path: root/plip/test/pdb/2q8q.pdb

HEADER    METAL TRANSPORT                         11-JUN-07   2Q8Q              
TITLE     CRYSTAL STRUCTURE OF S. AUREUS ISDE COMPLEXED WITH HEME               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON-REGULATED SURFACE DETERMINANT E;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 158879;                                              
SOURCE   4 STRAIN: N315;                                                        
SOURCE   5 GENE: ISDA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    HELICAL BACKBONE METAL RECEPTOR SUPERFAMILY, METAL TRANSPORT          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.GRIGG,M.E.MURPHY                                                  
REVDAT   4   13-JUL-11 2Q8Q    1       VERSN                                    
REVDAT   3   24-FEB-09 2Q8Q    1       VERSN                                    
REVDAT   2   09-OCT-07 2Q8Q    1       JRNL                                     
REVDAT   1   31-JUL-07 2Q8Q    0                                                
JRNL        AUTH   J.C.GRIGG,C.L.VERMEIREN,D.E.HEINRICHS,M.E.MURPHY             
JRNL        TITL   HEME COORDINATION BY STAPHYLOCOCCUS AUREUS ISDE.             
JRNL        REF    J.BIOL.CHEM.                  V. 282 28815 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17666394                                                     
JRNL        DOI    10.1074/JBC.M704602200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 16264                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 869                             
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1182                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2076                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 246                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.45000                                              
REMARK   3    B22 (A**2) : 1.45000                                              
REMARK   3    B33 (A**2) : -2.90000                                             
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): 0.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.151         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.222        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2169 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2939 ; 1.304 ; 2.041       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 5.715 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;35.595 ;25.914       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   414 ;16.652 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;21.539 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   317 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1601 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   987 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1471 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   188 ; 0.157 ; 0.200       
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):    10 ; 0.112 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.159 ; 0.200       
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):  1335 ; 0.562 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2104 ; 0.888 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   952 ; 1.546 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   833 ; 2.315 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    32        A    71                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.1016  50.4619  60.3705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1051 T22:   0.0537                                     
REMARK   3      T33:   0.0371 T12:  -0.0120                                     
REMARK   3      T13:  -0.0683 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4541 L22:   3.0939                                     
REMARK   3      L33:   5.9627 L12:   0.2421                                     
REMARK   3      L13:   0.4299 L23:   0.3459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3005 S12:   0.0770 S13:   0.1405                       
REMARK   3      S21:   0.1236 S22:   0.0935 S23:  -0.2758                       
REMARK   3      S31:  -0.4398 S32:   0.4382 S33:   0.2069                       
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    72        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3680  44.0323  48.6007              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0767 T22:   0.1993                                     
REMARK   3      T33:   0.0061 T12:  -0.0033                                     
REMARK   3      T13:   0.0892 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0289 L22:   4.3891                                     
REMARK   3      L33:   4.2957 L12:   1.2127                                     
REMARK   3      L13:   1.6594 L23:   0.7985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1804 S12:   0.4226 S13:  -0.0952                       
REMARK   3      S21:  -0.5646 S22:   0.1723 S23:  -0.4697                       
REMARK   3      S31:  -0.0425 S32:   0.8365 S33:   0.0081                       
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   116        A   209                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0517  34.9599  60.0654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1333 T22:   0.0109                                     
REMARK   3      T33:   0.0306 T12:   0.0330                                     
REMARK   3      T13:   0.0161 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1236 L22:   0.8703                                     
REMARK   3      L33:   1.3689 L12:   0.2913                                     
REMARK   3      L13:   0.2632 L23:   0.2331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0737 S12:  -0.0045 S13:  -0.2488                       
REMARK   3      S21:   0.1311 S22:   0.0415 S23:   0.0287                       
REMARK   3      S31:   0.1253 S32:  -0.0131 S33:   0.0322                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   210        A   218                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.7143  31.0382  40.3205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5937 T22:   0.4231                                     
REMARK   3      T33:   0.4247 T12:  -0.2794                                     
REMARK   3      T13:  -0.1701 T23:  -0.1294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  49.4913 L22:  11.8007                                     
REMARK   3      L33:   1.1814 L12:  20.7974                                     
REMARK   3      L13:   4.5206 L23:   3.4334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0254 S12:   2.2705 S13:  -0.6450                       
REMARK   3      S21:  -0.4148 S22:   0.1652 S23:   1.4428                       
REMARK   3      S31:   0.2661 S32:  -0.3748 S33:  -1.1906                       
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 :   A   219        A   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0573  45.1522  47.3063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1121 T22:   0.0011                                     
REMARK   3      T33:   0.0367 T12:   0.0596                                     
REMARK   3      T13:  -0.0600 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6902 L22:   4.7199                                     
REMARK   3      L33:   3.7544 L12:   2.4143                                     
REMARK   3      L13:  -1.0519 L23:  -0.6110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1177 S12:   0.1314 S13:   0.4687                       
REMARK   3      S21:  -0.1557 S22:   0.0045 S23:   0.2991                       
REMARK   3      S31:  -0.5450 S32:  -0.2244 S33:   0.1132                       
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 :   A   241        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3582  42.6121  53.5834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0966 T22:  -0.0443                                     
REMARK   3      T33:   0.0452 T12:   0.0525                                     
REMARK   3      T13:  -0.0027 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5702 L22:   2.1759                                     
REMARK   3      L33:   3.6738 L12:   0.2880                                     
REMARK   3      L13:   0.1421 L23:  -0.1244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0913 S12:   0.1208 S13:   0.1631                       
REMARK   3      S21:   0.0453 S22:  -0.0163 S23:   0.3296                       
REMARK   3      S31:  -0.2402 S32:  -0.3257 S33:   0.1076                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2Q8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043290.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR, DOUBLE    
REMARK 200                                   CRYSTAL MONOCHROMATOR, TOROID      
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17270                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2Q8P                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES, 0.2M AMMONIUM ACETATE, 28%    
REMARK 280  PEG 4000, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.49650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.10950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.10950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      108.74475            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.10950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.10950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       36.24825            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.10950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.10950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      108.74475            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.10950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.10950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       36.24825            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       72.49650            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    30                                                      
REMARK 465     SER A    31                                                      
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    GLU A 214   CG    GLU A 214   CD      0.094                       
REMARK 500    GLU A 214   CD    GLU A 214   OE2     0.112                       
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    GLU A 214   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 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    ARG A 138       36.92   -141.08                                   
REMARK 500    LEU A 216        6.86    -60.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A  78   SD                                                     
REMARK 620 2 HEM A 300   NA   86.4                                              
REMARK 620 3 HEM A 300   NB   86.3  87.6                                        
REMARK 620 4 HEM A 300   NC   88.7 174.0  88.8                                  
REMARK 620 5 HEM A 300   ND   92.0  92.7 178.2  90.8                            
REMARK 620 6 HIS A 229   NE2 177.9  93.3  91.6  91.5  90.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Q8P   RELATED DB: PDB                                   
DBREF  2Q8Q A   32   289  UNP    Q7A652   Q7A652_STAAN    32    289             
SEQADV 2Q8Q GLY A   30  UNP  Q7A652              EXPRESSION TAG                 
SEQADV 2Q8Q SER A   31  UNP  Q7A652              EXPRESSION TAG                 
SEQRES   1 A  260  GLY SER GLY GLU PHE ARG ILE VAL PRO THR THR VAL ALA          
SEQRES   2 A  260  LEU THR MET THR LEU ASP LYS LEU ASP LEU PRO ILE VAL          
SEQRES   3 A  260  GLY LYS PRO THR SER TYR LYS THR LEU PRO ASN ARG TYR          
SEQRES   4 A  260  LYS ASP VAL PRO GLU ILE GLY GLN PRO MET GLU PRO ASN          
SEQRES   5 A  260  VAL GLU ALA VAL LYS LYS LEU LYS PRO THR HIS VAL LEU          
SEQRES   6 A  260  SER VAL SER THR ILE LYS ASP GLU MET GLN PRO PHE TYR          
SEQRES   7 A  260  LYS GLN LEU ASN MET LYS GLY TYR PHE TYR ASP PHE ASP          
SEQRES   8 A  260  SER LEU LYS GLY MET GLN LYS SER ILE THR GLN LEU GLY          
SEQRES   9 A  260  ASP GLN PHE ASN ARG LYS ALA GLN ALA LYS GLU LEU ASN          
SEQRES  10 A  260  ASP HIS LEU ASN SER VAL LYS GLN LYS ILE GLU ASN LYS          
SEQRES  11 A  260  ALA ALA LYS GLN LYS LYS HIS PRO LYS VAL LEU ILE LEU          
SEQRES  12 A  260  MET GLY VAL PRO GLY SER TYR LEU VAL ALA THR ASP LYS          
SEQRES  13 A  260  SER TYR ILE GLY ASP LEU VAL LYS ILE ALA GLY GLY GLU          
SEQRES  14 A  260  ASN VAL ILE LYS VAL LYS ASP ARG GLN TYR ILE SER SER          
SEQRES  15 A  260  ASN THR GLU ASN LEU LEU ASN ILE ASN PRO ASP ILE ILE          
SEQRES  16 A  260  LEU ARG LEU PRO HIS GLY MET PRO GLU GLU VAL LYS LYS          
SEQRES  17 A  260  MET PHE GLN LYS GLU PHE LYS GLN ASN ASP ILE TRP LYS          
SEQRES  18 A  260  HIS PHE LYS ALA VAL LYS ASN ASN HIS VAL TYR ASP LEU          
SEQRES  19 A  260  GLU GLU VAL PRO PHE GLY ILE THR ALA ASN VAL ASP ALA          
SEQRES  20 A  260  ASP LYS ALA MET THR GLN LEU TYR ASP LEU PHE TYR LYS          
HET    HEM  A 300      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  HOH   *246(H2 O)                                                    
HELIX    1   1 THR A   40  LEU A   50  1                                  11    
HELIX    2   2 PRO A   65  LYS A   69  5                                   5    
HELIX    3   3 ASN A   81  LEU A   88  1                                   8    
HELIX    4   4 ILE A   99  ASN A  111  1                                  13    
HELIX    5   5 SER A  121  PHE A  136  1                                  16    
HELIX    6   6 ARG A  138  GLN A  163  1                                  26    
HELIX    7   7 SER A  186  ALA A  195  1                                  10    
HELIX    8   8 MET A  231  ASN A  246  1                                  16    
HELIX    9   9 ILE A  248  HIS A  251  5                                   4    
HELIX   10  10 PHE A  252  ASN A  257  1                                   6    
HELIX   11  11 ASP A  275  TYR A  288  1                                  14    
SHEET    1   A 3 ILE A  36  PRO A  38  0                                        
SHEET    2   A 3 HIS A  92  VAL A  96  1  O  LEU A  94   N  VAL A  37           
SHEET    3   A 3 TYR A 115  TYR A 117  1  O  TYR A 115   N  SER A  95           
SHEET    1   B 4 GLU A 198  ASN A 199  0                                        
SHEET    2   B 4 LYS A 168  VAL A 175  1  N  VAL A 169   O  GLU A 198           
SHEET    3   B 4 SER A 178  ALA A 182 -1  O  LEU A 180   N  MET A 173           
SHEET    4   B 4 TYR A 208  SER A 210 -1  O  ILE A 209   N  VAL A 181           
SHEET    1   C 4 GLU A 198  ASN A 199  0                                        
SHEET    2   C 4 LYS A 168  VAL A 175  1  N  VAL A 169   O  GLU A 198           
SHEET    3   C 4 ILE A 223  PRO A 228  1  O  LEU A 227   N  GLY A 174           
SHEET    4   C 4 VAL A 260  ASP A 262  1  O  TYR A 261   N  ARG A 226           
LINK         SD  MET A  78                FE   HEM A 300     1555   1555  2.28  
LINK         NE2 HIS A 229                FE   HEM A 300     1555   1555  2.01  
CISPEP   1 VAL A  266    PRO A  267          0        10.82                     
SITE     1 AC1 20 THR A  40  VAL A  41  ALA A  42  SER A  60                    
SITE     2 AC1 20 TYR A  61  LYS A  62  GLN A  76  PRO A  77                    
SITE     3 AC1 20 MET A  78  ILE A  99  ASN A 137  PRO A 176                    
SITE     4 AC1 20 HIS A 229  GLY A 230  ILE A 270  THR A 271                    
SITE     5 AC1 20 HOH A 307  HOH A 313  HOH A 316  HOH A 369                    
CRYST1   64.219   64.219  144.993  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015572  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015572  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006897        0.00000                         
ATOM      1  N   GLY A  32      86.838  42.472  65.065  1.00 36.27           N  
ATOM      2  CA  GLY A  32      85.662  42.469  65.988  1.00 36.07           C  
ATOM      3  C   GLY A  32      84.604  43.504  65.641  1.00 36.09           C  
ATOM      4  O   GLY A  32      83.419  43.326  65.976  1.00 35.97           O  
ATOM      5  N   GLU A  33      85.037  44.581  64.970  1.00 35.69           N  
ATOM      6  CA  GLU A  33      84.170  45.709  64.576  1.00 35.04           C  
ATOM      7  C   GLU A  33      83.248  45.402  63.402  1.00 33.91           C  
ATOM      8  O   GLU A  33      83.703  44.957  62.347  1.00 33.91           O  
ATOM      9  CB  GLU A  33      85.002  46.959  64.256  1.00 35.50           C  
ATOM     10  CG  GLU A  33      85.151  47.938  65.421  1.00 37.16           C  
ATOM     11  CD  GLU A  33      83.886  48.761  65.696  1.00 39.52           C  
ATOM     12  OE1 GLU A  33      82.808  48.477  65.112  1.00 39.36           O  
ATOM     13  OE2 GLU A  33      83.979  49.706  66.511  1.00 40.68           O  
ATOM     14  N   PHE A  34      81.955  45.650  63.607  1.00 32.56           N  
ATOM     15  CA  PHE A  34      80.928  45.363  62.614  1.00 31.23           C  
ATOM     16  C   PHE A  34      80.489  46.638  61.926  1.00 30.59           C  
ATOM     17  O   PHE A  34      80.303  47.676  62.576  1.00 30.66           O  
ATOM     18  CB  PHE A  34      79.703  44.703  63.253  1.00 30.80           C  
ATOM     19  CG  PHE A  34      80.002  43.424  63.965  1.00 31.47           C  
ATOM     20  CD1 PHE A  34      80.637  42.372  63.307  1.00 31.86           C  
ATOM     21  CD2 PHE A  34      79.636  43.257  65.297  1.00 31.53           C  
ATOM     22  CE1 PHE A  34      80.922  41.185  63.971  1.00 31.06           C  
ATOM     23  CE2 PHE A  34      79.911  42.071  65.963  1.00 32.07           C  
ATOM     24  CZ  PHE A  34      80.556  41.033  65.295  1.00 31.32           C  
ATOM     25  N   ARG A  35      80.319  46.547  60.612  1.00 29.19           N  
ATOM     26  CA  ARG A  35      79.750  47.621  59.815  1.00 28.06           C  
ATOM     27  C   ARG A  35      78.600  47.016  58.999  1.00 27.88           C  
ATOM     28  O   ARG A  35      78.822  46.363  57.973  1.00 28.12           O  
ATOM     29  CB  ARG A  35      80.828  48.273  58.934  1.00 27.90           C  
ATOM     30  CG  ARG A  35      81.929  49.004  59.726  1.00 27.03           C  
ATOM     31  CD  ARG A  35      83.017  49.597  58.820  1.00 27.55           C  
ATOM     32  NE  ARG A  35      82.484  50.607  57.896  1.00 27.31           N  
ATOM     33  CZ  ARG A  35      82.183  51.862  58.235  1.00 27.07           C  
ATOM     34  NH1 ARG A  35      82.359  52.285  59.487  1.00 26.25           N  
ATOM     35  NH2 ARG A  35      81.704  52.700  57.322  1.00 24.61           N  
ATOM     36  N   ILE A  36      77.376  47.214  59.482  1.00 26.74           N  
ATOM     37  CA  ILE A  36      76.225  46.465  58.998  1.00 26.06           C  
ATOM     38  C   ILE A  36      75.355  47.343  58.107  1.00 25.79           C  
ATOM     39  O   ILE A  36      75.030  48.465  58.470  1.00 25.40           O  
ATOM     40  CB  ILE A  36      75.382  45.887  60.180  1.00 25.88           C  
ATOM     41  CG1 ILE A  36      76.263  45.051  61.119  1.00 26.24           C  
ATOM     42  CG2 ILE A  36      74.228  45.005  59.671  1.00 25.45           C  
ATOM     43  CD1 ILE A  36      75.669  44.844  62.526  1.00 25.44           C  
ATOM     44  N   VAL A  37      75.028  46.848  56.919  1.00 25.82           N  
ATOM     45  CA  VAL A  37      73.983  47.482  56.113  1.00 26.33           C  
ATOM     46  C   VAL A  37      72.759  46.565  55.877  1.00 26.19           C  
ATOM     47  O   VAL A  37      72.831  45.569  55.153  1.00 26.24           O  
ATOM     48  CB  VAL A  37      74.510  48.292  54.845  1.00 26.61           C  
ATOM     49  CG1 VAL A  37      76.035  48.278  54.704  1.00 26.54           C  
ATOM     50  CG2 VAL A  37      73.778  47.940  53.546  1.00 26.77           C  
ATOM     51  N   PRO A  38      71.649  46.880  56.556  1.00 26.19           N  
ATOM     52  CA  PRO A  38      70.359  46.271  56.274  1.00 26.68           C  
ATOM     53  C   PRO A  38      69.841  46.846  54.971  1.00 26.86           C  
ATOM     54  O   PRO A  38      69.885  48.070  54.774  1.00 27.07           O  
ATOM     55  CB  PRO A  38      69.485  46.743  57.440  1.00 26.55           C  
ATOM     56  CG  PRO A  38      70.079  48.021  57.858  1.00 26.44           C  
ATOM     57  CD  PRO A  38      71.565  47.840  57.668  1.00 26.61           C  
ATOM     58  N   THR A  39      69.377  45.980  54.076  1.00 26.83           N  
ATOM     59  CA  THR A  39      68.892  46.454  52.785  1.00 26.88           C  
ATOM     60  C   THR A  39      67.372  46.505  52.746  1.00 26.59           C  
ATOM     61  O   THR A  39      66.808  47.005  51.789  1.00 27.07           O  
ATOM     62  CB  THR A  39      69.453  45.647  51.575  1.00 26.88           C  
ATOM     63  OG1 THR A  39      68.971  44.298  51.618  1.00 27.90           O  
ATOM     64  CG2 THR A  39      70.987  45.645  51.574  1.00 25.81           C  
ATOM     65  N   THR A  40      66.705  45.997  53.779  1.00 26.21           N  
ATOM     66  CA  THR A  40      65.260  46.175  53.859  1.00 25.42           C  
ATOM     67  C   THR A  40      64.840  46.976  55.084  1.00 25.17           C  
ATOM     68  O   THR A  40      65.608  47.127  56.031  1.00 25.00           O  
ATOM     69  CB  THR A  40      64.480  44.840  53.830  1.00 25.22           C  
ATOM     70  OG1 THR A  40      64.587  44.193  55.101  1.00 25.87           O  
ATOM     71  CG2 THR A  40      64.956  43.908  52.713  1.00 24.83           C  
ATOM     72  N   VAL A  41      63.611  47.492  55.042  1.00 25.01           N  
ATOM     73  CA  VAL A  41      63.018  48.223  56.146  1.00 24.69           C  
ATOM     74  C   VAL A  41      62.765  47.321  57.361  1.00 24.43           C  
ATOM     75  O   VAL A  41      63.061  47.713  58.462  1.00 24.54           O  
ATOM     76  CB  VAL A  41      61.713  48.951  55.735  1.00 24.64           C  
ATOM     77  CG1 VAL A  41      61.113  49.694  56.940  1.00 23.93           C  
ATOM     78  CG2 VAL A  41      61.976  49.921  54.576  1.00 24.36           C  
ATOM     79  N   ALA A  42      62.228  46.121  57.154  1.00 24.87           N  
ATOM     80  CA  ALA A  42      62.071  45.135  58.243  1.00 25.93           C  
ATOM     81  C   ALA A  42      63.380  44.771  58.953  1.00 26.24           C  
ATOM     82  O   ALA A  42      63.399  44.657  60.188  1.00 26.55           O  
ATOM     83  CB  ALA A  42      61.349  43.852  57.744  1.00 25.26           C  
ATOM     84  N   LEU A  43      64.454  44.577  58.174  1.00 26.90           N  
ATOM     85  CA  LEU A  43      65.790  44.334  58.737  1.00 27.32           C  
ATOM     86  C   LEU A  43      66.318  45.528  59.537  1.00 27.25           C  
ATOM     87  O   LEU A  43      66.843  45.361  60.629  1.00 27.84           O  
ATOM     88  CB  LEU A  43      66.801  43.901  57.662  1.00 26.99           C  
ATOM     89  CG  LEU A  43      66.690  42.455  57.142  1.00 26.78           C  
ATOM     90  CD1 LEU A  43      67.443  42.310  55.835  1.00 26.62           C  
ATOM     91  CD2 LEU A  43      67.179  41.408  58.149  1.00 25.32           C  
ATOM     92  N   THR A  44      66.158  46.728  58.999  1.00 27.29           N  
ATOM     93  CA  THR A  44      66.485  47.976  59.715  1.00 26.77           C  
ATOM     94  C   THR A  44      65.734  48.115  61.057  1.00 26.61           C  
ATOM     95  O   THR A  44      66.320  48.478  62.071  1.00 26.85           O  
ATOM     96  CB  THR A  44      66.215  49.201  58.803  1.00 26.60           C  
ATOM     97  OG1 THR A  44      66.980  49.058  57.602  1.00 26.87           O  
ATOM     98  CG2 THR A  44      66.613  50.532  59.475  1.00 27.42           C  
ATOM     99  N   MET A  45      64.445  47.803  61.065  1.00 26.01           N  
ATOM    100  CA  MET A  45      63.672  47.891  62.283  1.00 26.16           C  
ATOM    101  C   MET A  45      64.057  46.813  63.324  1.00 26.20           C  
ATOM    102  O   MET A  45      63.952  47.054  64.541  1.00 25.61           O  
ATOM    103  CB  MET A  45      62.178  47.876  61.966  1.00 26.01           C  
ATOM    104  CG  MET A  45      61.693  49.236  61.475  1.00 26.48           C  
ATOM    105  SD  MET A  45      60.043  49.230  60.791  1.00 27.36           S  
ATOM    106  CE  MET A  45      59.041  49.031  62.288  1.00 26.46           C  
ATOM    107  N   THR A  46      64.518  45.660  62.827  1.00 25.35           N  
ATOM    108  CA  THR A  46      64.991  44.553  63.655  1.00 25.58           C  
ATOM    109  C   THR A  46      66.319  44.902  64.306  1.00 25.37           C  
ATOM    110  O   THR A  46      66.515  44.625  65.484  1.00 25.67           O  
ATOM    111  CB  THR A  46      65.122  43.223  62.850  1.00 25.33           C  
ATOM    112  OG1 THR A  46      63.871  42.909  62.225  1.00 25.51           O  
ATOM    113  CG2 THR A  46      65.498  42.067  63.762  1.00 25.95           C  
ATOM    114  N   LEU A  47      67.224  45.514  63.545  1.00 25.21           N  
ATOM    115  CA  LEU A  47      68.507  45.944  64.097  1.00 25.61           C  
ATOM    116  C   LEU A  47      68.330  46.998  65.180  1.00 25.39           C  
ATOM    117  O   LEU A  47      69.059  46.986  66.156  1.00 26.00           O  
ATOM    118  CB  LEU A  47      69.461  46.425  63.010  1.00 25.47           C  
ATOM    119  CG  LEU A  47      69.838  45.325  62.024  1.00 27.06           C  
ATOM    120  CD1 LEU A  47      70.639  45.906  60.873  1.00 26.54           C  
ATOM    121  CD2 LEU A  47      70.601  44.200  62.704  1.00 26.13           C  
ATOM    122  N   ASP A  48      67.334  47.872  65.020  1.00 25.34           N  
ATOM    123  CA  ASP A  48      66.997  48.871  66.044  1.00 24.60           C  
ATOM    124  C   ASP A  48      66.517  48.232  67.337  1.00 24.03           C  
ATOM    125  O   ASP A  48      66.987  48.612  68.416  1.00 24.07           O  
ATOM    126  CB  ASP A  48      65.961  49.868  65.508  1.00 24.50           C  
ATOM    127  CG  ASP A  48      65.442  50.825  66.583  1.00 25.32           C  
