  37.645  80.237  1.00 59.64           C  
ATOM   1159  CZ  PHE B   6      22.075  37.715  80.196  1.00 59.54           C  
ATOM   1160  N   GLU B   7      25.821  32.848  80.817  1.00 56.14           N  
ATOM   1161  CA  GLU B   7      26.492  32.544  79.572  1.00 55.76           C  
ATOM   1162  C   GLU B   7      25.804  31.268  79.050  1.00 55.37           C  
ATOM   1163  O   GLU B   7      25.350  31.238  77.918  1.00 53.27           O  
ATOM   1164  CB  GLU B   7      27.995  32.379  79.792  1.00 55.55           C  
ATOM   1165  CG  GLU B   7      28.803  32.254  78.493  1.00 56.07           C  
ATOM   1166  CD  GLU B   7      30.337  32.206  78.723  1.00 56.37           C  
ATOM   1167  OE1 GLU B   7      30.760  32.024  79.894  1.00 56.22           O  
ATOM   1168  OE2 GLU B   7      31.110  32.348  77.730  1.00 56.11           O  
ATOM   1169  N   THR B   8      25.670  30.244  79.900  1.00 57.06           N  
ATOM   1170  CA  THR B   8      25.009  28.991  79.494  1.00 58.69           C  
ATOM   1171  C   THR B   8      23.716  29.352  78.815  1.00 60.29           C  
ATOM   1172  O   THR B   8      23.499  29.040  77.650  1.00 60.77           O  
ATOM   1173  CB  THR B   8      24.611  28.121  80.666  1.00 58.53           C  
ATOM   1174  OG1 THR B   8      25.778  27.727  81.383  1.00 59.13           O  
ATOM   1175  CG2 THR B   8      23.902  26.882  80.166  1.00 58.49           C  
ATOM   1176  N   PHE B   9      22.828  29.978  79.569  1.00 61.79           N  
ATOM   1177  CA  PHE B   9      21.574  30.375  78.992  1.00 63.24           C  
ATOM   1178  C   PHE B   9      21.723  30.981  77.636  1.00 64.15           C  
ATOM   1179  O   PHE B   9      21.124  30.540  76.655  1.00 64.61           O  
ATOM   1180  CB  PHE B   9      20.848  31.402  79.867  1.00 63.09           C  
ATOM   1181  CG  PHE B   9      19.726  32.103  79.140  1.00 62.98           C  
ATOM   1182  CD1 PHE B   9      18.496  31.489  78.939  1.00 63.26           C  
ATOM   1183  CD2 PHE B   9      19.915  33.398  78.656  1.00 63.05           C  
ATOM   1184  CE1 PHE B   9      17.471  32.146  78.246  1.00 63.68           C  
ATOM   1185  CE2 PHE B   9      18.908  34.070  77.974  1.00 63.23           C  
ATOM   1186  CZ  PHE B   9      17.681  33.445  77.763  1.00 63.65           C  
ATOM   1187  N   LEU B  10      22.549  32.001  77.600  1.00 65.73           N  
ATOM   1188  CA  LEU B  10      22.795  32.735  76.389  1.00 67.90           C  
ATOM   1189  C   LEU B  10      23.457  31.863  75.265  1.00 69.12           C  
ATOM   1190  O   LEU B  10      23.217  32.072  74.069  1.00 69.12           O  
ATOM   1191  CB  LEU B  10      23.555  33.970  76.805  1.00 68.14           C  
ATOM   1192  CG  LEU B  10      23.678  35.121  75.859  1.00 68.65           C  
ATOM   1193  CD1 LEU B  10      22.265  35.613  75.628  1.00 68.10           C  
ATOM   1194  CD2 LEU B  10      24.487  36.197  76.562  1.00 68.95           C  
ATOM   1195  N   LEU B  11      24.264  30.878  75.647  1.00 69.95           N  
ATOM   1196  CA  LEU B  11      24.885  30.003  74.662  1.00 70.91           C  
ATOM   1197  C   LEU B  11      23.770  29.258  73.952  1.00 71.70           C  
ATOM   1198  O   LEU B  11      23.925  28.831  72.807  1.00 72.78           O  
ATOM   1199  CB  LEU B  11      25.794  28.971  75.334  1.00 70.37           C  
ATOM   1200  CG  LEU B  11      27.087  29.403  76.021  1.00 69.89           C  
ATOM   1201  CD1 LEU B  11      27.651  28.290  76.844  1.00 70.31           C  
ATOM   1202  CD2 LEU B  11      28.097  29.915  75.001  1.00 69.32           C  
ATOM   1203  N   GLY B  12      22.652  29.089  74.647  1.00 71.97           N  
ATOM   1204  CA  GLY B  12      21.517  28.403  74.085  1.00 73.17           C  
ATOM   1205  C   GLY B  12      20.746  29.290  73.135  1.00 74.93           C  
ATOM   1206  O   GLY B  12      19.668  28.934  72.704  1.00 74.54           O  
ATOM   1207  N   GLN B  13      21.312  30.433  72.759  1.00 77.57           N  
ATOM   1208  CA  GLN B  13      20.619  31.350  71.850  1.00 79.79           C  
ATOM   1209  C   GLN B  13      21.246  31.596  70.466  1.00 81.69           C  
ATOM   1210  O   GLN B  13      20.681  32.349  69.674  1.00 82.44           O  
ATOM   1211  CB  GLN B  13      20.400  32.680  72.564  1.00 80.60           C  
ATOM   1212  CG  GLN B  13      19.582  32.549  73.861  1.00 81.99           C  
ATOM   1213  CD  GLN B  13      18.147  32.054  73.660  1.00 82.01           C  
ATOM   1214  OE1 GLN B  13      17.527  31.536  74.586  1.00 81.45           O  
ATOM   1215  NE2 GLN B  13      17.637  32.179  72.442  1.00 82.81           N  
ATOM   1216  N   GLU B  14      22.405  30.998  70.178  1.00 83.18           N  
ATOM   1217  CA  GLU B  14      23.083  31.163  68.884  1.00 83.99           C  
ATOM   1218  C   GLU B  14      22.138  31.455  67.727  1.00 83.70           C  
ATOM   1219  O   GLU B  14      22.389  32.358  66.919  1.00 83.80           O  
ATOM   1220  CB  GLU B  14      23.820  29.868  68.540  1.00 86.31           C  
ATOM   1221  CG  GLU B  14      24.954  29.468  69.475  1.00 88.66           C  
ATOM   1222  CD  GLU B  14      26.154  30.399  69.379  1.00 89.59           C  
ATOM   1223  OE1 GLU B  14      26.276  31.109  68.356  1.00 89.60           O  
ATOM   1224  OE2 GLU B  14      27.021  30.345  70.283  1.00 90.59           O  
ATOM   1225  N   GLU B  15      21.052  30.680  67.667  1.00 83.48           N  
ATOM   1226  CA AGLU B  15      20.033  30.799  66.624  0.50 83.49           C  
ATOM   1227  CA BGLU B  15      20.038  30.819  66.608  0.50 83.57           C  
ATOM   1228  C   GLU B  15      19.319  32.156  66.567  1.00 83.05           C  
ATOM   1229  O   GLU B  15      18.856  32.577  65.511  1.00 83.52           O  
ATOM   1230  CB AGLU B  15      18.969  29.703  66.796  0.50 83.96           C  
ATOM   1231  CB BGLU B  15      19.001  29.686  66.637  0.50 83.78           C  
ATOM   1232  CG AGLU B  15      19.498  28.263  66.842  0.50 84.53           C  
ATOM   1233  CG BGLU B  15      19.534  28.285  66.365  0.50 84.16           C  
ATOM   1234  CD AGLU B  15      20.348  27.956  68.080  0.50 84.75           C  
ATOM   1235  CD BGLU B  15      18.427  27.235  66.411  0.50 84.25           C  
ATOM   1236  OE1AGLU B  15      20.323  28.748  69.051  0.50 84.87           O  
ATOM   1237  OE1BGLU B  15      17.287  27.593  66.780  0.50 84.55           O  
ATOM   1238  OE2AGLU B  15      20.996  26.887  68.101  0.50 84.62           O  
ATOM   1239  OE2BGLU B  15      18.694  26.055  66.094  0.50 84.33           O  
ATOM   1240  N   THR B  16      19.210  32.823  67.704  1.00 81.76           N  
ATOM   1241  CA  THR B  16      18.541  34.109  67.745  1.00 80.45           C  
ATOM   1242  C   THR B  16      19.474  35.282  67.460  1.00 80.30           C  
ATOM   1243  O   THR B  16      19.239  36.080  66.539  1.00 80.76           O  
ATOM   1244  CB  THR B  16      17.885  34.322  69.112  1.00 80.40           C  
ATOM   1245  OG1 THR B  16      16.940  33.274  69.342  1.00 80.30           O  
ATOM   1246  CG2 THR B  16      17.182  35.677  69.186  1.00 79.91           C  
ATOM   1247  N   PHE B  17      20.547  35.390  68.234  1.00 79.07           N  
ATOM   1248  CA  PHE B  17      21.463  36.496  68.020  1.00 77.53           C  
ATOM   1249  C   PHE B  17      22.397  36.380  66.834  1.00 76.67           C  
ATOM   1250  O   PHE B  17      22.913  37.401  66.366  1.00 77.23           O  
ATOM   1251  CB  PHE B  17      22.298  36.777  69.266  1.00 77.32           C  
ATOM   1252  CG  PHE B  17      23.171  35.628  69.711  1.00 76.55           C  
ATOM   1253  CD1 PHE B  17      22.769  34.788  70.730  1.00 76.51           C  
ATOM   1254  CD2 PHE B  17      24.393  35.398  69.112  1.00 76.32           C  
ATOM   1255  CE1 PHE B  17      23.583  33.757  71.163  1.00 76.46           C  
ATOM   1256  CE2 PHE B  17      25.205  34.364  69.536  1.00 76.79           C  
ATOM   1257  CZ  PHE B  17      24.795  33.538  70.561  1.00 76.70           C  
ATOM   1258  N   LEU B  18      22.624  35.168  66.339  1.00 74.99           N  
ATOM   1259  CA  LEU B  18      23.525  35.057  65.227  1.00 73.59           C  
ATOM   1260  C   LEU B  18      22.777  34.747  63.973  1.00 72.33           C  
ATOM   1261  O   LEU B  18      22.225  33.660  63.839  1.00 72.04           O  
ATOM   1262  CB  LEU B  18      24.573  33.992  65.489  1.00 74.38           C  
ATOM   1263  CG  LEU B  18      25.689  33.884  64.443  1.00 74.96           C  
ATOM   1264  CD1 LEU B  18      26.650  32.789  64.881  1.00 75.29           C  
ATOM   1265  CD2 LEU B  18      25.178  33.586  63.056  1.00 75.39           C  
ATOM   1266  N   THR B  19      22.780  35.707  63.048  1.00 71.04           N  
ATOM   1267  CA  THR B  19      22.100  35.555  61.770  1.00 69.65           C  
ATOM   1268  C   THR B  19      23.135  35.244  60.690  1.00 69.22           C  
ATOM   1269  O   THR B  19      24.166  35.925  60.586  1.00 68.73           O  
ATOM   1270  CB  THR B  19      21.398  36.851  61.352  1.00 69.30           C  
ATOM   1271  OG1 THR B  19      20.535  37.308  62.393  1.00 69.51           O  
ATOM   1272  CG2 THR B  19      20.615  36.656  60.066  1.00 68.88           C  
ATOM   1273  N   PRO B  20      22.877  34.196  59.892  1.00 68.49           N  
ATOM   1274  CA  PRO B  20      23.805  33.827  58.829  1.00 67.83           C  
ATOM   1275  C   PRO B  20      23.561  34.634  57.542  1.00 67.21           C  
ATOM   1276  O   PRO B  20      22.411  34.895  57.174  1.00 67.30           O  
ATOM   1277  CB  PRO B  20      23.526  32.336  58.616  1.00 67.89           C  
ATOM   1278  CG  PRO B  20      22.146  32.090  59.179  1.00 67.72           C  
ATOM   1279  CD  PRO B  20      21.713  33.295  59.965  1.00 68.11           C  
ATOM   1280  N   ALA B  21      24.652  35.021  56.880  1.00 66.09           N  
ATOM   1281  CA  ALA B  21      24.630  35.799  55.641  1.00 64.69           C  
ATOM   1282  C   ALA B  21      23.653  35.215  54.663  1.00 63.95           C  
ATOM   1283  O   ALA B  21      23.062  35.905  53.848  1.00 63.73           O  
ATOM   1284  CB  ALA B  21      25.988  35.777  55.034  1.00 65.01           C  
ATOM   1285  N   LYS B  22      23.534  33.907  54.764  1.00 63.54           N  
ATOM   1286  CA  LYS B  22      22.680  33.080  53.964  1.00 62.78           C  
ATOM   1287  C   LYS B  22      21.254  33.667  53.998  1.00 61.96           C  
ATOM   1288  O   LYS B  22      20.482  33.503  53.054  1.00 60.59           O  
ATOM   1289  CB  LYS B  22      22.760  31.697  54.618  1.00 63.07           C  
ATOM   1290  CG  LYS B  22      24.240  31.253  54.795  1.00 63.28           C  
ATOM   1291  CD  LYS B  22      24.473  29.895  55.504  1.00 63.63           C  
ATOM   1292  CE  LYS B  22      23.910  28.674  54.757  1.00 63.91           C  
ATOM   1293  NZ  LYS B  22      24.182  27.386  55.481  1.00 63.60           N  
ATOM   1294  N   ASN B  23      20.937  34.383  55.084  1.00 61.91           N  
ATOM   1295  CA  ASN B  23      19.626  35.022  55.294  1.00 62.31           C  
ATOM   1296  C   ASN B  23      19.629  36.549  55.276  1.00 63.06           C  
ATOM   1297  O   ASN B  23      18.569  37.161  55.392  1.00 63.39           O  
ATOM   1298  CB  ASN B  23      19.060  34.660  56.659  1.00 62.21           C  
ATOM   1299  CG  ASN B  23      18.878  33.185  56.849  1.00 62.28           C  
ATOM   1300  OD1 ASN B  23      19.195  32.387  55.973  1.00 62.49           O  
ATOM   1301  ND2 ASN B  23      18.378  32.807  58.017  1.00 61.83           N  
ATOM   1302  N   LEU B  24      20.810  37.163  55.187  1.00 63.73           N  
ATOM   1303  CA  LEU B  24      20.953  38.638  55.162  1.00 63.96           C  
ATOM   1304  C   LEU B  24      21.087  39.246  53.770  1.00 64.01           C  
ATOM   1305  O   LEU B  24      21.435  38.553  52.803  1.00 64.73           O  
ATOM   1306  CB  LEU B  24      22.219  39.053  55.926  1.00 63.72           C  
ATOM   1307  CG  LEU B  24      22.370  38.783  57.412  1.00 63.83           C  
ATOM   1308  CD1 LEU B  24      23.779  39.050  57.873  1.00 63.56           C  
ATOM   1309  CD2 LEU B  24      21.331  39.590  58.190  1.00 64.08           C  
ATOM   1310  N   ALA B  25      20.824  40.546  53.676  1.00 63.32           N  
ATOM   1311  CA  ALA B  25      20.943  41.245  52.412  1.00 62.91           C  
ATOM   1312  C   ALA B  25      22.317  41.896  52.455  1.00 62.94           C  
ATOM   1313  O   ALA B  25      22.674  42.537  53.452  1.00 62.35           O  
ATOM   1314  CB  ALA B  25      19.872  42.308  52.273  1.00 62.46           C  
ATOM   1315  N   VAL B  26      23.117  41.690  51.418  1.00 63.18           N  
ATOM   1316  CA  VAL B  26      24.442  42.301  51.401  1.00 63.81           C  
ATOM   1317  C   VAL B  26      24.558  43.060  50.084  1.00 64.26           C  
ATOM   1318  O   VAL B  26      23.783  42.829  49.158  1.00 64.73           O  
ATOM   1319  CB  VAL B  26      25.581  41.261  51.510  1.00 63.72           C  
ATOM   1320  CG1 VAL B  26      25.372  40.384  52.720  1.00 63.59           C  
