CNRS Nantes University UFIP UFIP
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***  GtoFactin  ***

elNémo ID: 191023134855143894

Job options:

ID        	=	 191023134855143894
JOBID     	=	 GtoFactin
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER GtoFactin

HEADER    STRUCTURAL PROTEIN                      27-JUN-05   2A42              
TITLE     ACTIN-DNASE I COMPLEX                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-ACTIN 1;                                              
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DEOXYRIBONUCLEASE-1;                                       
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: DEOXYRIBONUCLEASE I, DNASE I;                               
COMPND   9 EC: 3.1.21.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 OTHER_DETAILS: SKELETAL MUSCLE;                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   8 ORGANISM_COMMON: CATTLE;                                             
SOURCE   9 ORGANISM_TAXID: 9913;                                                
SOURCE  10 OTHER_DETAILS: PANCREAS                                              
KEYWDS    ACTIN, DNASE I, STRUCTURAL PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.CHEREAU,F.KERFF,R.DOMINGUEZ                                         
REVDAT   4   13-JUL-11 2A42    1       VERSN                                    
REVDAT   3 2 24-FEB-09 2A42    1       VERSN                                    
REVDAT   2 3 22-NOV-05 2A42    1       JRNL                                     
REVDAT   1 4 01-NOV-05 2A42    0                                                
JRNL        AUTH   D.CHEREAU,F.KERFF,P.GRACEFFA,Z.GRABAREK,K.LANGSETMO,         
JRNL        AUTH 2 R.DOMINGUEZ                                                  
JRNL        TITL   ACTIN-BOUND STRUCTURES OF WISKOTT-ALDRICH SYNDROME PROTEIN   
JRNL        TITL 2 (WASP)-HOMOLOGY DOMAIN 2 AND THE IMPLICATIONS FOR FILAMENT   
JRNL        TITL 3 ASSEMBLY                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102 16644 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16275905                                                     
JRNL        DOI    10.1073/PNAS.0507021102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 55819                          
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2973                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3360                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 183                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4838                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 485                                     
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) : 43.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.80000                                             
REMARK   3    B22 (A**2) : 0.62000                                              
REMARK   3    B33 (A**2) : 0.52000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.52000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.293         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5189 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7088 ; 1.589 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   662 ; 6.200 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   228 ;36.369 ;24.211       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   872 ;14.384 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;17.355 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   805 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3908 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2374 ; 0.216 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3608 ; 0.320 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   776 ; 0.214 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.043 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.134 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.200 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3236 ; 1.508 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5161 ; 2.221 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2212 ; 3.646 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1905 ; 5.220 ; 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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A    33                          
REMARK   3    RESIDUE RANGE :   A    70        A   137                          
REMARK   3    RESIDUE RANGE :   A   339        A   365                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.8530 -11.2810  24.4720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.2760 T22:   -.0412                                     
REMARK   3      T33:   -.3255 T12:    .0682                                     
REMARK   3      T13:   -.0144 T23:    .0572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5208 L22:   1.8491                                     
REMARK   3      L33:   4.2842 L12:   -.2449                                     
REMARK   3      L13:   -.8901 L23:    .8076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0875 S12:   -.5609 S13:   -.1944                       
REMARK   3      S21:    .1995 S22:    .1565 S23:   -.1229                       
REMARK   3      S31:    .2507 S32:    .6537 S33:   -.0690                       
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    34        A    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8430   4.4150  35.1360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.2596 T22:    .0098                                     
REMARK   3      T33:   -.3091 T12:    .0474                                     
REMARK   3      T13:   -.0004 T23:   -.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8747 L22:    .9442                                     
REMARK   3      L33:   7.0125 L12:   -.8563                                     
REMARK   3      L13:  -5.3005 L23:   1.6281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0036 S12:   -.8019 S13:    .0791                       
REMARK   3      S21:   -.0606 S22:    .0432 S23:   -.1696                       
REMARK   3      S31:    .0869 S32:    .5598 S33:   -.0468                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   138        A   181                          
REMARK   3    RESIDUE RANGE :   A   274        A   338                          
REMARK   3    RESIDUE RANGE :   A  1649        A  1650                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3570 -12.5500   1.6870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.2449 T22:   -.2495                                     
REMARK   3      T33:   -.2456 T12:   -.0002                                     
REMARK   3      T13:    .0212 T23:    .0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2794 L22:    .5272                                     
REMARK   3      L33:    .9321 L12:   -.0795                                     
REMARK   3      L13:   -.1106 L23:   -.1465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0239 S12:    .0631 S13:   -.1977                       
REMARK   3      S21:   -.0187 S22:    .0286 S23:    .0157                       
REMARK   3      S31:    .0470 S32:   -.0014 S33:   -.0047                       
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   182        A   273                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0620  -1.4460   9.1460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.2450 T22:   -.1965                                     
REMARK   3      T33:   -.2630 T12:    .0085                                     
REMARK   3      T13:    .0009 T23:   -.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0782 L22:   1.9312                                     
REMARK   3      L33:    .8434 L12:   -.6331                                     
REMARK   3      L13:    .8081 L23:    .1480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1171 S12:   -.3259 S13:    .0295                       
REMARK   3      S21:    .0410 S22:    .0452 S23:    .0806                       
REMARK   3      S31:   -.0174 S32:   -.1829 S33:    .0719                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   260                          
REMARK   3    RESIDUE RANGE :   B   270        B   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.0410  11.0360  50.2120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   -.2795 T22:   -.1894                                     
REMARK   3      T33:   -.2443 T12:   -.0772                                     
REMARK   3      T13:    .0348 T23:   -.1236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4463 L22:   1.3944                                     
REMARK   3      L33:   3.7986 L12:   -.1013                                     
REMARK   3      L13:  -2.6237 L23:   -.5645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .3104 S12:   -.4417 S13:    .2643                       
REMARK   3      S21:    .1255 S22:   -.0621 S23:    .0735                       
REMARK   3      S31:   -.3346 S32:    .6978 S33:   -.2482                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2A42 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033461.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ATN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, PEG3350, PH 7.0, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       76.36450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.74200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       76.36450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.74200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1605  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     PRO A   367                                                      
REMARK 465     SER A   368                                                      
REMARK 465     ILE A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     ARG A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     CYS A   374                                                      
REMARK 465     PHE A   375                                                      
REMARK 465     GLY B   100                                                      
REMARK 465     CYS B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     SER B   103                                                      
REMARK 465     CYS B   104                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1573     O    HOH A  1589              1.93            
REMARK 500   O    HOH B  1391     O    HOH B  1401              2.01            
REMARK 500   OG1  THR A   148     O    HOH A  1659              2.10            
REMARK 500   OE1  GLU A   276     O    HOH A  1672              2.11            
REMARK 500   ND2  ASN A    12     O    HOH A  1556              2.12            
REMARK 500   O    HOH A  1440     O    HOH A  1669              2.17            
REMARK 500   O    HOH B  1310     O    HOH B  1391              2.18            
REMARK 500   O    HOH A  1476     O    HOH A  1671              2.19            
REMARK 500   O    HOH B  1290     O    HOH B  1372              2.19            
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    ALA A 181     -150.97   -157.65                                   
REMARK 500    VAL A 201      -37.85   -145.12                                   
REMARK 500    ASN A 296       57.38   -144.03                                   
REMARK 500    THR B  10       54.80     33.31                                   
REMARK 500    ASN B  74     -155.99   -136.16                                   
REMARK 500    ALA B 171       54.97    -91.45                                   
REMARK 500    CYS B 173     -129.74     60.70                                   
REMARK 500    SER B 206        1.00    -69.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1593        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A1596        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A1635        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A1687        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH A1708        DISTANCE =  5.13 ANGSTROMS                       
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                              CA A1381  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1410   O                                                      
REMARK 620 2 ATP A 376   O2G  74.5                                              
REMARK 620 3 ATP A 376   O1B  87.3  75.1                                        
REMARK 620 4 HOH A1572   O    76.6 142.8  80.5                                  
REMARK 620 5 HOH A1430   O    85.2 100.8 172.2  99.7                            
REMARK 620 6 HOH A1396   O   147.6 136.7  93.0  71.5  94.5                      
REMARK 620 7 HOH A1449   O   142.7  72.9 101.2 140.4  83.6  68.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1272  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 203   O                                                      
REMARK 620 2 ASP B 201   OD1  86.6                                              
REMARK 620 3 THR B 203   OG1  69.7  74.8                                        
REMARK 620 4 THR B 205   O    89.8 153.3  79.1                                  
REMARK 620 5 THR B 207   O   135.6  78.4  66.1  85.9                            
REMARK 620 6 ASP B 201   OD2  91.4  52.1 124.8 154.6 110.3                      
REMARK 620 7 HOH B1291   O    74.7 124.0 138.5  80.2 146.8  75.7                
REMARK 620 8 HOH B1299   O   149.5 107.3 139.5  88.8  74.6  77.5  75.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1273  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1366   O                                                      
REMARK 620 2 HOH B1381   O    84.6                                              
REMARK 620 3 ASP B 172   OD2  83.2 164.5                                        
REMARK 620 4 HOH B1303   O    88.0  97.4  91.7                                  
REMARK 620 5 ASP B 198   O   174.7  99.8  92.0  94.3                            
REMARK 620 6 HOH B1309   O    82.5  83.4  85.5 170.4  95.0                      
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 NAG B 270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 271                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1381                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1380                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1382                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1383                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1384                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2A3Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A40   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2A41   RELATED DB: PDB                                   
DBREF  2A42 A    1   375  UNP    P68135   ACTS_RABIT       3    377             
SEQADV 2A42 HIC A   73  UNP  P68135    HIS    75 MODIFIED RESIDUE               
SEQRES   1 A  375  ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY          
SEQRES   2 A  375  SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA          
SEQRES   3 A  375  PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG          
SEQRES   4 A  375  HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER          
SEQRES   5 A  375  TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU          
SEQRES   6 A  375  THR LEU LYS TYR PRO ILE GLU HIC GLY ILE ILE THR ASN          
SEQRES   7 A  375  TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR          
SEQRES   8 A  375  ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU          
SEQRES   9 A  375  LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU          
SEQRES  10 A  375  LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO          
SEQRES  11 A  375  ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR          
SEQRES  12 A  375  ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY          
SEQRES  13 A  375  ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR          
SEQRES  14 A  375  ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY          
SEQRES  15 A  375  ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU          
SEQRES  16 A  375  ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE          
SEQRES  17 A  375  VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU          
SEQRES  18 A  375  ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER          
SEQRES  19 A  375  SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL          
SEQRES  20 A  375  ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR          
SEQRES  21 A  375  LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY          
SEQRES  22 A  375  ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP          
SEQRES  23 A  375  ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET          
SEQRES  24 A  375  SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG          
SEQRES  25 A  375  MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET          
SEQRES  26 A  375  LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER          
SEQRES  27 A  375  VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR          
SEQRES  28 A  375  PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU          
SEQRES  29 A  375  ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE                  
MODRES 2A42 HIC A   73  HIS  4-METHYL-HISTIDINE                                 
HET    HIC  A  73      11                                                       
HET     CA  A1381       1                                                       
HET    ATP  A1380      31                                                       
HET    GOL  A1382       6                                                       
HET    GOL  A1383       6                                                       
HET    GOL  A1384       6                                                       
HETNAM     HIC 4-METHYL-HISTIDINE                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  HIC    C7 H11 N3 O2                                                 
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  ATP    C10 H16 N5 O13 P3                                            
FORMUL   8  GOL    3(C3 H8 O3)                                                  
FORMUL   1  HOH   *485(H2 O)                                                    
HELIX    1   1 GLY A   55  LYS A   61  1                                   7    
HELIX    2   2 ASN A   78  ASN A   92  1                                  15    
HELIX    3   3 ALA A   97  HIS A  101  5                                   5    
HELIX    4   4 PRO A  112  THR A  126  1                                  15    
HELIX    5   5 GLN A  137  SER A  145  1                                   9    
HELIX    6   6 PRO A  172  ILE A  175  5                                   4    
HELIX    7   7 ALA A  181  GLY A  197  1                                  17    
HELIX    8   8 THR A  202  CYS A  217  1                                  16    
HELIX    9   9 ASP A  222  SER A  233  1                                  12    
HELIX   10  10 ASN A  252  GLN A  263  1                                  12    
HELIX   11  11 PRO A  264  GLY A  268  5                                   5    
HELIX   12  12 GLY A  273  LYS A  284  1                                  12    
HELIX   13  13 ASP A  286  ALA A  295  1                                  10    
HELIX   14  14 GLY A  301  MET A  305  5                                   5    
HELIX   15  15 GLY A  308  ALA A  321  1                                  14    
HELIX   16  16 GLU A  334  LYS A  336  5                                   3    
HELIX   17  17 TYR A  337  SER A  348  1                                  12    
HELIX   18  18 LEU A  349  MET A  355  5                                   7    
HELIX   19  19 LYS A  359  ALA A  365  1                                   7    
HELIX   20  20 GLY B   12  SER B   17  1                                   6    
HELIX   21  21 ASN B   18  ARG B   30  1                                  13    
HELIX   22  22 LEU B   45  ASN B   56  1                                  12    
HELIX   23  23 ALA B  136  SER B  138  5                                   3    
HELIX   24  24 ASP B  139  HIS B  159  1                                  21    
HELIX   25  25 THR B  177  SER B  183  5                                   7    
HELIX   26  26 ILE B  184  SER B  189  1                                   6    
HELIX   27  27 GLY B  218  VAL B  225  1                                   8    
HELIX   28  28 ASP B  234  TYR B  239  1                                   6    
HELIX   29  29 SER B  242  SER B  250  1                                   9    
SHEET    1   A 6 ALA A  29  PRO A  32  0                                        
SHEET    2   A 6 LEU A  16  PHE A  21 -1  N  VAL A  17   O  PHE A  31           
SHEET    3   A 6 LEU A   8  ASN A  12 -1  N  ASP A  11   O  LYS A  18           
SHEET    4   A 6 THR A 103  GLU A 107  1  O  LEU A 104   N  CYS A  10           
SHEET    5   A 6 ALA A 131  ILE A 136  1  O  TYR A 133   N  LEU A 105           
SHEET    6   A 6 ILE A 357  THR A 358 -1  O  ILE A 357   N  MET A 132           
SHEET    1   B 3 TYR A  53  VAL A  54  0                                        
SHEET    2   B 3 VAL A  35  PRO A  38 -1  N  GLY A  36   O  TYR A  53           
SHEET    3   B 3 LEU A  65  LYS A  68 -1  O  LYS A  68   N  VAL A  35           
SHEET    1   C 7 GLY A  42  MET A  44  0                                        
SHEET    2   C 7 HIS B  64  VAL B  67  1  O  VAL B  67   N  VAL A  43           
SHEET    3   C 7 ARG B  79  PHE B  84 -1  O  PHE B  82   N  VAL B  66           
SHEET    4   C 7 ILE B  34  VAL B  40 -1  N  ILE B  37   O  LEU B  81           
SHEET    5   C 7 LYS B   2  PHE B  11  1  N  PHE B   6   O  LEU B  36           
SHEET    6   C 7 VAL B 255  THR B 258 -1  O  VAL B 257   N  ILE B   3           
SHEET    7   C 7 ALA B 231  PRO B 232 -1  N  ALA B 231   O  GLU B 256           
SHEET    1   D 2 ILE A  71  GLU A  72  0                                        
SHEET    2   D 2 ILE A  75  ILE A  76 -1  O  ILE A  75   N  GLU A  72           
SHEET    1   E 3 TYR A 169  ALA A 170  0                                        
SHEET    2   E 3 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3   E 3 MET A 176  LEU A 178 -1  O  LEU A 178   N  THR A 160           
SHEET    1   F 5 TYR A 169  ALA A 170  0                                        
SHEET    2   F 5 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3   F 5 GLY A 150  SER A 155 -1  N  GLY A 150   O  ILE A 165           
SHEET    4   F 5 ASN A 297  SER A 300  1  O  VAL A 298   N  LEU A 153           
SHEET    5   F 5 ILE A 329  ILE A 330  1  O  ILE A 330   N  ASN A 297           
SHEET    1   G 2 LYS A 238  GLU A 241  0                                        
SHEET    2   G 2 VAL A 247  ILE A 250 -1  O  ILE A 248   N  TYR A 240           
SHEET    1   H 6 VAL B  89  GLN B  96  0                                        
SHEET    2   H 6 ALA B 114  SER B 120 -1  O  LYS B 117   N  ASP B  93           
SHEET    3   H 6 GLU B 127  ALA B 132 -1  O  PHE B 128   N  PHE B 118           
SHEET    4   H 6 VAL B 163  ASP B 168  1  O  MET B 164   N  ALA B 129           
SHEET    5   H 6 ASP B 212  ALA B 217 -1  O  VAL B 215   N  LEU B 165           
SHEET    6   H 6 PHE B 192  TRP B 194 -1  N  GLN B 193   O  VAL B 216           
LINK         ND2 ASN B  18                 C1  NAG B 270     1555   1555 1.440  
LINK         O4  NAG B 270                 C1  NAG B 271     1555   1555 1.440  
LINK         C   GLU A  72                 N   HIC A  73     1555   1555 1.340  
LINK         C   HIC A  73                 N   GLY A  74     1555   1555 1.330  
LINK        CA    CA A1381                 O   HOH A1410     1555   1555 2.390  
LINK        CA    CA A1381                 O2G ATP A 376     1555   1555 2.420  
LINK        CA    CA A1381                 O1B ATP A 376     1555   1555 2.360  
LINK        CA    CA A1381                 O   HOH A1572     1555   1555 2.540  
LINK        CA    CA A1381                 O   HOH A1430     1555   1555 2.350  
LINK        CA    CA A1381                 O   HOH A1396     1555   1555 2.420  
LINK        CA    CA A1381                 O   HOH A1449     1555   1555 2.460  
LINK        CA    CA B1272                 O   THR B 203     1555   1555 2.380  
LINK        CA    CA B1272                 OD1 ASP B 201     1555   1555 2.510  
LINK        CA    CA B1272                 OG1 THR B 203     1555   1555 2.670  
LINK        CA    CA B1272                 O   THR B 205     1555   1555 2.460  
LINK        CA    CA B1272                 O   THR B 207     1555   1555 2.460  
LINK        CA    CA B1272                 OD2 ASP B 201     1555   1555 2.450  
LINK        CA    CA B1272                 O   HOH B1291     1555   1555 2.390  
LINK        MG    MG B1273                 O   HOH B1366     1555   1555 2.430  
LINK        MG    MG B1273                 O   HOH B1381     1555   1555 2.350  
LINK        MG    MG B1273                 OD2 ASP B 172     1555   1555 2.390  
LINK        MG    MG B1273                 O   HOH B1303     1555   1555 2.340  
LINK        MG    MG B1273                 O   ASP B 198     1555   1555 2.320  
LINK        MG    MG B1273                 O   HOH B1309     1555   1555 2.520  
LINK        CA    CA B1272                 O   HOH B1299     1555   4556 2.410  
SSBOND   1 CYS B  173    CYS B  209                          1555   1555  2.10  
SITE     1 AC1  4 ASN B  18  LEU B  21  ALA B 248  NAG B 271                    
SITE     1 AC2  4 GLU B 244  MET B 245  NAG B 270  HOH B1341                    
SITE     1 AC3  6 ATP A 376  HOH A1396  HOH A1410  HOH A1430                    
SITE     2 AC3  6 HOH A1449  HOH A1572                                          
SITE     1 AC4  6 ASP B 201  THR B 203  THR B 205  THR B 207                    
SITE     2 AC4  6 HOH B1291  HOH B1299                                          
SITE     1 AC5  6 ASP B 172  ASP B 198  HOH B1303  HOH B1309                    
SITE     2 AC5  6 HOH B1366  HOH B1381                                          
SITE     1 AC6 29 GLY A  13  SER A  14  GLY A  15  LEU A  16                    
SITE     2 AC6 29 LYS A  18  GLY A 156  ASP A 157  GLY A 158                    
SITE     3 AC6 29 VAL A 159  GLY A 182  ARG A 210  LYS A 213                    
SITE     4 AC6 29 GLU A 214  GLY A 301  GLY A 302  THR A 303                    
SITE     5 AC6 29 MET A 305  TYR A 306  LYS A 336   CA A1381                    
SITE     6 AC6 29 HOH A1385  HOH A1406  HOH A1410  HOH A1429                    
SITE     7 AC6 29 HOH A1449  HOH A1462  HOH A1492  HOH A1573                    
SITE     8 AC6 29 HOH A1589                                                     
SITE     1 AC7  4 TYR A 188  ARG A 256  PHE A 266  HOH A1467                    
SITE     1 AC8  7 TYR A 218  LEU A 236  ARG A 254  HOH A1437                    
SITE     2 AC8  7 HOH A1693  HOH A1694  HOH A1705                               
SITE     1 AC9  5 ASP A 211  LYS A 215  TYR A 240  GLU A 241                    
SITE     2 AC9  5 HOH A1702                                                     
CRYST1                                                 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   THR A   5      40.039  14.283  -3.469  1.00 65.60           N  
ATOM      2  CA  THR A   5      39.604  13.975  -4.864  1.00 64.90           C  
ATOM      3  C   THR A   5      38.798  12.682  -4.922  1.00 64.12           C  
ATOM      4  O   THR A   5      38.214  12.364  -5.961  1.00 65.60           O  
ATOM      5  CB  THR A   5      40.790  13.873  -5.853  1.00 65.74           C  
ATOM      6  OG1 THR A   5      41.871  13.149  -5.248  1.00 66.04           O  
ATOM      7  CG2 THR A   5      41.288  15.260  -6.272  1.00 66.29           C  
ATOM      8  N   THR A   6      38.755  11.924  -3.829  1.00 60.96           N  
ATOM      9  CA  THR A   6      37.959  10.708  -3.866  1.00 57.84           C  
ATOM     10  C   THR A   6      36.495  11.108  -3.853  1.00 54.26           C  
ATOM     11  O   THR A   6      36.066  11.935  -3.053  1.00 53.63           O  
ATOM     12  CB  THR A   6      38.293   9.685  -2.742  1.00 59.44           C  
ATOM     13  OG1 THR A   6      37.562   9.977  -1.539  1.00 62.92           O  
ATOM     14  CG2 THR A   6      39.797   9.616  -2.480  1.00 55.51           C  
ATOM     15  N   ALA A   7      35.733  10.545  -4.782  1.00 51.09           N  
ATOM     16  CA  ALA A   7      34.306  10.826  -4.847  1.00 46.94           C  
ATOM     17  C   ALA A   7      33.593  10.157  -3.670  1.00 45.69           C  
ATOM     18  O   ALA A   7      34.016   9.094  -3.207  1.00 44.17           O  
ATOM     19  CB  ALA A   7      33.744  10.312  -6.173  1.00 47.11           C  
ATOM     20  N   LEU A   8      32.506  10.764  -3.198  1.00 43.89           N  
ATOM     21  CA  LEU A   8      31.638  10.103  -2.216  1.00 42.70           C  
ATOM     22  C   LEU A   8      30.439   9.514  -2.915  1.00 43.30           C  
ATOM     23  O   LEU A   8      29.986  10.071  -3.907  1.00 43.53           O  
ATOM     24  CB  LEU A   8      31.119  11.089  -1.179  1.00 41.83           C  
ATOM     25  CG  LEU A   8      32.194  11.950  -0.506  1.00 43.82           C  
ATOM     26  CD1 LEU A   8      31.531  12.933   0.421  1.00 43.04           C  
ATOM     27  CD2 LEU A   8      33.236  11.090   0.194  1.00 43.43           C  
ATOM     28  N   VAL A   9      29.920   8.414  -2.369  1.00 43.15           N  
ATOM     29  CA  VAL A   9      28.706   7.783  -2.866  1.00 42.87           C  
ATOM     30  C   VAL A   9      27.700   7.693  -1.712  1.00 43.53           C  
ATOM     31  O   VAL A   9      27.963   7.053  -0.682  1.00 43.31           O  
ATOM     32  CB  VAL A   9      29.009   6.377  -3.445  1.00 44.01           C  
ATOM     33  CG1 VAL A   9      27.718   5.641  -3.858  1.00 42.96           C  
ATOM     34  CG2 VAL A   9      30.013   6.473  -4.602  1.00 42.44           C  
ATOM     35  N   CYS A  10      26.564   8.360  -1.870  1.00 43.23           N  
ATOM     36  CA ACYS A  10      25.524   8.328  -0.862  0.70 44.01           C  
ATOM     37  CA BCYS A  10      25.501   8.341  -0.872  0.30 43.32           C  
ATOM     38  C   CYS A  10      24.211   7.790  -1.452  1.00 43.89           C  
ATOM     39  O   CYS A  10      23.652   8.369  -2.383  1.00 43.64           O  
ATOM     40  CB ACYS A  10      25.319   9.719  -0.260  0.70 46.27           C  
ATOM     41  CB BCYS A  10      25.214   9.746  -0.359  0.30 44.44           C  
ATOM     42  SG ACYS A  10      24.172   9.750   1.114  0.70 50.35           S  
ATOM     43  SG BCYS A  10      26.593  10.450   0.507  0.30 44.02           S  
ATOM     44  N   ASP A  11      23.749   6.681  -0.887  1.00 41.31           N  
ATOM     45  CA  ASP A  11      22.530   6.015  -1.347  1.00 41.84           C  
ATOM     46  C   ASP A  11      21.529   6.118  -0.193  1.00 43.24           C  
ATOM     47  O   ASP A  11      21.586   5.384   0.797  1.00 43.00           O  
ATOM     48  CB  ASP A  11      22.822   4.574  -1.763  1.00 40.49           C  
ATOM     49  CG  ASP A  11      21.543   3.781  -2.016  1.00 43.40           C  
ATOM     50  OD1 ASP A  11      20.578   4.402  -2.503  1.00 45.37           O  
ATOM     51  OD2 ASP A  11      21.478   2.582  -1.672  1.00 44.12           O  
ATOM     52  N   ASN A  12      20.658   7.104  -0.310  1.00 43.45           N  
ATOM     53  CA AASN A  12      19.658   7.399   0.705  0.50 44.58           C  
ATOM     54  CA BASN A  12      19.677   7.367   0.736  0.50 46.19           C  
ATOM     55  C   ASN A  12      18.359   6.623   0.493  1.00 45.55           C  
ATOM     56  O   ASN A  12      17.703   6.779  -0.553  1.00 45.57           O  
ATOM     57  CB AASN A  12      19.413   8.900   0.690  0.50 45.99           C  
ATOM     58  CB BASN A  12      19.499   8.872   0.982  0.50 48.80           C  
ATOM     59  CG AASN A  12      20.656   9.676   1.063  0.50 41.74           C  
ATOM     60  CG BASN A  12      19.563   9.705  -0.297  0.50 51.88           C  
ATOM     61  OD1AASN A  12      21.121  10.546   0.328  0.50 44.04           O  
ATOM     62  OD1BASN A  12      20.517  10.455  -0.520  0.50 57.85           O  
ATOM     63  ND2AASN A  12      21.234   9.321   2.197  0.50 43.68           N  
ATOM     64  ND2BASN A  12      18.535   9.598  -1.124  0.50 58.48           N  
ATOM     65  N   GLY A  13      18.005   5.776   1.457  1.00 40.72           N  
ATOM     66  CA  GLY A  13      16.806   4.934   1.400  1.00 40.64           C  
ATOM     67  C   GLY A  13      15.782   5.341   2.455  1.00 40.93           C  
ATOM     68  O   GLY A  13      16.088   6.127   3.373  1.00 39.86           O  
ATOM     69  N   SER A  14      14.598   4.758   2.346  1.00 38.05           N  
ATOM     70  CA  SER A  14      13.470   5.019   3.271  1.00 39.14           C  
ATOM     71  C   SER A  14      13.858   4.610   4.710  1.00 42.73           C  
ATOM     72  O   SER A  14      13.409   5.211   5.675  1.00 42.23           O  
ATOM     73  CB  SER A  14      12.288   4.163   2.884  1.00 41.16           C  
ATOM     74  OG  SER A  14      11.831   4.424   1.557  1.00 40.25           O  
ATOM     75  N   GLY A  15      14.673   3.567   4.827  1.00 40.04           N  
ATOM     76  CA  GLY A  15      15.019   3.023   6.149  1.00 41.69           C  
ATOM     77  C   GLY A  15      16.461   3.268   6.539  1.00 42.35           C  
ATOM     78  O   GLY A  15      16.713   3.568   7.708  1.00 40.68           O  
ATOM     79  N   LEU A  16      17.388   3.128   5.581  1.00 40.47           N  
ATOM     80  CA  LEU A  16      18.836   3.204   5.813  1.00 42.00           C  
ATOM     81  C   LEU A  16      19.579   4.128   4.848  1.00 41.54           C  
ATOM     82  O   LEU A  16      19.307   4.086   3.631  1.00 39.98           O  
ATOM     83  CB  LEU A  16      19.463   1.828   5.641  1.00 41.72           C  
ATOM     84  CG  LEU A  16      19.004   0.763   6.651  1.00 40.14           C  
ATOM     85  CD1 LEU A  16      19.516  -0.615   6.268  1.00 41.83           C  
ATOM     86  CD2 LEU A  16      19.407   1.118   8.097  1.00 42.74           C  
ATOM     87  N   VAL A  17      20.557   4.878   5.373  1.00 39.65           N  
ATOM     88  CA  VAL A  17      21.543   5.552   4.524  1.00 41.66           C  
ATOM     89  C   VAL A  17      22.703   4.580   4.321  1.00 41.85           C  
ATOM     90  O   VAL A  17      23.188   3.997   5.293  1.00 42.10           O  
ATOM     91  CB  VAL A  17      22.083   6.833   5.212  1.00 42.65           C  
ATOM     92  CG1 VAL A  17      23.163   7.508   4.333  1.00 42.19           C  
ATOM     93  CG2 VAL A  17      20.898   7.770   5.469  1.00 42.82           C  
ATOM     94  N   LYS A  18      23.130   4.400   3.075  1.00 42.46           N  
