CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***  TRANSFERASE 16-JUL-17 5OHE  ***

elNémo ID: 18122012390829651

Job options:

ID        	=	 18122012390829651
JOBID     	=	 TRANSFERASE 16-JUL-17 5OHE
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             16-JUL-17   5OHE              
TITLE     GLOBIN SENSOR DOMAIN OF AFGCHK (FEIII FORM) IN COMPLEX WITH CYANIDE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLOBIN-COUPLED HISTIDINE KINASE;                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: AFGCHK,HEME-BASED OXYGEN-SENSOR HISTIDINE KINASE;           
COMPND   5 EC: 2.7.13.3;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANAEROMYXOBACTER SP. (STRAIN FW109-5);          
SOURCE   3 ORGANISM_TAXID: 404589;                                              
SOURCE   4 GENE: GCHK, ANAE109_2438;                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21C(+);                            
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21C(+)                                 
KEYWDS    HEME, SENSOR PROTEIN, OXYGEN SENSOR, GLOBIN SENSOR DOMAIN, GLOBIN     
KEYWDS   2 DOMAIN, CYANIDE, TRANSFERASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.SKALOVA,P.KOLENKO,J.DOHNALEK,M.STRANAVA,M.MARTINKOVA                
JRNL        AUTH   M.STRANAVA,M.MARTINKOVA,T.SKALOVA,P.KOLENKO,J.DOHNALEK       
JRNL        TITL   STRUCTURAL BASIS OF THE CATALYTIC REGULATION CAUSED BY THE   
JRNL        TITL 2 HEME REDOX AND LIGAND-BINDING OF HEME-BASED OXYGEN SENSOR    
JRNL        TITL 3 HISTIDINE KINASE, AFGCHK                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 118348                         
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 SELECTION                
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5826                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8197                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 425                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9891                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 361                                     
REMARK   3   SOLVENT ATOMS            : 1117                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.70000                                              
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -1.41000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.143         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.986         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10677 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9757 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14559 ; 1.628 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22270 ; 1.071 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1237 ; 5.097 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   550 ;30.145 ;21.218       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1662 ;15.262 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   140 ;20.350 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1423 ; 0.125 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12127 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2669 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4898 ; 1.687 ; 2.181       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4896 ; 1.684 ; 2.181       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6108 ; 2.557 ; 3.263       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6109 ; 2.557 ; 3.263       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5779 ; 2.113 ; 2.446       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5777 ; 2.112 ; 2.446       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8437 ; 3.328 ; 3.567       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13750 ; 5.324 ;26.829       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13149 ; 5.025 ;25.932       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5OHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003743.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918409                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118539                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.1000                            
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) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.15700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MORDA                                                 
REMARK 200 STARTING MODEL: 2W31                                                 
REMARK 200                                                                      
REMARK 200 REMARK: CRYSTAL SHAPE - RED WEDGE BLOCK 300X80X80 UM                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.7% (W/V) PEG3350, 200 MM MGCL2,       
REMARK 280  0.01 M KCN, 7.5% (V/V) GLYCEROL, 0.1 M MMT BUFFER SYSTEM (DL-       
REMARK 280  MALIC ACID, MES MONOHYDRATE, TRIS, NAOH, HCL), PH 6.7, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      220.90950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.03450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.03450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      110.45475            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.03450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.03450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      331.36425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.03450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.03450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      110.45475            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.03450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.03450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      331.36425            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      220.90950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 6420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 6320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 6540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 6460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     ASP C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     ASP D   160                                                      
REMARK 465     LEU D   161                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     THR E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     PRO E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     GLU E   159                                                      
REMARK 465     ASP E   160                                                      
REMARK 465     LEU E   161                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     VAL F     4                                                      
REMARK 465     PRO F     5                                                      
REMARK 465     LEU F   161                                                      
REMARK 465     GLY G     1                                                      
REMARK 465     THR G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     VAL G     4                                                      
REMARK 465     PRO G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     GLU G   159                                                      
REMARK 465     ASP G   160                                                      
REMARK 465     LEU G   161                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     THR H     2                                                      
REMARK 465     GLY H     3                                                      
REMARK 465     VAL H     4                                                      
REMARK 465     PRO H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     GLU H   159                                                      
REMARK 465     ASP H   160                                                      
REMARK 465     LEU H   161                                                      
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 B  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG C  94   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG D  27   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP E  85   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG E 139   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E 139   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG E 158   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG E 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG F 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG F 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG H  24   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    LEU A  58       75.66   -109.89                                   
REMARK 500    TRP A  84       59.11   -109.69                                   
REMARK 500    TRP B  84       51.87   -117.41                                   
REMARK 500    TRP C  84       51.24   -107.87                                   
REMARK 500    TRP E  84       50.89   -110.41                                   
REMARK 500    TRP F  84       55.89   -107.56                                   
REMARK 500    TRP G  84       54.68   -110.11                                   
REMARK 500    TRP H  84       65.69   -106.35                                   
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 D 448        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH F 461        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH G 400        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH H 445        DISTANCE =  5.83 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                             HEM A 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  99   NE2                                                    
REMARK 620 2 HEM A 200   NA   88.4                                              
REMARK 620 3 HEM A 200   NB   87.8  87.2                                        
REMARK 620 4 HEM A 200   NC   93.3 177.2  90.7                                  
REMARK 620 5 HEM A 200   ND   92.3  92.4 179.6  89.7                            
REMARK 620 6 CYN A 201   C   175.3  88.3  95.4  90.1  84.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  99   NE2                                                    
REMARK 620 2 HEM B 200   NA   88.0                                              
REMARK 620 3 HEM B 200   NB   86.1  88.2                                        
REMARK 620 4 HEM B 200   NC   92.6 176.6  88.5                                  
REMARK 620 5 HEM B 200   ND   93.9  92.3 179.5  91.0                            
REMARK 620 6 CYN B 201   C   171.1  92.0  84.9  86.8  95.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  99   NE2                                                    
REMARK 620 2 HEM C 200   NA   86.5                                              
REMARK 620 3 HEM C 200   NB   90.0  89.5                                        
REMARK 620 4 HEM C 200   NC   91.4 177.9  90.1                                  
REMARK 620 5 HEM C 200   ND   88.0  91.3 177.8  89.1                            
REMARK 620 6 CYN C 201   C   171.6  85.1  89.6  97.0  92.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  99   NE2                                                    
REMARK 620 2 HEM D 200   NA   90.9                                              
REMARK 620 3 HEM D 200   NB   87.6  87.6                                        
REMARK 620 4 HEM D 200   NC   91.7 177.1  91.4                                  
REMARK 620 5 HEM D 200   ND   94.1  92.1 178.3  88.8                            
REMARK 620 6 HOH D 391   O   174.7  87.4  87.4  89.9  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E 203  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG E  55   O                                                      
REMARK 620 2 LEU E  58   O    78.3                                              
REMARK 620 3 HOH E 412   O    84.4  87.5                                        
REMARK 620 4 HOH E 429   O   109.8 164.3 106.4                                  
REMARK 620 5 HOH H 381   O   148.4  75.6 111.6  92.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  99   NE2                                                    
REMARK 620 2 HEM E 200   NA   90.1                                              
REMARK 620 3 HEM E 200   NB   87.6  89.0                                        
REMARK 620 4 HEM E 200   NC   89.9 179.7  90.7                                  
REMARK 620 5 HEM E 200   ND   92.8  90.9 179.5  89.4                            
REMARK 620 6 CYN E 201   C   178.8  88.8  92.3  91.2  87.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  99   NE2                                                    