ATOM   1321  CG2 VAL B  26      25.609  40.376  50.304  1.00 64.36           C  
ATOM   1322  N   LEU B  27      25.500  43.986  50.005  1.00 65.18           N  
ATOM   1323  CA  LEU B  27      25.703  44.763  48.793  1.00 65.89           C  
ATOM   1324  C   LEU B  27      27.107  44.503  48.268  1.00 67.74           C  
ATOM   1325  O   LEU B  27      28.057  44.497  49.064  1.00 68.52           O  
ATOM   1326  CB  LEU B  27      25.624  46.245  49.120  1.00 65.03           C  
ATOM   1327  CG  LEU B  27      24.407  46.977  49.692  1.00 65.12           C  
ATOM   1328  CD1 LEU B  27      24.719  48.427  49.989  1.00 64.76           C  
ATOM   1329  CD2 LEU B  27      23.210  46.927  48.762  1.00 65.55           C  
ATOM   1330  N   ILE B  28      27.269  44.256  46.964  1.00 68.73           N  
ATOM   1331  CA  ILE B  28      28.632  44.030  46.454  1.00 69.78           C  
ATOM   1332  C   ILE B  28      29.386  45.352  46.526  1.00 70.08           C  
ATOM   1333  O   ILE B  28      28.780  46.413  46.363  1.00 69.87           O  
ATOM   1334  CB  ILE B  28      28.702  43.499  44.999  1.00 70.18           C  
ATOM   1335  CG1 ILE B  28      28.057  44.495  44.020  1.00 70.38           C  
ATOM   1336  CG2 ILE B  28      28.067  42.135  44.893  1.00 70.73           C  
ATOM   1337  CD1 ILE B  28      28.121  44.072  42.556  1.00 70.08           C  
ATOM   1338  N   ASP B  29      30.699  45.299  46.745  1.00 70.80           N  
ATOM   1339  CA  ASP B  29      31.505  46.533  46.838  1.00 72.31           C  
ATOM   1340  C   ASP B  29      31.526  47.474  45.607  1.00 71.20           C  
ATOM   1341  O   ASP B  29      31.952  48.632  45.705  1.00 70.37           O  
ATOM   1342  CB  ASP B  29      32.945  46.207  47.234  1.00 74.26           C  
ATOM   1343  CG  ASP B  29      33.619  45.306  46.239  1.00 76.33           C  
ATOM   1344  OD1 ASP B  29      34.868  45.182  46.283  1.00 77.53           O  
ATOM   1345  OD2 ASP B  29      32.894  44.751  45.385  1.00 77.32           O  
ATOM   1346  N   THR B  30      31.055  46.978  44.471  1.00 70.11           N  
ATOM   1347  CA  THR B  30      31.036  47.767  43.255  1.00 69.84           C  
ATOM   1348  C   THR B  30      29.659  48.311  42.890  1.00 70.01           C  
ATOM   1349  O   THR B  30      29.415  48.647  41.741  1.00 69.92           O  
ATOM   1350  CB  THR B  30      31.532  46.924  42.085  1.00 69.49           C  
ATOM   1351  OG1 THR B  30      30.649  45.805  41.924  1.00 68.86           O  
ATOM   1352  CG2 THR B  30      32.974  46.441  42.338  1.00 68.74           C  
ATOM   1353  N   HIS B  31      28.756  48.396  43.861  1.00 70.93           N  
ATOM   1354  CA  HIS B  31      27.409  48.907  43.603  1.00 70.68           C  
ATOM   1355  C   HIS B  31      27.636  50.416  43.595  1.00 69.97           C  
ATOM   1356  O   HIS B  31      28.419  50.907  44.406  1.00 69.34           O  
ATOM   1357  CB  HIS B  31      26.467  48.508  44.745  1.00 71.03           C  
ATOM   1358  CG  HIS B  31      25.021  48.759  44.453  1.00 72.15           C  
ATOM   1359  ND1 HIS B  31      24.180  47.766  43.994  1.00 72.41           N  
ATOM   1360  CD2 HIS B  31      24.281  49.892  44.486  1.00 72.73           C  
ATOM   1361  CE1 HIS B  31      22.977  48.268  43.787  1.00 72.42           C  
ATOM   1362  NE2 HIS B  31      23.011  49.557  44.073  1.00 72.61           N  
ATOM   1363  N   ASN B  32      26.997  51.168  42.701  1.00 69.82           N  
ATOM   1364  CA  ASN B  32      27.253  52.610  42.724  1.00 69.35           C  
ATOM   1365  C   ASN B  32      26.655  53.202  44.007  1.00 68.85           C  
ATOM   1366  O   ASN B  32      25.640  52.735  44.520  1.00 68.57           O  
ATOM   1367  CB  ASN B  32      26.808  53.352  41.443  1.00 69.51           C  
ATOM   1368  CG  ASN B  32      25.308  53.455  41.288  1.00 69.23           C  
ATOM   1369  OD1 ASN B  32      24.551  53.308  42.236  1.00 70.24           O  
ATOM   1370  ND2 ASN B  32      24.885  53.818  40.112  1.00 69.04           N  
ATOM   1371  N   ALA B  33      27.305  54.214  44.542  1.00 68.84           N  
ATOM   1372  CA  ALA B  33      26.830  54.827  45.759  1.00 69.78           C  
ATOM   1373  C   ALA B  33      25.423  55.385  45.643  1.00 70.48           C  
ATOM   1374  O   ALA B  33      24.625  55.290  46.573  1.00 70.59           O  
ATOM   1375  CB  ALA B  33      27.787  55.924  46.199  1.00 69.75           C  
ATOM   1376  N   ASP B  34      25.103  55.960  44.500  1.00 71.22           N  
ATOM   1377  CA  ASP B  34      23.782  56.526  44.330  1.00 71.97           C  
ATOM   1378  C   ASP B  34      22.592  55.507  44.459  1.00 71.82           C  
ATOM   1379  O   ASP B  34      21.642  55.740  45.229  1.00 71.57           O  
ATOM   1380  CB  ASP B  34      23.764  57.333  43.036  1.00 73.42           C  
ATOM   1381  CG  ASP B  34      22.467  58.058  42.818  1.00 74.92           C  
ATOM   1382  OD1 ASP B  34      21.552  57.937  43.651  1.00 76.14           O  
ATOM   1383  OD2 ASP B  34      22.351  58.769  41.807  1.00 75.90           O  
ATOM   1384  N   HIS B  35      22.636  54.376  43.756  1.00 70.65           N  
ATOM   1385  CA  HIS B  35      21.533  53.428  43.870  1.00 69.70           C  
ATOM   1386  C   HIS B  35      21.620  52.732  45.252  1.00 69.39           C  
ATOM   1387  O   HIS B  35      20.602  52.285  45.808  1.00 68.70           O  
ATOM   1388  CB  HIS B  35      21.543  52.432  42.700  1.00 70.29           C  
ATOM   1389  CG  HIS B  35      20.329  51.550  42.632  1.00 70.59           C  
ATOM   1390  ND1 HIS B  35      20.223  50.357  43.316  1.00 70.74           N  
ATOM   1391  CD2 HIS B  35      19.176  51.682  41.932  1.00 70.68           C  
ATOM   1392  CE1 HIS B  35      19.050  49.804  43.058  1.00 70.85           C  
ATOM   1393  NE2 HIS B  35      18.395  50.589  42.220  1.00 70.71           N  
ATOM   1394  N   ALA B  36      22.836  52.651  45.810  1.00 68.89           N  
ATOM   1395  CA  ALA B  36      23.040  52.026  47.124  1.00 68.00           C  
ATOM   1396  C   ALA B  36      22.215  52.848  48.093  1.00 68.13           C  
ATOM   1397  O   ALA B  36      21.509  52.314  48.941  1.00 69.14           O  
ATOM   1398  CB  ALA B  36      24.477  52.049  47.522  1.00 66.54           C  
ATOM   1399  N   THR B  37      22.276  54.160  47.928  1.00 67.84           N  
ATOM   1400  CA  THR B  37      21.525  55.062  48.782  1.00 67.82           C  
ATOM   1401  C   THR B  37      20.035  54.682  48.735  1.00 66.83           C  
ATOM   1402  O   THR B  37      19.429  54.422  49.766  1.00 66.55           O  
ATOM   1403  CB  THR B  37      21.772  56.565  48.401  1.00 68.33           C  
ATOM   1404  OG1 THR B  37      23.158  56.883  48.569  1.00 68.62           O  
ATOM   1405  CG2 THR B  37      20.974  57.506  49.287  1.00 68.51           C  
ATOM   1406  N   LEU B  38      19.447  54.646  47.546  1.00 66.28           N  
ATOM   1407  CA  LEU B  38      18.032  54.289  47.409  1.00 66.01           C  
ATOM   1408  C   LEU B  38      17.737  52.939  48.031  1.00 66.04           C  
ATOM   1409  O   LEU B  38      16.830  52.770  48.857  1.00 65.93           O  
ATOM   1410  CB  LEU B  38      17.648  54.191  45.913  1.00 65.67           C  
ATOM   1411  CG  LEU B  38      16.266  53.733  45.371  1.00 65.33           C  
ATOM   1412  CD1 LEU B  38      15.966  52.263  45.651  1.00 65.09           C  
ATOM   1413  CD2 LEU B  38      15.107  54.584  45.842  1.00 65.22           C  
ATOM   1414  N   LEU B  39      18.554  51.982  47.627  1.00 65.50           N  
ATOM   1415  CA  LEU B  39      18.430  50.619  48.059  1.00 64.67           C  
ATOM   1416  C   LEU B  39      18.491  50.524  49.575  1.00 63.19           C  
ATOM   1417  O   LEU B  39      17.622  49.966  50.262  1.00 60.84           O  
ATOM   1418  CB  LEU B  39      19.555  49.850  47.360  1.00 65.05           C  
ATOM   1419  CG  LEU B  39      19.537  48.336  47.343  1.00 65.25           C  
ATOM   1420  CD1 LEU B  39      18.279  47.921  46.611  1.00 64.73           C  
ATOM   1421  CD2 LEU B  39      20.739  47.884  46.573  1.00 65.76           C  
ATOM   1422  N   LEU B  40      19.506  51.175  50.083  1.00 63.17           N  
ATOM   1423  CA  LEU B  40      19.757  51.196  51.491  1.00 63.96           C  
ATOM   1424  C   LEU B  40      18.691  51.899  52.358  1.00 64.34           C  
ATOM   1425  O   LEU B  40      18.495  51.537  53.521  1.00 65.41           O  
ATOM   1426  CB  LEU B  40      21.175  51.711  51.677  1.00 63.04           C  
ATOM   1427  CG  LEU B  40      21.827  51.689  53.027  1.00 63.18           C  
ATOM   1428  CD1 LEU B  40      21.734  50.289  53.627  1.00 62.28           C  
ATOM   1429  CD2 LEU B  40      23.274  52.114  52.757  1.00 63.36           C  
ATOM   1430  N   SER B  41      17.967  52.859  51.792  1.00 64.63           N  
ATOM   1431  CA  SER B  41      16.930  53.574  52.540  1.00 64.24           C  
ATOM   1432  C   SER B  41      15.636  52.792  52.521  1.00 64.56           C  
ATOM   1433  O   SER B  41      14.621  53.283  52.979  1.00 64.90           O  
ATOM   1434  CB  SER B  41      16.609  54.913  51.885  1.00 64.15           C  
ATOM   1435  OG  SER B  41      16.032  54.736  50.598  1.00 63.64           O  
ATOM   1436  N   GLN B  42      15.647  51.608  51.931  1.00 65.20           N  
ATOM   1437  CA  GLN B  42      14.447  50.800  51.866  1.00 65.87           C  
ATOM   1438  C   GLN B  42      14.615  49.659  52.836  1.00 66.83           C  
ATOM   1439  O   GLN B  42      13.660  49.014  53.235  1.00 67.09           O  
ATOM   1440  CB  GLN B  42      14.266  50.272  50.445  1.00 65.54           C  
ATOM   1441  CG  GLN B  42      14.186  51.395  49.454  1.00 65.07           C  
ATOM   1442  CD  GLN B  42      13.004  52.291  49.701  1.00 64.80           C  
ATOM   1443  OE1 GLN B  42      11.927  51.827  50.055  1.00 64.74           O  
ATOM   1444  NE2 GLN B  42      13.171  53.572  49.422  1.00 64.97           N  
HETATM 1445  N   MSE B  43      15.850  49.450  53.249  1.00 68.50           N  
HETATM 1446  CA  MSE B  43      16.169  48.390  54.164  1.00 70.20           C  
HETATM 1447  C   MSE B  43      15.896  48.727  55.588  1.00 70.21           C  
HETATM 1448  O   MSE B  43      15.929  49.877  56.006  1.00 68.82           O  
HETATM 1449  CB  MSE B  43      17.611  48.032  54.011  1.00 71.07           C  
HETATM 1450  CG  MSE B  43      17.873  47.660  52.625  1.00 71.98           C  
HETATM 1451 SE   MSE B  43      19.707  47.356  52.621  0.50 73.13          SE  
HETATM 1452  CE  MSE B  43      19.949  47.025  50.712  1.00 72.29           C  
ATOM   1453  N   THR B  44      15.700  47.659  56.338  1.00 71.83           N  
ATOM   1454  CA  THR B  44      15.397  47.796  57.755  1.00 72.46           C  
ATOM   1455  C   THR B  44      16.625  48.188  58.554  1.00 72.89           C  
ATOM   1456  O   THR B  44      16.567  49.130  59.345  1.00 73.30           O  
ATOM   1457  CB  THR B  44      14.748  46.542  58.323  1.00 72.37           C  
ATOM   1458  N   TYR B  45      17.729  47.496  58.338  1.00 73.14           N  
ATOM   1459  CA  TYR B  45      18.953  47.789  59.025  1.00 73.50           C  
ATOM   1460  C   TYR B  45      19.572  49.117  58.726  1.00 72.80           C  
ATOM   1461  O   TYR B  45      19.347  49.706  57.669  1.00 72.04           O  
ATOM   1462  CB  TYR B  45      19.936  46.674  58.730  1.00 75.70           C  
ATOM   1463  CG  TYR B  45      19.323  45.386  59.162  1.00 76.83           C  
ATOM   1464  CD1 TYR B  45      19.433  44.956  60.481  1.00 77.31           C  
ATOM   1465  CD2 TYR B  45      18.578  44.622  58.277  1.00 77.19           C  
ATOM   1466  CE1 TYR B  45      18.844  43.793  60.907  1.00 77.31           C  
ATOM   1467  CE2 TYR B  45      17.986  43.446  58.690  1.00 77.36           C  
ATOM   1468  CZ  TYR B  45      18.121  43.034  60.009  1.00 77.17           C  
ATOM   1469  OH  TYR B  45      17.524  41.858  60.440  1.00 77.34           O  
ATOM   1470  N   THR B  46      20.342  49.589  59.703  1.00 72.20           N  
ATOM   1471  CA  THR B  46      21.040  50.851  59.589  1.00 71.11           C  
ATOM   1472  C   THR B  46      22.388  50.630  58.914  1.00 69.97           C  
ATOM   1473  O   THR B  46      22.940  51.558  58.323  1.00 69.53           O  
ATOM   1474  CB  THR B  46      21.208  51.540  60.929  1.00 71.21           C  
ATOM   1475  OG1 THR B  46      19.921  51.926  61.404  1.00 71.96           O  
ATOM   1476  CG2 THR B  46      21.998  52.804  60.758  1.00 71.93           C  
ATOM   1477  N   ARG B  47      22.908  49.402  58.996  1.00 70.06           N  
ATOM   1478  CA  ARG B  47      24.207  49.056  58.370  1.00 70.01           C  
ATOM   1479  C   ARG B  47      24.143  47.702  57.658  1.00 68.50           C  
ATOM   1480  O   ARG B  47      23.464  46.785  58.112  1.00 68.28           O  
ATOM   1481  CB  ARG B  47      25.373  49.064  59.373  1.00 70.63           C  
ATOM   1482  CG  ARG B  47      25.469  50.373  60.122  1.00 73.27           C  