ATOM     95  CA  LYS A  18      24.383   3.703   2.768  1.00 41.25           C  
ATOM     96  C   LYS A  18      25.305   4.751   2.151  1.00 42.00           C  
ATOM     97  O   LYS A  18      25.010   5.325   1.080  1.00 40.84           O  
ATOM     98  CB  LYS A  18      24.134   2.549   1.779  1.00 43.31           C  
ATOM     99  CG  LYS A  18      23.504   1.269   2.388  1.00 41.45           C  
ATOM    100  CD  LYS A  18      21.988   1.398   2.708  1.00 41.31           C  
ATOM    101  CE  LYS A  18      21.127   1.748   1.458  1.00 43.31           C  
ATOM    102  NZ  LYS A  18      19.669   1.767   1.848  1.00 41.76           N  
ATOM    103  N   ALA A  19      26.415   5.012   2.834  1.00 41.14           N  
ATOM    104  CA  ALA A  19      27.375   6.039   2.417  1.00 40.87           C  
ATOM    105  C   ALA A  19      28.811   5.550   2.503  1.00 41.57           C  
ATOM    106  O   ALA A  19      29.175   4.744   3.382  1.00 40.77           O  
ATOM    107  CB  ALA A  19      27.213   7.281   3.271  1.00 41.93           C  
ATOM    108  N   GLY A  20      29.640   6.078   1.615  1.00 40.87           N  
ATOM    109  CA  GLY A  20      31.052   5.691   1.614  1.00 41.04           C  
ATOM    110  C   GLY A  20      31.830   6.360   0.510  1.00 42.69           C  
ATOM    111  O   GLY A  20      31.389   7.349  -0.073  1.00 41.98           O  
ATOM    112  N   PHE A  21      32.994   5.797   0.216  1.00 42.35           N  
ATOM    113  CA  PHE A  21      33.909   6.377  -0.750  1.00 43.48           C  
ATOM    114  C   PHE A  21      33.942   5.524  -1.999  1.00 43.59           C  
ATOM    115  O   PHE A  21      33.964   4.292  -1.928  1.00 43.33           O  
ATOM    116  CB  PHE A  21      35.299   6.460  -0.129  1.00 44.72           C  
ATOM    117  CG  PHE A  21      35.330   7.260   1.132  1.00 47.06           C  
ATOM    118  CD2 PHE A  21      35.185   6.643   2.366  1.00 49.59           C  
ATOM    119  CD1 PHE A  21      35.491   8.635   1.086  1.00 50.99           C  
ATOM    120  CE2 PHE A  21      35.209   7.388   3.548  1.00 48.97           C  
ATOM    121  CE1 PHE A  21      35.525   9.386   2.254  1.00 52.06           C  
ATOM    122  CZ  PHE A  21      35.376   8.758   3.488  1.00 51.01           C  
ATOM    123  N   ALA A  22      33.919   6.199  -3.144  1.00 44.13           N  
ATOM    124  CA  ALA A  22      33.902   5.530  -4.422  1.00 43.25           C  
ATOM    125  C   ALA A  22      35.201   4.758  -4.602  1.00 44.96           C  
ATOM    126  O   ALA A  22      36.288   5.216  -4.220  1.00 44.10           O  
ATOM    127  CB  ALA A  22      33.669   6.530  -5.532  1.00 43.88           C  
ATOM    128  N   GLY A  23      35.072   3.551  -5.142  1.00 44.68           N  
ATOM    129  CA  GLY A  23      36.204   2.648  -5.227  1.00 45.34           C  
ATOM    130  C   GLY A  23      36.275   1.682  -4.061  1.00 46.24           C  
ATOM    131  O   GLY A  23      36.996   0.688  -4.152  1.00 46.69           O  
ATOM    132  N   ASP A  24      35.572   1.962  -2.958  1.00 44.80           N  
ATOM    133  CA  ASP A  24      35.490   0.973  -1.875  1.00 45.18           C  
ATOM    134  C   ASP A  24      34.481  -0.098  -2.286  1.00 46.31           C  
ATOM    135  O   ASP A  24      33.561   0.149  -3.090  1.00 45.95           O  
ATOM    136  CB  ASP A  24      35.061   1.565  -0.523  1.00 43.10           C  
ATOM    137  CG  ASP A  24      36.109   2.434   0.128  1.00 47.36           C  
ATOM    138  OD1 ASP A  24      37.246   2.532  -0.384  1.00 46.93           O  
ATOM    139  OD2 ASP A  24      35.779   3.016   1.192  1.00 47.98           O  
ATOM    140  N   ASP A  25      34.626  -1.293  -1.725  1.00 46.40           N  
ATOM    141  CA  ASP A  25      33.756  -2.375  -2.158  1.00 48.33           C  
ATOM    142  C   ASP A  25      32.492  -2.502  -1.307  1.00 46.21           C  
ATOM    143  O   ASP A  25      31.604  -3.285  -1.636  1.00 46.33           O  
ATOM    144  CB  ASP A  25      34.512  -3.696  -2.204  1.00 49.45           C  
ATOM    145  CG  ASP A  25      35.151  -4.027  -0.888  1.00 55.62           C  
ATOM    146  OD1 ASP A  25      34.509  -3.752   0.151  1.00 62.09           O  
ATOM    147  OD2 ASP A  25      36.288  -4.548  -0.895  1.00 59.38           O  
ATOM    148  N   ALA A  26      32.433  -1.753  -0.207  1.00 44.06           N  
ATOM    149  CA  ALA A  26      31.230  -1.707   0.613  1.00 44.01           C  
ATOM    150  C   ALA A  26      31.045  -0.315   1.227  1.00 42.91           C  
ATOM    151  O   ALA A  26      32.036   0.398   1.413  1.00 42.28           O  
ATOM    152  CB  ALA A  26      31.302  -2.773   1.698  1.00 44.13           C  
ATOM    153  N   PRO A  27      29.792   0.074   1.544  1.00 41.72           N  
ATOM    154  CA  PRO A  27      29.659   1.354   2.241  1.00 42.19           C  
ATOM    155  C   PRO A  27      30.335   1.363   3.611  1.00 44.51           C  
ATOM    156  O   PRO A  27      30.235   0.378   4.357  1.00 45.57           O  
ATOM    157  CB  PRO A  27      28.137   1.518   2.408  1.00 41.67           C  
ATOM    158  CG  PRO A  27      27.584   0.171   2.309  1.00 40.35           C  
ATOM    159  CD  PRO A  27      28.472  -0.537   1.292  1.00 41.75           C  
ATOM    160  N   ARG A  28      30.967   2.481   3.949  1.00 42.87           N  
ATOM    161  CA  ARG A  28      31.580   2.655   5.254  1.00 46.15           C  
ATOM    162  C   ARG A  28      30.559   2.908   6.352  1.00 46.79           C  
ATOM    163  O   ARG A  28      30.775   2.531   7.515  1.00 47.29           O  
ATOM    164  CB  ARG A  28      32.573   3.818   5.231  1.00 46.19           C  
ATOM    165  CG  ARG A  28      33.663   3.649   6.246  1.00 53.13           C  
ATOM    166  CD  ARG A  28      34.687   2.691   5.672  1.00 62.36           C  
ATOM    167  NE  ARG A  28      35.408   3.329   4.576  1.00 66.42           N  
ATOM    168  CZ  ARG A  28      36.634   3.822   4.714  1.00 68.57           C  
ATOM    169  NH1 ARG A  28      37.254   4.401   3.692  1.00 68.39           N  
ATOM    170  NH2 ARG A  28      37.237   3.716   5.887  1.00 67.76           N  
ATOM    171  N   ALA A  29      29.467   3.575   5.998  1.00 44.84           N  
ATOM    172  CA  ALA A  29      28.494   3.987   6.997  1.00 45.84           C  
ATOM    173  C   ALA A  29      27.128   3.502   6.561  1.00 45.65           C  
ATOM    174  O   ALA A  29      26.695   3.835   5.450  1.00 44.88           O  
ATOM    175  CB  ALA A  29      28.468   5.507   7.107  1.00 45.02           C  
ATOM    176  N   VAL A  30      26.447   2.752   7.421  1.00 43.28           N  
ATOM    177  CA  VAL A  30      25.059   2.343   7.145  1.00 42.78           C  
ATOM    178  C   VAL A  30      24.290   2.593   8.434  1.00 43.54           C  
ATOM    179  O   VAL A  30      24.676   2.077   9.497  1.00 40.51           O  
ATOM    180  CB  VAL A  30      24.973   0.844   6.822  1.00 42.34           C  
ATOM    181  CG1 VAL A  30      23.519   0.410   6.592  1.00 42.45           C  
ATOM    182  CG2 VAL A  30      25.861   0.508   5.642  1.00 43.25           C  
ATOM    183  N   PHE A  31      23.235   3.389   8.360  1.00 39.35           N  
ATOM    184  CA  PHE A  31      22.569   3.866   9.576  1.00 41.14           C  
ATOM    185  C   PHE A  31      21.142   4.308   9.244  1.00 41.09           C  
ATOM    186  O   PHE A  31      20.832   4.620   8.107  1.00 40.81           O  
ATOM    187  CB  PHE A  31      23.387   5.012  10.238  1.00 41.49           C  
ATOM    188  CG  PHE A  31      23.496   6.262   9.399  1.00 42.62           C  
ATOM    189  CD2 PHE A  31      24.551   6.441   8.518  1.00 43.96           C  
ATOM    190  CD1 PHE A  31      22.527   7.251   9.476  1.00 42.51           C  
ATOM    191  CE2 PHE A  31      24.643   7.569   7.724  1.00 44.12           C  
ATOM    192  CE1 PHE A  31      22.615   8.387   8.699  1.00 43.24           C  
ATOM    193  CZ  PHE A  31      23.697   8.554   7.825  1.00 46.23           C  
ATOM    194  N   PRO A  32      20.256   4.301  10.235  1.00 42.18           N  
ATOM    195  CA  PRO A  32      18.860   4.597   9.964  1.00 40.64           C  
ATOM    196  C   PRO A  32      18.612   6.017   9.480  1.00 41.40           C  
ATOM    197  O   PRO A  32      19.179   6.974  10.004  1.00 39.67           O  
ATOM    198  CB  PRO A  32      18.173   4.358  11.315  1.00 41.20           C  
ATOM    199  CG  PRO A  32      19.153   3.600  12.138  1.00 42.89           C  
ATOM    200  CD  PRO A  32      20.501   3.949  11.646  1.00 41.13           C  
ATOM    201  N   SER A  33      17.710   6.132   8.502  1.00 39.36           N  
ATOM    202  CA ASER A  33      17.332   7.413   7.901  0.60 39.37           C  
ATOM    203  CA BSER A  33      17.365   7.423   7.923  0.40 39.24           C  
ATOM    204  C   SER A  33      16.285   8.083   8.779  1.00 40.53           C  
ATOM    205  O   SER A  33      15.107   8.189   8.380  1.00 38.33           O  
ATOM    206  CB ASER A  33      16.665   7.139   6.536  0.60 42.30           C  
ATOM    207  CB BSER A  33      16.829   7.220   6.500  0.40 41.90           C  
ATOM    208  OG ASER A  33      17.571   6.450   5.699  0.60 40.63           O  
ATOM    209  OG BSER A  33      16.772   8.460   5.838  0.40 38.78           O  
ATOM    210  N   ILE A  34      16.683   8.506   9.980  1.00 37.62           N  
ATOM    211  CA AILE A  34      15.766   9.014  10.987  0.50 39.43           C  
ATOM    212  CA BILE A  34      15.728   9.084  10.903  0.50 38.51           C  
ATOM    213  C   ILE A  34      16.382  10.272  11.606  1.00 37.25           C  
ATOM    214  O   ILE A  34      17.604  10.327  11.793  1.00 37.85           O  
ATOM    215  CB AILE A  34      15.630   7.989  12.136  0.50 40.53           C  
ATOM    216  CB BILE A  34      15.223   8.046  11.934  0.50 39.47           C  
ATOM    217  CG1AILE A  34      15.142   6.636  11.632  0.50 42.56           C  
ATOM    218  CG1BILE A  34      16.348   7.650  12.903  0.50 37.58           C  
ATOM    219  CG2AILE A  34      14.700   8.493  13.214  0.50 40.84           C  
ATOM    220  CG2BILE A  34      14.611   6.854  11.224  0.50 39.22           C  
ATOM    221  CD1AILE A  34      15.036   5.631  12.755  0.50 42.16           C  
ATOM    222  CD1BILE A  34      15.937   6.680  13.996  0.50 38.42           C  
ATOM    223  N   VAL A  35      15.563  11.269  11.923  1.00 39.21           N  
ATOM    224  CA  VAL A  35      15.981  12.471  12.650  1.00 38.76           C  
ATOM    225  C   VAL A  35      15.022  12.550  13.827  1.00 40.35           C  
ATOM    226  O   VAL A  35      13.811  12.385  13.645  1.00 39.41           O  
ATOM    227  CB  VAL A  35      15.879  13.768  11.803  1.00 40.51           C  
ATOM    228  CG1 VAL A  35      16.281  15.019  12.645  1.00 40.76           C  
ATOM    229  CG2 VAL A  35      16.767  13.679  10.562  1.00 42.82           C  
ATOM    230  N   GLY A  36      15.548  12.744  15.037  1.00 41.05           N  
ATOM    231  CA  GLY A  36      14.694  12.789  16.215  1.00 40.56           C  
ATOM    232  C   GLY A  36      14.983  14.045  17.021  1.00 41.87           C  
ATOM    233  O   GLY A  36      16.137  14.369  17.257  1.00 43.72           O  
ATOM    234  N   ARG A  37      13.935  14.738  17.442  1.00 40.72           N  
ATOM    235  CA  ARG A  37      14.079  15.921  18.283  1.00 40.17           C  
ATOM    236  C   ARG A  37      13.432  15.638  19.636  1.00 39.62           C  
ATOM    237  O   ARG A  37      12.353  15.058  19.703  1.00 38.40           O  
ATOM    238  CB  ARG A  37      13.419  17.115  17.620  1.00 41.94           C  
ATOM    239  CG  ARG A  37      13.944  17.376  16.196  1.00 43.32           C  
ATOM    240  CD  ARG A  37      13.134  18.466  15.523  1.00 48.56           C  
ATOM    241  NE  ARG A  37      13.758  18.924  14.286  1.00 49.80           N  
ATOM    242  CZ  ARG A  37      13.634  18.325  13.106  1.00 53.52           C  
ATOM    243  NH1 ARG A  37      12.895  17.230  12.964  1.00 51.12           N  
ATOM    244  NH2 ARG A  37      14.235  18.846  12.043  1.00 54.86           N  
ATOM    245  N   PRO A  38      14.105  16.047  20.719  1.00 39.82           N  
ATOM    246  CA  PRO A  38      13.630  15.745  22.075  1.00 41.38           C  
ATOM    247  C   PRO A  38      12.231  16.334  22.283  1.00 40.53           C  
ATOM    248  O   PRO A  38      11.963  17.448  21.838  1.00 39.28           O  
ATOM    249  CB  PRO A  38      14.658  16.449  22.984  1.00 43.28           C  
ATOM    250  CG  PRO A  38      15.903  16.546  22.123  1.00 45.84           C  
ATOM    251  CD  PRO A  38      15.373  16.790  20.715  1.00 40.91           C  
ATOM    252  N   ARG A  39      11.349  15.576  22.926  1.00 41.06           N  
ATOM    253  CA  ARG A  39       9.986  16.011  23.217  1.00 41.44           C  
ATOM    254  C   ARG A  39       9.928  16.893  24.452  1.00 40.35           C  
ATOM    255  O   ARG A  39       8.920  17.560  24.683  1.00 38.45           O  
ATOM    256  CB  ARG A  39       9.085  14.796  23.494  1.00 42.41           C  
ATOM    257  CG  ARG A  39       9.041  13.794  22.385  1.00 46.14           C  
ATOM    258  CD  ARG A  39       7.760  12.985  22.360  1.00 45.74           C  
ATOM    259  NE  ARG A  39       7.519  12.211  23.576  1.00 45.06           N  
ATOM    260  CZ  ARG A  39       8.087  11.038  23.847  1.00 48.54           C  
ATOM    261  NH1 ARG A  39       8.978  10.493  23.009  1.00 42.08           N  
ATOM    262  NH2 ARG A  39       7.775  10.413  24.976  1.00 44.46           N  
ATOM    263  N   HIS A  40      10.998  16.870  25.254  1.00 38.23           N  
ATOM    264  CA  HIS A  40      11.060  17.609  26.512  1.00 37.38           C  
ATOM    265  C   HIS A  40      12.439  18.261  26.638  1.00 37.76           C  
ATOM    266  O   HIS A  40      13.367  17.900  25.906  1.00 39.56           O  
ATOM    267  CB  HIS A  40      10.798  16.647  27.680  1.00 38.02           C  
ATOM    268  CG  HIS A  40       9.508  15.885  27.549  1.00 36.23           C  
ATOM    269  ND1 HIS A  40       8.284  16.437  27.863  1.00 38.81           N  
ATOM    270  CD2 HIS A  40       9.258  14.612  27.153  1.00 35.97           C  
ATOM    271  CE1 HIS A  40       7.331  15.553  27.624  1.00 41.21           C  
ATOM    272  NE2 HIS A  40       7.897  14.435  27.204  1.00 36.71           N  
ATOM    273  N   GLN A  41      12.567  19.185  27.583  1.00 38.16           N  
ATOM    274  CA  GLN A  41      13.790  19.948  27.802  1.00 42.14           C  
ATOM    275  C   GLN A  41      14.654  19.246  28.838  1.00 41.33           C  
ATOM    276  O   GLN A  41      14.209  19.022  29.967  1.00 38.99           O  
ATOM    277  CB  GLN A  41      13.482  21.368  28.300  1.00 42.83           C  
ATOM    278  CG  GLN A  41      12.858  22.285  27.252  1.00 50.36           C  
ATOM    279  CD  GLN A  41      13.687  22.323  25.985  1.00 54.50           C  
ATOM    280  OE1 GLN A  41      13.359  21.682  24.977  1.00 59.48           O  
ATOM    281  NE2 GLN A  41      14.809  23.030  26.052  1.00 59.41           N  
ATOM    282  N   GLY A  42      15.873  18.882  28.454  1.00 42.17           N  
ATOM    283  CA  GLY A  42      16.801  18.290  29.439  1.00 42.32           C  
ATOM    284  C   GLY A  42      18.099  17.946  28.745  1.00 43.83           C  
ATOM    285  O   GLY A  42      18.242  18.231  27.560  1.00 41.45           O  
ATOM    286  N   VAL A  43      19.038  17.327  29.459  1.00 40.59           N  
ATOM    287  CA  VAL A  43      20.329  16.992  28.882  1.00 39.05           C  
ATOM    288  C   VAL A  43      20.735  15.595  29.298  1.00 40.88           C  
ATOM    289  O   VAL A  43      20.190  15.050  30.281  1.00 40.75           O  
ATOM    290  CB  VAL A  43      21.437  18.012  29.276  1.00 37.78           C  
ATOM    291  CG1 VAL A  43      21.133  19.426  28.753  1.00 37.60           C  
ATOM    292  CG2 VAL A  43      21.647  18.032  30.798  1.00 35.34           C  
ATOM    293  N   MET A  44      21.638  14.993  28.523  1.00 40.76           N  
ATOM    294  CA  MET A  44      22.360  13.781  28.951  1.00 38.95           C  
ATOM    295  C   MET A  44      23.495  14.280  29.852  1.00 37.98           C  
ATOM    296  O   MET A  44      24.070  15.322  29.585  1.00 37.61           O  
ATOM    297  CB  MET A  44      22.996  13.045  27.768  1.00 40.62           C  
ATOM    298  CG  MET A  44      22.044  12.593  26.637  1.00 39.33           C  
ATOM    299  SD  MET A  44      20.702  11.597  27.280  1.00 43.97           S  
ATOM    300  CE  MET A  44      21.586  10.117  27.735  1.00 47.43           C  
ATOM    301  N   VAL A  45      23.822  13.537  30.909  1.00 37.13           N  
ATOM    302  CA  VAL A  45      24.873  13.954  31.826  1.00 37.47           C  
ATOM    303  C   VAL A  45      26.164  14.283  31.076  1.00 37.48           C  
ATOM    304  O   VAL A  45      26.646  13.483  30.258  1.00 38.32           O  
ATOM    305  CB  VAL A  45      25.157  12.835  32.851  1.00 38.13           C  
ATOM    306  CG1 VAL A  45      26.254  13.229  33.782  1.00 40.10           C  
ATOM    307  CG2 VAL A  45      23.889  12.531  33.624  1.00 39.49           C  
ATOM    308  N   GLY A  46      26.702  15.453  31.372  1.00 37.03           N  
ATOM    309  CA  GLY A  46      27.967  15.938  30.807  1.00 37.20           C  
ATOM    310  C   GLY A  46      27.817  16.517  29.400  1.00 40.80           C  
ATOM    311  O   GLY A  46      28.808  16.877  28.762  1.00 39.81           O  
ATOM    312  N   MET A  47      26.581  16.602  28.921  1.00 40.70           N  
ATOM    313  CA  MET A  47      26.309  17.132  27.572  1.00 43.21           C  
ATOM    314  C   MET A  47      25.485  18.410  27.621  1.00 44.33           C  
ATOM    315  O   MET A  47      24.778  18.679  28.598  1.00 44.43           O  
ATOM    316  CB  MET A  47      25.530  16.111  26.742  1.00 41.85           C  
ATOM    317  CG  MET A  47      26.202  14.768  26.531  1.00 47.34           C  
ATOM    318  SD  MET A  47      27.833  14.938  25.784  1.00 59.43           S  
ATOM    319  CE  MET A  47      28.592  13.339  26.077  1.00 54.02           C  
ATOM    320  N   GLY A  48      25.555  19.204  26.553  1.00 46.85           N  
ATOM    321  CA  GLY A  48      24.654  20.341  26.425  1.00 46.24           C  
ATOM    322  C   GLY A  48      23.322  19.947  25.791  1.00 46.19           C  
ATOM    323  O   GLY A  48      23.142  18.820  25.303  1.00 43.59           O  
ATOM    324  N   GLN A  49      22.365  20.874  25.791  1.00 47.07           N  
ATOM    325  CA  GLN A  49      21.064  20.567  25.188  1.00 49.53           C  
ATOM    326  C   GLN A  49      21.302  20.308  23.695  1.00 49.00           C  
ATOM    327  O   GLN A  49      22.036  21.062  23.059  1.00 47.76           O  
ATOM    328  CB  GLN A  49      20.077  21.726  25.424  1.00 50.70           C  
ATOM    329  CG  GLN A  49      18.799  21.677  24.574  1.00 54.79           C  
ATOM    330  CD  GLN A  49      17.728  20.747  25.136  1.00 58.27           C  
ATOM    331  OE1 GLN A  49      17.341  20.871  26.300  1.00 56.80           O  
ATOM    332  NE2 GLN A  49      17.228  19.822  24.303  1.00 55.53           N  
ATOM    333  N   LYS A  50      20.743  19.215  23.173  1.00 48.34           N  
ATOM    334  CA  LYS A  50      20.826  18.874  21.742  1.00 49.65           C  
ATOM    335  C   LYS A  50      19.546  19.275  21.027  1.00 47.59           C  
ATOM    336  O   LYS A  50      18.450  19.059  21.547  1.00 47.98           O  
ATOM    337  CB  LYS A  50      21.025  17.367  21.547  1.00 49.61           C  
ATOM    338  CG  LYS A  50      22.447  16.915  21.245  1.00 54.14           C  
ATOM    339  CD  LYS A  50      23.477  17.652  22.099  1.00 63.81           C  
ATOM    340  CE  LYS A  50      24.899  17.179  21.815  1.00 66.93           C  
ATOM    341  NZ  LYS A  50      25.093  15.754  22.231  1.00 69.03           N  
ATOM    342  N   ASP A  51      19.685  19.840  19.830  1.00 45.52           N  
ATOM    343  CA  ASP A  51      18.533  20.153  18.993  1.00 45.82           C  
ATOM    344  C   ASP A  51      17.939  18.896  18.329  1.00 44.08           C  
ATOM    345  O   ASP A  51      16.723  18.754  18.224  1.00 43.50           O  
ATOM    346  CB  ASP A  51      18.929  21.205  17.936  1.00 47.00           C  
ATOM    347  CG  ASP A  51      20.163  20.796  17.136  1.00 52.13           C  
ATOM    348  OD2 ASP A  51      20.428  21.428  16.095  1.00 58.92           O  
ATOM    349  OD1 ASP A  51      20.869  19.837  17.531  1.00 60.36           O  
ATOM    350  N   SER A  52      18.787  17.969  17.899  1.00 42.15           N  
ATOM    351  CA  SER A  52      18.293  16.748  17.257  1.00 43.38           C  
ATOM    352  C   SER A  52      19.391  15.691  17.227  1.00 43.66           C  
ATOM    353  O   SER A  52      20.580  16.007  17.438  1.00 45.44           O  
ATOM    354  CB  SER A  52      17.844  17.038  15.824  1.00 43.89           C  
ATOM    355  OG  SER A  52      18.924  17.566  15.078  1.00 43.97           O  
ATOM    356  N   TYR A  53      18.973  14.450  17.026  1.00 40.32           N  
ATOM    357  CA  TYR A  53      19.875  13.330  16.846  1.00 40.17           C  
ATOM    358  C   TYR A  53      19.576  12.723  15.486  1.00 39.59           C  
ATOM    359  O   TYR A  53      18.422  12.722  15.056  1.00 39.35           O  
ATOM    360  CB  TYR A  53      19.594  12.257  17.896  1.00 40.46           C  
ATOM    361  CG  TYR A  53      19.931  12.694  19.319  1.00 42.50           C  
ATOM    362  CD1 TYR A  53      21.224  12.567  19.816  1.00 45.29           C  
ATOM    363  CD2 TYR A  53      18.946  13.212  20.165  1.00 46.63           C  
ATOM    364  CE1 TYR A  53      21.541  12.973  21.143  1.00 45.29           C  
ATOM    365  CE2 TYR A  53      19.246  13.602  21.478  1.00 43.41           C  
ATOM    366  CZ  TYR A  53      20.534  13.484  21.953  1.00 46.22           C  
ATOM    367  OH  TYR A  53      20.790  13.855  23.258  1.00 44.97           O  
ATOM    368  N   VAL A  54      20.597  12.178  14.841  1.00 39.38           N  
ATOM    369  CA  VAL A  54      20.361  11.513  13.549  1.00 40.08           C  
ATOM    370  C   VAL A  54      20.901  10.085  13.622  1.00 41.20           C  
ATOM    371  O   VAL A  54      21.929   9.837  14.278  1.00 42.21           O  
ATOM    372  CB  VAL A  54      21.085  12.276  12.432  1.00 39.78           C  
ATOM    373  CG1 VAL A  54      20.924  11.610  11.089  1.00 41.33           C  
ATOM    374  CG2 VAL A  54      20.604  13.717  12.367  1.00 42.10           C  
ATOM    375  N   GLY A  55      20.209   9.142  12.989  1.00 40.73           N  
ATOM    376  CA  GLY A  55      20.782   7.828  12.755  1.00 39.14           C  
ATOM    377  C   GLY A  55      20.729   6.969  14.001  1.00 38.21           C  
ATOM    378  O   GLY A  55      19.713   6.964  14.692  1.00 37.54           O  
ATOM    379  N   ASP A  56      21.804   6.223  14.266  1.00 36.87           N  
ATOM    380  CA  ASP A  56      21.799   5.237  15.344  1.00 38.22           C  
ATOM    381  C   ASP A  56      21.447   5.892  16.674  1.00 38.86           C  
ATOM    382  O   ASP A  56      20.728   5.298  17.476  1.00 40.89           O  
ATOM    383  CB  ASP A  56      23.149   4.538  15.485  1.00 39.83           C  
ATOM    384  CG  ASP A  56      23.542   3.736  14.256  1.00 46.32           C  
ATOM    385  OD2 ASP A  56      24.728   3.844  13.860  1.00 50.71           O  
ATOM    386  OD1 ASP A  56      22.699   2.993  13.693  1.00 44.05           O  
ATOM    387  N   GLU A  57      21.992   7.080  16.950  1.00 39.53           N  
ATOM    388  CA  GLU A  57      21.750   7.695  18.266  1.00 40.06           C  
ATOM    389  C   GLU A  57      20.277   8.084  18.412  1.00 41.57           C  
ATOM    390  O   GLU A  57      19.718   7.957  19.493  1.00 40.56           O  
ATOM    391  CB  GLU A  57      22.680   8.883  18.557  1.00 41.35           C  
ATOM    392  CG  GLU A  57      22.619   9.265  20.045  1.00 44.34           C  
ATOM    393  CD  GLU A  57      23.775  10.122  20.504  1.00 48.53           C  
ATOM    394  OE1 GLU A  57      24.470  10.643  19.617  1.00 48.35           O  
ATOM    395  OE2 GLU A  57      23.979  10.282  21.735  1.00 47.09           O  
ATOM    396  N   ALA A  58      19.625   8.490  17.315  1.00 40.61           N  
ATOM    397  CA  ALA A  58      18.195   8.794  17.358  1.00 42.76           C  
ATOM    398  C   ALA A  58      17.383   7.537  17.680  1.00 43.72           C  
ATOM    399  O   ALA A  58      16.372   7.602  18.393  1.00 44.46           O  
ATOM    400  CB  ALA A  58      17.720   9.398  15.991  1.00 44.46           C  
ATOM    401  N   GLN A  59      17.773   6.396  17.118  1.00 41.34           N  
ATOM    402  CA  GLN A  59      17.025   5.162  17.367  1.00 42.32           C  
ATOM    403  C   GLN A  59      17.201   4.729  18.835  1.00 45.20           C  
ATOM    404  O   GLN A  59      16.276   4.295  19.513  1.00 45.82           O  
ATOM    405  CB  GLN A  59      17.543   4.053  16.452  1.00 41.80           C  
ATOM    406  CG  GLN A  59      17.099   2.618  16.833  1.00 48.94           C  
ATOM    407  CD  GLN A  59      15.586   2.418  16.806  1.00 52.12           C  
ATOM    408  OE1 GLN A  59      14.865   3.211  16.203  1.00 54.33           O  
ATOM    409  NE2 GLN A  59      15.098   1.373  17.492  1.00 54.52           N  
ATOM    410  N   SER A  60      18.409   4.866  19.336  1.00 42.86           N  
ATOM    411  CA  SER A  60      18.668   4.343  20.668  1.00 44.75           C  
ATOM    412  C   SER A  60      18.190   5.289  21.761  1.00 44.01           C  
ATOM    413  O   SER A  60      18.080   4.874  22.914  1.00 45.25           O  
ATOM    414  CB  SER A  60      20.149   3.998  20.792  1.00 45.04           C  
ATOM    415  OG  SER A  60      20.879   5.189  20.838  1.00 44.72           O  
ATOM    416  N   LYS A  61      17.900   6.544  21.410  1.00 43.09           N  
ATOM    417  CA  LYS A  61      17.314   7.529  22.341  1.00 42.64           C  
ATOM    418  C   LYS A  61      15.855   7.859  22.036  1.00 43.18           C  
ATOM    419  O   LYS A  61      15.295   8.821  22.592  1.00 43.55           O  
ATOM    420  CB  LYS A  61      18.151   8.815  22.428  1.00 41.11           C  
ATOM    421  CG  LYS A  61      19.573   8.636  23.014  1.00 43.32           C  
ATOM    422  CD  LYS A  61      20.219   9.981  23.337  1.00 40.00           C  
ATOM    423  CE  LYS A  61      21.498   9.895  24.199  1.00 45.11           C  
ATOM    424  NZ  LYS A  61      22.546   8.899  23.800  1.00 48.39           N  
ATOM    425  N   ARG A  62      15.224   7.056  21.182  1.00 40.73           N  
ATOM    426  CA  ARG A  62      13.930   7.415  20.601  1.00 42.59           C  
ATOM    427  C   ARG A  62      12.810   7.642  21.616  1.00 44.52           C  
ATOM    428  O   ARG A  62      11.821   8.334  21.320  1.00 43.36           O  
ATOM    429  CB  ARG A  62      13.491   6.343  19.597  1.00 42.34           C  
ATOM    430  CG  ARG A  62      13.221   4.936  20.180  1.00 42.79           C  
ATOM    431  CD  ARG A  62      12.873   3.932  19.043  1.00 44.70           C  
ATOM    432  NE  ARG A  62      11.571   4.199  18.436  1.00 49.82           N  
ATOM    433  CZ  ARG A  62      11.179   3.847  17.204  1.00 53.27           C  
ATOM    434  NH1 ARG A  62      11.989   3.252  16.328  1.00 52.13           N  
ATOM    435  NH2 ARG A  62       9.942   4.137  16.823  1.00 52.71           N  
ATOM    436  N   GLY A  63      12.937   7.033  22.801  1.00 43.48           N  
ATOM    437  CA  GLY A  63      11.893   7.178  23.805  1.00 41.85           C  
ATOM    438  C   GLY A  63      11.645   8.597  24.282  1.00 41.43           C  
ATOM    439  O   GLY A  63      10.535   8.907  24.739  1.00 43.69           O  
ATOM    440  N   ILE A  64      12.646   9.471  24.181  1.00 39.82           N  
ATOM    441  CA  ILE A  64      12.439  10.863  24.568  1.00 40.02           C  
ATOM    442  C   ILE A  64      12.453  11.807  23.365  1.00 39.04           C  
ATOM    443  O   ILE A  64      12.543  13.021  23.547  1.00 38.19           O  
ATOM    444  CB  ILE A  64      13.509  11.388  25.558  1.00 41.45           C  
ATOM    445  CG1 ILE A  64      14.904  11.115  25.008  1.00 40.87           C  
ATOM    446  CG2 ILE A  64      13.274  10.792  26.933  1.00 43.77           C  
ATOM    447  CD1 ILE A  64      16.021  11.846  25.741  1.00 44.06           C  
ATOM    448  N   LEU A  65      12.327  11.230  22.169  1.00 40.32           N  
ATOM    449  CA  LEU A  65      12.331  11.983  20.919  1.00 41.51           C  
ATOM    450  C   LEU A  65      11.019  11.819  20.169  1.00 41.48           C  
ATOM    451  O   LEU A  65      10.221  10.921  20.472  1.00 41.51           O  
ATOM    452  CB  LEU A  65      13.471  11.502  19.999  1.00 42.01           C  
ATOM    453  CG  LEU A  65      14.870  11.426  20.650  1.00 43.27           C  
ATOM    454  CD1 LEU A  65      15.939  10.894  19.680  1.00 40.67           C  
ATOM    455  CD2 LEU A  65      15.323  12.757  21.205  1.00 38.62           C  
ATOM    456  N   THR A  66      10.780  12.736  19.239  1.00 38.90           N  
ATOM    457  CA  THR A  66       9.868  12.479  18.117  1.00 43.13           C  
ATOM    458  C   THR A  66      10.674  12.184  16.855  1.00 41.99           C  
ATOM    459  O   THR A  66      11.509  12.997  16.453  1.00 42.29           O  
ATOM    460  CB  THR A  66       8.990  13.686  17.807  1.00 43.55           C  
ATOM    461  OG1 THR A  66       8.193  13.952  18.959  1.00 48.74           O  
ATOM    462  CG2 THR A  66       8.081  13.365  16.611  1.00 45.19           C  
ATOM    463  N   LEU A  67      10.417  11.043  16.221  1.00 44.02           N  
ATOM    464  CA  LEU A  67      11.252  10.634  15.101  1.00 43.45           C  
ATOM    465  C   LEU A  67      10.564  11.046  13.804  1.00 44.03           C  
ATOM    466  O   LEU A  67       9.340  10.971  13.705  1.00 44.39           O  
ATOM    467  CB  LEU A  67      11.475   9.129  15.105  1.00 44.74           C  
ATOM    468  CG  LEU A  67      12.193   8.478  16.282  1.00 48.14           C  
ATOM    469  CD1 LEU A  67      12.303   6.961  16.041  1.00 46.09           C  
ATOM    470  CD2 LEU A  67      13.558   9.119  16.557  1.00 48.83           C  
ATOM    471  N   LYS A  68      11.357  11.496  12.840  1.00 43.49           N  
ATOM    472  CA  LYS A  68      10.906  11.793  11.485  1.00 43.64           C  
ATOM    473  C   LYS A  68      11.733  10.978  10.509  1.00 42.33           C  
ATOM    474  O   LYS A  68      12.933  10.806  10.674  1.00 41.09           O  
ATOM    475  CB  LYS A  68      11.093  13.284  11.166  1.00 43.74           C  
ATOM    476  CG  LYS A  68      10.398  14.230  12.170  1.00 49.80           C  
ATOM    477  CD  LYS A  68       8.982  14.596  11.741  1.00 57.31           C  
ATOM    478  CE  LYS A  68       8.385  15.676  12.649  1.00 58.56           C  
ATOM    479  NZ  LYS A  68       8.603  17.068  12.116  1.00 67.29           N  
ATOM    480  N   TYR A  69      11.073  10.506   9.461  1.00 42.69           N  
ATOM    481  CA  TYR A  69      11.698   9.763   8.380  1.00 42.41           C  
ATOM    482  C   TYR A  69      11.593  10.626   7.128  1.00 41.69           C  
ATOM    483  O   TYR A  69      10.520  10.696   6.549  1.00 41.89           O  
ATOM    484  CB  TYR A  69      10.858   8.524   8.099  1.00 43.74           C  
ATOM    485  CG  TYR A  69      11.115   7.423   9.096  1.00 49.79           C  
ATOM    486  CD1 TYR A  69      10.567   7.489  10.367  1.00 49.57           C  
ATOM    487  CD2 TYR A  69      11.941   6.342   8.766  1.00 51.77           C  
ATOM    488  CE1 TYR A  69      10.826   6.499  11.320  1.00 52.33           C  
ATOM    489  CE2 TYR A  69      12.181   5.324   9.689  1.00 55.86           C  
ATOM    490  CZ  TYR A  69      11.624   5.416  10.957  1.00 52.80           C  
ATOM    491  OH  TYR A  69      11.870   4.416  11.877  1.00 58.77           O  
ATOM    492  N   PRO A  70      12.679  11.288   6.722  1.00 41.60           N  
ATOM    493  CA  PRO A  70      12.598  12.294   5.645  1.00 41.96           C  
ATOM    494  C   PRO A  70      12.379  11.667   4.286  1.00 41.25           C  
ATOM    495  O   PRO A  70      11.989  12.380   3.358  1.00 39.52           O  
ATOM    496  CB  PRO A  70      13.971  12.978   5.692  1.00 44.39           C  
ATOM    497  CG  PRO A  70      14.509  12.603   7.080  1.00 45.64           C  
ATOM    498  CD  PRO A  70      14.031  11.212   7.282  1.00 43.69           C  
ATOM    499  N   ILE A  71      12.593  10.356   4.204  1.00 38.98           N  
ATOM    500  CA  ILE A  71      12.404   9.623   2.945  1.00 40.15           C  
ATOM    501  C   ILE A  71      11.264   8.636   3.065  1.00 41.22           C  
ATOM    502  O   ILE A  71      11.313   7.722   3.899  1.00 41.81           O  
ATOM    503  CB  ILE A  71      13.685   8.918   2.485  1.00 39.15           C  
ATOM    504  CG1 ILE A  71      14.748   9.984   2.215  1.00 45.96           C  
ATOM    505  CG2 ILE A  71      13.378   8.045   1.213  1.00 39.08           C  
ATOM    506  CD1 ILE A  71      16.090   9.388   1.837  1.00 52.69           C  
ATOM    507  N   GLU A  72      10.232   8.847   2.248  1.00 40.38           N  
ATOM    508  CA  GLU A  72       8.996   8.055   2.278  1.00 39.62           C  
ATOM    509  C   GLU A  72       8.818   7.306   0.964  1.00 41.12           C  
ATOM    510  O   GLU A  72       8.739   7.948  -0.095  1.00 42.16           O  
ATOM    511  CB  GLU A  72       7.755   8.933   2.486  1.00 39.17           C  
ATOM    512  CG  GLU A  72       7.723   9.644   3.817  1.00 47.50           C  
ATOM    513  CD  GLU A  72       6.414  10.373   4.036  1.00 53.50           C  
ATOM    514  OE1 GLU A  72       5.451  10.118   3.279  1.00 64.55           O  
ATOM    515  OE2 GLU A  72       6.350  11.181   4.977  1.00 55.03           O  
HETATM  516  N   HIC A  73       8.766   5.973   1.036  1.00 39.85           N  
HETATM  517  CA  HIC A  73       8.584   5.136  -0.149  1.00 41.49           C  
HETATM  518  C   HIC A  73       9.635   5.471  -1.158  1.00 41.14           C  
HETATM  519  O   HIC A  73       9.389   5.506  -2.357  1.00 42.07           O  
HETATM  520  CB  HIC A  73       7.174   5.272  -0.732  1.00 42.12           C  
HETATM  521  CG  HIC A  73       6.155   4.870   0.309  1.00 50.16           C  
HETATM  522  ND1 HIC A  73       6.013   3.647   0.873  1.00 57.64           N  
HETATM  523  CD2 HIC A  73       5.165   5.678   0.868  1.00 54.77           C  
HETATM  524  CE1 HIC A  73       4.969   3.682   1.742  1.00 57.15           C  
HETATM  525  NE2 HIC A  73       4.468   4.923   1.733  1.00 57.77           N  
HETATM  526  CZ  HIC A  73       3.328   5.386   2.559  1.00 59.05           C  
ATOM    527  N   GLY A  74      10.817   5.803  -0.648  1.00 38.23           N  
ATOM    528  CA  GLY A  74      11.985   6.092  -1.469  1.00 39.75           C  