REMARK 620 2 HEM F 200   NA   89.1                                              
REMARK 620 3 HEM F 200   NB   87.3  89.8                                        
REMARK 620 4 HEM F 200   NC   90.8 179.8  90.0                                  
REMARK 620 5 HEM F 200   ND   92.8  90.2 179.9  90.0                            
REMARK 620 6 HOH F 382   O   173.5  84.4  92.4  95.7  87.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  99   NE2                                                    
REMARK 620 2 HEM G 200   NA   92.0                                              
REMARK 620 3 HEM G 200   NB   85.7  90.1                                        
REMARK 620 4 HEM G 200   NC   91.6 176.1  88.7                                  
REMARK 620 5 HEM G 200   ND   97.5  90.5 176.7  90.5                            
REMARK 620 6 CYN G 201   C   157.7 104.3  79.3  71.8  97.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM H 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  99   NE2                                                    
REMARK 620 2 HEM H 200   NA   85.4                                              
REMARK 620 3 HEM H 200   NB   86.8  87.9                                        
REMARK 620 4 HEM H 200   NC   95.5 178.3  90.7                                  
REMARK 620 5 HEM H 200   ND   93.1  91.9 179.8  89.5                            
REMARK 620 6 CYN H 201   C   168.0  82.6  92.6  96.5  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA E 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM G 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM H 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYN H 201                 
DBREF  5OHE A    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE B    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE C    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE D    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE E    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE F    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE G    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
DBREF  5OHE H    2   161  UNP    A7HD43   GCHK_ANADF       2    161             
SEQADV 5OHE GLY A    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY B    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY C    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY D    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY E    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY F    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY G    1  UNP  A7HD43              EXPRESSION TAG                 
SEQADV 5OHE GLY H    1  UNP  A7HD43              EXPRESSION TAG                 
SEQRES   1 A  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 A  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 A  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 A  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 A  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 A  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 A  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 A  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 A  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 A  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 A  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 A  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 A  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 B  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 B  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 B  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 B  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 B  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 B  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 B  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 B  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 B  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 B  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 B  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 B  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 B  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 C  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 C  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 C  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 C  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 C  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 C  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 C  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 C  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 C  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 C  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 C  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 C  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 C  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 D  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 D  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 D  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 D  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 D  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 D  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 D  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 D  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 D  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 D  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 D  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 D  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 D  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 E  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 E  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 E  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 E  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 E  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 E  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 E  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 E  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 E  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 E  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 E  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 E  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 E  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 F  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 F  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 F  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 F  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 F  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 F  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 F  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 F  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 F  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 F  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 F  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 F  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 F  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 G  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 G  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 G  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 G  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 G  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 G  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 G  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 G  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 G  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 G  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 G  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 G  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 G  161  TYR ARG GLU ASP LEU                                          
SEQRES   1 H  161  GLY THR GLY VAL PRO GLU THR VAL PHE GLU GLU LEU LYS          
SEQRES   2 H  161  ARG TYR VAL GLY TRP GLY ASP GLY ASP GLU ARG ALA LEU          
SEQRES   3 H  161  ARG SER LEU HIS GLY ALA ALA ALA PRO HIS PHE PRO ARG          
SEQRES   4 H  161  LEU ALA GLU GLU PHE TYR ASP ARG ILE LEU GLY HIS GLU          
SEQRES   5 H  161  GLY ALA ARG THR ALA LEU VAL GLY GLY GLU SER GLN VAL          
SEQRES   6 H  161  GLY HIS LEU LYS VAL THR MET ILE ALA TRP LEU ASP GLU          
SEQRES   7 H  161  LEU LEU GLY GLY PRO TRP ASP GLU ALA TYR TRP ASP ARG          
SEQRES   8 H  161  ARG TYR ARG ILE GLY ARG VAL HIS VAL ARG ILE GLY LEU          
SEQRES   9 H  161  PRO GLN HIS TYR MET PHE GLY ALA MET ASN VAL HIS ARG          
SEQRES  10 H  161  THR GLY LEU ALA ARG LEU ALA TYR GLU ARG PHE HIS GLY          
SEQRES  11 H  161  ASP PRO PRO GLU LEU GLU ARG VAL ARG ASN ALA LEU GLY          
SEQRES  12 H  161  LYS VAL LEU ASP LEU GLU LEU ALA VAL MET LEU HIS THR          
SEQRES  13 H  161  TYR ARG GLU ASP LEU                                          
HET    HEM  A 200      43                                                       
HET    CYN  A 201       2                                                       
HET     CL  B 202       1                                                       
HET    HEM  B 200      43                                                       
HET    CYN  B 201       2                                                       
HET    HEM  C 200      43                                                       
HET    CYN  C 201       2                                                       
HET     CL  D 201       1                                                       
HET    HEM  D 200      43                                                       
HET    HEM  E 200      43                                                       
HET    CYN  E 201       2                                                       
HET     CL  E 202       1                                                       
HET     NA  E 203       1                                                       
HET    HEM  F 200      43                                                       
HET    HEM  G 200      43                                                       
HET    CYN  G 201       2                                                       
HET     CL  G 202       1                                                       
HET    HEM  H 200      43                                                       
HET    CYN  H 201       2                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CYN CYANIDE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETSYN     HEM HEME                                                             
FORMUL   9  HEM    8(C34 H32 FE N4 O4)                                          
FORMUL  10  CYN    6(C N 1-)                                                    
FORMUL  11   CL    4(CL 1-)                                                     
FORMUL  21   NA    NA 1+                                                        
FORMUL  28  HOH   *1117(H2 O)                                                   
HELIX    1 AA1 THR A    7  GLY A   17  1                                  11    
HELIX    2 AA2 GLY A   19  ALA A   34  1                                  16    
HELIX    3 AA3 HIS A   36  HIS A   51  1                                  16    
HELIX    4 AA4 GLY A   53  LEU A   58  5                                   6    
HELIX    5 AA5 GLY A   60  GLY A   82  1                                  23    
HELIX    6 AA6 ASP A   85  ILE A  102  1                                  18    
HELIX    7 AA7 GLN A  106  HIS A  129  1                                  24    
HELIX    8 AA8 ASP A  131  TYR A  157  1                                  27    
HELIX    9 AA9 VAL B    8  GLY B   17  1                                  10    
HELIX   10 AB1 GLY B   19  ALA B   34  1                                  16    
HELIX   11 AB2 HIS B   36  GLY B   50  1                                  15    
HELIX   12 AB3 GLY B   53  LEU B   58  5                                   6    
HELIX   13 AB4 GLY B   61  GLY B   82  1                                  22    
HELIX   14 AB5 ASP B   85  ILE B  102  1                                  18    
HELIX   15 AB6 GLN B  106  HIS B  129  1                                  24    
HELIX   16 AB7 ASP B  131  TYR B  157  1                                  27    
HELIX   17 AB8 PHE C    9  GLY C   17  1                                   9    
HELIX   18 AB9 GLY C   19  ALA C   34  1                                  16    
HELIX   19 AC1 HIS C   36  GLY C   50  1                                  15    
HELIX   20 AC2 GLY C   60  GLY C   82  1                                  23    
HELIX   21 AC3 ASP C   85  ILE C  102  1                                  18    
HELIX   22 AC4 GLN C  106  HIS C  129  1                                  24    
HELIX   23 AC5 ASP C  131  TYR C  157  1                                  27    