ATOM   1483  CD  ARG B  47      26.739  50.525  60.924  1.00 75.34           C  
ATOM   1484  NE  ARG B  47      27.862  50.507  59.986  1.00 76.88           N  
ATOM   1485  CZ  ARG B  47      28.317  51.586  59.348  1.00 77.50           C  
ATOM   1486  NH1 ARG B  47      27.740  52.768  59.543  1.00 78.14           N  
ATOM   1487  NH2 ARG B  47      29.338  51.485  58.501  1.00 78.00           N  
ATOM   1488  N   VAL B  48      24.811  47.585  56.521  1.00 67.16           N  
ATOM   1489  CA  VAL B  48      24.794  46.315  55.809  1.00 66.89           C  
ATOM   1490  C   VAL B  48      26.201  45.939  55.463  1.00 65.80           C  
ATOM   1491  O   VAL B  48      27.027  46.796  55.200  1.00 65.93           O  
ATOM   1492  CB  VAL B  48      23.981  46.336  54.530  1.00 66.63           C  
ATOM   1493  CG1 VAL B  48      22.596  46.726  54.857  1.00 67.26           C  
ATOM   1494  CG2 VAL B  48      24.559  47.316  53.567  1.00 67.40           C  
ATOM   1495  N   PRO B  49      26.486  44.652  55.516  1.00 64.91           N  
ATOM   1496  CA  PRO B  49      27.800  44.180  55.205  1.00 64.64           C  
ATOM   1497  C   PRO B  49      28.033  44.342  53.732  1.00 64.52           C  
ATOM   1498  O   PRO B  49      27.083  44.316  52.966  1.00 65.45           O  
ATOM   1499  CB  PRO B  49      27.722  42.705  55.557  1.00 64.78           C  
ATOM   1500  CG  PRO B  49      26.291  42.363  55.490  1.00 64.78           C  
ATOM   1501  CD  PRO B  49      25.573  43.575  55.920  1.00 65.01           C  
ATOM   1502  N   VAL B  50      29.283  44.563  53.358  1.00 64.37           N  
ATOM   1503  CA  VAL B  50      29.677  44.731  51.972  1.00 64.50           C  
ATOM   1504  C   VAL B  50      30.642  43.624  51.642  1.00 64.73           C  
ATOM   1505  O   VAL B  50      31.574  43.327  52.403  1.00 63.03           O  
ATOM   1506  CB  VAL B  50      30.361  46.093  51.679  1.00 64.48           C  
ATOM   1507  CG1 VAL B  50      30.889  46.125  50.283  1.00 64.17           C  
ATOM   1508  CG2 VAL B  50      29.420  47.250  51.903  1.00 64.08           C  
ATOM   1509  N   VAL B  51      30.418  43.034  50.477  1.00 66.25           N  
ATOM   1510  CA  VAL B  51      31.240  41.939  50.006  1.00 67.52           C  
ATOM   1511  C   VAL B  51      31.733  42.049  48.550  1.00 68.83           C  
ATOM   1512  O   VAL B  51      31.210  42.822  47.738  1.00 69.12           O  
ATOM   1513  CB  VAL B  51      30.464  40.640  50.203  1.00 66.97           C  
ATOM   1514  CG1 VAL B  51      30.206  40.406  51.678  1.00 66.81           C  
ATOM   1515  CG2 VAL B  51      29.155  40.736  49.469  1.00 67.04           C  
ATOM   1516  N   THR B  52      32.761  41.265  48.237  1.00 70.29           N  
ATOM   1517  CA  THR B  52      33.338  41.246  46.906  1.00 71.30           C  
ATOM   1518  C   THR B  52      32.450  40.302  46.093  1.00 72.72           C  
ATOM   1519  O   THR B  52      31.605  39.601  46.659  1.00 72.66           O  
ATOM   1520  CB  THR B  52      34.777  40.665  46.921  1.00 71.04           C  
ATOM   1521  OG1 THR B  52      34.762  39.254  47.181  1.00 70.87           O  
ATOM   1522  CG2 THR B  52      35.661  41.400  47.930  1.00 70.64           C  
ATOM   1523  N   ASP B  53      32.643  40.270  44.776  1.00 74.20           N  
ATOM   1524  CA  ASP B  53      31.843  39.395  43.897  1.00 75.30           C  
ATOM   1525  C   ASP B  53      31.884  37.913  44.305  1.00 75.58           C  
ATOM   1526  O   ASP B  53      30.977  37.139  43.981  1.00 75.75           O  
ATOM   1527  CB  ASP B  53      32.284  39.528  42.428  1.00 75.93           C  
ATOM   1528  CG  ASP B  53      33.740  39.108  42.197  1.00 76.29           C  
ATOM   1529  OD1 ASP B  53      34.158  39.073  41.022  1.00 75.91           O  
ATOM   1530  OD2 ASP B  53      34.459  38.787  43.174  1.00 76.77           O  
ATOM   1531  N   GLU B  54      32.949  37.524  45.001  1.00 75.73           N  
ATOM   1532  CA  GLU B  54      33.109  36.145  45.445  1.00 75.18           C  
ATOM   1533  C   GLU B  54      32.875  35.993  46.945  1.00 74.17           C  
ATOM   1534  O   GLU B  54      33.545  35.195  47.608  1.00 74.29           O  
ATOM   1535  CB  GLU B  54      34.476  35.602  45.045  1.00 76.08           C  
ATOM   1536  CG  GLU B  54      35.632  36.400  45.616  1.00 77.24           C  
ATOM   1537  CD  GLU B  54      36.958  35.835  45.188  1.00 77.83           C  
ATOM   1538  OE1 GLU B  54      36.954  34.848  44.423  1.00 78.04           O  
ATOM   1539  OE2 GLU B  54      38.000  36.376  45.608  1.00 78.39           O  
ATOM   1540  N   LYS B  55      31.947  36.802  47.462  1.00 72.45           N  
ATOM   1541  CA  LYS B  55      31.541  36.807  48.873  1.00 70.65           C  
ATOM   1542  C   LYS B  55      32.591  37.170  49.947  1.00 69.59           C  
ATOM   1543  O   LYS B  55      32.414  36.818  51.107  1.00 68.87           O  
ATOM   1544  CB  LYS B  55      30.893  35.456  49.189  1.00 70.46           C  
ATOM   1545  CG  LYS B  55      29.698  35.083  48.283  1.00 70.40           C  
ATOM   1546  CD  LYS B  55      29.192  33.658  48.625  1.00 71.12           C  
ATOM   1547  CE  LYS B  55      28.041  33.130  47.739  1.00 71.14           C  
ATOM   1548  NZ  LYS B  55      26.781  33.931  47.794  1.00 71.71           N  
ATOM   1549  N   GLN B  56      33.676  37.849  49.565  1.00 69.05           N  
ATOM   1550  CA  GLN B  56      34.728  38.258  50.522  1.00 68.32           C  
ATOM   1551  C   GLN B  56      34.242  39.399  51.370  1.00 67.79           C  
ATOM   1552  O   GLN B  56      33.748  40.397  50.854  1.00 68.01           O  
ATOM   1553  CB  GLN B  56      36.036  38.682  49.829  1.00 68.74           C  
ATOM   1554  CG  GLN B  56      36.802  37.561  49.159  1.00 68.57           C  
ATOM   1555  CD  GLN B  56      37.309  36.579  50.192  1.00 68.48           C  
ATOM   1556  OE1 GLN B  56      37.595  35.430  49.888  1.00 68.61           O  
ATOM   1557  NE2 GLN B  56      37.367  37.021  51.439  1.00 68.64           N  
ATOM   1558  N   PHE B  57      34.379  39.263  52.679  1.00 67.13           N  
ATOM   1559  CA  PHE B  57      33.930  40.324  53.542  1.00 66.06           C  
ATOM   1560  C   PHE B  57      34.766  41.553  53.396  1.00 66.65           C  
ATOM   1561  O   PHE B  57      35.964  41.525  53.652  1.00 67.96           O  
ATOM   1562  CB  PHE B  57      33.887  39.925  54.994  1.00 64.94           C  
ATOM   1563  CG  PHE B  57      33.557  41.069  55.882  1.00 64.56           C  
ATOM   1564  CD1 PHE B  57      32.242  41.494  56.022  1.00 63.85           C  
ATOM   1565  CD2 PHE B  57      34.561  41.728  56.584  1.00 64.35           C  
ATOM   1566  CE1 PHE B  57      31.939  42.574  56.815  1.00 63.74           C  
ATOM   1567  CE2 PHE B  57      34.263  42.805  57.402  1.00 64.59           C  
ATOM   1568  CZ  PHE B  57      32.948  43.229  57.520  1.00 64.30           C  
ATOM   1569  N   VAL B  58      34.119  42.640  53.003  1.00 66.36           N  
ATOM   1570  CA  VAL B  58      34.808  43.897  52.818  1.00 66.23           C  
ATOM   1571  C   VAL B  58      34.613  44.856  53.994  1.00 66.95           C  
ATOM   1572  O   VAL B  58      35.583  45.470  54.463  1.00 67.99           O  
ATOM   1573  CB  VAL B  58      34.338  44.595  51.525  1.00 66.08           C  
ATOM   1574  CG1 VAL B  58      34.970  45.961  51.408  1.00 65.30           C  
ATOM   1575  CG2 VAL B  58      34.639  43.730  50.292  1.00 65.74           C  
ATOM   1576  N   GLY B  59      33.372  45.007  54.467  1.00 66.23           N  
ATOM   1577  CA  GLY B  59      33.106  45.909  55.590  1.00 65.19           C  
ATOM   1578  C   GLY B  59      31.638  46.250  55.672  1.00 64.84           C  
ATOM   1579  O   GLY B  59      30.828  45.644  54.980  1.00 64.68           O  
ATOM   1580  N   THR B  60      31.283  47.200  56.532  1.00 64.56           N  
ATOM   1581  CA  THR B  60      29.887  47.590  56.662  1.00 65.38           C  
ATOM   1582  C   THR B  60      29.674  48.971  56.092  1.00 65.30           C  
ATOM   1583  O   THR B  60      30.631  49.714  55.892  1.00 64.65           O  
ATOM   1584  CB  THR B  60      29.401  47.578  58.090  1.00 66.18           C  
ATOM   1585  OG1 THR B  60      30.239  48.432  58.872  1.00 67.38           O  
ATOM   1586  CG2 THR B  60      29.472  46.182  58.659  1.00 66.97           C  
ATOM   1587  N   ILE B  61      28.412  49.308  55.827  1.00 65.82           N  
ATOM   1588  CA  ILE B  61      28.091  50.612  55.269  1.00 65.99           C  
ATOM   1589  C   ILE B  61      26.663  51.071  55.528  1.00 66.68           C  
ATOM   1590  O   ILE B  61      25.708  50.290  55.466  1.00 67.94           O  
ATOM   1591  CB  ILE B  61      28.263  50.604  53.763  1.00 65.85           C  
ATOM   1592  CG1 ILE B  61      28.276  52.030  53.234  1.00 66.01           C  
ATOM   1593  CG2 ILE B  61      27.213  49.704  53.099  1.00 65.30           C  
ATOM   1594  CD1 ILE B  61      28.532  52.116  51.773  1.00 65.95           C  
ATOM   1595  N   GLY B  62      26.508  52.352  55.800  1.00 66.72           N  
ATOM   1596  CA  GLY B  62      25.184  52.890  56.055  1.00 66.80           C  
ATOM   1597  C   GLY B  62      25.051  54.213  55.341  1.00 66.30           C  
ATOM   1598  O   GLY B  62      26.021  54.703  54.727  1.00 66.88           O  
ATOM   1599  N   LEU B  63      23.854  54.781  55.403  1.00 65.30           N  
ATOM   1600  CA  LEU B  63      23.590  56.060  54.770  1.00 65.00           C  
ATOM   1601  C   LEU B  63      24.546  57.171  55.217  1.00 65.45           C  
ATOM   1602  O   LEU B  63      24.913  58.028  54.406  1.00 64.59           O  
ATOM   1603  CB  LEU B  63      22.149  56.474  55.022  1.00 64.79           C  
ATOM   1604  CG  LEU B  63      21.108  55.578  54.363  1.00 64.53           C  
ATOM   1605  CD1 LEU B  63      19.649  55.937  54.765  1.00 63.81           C  
ATOM   1606  CD2 LEU B  63      21.348  55.701  52.862  1.00 64.36           C  
ATOM   1607  N   ARG B  64      24.938  57.177  56.494  1.00 66.51           N  
ATOM   1608  CA  ARG B  64      25.847  58.209  56.939  1.00 68.15           C  
ATOM   1609  C   ARG B  64      27.171  58.089  56.206  1.00 68.46           C  
ATOM   1610  O   ARG B  64      27.728  59.102  55.799  1.00 69.70           O  
ATOM   1611  CB  ARG B  64      26.064  58.224  58.432  1.00 69.96           C  
ATOM   1612  CG  ARG B  64      27.051  59.325  58.833  1.00 73.10           C  
ATOM   1613  CD  ARG B  64      27.248  59.343  60.329  1.00 75.76           C  
ATOM   1614  NE  ARG B  64      27.680  58.012  60.740  1.00 78.89           N  
ATOM   1615  CZ  ARG B  64      27.924  57.631  61.993  1.00 80.45           C  
ATOM   1616  NH1 ARG B  64      27.785  58.492  63.003  1.00 81.25           N  
ATOM   1617  NH2 ARG B  64      28.304  56.375  62.234  1.00 80.86           N  
ATOM   1618  N   ASP B  65      27.676  56.872  56.028  1.00 67.84           N  
ATOM   1619  CA  ASP B  65      28.940  56.678  55.320  1.00 67.90           C  
ATOM   1620  C   ASP B  65      28.845  57.338  53.959  1.00 66.51           C  
ATOM   1621  O   ASP B  65      29.733  58.082  53.552  1.00 66.13           O  
ATOM   1622  CB  ASP B  65      29.232  55.186  55.171  1.00 70.43           C  
ATOM   1623  CG  ASP B  65      29.487  54.482  56.521  1.00 73.07           C  
ATOM   1624  OD1 ASP B  65      28.798  53.462  56.763  1.00 74.45           O  
ATOM   1625  OD2 ASP B  65      30.257  54.991  57.395  1.00 73.64           O  
ATOM   1626  N   ILE B  66      27.748  57.079  53.262  1.00 64.92           N  
ATOM   1627  CA  ILE B  66      27.552  57.658  51.946  1.00 63.66           C  
ATOM   1628  C   ILE B  66      27.445  59.184  51.992  1.00 64.15           C  
ATOM   1629  O   ILE B  66      28.196  59.840  51.296  1.00 63.81           O  
ATOM   1630  CB  ILE B  66      26.390  57.004  51.255  1.00 62.79           C  
ATOM   1631  CG1 ILE B  66      26.677  55.515  51.165  1.00 61.88           C  
ATOM   1632  CG2 ILE B  66      26.169  57.597  49.882  1.00 62.05           C  
ATOM   1633  CD1 ILE B  66      25.633  54.795  50.423  1.00 62.19           C  
HETATM 1634  N   MSE B  67      26.481  59.752  52.731  1.00 64.63           N  
HETATM 1635  CA  MSE B  67      26.396  61.211  52.814  1.00 64.73           C  
HETATM 1636  C   MSE B  67      27.657  61.870  53.332  1.00 65.29           C  
HETATM 1637  O   MSE B  67      28.063  62.918  52.835  1.00 65.29           O  
HETATM 1638  CB  MSE B  67      25.183  61.744  53.585  1.00 65.39           C  
HETATM 1639  CG  MSE B  67      23.880  61.950  52.852  1.00 66.61           C  
HETATM 1640 SE   MSE B  67      23.007  60.642  51.824  0.50 68.00          SE  
HETATM 1641  CE  MSE B  67      24.348  60.357  50.484  1.00 67.91           C  
ATOM   1642  N   ALA B  68      28.283  61.279  54.336  1.00 65.27           N  
ATOM   1643  CA  ALA B  68      29.482  61.887  54.850  1.00 65.50           C  
ATOM   1644  C   ALA B  68      30.503  61.939  53.732  1.00 66.12           C  