ATOM    128  OD1 ASP A  48      66.198  51.740  67.009  1.00 25.56           O  
ATOM    129  OD2 ASP A  48      64.260  50.668  66.987  1.00 25.72           O  
ATOM    130  N   LYS A  49      65.609  47.253  67.243  1.00 23.47           N  
ATOM    131  CA  LYS A  49      65.208  46.470  68.434  1.00 23.61           C  
ATOM    132  C   LYS A  49      66.394  45.791  69.138  1.00 23.41           C  
ATOM    133  O   LYS A  49      66.379  45.606  70.354  1.00 23.33           O  
ATOM    134  CB  LYS A  49      64.138  45.414  68.085  1.00 24.09           C  
ATOM    135  CG  LYS A  49      62.785  45.975  67.627  1.00 24.13           C  
ATOM    136  CD  LYS A  49      62.076  46.717  68.752  1.00 26.83           C  
ATOM    137  CE  LYS A  49      60.745  47.276  68.278  1.00 26.88           C  
ATOM    138  NZ  LYS A  49      59.893  47.746  69.403  1.00 27.69           N  
ATOM    139  N   LEU A  50      67.415  45.422  68.371  1.00 23.31           N  
ATOM    140  CA  LEU A  50      68.594  44.743  68.910  1.00 24.39           C  
ATOM    141  C   LEU A  50      69.688  45.736  69.381  1.00 24.67           C  
ATOM    142  O   LEU A  50      70.741  45.319  69.854  1.00 24.73           O  
ATOM    143  CB  LEU A  50      69.144  43.755  67.869  1.00 24.08           C  
ATOM    144  CG  LEU A  50      68.695  42.283  67.851  1.00 26.63           C  
ATOM    145  CD1 LEU A  50      67.270  41.992  68.398  1.00 26.77           C  
ATOM    146  CD2 LEU A  50      68.903  41.664  66.468  1.00 25.39           C  
ATOM    147  N   ASP A  51      69.421  47.040  69.262  1.00 24.97           N  
ATOM    148  CA  ASP A  51      70.299  48.094  69.799  1.00 25.90           C  
ATOM    149  C   ASP A  51      71.634  48.123  69.029  1.00 25.70           C  
ATOM    150  O   ASP A  51      72.725  48.250  69.611  1.00 26.14           O  
ATOM    151  CB  ASP A  51      70.498  47.867  71.308  1.00 26.04           C  
ATOM    152  CG  ASP A  51      71.076  49.072  72.029  1.00 28.38           C  
ATOM    153  OD1 ASP A  51      71.310  48.951  73.259  1.00 28.05           O  
ATOM    154  OD2 ASP A  51      71.295  50.132  71.387  1.00 32.14           O  
ATOM    155  N   LEU A  52      71.530  47.969  67.712  1.00 25.37           N  
ATOM    156  CA  LEU A  52      72.695  47.848  66.857  1.00 24.84           C  
ATOM    157  C   LEU A  52      72.834  49.059  65.972  1.00 24.99           C  
ATOM    158  O   LEU A  52      71.855  49.473  65.323  1.00 24.71           O  
ATOM    159  CB  LEU A  52      72.597  46.594  65.985  1.00 24.65           C  
ATOM    160  CG  LEU A  52      72.989  45.291  66.687  1.00 24.16           C  
ATOM    161  CD1 LEU A  52      72.438  44.100  65.958  1.00 21.94           C  
ATOM    162  CD2 LEU A  52      74.502  45.186  66.845  1.00 21.58           C  
ATOM    163  N   PRO A  53      74.045  49.638  65.937  1.00 24.98           N  
ATOM    164  CA  PRO A  53      74.338  50.682  64.952  1.00 25.31           C  
ATOM    165  C   PRO A  53      74.463  50.091  63.537  1.00 25.31           C  
ATOM    166  O   PRO A  53      74.804  48.912  63.370  1.00 25.45           O  
ATOM    167  CB  PRO A  53      75.685  51.237  65.413  1.00 24.92           C  
ATOM    168  CG  PRO A  53      76.325  50.093  66.158  1.00 26.10           C  
ATOM    169  CD  PRO A  53      75.202  49.339  66.806  1.00 25.40           C  
ATOM    170  N   ILE A  54      74.185  50.913  62.537  1.00 25.24           N  
ATOM    171  CA  ILE A  54      74.318  50.527  61.129  1.00 25.36           C  
ATOM    172  C   ILE A  54      75.123  51.602  60.357  1.00 25.51           C  
ATOM    173  O   ILE A  54      75.215  52.749  60.809  1.00 25.25           O  
ATOM    174  CB  ILE A  54      72.932  50.271  60.470  1.00 25.39           C  
ATOM    175  CG1 ILE A  54      72.106  51.565  60.381  1.00 25.54           C  
ATOM    176  CG2 ILE A  54      72.177  49.152  61.206  1.00 25.65           C  
ATOM    177  CD1 ILE A  54      70.799  51.421  59.586  1.00 24.76           C  
ATOM    178  N   VAL A  55      75.710  51.234  59.218  1.00 25.60           N  
ATOM    179  CA  VAL A  55      76.481  52.206  58.407  1.00 25.75           C  
ATOM    180  C   VAL A  55      75.741  52.661  57.127  1.00 25.77           C  
ATOM    181  O   VAL A  55      76.103  53.668  56.526  1.00 25.76           O  
ATOM    182  CB  VAL A  55      77.962  51.747  58.102  1.00 25.63           C  
ATOM    183  CG1 VAL A  55      78.739  51.510  59.399  1.00 25.96           C  
ATOM    184  CG2 VAL A  55      78.012  50.521  57.185  1.00 24.95           C  
ATOM    185  N   GLY A  56      74.693  51.931  56.737  1.00 26.03           N  
ATOM    186  CA  GLY A  56      73.821  52.339  55.624  1.00 25.99           C  
ATOM    187  C   GLY A  56      72.407  51.842  55.833  1.00 26.26           C  
ATOM    188  O   GLY A  56      72.203  50.886  56.576  1.00 26.78           O  
ATOM    189  N   LYS A  57      71.429  52.490  55.197  1.00 26.27           N  
ATOM    190  CA  LYS A  57      70.008  52.101  55.340  1.00 26.49           C  
ATOM    191  C   LYS A  57      69.287  52.115  53.980  1.00 26.20           C  
ATOM    192  O   LYS A  57      69.728  52.816  53.062  1.00 26.89           O  
ATOM    193  CB  LYS A  57      69.288  53.037  56.333  1.00 26.53           C  
ATOM    194  CG  LYS A  57      69.069  54.452  55.794  1.00 26.24           C  
ATOM    195  CD  LYS A  57      68.742  55.459  56.890  1.00 26.88           C  
ATOM    196  CE  LYS A  57      68.089  56.705  56.289  1.00 26.03           C  
ATOM    197  NZ  LYS A  57      67.932  57.792  57.308  1.00 26.26           N  
ATOM    198  N   PRO A  58      68.176  51.359  53.844  1.00 25.47           N  
ATOM    199  CA  PRO A  58      67.431  51.405  52.589  1.00 25.21           C  
ATOM    200  C   PRO A  58      66.798  52.776  52.289  1.00 25.51           C  
ATOM    201  O   PRO A  58      66.508  53.558  53.214  1.00 25.43           O  
ATOM    202  CB  PRO A  58      66.349  50.325  52.781  1.00 25.21           C  
ATOM    203  CG  PRO A  58      66.208  50.176  54.287  1.00 25.20           C  
ATOM    204  CD  PRO A  58      67.583  50.409  54.811  1.00 25.81           C  
ATOM    205  N   THR A  59      66.622  53.071  50.999  1.00 25.29           N  
ATOM    206  CA  THR A  59      65.832  54.227  50.559  1.00 25.69           C  
ATOM    207  C   THR A  59      64.371  53.816  50.573  1.00 25.20           C  
ATOM    208  O   THR A  59      63.999  52.824  49.953  1.00 25.64           O  
ATOM    209  CB  THR A  59      66.204  54.683  49.129  1.00 25.31           C  
ATOM    210  OG1 THR A  59      67.620  54.849  49.042  1.00 26.70           O  
ATOM    211  CG2 THR A  59      65.515  56.018  48.781  1.00 25.75           C  
ATOM    212  N   SER A  60      63.547  54.578  51.278  1.00 24.79           N  
ATOM    213  CA  SER A  60      62.177  54.160  51.545  1.00 24.63           C  
ATOM    214  C   SER A  60      61.311  55.356  51.905  1.00 24.84           C  
ATOM    215  O   SER A  60      61.811  56.347  52.452  1.00 24.66           O  
ATOM    216  CB  SER A  60      62.161  53.131  52.686  1.00 24.31           C  
ATOM    217  OG  SER A  60      60.844  52.900  53.169  1.00 24.12           O  
ATOM    218  N   TYR A  61      60.022  55.270  51.576  1.00 24.62           N  
ATOM    219  CA  TYR A  61      59.038  56.272  52.017  1.00 24.43           C  
ATOM    220  C   TYR A  61      58.476  55.946  53.410  1.00 24.13           C  
ATOM    221  O   TYR A  61      57.675  56.692  53.942  1.00 23.93           O  
ATOM    222  CB  TYR A  61      57.891  56.383  51.010  1.00 24.53           C  
ATOM    223  CG  TYR A  61      57.168  55.078  50.749  1.00 25.61           C  
ATOM    224  CD1 TYR A  61      57.242  54.466  49.496  1.00 26.74           C  
ATOM    225  CD2 TYR A  61      56.410  54.450  51.747  1.00 25.54           C  
ATOM    226  CE1 TYR A  61      56.594  53.270  49.238  1.00 26.10           C  
ATOM    227  CE2 TYR A  61      55.752  53.246  51.493  1.00 26.46           C  
ATOM    228  CZ  TYR A  61      55.855  52.666  50.234  1.00 26.15           C  
ATOM    229  OH  TYR A  61      55.214  51.484  49.950  1.00 26.57           O  
ATOM    230  N   LYS A  62      58.883  54.808  53.984  1.00 24.13           N  
ATOM    231  CA  LYS A  62      58.397  54.394  55.298  1.00 23.78           C  
ATOM    232  C   LYS A  62      59.169  55.077  56.420  1.00 24.15           C  
ATOM    233  O   LYS A  62      60.329  55.477  56.242  1.00 23.54           O  
ATOM    234  CB  LYS A  62      58.474  52.875  55.456  1.00 23.16           C  
ATOM    235  CG  LYS A  62      57.698  52.113  54.385  1.00 24.90           C  
ATOM    236  CD  LYS A  62      57.613  50.640  54.647  1.00 25.05           C  
ATOM    237  CE  LYS A  62      56.756  49.972  53.582  1.00 28.33           C  
ATOM    238  NZ  LYS A  62      57.029  48.519  53.543  1.00 31.36           N  
ATOM    239  N   THR A  63      58.507  55.210  57.570  1.00 25.05           N  
ATOM    240  CA  THR A  63      59.167  55.641  58.817  1.00 26.13           C  
ATOM    241  C   THR A  63      60.267  54.655  59.240  1.00 26.17           C  
ATOM    242  O   THR A  63      60.014  53.440  59.333  1.00 26.30           O  
ATOM    243  CB  THR A  63      58.153  55.772  59.973  1.00 26.27           C  
ATOM    244  OG1 THR A  63      57.006  56.518  59.528  1.00 27.12           O  
ATOM    245  CG2 THR A  63      58.788  56.461  61.213  1.00 25.92           C  
ATOM    246  N   LEU A  64      61.474  55.189  59.466  1.00 26.10           N  
ATOM    247  CA  LEU A  64      62.605  54.422  60.008  1.00 26.20           C  
ATOM    248  C   LEU A  64      62.922  54.886  61.436  1.00 26.08           C  
ATOM    249  O   LEU A  64      62.527  55.992  61.835  1.00 25.43           O  
ATOM    250  CB  LEU A  64      63.860  54.536  59.114  1.00 26.19           C  
ATOM    251  CG  LEU A  64      63.837  53.978  57.674  1.00 27.80           C  
ATOM    252  CD1 LEU A  64      65.168  54.224  56.928  1.00 25.45           C  
ATOM    253  CD2 LEU A  64      63.447  52.512  57.632  1.00 27.25           C  
ATOM    254  N   PRO A  65      63.597  54.023  62.223  1.00 26.04           N  
ATOM    255  CA  PRO A  65      63.974  54.386  63.594  1.00 26.32           C  
ATOM    256  C   PRO A  65      64.799  55.660  63.652  1.00 26.57           C  
ATOM    257  O   PRO A  65      65.632  55.892  62.776  1.00 26.53           O  
ATOM    258  CB  PRO A  65      64.801  53.189  64.046  1.00 25.63           C  
ATOM    259  CG  PRO A  65      64.210  52.044  63.243  1.00 25.86           C  
ATOM    260  CD  PRO A  65      63.989  52.633  61.900  1.00 25.67           C  
ATOM    261  N   ASN A  66      64.547  56.465  64.681  1.00 27.25           N  
ATOM    262  CA  ASN A  66      65.134  57.799  64.824  1.00 28.43           C  
ATOM    263  C   ASN A  66      66.655  57.724  64.941  1.00 28.33           C  
ATOM    264  O   ASN A  66      67.353  58.612  64.482  1.00 28.39           O  
ATOM    265  CB  ASN A  66      64.521  58.532  66.043  1.00 28.55           C  
ATOM    266  CG  ASN A  66      64.708  60.051  65.994  1.00 30.83           C  
ATOM    267  OD1 ASN A  66      64.412  60.703  64.991  1.00 32.26           O  
ATOM    268  ND2 ASN A  66      65.172  60.624  67.105  1.00 33.39           N  
ATOM    269  N   ARG A  67      67.169  56.652  65.533  1.00 28.11           N  
ATOM    270  CA  ARG A  67      68.616  56.541  65.727  1.00 28.47           C  
ATOM    271  C   ARG A  67      69.409  56.425  64.413  1.00 27.66           C  
ATOM    272  O   ARG A  67      70.629  56.625  64.390  1.00 26.84           O  
ATOM    273  CB  ARG A  67      68.962  55.385  66.671  1.00 28.72           C  
ATOM    274  CG  ARG A  67      68.945  54.039  66.010  1.00 30.28           C  
ATOM    275  CD  ARG A  67      69.277  52.956  66.997  1.00 32.39           C  
ATOM    276  NE  ARG A  67      70.711  52.794  67.192  1.00 33.40           N  
ATOM    277  CZ  ARG A  67      71.239  52.068  68.175  1.00 34.40           C  
ATOM    278  NH1 ARG A  67      70.440  51.469  69.052  1.00 33.62           N  
ATOM    279  NH2 ARG A  67      72.558  51.966  68.302  1.00 34.01           N  
ATOM    280  N   TYR A  68      68.708  56.111  63.328  1.00 27.06           N  
ATOM    281  CA  TYR A  68      69.340  55.988  62.022  1.00 27.08           C  
ATOM    282  C   TYR A  68      69.117  57.207  61.126  1.00 27.10           C  
ATOM    283  O   TYR A  68      69.354  57.136  59.906  1.00 26.71           O  
ATOM    284  CB  TYR A  68      68.833  54.732  61.316  1.00 27.04           C  
ATOM    285  CG  TYR A  68      69.024  53.444  62.096  1.00 26.80           C  
ATOM    286  CD1 TYR A  68      70.176  53.212  62.842  1.00 26.04           C  
ATOM    287  CD2 TYR A  68      68.059  52.439  62.041  1.00 25.58           C  
ATOM    288  CE1 TYR A  68      70.350  52.006  63.549  1.00 26.43           C  
ATOM    289  CE2 TYR A  68      68.222  51.241  62.711  1.00 26.49           C  
ATOM    290  CZ  TYR A  68      69.363  51.028  63.472  1.00 27.08           C  
ATOM    291  OH  TYR A  68      69.505  49.828  64.136  1.00 27.25           O  
ATOM    292  N   LYS A  69      68.651  58.310  61.721  1.00 26.96           N  
ATOM    293  CA  LYS A  69      68.274  59.485  60.937  1.00 27.93           C  
ATOM    294  C   LYS A  69      69.438  60.035  60.106  1.00 27.93           C  
ATOM    295  O   LYS A  69      69.231  60.456  58.968  1.00 27.55           O  
ATOM    296  CB  LYS A  69      67.567  60.573  61.773  1.00 27.48           C  
ATOM    297  CG  LYS A  69      68.376  61.269  62.855  1.00 28.08           C  
ATOM    298  CD  LYS A  69      67.625  62.508  63.362  1.00 28.68           C  
ATOM    299  CE  LYS A  69      68.476  63.309  64.340  1.00 31.29           C  
ATOM    300  NZ  LYS A  69      68.117  64.767  64.297  1.00 33.41           N  
ATOM    301  N   ASP A  70      70.651  59.973  60.663  1.00 28.26           N  
ATOM    302  CA  ASP A  70      71.844  60.509  59.998  1.00 28.97           C  
ATOM    303  C   ASP A  70      72.642  59.503  59.142  1.00 28.97           C  
ATOM    304  O   ASP A  70      73.619  59.882  58.501  1.00 28.73           O  
ATOM    305  CB  ASP A  70      72.746  61.225  61.018  1.00 28.95           C  
ATOM    306  CG  ASP A  70      72.138  62.536  61.508  1.00 30.24           C  
ATOM    307  OD1 ASP A  70      71.403  63.182  60.737  1.00 32.57           O  
ATOM    308  OD2 ASP A  70      72.385  62.936  62.659  1.00 33.09           O  
ATOM    309  N   VAL A  71      72.231  58.236  59.115  1.00 29.18           N  
ATOM    310  CA  VAL A  71      72.959  57.261  58.289  1.00 29.63           C  
ATOM    311  C   VAL A  71      72.508  57.388  56.824  1.00 29.77           C  
ATOM    312  O   VAL A  71      71.337  57.636  56.564  1.00 29.80           O  
ATOM    313  CB  VAL A  71      72.974  55.764  58.844  1.00 29.71           C  
ATOM    314  CG1 VAL A  71      72.604  55.673  60.330  1.00 29.01           C  
ATOM    315  CG2 VAL A  71      72.155  54.830  58.015  1.00 28.66           C  
ATOM    316  N   PRO A  72      73.451  57.235  55.874  1.00 29.98           N  
ATOM    317  CA  PRO A  72      73.158  57.418  54.455  1.00 30.26           C  
ATOM    318  C   PRO A  72      72.258  56.314  53.894  1.00 30.65           C  
ATOM    319  O   PRO A  72      72.282  55.174  54.379  1.00 30.50           O  
ATOM    320  CB  PRO A  72      74.541  57.348  53.805  1.00 30.37           C  
ATOM    321  CG  PRO A  72      75.340  56.475  54.734  1.00 30.03           C  
ATOM    322  CD  PRO A  72      74.859  56.846  56.097  1.00 30.07           C  
ATOM    323  N   GLU A  73      71.479  56.670  52.878  1.00 30.68           N  
ATOM    324  CA  GLU A  73      70.631  55.720  52.157  1.00 31.28           C  
ATOM    325  C   GLU A  73      71.432  55.040  51.065  1.00 31.49           C  
ATOM    326  O   GLU A  73      72.279  55.673  50.423  1.00 31.67           O  
ATOM    327  CB  GLU A  73      69.456  56.441  51.519  1.00 31.15           C  
ATOM    328  CG  GLU A  73      68.494  57.037  52.508  1.00 31.70           C  
ATOM    329  CD  GLU A  73      67.403  57.844  51.836  1.00 33.52           C  
ATOM    330  OE1 GLU A  73      67.679  58.531  50.829  1.00 34.25           O  
ATOM    331  OE2 GLU A  73      66.256  57.792  52.316  1.00 35.61           O  
ATOM    332  N   ILE A  74      71.177  53.757  50.841  1.00 31.10           N  
ATOM    333  CA  ILE A  74      71.952  53.047  49.830  1.00 31.45           C  
ATOM    334  C   ILE A  74      71.101  52.516  48.672  1.00 31.47           C  
ATOM    335  O   ILE A  74      71.565  51.704  47.878  1.00 31.08           O  
ATOM    336  CB  ILE A  74      72.942  51.998  50.448  1.00 31.77           C  
ATOM    337  CG1 ILE A  74      72.310  51.211  51.592  1.00 32.12           C  
ATOM    338  CG2 ILE A  74      74.192  52.707  50.993  1.00 31.92           C  
ATOM    339  CD1 ILE A  74      71.247  50.198  51.149  1.00 32.92           C  
ATOM    340  N   GLY A  75      69.862  52.994  48.582  1.00 31.37           N  
ATOM    341  CA  GLY A  75      68.956  52.602  47.503  1.00 32.27           C  
ATOM    342  C   GLY A  75      67.756  51.804  47.987  1.00 32.52           C  
ATOM    343  O   GLY A  75      67.690  51.365  49.146  1.00 32.79           O  
ATOM    344  N   GLN A  76      66.804  51.609  47.088  1.00 32.96           N  
ATOM    345  CA  GLN A  76      65.579  50.866  47.402  1.00 33.18           C  
ATOM    346  C   GLN A  76      65.850  49.381  47.628  1.00 32.54           C  
ATOM    347  O   GLN A  76      66.735  48.821  46.991  1.00 31.95           O  
ATOM    348  CB  GLN A  76      64.543  51.094  46.319  1.00 33.57           C  
ATOM    349  CG  GLN A  76      63.905  52.472  46.430  1.00 35.41           C  
ATOM    350  CD  GLN A  76      62.986  52.789  45.283  1.00 38.76           C  
ATOM    351  OE1 GLN A  76      61.777  52.967  45.471  1.00 40.97           O  
ATOM    352  NE2 GLN A  76      63.547  52.869  44.077  1.00 39.55           N  
ATOM    353  N   PRO A  77      65.103  48.753  48.565  1.00 32.46           N  
ATOM    354  CA  PRO A  77      65.381  47.390  49.039  1.00 32.38           C  
ATOM    355  C   PRO A  77      65.542  46.327  47.948  1.00 32.67           C  
ATOM    356  O   PRO A  77      66.364  45.421  48.095  1.00 32.48           O  
ATOM    357  CB  PRO A  77      64.167  47.085  49.921  1.00 32.23           C  
ATOM    358  CG  PRO A  77      63.781  48.430  50.453  1.00 31.63           C  
ATOM    359  CD  PRO A  77      63.933  49.329  49.264  1.00 32.34           C  
ATOM    360  N   MET A  78      64.776  46.452  46.865  1.00 33.12           N  
ATOM    361  CA  MET A  78      64.794  45.475  45.779  1.00 33.16           C  
ATOM    362  C   MET A  78      65.951  45.710  44.810  1.00 33.94           C  
ATOM    363  O   MET A  78      66.275  44.839  44.010  1.00 33.85           O  
ATOM    364  CB  MET A  78      63.460  45.485  45.019  1.00 33.33           C  
ATOM    365  CG  MET A  78      62.288  44.942  45.822  1.00 32.34           C  
ATOM    366  SD  MET A  78      60.764  44.656  44.867  1.00 31.88           S  
ATOM    367  CE  MET A  78      61.142  43.073  44.123  1.00 31.75           C  
ATOM    368  N   GLU A  79      66.557  46.892  44.863  1.00 34.35           N  
ATOM    369  CA  GLU A  79      67.735  47.160  44.039  1.00 35.72           C  
ATOM    370  C   GLU A  79      68.685  48.158  44.702  1.00 35.20           C  
ATOM    371  O   GLU A  79      68.745  49.326  44.306  1.00 35.44           O  
ATOM    372  CB  GLU A  79      67.357  47.565  42.600  1.00 35.86           C  
ATOM    373  CG  GLU A  79      66.202  48.539  42.471  1.00 36.97           C  
ATOM    374  CD  GLU A  79      65.688  48.633  41.042  1.00 38.43           C  
ATOM    375  OE1 GLU A  79      65.697  47.598  40.328  1.00 42.88           O  
ATOM    376  OE2 GLU A  79      65.265  49.738  40.628  1.00 41.61           O  
ATOM    377  N   PRO A  80      69.425  47.698  45.736  1.00 35.05           N  
ATOM    378  CA  PRO A  80      70.365  48.591  46.404  1.00 34.76           C  
ATOM    379  C   PRO A  80      71.507  48.962  45.469  1.00 34.81           C  
ATOM    380  O   PRO A  80      71.832  48.217  44.523  1.00 34.34           O  
ATOM    381  CB  PRO A  80      70.868  47.766  47.598  1.00 34.80           C  
ATOM    382  CG  PRO A  80      69.906  46.620  47.728  1.00 35.18           C  
ATOM    383  CD  PRO A  80      69.433  46.351  46.333  1.00 34.67           C  
ATOM    384  N   ASN A  81      72.091  50.125  45.716  1.00 34.88           N  
ATOM    385  CA  ASN A  81      73.137  50.630  44.849  1.00 35.10           C  
ATOM    386  C   ASN A  81      74.469  49.989  45.221  1.00 35.07           C  
ATOM    387  O   ASN A  81      74.996  50.239  46.307  1.00 35.31           O  
ATOM    388  CB  ASN A  81      73.182  52.156  44.915  1.00 35.05           C  
ATOM    389  CG  ASN A  81      74.106  52.752  43.880  1.00 35.69           C  
ATOM    390  OD1 ASN A  81      75.310  52.841  44.097  1.00 36.99           O  
ATOM    391  ND2 ASN A  81      73.548  53.156  42.745  1.00 34.31           N  
ATOM    392  N   VAL A  82      74.977  49.140  44.323  1.00 35.04           N  
ATOM    393  CA  VAL A  82      76.209  48.367  44.524  1.00 35.39           C  
ATOM    394  C   VAL A  82      77.381  49.262  44.943  1.00 35.71           C  
ATOM    395  O   VAL A  82      78.077  48.967  45.918  1.00 35.83           O  
ATOM    396  CB  VAL A  82      76.595  47.557  43.240  1.00 35.47           C  
ATOM    397  CG1 VAL A  82      78.009  46.988  43.341  1.00 36.12           C  
ATOM    398  CG2 VAL A  82      75.591  46.437  42.962  1.00 35.35           C  
ATOM    399  N   GLU A  83      77.574  50.364  44.223  1.00 35.59           N  
ATOM    400  CA  GLU A  83      78.704  51.250  44.479  1.00 36.12           C  
ATOM    401  C   GLU A  83      78.547  52.099  45.749  1.00 35.77           C  
ATOM    402  O   GLU A  83      79.538  52.402  46.408  1.00 35.67           O  
ATOM    403  CB  GLU A  83      78.995  52.128  43.259  1.00 36.26           C  
ATOM    404  CG  GLU A  83      80.489  52.412  43.031  1.00 38.83           C  
ATOM    405  CD  GLU A  83      81.320  51.156  42.711  1.00 41.72           C  
ATOM    406  OE1 GLU A  83      80.780  50.186  42.116  1.00 42.42           O  
ATOM    407  OE2 GLU A  83      82.526  51.147  43.053  1.00 42.13           O  
ATOM    408  N   ALA A  84      77.312  52.475  46.086  1.00 35.64           N  
ATOM    409  CA  ALA A  84      77.040  53.194  47.334  1.00 35.39           C  
ATOM    410  C   ALA A  84      77.351  52.316  48.544  1.00 35.28           C  
ATOM    411  O   ALA A  84      77.982  52.774  49.498  1.00 35.34           O  
ATOM    412  CB  ALA A  84      75.601  53.679  47.388  1.00 35.25           C  
ATOM    413  N   VAL A  85      76.906  51.060  48.490  1.00 35.15           N  
ATOM    414  CA  VAL A  85      77.163  50.078  49.547  1.00 34.94           C  
ATOM    415  C   VAL A  85      78.673  49.809  49.722  1.00 35.43           C  
ATOM    416  O   VAL A  85      79.177  49.817  50.846  1.00 35.60           O  
ATOM    417  CB  VAL A  85      76.386  48.748  49.299  1.00 34.70           C  
ATOM    418  CG1 VAL A  85      76.892  47.643  50.216  1.00 33.89           C  
ATOM    419  CG2 VAL A  85      74.881  48.955  49.482  1.00 33.85           C  
ATOM    420  N   LYS A  86      79.381  49.585  48.612  1.00 35.74           N  
ATOM    421  CA  LYS A  86      80.833  49.358  48.629  1.00 36.03           C  
ATOM    422  C   LYS A  86      81.615  50.538  49.208  1.00 36.24           C  
ATOM    423  O   LYS A  86      82.682  50.354  49.800  1.00 36.55           O  
ATOM    424  CB  LYS A  86      81.352  49.008  47.227  1.00 36.03           C  
ATOM    425  CG  LYS A  86      81.064  47.560  46.809  1.00 36.09           C  
ATOM    426  CD  LYS A  86      82.081  47.022  45.805  1.00 36.74           C  
ATOM    427  CE  LYS A  86      81.604  47.189  44.378  1.00 36.53           C  
ATOM    428  NZ  LYS A  86      82.523  46.535  43.406  1.00 36.75           N  
ATOM    429  N   LYS A  87      81.067  51.742  49.039  1.00 36.23           N  
ATOM    430  CA  LYS A  87      81.665  52.982  49.539  1.00 35.93           C  
ATOM    431  C   LYS A  87      81.704  53.018  51.068  1.00 35.50           C  
ATOM    432  O   LYS A  87      82.508  53.730  51.657  1.00 35.39           O  
ATOM    433  CB  LYS A  87      80.855  54.175  49.025  1.00 35.96           C  
ATOM    434  CG  LYS A  87      81.627  55.474  48.890  1.00 37.28           C  
ATOM    435  CD  LYS A  87      82.187  55.681  47.476  1.00 38.61           C  
ATOM    436  CE  LYS A  87      81.086  55.927  46.438  1.00 38.84           C  
ATOM    437  NZ  LYS A  87      81.659  56.363  45.120  1.00 38.06           N  
ATOM    438  N   LEU A  88      80.816  52.260  51.702  1.00 35.29           N  
ATOM    439  CA  LEU A  88      80.691  52.261  53.164  1.00 34.95           C  
ATOM    440  C   LEU A  88      81.572  51.200  53.827  1.00 34.51           C  
ATOM    441  O   LEU A  88      81.662  51.139  55.053  1.00 33.99           O  
ATOM    442  CB  LEU A  88      79.228  52.079  53.584  1.00 34.87           C  
ATOM    443  CG  LEU A  88      78.180  53.078  53.085  1.00 34.92           C  
ATOM    444  CD1 LEU A  88      76.794  52.583  53.432  1.00 34.25           C  
ATOM    445  CD2 LEU A  88      78.405  54.476  53.642  1.00 34.26           C  
ATOM    446  N   LYS A  89      82.221  50.384  52.996  1.00 34.45           N  
ATOM    447  CA  LYS A  89      83.142  49.330  53.434  1.00 34.45           C  
ATOM    448  C   LYS A  89      82.527  48.451  54.526  1.00 34.18           C  
ATOM    449  O   LYS A  89      83.084  48.338  55.627  1.00 34.21           O  
ATOM    450  CB  LYS A  89      84.494  49.925  53.870  1.00 34.66           C  
ATOM    451  CG  LYS A  89      85.359  50.448  52.717  1.00 34.89           C  
ATOM    452  CD  LYS A  89      86.297  51.566  53.172  1.00 37.09           C  
ATOM    453  CE  LYS A  89      87.577  51.036  53.814  1.00 37.82           C  
ATOM    454  NZ  LYS A  89      88.562  52.120  54.100  1.00 37.90           N  