HELIX   24 AC6 VAL D    8  VAL D   16  1                                   9    
HELIX   25 AC7 GLY D   19  ALA D   34  1                                  16    
HELIX   26 AC8 HIS D   36  HIS D   51  1                                  16    
HELIX   27 AC9 ALA D   54  LEU D   58  5                                   5    
HELIX   28 AD1 GLY D   61  GLY D   82  1                                  22    
HELIX   29 AD2 ASP D   85  GLY D  103  1                                  19    
HELIX   30 AD3 HIS D  107  HIS D  129  1                                  23    
HELIX   31 AD4 ASP D  131  TYR D  157  1                                  27    
HELIX   32 AD5 VAL E    8  GLY E   17  1                                  10    
HELIX   33 AD6 GLY E   19  ALA E   34  1                                  16    
HELIX   34 AD7 HIS E   36  GLY E   50  1                                  15    
HELIX   35 AD8 HIS E   51  THR E   56  1                                   6    
HELIX   36 AD9 GLY E   60  GLY E   82  1                                  23    
HELIX   37 AE1 ASP E   85  ILE E  102  1                                  18    
HELIX   38 AE2 GLN E  106  HIS E  129  1                                  24    
HELIX   39 AE3 ASP E  131  TYR E  157  1                                  27    
HELIX   40 AE4 THR F    7  GLY F   17  1                                  11    
HELIX   41 AE5 GLY F   19  ALA F   34  1                                  16    
HELIX   42 AE6 HIS F   36  GLY F   50  1                                  15    
HELIX   43 AE7 GLY F   53  LEU F   58  5                                   6    
HELIX   44 AE8 GLY F   61  GLY F   82  1                                  22    
HELIX   45 AE9 ASP F   85  ILE F  102  1                                  18    
HELIX   46 AF1 HIS F  107  HIS F  129  1                                  23    
HELIX   47 AF2 ASP F  131  TYR F  157  1                                  27    
HELIX   48 AF3 VAL G    8  GLY G   17  1                                  10    
HELIX   49 AF4 GLY G   19  ALA G   34  1                                  16    
HELIX   50 AF5 HIS G   36  GLY G   50  1                                  15    
HELIX   51 AF6 HIS G   51  THR G   56  1                                   6    
HELIX   52 AF7 GLY G   61  GLY G   82  1                                  22    
HELIX   53 AF8 ASP G   85  ILE G  102  1                                  18    
HELIX   54 AF9 HIS G  107  HIS G  129  1                                  23    
HELIX   55 AG1 ASP G  131  THR G  156  1                                  26    
HELIX   56 AG2 VAL H    8  GLY H   17  1                                  10    
HELIX   57 AG3 GLY H   19  ALA H   34  1                                  16    
HELIX   58 AG4 HIS H   36  GLY H   50  1                                  15    
HELIX   59 AG5 HIS H   51  THR H   56  1                                   6    
HELIX   60 AG6 SER H   63  GLY H   82  1                                  20    
HELIX   61 AG7 ASP H   85  ILE H  102  1                                  18    
HELIX   62 AG8 HIS H  107  HIS H  129  1                                  23    
HELIX   63 AG9 ASP H  131  THR H  156  1                                  26    
LINK         NE2 HIS A  99                FE   HEM A 200     1555   1555  2.25  
LINK         NE2 HIS B  99                FE   HEM B 200     1555   1555  2.09  
LINK         NE2 HIS C  99                FE   HEM C 200     1555   1555  2.01  
LINK         NE2 HIS D  99                FE   HEM D 200     1555   1555  2.10  
LINK         O   ARG E  55                NA    NA E 203     1555   1555  2.74  
LINK         O   LEU E  58                NA    NA E 203     1555   1555  2.68  
LINK         NE2 HIS E  99                FE   HEM E 200     1555   1555  2.17  
LINK         NE2 HIS F  99                FE   HEM F 200     1555   1555  2.12  
LINK         NE2 HIS G  99                FE   HEM G 200     1555   1555  2.16  
LINK         NE2 HIS H  99                FE   HEM H 200     1555   1555  2.15  
LINK        FE   HEM D 200                 O   HOH D 391     1555   1555  2.54  
LINK        NA    NA E 203                 O   HOH E 412     1555   1555  2.20  
LINK        NA    NA E 203                 O   HOH E 429     1555   1555  2.81  
LINK        FE   HEM F 200                 O   HOH F 382     1555   1555  2.62  
LINK        NA    NA E 203                 O   HOH H 381     1555   6444  2.39  
LINK        FE   HEM G 200                 C   CYN G 201     1555   1555  2.10  
LINK        FE   HEM E 200                 C   CYN E 201     1555   1555  1.94  
LINK        FE   HEM A 200                 C   CYN A 201     1555   1555  2.02  
LINK        FE   HEM H 200                 C   CYN H 201     1555   1555  2.13  
LINK        FE   HEM B 200                 C   CYN B 201     1555   1555  2.10  
LINK        FE   HEM C 200                 C   CYN C 201     1555   1555  2.30  
CISPEP   1 GLY A   82    PRO A   83          0        -6.51                     
CISPEP   2 GLY B   82    PRO B   83          0         6.00                     
CISPEP   3 GLY C   82    PRO C   83          0        -4.66                     
CISPEP   4 GLY D   82    PRO D   83          0        -2.61                     
CISPEP   5 GLY E   82    PRO E   83          0         1.85                     
CISPEP   6 GLY F   82    PRO F   83          0        -7.21                     
CISPEP   7 GLY G   82    PRO G   83          0         0.05                     
CISPEP   8 GLY H   82    PRO H   83          0         1.93                     
SITE     1 AC1 12 ALA A  54  MET A  72  TRP A  75  HIS A  99                    
SITE     2 AC1 12 ILE A 102  LEU A 104  MET A 109  ALA A 112                    
SITE     3 AC1 12 MET A 113  MET A 153  CYN A 201  HOH A 304                    
SITE     1 AC2  4 TYR A  45  MET A  72  HEM A 200  HOH A 335                    
SITE     1 AC3  2 ARG A 139  ARG B 139                                          
SITE     1 AC4 14 ILE B  48  ALA B  54  ALA B  57  MET B  72                    
SITE     2 AC4 14 TRP B  75  HIS B  99  ILE B 102  LEU B 104                    
SITE     3 AC4 14 MET B 109  MET B 113  CYN B 201  HOH B 312                    
SITE     4 AC4 14 HOH B 319  HOH B 387                                          
SITE     1 AC5  4 TYR B  45  MET B  72  HEM B 200  HOH B 315                    
SITE     1 AC6 12 ILE C  48  ALA C  54  THR C  71  MET C  72                    
SITE     2 AC6 12 TRP C  75  VAL C  98  HIS C  99  ILE C 102                    
SITE     3 AC6 12 LEU C 104  ALA C 112  MET C 113  CYN C 201                    
SITE     1 AC7  4 TYR C  45  LEU C  68  MET C  72  HEM C 200                    
SITE     1 AC8  2 ARG C 139  ARG D 139                                          
SITE     1 AC9 13 PHE D  44  ILE D  48  ALA D  54  MET D  72                    
SITE     2 AC9 13 TRP D  75  HIS D  99  ARG D 101  LEU D 104                    
SITE     3 AC9 13 ALA D 112  MET D 113  HOH D 303  HOH D 345                    
SITE     4 AC9 13 HOH D 391                                                     
SITE     1 AD1 16 ILE E  48  ALA E  54  LEU E  68  MET E  72                    
SITE     2 AD1 16 TRP E  75  VAL E  98  HIS E  99  ARG E 101                    
SITE     3 AD1 16 ILE E 102  LEU E 104  ALA E 112  MET E 113                    
SITE     4 AD1 16 CYN E 201  HOH E 374  HOH E 375  HOH E 387                    
SITE     1 AD2  3 TYR E  45  MET E  72  HEM E 200                               
SITE     1 AD3  2 ARG E 139  ARG F 139                                          
SITE     1 AD4  5 ARG E  55  LEU E  58  HOH E 412  HOH E 429                    
SITE     2 AD4  5 HOH H 381                                                     
SITE     1 AD5 12 ILE F  48  ALA F  54  GLN F  64  TRP F  75                    
SITE     2 AD5 12 HIS F  99  ARG F 101  LEU F 104  ALA F 112                    
SITE     3 AD5 12 MET F 113  HOH F 375  HOH F 382  HOH F 389                    
SITE     1 AD6 16 VAL F  59  GLY F  60  PHE G  44  ALA G  54                    
SITE     2 AD6 16 LEU G  68  MET G  72  TRP G  75  VAL G  98                    
SITE     3 AD6 16 HIS G  99  ILE G 102  LEU G 104  MET G 109                    
SITE     4 AD6 16 ALA G 112  MET G 113  CYN G 201  HOH G 358                    
SITE     1 AD7  4 PHE G  44  TYR G  45  MET G  72  HEM G 200                    
SITE     1 AD8  2 ARG G 139  ARG H 139                                          
SITE     1 AD9 15 HOH E 321  ILE H  48  ALA H  54  GLN H  64                    
SITE     2 AD9 15 LEU H  68  MET H  72  TRP H  75  HIS H  99                    
SITE     3 AD9 15 LEU H 104  ALA H 112  MET H 113  CYN H 201                    
SITE     4 AD9 15 HOH H 322  HOH H 325  HOH H 381                               
SITE     1 AE1  4 PHE H  44  TYR H  45  MET H  72  HEM H 200                    
CRYST1   78.069   78.069  441.819  90.00  90.00  90.00 P 41 21 2    64          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012809  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002263        0.00000                         
ATOM      1  N   THR A   7      22.513   9.852  -2.900  1.00 51.85           N  
ATOM      2  CA  THR A   7      23.525  10.756  -2.255  1.00 51.41           C  
ATOM      3  C   THR A   7      24.772  10.005  -1.729  1.00 46.31           C  
ATOM      4  O   THR A   7      25.526  10.563  -0.913  1.00 37.99           O  
ATOM      5  CB  THR A   7      22.897  11.604  -1.095  1.00 52.42           C  
ATOM      6  OG1 THR A   7      21.485  11.716  -1.271  1.00 57.97           O  
ATOM      7  CG2 THR A   7      23.484  13.016  -1.036  1.00 50.47           C  
ATOM      8  N   VAL A   8      25.011   8.770  -2.203  1.00 44.97           N  
ATOM      9  CA  VAL A   8      26.150   7.966  -1.721  1.00 41.47           C  
ATOM     10  C   VAL A   8      27.402   8.815  -1.932  1.00 38.44           C  
ATOM     11  O   VAL A   8      28.125   9.109  -0.966  1.00 36.22           O  
ATOM     12  CB  VAL A   8      26.252   6.569  -2.409  1.00 44.72           C  
ATOM     13  CG1 VAL A   8      27.635   5.935  -2.245  1.00 43.11           C  
ATOM     14  CG2 VAL A   8      25.179   5.621  -1.876  1.00 46.26           C  
ATOM     15  N   PHE A   9      27.617   9.254  -3.175  1.00 35.40           N  
ATOM     16  CA  PHE A   9      28.767  10.091  -3.482  1.00 34.89           C  
ATOM     17  C   PHE A   9      28.906  11.292  -2.507  1.00 36.70           C  
ATOM     18  O   PHE A   9      29.965  11.458  -1.941  1.00 35.30           O  
ATOM     19  CB  PHE A   9      28.890  10.461  -4.980  1.00 33.80           C  
ATOM     20  CG  PHE A   9      27.728  11.249  -5.566  0.50 33.38           C  
ATOM     21  CD1 PHE A   9      26.554  10.614  -5.986  0.50 33.36           C  
ATOM     22  CD2 PHE A   9      27.848  12.616  -5.799  0.50 32.84           C  
ATOM     23  CE1 PHE A   9      25.519  11.336  -6.560  0.50 33.38           C  
ATOM     24  CE2 PHE A   9      26.815  13.338  -6.379  0.50 31.27           C  
ATOM     25  CZ  PHE A   9      25.649  12.700  -6.752  0.50 30.98           C  
ATOM     26  N   GLU A  10      27.834  12.047  -2.240  1.00 37.65           N  
ATOM     27  CA  GLU A  10      27.911  13.252  -1.361  1.00 39.48           C  
ATOM     28  C   GLU A  10      28.141  13.033   0.182  1.00 38.34           C  
ATOM     29  O   GLU A  10      28.983  13.717   0.795  1.00 38.60           O  
ATOM     30  CB  GLU A  10      26.707  14.194  -1.622  1.00 46.01           C  
ATOM     31  CG  GLU A  10      27.051  15.408  -2.497  1.00 48.82           C  
ATOM     32  CD  GLU A  10      28.104  16.315  -1.863  1.00 52.51           C  
ATOM     33  OE1 GLU A  10      28.154  16.376  -0.601  1.00 50.31           O  
ATOM     34  OE2 GLU A  10      28.887  16.950  -2.626  1.00 51.72           O  
ATOM     35  N   GLU A  11      27.420  12.098   0.800  1.00 34.59           N  
ATOM     36  CA  GLU A  11      27.707  11.699   2.192  1.00 34.13           C  
ATOM     37  C   GLU A  11      29.105  11.125   2.347  1.00 29.82           C  
ATOM     38  O   GLU A  11      29.801  11.393   3.317  1.00 26.36           O  
ATOM     39  CB  GLU A  11      26.770  10.597   2.654  1.00 40.58           C  
ATOM     40  CG  GLU A  11      25.410  11.037   3.145  1.00 43.47           C  
ATOM     41  CD  GLU A  11      24.943  10.101   4.229  1.00 46.22           C  
ATOM     42  OE1 GLU A  11      25.467  10.260   5.345  1.00 45.58           O  
ATOM     43  OE2 GLU A  11      24.128   9.186   3.952  1.00 48.90           O  
ATOM     44  N   LEU A  12      29.489  10.301   1.390  1.00 26.77           N  
ATOM     45  CA  LEU A  12      30.733   9.570   1.469  1.00 27.50           C  
ATOM     46  C   LEU A  12      31.889  10.506   1.147  1.00 27.55           C  
ATOM     47  O   LEU A  12      32.941  10.430   1.782  1.00 25.65           O  