ATOM   1645  O   ALA B  68      31.377  62.806  53.706  1.00 66.45           O  
ATOM   1646  CB  ALA B  68      30.010  61.109  56.025  1.00 65.47           C  
ATOM   1647  N   TYR B  69      30.372  61.025  52.785  1.00 66.62           N  
ATOM   1648  CA  TYR B  69      31.302  60.986  51.684  1.00 67.76           C  
ATOM   1649  C   TYR B  69      30.989  62.046  50.621  1.00 68.15           C  
ATOM   1650  O   TYR B  69      31.896  62.730  50.164  1.00 68.20           O  
ATOM   1651  CB  TYR B  69      31.310  59.601  51.111  1.00 69.63           C  
ATOM   1652  CG  TYR B  69      32.313  59.364  50.039  1.00 70.40           C  
ATOM   1653  CD1 TYR B  69      33.567  58.880  50.349  1.00 71.18           C  
ATOM   1654  CD2 TYR B  69      32.006  59.584  48.712  1.00 71.04           C  
ATOM   1655  CE1 TYR B  69      34.505  58.637  49.369  1.00 71.01           C  
ATOM   1656  CE2 TYR B  69      32.923  59.342  47.723  1.00 70.91           C  
ATOM   1657  CZ  TYR B  69      34.174  58.864  48.056  1.00 70.77           C  
ATOM   1658  OH  TYR B  69      35.098  58.606  47.063  1.00 70.84           O  
ATOM   1659  N   GLN B  70      29.731  62.197  50.217  1.00 68.35           N  
ATOM   1660  CA AGLN B  70      29.418  63.198  49.208  0.50 68.81           C  
ATOM   1661  CA BGLN B  70      29.378  63.197  49.226  0.50 69.27           C  
ATOM   1662  C   GLN B  70      29.892  64.545  49.695  1.00 69.19           C  
ATOM   1663  O   GLN B  70      30.599  65.252  48.977  1.00 69.46           O  
ATOM   1664  CB AGLN B  70      27.932  63.236  48.838  0.50 68.77           C  
ATOM   1665  CB BGLN B  70      27.854  63.315  49.075  0.50 69.59           C  
ATOM   1666  CG AGLN B  70      27.611  64.279  47.761  0.50 69.10           C  
ATOM   1667  CG BGLN B  70      27.108  62.071  48.580  0.50 70.60           C  
ATOM   1668  CD AGLN B  70      26.149  64.296  47.317  0.50 69.75           C  
ATOM   1669  CD BGLN B  70      25.575  62.266  48.503  0.50 70.93           C  
ATOM   1670  OE1AGLN B  70      25.324  63.509  47.783  0.50 70.57           O  
ATOM   1671  OE1BGLN B  70      25.023  63.246  49.023  0.50 71.57           O  
ATOM   1672  NE2AGLN B  70      25.829  65.196  46.396  0.50 70.31           N  
ATOM   1673  NE2BGLN B  70      24.888  61.304  47.885  0.50 71.56           N  
HETATM 1674  N   MSE B  71      29.508  64.872  50.917  1.00 69.76           N  
HETATM 1675  CA  MSE B  71      29.850  66.111  51.592  1.00 70.65           C  
HETATM 1676  C   MSE B  71      31.379  66.269  51.690  1.00 70.77           C  
HETATM 1677  O   MSE B  71      31.949  67.306  51.339  1.00 70.28           O  
HETATM 1678  CB  MSE B  71      29.184  66.073  52.966  1.00 71.47           C  
HETATM 1679  CG  MSE B  71      29.310  67.312  53.794  1.00 72.63           C  
HETATM 1680 SE   MSE B  71      28.459  68.845  52.974  0.50 73.44          SE  
HETATM 1681  CE  MSE B  71      29.452  69.062  51.328  1.00 73.88           C  
ATOM   1682  N   GLU B  72      32.044  65.249  52.208  1.00 71.36           N  
ATOM   1683  CA  GLU B  72      33.486  65.289  52.317  1.00 71.75           C  
ATOM   1684  C   GLU B  72      34.124  65.653  50.999  1.00 71.30           C  
ATOM   1685  O   GLU B  72      35.006  66.488  50.940  1.00 70.99           O  
ATOM   1686  CB  GLU B  72      33.988  63.895  52.696  1.00 73.55           C  
ATOM   1687  CG  GLU B  72      35.502  63.655  52.563  1.00 75.29           C  
ATOM   1688  CD  GLU B  72      36.377  64.532  53.406  1.00 76.66           C  
ATOM   1689  OE1 GLU B  72      37.617  64.505  53.207  1.00 77.22           O  
ATOM   1690  OE2 GLU B  72      35.835  65.267  54.253  1.00 78.59           O  
ATOM   1691  N   HIS B  73      33.641  65.047  49.923  1.00 71.65           N  
ATOM   1692  CA  HIS B  73      34.216  65.306  48.615  1.00 71.12           C  
ATOM   1693  C   HIS B  73      33.521  66.244  47.615  1.00 72.12           C  
ATOM   1694  O   HIS B  73      34.048  66.458  46.527  1.00 73.22           O  
ATOM   1695  CB  HIS B  73      34.568  63.973  47.993  1.00 70.04           C  
ATOM   1696  CG  HIS B  73      35.464  63.144  48.859  1.00 69.31           C  
ATOM   1697  ND1 HIS B  73      34.981  62.175  49.713  1.00 69.05           N  
ATOM   1698  CD2 HIS B  73      36.801  63.192  49.063  1.00 68.85           C  
ATOM   1699  CE1 HIS B  73      35.989  61.622  50.365  1.00 68.87           C  
ATOM   1700  NE2 HIS B  73      37.104  62.225  49.991  1.00 69.15           N  
ATOM   1701  N   ASP B  74      32.351  66.777  47.958  1.00 72.75           N  
ATOM   1702  CA  ASP B  74      31.615  67.707  47.081  1.00 72.37           C  
ATOM   1703  C   ASP B  74      31.223  67.096  45.737  1.00 71.59           C  
ATOM   1704  O   ASP B  74      31.317  67.724  44.692  1.00 70.43           O  
ATOM   1705  CB  ASP B  74      32.455  68.965  46.844  1.00 73.37           C  
ATOM   1706  CG  ASP B  74      31.708  70.036  46.057  1.00 74.61           C  
ATOM   1707  OD1 ASP B  74      32.379  70.910  45.450  1.00 74.66           O  
ATOM   1708  OD2 ASP B  74      30.453  69.985  46.017  1.00 75.13           O  
ATOM   1709  N   LEU B  75      30.804  65.847  45.765  1.00 71.81           N  
ATOM   1710  CA  LEU B  75      30.402  65.188  44.542  1.00 72.80           C  
ATOM   1711  C   LEU B  75      28.982  65.425  44.135  1.00 73.14           C  
ATOM   1712  O   LEU B  75      28.087  65.459  44.952  1.00 73.32           O  
ATOM   1713  CB  LEU B  75      30.674  63.687  44.603  1.00 73.08           C  
ATOM   1714  CG  LEU B  75      32.114  63.175  44.455  1.00 74.03           C  
ATOM   1715  CD1 LEU B  75      33.244  64.053  45.043  1.00 74.39           C  
ATOM   1716  CD2 LEU B  75      32.225  61.671  44.800  1.00 73.60           C  
ATOM   1717  N   SER B  76      28.794  65.572  42.836  1.00 74.34           N  
ATOM   1718  CA  SER B  76      27.489  65.789  42.259  1.00 74.50           C  
ATOM   1719  C   SER B  76      26.914  64.403  42.222  1.00 74.40           C  
ATOM   1720  O   SER B  76      27.601  63.435  42.557  1.00 73.85           O  
ATOM   1721  CB  SER B  76      27.658  66.188  40.810  1.00 74.63           C  
ATOM   1722  OG  SER B  76      28.301  65.119  40.117  1.00 74.18           O  
ATOM   1723  N   GLN B  77      25.672  64.285  41.779  1.00 74.48           N  
ATOM   1724  CA  GLN B  77      25.084  62.973  41.710  1.00 74.34           C  
ATOM   1725  C   GLN B  77      25.792  62.154  40.642  1.00 73.86           C  
ATOM   1726  O   GLN B  77      26.307  61.085  40.920  1.00 73.58           O  
ATOM   1727  CB  GLN B  77      23.632  63.036  41.316  1.00 75.08           C  
ATOM   1728  CG  GLN B  77      23.083  61.641  41.171  1.00 75.82           C  
ATOM   1729  CD  GLN B  77      21.694  61.611  40.620  1.00 76.11           C  
ATOM   1730  OE1 GLN B  77      21.102  62.649  40.331  1.00 76.87           O  
ATOM   1731  NE2 GLN B  77      21.168  60.412  40.431  1.00 76.52           N  
ATOM   1732  N   GLU B  78      25.800  62.657  39.411  1.00 73.84           N  
ATOM   1733  CA  GLU B  78      26.444  61.952  38.303  1.00 74.19           C  
ATOM   1734  C   GLU B  78      27.725  61.237  38.748  1.00 74.32           C  
ATOM   1735  O   GLU B  78      28.047  60.157  38.247  1.00 74.82           O  
ATOM   1736  CB  GLU B  78      26.707  62.903  37.104  1.00 74.10           C  
ATOM   1737  N   ILE B  79      28.454  61.837  39.686  1.00 74.02           N  
ATOM   1738  CA  ILE B  79      29.684  61.229  40.180  1.00 73.42           C  
ATOM   1739  C   ILE B  79      29.328  60.096  41.128  1.00 73.19           C  
ATOM   1740  O   ILE B  79      29.883  59.005  41.036  1.00 72.56           O  
ATOM   1741  CB  ILE B  79      30.598  62.263  40.806  1.00 73.05           C  
ATOM   1742  CG1 ILE B  79      30.991  63.273  39.722  1.00 72.38           C  
ATOM   1743  CG2 ILE B  79      31.828  61.595  41.352  1.00 72.31           C  
ATOM   1744  CD1 ILE B  79      31.863  64.407  40.193  1.00 72.11           C  
HETATM 1745  N   MSE B  80      28.391  60.362  42.029  1.00 73.86           N  
HETATM 1746  CA  MSE B  80      27.926  59.349  42.992  1.00 74.75           C  
HETATM 1747  C   MSE B  80      27.457  58.101  42.257  1.00 75.43           C  
HETATM 1748  O   MSE B  80      27.832  56.982  42.605  1.00 75.72           O  
HETATM 1749  CB  MSE B  80      26.816  59.927  43.904  1.00 74.38           C  
HETATM 1750  CG  MSE B  80      27.363  60.955  44.862  1.00 73.84           C  
HETATM 1751 SE   MSE B  80      28.459  59.892  46.050  0.50 74.08          SE  
HETATM 1752  CE  MSE B  80      29.492  61.234  46.895  1.00 74.53           C  
ATOM   1753  N   ALA B  81      26.658  58.308  41.216  1.00 76.01           N  
ATOM   1754  CA  ALA B  81      26.135  57.212  40.428  1.00 76.49           C  
ATOM   1755  C   ALA B  81      27.248  56.444  39.738  1.00 77.28           C  
ATOM   1756  O   ALA B  81      27.031  55.340  39.257  1.00 77.84           O  
ATOM   1757  CB  ALA B  81      25.130  57.722  39.415  1.00 76.07           C  
ATOM   1758  N   ASP B  82      28.450  57.000  39.691  1.00 78.15           N  
ATOM   1759  CA  ASP B  82      29.507  56.259  39.029  1.00 78.82           C  
ATOM   1760  C   ASP B  82      30.684  55.908  39.951  1.00 78.38           C  
ATOM   1761  O   ASP B  82      31.790  55.645  39.483  1.00 77.63           O  
ATOM   1762  CB  ASP B  82      30.017  57.026  37.829  1.00 80.44           C  
ATOM   1763  CG  ASP B  82      31.004  56.225  37.043  1.00 82.17           C  
ATOM   1764  OD1 ASP B  82      31.026  54.985  37.246  1.00 83.19           O  
ATOM   1765  OD2 ASP B  82      31.713  56.804  36.197  1.00 82.79           O  
ATOM   1766  N   THR B  83      30.435  55.894  41.260  1.00 77.91           N  
ATOM   1767  CA  THR B  83      31.464  55.577  42.247  1.00 77.07           C  
ATOM   1768  C   THR B  83      31.166  54.272  42.954  1.00 77.45           C  
ATOM   1769  O   THR B  83      30.029  54.016  43.319  1.00 77.99           O  
ATOM   1770  CB  THR B  83      31.521  56.648  43.326  1.00 76.24           C  
ATOM   1771  OG1 THR B  83      31.829  57.904  42.718  1.00 76.37           O  
ATOM   1772  CG2 THR B  83      32.584  56.301  44.347  1.00 75.80           C  
ATOM   1773  N   ASP B  84      32.177  53.443  43.164  1.00 77.50           N  
ATOM   1774  CA  ASP B  84      31.933  52.190  43.844  1.00 77.69           C  
ATOM   1775  C   ASP B  84      31.847  52.391  45.315  1.00 77.23           C  
ATOM   1776  O   ASP B  84      32.625  53.143  45.879  1.00 77.82           O  
ATOM   1777  CB  ASP B  84      33.022  51.176  43.554  1.00 78.96           C  
ATOM   1778  CG  ASP B  84      33.060  50.771  42.108  1.00 80.26           C  
ATOM   1779  OD1 ASP B  84      32.155  51.198  41.347  1.00 81.26           O  
ATOM   1780  OD2 ASP B  84      33.975  50.000  41.741  1.00 80.86           O  
ATOM   1781  N   ILE B  85      30.885  51.719  45.931  1.00 76.94           N  
ATOM   1782  CA  ILE B  85      30.678  51.802  47.376  1.00 77.20           C  
ATOM   1783  C   ILE B  85      31.931  51.525  48.193  1.00 75.47           C  
ATOM   1784  O   ILE B  85      32.108  52.049  49.288  1.00 74.55           O  
ATOM   1785  CB  ILE B  85      29.753  50.710  47.858  1.00 78.25           C  
ATOM   1786  CG1 ILE B  85      28.331  50.911  47.390  1.00 78.74           C  
ATOM   1787  CG2 ILE B  85      29.654  50.772  49.329  1.00 79.52           C  
ATOM   1788  CD1 ILE B  85      27.474  49.783  47.930  1.00 78.55           C  
ATOM   1789  N   VAL B  86      32.774  50.650  47.673  1.00 74.14           N  
ATOM   1790  CA  VAL B  86      33.987  50.306  48.361  1.00 73.29           C  
ATOM   1791  C   VAL B  86      34.757  51.524  48.856  1.00 72.65           C  
ATOM   1792  O   VAL B  86      35.381  51.488  49.924  1.00 72.53           O  
ATOM   1793  CB  VAL B  86      34.910  49.487  47.453  1.00 73.37           C  
ATOM   1794  CG1 VAL B  86      35.222  50.261  46.196  1.00 73.22           C  
ATOM   1795  CG2 VAL B  86      36.190  49.135  48.190  1.00 73.21           C  
ATOM   1796  N   HIS B  87      34.702  52.615  48.105  1.00 71.56           N  
ATOM   1797  CA  HIS B  87      35.431  53.797  48.521  1.00 71.00           C  
ATOM   1798  C   HIS B  87      34.855  54.495  49.739  1.00 71.33           C  
ATOM   1799  O   HIS B  87      35.482  55.417  50.261  1.00 71.86           O  
ATOM   1800  CB  HIS B  87      35.563  54.778  47.371  1.00 70.09           C  
ATOM   1801  CG  HIS B  87      36.196  54.179  46.166  1.00 69.89           C  
ATOM   1802  ND1 HIS B  87      37.560  54.026  46.043  1.00 70.36           N  
ATOM   1803  CD2 HIS B  87      35.657  53.709  45.019  1.00 69.93           C  
ATOM   1804  CE1 HIS B  87      37.835  53.467  44.877  1.00 69.76           C  
ATOM   1805  NE2 HIS B  87      36.697  53.264  44.236  1.00 69.85           N  
HETATM 1806  N   MSE B  88      33.701  54.041  50.222  1.00 70.99           N  
HETATM 1807  CA  MSE B  88      33.090  54.673  51.379  1.00 70.87           C  