ATOM    455  N   PRO A  90      81.373  47.822  54.217  1.00 34.01           N  
ATOM    456  CA  PRO A  90      80.623  47.006  55.192  1.00 33.95           C  
ATOM    457  C   PRO A  90      81.309  45.670  55.498  1.00 33.77           C  
ATOM    458  O   PRO A  90      82.177  45.231  54.729  1.00 33.50           O  
ATOM    459  CB  PRO A  90      79.286  46.766  54.482  1.00 34.14           C  
ATOM    460  CG  PRO A  90      79.628  46.837  53.011  1.00 33.67           C  
ATOM    461  CD  PRO A  90      80.720  47.840  52.891  1.00 33.70           C  
ATOM    462  N   THR A  91      80.944  45.046  56.619  1.00 33.28           N  
ATOM    463  CA  THR A  91      81.398  43.682  56.900  1.00 32.73           C  
ATOM    464  C   THR A  91      80.262  42.722  56.555  1.00 32.83           C  
ATOM    465  O   THR A  91      80.498  41.596  56.104  1.00 32.91           O  
ATOM    466  CB  THR A  91      81.856  43.479  58.377  1.00 32.97           C  
ATOM    467  OG1 THR A  91      80.762  43.753  59.265  1.00 32.26           O  
ATOM    468  CG2 THR A  91      83.031  44.391  58.728  1.00 31.82           C  
ATOM    469  N   HIS A  92      79.029  43.198  56.749  1.00 32.76           N  
ATOM    470  CA  HIS A  92      77.811  42.418  56.535  1.00 32.50           C  
ATOM    471  C   HIS A  92      76.753  43.249  55.809  1.00 32.51           C  
ATOM    472  O   HIS A  92      76.409  44.345  56.256  1.00 32.58           O  
ATOM    473  CB  HIS A  92      77.240  41.944  57.884  1.00 32.34           C  
ATOM    474  CG  HIS A  92      78.146  41.015  58.634  1.00 31.89           C  
ATOM    475  ND1 HIS A  92      79.271  41.452  59.297  1.00 31.69           N  
ATOM    476  CD2 HIS A  92      78.088  39.677  58.833  1.00 30.81           C  
ATOM    477  CE1 HIS A  92      79.878  40.422  59.859  1.00 32.09           C  
ATOM    478  NE2 HIS A  92      79.177  39.333  59.596  1.00 32.34           N  
ATOM    479  N   VAL A  93      76.248  42.720  54.693  1.00 32.17           N  
ATOM    480  CA  VAL A  93      75.154  43.342  53.943  1.00 31.65           C  
ATOM    481  C   VAL A  93      73.986  42.347  53.917  1.00 31.73           C  
ATOM    482  O   VAL A  93      74.139  41.194  53.472  1.00 31.72           O  
ATOM    483  CB  VAL A  93      75.584  43.779  52.515  1.00 31.54           C  
ATOM    484  CG1 VAL A  93      74.426  44.433  51.775  1.00 31.58           C  
ATOM    485  CG2 VAL A  93      76.734  44.756  52.584  1.00 30.67           C  
ATOM    486  N   LEU A  94      72.837  42.791  54.418  1.00 30.51           N  
ATOM    487  CA  LEU A  94      71.783  41.861  54.815  1.00 30.50           C  
ATOM    488  C   LEU A  94      70.506  42.021  54.006  1.00 30.90           C  
ATOM    489  O   LEU A  94      70.006  43.138  53.827  1.00 31.20           O  
ATOM    490  CB  LEU A  94      71.459  42.006  56.306  1.00 29.51           C  
ATOM    491  CG  LEU A  94      72.553  42.170  57.379  1.00 29.36           C  
ATOM    492  CD1 LEU A  94      71.899  42.442  58.726  1.00 26.80           C  
ATOM    493  CD2 LEU A  94      73.489  40.962  57.474  1.00 26.81           C  
ATOM    494  N   SER A  95      69.972  40.888  53.552  1.00 31.03           N  
ATOM    495  CA  SER A  95      68.716  40.859  52.792  1.00 31.46           C  
ATOM    496  C   SER A  95      67.777  39.784  53.361  1.00 30.69           C  
ATOM    497  O   SER A  95      68.063  39.208  54.408  1.00 31.32           O  
ATOM    498  CB  SER A  95      68.989  40.654  51.291  1.00 31.28           C  
ATOM    499  OG  SER A  95      67.817  40.934  50.545  1.00 34.22           O  
ATOM    500  N   VAL A  96      66.661  39.530  52.687  1.00 30.29           N  
ATOM    501  CA  VAL A  96      65.656  38.567  53.161  1.00 29.54           C  
ATOM    502  C   VAL A  96      65.388  37.448  52.138  1.00 29.50           C  
ATOM    503  O   VAL A  96      65.682  37.586  50.944  1.00 28.60           O  
ATOM    504  CB  VAL A  96      64.291  39.243  53.573  1.00 29.87           C  
ATOM    505  CG1 VAL A  96      64.443  40.160  54.789  1.00 28.36           C  
ATOM    506  CG2 VAL A  96      63.632  39.983  52.386  1.00 29.39           C  
ATOM    507  N   SER A  97      64.807  36.354  52.625  1.00 29.25           N  
ATOM    508  CA  SER A  97      64.556  35.144  51.837  1.00 29.84           C  
ATOM    509  C   SER A  97      63.503  35.310  50.750  1.00 29.50           C  
ATOM    510  O   SER A  97      63.503  34.571  49.767  1.00 30.14           O  
ATOM    511  CB  SER A  97      64.130  34.000  52.765  1.00 29.45           C  
ATOM    512  OG  SER A  97      62.932  34.347  53.451  1.00 32.39           O  
ATOM    513  N   THR A  98      62.608  36.276  50.936  1.00 29.76           N  
ATOM    514  CA  THR A  98      61.475  36.506  50.039  1.00 29.39           C  
ATOM    515  C   THR A  98      61.928  36.895  48.628  1.00 30.04           C  
ATOM    516  O   THR A  98      61.266  36.584  47.631  1.00 29.20           O  
ATOM    517  CB  THR A  98      60.516  37.577  50.622  1.00 29.50           C  
ATOM    518  OG1 THR A  98      60.372  37.369  52.038  1.00 27.99           O  
ATOM    519  CG2 THR A  98      59.155  37.505  49.959  1.00 27.16           C  
ATOM    520  N   ILE A  99      63.067  37.578  48.552  1.00 30.26           N  
ATOM    521  CA  ILE A  99      63.606  37.993  47.269  1.00 30.27           C  
ATOM    522  C   ILE A  99      65.041  37.487  47.059  1.00 30.31           C  
ATOM    523  O   ILE A  99      65.858  38.140  46.406  1.00 30.42           O  
ATOM    524  CB  ILE A  99      63.513  39.511  47.113  1.00 30.12           C  
ATOM    525  CG1 ILE A  99      64.151  40.215  48.329  1.00 29.57           C  
ATOM    526  CG2 ILE A  99      62.064  39.904  46.876  1.00 29.13           C  
ATOM    527  CD1 ILE A  99      64.265  41.729  48.180  1.00 30.56           C  
ATOM    528  N   LYS A 100      65.331  36.313  47.606  1.00 30.04           N  
ATOM    529  CA  LYS A 100      66.681  35.739  47.538  1.00 29.95           C  
ATOM    530  C   LYS A 100      67.189  35.582  46.099  1.00 29.97           C  
ATOM    531  O   LYS A 100      68.265  36.083  45.777  1.00 30.13           O  
ATOM    532  CB  LYS A 100      66.762  34.403  48.291  1.00 29.47           C  
ATOM    533  CG  LYS A 100      68.164  33.823  48.328  1.00 29.66           C  
ATOM    534  CD  LYS A 100      68.204  32.480  49.012  1.00 31.32           C  
ATOM    535  CE  LYS A 100      69.563  31.826  48.848  1.00 32.39           C  
ATOM    536  NZ  LYS A 100      69.494  30.340  49.057  1.00 33.87           N  
ATOM    537  N   ASP A 101      66.419  34.898  45.250  1.00 30.50           N  
ATOM    538  CA  ASP A 101      66.819  34.657  43.859  1.00 31.40           C  
ATOM    539  C   ASP A 101      67.091  35.954  43.106  1.00 31.87           C  
ATOM    540  O   ASP A 101      68.085  36.057  42.386  1.00 32.37           O  
ATOM    541  CB  ASP A 101      65.772  33.836  43.104  1.00 31.31           C  
ATOM    542  CG  ASP A 101      65.603  32.428  43.660  1.00 33.17           C  
ATOM    543  OD1 ASP A 101      64.542  31.827  43.381  1.00 35.13           O  
ATOM    544  OD2 ASP A 101      66.510  31.911  44.362  1.00 33.33           O  
ATOM    545  N   GLU A 102      66.220  36.945  43.282  1.00 32.26           N  
ATOM    546  CA  GLU A 102      66.341  38.194  42.536  1.00 33.32           C  
ATOM    547  C   GLU A 102      67.424  39.131  43.091  1.00 33.50           C  
ATOM    548  O   GLU A 102      67.829  40.075  42.416  1.00 33.76           O  
ATOM    549  CB  GLU A 102      64.968  38.892  42.331  1.00 33.36           C  
ATOM    550  CG  GLU A 102      63.909  38.652  43.411  1.00 35.84           C  
ATOM    551  CD  GLU A 102      63.235  37.278  43.331  1.00 36.81           C  
ATOM    552  OE1 GLU A 102      62.552  36.984  42.334  1.00 39.37           O  
ATOM    553  OE2 GLU A 102      63.387  36.483  44.272  1.00 37.58           O  
ATOM    554  N   MET A 103      67.902  38.857  44.305  1.00 33.88           N  
ATOM    555  CA  MET A 103      69.007  39.619  44.899  1.00 34.58           C  
ATOM    556  C   MET A 103      70.391  39.044  44.570  1.00 34.79           C  
ATOM    557  O   MET A 103      71.413  39.636  44.927  1.00 35.26           O  
ATOM    558  CB  MET A 103      68.847  39.715  46.427  1.00 34.78           C  
ATOM    559  CG  MET A 103      67.700  40.577  46.899  1.00 35.19           C  
ATOM    560  SD  MET A 103      67.912  42.280  46.398  1.00 40.01           S  
ATOM    561  CE  MET A 103      69.364  42.739  47.333  1.00 38.80           C  
ATOM    562  N   GLN A 104      70.423  37.894  43.903  1.00 34.90           N  
ATOM    563  CA  GLN A 104      71.680  37.198  43.616  1.00 35.35           C  
ATOM    564  C   GLN A 104      72.666  38.003  42.743  1.00 35.15           C  
ATOM    565  O   GLN A 104      73.854  38.038  43.056  1.00 34.98           O  
ATOM    566  CB  GLN A 104      71.429  35.792  43.029  1.00 35.57           C  
ATOM    567  CG  GLN A 104      70.867  34.761  44.027  1.00 36.87           C  
ATOM    568  CD  GLN A 104      71.855  34.363  45.127  1.00 38.85           C  
ATOM    569  OE1 GLN A 104      73.026  34.736  45.098  1.00 39.69           O  
ATOM    570  NE2 GLN A 104      71.380  33.589  46.097  1.00 39.66           N  
ATOM    571  N   PRO A 105      72.181  38.635  41.642  1.00 35.17           N  
ATOM    572  CA  PRO A 105      73.044  39.527  40.857  1.00 35.12           C  
ATOM    573  C   PRO A 105      73.691  40.636  41.693  1.00 35.10           C  
ATOM    574  O   PRO A 105      74.874  40.918  41.512  1.00 35.46           O  
ATOM    575  CB  PRO A 105      72.081  40.134  39.834  1.00 35.07           C  
ATOM    576  CG  PRO A 105      71.015  39.118  39.677  1.00 35.03           C  
ATOM    577  CD  PRO A 105      70.832  38.540  41.048  1.00 35.14           C  
ATOM    578  N   PHE A 106      72.915  41.244  42.593  1.00 35.08           N  
ATOM    579  CA  PHE A 106      73.396  42.304  43.494  1.00 34.95           C  
ATOM    580  C   PHE A 106      74.635  41.850  44.256  1.00 35.06           C  
ATOM    581  O   PHE A 106      75.689  42.498  44.180  1.00 34.60           O  
ATOM    582  CB  PHE A 106      72.281  42.741  44.467  1.00 34.56           C  
ATOM    583  CG  PHE A 106      72.755  43.640  45.589  1.00 34.45           C  
ATOM    584  CD1 PHE A 106      73.076  44.973  45.347  1.00 34.11           C  
ATOM    585  CD2 PHE A 106      72.868  43.156  46.887  1.00 33.87           C  
ATOM    586  CE1 PHE A 106      73.512  45.809  46.380  1.00 33.76           C  
ATOM    587  CE2 PHE A 106      73.301  43.986  47.928  1.00 35.06           C  
ATOM    588  CZ  PHE A 106      73.630  45.323  47.663  1.00 33.59           C  
ATOM    589  N   TYR A 107      74.496  40.724  44.961  1.00 35.17           N  
ATOM    590  CA  TYR A 107      75.582  40.127  45.738  1.00 35.66           C  
ATOM    591  C   TYR A 107      76.794  39.715  44.906  1.00 35.92           C  
ATOM    592  O   TYR A 107      77.922  39.790  45.393  1.00 36.06           O  
ATOM    593  CB  TYR A 107      75.076  38.961  46.597  1.00 35.50           C  
ATOM    594  CG  TYR A 107      74.361  39.428  47.847  1.00 35.11           C  
ATOM    595  CD1 TYR A 107      75.084  39.923  48.942  1.00 35.31           C  
ATOM    596  CD2 TYR A 107      72.961  39.413  47.931  1.00 34.90           C  
ATOM    597  CE1 TYR A 107      74.432  40.376  50.095  1.00 34.36           C  
ATOM    598  CE2 TYR A 107      72.293  39.869  49.098  1.00 34.08           C  
ATOM    599  CZ  TYR A 107      73.037  40.346  50.164  1.00 35.01           C  
ATOM    600  OH  TYR A 107      72.407  40.790  51.310  1.00 35.09           O  
ATOM    601  N   LYS A 108      76.561  39.287  43.663  1.00 36.66           N  
ATOM    602  CA  LYS A 108      77.658  39.009  42.704  1.00 37.11           C  
ATOM    603  C   LYS A 108      78.524  40.237  42.428  1.00 37.25           C  
ATOM    604  O   LYS A 108      79.753  40.160  42.483  1.00 37.10           O  
ATOM    605  CB  LYS A 108      77.111  38.485  41.375  1.00 37.09           C  
ATOM    606  CG  LYS A 108      77.030  36.974  41.268  1.00 37.74           C  
ATOM    607  CD  LYS A 108      77.051  36.527  39.802  1.00 37.25           C  
ATOM    608  CE  LYS A 108      78.458  36.535  39.228  1.00 38.16           C  
ATOM    609  NZ  LYS A 108      78.509  35.994  37.832  1.00 36.52           N  
ATOM    610  N   GLN A 109      77.867  41.357  42.122  1.00 37.76           N  
ATOM    611  CA  GLN A 109      78.537  42.630  41.817  1.00 38.52           C  
ATOM    612  C   GLN A 109      79.172  43.230  43.061  1.00 38.37           C  
ATOM    613  O   GLN A 109      80.230  43.859  42.991  1.00 38.39           O  
ATOM    614  CB  GLN A 109      77.550  43.635  41.218  1.00 38.80           C  
ATOM    615  CG  GLN A 109      77.038  43.279  39.817  1.00 40.50           C  
ATOM    616  CD  GLN A 109      75.681  43.903  39.523  1.00 42.47           C  
ATOM    617  OE1 GLN A 109      74.717  43.202  39.196  1.00 42.42           O  
ATOM    618  NE2 GLN A 109      75.596  45.227  39.655  1.00 43.39           N  
ATOM    619  N   LEU A 110      78.513  43.032  44.196  1.00 38.38           N  
ATOM    620  CA  LEU A 110      79.041  43.445  45.493  1.00 38.55           C  
ATOM    621  C   LEU A 110      80.311  42.669  45.845  1.00 38.59           C  
ATOM    622  O   LEU A 110      81.258  43.227  46.408  1.00 38.41           O  
ATOM    623  CB  LEU A 110      77.982  43.220  46.572  1.00 38.53           C  
ATOM    624  CG  LEU A 110      78.101  44.008  47.873  1.00 38.80           C  
ATOM    625  CD1 LEU A 110      78.092  45.510  47.593  1.00 38.37           C  
ATOM    626  CD2 LEU A 110      76.967  43.613  48.803  1.00 38.28           C  
ATOM    627  N   ASN A 111      80.309  41.386  45.476  1.00 38.72           N  
ATOM    628  CA  ASN A 111      81.338  40.408  45.847  1.00 38.87           C  
ATOM    629  C   ASN A 111      81.373  40.095  47.350  1.00 38.95           C  
ATOM    630  O   ASN A 111      82.442  39.956  47.952  1.00 38.85           O  
ATOM    631  CB  ASN A 111      82.720  40.799  45.310  1.00 38.74           C  
ATOM    632  CG  ASN A 111      83.597  39.592  45.047  1.00 39.78           C  
ATOM    633  OD1 ASN A 111      84.831  39.664  45.143  1.00 38.81           O  
ATOM    634  ND2 ASN A 111      82.962  38.463  44.716  1.00 40.05           N  
ATOM    635  N   MET A 112      80.188  39.971  47.946  1.00 39.03           N  
ATOM    636  CA  MET A 112      80.075  39.670  49.366  1.00 39.39           C  
ATOM    637  C   MET A 112      79.094  38.529  49.627  1.00 39.18           C  
ATOM    638  O   MET A 112      78.309  38.171  48.744  1.00 39.50           O  
ATOM    639  CB  MET A 112      79.680  40.928  50.146  1.00 39.56           C  
ATOM    640  CG  MET A 112      80.807  41.953  50.261  1.00 39.78           C  
ATOM    641  SD  MET A 112      80.351  43.419  51.195  1.00 40.20           S  
ATOM    642  CE  MET A 112      80.218  42.752  52.854  1.00 40.14           C  
ATOM    643  N   LYS A 113      79.167  37.953  50.830  1.00 38.89           N  
ATOM    644  CA  LYS A 113      78.284  36.861  51.251  1.00 38.42           C  
ATOM    645  C   LYS A 113      76.816  37.292  51.345  1.00 38.04           C  
ATOM    646  O   LYS A 113      76.469  38.294  51.978  1.00 38.09           O  
ATOM    647  CB  LYS A 113      78.755  36.239  52.583  1.00 38.44           C  
ATOM    648  CG  LYS A 113      77.779  35.196  53.143  1.00 38.07           C  
ATOM    649  CD  LYS A 113      78.300  34.419  54.340  1.00 38.67           C  
ATOM    650  CE  LYS A 113      77.184  33.557  54.919  1.00 39.16           C  
ATOM    651  NZ  LYS A 113      77.674  32.443  55.769  1.00 39.38           N  
ATOM    652  N   GLY A 114      75.958  36.524  50.690  1.00 37.69           N  
ATOM    653  CA  GLY A 114      74.532  36.730  50.788  1.00 36.80           C  
ATOM    654  C   GLY A 114      74.029  36.252  52.134  1.00 36.00           C  
ATOM    655  O   GLY A 114      74.317  35.139  52.552  1.00 36.11           O  
ATOM    656  N   TYR A 115      73.302  37.125  52.815  1.00 35.50           N  
ATOM    657  CA  TYR A 115      72.535  36.775  54.001  1.00 34.91           C  
ATOM    658  C   TYR A 115      71.081  36.985  53.631  1.00 34.14           C  
ATOM    659  O   TYR A 115      70.702  38.083  53.229  1.00 34.99           O  
ATOM    660  CB  TYR A 115      72.917  37.685  55.168  1.00 35.25           C  
ATOM    661  CG  TYR A 115      74.232  37.341  55.816  1.00 34.89           C  
ATOM    662  CD1 TYR A 115      75.390  38.056  55.517  1.00 36.05           C  
ATOM    663  CD2 TYR A 115      74.323  36.285  56.725  1.00 35.68           C  
ATOM    664  CE1 TYR A 115      76.625  37.720  56.122  1.00 36.09           C  
ATOM    665  CE2 TYR A 115      75.537  35.940  57.326  1.00 34.02           C  
ATOM    666  CZ  TYR A 115      76.677  36.660  57.026  1.00 35.40           C  
ATOM    667  OH  TYR A 115      77.867  36.315  57.633  1.00 36.36           O  
ATOM    668  N   PHE A 116      70.274  35.934  53.733  1.00 33.00           N  
ATOM    669  CA  PHE A 116      68.868  36.002  53.345  1.00 31.69           C  
ATOM    670  C   PHE A 116      67.985  35.427  54.432  1.00 30.71           C  
ATOM    671  O   PHE A 116      67.444  34.334  54.289  1.00 31.51           O  
ATOM    672  CB  PHE A 116      68.622  35.262  52.034  1.00 31.69           C  
ATOM    673  CG  PHE A 116      69.537  35.680  50.934  1.00 32.19           C  
ATOM    674  CD1 PHE A 116      69.247  36.798  50.160  1.00 30.82           C  
ATOM    675  CD2 PHE A 116      70.706  34.965  50.683  1.00 32.53           C  
ATOM    676  CE1 PHE A 116      70.099  37.200  49.150  1.00 31.70           C  
ATOM    677  CE2 PHE A 116      71.564  35.353  49.652  1.00 33.65           C  
ATOM    678  CZ  PHE A 116      71.259  36.480  48.886  1.00 31.96           C  
ATOM    679  N   TYR A 117      67.834  36.190  55.502  1.00 28.90           N  
ATOM    680  CA  TYR A 117      67.048  35.807  56.657  1.00 27.70           C  
ATOM    681  C   TYR A 117      65.597  35.536  56.302  1.00 27.54           C  
ATOM    682  O   TYR A 117      64.986  36.260  55.525  1.00 27.24           O  
ATOM    683  CB  TYR A 117      67.125  36.912  57.714  1.00 27.12           C  
ATOM    684  CG  TYR A 117      68.536  37.243  58.126  1.00 26.73           C  
ATOM    685  CD1 TYR A 117      69.134  36.581  59.195  1.00 25.96           C  
ATOM    686  CD2 TYR A 117      69.291  38.198  57.431  1.00 26.94           C  
ATOM    687  CE1 TYR A 117      70.438  36.866  59.578  1.00 26.91           C  
ATOM    688  CE2 TYR A 117      70.607  38.493  57.813  1.00 25.05           C  
ATOM    689  CZ  TYR A 117      71.165  37.817  58.892  1.00 26.25           C  
ATOM    690  OH  TYR A 117      72.448  38.077  59.305  1.00 25.80           O  
ATOM    691  N   ASP A 118      65.062  34.480  56.896  1.00 27.75           N  
ATOM    692  CA  ASP A 118      63.669  34.103  56.762  1.00 27.95           C  
ATOM    693  C   ASP A 118      62.749  35.087  57.489  1.00 27.90           C  
ATOM    694  O   ASP A 118      62.697  35.100  58.728  1.00 28.38           O  
ATOM    695  CB  ASP A 118      63.508  32.695  57.332  1.00 28.14           C  
ATOM    696  CG  ASP A 118      62.124  32.083  57.062  1.00 30.36           C  
ATOM    697  OD1 ASP A 118      61.185  32.789  56.595  1.00 29.59           O  
ATOM    698  OD2 ASP A 118      61.986  30.873  57.366  1.00 31.04           O  
ATOM    699  N   PHE A 119      62.051  35.929  56.715  1.00 26.99           N  
ATOM    700  CA  PHE A 119      61.026  36.833  57.232  1.00 25.99           C  
ATOM    701  C   PHE A 119      59.669  36.548  56.584  1.00 26.05           C  
ATOM    702  O   PHE A 119      58.854  37.463  56.428  1.00 26.26           O  
ATOM    703  CB  PHE A 119      61.414  38.302  56.999  1.00 25.88           C  
ATOM    704  CG  PHE A 119      62.333  38.873  58.055  1.00 25.64           C  
ATOM    705  CD1 PHE A 119      61.866  39.830  58.948  1.00 26.00           C  
ATOM    706  CD2 PHE A 119      63.666  38.445  58.161  1.00 23.97           C  
ATOM    707  CE1 PHE A 119      62.719  40.358  59.942  1.00 25.99           C  
ATOM    708  CE2 PHE A 119      64.501  38.956  59.145  1.00 22.43           C  
ATOM    709  CZ  PHE A 119      64.026  39.915  60.036  1.00 24.08           C  
ATOM    710  N   ASP A 120      59.428  35.285  56.230  1.00 26.11           N  
ATOM    711  CA  ASP A 120      58.156  34.855  55.601  1.00 26.14           C  
ATOM    712  C   ASP A 120      57.107  34.279  56.581  1.00 26.51           C  
ATOM    713  O   ASP A 120      56.013  33.885  56.171  1.00 26.85           O  
ATOM    714  CB  ASP A 120      58.430  33.887  54.438  1.00 25.33           C  
ATOM    715  CG  ASP A 120      59.132  34.567  53.256  1.00 25.92           C  
ATOM    716  OD1 ASP A 120      58.713  35.684  52.866  1.00 24.53           O  
ATOM    717  OD2 ASP A 120      60.101  33.990  52.707  1.00 24.77           O  
ATOM    718  N   SER A 121      57.451  34.240  57.867  1.00 26.52           N  
ATOM    719  CA  SER A 121      56.550  33.788  58.933  1.00 26.62           C  
ATOM    720  C   SER A 121      57.013  34.313  60.296  1.00 26.63           C  
ATOM    721  O   SER A 121      58.124  34.829  60.427  1.00 26.85           O  
ATOM    722  CB  SER A 121      56.433  32.251  58.970  1.00 26.56           C  
ATOM    723  OG  SER A 121      57.662  31.591  59.263  1.00 26.37           O  
ATOM    724  N   LEU A 122      56.155  34.175  61.302  1.00 26.43           N  
ATOM    725  CA  LEU A 122      56.530  34.432  62.698  1.00 26.51           C  
ATOM    726  C   LEU A 122      57.687  33.532  63.176  1.00 26.52           C  
ATOM    727  O   LEU A 122      58.661  34.015  63.763  1.00 26.56           O  
ATOM    728  CB  LEU A 122      55.312  34.242  63.602  1.00 26.37           C  
ATOM    729  CG  LEU A 122      54.363  35.431  63.813  1.00 27.41           C  
ATOM    730  CD1 LEU A 122      54.951  36.367  64.839  1.00 28.60           C  
ATOM    731  CD2 LEU A 122      53.986  36.203  62.523  1.00 27.96           C  
ATOM    732  N   LYS A 123      57.577  32.235  62.923  1.00 25.86           N  
ATOM    733  CA  LYS A 123      58.623  31.287  63.318  1.00 27.02           C  
ATOM    734  C   LYS A 123      59.946  31.572  62.593  1.00 25.65           C  
ATOM    735  O   LYS A 123      61.017  31.518  63.203  1.00 24.84           O  
ATOM    736  CB  LYS A 123      58.160  29.841  63.076  1.00 27.10           C  
ATOM    737  CG  LYS A 123      59.102  28.756  63.592  1.00 29.31           C  
ATOM    738  CD  LYS A 123      58.517  27.358  63.330  1.00 29.81           C  
ATOM    739  CE  LYS A 123      59.495  26.234  63.729  1.00 33.01           C  
ATOM    740  NZ  LYS A 123      60.719  26.162  62.844  1.00 35.64           N  
ATOM    741  N   GLY A 124      59.859  31.878  61.298  1.00 24.78           N  
ATOM    742  CA  GLY A 124      61.036  32.245  60.508  1.00 24.28           C  
ATOM    743  C   GLY A 124      61.759  33.477  61.016  1.00 24.23           C  
ATOM    744  O   GLY A 124      62.988  33.465  61.216  1.00 24.02           O  
ATOM    745  N   MET A 125      60.994  34.547  61.230  1.00 23.87           N  
ATOM    746  CA  MET A 125      61.532  35.784  61.780  1.00 23.91           C  
ATOM    747  C   MET A 125      62.112  35.619  63.194  1.00 24.01           C  
ATOM    748  O   MET A 125      63.121  36.245  63.509  1.00 24.46           O  
ATOM    749  CB  MET A 125      60.476  36.900  61.740  1.00 22.96           C  
ATOM    750  CG  MET A 125      60.930  38.233  62.356  1.00 24.68           C  
ATOM    751  SD  MET A 125      59.685  39.568  62.446  1.00 23.06           S  
ATOM    752  CE  MET A 125      58.417  38.814  63.453  1.00 24.63           C  
ATOM    753  N   GLN A 126      61.480  34.804  64.034  1.00 24.61           N  
ATOM    754  CA  GLN A 126      62.005  34.493  65.389  1.00 26.39           C  
ATOM    755  C   GLN A 126      63.404  33.827  65.314  1.00 25.48           C  
ATOM    756  O   GLN A 126      64.343  34.212  66.026  1.00 25.70           O  
ATOM    757  CB  GLN A 126      61.007  33.625  66.194  1.00 25.61           C  
ATOM    758  CG  GLN A 126      61.639  32.854  67.395  1.00 29.19           C  
ATOM    759  CD  GLN A 126      60.749  31.746  68.048  1.00 31.06           C  
ATOM    760  OE1 GLN A 126      61.040  31.287  69.172  1.00 36.60           O  
ATOM    761  NE2 GLN A 126      59.676  31.321  67.349  1.00 35.72           N  
ATOM    762  N   LYS A 127      63.540  32.848  64.432  1.00 25.25           N  
ATOM    763  CA  LYS A 127      64.835  32.214  64.150  1.00 25.72           C  
ATOM    764  C   LYS A 127      65.858  33.243  63.636  1.00 24.99           C  
ATOM    765  O   LYS A 127      66.996  33.236  64.073  1.00 25.29           O  
ATOM    766  CB  LYS A 127      64.653  31.055  63.151  1.00 25.63           C  
ATOM    767  CG  LYS A 127      65.883  30.171  62.930  1.00 28.10           C  
ATOM    768  CD  LYS A 127      65.508  28.888  62.141  1.00 27.47           C  
ATOM    769  CE  LYS A 127      66.703  27.931  62.014  1.00 30.54           C  
ATOM    770  NZ  LYS A 127      66.323  26.662  61.295  1.00 33.28           N  
ATOM    771  N   SER A 128      65.448  34.132  62.729  1.00 24.32           N  
ATOM    772  CA  SER A 128      66.352  35.169  62.206  1.00 23.91           C  
ATOM    773  C   SER A 128      66.829  36.149  63.299  1.00 24.34           C  
ATOM    774  O   SER A 128      67.994  36.547  63.312  1.00 24.67           O  
ATOM    775  CB  SER A 128      65.681  35.933  61.061  1.00 23.02           C  
ATOM    776  OG  SER A 128      65.264  35.015  60.061  1.00 22.71           O  
ATOM    777  N   ILE A 129      65.921  36.521  64.201  1.00 23.68           N  
ATOM    778  CA  ILE A 129      66.238  37.402  65.334  1.00 23.78           C  
ATOM    779  C   ILE A 129      67.295  36.773  66.255  1.00 23.88           C  
ATOM    780  O   ILE A 129      68.254  37.424  66.654  1.00 24.09           O  