ATOM    529  C   GLY A  74      12.118   7.533  -1.930  1.00 39.02           C  
ATOM    530  O   GLY A  74      13.159   7.929  -2.486  1.00 41.31           O  
ATOM    531  N   ILE A  75      11.090   8.340  -1.693  1.00 39.60           N  
ATOM    532  CA  ILE A  75      11.132   9.722  -2.171  1.00 40.42           C  
ATOM    533  C   ILE A  75      11.384  10.676  -1.001  1.00 39.80           C  
ATOM    534  O   ILE A  75      10.734  10.545   0.035  1.00 39.03           O  
ATOM    535  CB  ILE A  75       9.767  10.118  -2.803  1.00 41.25           C  
ATOM    536  CG1 ILE A  75       9.391   9.134  -3.929  1.00 46.25           C  
ATOM    537  CG2 ILE A  75       9.777  11.596  -3.291  1.00 39.79           C  
ATOM    538  CD1 ILE A  75      10.143   9.321  -5.199  1.00 52.43           C  
ATOM    539  N   ILE A  76      12.241  11.675  -1.193  1.00 40.71           N  
ATOM    540  CA  ILE A  76      12.492  12.675  -0.126  1.00 40.09           C  
ATOM    541  C   ILE A  76      11.289  13.568   0.062  1.00 39.67           C  
ATOM    542  O   ILE A  76      10.838  14.239  -0.892  1.00 39.33           O  
ATOM    543  CB  ILE A  76      13.698  13.569  -0.432  1.00 39.89           C  
ATOM    544  CG1 ILE A  76      14.973  12.727  -0.505  1.00 42.93           C  
ATOM    545  CG2 ILE A  76      13.848  14.617   0.654  1.00 38.93           C  
ATOM    546  CD1 ILE A  76      16.127  13.467  -1.182  1.00 51.45           C  
ATOM    547  N   THR A  77      10.742  13.594   1.276  1.00 36.26           N  
ATOM    548  CA  THR A  77       9.559  14.420   1.502  1.00 38.10           C  
ATOM    549  C   THR A  77       9.695  15.502   2.592  1.00 38.59           C  
ATOM    550  O   THR A  77       8.827  16.361   2.715  1.00 38.57           O  
ATOM    551  CB  THR A  77       8.268  13.601   1.755  1.00 39.94           C  
ATOM    552  OG1 THR A  77       8.438  12.862   2.972  1.00 45.85           O  
ATOM    553  CG2 THR A  77       7.933  12.657   0.601  1.00 39.26           C  
ATOM    554  N   ASN A  78      10.781  15.504   3.364  1.00 38.26           N  
ATOM    555  CA  ASN A  78      10.989  16.540   4.372  1.00 40.14           C  
ATOM    556  C   ASN A  78      12.418  17.030   4.107  1.00 40.44           C  
ATOM    557  O   ASN A  78      13.379  16.324   4.416  1.00 39.38           O  
ATOM    558  CB  ASN A  78      10.813  15.888   5.757  1.00 41.15           C  
ATOM    559  CG  ASN A  78      11.232  16.766   6.929  1.00 47.46           C  
ATOM    560  OD1 ASN A  78      11.692  17.907   6.782  1.00 44.00           O  
ATOM    561  ND2 ASN A  78      11.098  16.192   8.139  1.00 50.94           N  
ATOM    562  N   TRP A  79      12.546  18.208   3.489  1.00 38.88           N  
ATOM    563  CA  TRP A  79      13.857  18.717   3.063  1.00 39.86           C  
ATOM    564  C   TRP A  79      14.741  19.219   4.204  1.00 40.48           C  
ATOM    565  O   TRP A  79      15.965  19.131   4.146  1.00 41.63           O  
ATOM    566  CB  TRP A  79      13.694  19.821   2.008  1.00 38.40           C  
ATOM    567  CG  TRP A  79      13.156  19.220   0.769  1.00 39.89           C  
ATOM    568  CD1 TRP A  79      11.860  19.261   0.333  1.00 41.59           C  
ATOM    569  CD2 TRP A  79      13.868  18.390  -0.153  1.00 40.23           C  
ATOM    570  NE1 TRP A  79      11.728  18.518  -0.812  1.00 41.36           N  
ATOM    571  CE2 TRP A  79      12.945  17.977  -1.134  1.00 39.60           C  
ATOM    572  CE3 TRP A  79      15.205  17.981  -0.263  1.00 40.79           C  
ATOM    573  CZ2 TRP A  79      13.313  17.195  -2.213  1.00 41.55           C  
ATOM    574  CZ3 TRP A  79      15.566  17.153  -1.331  1.00 40.19           C  
ATOM    575  CH2 TRP A  79      14.616  16.795  -2.301  1.00 41.86           C  
ATOM    576  N   ASP A  80      14.120  19.745   5.243  1.00 39.30           N  
ATOM    577  CA  ASP A  80      14.889  20.228   6.380  1.00 41.79           C  
ATOM    578  C   ASP A  80      15.564  19.058   7.100  1.00 41.39           C  
ATOM    579  O   ASP A  80      16.735  19.141   7.477  1.00 41.35           O  
ATOM    580  CB  ASP A  80      13.972  21.009   7.312  1.00 43.22           C  
ATOM    581  CG  ASP A  80      13.543  22.353   6.727  1.00 52.45           C  
ATOM    582  OD1 ASP A  80      14.397  23.137   6.245  1.00 61.29           O  
ATOM    583  OD2 ASP A  80      12.329  22.642   6.767  1.00 60.97           O  
ATOM    584  N   ASP A  81      14.833  17.957   7.246  1.00 40.45           N  
ATOM    585  CA  ASP A  81      15.350  16.774   7.920  1.00 41.09           C  
ATOM    586  C   ASP A  81      16.284  16.009   6.996  1.00 39.55           C  
ATOM    587  O   ASP A  81      17.271  15.445   7.451  1.00 38.57           O  
ATOM    588  CB  ASP A  81      14.197  15.934   8.461  1.00 42.07           C  
ATOM    589  CG  ASP A  81      13.555  16.601   9.684  1.00 47.96           C  
ATOM    590  OD1 ASP A  81      14.165  17.553  10.223  1.00 53.35           O  
ATOM    591  OD2 ASP A  81      12.464  16.187  10.112  1.00 57.49           O  
ATOM    592  N   MET A  82      16.014  16.034   5.689  1.00 38.65           N  
ATOM    593  CA  MET A  82      16.989  15.465   4.765  1.00 39.36           C  
ATOM    594  C   MET A  82      18.339  16.187   4.849  1.00 39.23           C  
ATOM    595  O   MET A  82      19.387  15.542   4.767  1.00 40.87           O  
ATOM    596  CB  MET A  82      16.452  15.458   3.322  1.00 41.13           C  
ATOM    597  CG  MET A  82      17.282  14.553   2.428  1.00 44.91           C  
ATOM    598  SD  MET A  82      17.134  12.830   2.955  1.00 50.64           S  
ATOM    599  CE  MET A  82      18.822  12.246   2.824  1.00 47.55           C  
ATOM    600  N   GLU A  83      18.327  17.510   4.997  1.00 39.41           N  
ATOM    601  CA  GLU A  83      19.584  18.262   5.167  1.00 41.45           C  
ATOM    602  C   GLU A  83      20.343  17.806   6.396  1.00 41.37           C  
ATOM    603  O   GLU A  83      21.581  17.699   6.376  1.00 43.67           O  
ATOM    604  CB  GLU A  83      19.327  19.762   5.300  1.00 42.70           C  
ATOM    605  CG  GLU A  83      18.969  20.392   4.010  1.00 50.00           C  
ATOM    606  CD  GLU A  83      19.093  21.898   4.082  1.00 59.19           C  
ATOM    607  OE1 GLU A  83      18.469  22.571   3.235  1.00 66.21           O  
ATOM    608  OE2 GLU A  83      19.796  22.397   4.989  1.00 62.65           O  
ATOM    609  N   LYS A  84      19.615  17.584   7.484  1.00 41.02           N  
ATOM    610  CA  LYS A  84      20.240  17.059   8.711  1.00 42.20           C  
ATOM    611  C   LYS A  84      20.886  15.698   8.498  1.00 42.27           C  
ATOM    612  O   LYS A  84      21.964  15.428   9.042  1.00 41.92           O  
ATOM    613  CB  LYS A  84      19.260  17.022   9.894  1.00 41.31           C  
ATOM    614  CG  LYS A  84      18.718  18.397  10.220  1.00 43.85           C  
ATOM    615  CD  LYS A  84      17.831  18.394  11.437  1.00 50.75           C  
ATOM    616  CE  LYS A  84      16.993  19.667  11.489  1.00 56.53           C  
ATOM    617  NZ  LYS A  84      17.798  20.915  11.463  1.00 60.48           N  
ATOM    618  N   ILE A  85      20.231  14.834   7.725  1.00 39.89           N  
ATOM    619  CA  ILE A  85      20.762  13.510   7.422  1.00 40.76           C  
ATOM    620  C   ILE A  85      22.056  13.611   6.609  1.00 41.69           C  
ATOM    621  O   ILE A  85      23.029  12.931   6.924  1.00 40.16           O  
ATOM    622  CB  ILE A  85      19.713  12.589   6.735  1.00 42.76           C  
ATOM    623  CG1 ILE A  85      18.672  12.193   7.791  1.00 42.63           C  
ATOM    624  CG2 ILE A  85      20.391  11.389   6.049  1.00 43.85           C  
ATOM    625  CD1 ILE A  85      17.617  11.240   7.330  1.00 48.88           C  
ATOM    626  N   TRP A  86      22.063  14.446   5.571  1.00 39.85           N  
ATOM    627  CA  TRP A  86      23.261  14.675   4.774  1.00 39.72           C  
ATOM    628  C   TRP A  86      24.388  15.291   5.625  1.00 39.53           C  
ATOM    629  O   TRP A  86      25.547  14.878   5.508  1.00 41.24           O  
ATOM    630  CB  TRP A  86      22.941  15.562   3.561  1.00 40.21           C  
ATOM    631  CG  TRP A  86      22.224  14.780   2.467  1.00 42.08           C  
ATOM    632  CD1 TRP A  86      22.427  13.480   2.102  1.00 45.81           C  
ATOM    633  CD2 TRP A  86      21.229  15.301   1.581  1.00 42.91           C  
ATOM    634  NE1 TRP A  86      21.593  13.148   1.035  1.00 47.34           N  
ATOM    635  CE2 TRP A  86      20.870  14.264   0.688  1.00 44.73           C  
ATOM    636  CE3 TRP A  86      20.626  16.564   1.440  1.00 45.83           C  
ATOM    637  CZ2 TRP A  86      19.902  14.440  -0.311  1.00 45.94           C  
ATOM    638  CZ3 TRP A  86      19.688  16.742   0.435  1.00 44.46           C  
ATOM    639  CH2 TRP A  86      19.329  15.677  -0.428  1.00 44.99           C  
ATOM    640  N   HIS A  87      24.073  16.262   6.487  1.00 38.32           N  
ATOM    641  CA  HIS A  87      25.105  16.869   7.324  1.00 38.44           C  
ATOM    642  C   HIS A  87      25.756  15.825   8.217  1.00 39.02           C  
ATOM    643  O   HIS A  87      26.982  15.789   8.388  1.00 40.99           O  
ATOM    644  CB  HIS A  87      24.486  17.959   8.200  1.00 39.62           C  
ATOM    645  CG  HIS A  87      25.494  18.799   8.924  1.00 42.00           C  
ATOM    646  ND1 HIS A  87      25.948  18.508  10.193  1.00 46.46           N  
ATOM    647  CD2 HIS A  87      26.112  19.941   8.554  1.00 39.11           C  
ATOM    648  CE1 HIS A  87      26.809  19.438  10.574  1.00 45.07           C  
ATOM    649  NE2 HIS A  87      26.927  20.320   9.595  1.00 42.82           N  
ATOM    650  N   HIS A  88      24.909  15.010   8.833  1.00 39.11           N  
ATOM    651  CA  HIS A  88      25.360  13.919   9.696  1.00 40.97           C  
ATOM    652  C   HIS A  88      26.210  12.943   8.892  1.00 41.24           C  
ATOM    653  O   HIS A  88      27.254  12.476   9.383  1.00 42.47           O  
ATOM    654  CB  HIS A  88      24.166  13.174  10.289  1.00 40.89           C  
ATOM    655  CG  HIS A  88      24.566  12.063  11.209  1.00 40.55           C  
ATOM    656  ND1 HIS A  88      25.049  12.294  12.477  1.00 42.56           N  
ATOM    657  CD2 HIS A  88      24.547  10.718  11.048  1.00 40.31           C  
ATOM    658  CE1 HIS A  88      25.331  11.144  13.058  1.00 42.26           C  
ATOM    659  NE2 HIS A  88      25.035  10.173  12.212  1.00 40.89           N  
ATOM    660  N   THR A  89      25.774  12.651   7.664  1.00 41.86           N  
ATOM    661  CA  THR A  89      26.519  11.749   6.789  1.00 42.85           C  
ATOM    662  C   THR A  89      27.927  12.290   6.519  1.00 41.98           C  
ATOM    663  O   THR A  89      28.929  11.628   6.788  1.00 41.41           O  
ATOM    664  CB  THR A  89      25.757  11.463   5.451  1.00 43.36           C  
ATOM    665  OG1 THR A  89      24.421  11.004   5.709  1.00 42.38           O  
ATOM    666  CG2 THR A  89      26.528  10.463   4.591  1.00 45.16           C  
ATOM    667  N   PHE A  90      28.034  13.509   6.001  1.00 40.96           N  
ATOM    668  CA  PHE A  90      29.350  14.076   5.745  1.00 41.52           C  
ATOM    669  C   PHE A  90      30.210  14.241   7.002  1.00 42.37           C  
ATOM    670  O   PHE A  90      31.349  13.748   7.087  1.00 43.16           O  
ATOM    671  CB  PHE A  90      29.198  15.455   5.104  1.00 41.29           C  
ATOM    672  CG  PHE A  90      28.558  15.432   3.770  1.00 47.34           C  
ATOM    673  CD1 PHE A  90      29.010  14.554   2.788  1.00 49.64           C  
ATOM    674  CD2 PHE A  90      27.545  16.336   3.458  1.00 46.19           C  
ATOM    675  CE1 PHE A  90      28.450  14.568   1.531  1.00 54.03           C  
ATOM    676  CE2 PHE A  90      26.998  16.354   2.200  1.00 48.32           C  
ATOM    677  CZ  PHE A  90      27.431  15.458   1.246  1.00 52.36           C  
ATOM    678  N   TYR A  91      29.678  14.965   7.983  1.00 42.20           N  
ATOM    679  CA  TYR A  91      30.513  15.405   9.102  1.00 42.02           C  
ATOM    680  C   TYR A  91      30.747  14.366  10.195  1.00 42.70           C  
ATOM    681  O   TYR A  91      31.822  14.329  10.795  1.00 41.14           O  
ATOM    682  CB  TYR A  91      29.956  16.706   9.693  1.00 43.03           C  
ATOM    683  CG  TYR A  91      30.107  17.892   8.752  1.00 44.81           C  
ATOM    684  CD1 TYR A  91      31.286  18.623   8.719  1.00 48.33           C  
ATOM    685  CD2 TYR A  91      29.087  18.254   7.886  1.00 49.89           C  
ATOM    686  CE1 TYR A  91      31.444  19.696   7.858  1.00 50.21           C  
ATOM    687  CE2 TYR A  91      29.236  19.324   7.012  1.00 49.79           C  
ATOM    688  CZ  TYR A  91      30.416  20.035   7.007  1.00 48.86           C  
ATOM    689  OH  TYR A  91      30.561  21.102   6.162  1.00 49.26           O  
ATOM    690  N   ASN A  92      29.732  13.569  10.499  1.00 40.15           N  
ATOM    691  CA  ASN A  92      29.766  12.622  11.602  1.00 43.41           C  
ATOM    692  C   ASN A  92      30.131  11.189  11.278  1.00 44.01           C  
ATOM    693  O   ASN A  92      30.873  10.544  12.044  1.00 45.71           O  
ATOM    694  CB  ASN A  92      28.445  12.664  12.373  1.00 44.67           C  
ATOM    695  CG  ASN A  92      28.245  14.011  13.033  1.00 49.89           C  
ATOM    696  OD1 ASN A  92      27.183  14.628  12.945  1.00 56.87           O  
ATOM    697  ND2 ASN A  92      29.315  14.515  13.628  1.00 53.52           N  
ATOM    698  N   GLU A  93      29.593  10.702  10.168  1.00 43.53           N  
ATOM    699  CA  GLU A  93      29.777   9.333   9.727  1.00 43.52           C  
ATOM    700  C   GLU A  93      31.039   9.157   8.863  1.00 43.44           C  
ATOM    701  O   GLU A  93      31.899   8.359   9.208  1.00 45.68           O  
ATOM    702  CB  GLU A  93      28.511   8.874   9.000  1.00 45.59           C  
ATOM    703  CG  GLU A  93      27.304   8.821   9.933  1.00 43.77           C  
ATOM    704  CD  GLU A  93      27.299   7.565  10.799  1.00 56.34           C  
ATOM    705  OE1 GLU A  93      27.963   6.571  10.419  1.00 55.59           O  
ATOM    706  OE2 GLU A  93      26.607   7.559  11.844  1.00 53.47           O  
ATOM    707  N   LEU A  94      31.183   9.931   7.787  1.00 41.25           N  
ATOM    708  CA  LEU A  94      32.324   9.801   6.882  1.00 39.06           C  
ATOM    709  C   LEU A  94      33.473  10.687   7.344  1.00 39.98           C  
ATOM    710  O   LEU A  94      34.633  10.395   7.044  1.00 40.37           O  
ATOM    711  CB  LEU A  94      31.927  10.145   5.433  1.00 38.62           C  
ATOM    712  CG  LEU A  94      30.818   9.295   4.766  1.00 37.49           C  
ATOM    713  CD1 LEU A  94      30.598   9.729   3.328  1.00 41.05           C  
ATOM    714  CD2 LEU A  94      31.238   7.823   4.806  1.00 44.38           C  
ATOM    715  N   ARG A  95      33.142  11.735   8.104  1.00 39.02           N  
ATOM    716  CA  ARG A  95      34.121  12.696   8.632  1.00 40.25           C  
ATOM    717  C   ARG A  95      34.922  13.335   7.506  1.00 40.33           C  
ATOM    718  O   ARG A  95      36.149  13.403   7.551  1.00 40.80           O  
ATOM    719  CB  ARG A  95      35.061  12.037   9.654  1.00 40.37           C  
ATOM    720  CG  ARG A  95      34.321  11.407  10.825  1.00 41.09           C  
ATOM    721  CD  ARG A  95      35.301  10.660  11.712  1.00 52.36           C  
ATOM    722  NE  ARG A  95      34.671  10.301  12.974  1.00 57.83           N  
ATOM    723  CZ  ARG A  95      34.957  10.888  14.132  1.00 59.36           C  
ATOM    724  NH1 ARG A  95      35.868  11.855  14.183  1.00 59.95           N  
ATOM    725  NH2 ARG A  95      34.341  10.493  15.240  1.00 60.19           N  
ATOM    726  N   VAL A  96      34.210  13.813   6.495  1.00 42.26           N  
ATOM    727  CA  VAL A  96      34.824  14.551   5.388  1.00 43.87           C  
ATOM    728  C   VAL A  96      34.290  15.983   5.368  1.00 44.85           C  
ATOM    729  O   VAL A  96      33.239  16.258   5.961  1.00 45.68           O  
ATOM    730  CB  VAL A  96      34.444  13.883   4.054  1.00 44.01           C  
ATOM    731  CG1 VAL A  96      34.902  12.446   4.046  1.00 43.86           C  
ATOM    732  CG2 VAL A  96      32.938  13.913   3.886  1.00 42.29           C  
ATOM    733  N   ALA A  97      35.009  16.883   4.692  1.00 45.02           N  
ATOM    734  CA  ALA A  97      34.473  18.187   4.311  1.00 44.50           C  
ATOM    735  C   ALA A  97      33.873  18.060   2.909  1.00 44.91           C  
ATOM    736  O   ALA A  97      34.574  17.693   1.964  1.00 46.24           O  
ATOM    737  CB  ALA A  97      35.556  19.266   4.362  1.00 43.85           C  
ATOM    738  N   PRO A  98      32.568  18.339   2.775  1.00 45.21           N  
ATOM    739  CA  PRO A  98      31.849  18.080   1.521  1.00 45.42           C  
ATOM    740  C   PRO A  98      32.338  18.959   0.374  1.00 45.16           C  
ATOM    741  O   PRO A  98      32.250  18.552  -0.784  1.00 45.60           O  
ATOM    742  CB  PRO A  98      30.377  18.343   1.862  1.00 44.42           C  
ATOM    743  CG  PRO A  98      30.340  18.882   3.251  1.00 44.08           C  
ATOM    744  CD  PRO A  98      31.711  18.896   3.839  1.00 47.16           C  
ATOM    745  N   GLU A  99      32.899  20.131   0.669  1.00 44.93           N  
ATOM    746  CA  GLU A  99      33.411  20.962  -0.422  1.00 45.40           C  
ATOM    747  C   GLU A  99      34.670  20.398  -1.092  1.00 44.85           C  
ATOM    748  O   GLU A  99      35.149  20.957  -2.085  1.00 43.64           O  
ATOM    749  CB  GLU A  99      33.623  22.422  -0.007  1.00 45.81           C  
ATOM    750  CG  GLU A  99      34.581  22.636   1.133  1.00 52.08           C  
ATOM    751  CD  GLU A  99      33.847  22.693   2.458  1.00 58.96           C  
ATOM    752  OE1 GLU A  99      33.592  23.817   2.942  1.00 68.14           O  
ATOM    753  OE2 GLU A  99      33.513  21.627   3.009  1.00 52.67           O  
ATOM    754  N   GLU A 100      35.187  19.288  -0.567  1.00 43.95           N  
ATOM    755  CA  GLU A 100      36.422  18.680  -1.069  1.00 43.15           C  
ATOM    756  C   GLU A 100      36.196  17.440  -1.946  1.00 42.13           C  
ATOM    757  O   GLU A 100      37.146  16.849  -2.474  1.00 41.01           O  
ATOM    758  CB  GLU A 100      37.323  18.315   0.111  1.00 41.65           C  
ATOM    759  CG  GLU A 100      37.830  19.533   0.868  1.00 48.15           C  
ATOM    760  CD  GLU A 100      38.679  19.145   2.059  1.00 52.33           C  
ATOM    761  OE1 GLU A 100      38.885  17.924   2.246  1.00 53.20           O  
ATOM    762  OE2 GLU A 100      39.139  20.049   2.799  1.00 55.47           O  
ATOM    763  N   HIS A 101      34.933  17.060  -2.122  1.00 42.40           N  
ATOM    764  CA  HIS A 101      34.616  15.766  -2.706  1.00 43.08           C  
ATOM    765  C   HIS A 101      33.491  15.842  -3.727  1.00 43.20           C  
ATOM    766  O   HIS A 101      32.385  16.260  -3.387  1.00 44.33           O  
ATOM    767  CB  HIS A 101      34.184  14.777  -1.614  1.00 43.51           C  
ATOM    768  CG  HIS A 101      35.258  14.468  -0.615  1.00 45.25           C  
ATOM    769  ND1 HIS A 101      36.215  13.499  -0.825  1.00 46.82           N  
ATOM    770  CD2 HIS A 101      35.537  15.017   0.591  1.00 46.75           C  
ATOM    771  CE1 HIS A 101      37.035  13.462   0.210  1.00 49.27           C  
ATOM    772  NE2 HIS A 101      36.646  14.374   1.082  1.00 46.49           N  
ATOM    773  N   PRO A 102      33.746  15.387  -4.962  1.00 43.58           N  
ATOM    774  CA  PRO A 102      32.579  15.158  -5.815  1.00 44.07           C  
ATOM    775  C   PRO A 102      31.661  14.119  -5.155  1.00 44.77           C  
ATOM    776  O   PRO A 102      32.151  13.157  -4.558  1.00 44.54           O  
ATOM    777  CB  PRO A 102      33.191  14.589  -7.096  1.00 43.47           C  
ATOM    778  CG  PRO A 102      34.637  15.134  -7.095  1.00 45.37           C  
ATOM    779  CD  PRO A 102      35.013  15.072  -5.645  1.00 44.06           C  
ATOM    780  N   THR A 103      30.344  14.306  -5.262  1.00 44.74           N  
ATOM    781  CA  THR A 103      29.371  13.465  -4.554  1.00 44.18           C  
ATOM    782  C   THR A 103      28.339  12.863  -5.504  1.00 44.35           C  
ATOM    783  O   THR A 103      27.702  13.585  -6.260  1.00 45.53           O  
ATOM    784  CB  THR A 103      28.684  14.223  -3.396  1.00 45.56           C  
ATOM    785  OG1 THR A 103      29.692  14.674  -2.463  1.00 45.85           O  
ATOM    786  CG2 THR A 103      27.764  13.312  -2.629  1.00 45.90           C  
ATOM    787  N   LEU A 104      28.244  11.538  -5.507  1.00 41.85           N  
ATOM    788  CA  LEU A 104      27.187  10.840  -6.236  1.00 42.25           C  
ATOM    789  C   LEU A 104      26.040  10.528  -5.270  1.00 41.91           C  
ATOM    790  O   LEU A 104      26.236   9.919  -4.195  1.00 42.09           O  
ATOM    791  CB  LEU A 104      27.727   9.575  -6.925  1.00 41.10           C  
ATOM    792  CG  LEU A 104      26.722   8.831  -7.817  1.00 43.05           C  
ATOM    793  CD1 LEU A 104      27.434   8.106  -8.946  1.00 46.05           C  
ATOM    794  CD2 LEU A 104      25.895   7.829  -6.995  1.00 47.68           C  
ATOM    795  N   LEU A 105      24.837  10.957  -5.646  1.00 43.34           N  
ATOM    796  CA  LEU A 105      23.625  10.653  -4.896  1.00 42.28           C  
ATOM    797  C   LEU A 105      22.736   9.749  -5.757  1.00 42.78           C  
ATOM    798  O   LEU A 105      22.926   9.636  -6.951  1.00 43.31           O  
ATOM    799  CB  LEU A 105      22.856  11.919  -4.514  1.00 42.31           C  
ATOM    800  CG  LEU A 105      23.531  12.999  -3.639  1.00 46.98           C  
ATOM    801  CD1 LEU A 105      22.619  14.198  -3.463  1.00 49.43           C  
ATOM    802  CD2 LEU A 105      23.885  12.456  -2.273  1.00 44.42           C  
ATOM    803  N   THR A 106      21.793   9.071  -5.129  1.00 44.24           N  
ATOM    804  CA  THR A 106      20.941   8.127  -5.846  1.00 42.65           C  
ATOM    805  C   THR A 106      19.527   8.653  -5.659  1.00 44.10           C  
ATOM    806  O   THR A 106      19.275   9.414  -4.718  1.00 44.50           O  
ATOM    807  CB  THR A 106      21.058   6.707  -5.271  1.00 43.55           C  
ATOM    808  OG1 THR A 106      20.396   6.642  -3.990  1.00 43.65           O  
ATOM    809  CG2 THR A 106      22.537   6.215  -5.165  1.00 44.09           C  
ATOM    810  N   GLU A 107      18.613   8.211  -6.517  1.00 41.85           N  
ATOM    811  CA  GLU A 107      17.206   8.573  -6.383  1.00 43.65           C  
ATOM    812  C   GLU A 107      16.309   7.399  -6.777  1.00 42.33           C  
ATOM    813  O   GLU A 107      16.718   6.445  -7.481  1.00 42.43           O  
ATOM    814  CB  GLU A 107      16.891   9.782  -7.290  1.00 42.34           C  
ATOM    815  CG  GLU A 107      16.859   9.478  -8.785  1.00 44.86           C  
ATOM    816  CD  GLU A 107      16.389  10.694  -9.633  1.00 49.01           C  
ATOM    817  OE1 GLU A 107      16.355  11.827  -9.114  1.00 49.64           O  
ATOM    818  OE2 GLU A 107      16.066  10.534 -10.822  1.00 49.44           O  
ATOM    819  N   ALA A 108      15.056   7.480  -6.335  1.00 41.36           N  
ATOM    820  CA  ALA A 108      14.103   6.416  -6.586  1.00 42.03           C  
ATOM    821  C   ALA A 108      13.637   6.487  -8.039  1.00 42.77           C  
ATOM    822  O   ALA A 108      13.699   7.545  -8.667  1.00 42.57           O  
ATOM    823  CB  ALA A 108      12.895   6.597  -5.652  1.00 43.86           C  
ATOM    824  N   PRO A 109      13.182   5.349  -8.586  1.00 42.99           N  
ATOM    825  CA  PRO A 109      12.496   5.293  -9.882  1.00 42.54           C  
ATOM    826  C   PRO A 109      11.328   6.270  -9.835  1.00 43.36           C  
ATOM    827  O   PRO A 109      10.668   6.382  -8.800  1.00 42.89           O  
ATOM    828  CB  PRO A 109      11.920   3.874  -9.921  1.00 43.84           C  
ATOM    829  CG  PRO A 109      12.843   3.075  -9.046  1.00 43.74           C  
ATOM    830  CD  PRO A 109      13.300   4.024  -7.953  1.00 44.41           C  
ATOM    831  N   LEU A 110      11.108   7.008 -10.924  1.00 40.83           N  
ATOM    832  CA  LEU A 110      10.009   7.967 -10.964  1.00 39.36           C  
ATOM    833  C   LEU A 110      10.121   9.158 -10.000  1.00 40.08           C  
ATOM    834  O   LEU A 110       9.144   9.814  -9.715  1.00 38.96           O  
ATOM    835  CB  LEU A 110       8.665   7.246 -10.790  1.00 39.02           C  
ATOM    836  CG  LEU A 110       8.403   6.053 -11.714  1.00 43.41           C  
ATOM    837  CD1 LEU A 110       7.053   5.373 -11.411  1.00 41.95           C  
ATOM    838  CD2 LEU A 110       8.425   6.592 -13.137  1.00 42.73           C  
ATOM    839  N   ASN A 111      11.321   9.509  -9.560  1.00 38.39           N  
ATOM    840  CA  ASN A 111      11.498  10.689  -8.714  1.00 40.67           C  
ATOM    841  C   ASN A 111      11.163  11.922  -9.550  1.00 43.94           C  
ATOM    842  O   ASN A 111      11.682  12.072 -10.663  1.00 41.95           O  
ATOM    843  CB  ASN A 111      12.952  10.763  -8.262  1.00 39.90           C  
ATOM    844  CG  ASN A 111      13.163  11.769  -7.139  1.00 42.08           C  
ATOM    845  OD1 ASN A 111      12.280  11.976  -6.317  1.00 43.92           O  
ATOM    846  ND2 ASN A 111      14.317  12.424  -7.128  1.00 41.95           N  
ATOM    847  N   PRO A 112      10.266  12.789  -9.055  1.00 43.37           N  
ATOM    848  CA  PRO A 112       9.940  13.963  -9.857  1.00 43.04           C  
ATOM    849  C   PRO A 112      11.160  14.840 -10.162  1.00 41.99           C  
ATOM    850  O   PRO A 112      12.056  14.988  -9.344  1.00 39.90           O  
ATOM    851  CB  PRO A 112       8.961  14.731  -8.961  1.00 43.78           C  
ATOM    852  CG  PRO A 112       8.314  13.673  -8.138  1.00 43.78           C  
ATOM    853  CD  PRO A 112       9.470  12.737  -7.817  1.00 41.56           C  
ATOM    854  N   LYS A 113      11.183  15.455 -11.336  1.00 42.12           N  
ATOM    855  CA  LYS A 113      12.288  16.326 -11.700  1.00 43.06           C  
ATOM    856  C   LYS A 113      12.518  17.443 -10.675  1.00 39.46           C  
ATOM    857  O   LYS A 113      13.659  17.815 -10.404  1.00 40.39           O  
ATOM    858  CB  LYS A 113      12.038  16.898 -13.106  1.00 42.26           C  
ATOM    859  CG  LYS A 113      13.055  17.938 -13.543  1.00 47.76           C  
ATOM    860  CD  LYS A 113      12.720  18.594 -14.892  1.00 48.67           C  
ATOM    861  CE  LYS A 113      11.498  19.511 -14.799  1.00 57.20           C  
ATOM    862  NZ  LYS A 113      10.263  18.855 -15.356  1.00 56.91           N  
ATOM    863  N   ALA A 114      11.447  17.997 -10.108  1.00 39.50           N  
ATOM    864  CA  ALA A 114      11.584  19.090  -9.134  1.00 39.44           C  
ATOM    865  C   ALA A 114      12.325  18.624  -7.888  1.00 39.02           C  
ATOM    866  O   ALA A 114      13.031  19.397  -7.237  1.00 38.44           O  
ATOM    867  CB  ALA A 114      10.216  19.664  -8.761  1.00 40.52           C  
ATOM    868  N   ASN A 115      12.144  17.356  -7.546  1.00 39.41           N  
ATOM    869  CA  ASN A 115      12.831  16.743  -6.388  1.00 39.87           C  
ATOM    870  C   ASN A 115      14.330  16.644  -6.696  1.00 39.08           C  
ATOM    871  O   ASN A 115      15.158  17.060  -5.898  1.00 40.27           O  
ATOM    872  CB  ASN A 115      12.249  15.340  -6.192  1.00 41.68           C  
ATOM    873  CG  ASN A 115      12.593  14.722  -4.857  1.00 48.05           C  
ATOM    874  OD1 ASN A 115      13.744  14.345  -4.607  1.00 52.52           O  
ATOM    875  ND2 ASN A 115      11.572  14.564  -4.004  1.00 48.45           N  
ATOM    876  N   ARG A 116      14.696  16.075  -7.845  1.00 40.79           N  
ATOM    877  CA  ARG A 116      16.106  16.038  -8.244  1.00 42.05           C  
ATOM    878  C   ARG A 116      16.760  17.422  -8.280  1.00 41.18           C  
ATOM    879  O   ARG A 116      17.911  17.577  -7.849  1.00 43.84           O  
ATOM    880  CB  ARG A 116      16.317  15.340  -9.596  1.00 43.71           C  
ATOM    881  CG  ARG A 116      17.817  15.181  -9.867  1.00 49.78           C  
ATOM    882  CD  ARG A 116      18.122  14.690 -11.279  1.00 54.23           C  
ATOM    883  NE  ARG A 116      17.864  13.261 -11.411  1.00 55.13           N  
ATOM    884  CZ  ARG A 116      18.419  12.476 -12.339  1.00 58.17           C  
ATOM    885  NH1 ARG A 116      19.307  12.986 -13.196  1.00 52.49           N  
ATOM    886  NH2 ARG A 116      18.116  11.178 -12.390  1.00 56.19           N  
ATOM    887  N   GLU A 117      16.038  18.436  -8.763  1.00 42.66           N  
ATOM    888  CA  GLU A 117      16.566  19.799  -8.788  1.00 42.50           C  
ATOM    889  C   GLU A 117      16.813  20.354  -7.384  1.00 42.20           C  
ATOM    890  O   GLU A 117      17.759  21.104  -7.159  1.00 41.06           O  
ATOM    891  CB  GLU A 117      15.636  20.731  -9.593  1.00 44.10           C  
ATOM    892  CG  GLU A 117      15.567  20.376 -11.066  1.00 43.89           C  
ATOM    893  CD  GLU A 117      14.390  21.018 -11.793  1.00 50.09           C  
ATOM    894  OE1 GLU A 117      13.535  21.652 -11.129  1.00 59.00           O  
ATOM    895  OE2 GLU A 117      14.333  20.899 -13.040  1.00 58.62           O  
ATOM    896  N   LYS A 118      15.958  20.001  -6.432  1.00 42.56           N  
ATOM    897  CA  LYS A 118      16.126  20.464  -5.045  1.00 43.75           C  
ATOM    898  C   LYS A 118      17.319  19.767  -4.385  1.00 43.57           C  
ATOM    899  O   LYS A 118      18.087  20.392  -3.655  1.00 44.64           O  
ATOM    900  CB  LYS A 118      14.848  20.196  -4.241  1.00 43.51           C  
ATOM    901  CG  LYS A 118      14.890  20.589  -2.771  1.00 45.62           C  
ATOM    902  CD  LYS A 118      14.353  21.972  -2.537  1.00 48.34           C  
ATOM    903  CE  LYS A 118      14.466  22.361  -1.068  1.00 50.39           C  
ATOM    904  NZ  LYS A 118      14.730  23.818  -0.990  1.00 58.63           N  
ATOM    905  N   MET A 119      17.464  18.467  -4.630  1.00 43.48           N  
ATOM    906  CA AMET A 119      18.626  17.719  -4.160  0.60 43.18           C  
ATOM    907  CA BMET A 119      18.621  17.721  -4.171  0.40 45.26           C  
ATOM    908  C   MET A 119      19.901  18.413  -4.636  1.00 43.71           C  
ATOM    909  O   MET A 119      20.823  18.665  -3.855  1.00 42.15           O  
ATOM    910  CB AMET A 119      18.601  16.271  -4.674  0.60 44.21           C  
ATOM    911  CB BMET A 119      18.560  16.312  -4.751  0.40 45.62           C  
ATOM    912  CG AMET A 119      17.441  15.406  -4.172  0.60 40.92           C  
ATOM    913  CG BMET A 119      19.622  15.373  -4.241  0.40 47.54           C  
ATOM    914  SD AMET A 119      17.298  13.828  -5.045  0.60 44.13           S  
ATOM    915  SD BMET A 119      19.727  13.913  -5.293  0.40 51.99           S  
ATOM    916  CE AMET A 119      18.800  12.983  -4.515  0.60 46.18           C  
ATOM    917  CE BMET A 119      18.007  13.437  -5.426  0.40 49.07           C  
ATOM    918  N   THR A 120      19.935  18.746  -5.922  1.00 41.05           N  
ATOM    919  CA  THR A 120      21.088  19.381  -6.551  1.00 41.56           C  
ATOM    920  C   THR A 120      21.366  20.766  -5.961  1.00 42.37           C  
ATOM    921  O   THR A 120      22.516  21.095  -5.631  1.00 42.26           O  
ATOM    922  CB  THR A 120      20.851  19.467  -8.070  1.00 41.16           C  
ATOM    923  OG1 THR A 120      20.696  18.139  -8.593  1.00 42.25           O  
ATOM    924  CG2 THR A 120      22.013  20.159  -8.770  1.00 44.17           C  
ATOM    925  N   GLN A 121      20.321  21.581  -5.825  1.00 42.03           N  
ATOM    926  CA  GLN A 121      20.470  22.886  -5.203  1.00 43.39           C  
ATOM    927  C   GLN A 121      21.093  22.812  -3.804  1.00 42.52           C  
ATOM    928  O   GLN A 121      22.006  23.571  -3.482  1.00 43.23           O  
ATOM    929  CB  GLN A 121      19.109  23.557  -5.102  1.00 44.80           C  
ATOM    930  CG  GLN A 121      19.158  24.943  -4.500  1.00 53.46           C  
ATOM    931  CD  GLN A 121      17.854  25.261  -3.822  1.00 62.81           C  
ATOM    932  OE1 GLN A 121      16.868  25.606  -4.478  1.00 63.52           O  
ATOM    933  NE2 GLN A 121      17.823  25.094  -2.499  1.00 66.71           N  
ATOM    934  N   ILE A 122      20.584  21.913  -2.967  1.00 41.74           N  
ATOM    935  CA  ILE A 122      21.093  21.770  -1.602  1.00 43.02           C  
ATOM    936  C   ILE A 122      22.566  21.369  -1.595  1.00 42.53           C  
ATOM    937  O   ILE A 122      23.360  21.944  -0.860  1.00 42.85           O  
ATOM    938  CB  ILE A 122      20.246  20.756  -0.803  1.00 42.93           C  
ATOM    939  CG1 ILE A 122      18.863  21.359  -0.525  1.00 46.55           C  
ATOM    940  CG2 ILE A 122      20.944  20.361   0.538  1.00 42.47           C  
ATOM    941  CD1 ILE A 122      17.812  20.308  -0.089  1.00 50.14           C  
ATOM    942  N   MET A 123      22.931  20.389  -2.415  1.00 42.87           N  
ATOM    943  CA  MET A 123      24.321  19.924  -2.468  1.00 43.33           C  
ATOM    944  C   MET A 123      25.277  21.050  -2.862  1.00 43.91           C  
ATOM    945  O   MET A 123      26.337  21.225  -2.253  1.00 43.89           O  
ATOM    946  CB  MET A 123      24.466  18.750  -3.437  1.00 41.30           C  
ATOM    947  CG  MET A 123      23.901  17.435  -2.894  1.00 46.18           C  
ATOM    948  SD  MET A 123      24.903  16.924  -1.488  1.00 46.68           S  
ATOM    949  CE  MET A 123      23.657  16.421  -0.328  1.00 45.73           C  
ATOM    950  N   PHE A 124      24.894  21.829  -3.870  1.00 42.80           N  
ATOM    951  CA  PHE A 124      25.769  22.901  -4.336  1.00 42.58           C  
ATOM    952  C   PHE A 124      25.779  24.122  -3.427  1.00 42.85           C  
ATOM    953  O   PHE A 124      26.833  24.706  -3.197  1.00 43.03           O  
ATOM    954  CB  PHE A 124      25.419  23.340  -5.756  1.00 42.46           C  
ATOM    955  CG  PHE A 124      25.920  22.412  -6.816  1.00 44.38           C  
ATOM    956  CD1 PHE A 124      27.269  22.108  -6.909  1.00 47.74           C  
ATOM    957  CD2 PHE A 124      25.052  21.882  -7.747  1.00 45.73           C  
ATOM    958  CE1 PHE A 124      27.730  21.253  -7.899  1.00 47.70           C  
ATOM    959  CE2 PHE A 124      25.507  21.030  -8.746  1.00 48.53           C  
ATOM    960  CZ  PHE A 124      26.850  20.721  -8.818  1.00 45.84           C  
ATOM    961  N   GLU A 125      24.614  24.487  -2.906  1.00 42.73           N  
ATOM    962  CA  GLU A 125      24.457  25.744  -2.198  1.00 45.91           C  
ATOM    963  C   GLU A 125      24.626  25.614  -0.692  1.00 46.03           C  