HETATM 1808  C   MSE B  88      32.606  53.659  52.409  1.00 71.84           C  
HETATM 1809  O   MSE B  88      31.879  53.977  53.333  1.00 73.13           O  
HETATM 1810  CB  MSE B  88      32.005  55.604  50.867  1.00 70.51           C  
HETATM 1811  CG  MSE B  88      30.917  54.864  50.141  1.00 70.95           C  
HETATM 1812 SE   MSE B  88      29.902  56.135  49.126  0.50 69.65          SE  
HETATM 1813  CE  MSE B  88      31.416  56.602  48.035  1.00 69.54           C  
ATOM   1814  N   THR B  89      33.066  52.432  52.255  1.00 72.96           N  
ATOM   1815  CA  THR B  89      32.724  51.335  53.141  1.00 73.70           C  
ATOM   1816  C   THR B  89      33.635  51.449  54.343  1.00 73.67           C  
ATOM   1817  O   THR B  89      34.833  51.648  54.188  1.00 73.12           O  
ATOM   1818  CB  THR B  89      33.010  50.009  52.452  1.00 74.08           C  
ATOM   1819  OG1 THR B  89      32.267  49.950  51.232  1.00 74.51           O  
ATOM   1820  CG2 THR B  89      32.623  48.852  53.333  1.00 74.41           C  
ATOM   1821  N   LYS B  90      33.070  51.266  55.531  1.00 75.14           N  
ATOM   1822  CA  LYS B  90      33.819  51.368  56.772  1.00 76.18           C  
ATOM   1823  C   LYS B  90      34.503  50.000  56.828  1.00 76.25           C  
ATOM   1824  O   LYS B  90      33.859  48.967  56.907  1.00 76.29           O  
ATOM   1825  CB  LYS B  90      32.850  51.550  57.946  1.00 77.22           C  
ATOM   1826  CG  LYS B  90      33.459  52.204  59.183  1.00 78.16           C  
ATOM   1827  CD  LYS B  90      34.745  51.611  59.732  1.00 79.03           C  
ATOM   1828  CE  LYS B  90      35.192  52.477  60.929  1.00 78.89           C  
ATOM   1829  NZ  LYS B  90      36.507  52.103  61.554  1.00 79.16           N  
ATOM   1830  N   THR B  91      35.818  49.984  56.770  1.00 77.39           N  
ATOM   1831  CA  THR B  91      36.532  48.719  56.796  1.00 78.37           C  
ATOM   1832  C   THR B  91      37.206  48.490  58.142  1.00 78.62           C  
ATOM   1833  O   THR B  91      37.480  47.360  58.538  1.00 78.37           O  
ATOM   1834  CB  THR B  91      37.624  48.718  55.705  1.00 78.46           C  
ATOM   1835  OG1 THR B  91      38.598  49.722  56.008  1.00 78.89           O  
ATOM   1836  CG2 THR B  91      37.022  48.995  54.319  1.00 78.15           C  
ATOM   1837  N   ASP B  92      37.481  49.580  58.838  1.00 79.00           N  
ATOM   1838  CA  ASP B  92      38.120  49.492  60.119  1.00 79.61           C  
ATOM   1839  C   ASP B  92      37.055  49.196  61.147  1.00 79.47           C  
ATOM   1840  O   ASP B  92      36.748  50.030  61.982  1.00 79.54           O  
ATOM   1841  CB  ASP B  92      38.805  50.813  60.431  1.00 80.76           C  
ATOM   1842  CG  ASP B  92      39.536  50.793  61.761  1.00 81.62           C  
ATOM   1843  OD1 ASP B  92      39.548  49.737  62.443  1.00 81.96           O  
ATOM   1844  OD2 ASP B  92      40.113  51.841  62.118  1.00 81.96           O  
ATOM   1845  N   VAL B  93      36.510  47.992  61.095  1.00 79.52           N  
ATOM   1846  CA  VAL B  93      35.470  47.579  62.011  1.00 79.33           C  
ATOM   1847  C   VAL B  93      35.798  46.242  62.662  1.00 79.06           C  
ATOM   1848  O   VAL B  93      36.313  45.360  62.010  1.00 78.75           O  
ATOM   1849  CB  VAL B  93      34.124  47.500  61.245  1.00 79.43           C  
ATOM   1850  CG1 VAL B  93      34.270  46.646  59.997  1.00 79.44           C  
ATOM   1851  CG2 VAL B  93      33.000  46.986  62.141  1.00 79.66           C  
ATOM   1852  N   ALA B  94      35.495  46.100  63.949  1.00 79.71           N  
ATOM   1853  CA  ALA B  94      35.765  44.851  64.683  1.00 80.90           C  
ATOM   1854  C   ALA B  94      34.897  43.685  64.205  1.00 81.12           C  
ATOM   1855  O   ALA B  94      33.702  43.861  63.978  1.00 81.57           O  
ATOM   1856  CB  ALA B  94      35.575  45.059  66.192  1.00 80.50           C  
ATOM   1857  N   VAL B  95      35.483  42.496  64.073  1.00 81.02           N  
ATOM   1858  CA  VAL B  95      34.719  41.326  63.619  1.00 81.44           C  
ATOM   1859  C   VAL B  95      35.126  40.085  64.416  1.00 81.80           C  
ATOM   1860  O   VAL B  95      36.028  40.178  65.244  1.00 82.74           O  
ATOM   1861  CB  VAL B  95      34.988  41.056  62.135  1.00 81.61           C  
ATOM   1862  CG1 VAL B  95      34.623  42.284  61.314  1.00 82.05           C  
ATOM   1863  CG2 VAL B  95      36.448  40.735  61.912  1.00 80.90           C  
ATOM   1864  N   VAL B  96      34.470  38.936  64.194  1.00 81.52           N  
ATOM   1865  CA  VAL B  96      34.814  37.677  64.916  1.00 80.65           C  
ATOM   1866  C   VAL B  96      34.744  36.420  64.028  1.00 80.33           C  
ATOM   1867  O   VAL B  96      33.938  36.354  63.106  1.00 80.62           O  
ATOM   1868  CB  VAL B  96      33.915  37.411  66.158  1.00 80.38           C  
ATOM   1869  CG1 VAL B  96      34.104  38.493  67.228  1.00 79.98           C  
ATOM   1870  CG2 VAL B  96      32.455  37.262  65.754  1.00 80.22           C  
ATOM   1871  N   SER B  97      35.582  35.423  64.296  1.00 80.14           N  
ATOM   1872  CA  SER B  97      35.543  34.208  63.490  1.00 79.96           C  
ATOM   1873  C   SER B  97      34.296  33.472  63.951  1.00 79.94           C  
ATOM   1874  O   SER B  97      33.705  33.848  64.965  1.00 79.73           O  
ATOM   1875  CB  SER B  97      36.760  33.346  63.747  1.00 79.60           C  
ATOM   1876  OG  SER B  97      36.783  32.963  65.102  1.00 79.47           O  
ATOM   1877  N   PRO B  98      33.864  32.443  63.209  1.00 79.80           N  
ATOM   1878  CA  PRO B  98      32.662  31.737  63.658  1.00 80.04           C  
ATOM   1879  C   PRO B  98      32.867  31.030  65.003  1.00 80.67           C  
ATOM   1880  O   PRO B  98      31.971  30.322  65.481  1.00 80.76           O  
ATOM   1881  CB  PRO B  98      32.414  30.718  62.543  1.00 79.40           C  
ATOM   1882  CG  PRO B  98      33.193  31.219  61.385  1.00 79.35           C  
ATOM   1883  CD  PRO B  98      34.386  31.901  61.950  1.00 79.24           C  
ATOM   1884  N   ASP B  99      34.019  31.253  65.628  1.00 80.99           N  
ATOM   1885  CA  ASP B  99      34.303  30.612  66.906  1.00 81.41           C  
ATOM   1886  C   ASP B  99      34.364  31.520  68.112  1.00 81.02           C  
ATOM   1887  O   ASP B  99      35.053  31.225  69.081  1.00 81.15           O  
ATOM   1888  CB  ASP B  99      35.592  29.812  66.815  1.00 82.32           C  
ATOM   1889  CG  ASP B  99      35.533  28.788  65.731  1.00 83.09           C  
ATOM   1890  OD1 ASP B  99      36.442  27.937  65.652  1.00 83.15           O  
ATOM   1891  OD2 ASP B  99      34.545  28.833  64.966  1.00 83.71           O  
ATOM   1892  N   PHE B 100      33.658  32.634  68.028  1.00 80.47           N  
ATOM   1893  CA  PHE B 100      33.578  33.617  69.089  1.00 80.16           C  
ATOM   1894  C   PHE B 100      33.061  33.004  70.394  1.00 80.56           C  
ATOM   1895  O   PHE B 100      32.345  31.985  70.397  1.00 79.81           O  
ATOM   1896  CB  PHE B 100      32.524  34.634  68.671  1.00 80.42           C  
ATOM   1897  CG  PHE B 100      31.186  33.999  68.374  1.00 80.31           C  
ATOM   1898  CD1 PHE B 100      30.861  33.614  67.080  1.00 80.23           C  
ATOM   1899  CD2 PHE B 100      30.303  33.691  69.392  1.00 80.73           C  
ATOM   1900  CE1 PHE B 100      29.661  32.985  66.799  1.00 80.29           C  
ATOM   1901  CE2 PHE B 100      29.093  33.053  69.112  1.00 81.03           C  
ATOM   1902  CZ  PHE B 100      28.772  32.709  67.816  1.00 80.50           C  
ATOM   1903  N   THR B 101      33.420  33.654  71.499  1.00 81.00           N  
ATOM   1904  CA  THR B 101      32.998  33.235  72.825  1.00 81.84           C  
ATOM   1905  C   THR B 101      31.979  34.321  73.195  1.00 82.65           C  
ATOM   1906  O   THR B 101      32.113  35.467  72.764  1.00 83.11           O  
ATOM   1907  CB  THR B 101      34.139  33.235  73.851  1.00 81.43           C  
ATOM   1908  OG1 THR B 101      34.617  34.568  74.057  1.00 81.02           O  
ATOM   1909  CG2 THR B 101      35.271  32.327  73.402  1.00 81.02           C  
ATOM   1910  N   ILE B 102      30.950  33.984  73.961  1.00 83.02           N  
ATOM   1911  CA  ILE B 102      29.973  35.003  74.314  1.00 82.36           C  
ATOM   1912  C   ILE B 102      30.701  36.215  74.898  1.00 82.61           C  
ATOM   1913  O   ILE B 102      30.591  37.315  74.378  1.00 81.85           O  
ATOM   1914  CB  ILE B 102      28.962  34.488  75.319  1.00 82.08           C  
ATOM   1915  CG1 ILE B 102      28.274  33.220  74.809  1.00 82.49           C  
ATOM   1916  CG2 ILE B 102      27.966  35.545  75.589  1.00 82.56           C  
ATOM   1917  CD1 ILE B 102      27.525  33.373  73.512  1.00 82.53           C  
ATOM   1918  N   THR B 103      31.450  36.000  75.978  1.00 83.79           N  
ATOM   1919  CA  THR B 103      32.212  37.064  76.646  1.00 84.81           C  
ATOM   1920  C   THR B 103      32.896  37.983  75.607  1.00 85.24           C  
ATOM   1921  O   THR B 103      32.958  39.208  75.771  1.00 85.33           O  
ATOM   1922  CB  THR B 103      33.252  36.468  77.624  1.00 84.95           C  
ATOM   1923  OG1 THR B 103      34.151  35.619  76.903  1.00 85.43           O  
ATOM   1924  CG2 THR B 103      32.573  35.638  78.708  1.00 84.73           C  
ATOM   1925  N   GLU B 104      33.402  37.368  74.543  1.00 85.34           N  
ATOM   1926  CA  GLU B 104      34.068  38.072  73.450  1.00 86.09           C  
ATOM   1927  C   GLU B 104      33.059  38.929  72.686  1.00 85.10           C  
ATOM   1928  O   GLU B 104      33.311  40.099  72.452  1.00 85.58           O  
ATOM   1929  CB  GLU B 104      34.753  37.063  72.529  1.00 86.65           C  
ATOM   1930  CG  GLU B 104      35.373  37.621  71.270  1.00 87.85           C  
ATOM   1931  CD  GLU B 104      36.050  36.528  70.445  1.00 88.44           C  
ATOM   1932  OE1 GLU B 104      36.384  35.466  71.035  1.00 88.85           O  
ATOM   1933  OE2 GLU B 104      36.296  36.749  69.226  1.00 89.31           O  
ATOM   1934  N   VAL B 105      31.940  38.339  72.272  1.00 84.26           N  
ATOM   1935  CA  VAL B 105      30.885  39.064  71.551  1.00 83.08           C  
ATOM   1936  C   VAL B 105      30.432  40.309  72.306  1.00 83.93           C  
ATOM   1937  O   VAL B 105      30.639  41.407  71.828  1.00 85.14           O  
ATOM   1938  CB  VAL B 105      29.655  38.174  71.272  1.00 81.74           C  
ATOM   1939  CG1 VAL B 105      28.486  38.975  70.823  1.00 80.19           C  
ATOM   1940  CG2 VAL B 105      30.013  37.065  70.297  1.00 81.32           C  
ATOM   1941  N   LEU B 106      29.838  40.169  73.484  1.00 84.44           N  
ATOM   1942  CA  LEU B 106      29.407  41.357  74.206  1.00 85.49           C  
ATOM   1943  C   LEU B 106      30.473  42.408  74.343  1.00 86.77           C  
ATOM   1944  O   LEU B 106      30.157  43.595  74.390  1.00 87.22           O  
ATOM   1945  CB  LEU B 106      28.825  41.038  75.562  1.00 85.90           C  
ATOM   1946  CG  LEU B 106      27.540  40.247  75.492  1.00 86.02           C  
ATOM   1947  CD1 LEU B 106      27.801  38.963  74.795  1.00 86.49           C  
ATOM   1948  CD2 LEU B 106      27.118  40.000  76.908  1.00 87.04           C  
ATOM   1949  N   HIS B 107      31.727  41.986  74.475  1.00 88.59           N  
ATOM   1950  CA  HIS B 107      32.815  42.949  74.587  1.00 89.70           C  
ATOM   1951  C   HIS B 107      32.785  43.815  73.326  1.00 89.77           C  
ATOM   1952  O   HIS B 107      32.908  45.034  73.403  1.00 89.66           O  
ATOM   1953  CB  HIS B 107      34.166  42.249  74.747  1.00 91.44           C  
ATOM   1954  CG  HIS B 107      35.339  43.186  74.737  1.00 93.29           C  
ATOM   1955  ND1 HIS B 107      36.043  43.484  73.584  1.00 94.08           N  
ATOM   1956  CD2 HIS B 107      35.916  43.912  75.725  1.00 93.85           C  
ATOM   1957  CE1 HIS B 107      37.009  44.342  73.865  1.00 94.08           C  
ATOM   1958  NE2 HIS B 107      36.956  44.616  75.157  1.00 94.31           N  
ATOM   1959  N   LYS B 108      32.597  43.175  72.173  1.00 90.32           N  
ATOM   1960  CA  LYS B 108      32.544  43.872  70.892  1.00 91.31           C  
ATOM   1961  C   LYS B 108      31.252  44.693  70.731  1.00 91.52           C  
ATOM   1962  O   LYS B 108      31.302  45.813  70.192  1.00 92.12           O  
ATOM   1963  CB  LYS B 108      32.737  42.907  69.714  1.00 92.12           C  
ATOM   1964  CG  LYS B 108      34.061  42.155  69.714  1.00 92.35           C  
ATOM   1965  CD  LYS B 108      35.240  43.108  69.610  1.00 93.79           C  
ATOM   1966  CE  LYS B 108      36.603  42.383  69.631  1.00 93.65           C  
ATOM   1967  NZ  LYS B 108      36.769  41.409  68.522  1.00 94.05           N  
ATOM   1968  N   LEU B 109      30.105  44.172  71.175  1.00 90.24           N  
ATOM   1969  CA  LEU B 109      28.891  44.973  71.019  1.00 90.35           C  