ATOM    781  CB  ILE A 129      64.955  37.772  66.124  1.00 23.15           C  
ATOM    782  CG1 ILE A 129      64.075  38.728  65.288  1.00 22.72           C  
ATOM    783  CG2 ILE A 129      65.300  38.386  67.491  1.00 22.95           C  
ATOM    784  CD1 ILE A 129      62.584  38.772  65.730  1.00 22.98           C  
ATOM    785  N   THR A 130      67.114  35.502  66.573  1.00 23.76           N  
ATOM    786  CA  THR A 130      68.129  34.743  67.325  1.00 24.15           C  
ATOM    787  C   THR A 130      69.471  34.756  66.596  1.00 24.53           C  
ATOM    788  O   THR A 130      70.504  35.023  67.202  1.00 24.95           O  
ATOM    789  CB  THR A 130      67.661  33.308  67.568  1.00 23.34           C  
ATOM    790  OG1 THR A 130      66.465  33.363  68.346  1.00 24.27           O  
ATOM    791  CG2 THR A 130      68.725  32.466  68.309  1.00 23.16           C  
ATOM    792  N   GLN A 131      69.453  34.488  65.293  1.00 24.86           N  
ATOM    793  CA  GLN A 131      70.690  34.456  64.510  1.00 25.15           C  
ATOM    794  C   GLN A 131      71.422  35.802  64.564  1.00 24.98           C  
ATOM    795  O   GLN A 131      72.616  35.839  64.857  1.00 24.72           O  
ATOM    796  CB  GLN A 131      70.409  34.026  63.069  1.00 25.54           C  
ATOM    797  CG  GLN A 131      71.666  33.821  62.235  1.00 27.41           C  
ATOM    798  CD  GLN A 131      71.345  33.480  60.796  1.00 30.49           C  
ATOM    799  OE1 GLN A 131      70.166  33.395  60.411  1.00 30.77           O  
ATOM    800  NE2 GLN A 131      72.391  33.278  59.987  1.00 30.10           N  
ATOM    801  N   LEU A 132      70.698  36.899  64.315  1.00 24.94           N  
ATOM    802  CA  LEU A 132      71.262  38.248  64.424  1.00 25.10           C  
ATOM    803  C   LEU A 132      71.796  38.564  65.840  1.00 25.21           C  
ATOM    804  O   LEU A 132      72.822  39.229  65.975  1.00 25.15           O  
ATOM    805  CB  LEU A 132      70.245  39.308  63.996  1.00 25.02           C  
ATOM    806  CG  LEU A 132      69.734  39.318  62.551  1.00 25.70           C  
ATOM    807  CD1 LEU A 132      68.335  39.927  62.514  1.00 27.18           C  
ATOM    808  CD2 LEU A 132      70.679  40.089  61.630  1.00 25.29           C  
ATOM    809  N   GLY A 133      71.103  38.097  66.883  1.00 25.03           N  
ATOM    810  CA  GLY A 133      71.584  38.249  68.265  1.00 24.97           C  
ATOM    811  C   GLY A 133      72.932  37.564  68.465  1.00 24.90           C  
ATOM    812  O   GLY A 133      73.845  38.119  69.077  1.00 24.68           O  
ATOM    813  N   ASP A 134      73.045  36.359  67.921  1.00 25.33           N  
ATOM    814  CA  ASP A 134      74.266  35.557  67.987  1.00 26.04           C  
ATOM    815  C   ASP A 134      75.430  36.162  67.196  1.00 25.63           C  
ATOM    816  O   ASP A 134      76.554  36.174  67.678  1.00 25.35           O  
ATOM    817  CB  ASP A 134      73.990  34.133  67.488  1.00 26.68           C  
ATOM    818  CG  ASP A 134      73.131  33.309  68.465  1.00 29.54           C  
ATOM    819  OD1 ASP A 134      72.944  33.725  69.638  1.00 30.66           O  
ATOM    820  OD2 ASP A 134      72.653  32.217  68.052  1.00 33.08           O  
ATOM    821  N   GLN A 135      75.151  36.659  65.987  1.00 25.66           N  
ATOM    822  CA  GLN A 135      76.177  37.215  65.101  1.00 25.93           C  
ATOM    823  C   GLN A 135      76.775  38.503  65.660  1.00 25.55           C  
ATOM    824  O   GLN A 135      77.976  38.743  65.550  1.00 25.80           O  
ATOM    825  CB  GLN A 135      75.575  37.535  63.730  1.00 26.05           C  
ATOM    826  CG  GLN A 135      75.235  36.356  62.849  1.00 26.52           C  
ATOM    827  CD  GLN A 135      74.654  36.801  61.509  1.00 27.76           C  
ATOM    828  OE1 GLN A 135      75.386  37.028  60.541  1.00 30.53           O  
ATOM    829  NE2 GLN A 135      73.335  36.912  61.447  1.00 29.74           N  
ATOM    830  N   PHE A 136      75.915  39.326  66.258  1.00 25.41           N  
ATOM    831  CA  PHE A 136      76.243  40.702  66.565  1.00 25.17           C  
ATOM    832  C   PHE A 136      76.153  41.045  68.051  1.00 24.77           C  
ATOM    833  O   PHE A 136      75.908  42.198  68.385  1.00 25.36           O  
ATOM    834  CB  PHE A 136      75.358  41.653  65.732  1.00 24.84           C  
ATOM    835  CG  PHE A 136      75.386  41.372  64.256  1.00 24.98           C  
ATOM    836  CD1 PHE A 136      74.220  40.999  63.582  1.00 25.10           C  
ATOM    837  CD2 PHE A 136      76.577  41.466  63.533  1.00 25.25           C  
ATOM    838  CE1 PHE A 136      74.237  40.729  62.214  1.00 25.41           C  
ATOM    839  CE2 PHE A 136      76.613  41.196  62.161  1.00 25.18           C  
ATOM    840  CZ  PHE A 136      75.439  40.824  61.500  1.00 25.90           C  
ATOM    841  N   ASN A 137      76.336  40.049  68.923  1.00 24.04           N  
ATOM    842  CA  ASN A 137      76.431  40.247  70.396  1.00 23.62           C  
ATOM    843  C   ASN A 137      75.221  40.970  71.049  1.00 23.17           C  
ATOM    844  O   ASN A 137      75.382  41.945  71.800  1.00 22.85           O  
ATOM    845  CB  ASN A 137      77.789  40.894  70.785  1.00 23.44           C  
ATOM    846  CG  ASN A 137      78.080  40.830  72.288  1.00 23.10           C  
ATOM    847  OD1 ASN A 137      77.606  39.936  72.986  1.00 20.98           O  
ATOM    848  ND2 ASN A 137      78.859  41.794  72.788  1.00 21.95           N  
ATOM    849  N   ARG A 138      74.022  40.458  70.759  1.00 22.49           N  
ATOM    850  CA  ARG A 138      72.759  41.019  71.229  1.00 22.81           C  
ATOM    851  C   ARG A 138      71.796  39.895  71.597  1.00 23.38           C  
ATOM    852  O   ARG A 138      70.576  39.988  71.349  1.00 22.44           O  
ATOM    853  CB  ARG A 138      72.102  41.904  70.155  1.00 22.67           C  
ATOM    854  CG  ARG A 138      72.850  43.199  69.804  1.00 22.31           C  
ATOM    855  CD  ARG A 138      73.182  44.045  71.042  1.00 21.97           C  
ATOM    856  NE  ARG A 138      73.667  45.370  70.648  1.00 21.77           N  
ATOM    857  CZ  ARG A 138      74.949  45.702  70.543  1.00 20.95           C  
ATOM    858  NH1 ARG A 138      75.896  44.822  70.835  1.00 21.26           N  
ATOM    859  NH2 ARG A 138      75.282  46.923  70.166  1.00 21.18           N  
ATOM    860  N   LYS A 139      72.364  38.832  72.166  1.00 23.46           N  
ATOM    861  CA  LYS A 139      71.632  37.637  72.568  1.00 24.43           C  
ATOM    862  C   LYS A 139      70.464  37.970  73.506  1.00 24.16           C  
ATOM    863  O   LYS A 139      69.335  37.523  73.275  1.00 24.54           O  
ATOM    864  CB  LYS A 139      72.593  36.629  73.219  1.00 24.32           C  
ATOM    865  CG  LYS A 139      72.032  35.220  73.416  1.00 25.85           C  
ATOM    866  CD  LYS A 139      73.118  34.228  73.924  1.00 25.93           C  
ATOM    867  CE  LYS A 139      72.483  32.913  74.448  1.00 26.12           C  
ATOM    868  NZ  LYS A 139      73.450  32.004  75.166  1.00 28.26           N  
ATOM    869  N   ALA A 140      70.742  38.750  74.554  1.00 23.25           N  
ATOM    870  CA  ALA A 140      69.717  39.195  75.490  1.00 22.75           C  
ATOM    871  C   ALA A 140      68.623  40.038  74.825  1.00 22.42           C  
ATOM    872  O   ALA A 140      67.446  39.811  75.087  1.00 22.40           O  
ATOM    873  CB  ALA A 140      70.350  39.943  76.702  1.00 21.98           C  
ATOM    874  N   GLN A 141      68.997  40.996  73.968  1.00 22.14           N  
ATOM    875  CA  GLN A 141      67.994  41.821  73.242  1.00 21.51           C  
ATOM    876  C   GLN A 141      67.108  40.971  72.335  1.00 21.56           C  
ATOM    877  O   GLN A 141      65.901  41.221  72.200  1.00 21.08           O  
ATOM    878  CB  GLN A 141      68.653  42.926  72.414  1.00 21.63           C  
ATOM    879  CG  GLN A 141      69.291  44.078  73.241  1.00 20.82           C  
ATOM    880  CD  GLN A 141      70.668  43.736  73.830  1.00 20.13           C  
ATOM    881  OE1 GLN A 141      71.143  42.596  73.748  1.00 19.38           O  
ATOM    882  NE2 GLN A 141      71.313  44.735  74.425  1.00 20.82           N  
ATOM    883  N   ALA A 142      67.730  39.984  71.697  1.00 21.25           N  
ATOM    884  CA  ALA A 142      67.041  39.072  70.784  1.00 21.07           C  
ATOM    885  C   ALA A 142      66.034  38.208  71.528  1.00 21.40           C  
ATOM    886  O   ALA A 142      64.895  38.059  71.095  1.00 21.29           O  
ATOM    887  CB  ALA A 142      68.050  38.205  70.039  1.00 20.82           C  
ATOM    888  N   LYS A 143      66.459  37.650  72.655  1.00 22.08           N  
ATOM    889  CA  LYS A 143      65.573  36.863  73.513  1.00 23.34           C  
ATOM    890  C   LYS A 143      64.348  37.664  73.981  1.00 23.26           C  
ATOM    891  O   LYS A 143      63.218  37.157  73.983  1.00 22.77           O  
ATOM    892  CB  LYS A 143      66.343  36.323  74.725  1.00 24.02           C  
ATOM    893  CG  LYS A 143      65.507  35.408  75.601  1.00 26.33           C  
ATOM    894  CD  LYS A 143      66.178  35.107  76.922  1.00 29.66           C  
ATOM    895  CE  LYS A 143      65.302  34.169  77.745  1.00 31.70           C  
ATOM    896  NZ  LYS A 143      64.746  33.092  76.847  1.00 32.63           N  
ATOM    897  N   GLU A 144      64.584  38.904  74.396  1.00 23.19           N  
ATOM    898  CA  GLU A 144      63.501  39.778  74.821  1.00 23.38           C  
ATOM    899  C   GLU A 144      62.470  40.022  73.710  1.00 22.90           C  
ATOM    900  O   GLU A 144      61.271  39.852  73.921  1.00 22.81           O  
ATOM    901  CB  GLU A 144      64.045  41.118  75.300  1.00 22.89           C  
ATOM    902  CG  GLU A 144      62.956  42.065  75.798  1.00 24.19           C  
ATOM    903  CD  GLU A 144      63.515  43.407  76.224  1.00 27.16           C  
ATOM    904  OE1 GLU A 144      64.743  43.594  76.179  1.00 25.96           O  
ATOM    905  OE2 GLU A 144      62.719  44.288  76.593  1.00 32.45           O  
ATOM    906  N   LEU A 145      62.941  40.444  72.544  1.00 22.82           N  
ATOM    907  CA  LEU A 145      62.062  40.631  71.395  1.00 23.05           C  
ATOM    908  C   LEU A 145      61.284  39.344  71.073  1.00 23.10           C  
ATOM    909  O   LEU A 145      60.069  39.404  70.895  1.00 23.72           O  
ATOM    910  CB  LEU A 145      62.849  41.134  70.170  1.00 23.17           C  
ATOM    911  CG  LEU A 145      62.109  41.330  68.839  1.00 23.92           C  
ATOM    912  CD1 LEU A 145      60.942  42.362  68.987  1.00 22.69           C  
ATOM    913  CD2 LEU A 145      63.101  41.779  67.774  1.00 21.94           C  
ATOM    914  N   ASN A 146      61.982  38.207  71.022  1.00 22.84           N  
ATOM    915  CA  ASN A 146      61.377  36.907  70.716  1.00 23.75           C  
ATOM    916  C   ASN A 146      60.339  36.483  71.753  1.00 23.91           C  
ATOM    917  O   ASN A 146      59.278  36.011  71.384  1.00 24.07           O  
ATOM    918  CB  ASN A 146      62.426  35.789  70.526  1.00 22.38           C  
ATOM    919  CG  ASN A 146      63.001  35.738  69.107  1.00 23.09           C  
ATOM    920  OD1 ASN A 146      62.408  36.246  68.157  1.00 24.12           O  
ATOM    921  ND2 ASN A 146      64.169  35.125  68.966  1.00 19.36           N  
ATOM    922  N   ASP A 147      60.639  36.672  73.033  1.00 24.04           N  
ATOM    923  CA  ASP A 147      59.695  36.350  74.106  1.00 25.02           C  
ATOM    924  C   ASP A 147      58.405  37.181  73.965  1.00 25.17           C  
ATOM    925  O   ASP A 147      57.299  36.671  74.164  1.00 24.94           O  
ATOM    926  CB  ASP A 147      60.322  36.593  75.489  1.00 24.53           C  
ATOM    927  CG  ASP A 147      61.242  35.445  75.961  1.00 27.04           C  
ATOM    928  OD1 ASP A 147      61.456  34.439  75.240  1.00 25.98           O  
ATOM    929  OD2 ASP A 147      61.747  35.545  77.104  1.00 29.01           O  
ATOM    930  N   HIS A 148      58.545  38.454  73.603  1.00 25.21           N  
ATOM    931  CA  HIS A 148      57.378  39.325  73.483  1.00 25.67           C  
ATOM    932  C   HIS A 148      56.479  38.937  72.290  1.00 25.90           C  
ATOM    933  O   HIS A 148      55.254  38.839  72.424  1.00 25.84           O  
ATOM    934  CB  HIS A 148      57.805  40.783  73.362  1.00 25.90           C  
ATOM    935  CG  HIS A 148      56.700  41.683  72.914  1.00 26.39           C  
ATOM    936  ND1 HIS A 148      55.675  42.073  73.750  1.00 27.50           N  
ATOM    937  CD2 HIS A 148      56.435  42.236  71.706  1.00 28.17           C  
ATOM    938  CE1 HIS A 148      54.833  42.839  73.076  1.00 27.68           C  
ATOM    939  NE2 HIS A 148      55.273  42.953  71.834  1.00 27.36           N  
ATOM    940  N   LEU A 149      57.098  38.742  71.133  1.00 25.62           N  
ATOM    941  CA  LEU A 149      56.413  38.307  69.917  1.00 26.05           C  
ATOM    942  C   LEU A 149      55.728  36.935  70.133  1.00 25.92           C  
ATOM    943  O   LEU A 149      54.572  36.756  69.754  1.00 25.81           O  
ATOM    944  CB  LEU A 149      57.421  38.235  68.756  1.00 25.65           C  
ATOM    945  CG  LEU A 149      57.589  39.333  67.682  1.00 27.21           C  
ATOM    946  CD1 LEU A 149      56.995  40.686  68.017  1.00 25.81           C  
ATOM    947  CD2 LEU A 149      59.058  39.437  67.252  1.00 26.31           C  
ATOM    948  N   ASN A 150      56.448  35.995  70.751  1.00 25.94           N  
ATOM    949  CA  ASN A 150      55.922  34.676  71.125  1.00 26.53           C  
ATOM    950  C   ASN A 150      54.702  34.742  72.042  1.00 26.61           C  
ATOM    951  O   ASN A 150      53.738  33.987  71.877  1.00 25.91           O  
ATOM    952  CB  ASN A 150      56.984  33.874  71.887  1.00 27.20           C  
ATOM    953  CG  ASN A 150      58.012  33.219  70.986  1.00 28.71           C  
ATOM    954  OD1 ASN A 150      58.933  32.557  71.485  1.00 30.90           O  
ATOM    955  ND2 ASN A 150      57.882  33.398  69.672  1.00 29.40           N  
ATOM    956  N   SER A 151      54.790  35.628  73.034  1.00 26.58           N  
ATOM    957  CA  SER A 151      53.725  35.838  73.997  1.00 27.07           C  
ATOM    958  C   SER A 151      52.437  36.414  73.373  1.00 26.66           C  
ATOM    959  O   SER A 151      51.335  35.937  73.679  1.00 27.03           O  
ATOM    960  CB  SER A 151      54.233  36.706  75.149  1.00 26.93           C  
ATOM    961  OG  SER A 151      53.154  37.156  75.936  1.00 29.59           O  
ATOM    962  N   VAL A 152      52.574  37.420  72.508  1.00 26.18           N  
ATOM    963  CA  VAL A 152      51.434  37.952  71.745  1.00 25.69           C  
ATOM    964  C   VAL A 152      50.848  36.873  70.837  1.00 25.77           C  
ATOM    965  O   VAL A 152      49.626  36.733  70.760  1.00 25.59           O  
ATOM    966  CB  VAL A 152      51.817  39.192  70.894  1.00 25.82           C  
ATOM    967  CG1 VAL A 152      50.639  39.647  70.027  1.00 25.53           C  
ATOM    968  CG2 VAL A 152      52.276  40.336  71.797  1.00 26.14           C  
ATOM    969  N   LYS A 153      51.725  36.113  70.168  1.00 25.70           N  
ATOM    970  CA  LYS A 153      51.303  35.083  69.214  1.00 26.60           C  
ATOM    971  C   LYS A 153      50.481  33.994  69.917  1.00 26.30           C  
ATOM    972  O   LYS A 153      49.386  33.650  69.462  1.00 25.91           O  
ATOM    973  CB  LYS A 153      52.519  34.473  68.498  1.00 26.42           C  
ATOM    974  CG  LYS A 153      52.196  33.509  67.357  1.00 27.69           C  
ATOM    975  CD  LYS A 153      53.496  32.841  66.814  1.00 27.71           C  
ATOM    976  CE  LYS A 153      53.209  31.814  65.719  1.00 29.69           C  
ATOM    977  NZ  LYS A 153      52.668  30.528  66.278  1.00 31.67           N  
ATOM    978  N   GLN A 154      51.011  33.470  71.025  1.00 26.25           N  
ATOM    979  CA  GLN A 154      50.292  32.479  71.811  1.00 27.06           C  
ATOM    980  C   GLN A 154      48.955  32.989  72.331  1.00 26.43           C  
ATOM    981  O   GLN A 154      47.975  32.264  72.302  1.00 26.96           O  
ATOM    982  CB  GLN A 154      51.144  31.918  72.952  1.00 27.41           C  
ATOM    983  CG  GLN A 154      50.685  30.528  73.453  1.00 31.36           C  
ATOM    984  CD  GLN A 154      50.229  29.570  72.328  1.00 35.93           C  
ATOM    985  OE1 GLN A 154      49.225  28.863  72.474  1.00 36.90           O  
ATOM    986  NE2 GLN A 154      50.956  29.563  71.202  1.00 37.45           N  
ATOM    987  N   LYS A 155      48.910  34.234  72.785  1.00 25.87           N  
ATOM    988  CA  LYS A 155      47.659  34.817  73.284  1.00 26.15           C  
ATOM    989  C   LYS A 155      46.586  34.936  72.192  1.00 24.25           C  
ATOM    990  O   LYS A 155      45.423  34.664  72.448  1.00 23.65           O  
ATOM    991  CB  LYS A 155      47.932  36.166  73.970  1.00 26.27           C  
ATOM    992  CG  LYS A 155      46.733  37.108  74.093  1.00 28.55           C  
ATOM    993  CD  LYS A 155      47.156  38.513  74.583  1.00 28.71           C  
ATOM    994  CE  LYS A 155      48.193  39.170  73.618  1.00 30.77           C  
ATOM    995  NZ  LYS A 155      47.597  40.139  72.664  1.00 30.93           N  
ATOM    996  N   ILE A 156      46.986  35.321  70.980  1.00 23.49           N  
ATOM    997  CA  ILE A 156      46.048  35.449  69.840  1.00 22.37           C  
ATOM    998  C   ILE A 156      45.583  34.065  69.387  1.00 22.42           C  
ATOM    999  O   ILE A 156      44.397  33.842  69.125  1.00 22.12           O  
ATOM   1000  CB  ILE A 156      46.671  36.231  68.630  1.00 22.11           C  
ATOM   1001  CG1 ILE A 156      46.970  37.696  68.993  1.00 22.03           C  
ATOM   1002  CG2 ILE A 156      45.768  36.129  67.393  1.00 20.61           C  
ATOM   1003  CD1 ILE A 156      45.767  38.518  69.540  1.00 20.75           C  
ATOM   1004  N   GLU A 157      46.531  33.133  69.321  1.00 22.44           N  
ATOM   1005  CA  GLU A 157      46.226  31.728  69.058  1.00 23.36           C  
ATOM   1006  C   GLU A 157      45.249  31.138  70.058  1.00 22.35           C  
ATOM   1007  O   GLU A 157      44.322  30.439  69.667  1.00 22.21           O  
ATOM   1008  CB  GLU A 157      47.510  30.882  68.984  1.00 23.27           C  
ATOM   1009  CG  GLU A 157      48.233  31.101  67.661  1.00 24.16           C  
ATOM   1010  CD  GLU A 157      49.519  30.304  67.525  1.00 25.31           C  
ATOM   1011  OE1 GLU A 157      50.058  29.803  68.537  1.00 28.00           O  
ATOM   1012  OE2 GLU A 157      50.014  30.214  66.385  1.00 28.93           O  
ATOM   1013  N   ASN A 158      45.445  31.429  71.341  1.00 22.37           N  
ATOM   1014  CA  ASN A 158      44.510  30.967  72.371  1.00 22.84           C  
ATOM   1015  C   ASN A 158      43.089  31.552  72.233  1.00 22.64           C  
ATOM   1016  O   ASN A 158      42.092  30.835  72.401  1.00 22.76           O  
ATOM   1017  CB  ASN A 158      45.087  31.184  73.773  1.00 22.85           C  
ATOM   1018  CG  ASN A 158      46.261  30.245  74.075  1.00 24.16           C  
ATOM   1019  OD1 ASN A 158      46.525  29.297  73.330  1.00 26.85           O  
ATOM   1020  ND2 ASN A 158      46.966  30.508  75.171  1.00 22.88           N  
ATOM   1021  N   LYS A 159      42.998  32.838  71.907  1.00 22.82           N  
ATOM   1022  CA  LYS A 159      41.695  33.479  71.662  1.00 23.04           C  
ATOM   1023  C   LYS A 159      41.008  32.857  70.444  1.00 23.09           C  
ATOM   1024  O   LYS A 159      39.833  32.478  70.516  1.00 22.34           O  
ATOM   1025  CB  LYS A 159      41.837  34.990  71.471  1.00 23.24           C  
ATOM   1026  CG  LYS A 159      42.031  35.769  72.751  1.00 24.15           C  
ATOM   1027  CD  LYS A 159      42.247  37.247  72.437  1.00 27.33           C  
ATOM   1028  CE  LYS A 159      42.670  38.050  73.694  1.00 29.67           C  
ATOM   1029  NZ  LYS A 159      41.666  38.212  74.808  1.00 30.98           N  
ATOM   1030  N   ALA A 160      41.756  32.734  69.342  1.00 23.04           N  
ATOM   1031  CA  ALA A 160      41.226  32.180  68.094  1.00 23.84           C  
ATOM   1032  C   ALA A 160      40.638  30.786  68.284  1.00 24.31           C  
ATOM   1033  O   ALA A 160      39.586  30.486  67.731  1.00 23.98           O  
ATOM   1034  CB  ALA A 160      42.307  32.150  67.011  1.00 23.39           C  
ATOM   1035  N   ALA A 161      41.329  29.950  69.066  1.00 25.07           N  
ATOM   1036  CA  ALA A 161      40.935  28.556  69.312  1.00 26.01           C  
ATOM   1037  C   ALA A 161      39.613  28.454  70.068  1.00 26.60           C  
ATOM   1038  O   ALA A 161      38.890  27.467  69.940  1.00 26.59           O  
ATOM   1039  CB  ALA A 161      42.037  27.826  70.094  1.00 26.12           C  
ATOM   1040  N   LYS A 162      39.313  29.474  70.865  1.00 27.25           N  
ATOM   1041  CA  LYS A 162      38.071  29.524  71.618  1.00 27.66           C  
ATOM   1042  C   LYS A 162      36.881  29.967  70.753  1.00 27.78           C  
ATOM   1043  O   LYS A 162      35.722  29.779  71.151  1.00 27.79           O  
ATOM   1044  CB  LYS A 162      38.219  30.436  72.838  1.00 27.92           C  
ATOM   1045  CG  LYS A 162      39.143  29.883  73.912  1.00 29.22           C  
ATOM   1046  CD  LYS A 162      39.210  30.814  75.117  1.00 31.81           C  
ATOM   1047  CE  LYS A 162      40.014  30.191  76.246  1.00 32.96           C  
ATOM   1048  NZ  LYS A 162      39.758  30.824  77.574  1.00 34.76           N  
ATOM   1049  N   GLN A 163      37.157  30.548  69.583  1.00 27.30           N  
ATOM   1050  CA  GLN A 163      36.085  30.996  68.687  1.00 27.58           C  
ATOM   1051  C   GLN A 163      35.375  29.804  68.056  1.00 28.07           C  
ATOM   1052  O   GLN A 163      36.017  28.828  67.679  1.00 28.52           O  
ATOM   1053  CB  GLN A 163      36.600  31.926  67.586  1.00 27.10           C  
ATOM   1054  CG  GLN A 163      37.082  33.275  68.067  1.00 27.46           C  
ATOM   1055  CD  GLN A 163      35.943  34.201  68.494  1.00 28.11           C  
ATOM   1056  OE1 GLN A 163      34.777  33.982  68.172  1.00 28.22           O  
ATOM   1057  NE2 GLN A 163      36.288  35.241  69.220  1.00 29.89           N  
ATOM   1058  N   LYS A 164      34.051  29.902  67.939  1.00 28.55           N  
ATOM   1059  CA  LYS A 164      33.231  28.844  67.352  1.00 29.40           C  
ATOM   1060  C   LYS A 164      33.398  28.821  65.827  1.00 28.82           C  
ATOM   1061  O   LYS A 164      33.415  27.759  65.213  1.00 28.90           O  
ATOM   1062  CB  LYS A 164      31.753  29.069  67.697  1.00 29.94           C  
ATOM   1063  CG  LYS A 164      31.033  27.877  68.335  1.00 32.82           C  
ATOM   1064  CD  LYS A 164      30.848  26.689  67.366  1.00 35.49           C  
ATOM   1065  CE  LYS A 164      30.366  25.433  68.108  1.00 34.35           C  
ATOM   1066  NZ  LYS A 164      30.619  24.194  67.294  1.00 36.63           N  
ATOM   1067  N   LYS A 165      33.508  30.001  65.227  1.00 28.21           N  
ATOM   1068  CA  LYS A 165      33.590  30.117  63.779  1.00 27.77           C  
ATOM   1069  C   LYS A 165      34.950  30.621  63.347  1.00 26.90           C  
ATOM   1070  O   LYS A 165      35.622  31.351  64.088  1.00 26.54           O  
ATOM   1071  CB  LYS A 165      32.493  31.039  63.230  1.00 28.05           C  
ATOM   1072  CG  LYS A 165      31.126  30.365  63.030  1.00 30.82           C  
ATOM   1073  CD  LYS A 165      30.272  31.176  62.037  1.00 34.17           C  
ATOM   1074  CE  LYS A 165      29.101  30.377  61.468  1.00 34.17           C  
ATOM   1075  NZ  LYS A 165      27.951  30.336  62.421  1.00 36.28           N  
ATOM   1076  N   HIS A 166      35.346  30.219  62.143  1.00 25.77           N  
ATOM   1077  CA  HIS A 166      36.555  30.716  61.518  1.00 25.04           C  
ATOM   1078  C   HIS A 166      36.248  31.195  60.106  1.00 24.73           C  
ATOM   1079  O   HIS A 166      35.625  30.466  59.342  1.00 25.58           O  
ATOM   1080  CB  HIS A 166      37.625  29.638  61.550  1.00 24.91           C  
ATOM   1081  CG  HIS A 166      37.971  29.205  62.937  1.00 24.56           C  
ATOM   1082  ND1 HIS A 166      38.860  29.902  63.733  1.00 23.87           N  
ATOM   1083  CD2 HIS A 166      37.506  28.183  63.693  1.00 23.64           C  
ATOM   1084  CE1 HIS A 166      38.947  29.308  64.911  1.00 24.22           C  
ATOM   1085  NE2 HIS A 166      38.145  28.256  64.908  1.00 24.94           N  
ATOM   1086  N   PRO A 167      36.634  32.442  59.773  1.00 24.00           N  
ATOM   1087  CA  PRO A 167      36.352  32.921  58.426  1.00 23.62           C  
ATOM   1088  C   PRO A 167      37.265  32.293  57.378  1.00 23.71           C  
ATOM   1089  O   PRO A 167      38.458  32.069  57.629  1.00 23.19           O  
ATOM   1090  CB  PRO A 167      36.643  34.426  58.516  1.00 23.71           C  
ATOM   1091  CG  PRO A 167      37.647  34.559  59.610  1.00 23.26           C  
ATOM   1092  CD  PRO A 167      37.330  33.458  60.593  1.00 23.85           C  
ATOM   1093  N   LYS A 168      36.696  32.010  56.212  1.00 23.39           N  
ATOM   1094  CA  LYS A 168      37.487  31.683  55.043  1.00 23.00           C  
ATOM   1095  C   LYS A 168      37.983  32.976  54.420  1.00 22.42           C  
ATOM   1096  O   LYS A 168      37.229  33.921  54.251  1.00 22.57           O  
ATOM   1097  CB  LYS A 168      36.671  30.844  54.062  1.00 22.90           C  
ATOM   1098  CG  LYS A 168      36.322  29.491  54.627  1.00 23.77           C  
ATOM   1099  CD  LYS A 168      35.747  28.574  53.557  1.00 23.85           C  
ATOM   1100  CE  LYS A 168      35.763  27.128  54.012  1.00 24.24           C  
ATOM   1101  NZ  LYS A 168      34.747  26.846  55.041  1.00 22.27           N  
ATOM   1102  N   VAL A 169      39.269  33.023  54.104  1.00 22.31           N  
ATOM   1103  CA  VAL A 169      39.900  34.270  53.722  1.00 21.73           C  
ATOM   1104  C   VAL A 169      40.621  34.103  52.396  1.00 22.22           C  
ATOM   1105  O   VAL A 169      41.296  33.084  52.170  1.00 21.93           O  
ATOM   1106  CB  VAL A 169      40.910  34.750  54.787  1.00 21.65           C  
ATOM   1107  CG1 VAL A 169      41.515  36.100  54.394  1.00 20.06           C  