ATOM    964  O   GLU A 125      25.140  26.521  -0.031  1.00 45.76           O  
ATOM    965  CB  GLU A 125      23.092  26.350  -2.519  1.00 46.14           C  
ATOM    966  CG  GLU A 125      22.938  26.699  -3.987  1.00 50.80           C  
ATOM    967  CD  GLU A 125      21.747  27.596  -4.221  1.00 56.61           C  
ATOM    968  OE1 GLU A 125      21.079  27.927  -3.212  1.00 59.34           O  
ATOM    969  OE2 GLU A 125      21.488  27.954  -5.393  1.00 55.52           O  
ATOM    970  N   THR A 126      24.180  24.497  -0.135  1.00 44.80           N  
ATOM    971  CA  THR A 126      24.319  24.302   1.304  1.00 45.12           C  
ATOM    972  C   THR A 126      25.637  23.621   1.629  1.00 44.69           C  
ATOM    973  O   THR A 126      26.331  24.019   2.556  1.00 42.41           O  
ATOM    974  CB  THR A 126      23.155  23.501   1.929  1.00 46.30           C  
ATOM    975  OG1 THR A 126      21.935  24.241   1.780  1.00 49.92           O  
ATOM    976  CG2 THR A 126      23.403  23.275   3.420  1.00 48.37           C  
ATOM    977  N   PHE A 127      25.983  22.582   0.883  1.00 44.58           N  
ATOM    978  CA  PHE A 127      27.179  21.813   1.201  1.00 43.68           C  
ATOM    979  C   PHE A 127      28.403  22.186   0.382  1.00 44.96           C  
ATOM    980  O   PHE A 127      29.511  21.741   0.682  1.00 44.94           O  
ATOM    981  CB  PHE A 127      26.870  20.328   1.118  1.00 44.02           C  
ATOM    982  CG  PHE A 127      25.871  19.890   2.157  1.00 44.36           C  
ATOM    983  CD1 PHE A 127      26.221  19.873   3.494  1.00 46.21           C  
ATOM    984  CD2 PHE A 127      24.576  19.548   1.802  1.00 45.12           C  
ATOM    985  CE1 PHE A 127      25.307  19.461   4.467  1.00 46.03           C  
ATOM    986  CE2 PHE A 127      23.657  19.150   2.764  1.00 47.14           C  
ATOM    987  CZ  PHE A 127      24.027  19.116   4.101  1.00 43.27           C  
ATOM    988  N   ASN A 128      28.202  23.010  -0.641  1.00 43.95           N  
ATOM    989  CA  ASN A 128      29.313  23.477  -1.460  1.00 43.85           C  
ATOM    990  C   ASN A 128      30.154  22.371  -2.096  1.00 43.23           C  
ATOM    991  O   ASN A 128      31.348  22.545  -2.282  1.00 43.13           O  
ATOM    992  CB  ASN A 128      30.201  24.430  -0.658  1.00 44.65           C  
ATOM    993  CG  ASN A 128      29.515  25.746  -0.381  1.00 50.99           C  
ATOM    994  OD1 ASN A 128      29.341  26.567  -1.290  1.00 57.78           O  
ATOM    995  ND2 ASN A 128      29.120  25.960   0.873  1.00 55.37           N  
ATOM    996  N   VAL A 129      29.532  21.272  -2.510  1.00 42.17           N  
ATOM    997  CA  VAL A 129      30.283  20.204  -3.169  1.00 42.56           C  
ATOM    998  C   VAL A 129      30.820  20.746  -4.506  1.00 43.15           C  
ATOM    999  O   VAL A 129      30.222  21.655  -5.092  1.00 42.75           O  
ATOM   1000  CB  VAL A 129      29.441  18.922  -3.379  1.00 43.29           C  
ATOM   1001  CG1 VAL A 129      28.782  18.404  -2.071  1.00 43.47           C  
ATOM   1002  CG2 VAL A 129      28.414  19.141  -4.450  1.00 43.35           C  
ATOM   1003  N   PRO A 130      31.981  20.238  -4.969  1.00 43.57           N  
ATOM   1004  CA  PRO A 130      32.580  20.790  -6.186  1.00 42.55           C  
ATOM   1005  C   PRO A 130      31.951  20.236  -7.467  1.00 42.75           C  
ATOM   1006  O   PRO A 130      32.002  20.872  -8.530  1.00 39.96           O  
ATOM   1007  CB  PRO A 130      34.059  20.397  -6.057  1.00 42.77           C  
ATOM   1008  CG  PRO A 130      34.065  19.166  -5.191  1.00 42.22           C  
ATOM   1009  CD  PRO A 130      32.787  19.145  -4.393  1.00 42.68           C  
ATOM   1010  N   ALA A 131      31.357  19.057  -7.354  1.00 42.76           N  
ATOM   1011  CA  ALA A 131      30.669  18.404  -8.460  1.00 43.52           C  
ATOM   1012  C   ALA A 131      29.666  17.431  -7.862  1.00 44.48           C  
ATOM   1013  O   ALA A 131      29.822  16.990  -6.713  1.00 43.94           O  
ATOM   1014  CB  ALA A 131      31.661  17.656  -9.322  1.00 43.49           C  
ATOM   1015  N   MET A 132      28.632  17.088  -8.624  1.00 43.57           N  
ATOM   1016  CA  MET A 132      27.756  16.018  -8.198  1.00 44.69           C  
ATOM   1017  C   MET A 132      27.084  15.296  -9.359  1.00 44.08           C  
ATOM   1018  O   MET A 132      27.181  15.711 -10.507  1.00 40.83           O  
ATOM   1019  CB  MET A 132      26.751  16.443  -7.118  1.00 47.44           C  
ATOM   1020  CG  MET A 132      25.916  17.673  -7.370  1.00 49.83           C  
ATOM   1021  SD  MET A 132      24.238  17.284  -7.887  1.00 68.71           S  
ATOM   1022  CE  MET A 132      23.677  16.092  -6.676  1.00 55.45           C  
ATOM   1023  N   TYR A 133      26.435  14.195  -9.035  1.00 43.21           N  
ATOM   1024  CA  TYR A 133      25.726  13.421 -10.030  1.00 45.48           C  
ATOM   1025  C   TYR A 133      24.557  12.750  -9.340  1.00 43.97           C  
ATOM   1026  O   TYR A 133      24.691  12.366  -8.173  1.00 45.00           O  
ATOM   1027  CB  TYR A 133      26.666  12.375 -10.620  1.00 47.44           C  
ATOM   1028  CG  TYR A 133      26.062  11.652 -11.805  1.00 51.77           C  
ATOM   1029  CD1 TYR A 133      26.051  12.243 -13.073  1.00 52.17           C  
ATOM   1030  CD2 TYR A 133      25.508  10.387 -11.656  1.00 51.87           C  
ATOM   1031  CE1 TYR A 133      25.495  11.589 -14.160  1.00 55.33           C  
ATOM   1032  CE2 TYR A 133      24.953   9.716 -12.740  1.00 51.98           C  
ATOM   1033  CZ  TYR A 133      24.952  10.328 -13.988  1.00 54.26           C  
ATOM   1034  OH  TYR A 133      24.395   9.660 -15.065  1.00 54.44           O  
ATOM   1035  N   VAL A 134      23.406  12.634 -10.017  1.00 41.20           N  
ATOM   1036  CA  VAL A 134      22.312  11.852  -9.431  1.00 43.78           C  
ATOM   1037  C   VAL A 134      22.009  10.680 -10.337  1.00 42.58           C  
ATOM   1038  O   VAL A 134      21.775  10.868 -11.532  1.00 43.79           O  
ATOM   1039  CB  VAL A 134      21.009  12.659  -9.145  1.00 44.73           C  
ATOM   1040  CG1 VAL A 134      19.947  11.754  -8.477  1.00 44.29           C  
ATOM   1041  CG2 VAL A 134      21.298  13.885  -8.267  1.00 44.92           C  
ATOM   1042  N   ALA A 135      22.011   9.484  -9.765  1.00 42.06           N  
ATOM   1043  CA  ALA A 135      21.733   8.257 -10.505  1.00 43.78           C  
ATOM   1044  C   ALA A 135      20.471   7.567 -10.009  1.00 43.23           C  
ATOM   1045  O   ALA A 135      20.117   7.648  -8.834  1.00 44.67           O  
ATOM   1046  CB  ALA A 135      22.925   7.295 -10.377  1.00 45.16           C  
ATOM   1047  N   ILE A 136      19.814   6.833 -10.891  1.00 39.64           N  
ATOM   1048  CA  ILE A 136      18.641   6.076 -10.494  1.00 41.46           C  
ATOM   1049  C   ILE A 136      19.109   4.787  -9.807  1.00 42.04           C  
ATOM   1050  O   ILE A 136      19.948   4.052 -10.359  1.00 40.26           O  
ATOM   1051  CB  ILE A 136      17.828   5.702 -11.778  1.00 40.77           C  
ATOM   1052  CG1 ILE A 136      17.369   6.989 -12.486  1.00 45.80           C  
ATOM   1053  CG2 ILE A 136      16.651   4.796 -11.450  1.00 41.59           C  
ATOM   1054  CD1 ILE A 136      16.681   6.704 -13.822  1.00 42.94           C  
ATOM   1055  N   GLN A 137      18.554   4.515  -8.630  1.00 41.63           N  
ATOM   1056  CA  GLN A 137      18.975   3.343  -7.835  1.00 41.82           C  
ATOM   1057  C   GLN A 137      18.957   2.039  -8.639  1.00 41.49           C  
ATOM   1058  O   GLN A 137      19.972   1.342  -8.700  1.00 40.76           O  
ATOM   1059  CB  GLN A 137      18.118   3.218  -6.578  1.00 41.99           C  
ATOM   1060  CG  GLN A 137      18.453   4.363  -5.638  1.00 41.07           C  
ATOM   1061  CD  GLN A 137      17.287   4.864  -4.818  1.00 46.00           C  
ATOM   1062  OE1 GLN A 137      17.416   5.874  -4.088  1.00 51.25           O  
ATOM   1063  NE2 GLN A 137      16.157   4.196  -4.927  1.00 39.65           N  
ATOM   1064  N   ALA A 138      17.833   1.693  -9.267  1.00 39.02           N  
ATOM   1065  CA  ALA A 138      17.772   0.435 -10.055  1.00 38.36           C  
ATOM   1066  C   ALA A 138      18.806   0.330 -11.192  1.00 39.20           C  
ATOM   1067  O   ALA A 138      19.327  -0.745 -11.500  1.00 38.07           O  
ATOM   1068  CB  ALA A 138      16.336   0.232 -10.605  1.00 36.46           C  
ATOM   1069  N   VAL A 139      19.116   1.440 -11.852  1.00 38.16           N  
ATOM   1070  CA  VAL A 139      20.125   1.424 -12.922  1.00 36.74           C  
ATOM   1071  C   VAL A 139      21.487   1.116 -12.350  1.00 38.42           C  
ATOM   1072  O   VAL A 139      22.294   0.418 -12.991  1.00 37.08           O  
ATOM   1073  CB  VAL A 139      20.129   2.792 -13.671  1.00 36.50           C  
ATOM   1074  CG1 VAL A 139      21.250   2.907 -14.670  1.00 41.00           C  
ATOM   1075  CG2 VAL A 139      18.721   2.973 -14.373  1.00 37.57           C  
ATOM   1076  N   LEU A 140      21.769   1.645 -11.154  1.00 37.85           N  
ATOM   1077  CA  LEU A 140      23.030   1.301 -10.475  1.00 36.69           C  
ATOM   1078  C   LEU A 140      23.163  -0.174 -10.098  1.00 36.68           C  
ATOM   1079  O   LEU A 140      24.244  -0.757 -10.266  1.00 36.73           O  
ATOM   1080  CB  LEU A 140      23.299   2.200  -9.254  1.00 35.88           C  
ATOM   1081  CG  LEU A 140      23.554   3.693  -9.508  1.00 38.81           C  
ATOM   1082  CD1 LEU A 140      23.737   4.418  -8.146  1.00 35.13           C  
ATOM   1083  CD2 LEU A 140      24.783   3.902 -10.429  1.00 38.70           C  
ATOM   1084  N   SER A 141      22.088  -0.762  -9.566  1.00 38.36           N  
ATOM   1085  CA  SER A 141      22.061  -2.181  -9.264  1.00 41.23           C  
ATOM   1086  C   SER A 141      22.327  -2.983 -10.523  1.00 40.38           C  
ATOM   1087  O   SER A 141      23.100  -3.935 -10.480  1.00 40.13           O  
ATOM   1088  CB  SER A 141      20.666  -2.567  -8.741  1.00 43.38           C  
ATOM   1089  OG  SER A 141      20.595  -2.138  -7.399  1.00 51.17           O  
ATOM   1090  N   LEU A 142      21.657  -2.638 -11.627  1.00 38.46           N  
ATOM   1091  CA  LEU A 142      21.903  -3.374 -12.891  1.00 38.77           C  
ATOM   1092  C   LEU A 142      23.364  -3.267 -13.304  1.00 38.74           C  
ATOM   1093  O   LEU A 142      24.024  -4.264 -13.628  1.00 39.10           O  
ATOM   1094  CB  LEU A 142      20.986  -2.867 -14.028  1.00 39.54           C  
ATOM   1095  CG  LEU A 142      21.026  -3.779 -15.274  1.00 38.51           C  
ATOM   1096  CD1 LEU A 142      20.348  -5.073 -14.874  1.00 37.14           C  
ATOM   1097  CD2 LEU A 142      20.281  -3.103 -16.449  1.00 40.78           C  
ATOM   1098  N   TYR A 143      23.894  -2.049 -13.254  1.00 39.41           N  
ATOM   1099  CA  TYR A 143      25.279  -1.800 -13.627  1.00 39.27           C  
ATOM   1100  C   TYR A 143      26.233  -2.635 -12.768  1.00 40.17           C  
ATOM   1101  O   TYR A 143      27.206  -3.195 -13.251  1.00 38.80           O  
ATOM   1102  CB  TYR A 143      25.531  -0.319 -13.409  1.00 40.56           C  
ATOM   1103  CG  TYR A 143      26.890   0.166 -13.807  1.00 45.92           C  
ATOM   1104  CD1 TYR A 143      27.272   0.224 -15.144  1.00 49.09           C  
ATOM   1105  CD2 TYR A 143      27.787   0.590 -12.834  1.00 45.70           C  
ATOM   1106  CE1 TYR A 143      28.536   0.679 -15.492  1.00 52.24           C  
ATOM   1107  CE2 TYR A 143      29.020   1.043 -13.161  1.00 50.58           C  
ATOM   1108  CZ  TYR A 143      29.403   1.079 -14.479  1.00 49.82           C  
ATOM   1109  OH  TYR A 143      30.665   1.550 -14.746  1.00 49.78           O  
ATOM   1110  N   ALA A 144      25.944  -2.722 -11.480  1.00 38.07           N  
ATOM   1111  CA  ALA A 144      26.776  -3.502 -10.571  1.00 40.56           C  
ATOM   1112  C   ALA A 144      26.850  -4.985 -10.978  1.00 41.86           C  
ATOM   1113  O   ALA A 144      27.868  -5.637 -10.731  1.00 40.91           O  
ATOM   1114  CB  ALA A 144      26.275  -3.372  -9.132  1.00 40.76           C  
ATOM   1115  N   SER A 145      25.772  -5.524 -11.546  1.00 42.29           N  
ATOM   1116  CA  SER A 145      25.721  -6.910 -12.019  1.00 42.31           C  
ATOM   1117  C   SER A 145      26.374  -7.095 -13.387  1.00 44.14           C  
ATOM   1118  O   SER A 145      26.369  -8.200 -13.915  1.00 43.34           O  
ATOM   1119  CB  SER A 145      24.279  -7.425 -12.125  1.00 42.05           C  
ATOM   1120  OG  SER A 145      23.645  -6.882 -13.276  1.00 45.84           O  
ATOM   1121  N   GLY A 146      26.897  -6.023 -13.972  1.00 42.93           N  
ATOM   1122  CA  GLY A 146      27.623  -6.097 -15.227  1.00 45.48           C  
ATOM   1123  C   GLY A 146      26.733  -6.137 -16.459  1.00 46.62           C  
ATOM   1124  O   GLY A 146      27.158  -6.597 -17.511  1.00 44.77           O  
ATOM   1125  N   ARG A 147      25.495  -5.665 -16.329  1.00 43.97           N  
ATOM   1126  CA  ARG A 147      24.552  -5.690 -17.434  1.00 46.55           C  
ATOM   1127  C   ARG A 147      24.048  -4.279 -17.712  1.00 44.34           C  
ATOM   1128  O   ARG A 147      24.039  -3.435 -16.806  1.00 44.00           O  
ATOM   1129  CB  ARG A 147      23.308  -6.499 -17.050  1.00 45.82           C  
ATOM   1130  CG  ARG A 147      23.580  -7.922 -16.866  1.00 49.44           C  
ATOM   1131  CD  ARG A 147      22.483  -8.511 -16.015  1.00 44.55           C  
ATOM   1132  NE  ARG A 147      22.660  -9.942 -16.126  1.00 47.33           N  
ATOM   1133  CZ  ARG A 147      23.461 -10.658 -15.363  1.00 44.41           C  
ATOM   1134  NH1 ARG A 147      24.137 -10.084 -14.359  1.00 44.36           N  
ATOM   1135  NH2 ARG A 147      23.571 -11.955 -15.608  1.00 45.87           N  
ATOM   1136  N   THR A 148      23.654  -4.028 -18.964  1.00 47.17           N  
ATOM   1137  CA  THR A 148      22.903  -2.802 -19.292  1.00 44.90           C  
ATOM   1138  C   THR A 148      21.459  -3.051 -19.742  1.00 43.04           C  
ATOM   1139  O   THR A 148      20.674  -2.100 -19.850  1.00 41.50           O  
ATOM   1140  CB  THR A 148      23.599  -1.912 -20.357  1.00 47.52           C  
ATOM   1141  OG1 THR A 148      23.854  -2.709 -21.522  1.00 46.72           O  
ATOM   1142  CG2 THR A 148      24.888  -1.306 -19.794  1.00 50.13           C  
ATOM   1143  N   THR A 149      21.089  -4.308 -19.983  1.00 39.98           N  
ATOM   1144  CA  THR A 149      19.672  -4.643 -20.175  1.00 38.92           C  
ATOM   1145  C   THR A 149      19.151  -5.674 -19.159  1.00 38.57           C  
ATOM   1146  O   THR A 149      19.781  -6.727 -18.972  1.00 37.97           O  
ATOM   1147  CB  THR A 149      19.411  -5.134 -21.631  1.00 41.46           C  
ATOM   1148  OG1 THR A 149      19.676  -4.051 -22.543  1.00 39.28           O  
ATOM   1149  CG2 THR A 149      17.969  -5.597 -21.772  1.00 41.29           C  
ATOM   1150  N   GLY A 150      18.020  -5.397 -18.508  1.00 36.34           N  
ATOM   1151  CA  GLY A 150      17.440  -6.394 -17.629  1.00 33.83           C  
ATOM   1152  C   GLY A 150      16.311  -5.728 -16.856  1.00 36.01           C  
ATOM   1153  O   GLY A 150      16.027  -4.562 -17.075  1.00 34.51           O  
ATOM   1154  N   ILE A 151      15.685  -6.448 -15.943  1.00 34.12           N  
ATOM   1155  CA  ILE A 151      14.571  -5.853 -15.152  1.00 36.05           C  
ATOM   1156  C   ILE A 151      14.957  -6.051 -13.701  1.00 36.24           C  
ATOM   1157  O   ILE A 151      15.276  -7.144 -13.272  1.00 36.77           O  
ATOM   1158  CB  ILE A 151      13.193  -6.463 -15.441  1.00 36.04           C  
ATOM   1159  CG1 ILE A 151      12.110  -5.856 -14.512  1.00 37.49           C  
ATOM   1160  CG2 ILE A 151      13.225  -8.034 -15.366  1.00 36.33           C  
ATOM   1161  CD1 ILE A 151      10.667  -6.114 -15.005  1.00 36.67           C  
ATOM   1162  N   VAL A 152      14.959  -4.963 -12.941  1.00 37.49           N  
ATOM   1163  CA  VAL A 152      15.479  -5.019 -11.590  1.00 36.84           C  
ATOM   1164  C   VAL A 152      14.259  -5.126 -10.671  1.00 37.34           C  
ATOM   1165  O   VAL A 152      13.256  -4.405 -10.842  1.00 37.26           O  
ATOM   1166  CB  VAL A 152      16.273  -3.714 -11.289  1.00 35.00           C  
ATOM   1167  CG1 VAL A 152      16.498  -3.560  -9.716  1.00 37.13           C  
ATOM   1168  CG2 VAL A 152      17.643  -3.708 -12.035  1.00 37.76           C  
ATOM   1169  N   LEU A 153      14.306  -6.051  -9.713  1.00 36.02           N  
ATOM   1170  CA  LEU A 153      13.331  -6.004  -8.614  1.00 39.09           C  
ATOM   1171  C   LEU A 153      14.093  -5.393  -7.436  1.00 37.80           C  
ATOM   1172  O   LEU A 153      15.060  -6.005  -6.968  1.00 37.09           O  
ATOM   1173  CB  LEU A 153      12.914  -7.418  -8.217  1.00 37.25           C  
ATOM   1174  CG  LEU A 153      12.062  -7.431  -6.922  1.00 43.31           C  
ATOM   1175  CD1 LEU A 153      10.660  -6.894  -7.187  1.00 44.71           C  
ATOM   1176  CD2 LEU A 153      12.025  -8.820  -6.237  1.00 45.27           C  
ATOM   1177  N   ASP A 154      13.719  -4.194  -6.988  1.00 35.55           N  
ATOM   1178  CA  ASP A 154      14.459  -3.537  -5.874  1.00 38.10           C  
ATOM   1179  C   ASP A 154      13.471  -3.445  -4.705  1.00 37.94           C  
ATOM   1180  O   ASP A 154      12.404  -2.856  -4.854  1.00 38.75           O  
ATOM   1181  CB  ASP A 154      14.901  -2.135  -6.299  1.00 40.00           C  
ATOM   1182  CG  ASP A 154      15.930  -1.498  -5.328  1.00 50.70           C  
ATOM   1183  OD1 ASP A 154      16.170  -2.033  -4.216  1.00 56.39           O  
ATOM   1184  OD2 ASP A 154      16.486  -0.419  -5.661  1.00 53.31           O  
ATOM   1185  N   SER A 155      13.796  -4.022  -3.543  1.00 36.60           N  
ATOM   1186  CA  SER A 155      12.820  -4.031  -2.441  1.00 35.29           C  
ATOM   1187  C   SER A 155      13.635  -3.704  -1.189  1.00 34.10           C  
ATOM   1188  O   SER A 155      14.632  -4.387  -0.942  1.00 37.47           O  
ATOM   1189  CB  SER A 155      12.224  -5.429  -2.306  1.00 36.54           C  
ATOM   1190  OG  SER A 155      11.207  -5.412  -1.301  1.00 36.17           O  
ATOM   1191  N   GLY A 156      13.296  -2.624  -0.494  1.00 33.94           N  
ATOM   1192  CA  GLY A 156      14.106  -2.123   0.612  1.00 34.59           C  
ATOM   1193  C   GLY A 156      13.251  -2.148   1.858  1.00 34.87           C  
ATOM   1194  O   GLY A 156      12.676  -3.166   2.204  1.00 37.94           O  
ATOM   1195  N   ASP A 157      13.247  -1.049   2.587  1.00 36.37           N  
ATOM   1196  CA  ASP A 157      12.547  -0.989   3.862  1.00 35.11           C  
ATOM   1197  C   ASP A 157      11.149  -0.424   3.664  1.00 35.84           C  
ATOM   1198  O   ASP A 157      10.264  -0.700   4.479  1.00 35.62           O  
ATOM   1199  CB  ASP A 157      13.288  -0.070   4.805  1.00 32.74           C  
ATOM   1200  CG  ASP A 157      12.747  -0.126   6.239  1.00 39.67           C  
ATOM   1201  OD1 ASP A 157      12.746  -1.228   6.845  1.00 42.68           O  
ATOM   1202  OD2 ASP A 157      12.289   0.918   6.761  1.00 41.10           O  
ATOM   1203  N   GLY A 158      10.988   0.458   2.676  1.00 33.35           N  
ATOM   1204  CA  GLY A 158       9.719   1.193   2.509  1.00 33.93           C  
ATOM   1205  C   GLY A 158       8.954   0.937   1.201  1.00 35.39           C  
ATOM   1206  O   GLY A 158       7.725   1.110   1.141  1.00 37.23           O  
ATOM   1207  N   VAL A 159       9.656   0.539   0.163  1.00 33.96           N  
ATOM   1208  CA  VAL A 159       9.042   0.404  -1.165  1.00 34.94           C  
ATOM   1209  C   VAL A 159       9.677  -0.715  -1.987  1.00 34.55           C  
ATOM   1210  O   VAL A 159      10.855  -1.084  -1.799  1.00 35.01           O  
ATOM   1211  CB  VAL A 159       9.059   1.765  -1.914  1.00 33.48           C  
ATOM   1212  CG1 VAL A 159      10.482   2.190  -2.300  1.00 35.57           C  
ATOM   1213  CG2 VAL A 159       8.164   1.723  -3.210  1.00 36.90           C  
ATOM   1214  N   THR A 160       8.892  -1.295  -2.894  1.00 33.84           N  
ATOM   1215  CA  THR A 160       9.404  -2.292  -3.838  1.00 34.46           C  
ATOM   1216  C   THR A 160       9.046  -1.777  -5.251  1.00 35.66           C  
ATOM   1217  O   THR A 160       7.935  -1.296  -5.497  1.00 36.81           O  
ATOM   1218  CB  THR A 160       8.755  -3.671  -3.578  1.00 34.46           C  
ATOM   1219  OG1 THR A 160       9.166  -4.137  -2.280  1.00 38.55           O  
ATOM   1220  CG2 THR A 160       9.100  -4.719  -4.660  1.00 35.84           C  
ATOM   1221  N   HIS A 161      10.026  -1.782  -6.135  1.00 35.23           N  
ATOM   1222  CA  HIS A 161       9.772  -1.425  -7.537  1.00 38.84           C  
ATOM   1223  C   HIS A 161      10.258  -2.534  -8.477  1.00 37.22           C  
ATOM   1224  O   HIS A 161      11.250  -3.249  -8.182  1.00 38.14           O  
ATOM   1225  CB  HIS A 161      10.609  -0.203  -7.906  1.00 37.71           C  
ATOM   1226  CG  HIS A 161      10.098   1.097  -7.362  1.00 39.88           C  
ATOM   1227  ND1 HIS A 161      10.686   1.717  -6.278  1.00 40.79           N  
ATOM   1228  CD2 HIS A 161       9.101   1.916  -7.775  1.00 41.19           C  
ATOM   1229  CE1 HIS A 161      10.047   2.850  -6.020  1.00 42.75           C  
ATOM   1230  NE2 HIS A 161       9.091   2.996  -6.924  1.00 43.15           N  
ATOM   1231  N   ASN A 162       9.590  -2.633  -9.633  1.00 36.87           N  
ATOM   1232  CA AASN A 162      10.152  -3.312 -10.789  0.50 37.15           C  
ATOM   1233  CA BASN A 162      10.131  -3.331 -10.786  0.50 37.41           C  
ATOM   1234  C   ASN A 162      10.562  -2.278 -11.815  1.00 38.27           C  
ATOM   1235  O   ASN A 162       9.774  -1.409 -12.184  1.00 37.72           O  
ATOM   1236  CB AASN A 162       9.134  -4.249 -11.448  0.50 36.88           C  
ATOM   1237  CB BASN A 162       9.081  -4.271 -11.418  0.50 37.40           C  
ATOM   1238  CG AASN A 162       9.059  -5.578 -10.767  0.50 37.76           C  
ATOM   1239  CG BASN A 162       8.323  -5.105 -10.389  0.50 38.53           C  
ATOM   1240  OD1AASN A 162       8.100  -5.864 -10.042  0.50 39.34           O  
ATOM   1241  OD1BASN A 162       8.801  -6.159  -9.960  0.50 45.38           O  
ATOM   1242  ND2AASN A 162      10.093  -6.395 -10.959  0.50 34.80           N  
ATOM   1243  ND2BASN A 162       7.115  -4.667 -10.024  0.50 38.28           N  
ATOM   1244  N   VAL A 163      11.806  -2.365 -12.282  1.00 36.32           N  
ATOM   1245  CA  VAL A 163      12.283  -1.374 -13.204  1.00 35.77           C  
ATOM   1246  C   VAL A 163      12.948  -2.034 -14.411  1.00 36.53           C  
ATOM   1247  O   VAL A 163      14.070  -2.511 -14.310  1.00 36.10           O  
ATOM   1248  CB  VAL A 163      13.301  -0.430 -12.556  1.00 34.97           C  
ATOM   1249  CG1 VAL A 163      13.613   0.740 -13.548  1.00 35.39           C  
ATOM   1250  CG2 VAL A 163      12.760   0.088 -11.197  1.00 39.33           C  
ATOM   1251  N   PRO A 164      12.239  -2.071 -15.551  1.00 37.49           N  
ATOM   1252  CA  PRO A 164      12.888  -2.571 -16.740  1.00 35.84           C  
ATOM   1253  C   PRO A 164      13.835  -1.522 -17.321  1.00 35.75           C  
ATOM   1254  O   PRO A 164      13.529  -0.307 -17.394  1.00 36.12           O  
ATOM   1255  CB  PRO A 164      11.717  -2.913 -17.698  1.00 36.93           C  
ATOM   1256  CG  PRO A 164      10.459  -2.383 -17.047  1.00 40.13           C  
ATOM   1257  CD  PRO A 164      10.841  -1.650 -15.778  1.00 40.27           C  
ATOM   1258  N   ILE A 165      15.002  -2.009 -17.723  1.00 34.73           N  
ATOM   1259  CA  ILE A 165      16.056  -1.132 -18.233  1.00 34.58           C  
ATOM   1260  C   ILE A 165      16.564  -1.671 -19.553  1.00 35.34           C  
ATOM   1261  O   ILE A 165      16.897  -2.842 -19.649  1.00 36.10           O  
ATOM   1262  CB  ILE A 165      17.247  -1.086 -17.211  1.00 33.82           C  
ATOM   1263  CG1 ILE A 165      16.714  -0.451 -15.922  1.00 34.94           C  
ATOM   1264  CG2 ILE A 165      18.458  -0.285 -17.774  1.00 35.14           C  
ATOM   1265  CD1 ILE A 165      17.546  -0.767 -14.659  1.00 37.54           C  
ATOM   1266  N   TYR A 166      16.615  -0.820 -20.588  1.00 35.27           N  
ATOM   1267  CA  TYR A 166      17.004  -1.270 -21.920  1.00 37.24           C  
ATOM   1268  C   TYR A 166      18.243  -0.468 -22.318  1.00 36.69           C  
ATOM   1269  O   TYR A 166      18.162   0.759 -22.390  1.00 36.56           O  
ATOM   1270  CB  TYR A 166      15.846  -1.012 -22.927  1.00 36.51           C  
ATOM   1271  CG  TYR A 166      16.264  -1.251 -24.358  1.00 38.60           C  
ATOM   1272  CD1 TYR A 166      16.735  -2.501 -24.760  1.00 41.54           C  
ATOM   1273  CD2 TYR A 166      16.243  -0.220 -25.303  1.00 39.16           C  
ATOM   1274  CE1 TYR A 166      17.156  -2.731 -26.042  1.00 37.56           C  
ATOM   1275  CE2 TYR A 166      16.668  -0.441 -26.600  1.00 36.30           C  
ATOM   1276  CZ  TYR A 166      17.130  -1.691 -26.970  1.00 38.39           C  
ATOM   1277  OH  TYR A 166      17.560  -1.924 -28.269  1.00 37.91           O  
ATOM   1278  N   GLU A 167      19.376  -1.139 -22.552  1.00 36.74           N  
ATOM   1279  CA  GLU A 167      20.637  -0.495 -22.886  1.00 38.14           C  
ATOM   1280  C   GLU A 167      20.874   0.709 -21.987  1.00 37.66           C  
ATOM   1281  O   GLU A 167      21.244   1.794 -22.461  1.00 37.64           O  
ATOM   1282  CB  GLU A 167      20.695  -0.097 -24.371  1.00 37.01           C  
ATOM   1283  CG  GLU A 167      20.317  -1.235 -25.286  1.00 43.80           C  
ATOM   1284  CD  GLU A 167      21.442  -2.233 -25.481  1.00 55.42           C  
ATOM   1285  OE1 GLU A 167      22.566  -2.001 -24.968  1.00 57.91           O  
ATOM   1286  OE2 GLU A 167      21.205  -3.250 -26.164  1.00 61.47           O  
ATOM   1287  N   GLY A 168      20.683   0.505 -20.685  1.00 36.52           N  
ATOM   1288  CA  GLY A 168      21.009   1.532 -19.674  1.00 36.78           C  
ATOM   1289  C   GLY A 168      19.896   2.550 -19.441  1.00 39.18           C  
ATOM   1290  O   GLY A 168      20.030   3.421 -18.595  1.00 38.96           O  
ATOM   1291  N   TYR A 169      18.795   2.429 -20.182  1.00 37.14           N  
ATOM   1292  CA  TYR A 169      17.685   3.398 -20.127  1.00 39.26           C  
ATOM   1293  C   TYR A 169      16.560   2.788 -19.319  1.00 36.54           C  
ATOM   1294  O   TYR A 169      15.907   1.850 -19.792  1.00 36.31           O  
ATOM   1295  CB  TYR A 169      17.137   3.748 -21.548  1.00 39.68           C  
ATOM   1296  CG  TYR A 169      16.375   5.070 -21.579  1.00 40.63           C  
ATOM   1297  CD2 TYR A 169      16.931   6.209 -22.152  1.00 42.61           C  
ATOM   1298  CD1 TYR A 169      15.118   5.170 -21.012  1.00 39.66           C  
ATOM   1299  CE2 TYR A 169      16.244   7.433 -22.131  1.00 43.25           C  
ATOM   1300  CE1 TYR A 169      14.433   6.373 -20.953  1.00 40.95           C  
ATOM   1301  CZ  TYR A 169      15.015   7.498 -21.503  1.00 43.46           C  
ATOM   1302  OH  TYR A 169      14.351   8.692 -21.405  1.00 41.90           O  
ATOM   1303  N   ALA A 170      16.292   3.304 -18.126  1.00 36.08           N  
ATOM   1304  CA  ALA A 170      15.132   2.821 -17.353  1.00 36.28           C  
ATOM   1305  C   ALA A 170      13.830   3.323 -18.007  1.00 39.02           C  
ATOM   1306  O   ALA A 170      13.683   4.516 -18.316  1.00 39.12           O  
ATOM   1307  CB  ALA A 170      15.202   3.327 -15.933  1.00 37.97           C  
ATOM   1308  N   LEU A 171      12.909   2.411 -18.286  1.00 35.74           N  
ATOM   1309  CA  LEU A 171      11.721   2.764 -19.038  1.00 35.18           C  
ATOM   1310  C   LEU A 171      10.589   3.149 -18.099  1.00 37.37           C  
ATOM   1311  O   LEU A 171       9.968   2.268 -17.510  1.00 34.94           O  
ATOM   1312  CB  LEU A 171      11.291   1.568 -19.894  1.00 36.04           C  
ATOM   1313  CG  LEU A 171      12.362   1.100 -20.888  1.00 35.88           C  
ATOM   1314  CD1 LEU A 171      11.993  -0.253 -21.532  1.00 37.63           C  
ATOM   1315  CD2 LEU A 171      12.547   2.120 -22.018  1.00 39.46           C  
ATOM   1316  N   PRO A 172      10.308   4.457 -17.965  1.00 36.45           N  
ATOM   1317  CA  PRO A 172       9.414   4.788 -16.845  1.00 39.79           C  
ATOM   1318  C   PRO A 172       7.967   4.364 -17.057  1.00 39.96           C  
ATOM   1319  O   PRO A 172       7.265   4.117 -16.059  1.00 38.37           O  
ATOM   1320  CB  PRO A 172       9.531   6.317 -16.716  1.00 41.59           C  
ATOM   1321  CG  PRO A 172       9.982   6.780 -18.026  1.00 41.34           C  
ATOM   1322  CD  PRO A 172      10.760   5.654 -18.697  1.00 40.03           C  
ATOM   1323  N   HIS A 173       7.519   4.240 -18.314  1.00 37.68           N  
ATOM   1324  CA  HIS A 173       6.132   3.795 -18.529  1.00 37.33           C  
ATOM   1325  C   HIS A 173       5.864   2.377 -17.975  1.00 37.37           C  
ATOM   1326  O   HIS A 173       4.700   1.989 -17.742  1.00 39.84           O  
ATOM   1327  CB  HIS A 173       5.749   3.844 -20.022  1.00 36.88           C  
ATOM   1328  CG  HIS A 173       6.434   2.791 -20.834  1.00 38.69           C  
ATOM   1329  ND1 HIS A 173       7.763   2.877 -21.193  1.00 39.09           N  
ATOM   1330  CD2 HIS A 173       5.988   1.613 -21.332  1.00 43.45           C  
ATOM   1331  CE1 HIS A 173       8.091   1.830 -21.928  1.00 41.78           C  
ATOM   1332  NE2 HIS A 173       7.046   1.031 -21.992  1.00 44.39           N  
ATOM   1333  N   ALA A 174       6.925   1.603 -17.772  1.00 37.15           N  
ATOM   1334  CA  ALA A 174       6.806   0.180 -17.412  1.00 36.07           C  
ATOM   1335  C   ALA A 174       7.208  -0.097 -15.968  1.00 37.52           C  
ATOM   1336  O   ALA A 174       7.151  -1.247 -15.492  1.00 36.71           O  
ATOM   1337  CB  ALA A 174       7.704  -0.684 -18.325  1.00 36.07           C  
ATOM   1338  N   ILE A 175       7.608   0.948 -15.265  1.00 34.74           N  
ATOM   1339  CA  ILE A 175       7.991   0.797 -13.851  1.00 36.73           C  
ATOM   1340  C   ILE A 175       6.766   0.548 -12.998  1.00 38.81           C  
ATOM   1341  O   ILE A 175       5.740   1.207 -13.193  1.00 39.00           O  
ATOM   1342  CB  ILE A 175       8.688   2.083 -13.388  1.00 35.00           C  
ATOM   1343  CG1 ILE A 175      10.075   2.130 -14.030  1.00 38.71           C  
ATOM   1344  CG2 ILE A 175       8.941   2.022 -11.857  1.00 35.96           C  
ATOM   1345  CD1 ILE A 175      10.815   3.431 -13.701  1.00 39.86           C  
ATOM   1346  N   MET A 176       6.831  -0.431 -12.089  1.00 38.56           N  
ATOM   1347  CA  MET A 176       5.722  -0.724 -11.183  1.00 40.91           C  
ATOM   1348  C   MET A 176       6.228  -0.436  -9.754  1.00 41.03           C  
ATOM   1349  O   MET A 176       7.394  -0.687  -9.445  1.00 39.32           O  
ATOM   1350  CB  MET A 176       5.360  -2.215 -11.236  1.00 40.11           C  
ATOM   1351  CG  MET A 176       5.041  -2.721 -12.632  1.00 45.90           C  
ATOM   1352  SD  MET A 176       3.399  -2.157 -13.057  1.00 50.01           S  
ATOM   1353  CE  MET A 176       3.401  -2.598 -14.817  1.00 49.87           C  
ATOM   1354  N   ARG A 177       5.353   0.110  -8.925  1.00 42.65           N  
ATOM   1355  CA  ARG A 177       5.682   0.434  -7.530  1.00 43.05           C  
ATOM   1356  C   ARG A 177       4.714  -0.333  -6.656  1.00 46.14           C  
ATOM   1357  O   ARG A 177       3.486  -0.277  -6.897  1.00 44.25           O  
ATOM   1358  CB  ARG A 177       5.519   1.938  -7.273  1.00 45.11           C  
ATOM   1359  CG  ARG A 177       5.582   2.367  -5.789  1.00 44.42           C  
ATOM   1360  CD  ARG A 177       5.444   3.866  -5.651  1.00 45.55           C  
ATOM   1361  NE  ARG A 177       5.007   4.258  -4.321  1.00 44.99           N  
ATOM   1362  CZ  ARG A 177       4.824   5.515  -3.926  1.00 55.15           C  
ATOM   1363  NH1 ARG A 177       5.065   6.523  -4.774  1.00 53.04           N  
ATOM   1364  NH2 ARG A 177       4.398   5.756  -2.680  1.00 50.37           N  
ATOM   1365  N   LEU A 178       5.250  -1.006  -5.627  1.00 42.98           N  
ATOM   1366  CA  LEU A 178       4.450  -1.705  -4.612  1.00 42.44           C  
ATOM   1367  C   LEU A 178       4.819  -1.158  -3.220  1.00 40.64           C  
ATOM   1368  O   LEU A 178       5.992  -1.240  -2.832  1.00 38.83           O  
ATOM   1369  CB  LEU A 178       4.707  -3.223  -4.695  1.00 43.49           C  
ATOM   1370  CG  LEU A 178       4.166  -4.126  -3.552  1.00 45.89           C  
ATOM   1371  CD1 LEU A 178       2.623  -4.118  -3.477  1.00 51.41           C  
ATOM   1372  CD2 LEU A 178       4.645  -5.577  -3.652  1.00 48.13           C  
ATOM   1373  N   ASP A 179       3.845  -0.602  -2.490  1.00 40.06           N  
ATOM   1374  CA  ASP A 179       4.140   0.039  -1.211  1.00 41.63           C  
ATOM   1375  C   ASP A 179       4.058  -1.021  -0.107  1.00 40.74           C  
ATOM   1376  O   ASP A 179       3.218  -0.952   0.793  1.00 39.30           O  
ATOM   1377  CB  ASP A 179       3.207   1.238  -0.942  1.00 44.32           C  
ATOM   1378  CG  ASP A 179       3.690   2.519  -1.657  1.00 49.00           C  
ATOM   1379  OD1 ASP A 179       4.762   2.466  -2.306  1.00 52.34           O  
ATOM   1380  OD2 ASP A 179       3.031   3.586  -1.600  1.00 53.51           O  
ATOM   1381  N   LEU A 180       4.909  -2.025  -0.258  1.00 38.18           N  
ATOM   1382  CA ALEU A 180       5.080  -3.079   0.735  0.50 37.16           C  
ATOM   1383  CA BLEU A 180       5.067  -3.129   0.695  0.50 37.93           C  
ATOM   1384  C   LEU A 180       6.548  -3.470   0.680  1.00 37.42           C  
ATOM   1385  O   LEU A 180       7.086  -3.785  -0.380  1.00 38.38           O  
ATOM   1386  CB ALEU A 180       4.202  -4.270   0.375  0.50 38.88           C  
ATOM   1387  CB BLEU A 180       4.269  -4.345   0.209  0.50 40.19           C  
ATOM   1388  CG ALEU A 180       3.983  -5.412   1.348  0.50 32.53           C  
ATOM   1389  CG BLEU A 180       4.598  -5.780   0.611  0.50 40.02           C  
ATOM   1390  CD1ALEU A 180       2.793  -6.229   0.866  0.50 34.62           C  
ATOM   1391  CD1BLEU A 180       4.560  -5.902   2.132  0.50 40.71           C  
ATOM   1392  CD2ALEU A 180       5.270  -6.267   1.379  0.50 31.67           C  
ATOM   1393  CD2BLEU A 180       3.617  -6.749  -0.042  0.50 36.40           C  
ATOM   1394  N   ALA A 181       7.214  -3.397   1.820  1.00 36.46           N  
ATOM   1395  CA  ALA A 181       8.609  -3.841   1.831  1.00 35.06           C  
ATOM   1396  C   ALA A 181       9.015  -4.204   3.257  1.00 35.73           C  
ATOM   1397  O   ALA A 181       8.192  -4.725   3.998  1.00 35.14           O  