ATOM     48  CB  LEU A  12      30.676   8.319   0.569  1.00 27.55           C  
ATOM     49  CG  LEU A  12      31.268   6.990   1.048  1.00 30.40           C  
ATOM     50  CD1 LEU A  12      30.940   6.674   2.500  1.00 31.86           C  
ATOM     51  CD2 LEU A  12      30.776   5.875   0.162  1.00 31.02           C  
ATOM     52  N   LYS A  13      31.697  11.442   0.215  1.00 28.19           N  
ATOM     53  CA  LYS A  13      32.758  12.422  -0.069  1.00 27.22           C  
ATOM     54  C   LYS A  13      33.200  13.220   1.175  1.00 23.87           C  
ATOM     55  O   LYS A  13      34.381  13.477   1.373  1.00 22.39           O  
ATOM     56  CB  LYS A  13      32.368  13.333  -1.244  1.00 32.29           C  
ATOM     57  CG  LYS A  13      32.541  12.660  -2.615  1.00 35.82           C  
ATOM     58  CD  LYS A  13      32.584  13.610  -3.809  1.00 37.47           C  
ATOM     59  CE  LYS A  13      31.220  14.052  -4.281  1.00 38.34           C  
ATOM     60  NZ  LYS A  13      31.370  15.125  -5.308  1.00 38.93           N  
ATOM     61  N   ARG A  14      32.255  13.612   2.007  1.00 22.91           N  
ATOM     62  CA  ARG A  14      32.575  14.259   3.288  1.00 24.05           C  
ATOM     63  C   ARG A  14      33.293  13.320   4.251  1.00 20.76           C  
ATOM     64  O   ARG A  14      34.260  13.706   4.896  1.00 22.23           O  
ATOM     65  CB  ARG A  14      31.311  14.799   3.945  1.00 28.19           C  
ATOM     66  CG  ARG A  14      30.774  16.087   3.330  1.00 32.19           C  
ATOM     67  CD  ARG A  14      29.752  16.804   4.219  1.00 35.26           C  
ATOM     68  NE  ARG A  14      28.984  15.891   5.100  1.00 39.63           N  
ATOM     69  CZ  ARG A  14      27.769  15.373   4.860  1.00 41.18           C  
ATOM     70  NH1 ARG A  14      27.083  15.659   3.759  1.00 43.72           N  
ATOM     71  NH2 ARG A  14      27.224  14.550   5.757  1.00 45.85           N  
ATOM     72  N   TYR A  15      32.834  12.078   4.340  1.00 19.85           N  
ATOM     73  CA  TYR A  15      33.486  11.069   5.187  1.00 18.94           C  
ATOM     74  C   TYR A  15      34.976  10.911   4.898  1.00 18.21           C  
ATOM     75  O   TYR A  15      35.771  10.925   5.833  1.00 18.13           O  
ATOM     76  CB  TYR A  15      32.795   9.721   5.031  1.00 20.55           C  
ATOM     77  CG  TYR A  15      33.013   8.750   6.160  1.00 21.35           C  
ATOM     78  CD1 TYR A  15      34.270   8.188   6.403  1.00 22.76           C  
ATOM     79  CD2 TYR A  15      31.940   8.342   6.961  1.00 25.18           C  
ATOM     80  CE1 TYR A  15      34.454   7.277   7.419  1.00 23.26           C  
ATOM     81  CE2 TYR A  15      32.117   7.425   7.995  1.00 25.89           C  
ATOM     82  CZ  TYR A  15      33.384   6.906   8.225  1.00 24.25           C  
ATOM     83  OH  TYR A  15      33.582   5.974   9.219  1.00 22.60           O  
ATOM     84  N   VAL A  16      35.350  10.754   3.617  1.00 17.77           N  
ATOM     85  CA  VAL A  16      36.740  10.477   3.238  1.00 19.19           C  
ATOM     86  C   VAL A  16      37.572  11.734   3.111  1.00 20.96           C  
ATOM     87  O   VAL A  16      38.777  11.647   2.876  1.00 20.53           O  
ATOM     88  CB  VAL A  16      36.906   9.576   1.965  1.00 17.96           C  
ATOM     89  CG1 VAL A  16      36.002   8.345   2.043  1.00 17.97           C  
ATOM     90  CG2 VAL A  16      36.673  10.351   0.681  1.00 18.91           C  
ATOM     91  N   GLY A  17      36.936  12.899   3.242  1.00 24.38           N  
ATOM     92  CA  GLY A  17      37.635  14.184   3.139  1.00 25.47           C  
ATOM     93  C   GLY A  17      37.970  14.510   1.678  1.00 25.91           C  
ATOM     94  O   GLY A  17      39.059  15.002   1.407  1.00 27.19           O  
ATOM     95  N   TRP A  18      37.061  14.204   0.751  1.00 24.24           N  
ATOM     96  CA  TRP A  18      37.282  14.490  -0.677  1.00 25.09           C  
ATOM     97  C   TRP A  18      37.259  15.995  -0.911  1.00 27.72           C  
ATOM     98  O   TRP A  18      36.310  16.659  -0.507  1.00 26.08           O  
ATOM     99  CB  TRP A  18      36.207  13.844  -1.521  1.00 24.86           C  
ATOM    100  CG  TRP A  18      36.320  14.025  -3.030  1.00 24.45           C  
ATOM    101  CD1 TRP A  18      35.744  15.019  -3.796  1.00 24.50           C  
ATOM    102  CD2 TRP A  18      36.975  13.154  -3.942  1.00 24.04           C  
ATOM    103  NE1 TRP A  18      36.033  14.836  -5.113  1.00 25.41           N  
ATOM    104  CE2 TRP A  18      36.791  13.693  -5.240  1.00 25.42           C  
ATOM    105  CE3 TRP A  18      37.711  11.977  -3.797  1.00 23.19           C  
ATOM    106  CZ2 TRP A  18      37.299  13.079  -6.374  1.00 23.01           C  
ATOM    107  CZ3 TRP A  18      38.246  11.393  -4.927  1.00 23.11           C  
ATOM    108  CH2 TRP A  18      38.040  11.949  -6.201  1.00 21.56           C  
ATOM    109  N   GLY A  19      38.314  16.536  -1.519  1.00 27.62           N  
ATOM    110  CA  GLY A  19      38.364  17.966  -1.787  1.00 29.36           C  
ATOM    111  C   GLY A  19      38.999  18.309  -3.111  1.00 29.82           C  
ATOM    112  O   GLY A  19      39.447  17.425  -3.870  1.00 25.33           O  
ATOM    113  N   ASP A  20      39.079  19.616  -3.355  1.00 31.29           N  
ATOM    114  CA  ASP A  20      39.800  20.149  -4.510  1.00 33.21           C  
ATOM    115  C   ASP A  20      41.211  19.597  -4.640  1.00 28.79           C  
ATOM    116  O   ASP A  20      41.647  19.359  -5.773  1.00 27.52           O  
ATOM    117  CB  ASP A  20      39.827  21.686  -4.505  1.00 37.51           C  
ATOM    118  CG  ASP A  20      38.520  22.303  -4.972  1.00 42.51           C  
ATOM    119  OD1 ASP A  20      37.560  21.557  -5.300  1.00 41.25           O  
ATOM    120  OD2 ASP A  20      38.470  23.559  -5.032  1.00 46.83           O  
ATOM    121  N   GLY A  21      41.912  19.362  -3.520  1.00 26.31           N  
ATOM    122  CA  GLY A  21      43.277  18.789  -3.574  1.00 25.73           C  
ATOM    123  C   GLY A  21      43.340  17.328  -4.106  1.00 24.84           C  
ATOM    124  O   GLY A  21      44.338  16.892  -4.716  1.00 25.27           O  
ATOM    125  N   ASP A  22      42.298  16.545  -3.848  1.00 22.79           N  
ATOM    126  CA  ASP A  22      42.240  15.190  -4.420  1.00 21.49           C  
ATOM    127  C   ASP A  22      42.074  15.278  -5.952  1.00 20.34           C  
ATOM    128  O   ASP A  22      42.706  14.506  -6.689  1.00 19.27           O  
ATOM    129  CB  ASP A  22      41.108  14.369  -3.794  1.00 19.54           C  
ATOM    130  CG  ASP A  22      41.330  14.142  -2.303  1.00 19.54           C  
ATOM    131  OD1 ASP A  22      42.290  13.446  -1.923  1.00 18.61           O  
ATOM    132  OD2 ASP A  22      40.546  14.668  -1.502  1.00 19.06           O  
ATOM    133  N   GLU A  23      41.256  16.240  -6.392  1.00 20.82           N  
ATOM    134  CA  GLU A  23      40.985  16.461  -7.815  1.00 22.97           C  
ATOM    135  C   GLU A  23      42.283  16.888  -8.508  1.00 23.44           C  
ATOM    136  O   GLU A  23      42.609  16.346  -9.582  1.00 26.58           O  
ATOM    137  CB  GLU A  23      39.780  17.412  -8.030  1.00 23.19           C  
ATOM    138  CG  GLU A  23      38.547  16.958  -7.262  1.00 23.15           C  
ATOM    139  CD  GLU A  23      37.218  17.595  -7.642  1.00 25.04           C  
ATOM    140  OE1 GLU A  23      37.126  18.518  -8.479  1.00 28.37           O  
ATOM    141  OE2 GLU A  23      36.222  17.128  -7.087  1.00 26.49           O  
ATOM    142  N   ARG A  24      43.080  17.760  -7.886  1.00 23.49           N  
ATOM    143  CA  ARG A  24      44.385  18.177  -8.464  1.00 24.39           C  
ATOM    144  C   ARG A  24      45.417  17.055  -8.489  1.00 23.42           C  
ATOM    145  O   ARG A  24      46.246  16.961  -9.430  1.00 23.36           O  
ATOM    146  CB  ARG A  24      45.005  19.396  -7.727  1.00 25.92           C  
ATOM    147  CG  ARG A  24      44.148  20.643  -7.822  1.00 29.48           C  
ATOM    148  CD  ARG A  24      44.844  21.938  -7.408  1.00 34.05           C  
ATOM    149  NE  ARG A  24      45.191  21.922  -5.990  1.00 39.25           N  
ATOM    150  CZ  ARG A  24      44.370  22.211  -4.977  1.00 39.43           C  
ATOM    151  NH1 ARG A  24      43.105  22.587  -5.180  1.00 41.33           N  
ATOM    152  NH2 ARG A  24      44.834  22.130  -3.730  1.00 41.87           N  
ATOM    153  N   ALA A  25      45.409  16.206  -7.467  1.00 20.31           N  
ATOM    154  CA  ALA A  25      46.390  15.116  -7.440  1.00 19.19           C  
ATOM    155  C   ALA A  25      46.113  14.099  -8.572  1.00 18.66           C  
ATOM    156  O   ALA A  25      47.014  13.679  -9.300  1.00 19.25           O  
ATOM    157  CB  ALA A  25      46.426  14.460  -6.063  1.00 18.53           C  
ATOM    158  N   LEU A  26      44.860  13.730  -8.733  1.00 19.07           N  
ATOM    159  CA  LEU A  26      44.448  12.774  -9.748  1.00 18.78           C  
ATOM    160  C   LEU A  26      44.684  13.304 -11.161  1.00 19.83           C  
ATOM    161  O   LEU A  26      45.154  12.561 -12.012  1.00 19.47           O  
ATOM    162  CB  LEU A  26      42.994  12.366  -9.556  1.00 18.07           C  
ATOM    163  CG  LEU A  26      42.563  11.577  -8.313  1.00 17.63           C  
ATOM    164  CD1 LEU A  26      41.067  11.294  -8.436  1.00 17.60           C  
ATOM    165  CD2 LEU A  26      43.304  10.252  -8.188  1.00 18.10           C  
ATOM    166  N   ARG A  27      44.396  14.585 -11.413  1.00 20.70           N  
ATOM    167  CA  ARG A  27      44.758  15.228 -12.717  1.00 22.08           C  
ATOM    168  C   ARG A  27      46.239  15.211 -13.004  1.00 21.01           C  
ATOM    169  O   ARG A  27      46.660  15.092 -14.152  1.00 21.88           O  
ATOM    170  CB  ARG A  27      44.263  16.673 -12.801  1.00 22.88           C  
ATOM    171  CG  ARG A  27      42.795  16.782 -13.066  1.00 24.93           C  
ATOM    172  CD  ARG A  27      42.424  18.198 -13.539  1.00 27.44           C  
ATOM    173  NE  ARG A  27      41.076  18.499 -13.119  1.00 29.66           N  
ATOM    174  CZ  ARG A  27      40.736  19.138 -12.001  1.00 31.05           C  
ATOM    175  NH1 ARG A  27      41.643  19.655 -11.174  1.00 34.40           N  
ATOM    176  NH2 ARG A  27      39.449  19.297 -11.729  1.00 32.66           N  
ATOM    177  N   SER A  28      47.042  15.357 -11.970  1.00 22.50           N  
ATOM    178  CA  SER A  28      48.482  15.323 -12.102  1.00 23.98           C  
ATOM    179  C   SER A  28      48.945  13.911 -12.488  1.00 24.96           C  
ATOM    180  O   SER A  28      49.828  13.751 -13.326  1.00 25.83           O  
ATOM    181  CB  SER A  28      49.126  15.782 -10.793  1.00 25.27           C  
ATOM    182  OG  SER A  28      50.524  15.859 -10.935  1.00 29.05           O  
ATOM    183  N   LEU A  29      48.320  12.893 -11.905  1.00 21.94           N  
ATOM    184  CA  LEU A  29      48.639  11.495 -12.248  1.00 22.23           C  
ATOM    185  C   LEU A  29      48.228  11.113 -13.676  1.00 22.17           C  
ATOM    186  O   LEU A  29      48.904  10.297 -14.309  1.00 21.57           O  
ATOM    187  CB  LEU A  29      47.930  10.556 -11.271  1.00 21.08           C  
ATOM    188  CG  LEU A  29      48.073   9.039 -11.405  1.00 20.66           C  
ATOM    189  CD1 LEU A  29      49.505   8.622 -11.413  1.00 20.91           C  
ATOM    190  CD2 LEU A  29      47.319   8.306 -10.309  1.00 21.03           C  
ATOM    191  N   HIS A  30      47.122  11.690 -14.146  1.00 22.32           N  
ATOM    192  CA  HIS A  30      46.495  11.400 -15.445  1.00 24.36           C  
ATOM    193  C   HIS A  30      47.502  11.486 -16.536  1.00 23.20           C  
ATOM    194  O   HIS A  30      47.600  10.578 -17.334  1.00 20.94           O  
ATOM    195  CB  HIS A  30      45.338  12.378 -15.718  1.00 25.12           C  
ATOM    196  CG  HIS A  30      44.592  12.124 -16.994  1.00 27.39           C  
ATOM    197  ND1 HIS A  30      44.801  12.860 -18.144  1.00 28.18           N  
ATOM    198  CD2 HIS A  30      43.634  11.222 -17.296  1.00 27.17           C  
ATOM    199  CE1 HIS A  30      43.990  12.430 -19.093  1.00 30.39           C  
ATOM    200  NE2 HIS A  30      43.259  11.445 -18.597  1.00 26.90           N  
ATOM    201  N   GLY A  31      48.292  12.568 -16.527  1.00 25.50           N  
ATOM    202  CA  GLY A  31      49.301  12.813 -17.543  1.00 24.72           C  
ATOM    203  C   GLY A  31      50.405  11.782 -17.525  1.00 25.87           C  
ATOM    204  O   GLY A  31      50.909  11.409 -18.574  1.00 27.86           O  
ATOM    205  N   ALA A  32      50.781  11.294 -16.347  1.00 25.10           N  
ATOM    206  CA  ALA A  32      51.743  10.189 -16.277  1.00 25.08           C  
ATOM    207  C   ALA A  32      51.149   8.831 -16.665  1.00 23.97           C  