ATOM   1108  CG2 VAL A 169      40.255  34.818  56.165  1.00 21.09           C  
ATOM   1109  N   LEU A 170      40.455  35.101  51.522  1.00 21.77           N  
ATOM   1110  CA  LEU A 170      41.288  35.229  50.320  1.00 21.82           C  
ATOM   1111  C   LEU A 170      42.189  36.466  50.473  1.00 21.87           C  
ATOM   1112  O   LEU A 170      41.704  37.566  50.774  1.00 21.60           O  
ATOM   1113  CB  LEU A 170      40.416  35.318  49.048  1.00 21.53           C  
ATOM   1114  CG  LEU A 170      41.055  35.812  47.748  1.00 20.94           C  
ATOM   1115  CD1 LEU A 170      42.099  34.818  47.202  1.00 22.18           C  
ATOM   1116  CD2 LEU A 170      39.978  36.101  46.701  1.00 21.99           C  
ATOM   1117  N   ILE A 171      43.499  36.274  50.302  1.00 21.58           N  
ATOM   1118  CA  ILE A 171      44.463  37.366  50.495  1.00 20.88           C  
ATOM   1119  C   ILE A 171      45.048  37.805  49.163  1.00 21.64           C  
ATOM   1120  O   ILE A 171      45.690  36.998  48.460  1.00 21.87           O  
ATOM   1121  CB  ILE A 171      45.641  36.953  51.403  1.00 21.15           C  
ATOM   1122  CG1 ILE A 171      45.154  36.127  52.614  1.00 19.48           C  
ATOM   1123  CG2 ILE A 171      46.443  38.206  51.819  1.00 19.75           C  
ATOM   1124  CD1 ILE A 171      46.192  35.148  53.165  1.00 19.26           C  
ATOM   1125  N   LEU A 172      44.819  39.073  48.809  1.00 21.65           N  
ATOM   1126  CA  LEU A 172      45.438  39.674  47.618  1.00 21.64           C  
ATOM   1127  C   LEU A 172      46.646  40.571  47.977  1.00 22.03           C  
ATOM   1128  O   LEU A 172      46.597  41.364  48.908  1.00 21.35           O  
ATOM   1129  CB  LEU A 172      44.394  40.450  46.791  1.00 21.00           C  
ATOM   1130  CG  LEU A 172      43.120  39.666  46.429  1.00 21.86           C  
ATOM   1131  CD1 LEU A 172      42.134  40.488  45.586  1.00 18.46           C  
ATOM   1132  CD2 LEU A 172      43.465  38.341  45.713  1.00 17.68           C  
ATOM   1133  N   MET A 173      47.734  40.411  47.227  1.00 22.23           N  
ATOM   1134  CA  MET A 173      48.913  41.253  47.361  1.00 22.09           C  
ATOM   1135  C   MET A 173      49.051  42.034  46.062  1.00 22.25           C  
ATOM   1136  O   MET A 173      49.358  41.466  45.013  1.00 21.77           O  
ATOM   1137  CB  MET A 173      50.175  40.415  47.634  1.00 22.22           C  
ATOM   1138  CG  MET A 173      51.477  41.241  47.714  1.00 22.32           C  
ATOM   1139  SD  MET A 173      51.453  42.491  49.011  1.00 22.84           S  
ATOM   1140  CE  MET A 173      51.515  41.462  50.492  1.00 19.85           C  
ATOM   1141  N   GLY A 174      48.788  43.335  46.138  1.00 22.29           N  
ATOM   1142  CA  GLY A 174      48.837  44.181  44.971  1.00 22.16           C  
ATOM   1143  C   GLY A 174      50.195  44.817  44.869  1.00 22.39           C  
ATOM   1144  O   GLY A 174      50.733  45.326  45.855  1.00 22.92           O  
ATOM   1145  N   VAL A 175      50.750  44.772  43.669  1.00 22.88           N  
ATOM   1146  CA  VAL A 175      52.024  45.409  43.359  1.00 23.57           C  
ATOM   1147  C   VAL A 175      51.794  46.374  42.183  1.00 23.70           C  
ATOM   1148  O   VAL A 175      50.716  46.361  41.582  1.00 24.29           O  
ATOM   1149  CB  VAL A 175      53.123  44.355  43.049  1.00 23.21           C  
ATOM   1150  CG1 VAL A 175      53.240  43.387  44.198  1.00 24.39           C  
ATOM   1151  CG2 VAL A 175      52.817  43.600  41.750  1.00 22.67           C  
ATOM   1152  N   PRO A 176      52.772  47.256  41.883  1.00 24.08           N  
ATOM   1153  CA  PRO A 176      52.569  48.094  40.702  1.00 24.12           C  
ATOM   1154  C   PRO A 176      52.325  47.264  39.434  1.00 24.37           C  
ATOM   1155  O   PRO A 176      53.191  46.490  39.031  1.00 24.92           O  
ATOM   1156  CB  PRO A 176      53.877  48.887  40.611  1.00 23.95           C  
ATOM   1157  CG  PRO A 176      54.380  48.923  42.041  1.00 24.93           C  
ATOM   1158  CD  PRO A 176      54.030  47.580  42.587  1.00 23.58           C  
ATOM   1159  N   GLY A 177      51.144  47.412  38.830  1.00 24.55           N  
ATOM   1160  CA  GLY A 177      50.812  46.724  37.576  1.00 23.53           C  
ATOM   1161  C   GLY A 177      49.819  45.560  37.640  1.00 23.59           C  
ATOM   1162  O   GLY A 177      49.103  45.305  36.676  1.00 23.56           O  
ATOM   1163  N   SER A 178      49.772  44.842  38.764  1.00 23.61           N  
ATOM   1164  CA  SER A 178      48.960  43.627  38.851  1.00 23.18           C  
ATOM   1165  C   SER A 178      48.824  43.174  40.297  1.00 22.63           C  
ATOM   1166  O   SER A 178      49.451  43.731  41.179  1.00 22.42           O  
ATOM   1167  CB  SER A 178      49.627  42.510  38.028  1.00 23.01           C  
ATOM   1168  OG  SER A 178      50.923  42.239  38.532  1.00 23.63           O  
ATOM   1169  N   TYR A 179      48.004  42.157  40.543  1.00 22.62           N  
ATOM   1170  CA  TYR A 179      47.946  41.558  41.870  1.00 22.99           C  
ATOM   1171  C   TYR A 179      48.221  40.054  41.887  1.00 23.05           C  
ATOM   1172  O   TYR A 179      48.036  39.335  40.901  1.00 23.03           O  
ATOM   1173  CB  TYR A 179      46.642  41.907  42.605  1.00 22.85           C  
ATOM   1174  CG  TYR A 179      45.410  41.300  41.972  1.00 23.92           C  
ATOM   1175  CD1 TYR A 179      44.758  41.941  40.927  1.00 21.92           C  
ATOM   1176  CD2 TYR A 179      44.901  40.083  42.419  1.00 21.58           C  
ATOM   1177  CE1 TYR A 179      43.646  41.379  40.338  1.00 23.13           C  
ATOM   1178  CE2 TYR A 179      43.781  39.540  41.855  1.00 21.22           C  
ATOM   1179  CZ  TYR A 179      43.166  40.185  40.808  1.00 21.86           C  
ATOM   1180  OH  TYR A 179      42.054  39.623  40.235  1.00 25.62           O  
ATOM   1181  N   LEU A 180      48.685  39.599  43.040  1.00 23.37           N  
ATOM   1182  CA  LEU A 180      49.046  38.218  43.257  1.00 23.68           C  
ATOM   1183  C   LEU A 180      48.192  37.694  44.408  1.00 23.68           C  
ATOM   1184  O   LEU A 180      47.454  38.458  45.044  1.00 22.72           O  
ATOM   1185  CB  LEU A 180      50.534  38.126  43.612  1.00 23.93           C  
ATOM   1186  CG  LEU A 180      51.504  38.808  42.641  1.00 26.00           C  
ATOM   1187  CD1 LEU A 180      52.885  38.889  43.252  1.00 29.00           C  
ATOM   1188  CD2 LEU A 180      51.559  38.056  41.331  1.00 27.14           C  
ATOM   1189  N   VAL A 181      48.300  36.391  44.664  1.00 23.61           N  
ATOM   1190  CA  VAL A 181      47.506  35.736  45.696  1.00 23.10           C  
ATOM   1191  C   VAL A 181      48.487  35.189  46.724  1.00 22.69           C  
ATOM   1192  O   VAL A 181      49.457  34.501  46.369  1.00 22.22           O  
ATOM   1193  CB  VAL A 181      46.583  34.639  45.095  1.00 23.14           C  
ATOM   1194  CG1 VAL A 181      45.862  33.848  46.185  1.00 22.41           C  
ATOM   1195  CG2 VAL A 181      45.552  35.260  44.146  1.00 24.21           C  
ATOM   1196  N   ALA A 182      48.250  35.530  47.992  1.00 22.25           N  
ATOM   1197  CA  ALA A 182      49.176  35.148  49.067  1.00 21.95           C  
ATOM   1198  C   ALA A 182      48.836  33.770  49.624  1.00 21.79           C  
ATOM   1199  O   ALA A 182      47.676  33.484  49.917  1.00 21.35           O  
ATOM   1200  CB  ALA A 182      49.161  36.170  50.161  1.00 20.81           C  
ATOM   1201  N   THR A 183      49.861  32.933  49.771  1.00 22.05           N  
ATOM   1202  CA  THR A 183      49.697  31.583  50.307  1.00 21.50           C  
ATOM   1203  C   THR A 183      50.071  31.549  51.788  1.00 22.43           C  
ATOM   1204  O   THR A 183      50.515  32.567  52.333  1.00 22.19           O  
ATOM   1205  CB  THR A 183      50.546  30.567  49.527  1.00 21.63           C  
ATOM   1206  OG1 THR A 183      51.925  30.682  49.919  1.00 18.63           O  
ATOM   1207  CG2 THR A 183      50.352  30.761  47.973  1.00 19.99           C  
ATOM   1208  N   ASP A 184      49.892  30.385  52.428  1.00 23.03           N  
ATOM   1209  CA  ASP A 184      50.358  30.162  53.809  1.00 23.71           C  
ATOM   1210  C   ASP A 184      51.878  30.356  54.015  1.00 23.75           C  
ATOM   1211  O   ASP A 184      52.320  30.565  55.145  1.00 24.33           O  
ATOM   1212  CB  ASP A 184      49.947  28.769  54.308  1.00 23.81           C  
ATOM   1213  CG  ASP A 184      48.437  28.596  54.429  1.00 25.19           C  
ATOM   1214  OD1 ASP A 184      47.690  29.604  54.339  1.00 26.89           O  
ATOM   1215  OD2 ASP A 184      47.991  27.439  54.630  1.00 26.57           O  
ATOM   1216  N   LYS A 185      52.661  30.299  52.931  1.00 23.81           N  
ATOM   1217  CA  LYS A 185      54.128  30.460  52.977  1.00 23.64           C  
ATOM   1218  C   LYS A 185      54.545  31.916  53.135  1.00 23.48           C  
ATOM   1219  O   LYS A 185      55.718  32.221  53.430  1.00 23.92           O  
ATOM   1220  CB  LYS A 185      54.758  29.922  51.695  1.00 23.59           C  
ATOM   1221  CG  LYS A 185      56.238  29.570  51.791  1.00 26.14           C  
ATOM   1222  CD  LYS A 185      56.883  29.640  50.379  1.00 29.67           C  
ATOM   1223  CE  LYS A 185      58.010  28.668  50.140  1.00 30.68           C  
ATOM   1224  NZ  LYS A 185      59.149  28.830  51.064  1.00 33.04           N  
ATOM   1225  N   SER A 186      53.594  32.819  52.907  1.00 23.20           N  
ATOM   1226  CA  SER A 186      53.828  34.234  53.058  1.00 21.88           C  
ATOM   1227  C   SER A 186      53.517  34.689  54.477  1.00 22.02           C  
ATOM   1228  O   SER A 186      52.787  34.017  55.226  1.00 20.98           O  
ATOM   1229  CB  SER A 186      52.977  35.023  52.073  1.00 21.91           C  
ATOM   1230  OG  SER A 186      51.623  34.974  52.436  1.00 22.55           O  
ATOM   1231  N   TYR A 187      54.082  35.840  54.842  1.00 21.47           N  
ATOM   1232  CA  TYR A 187      53.861  36.426  56.163  1.00 21.21           C  
ATOM   1233  C   TYR A 187      52.378  36.686  56.461  1.00 20.64           C  
ATOM   1234  O   TYR A 187      51.884  36.265  57.501  1.00 20.40           O  
ATOM   1235  CB  TYR A 187      54.663  37.709  56.284  1.00 21.13           C  
ATOM   1236  CG  TYR A 187      54.331  38.532  57.510  1.00 23.09           C  
ATOM   1237  CD1 TYR A 187      54.398  37.973  58.789  1.00 22.42           C  
ATOM   1238  CD2 TYR A 187      53.991  39.883  57.389  1.00 23.09           C  
ATOM   1239  CE1 TYR A 187      54.142  38.731  59.903  1.00 21.64           C  
ATOM   1240  CE2 TYR A 187      53.732  40.663  58.516  1.00 23.56           C  
ATOM   1241  CZ  TYR A 187      53.820  40.064  59.764  1.00 22.71           C  
ATOM   1242  OH  TYR A 187      53.592  40.794  60.885  1.00 23.58           O  
ATOM   1243  N   ILE A 188      51.669  37.331  55.532  1.00 19.66           N  
ATOM   1244  CA  ILE A 188      50.231  37.557  55.695  1.00 20.15           C  
ATOM   1245  C   ILE A 188      49.436  36.245  55.825  1.00 20.31           C  
ATOM   1246  O   ILE A 188      48.519  36.159  56.647  1.00 21.03           O  
ATOM   1247  CB  ILE A 188      49.618  38.547  54.638  1.00 19.69           C  
ATOM   1248  CG1 ILE A 188      48.127  38.801  54.896  1.00 20.58           C  
ATOM   1249  CG2 ILE A 188      49.831  38.068  53.204  1.00 19.37           C  
ATOM   1250  CD1 ILE A 188      47.791  39.602  56.190  1.00 18.29           C  
ATOM   1251  N   GLY A 189      49.836  35.212  55.086  1.00 20.18           N  
ATOM   1252  CA  GLY A 189      49.280  33.882  55.271  1.00 19.76           C  
ATOM   1253  C   GLY A 189      49.474  33.359  56.682  1.00 20.30           C  
ATOM   1254  O   GLY A 189      48.557  32.778  57.265  1.00 20.62           O  
ATOM   1255  N   ASP A 190      50.662  33.556  57.247  1.00 20.76           N  
ATOM   1256  CA  ASP A 190      50.899  33.170  58.639  1.00 21.45           C  
ATOM   1257  C   ASP A 190      50.028  33.954  59.621  1.00 21.25           C  
ATOM   1258  O   ASP A 190      49.478  33.375  60.551  1.00 22.25           O  
ATOM   1259  CB  ASP A 190      52.376  33.326  59.021  1.00 21.24           C  
ATOM   1260  CG  ASP A 190      52.778  32.398  60.149  1.00 23.18           C  
ATOM   1261  OD1 ASP A 190      53.651  32.776  60.962  1.00 23.45           O  
ATOM   1262  OD2 ASP A 190      52.232  31.265  60.210  1.00 26.70           O  
ATOM   1263  N   LEU A 191      49.903  35.266  59.410  1.00 21.67           N  
ATOM   1264  CA  LEU A 191      49.075  36.109  60.267  1.00 21.79           C  
ATOM   1265  C   LEU A 191      47.624  35.648  60.241  1.00 21.64           C  
ATOM   1266  O   LEU A 191      46.966  35.572  61.285  1.00 21.80           O  
ATOM   1267  CB  LEU A 191      49.151  37.578  59.844  1.00 21.55           C  
ATOM   1268  CG  LEU A 191      50.436  38.383  60.008  1.00 22.63           C  
ATOM   1269  CD1 LEU A 191      50.312  39.732  59.306  1.00 22.63           C  
ATOM   1270  CD2 LEU A 191      50.758  38.576  61.493  1.00 21.62           C  
ATOM   1271  N   VAL A 192      47.118  35.378  59.041  1.00 21.18           N  
ATOM   1272  CA  VAL A 192      45.732  34.929  58.875  1.00 20.85           C  
ATOM   1273  C   VAL A 192      45.495  33.635  59.652  1.00 21.55           C  
ATOM   1274  O   VAL A 192      44.482  33.502  60.345  1.00 21.80           O  
ATOM   1275  CB  VAL A 192      45.385  34.731  57.392  1.00 21.00           C  
ATOM   1276  CG1 VAL A 192      44.188  33.753  57.223  1.00 20.42           C  
ATOM   1277  CG2 VAL A 192      45.151  36.076  56.717  1.00 20.01           C  
ATOM   1278  N   LYS A 193      46.451  32.706  59.556  1.00 21.64           N  
ATOM   1279  CA  LYS A 193      46.404  31.450  60.304  1.00 22.78           C  
ATOM   1280  C   LYS A 193      46.383  31.668  61.821  1.00 22.64           C  
ATOM   1281  O   LYS A 193      45.527  31.112  62.535  1.00 22.36           O  
ATOM   1282  CB  LYS A 193      47.553  30.515  59.874  1.00 22.55           C  
ATOM   1283  CG  LYS A 193      47.554  29.140  60.545  1.00 26.20           C  
ATOM   1284  CD  LYS A 193      48.142  28.040  59.620  1.00 27.91           C  
ATOM   1285  CE  LYS A 193      49.646  27.859  59.801  1.00 29.76           C  
ATOM   1286  NZ  LYS A 193      50.315  27.146  58.636  1.00 29.44           N  
ATOM   1287  N   ILE A 194      47.329  32.475  62.302  1.00 22.73           N  
ATOM   1288  CA  ILE A 194      47.451  32.809  63.734  1.00 22.33           C  
ATOM   1289  C   ILE A 194      46.162  33.425  64.279  1.00 22.36           C  
ATOM   1290  O   ILE A 194      45.676  33.025  65.337  1.00 21.61           O  
ATOM   1291  CB  ILE A 194      48.647  33.765  63.971  1.00 22.05           C  
ATOM   1292  CG1 ILE A 194      49.958  33.027  63.722  1.00 20.90           C  
ATOM   1293  CG2 ILE A 194      48.631  34.366  65.382  1.00 22.98           C  
ATOM   1294  CD1 ILE A 194      51.079  33.958  63.374  1.00 21.09           C  
ATOM   1295  N   ALA A 195      45.608  34.379  63.530  1.00 21.99           N  
ATOM   1296  CA  ALA A 195      44.396  35.104  63.945  1.00 22.28           C  
ATOM   1297  C   ALA A 195      43.106  34.298  63.797  1.00 22.24           C  
ATOM   1298  O   ALA A 195      42.038  34.804  64.129  1.00 22.61           O  
ATOM   1299  CB  ALA A 195      44.272  36.420  63.180  1.00 21.41           C  
ATOM   1300  N   GLY A 196      43.193  33.084  63.252  1.00 22.28           N  
ATOM   1301  CA  GLY A 196      42.050  32.173  63.218  1.00 22.37           C  
ATOM   1302  C   GLY A 196      41.297  32.074  61.902  1.00 23.19           C  
ATOM   1303  O   GLY A 196      40.205  31.505  61.857  1.00 22.84           O  
ATOM   1304  N   GLY A 197      41.865  32.620  60.830  1.00 23.07           N  
ATOM   1305  CA  GLY A 197      41.250  32.488  59.517  1.00 23.02           C  
ATOM   1306  C   GLY A 197      41.672  31.215  58.806  1.00 23.40           C  
ATOM   1307  O   GLY A 197      42.666  30.576  59.181  1.00 23.88           O  
ATOM   1308  N   GLU A 198      40.922  30.849  57.777  1.00 23.08           N  
ATOM   1309  CA  GLU A 198      41.245  29.688  56.953  1.00 24.09           C  
ATOM   1310  C   GLU A 198      41.459  30.122  55.507  1.00 23.23           C  
ATOM   1311  O   GLU A 198      40.508  30.501  54.809  1.00 22.82           O  
ATOM   1312  CB  GLU A 198      40.143  28.628  57.058  1.00 24.10           C  
ATOM   1313  CG  GLU A 198      40.525  27.281  56.441  1.00 30.40           C  
ATOM   1314  CD  GLU A 198      41.655  26.554  57.195  1.00 35.45           C  
ATOM   1315  OE1 GLU A 198      41.553  26.404  58.444  1.00 36.89           O  
ATOM   1316  OE2 GLU A 198      42.626  26.121  56.522  1.00 38.26           O  
ATOM   1317  N   ASN A 199      42.712  30.100  55.070  1.00 22.61           N  
ATOM   1318  CA  ASN A 199      43.056  30.514  53.709  1.00 23.54           C  
ATOM   1319  C   ASN A 199      42.381  29.572  52.696  1.00 23.68           C  
ATOM   1320  O   ASN A 199      42.536  28.355  52.775  1.00 24.39           O  
ATOM   1321  CB  ASN A 199      44.577  30.505  53.534  1.00 23.36           C  
ATOM   1322  CG  ASN A 199      45.056  31.245  52.278  1.00 24.21           C  
ATOM   1323  OD1 ASN A 199      44.293  31.548  51.349  1.00 23.56           O  
ATOM   1324  ND2 ASN A 199      46.350  31.526  52.251  1.00 22.78           N  
ATOM   1325  N   VAL A 200      41.614  30.149  51.779  1.00 23.55           N  
ATOM   1326  CA  VAL A 200      40.936  29.405  50.719  1.00 23.52           C  
ATOM   1327  C   VAL A 200      41.955  28.851  49.719  1.00 23.83           C  
ATOM   1328  O   VAL A 200      41.702  27.852  49.036  1.00 23.62           O  
ATOM   1329  CB  VAL A 200      39.874  30.287  49.967  1.00 23.57           C  
ATOM   1330  CG1 VAL A 200      38.738  30.736  50.905  1.00 21.76           C  
ATOM   1331  CG2 VAL A 200      40.524  31.498  49.285  1.00 22.90           C  
ATOM   1332  N   ILE A 201      43.112  29.508  49.643  1.00 24.34           N  
ATOM   1333  CA  ILE A 201      44.200  29.065  48.769  1.00 23.74           C  
ATOM   1334  C   ILE A 201      45.034  28.045  49.515  1.00 24.22           C  
ATOM   1335  O   ILE A 201      45.507  28.306  50.623  1.00 23.49           O  
ATOM   1336  CB  ILE A 201      45.065  30.264  48.300  1.00 23.72           C  
ATOM   1337  CG1 ILE A 201      44.197  31.237  47.501  1.00 21.36           C  
ATOM   1338  CG2 ILE A 201      46.308  29.780  47.491  1.00 22.82           C  
ATOM   1339  CD1 ILE A 201      43.471  30.595  46.291  1.00 19.82           C  
ATOM   1340  N   LYS A 202      45.218  26.880  48.902  1.00 25.41           N  
ATOM   1341  CA  LYS A 202      45.802  25.747  49.609  1.00 26.52           C  
ATOM   1342  C   LYS A 202      47.224  25.445  49.194  1.00 27.45           C  
ATOM   1343  O   LYS A 202      47.974  24.842  49.961  1.00 27.94           O  
ATOM   1344  CB  LYS A 202      44.915  24.508  49.444  1.00 26.95           C  
ATOM   1345  CG  LYS A 202      43.466  24.724  49.877  1.00 26.78           C  
ATOM   1346  CD  LYS A 202      43.295  24.755  51.392  1.00 26.61           C  
ATOM   1347  CE  LYS A 202      41.936  25.343  51.745  1.00 26.79           C  
ATOM   1348  NZ  LYS A 202      41.421  24.876  53.065  1.00 29.70           N  
ATOM   1349  N   VAL A 203      47.592  25.855  47.980  1.00 28.74           N  
ATOM   1350  CA  VAL A 203      48.956  25.661  47.473  1.00 30.00           C  
ATOM   1351  C   VAL A 203      49.908  26.462  48.349  1.00 29.75           C  
ATOM   1352  O   VAL A 203      49.535  27.505  48.858  1.00 30.10           O  
ATOM   1353  CB  VAL A 203      49.106  26.006  45.960  1.00 29.93           C  
ATOM   1354  CG1 VAL A 203      48.262  25.061  45.120  1.00 31.73           C  
ATOM   1355  CG2 VAL A 203      48.726  27.445  45.681  1.00 31.81           C  
ATOM   1356  N   LYS A 204      51.123  25.964  48.530  1.00 30.50           N  
ATOM   1357  CA  LYS A 204      51.961  26.395  49.649  1.00 31.72           C  
ATOM   1358  C   LYS A 204      53.449  26.516  49.297  1.00 31.21           C  
ATOM   1359  O   LYS A 204      54.263  26.770  50.175  1.00 32.10           O  
ATOM   1360  CB  LYS A 204      51.815  25.357  50.768  1.00 32.55           C  
ATOM   1361  CG  LYS A 204      51.661  25.922  52.161  1.00 34.31           C  
ATOM   1362  CD  LYS A 204      51.405  24.794  53.147  1.00 36.22           C  
ATOM   1363  CE  LYS A 204      50.131  24.016  52.816  1.00 39.35           C  
ATOM   1364  NZ  LYS A 204      48.926  24.901  52.663  1.00 41.06           N  
ATOM   1365  N   ASP A 205      53.789  26.335  48.026  1.00 29.97           N  
ATOM   1366  CA  ASP A 205      55.182  26.186  47.592  1.00 29.42           C  
ATOM   1367  C   ASP A 205      55.878  27.501  47.202  1.00 28.54           C  
ATOM   1368  O   ASP A 205      57.101  27.538  47.025  1.00 28.56           O  
ATOM   1369  CB  ASP A 205      55.268  25.172  46.442  1.00 29.54           C  
ATOM   1370  CG  ASP A 205      54.445  25.594  45.235  1.00 31.08           C  
ATOM   1371  OD1 ASP A 205      54.902  25.375  44.100  1.00 32.64           O  
ATOM   1372  OD2 ASP A 205      53.341  26.167  45.415  1.00 33.89           O  
ATOM   1373  N   ARG A 206      55.108  28.572  47.049  1.00 27.31           N  
ATOM   1374  CA  ARG A 206      55.687  29.912  47.035  1.00 26.28           C  
ATOM   1375  C   ARG A 206      54.803  30.875  47.798  1.00 25.10           C  
ATOM   1376  O   ARG A 206      53.621  30.591  48.010  1.00 23.93           O  
ATOM   1377  CB  ARG A 206      56.047  30.419  45.618  1.00 26.93           C  
ATOM   1378  CG  ARG A 206      55.001  30.326  44.550  1.00 27.08           C  
ATOM   1379  CD  ARG A 206      55.617  29.897  43.166  1.00 29.70           C  
ATOM   1380  NE  ARG A 206      56.530  30.896  42.601  1.00 28.35           N  
ATOM   1381  CZ  ARG A 206      57.767  30.651  42.168  1.00 28.13           C  
ATOM   1382  NH1 ARG A 206      58.279  29.428  42.203  1.00 29.57           N  
ATOM   1383  NH2 ARG A 206      58.504  31.639  41.692  1.00 28.45           N  
ATOM   1384  N   GLN A 207      55.397  31.988  48.230  1.00 23.64           N  
ATOM   1385  CA  GLN A 207      54.712  33.019  49.028  1.00 22.94           C  
ATOM   1386  C   GLN A 207      53.514  33.647  48.312  1.00 22.91           C  
ATOM   1387  O   GLN A 207      52.455  33.838  48.904  1.00 23.24           O  
ATOM   1388  CB  GLN A 207      55.710  34.107  49.482  1.00 22.83           C  
ATOM   1389  CG  GLN A 207      56.877  33.592  50.330  1.00 22.93           C  
ATOM   1390  CD  GLN A 207      58.090  33.175  49.499  1.00 26.43           C  
ATOM   1391  OE1 GLN A 207      57.977  32.829  48.316  1.00 26.65           O  
ATOM   1392  NE2 GLN A 207      59.267  33.224  50.117  1.00 27.07           N  
ATOM   1393  N   TYR A 208      53.692  33.971  47.037  1.00 22.66           N  
ATOM   1394  CA  TYR A 208      52.682  34.668  46.245  1.00 22.40           C  
ATOM   1395  C   TYR A 208      52.591  33.963  44.890  1.00 22.97           C  
ATOM   1396  O   TYR A 208      53.600  33.466  44.366  1.00 21.87           O  
ATOM   1397  CB  TYR A 208      53.040  36.159  46.104  1.00 22.63           C  
ATOM   1398  CG  TYR A 208      53.263  36.850  47.445  1.00 22.68           C  
ATOM   1399  CD1 TYR A 208      52.176  37.194  48.270  1.00 23.64           C  
ATOM   1400  CD2 TYR A 208      54.555  37.125  47.913  1.00 22.96           C  
ATOM   1401  CE1 TYR A 208      52.372  37.808  49.514  1.00 21.81           C  
ATOM   1402  CE2 TYR A 208      54.757  37.726  49.165  1.00 21.45           C  
ATOM   1403  CZ  TYR A 208      53.663  38.076  49.943  1.00 21.95           C  
ATOM   1404  OH  TYR A 208      53.855  38.674  51.172  1.00 21.75           O  
ATOM   1405  N   ILE A 209      51.378  33.857  44.351  1.00 22.73           N  
ATOM   1406  CA  ILE A 209      51.181  33.172  43.077  1.00 22.64           C  
ATOM   1407  C   ILE A 209      50.339  34.030  42.111  1.00 22.53           C  
ATOM   1408  O   ILE A 209      49.585  34.875  42.568  1.00 22.12           O  
ATOM   1409  CB  ILE A 209      50.516  31.777  43.284  1.00 22.74           C  
ATOM   1410  CG1 ILE A 209      49.130  31.918  43.929  1.00 22.96           C  
ATOM   1411  CG2 ILE A 209      51.431  30.864  44.119  1.00 23.01           C  
ATOM   1412  CD1 ILE A 209      48.307  30.654  43.956  1.00 23.28           C  
ATOM   1413  N   SER A 210      50.431  33.786  40.797  1.00 22.62           N  
ATOM   1414  CA  SER A 210      49.632  34.553  39.834  1.00 23.41           C  
ATOM   1415  C   SER A 210      48.165  34.578  40.235  1.00 23.53           C  
ATOM   1416  O   SER A 210      47.648  33.602  40.781  1.00 23.12           O  
ATOM   1417  CB  SER A 210      49.760  33.989  38.421  1.00 23.67           C  
ATOM   1418  OG  SER A 210      51.102  34.066  37.987  1.00 26.55           O  
ATOM   1419  N   SER A 211      47.499  35.694  39.958  1.00 24.03           N  
ATOM   1420  CA  SER A 211      46.060  35.797  40.175  1.00 24.80           C  
ATOM   1421  C   SER A 211      45.288  34.729  39.382  1.00 25.61           C  
ATOM   1422  O   SER A 211      44.137  34.432  39.706  1.00 25.86           O  
ATOM   1423  CB  SER A 211      45.557  37.205  39.841  1.00 24.62           C  
ATOM   1424  OG  SER A 211      45.683  37.485  38.459  1.00 24.64           O  
ATOM   1425  N   ASN A 212      45.939  34.140  38.372  1.00 26.54           N  
ATOM   1426  CA  ASN A 212      45.349  33.069  37.543  1.00 27.64           C  
ATOM   1427  C   ASN A 212      45.800  31.622  37.869  1.00 28.33           C  
ATOM   1428  O   ASN A 212      45.256  30.669  37.311  1.00 28.61           O  
ATOM   1429  CB  ASN A 212      45.585  33.368  36.045  1.00 27.65           C  
ATOM   1430  CG  ASN A 212      47.071  33.613  35.712  1.00 27.90           C  
ATOM   1431  OD1 ASN A 212      47.433  34.822  35.455  1.00 27.28           O  
ATOM   1432  ND2 ASN A 212      47.928  32.465  35.575  1.00 28.91           N  
ATOM   1433  N   THR A 213      46.779  31.464  38.772  1.00 29.40           N  