ATOM   1398  CB  ALA A 181       9.539  -2.779   1.199  1.00 39.11           C  
ATOM   1399  N   GLY A 182      10.295  -4.056   3.588  1.00 35.21           N  
ATOM   1400  CA  GLY A 182      10.845  -4.675   4.804  1.00 37.95           C  
ATOM   1401  C   GLY A 182      10.156  -4.273   6.091  1.00 37.56           C  
ATOM   1402  O   GLY A 182       9.971  -5.111   6.973  1.00 35.99           O  
ATOM   1403  N   ARG A 183       9.819  -2.999   6.234  1.00 36.26           N  
ATOM   1404  CA  ARG A 183       9.188  -2.561   7.496  1.00 39.93           C  
ATOM   1405  C   ARG A 183       7.826  -3.234   7.675  1.00 38.23           C  
ATOM   1406  O   ARG A 183       7.435  -3.595   8.792  1.00 37.40           O  
ATOM   1407  CB  ARG A 183       9.085  -1.032   7.591  1.00 40.25           C  
ATOM   1408  CG  ARG A 183       7.941  -0.427   6.753  1.00 45.70           C  
ATOM   1409  CD  ARG A 183       7.916   1.118   6.840  1.00 46.91           C  
ATOM   1410  NE  ARG A 183       9.229   1.694   6.514  1.00 49.04           N  
ATOM   1411  CZ  ARG A 183       9.568   2.959   6.742  1.00 50.80           C  
ATOM   1412  NH1 ARG A 183       8.695   3.806   7.284  1.00 46.47           N  
ATOM   1413  NH2 ARG A 183      10.791   3.362   6.448  1.00 48.75           N  
ATOM   1414  N   ASP A 184       7.091  -3.427   6.576  1.00 37.44           N  
ATOM   1415  CA  ASP A 184       5.824  -4.159   6.653  1.00 35.20           C  
ATOM   1416  C   ASP A 184       6.006  -5.613   7.015  1.00 35.11           C  
ATOM   1417  O   ASP A 184       5.136  -6.208   7.651  1.00 35.98           O  
ATOM   1418  CB  ASP A 184       5.059  -4.079   5.330  1.00 36.90           C  
ATOM   1419  CG  ASP A 184       4.864  -2.643   4.875  1.00 38.27           C  
ATOM   1420  OD2 ASP A 184       5.595  -2.208   3.953  1.00 44.39           O  
ATOM   1421  OD1 ASP A 184       4.045  -1.919   5.493  1.00 42.23           O  
ATOM   1422  N   LEU A 185       7.087  -6.219   6.522  1.00 33.86           N  
ATOM   1423  CA  LEU A 185       7.351  -7.632   6.794  1.00 35.80           C  
ATOM   1424  C   LEU A 185       7.715  -7.788   8.278  1.00 34.73           C  
ATOM   1425  O   LEU A 185       7.288  -8.741   8.929  1.00 34.18           O  
ATOM   1426  CB  LEU A 185       8.500  -8.117   5.896  1.00 36.82           C  
ATOM   1427  CG  LEU A 185       8.133  -8.851   4.602  1.00 43.31           C  
ATOM   1428  CD1 LEU A 185       6.813  -8.540   4.003  1.00 41.27           C  
ATOM   1429  CD2 LEU A 185       9.282  -9.046   3.558  1.00 38.58           C  
ATOM   1430  N   THR A 186       8.501  -6.851   8.799  1.00 34.83           N  
ATOM   1431  CA  THR A 186       8.874  -6.885  10.237  1.00 35.05           C  
ATOM   1432  C   THR A 186       7.616  -6.774  11.104  1.00 36.07           C  
ATOM   1433  O   THR A 186       7.431  -7.542  12.058  1.00 36.23           O  
ATOM   1434  CB  THR A 186       9.871  -5.733  10.587  1.00 35.42           C  
ATOM   1435  OG1 THR A 186      11.115  -5.945   9.898  1.00 37.20           O  
ATOM   1436  CG2 THR A 186      10.124  -5.722  12.091  1.00 37.02           C  
ATOM   1437  N   ASP A 187       6.727  -5.854  10.754  1.00 35.68           N  
ATOM   1438  CA  ASP A 187       5.482  -5.681  11.532  1.00 37.37           C  
ATOM   1439  C   ASP A 187       4.588  -6.900  11.442  1.00 36.57           C  
ATOM   1440  O   ASP A 187       3.986  -7.317  12.435  1.00 37.06           O  
ATOM   1441  CB  ASP A 187       4.713  -4.461  11.059  1.00 38.73           C  
ATOM   1442  CG  ASP A 187       5.434  -3.150  11.355  1.00 46.52           C  
ATOM   1443  OD1 ASP A 187       6.449  -3.104  12.097  1.00 51.91           O  
ATOM   1444  OD2 ASP A 187       4.968  -2.131  10.803  1.00 51.71           O  
ATOM   1445  N   TYR A 188       4.531  -7.514  10.270  1.00 36.24           N  
ATOM   1446  CA  TYR A 188       3.713  -8.706  10.112  1.00 36.18           C  
ATOM   1447  C   TYR A 188       4.299  -9.883  10.894  1.00 35.74           C  
ATOM   1448  O   TYR A 188       3.550 -10.658  11.495  1.00 35.18           O  
ATOM   1449  CB  TYR A 188       3.633  -9.070   8.639  1.00 35.01           C  
ATOM   1450  CG  TYR A 188       2.757 -10.270   8.382  1.00 37.47           C  
ATOM   1451  CD1 TYR A 188       1.412 -10.272   8.788  1.00 39.49           C  
ATOM   1452  CD2 TYR A 188       3.250 -11.359   7.704  1.00 39.92           C  
ATOM   1453  CE1 TYR A 188       0.592 -11.368   8.533  1.00 42.89           C  
ATOM   1454  CE2 TYR A 188       2.432 -12.463   7.426  1.00 40.88           C  
ATOM   1455  CZ  TYR A 188       1.120 -12.441   7.853  1.00 39.42           C  
ATOM   1456  OH  TYR A 188       0.320 -13.531   7.601  1.00 43.94           O  
ATOM   1457  N   LEU A 189       5.623 -10.057  10.837  1.00 34.95           N  
ATOM   1458  CA  LEU A 189       6.271 -11.071  11.700  1.00 35.66           C  
ATOM   1459  C   LEU A 189       5.948 -10.848  13.174  1.00 35.50           C  
ATOM   1460  O   LEU A 189       5.670 -11.811  13.906  1.00 34.43           O  
ATOM   1461  CB  LEU A 189       7.808 -11.132  11.482  1.00 35.91           C  
ATOM   1462  CG  LEU A 189       8.493 -12.306  12.248  1.00 35.53           C  
ATOM   1463  CD1 LEU A 189       7.945 -13.663  11.790  1.00 34.11           C  
ATOM   1464  CD2 LEU A 189      10.030 -12.284  12.055  1.00 35.73           C  
ATOM   1465  N   MET A 190       6.013  -9.606  13.638  1.00 35.30           N  
ATOM   1466  CA AMET A 190       5.652  -9.297  15.020  0.50 39.46           C  
ATOM   1467  CA BMET A 190       5.646  -9.289  15.022  0.50 38.41           C  
ATOM   1468  C   MET A 190       4.229  -9.773  15.310  1.00 39.39           C  
ATOM   1469  O   MET A 190       3.968 -10.406  16.336  1.00 35.60           O  
ATOM   1470  CB AMET A 190       5.802  -7.792  15.290  0.50 39.01           C  
ATOM   1471  CB BMET A 190       5.762  -7.782  15.312  0.50 38.08           C  
ATOM   1472  CG AMET A 190       5.489  -7.380  16.719  0.50 43.43           C  
ATOM   1473  CG BMET A 190       7.166  -7.216  15.165  0.50 40.28           C  
ATOM   1474  SD AMET A 190       5.887  -5.659  17.107  0.50 45.29           S  
ATOM   1475  SD BMET A 190       7.416  -5.488  15.687  0.50 41.42           S  
ATOM   1476  CE AMET A 190       6.068  -4.942  15.474  0.50 44.00           C  
ATOM   1477  CE BMET A 190       7.305  -5.693  17.465  0.50 42.99           C  
ATOM   1478  N   LYS A 191       3.317  -9.465  14.403  1.00 39.47           N  
ATOM   1479  CA  LYS A 191       1.915  -9.860  14.556  1.00 38.16           C  
ATOM   1480  C   LYS A 191       1.694 -11.366  14.626  1.00 36.94           C  
ATOM   1481  O   LYS A 191       1.004 -11.879  15.529  1.00 36.37           O  
ATOM   1482  CB  LYS A 191       1.094  -9.277  13.426  1.00 39.77           C  
ATOM   1483  CG  LYS A 191      -0.397  -9.561  13.537  1.00 44.43           C  
ATOM   1484  CD  LYS A 191      -1.131  -9.115  12.253  1.00 49.62           C  
ATOM   1485  CE  LYS A 191      -2.608  -9.540  12.271  1.00 53.18           C  
ATOM   1486  NZ  LYS A 191      -3.414  -9.162  11.044  1.00 50.17           N  
ATOM   1487  N   ILE A 192       2.305 -12.111  13.707  1.00 36.36           N  
ATOM   1488  CA  ILE A 192       2.048 -13.536  13.700  1.00 34.45           C  
ATOM   1489  C   ILE A 192       2.801 -14.256  14.823  1.00 35.57           C  
ATOM   1490  O   ILE A 192       2.314 -15.266  15.303  1.00 35.79           O  
ATOM   1491  CB  ILE A 192       2.286 -14.183  12.312  1.00 36.79           C  
ATOM   1492  CG1 ILE A 192       3.748 -14.072  11.869  1.00 34.52           C  
ATOM   1493  CG2 ILE A 192       1.312 -13.569  11.277  1.00 33.78           C  
ATOM   1494  CD1 ILE A 192       3.943 -14.769  10.498  1.00 36.02           C  
ATOM   1495  N   LEU A 193       3.952 -13.736  15.262  1.00 34.54           N  
ATOM   1496  CA  LEU A 193       4.582 -14.337  16.442  1.00 35.73           C  
ATOM   1497  C   LEU A 193       3.731 -14.107  17.680  1.00 34.72           C  
ATOM   1498  O   LEU A 193       3.608 -14.991  18.554  1.00 34.83           O  
ATOM   1499  CB  LEU A 193       6.014 -13.821  16.653  1.00 34.20           C  
ATOM   1500  CG  LEU A 193       7.038 -14.321  15.606  1.00 35.27           C  
ATOM   1501  CD1 LEU A 193       8.344 -13.552  15.788  1.00 38.30           C  
ATOM   1502  CD2 LEU A 193       7.295 -15.819  15.763  1.00 38.58           C  
ATOM   1503  N   THR A 194       3.121 -12.935  17.734  1.00 33.90           N  
ATOM   1504  CA  THR A 194       2.213 -12.612  18.822  1.00 36.27           C  
ATOM   1505  C   THR A 194       0.978 -13.529  18.835  1.00 37.00           C  
ATOM   1506  O   THR A 194       0.583 -14.064  19.896  1.00 37.54           O  
ATOM   1507  CB  THR A 194       1.879 -11.122  18.824  1.00 38.39           C  
ATOM   1508  OG1 THR A 194       3.102 -10.396  19.042  1.00 40.30           O  
ATOM   1509  CG2 THR A 194       0.928 -10.810  19.994  1.00 40.08           C  
ATOM   1510  N   GLU A 195       0.424 -13.804  17.660  1.00 34.04           N  
ATOM   1511  CA  GLU A 195      -0.678 -14.776  17.550  1.00 34.84           C  
ATOM   1512  C   GLU A 195      -0.300 -16.160  18.049  1.00 35.95           C  
ATOM   1513  O   GLU A 195      -1.135 -16.897  18.577  1.00 35.94           O  
ATOM   1514  CB  GLU A 195      -1.155 -14.883  16.093  1.00 35.83           C  
ATOM   1515  CG  GLU A 195      -1.785 -13.556  15.658  1.00 37.33           C  
ATOM   1516  CD  GLU A 195      -2.428 -13.620  14.281  1.00 45.03           C  
ATOM   1517  OE1 GLU A 195      -2.323 -14.696  13.648  1.00 48.52           O  
ATOM   1518  OE2 GLU A 195      -3.086 -12.620  13.875  1.00 47.07           O  
ATOM   1519  N   ARG A 196       0.953 -16.536  17.829  1.00 36.46           N  
ATOM   1520  CA  ARG A 196       1.422 -17.835  18.282  1.00 35.68           C  
ATOM   1521  C   ARG A 196       1.464 -17.956  19.805  1.00 37.06           C  
ATOM   1522  O   ARG A 196       1.414 -19.064  20.327  1.00 36.45           O  
ATOM   1523  CB  ARG A 196       2.787 -18.149  17.631  1.00 36.15           C  
ATOM   1524  CG  ARG A 196       3.366 -19.516  18.049  1.00 36.97           C  
ATOM   1525  CD  ARG A 196       2.696 -20.719  17.412  1.00 37.89           C  
ATOM   1526  NE  ARG A 196       2.790 -20.657  15.955  1.00 41.35           N  
ATOM   1527  CZ  ARG A 196       2.170 -21.482  15.108  1.00 46.88           C  
ATOM   1528  NH1 ARG A 196       1.378 -22.456  15.560  1.00 41.51           N  
ATOM   1529  NH2 ARG A 196       2.344 -21.332  13.794  1.00 42.87           N  
ATOM   1530  N   GLY A 197       1.591 -16.841  20.523  1.00 38.66           N  
ATOM   1531  CA  GLY A 197       1.623 -16.876  21.973  1.00 38.04           C  
ATOM   1532  C   GLY A 197       2.759 -16.041  22.542  1.00 38.93           C  
ATOM   1533  O   GLY A 197       2.865 -15.865  23.757  1.00 38.83           O  
ATOM   1534  N   TYR A 198       3.626 -15.532  21.673  1.00 40.28           N  
ATOM   1535  CA  TYR A 198       4.755 -14.710  22.135  1.00 41.07           C  
ATOM   1536  C   TYR A 198       4.284 -13.293  22.388  1.00 42.55           C  
ATOM   1537  O   TYR A 198       3.142 -12.942  22.100  1.00 43.81           O  
ATOM   1538  CB  TYR A 198       5.935 -14.727  21.153  1.00 42.19           C  
ATOM   1539  CG  TYR A 198       6.498 -16.123  20.962  1.00 42.10           C  
ATOM   1540  CD1 TYR A 198       7.129 -16.778  22.008  1.00 44.46           C  
ATOM   1541  CD2 TYR A 198       6.389 -16.783  19.744  1.00 41.49           C  
ATOM   1542  CE1 TYR A 198       7.625 -18.059  21.855  1.00 49.10           C  
ATOM   1543  CE2 TYR A 198       6.902 -18.052  19.568  1.00 45.17           C  
ATOM   1544  CZ  TYR A 198       7.510 -18.683  20.627  1.00 50.55           C  
ATOM   1545  OH  TYR A 198       8.024 -19.949  20.471  1.00 53.37           O  
ATOM   1546  N   SER A 199       5.145 -12.490  22.986  1.00 41.31           N  
ATOM   1547  CA  SER A 199       4.787 -11.108  23.190  1.00 44.31           C  
ATOM   1548  C   SER A 199       5.936 -10.215  22.735  1.00 44.39           C  
ATOM   1549  O   SER A 199       7.032 -10.278  23.263  1.00 42.97           O  
ATOM   1550  CB  SER A 199       4.477 -10.837  24.653  1.00 46.58           C  
ATOM   1551  OG  SER A 199       4.038  -9.496  24.777  1.00 53.52           O  
ATOM   1552  N  APHE A 200       5.719  -9.691  21.524  0.60 44.83           N  
ATOM   1553  N  BPHE A 200       5.624  -9.174  21.996  0.40 44.51           N  
ATOM   1554  CA APHE A 200       6.653  -8.826  20.787  0.60 44.03           C  
ATOM   1555  CA BPHE A 200       6.670  -8.195  21.789  0.40 44.22           C  
ATOM   1556  C  APHE A 200       5.906  -7.579  20.310  0.60 44.19           C  
ATOM   1557  C  BPHE A 200       6.154  -6.824  22.196  0.40 43.55           C  
ATOM   1558  O  APHE A 200       5.183  -7.623  19.308  0.60 44.43           O  
ATOM   1559  O  BPHE A 200       5.540  -6.111  21.410  0.40 44.62           O  
ATOM   1560  CB APHE A 200       7.215  -9.509  19.546  0.60 43.92           C  
ATOM   1561  CB BPHE A 200       7.181  -8.311  20.354  0.40 44.25           C  
ATOM   1562  CG APHE A 200       8.188 -10.621  19.817  0.60 41.94           C  
ATOM   1563  CG BPHE A 200       7.707  -9.684  20.032  0.40 42.56           C  
ATOM   1564  CD1APHE A 200       9.487 -10.352  20.226  0.60 41.64           C  
ATOM   1565  CD1BPHE A 200       9.033 -10.009  20.278  0.40 44.40           C  
ATOM   1566  CD2APHE A 200       7.824 -11.937  19.573  0.60 39.84           C  
ATOM   1567  CD2BPHE A 200       6.869 -10.664  19.513  0.40 44.90           C  
ATOM   1568  CE1APHE A 200      10.388 -11.378  20.429  0.60 39.81           C  
ATOM   1569  CE1BPHE A 200       9.522 -11.275  19.994  0.40 44.03           C  
ATOM   1570  CE2APHE A 200       8.727 -12.967  19.769  0.60 39.41           C  
ATOM   1571  CE2BPHE A 200       7.345 -11.930  19.235  0.40 41.89           C  
ATOM   1572  CZ APHE A 200      10.003 -12.689  20.207  0.60 39.08           C  
ATOM   1573  CZ BPHE A 200       8.676 -12.238  19.469  0.40 43.03           C  
ATOM   1574  N  AVAL A 201       6.069  -6.471  21.025  0.60 43.74           N  
ATOM   1575  N  BVAL A 201       6.390  -6.496  23.463  0.40 43.53           N  
ATOM   1576  CA AVAL A 201       5.351  -5.236  20.690  0.60 44.51           C  
ATOM   1577  CA BVAL A 201       5.779  -5.336  24.102  0.40 42.89           C  
ATOM   1578  C  AVAL A 201       6.185  -3.983  20.963  0.60 42.81           C  
ATOM   1579  C  BVAL A 201       6.768  -4.183  24.266  0.40 41.39           C  
ATOM   1580  O  AVAL A 201       6.143  -3.041  20.189  0.60 42.46           O  
ATOM   1581  O  BVAL A 201       6.576  -3.120  23.671  0.40 42.15           O  
ATOM   1582  CB AVAL A 201       3.972  -5.155  21.400  0.60 46.00           C  
ATOM   1583  CB BVAL A 201       5.154  -5.703  25.467  0.40 42.36           C  
ATOM   1584  CG1AVAL A 201       4.145  -5.091  22.906  0.60 46.95           C  
ATOM   1585  CG1BVAL A 201       4.295  -4.565  25.982  0.40 43.35           C  
ATOM   1586  CG2AVAL A 201       3.179  -3.953  20.905  0.60 48.78           C  
ATOM   1587  CG2BVAL A 201       4.317  -6.960  25.339  0.40 44.65           C  
ATOM   1588  N  ATHR A 202       6.961  -3.976  22.042  0.60 43.29           N  
ATOM   1589  N  BTHR A 202       7.821  -4.376  25.058  0.40 39.49           N  
ATOM   1590  CA ATHR A 202       7.780  -2.806  22.381  0.60 42.93           C  
ATOM   1591  CA BTHR A 202       8.810  -3.306  25.216  0.40 37.55           C  
ATOM   1592  C  ATHR A 202       8.805  -2.467  21.298  0.60 43.33           C  
ATOM   1593  C  BTHR A 202       9.424  -2.920  23.873  0.40 38.35           C  
ATOM   1594  O  ATHR A 202       9.106  -3.290  20.435  0.60 41.91           O  
ATOM   1595  O  BTHR A 202       9.092  -3.492  22.828  0.40 38.35           O  
ATOM   1596  CB ATHR A 202       8.531  -2.980  23.727  0.60 44.59           C  
ATOM   1597  CB BTHR A 202       9.949  -3.650  26.202  0.40 36.76           C  
ATOM   1598  OG1ATHR A 202       9.511  -4.026  23.616  0.60 43.95           O  
ATOM   1599  OG1BTHR A 202      10.781  -4.682  25.655  0.40 31.03           O  
ATOM   1600  CG2ATHR A 202       7.554  -3.297  24.852  0.60 44.76           C  
ATOM   1601  CG2BTHR A 202       9.407  -4.065  27.578  0.40 34.35           C  
ATOM   1602  N  ATHR A 203       9.328  -1.243  21.358  0.60 43.42           N  
ATOM   1603  N  BTHR A 203      10.321  -1.944  23.915  0.40 38.82           N  
ATOM   1604  CA ATHR A 203      10.422  -0.780  20.503  0.60 44.42           C  
ATOM   1605  CA BTHR A 203      10.965  -1.419  22.720  0.40 39.33           C  
ATOM   1606  C  ATHR A 203      11.548  -1.794  20.425  0.60 43.27           C  
ATOM   1607  C  BTHR A 203      12.096  -2.336  22.294  0.40 39.48           C  
ATOM   1608  O  ATHR A 203      12.026  -2.111  19.332  0.60 42.17           O  
ATOM   1609  O  BTHR A 203      12.369  -2.503  21.109  0.40 40.52           O  
ATOM   1610  CB ATHR A 203      11.055   0.502  21.105  0.60 44.42           C  
ATOM   1611  CB BTHR A 203      11.505  -0.004  23.002  0.40 37.25           C  
ATOM   1612  OG1ATHR A 203      10.129   1.586  21.016  0.60 49.09           O  
ATOM   1613  OG1BTHR A 203      10.395   0.845  23.282  0.40 40.55           O  
ATOM   1614  CG2ATHR A 203      12.352   0.874  20.401  0.60 48.00           C  
ATOM   1615  CG2BTHR A 203      12.259   0.571  21.832  0.40 38.07           C  
ATOM   1616  N  AALA A 204      11.978  -2.263  21.599  0.60 42.36           N  
ATOM   1617  N  BALA A 204      12.751  -2.945  23.270  0.40 41.37           N  
ATOM   1618  CA AALA A 204      13.055  -3.243  21.727  0.60 42.06           C  
ATOM   1619  CA BALA A 204      13.837  -3.845  22.947  0.40 43.54           C  
ATOM   1620  C  AALA A 204      12.691  -4.609  21.135  0.60 42.95           C  
ATOM   1621  C  BALA A 204      13.319  -5.084  22.211  0.40 45.23           C  
ATOM   1622  O  AALA A 204      13.550  -5.298  20.577  0.60 41.49           O  
ATOM   1623  O  BALA A 204      13.955  -6.133  22.283  0.40 46.28           O  
ATOM   1624  CB AALA A 204      13.457  -3.392  23.200  0.60 41.34           C  
ATOM   1625  CB BALA A 204      14.589  -4.231  24.206  0.40 42.99           C  
ATOM   1626  N  AGLU A 205      11.427  -5.006  21.314  0.60 43.44           N  
ATOM   1627  N  BGLU A 205      12.204  -4.952  21.481  0.40 47.15           N  
ATOM   1628  CA AGLU A 205      10.907  -6.284  20.828  0.60 42.76           C  
ATOM   1629  CA BGLU A 205      11.518  -6.105  20.860  0.40 46.93           C  
ATOM   1630  C  AGLU A 205      10.830  -6.226  19.316  0.60 45.36           C  
ATOM   1631  C  BGLU A 205      11.247  -6.091  19.334  0.40 47.67           C  
ATOM   1632  O  AGLU A 205      10.984  -7.239  18.624  0.60 44.65           O  
ATOM   1633  O  BGLU A 205      11.560  -7.072  18.653  0.40 46.68           O  
ATOM   1634  CB AGLU A 205       9.539  -6.568  21.458  0.60 44.26           C  
ATOM   1635  CB BGLU A 205      10.304  -6.521  21.694  0.40 48.30           C  
ATOM   1636  CG AGLU A 205       9.620  -6.912  22.968  0.60 42.05           C  
ATOM   1637  CG BGLU A 205      10.735  -7.197  23.009  0.40 48.05           C  
ATOM   1638  CD AGLU A 205       8.257  -6.930  23.689  0.60 43.88           C  
ATOM   1639  CD BGLU A 205       9.715  -7.088  24.130  0.40 53.77           C  
ATOM   1640  OE1AGLU A 205       7.239  -6.529  23.079  0.60 40.89           O  
ATOM   1641  OE1BGLU A 205       8.776  -6.270  24.011  0.40 57.13           O  
ATOM   1642  OE2AGLU A 205       8.210  -7.321  24.884  0.60 43.88           O  
ATOM   1643  OE2BGLU A 205       9.860  -7.813  25.142  0.40 53.82           O  
ATOM   1644  N   ARG A 206      10.671  -5.021  18.785  1.00 45.63           N  
ATOM   1645  CA  ARG A 206      10.615  -4.890  17.322  1.00 47.55           C  
ATOM   1646  C   ARG A 206      12.014  -5.057  16.757  1.00 47.33           C  
ATOM   1647  O   ARG A 206      12.199  -5.579  15.645  1.00 46.51           O  
ATOM   1648  CB  ARG A 206      10.103  -3.511  16.879  1.00 48.95           C  
ATOM   1649  CG  ARG A 206       9.923  -3.406  15.363  1.00 49.89           C  
ATOM   1650  CD  ARG A 206       9.533  -1.999  14.876  1.00 53.13           C  
ATOM   1651  NE  ARG A 206       8.934  -2.112  13.541  1.00 60.67           N  
ATOM   1652  CZ  ARG A 206       9.618  -2.051  12.400  1.00 63.79           C  
ATOM   1653  NH1 ARG A 206      10.935  -1.844  12.435  1.00 64.09           N  
ATOM   1654  NH2 ARG A 206       8.986  -2.200  11.231  1.00 54.45           N  
ATOM   1655  N   GLU A 207      12.985  -4.543  17.513  1.00 45.89           N  
ATOM   1656  CA  GLU A 207      14.376  -4.717  17.158  1.00 44.99           C  
ATOM   1657  C   GLU A 207      14.709  -6.190  17.131  1.00 40.64           C  
ATOM   1658  O   GLU A 207      15.427  -6.642  16.236  1.00 41.54           O  
ATOM   1659  CB  GLU A 207      15.295  -3.965  18.142  1.00 46.09           C  
ATOM   1660  CG  GLU A 207      15.482  -2.487  17.804  1.00 47.73           C  
ATOM   1661  CD  GLU A 207      16.349  -1.732  18.832  1.00 49.58           C  
ATOM   1662  OE1 GLU A 207      16.502  -2.214  19.981  1.00 51.60           O  
ATOM   1663  OE2 GLU A 207      16.877  -0.639  18.499  1.00 54.96           O  
ATOM   1664  N   ILE A 208      14.210  -6.947  18.106  1.00 36.61           N  
ATOM   1665  CA  ILE A 208      14.513  -8.362  18.112  1.00 37.42           C  
ATOM   1666  C   ILE A 208      13.803  -9.013  16.917  1.00 36.93           C  
ATOM   1667  O   ILE A 208      14.361  -9.906  16.290  1.00 37.85           O  
ATOM   1668  CB  ILE A 208      14.067  -9.051  19.424  1.00 37.60           C  
ATOM   1669  CG1 ILE A 208      14.938  -8.594  20.601  1.00 44.03           C  
ATOM   1670  CG2 ILE A 208      14.059 -10.578  19.269  1.00 42.58           C  
ATOM   1671  CD1 ILE A 208      14.270  -8.797  21.977  1.00 43.25           C  
ATOM   1672  N   VAL A 209      12.566  -8.597  16.640  1.00 35.03           N  
ATOM   1673  CA  VAL A 209      11.795  -9.231  15.559  1.00 36.33           C  
ATOM   1674  C   VAL A 209      12.467  -8.982  14.209  1.00 36.53           C  
ATOM   1675  O   VAL A 209      12.543  -9.876  13.356  1.00 36.67           O  
ATOM   1676  CB  VAL A 209      10.340  -8.773  15.553  1.00 35.19           C  
ATOM   1677  CG1 VAL A 209       9.589  -9.340  14.301  1.00 39.72           C  
ATOM   1678  CG2 VAL A 209       9.638  -9.346  16.790  1.00 39.37           C  
ATOM   1679  N   ARG A 210      12.974  -7.769  14.017  1.00 36.28           N  
ATOM   1680  CA  ARG A 210      13.725  -7.494  12.795  1.00 36.59           C  
ATOM   1681  C   ARG A 210      14.901  -8.448  12.647  1.00 37.71           C  
ATOM   1682  O   ARG A 210      15.196  -8.928  11.549  1.00 37.02           O  
ATOM   1683  CB  ARG A 210      14.232  -6.052  12.783  1.00 35.71           C  
ATOM   1684  CG  ARG A 210      14.862  -5.710  11.427  1.00 41.53           C  
ATOM   1685  CD  ARG A 210      15.146  -4.223  11.348  1.00 47.57           C  
ATOM   1686  NE  ARG A 210      16.062  -3.840  12.405  1.00 54.46           N  
ATOM   1687  CZ  ARG A 210      17.376  -4.022  12.335  1.00 62.05           C  
ATOM   1688  NH1 ARG A 210      17.911  -4.574  11.248  1.00 59.99           N  
ATOM   1689  NH2 ARG A 210      18.148  -3.630  13.345  1.00 65.03           N  
ATOM   1690  N   ASP A 211      15.610  -8.698  13.749  1.00 37.65           N  
ATOM   1691  CA  ASP A 211      16.709  -9.674  13.756  1.00 39.10           C  
ATOM   1692  C   ASP A 211      16.266 -11.111  13.461  1.00 37.81           C  
ATOM   1693  O   ASP A 211      16.911 -11.828  12.667  1.00 36.36           O  
ATOM   1694  CB  ASP A 211      17.502  -9.607  15.070  1.00 39.22           C  
ATOM   1695  CG  ASP A 211      18.814 -10.367  14.982  1.00 45.07           C  
ATOM   1696  OD2 ASP A 211      19.000 -11.370  15.705  1.00 47.26           O  
ATOM   1697  OD1 ASP A 211      19.634  -9.996  14.117  1.00 46.71           O  
ATOM   1698  N   ILE A 212      15.150 -11.530  14.055  1.00 35.70           N  
ATOM   1699  CA  ILE A 212      14.604 -12.853  13.743  1.00 35.02           C  
ATOM   1700  C   ILE A 212      14.268 -12.932  12.233  1.00 36.92           C  
ATOM   1701  O   ILE A 212      14.566 -13.922  11.550  1.00 36.16           O  
ATOM   1702  CB  ILE A 212      13.336 -13.158  14.563  1.00 36.66           C  
ATOM   1703  CG1 ILE A 212      13.678 -13.319  16.058  1.00 35.12           C  
ATOM   1704  CG2 ILE A 212      12.645 -14.451  14.098  1.00 34.85           C  
ATOM   1705  CD1 ILE A 212      12.427 -13.185  16.933  1.00 40.59           C  
ATOM   1706  N   LYS A 213      13.623 -11.892  11.727  1.00 32.53           N  
ATOM   1707  CA  LYS A 213      13.312 -11.819  10.276  1.00 36.61           C  
ATOM   1708  C   LYS A 213      14.557 -12.048   9.391  1.00 38.18           C  
ATOM   1709  O   LYS A 213      14.549 -12.849   8.442  1.00 38.03           O  
ATOM   1710  CB  LYS A 213      12.703 -10.438   9.973  1.00 34.78           C  
ATOM   1711  CG  LYS A 213      12.154 -10.347   8.542  1.00 37.16           C  
ATOM   1712  CD  LYS A 213      11.768  -8.896   8.192  1.00 34.08           C  
ATOM   1713  CE  LYS A 213      12.947  -7.939   8.119  1.00 38.20           C  
ATOM   1714  NZ  LYS A 213      12.445  -6.627   7.512  1.00 36.10           N  
ATOM   1715  N   GLU A 214      15.636 -11.346   9.709  1.00 36.60           N  
ATOM   1716  CA  GLU A 214      16.835 -11.319   8.873  1.00 39.27           C  
ATOM   1717  C   GLU A 214      17.654 -12.601   9.003  1.00 41.07           C  
ATOM   1718  O   GLU A 214      18.507 -12.870   8.162  1.00 46.31           O  
ATOM   1719  CB  GLU A 214      17.712 -10.096   9.183  1.00 39.43           C  
ATOM   1720  CG  GLU A 214      17.013  -8.775   8.858  1.00 39.31           C  
ATOM   1721  CD  GLU A 214      17.848  -7.551   9.177  1.00 45.19           C  
ATOM   1722  OE1 GLU A 214      18.976  -7.699   9.703  1.00 42.77           O  
ATOM   1723  OE2 GLU A 214      17.363  -6.425   8.914  1.00 42.05           O  
ATOM   1724  N   LYS A 215      17.434 -13.361  10.071  1.00 39.67           N  
ATOM   1725  CA  LYS A 215      18.263 -14.544  10.391  1.00 39.38           C  
ATOM   1726  C   LYS A 215      17.567 -15.886  10.158  1.00 39.00           C  
ATOM   1727  O   LYS A 215      18.233 -16.870   9.841  1.00 39.83           O  
ATOM   1728  CB  LYS A 215      18.736 -14.521  11.843  1.00 40.01           C  
ATOM   1729  CG  LYS A 215      19.868 -13.511  12.063  1.00 43.63           C  
ATOM   1730  CD  LYS A 215      20.340 -13.578  13.497  1.00 52.54           C  
ATOM   1731  CE  LYS A 215      21.787 -13.109  13.616  1.00 57.56           C  
ATOM   1732  NZ  LYS A 215      21.972 -11.811  12.916  1.00 56.33           N  
ATOM   1733  N   LEU A 216      16.248 -15.919  10.309  1.00 35.91           N  
ATOM   1734  CA  LEU A 216      15.515 -17.180  10.279  1.00 37.66           C  
ATOM   1735  C   LEU A 216      14.444 -17.265   9.180  1.00 37.33           C  
ATOM   1736  O   LEU A 216      13.945 -18.350   8.925  1.00 36.47           O  
ATOM   1737  CB  LEU A 216      14.851 -17.477  11.620  1.00 39.29           C  
ATOM   1738  CG  LEU A 216      15.821 -17.683  12.805  1.00 44.51           C  
ATOM   1739  CD1 LEU A 216      14.989 -18.216  13.931  1.00 46.07           C  
ATOM   1740  CD2 LEU A 216      16.940 -18.652  12.461  1.00 51.37           C  
ATOM   1741  N   CYS A 217      14.084 -16.155   8.536  1.00 35.09           N  
ATOM   1742  CA  CYS A 217      12.977 -16.268   7.565  1.00 35.70           C  
ATOM   1743  C   CYS A 217      13.501 -16.759   6.211  1.00 35.20           C  
ATOM   1744  O   CYS A 217      14.686 -16.600   5.907  1.00 34.74           O  
ATOM   1745  CB  CYS A 217      12.280 -14.903   7.384  1.00 37.11           C  
ATOM   1746  SG  CYS A 217      11.213 -14.496   8.752  1.00 40.33           S  
ATOM   1747  N   TYR A 218      12.600 -17.299   5.376  1.00 34.65           N  
ATOM   1748  CA  TYR A 218      12.997 -17.747   4.040  1.00 34.91           C  
ATOM   1749  C   TYR A 218      11.738 -17.849   3.184  1.00 35.58           C  
ATOM   1750  O   TYR A 218      10.630 -17.846   3.724  1.00 34.64           O  
ATOM   1751  CB  TYR A 218      13.670 -19.106   4.083  1.00 34.02           C  
ATOM   1752  CG  TYR A 218      12.789 -20.307   4.502  1.00 36.68           C  
ATOM   1753  CD2 TYR A 218      12.208 -21.127   3.541  1.00 35.79           C  
ATOM   1754  CD1 TYR A 218      12.537 -20.593   5.834  1.00 37.33           C  
ATOM   1755  CE2 TYR A 218      11.421 -22.219   3.894  1.00 39.87           C  
ATOM   1756  CE1 TYR A 218      11.766 -21.707   6.221  1.00 36.35           C  
ATOM   1757  CZ  TYR A 218      11.215 -22.511   5.246  1.00 40.21           C  
ATOM   1758  OH  TYR A 218      10.484 -23.626   5.596  1.00 37.06           O  
ATOM   1759  N   VAL A 219      11.901 -17.924   1.864  1.00 35.26           N  
ATOM   1760  CA  VAL A 219      10.731 -17.995   0.967  1.00 33.77           C  
ATOM   1761  C   VAL A 219      10.553 -19.460   0.566  1.00 34.37           C  
ATOM   1762  O   VAL A 219      11.491 -20.112   0.073  1.00 35.35           O  
ATOM   1763  CB  VAL A 219      10.934 -17.076  -0.303  1.00 35.20           C  
ATOM   1764  CG1 VAL A 219       9.845 -17.338  -1.384  1.00 34.87           C  
ATOM   1765  CG2 VAL A 219      10.958 -15.609   0.108  1.00 35.32           C  
ATOM   1766  N   ALA A 220       9.368 -20.004   0.826  1.00 34.47           N  
ATOM   1767  CA  ALA A 220       9.082 -21.384   0.455  1.00 36.04           C  
ATOM   1768  C   ALA A 220       8.975 -21.488  -1.074  1.00 36.35           C  
ATOM   1769  O   ALA A 220       8.336 -20.636  -1.699  1.00 36.24           O  
ATOM   1770  CB  ALA A 220       7.734 -21.774   1.066  1.00 35.99           C  
ATOM   1771  N   LEU A 221       9.511 -22.552  -1.666  1.00 35.47           N  
ATOM   1772  CA  LEU A 221       9.275 -22.809  -3.093  1.00 34.77           C  
ATOM   1773  C   LEU A 221       7.807 -23.121  -3.431  1.00 38.29           C  
ATOM   1774  O   LEU A 221       7.295 -22.703  -4.490  1.00 37.87           O  
ATOM   1775  CB  LEU A 221      10.180 -23.921  -3.604  1.00 34.44           C  
ATOM   1776  CG  LEU A 221      10.210 -24.110  -5.119  1.00 34.68           C  
ATOM   1777  CD1 LEU A 221      10.614 -22.838  -5.895  1.00 33.25           C  
ATOM   1778  CD2 LEU A 221      11.155 -25.279  -5.433  1.00 36.91           C  
ATOM   1779  N   ASP A 222       7.149 -23.868  -2.549  1.00 37.67           N  
ATOM   1780  CA  ASP A 222       5.738 -24.228  -2.701  1.00 37.85           C  
ATOM   1781  C   ASP A 222       5.084 -23.941  -1.353  1.00 37.99           C  
ATOM   1782  O   ASP A 222       5.233 -24.753  -0.423  1.00 36.42           O  
ATOM   1783  CB  ASP A 222       5.641 -25.728  -3.051  1.00 37.70           C  
ATOM   1784  CG  ASP A 222       4.222 -26.201  -3.337  1.00 42.32           C  
ATOM   1785  OD1 ASP A 222       3.242 -25.751  -2.687  1.00 42.77           O  
ATOM   1786  OD2 ASP A 222       4.088 -27.125  -4.184  1.00 46.03           O  
ATOM   1787  N   PHE A 223       4.379 -22.816  -1.228  1.00 36.67           N  
ATOM   1788  CA  PHE A 223       3.919 -22.341   0.090  1.00 37.96           C  
ATOM   1789  C   PHE A 223       2.928 -23.320   0.738  1.00 40.41           C  
ATOM   1790  O   PHE A 223       3.030 -23.617   1.922  1.00 36.44           O  
ATOM   1791  CB  PHE A 223       3.278 -20.947  -0.022  1.00 37.28           C  
ATOM   1792  CG  PHE A 223       2.660 -20.450   1.267  1.00 35.80           C  
ATOM   1793  CD1 PHE A 223       3.487 -19.956   2.286  1.00 39.29           C  
ATOM   1794  CD2 PHE A 223       1.279 -20.484   1.456  1.00 39.28           C  
ATOM   1795  CE1 PHE A 223       2.932 -19.515   3.475  1.00 38.28           C  
ATOM   1796  CE2 PHE A 223       0.711 -20.053   2.635  1.00 36.64           C  
ATOM   1797  CZ  PHE A 223       1.551 -19.547   3.642  1.00 35.22           C  
ATOM   1798  N   GLU A 224       1.994 -23.866  -0.043  1.00 38.47           N  
ATOM   1799  CA  GLU A 224       0.987 -24.723   0.596  1.00 40.51           C  
ATOM   1800  C   GLU A 224       1.606 -26.047   1.031  1.00 39.67           C  
ATOM   1801  O   GLU A 224       1.264 -26.592   2.087  1.00 38.75           O  
ATOM   1802  CB  GLU A 224      -0.253 -24.911  -0.284  1.00 44.20           C  
ATOM   1803  CG  GLU A 224      -1.019 -23.613  -0.557  1.00 51.89           C  
ATOM   1804  CD  GLU A 224      -1.736 -23.063   0.676  1.00 64.39           C  
ATOM   1805  OE1 GLU A 224      -2.010 -23.838   1.627  1.00 68.64           O  
ATOM   1806  OE2 GLU A 224      -2.022 -21.845   0.698  1.00 63.91           O  
ATOM   1807  N   ASN A 225       2.543 -26.566   0.235  1.00 38.27           N  
ATOM   1808  CA  ASN A 225       3.272 -27.751   0.659  1.00 39.29           C  
ATOM   1809  C   ASN A 225       4.112 -27.488   1.887  1.00 39.19           C  
ATOM   1810  O   ASN A 225       4.238 -28.363   2.748  1.00 37.94           O  
ATOM   1811  CB  ASN A 225       4.209 -28.259  -0.445  1.00 41.69           C  
ATOM   1812  CG  ASN A 225       3.790 -29.577  -0.969  1.00 43.79           C  
ATOM   1813  OD1 ASN A 225       2.588 -29.852  -1.066  1.00 48.53           O  
ATOM   1814  ND2 ASN A 225       4.762 -30.425  -1.288  1.00 44.09           N  
ATOM   1815  N   GLU A 226       4.737 -26.314   1.939  1.00 37.17           N  
ATOM   1816  CA  GLU A 226       5.556 -25.946   3.101  1.00 36.34           C  
ATOM   1817  C   GLU A 226       4.679 -25.831   4.359  1.00 37.23           C  
ATOM   1818  O   GLU A 226       5.083 -26.259   5.453  1.00 34.61           O  
ATOM   1819  CB  GLU A 226       6.309 -24.629   2.853  1.00 35.47           C  
ATOM   1820  CG  GLU A 226       7.592 -24.512   3.684  1.00 37.34           C  
ATOM   1821  CD  GLU A 226       8.775 -25.308   3.108  1.00 42.71           C  
ATOM   1822  OE1 GLU A 226       8.592 -26.058   2.126  1.00 43.60           O  
ATOM   1823  OE2 GLU A 226       9.902 -25.195   3.651  1.00 42.40           O  
ATOM   1824  N   MET A 227       3.454 -25.317   4.212  1.00 34.33           N  
ATOM   1825  CA  MET A 227       2.569 -25.225   5.385  1.00 37.68           C  
ATOM   1826  C   MET A 227       2.241 -26.631   5.912  1.00 37.38           C  
ATOM   1827  O   MET A 227       2.236 -26.868   7.121  1.00 36.80           O  
ATOM   1828  CB  MET A 227       1.262 -24.513   5.047  1.00 36.49           C  
ATOM   1829  CG  MET A 227       1.420 -22.988   4.880  1.00 35.81           C  
ATOM   1830  SD  MET A 227       1.816 -22.162   6.456  1.00 38.30           S  
ATOM   1831  CE  MET A 227       0.172 -22.095   7.213  1.00 40.64           C  
ATOM   1832  N   ALA A 228       1.992 -27.547   4.986  1.00 36.39           N  