ATOM    208  O   ALA A  32      51.810   8.027 -17.280  1.00 24.43           O  
ATOM    209  CB  ALA A  32      52.321  10.088 -14.882  1.00 25.78           C  
ATOM    210  N   ALA A  33      49.915   8.559 -16.269  1.00 21.36           N  
ATOM    211  CA  ALA A  33      49.367   7.201 -16.356  1.00 20.19           C  
ATOM    212  C   ALA A  33      48.711   6.868 -17.701  1.00 19.59           C  
ATOM    213  O   ALA A  33      48.738   5.708 -18.110  1.00 17.62           O  
ATOM    214  CB  ALA A  33      48.394   6.961 -15.186  1.00 19.16           C  
ATOM    215  N   ALA A  34      48.105   7.869 -18.358  1.00 18.71           N  
ATOM    216  CA  ALA A  34      47.412   7.693 -19.624  1.00 19.70           C  
ATOM    217  C   ALA A  34      48.118   6.850 -20.669  1.00 19.22           C  
ATOM    218  O   ALA A  34      47.470   5.971 -21.253  1.00 19.85           O  
ATOM    219  CB  ALA A  34      47.022   9.040 -20.223  1.00 22.51           C  
ATOM    220  N   PRO A  35      49.424   7.075 -20.908  1.00 19.41           N  
ATOM    221  CA  PRO A  35      50.125   6.208 -21.860  1.00 19.27           C  
ATOM    222  C   PRO A  35      50.107   4.691 -21.522  1.00 20.89           C  
ATOM    223  O   PRO A  35      50.315   3.849 -22.420  1.00 19.65           O  
ATOM    224  CB  PRO A  35      51.580   6.718 -21.802  1.00 21.50           C  
ATOM    225  CG  PRO A  35      51.489   8.147 -21.362  1.00 20.97           C  
ATOM    226  CD  PRO A  35      50.249   8.239 -20.493  1.00 20.17           C  
ATOM    227  N   HIS A  36      49.902   4.355 -20.240  1.00 19.94           N  
ATOM    228  CA  HIS A  36      49.830   2.971 -19.774  1.00 19.14           C  
ATOM    229  C   HIS A  36      48.432   2.405 -19.723  1.00 17.62           C  
ATOM    230  O   HIS A  36      48.285   1.229 -19.421  1.00 19.86           O  
ATOM    231  CB  HIS A  36      50.469   2.855 -18.399  1.00 21.26           C  
ATOM    232  CG  HIS A  36      51.863   3.375 -18.371  1.00 25.09           C  
ATOM    233  ND1 HIS A  36      52.949   2.588 -18.676  1.00 26.75           N  
ATOM    234  CD2 HIS A  36      52.343   4.624 -18.158  1.00 25.97           C  
ATOM    235  CE1 HIS A  36      54.047   3.320 -18.618  1.00 29.04           C  
ATOM    236  NE2 HIS A  36      53.709   4.557 -18.305  1.00 29.50           N  
ATOM    237  N   PHE A  37      47.406   3.187 -20.018  1.00 17.48           N  
ATOM    238  CA  PHE A  37      46.017   2.678 -19.918  1.00 17.44           C  
ATOM    239  C   PHE A  37      45.804   1.438 -20.785  1.00 17.75           C  
ATOM    240  O   PHE A  37      45.117   0.517 -20.342  1.00 16.92           O  
ATOM    241  CB  PHE A  37      44.966   3.727 -20.266  1.00 18.73           C  
ATOM    242  CG  PHE A  37      44.812   4.868 -19.274  1.00 18.98           C  
ATOM    243  CD1 PHE A  37      45.311   4.836 -17.976  1.00 20.42           C  
ATOM    244  CD2 PHE A  37      44.084   5.977 -19.655  1.00 21.40           C  
ATOM    245  CE1 PHE A  37      45.071   5.883 -17.091  1.00 20.11           C  
ATOM    246  CE2 PHE A  37      43.885   7.060 -18.788  1.00 20.73           C  
ATOM    247  CZ  PHE A  37      44.369   7.010 -17.501  1.00 19.99           C  
ATOM    248  N   PRO A  38      46.400   1.387 -22.026  1.00 17.11           N  
ATOM    249  CA  PRO A  38      46.275   0.137 -22.772  1.00 17.25           C  
ATOM    250  C   PRO A  38      46.820  -1.091 -22.073  1.00 16.44           C  
ATOM    251  O   PRO A  38      46.186  -2.122 -22.121  1.00 17.13           O  
ATOM    252  CB  PRO A  38      46.993   0.425 -24.115  1.00 17.00           C  
ATOM    253  CG  PRO A  38      46.915   1.911 -24.275  1.00 16.47           C  
ATOM    254  CD  PRO A  38      47.028   2.440 -22.857  1.00 16.89           C  
ATOM    255  N   ARG A  39      47.975  -0.983 -21.445  1.00 19.45           N  
ATOM    256  CA  ARG A  39      48.542  -2.052 -20.595  1.00 21.18           C  
ATOM    257  C   ARG A  39      47.618  -2.434 -19.402  1.00 20.41           C  
ATOM    258  O   ARG A  39      47.346  -3.602 -19.148  1.00 18.38           O  
ATOM    259  CB  ARG A  39      49.918  -1.616 -20.123  1.00 24.57           C  
ATOM    260  CG  ARG A  39      50.701  -2.614 -19.289  1.00 28.78           C  
ATOM    261  CD  ARG A  39      51.966  -1.964 -18.666  1.00 33.88           C  
ATOM    262  NE  ARG A  39      52.421  -2.766 -17.515  1.00 41.48           N  
ATOM    263  CZ  ARG A  39      53.573  -2.642 -16.843  1.00 41.47           C  
ATOM    264  NH1 ARG A  39      54.490  -1.727 -17.151  1.00 43.14           N  
ATOM    265  NH2 ARG A  39      53.807  -3.466 -15.832  1.00 44.40           N  
ATOM    266  N   LEU A  40      47.132  -1.441 -18.679  1.00 17.88           N  
ATOM    267  CA  LEU A  40      46.185  -1.697 -17.611  1.00 17.32           C  
ATOM    268  C   LEU A  40      44.907  -2.430 -18.081  1.00 16.01           C  
ATOM    269  O   LEU A  40      44.406  -3.323 -17.392  1.00 13.22           O  
ATOM    270  CB  LEU A  40      45.794  -0.394 -16.943  1.00 18.03           C  
ATOM    271  CG  LEU A  40      46.902   0.319 -16.209  1.00 19.39           C  
ATOM    272  CD1 LEU A  40      46.301   1.551 -15.571  1.00 19.97           C  
ATOM    273  CD2 LEU A  40      47.503  -0.587 -15.165  1.00 20.52           C  
ATOM    274  N   ALA A  41      44.405  -2.052 -19.253  1.00 16.18           N  
ATOM    275  CA  ALA A  41      43.247  -2.677 -19.821  1.00 16.52           C  
ATOM    276  C   ALA A  41      43.568  -4.131 -20.191  1.00 16.71           C  
ATOM    277  O   ALA A  41      42.805  -5.035 -19.893  1.00 16.33           O  
ATOM    278  CB  ALA A  41      42.758  -1.867 -21.000  1.00 17.33           C  
ATOM    279  N   GLU A  42      44.746  -4.359 -20.762  1.00 18.45           N  
ATOM    280  CA  GLU A  42      45.183  -5.724 -21.056  1.00 19.55           C  
ATOM    281  C   GLU A  42      45.252  -6.580 -19.804  1.00 17.02           C  
ATOM    282  O   GLU A  42      44.800  -7.723 -19.807  1.00 16.51           O  
ATOM    283  CB  GLU A  42      46.563  -5.723 -21.723  1.00 23.46           C  
ATOM    284  CG  GLU A  42      46.729  -6.873 -22.695  1.00 28.10           C  
ATOM    285  CD  GLU A  42      46.373  -6.513 -24.119  1.00 29.36           C  
ATOM    286  OE1 GLU A  42      47.139  -6.936 -24.998  1.00 40.67           O  
ATOM    287  OE2 GLU A  42      45.373  -5.818 -24.384  1.00 31.26           O  
ATOM    288  N   GLU A  43      45.838  -6.027 -18.748  1.00 14.56           N  
ATOM    289  CA  GLU A  43      46.007  -6.735 -17.465  1.00 14.54           C  
ATOM    290  C   GLU A  43      44.618  -7.099 -16.886  1.00 13.42           C  
ATOM    291  O   GLU A  43      44.433  -8.187 -16.341  1.00 14.14           O  
ATOM    292  CB  GLU A  43      46.909  -5.914 -16.481  1.00 16.36           C  
ATOM    293  CG  GLU A  43      48.438  -5.990 -16.784  0.50 18.16           C  
ATOM    294  CD  GLU A  43      49.334  -4.870 -16.164  0.50 20.64           C  
ATOM    295  OE1 GLU A  43      50.561  -4.825 -16.433  0.50 18.82           O  
ATOM    296  OE2 GLU A  43      48.859  -3.989 -15.403  1.00 30.66           O  
ATOM    297  N   PHE A  44      43.664  -6.162 -16.978  1.00 12.26           N  
ATOM    298  CA  PHE A  44      42.305  -6.333 -16.510  1.00 11.64           C  
ATOM    299  C   PHE A  44      41.608  -7.494 -17.222  1.00 12.24           C  
ATOM    300  O   PHE A  44      40.975  -8.350 -16.562  1.00 13.83           O  
ATOM    301  CB  PHE A  44      41.535  -5.010 -16.755  1.00 11.18           C  
ATOM    302  CG  PHE A  44      40.189  -4.924 -16.129  1.00 10.95           C  
ATOM    303  CD1 PHE A  44      39.039  -5.299 -16.802  1.00 10.76           C  
ATOM    304  CD2 PHE A  44      40.062  -4.370 -14.856  1.00 11.63           C  
ATOM    305  CE1 PHE A  44      37.793  -5.169 -16.226  1.00 10.50           C  
ATOM    306  CE2 PHE A  44      38.841  -4.210 -14.268  1.00 11.17           C  
ATOM    307  CZ  PHE A  44      37.685  -4.633 -14.942  1.00 11.17           C  
ATOM    308  N   TYR A  45      41.622  -7.476 -18.563  1.00 11.56           N  
ATOM    309  CA  TYR A  45      40.990  -8.565 -19.315  1.00 12.73           C  
ATOM    310  C   TYR A  45      41.690  -9.907 -19.171  1.00 12.78           C  
ATOM    311  O   TYR A  45      40.989 -10.914 -19.083  1.00 15.25           O  
ATOM    312  CB  TYR A  45      40.598  -8.163 -20.766  1.00 11.56           C  
ATOM    313  CG  TYR A  45      39.592  -7.046 -20.649  1.00 11.66           C  
ATOM    314  CD1 TYR A  45      38.299  -7.267 -20.238  1.00 11.22           C  
ATOM    315  CD2 TYR A  45      39.996  -5.723 -20.839  1.00 11.60           C  
ATOM    316  CE1 TYR A  45      37.413  -6.212 -20.061  1.00 11.02           C  
ATOM    317  CE2 TYR A  45      39.152  -4.688 -20.592  1.00 11.52           C  
ATOM    318  CZ  TYR A  45      37.867  -4.933 -20.218  1.00 11.75           C  
ATOM    319  OH  TYR A  45      37.072  -3.827 -20.058  1.00 11.48           O  
ATOM    320  N   ASP A  46      43.013  -9.940 -19.092  1.00 13.84           N  
ATOM    321  CA  ASP A  46      43.731 -11.206 -18.912  1.00 15.35           C  
ATOM    322  C   ASP A  46      43.353 -11.843 -17.566  1.00 14.99           C  
ATOM    323  O   ASP A  46      43.214 -13.063 -17.479  1.00 13.00           O  
ATOM    324  CB  ASP A  46      45.247 -11.052 -19.034  1.00 18.18           C  
ATOM    325  CG  ASP A  46      45.731 -10.955 -20.492  1.00 22.90           C  
ATOM    326  OD1 ASP A  46      44.982 -11.247 -21.471  1.00 27.61           O  
ATOM    327  OD2 ASP A  46      46.902 -10.582 -20.659  1.00 29.62           O  
ATOM    328  N   ARG A  47      43.080 -11.019 -16.545  1.00 14.00           N  
ATOM    329  CA  ARG A  47      42.661 -11.565 -15.265  1.00 13.99           C  
ATOM    330  C   ARG A  47      41.276 -12.191 -15.344  1.00 13.63           C  
ATOM    331  O   ARG A  47      41.074 -13.272 -14.795  1.00 13.82           O  
ATOM    332  CB  ARG A  47      42.759 -10.533 -14.156  1.00 14.69           C  
ATOM    333  CG  ARG A  47      42.957 -11.111 -12.761  1.00 15.84           C  
ATOM    334  CD  ARG A  47      44.354 -11.673 -12.525  1.00 16.26           C  
ATOM    335  NE  ARG A  47      45.372 -10.645 -12.572  1.00 17.88           N  
ATOM    336  CZ  ARG A  47      45.766  -9.884 -11.544  1.00 19.45           C  
ATOM    337  NH1 ARG A  47      45.242 -10.028 -10.320  1.00 19.85           N  
ATOM    338  NH2 ARG A  47      46.718  -8.971 -11.740  1.00 20.56           N  
ATOM    339  N   ILE A  48      40.343 -11.561 -16.060  1.00 13.01           N  
ATOM    340  CA  ILE A  48      39.017 -12.101 -16.229  1.00 11.97           C  
ATOM    341  C   ILE A  48      39.084 -13.467 -16.979  1.00 12.27           C  
ATOM    342  O   ILE A  48      38.435 -14.440 -16.564  1.00 11.01           O  
ATOM    343  CB  ILE A  48      38.060 -11.146 -16.968  1.00 11.99           C  
ATOM    344  CG1 ILE A  48      37.728  -9.908 -16.091  1.00 12.04           C  
ATOM    345  CG2 ILE A  48      36.779 -11.889 -17.311  1.00 12.67           C  
ATOM    346  CD1 ILE A  48      37.156  -8.711 -16.800  1.00 11.74           C  
ATOM    347  N   LEU A  49      39.829 -13.504 -18.083  1.00 13.02           N  
ATOM    348  CA  LEU A  49      39.957 -14.702 -18.914  1.00 13.75           C  
ATOM    349  C   LEU A  49      40.684 -15.855 -18.251  1.00 15.25           C  
ATOM    350  O   LEU A  49      40.388 -17.013 -18.539  1.00 15.52           O  
ATOM    351  CB  LEU A  49      40.622 -14.344 -20.247  1.00 14.27           C  
ATOM    352  CG  LEU A  49      39.749 -13.552 -21.229  1.00 14.20           C  
ATOM    353  CD1 LEU A  49      40.562 -13.066 -22.437  1.00 15.14           C  
ATOM    354  CD2 LEU A  49      38.524 -14.305 -21.697  1.00 15.14           C  
ATOM    355  N   GLY A  50      41.575 -15.557 -17.307  1.00 16.72           N  
ATOM    356  CA  GLY A  50      42.235 -16.591 -16.526  1.00 18.30           C  
ATOM    357  C   GLY A  50      41.476 -17.086 -15.305  1.00 18.95           C  
ATOM    358  O   GLY A  50      41.899 -18.053 -14.650  1.00 21.22           O  
ATOM    359  N   HIS A  51      40.361 -16.452 -14.972  1.00 18.44           N  
ATOM    360  CA  HIS A  51      39.613 -16.805 -13.757  1.00 17.80           C  
ATOM    361  C   HIS A  51      38.439 -17.696 -14.073  1.00 17.13           C  
ATOM    362  O   HIS A  51      37.592 -17.332 -14.869  1.00 15.86           O  
ATOM    363  CB  HIS A  51      39.146 -15.532 -13.034  1.00 16.97           C  
ATOM    364  CG  HIS A  51      38.527 -15.803 -11.690  1.00 16.59           C  
ATOM    365  ND1 HIS A  51      37.164 -15.925 -11.512  1.00 16.24           N  
ATOM    366  CD2 HIS A  51      39.088 -15.989 -10.469  1.00 16.38           C  