ATOM   1970  C   LEU B 109      28.802  46.182  71.966  1.00 91.22           C  
ATOM   1971  O   LEU B 109      27.754  46.816  72.089  1.00 91.53           O  
ATOM   1972  CB  LEU B 109      27.563  44.205  71.074  1.00 89.45           C  
ATOM   1973  CG  LEU B 109      27.048  43.102  70.157  1.00 88.96           C  
ATOM   1974  CD1 LEU B 109      27.293  43.649  68.775  1.00 88.47           C  
ATOM   1975  CD2 LEU B 109      27.742  41.806  70.296  1.00 88.91           C  
ATOM   1976  N   VAL B 110      29.867  46.526  72.659  1.00 91.64           N  
ATOM   1977  CA  VAL B 110      29.699  47.675  73.509  1.00 92.54           C  
ATOM   1978  C   VAL B 110      30.407  48.833  72.783  1.00 93.09           C  
ATOM   1979  O   VAL B 110      29.970  49.983  72.834  1.00 93.30           O  
ATOM   1980  CB  VAL B 110      30.174  47.418  74.958  1.00 92.61           C  
ATOM   1981  CG1 VAL B 110      31.661  47.132  74.992  1.00 93.19           C  
ATOM   1982  CG2 VAL B 110      29.869  48.602  75.837  1.00 92.71           C  
ATOM   1983  N   ASP B 111      31.475  48.514  72.060  1.00 93.26           N  
ATOM   1984  CA AASP B 111      32.219  49.534  71.331  0.50 93.46           C  
ATOM   1985  CA BASP B 111      32.228  49.511  71.324  0.50 93.56           C  
ATOM   1986  C   ASP B 111      31.463  49.821  70.041  1.00 93.64           C  
ATOM   1987  O   ASP B 111      31.358  50.965  69.621  1.00 93.52           O  
ATOM   1988  CB AASP B 111      33.656  49.074  71.050  0.50 93.58           C  
ATOM   1989  CB BASP B 111      33.624  48.968  70.994  0.50 93.86           C  
ATOM   1990  CG AASP B 111      34.503  50.145  70.357  0.50 93.49           C  
ATOM   1991  CG BASP B 111      34.438  48.615  72.240  0.50 93.93           C  
ATOM   1992  OD1AASP B 111      35.682  49.861  70.045  0.50 93.28           O  
ATOM   1993  OD1BASP B 111      33.995  48.943  73.362  0.50 93.91           O  
ATOM   1994  OD2AASP B 111      34.002  51.268  70.131  0.50 93.37           O  
ATOM   1995  OD2BASP B 111      35.535  48.029  72.093  0.50 93.90           O  
ATOM   1996  N   GLU B 112      30.925  48.776  69.424  1.00 94.54           N  
ATOM   1997  CA  GLU B 112      30.161  48.899  68.182  1.00 95.54           C  
ATOM   1998  C   GLU B 112      28.801  48.228  68.377  1.00 95.00           C  
ATOM   1999  O   GLU B 112      28.522  47.700  69.450  1.00 95.18           O  
ATOM   2000  CB  GLU B 112      30.923  48.304  67.003  1.00 95.84           C  
ATOM   2001  CG  GLU B 112      31.265  46.841  67.159  1.00 97.16           C  
ATOM   2002  CD  GLU B 112      32.078  46.302  65.988  1.00 97.73           C  
ATOM   2003  OE1 GLU B 112      32.333  47.070  65.028  1.00 98.32           O  
ATOM   2004  OE2 GLU B 112      32.473  45.110  66.037  1.00 98.86           O  
ATOM   2005  N   SER B 113      27.959  48.228  67.354  1.00 94.48           N  
ATOM   2006  CA  SER B 113      26.639  47.615  67.496  1.00 94.38           C  
ATOM   2007  C   SER B 113      26.299  46.663  66.384  1.00 93.76           C  
ATOM   2008  O   SER B 113      25.198  46.115  66.340  1.00 93.76           O  
ATOM   2009  CB  SER B 113      25.572  48.698  67.442  1.00 94.86           C  
ATOM   2010  OG  SER B 113      25.619  49.340  66.179  1.00 95.57           O  
ATOM   2011  N   PHE B 114      27.224  46.466  65.467  1.00 93.11           N  
ATOM   2012  CA  PHE B 114      26.932  45.573  64.381  1.00 92.06           C  
ATOM   2013  C   PHE B 114      28.178  44.729  64.326  1.00 90.34           C  
ATOM   2014  O   PHE B 114      29.255  45.234  63.994  1.00 89.94           O  
ATOM   2015  CB  PHE B 114      26.785  46.415  63.140  1.00 93.38           C  
ATOM   2016  CG  PHE B 114      26.185  45.700  62.005  1.00 94.06           C  
ATOM   2017  CD1 PHE B 114      24.811  45.822  61.780  1.00 94.16           C  
ATOM   2018  CD2 PHE B 114      26.956  44.892  61.176  1.00 94.30           C  
ATOM   2019  CE1 PHE B 114      24.212  45.178  60.731  1.00 94.55           C  
ATOM   2020  CE2 PHE B 114      26.375  44.238  60.119  1.00 94.56           C  
ATOM   2021  CZ  PHE B 114      24.991  44.380  59.888  1.00 94.66           C  
ATOM   2022  N   LEU B 115      28.038  43.446  64.654  1.00 87.98           N  
ATOM   2023  CA  LEU B 115      29.191  42.563  64.662  1.00 85.99           C  
ATOM   2024  C   LEU B 115      29.170  41.440  63.617  1.00 84.97           C  
ATOM   2025  O   LEU B 115      28.454  40.453  63.755  1.00 84.90           O  
ATOM   2026  CB  LEU B 115      29.325  42.011  66.063  1.00 85.46           C  
ATOM   2027  CG  LEU B 115      30.529  41.162  66.350  1.00 85.38           C  
ATOM   2028  CD1 LEU B 115      31.747  42.026  66.135  1.00 85.68           C  
ATOM   2029  CD2 LEU B 115      30.438  40.725  67.782  1.00 85.17           C  
ATOM   2030  N   PRO B 116      29.977  41.599  62.560  1.00 84.32           N  
ATOM   2031  CA  PRO B 116      30.075  40.632  61.470  1.00 84.16           C  
ATOM   2032  C   PRO B 116      30.801  39.343  61.844  1.00 84.37           C  
ATOM   2033  O   PRO B 116      31.534  39.305  62.835  1.00 85.44           O  
ATOM   2034  CB  PRO B 116      30.892  41.394  60.414  1.00 83.32           C  
ATOM   2035  CG  PRO B 116      30.875  42.831  60.855  1.00 82.83           C  
ATOM   2036  CD  PRO B 116      30.849  42.762  62.322  1.00 83.40           C  
ATOM   2037  N   VAL B 117      30.596  38.288  61.067  1.00 83.39           N  
ATOM   2038  CA  VAL B 117      31.269  37.044  61.367  1.00 82.42           C  
ATOM   2039  C   VAL B 117      32.031  36.586  60.133  1.00 81.91           C  
ATOM   2040  O   VAL B 117      31.449  36.344  59.075  1.00 81.33           O  
ATOM   2041  CB  VAL B 117      30.323  35.982  61.928  1.00 82.60           C  
ATOM   2042  CG1 VAL B 117      31.083  34.680  62.209  1.00 82.66           C  
ATOM   2043  CG2 VAL B 117      29.706  36.491  63.200  1.00 82.25           C  
ATOM   2044  N   VAL B 118      33.349  36.487  60.294  1.00 81.83           N  
ATOM   2045  CA  VAL B 118      34.246  36.079  59.226  1.00 81.48           C  
ATOM   2046  C   VAL B 118      35.346  35.161  59.774  1.00 81.66           C  
ATOM   2047  O   VAL B 118      35.897  35.371  60.858  1.00 81.10           O  
ATOM   2048  CB  VAL B 118      34.925  37.320  58.647  1.00 81.27           C  
ATOM   2049  CG1 VAL B 118      35.706  36.962  57.418  1.00 81.50           C  
ATOM   2050  CG2 VAL B 118      33.887  38.322  58.259  1.00 81.43           C  
ATOM   2051  N   ASP B 119      35.666  34.133  59.010  1.00 82.44           N  
ATOM   2052  CA  ASP B 119      36.692  33.182  59.402  1.00 83.47           C  
ATOM   2053  C   ASP B 119      38.102  33.676  59.065  1.00 83.48           C  
ATOM   2054  O   ASP B 119      38.264  34.650  58.329  1.00 83.59           O  
ATOM   2055  CB  ASP B 119      36.420  31.851  58.704  1.00 84.30           C  
ATOM   2056  CG  ASP B 119      36.325  32.000  57.192  1.00 84.91           C  
ATOM   2057  OD1 ASP B 119      36.367  30.967  56.491  1.00 85.41           O  
ATOM   2058  OD2 ASP B 119      36.239  33.153  56.703  1.00 85.08           O  
ATOM   2059  N   ALA B 120      39.123  33.005  59.594  1.00 83.36           N  
ATOM   2060  CA  ALA B 120      40.499  33.407  59.317  1.00 83.20           C  
ATOM   2061  C   ALA B 120      40.774  33.294  57.819  1.00 83.50           C  
ATOM   2062  O   ALA B 120      41.929  33.287  57.377  1.00 84.17           O  
ATOM   2063  CB  ALA B 120      41.478  32.557  60.105  1.00 82.86           C  
ATOM   2064  N   GLU B 121      39.702  33.214  57.036  1.00 83.39           N  
ATOM   2065  CA  GLU B 121      39.813  33.102  55.585  1.00 83.18           C  
ATOM   2066  C   GLU B 121      39.488  34.425  54.857  1.00 82.97           C  
ATOM   2067  O   GLU B 121      40.240  34.866  53.985  1.00 82.32           O  
ATOM   2068  CB  GLU B 121      38.919  31.960  55.101  1.00 83.15           C  
ATOM   2069  CG  GLU B 121      38.970  31.711  53.618  1.00 83.71           C  
ATOM   2070  CD  GLU B 121      38.109  30.534  53.196  1.00 83.84           C  
ATOM   2071  OE1 GLU B 121      37.388  29.969  54.053  1.00 83.80           O  
ATOM   2072  OE2 GLU B 121      38.160  30.176  51.997  1.00 83.83           O  
ATOM   2073  N   GLY B 122      38.374  35.054  55.234  1.00 82.99           N  
ATOM   2074  CA  GLY B 122      37.940  36.316  54.636  1.00 83.24           C  
ATOM   2075  C   GLY B 122      36.484  36.276  54.207  1.00 83.30           C  
ATOM   2076  O   GLY B 122      35.883  37.298  53.872  1.00 83.18           O  
ATOM   2077  N   ILE B 123      35.928  35.073  54.237  1.00 83.79           N  
ATOM   2078  CA  ILE B 123      34.542  34.802  53.864  1.00 84.21           C  
ATOM   2079  C   ILE B 123      33.519  35.127  54.956  1.00 84.32           C  
ATOM   2080  O   ILE B 123      33.545  34.600  56.122  1.00 83.95           O  
ATOM   2081  CB  ILE B 123      34.353  33.276  53.561  1.00 84.67           C  
ATOM   2082  CG1 ILE B 123      35.336  32.807  52.482  1.00 84.79           C  
ATOM   2083  CG2 ILE B 123      32.890  32.949  53.194  1.00 84.88           C  
ATOM   2084  CD1 ILE B 123      35.204  33.562  51.136  1.00 85.02           C  
ATOM   2085  N   PHE B 124      32.597  36.063  54.554  1.00 83.67           N  
ATOM   2086  CA  PHE B 124      31.490  36.513  55.418  1.00 83.00           C  
ATOM   2087  C   PHE B 124      30.337  35.512  55.695  1.00 83.57           C  
ATOM   2088  O   PHE B 124      29.457  35.333  54.832  1.00 84.60           O  
ATOM   2089  CB  PHE B 124      30.912  37.796  54.829  1.00 81.27           C  
ATOM   2090  CG  PHE B 124      29.665  38.289  55.524  1.00 80.95           C  
ATOM   2091  CD1 PHE B 124      29.739  38.995  56.716  1.00 80.81           C  
ATOM   2092  CD2 PHE B 124      28.420  38.135  54.929  1.00 80.42           C  
ATOM   2093  CE1 PHE B 124      28.583  39.470  57.340  1.00 80.11           C  
ATOM   2094  CE2 PHE B 124      27.267  38.614  55.544  1.00 79.84           C  
ATOM   2095  CZ  PHE B 124      27.351  39.277  56.749  1.00 80.04           C  
ATOM   2096  N   GLN B 125      30.359  34.836  56.876  1.00 83.43           N  
ATOM   2097  CA  GLN B 125      29.260  33.899  57.202  1.00 83.69           C  
ATOM   2098  C   GLN B 125      28.066  34.522  57.909  1.00 83.07           C  
ATOM   2099  O   GLN B 125      26.960  33.968  57.816  1.00 83.75           O  
ATOM   2100  CB  GLN B 125      29.630  32.656  58.089  1.00 84.94           C  
ATOM   2101  CG  GLN B 125      30.527  31.474  57.513  1.00 86.87           C  
ATOM   2102  CD  GLN B 125      31.934  31.957  57.151  1.00 88.96           C  
ATOM   2103  OE1 GLN B 125      32.287  33.527  57.157  1.00 89.92           O  
ATOM   2104  NE2 GLN B 125      32.910  30.971  57.104  1.00 88.36           N  
ATOM   2105  N   GLY B 126      28.255  35.606  58.666  1.00 81.62           N  
ATOM   2106  CA  GLY B 126      27.079  36.159  59.342  1.00 79.60           C  
ATOM   2107  C   GLY B 126      27.158  37.398  60.196  1.00 78.19           C  
ATOM   2108  O   GLY B 126      28.169  38.102  60.217  1.00 78.56           O  
ATOM   2109  N   ILE B 127      26.074  37.631  60.937  1.00 76.73           N  
ATOM   2110  CA  ILE B 127      25.950  38.798  61.820  1.00 74.88           C  
ATOM   2111  C   ILE B 127      25.254  38.725  63.186  1.00 73.23           C  
ATOM   2112  O   ILE B 127      24.250  38.023  63.382  1.00 73.68           O  
ATOM   2113  CB  ILE B 127      25.378  39.985  61.019  1.00 74.78           C  
ATOM   2114  CG1 ILE B 127      26.515  40.546  60.190  1.00 75.97           C  
ATOM   2115  CG2 ILE B 127      25.009  41.123  61.880  1.00 74.38           C  
ATOM   2116  CD1 ILE B 127      26.153  41.752  59.348  1.00 76.75           C  
ATOM   2117  N   ILE B 128      25.822  39.477  64.121  1.00 70.75           N  
ATOM   2118  CA  ILE B 128      25.324  39.570  65.468  1.00 69.17           C  
ATOM   2119  C   ILE B 128      25.166  41.031  65.808  1.00 67.64           C  
ATOM   2120  O   ILE B 128      26.096  41.806  65.673  1.00 67.07           O  
ATOM   2121  CB  ILE B 128      26.289  38.970  66.449  1.00 69.37           C  
ATOM   2122  CG1 ILE B 128      26.500  37.497  66.114  1.00 69.21           C  
ATOM   2123  CG2 ILE B 128      25.723  39.102  67.852  1.00 69.58           C  
ATOM   2124  CD1 ILE B 128      27.472  36.814  67.032  1.00 69.04           C  
ATOM   2125  N   THR B 129      23.985  41.402  66.271  1.00 66.99           N  
ATOM   2126  CA  THR B 129      23.707  42.794  66.627  1.00 66.63           C  
ATOM   2127  C   THR B 129      23.128  43.029  68.024  1.00 65.68           C  
ATOM   2128  O   THR B 129      22.536  42.114  68.603  1.00 66.61           O  
ATOM   2129  CB  THR B 129      22.749  43.387  65.599  1.00 66.55           C  
ATOM   2130  OG1 THR B 129      21.594  42.541  65.510  1.00 66.39           O  
ATOM   2131  CG2 THR B 129      23.427  43.403  64.252  1.00 66.11           C  