ATOM   1833  CA  ALA A 228       1.697 -28.938   5.307  1.00 37.83           C  
ATOM   1834  C   ALA A 228       2.898 -29.605   5.957  1.00 38.04           C  
ATOM   1835  O   ALA A 228       2.734 -30.371   6.915  1.00 39.81           O  
ATOM   1836  CB  ALA A 228       1.275 -29.718   4.023  1.00 36.89           C  
ATOM   1837  N   THR A 229       4.089 -29.370   5.413  1.00 37.89           N  
ATOM   1838  CA  THR A 229       5.334 -29.894   6.018  1.00 39.59           C  
ATOM   1839  C   THR A 229       5.498 -29.395   7.471  1.00 38.94           C  
ATOM   1840  O   THR A 229       5.781 -30.184   8.381  1.00 40.43           O  
ATOM   1841  CB  THR A 229       6.571 -29.517   5.180  1.00 37.77           C  
ATOM   1842  OG1 THR A 229       6.444 -30.096   3.876  1.00 40.69           O  
ATOM   1843  CG2 THR A 229       7.872 -30.005   5.835  1.00 42.26           C  
ATOM   1844  N   ALA A 230       5.304 -28.097   7.693  1.00 37.31           N  
ATOM   1845  CA  ALA A 230       5.376 -27.505   9.032  1.00 39.40           C  
ATOM   1846  C   ALA A 230       4.345 -28.102   9.992  1.00 40.15           C  
ATOM   1847  O   ALA A 230       4.567 -28.114  11.203  1.00 40.60           O  
ATOM   1848  CB  ALA A 230       5.145 -25.995   8.951  1.00 37.53           C  
ATOM   1849  N   ALA A 231       3.209 -28.554   9.461  1.00 40.34           N  
ATOM   1850  CA  ALA A 231       2.152 -29.127  10.301  1.00 40.83           C  
ATOM   1851  C   ALA A 231       2.432 -30.599  10.619  1.00 42.17           C  
ATOM   1852  O   ALA A 231       2.012 -31.108  11.671  1.00 46.00           O  
ATOM   1853  CB  ALA A 231       0.766 -28.970   9.656  1.00 40.27           C  
ATOM   1854  N   SER A 232       3.127 -31.284   9.723  1.00 42.54           N  
ATOM   1855  CA  SER A 232       3.333 -32.730   9.907  1.00 42.40           C  
ATOM   1856  C   SER A 232       4.613 -33.102  10.661  1.00 41.39           C  
ATOM   1857  O   SER A 232       4.769 -34.253  11.083  1.00 42.05           O  
ATOM   1858  CB  SER A 232       3.240 -33.450   8.564  1.00 42.73           C  
ATOM   1859  OG  SER A 232       4.251 -33.001   7.687  1.00 43.92           O  
ATOM   1860  N   SER A 233       5.540 -32.161  10.826  1.00 40.57           N  
ATOM   1861  CA  SER A 233       6.829 -32.477  11.438  1.00 41.80           C  
ATOM   1862  C   SER A 233       7.399 -31.220  12.077  1.00 41.29           C  
ATOM   1863  O   SER A 233       6.924 -30.119  11.824  1.00 41.71           O  
ATOM   1864  CB  SER A 233       7.837 -32.971  10.379  1.00 40.45           C  
ATOM   1865  OG  SER A 233       8.064 -31.945   9.392  1.00 45.95           O  
ATOM   1866  N   SER A 234       8.480 -31.389  12.831  1.00 40.89           N  
ATOM   1867  CA ASER A 234       9.189 -30.266  13.437  0.50 40.27           C  
ATOM   1868  CA BSER A 234       9.174 -30.249  13.423  0.50 39.73           C  
ATOM   1869  C   SER A 234      10.408 -29.870  12.611  1.00 39.87           C  
ATOM   1870  O   SER A 234      11.242 -29.112  13.076  1.00 38.66           O  
ATOM   1871  CB ASER A 234       9.662 -30.647  14.844  0.50 40.91           C  
ATOM   1872  CB BSER A 234       9.582 -30.563  14.866  0.50 40.42           C  
ATOM   1873  OG ASER A 234       8.601 -31.158  15.630  0.50 42.10           O  
ATOM   1874  OG BSER A 234      10.464 -31.671  14.930  0.50 38.16           O  
ATOM   1875  N   SER A 235      10.521 -30.391  11.394  1.00 38.87           N  
ATOM   1876  CA ASER A 235      11.757 -30.250  10.622  0.50 39.34           C  
ATOM   1877  CA BSER A 235      11.750 -30.243  10.604  0.50 38.81           C  
ATOM   1878  C   SER A 235      12.036 -28.812  10.196  1.00 39.42           C  
ATOM   1879  O   SER A 235      13.171 -28.472   9.888  1.00 39.50           O  
ATOM   1880  CB ASER A 235      11.712 -31.165   9.397  0.50 40.78           C  
ATOM   1881  CB BSER A 235      11.675 -31.082   9.333  0.50 40.34           C  
ATOM   1882  OG ASER A 235      10.557 -30.897   8.613  0.50 40.95           O  
ATOM   1883  OG BSER A 235      11.870 -32.447   9.620  0.50 36.78           O  
ATOM   1884  N   LEU A 236      11.006 -27.962  10.160  1.00 36.28           N  
ATOM   1885  CA  LEU A 236      11.247 -26.593   9.714  1.00 36.82           C  
ATOM   1886  C   LEU A 236      11.388 -25.633  10.898  1.00 38.13           C  
ATOM   1887  O   LEU A 236      11.568 -24.431  10.714  1.00 38.73           O  
ATOM   1888  CB  LEU A 236      10.118 -26.133   8.804  1.00 34.44           C  
ATOM   1889  CG  LEU A 236       9.892 -27.063   7.615  1.00 35.46           C  
ATOM   1890  CD1 LEU A 236       8.740 -26.485   6.800  1.00 39.38           C  
ATOM   1891  CD2 LEU A 236      11.181 -27.126   6.792  1.00 39.53           C  
ATOM   1892  N   GLU A 237      11.326 -26.157  12.122  1.00 40.09           N  
ATOM   1893  CA  GLU A 237      11.479 -25.276  13.290  1.00 40.37           C  
ATOM   1894  C   GLU A 237      12.930 -24.847  13.459  1.00 41.63           C  
ATOM   1895  O   GLU A 237      13.857 -25.611  13.169  1.00 40.56           O  
ATOM   1896  CB  GLU A 237      10.959 -25.957  14.547  1.00 42.21           C  
ATOM   1897  CG  GLU A 237       9.449 -26.097  14.438  1.00 46.71           C  
ATOM   1898  CD  GLU A 237       8.821 -26.853  15.575  1.00 53.72           C  
ATOM   1899  OE1 GLU A 237       9.549 -27.344  16.473  1.00 54.17           O  
ATOM   1900  OE2 GLU A 237       7.569 -26.951  15.556  1.00 58.43           O  
ATOM   1901  N   LYS A 238      13.115 -23.616  13.917  1.00 41.72           N  
ATOM   1902  CA  LYS A 238      14.444 -23.088  14.178  1.00 44.71           C  
ATOM   1903  C   LYS A 238      14.344 -22.436  15.533  1.00 44.67           C  
ATOM   1904  O   LYS A 238      13.289 -21.903  15.873  1.00 44.77           O  
ATOM   1905  CB  LYS A 238      14.809 -22.056  13.115  1.00 45.27           C  
ATOM   1906  CG  LYS A 238      16.103 -22.321  12.367  1.00 54.28           C  
ATOM   1907  CD  LYS A 238      16.031 -23.667  11.692  1.00 59.61           C  
ATOM   1908  CE  LYS A 238      17.244 -23.921  10.808  1.00 65.34           C  
ATOM   1909  NZ  LYS A 238      17.515 -25.386  10.670  1.00 68.35           N  
ATOM   1910  N   SER A 239      15.426 -22.507  16.308  1.00 45.28           N  
ATOM   1911  CA  SER A 239      15.455 -21.889  17.625  1.00 46.38           C  
ATOM   1912  C   SER A 239      16.140 -20.534  17.525  1.00 45.76           C  
ATOM   1913  O   SER A 239      16.945 -20.292  16.619  1.00 46.74           O  
ATOM   1914  CB  SER A 239      16.158 -22.799  18.629  1.00 47.86           C  
ATOM   1915  OG  SER A 239      15.328 -23.911  18.939  1.00 52.73           O  
ATOM   1916  N   TYR A 240      15.745 -19.625  18.407  1.00 43.23           N  
ATOM   1917  CA  TYR A 240      16.326 -18.295  18.438  1.00 41.39           C  
ATOM   1918  C   TYR A 240      16.442 -17.885  19.898  1.00 41.99           C  
ATOM   1919  O   TYR A 240      15.437 -17.820  20.607  1.00 40.89           O  
ATOM   1920  CB  TYR A 240      15.452 -17.298  17.675  1.00 40.64           C  
ATOM   1921  CG  TYR A 240      15.994 -15.903  17.637  1.00 42.40           C  
ATOM   1922  CD1 TYR A 240      15.718 -15.013  18.668  1.00 40.10           C  
ATOM   1923  CD2 TYR A 240      16.809 -15.476  16.590  1.00 40.39           C  
ATOM   1924  CE1 TYR A 240      16.201 -13.721  18.646  1.00 37.98           C  
ATOM   1925  CE2 TYR A 240      17.316 -14.182  16.565  1.00 43.35           C  
ATOM   1926  CZ  TYR A 240      17.015 -13.320  17.606  1.00 42.48           C  
ATOM   1927  OH  TYR A 240      17.505 -12.043  17.625  1.00 40.89           O  
ATOM   1928  N   GLU A 241      17.675 -17.583  20.301  1.00 42.44           N  
ATOM   1929  CA  GLU A 241      17.988 -17.193  21.659  1.00 44.53           C  
ATOM   1930  C   GLU A 241      17.883 -15.686  21.801  1.00 43.61           C  
ATOM   1931  O   GLU A 241      18.553 -14.938  21.098  1.00 43.46           O  
ATOM   1932  CB  GLU A 241      19.400 -17.645  22.031  1.00 44.92           C  
ATOM   1933  CG  GLU A 241      19.723 -17.355  23.492  1.00 50.80           C  
ATOM   1934  CD  GLU A 241      21.210 -17.323  23.751  1.00 58.83           C  
ATOM   1935  OE1 GLU A 241      21.986 -17.519  22.785  1.00 62.30           O  
ATOM   1936  OE2 GLU A 241      21.596 -17.073  24.912  1.00 58.63           O  
ATOM   1937  N   LEU A 242      17.010 -15.260  22.702  1.00 44.57           N  
ATOM   1938  CA  LEU A 242      16.759 -13.854  22.919  1.00 46.51           C  
ATOM   1939  C   LEU A 242      17.909 -13.244  23.736  1.00 49.15           C  
ATOM   1940  O   LEU A 242      18.718 -13.975  24.328  1.00 47.85           O  
ATOM   1941  CB  LEU A 242      15.415 -13.694  23.633  1.00 47.36           C  
ATOM   1942  CG  LEU A 242      14.201 -14.270  22.887  1.00 48.45           C  
ATOM   1943  CD1 LEU A 242      12.951 -14.245  23.759  1.00 51.76           C  
ATOM   1944  CD2 LEU A 242      13.954 -13.527  21.591  1.00 49.99           C  
ATOM   1945  N   PRO A 243      18.009 -11.904  23.728  1.00 50.61           N  
ATOM   1946  CA  PRO A 243      19.008 -11.174  24.509  1.00 52.08           C  
ATOM   1947  C   PRO A 243      19.129 -11.679  25.947  1.00 53.98           C  
ATOM   1948  O   PRO A 243      20.246 -11.812  26.438  1.00 56.06           O  
ATOM   1949  CB  PRO A 243      18.499  -9.727  24.502  1.00 50.67           C  
ATOM   1950  CG  PRO A 243      17.343  -9.680  23.570  1.00 53.46           C  
ATOM   1951  CD  PRO A 243      17.194 -11.007  22.889  1.00 50.16           C  
ATOM   1952  N   ASP A 244      18.008 -11.942  26.621  1.00 56.33           N  
ATOM   1953  CA  ASP A 244      18.054 -12.436  28.003  1.00 59.13           C  
ATOM   1954  C   ASP A 244      18.524 -13.887  28.132  1.00 59.34           C  
ATOM   1955  O   ASP A 244      18.823 -14.354  29.228  1.00 60.86           O  
ATOM   1956  CB  ASP A 244      16.722 -12.226  28.749  1.00 59.46           C  
ATOM   1957  CG  ASP A 244      15.620 -13.172  28.288  1.00 66.17           C  
ATOM   1958  OD1 ASP A 244      15.921 -14.238  27.700  1.00 70.18           O  
ATOM   1959  OD2 ASP A 244      14.431 -12.850  28.519  1.00 72.01           O  
ATOM   1960  N   GLY A 245      18.591 -14.607  27.018  1.00 59.76           N  
ATOM   1961  CA  GLY A 245      19.100 -15.973  27.039  1.00 59.40           C  
ATOM   1962  C   GLY A 245      18.055 -17.057  26.858  1.00 59.00           C  
ATOM   1963  O   GLY A 245      18.400 -18.202  26.572  1.00 59.92           O  
ATOM   1964  N   GLN A 246      16.782 -16.719  27.038  1.00 58.11           N  
ATOM   1965  CA  GLN A 246      15.725 -17.689  26.793  1.00 57.89           C  
ATOM   1966  C   GLN A 246      15.619 -17.973  25.288  1.00 57.00           C  
ATOM   1967  O   GLN A 246      15.718 -17.058  24.464  1.00 55.04           O  
ATOM   1968  CB  GLN A 246      14.390 -17.208  27.361  1.00 57.84           C  
ATOM   1969  CG  GLN A 246      13.688 -16.170  26.501  1.00 61.74           C  
ATOM   1970  CD  GLN A 246      12.289 -15.819  26.994  1.00 62.66           C  
ATOM   1971  OE1 GLN A 246      11.288 -16.367  26.515  1.00 69.71           O  
ATOM   1972  NE2 GLN A 246      12.214 -14.889  27.948  1.00 69.00           N  
ATOM   1973  N   VAL A 247      15.436 -19.245  24.947  1.00 55.30           N  
ATOM   1974  CA  VAL A 247      15.360 -19.671  23.563  1.00 56.05           C  
ATOM   1975  C   VAL A 247      13.911 -19.862  23.143  1.00 54.42           C  
ATOM   1976  O   VAL A 247      13.146 -20.531  23.824  1.00 56.10           O  
ATOM   1977  CB  VAL A 247      16.107 -20.996  23.371  1.00 56.62           C  
ATOM   1978  CG1 VAL A 247      15.921 -21.517  21.956  1.00 57.78           C  
ATOM   1979  CG2 VAL A 247      17.589 -20.828  23.704  1.00 59.21           C  
ATOM   1980  N   ILE A 248      13.521 -19.283  22.014  1.00 53.12           N  
ATOM   1981  CA  ILE A 248      12.204 -19.588  21.454  1.00 51.50           C  
ATOM   1982  C   ILE A 248      12.286 -20.335  20.131  1.00 51.20           C  
ATOM   1983  O   ILE A 248      13.321 -20.360  19.482  1.00 49.82           O  
ATOM   1984  CB  ILE A 248      11.335 -18.344  21.274  1.00 50.57           C  
ATOM   1985  CG1 ILE A 248      12.013 -17.379  20.307  1.00 47.45           C  
ATOM   1986  CG2 ILE A 248      11.101 -17.689  22.637  1.00 51.53           C  
ATOM   1987  CD1 ILE A 248      11.171 -16.191  20.014  1.00 43.00           C  
ATOM   1988  N   THR A 249      11.170 -20.933  19.737  1.00 53.23           N  
ATOM   1989  CA  THR A 249      11.135 -21.767  18.542  1.00 53.56           C  
ATOM   1990  C   THR A 249      10.183 -21.145  17.540  1.00 53.80           C  
ATOM   1991  O   THR A 249       9.075 -20.709  17.888  1.00 55.04           O  
ATOM   1992  CB  THR A 249      10.712 -23.195  18.900  1.00 56.57           C  
ATOM   1993  OG1 THR A 249      11.728 -23.773  19.739  1.00 58.51           O  
ATOM   1994  CG2 THR A 249      10.563 -24.039  17.649  1.00 57.83           C  
ATOM   1995  N   ILE A 250      10.628 -21.014  16.297  1.00 47.96           N  
ATOM   1996  CA  ILE A 250       9.713 -20.486  15.313  1.00 47.34           C  
ATOM   1997  C   ILE A 250       9.556 -21.488  14.165  1.00 44.26           C  
ATOM   1998  O   ILE A 250      10.536 -22.102  13.706  1.00 39.84           O  
ATOM   1999  CB  ILE A 250      10.058 -19.036  14.879  1.00 48.77           C  
ATOM   2000  CG1 ILE A 250      11.091 -18.985  13.782  1.00 53.61           C  
ATOM   2001  CG2 ILE A 250      10.628 -18.169  16.044  1.00 52.04           C  
ATOM   2002  CD1 ILE A 250      10.902 -17.720  12.913  1.00 60.72           C  
ATOM   2003  N   GLY A 251       8.310 -21.676  13.739  1.00 42.13           N  
ATOM   2004  CA  GLY A 251       7.970 -22.701  12.766  1.00 38.91           C  
ATOM   2005  C   GLY A 251       7.522 -22.011  11.483  1.00 39.19           C  
ATOM   2006  O   GLY A 251       8.322 -21.374  10.798  1.00 38.96           O  
ATOM   2007  N   ASN A 252       6.255 -22.157  11.122  1.00 37.51           N  
ATOM   2008  CA  ASN A 252       5.811 -21.640   9.815  1.00 36.10           C  
ATOM   2009  C   ASN A 252       5.874 -20.123   9.698  1.00 35.92           C  
ATOM   2010  O   ASN A 252       5.793 -19.557   8.572  1.00 35.46           O  
ATOM   2011  CB  ASN A 252       4.439 -22.200   9.429  1.00 37.76           C  
ATOM   2012  CG  ASN A 252       3.312 -21.717  10.345  1.00 35.35           C  
ATOM   2013  OD1 ASN A 252       3.466 -20.766  11.124  1.00 36.89           O  
ATOM   2014  ND2 ASN A 252       2.166 -22.402  10.268  1.00 36.69           N  
ATOM   2015  N   GLU A 253       6.055 -19.424  10.822  1.00 35.01           N  
ATOM   2016  CA  GLU A 253       6.272 -17.984  10.689  1.00 37.02           C  
ATOM   2017  C   GLU A 253       7.508 -17.646   9.847  1.00 36.00           C  
ATOM   2018  O   GLU A 253       7.615 -16.530   9.281  1.00 37.83           O  
ATOM   2019  CB  GLU A 253       6.372 -17.309  12.070  1.00 38.71           C  
ATOM   2020  CG  GLU A 253       5.070 -17.389  12.885  1.00 36.58           C  
ATOM   2021  CD  GLU A 253       4.907 -18.701  13.661  1.00 45.61           C  
ATOM   2022  OE1 GLU A 253       5.832 -19.539  13.656  1.00 38.98           O  
ATOM   2023  OE2 GLU A 253       3.834 -18.896  14.285  1.00 45.79           O  
ATOM   2024  N   ARG A 254       8.485 -18.562   9.808  1.00 35.63           N  
ATOM   2025  CA  ARG A 254       9.724 -18.316   9.058  1.00 36.20           C  
ATOM   2026  C   ARG A 254       9.441 -18.013   7.583  1.00 36.44           C  
ATOM   2027  O   ARG A 254      10.100 -17.146   7.002  1.00 37.42           O  
ATOM   2028  CB  ARG A 254      10.608 -19.578   9.074  1.00 35.05           C  
ATOM   2029  CG  ARG A 254      11.208 -19.900  10.468  1.00 36.19           C  
ATOM   2030  CD  ARG A 254      12.003 -21.200  10.442  1.00 36.09           C  
ATOM   2031  NE  ARG A 254      13.206 -20.959   9.658  1.00 36.46           N  
ATOM   2032  CZ  ARG A 254      13.904 -21.898   9.033  1.00 36.58           C  
ATOM   2033  NH1 ARG A 254      13.584 -23.182   9.176  1.00 39.98           N  
ATOM   2034  NH2 ARG A 254      14.971 -21.552   8.328  1.00 37.93           N  
ATOM   2035  N   PHE A 255       8.498 -18.743   6.982  1.00 35.31           N  
ATOM   2036  CA  PHE A 255       8.181 -18.548   5.547  1.00 35.80           C  
ATOM   2037  C   PHE A 255       6.844 -17.833   5.292  1.00 36.49           C  
ATOM   2038  O   PHE A 255       6.649 -17.276   4.214  1.00 36.85           O  
ATOM   2039  CB  PHE A 255       8.279 -19.879   4.759  1.00 34.08           C  
ATOM   2040  CG  PHE A 255       7.348 -20.952   5.249  1.00 34.76           C  
ATOM   2041  CD1 PHE A 255       6.073 -21.047   4.707  1.00 37.86           C  
ATOM   2042  CD2 PHE A 255       7.745 -21.870   6.213  1.00 34.75           C  
ATOM   2043  CE1 PHE A 255       5.169 -21.993   5.156  1.00 41.49           C  
ATOM   2044  CE2 PHE A 255       6.865 -22.850   6.652  1.00 36.43           C  
ATOM   2045  CZ  PHE A 255       5.570 -22.896   6.141  1.00 35.63           C  
ATOM   2046  N   ARG A 256       5.979 -17.750   6.300  1.00 33.91           N  
ATOM   2047  CA  ARG A 256       4.750 -16.968   6.125  1.00 33.99           C  
ATOM   2048  C   ARG A 256       5.071 -15.485   6.014  1.00 36.06           C  
ATOM   2049  O   ARG A 256       4.393 -14.740   5.303  1.00 36.82           O  
ATOM   2050  CB  ARG A 256       3.786 -17.214   7.261  1.00 35.69           C  
ATOM   2051  CG  ARG A 256       3.053 -18.530   7.126  1.00 34.93           C  
ATOM   2052  CD  ARG A 256       2.478 -18.922   8.471  1.00 38.74           C  
ATOM   2053  NE  ARG A 256       1.413 -17.985   8.836  1.00 39.26           N  
ATOM   2054  CZ  ARG A 256       1.085 -17.713  10.089  1.00 39.33           C  
ATOM   2055  NH1 ARG A 256       1.736 -18.319  11.083  1.00 40.10           N  
ATOM   2056  NH2 ARG A 256       0.108 -16.855  10.353  1.00 39.81           N  
ATOM   2057  N   CYS A 257       6.079 -15.019   6.747  1.00 37.31           N  
ATOM   2058  CA  CYS A 257       6.415 -13.589   6.725  1.00 38.21           C  
ATOM   2059  C   CYS A 257       6.805 -13.076   5.308  1.00 37.97           C  
ATOM   2060  O   CYS A 257       6.130 -12.193   4.759  1.00 36.84           O  
ATOM   2061  CB  CYS A 257       7.496 -13.304   7.783  1.00 39.27           C  
ATOM   2062  SG  CYS A 257       8.392 -11.740   7.562  1.00 41.19           S  
ATOM   2063  N   PRO A 258       7.843 -13.661   4.661  1.00 37.85           N  
ATOM   2064  CA  PRO A 258       8.101 -13.157   3.312  1.00 37.18           C  
ATOM   2065  C   PRO A 258       7.149 -13.656   2.203  1.00 37.51           C  
ATOM   2066  O   PRO A 258       7.170 -13.106   1.078  1.00 36.24           O  
ATOM   2067  CB  PRO A 258       9.537 -13.578   3.028  1.00 38.08           C  
ATOM   2068  CG  PRO A 258       9.730 -14.821   3.883  1.00 38.76           C  
ATOM   2069  CD  PRO A 258       8.879 -14.610   5.106  1.00 37.76           C  
ATOM   2070  N   GLU A 259       6.357 -14.688   2.486  1.00 34.66           N  
ATOM   2071  CA  GLU A 259       5.260 -15.021   1.550  1.00 36.18           C  
ATOM   2072  C   GLU A 259       4.426 -13.791   1.189  1.00 36.64           C  
ATOM   2073  O   GLU A 259       3.822 -13.715   0.106  1.00 35.78           O  
ATOM   2074  CB  GLU A 259       4.369 -16.126   2.122  1.00 37.37           C  
ATOM   2075  CG  GLU A 259       3.280 -16.635   1.123  1.00 35.62           C  
ATOM   2076  CD  GLU A 259       3.847 -17.360  -0.094  1.00 38.60           C  
ATOM   2077  OE1 GLU A 259       5.041 -17.765  -0.057  1.00 36.19           O  
ATOM   2078  OE2 GLU A 259       3.077 -17.556  -1.069  1.00 39.20           O  
ATOM   2079  N   THR A 260       4.340 -12.840   2.116  1.00 36.86           N  
ATOM   2080  CA  THR A 260       3.554 -11.608   1.924  1.00 36.46           C  
ATOM   2081  C   THR A 260       3.971 -10.852   0.647  1.00 35.03           C  
ATOM   2082  O   THR A 260       3.142 -10.203   0.025  1.00 35.03           O  
ATOM   2083  CB  THR A 260       3.777 -10.667   3.141  1.00 37.55           C  
ATOM   2084  OG1 THR A 260       3.311 -11.373   4.303  1.00 40.80           O  
ATOM   2085  CG2 THR A 260       2.982  -9.354   3.004  1.00 36.24           C  
ATOM   2086  N   LEU A 261       5.246 -10.955   0.265  1.00 34.16           N  
ATOM   2087  CA  LEU A 261       5.716 -10.346  -1.001  1.00 34.47           C  
ATOM   2088  C   LEU A 261       4.988 -10.930  -2.218  1.00 35.68           C  
ATOM   2089  O   LEU A 261       4.702 -10.219  -3.172  1.00 34.25           O  
ATOM   2090  CB  LEU A 261       7.240 -10.565  -1.165  1.00 34.42           C  
ATOM   2091  CG  LEU A 261       8.103  -9.892  -0.099  1.00 36.48           C  
ATOM   2092  CD1 LEU A 261       9.512 -10.516  -0.243  1.00 39.73           C  
ATOM   2093  CD2 LEU A 261       8.136  -8.395  -0.321  1.00 35.61           C  
ATOM   2094  N   PHE A 262       4.727 -12.229  -2.186  1.00 32.75           N  
ATOM   2095  CA  PHE A 262       3.990 -12.873  -3.260  1.00 34.42           C  
ATOM   2096  C   PHE A 262       2.481 -12.848  -3.046  1.00 33.81           C  
ATOM   2097  O   PHE A 262       1.742 -12.947  -4.045  1.00 34.13           O  
ATOM   2098  CB  PHE A 262       4.445 -14.326  -3.355  1.00 36.08           C  
ATOM   2099  CG  PHE A 262       5.888 -14.430  -3.715  1.00 35.94           C  
ATOM   2100  CD1 PHE A 262       6.275 -14.452  -5.051  1.00 36.75           C  
ATOM   2101  CD2 PHE A 262       6.864 -14.416  -2.714  1.00 35.51           C  
ATOM   2102  CE1 PHE A 262       7.656 -14.482  -5.382  1.00 33.72           C  
ATOM   2103  CE2 PHE A 262       8.247 -14.450  -3.037  1.00 37.31           C  
ATOM   2104  CZ  PHE A 262       8.619 -14.460  -4.363  1.00 36.93           C  
ATOM   2105  N   GLN A 263       2.047 -12.715  -1.792  1.00 33.54           N  
ATOM   2106  CA  GLN A 263       0.605 -12.627  -1.451  1.00 35.90           C  
ATOM   2107  C   GLN A 263       0.336 -11.435  -0.531  1.00 34.92           C  
ATOM   2108  O   GLN A 263       0.253 -11.597   0.693  1.00 36.75           O  
ATOM   2109  CB  GLN A 263       0.126 -13.899  -0.732  1.00 35.42           C  
ATOM   2110  CG  GLN A 263       0.289 -15.161  -1.610  1.00 38.07           C  
ATOM   2111  CD  GLN A 263      -0.476 -16.314  -1.044  1.00 44.40           C  
ATOM   2112  OE1 GLN A 263      -1.697 -16.271  -0.972  1.00 38.37           O  
ATOM   2113  NE2 GLN A 263       0.233 -17.351  -0.622  1.00 40.51           N  
ATOM   2114  N   PRO A 264       0.270 -10.226  -1.098  1.00 33.41           N  
ATOM   2115  CA  PRO A 264       0.129  -9.052  -0.229  1.00 33.22           C  
ATOM   2116  C   PRO A 264      -1.176  -9.051   0.584  1.00 34.01           C  
ATOM   2117  O   PRO A 264      -1.261  -8.331   1.579  1.00 35.19           O  
ATOM   2118  CB  PRO A 264       0.158  -7.874  -1.230  1.00 32.09           C  
ATOM   2119  CG  PRO A 264       1.031  -8.406  -2.394  1.00 33.88           C  
ATOM   2120  CD  PRO A 264       0.499  -9.846  -2.511  1.00 34.32           C  
ATOM   2121  N   SER A 265      -2.126  -9.908   0.216  1.00 36.25           N  
ATOM   2122  CA  SER A 265      -3.379 -10.063   0.958  1.00 36.06           C  
ATOM   2123  C   SER A 265      -3.096 -10.511   2.405  1.00 38.40           C  
ATOM   2124  O   SER A 265      -3.918 -10.291   3.261  1.00 37.15           O  
ATOM   2125  CB  SER A 265      -4.306 -11.057   0.243  1.00 40.35           C  
ATOM   2126  OG  SER A 265      -3.737 -12.361   0.262  1.00 41.36           O  
ATOM   2127  N   PHE A 266      -1.921 -11.079   2.680  1.00 36.78           N  
ATOM   2128  CA  PHE A 266      -1.551 -11.507   4.061  1.00 36.96           C  
ATOM   2129  C   PHE A 266      -1.547 -10.281   4.974  1.00 39.73           C  
ATOM   2130  O   PHE A 266      -1.749 -10.409   6.169  1.00 38.93           O  
ATOM   2131  CB  PHE A 266      -0.154 -12.125   4.105  1.00 38.37           C  
ATOM   2132  CG  PHE A 266      -0.107 -13.589   3.682  1.00 37.77           C  
ATOM   2133  CD1 PHE A 266      -1.118 -14.130   2.924  1.00 37.74           C  
ATOM   2134  CD2 PHE A 266       0.960 -14.394   4.021  1.00 41.28           C  
ATOM   2135  CE1 PHE A 266      -1.063 -15.457   2.494  1.00 41.99           C  
ATOM   2136  CE2 PHE A 266       1.022 -15.721   3.599  1.00 38.37           C  
ATOM   2137  CZ  PHE A 266       0.014 -16.251   2.831  1.00 39.29           C  
ATOM   2138  N   ILE A 267      -1.270  -9.097   4.445  1.00 36.54           N  
ATOM   2139  CA  ILE A 267      -1.403  -7.908   5.278  1.00 39.76           C  
ATOM   2140  C   ILE A 267      -2.560  -7.009   4.859  1.00 40.27           C  
ATOM   2141  O   ILE A 267      -2.523  -5.802   5.089  1.00 39.40           O  
ATOM   2142  CB  ILE A 267      -0.100  -7.105   5.366  1.00 39.53           C  
ATOM   2143  CG1 ILE A 267       0.342  -6.538   4.001  1.00 40.33           C  
ATOM   2144  CG2 ILE A 267       0.959  -7.999   5.956  1.00 40.02           C  
ATOM   2145  CD1 ILE A 267       1.487  -5.478   4.164  1.00 41.58           C  
ATOM   2146  N   GLY A 268      -3.560  -7.595   4.211  1.00 37.61           N  
ATOM   2147  CA  GLY A 268      -4.741  -6.854   3.772  1.00 38.01           C  
ATOM   2148  C   GLY A 268      -4.609  -5.870   2.624  1.00 38.20           C  
ATOM   2149  O   GLY A 268      -5.425  -4.951   2.519  1.00 37.30           O  
ATOM   2150  N   MET A 269      -3.585  -6.061   1.786  1.00 39.15           N  
ATOM   2151  CA AMET A 269      -3.366  -5.247   0.598  0.60 41.29           C  
ATOM   2152  CA BMET A 269      -3.350  -5.245   0.602  0.40 41.97           C  
ATOM   2153  C   MET A 269      -3.914  -5.984  -0.620  1.00 42.34           C  
ATOM   2154  O   MET A 269      -3.639  -7.164  -0.797  1.00 42.00           O  
ATOM   2155  CB AMET A 269      -1.876  -5.021   0.362  0.60 40.74           C  
ATOM   2156  CB BMET A 269      -1.843  -5.010   0.431  0.40 41.48           C  
ATOM   2157  CG AMET A 269      -1.229  -4.130   1.376  0.60 41.35           C  
ATOM   2158  CG BMET A 269      -1.456  -4.043  -0.673  0.40 43.21           C  
ATOM   2159  SD AMET A 269       0.445  -3.824   0.836  0.60 45.38           S  
ATOM   2160  SD BMET A 269       0.287  -3.598  -0.625  0.40 47.28           S  
ATOM   2161  CE AMET A 269       0.138  -2.711  -0.567  0.60 45.06           C  
ATOM   2162  CE BMET A 269       0.384  -2.921   1.042  0.40 49.13           C  
ATOM   2163  N   GLU A 270      -4.673  -5.286  -1.464  1.00 42.30           N  
ATOM   2164  CA  GLU A 270      -5.317  -5.942  -2.605  1.00 44.54           C  
ATOM   2165  C   GLU A 270      -4.446  -6.059  -3.873  1.00 47.58           C  
ATOM   2166  O   GLU A 270      -4.907  -6.474  -4.944  1.00 50.73           O  
ATOM   2167  CB  GLU A 270      -6.710  -5.329  -2.850  1.00 45.88           C  
ATOM   2168  CG  GLU A 270      -7.669  -5.900  -1.806  1.00 48.14           C  
ATOM   2169  CD  GLU A 270      -9.012  -5.197  -1.729  1.00 56.65           C  
ATOM   2170  OE1 GLU A 270      -9.268  -4.270  -2.535  1.00 53.19           O  
ATOM   2171  OE2 GLU A 270      -9.814  -5.600  -0.853  1.00 55.92           O  
ATOM   2172  N   SER A 271      -3.161  -5.796  -3.715  1.00 43.94           N  
ATOM   2173  CA  SER A 271      -2.221  -5.617  -4.819  1.00 42.85           C  
ATOM   2174  C   SER A 271      -1.689  -6.934  -5.374  1.00 41.07           C  
ATOM   2175  O   SER A 271      -1.642  -7.936  -4.661  1.00 37.93           O  
ATOM   2176  CB  SER A 271      -1.047  -4.790  -4.280  1.00 44.94           C  
ATOM   2177  OG  SER A 271       0.124  -5.090  -5.004  1.00 52.04           O  
ATOM   2178  N   ALA A 272      -1.260  -6.932  -6.638  1.00 39.28           N  
ATOM   2179  CA  ALA A 272      -0.500  -8.071  -7.186  1.00 37.41           C  
ATOM   2180  C   ALA A 272       0.774  -8.286  -6.390  1.00 36.81           C  
ATOM   2181  O   ALA A 272       1.398  -7.300  -5.941  1.00 35.73           O  
ATOM   2182  CB  ALA A 272      -0.115  -7.778  -8.632  1.00 37.93           C  
ATOM   2183  N   GLY A 273       1.184  -9.549  -6.240  1.00 33.62           N  
ATOM   2184  CA  GLY A 273       2.497  -9.879  -5.650  1.00 35.78           C  
ATOM   2185  C   GLY A 273       3.667  -9.552  -6.569  1.00 34.27           C  
ATOM   2186  O   GLY A 273       3.471  -9.186  -7.730  1.00 33.58           O  
ATOM   2187  N   ILE A 274       4.885  -9.721  -6.073  1.00 34.95           N  
ATOM   2188  CA  ILE A 274       6.085  -9.300  -6.817  1.00 35.49           C  
ATOM   2189  C   ILE A 274       6.330 -10.101  -8.094  1.00 36.65           C  
ATOM   2190  O   ILE A 274       6.954  -9.618  -9.050  1.00 36.72           O  
ATOM   2191  CB  ILE A 274       7.358  -9.297  -5.945  1.00 36.37           C  
ATOM   2192  CG1 ILE A 274       7.585 -10.657  -5.268  1.00 33.25           C  
ATOM   2193  CG2 ILE A 274       7.272  -8.160  -4.880  1.00 39.71           C  
ATOM   2194  CD1 ILE A 274       9.002 -10.726  -4.588  1.00 38.09           C  
ATOM   2195  N   HIS A 275       5.866 -11.339  -8.123  1.00 35.06           N  
ATOM   2196  CA  HIS A 275       6.019 -12.102  -9.360  1.00 37.67           C  
ATOM   2197  C   HIS A 275       5.114 -11.530 -10.475  1.00 38.35           C  
ATOM   2198  O   HIS A 275       5.499 -11.498 -11.667  1.00 35.45           O  
ATOM   2199  CB  HIS A 275       5.687 -13.593  -9.128  1.00 36.26           C  
ATOM   2200  CG  HIS A 275       4.326 -13.832  -8.546  1.00 35.88           C  
ATOM   2201  ND1 HIS A 275       3.889 -13.238  -7.380  1.00 39.06           N  
ATOM   2202  CD2 HIS A 275       3.312 -14.629  -8.968  1.00 36.58           C  
ATOM   2203  CE1 HIS A 275       2.654 -13.636  -7.120  1.00 38.02           C  
ATOM   2204  NE2 HIS A 275       2.277 -14.483  -8.069  1.00 38.52           N  
ATOM   2205  N   GLU A 276       3.913 -11.119 -10.070  1.00 37.18           N  
ATOM   2206  CA AGLU A 276       2.908 -10.568 -10.968  0.50 38.71           C  
ATOM   2207  CA BGLU A 276       2.950 -10.595 -11.021  0.50 39.84           C  
ATOM   2208  C   GLU A 276       3.319  -9.174 -11.417  1.00 38.58           C  
ATOM   2209  O   GLU A 276       3.117  -8.778 -12.567  1.00 39.70           O  
ATOM   2210  CB AGLU A 276       1.541 -10.528 -10.265  0.50 40.29           C  
ATOM   2211  CB BGLU A 276       1.518 -10.691 -10.479  0.50 41.12           C  
ATOM   2212  CG AGLU A 276       1.004 -11.911  -9.888  0.50 37.98           C  
ATOM   2213  CG BGLU A 276       0.460 -10.024 -11.347  0.50 43.72           C  
ATOM   2214  CD AGLU A 276      -0.191 -11.921  -8.929  0.50 41.86           C  
ATOM   2215  CD BGLU A 276      -0.959 -10.475 -11.018  0.50 44.90           C  
ATOM   2216  OE1AGLU A 276      -1.230 -12.448  -9.363  0.50 40.50           O  
ATOM   2217  OE1BGLU A 276      -1.910  -9.948 -11.641  0.50 46.56           O  
ATOM   2218  OE2AGLU A 276      -0.117 -11.461  -7.762  0.50 40.63           O  
ATOM   2219  OE2BGLU A 276      -1.120 -11.344 -10.128  0.50 45.96           O  
ATOM   2220  N   THR A 277       3.879  -8.381 -10.506  1.00 37.23           N  
ATOM   2221  CA  THR A 277       4.250  -7.041 -10.955  1.00 38.67           C  
ATOM   2222  C   THR A 277       5.482  -7.139 -11.867  1.00 38.88           C  
ATOM   2223  O   THR A 277       5.670  -6.331 -12.778  1.00 38.58           O  
ATOM   2224  CB  THR A 277       4.497  -6.066  -9.770  1.00 40.92           C  
ATOM   2225  OG1 THR A 277       5.540  -6.571  -8.928  1.00 42.71           O  
ATOM   2226  CG2 THR A 277       3.199  -5.893  -8.942  1.00 44.35           C  
ATOM   2227  N   THR A 278       6.339  -8.132 -11.633  1.00 34.84           N  
ATOM   2228  CA  THR A 278       7.476  -8.360 -12.539  1.00 34.24           C  
ATOM   2229  C   THR A 278       7.012  -8.698 -13.963  1.00 35.90           C  
ATOM   2230  O   THR A 278       7.372  -8.053 -14.973  1.00 36.11           O  
ATOM   2231  CB  THR A 278       8.376  -9.505 -12.021  1.00 35.03           C  
ATOM   2232  OG1 THR A 278       8.974  -9.133 -10.764  1.00 37.85           O  
ATOM   2233  CG2 THR A 278       9.497  -9.732 -13.021  1.00 39.82           C  
ATOM   2234  N   TYR A 279       6.113  -9.663 -14.036  1.00 36.38           N  
ATOM   2235  CA  TYR A 279       5.528 -10.031 -15.312  1.00 36.79           C  
ATOM   2236  C   TYR A 279       4.817  -8.847 -15.967  1.00 37.37           C  
ATOM   2237  O   TYR A 279       5.004  -8.554 -17.163  1.00 35.90           O  
ATOM   2238  CB  TYR A 279       4.523 -11.125 -15.051  1.00 36.95           C  
ATOM   2239  CG  TYR A 279       3.816 -11.570 -16.312  1.00 38.91           C  
ATOM   2240  CD1 TYR A 279       4.507 -12.212 -17.323  1.00 39.03           C  
ATOM   2241  CD2 TYR A 279       2.470 -11.325 -16.479  1.00 38.34           C  
ATOM   2242  CE1 TYR A 279       3.854 -12.598 -18.490  1.00 39.13           C  
ATOM   2243  CE2 TYR A 279       1.811 -11.722 -17.625  1.00 41.64           C  
ATOM   2244  CZ  TYR A 279       2.508 -12.371 -18.607  1.00 38.68           C  
ATOM   2245  OH  TYR A 279       1.835 -12.753 -19.736  1.00 43.06           O  
ATOM   2246  N   ASN A 280       3.973  -8.155 -15.205  1.00 35.69           N  
ATOM   2247  CA  ASN A 280       3.248  -7.023 -15.772  1.00 37.08           C  
ATOM   2248  C   ASN A 280       4.151  -5.943 -16.345  1.00 38.55           C  
ATOM   2249  O   ASN A 280       3.825  -5.316 -17.347  1.00 35.87           O  
ATOM   2250  CB  ASN A 280       2.378  -6.371 -14.686  1.00 38.20           C  
ATOM   2251  CG  ASN A 280       1.180  -7.242 -14.254  1.00 44.23           C  
ATOM   2252  OD1 ASN A 280       0.550  -6.998 -13.197  1.00 46.69           O  
ATOM   2253  ND2 ASN A 280       0.829  -8.222 -15.077  1.00 39.76           N  
ATOM   2254  N   SER A 281       5.253  -5.653 -15.646  1.00 35.87           N  
ATOM   2255  CA  SER A 281       6.269  -4.703 -16.120  1.00 37.07           C  
ATOM   2256  C   SER A 281       6.929  -5.142 -17.434  1.00 35.95           C  
ATOM   2257  O   SER A 281       7.053  -4.359 -18.372  1.00 37.27           O  
ATOM   2258  CB  SER A 281       7.308  -4.599 -15.019  1.00 36.54           C  
ATOM   2259  OG  SER A 281       8.313  -3.613 -15.275  1.00 42.41           O  
ATOM   2260  N   ILE A 282       7.312  -6.404 -17.522  1.00 36.01           N  
ATOM   2261  CA  ILE A 282       7.907  -6.940 -18.754  1.00 35.38           C  
ATOM   2262  C   ILE A 282       6.862  -6.783 -19.895  1.00 37.83           C  
ATOM   2263  O   ILE A 282       7.191  -6.395 -21.034  1.00 35.45           O  
ATOM   2264  CB  ILE A 282       8.332  -8.410 -18.538  1.00 36.22           C  
ATOM   2265  CG1 ILE A 282       9.566  -8.500 -17.640  1.00 32.78           C  
ATOM   2266  CG2 ILE A 282       8.716  -9.113 -19.871  1.00 37.29           C  