ATOM    367  CE1 HIS A  51      36.908 -16.157 -10.233  1.00 16.59           C  
ATOM    368  NE2 HIS A  51      38.060 -16.220  -9.581  1.00 16.74           N  
ATOM    369  N   GLU A  52      38.379 -18.871 -13.437  1.00 20.49           N  
ATOM    370  CA  GLU A  52      37.397 -19.903 -13.795  1.00 22.24           C  
ATOM    371  C   GLU A  52      35.906 -19.479 -13.826  1.00 21.54           C  
ATOM    372  O   GLU A  52      35.130 -19.949 -14.683  1.00 26.17           O  
ATOM    373  CB  GLU A  52      37.573 -21.166 -12.901  1.00 24.70           C  
ATOM    374  CG  GLU A  52      36.761 -22.340 -13.444  1.00 28.50           C  
ATOM    375  CD  GLU A  52      36.871 -23.607 -12.622  1.00 32.94           C  
ATOM    376  OE1 GLU A  52      36.258 -24.628 -13.016  1.00 38.17           O  
ATOM    377  OE2 GLU A  52      37.554 -23.591 -11.582  1.00 39.42           O  
ATOM    378  N   GLY A  53      35.502 -18.674 -12.864  1.00 19.05           N  
ATOM    379  CA  GLY A  53      34.124 -18.159 -12.772  1.00 18.92           C  
ATOM    380  C   GLY A  53      33.861 -16.924 -13.605  1.00 17.99           C  
ATOM    381  O   GLY A  53      32.847 -16.852 -14.317  1.00 19.50           O  
ATOM    382  N   ALA A  54      34.802 -15.976 -13.590  1.00 15.79           N  
ATOM    383  CA  ALA A  54      34.604 -14.679 -14.241  1.00 14.32           C  
ATOM    384  C   ALA A  54      34.676 -14.804 -15.761  1.00 14.08           C  
ATOM    385  O   ALA A  54      33.925 -14.162 -16.465  1.00 12.83           O  
ATOM    386  CB  ALA A  54      35.655 -13.655 -13.761  1.00 14.47           C  
ATOM    387  N   ARG A  55      35.575 -15.651 -16.250  1.00 15.51           N  
ATOM    388  CA  ARG A  55      35.804 -15.826 -17.697  1.00 16.76           C  
ATOM    389  C   ARG A  55      34.533 -16.114 -18.502  1.00 16.62           C  
ATOM    390  O   ARG A  55      34.500 -15.827 -19.681  1.00 15.39           O  
ATOM    391  CB  ARG A  55      36.822 -16.936 -17.961  1.00 18.06           C  
ATOM    392  CG  ARG A  55      36.270 -18.298 -17.619  1.00 20.35           C  
ATOM    393  CD  ARG A  55      36.937 -19.380 -18.349  1.00 24.13           C  
ATOM    394  NE  ARG A  55      37.962 -20.093 -17.602  1.00 26.91           N  
ATOM    395  CZ  ARG A  55      37.911 -21.375 -17.226  1.00 25.03           C  
ATOM    396  NH1 ARG A  55      38.962 -21.893 -16.618  1.00 23.65           N  
ATOM    397  NH2 ARG A  55      36.848 -22.137 -17.427  1.00 30.09           N  
ATOM    398  N   THR A  56      33.511 -16.724 -17.878  1.00 18.18           N  
ATOM    399  CA  THR A  56      32.288 -17.117 -18.597  1.00 18.19           C  
ATOM    400  C   THR A  56      31.416 -15.914 -18.952  1.00 17.50           C  
ATOM    401  O   THR A  56      30.486 -16.040 -19.749  1.00 17.59           O  
ATOM    402  CB  THR A  56      31.439 -18.128 -17.786  1.00 21.38           C  
ATOM    403  OG1 THR A  56      30.831 -17.467 -16.676  1.00 26.15           O  
ATOM    404  CG2 THR A  56      32.266 -19.258 -17.265  1.00 21.81           C  
ATOM    405  N   ALA A  57      31.716 -14.729 -18.413  1.00 16.43           N  
ATOM    406  CA  ALA A  57      31.009 -13.528 -18.812  1.00 16.99           C  
ATOM    407  C   ALA A  57      31.500 -12.987 -20.160  1.00 17.91           C  
ATOM    408  O   ALA A  57      30.872 -12.079 -20.684  1.00 20.35           O  
ATOM    409  CB  ALA A  57      31.131 -12.456 -17.745  1.00 16.83           C  
ATOM    410  N   LEU A  58      32.649 -13.467 -20.671  1.00 17.17           N  
ATOM    411  CA  LEU A  58      33.196 -13.015 -21.968  1.00 17.96           C  
ATOM    412  C   LEU A  58      33.099 -14.101 -23.022  1.00 16.79           C  
ATOM    413  O   LEU A  58      34.099 -14.738 -23.355  1.00 17.84           O  
ATOM    414  CB  LEU A  58      34.638 -12.504 -21.831  1.00 17.99           C  
ATOM    415  CG  LEU A  58      34.831 -11.384 -20.780  1.00 19.46           C  
ATOM    416  CD1 LEU A  58      36.273 -10.867 -20.763  1.00 20.79           C  
ATOM    417  CD2 LEU A  58      33.854 -10.233 -20.937  1.00 19.69           C  
ATOM    418  N   VAL A  59      31.880 -14.305 -23.533  1.00 16.01           N  
ATOM    419  CA  VAL A  59      31.627 -15.251 -24.619  1.00 17.54           C  
ATOM    420  C   VAL A  59      31.165 -14.540 -25.919  1.00 18.30           C  
ATOM    421  O   VAL A  59      30.632 -15.174 -26.813  1.00 17.54           O  
ATOM    422  CB  VAL A  59      30.577 -16.378 -24.263  1.00 17.97           C  
ATOM    423  CG1 VAL A  59      31.125 -17.387 -23.261  1.00 18.96           C  
ATOM    424  CG2 VAL A  59      29.241 -15.773 -23.819  1.00 19.29           C  
ATOM    425  N   GLY A  60      31.375 -13.231 -26.054  1.00 18.28           N  
ATOM    426  CA  GLY A  60      30.971 -12.528 -27.273  1.00 19.06           C  
ATOM    427  C   GLY A  60      32.073 -12.307 -28.293  1.00 18.62           C  
ATOM    428  O   GLY A  60      31.893 -11.542 -29.227  1.00 22.02           O  
ATOM    429  N   GLY A  61      33.235 -12.913 -28.082  1.00 18.35           N  
ATOM    430  CA  GLY A  61      34.289 -12.969 -29.072  1.00 17.71           C  
ATOM    431  C   GLY A  61      35.316 -11.877 -28.995  1.00 17.76           C  
ATOM    432  O   GLY A  61      35.315 -11.072 -28.071  1.00 18.79           O  
ATOM    433  N   GLU A  62      36.213 -11.856 -29.970  1.00 17.89           N  
ATOM    434  CA  GLU A  62      37.360 -10.949 -29.919  1.00 19.83           C  
ATOM    435  C   GLU A  62      36.896  -9.476 -30.036  1.00 18.17           C  
ATOM    436  O   GLU A  62      37.546  -8.556 -29.450  1.00 17.53           O  
ATOM    437  CB  GLU A  62      38.466 -11.320 -30.954  1.00 22.36           C  
ATOM    438  CG  GLU A  62      38.870 -12.799 -30.958  1.00 25.38           C  
ATOM    439  CD  GLU A  62      40.367 -13.141 -30.835  1.00 30.23           C  
ATOM    440  OE1 GLU A  62      40.901 -13.671 -31.858  1.00 29.85           O  
ATOM    441  OE2 GLU A  62      40.992 -13.028 -29.712  1.00 29.43           O  
ATOM    442  N   SER A  63      35.775  -9.248 -30.736  1.00 16.97           N  
ATOM    443  CA  SER A  63      35.166  -7.921 -30.842  1.00 17.10           C  
ATOM    444  C   SER A  63      34.583  -7.480 -29.508  1.00 16.65           C  
ATOM    445  O   SER A  63      34.772  -6.352 -29.142  1.00 14.87           O  
ATOM    446  CB  SER A  63      34.136  -7.832 -31.969  1.00 17.67           C  
ATOM    447  OG  SER A  63      34.826  -8.016 -33.216  1.00 19.22           O  
ATOM    448  N   GLN A  64      33.926  -8.362 -28.756  1.00 16.53           N  
ATOM    449  CA  GLN A  64      33.430  -7.949 -27.426  1.00 16.46           C  
ATOM    450  C   GLN A  64      34.620  -7.468 -26.571  1.00 15.38           C  
ATOM    451  O   GLN A  64      34.531  -6.397 -25.975  1.00 15.06           O  
ATOM    452  CB  GLN A  64      32.621  -9.053 -26.730  1.00 16.93           C  
ATOM    453  CG  GLN A  64      32.137  -8.730 -25.279  1.00 17.08           C  
ATOM    454  CD  GLN A  64      31.717  -9.975 -24.544  1.00 16.37           C  
ATOM    455  OE1 GLN A  64      32.483 -10.958 -24.471  1.00 17.12           O  
ATOM    456  NE2 GLN A  64      30.532  -9.958 -23.989  1.00 17.00           N  
ATOM    457  N   VAL A  65      35.732  -8.222 -26.546  1.00 14.33           N  
ATOM    458  CA  VAL A  65      36.890  -7.844 -25.719  1.00 15.15           C  
ATOM    459  C   VAL A  65      37.470  -6.539 -26.250  1.00 14.15           C  
ATOM    460  O   VAL A  65      37.768  -5.633 -25.484  1.00 11.65           O  
ATOM    461  CB  VAL A  65      38.009  -8.917 -25.653  1.00 15.79           C  
ATOM    462  CG1 VAL A  65      39.222  -8.409 -24.880  1.00 17.50           C  
ATOM    463  CG2 VAL A  65      37.496 -10.229 -25.076  1.00 17.22           C  
ATOM    464  N   GLY A  66      37.612  -6.433 -27.570  1.00 13.23           N  
ATOM    465  CA  GLY A  66      38.140  -5.185 -28.167  1.00 12.95           C  
ATOM    466  C   GLY A  66      37.333  -3.935 -27.805  1.00 12.40           C  
ATOM    467  O   GLY A  66      37.915  -2.889 -27.496  1.00 13.89           O  
ATOM    468  N   HIS A  67      36.013  -4.040 -27.841  1.00 13.13           N  
ATOM    469  CA  HIS A  67      35.147  -2.927 -27.506  1.00 13.45           C  
ATOM    470  C   HIS A  67      35.239  -2.607 -25.989  1.00 14.03           C  
ATOM    471  O   HIS A  67      35.273  -1.422 -25.575  1.00 14.07           O  
ATOM    472  CB  HIS A  67      33.711  -3.207 -27.921  1.00 14.57           C  
ATOM    473  CG  HIS A  67      33.463  -3.024 -29.401  1.00 14.93           C  
ATOM    474  ND1 HIS A  67      33.817  -1.873 -30.082  1.00 15.69           N  
ATOM    475  CD2 HIS A  67      32.909  -3.850 -30.317  1.00 15.73           C  
ATOM    476  CE1 HIS A  67      33.494  -2.009 -31.362  1.00 15.82           C  
ATOM    477  NE2 HIS A  67      32.926  -3.195 -31.524  1.00 14.59           N  
ATOM    478  N   LEU A  68      35.273  -3.650 -25.166  1.00 13.44           N  
ATOM    479  CA  LEU A  68      35.393  -3.426 -23.708  1.00 13.44           C  
ATOM    480  C   LEU A  68      36.701  -2.703 -23.377  1.00 13.96           C  
ATOM    481  O   LEU A  68      36.712  -1.865 -22.505  1.00 14.19           O  
ATOM    482  CB  LEU A  68      35.283  -4.740 -22.933  1.00 13.96           C  
ATOM    483  CG  LEU A  68      33.887  -5.299 -22.865  1.00 14.70           C  
ATOM    484  CD1 LEU A  68      33.954  -6.545 -22.048  1.00 15.94           C  
ATOM    485  CD2 LEU A  68      32.852  -4.344 -22.282  1.00 15.29           C  
ATOM    486  N   LYS A  69      37.811  -3.025 -24.068  1.00 13.52           N  
ATOM    487  CA  LYS A  69      39.065  -2.314 -23.867  1.00 14.33           C  
ATOM    488  C   LYS A  69      38.952  -0.811 -24.120  1.00 14.04           C  
ATOM    489  O   LYS A  69      39.498  -0.001 -23.356  1.00 13.08           O  
ATOM    490  CB  LYS A  69      40.192  -2.934 -24.696  1.00 15.15           C  
ATOM    491  CG  LYS A  69      40.802  -4.193 -24.040  1.00 17.16           C  
ATOM    492  CD  LYS A  69      41.677  -4.995 -24.969  1.00 17.58           C  
ATOM    493  CE  LYS A  69      42.092  -6.286 -24.331  1.00 19.21           C  
ATOM    494  NZ  LYS A  69      42.971  -7.110 -25.204  1.00 20.34           N  
ATOM    495  N   VAL A  70      38.237  -0.450 -25.179  1.00 14.12           N  
ATOM    496  CA  VAL A  70      37.995   0.978 -25.522  1.00 13.96           C  
ATOM    497  C   VAL A  70      37.201   1.672 -24.413  1.00 13.97           C  
ATOM    498  O   VAL A  70      37.584   2.714 -23.963  1.00 13.05           O  
ATOM    499  CB  VAL A  70      37.282   1.121 -26.898  1.00 14.05           C  
ATOM    500  CG1 VAL A  70      36.910   2.564 -27.185  1.00 14.71           C  
ATOM    501  CG2 VAL A  70      38.162   0.570 -28.004  1.00 15.01           C  
ATOM    502  N   THR A  71      36.093   1.096 -23.970  1.00 14.17           N  
ATOM    503  CA  THR A  71      35.349   1.711 -22.915  1.00 14.68           C  
ATOM    504  C   THR A  71      36.112   1.709 -21.569  1.00 13.41           C  
ATOM    505  O   THR A  71      35.897   2.585 -20.757  1.00 13.60           O  
ATOM    506  CB  THR A  71      33.934   1.129 -22.791  1.00 15.78           C  
ATOM    507  OG1 THR A  71      33.967  -0.288 -22.685  1.00 16.54           O  
ATOM    508  CG2 THR A  71      33.145   1.455 -24.042  1.00 17.74           C  
ATOM    509  N   MET A  72      37.002   0.756 -21.347  1.00 12.55           N  
ATOM    510  CA  MET A  72      37.831   0.735 -20.138  1.00 11.60           C  
ATOM    511  C   MET A  72      38.900   1.809 -20.146  1.00 11.54           C  
ATOM    512  O   MET A  72      39.101   2.468 -19.137  1.00 10.09           O  
ATOM    513  CB  MET A  72      38.444  -0.646 -19.886  1.00 11.75           C  
ATOM    514  CG  MET A  72      39.111  -0.752 -18.505  1.00 11.65           C  
ATOM    515  SD  MET A  72      37.991  -0.363 -17.176  1.00 12.36           S  
ATOM    516  CE  MET A  72      36.971  -1.815 -17.215  1.00 11.87           C  
ATOM    517  N   ILE A  73      39.541   2.061 -21.283  1.00 11.85           N  
ATOM    518  CA  ILE A  73      40.452   3.199 -21.421  1.00 11.91           C  
ATOM    519  C   ILE A  73      39.708   4.558 -21.224  1.00 12.12           C  
ATOM    520  O   ILE A  73      40.229   5.449 -20.583  1.00 11.55           O  
ATOM    521  CB  ILE A  73      41.177   3.172 -22.783  1.00 13.04           C  
ATOM    522  CG1 ILE A  73      42.264   2.058 -22.769  1.00 14.73           C  
ATOM    523  CG2 ILE A  73      41.911   4.487 -23.052  1.00 13.73           C  
ATOM    524  CD1 ILE A  73      42.809   1.758 -24.164  1.00 15.42           C  
ATOM    525  N   ALA A  74      38.486   4.685 -21.729  1.00 14.04           N  
ATOM    526  CA  ALA A  74      37.637   5.855 -21.446  1.00 14.32           C  