ATOM   1434  CA  THR A 213      47.368  30.145  39.094  1.00 30.01           C  
ATOM   1435  C   THR A 213      46.391  29.189  39.780  1.00 30.47           C  
ATOM   1436  O   THR A 213      46.053  28.142  39.212  1.00 30.62           O  
ATOM   1437  CB  THR A 213      48.679  30.305  39.925  1.00 29.70           C  
ATOM   1438  OG1 THR A 213      49.792  30.915  39.258  1.00 30.23           O  
ATOM   1439  CG2 THR A 213      49.109  28.842  40.432  1.00 29.70           C  
ATOM   1440  N   GLU A 214      45.968  29.526  41.000  1.00 30.92           N  
ATOM   1441  CA  GLU A 214      44.781  28.902  41.564  1.00 31.62           C  
ATOM   1442  C   GLU A 214      43.625  29.666  40.955  1.00 31.70           C  
ATOM   1443  O   GLU A 214      43.706  30.880  40.784  1.00 31.85           O  
ATOM   1444  CB  GLU A 214      44.745  28.970  43.099  1.00 31.87           C  
ATOM   1445  CG  GLU A 214      45.386  27.736  43.813  1.00 32.45           C  
ATOM   1446  CD  GLU A 214      44.304  26.726  44.445  1.00 33.40           C  
ATOM   1447  OE1 GLU A 214      44.566  26.234  45.572  1.00 33.63           O  
ATOM   1448  OE2 GLU A 214      43.169  26.669  43.691  1.00 35.40           O  
ATOM   1449  N   ASN A 215      42.562  28.972  40.574  1.00 31.95           N  
ATOM   1450  CA  ASN A 215      41.452  29.712  39.996  1.00 32.03           C  
ATOM   1451  C   ASN A 215      40.335  30.139  40.959  1.00 32.14           C  
ATOM   1452  O   ASN A 215      39.646  29.319  41.591  1.00 31.83           O  
ATOM   1453  CB  ASN A 215      41.001  29.120  38.664  1.00 32.03           C  
ATOM   1454  CG  ASN A 215      41.939  29.539  37.526  1.00 31.89           C  
ATOM   1455  OD1 ASN A 215      42.130  30.756  37.274  1.00 29.96           O  
ATOM   1456  ND2 ASN A 215      42.553  28.536  36.858  1.00 31.86           N  
ATOM   1457  N   LEU A 216      40.224  31.466  41.051  1.00 32.23           N  
ATOM   1458  CA  LEU A 216      39.377  32.205  41.984  1.00 32.20           C  
ATOM   1459  C   LEU A 216      37.874  31.933  41.858  1.00 32.24           C  
ATOM   1460  O   LEU A 216      37.067  32.593  42.512  1.00 32.46           O  
ATOM   1461  CB  LEU A 216      39.643  33.713  41.816  1.00 32.24           C  
ATOM   1462  CG  LEU A 216      40.780  34.452  42.539  1.00 32.10           C  
ATOM   1463  CD1 LEU A 216      41.980  33.569  42.876  1.00 32.36           C  
ATOM   1464  CD2 LEU A 216      41.213  35.657  41.719  1.00 32.04           C  
ATOM   1465  N   LEU A 217      37.495  30.967  41.029  1.00 32.19           N  
ATOM   1466  CA  LEU A 217      36.087  30.615  40.879  1.00 31.97           C  
ATOM   1467  C   LEU A 217      35.762  29.279  41.555  1.00 31.87           C  
ATOM   1468  O   LEU A 217      34.635  28.787  41.466  1.00 31.82           O  
ATOM   1469  CB  LEU A 217      35.682  30.626  39.397  1.00 32.03           C  
ATOM   1470  CG  LEU A 217      35.490  31.999  38.728  1.00 31.97           C  
ATOM   1471  CD1 LEU A 217      36.816  32.725  38.452  1.00 31.77           C  
ATOM   1472  CD2 LEU A 217      34.686  31.859  37.443  1.00 31.93           C  
ATOM   1473  N   ASN A 218      36.757  28.711  42.239  1.00 31.74           N  
ATOM   1474  CA  ASN A 218      36.594  27.472  43.001  1.00 31.85           C  
ATOM   1475  C   ASN A 218      36.566  27.671  44.525  1.00 31.72           C  
ATOM   1476  O   ASN A 218      36.385  26.719  45.285  1.00 31.98           O  
ATOM   1477  CB  ASN A 218      37.668  26.452  42.597  1.00 32.00           C  
ATOM   1478  CG  ASN A 218      37.230  25.567  41.427  1.00 32.60           C  
ATOM   1479  OD1 ASN A 218      37.166  26.011  40.274  1.00 32.11           O  
ATOM   1480  ND2 ASN A 218      36.925  24.305  41.727  1.00 33.79           N  
ATOM   1481  N   ILE A 219      36.704  28.923  44.949  1.00 31.41           N  
ATOM   1482  CA  ILE A 219      36.799  29.312  46.362  1.00 31.59           C  
ATOM   1483  C   ILE A 219      35.569  30.110  46.847  1.00 31.54           C  
ATOM   1484  O   ILE A 219      34.835  30.692  46.034  1.00 31.48           O  
ATOM   1485  CB  ILE A 219      38.098  30.122  46.616  1.00 31.67           C  
ATOM   1486  CG1 ILE A 219      38.251  31.218  45.556  1.00 31.86           C  
ATOM   1487  CG2 ILE A 219      39.314  29.186  46.571  1.00 31.34           C  
ATOM   1488  CD1 ILE A 219      38.687  32.565  46.067  1.00 32.90           C  
ATOM   1489  N   ASN A 220      35.345  30.129  48.165  1.00 31.27           N  
ATOM   1490  CA  ASN A 220      34.177  30.794  48.756  1.00 30.49           C  
ATOM   1491  C   ASN A 220      34.520  31.563  50.048  1.00 29.86           C  
ATOM   1492  O   ASN A 220      34.057  31.185  51.131  1.00 29.65           O  
ATOM   1493  CB  ASN A 220      33.060  29.754  48.990  1.00 30.74           C  
ATOM   1494  CG  ASN A 220      31.694  30.384  49.287  1.00 32.02           C  
ATOM   1495  OD1 ASN A 220      31.378  31.493  48.829  1.00 33.12           O  
ATOM   1496  ND2 ASN A 220      30.858  29.650  50.036  1.00 30.92           N  
ATOM   1497  N   PRO A 221      35.328  32.657  49.941  1.00 29.04           N  
ATOM   1498  CA  PRO A 221      35.770  33.345  51.164  1.00 28.40           C  
ATOM   1499  C   PRO A 221      34.669  34.166  51.836  1.00 27.50           C  
ATOM   1500  O   PRO A 221      33.832  34.751  51.162  1.00 27.42           O  
ATOM   1501  CB  PRO A 221      36.897  34.268  50.675  1.00 27.83           C  
ATOM   1502  CG  PRO A 221      36.635  34.504  49.264  1.00 28.30           C  
ATOM   1503  CD  PRO A 221      35.875  33.300  48.728  1.00 28.86           C  
ATOM   1504  N   ASP A 222      34.679  34.168  53.160  1.00 26.90           N  
ATOM   1505  CA  ASP A 222      33.869  35.084  53.959  1.00 26.75           C  
ATOM   1506  C   ASP A 222      34.473  36.488  53.921  1.00 26.17           C  
ATOM   1507  O   ASP A 222      33.748  37.480  53.951  1.00 26.73           O  
ATOM   1508  CB  ASP A 222      33.793  34.583  55.400  1.00 26.31           C  
ATOM   1509  CG  ASP A 222      33.165  33.210  55.502  1.00 26.96           C  
ATOM   1510  OD1 ASP A 222      31.929  33.114  55.381  1.00 29.03           O  
ATOM   1511  OD2 ASP A 222      33.901  32.224  55.714  1.00 26.11           O  
ATOM   1512  N   ILE A 223      35.800  36.548  53.833  1.00 25.85           N  
ATOM   1513  CA  ILE A 223      36.573  37.789  53.923  1.00 25.31           C  
ATOM   1514  C   ILE A 223      37.608  37.853  52.795  1.00 25.52           C  
ATOM   1515  O   ILE A 223      38.273  36.859  52.496  1.00 26.32           O  
ATOM   1516  CB  ILE A 223      37.296  37.895  55.301  1.00 25.23           C  
ATOM   1517  CG1 ILE A 223      36.283  37.949  56.464  1.00 25.08           C  
ATOM   1518  CG2 ILE A 223      38.235  39.110  55.346  1.00 24.71           C  
ATOM   1519  CD1 ILE A 223      36.929  37.980  57.867  1.00 24.55           C  
ATOM   1520  N   ILE A 224      37.728  39.013  52.162  1.00 25.30           N  
ATOM   1521  CA  ILE A 224      38.817  39.277  51.223  1.00 25.34           C  
ATOM   1522  C   ILE A 224      39.699  40.364  51.820  1.00 25.12           C  
ATOM   1523  O   ILE A 224      39.203  41.388  52.245  1.00 24.90           O  
ATOM   1524  CB  ILE A 224      38.303  39.709  49.825  1.00 25.42           C  
ATOM   1525  CG1 ILE A 224      37.510  38.567  49.174  1.00 25.76           C  
ATOM   1526  CG2 ILE A 224      39.473  40.101  48.906  1.00 26.13           C  
ATOM   1527  CD1 ILE A 224      36.778  38.962  47.924  1.00 26.91           C  
ATOM   1528  N   LEU A 225      41.004  40.102  51.884  1.00 25.09           N  
ATOM   1529  CA  LEU A 225      41.987  41.081  52.356  1.00 24.66           C  
ATOM   1530  C   LEU A 225      42.787  41.575  51.160  1.00 24.65           C  
ATOM   1531  O   LEU A 225      43.190  40.763  50.314  1.00 24.53           O  
ATOM   1532  CB  LEU A 225      42.938  40.458  53.401  1.00 24.35           C  
ATOM   1533  CG  LEU A 225      42.324  39.892  54.690  1.00 22.43           C  
ATOM   1534  CD1 LEU A 225      43.375  39.187  55.509  1.00 20.08           C  
ATOM   1535  CD2 LEU A 225      41.599  40.945  55.552  1.00 22.06           C  
ATOM   1536  N   ARG A 226      42.994  42.892  51.081  1.00 23.94           N  
ATOM   1537  CA  ARG A 226      43.802  43.497  50.007  1.00 24.08           C  
ATOM   1538  C   ARG A 226      44.974  44.285  50.590  1.00 23.65           C  
ATOM   1539  O   ARG A 226      44.778  45.280  51.282  1.00 23.76           O  
ATOM   1540  CB  ARG A 226      42.937  44.379  49.081  1.00 23.80           C  
ATOM   1541  CG  ARG A 226      41.716  43.660  48.511  1.00 24.02           C  
ATOM   1542  CD  ARG A 226      41.025  44.425  47.377  1.00 23.41           C  
ATOM   1543  NE  ARG A 226      40.474  45.705  47.817  1.00 21.15           N  
ATOM   1544  CZ  ARG A 226      39.500  46.360  47.194  1.00 22.78           C  
ATOM   1545  NH1 ARG A 226      38.967  45.841  46.095  1.00 22.03           N  
ATOM   1546  NH2 ARG A 226      39.057  47.538  47.661  1.00 19.61           N  
ATOM   1547  N   LEU A 227      46.190  43.794  50.350  1.00 23.61           N  
ATOM   1548  CA  LEU A 227      47.404  44.442  50.833  1.00 23.15           C  
ATOM   1549  C   LEU A 227      48.112  45.082  49.654  1.00 23.98           C  
ATOM   1550  O   LEU A 227      48.181  44.472  48.582  1.00 24.83           O  
ATOM   1551  CB  LEU A 227      48.377  43.444  51.482  1.00 22.98           C  
ATOM   1552  CG  LEU A 227      48.043  42.825  52.843  1.00 21.67           C  
ATOM   1553  CD1 LEU A 227      46.834  41.875  52.719  1.00 18.54           C  
ATOM   1554  CD2 LEU A 227      49.269  42.080  53.367  1.00 21.40           C  
ATOM   1555  N   PRO A 228      48.625  46.315  49.848  1.00 24.46           N  
ATOM   1556  CA  PRO A 228      49.360  47.067  48.833  1.00 24.69           C  
ATOM   1557  C   PRO A 228      50.873  46.947  48.974  1.00 24.73           C  
ATOM   1558  O   PRO A 228      51.379  46.770  50.084  1.00 25.67           O  
ATOM   1559  CB  PRO A 228      48.930  48.500  49.122  1.00 24.25           C  
ATOM   1560  CG  PRO A 228      48.755  48.521  50.623  1.00 23.93           C  
ATOM   1561  CD  PRO A 228      48.462  47.118  51.083  1.00 23.89           C  
ATOM   1562  N   HIS A 229      51.579  47.039  47.850  1.00 24.59           N  
ATOM   1563  CA  HIS A 229      53.036  46.951  47.837  1.00 24.00           C  
ATOM   1564  C   HIS A 229      53.662  47.846  46.791  1.00 24.12           C  
ATOM   1565  O   HIS A 229      53.160  47.934  45.681  1.00 24.05           O  
ATOM   1566  CB  HIS A 229      53.506  45.516  47.606  1.00 23.76           C  
ATOM   1567  CG  HIS A 229      54.998  45.386  47.565  1.00 21.89           C  
ATOM   1568  ND1 HIS A 229      55.776  45.419  48.701  1.00 18.61           N  
ATOM   1569  CD2 HIS A 229      55.852  45.271  46.525  1.00 20.92           C  
ATOM   1570  CE1 HIS A 229      57.046  45.310  48.364  1.00 20.72           C  
ATOM   1571  NE2 HIS A 229      57.123  45.226  47.047  1.00 21.23           N  
ATOM   1572  N   GLY A 230      54.759  48.503  47.166  1.00 24.27           N  
ATOM   1573  CA  GLY A 230      55.636  49.198  46.230  1.00 25.31           C  
ATOM   1574  C   GLY A 230      55.225  50.629  45.945  1.00 26.48           C  
ATOM   1575  O   GLY A 230      55.997  51.574  46.174  1.00 26.07           O  
ATOM   1576  N   MET A 231      54.018  50.768  45.404  1.00 27.53           N  
ATOM   1577  CA  MET A 231      53.393  52.057  45.109  1.00 29.07           C  
ATOM   1578  C   MET A 231      51.953  51.953  45.620  1.00 29.62           C  
ATOM   1579  O   MET A 231      51.047  51.647  44.851  1.00 28.65           O  
ATOM   1580  CB  MET A 231      53.399  52.346  43.596  1.00 29.30           C  
ATOM   1581  CG  MET A 231      54.775  52.494  42.951  1.00 31.83           C  
ATOM   1582  SD  MET A 231      55.428  54.178  43.037  1.00 42.01           S  
ATOM   1583  CE  MET A 231      54.830  54.882  41.491  1.00 40.22           C  
ATOM   1584  N   PRO A 232      51.741  52.183  46.930  1.00 30.68           N  
ATOM   1585  CA  PRO A 232      50.432  51.902  47.553  1.00 31.94           C  
ATOM   1586  C   PRO A 232      49.265  52.680  46.942  1.00 32.55           C  
ATOM   1587  O   PRO A 232      48.147  52.163  46.882  1.00 32.86           O  
ATOM   1588  CB  PRO A 232      50.628  52.299  49.026  1.00 32.05           C  
ATOM   1589  CG  PRO A 232      52.109  52.347  49.224  1.00 32.64           C  
ATOM   1590  CD  PRO A 232      52.710  52.725  47.896  1.00 31.18           C  
ATOM   1591  N   GLU A 233      49.544  53.894  46.483  1.00 33.56           N  
ATOM   1592  CA  GLU A 233      48.565  54.764  45.846  1.00 34.81           C  
ATOM   1593  C   GLU A 233      48.106  54.173  44.505  1.00 34.96           C  
ATOM   1594  O   GLU A 233      46.905  54.038  44.258  1.00 35.04           O  
ATOM   1595  CB  GLU A 233      49.151  56.183  45.637  1.00 35.15           C  
ATOM   1596  CG  GLU A 233      50.342  56.562  46.571  1.00 37.44           C  
ATOM   1597  CD  GLU A 233      51.693  55.869  46.213  1.00 39.62           C  
ATOM   1598  OE1 GLU A 233      51.820  55.249  45.117  1.00 38.06           O  
ATOM   1599  OE2 GLU A 233      52.632  55.958  47.045  1.00 40.73           O  
ATOM   1600  N   GLU A 234      49.062  53.834  43.642  1.00 34.93           N  
ATOM   1601  CA  GLU A 234      48.755  53.164  42.391  1.00 35.61           C  
ATOM   1602  C   GLU A 234      47.992  51.859  42.644  1.00 35.00           C  
ATOM   1603  O   GLU A 234      47.037  51.547  41.937  1.00 34.99           O  
ATOM   1604  CB  GLU A 234      50.038  52.896  41.596  1.00 35.80           C  
ATOM   1605  CG  GLU A 234      49.831  52.059  40.313  1.00 36.89           C  
ATOM   1606  CD  GLU A 234      51.117  51.809  39.514  1.00 37.71           C  
ATOM   1607  OE1 GLU A 234      51.118  50.871  38.669  1.00 41.58           O  
ATOM   1608  OE2 GLU A 234      52.113  52.556  39.707  1.00 40.21           O  
ATOM   1609  N   VAL A 235      48.408  51.118  43.670  1.00 34.60           N  
ATOM   1610  CA  VAL A 235      47.851  49.795  43.965  1.00 34.32           C  
ATOM   1611  C   VAL A 235      46.367  49.824  44.386  1.00 34.71           C  
ATOM   1612  O   VAL A 235      45.553  49.047  43.874  1.00 34.20           O  
ATOM   1613  CB  VAL A 235      48.728  49.037  44.992  1.00 34.05           C  
ATOM   1614  CG1 VAL A 235      48.011  47.791  45.497  1.00 33.74           C  
ATOM   1615  CG2 VAL A 235      50.077  48.687  44.367  1.00 32.49           C  
ATOM   1616  N   LYS A 236      46.020  50.731  45.298  1.00 35.35           N  
ATOM   1617  CA  LYS A 236      44.640  50.846  45.768  1.00 35.76           C  
ATOM   1618  C   LYS A 236      43.680  51.232  44.658  1.00 35.70           C  
ATOM   1619  O   LYS A 236      42.595  50.657  44.569  1.00 35.87           O  
ATOM   1620  CB  LYS A 236      44.501  51.810  46.960  1.00 36.51           C  
ATOM   1621  CG  LYS A 236      44.298  51.092  48.324  1.00 37.54           C  
ATOM   1622  CD  LYS A 236      43.127  51.673  49.163  1.00 37.09           C  
ATOM   1623  CE  LYS A 236      43.446  53.059  49.715  1.00 39.03           C  
ATOM   1624  NZ  LYS A 236      42.441  53.562  50.714  1.00 38.93           N  
ATOM   1625  N   LYS A 237      44.067  52.185  43.811  1.00 35.25           N  
ATOM   1626  CA  LYS A 237      43.226  52.541  42.669  1.00 35.39           C  
ATOM   1627  C   LYS A 237      43.130  51.385  41.651  1.00 34.79           C  
ATOM   1628  O   LYS A 237      42.085  51.165  41.028  1.00 34.40           O  
ATOM   1629  CB  LYS A 237      43.641  53.888  42.039  1.00 35.50           C  
ATOM   1630  CG  LYS A 237      44.892  53.887  41.149  1.00 36.38           C  
ATOM   1631  CD  LYS A 237      44.800  54.964  40.021  1.00 37.00           C  
ATOM   1632  CE  LYS A 237      44.977  56.413  40.514  1.00 38.32           C  
ATOM   1633  NZ  LYS A 237      46.294  56.631  41.198  1.00 40.12           N  
ATOM   1634  N   MET A 238      44.215  50.627  41.524  1.00 34.19           N  
ATOM   1635  CA  MET A 238      44.224  49.423  40.716  1.00 34.18           C  
ATOM   1636  C   MET A 238      43.200  48.394  41.247  1.00 32.77           C  
ATOM   1637  O   MET A 238      42.413  47.846  40.481  1.00 31.97           O  
ATOM   1638  CB  MET A 238      45.634  48.835  40.689  1.00 34.07           C  
ATOM   1639  CG  MET A 238      45.898  47.879  39.554  1.00 35.17           C  
ATOM   1640  SD  MET A 238      46.693  46.395  40.161  1.00 37.99           S  
ATOM   1641  CE  MET A 238      45.246  45.541  40.806  1.00 36.54           C  
ATOM   1642  N   PHE A 239      43.203  48.159  42.560  1.00 32.13           N  
ATOM   1643  CA  PHE A 239      42.228  47.270  43.205  1.00 31.34           C  
ATOM   1644  C   PHE A 239      40.776  47.754  43.019  1.00 31.24           C  
ATOM   1645  O   PHE A 239      39.855  46.949  42.846  1.00 31.00           O  
ATOM   1646  CB  PHE A 239      42.540  47.109  44.699  1.00 30.58           C  
ATOM   1647  CG  PHE A 239      43.491  45.979  45.026  1.00 30.34           C  
ATOM   1648  CD1 PHE A 239      44.534  46.176  45.934  1.00 29.71           C  
ATOM   1649  CD2 PHE A 239      43.343  44.709  44.446  1.00 30.38           C  
ATOM   1650  CE1 PHE A 239      45.412  45.139  46.263  1.00 28.79           C  
ATOM   1651  CE2 PHE A 239      44.215  43.674  44.776  1.00 28.80           C  
ATOM   1652  CZ  PHE A 239      45.249  43.892  45.686  1.00 29.37           C  
ATOM   1653  N   GLN A 240      40.591  49.070  43.060  1.00 31.07           N  
ATOM   1654  CA  GLN A 240      39.282  49.700  42.895  1.00 31.37           C  
ATOM   1655  C   GLN A 240      38.712  49.466  41.492  1.00 30.54           C  
ATOM   1656  O   GLN A 240      37.527  49.177  41.333  1.00 30.25           O  
ATOM   1657  CB  GLN A 240      39.409  51.201  43.150  1.00 31.79           C  
ATOM   1658  CG  GLN A 240      38.472  51.745  44.206  1.00 35.24           C  
ATOM   1659  CD  GLN A 240      39.089  51.739  45.594  1.00 38.74           C  
ATOM   1660  OE1 GLN A 240      39.591  52.769  46.069  1.00 40.52           O  
ATOM   1661  NE2 GLN A 240      39.057  50.583  46.254  1.00 38.39           N  
ATOM   1662  N   LYS A 241      39.577  49.599  40.488  1.00 30.05           N  
ATOM   1663  CA  LYS A 241      39.225  49.404  39.081  1.00 29.58           C  
ATOM   1664  C   LYS A 241      38.970  47.931  38.775  1.00 29.04           C  
ATOM   1665  O   LYS A 241      38.021  47.603  38.073  1.00 28.86           O  
ATOM   1666  CB  LYS A 241      40.338  49.957  38.183  1.00 29.72           C  
ATOM   1667  CG  LYS A 241      40.059  49.951  36.700  1.00 30.60           C  
ATOM   1668  CD  LYS A 241      41.128  50.733  35.947  1.00 32.58           C  
ATOM   1669  CE  LYS A 241      40.758  50.884  34.482  1.00 33.55           C  
ATOM   1670  NZ  LYS A 241      41.744  51.707  33.707  1.00 35.53           N  
ATOM   1671  N   GLU A 242      39.818  47.058  39.321  1.00 28.32           N  
ATOM   1672  CA  GLU A 242      39.686  45.611  39.167  1.00 27.55           C  
ATOM   1673  C   GLU A 242      38.342  45.089  39.666  1.00 26.96           C  
ATOM   1674  O   GLU A 242      37.710  44.279  38.995  1.00 26.63           O  
ATOM   1675  CB  GLU A 242      40.823  44.888  39.900  1.00 27.45           C  
ATOM   1676  CG  GLU A 242      40.566  43.392  40.175  1.00 27.51           C  
ATOM   1677  CD  GLU A 242      40.689  42.513  38.918  1.00 29.23           C  
ATOM   1678  OE1 GLU A 242      41.107  43.024  37.852  1.00 27.88           O  
ATOM   1679  OE2 GLU A 242      40.380  41.300  39.004  1.00 29.56           O  
ATOM   1680  N   PHE A 243      37.928  45.546  40.845  1.00 26.28           N  
ATOM   1681  CA  PHE A 243      36.731  45.024  41.502  1.00 26.30           C  
ATOM   1682  C   PHE A 243      35.450  45.571  40.848  1.00 26.67           C  
ATOM   1683  O   PHE A 243      34.379  44.970  40.952  1.00 26.52           O  
ATOM   1684  CB  PHE A 243      36.780  45.287  43.017  1.00 25.81           C  
ATOM   1685  CG  PHE A 243      37.412  44.157  43.822  1.00 25.70           C  
ATOM   1686  CD1 PHE A 243      38.733  43.759  43.592  1.00 23.93           C  
ATOM   1687  CD2 PHE A 243      36.675  43.493  44.807  1.00 25.09           C  
ATOM   1688  CE1 PHE A 243      39.312  42.718  44.327  1.00 26.40           C  
ATOM   1689  CE2 PHE A 243      37.241  42.430  45.546  1.00 25.57           C  
ATOM   1690  CZ  PHE A 243      38.563  42.047  45.312  1.00 24.89           C  
ATOM   1691  N   LYS A 244      35.585  46.698  40.154  1.00 27.55           N  
ATOM   1692  CA  LYS A 244      34.503  47.274  39.367  1.00 28.43           C  
ATOM   1693  C   LYS A 244      34.414  46.633  37.989  1.00 28.92           C  
ATOM   1694  O   LYS A 244      33.316  46.365  37.487  1.00 28.95           O  
ATOM   1695  CB  LYS A 244      34.702  48.785  39.201  1.00 28.73           C  
ATOM   1696  CG  LYS A 244      34.295  49.616  40.405  1.00 29.95           C  
ATOM   1697  CD  LYS A 244      33.818  50.987  39.962  1.00 32.24           C  
ATOM   1698  CE  LYS A 244      32.991  51.661  41.055  1.00 34.13           C  
ATOM   1699  NZ  LYS A 244      32.089  52.739  40.509  1.00 34.92           N  
ATOM   1700  N   GLN A 245      35.577  46.390  37.385  1.00 29.41           N  
ATOM   1701  CA  GLN A 245      35.665  46.008  35.979  1.00 30.15           C  
ATOM   1702  C   GLN A 245      35.617  44.513  35.706  1.00 30.13           C  
ATOM   1703  O   GLN A 245      34.971  44.083  34.759  1.00 30.09           O  
ATOM   1704  CB  GLN A 245      36.917  46.605  35.349  1.00 30.40           C  
ATOM   1705  CG  GLN A 245      36.797  48.086  35.054  1.00 32.34           C  
ATOM   1706  CD  GLN A 245      37.870  48.580  34.110  1.00 34.79           C  
ATOM   1707  OE1 GLN A 245      38.917  47.941  33.945  1.00 35.81           O  
ATOM   1708  NE2 GLN A 245      37.620  49.725  33.479  1.00 34.69           N  
ATOM   1709  N   ASN A 246      36.327  43.725  36.502  1.00 30.15           N  
ATOM   1710  CA  ASN A 246      36.296  42.275  36.338  1.00 30.41           C  
ATOM   1711  C   ASN A 246      34.997  41.715  36.926  1.00 30.77           C  
ATOM   1712  O   ASN A 246      34.696  41.920  38.102  1.00 31.08           O  
ATOM   1713  CB  ASN A 246      37.534  41.648  36.983  1.00 30.39           C  
ATOM   1714  CG  ASN A 246      37.707  40.173  36.649  1.00 29.50           C  
ATOM   1715  OD1 ASN A 246      36.812  39.519  36.119  1.00 29.88           O  
ATOM   1716  ND2 ASN A 246      38.870  39.641  36.984  1.00 28.68           N  
ATOM   1717  N   ASP A 247      34.231  41.007  36.103  1.00 31.04           N  
ATOM   1718  CA  ASP A 247      32.875  40.601  36.474  1.00 31.53           C  
ATOM   1719  C   ASP A 247      32.748  39.586  37.610  1.00 31.31           C  
ATOM   1720  O   ASP A 247      31.694  39.489  38.237  1.00 31.24           O  
ATOM   1721  CB  ASP A 247      32.097  40.136  35.242  1.00 31.84           C  
ATOM   1722  CG  ASP A 247      31.513  41.301  34.461  1.00 34.09           C  
ATOM   1723  OD1 ASP A 247      31.249  42.366  35.080  1.00 35.96           O  
ATOM   1724  OD2 ASP A 247      31.315  41.157  33.230  1.00 36.02           O  
ATOM   1725  N   ILE A 248      33.819  38.850  37.882  1.00 31.25           N  
ATOM   1726  CA  ILE A 248      33.798  37.821  38.922  1.00 31.35           C  
ATOM   1727  C   ILE A 248      33.537  38.326  40.354  1.00 31.26           C  
ATOM   1728  O   ILE A 248      32.870  37.645  41.137  1.00 31.75           O  
ATOM   1729  CB  ILE A 248      35.077  36.954  38.890  1.00 31.57           C  
ATOM   1730  CG1 ILE A 248      36.332  37.842  38.963  1.00 31.29           C  
ATOM   1731  CG2 ILE A 248      35.066  36.073  37.632  1.00 31.58           C  
ATOM   1732  CD1 ILE A 248      37.515  37.205  39.651  1.00 32.06           C  
ATOM   1733  N   TRP A 249      34.033  39.521  40.673  1.00 30.57           N  
ATOM   1734  CA  TRP A 249      34.021  40.035  42.045  1.00 30.16           C  
ATOM   1735  C   TRP A 249      32.630  40.321  42.622  1.00 31.15           C  
ATOM   1736  O   TRP A 249      32.371  40.023  43.793  1.00 31.10           O  
ATOM   1737  CB  TRP A 249      34.912  41.275  42.158  1.00 29.15           C  
ATOM   1738  CG  TRP A 249      36.330  40.984  41.803  1.00 27.77           C  
ATOM   1739  CD1 TRP A 249      37.017  41.453  40.724  1.00 27.02           C  
ATOM   1740  CD2 TRP A 249      37.233  40.131  42.518  1.00 26.78           C  
ATOM   1741  NE1 TRP A 249      38.299  40.959  40.728  1.00 26.19           N  
ATOM   1742  CE2 TRP A 249      38.457  40.135  41.811  1.00 26.70           C  
ATOM   1743  CE3 TRP A 249      37.129  39.364  43.690  1.00 26.18           C  
ATOM   1744  CZ2 TRP A 249      39.579  39.404  42.240  1.00 26.94           C  
ATOM   1745  CZ3 TRP A 249      38.245  38.644  44.120  1.00 27.34           C  
ATOM   1746  CH2 TRP A 249      39.454  38.671  43.391  1.00 27.44           C  
ATOM   1747  N   LYS A 250      31.735  40.870  41.801  1.00 31.79           N  
ATOM   1748  CA  LYS A 250      30.378  41.199  42.249  1.00 32.89           C  
ATOM   1749  C   LYS A 250      29.605  39.954  42.715  1.00 32.93           C  
ATOM   1750  O   LYS A 250      28.643  40.064  43.482  1.00 33.35           O  
ATOM   1751  CB  LYS A 250      29.602  41.937  41.145  1.00 32.95           C  
ATOM   1752  CG  LYS A 250      29.263  41.090  39.926  1.00 33.24           C  
ATOM   1753  CD  LYS A 250      28.362  41.848  38.956  1.00 34.11           C  
ATOM   1754  CE  LYS A 250      29.082  42.183  37.653  1.00 36.97           C  
ATOM   1755  NZ  LYS A 250      29.044  41.039  36.677  1.00 38.16           N  
ATOM   1756  N   HIS A 251      30.050  38.787  42.250  1.00 32.68           N  
ATOM   1757  CA  HIS A 251      29.449  37.498  42.572  1.00 32.30           C  
ATOM   1758  C   HIS A 251      29.973  36.848  43.870  1.00 31.80           C  
ATOM   1759  O   HIS A 251      29.347  35.916  44.390  1.00 31.88           O  
ATOM   1760  CB  HIS A 251      29.630  36.544  41.393  1.00 32.54           C  