ATOM   2267  CD1 ILE A 282       9.821  -9.968 -17.116  1.00 38.15           C  
ATOM   2268  N   MET A 283       5.601  -7.069 -19.580  1.00 36.77           N  
ATOM   2269  CA  MET A 283       4.527  -7.007 -20.595  1.00 38.43           C  
ATOM   2270  C   MET A 283       4.208  -5.586 -21.027  1.00 39.16           C  
ATOM   2271  O   MET A 283       3.633  -5.410 -22.078  1.00 38.97           O  
ATOM   2272  CB  MET A 283       3.263  -7.731 -20.127  1.00 39.13           C  
ATOM   2273  CG  MET A 283       3.448  -9.268 -20.013  1.00 37.63           C  
ATOM   2274  SD  MET A 283       3.994  -9.997 -21.588  1.00 46.20           S  
ATOM   2275  CE  MET A 283       2.500  -9.803 -22.537  1.00 45.31           C  
ATOM   2276  N   LYS A 284       4.575  -4.570 -20.244  1.00 37.08           N  
ATOM   2277  CA  LYS A 284       4.487  -3.199 -20.736  1.00 36.58           C  
ATOM   2278  C   LYS A 284       5.584  -2.815 -21.722  1.00 37.10           C  
ATOM   2279  O   LYS A 284       5.485  -1.767 -22.353  1.00 39.52           O  
ATOM   2280  CB  LYS A 284       4.485  -2.196 -19.574  1.00 36.53           C  
ATOM   2281  CG  LYS A 284       3.129  -2.293 -18.844  1.00 41.42           C  
ATOM   2282  CD  LYS A 284       2.946  -1.242 -17.799  1.00 53.84           C  
ATOM   2283  CE  LYS A 284       1.546  -1.318 -17.195  1.00 63.40           C  
ATOM   2284  NZ  LYS A 284       1.512  -0.571 -15.888  1.00 68.66           N  
ATOM   2285  N   CYS A 285       6.624  -3.627 -21.832  1.00 37.20           N  
ATOM   2286  CA  CYS A 285       7.733  -3.330 -22.749  1.00 38.58           C  
ATOM   2287  C   CYS A 285       7.492  -3.931 -24.132  1.00 40.03           C  
ATOM   2288  O   CYS A 285       6.804  -4.949 -24.261  1.00 39.06           O  
ATOM   2289  CB  CYS A 285       9.060  -3.855 -22.185  1.00 36.01           C  
ATOM   2290  SG  CYS A 285       9.436  -3.062 -20.585  1.00 38.64           S  
ATOM   2291  N   ASP A 286       8.068  -3.287 -25.144  1.00 38.78           N  
ATOM   2292  CA  ASP A 286       8.100  -3.858 -26.488  1.00 41.07           C  
ATOM   2293  C   ASP A 286       8.437  -5.344 -26.479  1.00 39.80           C  
ATOM   2294  O   ASP A 286       9.413  -5.779 -25.868  1.00 37.66           O  
ATOM   2295  CB  ASP A 286       9.194  -3.195 -27.314  1.00 42.04           C  
ATOM   2296  CG  ASP A 286       8.838  -1.798 -27.767  1.00 50.64           C  
ATOM   2297  OD1 ASP A 286       7.733  -1.314 -27.432  1.00 56.35           O  
ATOM   2298  OD2 ASP A 286       9.683  -1.208 -28.494  1.00 61.66           O  
ATOM   2299  N   ILE A 287       7.691  -6.114 -27.267  1.00 37.66           N  
ATOM   2300  CA  ILE A 287       7.877  -7.554 -27.250  1.00 39.35           C  
ATOM   2301  C   ILE A 287       9.303  -7.924 -27.600  1.00 38.47           C  
ATOM   2302  O   ILE A 287       9.825  -8.923 -27.114  1.00 39.03           O  
ATOM   2303  CB  ILE A 287       6.859  -8.264 -28.182  1.00 39.10           C  
ATOM   2304  CG1 ILE A 287       6.981  -9.785 -28.073  1.00 41.46           C  
ATOM   2305  CG2 ILE A 287       7.010  -7.754 -29.590  1.00 41.81           C  
ATOM   2306  CD1 ILE A 287       5.831 -10.543 -28.789  1.00 44.47           C  
ATOM   2307  N   ASP A 288       9.952  -7.138 -28.451  1.00 38.60           N  
ATOM   2308  CA  ASP A 288      11.288  -7.510 -28.907  1.00 41.60           C  
ATOM   2309  C   ASP A 288      12.388  -7.377 -27.832  1.00 41.38           C  
ATOM   2310  O   ASP A 288      13.490  -7.873 -28.018  1.00 44.53           O  
ATOM   2311  CB  ASP A 288      11.605  -6.693 -30.159  1.00 45.91           C  
ATOM   2312  CG  ASP A 288      10.326  -6.319 -30.927  1.00 55.88           C  
ATOM   2313  OD2 ASP A 288      10.090  -6.924 -31.997  1.00 64.27           O  
ATOM   2314  OD1 ASP A 288       9.533  -5.457 -30.436  1.00 59.82           O  
ATOM   2315  N   ILE A 289      12.118  -6.710 -26.719  1.00 36.74           N  
ATOM   2316  CA  ILE A 289      13.135  -6.727 -25.665  1.00 38.57           C  
ATOM   2317  C   ILE A 289      12.822  -7.697 -24.504  1.00 37.26           C  
ATOM   2318  O   ILE A 289      13.628  -7.873 -23.578  1.00 35.76           O  
ATOM   2319  CB  ILE A 289      13.458  -5.309 -25.141  1.00 39.55           C  
ATOM   2320  CG1 ILE A 289      12.361  -4.803 -24.219  1.00 36.61           C  
ATOM   2321  CG2 ILE A 289      13.708  -4.366 -26.331  1.00 40.04           C  
ATOM   2322  CD1 ILE A 289      12.838  -3.702 -23.226  1.00 33.42           C  
ATOM   2323  N   ARG A 290      11.661  -8.340 -24.565  1.00 36.64           N  
ATOM   2324  CA  ARG A 290      11.207  -9.169 -23.432  1.00 35.69           C  
ATOM   2325  C   ARG A 290      12.099 -10.390 -23.176  1.00 37.30           C  
ATOM   2326  O   ARG A 290      12.331 -10.744 -22.015  1.00 37.16           O  
ATOM   2327  CB  ARG A 290       9.741  -9.596 -23.617  1.00 37.80           C  
ATOM   2328  CG  ARG A 290       8.737  -8.452 -23.463  1.00 34.39           C  
ATOM   2329  CD  ARG A 290       7.323  -8.981 -23.664  1.00 39.95           C  
ATOM   2330  NE  ARG A 290       6.419  -7.880 -23.967  1.00 39.50           N  
ATOM   2331  CZ  ARG A 290       5.259  -8.006 -24.598  1.00 39.92           C  
ATOM   2332  NH1 ARG A 290       4.852  -9.192 -25.064  1.00 38.35           N  
ATOM   2333  NH2 ARG A 290       4.552  -6.905 -24.849  1.00 41.15           N  
ATOM   2334  N   LYS A 291      12.588 -11.037 -24.239  1.00 37.68           N  
ATOM   2335  CA  LYS A 291      13.470 -12.174 -24.073  1.00 40.53           C  
ATOM   2336  C   LYS A 291      14.632 -11.749 -23.171  1.00 38.94           C  
ATOM   2337  O   LYS A 291      15.030 -12.489 -22.251  1.00 39.41           O  
ATOM   2338  CB  LYS A 291      13.957 -12.632 -25.457  1.00 37.76           C  
ATOM   2339  CG  LYS A 291      14.864 -13.848 -25.523  1.00 47.02           C  
ATOM   2340  CD  LYS A 291      15.170 -14.166 -27.001  1.00 45.73           C  
ATOM   2341  CE  LYS A 291      16.163 -15.314 -27.165  1.00 57.63           C  
ATOM   2342  NZ  LYS A 291      17.521 -14.939 -26.667  1.00 58.64           N  
ATOM   2343  N   ASP A 292      15.190 -10.565 -23.430  1.00 36.73           N  
ATOM   2344  CA  ASP A 292      16.333 -10.100 -22.632  1.00 39.44           C  
ATOM   2345  C   ASP A 292      16.000  -9.708 -21.206  1.00 39.09           C  
ATOM   2346  O   ASP A 292      16.824  -9.872 -20.316  1.00 41.45           O  
ATOM   2347  CB  ASP A 292      17.078  -8.949 -23.303  1.00 38.60           C  
ATOM   2348  CG  ASP A 292      17.710  -9.392 -24.617  1.00 49.38           C  
ATOM   2349  OD1 ASP A 292      18.361 -10.460 -24.629  1.00 48.04           O  
ATOM   2350  OD2 ASP A 292      17.527  -8.685 -25.626  1.00 52.81           O  
ATOM   2351  N   LEU A 293      14.797  -9.197 -20.980  1.00 36.07           N  
ATOM   2352  CA  LEU A 293      14.368  -8.906 -19.620  1.00 33.86           C  
ATOM   2353  C   LEU A 293      14.163 -10.201 -18.831  1.00 36.12           C  
ATOM   2354  O   LEU A 293      14.646 -10.329 -17.696  1.00 36.15           O  
ATOM   2355  CB  LEU A 293      13.056  -8.112 -19.649  1.00 36.27           C  
ATOM   2356  CG  LEU A 293      13.084  -6.731 -20.315  1.00 35.32           C  
ATOM   2357  CD1 LEU A 293      11.686  -6.066 -20.113  1.00 36.42           C  
ATOM   2358  CD2 LEU A 293      14.227  -5.837 -19.731  1.00 36.73           C  
ATOM   2359  N   TYR A 294      13.474 -11.180 -19.413  1.00 35.87           N  
ATOM   2360  CA  TYR A 294      13.249 -12.461 -18.714  1.00 35.02           C  
ATOM   2361  C   TYR A 294      14.556 -13.191 -18.376  1.00 35.97           C  
ATOM   2362  O   TYR A 294      14.606 -13.935 -17.392  1.00 36.78           O  
ATOM   2363  CB  TYR A 294      12.452 -13.441 -19.578  1.00 37.25           C  
ATOM   2364  CG  TYR A 294      10.968 -13.211 -19.642  1.00 37.48           C  
ATOM   2365  CD1 TYR A 294      10.171 -13.359 -18.515  1.00 36.91           C  
ATOM   2366  CD2 TYR A 294      10.351 -12.933 -20.862  1.00 39.27           C  
ATOM   2367  CE1 TYR A 294       8.796 -13.168 -18.583  1.00 39.77           C  
ATOM   2368  CE2 TYR A 294       8.959 -12.795 -20.945  1.00 40.35           C  
ATOM   2369  CZ  TYR A 294       8.199 -12.887 -19.791  1.00 36.91           C  
ATOM   2370  OH  TYR A 294       6.816 -12.749 -19.847  1.00 43.40           O  
ATOM   2371  N   ALA A 295      15.594 -13.045 -19.196  1.00 34.20           N  
ATOM   2372  CA  ALA A 295      16.866 -13.734 -18.948  1.00 35.39           C  
ATOM   2373  C   ALA A 295      17.787 -12.926 -18.010  1.00 34.96           C  
ATOM   2374  O   ALA A 295      18.912 -13.345 -17.730  1.00 36.89           O  
ATOM   2375  CB  ALA A 295      17.564 -13.992 -20.280  1.00 37.31           C  
ATOM   2376  N   ASN A 296      17.339 -11.753 -17.558  1.00 36.70           N  
ATOM   2377  CA  ASN A 296      18.181 -10.845 -16.743  1.00 35.39           C  
ATOM   2378  C   ASN A 296      17.339 -10.136 -15.687  1.00 36.23           C  
ATOM   2379  O   ASN A 296      17.340  -8.895 -15.619  1.00 35.81           O  
ATOM   2380  CB  ASN A 296      18.922  -9.799 -17.627  1.00 37.08           C  
ATOM   2381  CG  ASN A 296      19.910 -10.423 -18.613  1.00 37.98           C  
ATOM   2382  OD1 ASN A 296      21.023 -10.722 -18.213  1.00 36.28           O  
ATOM   2383  ND2 ASN A 296      19.522 -10.610 -19.899  1.00 35.82           N  
ATOM   2384  N   ASN A 297      16.664 -10.920 -14.835  1.00 34.89           N  
ATOM   2385  CA AASN A 297      15.921 -10.416 -13.670  0.50 37.59           C  
ATOM   2386  CA BASN A 297      15.933 -10.355 -13.702  0.50 36.60           C  
ATOM   2387  C   ASN A 297      16.895 -10.279 -12.517  1.00 37.36           C  
ATOM   2388  O   ASN A 297      17.285 -11.294 -11.924  1.00 40.03           O  
ATOM   2389  CB AASN A 297      14.882 -11.416 -13.163  0.50 37.12           C  
ATOM   2390  CB BASN A 297      14.677 -11.194 -13.440  0.50 34.47           C  
ATOM   2391  CG AASN A 297      13.651 -11.512 -14.023  0.50 42.19           C  
ATOM   2392  CG BASN A 297      13.792 -10.695 -12.309  0.50 37.30           C  
ATOM   2393  OD1AASN A 297      12.697 -10.750 -13.849  0.50 44.67           O  
ATOM   2394  OD1BASN A 297      13.009 -11.501 -11.795  0.50 40.91           O  
ATOM   2395  ND2AASN A 297      13.614 -12.527 -14.885  0.50 46.19           N  
ATOM   2396  ND2BASN A 297      13.842  -9.405 -11.948  0.50 32.31           N  
ATOM   2397  N   VAL A 298      17.269  -9.058 -12.191  1.00 36.44           N  
ATOM   2398  CA  VAL A 298      18.256  -8.811 -11.163  1.00 37.17           C  
ATOM   2399  C   VAL A 298      17.558  -8.345  -9.894  1.00 38.28           C  
ATOM   2400  O   VAL A 298      16.779  -7.390  -9.932  1.00 37.94           O  
ATOM   2401  CB  VAL A 298      19.241  -7.725 -11.665  1.00 37.29           C  
ATOM   2402  CG1 VAL A 298      20.158  -7.239 -10.486  1.00 40.34           C  
ATOM   2403  CG2 VAL A 298      20.086  -8.285 -12.818  1.00 37.68           C  
ATOM   2404  N   MET A 299      17.849  -9.017  -8.777  1.00 35.87           N  
ATOM   2405  CA AMET A 299      17.298  -8.599  -7.496  0.60 36.82           C  
ATOM   2406  CA BMET A 299      17.310  -8.664  -7.466  0.40 37.23           C  
ATOM   2407  C   MET A 299      18.245  -7.720  -6.709  1.00 36.13           C  
ATOM   2408  O   MET A 299      19.456  -7.953  -6.681  1.00 36.73           O  
ATOM   2409  CB AMET A 299      17.002  -9.833  -6.656  0.60 37.66           C  
ATOM   2410  CB BMET A 299      17.153  -9.956  -6.652  0.40 37.55           C  
ATOM   2411  CG AMET A 299      15.833 -10.559  -7.257  0.60 38.23           C  
ATOM   2412  CG BMET A 299      16.360 -11.022  -7.421  0.40 42.21           C  
ATOM   2413  SD AMET A 299      15.463 -11.957  -6.211  0.60 38.52           S  
ATOM   2414  SD BMET A 299      14.574 -10.824  -7.273  0.40 48.70           S  
ATOM   2415  CE AMET A 299      13.887 -12.362  -6.916  0.60 37.33           C  
ATOM   2416  CE BMET A 299      14.281 -11.632  -5.710  0.40 43.21           C  
ATOM   2417  N   SER A 300      17.662  -6.730  -6.038  1.00 35.67           N  
ATOM   2418  CA  SER A 300      18.407  -5.674  -5.375  1.00 36.81           C  
ATOM   2419  C   SER A 300      17.711  -5.273  -4.070  1.00 37.65           C  
ATOM   2420  O   SER A 300      16.498  -5.214  -4.032  1.00 38.70           O  
ATOM   2421  CB  SER A 300      18.338  -4.438  -6.309  1.00 37.94           C  
ATOM   2422  OG  SER A 300      19.243  -3.490  -5.813  1.00 50.53           O  
ATOM   2423  N   GLY A 301      18.456  -4.950  -3.010  1.00 36.51           N  
ATOM   2424  CA  GLY A 301      17.749  -4.393  -1.852  1.00 34.00           C  
ATOM   2425  C   GLY A 301      17.717  -5.392  -0.689  1.00 34.81           C  
ATOM   2426  O   GLY A 301      17.677  -6.600  -0.902  1.00 35.97           O  
ATOM   2427  N   GLY A 302      17.641  -4.874   0.527  1.00 32.90           N  
ATOM   2428  CA  GLY A 302      17.668  -5.764   1.716  1.00 35.83           C  
ATOM   2429  C   GLY A 302      16.540  -6.793   1.738  1.00 36.15           C  
ATOM   2430  O   GLY A 302      16.687  -7.906   2.246  1.00 36.37           O  
ATOM   2431  N   THR A 303      15.376  -6.423   1.216  1.00 35.74           N  
ATOM   2432  CA  THR A 303      14.210  -7.301   1.341  1.00 36.52           C  
ATOM   2433  C   THR A 303      14.204  -8.417   0.299  1.00 37.21           C  
ATOM   2434  O   THR A 303      13.367  -9.327   0.332  1.00 38.14           O  
ATOM   2435  CB  THR A 303      12.906  -6.449   1.419  1.00 34.89           C  
ATOM   2436  OG1 THR A 303      12.854  -5.806   2.691  1.00 35.28           O  
ATOM   2437  CG2 THR A 303      11.595  -7.262   1.223  1.00 34.59           C  
ATOM   2438  N   THR A 304      15.149  -8.374  -0.631  1.00 36.84           N  
ATOM   2439  CA  THR A 304      15.369  -9.531  -1.499  1.00 37.03           C  
ATOM   2440  C   THR A 304      16.397 -10.511  -0.942  1.00 37.14           C  
ATOM   2441  O   THR A 304      16.747 -11.472  -1.631  1.00 39.72           O  
ATOM   2442  CB  THR A 304      15.882  -9.139  -2.924  1.00 36.72           C  
ATOM   2443  OG1 THR A 304      17.234  -8.663  -2.861  1.00 35.92           O  
ATOM   2444  CG2 THR A 304      15.005  -8.088  -3.519  1.00 35.86           C  
ATOM   2445  N   MET A 305      16.868 -10.299   0.291  1.00 35.95           N  
ATOM   2446  CA  MET A 305      17.903 -11.175   0.836  1.00 34.98           C  
ATOM   2447  C   MET A 305      17.402 -12.559   1.317  1.00 37.74           C  
ATOM   2448  O   MET A 305      18.230 -13.423   1.648  1.00 39.66           O  
ATOM   2449  CB  MET A 305      18.656 -10.465   1.989  1.00 33.40           C  
ATOM   2450  CG  MET A 305      19.505  -9.292   1.541  1.00 40.93           C  
ATOM   2451  SD  MET A 305      20.911  -9.908   0.595  1.00 44.72           S  
ATOM   2452  CE  MET A 305      21.812 -10.796   1.891  1.00 48.35           C  
ATOM   2453  N   TYR A 306      16.086 -12.790   1.378  1.00 35.31           N  
ATOM   2454  CA  TYR A 306      15.556 -14.076   1.903  1.00 35.99           C  
ATOM   2455  C   TYR A 306      16.121 -15.248   1.127  1.00 34.86           C  
ATOM   2456  O   TYR A 306      16.041 -15.265  -0.111  1.00 34.63           O  
ATOM   2457  CB  TYR A 306      14.019 -14.147   1.818  1.00 35.40           C  
ATOM   2458  CG  TYR A 306      13.355 -13.074   2.702  1.00 34.90           C  
ATOM   2459  CD2 TYR A 306      12.964 -11.839   2.181  1.00 33.64           C  
ATOM   2460  CD1 TYR A 306      13.196 -13.289   4.059  1.00 36.42           C  
ATOM   2461  CE2 TYR A 306      12.417 -10.864   2.992  1.00 36.28           C  
ATOM   2462  CE1 TYR A 306      12.663 -12.308   4.891  1.00 36.77           C  
ATOM   2463  CZ  TYR A 306      12.301 -11.097   4.370  1.00 35.69           C  
ATOM   2464  OH  TYR A 306      11.743 -10.173   5.237  1.00 39.22           O  
ATOM   2465  N   PRO A 307      16.610 -16.271   1.838  1.00 34.42           N  
ATOM   2466  CA  PRO A 307      16.883 -17.528   1.135  1.00 33.72           C  
ATOM   2467  C   PRO A 307      15.647 -18.031   0.407  1.00 34.94           C  
ATOM   2468  O   PRO A 307      14.537 -17.898   0.937  1.00 34.91           O  
ATOM   2469  CB  PRO A 307      17.202 -18.514   2.282  1.00 33.39           C  
ATOM   2470  CG  PRO A 307      17.858 -17.595   3.374  1.00 35.58           C  
ATOM   2471  CD  PRO A 307      16.981 -16.309   3.275  1.00 34.75           C  
ATOM   2472  N   GLY A 308      15.820 -18.655  -0.760  1.00 31.97           N  
ATOM   2473  CA  GLY A 308      14.620 -19.173  -1.471  1.00 32.81           C  
ATOM   2474  C   GLY A 308      13.995 -18.182  -2.465  1.00 33.48           C  
ATOM   2475  O   GLY A 308      13.166 -18.563  -3.314  1.00 35.12           O  
ATOM   2476  N   ILE A 309      14.271 -16.888  -2.324  1.00 33.84           N  
ATOM   2477  CA  ILE A 309      13.461 -15.924  -3.084  1.00 36.40           C  
ATOM   2478  C   ILE A 309      13.732 -16.015  -4.578  1.00 34.49           C  
ATOM   2479  O   ILE A 309      12.776 -15.931  -5.386  1.00 34.44           O  
ATOM   2480  CB  ILE A 309      13.631 -14.446  -2.596  1.00 37.17           C  
ATOM   2481  CG1 ILE A 309      12.520 -13.595  -3.220  1.00 39.12           C  
ATOM   2482  CG2 ILE A 309      14.976 -13.875  -2.990  1.00 40.00           C  
ATOM   2483  CD1 ILE A 309      12.426 -12.170  -2.550  1.00 41.47           C  
ATOM   2484  N   ALA A 310      15.003 -16.224  -4.952  1.00 35.49           N  
ATOM   2485  CA  ALA A 310      15.337 -16.358  -6.375  1.00 35.59           C  
ATOM   2486  C   ALA A 310      14.691 -17.592  -6.997  1.00 34.79           C  
ATOM   2487  O   ALA A 310      14.101 -17.505  -8.070  1.00 35.25           O  
ATOM   2488  CB  ALA A 310      16.849 -16.333  -6.620  1.00 38.24           C  
ATOM   2489  N   ASP A 311      14.772 -18.737  -6.322  1.00 34.47           N  
ATOM   2490  CA  ASP A 311      14.093 -19.928  -6.830  1.00 34.90           C  
ATOM   2491  C   ASP A 311      12.586 -19.772  -6.994  1.00 33.80           C  
ATOM   2492  O   ASP A 311      11.985 -20.310  -7.917  1.00 31.75           O  
ATOM   2493  CB  ASP A 311      14.386 -21.129  -5.918  1.00 34.39           C  
ATOM   2494  CG  ASP A 311      15.871 -21.528  -5.951  1.00 47.57           C  
ATOM   2495  OD2 ASP A 311      16.218 -22.527  -6.597  1.00 52.46           O  
ATOM   2496  OD1 ASP A 311      16.697 -20.811  -5.340  1.00 64.37           O  
ATOM   2497  N   ARG A 312      11.951 -19.113  -6.041  1.00 32.63           N  
ATOM   2498  CA  ARG A 312      10.513 -18.976  -6.085  1.00 33.35           C  
ATOM   2499  C   ARG A 312      10.177 -17.982  -7.216  1.00 32.68           C  
ATOM   2500  O   ARG A 312       9.266 -18.225  -7.982  1.00 32.90           O  
ATOM   2501  CB  ARG A 312      10.013 -18.460  -4.715  1.00 32.12           C  
ATOM   2502  CG  ARG A 312       8.512 -18.093  -4.718  1.00 33.06           C  
ATOM   2503  CD  ARG A 312       7.600 -19.347  -4.755  1.00 33.84           C  
ATOM   2504  NE  ARG A 312       6.206 -18.894  -4.682  1.00 33.62           N  
ATOM   2505  CZ  ARG A 312       5.613 -18.565  -3.537  1.00 38.24           C  
ATOM   2506  NH1 ARG A 312       6.249 -18.736  -2.372  1.00 35.97           N  
ATOM   2507  NH2 ARG A 312       4.383 -18.048  -3.556  1.00 37.38           N  
ATOM   2508  N   MET A 313      10.942 -16.903  -7.383  1.00 33.91           N  
ATOM   2509  CA AMET A 313      10.706 -16.004  -8.520  0.50 34.63           C  
ATOM   2510  CA BMET A 313      10.698 -16.015  -8.521  0.50 35.27           C  
ATOM   2511  C   MET A 313      10.866 -16.740  -9.853  1.00 34.42           C  
ATOM   2512  O   MET A 313      10.081 -16.558 -10.777  1.00 34.98           O  
ATOM   2513  CB AMET A 313      11.647 -14.790  -8.457  0.50 34.06           C  
ATOM   2514  CB BMET A 313      11.603 -14.778  -8.442  0.50 35.18           C  
ATOM   2515  CG AMET A 313      11.332 -13.711  -9.492  0.50 33.45           C  
ATOM   2516  CG BMET A 313      11.128 -13.793  -7.386  0.50 37.78           C  
ATOM   2517  SD AMET A 313       9.711 -12.917  -9.369  0.50 34.91           S  
ATOM   2518  SD BMET A 313       9.770 -12.696  -7.854  0.50 42.35           S  
ATOM   2519  CE AMET A 313      10.038 -11.701  -8.088  0.50 33.49           C  
ATOM   2520  CE BMET A 313       9.132 -13.472  -9.334  0.50 34.97           C  
ATOM   2521  N   GLN A 314      11.911 -17.555  -9.967  1.00 33.86           N  
ATOM   2522  CA  GLN A 314      12.122 -18.317 -11.208  1.00 34.56           C  
ATOM   2523  C   GLN A 314      10.896 -19.181 -11.525  1.00 37.02           C  
ATOM   2524  O   GLN A 314      10.413 -19.223 -12.660  1.00 36.22           O  
ATOM   2525  CB  GLN A 314      13.413 -19.172 -11.081  1.00 36.68           C  
ATOM   2526  CG  GLN A 314      13.624 -20.241 -12.192  1.00 43.00           C  
ATOM   2527  CD  GLN A 314      14.344 -19.682 -13.387  1.00 49.34           C  
ATOM   2528  OE1 GLN A 314      14.988 -18.639 -13.280  1.00 49.41           O  
ATOM   2529  NE2 GLN A 314      14.275 -20.383 -14.527  1.00 47.52           N  
ATOM   2530  N   LYS A 315      10.371 -19.859 -10.510  1.00 34.45           N  
ATOM   2531  CA  LYS A 315       9.192 -20.701 -10.675  1.00 35.38           C  
ATOM   2532  C   LYS A 315       7.944 -19.908 -11.105  1.00 35.70           C  
ATOM   2533  O   LYS A 315       7.210 -20.311 -12.047  1.00 33.99           O  
ATOM   2534  CB  LYS A 315       8.905 -21.417  -9.332  1.00 35.00           C  
ATOM   2535  CG  LYS A 315       7.617 -22.252  -9.321  1.00 34.47           C  
ATOM   2536  CD  LYS A 315       7.359 -22.903  -7.940  1.00 34.47           C  
ATOM   2537  CE  LYS A 315       6.033 -23.644  -7.896  1.00 36.92           C  
ATOM   2538  NZ  LYS A 315       5.700 -24.152  -6.529  1.00 38.58           N  
ATOM   2539  N   GLU A 316       7.699 -18.797 -10.404  1.00 33.56           N  
ATOM   2540  CA  GLU A 316       6.461 -18.041 -10.625  1.00 37.05           C  
ATOM   2541  C   GLU A 316       6.518 -17.324 -11.980  1.00 37.04           C  
ATOM   2542  O   GLU A 316       5.508 -17.266 -12.688  1.00 39.12           O  
ATOM   2543  CB  GLU A 316       6.197 -16.995  -9.527  1.00 37.08           C  
ATOM   2544  CG  GLU A 316       5.989 -17.574  -8.106  1.00 37.77           C  
ATOM   2545  CD  GLU A 316       4.835 -18.549  -8.028  1.00 45.80           C  
ATOM   2546  OE1 GLU A 316       4.020 -18.625  -8.982  1.00 42.68           O  
ATOM   2547  OE2 GLU A 316       4.743 -19.284  -7.016  1.00 46.00           O  
ATOM   2548  N   ILE A 317       7.684 -16.809 -12.357  1.00 35.83           N  
ATOM   2549  CA AILE A 317       7.772 -16.152 -13.654  0.50 36.75           C  
ATOM   2550  CA BILE A 317       7.841 -16.169 -13.666  0.50 35.95           C  
ATOM   2551  C   ILE A 317       7.693 -17.209 -14.776  1.00 35.59           C  
ATOM   2552  O   ILE A 317       7.033 -16.991 -15.772  1.00 35.67           O  
ATOM   2553  CB AILE A 317       9.006 -15.224 -13.757  0.50 37.60           C  
ATOM   2554  CB BILE A 317       9.223 -15.506 -13.827  0.50 36.78           C  
ATOM   2555  CG1AILE A 317       9.029 -14.246 -12.582  0.50 37.99           C  
ATOM   2556  CG1BILE A 317       9.353 -14.326 -12.871  0.50 33.94           C  
ATOM   2557  CG2AILE A 317       8.995 -14.467 -15.085  0.50 38.54           C  
ATOM   2558  CG2BILE A 317       9.438 -15.059 -15.286  0.50 35.47           C  
ATOM   2559  CD1AILE A 317      10.141 -13.208 -12.626  0.50 37.09           C  
ATOM   2560  CD1BILE A 317       8.186 -13.334 -12.949  0.50 33.15           C  
ATOM   2561  N   THR A 318       8.312 -18.374 -14.586  1.00 35.67           N  
ATOM   2562  CA  THR A 318       8.200 -19.485 -15.551  1.00 36.55           C  
ATOM   2563  C   THR A 318       6.726 -19.858 -15.788  1.00 38.42           C  
ATOM   2564  O   THR A 318       6.322 -20.073 -16.947  1.00 37.48           O  
ATOM   2565  CB  THR A 318       8.998 -20.726 -15.082  1.00 34.97           C  
ATOM   2566  OG1 THR A 318      10.398 -20.436 -15.076  1.00 36.52           O  
ATOM   2567  CG2 THR A 318       8.749 -21.967 -15.984  1.00 35.16           C  
ATOM   2568  N   ALA A 319       5.912 -19.867 -14.725  1.00 38.14           N  
ATOM   2569  CA  ALA A 319       4.473 -20.123 -14.845  1.00 37.82           C  
ATOM   2570  C   ALA A 319       3.703 -19.075 -15.660  1.00 40.40           C  
ATOM   2571  O   ALA A 319       2.723 -19.404 -16.359  1.00 41.25           O  
ATOM   2572  CB  ALA A 319       3.826 -20.300 -13.492  1.00 37.89           C  
ATOM   2573  N   LEU A 320       4.137 -17.827 -15.577  1.00 40.25           N  
ATOM   2574  CA  LEU A 320       3.525 -16.736 -16.348  1.00 39.54           C  
ATOM   2575  C   LEU A 320       4.064 -16.538 -17.770  1.00 40.40           C  
ATOM   2576  O   LEU A 320       3.326 -16.070 -18.650  1.00 38.69           O  
ATOM   2577  CB  LEU A 320       3.672 -15.429 -15.555  1.00 39.00           C  
ATOM   2578  CG  LEU A 320       2.960 -15.404 -14.201  1.00 39.50           C  
ATOM   2579  CD1 LEU A 320       3.484 -14.249 -13.343  1.00 43.45           C  
ATOM   2580  CD2 LEU A 320       1.419 -15.281 -14.412  1.00 43.90           C  
ATOM   2581  N   ALA A 321       5.341 -16.837 -18.001  1.00 37.19           N  
ATOM   2582  CA  ALA A 321       5.996 -16.546 -19.284  1.00 38.82           C  
ATOM   2583  C   ALA A 321       5.626 -17.600 -20.344  1.00 38.50           C  
ATOM   2584  O   ALA A 321       5.189 -18.698 -20.000  1.00 39.76           O  
ATOM   2585  CB  ALA A 321       7.519 -16.540 -19.100  1.00 38.56           C  
ATOM   2586  N   PRO A 322       5.850 -17.289 -21.628  1.00 40.92           N  
ATOM   2587  CA  PRO A 322       5.672 -18.249 -22.728  1.00 40.64           C  
ATOM   2588  C   PRO A 322       6.502 -19.492 -22.410  1.00 41.74           C  
ATOM   2589  O   PRO A 322       7.562 -19.382 -21.789  1.00 38.83           O  
ATOM   2590  CB  PRO A 322       6.289 -17.522 -23.919  1.00 42.31           C  
ATOM   2591  CG  PRO A 322       6.122 -16.096 -23.592  1.00 43.16           C  
ATOM   2592  CD  PRO A 322       6.291 -15.967 -22.116  1.00 40.52           C  
ATOM   2593  N   SER A 323       6.040 -20.662 -22.821  1.00 41.10           N  
ATOM   2594  CA  SER A 323       6.598 -21.898 -22.261  1.00 45.94           C  
ATOM   2595  C   SER A 323       8.035 -22.190 -22.708  1.00 46.08           C  
ATOM   2596  O   SER A 323       8.750 -22.960 -22.058  1.00 48.29           O  
ATOM   2597  CB  SER A 323       5.701 -23.093 -22.614  1.00 45.02           C  
ATOM   2598  OG  SER A 323       5.732 -23.283 -24.013  1.00 47.53           O  
ATOM   2599  N   THR A 324       8.476 -21.571 -23.792  1.00 45.60           N  
ATOM   2600  CA  THR A 324       9.851 -21.806 -24.218  1.00 47.74           C  
ATOM   2601  C   THR A 324      10.817 -20.689 -23.797  1.00 46.17           C  
ATOM   2602  O   THR A 324      11.978 -20.682 -24.213  1.00 47.10           O  
ATOM   2603  CB  THR A 324       9.915 -21.994 -25.745  1.00 48.25           C  
ATOM   2604  OG1 THR A 324       9.513 -20.772 -26.385  1.00 52.71           O  
ATOM   2605  CG2 THR A 324       8.950 -23.098 -26.177  1.00 51.97           C  
ATOM   2606  N   MET A 325      10.351 -19.755 -22.973  1.00 43.64           N  
ATOM   2607  CA  MET A 325      11.171 -18.590 -22.630  1.00 43.15           C  
ATOM   2608  C   MET A 325      12.280 -18.935 -21.634  1.00 43.22           C  
ATOM   2609  O   MET A 325      12.008 -19.575 -20.610  1.00 41.81           O  
ATOM   2610  CB  MET A 325      10.299 -17.497 -22.003  1.00 44.34           C  
ATOM   2611  CG  MET A 325      11.072 -16.199 -21.723  1.00 42.58           C  
ATOM   2612  SD  MET A 325      11.534 -15.343 -23.276  1.00 45.45           S  
ATOM   2613  CE  MET A 325       9.905 -15.083 -23.978  1.00 42.41           C  
ATOM   2614  N   LYS A 326      13.500 -18.475 -21.894  1.00 40.43           N  
ATOM   2615  CA  LYS A 326      14.601 -18.705 -20.962  1.00 40.70           C  
ATOM   2616  C   LYS A 326      14.458 -17.698 -19.832  1.00 37.95           C  
ATOM   2617  O   LYS A 326      14.414 -16.499 -20.077  1.00 36.67           O  
ATOM   2618  CB  LYS A 326      15.955 -18.573 -21.659  1.00 42.32           C  
ATOM   2619  CG  LYS A 326      17.180 -18.378 -20.769  1.00 48.57           C  
ATOM   2620  CD  LYS A 326      17.366 -19.484 -19.740  1.00 59.52           C  
ATOM   2621  CE  LYS A 326      18.139 -20.670 -20.290  1.00 66.04           C  
ATOM   2622  NZ  LYS A 326      18.404 -21.657 -19.195  1.00 67.74           N  
ATOM   2623  N   ILE A 327      14.371 -18.177 -18.602  1.00 37.56           N  
ATOM   2624  CA  ILE A 327      14.120 -17.268 -17.474  1.00 37.92           C  
ATOM   2625  C   ILE A 327      15.317 -17.374 -16.540  1.00 39.41           C  
ATOM   2626  O   ILE A 327      15.639 -18.489 -16.112  1.00 40.15           O  
ATOM   2627  CB  ILE A 327      12.805 -17.630 -16.767  1.00 36.56           C  
ATOM   2628  CG1 ILE A 327      11.636 -17.324 -17.733  1.00 40.42           C  
ATOM   2629  CG2 ILE A 327      12.629 -16.855 -15.440  1.00 36.88           C  
ATOM   2630  CD1 ILE A 327      10.532 -18.272 -17.587  1.00 48.55           C  
ATOM   2631  N   LYS A 328      15.918 -16.242 -16.164  1.00 36.92           N  
ATOM   2632  CA  LYS A 328      17.043 -16.304 -15.214  1.00 38.33           C  
ATOM   2633  C   LYS A 328      16.934 -15.209 -14.169  1.00 38.04           C  
ATOM   2634  O   LYS A 328      16.729 -14.057 -14.507  1.00 37.25           O  
ATOM   2635  CB  LYS A 328      18.386 -16.222 -15.949  1.00 38.38           C  
ATOM   2636  CG  LYS A 328      19.644 -16.206 -15.068  1.00 41.70           C  
ATOM   2637  CD  LYS A 328      20.910 -16.213 -15.964  1.00 43.57           C  
ATOM   2638  CE  LYS A 328      22.208 -16.112 -15.159  1.00 47.52           C  
ATOM   2639  NZ  LYS A 328      23.337 -15.965 -16.118  1.00 50.37           N  
ATOM   2640  N   ILE A 329      17.094 -15.579 -12.902  1.00 36.58           N  
ATOM   2641  CA  ILE A 329      17.013 -14.591 -11.815  1.00 39.30           C  
ATOM   2642  C   ILE A 329      18.435 -14.467 -11.306  1.00 39.79           C  
ATOM   2643  O   ILE A 329      19.097 -15.492 -11.066  1.00 41.41           O  
ATOM   2644  CB  ILE A 329      16.145 -15.105 -10.654  1.00 39.69           C  
ATOM   2645  CG1 ILE A 329      14.787 -15.625 -11.168  1.00 40.79           C  
ATOM   2646  CG2 ILE A 329      16.101 -14.048  -9.504  1.00 38.98           C  
ATOM   2647  CD1 ILE A 329      13.883 -14.649 -11.908  1.00 37.55           C  
ATOM   2648  N   ILE A 330      18.911 -13.237 -11.163  1.00 36.77           N  
ATOM   2649  CA  ILE A 330      20.285 -12.994 -10.737  1.00 38.13           C  
ATOM   2650  C   ILE A 330      20.236 -12.339  -9.355  1.00 39.69           C  
ATOM   2651  O   ILE A 330      19.641 -11.280  -9.180  1.00 39.49           O  
ATOM   2652  CB  ILE A 330      21.066 -12.117 -11.728  1.00 37.82           C  
ATOM   2653  CG1 ILE A 330      21.186 -12.819 -13.095  1.00 40.84           C  
ATOM   2654  CG2 ILE A 330      22.480 -11.838 -11.209  1.00 39.02           C  
ATOM   2655  CD1 ILE A 330      20.283 -12.256 -14.109  1.00 41.99           C  
ATOM   2656  N   ALA A 331      20.737 -13.017  -8.334  1.00 37.91           N  
ATOM   2657  CA  ALA A 331      20.584 -12.466  -6.994  1.00 39.30           C  
ATOM   2658  C   ALA A 331      21.961 -12.441  -6.340  1.00 42.07           C  
ATOM   2659  O   ALA A 331      22.371 -13.418  -5.711  1.00 42.59           O  
ATOM   2660  CB  ALA A 331      19.553 -13.261  -6.186  1.00 39.49           C  
ATOM   2661  N   PRO A 332      22.702 -11.335  -6.534  1.00 43.65           N  
ATOM   2662  CA  PRO A 332      24.091 -11.227  -6.033  1.00 44.46           C  
ATOM   2663  C   PRO A 332      24.218 -11.361  -4.513  1.00 44.94           C  
ATOM   2664  O   PRO A 332      23.330 -10.933  -3.779  1.00 41.00           O  
ATOM   2665  CB  PRO A 332      24.523  -9.839  -6.504  1.00 44.48           C  
ATOM   2666  CG  PRO A 332      23.625  -9.542  -7.708  1.00 49.02           C  
ATOM   2667  CD  PRO A 332      22.294 -10.140  -7.290  1.00 41.45           C  
ATOM   2668  N   PRO A 333      25.307 -11.967  -4.034  1.00 46.29           N  
ATOM   2669  CA  PRO A 333      25.377 -12.153  -2.569  1.00 47.08           C  
ATOM   2670  C   PRO A 333      25.417 -10.786  -1.859  1.00 45.12           C  
ATOM   2671  O   PRO A 333      24.941 -10.649  -0.747  1.00 45.64           O  
ATOM   2672  CB  PRO A 333      26.699 -12.911  -2.345  1.00 48.53           C  
ATOM   2673  CG  PRO A 333      27.265 -13.214  -3.705  1.00 49.63           C  
ATOM   2674  CD  PRO A 333      26.482 -12.476  -4.759  1.00 47.17           C  
ATOM   2675  N   GLU A 334      25.943  -9.767  -2.516  1.00 46.52           N  
ATOM   2676  CA  GLU A 334      26.055  -8.465  -1.854  1.00 48.93           C  
ATOM   2677  C   GLU A 334      24.882  -7.542  -2.186  1.00 48.22           C  
ATOM   2678  O   GLU A 334      24.983  -6.325  -2.033  1.00 47.15           O  
ATOM   2679  CB  GLU A 334      27.374  -7.797  -2.232  1.00 52.65           C  
ATOM   2680  CG  GLU A 334      28.263  -8.684  -3.109  1.00 60.01           C  
ATOM   2681  CD  GLU A 334      27.764  -8.749  -4.558  1.00 69.35           C  
ATOM   2682  OE1 GLU A 334      27.436  -7.685  -5.146  1.00 76.37           O  
ATOM   2683  OE2 GLU A 334      27.710  -9.868  -5.116  1.00 69.51           O  
ATOM   2684  N   ARG A 335      23.758  -8.129  -2.600  1.00 44.41           N  
ATOM   2685  CA  ARG A 335      22.664  -7.326  -3.165  1.00 42.32           C  
ATOM   2686  C   ARG A 335      21.954  -6.387  -2.199  1.00 42.98           C  
ATOM   2687  O   ARG A 335      21.269  -5.481  -2.646  1.00 40.91           O  
ATOM   2688  CB  ARG A 335      21.647  -8.230  -3.872  1.00 40.80           C  
ATOM   2689  CG  ARG A 335      20.863  -9.150  -2.958  1.00 40.91           C  
ATOM   2690  CD  ARG A 335      20.080 -10.162  -3.833  1.00 43.21           C  
ATOM   2691  NE  ARG A 335      19.324 -11.153  -3.059  1.00 39.56           N  
ATOM   2692  CZ  ARG A 335      19.822 -12.282  -2.547  1.00 42.81           C  
ATOM   2693  NH1 ARG A 335      21.092 -12.617  -2.695  1.00 43.59           N  
ATOM   2694  NH2 ARG A 335      19.025 -13.116  -1.886  1.00 40.20           N  
ATOM   2695  N   LYS A 336      22.145  -6.545  -0.890  1.00 43.61           N  
ATOM   2696  CA  LYS A 336      21.636  -5.515   0.026  1.00 44.17           C  
ATOM   2697  C   LYS A 336      22.307  -4.163  -0.180  1.00 43.13           C  
ATOM   2698  O   LYS A 336      21.753  -3.122   0.191  1.00 42.95           O  
ATOM   2699  CB  LYS A 336      21.729  -5.931   1.501  1.00 46.22           C  
ATOM   2700  CG  LYS A 336      23.123  -6.080   2.007  1.00 50.08           C  