ATOM    527  C   ALA A  74      37.297   5.898 -19.921  1.00 14.69           C  
ATOM    528  O   ALA A  74      37.345   6.956 -19.299  1.00 14.12           O  
ATOM    529  CB  ALA A  74      36.382   5.774 -22.257  1.00 15.22           C  
ATOM    530  N   TRP A  75      37.000   4.736 -19.341  1.00 13.33           N  
ATOM    531  CA  TRP A  75      36.675   4.659 -17.899  1.00 13.17           C  
ATOM    532  C   TRP A  75      37.846   5.202 -17.073  1.00 12.65           C  
ATOM    533  O   TRP A  75      37.627   6.052 -16.214  1.00 13.78           O  
ATOM    534  CB  TRP A  75      36.264   3.225 -17.482  1.00 13.23           C  
ATOM    535  CG  TRP A  75      35.756   3.153 -16.061  1.00 13.45           C  
ATOM    536  CD1 TRP A  75      34.489   3.356 -15.638  1.00 13.32           C  
ATOM    537  CD2 TRP A  75      36.556   2.943 -14.891  1.00 13.18           C  
ATOM    538  NE1 TRP A  75      34.441   3.285 -14.257  1.00 13.17           N  
ATOM    539  CE2 TRP A  75      35.701   3.019 -13.783  1.00 12.54           C  
ATOM    540  CE3 TRP A  75      37.917   2.683 -14.686  1.00 13.63           C  
ATOM    541  CZ2 TRP A  75      36.157   2.840 -12.461  1.00 13.07           C  
ATOM    542  CZ3 TRP A  75      38.378   2.495 -13.356  1.00 13.93           C  
ATOM    543  CH2 TRP A  75      37.480   2.557 -12.274  1.00 13.38           C  
ATOM    544  N   LEU A  76      39.063   4.765 -17.367  1.00 11.72           N  
ATOM    545  CA  LEU A  76      40.261   5.247 -16.705  1.00 12.80           C  
ATOM    546  C   LEU A  76      40.584   6.724 -16.940  1.00 14.40           C  
ATOM    547  O   LEU A  76      41.031   7.419 -16.036  1.00 14.52           O  
ATOM    548  CB  LEU A  76      41.467   4.371 -17.094  1.00 12.25           C  
ATOM    549  CG  LEU A  76      41.456   2.861 -16.667  1.00 11.83           C  
ATOM    550  CD1 LEU A  76      42.431   2.021 -17.456  1.00 11.52           C  
ATOM    551  CD2 LEU A  76      41.754   2.703 -15.201  1.00 12.40           C  
ATOM    552  N   ASP A  77      40.394   7.201 -18.165  1.00 16.45           N  
ATOM    553  CA  ASP A  77      40.592   8.625 -18.460  1.00 19.00           C  
ATOM    554  C   ASP A  77      39.703   9.576 -17.634  1.00 17.83           C  
ATOM    555  O   ASP A  77      40.163  10.638 -17.189  1.00 16.95           O  
ATOM    556  CB  ASP A  77      40.345   8.889 -19.944  1.00 21.65           C  
ATOM    557  CG  ASP A  77      41.102  10.068 -20.428  1.00 26.95           C  
ATOM    558  OD1 ASP A  77      42.336   9.907 -20.577  1.00 30.53           O  
ATOM    559  OD2 ASP A  77      40.482  11.145 -20.621  1.00 28.21           O  
ATOM    560  N   GLU A  78      38.450   9.167 -17.447  1.00 17.26           N  
ATOM    561  CA  GLU A  78      37.485   9.855 -16.625  1.00 18.27           C  
ATOM    562  C   GLU A  78      37.907   9.743 -15.150  1.00 17.08           C  
ATOM    563  O   GLU A  78      37.908  10.744 -14.432  1.00 15.51           O  
ATOM    564  CB  GLU A  78      36.118   9.223 -16.833  1.00 21.46           C  
ATOM    565  CG  GLU A  78      35.488   9.414 -18.221  1.00 23.89           C  
ATOM    566  CD  GLU A  78      34.190   8.635 -18.407  1.00 28.12           C  
ATOM    567  OE1 GLU A  78      34.085   7.452 -18.020  1.00 30.11           O  
ATOM    568  OE2 GLU A  78      33.233   9.179 -18.992  1.00 33.76           O  
ATOM    569  N   LEU A  79      38.291   8.525 -14.719  1.00 16.59           N  
ATOM    570  CA  LEU A  79      38.739   8.296 -13.309  1.00 15.57           C  
ATOM    571  C   LEU A  79      39.772   9.309 -12.832  1.00 14.37           C  
ATOM    572  O   LEU A  79      39.698   9.843 -11.727  1.00 15.13           O  
ATOM    573  CB  LEU A  79      39.361   6.873 -13.136  1.00 15.72           C  
ATOM    574  CG  LEU A  79      39.622   6.431 -11.680  1.00 14.65           C  
ATOM    575  CD1 LEU A  79      38.308   6.061 -11.009  1.00 14.32           C  
ATOM    576  CD2 LEU A  79      40.508   5.194 -11.622  1.00 16.27           C  
ATOM    577  N   LEU A  80      40.791   9.521 -13.640  1.00 15.27           N  
ATOM    578  CA  LEU A  80      41.906  10.349 -13.256  1.00 15.00           C  
ATOM    579  C   LEU A  80      41.791  11.764 -13.810  1.00 16.70           C  
ATOM    580  O   LEU A  80      42.355  12.666 -13.243  1.00 16.22           O  
ATOM    581  CB  LEU A  80      43.192   9.705 -13.729  1.00 15.11           C  
ATOM    582  CG  LEU A  80      43.491   8.293 -13.216  1.00 15.06           C  
ATOM    583  CD1 LEU A  80      44.867   7.961 -13.690  1.00 15.19           C  
ATOM    584  CD2 LEU A  80      43.474   8.114 -11.699  1.00 15.06           C  
ATOM    585  N   GLY A  81      41.082  11.949 -14.925  1.00 18.54           N  
ATOM    586  CA  GLY A  81      40.937  13.271 -15.539  1.00 20.57           C  
ATOM    587  C   GLY A  81      39.783  14.078 -15.020  1.00 20.89           C  
ATOM    588  O   GLY A  81      39.855  15.327 -14.961  1.00 22.47           O  
ATOM    589  N   GLY A  82      38.702  13.409 -14.663  1.00 21.69           N  
ATOM    590  CA  GLY A  82      37.535  14.137 -14.159  1.00 22.67           C  
ATOM    591  C   GLY A  82      36.660  14.833 -15.197  1.00 22.90           C  
ATOM    592  O   GLY A  82      36.661  14.443 -16.371  1.00 23.78           O  
ATOM    593  N   PRO A  83      35.833  15.794 -14.768  1.00 24.50           N  
ATOM    594  CA  PRO A  83      35.611  16.128 -13.380  1.00 23.99           C  
ATOM    595  C   PRO A  83      34.768  15.088 -12.677  1.00 24.64           C  
ATOM    596  O   PRO A  83      34.213  14.202 -13.316  1.00 26.36           O  
ATOM    597  CB  PRO A  83      34.847  17.463 -13.468  1.00 26.30           C  
ATOM    598  CG  PRO A  83      34.285  17.539 -14.831  1.00 26.00           C  
ATOM    599  CD  PRO A  83      34.786  16.371 -15.626  1.00 26.12           C  
ATOM    600  N   TRP A  84      34.669  15.216 -11.365  1.00 24.10           N  
ATOM    601  CA  TRP A  84      34.001  14.238 -10.526  1.00 24.55           C  
ATOM    602  C   TRP A  84      32.697  14.856 -10.004  1.00 24.48           C  
ATOM    603  O   TRP A  84      32.449  14.900  -8.796  1.00 25.42           O  
ATOM    604  CB  TRP A  84      34.955  13.813  -9.383  1.00 21.03           C  
ATOM    605  CG  TRP A  84      36.164  13.127  -9.878  1.00 19.53           C  
ATOM    606  CD1 TRP A  84      36.328  11.779 -10.040  1.00 18.49           C  
ATOM    607  CD2 TRP A  84      37.396  13.729 -10.312  1.00 19.06           C  
ATOM    608  NE1 TRP A  84      37.580  11.507 -10.556  1.00 17.79           N  
ATOM    609  CE2 TRP A  84      38.266  12.673 -10.709  1.00 18.60           C  
ATOM    610  CE3 TRP A  84      37.852  15.046 -10.409  1.00 19.88           C  
ATOM    611  CZ2 TRP A  84      39.541  12.900 -11.197  1.00 18.23           C  
ATOM    612  CZ3 TRP A  84      39.133  15.275 -10.886  1.00 18.81           C  
ATOM    613  CH2 TRP A  84      39.963  14.212 -11.275  1.00 20.04           C  
ATOM    614  N   ASP A  85      31.843  15.239 -10.945  1.00 27.22           N  
ATOM    615  CA  ASP A  85      30.591  15.986 -10.665  1.00 30.29           C  
ATOM    616  C   ASP A  85      29.352  15.068 -10.695  1.00 31.66           C  
ATOM    617  O   ASP A  85      29.470  13.848 -10.792  1.00 30.08           O  
ATOM    618  CB  ASP A  85      30.482  17.177 -11.645  1.00 31.05           C  
ATOM    619  CG  ASP A  85      30.552  16.765 -13.112  1.00 32.11           C  
ATOM    620  OD1 ASP A  85      30.494  15.548 -13.424  1.00 28.42           O  
ATOM    621  OD2 ASP A  85      30.640  17.674 -13.976  1.00 35.41           O  
ATOM    622  N   GLU A  86      28.162  15.642 -10.577  1.00 34.66           N  
ATOM    623  CA  GLU A  86      26.922  14.862 -10.564  1.00 35.04           C  
ATOM    624  C   GLU A  86      26.756  13.978 -11.816  1.00 31.81           C  
ATOM    625  O   GLU A  86      26.257  12.838 -11.733  1.00 31.94           O  
ATOM    626  CB  GLU A  86      25.710  15.802 -10.330  1.00 40.60           C  
ATOM    627  CG  GLU A  86      24.348  15.277 -10.771  1.00 41.56           C  
ATOM    628  CD  GLU A  86      23.179  16.042 -10.145  1.00 45.97           C  
ATOM    629  OE1 GLU A  86      22.965  17.219 -10.511  1.00 49.99           O  
ATOM    630  OE2 GLU A  86      22.466  15.451  -9.296  1.00 46.63           O  
ATOM    631  N   ALA A  87      27.191  14.493 -12.958  1.00 29.38           N  
ATOM    632  CA  ALA A  87      27.114  13.778 -14.235  1.00 27.65           C  
ATOM    633  C   ALA A  87      28.025  12.542 -14.272  1.00 26.59           C  
ATOM    634  O   ALA A  87      27.618  11.461 -14.733  1.00 27.54           O  
ATOM    635  CB  ALA A  87      27.489  14.712 -15.368  1.00 27.94           C  
ATOM    636  N   TYR A  88      29.252  12.724 -13.794  1.00 22.12           N  
ATOM    637  CA  TYR A  88      30.201  11.635 -13.588  1.00 20.90           C  
ATOM    638  C   TYR A  88      29.536  10.520 -12.780  1.00 19.72           C  
ATOM    639  O   TYR A  88      29.417   9.380 -13.281  1.00 20.23           O  
ATOM    640  CB  TYR A  88      31.490  12.170 -12.920  1.00 20.01           C  
ATOM    641  CG  TYR A  88      32.570  11.153 -12.608  1.00 20.59           C  
ATOM    642  CD1 TYR A  88      32.460  10.285 -11.491  1.00 21.05           C  
ATOM    643  CD2 TYR A  88      33.732  11.080 -13.360  1.00 19.92           C  
ATOM    644  CE1 TYR A  88      33.464   9.366 -11.193  1.00 19.19           C  
ATOM    645  CE2 TYR A  88      34.726  10.167 -13.053  1.00 19.85           C  
ATOM    646  CZ  TYR A  88      34.599   9.315 -11.962  1.00 19.67           C  
ATOM    647  OH  TYR A  88      35.622   8.389 -11.647  1.00 17.69           O  
ATOM    648  N   TRP A  89      29.053  10.858 -11.585  1.00 19.85           N  
ATOM    649  CA  TRP A  89      28.594   9.868 -10.638  1.00 21.64           C  
ATOM    650  C   TRP A  89      27.320   9.191 -11.127  1.00 23.38           C  
ATOM    651  O   TRP A  89      27.202   7.985 -10.962  1.00 24.13           O  
ATOM    652  CB  TRP A  89      28.525  10.404  -9.175  1.00 20.98           C  
ATOM    653  CG  TRP A  89      29.929  10.710  -8.611  1.00 21.84           C  
ATOM    654  CD1 TRP A  89      30.461  11.931  -8.338  1.00 19.95           C  
ATOM    655  CD2 TRP A  89      30.954   9.744  -8.297  1.00 19.93           C  
ATOM    656  NE1 TRP A  89      31.746  11.796  -7.850  1.00 21.92           N  
ATOM    657  CE2 TRP A  89      32.067  10.460  -7.811  1.00 20.81           C  
ATOM    658  CE3 TRP A  89      31.017   8.345  -8.357  1.00 19.99           C  
ATOM    659  CZ2 TRP A  89      33.268   9.834  -7.427  1.00 20.14           C  
ATOM    660  CZ3 TRP A  89      32.223   7.705  -7.946  1.00 19.00           C  
ATOM    661  CH2 TRP A  89      33.331   8.470  -7.510  1.00 18.24           C  
ATOM    662  N   ASP A  90      26.437   9.923 -11.810  1.00 26.52           N  
ATOM    663  CA  ASP A  90      25.313   9.337 -12.576  1.00 29.57           C  
ATOM    664  C   ASP A  90      25.771   8.333 -13.660  1.00 27.47           C  
ATOM    665  O   ASP A  90      25.136   7.277 -13.835  1.00 31.46           O  
ATOM    666  CB  ASP A  90      24.471  10.428 -13.278  1.00 31.37           C  
ATOM    667  CG  ASP A  90      23.588  11.248 -12.323  1.00 35.43           C  
ATOM    668  OD1 ASP A  90      23.413  10.859 -11.145  1.00 39.08           O  
ATOM    669  OD2 ASP A  90      23.053  12.306 -12.772  1.00 36.36           O  
ATOM    670  N   ARG A  91      26.832   8.644 -14.397  1.00 25.22           N  
ATOM    671  CA  ARG A  91      27.392   7.678 -15.386  1.00 25.91           C  
ATOM    672  C   ARG A  91      27.876   6.385 -14.634  1.00 21.02           C  
ATOM    673  O   ARG A  91      27.581   5.257 -15.059  1.00 20.82           O  
ATOM    674  CB  ARG A  91      28.511   8.326 -16.240  1.00 26.58           C  
ATOM    675  CG  ARG A  91      28.572   7.953 -17.725  1.00 29.55           C  
ATOM    676  CD  ARG A  91      28.642   6.433 -17.973  0.50 29.03           C  
ATOM    677  NE  ARG A  91      29.574   5.979 -19.013  0.50 26.92           N  
ATOM    678  CZ  ARG A  91      30.886   6.168 -18.958  0.50 28.14           C  
ATOM    679  NH1 ARG A  91      31.680   5.691 -19.900  0.50 28.80           N  
ATOM    680  NH2 ARG A  91      31.421   6.838 -17.951  0.50 28.72           N  
ATOM    681  N   ARG A  92      28.510   6.564 -13.485  1.00 19.37           N  
ATOM    682  CA  ARG A  92      28.984   5.429 -12.647  1.00 18.29           C  
ATOM    683  C   ARG A  92      27.840   4.555 -12.131  1.00 19.22           C  
ATOM    684  O   ARG A  92      27.975   3.312 -12.162  1.00 18.71           O  
ATOM    685  CB  ARG A  92      29.897   5.879 -11.514  1.00 17.96           C  
ATOM    686  CG  ARG A  92      31.119   6.709 -11.900  1.00 16.35           C  