ATOM   2132  N   ARG B 130      23.301  44.239  68.569  1.00 63.65           N  
ATOM   2133  CA  ARG B 130      22.759  44.514  69.893  1.00 62.58           C  
ATOM   2134  C   ARG B 130      21.301  44.057  69.859  1.00 62.74           C  
ATOM   2135  O   ARG B 130      20.875  43.234  70.679  1.00 63.02           O  
ATOM   2136  CB  ARG B 130      22.900  45.970  70.257  1.00 61.32           C  
ATOM   2137  CG  ARG B 130      24.328  46.427  70.325  1.00 60.54           C  
ATOM   2138  CD  ARG B 130      24.388  47.924  70.590  1.00 60.12           C  
ATOM   2139  NE  ARG B 130      25.757  48.410  70.611  1.00 60.40           N  
ATOM   2140  CZ  ARG B 130      26.090  49.697  70.658  1.00 61.48           C  
ATOM   2141  NH1 ARG B 130      25.141  50.621  70.630  1.00 62.07           N  
ATOM   2142  NH2 ARG B 130      27.368  50.075  70.660  1.00 61.25           N  
ATOM   2143  N   LYS B 131      20.570  44.544  68.866  1.00 61.95           N  
ATOM   2144  CA  LYS B 131      19.186  44.199  68.678  1.00 62.08           C  
ATOM   2145  C   LYS B 131      19.046  42.694  68.786  1.00 62.36           C  
ATOM   2146  O   LYS B 131      18.265  42.202  69.576  1.00 61.87           O  
ATOM   2147  CB  LYS B 131      18.785  44.637  67.276  1.00 63.12           C  
ATOM   2148  CG  LYS B 131      17.368  44.343  66.793  1.00 63.81           C  
ATOM   2149  CD  LYS B 131      17.291  44.813  65.331  1.00 65.04           C  
ATOM   2150  CE  LYS B 131      15.956  44.572  64.629  1.00 65.73           C  
ATOM   2151  NZ  LYS B 131      14.842  45.297  65.282  1.00 66.56           N  
ATOM   2152  N   SER B 132      19.829  41.950  68.012  1.00 64.39           N  
ATOM   2153  CA  SER B 132      19.749  40.473  68.047  1.00 66.61           C  
ATOM   2154  C   SER B 132      20.013  39.896  69.439  1.00 67.87           C  
ATOM   2155  O   SER B 132      19.446  38.863  69.823  1.00 68.57           O  
ATOM   2156  CB  SER B 132      20.622  39.812  66.973  1.00 67.32           C  
ATOM   2157  OG  SER B 132      21.993  40.145  67.111  1.00 68.17           O  
ATOM   2158  N   ILE B 133      20.891  40.542  70.193  1.00 67.84           N  
ATOM   2159  CA  ILE B 133      21.154  40.056  71.525  1.00 67.93           C  
ATOM   2160  C   ILE B 133      19.948  40.373  72.397  1.00 67.69           C  
ATOM   2161  O   ILE B 133      19.533  39.537  73.190  1.00 67.81           O  
ATOM   2162  CB  ILE B 133      22.470  40.528  72.048  1.00 68.57           C  
ATOM   2163  CG1 ILE B 133      23.532  39.695  71.343  1.00 68.47           C  
ATOM   2164  CG2 ILE B 133      22.601  40.178  73.478  1.00 68.23           C  
ATOM   2165  CD1 ILE B 133      24.900  40.056  71.726  1.00 69.42           C  
ATOM   2166  N   LEU B 134      19.374  41.564  72.262  1.00 67.28           N  
ATOM   2167  CA  LEU B 134      18.202  41.845  73.069  1.00 67.79           C  
ATOM   2168  C   LEU B 134      17.152  40.788  72.811  1.00 68.14           C  
ATOM   2169  O   LEU B 134      16.496  40.321  73.743  1.00 67.99           O  
ATOM   2170  CB  LEU B 134      17.575  43.213  72.811  1.00 68.37           C  
ATOM   2171  CG  LEU B 134      18.240  44.504  73.258  1.00 68.70           C  
ATOM   2172  CD1 LEU B 134      18.297  44.440  74.757  1.00 68.79           C  
ATOM   2173  CD2 LEU B 134      19.617  44.713  72.683  1.00 69.75           C  
ATOM   2174  N   LYS B 135      16.989  40.382  71.556  1.00 68.39           N  
ATOM   2175  CA  LYS B 135      15.977  39.373  71.331  1.00 69.51           C  
ATOM   2176  C   LYS B 135      16.269  38.175  72.204  1.00 69.04           C  
ATOM   2177  O   LYS B 135      15.355  37.620  72.807  1.00 69.35           O  
ATOM   2178  CB  LYS B 135      15.729  39.022  69.855  1.00 69.92           C  
ATOM   2179  CG  LYS B 135      15.300  40.253  69.057  1.00 71.30           C  
ATOM   2180  CD  LYS B 135      14.801  40.010  67.628  1.00 71.24           C  
ATOM   2181  CE  LYS B 135      13.487  39.204  67.645  1.00 72.48           C  
ATOM   2182  NZ  LYS B 135      12.847  38.998  66.286  1.00 72.34           N  
ATOM   2183  N   ALA B 136      17.549  37.835  72.346  1.00 68.71           N  
ATOM   2184  CA  ALA B 136      17.917  36.690  73.170  1.00 67.92           C  
ATOM   2185  C   ALA B 136      17.528  36.841  74.619  1.00 67.73           C  
ATOM   2186  O   ALA B 136      16.904  35.935  75.163  1.00 67.77           O  
ATOM   2187  CB  ALA B 136      19.376  36.355  73.055  1.00 67.91           C  
ATOM   2188  N   VAL B 137      17.856  37.965  75.258  1.00 67.40           N  
ATOM   2189  CA  VAL B 137      17.466  38.065  76.666  1.00 67.27           C  
ATOM   2190  C   VAL B 137      15.952  38.181  76.774  1.00 67.95           C  
ATOM   2191  O   VAL B 137      15.377  37.764  77.769  1.00 68.58           O  
ATOM   2192  CB  VAL B 137      18.090  39.208  77.429  1.00 65.98           C  
ATOM   2193  CG1 VAL B 137      19.579  39.139  77.267  1.00 65.69           C  
ATOM   2194  CG2 VAL B 137      17.584  40.488  76.910  1.00 66.22           C  
ATOM   2195  N   ASN B 138      15.278  38.733  75.779  1.00 67.68           N  
ATOM   2196  CA  ASN B 138      13.854  38.788  75.963  1.00 68.50           C  
ATOM   2197  C   ASN B 138      13.240  37.417  76.150  1.00 68.45           C  
ATOM   2198  O   ASN B 138      12.060  37.291  76.497  1.00 68.35           O  
ATOM   2199  CB  ASN B 138      13.135  39.650  74.937  1.00 69.91           C  
ATOM   2200  CG  ASN B 138      13.466  41.101  75.105  1.00 70.92           C  
ATOM   2201  OD1 ASN B 138      14.232  41.469  75.996  1.00 72.03           O  
ATOM   2202  ND2 ASN B 138      12.867  41.943  74.290  1.00 71.23           N  
ATOM   2203  N   ALA B 139      14.047  36.385  75.937  1.00 67.97           N  
ATOM   2204  CA  ALA B 139      13.547  35.021  76.111  1.00 68.12           C  
ATOM   2205  C   ALA B 139      13.328  34.750  77.611  1.00 67.50           C  
ATOM   2206  O   ALA B 139      12.726  33.750  77.982  1.00 68.20           O  
ATOM   2207  CB  ALA B 139      14.504  33.990  75.498  1.00 68.15           C  
ATOM   2208  N   LEU B 140      13.813  35.660  78.455  1.00 66.26           N  
ATOM   2209  CA  LEU B 140      13.691  35.559  79.894  1.00 65.83           C  
ATOM   2210  C   LEU B 140      12.664  36.540  80.381  1.00 67.42           C  
ATOM   2211  O   LEU B 140      12.296  36.533  81.543  1.00 67.27           O  
ATOM   2212  CB  LEU B 140      14.998  35.997  80.537  1.00 64.04           C  
ATOM   2213  CG  LEU B 140      16.302  35.269  80.292  1.00 62.38           C  
ATOM   2214  CD1 LEU B 140      17.444  35.992  80.985  1.00 61.59           C  
ATOM   2215  CD2 LEU B 140      16.134  33.878  80.817  1.00 61.96           C  
ATOM   2216  N   LEU B 141      12.211  37.395  79.477  1.00 70.22           N  
ATOM   2217  CA  LEU B 141      11.237  38.425  79.791  1.00 72.18           C  
ATOM   2218  C   LEU B 141       9.942  37.916  80.427  1.00 73.06           C  
ATOM   2219  O   LEU B 141       9.443  38.523  81.364  1.00 73.12           O  
ATOM   2220  CB  LEU B 141      10.899  39.225  78.537  1.00 72.72           C  
ATOM   2221  CG  LEU B 141      10.087  40.470  78.891  1.00 73.61           C  
ATOM   2222  CD1 LEU B 141      11.115  41.333  79.634  1.00 73.44           C  
ATOM   2223  CD2 LEU B 141       9.519  41.279  77.696  1.00 73.32           C  
ATOM   2224  N   HIS B 142       9.388  36.815  79.931  1.00 74.90           N  
ATOM   2225  CA  HIS B 142       8.144  36.298  80.506  1.00 76.87           C  
ATOM   2226  C   HIS B 142       8.296  35.977  81.986  1.00 78.48           C  
ATOM   2227  O   HIS B 142       7.312  35.947  82.699  1.00 79.04           O  
ATOM   2228  CB  HIS B 142       7.653  35.060  79.756  1.00 76.95           C  
ATOM   2229  CG  HIS B 142       8.590  33.893  79.835  1.00 77.26           C  
ATOM   2230  ND1 HIS B 142       9.652  33.723  78.970  1.00 77.33           N  
ATOM   2231  CD2 HIS B 142       8.605  32.818  80.658  1.00 77.19           C  
ATOM   2232  CE1 HIS B 142      10.293  32.607  79.272  1.00 76.92           C  
ATOM   2233  NE2 HIS B 142       9.678  32.039  80.292  1.00 76.96           N  
ATOM   2234  N   ASP B 143       9.529  35.742  82.435  1.00 80.97           N  
ATOM   2235  CA  ASP B 143       9.850  35.415  83.849  1.00 83.44           C  
ATOM   2236  C   ASP B 143      10.178  36.569  84.788  1.00 84.76           C  
ATOM   2237  O   ASP B 143      10.901  36.391  85.774  1.00 84.62           O  
ATOM   2238  CB  ASP B 143      10.986  34.385  83.937  1.00 84.24           C  
ATOM   2239  CG  ASP B 143      10.588  33.013  83.417  1.00 84.99           C  
ATOM   2240  OD1 ASP B 143       9.373  32.692  83.430  1.00 85.27           O  
ATOM   2241  OD2 ASP B 143      11.506  32.224  83.086  1.00 85.33           O  
ATOM   2242  N   PHE B 144       9.651  37.745  84.468  1.00 86.86           N  
ATOM   2243  CA  PHE B 144       9.848  38.972  85.258  1.00 89.40           C  
ATOM   2244  C   PHE B 144       8.667  39.383  86.128  1.00 90.28           C  
ATOM   2245  O   PHE B 144       7.540  39.508  85.650  1.00 90.55           O  
ATOM   2246  CB  PHE B 144      10.244  40.160  84.362  1.00 90.58           C  
ATOM   2247  CG  PHE B 144      11.678  40.140  83.863  1.00 91.32           C  
ATOM   2248  CD1 PHE B 144      12.094  39.289  82.860  1.00 91.89           C  
ATOM   2249  CD2 PHE B 144      12.575  41.108  84.315  1.00 91.28           C  
ATOM   2250  CE1 PHE B 144      13.413  39.337  82.403  1.00 92.04           C  
ATOM   2251  CE2 PHE B 144      13.872  41.173  83.848  1.00 91.07           C  
ATOM   2252  CZ  PHE B 144      14.294  40.289  82.901  1.00 91.36           C  
ATOM   2253  N   SER B 145       8.931  39.594  87.411  1.00 91.51           N  
ATOM   2254  CA  SER B 145       7.877  40.002  88.325  1.00 92.71           C  
ATOM   2255  C   SER B 145       7.729  41.510  88.113  1.00 93.15           C  
ATOM   2256  O   SER B 145       8.624  42.131  87.563  1.00 92.40           O  
ATOM   2257  CB  SER B 145       8.271  39.679  89.768  1.00 92.24           C  
ATOM   2258  N   LYS B 146       6.607  42.106  88.498  1.00 94.38           N  
ATOM   2259  CA  LYS B 146       6.477  43.549  88.303  1.00 95.22           C  
ATOM   2260  C   LYS B 146       7.456  44.245  89.240  1.00 95.60           C  
ATOM   2261  O   LYS B 146       8.063  43.598  90.093  1.00 95.61           O  
ATOM   2262  CB  LYS B 146       5.044  44.015  88.515  1.00 95.52           C  
ATOM   2263  CG  LYS B 146       4.124  43.290  87.569  1.00 96.39           C  
ATOM   2264  CD  LYS B 146       2.693  43.752  87.632  1.00 96.96           C  
ATOM   2265  CE  LYS B 146       1.842  42.923  86.660  1.00 97.38           C  
ATOM   2266  NZ  LYS B 146       2.311  43.001  85.245  1.00 97.91           N  
ATOM   2267  N   GLU B 147       7.640  45.549  89.076  1.00 96.31           N  
ATOM   2268  CA  GLU B 147       8.576  46.272  89.937  1.00 96.45           C  
ATOM   2269  C   GLU B 147       8.290  46.002  91.416  1.00 96.48           C  
ATOM   2270  O   GLU B 147       9.147  45.487  92.148  1.00 96.40           O  
ATOM   2271  CB  GLU B 147       8.545  47.774  89.634  1.00 96.64           C  
ATOM   2272  N   TYR B 148       7.072  46.324  91.839  1.00 96.36           N  
ATOM   2273  CA  TYR B 148       6.662  46.127  93.227  1.00 96.66           C  
ATOM   2274  C   TYR B 148       6.558  44.673  93.689  1.00 96.34           C  
ATOM   2275  O   TYR B 148       6.142  44.400  94.814  1.00 96.28           O  
ATOM   2276  CB  TYR B 148       5.359  46.876  93.534  1.00 96.98           C  
ATOM   2277  CG  TYR B 148       4.193  46.471  92.660  1.00 97.14           C  
ATOM   2278  CD1 TYR B 148       3.421  45.347  92.968  1.00 97.12           C  
ATOM   2279  CD2 TYR B 148       3.833  47.239  91.558  1.00 97.04           C  
ATOM   2280  CE1 TYR B 148       2.349  44.982  92.181  1.00 97.11           C  
ATOM   2281  CE2 TYR B 148       2.763  46.887  90.767  1.00 97.09           C  
ATOM   2282  CZ  TYR B 148       2.023  45.760  91.078  1.00 97.16           C  
ATOM   2283  OH  TYR B 148       0.952  45.418  90.283  1.00 97.01           O  
ATOM   2284  N   GLU B 149       6.902  43.736  92.820  1.00 96.35           N  
ATOM   2285  CA  GLU B 149       6.844  42.332  93.195  1.00 95.93           C  
ATOM   2286  C   GLU B 149       8.240  41.934  93.694  1.00 95.74           C  
ATOM   2287  O   GLU B 149       8.366  41.120  94.608  1.00 95.46           O  
ATOM   2288  CB  GLU B 149       6.415  41.477  92.029  1.00 95.50           C  
ATOM   2289  N   ILE B 150       9.276  42.546  93.111  1.00 95.47           N  
ATOM   2290  CA  ILE B 150      10.664  42.268  93.480  1.00 95.10           C  
ATOM   2291  C   ILE B 150      11.448  43.552  93.790  1.00 95.28           C  
ATOM   2292  O   ILE B 150      11.465  44.045  94.930  1.00 95.52           O  
ATOM   2293  CB  ILE B 150      11.344  41.471  92.379  1.00 94.35           C  
TER    2294      ILE B 150                                                      