ATOM   2701  CD  LYS A 336      23.126  -6.886   3.322  1.00 60.11           C  
ATOM   2702  CE  LYS A 336      22.315  -6.200   4.411  1.00 59.56           C  
ATOM   2703  NZ  LYS A 336      21.768  -7.154   5.422  1.00 66.33           N  
ATOM   2704  N   TYR A 337      23.504  -4.182  -0.753  1.00 40.76           N  
ATOM   2705  CA  TYR A 337      24.219  -2.955  -1.054  1.00 38.80           C  
ATOM   2706  C   TYR A 337      24.482  -2.718  -2.540  1.00 38.31           C  
ATOM   2707  O   TYR A 337      25.355  -1.937  -2.879  1.00 37.03           O  
ATOM   2708  CB  TYR A 337      25.570  -2.929  -0.332  1.00 40.65           C  
ATOM   2709  CG  TYR A 337      25.444  -3.061   1.165  1.00 40.55           C  
ATOM   2710  CD1 TYR A 337      24.500  -2.332   1.875  1.00 43.98           C  
ATOM   2711  CD2 TYR A 337      26.292  -3.909   1.878  1.00 46.02           C  
ATOM   2712  CE1 TYR A 337      24.393  -2.452   3.271  1.00 45.05           C  
ATOM   2713  CE2 TYR A 337      26.193  -4.024   3.261  1.00 49.37           C  
ATOM   2714  CZ  TYR A 337      25.236  -3.304   3.948  1.00 48.44           C  
ATOM   2715  OH  TYR A 337      25.144  -3.444   5.329  1.00 48.25           O  
ATOM   2716  N   SER A 338      23.790  -3.406  -3.436  1.00 39.06           N  
ATOM   2717  CA  SER A 338      24.216  -3.343  -4.828  1.00 42.13           C  
ATOM   2718  C   SER A 338      23.966  -1.973  -5.490  1.00 39.37           C  
ATOM   2719  O   SER A 338      24.719  -1.554  -6.356  1.00 38.81           O  
ATOM   2720  CB  SER A 338      23.604  -4.503  -5.613  1.00 41.98           C  
ATOM   2721  OG  SER A 338      22.246  -4.218  -5.777  1.00 49.29           O  
ATOM   2722  N   VAL A 339      22.951  -1.244  -5.046  1.00 40.84           N  
ATOM   2723  CA  VAL A 339      22.824   0.150  -5.505  1.00 40.13           C  
ATOM   2724  C   VAL A 339      24.092   0.923  -5.178  1.00 42.98           C  
ATOM   2725  O   VAL A 339      24.677   1.573  -6.045  1.00 40.60           O  
ATOM   2726  CB  VAL A 339      21.618   0.880  -4.879  1.00 43.56           C  
ATOM   2727  CG1 VAL A 339      21.644   2.386  -5.303  1.00 41.03           C  
ATOM   2728  CG2 VAL A 339      20.281   0.212  -5.324  1.00 42.30           C  
ATOM   2729  N   TRP A 340      24.535   0.852  -3.917  1.00 41.61           N  
ATOM   2730  CA  TRP A 340      25.708   1.603  -3.476  1.00 41.00           C  
ATOM   2731  C   TRP A 340      26.947   1.115  -4.228  1.00 39.98           C  
ATOM   2732  O   TRP A 340      27.749   1.912  -4.695  1.00 40.13           O  
ATOM   2733  CB  TRP A 340      25.916   1.449  -1.942  1.00 40.55           C  
ATOM   2734  CG  TRP A 340      27.055   2.322  -1.474  1.00 40.28           C  
ATOM   2735  CD1 TRP A 340      26.975   3.612  -0.973  1.00 40.17           C  
ATOM   2736  CD2 TRP A 340      28.449   2.023  -1.587  1.00 44.35           C  
ATOM   2737  NE1 TRP A 340      28.254   4.091  -0.715  1.00 41.46           N  
ATOM   2738  CE2 TRP A 340      29.165   3.139  -1.099  1.00 42.25           C  
ATOM   2739  CE3 TRP A 340      29.168   0.891  -2.017  1.00 41.93           C  
ATOM   2740  CZ2 TRP A 340      30.548   3.171  -1.071  1.00 41.41           C  
ATOM   2741  CZ3 TRP A 340      30.550   0.932  -1.981  1.00 41.50           C  
ATOM   2742  CH2 TRP A 340      31.217   2.067  -1.521  1.00 41.55           C  
ATOM   2743  N   ILE A 341      27.078  -0.194  -4.400  1.00 39.51           N  
ATOM   2744  CA  ILE A 341      28.236  -0.734  -5.132  1.00 41.56           C  
ATOM   2745  C   ILE A 341      28.261  -0.261  -6.586  1.00 39.63           C  
ATOM   2746  O   ILE A 341      29.324   0.091  -7.130  1.00 39.65           O  
ATOM   2747  CB  ILE A 341      28.260  -2.289  -5.056  1.00 40.91           C  
ATOM   2748  CG1 ILE A 341      28.573  -2.745  -3.617  1.00 41.84           C  
ATOM   2749  CG2 ILE A 341      29.273  -2.888  -6.048  1.00 42.26           C  
ATOM   2750  CD1 ILE A 341      28.064  -4.148  -3.344  1.00 41.52           C  
ATOM   2751  N   GLY A 342      27.097  -0.211  -7.223  1.00 39.41           N  
ATOM   2752  CA  GLY A 342      27.053   0.247  -8.613  1.00 40.28           C  
ATOM   2753  C   GLY A 342      27.510   1.685  -8.675  1.00 41.08           C  
ATOM   2754  O   GLY A 342      28.237   2.091  -9.576  1.00 41.38           O  
ATOM   2755  N   GLY A 343      27.098   2.461  -7.687  1.00 40.33           N  
ATOM   2756  CA  GLY A 343      27.527   3.854  -7.584  1.00 40.70           C  
ATOM   2757  C   GLY A 343      29.015   3.994  -7.364  1.00 41.16           C  
ATOM   2758  O   GLY A 343      29.663   4.853  -7.958  1.00 41.24           O  
ATOM   2759  N   SER A 344      29.572   3.119  -6.536  1.00 40.81           N  
ATOM   2760  CA  SER A 344      31.004   3.118  -6.221  1.00 42.34           C  
ATOM   2761  C   SER A 344      31.846   2.779  -7.443  1.00 41.29           C  
ATOM   2762  O   SER A 344      32.877   3.411  -7.709  1.00 40.76           O  
ATOM   2763  CB  SER A 344      31.271   2.093  -5.116  1.00 39.61           C  
ATOM   2764  OG  SER A 344      32.658   2.010  -4.860  1.00 47.28           O  
ATOM   2765  N   ILE A 345      31.391   1.793  -8.206  1.00 42.59           N  
ATOM   2766  CA  ILE A 345      32.040   1.474  -9.479  1.00 45.09           C  
ATOM   2767  C   ILE A 345      31.987   2.633 -10.473  1.00 45.25           C  
ATOM   2768  O   ILE A 345      33.007   2.986 -11.081  1.00 44.97           O  
ATOM   2769  CB  ILE A 345      31.437   0.219 -10.144  1.00 44.38           C  
ATOM   2770  CG1 ILE A 345      31.559  -0.982  -9.207  1.00 45.51           C  
ATOM   2771  CG2 ILE A 345      32.151  -0.067 -11.480  1.00 45.03           C  
ATOM   2772  CD1 ILE A 345      30.666  -2.172  -9.608  1.00 46.27           C  
ATOM   2773  N   LEU A 346      30.805   3.219 -10.632  1.00 45.49           N  
ATOM   2774  CA  LEU A 346      30.594   4.276 -11.608  1.00 45.93           C  
ATOM   2775  C   LEU A 346      31.409   5.524 -11.269  1.00 46.15           C  
ATOM   2776  O   LEU A 346      32.079   6.080 -12.144  1.00 45.02           O  
ATOM   2777  CB  LEU A 346      29.110   4.633 -11.698  1.00 46.09           C  
ATOM   2778  CG  LEU A 346      28.652   5.609 -12.787  1.00 48.91           C  
ATOM   2779  CD1 LEU A 346      28.801   5.005 -14.178  1.00 47.89           C  
ATOM   2780  CD2 LEU A 346      27.210   6.035 -12.530  1.00 48.17           C  
ATOM   2781  N   ALA A 347      31.345   5.952 -10.005  1.00 45.73           N  
ATOM   2782  CA  ALA A 347      32.021   7.173  -9.560  1.00 47.09           C  
ATOM   2783  C   ALA A 347      33.537   7.037  -9.578  1.00 48.50           C  
ATOM   2784  O   ALA A 347      34.239   8.047  -9.574  1.00 49.60           O  
ATOM   2785  CB  ALA A 347      31.550   7.590  -8.163  1.00 46.06           C  
ATOM   2786  N   SER A 348      34.038   5.809  -9.615  1.00 48.87           N  
ATOM   2787  CA  SER A 348      35.477   5.579  -9.594  1.00 52.16           C  
ATOM   2788  C   SER A 348      36.057   5.309 -10.988  1.00 54.26           C  
ATOM   2789  O   SER A 348      37.236   4.970 -11.129  1.00 55.88           O  
ATOM   2790  CB  SER A 348      35.810   4.432  -8.645  1.00 50.52           C  
ATOM   2791  OG  SER A 348      35.710   3.209  -9.343  1.00 53.52           O  
ATOM   2792  N   LEU A 349      35.237   5.461 -12.021  1.00 57.12           N  
ATOM   2793  CA  LEU A 349      35.701   5.272 -13.392  1.00 59.45           C  
ATOM   2794  C   LEU A 349      36.323   6.556 -13.914  1.00 60.81           C  
ATOM   2795  O   LEU A 349      35.719   7.621 -13.810  1.00 61.22           O  
ATOM   2796  CB  LEU A 349      34.537   4.909 -14.310  1.00 59.71           C  
ATOM   2797  CG  LEU A 349      34.012   3.478 -14.369  1.00 61.99           C  
ATOM   2798  CD1 LEU A 349      32.888   3.410 -15.391  1.00 62.03           C  
ATOM   2799  CD2 LEU A 349      35.140   2.525 -14.737  1.00 64.54           C  
ATOM   2800  N   SER A 350      37.517   6.462 -14.494  1.00 62.86           N  
ATOM   2801  CA  SER A 350      38.087   7.606 -15.201  1.00 63.60           C  
ATOM   2802  C   SER A 350      37.140   8.020 -16.337  1.00 64.66           C  
ATOM   2803  O   SER A 350      36.934   9.208 -16.584  1.00 65.00           O  
ATOM   2804  CB  SER A 350      39.472   7.263 -15.745  1.00 63.97           C  
ATOM   2805  OG  SER A 350      39.377   6.255 -16.737  1.00 63.91           O  
ATOM   2806  N   THR A 351      36.559   7.028 -17.008  1.00 65.86           N  
ATOM   2807  CA  THR A 351      35.554   7.221 -18.058  1.00 66.88           C  
ATOM   2808  C   THR A 351      34.406   8.151 -17.650  1.00 67.23           C  
ATOM   2809  O   THR A 351      33.901   8.924 -18.463  1.00 67.77           O  
ATOM   2810  CB  THR A 351      34.933   5.862 -18.460  1.00 67.10           C  
ATOM   2811  OG1 THR A 351      35.965   4.974 -18.898  1.00 68.43           O  
ATOM   2812  CG2 THR A 351      33.896   6.027 -19.573  1.00 68.24           C  
ATOM   2813  N   PHE A 352      34.000   8.063 -16.388  1.00 66.66           N  
ATOM   2814  CA  PHE A 352      32.832   8.783 -15.874  1.00 66.29           C  
ATOM   2815  C   PHE A 352      33.071  10.270 -15.589  1.00 66.78           C  
ATOM   2816  O   PHE A 352      32.131  11.068 -15.584  1.00 66.51           O  
ATOM   2817  CB  PHE A 352      32.357   8.082 -14.596  1.00 64.73           C  
ATOM   2818  CG  PHE A 352      31.198   8.748 -13.918  1.00 62.31           C  
ATOM   2819  CD1 PHE A 352      29.936   8.729 -14.491  1.00 59.04           C  
ATOM   2820  CD2 PHE A 352      31.361   9.361 -12.683  1.00 61.41           C  
ATOM   2821  CE1 PHE A 352      28.853   9.318 -13.853  1.00 58.08           C  
ATOM   2822  CE2 PHE A 352      30.283   9.954 -12.035  1.00 58.33           C  
ATOM   2823  CZ  PHE A 352      29.030   9.932 -12.627  1.00 59.24           C  
ATOM   2824  N   GLN A 353      34.328  10.639 -15.366  1.00 66.97           N  
ATOM   2825  CA  GLN A 353      34.666  11.951 -14.813  1.00 67.72           C  
ATOM   2826  C   GLN A 353      34.128  13.175 -15.570  1.00 67.75           C  
ATOM   2827  O   GLN A 353      34.190  14.294 -15.058  1.00 68.24           O  
ATOM   2828  CB  GLN A 353      36.182  12.055 -14.604  1.00 68.53           C  
ATOM   2829  CG  GLN A 353      36.759  10.881 -13.812  1.00 70.37           C  
ATOM   2830  CD  GLN A 353      35.994  10.595 -12.523  1.00 72.78           C  
ATOM   2831  OE1 GLN A 353      35.894  11.447 -11.640  1.00 73.54           O  
ATOM   2832  NE2 GLN A 353      35.461   9.386 -12.407  1.00 71.53           N  
ATOM   2833  N   GLN A 354      33.593  12.982 -16.773  1.00 67.50           N  
ATOM   2834  CA  GLN A 354      33.030  14.114 -17.512  1.00 67.38           C  
ATOM   2835  C   GLN A 354      31.501  14.132 -17.427  1.00 66.06           C  
ATOM   2836  O   GLN A 354      30.837  14.939 -18.078  1.00 64.57           O  
ATOM   2837  CB  GLN A 354      33.563  14.184 -18.959  1.00 68.22           C  
ATOM   2838  CG  GLN A 354      32.611  13.750 -20.078  1.00 71.95           C  
ATOM   2839  CD  GLN A 354      32.320  12.259 -20.074  1.00 75.70           C  
ATOM   2840  OE1 GLN A 354      33.147  11.457 -19.634  1.00 77.13           O  
ATOM   2841  NE2 GLN A 354      31.142  11.879 -20.568  1.00 75.80           N  
ATOM   2842  N   MET A 355      30.948  13.258 -16.589  1.00 65.27           N  
ATOM   2843  CA  MET A 355      29.497  13.213 -16.390  1.00 65.10           C  
ATOM   2844  C   MET A 355      29.045  13.969 -15.131  1.00 61.43           C  
ATOM   2845  O   MET A 355      27.865  14.313 -15.005  1.00 60.05           O  
ATOM   2846  CB  MET A 355      28.978  11.770 -16.406  1.00 65.05           C  
ATOM   2847  CG  MET A 355      28.799  11.173 -17.813  1.00 66.97           C  
ATOM   2848  SD  MET A 355      27.528   9.883 -17.815  1.00 73.21           S  
ATOM   2849  CE  MET A 355      28.393   8.493 -17.070  1.00 75.19           C  
ATOM   2850  N   TRP A 356      29.994  14.240 -14.231  1.00 58.29           N  
ATOM   2851  CA  TRP A 356      29.805  15.130 -13.081  1.00 55.73           C  
ATOM   2852  C   TRP A 356      29.251  16.490 -13.488  1.00 53.84           C  
ATOM   2853  O   TRP A 356      29.763  17.123 -14.416  1.00 53.09           O  
ATOM   2854  CB  TRP A 356      31.149  15.400 -12.380  1.00 56.54           C  
ATOM   2855  CG  TRP A 356      31.775  14.206 -11.712  1.00 56.99           C  
ATOM   2856  CD1 TRP A 356      32.943  13.583 -12.067  1.00 56.83           C  
ATOM   2857  CD2 TRP A 356      31.272  13.499 -10.572  1.00 56.17           C  
ATOM   2858  NE1 TRP A 356      33.192  12.531 -11.217  1.00 57.35           N  
ATOM   2859  CE2 TRP A 356      32.183  12.460 -10.289  1.00 57.47           C  
ATOM   2860  CE3 TRP A 356      30.143  13.646  -9.759  1.00 54.51           C  
ATOM   2861  CZ2 TRP A 356      31.995  11.569  -9.229  1.00 57.23           C  
ATOM   2862  CZ3 TRP A 356      29.961  12.756  -8.697  1.00 56.64           C  
ATOM   2863  CH2 TRP A 356      30.873  11.728  -8.454  1.00 55.27           C  
ATOM   2864  N   ILE A 357      28.222  16.957 -12.791  1.00 50.87           N  
ATOM   2865  CA  ILE A 357      27.793  18.340 -12.958  1.00 49.73           C  
ATOM   2866  C   ILE A 357      28.693  19.162 -12.038  1.00 49.27           C  
ATOM   2867  O   ILE A 357      28.759  18.874 -10.847  1.00 45.58           O  
ATOM   2868  CB  ILE A 357      26.321  18.513 -12.552  1.00 50.03           C  
ATOM   2869  CG1 ILE A 357      25.457  17.513 -13.323  1.00 52.59           C  
ATOM   2870  CG2 ILE A 357      25.840  19.939 -12.807  1.00 48.26           C  
ATOM   2871  CD1 ILE A 357      24.155  17.207 -12.641  1.00 54.72           C  
ATOM   2872  N   THR A 358      29.409  20.145 -12.576  1.00 47.92           N  
ATOM   2873  CA  THR A 358      30.307  20.930 -11.738  1.00 47.89           C  
ATOM   2874  C   THR A 358      29.574  22.148 -11.178  1.00 48.32           C  
ATOM   2875  O   THR A 358      28.534  22.547 -11.696  1.00 48.86           O  
ATOM   2876  CB  THR A 358      31.585  21.347 -12.494  1.00 48.99           C  
ATOM   2877  OG1 THR A 358      31.248  22.281 -13.526  1.00 47.08           O  
ATOM   2878  CG2 THR A 358      32.280  20.132 -13.106  1.00 47.32           C  
ATOM   2879  N   LYS A 359      30.092  22.731 -10.105  1.00 48.80           N  
ATOM   2880  CA  LYS A 359      29.455  23.914  -9.544  1.00 51.20           C  
ATOM   2881  C   LYS A 359      29.427  25.059 -10.564  1.00 51.81           C  
ATOM   2882  O   LYS A 359      28.472  25.839 -10.614  1.00 50.11           O  
ATOM   2883  CB  LYS A 359      30.161  24.337  -8.254  1.00 51.56           C  
ATOM   2884  CG  LYS A 359      29.855  25.764  -7.821  1.00 57.24           C  
ATOM   2885  CD  LYS A 359      28.605  25.840  -6.945  1.00 62.43           C  
ATOM   2886  CE  LYS A 359      28.432  27.260  -6.405  1.00 64.22           C  
ATOM   2887  NZ  LYS A 359      27.295  27.333  -5.447  1.00 66.17           N  
ATOM   2888  N   GLN A 360      30.468  25.139 -11.389  1.00 52.28           N  
ATOM   2889  CA  GLN A 360      30.514  26.134 -12.458  1.00 54.73           C  
ATOM   2890  C   GLN A 360      29.339  26.005 -13.432  1.00 55.72           C  
ATOM   2891  O   GLN A 360      28.695  27.005 -13.754  1.00 55.51           O  
ATOM   2892  CB  GLN A 360      31.835  26.041 -13.210  1.00 54.51           C  
ATOM   2893  CG  GLN A 360      31.916  26.994 -14.389  1.00 57.33           C  
ATOM   2894  CD  GLN A 360      33.225  27.732 -14.417  1.00 60.38           C  
ATOM   2895  OE1 GLN A 360      34.055  27.568 -13.520  1.00 63.08           O  
ATOM   2896  NE2 GLN A 360      33.420  28.567 -15.434  1.00 61.26           N  
ATOM   2897  N   GLU A 361      29.071  24.782 -13.892  1.00 56.58           N  
ATOM   2898  CA  GLU A 361      27.876  24.474 -14.685  1.00 59.41           C  
ATOM   2899  C   GLU A 361      26.588  24.859 -13.953  1.00 59.20           C  
ATOM   2900  O   GLU A 361      25.694  25.468 -14.542  1.00 59.30           O  
ATOM   2901  CB  GLU A 361      27.796  22.982 -15.020  1.00 58.90           C  
ATOM   2902  CG  GLU A 361      28.888  22.433 -15.926  1.00 62.00           C  
ATOM   2903  CD  GLU A 361      28.973  20.912 -15.841  1.00 63.72           C  
ATOM   2904  OE1 GLU A 361      30.106  20.386 -15.751  1.00 70.57           O  
ATOM   2905  OE2 GLU A 361      27.912  20.242 -15.844  1.00 68.36           O  
ATOM   2906  N   TYR A 362      26.489  24.495 -12.676  1.00 58.23           N  
ATOM   2907  CA  TYR A 362      25.320  24.866 -11.882  1.00 59.39           C  
ATOM   2908  C   TYR A 362      25.157  26.386 -11.765  1.00 60.62           C  
ATOM   2909  O   TYR A 362      24.037  26.901 -11.771  1.00 60.69           O  
ATOM   2910  CB  TYR A 362      25.372  24.227 -10.493  1.00 58.05           C  
ATOM   2911  CG  TYR A 362      24.199  24.592  -9.606  1.00 57.32           C  
ATOM   2912  CD1 TYR A 362      22.966  23.938  -9.710  1.00 54.56           C  
ATOM   2913  CD2 TYR A 362      24.330  25.594  -8.652  1.00 59.59           C  
ATOM   2914  CE1 TYR A 362      21.900  24.281  -8.876  1.00 53.12           C  
ATOM   2915  CE2 TYR A 362      23.279  25.947  -7.835  1.00 59.18           C  
ATOM   2916  CZ  TYR A 362      22.068  25.299  -7.952  1.00 58.15           C  
ATOM   2917  OH  TYR A 362      21.057  25.704  -7.105  1.00 60.47           O  
ATOM   2918  N   ASP A 363      26.277  27.095 -11.656  1.00 62.61           N  
ATOM   2919  CA  ASP A 363      26.278  28.563 -11.658  1.00 64.90           C  
ATOM   2920  C   ASP A 363      25.855  29.164 -13.003  1.00 66.01           C  
ATOM   2921  O   ASP A 363      25.217  30.215 -13.038  1.00 66.20           O  
ATOM   2922  CB  ASP A 363      27.648  29.104 -11.241  1.00 64.79           C  
ATOM   2923  CG  ASP A 363      27.947  28.878  -9.766  1.00 66.11           C  
ATOM   2924  OD1 ASP A 363      27.008  28.555  -9.005  1.00 67.95           O  
ATOM   2925  OD2 ASP A 363      29.122  29.029  -9.363  1.00 66.98           O  
ATOM   2926  N   GLU A 364      26.201  28.500 -14.102  1.00 67.93           N  
ATOM   2927  CA  GLU A 364      25.832  28.965 -15.439  1.00 69.99           C  
ATOM   2928  C   GLU A 364      24.430  28.554 -15.888  1.00 70.71           C  
ATOM   2929  O   GLU A 364      23.892  29.114 -16.846  1.00 71.12           O  
ATOM   2930  CB  GLU A 364      26.847  28.489 -16.485  1.00 70.45           C  
ATOM   2931  CG  GLU A 364      28.063  29.390 -16.631  1.00 73.84           C  
ATOM   2932  CD  GLU A 364      29.247  28.903 -15.822  1.00 77.48           C  
ATOM   2933  OE1 GLU A 364      29.840  27.876 -16.217  1.00 79.81           O  
ATOM   2934  OE2 GLU A 364      29.586  29.540 -14.799  1.00 77.94           O  
ATOM   2935  N   ALA A 365      23.847  27.566 -15.219  1.00 71.71           N  
ATOM   2936  CA  ALA A 365      22.536  27.046 -15.604  1.00 72.45           C  
ATOM   2937  C   ALA A 365      21.427  27.677 -14.768  1.00 72.99           C  
ATOM   2938  O   ALA A 365      20.709  28.561 -15.240  1.00 73.25           O  
ATOM   2939  CB  ALA A 365      22.500  25.524 -15.477  1.00 72.19           C  
TER    2940      ALA A 365                                                      
HETATM 2941  PG  ATP A 376      13.786   1.704   0.268  1.00 35.15           P  
HETATM 2942  O1G ATP A 376      12.465   0.998   0.465  1.00 36.65           O  
HETATM 2943  O2G ATP A 376      14.617   1.115  -0.807  1.00 33.23           O  
HETATM 2944  O3G ATP A 376      13.646   3.195   0.239  1.00 33.08           O  
HETATM 2945  PB  ATP A 376      16.112   1.220   1.973  1.00 34.61           P  
HETATM 2946  O1B ATP A 376      16.978   1.604   0.825  1.00 35.47           O  
HETATM 2947  O2B ATP A 376      16.395   1.866   3.296  1.00 31.89           O  
HETATM 2948  O3B ATP A 376      14.522   1.349   1.682  1.00 35.70           O  
HETATM 2949  PA  ATP A 376      17.472  -1.363   2.052  1.00 35.69           P  
HETATM 2950  O1A ATP A 376      17.629  -1.885   0.662  1.00 38.10           O  
HETATM 2951  O2A ATP A 376      18.650  -0.705   2.683  1.00 33.64           O  
HETATM 2952  O3A ATP A 376      16.209  -0.372   2.187  1.00 37.56           O  
HETATM 2953  O5' ATP A 376      16.981  -2.600   2.962  1.00 36.93           O  
HETATM 2954  C5' ATP A 376      16.569  -2.427   4.329  1.00 37.23           C  
HETATM 2955  C4' ATP A 376      15.491  -3.475   4.643  1.00 34.63           C  
HETATM 2956  O4' ATP A 376      16.084  -4.723   4.295  1.00 38.60           O  
HETATM 2957  C3' ATP A 376      15.126  -3.535   6.124  1.00 38.26           C  
HETATM 2958  O3' ATP A 376      13.714  -3.693   6.234  1.00 37.12           O  
HETATM 2959  C2' ATP A 376      15.825  -4.794   6.600  1.00 36.23           C  
HETATM 2960  O2' ATP A 376      15.204  -5.334   7.784  1.00 36.45           O  
HETATM 2961  C1' ATP A 376      15.785  -5.648   5.338  1.00 37.30           C  
HETATM 2962  N9  ATP A 376      16.843  -6.663   5.366  1.00 36.76           N  
HETATM 2963  C8  ATP A 376      18.170  -6.442   5.487  1.00 39.51           C  
HETATM 2964  N7  ATP A 376      18.841  -7.634   5.522  1.00 39.07           N  
HETATM 2965  C5  ATP A 376      17.925  -8.610   5.367  1.00 39.73           C  
HETATM 2966  C6  ATP A 376      17.953 -10.079   5.351  1.00 40.00           C  
HETATM 2967  N6  ATP A 376      19.145 -10.725   5.431  1.00 37.74           N  
HETATM 2968  N1  ATP A 376      16.784 -10.701   5.180  1.00 38.77           N  
HETATM 2969  C2  ATP A 376      15.589 -10.073   5.092  1.00 37.48           C  
HETATM 2970  N3  ATP A 376      15.478  -8.729   5.128  1.00 35.97           N  
HETATM 2971  C4  ATP A 376      16.594  -7.974   5.285  1.00 37.49           C  
HETATM 2972 CA    CA A 377      16.826   1.781  -1.522  1.00 36.05          CA  
END


A second structure was input as follows:


HEADER    CONTRACTILE PROTEIN                     05-DEC-08   2ZWH              
TITLE     MODEL FOR THE F-ACTIN STRUCTURE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-ACTIN-1                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 OTHER_DETAILS: RABBIT SKELETAL MUSCLE                                
KEYWDS    F-ACTIN, G-ACTIN, CYTOSKELTON, FIBER-DIFFRACTION,                     
KEYWDS   2 CONTRACTILE PROTEIN, ACETYLATION, ATP-BINDING, CYTOPLASM,            
KEYWDS   3 CYTOSKELETON, METHYLATION, MUSCLE PROTEIN, NUCLEOTIDE-               
KEYWDS   4 BINDING, PHOSPHOPROTEIN                                              
EXPDTA    FIBER DIFFRACTION                                                     
AUTHOR    T.ODA,M.IWASA,T.AIHARA,Y.MAEDA,A.NARITA                               
REVDAT   3   05-JAN-10 2ZWH    1       JRNL                                     
REVDAT   2   27-JAN-09 2ZWH    1       JRNL                                     
REVDAT   1   20-JAN-09 2ZWH    0                                                
JRNL        AUTH   T.ODA,M.IWASA,T.AIHARA,Y.MAEDA,A.NARITA                      
JRNL        TITL   THE NATURE OF THE GLOBULAR- TO FIBROUS-ACTIN                 
JRNL        TITL 2 TRANSITION.                                                  
JRNL        REF    NATURE                        V. 457   441 2009              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   19158791                                                     
JRNL        DOI    10.1038/NATURE07685                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : FX-PLOR 3.1                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2933                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE DIFFRACTION DATA WERE EXTRACTED USING THE PROPER HELICAL        
REMARK   3  SYMMETRY SUCH AS A SELECTION RULE L=-153N+331M AND A REPEAT         
REMARK   3  DISTANCE 9135 ANGSTRUM. THE LAYER-LINE DISTRIBUTION BY THE          
REMARK   3  SELECTOIN RULE IS CLOSE TO THAT BY L=-6N+13M IN PRINCILE            
REMARK   3  ONE LAYER-LINE BY L=-6N+13M SEPARATES SEVERAL LAYER-LINES           
REMARK   3  BY L=-153N+331M. BUT THE SEPARATIONS WERE NOT CLEAR AND             
REMARK   3  THE LAYER-LINE INTENSITYIES WERE EXTRACTED AS "GROUPING             
REMARK   3  LAYER-LINE INTENSITIES" FROM EXPERIMANTAL PATTERNS.                 
REMARK   3  THEN THE LAYER-LINE INTENSTITIES WERE HANDLED AS                    
REMARK   3  "GROUPING LAYER-LINE INTENSITIES" RE-INDEXED BY L=-6N+13M.          
REMARK   3  THE INITIAL MODELS OF F-ACTIN WERE MADE FROM THE THREE              
REMARK   3  CRYSTAL STRUCTURE OF 1J6Z, 2BTF AND 1HLU.                           
REMARK   3  FIRST THE RADIUS AND THREE ORIENTAIONS OF THE SUBUNIT IN            
REMARK   3  F-ACTIN WERE DETERMINED BY THE RIGID BODY SEARCH USING THE          
REMARK   3  DIFFRACTION DATA OF 56-7.2 ANGSTROM. NEXT THE SUBUNIT               
REMARK   3  COMFORMATIONS WERE SEARCHED ALONG THE ADDITIONAL 12 LOWEST          
REMARK   3  ELASTIC NORMAL MODES OF ACTIN MONOMER VIBRATIONS BY                 
REMARK   3  COMPARISON BETWEEN THE EXPERIMETAL DIFFRACTION DATA AND THE         
REMARK   3  CALCULATION AT 56-7.2 ANGSTROM. THE DIFFRACTION WAS                 
REMARK   3  CALCULATED USING A REPEAT DISTANCE OF 9135A AND A SELECTION         
REMARK   3  RULE L=-153N+331M. THE CALCULATED LAYER-LINE INTENSTITIES           
REMARK   3  ALSO WERE HANDLED A "GROUPING LAYER-LINE INTENSITIES"               
REMARK   3  RE-INDEXED BY L=- 6N+13M. WE CAN NOT FIND THE GOOD SOLVENT          
REMARK   3  MODEL AROUND F-ACTIN. THEN WE USED TWO KINDS OF ATOMIC              
REMARK   3  SCATTERING FACTORS AT THE HIGH RESOLUTION AND THE LOW               
REMARK   3  RESOLUTION DATA.THE MOLECULAR DYNAMICS REFINEMENT AND               
REMARK   3  ENERGY-MINIMIZATION WERE REPEATED IN TRUN USING THE LOW             
REMARK   3  RESOLUTION DATA (RADIALLY 6.5-56 A FROM ORIGIN) AND                 
REMARK   3  THE HIGH RESOLUTION DATA (RADIALLY 3.3-5.5 A AND LATERALLY          
REMARK   3  FROM THE MERIDIAN TO 5.5 A) BY FX-PLOR. TO JUDGE THE MODELS,        
REMARK   3  TWO KINDS OF R-FACTORS WERE CALUCLATED AGAINT THE DIFFRACTION       
REMARK   3  PATTERN TO AVOID THE DECOMVOLUTION ERROR. R-FACTOR-FIT IS AN        
REMARK   3  R-FACTOR AGAINST FITTING AREA (THE AREA RADIAL 6.5-56 AND           
REMARK   3  3.6-5.5A AND LATERALLY FROM THE MERIDIAN TO 5.8 A).                 
REMARK   3  THE R-FACTOR-NON-FIT IS AN R-FACTOR AGAINST NON-FITTING AREA        
REMARK   3  (THE AREA RADIALLY 5.5 - 6.5 A AND LATERALLY TO 15 A).              
REMARK   3  R-FACTOR-FIT : 0.143 R-FACTOR-NON-FIT : 0.207                       
REMARK   4                                                                      
REMARK   4 2ZWH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028512.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : FIBER DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-98; 17-SEP-01; 28-MAY-      
REMARK 200                                   04; 18-NOV-06                      
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL; NULL; NULL             
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : SPRING-8; SPRING-8; SPRING-8;      
REMARK 200                                   SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU; BL40B2; BL40B2; BL45XU     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M; M                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.0; 1.0; 0.9                 
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL; NULL             
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE;          
REMARK 200                                   IMAGE PLATE; IMAGE PLATE           
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV; RIGAKU RAXIS      
REMARK 200                                   IV; RIGAKU RAXIS IV; RIGAKU        
REMARK 200                                   RAXIS IV                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL; NULL; NULL; NULL                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FIBER-DIFFRACTION            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 205                                                                      
REMARK 205 FIBER DIFFRACTION                                                    
REMARK 205 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM FIBER              
REMARK 205 DIFFRACTION DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE             
REMARK 205 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE                   
REMARK 205 VALUES ON THESE RECORDS ARE MEANINGLESS.                             
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: F-ACTIN IS A HELICAL POLYMER OF ACTIN MOLECULES. THE Z-      
REMARK 300 AXIS OF THE ACTIN COORDINATES SHOWN IN THIS PDB-FILE IS A HELIX      
REMARK 300 AXIS. THE NEXT SUBUNIT IN F-ACTIN IS POSITIONED BY 166.4 DEGREE      
REMARK 300 RIGHT ROTATION ABOUT THE HELIX AXIS AND 27.59 ANGSTROM SHIFT         
REMARK 300 ALONG THE HELIX AXIS.                                                
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 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    HIS A  88   NE2   HIS A  88   CD2    -0.069                       
REMARK 500    HIS A 101   NE2   HIS A 101   CD2    -0.074                       
REMARK 500    HIS A 161   NE2   HIS A 161   CD2    -0.073                       
REMARK 500    HIS A 173   NE2   HIS A 173   CD2    -0.073                       
REMARK 500    HIS A 275   NE2   HIS A 275   CD2    -0.070                       
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    ARG A  28   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    PRO A  70   C   -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    TRP A  79   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TRP A  79   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TRP A  86   CD1 -  CG  -  CD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TRP A  86   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A 147   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    TYR A 169   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR A 240   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    PRO A 264   C   -  N   -  CD  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    TYR A 279   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TRP A 340   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TRP A 340   CB  -  CG  -  CD1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TRP A 340   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    TRP A 340   CG  -  CD2 -  CE3 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP A 356   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP A 356   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 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    GLU A   2     -134.03     41.64                                   
REMARK 500    ASP A   3       -7.88    -59.04                                   
REMARK 500    THR A   6     -165.24     59.86                                   
REMARK 500    ALA A   7     -172.77    173.62                                   
REMARK 500    PHE A  21     -116.00    -92.74                                   
REMARK 500    ARG A  28      -68.78   -130.01                                   
REMARK 500    GLN A  41     -136.81     54.20                                   
REMARK 500    VAL A  45      -64.97   -156.34                                   
REMARK 500    GLN A  49       25.43     43.50                                   
REMARK 500    ASP A  51      -68.14    -90.33                                   
REMARK 500    LYS A  61       42.29   -109.56                                   
REMARK 500    PRO A  70      -73.60   -104.11                                   
REMARK 500    ILE A  71       46.90    -82.57                                   
REMARK 500    HIS A  88      -79.30    -66.15                                   
REMARK 500    THR A  89      -72.68    -15.23                                   
REMARK 500    GLU A 100      -42.16   -175.03                                   
REMARK 500    LEU A 110       43.08     77.64                                   
REMARK 500    MET A 123      -92.55    -75.91                                   
REMARK 500    ASN A 128       74.00    -37.57                                   
REMARK 500    GLN A 137      -93.96      9.95                                   
REMARK 500    ASP A 157      -71.78   -114.21                                   
REMARK 500    GLU A 167       -1.84    -55.23                                   
REMARK 500    HIS A 173      -30.73    166.07                                   
REMARK 500    LEU A 180       28.74   -170.50                                   
REMARK 500    SER A 199       96.77   -169.53                                   
REMARK 500    THR A 202     -168.02   -101.39                                   
REMARK 500    LEU A 216      -34.28   -153.83                                   
REMARK 500    ASP A 222       86.65   -154.04                                   
REMARK 500    SER A 234      -63.90   -167.51                                   
REMARK 500    LEU A 236      -83.90    -66.93                                   
REMARK 500    PRO A 243       72.50    -68.76                                   
REMARK 500    ASP A 244      -64.30   -169.47                                   
REMARK 500    GLN A 246      125.24    174.58                                   
REMARK 500    ILE A 250       92.01    -68.98                                   
REMARK 500    ASP A 286      153.48    -44.84                                   
REMARK 500    ILE A 309      -41.55   -143.19                                   
REMARK 500    LYS A 315      -71.30    -72.07                                   
REMARK 500    THR A 324       -6.28    -41.65                                   
REMARK 500    LYS A 328      113.18   -161.39                                   
REMARK 500    TYR A 337       30.06    -79.13                                   
REMARK 500    ALA A 347       58.62    -91.78                                   
REMARK 500    SER A 348      -32.89   -163.48                                   
REMARK 500    GLN A 354       52.74    -91.39                                   
REMARK 500    MET A 355      -85.73   -154.54                                   
REMARK 500    TRP A 356      166.14    -33.44                                   
REMARK 500    SER A 368       -6.48    -57.66                                   
REMARK 500    LYS A 373      -64.70    -92.69                                   
REMARK 500    CYS A 374     -143.83    -95.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  108     PRO A  109                 -147.36                    
REMARK 500 ALA A  321     PRO A  322                  147.56                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 116         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.