ATOM   1761  CG  HIS A 251      28.997  37.032  40.125  1.00 34.21           C  
ATOM   1762  ND1 HIS A 251      29.728  37.352  39.000  1.00 34.54           N  
ATOM   1763  CD2 HIS A 251      27.699  37.260  39.808  1.00 35.01           C  
ATOM   1764  CE1 HIS A 251      28.908  37.751  38.043  1.00 34.89           C  
ATOM   1765  NE2 HIS A 251      27.671  37.705  38.508  1.00 35.63           N  
ATOM   1766  N   PHE A 252      31.111  37.335  44.370  1.00 30.60           N  
ATOM   1767  CA  PHE A 252      31.679  36.913  45.650  1.00 29.74           C  
ATOM   1768  C   PHE A 252      30.790  37.379  46.804  1.00 29.13           C  
ATOM   1769  O   PHE A 252      30.358  38.534  46.840  1.00 28.63           O  
ATOM   1770  CB  PHE A 252      33.089  37.495  45.831  1.00 29.71           C  
ATOM   1771  CG  PHE A 252      34.177  36.716  45.128  1.00 30.71           C  
ATOM   1772  CD1 PHE A 252      35.133  36.007  45.863  1.00 31.71           C  
ATOM   1773  CD2 PHE A 252      34.251  36.684  43.741  1.00 30.24           C  
ATOM   1774  CE1 PHE A 252      36.145  35.282  45.224  1.00 31.17           C  
ATOM   1775  CE2 PHE A 252      35.260  35.957  43.089  1.00 31.43           C  
ATOM   1776  CZ  PHE A 252      36.211  35.259  43.833  1.00 30.27           C  
ATOM   1777  N   LYS A 253      30.509  36.474  47.738  1.00 28.32           N  
ATOM   1778  CA  LYS A 253      29.712  36.822  48.903  1.00 27.56           C  
ATOM   1779  C   LYS A 253      30.438  37.816  49.814  1.00 27.59           C  
ATOM   1780  O   LYS A 253      29.799  38.667  50.435  1.00 26.95           O  
ATOM   1781  CB  LYS A 253      29.232  35.577  49.663  1.00 27.60           C  
ATOM   1782  CG  LYS A 253      30.263  34.868  50.510  1.00 26.87           C  
ATOM   1783  CD  LYS A 253      29.571  33.975  51.530  1.00 26.92           C  
ATOM   1784  CE  LYS A 253      30.556  33.003  52.149  1.00 27.80           C  
ATOM   1785  NZ  LYS A 253      29.829  31.850  52.747  1.00 29.79           N  
ATOM   1786  N   ALA A 254      31.769  37.740  49.854  1.00 27.72           N  
ATOM   1787  CA  ALA A 254      32.572  38.714  50.606  1.00 28.22           C  
ATOM   1788  C   ALA A 254      32.357  40.151  50.115  1.00 28.41           C  
ATOM   1789  O   ALA A 254      32.410  41.097  50.910  1.00 28.22           O  
ATOM   1790  CB  ALA A 254      34.045  38.349  50.557  1.00 27.81           C  
ATOM   1791  N   VAL A 255      32.118  40.300  48.812  1.00 28.74           N  
ATOM   1792  CA  VAL A 255      31.876  41.602  48.189  1.00 29.58           C  
ATOM   1793  C   VAL A 255      30.465  42.083  48.497  1.00 30.29           C  
ATOM   1794  O   VAL A 255      30.279  43.221  48.930  1.00 30.26           O  
ATOM   1795  CB  VAL A 255      32.096  41.552  46.647  1.00 29.83           C  
ATOM   1796  CG1 VAL A 255      31.407  42.742  45.933  1.00 29.08           C  
ATOM   1797  CG2 VAL A 255      33.590  41.488  46.319  1.00 28.93           C  
ATOM   1798  N   LYS A 256      29.484  41.206  48.269  1.00 31.15           N  
ATOM   1799  CA  LYS A 256      28.073  41.485  48.548  1.00 32.01           C  
ATOM   1800  C   LYS A 256      27.828  41.827  50.016  1.00 31.93           C  
ATOM   1801  O   LYS A 256      26.894  42.559  50.338  1.00 32.26           O  
ATOM   1802  CB  LYS A 256      27.212  40.281  48.151  1.00 32.27           C  
ATOM   1803  CG  LYS A 256      26.686  40.312  46.713  1.00 34.20           C  
ATOM   1804  CD  LYS A 256      26.852  38.968  45.971  1.00 36.36           C  
ATOM   1805  CE  LYS A 256      26.387  37.755  46.776  1.00 37.44           C  
ATOM   1806  NZ  LYS A 256      26.762  36.470  46.111  1.00 37.21           N  
ATOM   1807  N   ASN A 257      28.664  41.293  50.902  1.00 31.76           N  
ATOM   1808  CA  ASN A 257      28.471  41.462  52.339  1.00 31.85           C  
ATOM   1809  C   ASN A 257      29.398  42.494  52.955  1.00 31.79           C  
ATOM   1810  O   ASN A 257      29.482  42.584  54.187  1.00 31.61           O  
ATOM   1811  CB  ASN A 257      28.648  40.127  53.072  1.00 32.03           C  
ATOM   1812  CG  ASN A 257      27.660  39.072  52.622  1.00 32.11           C  
ATOM   1813  OD1 ASN A 257      26.529  39.377  52.248  1.00 32.86           O  
ATOM   1814  ND2 ASN A 257      28.087  37.815  52.657  1.00 32.30           N  
ATOM   1815  N   ASN A 258      30.084  43.261  52.100  1.00 31.60           N  
ATOM   1816  CA  ASN A 258      31.055  44.284  52.521  1.00 31.82           C  
ATOM   1817  C   ASN A 258      32.120  43.784  53.508  1.00 31.57           C  
ATOM   1818  O   ASN A 258      32.389  44.420  54.537  1.00 31.68           O  
ATOM   1819  CB  ASN A 258      30.339  45.535  53.060  1.00 32.19           C  
ATOM   1820  CG  ASN A 258      29.251  46.045  52.112  1.00 34.16           C  
ATOM   1821  OD1 ASN A 258      28.075  46.164  52.494  1.00 35.46           O  
ATOM   1822  ND2 ASN A 258      29.637  46.350  50.870  1.00 35.35           N  
ATOM   1823  N   HIS A 259      32.719  42.635  53.185  1.00 31.24           N  
ATOM   1824  CA  HIS A 259      33.835  42.091  53.961  1.00 30.62           C  
ATOM   1825  C   HIS A 259      35.096  42.017  53.105  1.00 29.80           C  
ATOM   1826  O   HIS A 259      35.839  41.050  53.151  1.00 28.96           O  
ATOM   1827  CB  HIS A 259      33.481  40.742  54.603  1.00 30.65           C  
ATOM   1828  CG  HIS A 259      32.355  40.823  55.593  1.00 32.57           C  
ATOM   1829  ND1 HIS A 259      31.435  39.811  55.762  1.00 33.89           N  
ATOM   1830  CD2 HIS A 259      31.980  41.814  56.440  1.00 32.46           C  
ATOM   1831  CE1 HIS A 259      30.558  40.163  56.686  1.00 34.32           C  
ATOM   1832  NE2 HIS A 259      30.866  41.375  57.112  1.00 33.38           N  
ATOM   1833  N   VAL A 260      35.306  43.076  52.327  1.00 29.42           N  
ATOM   1834  CA  VAL A 260      36.528  43.296  51.559  1.00 28.97           C  
ATOM   1835  C   VAL A 260      37.313  44.396  52.282  1.00 28.66           C  
ATOM   1836  O   VAL A 260      36.833  45.525  52.390  1.00 28.46           O  
ATOM   1837  CB  VAL A 260      36.190  43.762  50.118  1.00 29.20           C  
ATOM   1838  CG1 VAL A 260      37.463  44.166  49.355  1.00 29.37           C  
ATOM   1839  CG2 VAL A 260      35.378  42.686  49.354  1.00 28.03           C  
ATOM   1840  N   TYR A 261      38.512  44.077  52.767  1.00 28.54           N  
ATOM   1841  CA  TYR A 261      39.283  45.034  53.577  1.00 28.56           C  
ATOM   1842  C   TYR A 261      40.623  45.430  52.955  1.00 28.13           C  
ATOM   1843  O   TYR A 261      41.404  44.582  52.540  1.00 27.93           O  
ATOM   1844  CB  TYR A 261      39.524  44.477  54.984  1.00 28.76           C  
ATOM   1845  CG  TYR A 261      38.261  44.099  55.721  1.00 30.23           C  
ATOM   1846  CD1 TYR A 261      37.474  45.073  56.355  1.00 31.77           C  
ATOM   1847  CD2 TYR A 261      37.843  42.774  55.782  1.00 31.50           C  
ATOM   1848  CE1 TYR A 261      36.296  44.724  57.037  1.00 31.64           C  
ATOM   1849  CE2 TYR A 261      36.678  42.418  56.458  1.00 32.42           C  
ATOM   1850  CZ  TYR A 261      35.909  43.395  57.085  1.00 31.99           C  
ATOM   1851  OH  TYR A 261      34.757  43.031  57.758  1.00 30.93           O  
ATOM   1852  N   ASP A 262      40.878  46.728  52.899  1.00 27.65           N  
ATOM   1853  CA  ASP A 262      42.169  47.247  52.474  1.00 27.80           C  
ATOM   1854  C   ASP A 262      43.026  47.451  53.724  1.00 27.67           C  
ATOM   1855  O   ASP A 262      42.679  48.239  54.600  1.00 28.43           O  
ATOM   1856  CB  ASP A 262      41.990  48.537  51.650  1.00 27.50           C  
ATOM   1857  CG  ASP A 262      41.493  48.249  50.235  1.00 29.30           C  
ATOM   1858  OD1 ASP A 262      42.212  47.559  49.455  1.00 31.60           O  
ATOM   1859  OD2 ASP A 262      40.373  48.680  49.904  1.00 28.88           O  
ATOM   1860  N   LEU A 263      44.104  46.685  53.832  1.00 27.57           N  
ATOM   1861  CA  LEU A 263      44.985  46.762  55.002  1.00 27.57           C  
ATOM   1862  C   LEU A 263      46.103  47.782  54.749  1.00 27.69           C  
ATOM   1863  O   LEU A 263      46.513  47.983  53.605  1.00 27.79           O  
ATOM   1864  CB  LEU A 263      45.556  45.366  55.333  1.00 27.01           C  
ATOM   1865  CG  LEU A 263      44.560  44.243  55.661  1.00 27.03           C  
ATOM   1866  CD1 LEU A 263      45.278  42.914  56.073  1.00 28.40           C  
ATOM   1867  CD2 LEU A 263      43.529  44.685  56.743  1.00 26.71           C  
ATOM   1868  N   GLU A 264      46.568  48.449  55.801  1.00 27.95           N  
ATOM   1869  CA  GLU A 264      47.689  49.372  55.679  1.00 28.20           C  
ATOM   1870  C   GLU A 264      48.957  48.571  55.566  1.00 28.11           C  
ATOM   1871  O   GLU A 264      49.170  47.659  56.349  1.00 28.66           O  
ATOM   1872  CB  GLU A 264      47.806  50.280  56.908  1.00 28.64           C  
ATOM   1873  CG  GLU A 264      46.697  51.300  57.062  1.00 30.13           C  
ATOM   1874  CD  GLU A 264      46.584  52.180  55.856  1.00 31.94           C  
ATOM   1875  OE1 GLU A 264      47.621  52.710  55.399  1.00 32.49           O  
ATOM   1876  OE2 GLU A 264      45.458  52.309  55.344  1.00 34.09           O  
ATOM   1877  N   GLU A 265      49.805  48.930  54.608  1.00 28.09           N  
ATOM   1878  CA  GLU A 265      51.103  48.269  54.393  1.00 28.29           C  
ATOM   1879  C   GLU A 265      51.972  48.179  55.671  1.00 27.58           C  
ATOM   1880  O   GLU A 265      52.791  47.263  55.826  1.00 28.11           O  
ATOM   1881  CB  GLU A 265      51.857  49.020  53.295  1.00 28.44           C  
ATOM   1882  CG  GLU A 265      53.046  48.258  52.743  1.00 30.59           C  
ATOM   1883  CD  GLU A 265      53.813  49.060  51.737  1.00 30.91           C  
ATOM   1884  OE1 GLU A 265      53.536  50.273  51.616  1.00 30.82           O  
ATOM   1885  OE2 GLU A 265      54.690  48.483  51.053  1.00 34.18           O  
ATOM   1886  N   VAL A 266      51.804  49.141  56.571  1.00 26.94           N  
ATOM   1887  CA  VAL A 266      52.388  49.084  57.904  1.00 26.31           C  
ATOM   1888  C   VAL A 266      51.194  48.979  58.856  1.00 26.20           C  
ATOM   1889  O   VAL A 266      50.427  49.933  58.955  1.00 26.90           O  
ATOM   1890  CB  VAL A 266      53.244  50.340  58.198  1.00 26.67           C  
ATOM   1891  CG1 VAL A 266      53.664  50.412  59.676  1.00 25.15           C  
ATOM   1892  CG2 VAL A 266      54.472  50.393  57.264  1.00 27.00           C  
ATOM   1893  N   PRO A 267      51.029  47.835  59.563  1.00 25.97           N  
ATOM   1894  CA  PRO A 267      51.933  46.677  59.757  1.00 25.34           C  
ATOM   1895  C   PRO A 267      51.789  45.486  58.806  1.00 25.28           C  
ATOM   1896  O   PRO A 267      52.439  44.449  59.023  1.00 25.06           O  
ATOM   1897  CB  PRO A 267      51.572  46.209  61.162  1.00 25.24           C  
ATOM   1898  CG  PRO A 267      50.073  46.509  61.280  1.00 25.27           C  
ATOM   1899  CD  PRO A 267      49.766  47.651  60.314  1.00 26.33           C  
ATOM   1900  N   PHE A 268      50.960  45.612  57.773  1.00 25.07           N  
ATOM   1901  CA  PHE A 268      50.680  44.474  56.906  1.00 24.81           C  
ATOM   1902  C   PHE A 268      51.525  44.465  55.621  1.00 24.58           C  
ATOM   1903  O   PHE A 268      51.035  44.719  54.511  1.00 24.94           O  
ATOM   1904  CB  PHE A 268      49.171  44.326  56.646  1.00 24.20           C  
ATOM   1905  CG  PHE A 268      48.348  44.142  57.919  1.00 24.77           C  
ATOM   1906  CD1 PHE A 268      48.250  42.892  58.534  1.00 23.32           C  
ATOM   1907  CD2 PHE A 268      47.645  45.218  58.474  1.00 23.14           C  
ATOM   1908  CE1 PHE A 268      47.491  42.710  59.702  1.00 24.17           C  
ATOM   1909  CE2 PHE A 268      46.858  45.052  59.645  1.00 23.83           C  
ATOM   1910  CZ  PHE A 268      46.777  43.800  60.261  1.00 22.59           C  
ATOM   1911  N   GLY A 269      52.806  44.152  55.793  1.00 24.36           N  
ATOM   1912  CA  GLY A 269      53.778  44.236  54.698  1.00 23.60           C  
ATOM   1913  C   GLY A 269      53.944  42.935  53.942  1.00 22.99           C  
ATOM   1914  O   GLY A 269      53.290  41.941  54.245  1.00 22.91           O  
ATOM   1915  N   ILE A 270      54.841  42.956  52.958  1.00 22.89           N  
ATOM   1916  CA  ILE A 270      55.137  41.813  52.091  1.00 21.75           C  
ATOM   1917  C   ILE A 270      56.065  40.788  52.759  1.00 22.01           C  
ATOM   1918  O   ILE A 270      56.274  39.693  52.243  1.00 23.00           O  
ATOM   1919  CB  ILE A 270      55.680  42.287  50.707  1.00 22.12           C  
ATOM   1920  CG1 ILE A 270      55.441  41.214  49.628  1.00 22.16           C  
ATOM   1921  CG2 ILE A 270      57.142  42.709  50.775  1.00 18.98           C  
ATOM   1922  CD1 ILE A 270      55.540  41.749  48.173  1.00 21.69           C  
ATOM   1923  N   THR A 271      56.627  41.154  53.908  1.00 21.82           N  
ATOM   1924  CA  THR A 271      57.387  40.234  54.748  1.00 20.67           C  
ATOM   1925  C   THR A 271      57.032  40.549  56.201  1.00 20.56           C  
ATOM   1926  O   THR A 271      56.370  41.556  56.495  1.00 20.09           O  
ATOM   1927  CB  THR A 271      58.969  40.336  54.594  1.00 20.71           C  
ATOM   1928  OG1 THR A 271      59.500  41.394  55.422  1.00 20.14           O  
ATOM   1929  CG2 THR A 271      59.427  40.529  53.158  1.00 19.08           C  
ATOM   1930  N   ALA A 272      57.519  39.696  57.100  1.00 20.12           N  
ATOM   1931  CA  ALA A 272      57.353  39.906  58.520  1.00 19.69           C  
ATOM   1932  C   ALA A 272      58.176  41.128  58.939  1.00 19.30           C  
ATOM   1933  O   ALA A 272      59.099  41.545  58.230  1.00 19.01           O  
ATOM   1934  CB  ALA A 272      57.772  38.646  59.299  1.00 19.42           C  
ATOM   1935  N   ASN A 273      57.836  41.678  60.100  1.00 18.80           N  
ATOM   1936  CA  ASN A 273      58.541  42.816  60.661  1.00 18.78           C  
ATOM   1937  C   ASN A 273      58.278  42.766  62.162  1.00 18.36           C  
ATOM   1938  O   ASN A 273      57.400  42.040  62.608  1.00 17.80           O  
ATOM   1939  CB  ASN A 273      58.022  44.127  60.022  1.00 17.99           C  
ATOM   1940  CG  ASN A 273      58.981  45.315  60.189  1.00 18.52           C  
ATOM   1941  OD1 ASN A 273      58.800  46.378  59.552  1.00 22.44           O  
ATOM   1942  ND2 ASN A 273      59.974  45.160  61.025  1.00 13.01           N  
ATOM   1943  N   VAL A 274      59.039  43.532  62.932  1.00 18.29           N  
ATOM   1944  CA  VAL A 274      58.958  43.475  64.390  1.00 19.00           C  
ATOM   1945  C   VAL A 274      57.680  44.082  64.975  1.00 19.67           C  
ATOM   1946  O   VAL A 274      57.490  44.040  66.190  1.00 20.22           O  
ATOM   1947  CB  VAL A 274      60.185  44.123  65.053  1.00 18.84           C  
ATOM   1948  CG1 VAL A 274      61.434  43.314  64.728  1.00 18.18           C  
ATOM   1949  CG2 VAL A 274      60.308  45.606  64.627  1.00 18.30           C  
ATOM   1950  N   ASP A 275      56.823  44.642  64.119  1.00 19.72           N  
ATOM   1951  CA  ASP A 275      55.499  45.069  64.533  1.00 20.80           C  
ATOM   1952  C   ASP A 275      54.447  43.963  64.280  1.00 20.89           C  
ATOM   1953  O   ASP A 275      53.258  44.246  64.178  1.00 21.56           O  
ATOM   1954  CB  ASP A 275      55.105  46.408  63.864  1.00 20.50           C  
ATOM   1955  CG  ASP A 275      55.232  46.375  62.338  1.00 23.42           C  
ATOM   1956  OD1 ASP A 275      55.684  45.348  61.772  1.00 24.70           O  
ATOM   1957  OD2 ASP A 275      54.890  47.390  61.697  1.00 24.24           O  
ATOM   1958  N   ALA A 276      54.892  42.714  64.174  1.00 21.24           N  
ATOM   1959  CA  ALA A 276      53.974  41.576  64.039  1.00 21.78           C  
ATOM   1960  C   ALA A 276      53.021  41.474  65.236  1.00 21.76           C  
ATOM   1961  O   ALA A 276      51.919  40.957  65.101  1.00 22.04           O  
ATOM   1962  CB  ALA A 276      54.732  40.287  63.854  1.00 21.41           C  
ATOM   1963  N   ASP A 277      53.434  41.993  66.389  1.00 21.81           N  
ATOM   1964  CA  ASP A 277      52.508  42.137  67.522  1.00 22.20           C  
ATOM   1965  C   ASP A 277      51.232  42.948  67.179  1.00 22.47           C  
ATOM   1966  O   ASP A 277      50.107  42.486  67.469  1.00 22.10           O  
ATOM   1967  CB  ASP A 277      53.210  42.625  68.808  1.00 21.42           C  
ATOM   1968  CG  ASP A 277      53.939  43.962  68.651  1.00 22.38           C  
ATOM   1969  OD1 ASP A 277      53.961  44.572  67.558  1.00 22.98           O  
ATOM   1970  OD2 ASP A 277      54.510  44.409  69.670  1.00 22.84           O  
ATOM   1971  N   LYS A 278      51.409  44.112  66.540  1.00 22.27           N  
ATOM   1972  CA  LYS A 278      50.285  44.942  66.081  1.00 23.09           C  
ATOM   1973  C   LYS A 278      49.496  44.272  64.959  1.00 22.53           C  
ATOM   1974  O   LYS A 278      48.278  44.369  64.933  1.00 22.46           O  
ATOM   1975  CB  LYS A 278      50.747  46.300  65.548  1.00 22.86           C  
ATOM   1976  CG  LYS A 278      51.433  47.236  66.536  1.00 25.28           C  
ATOM   1977  CD  LYS A 278      51.470  48.655  65.907  1.00 25.23           C  
ATOM   1978  CE  LYS A 278      52.532  49.531  66.545  1.00 28.39           C  
ATOM   1979  NZ  LYS A 278      52.353  49.641  68.009  1.00 31.39           N  
ATOM   1980  N   ALA A 279      50.195  43.632  64.017  1.00 22.61           N  
ATOM   1981  CA  ALA A 279      49.546  42.951  62.901  1.00 21.94           C  
ATOM   1982  C   ALA A 279      48.653  41.796  63.334  1.00 21.85           C  
ATOM   1983  O   ALA A 279      47.543  41.658  62.831  1.00 22.06           O  
ATOM   1984  CB  ALA A 279      50.578  42.476  61.870  1.00 21.92           C  
ATOM   1985  N   MET A 280      49.152  40.959  64.245  1.00 22.19           N  
ATOM   1986  CA  MET A 280      48.403  39.814  64.792  1.00 22.27           C  
ATOM   1987  C   MET A 280      47.148  40.240  65.539  1.00 22.21           C  
ATOM   1988  O   MET A 280      46.089  39.647  65.355  1.00 22.72           O  
ATOM   1989  CB  MET A 280      49.284  38.972  65.738  1.00 21.88           C  
ATOM   1990  CG  MET A 280      50.308  38.055  65.034  1.00 22.06           C  
ATOM   1991  SD  MET A 280      51.284  37.021  66.153  1.00 22.82           S  
ATOM   1992  CE  MET A 280      52.431  38.183  66.880  1.00 19.75           C  
ATOM   1993  N   THR A 281      47.298  41.239  66.410  1.00 21.72           N  
ATOM   1994  CA  THR A 281      46.222  41.774  67.245  1.00 21.74           C  
ATOM   1995  C   THR A 281      45.153  42.436  66.381  1.00 21.84           C  
ATOM   1996  O   THR A 281      43.987  42.152  66.545  1.00 20.86           O  
ATOM   1997  CB  THR A 281      46.780  42.800  68.252  1.00 21.56           C  
ATOM   1998  OG1 THR A 281      47.817  42.184  69.028  1.00 21.81           O  
ATOM   1999  CG2 THR A 281      45.707  43.335  69.177  1.00 21.50           C  
ATOM   2000  N   GLN A 282      45.576  43.297  65.453  1.00 22.89           N  
ATOM   2001  CA  GLN A 282      44.670  43.998  64.547  1.00 24.56           C  
ATOM   2002  C   GLN A 282      43.862  43.047  63.669  1.00 24.91           C  
ATOM   2003  O   GLN A 282      42.661  43.229  63.515  1.00 25.91           O  
ATOM   2004  CB  GLN A 282      45.428  45.020  63.679  1.00 24.04           C  
ATOM   2005  CG  GLN A 282      45.911  46.242  64.458  1.00 25.54           C  
ATOM   2006  CD  GLN A 282      46.599  47.301  63.599  1.00 26.27           C  
ATOM   2007  OE1 GLN A 282      46.444  47.327  62.388  1.00 28.49           O  
ATOM   2008  NE2 GLN A 282      47.335  48.203  64.243  1.00 28.84           N  
ATOM   2009  N   LEU A 283      44.505  42.017  63.124  1.00 25.81           N  
ATOM   2010  CA  LEU A 283      43.816  41.069  62.247  1.00 25.35           C  
ATOM   2011  C   LEU A 283      42.806  40.216  63.006  1.00 25.31           C  
ATOM   2012  O   LEU A 283      41.683  40.011  62.544  1.00 24.92           O  
ATOM   2013  CB  LEU A 283      44.817  40.191  61.510  1.00 25.60           C  
ATOM   2014  CG  LEU A 283      44.300  39.408  60.306  1.00 26.13           C  
ATOM   2015  CD1 LEU A 283      43.625  40.358  59.308  1.00 25.37           C  
ATOM   2016  CD2 LEU A 283      45.437  38.632  59.643  1.00 25.56           C  
ATOM   2017  N   TYR A 284      43.200  39.719  64.174  1.00 25.46           N  
ATOM   2018  CA  TYR A 284      42.250  39.057  65.056  1.00 25.14           C  
ATOM   2019  C   TYR A 284      41.040  39.945  65.349  1.00 25.50           C  
ATOM   2020  O   TYR A 284      39.906  39.474  65.333  1.00 25.34           O  
ATOM   2021  CB  TYR A 284      42.901  38.633  66.372  1.00 25.09           C  
ATOM   2022  CG  TYR A 284      41.905  37.982  67.306  1.00 24.83           C  
ATOM   2023  CD1 TYR A 284      41.187  38.743  68.235  1.00 26.16           C  
ATOM   2024  CD2 TYR A 284      41.643  36.613  67.231  1.00 23.85           C  
ATOM   2025  CE1 TYR A 284      40.245  38.141  69.094  1.00 26.38           C  
ATOM   2026  CE2 TYR A 284      40.714  36.006  68.073  1.00 23.53           C  
ATOM   2027  CZ  TYR A 284      40.017  36.769  69.003  1.00 24.93           C  
ATOM   2028  OH  TYR A 284      39.085  36.169  69.832  1.00 25.20           O  
ATOM   2029  N   ASP A 285      41.275  41.227  65.622  1.00 25.75           N  
ATOM   2030  CA  ASP A 285      40.169  42.130  65.941  1.00 25.96           C  
ATOM   2031  C   ASP A 285      39.299  42.449  64.717  1.00 26.63           C  
ATOM   2032  O   ASP A 285      38.102  42.705  64.856  1.00 27.25           O  
ATOM   2033  CB  ASP A 285      40.673  43.403  66.609  1.00 25.69           C  
ATOM   2034  CG  ASP A 285      41.165  43.162  68.023  1.00 25.66           C  
ATOM   2035  OD1 ASP A 285      40.702  42.212  68.675  1.00 23.35           O  
ATOM   2036  OD2 ASP A 285      42.025  43.930  68.489  1.00 27.73           O  
ATOM   2037  N   LEU A 286      39.898  42.426  63.531  1.00 26.89           N  
ATOM   2038  CA  LEU A 286      39.146  42.541  62.291  1.00 27.33           C  
ATOM   2039  C   LEU A 286      38.251  41.318  62.077  1.00 27.14           C  
ATOM   2040  O   LEU A 286      37.099  41.461  61.681  1.00 27.38           O  
ATOM   2041  CB  LEU A 286      40.093  42.725  61.084  1.00 27.59           C  
ATOM   2042  CG  LEU A 286      39.485  42.935  59.683  1.00 28.25           C  
ATOM   2043  CD1 LEU A 286      40.522  43.399  58.651  1.00 29.38           C  
ATOM   2044  CD2 LEU A 286      38.830  41.677  59.153  1.00 31.77           C  
ATOM   2045  N   PHE A 287      38.787  40.124  62.333  1.00 27.24           N  
ATOM   2046  CA  PHE A 287      38.075  38.865  62.072  1.00 27.03           C  
ATOM   2047  C   PHE A 287      36.892  38.687  63.003  1.00 26.91           C  
ATOM   2048  O   PHE A 287      35.844  38.178  62.606  1.00 26.14           O  
ATOM   2049  CB  PHE A 287      39.005  37.663  62.250  1.00 27.05           C  
ATOM   2050  CG  PHE A 287      39.963  37.434  61.105  1.00 28.43           C  
ATOM   2051  CD1 PHE A 287      40.966  36.482  61.219  1.00 27.45           C  
ATOM   2052  CD2 PHE A 287      39.881  38.173  59.925  1.00 28.77           C  
ATOM   2053  CE1 PHE A 287      41.862  36.260  60.173  1.00 28.58           C  
ATOM   2054  CE2 PHE A 287      40.777  37.950  58.873  1.00 28.69           C  
ATOM   2055  CZ  PHE A 287      41.758  37.000  58.997  1.00 27.37           C  
ATOM   2056  N   TYR A 288      37.096  39.075  64.255  1.00 27.33           N  
ATOM   2057  CA  TYR A 288      36.120  38.864  65.310  1.00 28.71           C  
ATOM   2058  C   TYR A 288      35.732  40.208  65.901  1.00 30.17           C  
ATOM   2059  O   TYR A 288      36.443  40.751  66.751  1.00 31.01           O  
ATOM   2060  CB  TYR A 288      36.678  37.908  66.364  1.00 27.74           C  
ATOM   2061  CG  TYR A 288      37.052  36.566  65.771  1.00 27.10           C  
ATOM   2062  CD1 TYR A 288      36.068  35.640  65.434  1.00 26.13           C  
ATOM   2063  CD2 TYR A 288      38.387  36.241  65.514  1.00 24.53           C  
ATOM   2064  CE1 TYR A 288      36.403  34.411  64.866  1.00 26.76           C  
ATOM   2065  CE2 TYR A 288      38.741  35.012  64.948  1.00 26.77           C  
ATOM   2066  CZ  TYR A 288      37.736  34.102  64.630  1.00 27.41           C  
ATOM   2067  OH  TYR A 288      38.054  32.882  64.089  1.00 28.12           O  
ATOM   2068  N   LYS A 289      34.635  40.767  65.392  1.00 31.93           N  
ATOM   2069  CA  LYS A 289      34.153  42.081  65.830  1.00 33.11           C  
ATOM   2070  C   LYS A 289      32.633  42.177  65.791  1.00 33.20           C  
ATOM   2071  O   LYS A 289      32.034  42.984  66.523  1.00 34.05           O  
ATOM   2072  CB  LYS A 289      34.813  43.232  65.034  1.00 33.34           C  
ATOM   2073  CG  LYS A 289      34.759  43.148  63.491  1.00 34.24           C  
ATOM   2074  CD  LYS A 289      35.370  44.429  62.854  1.00 34.55           C  
ATOM   2075  CE  LYS A 289      35.505  44.360  61.317  1.00 36.32           C  
ATOM   2076  NZ  LYS A 289      34.291  44.834  60.539  1.00 38.26           N  
TER    2077      LYS A 289                                                      
HETATM 2078  CHA HEM A 300      60.293  46.665  48.583  1.00 30.86           C  
HETATM 2079  CHB HEM A 300      58.662  47.876  44.153  1.00 30.43           C  
HETATM 2080  CHC HEM A 300      57.021  43.296  43.624  1.00 30.86           C  
HETATM 2081  CHD HEM A 300      59.464  41.926  47.551  1.00 30.58           C  
HETATM 2082  C1A HEM A 300      59.881  47.437  47.499  1.00 31.87           C  
HETATM 2083  C2A HEM A 300      59.855  48.887  47.398  1.00 32.63           C  
HETATM 2084  C3A HEM A 300      59.407  49.220  46.171  1.00 33.02           C  
HETATM 2085  C4A HEM A 300      59.127  47.995  45.450  1.00 31.66           C  
HETATM 2086  CMA HEM A 300      59.209  50.653  45.600  1.00 31.81           C  