HETATM 2295  C1  GOL A 154      17.434  72.062  61.317  0.50 62.71           C  
HETATM 2296  O1  GOL A 154      17.440  70.801  60.675  0.50 62.91           O  
HETATM 2297  C2  GOL A 154      16.993  71.866  62.766  0.50 62.28           C  
HETATM 2298  O2  GOL A 154      15.857  72.656  63.048  0.50 62.37           O  
HETATM 2299  C3  GOL A 154      18.136  72.228  63.702  0.50 61.25           C  
HETATM 2300  O3  GOL A 154      17.952  71.542  64.918  0.50 60.22           O  
HETATM 2301  P   PO4 B 154      27.528  53.482  69.574  0.50 63.08           P  
HETATM 2302  O1  PO4 B 154      28.303  54.698  69.133  0.50 62.57           O  
HETATM 2303  O2  PO4 B 154      26.984  52.788  68.341  0.50 62.40           O  
HETATM 2304  O3  PO4 B 154      28.490  52.627  70.372  0.50 62.18           O  
HETATM 2305  O4  PO4 B 154      26.345  53.854  70.444  0.50 62.71           O  
HETATM 2306  O   HOH A 155      21.713  49.620  68.282  1.00 46.13           O  
HETATM 2307  O   HOH A 156      18.127  52.633  64.385  1.00 60.59           O  
HETATM 2308  O   HOH A 157      10.897  48.260  87.729  1.00 67.92           O  
HETATM 2309  O   HOH A 158      18.477  55.440  61.216  1.00 67.36           O  
HETATM 2310  O   HOH A 159      15.938  48.722  65.437  1.00 41.39           O  
HETATM 2311  O   HOH A 160       9.300  53.452  87.163  1.00 88.71           O  
HETATM 2312  O   HOH A 161       4.731  45.985  72.807  1.00 72.94           O  
HETATM 2313  O   HOH A 162      14.497  75.841  58.375  1.00 54.28           O  
HETATM 2314  O   HOH A 163      31.178  54.381  76.413  1.00 73.37           O  
HETATM 2315  O   HOH A 164      25.639  54.342  76.109  1.00 56.52           O  
HETATM 2316  O   HOH A 165      26.267  64.866  67.672  1.00 76.83           O  
HETATM 2317  O   HOH A 166       6.275  45.779  85.291  1.00 74.20           O  
HETATM 2318  O   HOH A 167       5.424  61.575  84.693  1.00 81.30           O  
HETATM 2319  O   HOH A 168      10.072  52.916  59.076  1.00 62.67           O  
HETATM 2320  O   HOH B 155      19.764  34.187  63.638  1.00 90.23           O  
HETATM 2321  O   HOH B 156       4.640  40.590  90.719  1.00 55.05           O  
HETATM 2322  O   HOH B 157      13.493  41.159  62.794  1.00 77.05           O  
HETATM 2323  O   HOH B 158      37.320  52.649  57.736  1.00 68.26           O  
CONECT   17   20                                                                
CONECT   20   17   21                                                           
CONECT   21   20   22   24                                                      
CONECT   22   21   23   28                                                      
CONECT   23   22                                                                
CONECT   24   21   25                                                           
CONECT   25   24   26                                                           
CONECT   26   25   27                                                           
CONECT   27   26                                                                
CONECT   28   22                                                                
CONECT  342  349                                                                
CONECT  349  342  350                                                           
CONECT  350  349  351  353                                                      
CONECT  351  350  352  357                                                      
CONECT  352  351                                                                
CONECT  353  350  354                                                           
CONECT  354  353  355                                                           
CONECT  355  354  356                                                           
CONECT  356  355                                                                
CONECT  357  351                                                                
CONECT  506  512                                                                
CONECT  512  506  513                                                           
CONECT  513  512  514  516                                                      
CONECT  514  513  515  520                                                      
CONECT  515  514                                                                
CONECT  516  513  517                                                           
CONECT  517  516  518                                                           
CONECT  518  517  519                                                           
CONECT  519  518                                                                
CONECT  520  514                                                                
CONECT  539  546                                                                
CONECT  546  539  547                                                           
CONECT  547  546  548  550                                                      
CONECT  548  547  549  554                                                      
CONECT  549  548                                                                
CONECT  550  547  551                                                           
CONECT  551  550  552                                                           
CONECT  552  551  553                                                           
CONECT  553  552                                                                
CONECT  554  548                                                                
CONECT  615  621                                                                
CONECT  621  615  622                                                           
CONECT  622  621  623  625                                                      
CONECT  623  622  624  629                                                      
CONECT  624  623                                                                
CONECT  625  622  626                                                           
CONECT  626  625  627                                                           
CONECT  627  626  628                                                           
CONECT  628  627                                                                
CONECT  629  623                                                                
CONECT  674  682                                                                
CONECT  682  674  683                                                           
CONECT  683  682  684  686                                                      
CONECT  684  683  685  690                                                      
CONECT  685  684                                                                
CONECT  686  683  687                                                           
CONECT  687  686  688                                                           
CONECT  688  687  689                                                           
CONECT  689  688                                                                
CONECT  690  684                                                                
CONECT 1101 1104                                                                
CONECT 1104 1101 1105                                                           
CONECT 1105 1104 1106 1108                                                      
CONECT 1106 1105 1107 1112                                                      
CONECT 1107 1106                                                                
CONECT 1108 1105 1109                                                           
CONECT 1109 1108 1110                                                           
CONECT 1110 1109 1111                                                           
CONECT 1111 1110                                                                
CONECT 1112 1106                                                                
CONECT 1438 1445                                                                
CONECT 1445 1438 1446                                                           
CONECT 1446 1445 1447 1449                                                      
CONECT 1447 1446 1448 1453                                                      
CONECT 1448 1447                                                                
CONECT 1449 1446 1450                                                           
CONECT 1450 1449 1451                                                           
CONECT 1451 1450 1452                                                           
CONECT 1452 1451                                                                
CONECT 1453 1447                                                                
CONECT 1628 1634                                                                
CONECT 1634 1628 1635                                                           
CONECT 1635 1634 1636 1638                                                      
CONECT 1636 1635 1637 1642                                                      
CONECT 1637 1636                                                                
CONECT 1638 1635 1639                                                           
CONECT 1639 1638 1640                                                           
CONECT 1640 1639 1641                                                           
CONECT 1641 1640                                                                
CONECT 1642 1636                                                                
CONECT 1662 1674                                                                
CONECT 1674 1662 1675                                                           
CONECT 1675 1674 1676 1678                                                      
CONECT 1676 1675 1677 1682                                                      
CONECT 1677 1676                                                                
CONECT 1678 1675 1679                                                           
CONECT 1679 1678 1680                                                           
CONECT 1680 1679 1681                                                           
CONECT 1681 1680                                                                
CONECT 1682 1676                                                                
CONECT 1739 1745                                                                
CONECT 1745 1739 1746                                                           
CONECT 1746 1745 1747 1749                                                      
CONECT 1747 1746 1748 1753                                                      
CONECT 1748 1747                                                                
CONECT 1749 1746 1750                                                           
CONECT 1750 1749 1751                                                           
CONECT 1751 1750 1752                                                           
CONECT 1752 1751                                                                
CONECT 1753 1747                                                                
CONECT 1798 1806                                                                
CONECT 1806 1798 1807                                                           
CONECT 1807 1806 1808 1810                                                      
CONECT 1808 1807 1809 1814                                                      
CONECT 1809 1808                                                                
CONECT 1810 1807 1811                                                           
CONECT 1811 1810 1812                                                           
CONECT 1812 1811 1813                                                           
CONECT 1813 1812                                                                
CONECT 1814 1808                                                                
CONECT 2295 2296 2297                                                           
CONECT 2296 2295                                                                
CONECT 2297 2295 2298 2299                                                      
CONECT 2298 2297                                                                
CONECT 2299 2297 2300                                                           
CONECT 2300 2299                                                                
CONECT 2301 2302 2303 2304 2305                                                 
CONECT 2302 2301                                                                
CONECT 2303 2301                                                                
CONECT 2304 2301                                                                
CONECT 2305 2301                                                                
MASTER      485    0   14   21   12    0    3    6 2321    2  131   24          
END                                                                             