HETATM 2087  CAA HEM A 300      60.280  49.876  48.511  1.00 30.23           C  
HETATM 2088  CBA HEM A 300      59.072  50.324  49.331  1.00 31.81           C  
HETATM 2089  CGA HEM A 300      59.576  51.370  50.301  1.00 32.32           C  
HETATM 2090  O1A HEM A 300      59.743  51.057  51.502  1.00 31.75           O  
HETATM 2091  O2A HEM A 300      59.833  52.518  49.866  1.00 31.18           O  
HETATM 2092  C1B HEM A 300      58.111  46.736  43.592  1.00 31.76           C  
HETATM 2093  C2B HEM A 300      57.566  46.605  42.252  1.00 31.10           C  
HETATM 2094  C3B HEM A 300      57.117  45.337  42.122  1.00 31.45           C  
HETATM 2095  C4B HEM A 300      57.362  44.618  43.363  1.00 31.35           C  
HETATM 2096  CMB HEM A 300      57.552  47.768  41.217  1.00 31.28           C  
HETATM 2097  CAB HEM A 300      56.441  44.648  40.918  1.00 31.62           C  
HETATM 2098  CBB HEM A 300      56.191  45.308  39.783  1.00 34.77           C  
HETATM 2099  C1C HEM A 300      57.493  42.490  44.638  1.00 30.98           C  
HETATM 2100  C2C HEM A 300      57.219  41.091  44.884  1.00 32.32           C  
HETATM 2101  C3C HEM A 300      57.917  40.726  45.980  1.00 32.71           C  
HETATM 2102  C4C HEM A 300      58.633  41.877  46.454  1.00 31.26           C  
HETATM 2103  CMC HEM A 300      56.298  40.173  44.034  1.00 32.35           C  
HETATM 2104  CAC HEM A 300      57.967  39.350  46.702  1.00 31.83           C  
HETATM 2105  CBC HEM A 300      57.909  38.187  46.053  1.00 35.13           C  
HETATM 2106  C1D HEM A 300      59.926  43.047  48.207  1.00 30.86           C  
HETATM 2107  C2D HEM A 300      60.645  43.027  49.470  1.00 29.53           C  
HETATM 2108  C3D HEM A 300      60.893  44.505  49.792  1.00 30.10           C  
HETATM 2109  C4D HEM A 300      60.314  45.278  48.700  1.00 29.95           C  
HETATM 2110  CMD HEM A 300      61.044  41.776  50.281  1.00 28.39           C  
HETATM 2111  CAD HEM A 300      61.607  45.054  51.036  1.00 29.57           C  
HETATM 2112  CBD HEM A 300      60.561  45.180  52.144  1.00 28.29           C  
HETATM 2113  CGD HEM A 300      61.187  45.921  53.309  1.00 29.20           C  
HETATM 2114  O1D HEM A 300      61.043  45.464  54.477  1.00 28.33           O  
HETATM 2115  O2D HEM A 300      61.853  46.954  53.048  1.00 27.94           O  
HETATM 2116  NA  HEM A 300      59.444  46.943  46.286  1.00 31.29           N  
HETATM 2117  NB  HEM A 300      57.959  45.511  44.232  1.00 31.73           N  
HETATM 2118  NC  HEM A 300      58.334  42.927  45.627  1.00 31.05           N  
HETATM 2119  ND  HEM A 300      59.758  44.369  47.802  1.00 30.51           N  
HETATM 2120 FE   HEM A 300      58.845  44.944  46.058  1.00 29.54          FE  
HETATM 2121  O   HOH A 301      55.198  43.467  57.822  1.00 20.89           O  
HETATM 2122  O   HOH A 302      52.968  39.185  53.773  1.00 26.36           O  
HETATM 2123  O   HOH A 303      51.992  44.752  51.828  1.00 29.80           O  
HETATM 2124  O   HOH A 304      44.795  33.729  49.708  1.00 26.49           O  
HETATM 2125  O   HOH A 305      44.569  34.439  75.200  1.00 35.83           O  
HETATM 2126  O   HOH A 306      56.135  36.785  53.167  1.00 29.17           O  
HETATM 2127  O   HOH A 307      58.479  44.306  55.117  1.00 27.82           O  
HETATM 2128  O   HOH A 308      70.165  47.425  75.017  1.00 37.01           O  
HETATM 2129  O   HOH A 309      73.458  39.300  75.367  1.00 36.45           O  
HETATM 2130  O   HOH A 310      53.178  43.858  38.028  1.00 28.59           O  
HETATM 2131  O   HOH A 311      48.347  28.432  51.108  1.00 29.32           O  
HETATM 2132  O   HOH A 312      57.685  51.804  59.010  1.00 29.32           O  
HETATM 2133  O   HOH A 313      59.531  48.517  52.166  1.00 34.77           O  
HETATM 2134  O   HOH A 314      63.064  34.312  45.718  1.00 36.95           O  
HETATM 2135  O   HOH A 315      54.407  45.669  51.188  1.00 28.12           O  
HETATM 2136  O   HOH A 316      62.133  42.814  54.735  1.00 25.77           O  
HETATM 2137  O   HOH A 317      67.227  43.352  49.865  1.00 32.92           O  
HETATM 2138  O   HOH A 318      68.807  35.274  71.932  1.00 29.58           O  
HETATM 2139  O   HOH A 319      54.232  31.726  56.547  1.00 25.31           O  
HETATM 2140  O   HOH A 320      57.644  46.857  51.044  1.00 29.95           O  
HETATM 2141  O   HOH A 321      56.697  45.232  53.441  1.00 27.81           O  
HETATM 2142  O   HOH A 322      36.464  27.849  49.783  1.00 33.78           O  
HETATM 2143  O   HOH A 323      73.854  55.175  66.574  1.00 52.45           O  
HETATM 2144  O   HOH A 324      54.317  43.479  60.387  1.00 23.20           O  
HETATM 2145  O   HOH A 325      62.925  56.622  55.125  1.00 43.57           O  
HETATM 2146  O   HOH A 326      54.338  49.682  62.963  1.00 39.56           O  
HETATM 2147  O   HOH A 327      60.566  37.939  40.655  1.00 42.12           O  
HETATM 2148  O   HOH A 328      34.877  36.440  60.847  1.00 44.81           O  
HETATM 2149  O   HOH A 329      55.100  30.989  62.184  1.00 28.24           O  
HETATM 2150  O   HOH A 330      57.880  53.664  45.825  1.00 38.13           O  
HETATM 2151  O   HOH A 331      41.665  45.569  63.563  1.00 31.44           O  
HETATM 2152  O   HOH A 332      73.565  41.944  75.439  1.00 30.07           O  
HETATM 2153  O   HOH A 333      67.819  51.336  69.795  1.00 47.62           O  
HETATM 2154  O   HOH A 334      31.800  33.311  47.225  1.00 41.68           O  
HETATM 2155  O   HOH A 335      44.864  47.602  49.707  1.00 33.94           O  
HETATM 2156  O   HOH A 336      46.816  31.452  56.024  1.00 37.58           O  
HETATM 2157  O   HOH A 337      45.507  49.468  51.647  1.00 34.88           O  
HETATM 2158  O   HOH A 338      36.810  38.126  70.814  0.50 35.13           O  
HETATM 2159  O   HOH A 339      45.245  48.065  58.387  1.00 34.12           O  
HETATM 2160  O   HOH A 340      59.021  31.150  57.056  1.00 28.68           O  
HETATM 2161  O   HOH A 341      32.644  42.951  39.636  1.00 40.75           O  
HETATM 2162  O   HOH A 342      46.381  49.103  60.543  1.00 28.83           O  
HETATM 2163  O   HOH A 343      77.100  48.767  61.978  1.00 41.21           O  
HETATM 2164  O   HOH A 344      73.585  53.675  63.509  1.00 33.84           O  
HETATM 2165  O   HOH A 345      66.595  32.700  59.200  1.00 48.65           O  
HETATM 2166  O   HOH A 346      77.308  55.597  50.475  1.00 41.52           O  
HETATM 2167  O   HOH A 347      50.883  52.068  55.954  1.00 47.80           O  
HETATM 2168  O   HOH A 348      41.713  21.887  53.158  1.00 31.49           O  
HETATM 2169  O   HOH A 349      49.014  51.361  52.953  1.00 35.43           O  
HETATM 2170  O   HOH A 350      47.226  39.579  77.651  1.00 47.49           O  
HETATM 2171  O   HOH A 351      38.803  48.503  54.327  1.00 45.66           O  
HETATM 2172  O   HOH A 352      55.859  53.516  58.105  1.00 29.00           O  
HETATM 2173  O   HOH A 353      41.852  33.217  75.485  1.00 41.95           O  
HETATM 2174  O   HOH A 354      43.611  29.415  61.656  1.00 38.60           O  
HETATM 2175  O   HOH A 355      44.852  29.466  57.415  1.00 32.02           O  
HETATM 2176  O   HOH A 356      42.818  47.294  37.841  1.00 43.32           O  
HETATM 2177  O   HOH A 357      73.393  49.915  74.370  1.00 33.27           O  
HETATM 2178  O   HOH A 358      51.946  23.304  47.975  1.00 47.91           O  
HETATM 2179  O   HOH A 359      32.660  30.717  53.299  1.00 40.97           O  
HETATM 2180  O   HOH A 360      73.787  49.505  41.461  1.00 50.54           O  
HETATM 2181  O   HOH A 361      59.065  35.336  47.019  1.00 45.53           O  
HETATM 2182  O   HOH A 362      55.861  28.857  60.071  1.00 42.74           O  
HETATM 2183  O   HOH A 363      39.160  26.438  52.726  1.00 37.93           O  
HETATM 2184  O   HOH A 364      33.029  33.008  66.392  1.00 48.11           O  
HETATM 2185  O   HOH A 365      45.687  26.676  53.211  1.00 47.44           O  
HETATM 2186  O   HOH A 366      56.617  34.186  45.990  1.00 27.09           O  
HETATM 2187  O   HOH A 367      57.502  49.167  58.262  1.00 32.86           O  
HETATM 2188  O   HOH A 368      79.397  36.857  63.842  1.00 49.51           O  
HETATM 2189  O   HOH A 369      60.099  53.598  47.577  1.00 34.11           O  
HETATM 2190  O   HOH A 370      54.722  47.033  67.810  1.00 45.06           O  
HETATM 2191  O   HOH A 371      51.327  29.603  57.648  1.00 36.88           O  
HETATM 2192  O   HOH A 372      76.423  50.606  41.555  1.00 49.85           O  
HETATM 2193  O   HOH A 373      73.174  37.358  77.169  1.00 45.09           O  
HETATM 2194  O   HOH A 374      81.194  38.657  52.564  1.00 50.62           O  
HETATM 2195  O   HOH A 375      44.418  28.913  67.454  1.00 36.79           O  
HETATM 2196  O   HOH A 376      54.643  54.057  60.476  1.00 45.01           O  
HETATM 2197  O   HOH A 377      62.490  44.520  72.690  1.00 39.58           O  
HETATM 2198  O   HOH A 378      56.721  51.974  61.442  1.00 35.85           O  
HETATM 2199  O   HOH A 379      58.453  57.645  47.627  1.00 46.73           O  
HETATM 2200  O   HOH A 380      32.722  34.497  64.234  1.00 48.72           O  
HETATM 2201  O   HOH A 381      55.794  40.817  76.479  1.00 46.65           O  
HETATM 2202  O   HOH A 382      63.346  60.473  62.915  1.00 47.37           O  
HETATM 2203  O   HOH A 383      44.899  30.006  65.508  1.00 50.98           O  
HETATM 2204  O   HOH A 384      55.650  47.363  59.170  1.00 32.81           O  
HETATM 2205  O   HOH A 385      57.593  34.057  41.417  1.00 49.11           O  
HETATM 2206  O   HOH A 386      65.145  55.839  53.758  1.00 37.45           O  
HETATM 2207  O   HOH A 387      62.636  49.147  65.639  1.00 31.92           O  
HETATM 2208  O   HOH A 388      70.945  46.381  42.912  1.00 44.40           O  
HETATM 2209  O   HOH A 389      68.966  31.830  44.629  1.00 54.48           O  
HETATM 2210  O   HOH A 390      75.390  38.575  73.277  1.00 31.13           O  
HETATM 2211  O   HOH A 391      55.470  49.966  65.391  1.00 45.99           O  
HETATM 2212  O   HOH A 392      49.607  46.441  34.291  1.00 53.44           O  
HETATM 2213  O   HOH A 393      51.456  29.666  62.447  1.00 36.97           O  
HETATM 2214  O   HOH A 394      50.775  52.648  58.715  1.00 40.99           O  
HETATM 2215  O   HOH A 395      34.995  40.402  59.680  1.00 52.19           O  
HETATM 2216  O   HOH A 396      59.183  43.541  74.977  1.00 44.36           O  
HETATM 2217  O   HOH A 397      33.914  34.454  61.796  1.00 46.50           O  
HETATM 2218  O   HOH A 398      64.951  43.847  72.203  1.00 34.05           O  
HETATM 2219  O   HOH A 399      43.907  46.056  67.612  1.00 39.33           O  
HETATM 2220  O   HOH A 400      57.046  45.340  57.099  1.00 42.96           O  
HETATM 2221  O   HOH A 401      57.256  30.641  54.996  1.00 28.53           O  
HETATM 2222  O   HOH A 402      57.684  44.424  68.826  1.00 44.74           O  
HETATM 2223  O   HOH A 403      52.006  51.046  62.837  1.00 43.11           O  
HETATM 2224  O   HOH A 404      51.866  52.327  52.501  1.00 46.51           O  
HETATM 2225  O   HOH A 405      65.525  57.692  60.895  1.00 40.99           O  
HETATM 2226  O   HOH A 406      32.423  31.763  69.643  1.00 45.67           O  
HETATM 2227  O   HOH A 407      39.058  23.336  35.813  1.00 50.01           O  
HETATM 2228  O   HOH A 408      58.467  51.392  41.987  1.00 49.26           O  
HETATM 2229  O   HOH A 409      52.038  53.080  61.031  1.00 33.54           O  
HETATM 2230  O   HOH A 410      60.035  43.469  72.433  1.00 45.38           O  
HETATM 2231  O   HOH A 411      57.473  38.747  76.985  1.00 38.57           O  
HETATM 2232  O   HOH A 412      34.225  45.883  51.757  1.00 36.52           O  
HETATM 2233  O   HOH A 413      49.441  25.623  55.959  1.00 38.89           O  
HETATM 2234  O   HOH A 414      36.841  47.484  45.922  1.00 52.83           O  
HETATM 2235  O   HOH A 415      63.743  29.740  59.397  1.00 53.94           O  
HETATM 2236  O   HOH A 416      66.380  34.470  70.912  1.00 35.84           O  
HETATM 2237  O   HOH A 417      48.339  42.508  71.635  1.00 38.61           O  
HETATM 2238  O   HOH A 418      70.100  33.328  57.306  1.00 46.20           O  
HETATM 2239  O   HOH A 419      35.854  49.137  43.455  1.00 43.86           O  
HETATM 2240  O   HOH A 420      69.164  59.867  66.226  1.00 42.49           O  
HETATM 2241  O   HOH A 421      79.406  43.920  70.855  1.00 45.81           O  
HETATM 2242  O   HOH A 422      58.662  45.102  70.915  1.00 37.28           O  
HETATM 2243  O   HOH A 423      49.085  29.493  64.206  1.00 38.66           O  
HETATM 2244  O   HOH A 424      32.490  26.021  51.844  1.00 40.35           O  
HETATM 2245  O   HOH A 425      68.422  31.460  61.012  1.00 40.86           O  
HETATM 2246  O   HOH A 426      53.538  27.143  54.670  1.00 50.43           O  
HETATM 2247  O   HOH A 427      32.895  39.166  63.232  1.00 43.42           O  
HETATM 2248  O   HOH A 428      31.147  37.417  53.982  1.00 43.75           O  
HETATM 2249  O   HOH A 429      69.671  41.846  42.181  1.00 46.44           O  
HETATM 2250  O   HOH A 430      70.648  35.103  70.080  1.00 32.20           O  
HETATM 2251  O   HOH A 431      77.781  44.221  68.120  1.00 51.43           O  
HETATM 2252  O   HOH A 432      60.111  49.829  65.456  1.00 36.27           O  
HETATM 2253  O   HOH A 433      63.530  58.703  61.476  1.00 45.02           O  
HETATM 2254  O   HOH A 434      43.227  31.414  34.436  1.00 47.02           O  
HETATM 2255  O   HOH A 435      60.721  58.225  48.876  1.00 45.55           O  
HETATM 2256  O   HOH A 436      68.823  30.812  65.084  1.00 47.63           O  
HETATM 2257  O   HOH A 437      45.830  23.848  54.554  1.00 44.37           O  
HETATM 2258  O   HOH A 438      79.326  34.443  64.291  1.00 51.15           O  
HETATM 2259  O   HOH A 439      57.254  34.263  75.367  1.00 41.73           O  
HETATM 2260  O   HOH A 440      71.490  59.492  52.192  1.00 42.03           O  
HETATM 2261  O   HOH A 441      64.595  32.915  72.236  1.00 39.18           O  
HETATM 2262  O   HOH A 442      65.812  57.776  58.544  1.00 44.70           O  
HETATM 2263  O   HOH A 443      60.089  52.809  62.404  1.00 51.08           O  
HETATM 2264  O   HOH A 444      75.493  35.724  44.523  1.00 47.78           O  
HETATM 2265  O   HOH A 445      38.837  45.756  63.516  1.00 47.96           O  
HETATM 2266  O   HOH A 446      33.434  30.270  57.665  1.00 41.89           O  
HETATM 2267  O   HOH A 447      48.385  50.752  60.520  1.00 30.20           O  
HETATM 2268  O   HOH A 448      42.788  43.667  71.297  1.00 40.14           O  
HETATM 2269  O   HOH A 449      41.844  26.769  46.428  1.00 55.48           O  
HETATM 2270  O   HOH A 450      74.980  56.481  49.995  1.00 47.86           O  
HETATM 2271  O   HOH A 451      51.176  41.252  56.205  1.00 41.12           O  
HETATM 2272  O   HOH A 452      55.345  29.121  56.408  1.00 48.66           O  
HETATM 2273  O   HOH A 453      39.852  26.719  61.104  1.00 44.25           O  
HETATM 2274  O   HOH A 454      61.882  58.181  59.004  1.00 41.26           O  
HETATM 2275  O   HOH A 455      60.986  31.545  53.212  1.00 38.90           O  
HETATM 2276  O   HOH A 456      54.943  56.338  61.906  1.00 44.94           O  
HETATM 2277  O   HOH A 457      77.611  37.034  69.875  1.00 44.88           O  
HETATM 2278  O   HOH A 458      43.960  51.628  52.941  1.00 49.42           O  
HETATM 2279  O   HOH A 459      47.617  47.704  67.462  1.00 49.16           O  
HETATM 2280  O   HOH A 460      59.777  40.286  76.379  1.00 33.48           O  
HETATM 2281  O   HOH A 461      71.663  58.504  62.823  1.00 35.70           O  
HETATM 2282  O   HOH A 462      59.028  31.036  46.044  1.00 51.98           O  
HETATM 2283  O   HOH A 463      77.296  40.460  53.642  1.00 38.13           O  
HETATM 2284  O   HOH A 464      33.232  35.447  48.840  1.00 42.19           O  
HETATM 2285  O   HOH A 465      45.978  27.467  56.866  1.00 49.59           O  
HETATM 2286  O   HOH A 466      32.578  34.964  40.876  1.00 42.90           O  
HETATM 2287  O   HOH A 467      61.688  56.346  65.672  1.00 52.60           O  
HETATM 2288  O   HOH A 468      40.326  40.109  73.001  0.50 27.84           O  
HETATM 2289  O   HOH A 469      57.682  58.639  58.541  1.00 46.64           O  
HETATM 2290  O   HOH A 470      60.594  44.217  40.088  1.00 47.55           O  
HETATM 2291  O   HOH A 471      60.128  39.978  43.027  1.00 48.63           O  
HETATM 2292  O   HOH A 472      37.906  33.747  72.020  1.00 40.80           O  
HETATM 2293  O   HOH A 473      67.492  42.620  76.614  1.00 42.23           O  
HETATM 2294  O   HOH A 474      40.097  36.733  36.916  1.00 43.65           O  
HETATM 2295  O   HOH A 475      33.897  27.718  61.193  1.00 41.22           O  
HETATM 2296  O   HOH A 476      57.982  36.195  65.446  1.00 43.37           O  
HETATM 2297  O   HOH A 477      42.566  28.610  73.954  1.00 47.51           O  
HETATM 2298  O   HOH A 478      72.414  32.417  57.329  1.00 46.38           O  
HETATM 2299  O   HOH A 479      65.823  54.570  67.157  1.00 40.84           O  
HETATM 2300  O   HOH A 480      59.461  53.346  43.493  1.00 49.60           O  
HETATM 2301  O   HOH A 481      67.769  60.221  55.589  1.00 40.37           O  
HETATM 2302  O   HOH A 482      74.385  34.656  47.410  1.00 53.22           O  
HETATM 2303  O   HOH A 483      46.217  57.465  46.385  1.00 50.23           O  
HETATM 2304  O   HOH A 484      59.277  29.791  53.470  1.00 44.49           O  
HETATM 2305  O   HOH A 485      77.902  55.448  57.349  1.00 47.18           O  
HETATM 2306  O   HOH A 486      69.411  31.326  52.237  1.00 44.46           O  
HETATM 2307  O   HOH A 487      68.635  49.069  50.120  1.00 48.86           O  
HETATM 2308  O   HOH A 488      32.556  32.912  59.431  1.00 54.63           O  
HETATM 2309  O   HOH A 489      82.372  41.082  41.372  1.00 50.78           O  
HETATM 2310  O   HOH A 490      31.418  38.420  60.310  1.00 50.64           O  
HETATM 2311  O   HOH A 491      42.985  40.884  69.301  1.00 50.08           O  
HETATM 2312  O   HOH A 492      63.949  58.232  51.435  1.00 42.59           O  
HETATM 2313  O   HOH A 493      56.952  47.276  67.461  1.00 47.34           O  
HETATM 2314  O   HOH A 494      78.044  46.873  67.248  1.00 53.20           O  
HETATM 2315  O   HOH A 495      51.532  39.688  75.644  1.00 49.14           O  
HETATM 2316  O   HOH A 496      49.640  37.107  77.291  1.00 51.81           O  
HETATM 2317  O   HOH A 497      67.156  31.940  53.266  1.00 54.56           O  
HETATM 2318  O   HOH A 498      40.791  44.598  71.754  1.00 40.31           O  
HETATM 2319  O   HOH A 499      78.899  50.854  63.085  1.00 47.61           O  
HETATM 2320  O   HOH A 500      68.681  56.257  47.002  1.00 53.11           O  
HETATM 2321  O   HOH A 501      77.645  33.526  69.211  1.00 54.13           O  
HETATM 2322  O   HOH A 502      75.390  33.181  61.367  1.00 49.96           O  
HETATM 2323  O   HOH A 503      47.226  51.400  51.064  1.00 49.34           O  
HETATM 2324  O   HOH A 504      67.870  51.783  44.385  1.00 48.46           O  
HETATM 2325  O   HOH A 505      49.169  50.203  63.214  1.00 41.43           O  
HETATM 2326  O   HOH A 506      56.504  51.228  39.812  1.00 52.77           O  
HETATM 2327  O   HOH A 507      46.124  33.021  76.782  1.00 51.23           O  
HETATM 2328  O   HOH A 508      69.623  63.998  59.330  1.00 50.33           O  
HETATM 2329  O   HOH A 509      65.377  30.804  51.528  1.00 42.54           O  
HETATM 2330  O   HOH A 510      39.516  31.037  36.352  1.00 44.41           O  
HETATM 2331  O   HOH A 511      61.964  55.820  48.057  1.00 45.81           O  
HETATM 2332  O   HOH A 512      62.805  48.199  45.956  1.00 33.89           O  
HETATM 2333  O   HOH A 513      62.872  49.214  43.494  1.00 46.42           O  
HETATM 2334  O   HOH A 514      89.804  41.690  62.381  1.00 47.76           O  
HETATM 2335  O   HOH A 515      32.238  28.079  53.889  1.00 41.74           O  
HETATM 2336  O   HOH A 516      42.127  41.638  35.867  1.00 52.29           O  
HETATM 2337  O   HOH A 517      75.596  56.025  63.040  1.00 48.56           O  
HETATM 2338  O   HOH A 518      85.188  43.417  44.709  1.00 52.40           O  
HETATM 2339  O   HOH A 519      83.204  44.416  48.038  1.00 52.82           O  
HETATM 2340  O   HOH A 520      84.379  43.021  52.954  1.00 49.89           O  
HETATM 2341  O   HOH A 521      81.524  59.184  47.830  1.00 50.80           O  
HETATM 2342  O   HOH A 522      64.981  46.071  37.261  1.00 56.13           O  
HETATM 2343  O   HOH A 523      59.208  32.626  74.600  1.00 49.15           O  
HETATM 2344  O   HOH A 524      54.973  32.155  74.970  1.00 49.73           O  
HETATM 2345  O   HOH A 525      48.801  28.642  76.324  1.00 49.02           O  
HETATM 2346  O   HOH A 526      42.751  55.430  53.000  1.00 54.26           O  
HETATM 2347  O   HOH A 527      27.918  42.838  44.476  1.00 51.86           O  
HETATM 2348  O   HOH A 528      80.727  46.850  66.047  1.00 51.05           O  
HETATM 2349  O   HOH A 529      74.895  28.645  54.914  1.00 52.56           O  
HETATM 2350  O   HOH A 530      66.710  30.401  55.658  1.00 45.62           O  
HETATM 2351  O   HOH A 531      70.626  31.614  71.588  1.00 49.99           O  
HETATM 2352  O   HOH A 532      57.490  26.032  43.468  1.00 47.10           O  
HETATM 2353  O   HOH A 533      53.293  24.570  42.122  1.00 51.42           O  
HETATM 2354  O   HOH A 534      61.847  32.115  48.874  1.00 53.71           O  
HETATM 2355  O   HOH A 535      36.907  21.498  40.286  1.00 52.75           O  
HETATM 2356  O   HOH A 536      40.715  53.437  40.303  1.00 57.47           O  
HETATM 2357  O   HOH A 537      28.512  34.415  38.668  1.00 52.76           O  
HETATM 2358  O   HOH A 538      56.867  46.241  72.829  1.00 54.58           O  
HETATM 2359  O   HOH A 539      49.478  40.858  75.354  1.00 54.25           O  
HETATM 2360  O   HOH A 540      38.153  26.800  67.431  1.00 50.77           O  
HETATM 2361  O   HOH A 541      55.303  26.251  52.991  1.00 53.00           O  
HETATM 2362  O   HOH A 542      50.706  43.925  71.513  1.00 48.61           O  
HETATM 2363  O   HOH A 543      57.863  48.428  65.513  1.00 51.84           O  
HETATM 2364  O   HOH A 544      78.481  34.339  66.759  1.00 49.38           O  
HETATM 2365  O   HOH A 545      42.393  47.178  65.419  1.00 45.95           O  
HETATM 2366  O   HOH A 546      71.337  60.163  65.304  1.00 50.38           O  
CONECT  366 2120                                                                
CONECT 1571 2120                                                                
CONECT 2078 2082 2109                                                           
CONECT 2079 2085 2092                                                           
CONECT 2080 2095 2099                                                           
CONECT 2081 2102 2106                                                           
CONECT 2082 2078 2083 2116                                                      
CONECT 2083 2082 2084 2087                                                      
CONECT 2084 2083 2085 2086                                                      
CONECT 2085 2079 2084 2116                                                      
CONECT 2086 2084                                                                
CONECT 2087 2083 2088                                                           
CONECT 2088 2087 2089                                                           
CONECT 2089 2088 2090 2091                                                      
CONECT 2090 2089                                                                
CONECT 2091 2089                                                                
CONECT 2092 2079 2093 2117                                                      
CONECT 2093 2092 2094 2096                                                      
CONECT 2094 2093 2095 2097                                                      
CONECT 2095 2080 2094 2117                                                      
CONECT 2096 2093                                                                
CONECT 2097 2094 2098                                                           
CONECT 2098 2097                                                                
CONECT 2099 2080 2100 2118                                                      
CONECT 2100 2099 2101 2103                                                      
CONECT 2101 2100 2102 2104                                                      
CONECT 2102 2081 2101 2118                                                      
CONECT 2103 2100                                                                
CONECT 2104 2101 2105                                                           
CONECT 2105 2104                                                                
CONECT 2106 2081 2107 2119                                                      
CONECT 2107 2106 2108 2110                                                      
CONECT 2108 2107 2109 2111                                                      
CONECT 2109 2078 2108 2119                                                      
CONECT 2110 2107                                                                
CONECT 2111 2108 2112                                                           
CONECT 2112 2111 2113                                                           
CONECT 2113 2112 2114 2115                                                      
CONECT 2114 2113                                                                
CONECT 2115 2113                                                                
CONECT 2116 2082 2085 2120                                                      
CONECT 2117 2092 2095 2120                                                      
CONECT 2118 2099 2102 2120                                                      
CONECT 2119 2106 2109 2120                                                      
CONECT 2120  366 1571 2116 2117                                                 
CONECT 2120 2118 2119                                                           
MASTER      445    0    1   11   11    0    5    6 2365    1   46   20          
END