ATOM    687  CD  ARG A  92      31.795   6.246 -13.180  1.00 17.00           C  
ATOM    688  NE  ARG A  92      33.243   6.389 -13.164  1.00 16.82           N  
ATOM    689  CZ  ARG A  92      34.034   6.500 -14.231  1.00 17.74           C  
ATOM    690  NH1 ARG A  92      35.355   6.566 -14.040  1.00 17.56           N  
ATOM    691  NH2 ARG A  92      33.543   6.563 -15.484  1.00 18.61           N  
ATOM    692  N   TYR A  93      26.714   5.146 -11.722  1.00 19.00           N  
ATOM    693  CA ATYR A  93      25.510   4.374 -11.368  0.50 21.18           C  
ATOM    694  CA BTYR A  93      25.570   4.312 -11.336  0.50 19.95           C  
ATOM    695  C   TYR A  93      25.067   3.501 -12.527  1.00 20.91           C  
ATOM    696  O   TYR A  93      24.752   2.320 -12.359  1.00 21.78           O  
ATOM    697  CB ATYR A  93      24.321   5.301 -11.001  0.50 23.86           C  
ATOM    698  CB BTYR A  93      24.402   5.131 -10.770  0.50 20.91           C  
ATOM    699  CG ATYR A  93      23.141   4.545 -10.410  0.50 24.65           C  
ATOM    700  CG BTYR A  93      24.568   5.649  -9.358  0.50 20.17           C  
ATOM    701  CD1ATYR A  93      23.062   4.340  -9.050  0.50 26.36           C  
ATOM    702  CD1BTYR A  93      24.270   4.857  -8.261  0.50 20.48           C  
ATOM    703  CD2ATYR A  93      22.125   4.025 -11.213  0.50 26.47           C  
ATOM    704  CD2BTYR A  93      24.986   6.947  -9.130  0.50 19.53           C  
ATOM    705  CE1ATYR A  93      22.013   3.635  -8.497  0.50 26.15           C  
ATOM    706  CE1BTYR A  93      24.404   5.355  -6.968  0.50 20.58           C  
ATOM    707  CE2ATYR A  93      21.071   3.303 -10.664  0.50 26.57           C  
ATOM    708  CE2BTYR A  93      25.112   7.451  -7.861  0.50 20.12           C  
ATOM    709  CZ ATYR A  93      21.035   3.114  -9.296  0.50 26.47           C  
ATOM    710  CZ BTYR A  93      24.823   6.650  -6.781  0.50 19.93           C  
ATOM    711  OH ATYR A  93      20.036   2.414  -8.660  0.50 27.35           O  
ATOM    712  OH BTYR A  93      24.956   7.159  -5.522  0.50 20.31           O  
ATOM    713  N   ARG A  94      24.972   4.122 -13.717  1.00 21.42           N  
ATOM    714  CA  ARG A  94      24.516   3.398 -14.918  1.00 22.21           C  
ATOM    715  C   ARG A  94      25.442   2.210 -15.216  1.00 18.74           C  
ATOM    716  O   ARG A  94      24.960   1.147 -15.505  1.00 20.43           O  
ATOM    717  CB  ARG A  94      24.369   4.345 -16.141  1.00 24.82           C  
ATOM    718  CG  ARG A  94      23.205   5.320 -15.948  1.00 31.85           C  
ATOM    719  CD  ARG A  94      22.821   6.104 -17.206  1.00 37.85           C  
ATOM    720  NE  ARG A  94      23.785   7.151 -17.565  1.00 42.68           N  
ATOM    721  CZ  ARG A  94      23.819   8.393 -17.066  1.00 44.17           C  
ATOM    722  NH1 ARG A  94      22.950   8.806 -16.138  1.00 45.64           N  
ATOM    723  NH2 ARG A  94      24.750   9.235 -17.498  1.00 42.17           N  
ATOM    724  N   ILE A  95      26.748   2.408 -15.103  1.00 17.00           N  
ATOM    725  CA  ILE A  95      27.749   1.361 -15.329  1.00 16.85           C  
ATOM    726  C   ILE A  95      27.593   0.219 -14.348  1.00 16.40           C  
ATOM    727  O   ILE A  95      27.581  -0.936 -14.737  1.00 17.48           O  
ATOM    728  CB  ILE A  95      29.174   1.949 -15.253  1.00 17.15           C  
ATOM    729  CG1 ILE A  95      29.413   2.854 -16.490  1.00 16.52           C  
ATOM    730  CG2 ILE A  95      30.221   0.827 -15.120  1.00 17.08           C  
ATOM    731  CD1 ILE A  95      30.569   3.832 -16.356  1.00 16.78           C  
ATOM    732  N   GLY A  96      27.460   0.556 -13.073  1.00 17.45           N  
ATOM    733  CA  GLY A  96      27.051  -0.395 -12.056  1.00 19.06           C  
ATOM    734  C   GLY A  96      25.843  -1.217 -12.494  1.00 19.93           C  
ATOM    735  O   GLY A  96      25.882  -2.451 -12.434  1.00 19.93           O  
ATOM    736  N   ARG A  97      24.769  -0.543 -12.933  1.00 21.30           N  
ATOM    737  CA  ARG A  97      23.540  -1.258 -13.365  1.00 24.19           C  
ATOM    738  C   ARG A  97      23.705  -2.250 -14.507  1.00 22.16           C  
ATOM    739  O   ARG A  97      23.063  -3.296 -14.474  1.00 23.09           O  
ATOM    740  CB  ARG A  97      22.395  -0.309 -13.731  1.00 27.11           C  
ATOM    741  CG  ARG A  97      21.861   0.532 -12.604  1.00 32.34           C  
ATOM    742  CD  ARG A  97      21.306  -0.277 -11.465  1.00 37.52           C  
ATOM    743  NE  ARG A  97      20.246  -1.220 -11.830  1.00 44.71           N  
ATOM    744  CZ  ARG A  97      19.498  -1.868 -10.934  1.00 43.66           C  
ATOM    745  NH1 ARG A  97      19.660  -1.648  -9.632  1.00 42.32           N  
ATOM    746  NH2 ARG A  97      18.569  -2.725 -11.347  1.00 46.23           N  
ATOM    747  N   VAL A  98      24.543  -1.920 -15.495  1.00 23.74           N  
ATOM    748  CA  VAL A  98      24.946  -2.868 -16.574  1.00 22.73           C  
ATOM    749  C   VAL A  98      25.298  -4.228 -15.998  1.00 22.16           C  
ATOM    750  O   VAL A  98      24.779  -5.261 -16.464  1.00 22.37           O  
ATOM    751  CB  VAL A  98      26.113  -2.316 -17.468  1.00 25.37           C  
ATOM    752  CG1 VAL A  98      26.702  -3.373 -18.405  1.00 25.71           C  
ATOM    753  CG2 VAL A  98      25.673  -1.095 -18.287  1.00 26.80           C  
ATOM    754  N   HIS A  99      26.114  -4.232 -14.948  1.00 20.96           N  
ATOM    755  CA  HIS A  99      26.649  -5.475 -14.379  1.00 19.46           C  
ATOM    756  C   HIS A  99      25.596  -6.266 -13.598  1.00 19.49           C  
ATOM    757  O   HIS A  99      25.560  -7.476 -13.647  1.00 22.48           O  
ATOM    758  CB  HIS A  99      27.874  -5.160 -13.539  1.00 18.30           C  
ATOM    759  CG  HIS A  99      28.970  -4.542 -14.338  1.00 16.96           C  
ATOM    760  ND1 HIS A  99      29.056  -3.185 -14.543  1.00 16.09           N  
ATOM    761  CD2 HIS A  99      29.979  -5.105 -15.041  1.00 15.54           C  
ATOM    762  CE1 HIS A  99      30.086  -2.933 -15.327  1.00 16.83           C  
ATOM    763  NE2 HIS A  99      30.650  -4.084 -15.667  1.00 17.75           N  
ATOM    764  N   VAL A 100      24.738  -5.566 -12.879  1.00 21.59           N  
ATOM    765  CA  VAL A 100      23.568  -6.158 -12.245  1.00 21.50           C  
ATOM    766  C   VAL A 100      22.712  -6.801 -13.340  1.00 21.78           C  
ATOM    767  O   VAL A 100      22.366  -7.966 -13.228  1.00 24.89           O  
ATOM    768  CB  VAL A 100      22.730  -5.114 -11.445  1.00 21.17           C  
ATOM    769  CG1 VAL A 100      21.543  -5.779 -10.736  1.00 21.15           C  
ATOM    770  CG2 VAL A 100      23.588  -4.442 -10.377  1.00 22.57           C  
ATOM    771  N   ARG A 101      22.446  -6.065 -14.413  1.00 24.17           N  
ATOM    772  CA  ARG A 101      21.579  -6.513 -15.556  1.00 26.18           C  
ATOM    773  C   ARG A 101      22.064  -7.812 -16.235  1.00 26.02           C  
ATOM    774  O   ARG A 101      21.266  -8.720 -16.525  1.00 26.73           O  
ATOM    775  CB  ARG A 101      21.406  -5.348 -16.560  1.00 27.14           C  
ATOM    776  CG  ARG A 101      20.348  -5.538 -17.631  1.00 30.76           C  
ATOM    777  CD  ARG A 101      19.944  -4.226 -18.284  0.50 31.86           C  
ATOM    778  NE  ARG A 101      19.096  -3.388 -17.422  0.50 32.83           N  
ATOM    779  CZ  ARG A 101      19.507  -2.264 -16.837  0.50 32.03           C  
ATOM    780  NH1 ARG A 101      20.756  -1.842 -17.011  0.50 32.11           N  
ATOM    781  NH2 ARG A 101      18.677  -1.560 -16.082  0.50 29.80           N  
ATOM    782  N   ILE A 102      23.381  -7.952 -16.391  1.00 25.03           N  
ATOM    783  CA  ILE A 102      23.958  -9.153 -17.018  1.00 25.06           C  
ATOM    784  C   ILE A 102      24.220 -10.282 -16.014  1.00 24.59           C  
ATOM    785  O   ILE A 102      24.768 -11.311 -16.374  1.00 27.47           O  
ATOM    786  CB  ILE A 102      25.248  -8.816 -17.827  1.00 26.05           C  
ATOM    787  CG1 ILE A 102      26.404  -8.347 -16.929  1.00 26.27           C  
ATOM    788  CG2 ILE A 102      24.942  -7.806 -18.910  1.00 27.41           C  
ATOM    789  CD1 ILE A 102      27.754  -8.361 -17.612  1.00 26.91           C  
ATOM    790  N   GLY A 103      23.913 -10.057 -14.737  1.00 22.69           N  
ATOM    791  CA  GLY A 103      23.948 -11.101 -13.728  1.00 22.81           C  
ATOM    792  C   GLY A 103      25.324 -11.449 -13.203  1.00 23.52           C  
ATOM    793  O   GLY A 103      25.554 -12.552 -12.754  1.00 22.87           O  
ATOM    794  N   LEU A 104      26.252 -10.498 -13.268  1.00 22.79           N  
ATOM    795  CA  LEU A 104      27.579 -10.720 -12.759  1.00 21.03           C  
ATOM    796  C   LEU A 104      27.512 -10.713 -11.234  1.00 19.73           C  
ATOM    797  O   LEU A 104      26.901  -9.816 -10.640  1.00 19.27           O  
ATOM    798  CB  LEU A 104      28.517  -9.643 -13.291  1.00 21.92           C  
ATOM    799  CG  LEU A 104      29.987  -9.979 -13.115  1.00 23.32           C  
ATOM    800  CD1 LEU A 104      30.448 -10.975 -14.168  1.00 24.96           C  
ATOM    801  CD2 LEU A 104      30.804  -8.711 -13.194  1.00 24.48           C  
ATOM    802  N   PRO A 105      28.051 -11.764 -10.589  1.00 19.94           N  
ATOM    803  CA  PRO A 105      28.168 -11.818  -9.135  1.00 19.09           C  
ATOM    804  C   PRO A 105      28.848 -10.575  -8.612  1.00 19.87           C  
ATOM    805  O   PRO A 105      29.876 -10.189  -9.152  1.00 17.30           O  
ATOM    806  CB  PRO A 105      29.049 -13.026  -8.904  1.00 19.03           C  
ATOM    807  CG  PRO A 105      28.824 -13.892 -10.100  1.00 20.19           C  
ATOM    808  CD  PRO A 105      28.490 -13.018 -11.232  1.00 19.07           C  
ATOM    809  N   GLN A 106      28.278  -9.927  -7.601  1.00 20.22           N  
ATOM    810  CA  GLN A 106      28.825  -8.634  -7.154  1.00 19.61           C  
ATOM    811  C   GLN A 106      30.286  -8.710  -6.699  1.00 19.58           C  
ATOM    812  O   GLN A 106      31.007  -7.737  -6.845  1.00 18.57           O  
ATOM    813  CB  GLN A 106      27.943  -7.997  -6.082  1.00 21.03           C  
ATOM    814  CG  GLN A 106      28.026  -8.611  -4.704  1.00 22.18           C  
ATOM    815  CD  GLN A 106      27.254  -7.785  -3.689  1.00 23.31           C  
ATOM    816  OE1 GLN A 106      26.126  -7.343  -3.950  1.00 23.45           O  
ATOM    817  NE2 GLN A 106      27.854  -7.585  -2.520  1.00 23.38           N  
ATOM    818  N   HIS A 107      30.717  -9.849  -6.158  1.00 18.03           N  
ATOM    819  CA  HIS A 107      32.070  -9.955  -5.597  1.00 18.17           C  
ATOM    820  C   HIS A 107      33.165  -9.810  -6.632  1.00 16.75           C  
ATOM    821  O   HIS A 107      34.284  -9.440  -6.285  1.00 14.17           O  
ATOM    822  CB  HIS A 107      32.298 -11.229  -4.706  1.00 20.05           C  
ATOM    823  CG  HIS A 107      32.094 -12.544  -5.389  1.00 21.20           C  
ATOM    824  ND1 HIS A 107      30.842 -13.088  -5.595  1.00 23.90           N  
ATOM    825  CD2 HIS A 107      32.982 -13.476  -5.826  1.00 22.91           C  
ATOM    826  CE1 HIS A 107      30.964 -14.259  -6.201  1.00 22.98           C  
ATOM    827  NE2 HIS A 107      32.249 -14.524  -6.347  1.00 21.90           N  
ATOM    828  N   TYR A 108      32.844 -10.077  -7.905  1.00 14.67           N  
ATOM    829  CA  TYR A 108      33.802  -9.877  -8.945  1.00 15.66           C  
ATOM    830  C   TYR A 108      34.179  -8.436  -9.132  1.00 13.96           C  
ATOM    831  O   TYR A 108      35.250  -8.189  -9.651  1.00 14.49           O  
ATOM    832  CB  TYR A 108      33.327 -10.448 -10.295  1.00 16.36           C  
ATOM    833  CG  TYR A 108      33.160 -11.960 -10.326  1.00 19.57           C  
ATOM    834  CD1 TYR A 108      33.922 -12.783  -9.523  1.00 22.22           C  
ATOM    835  CD2 TYR A 108      32.246 -12.567 -11.200  1.00 19.87           C  
ATOM    836  CE1 TYR A 108      33.767 -14.169  -9.574  1.00 24.16           C  
ATOM    837  CE2 TYR A 108      32.103 -13.939 -11.264  1.00 20.04           C  
ATOM    838  CZ  TYR A 108      32.853 -14.731 -10.442  1.00 22.45           C  
ATOM    839  OH  TYR A 108      32.748 -16.088 -10.449  1.00 22.22           O  
ATOM    840  N   MET A 109      33.303  -7.504  -8.776  1.00 14.60           N  
ATOM    841  CA  MET A 109      33.624  -6.083  -8.896  1.00 14.93           C  
ATOM    842  C   MET A 109      34.808  -5.709  -8.022  1.00 13.99           C  
ATOM    843  O   MET A 109      35.626  -4.857  -8.409  1.00 12.93           O  
ATOM    844  CB  MET A 109      32.421  -5.194  -8.589  1.00 17.08           C  
ATOM    845  CG  MET A 109      31.165  -5.462  -9.466  1.00 17.86           C  
ATOM    846  SD  MET A 109      31.456  -5.498 -11.250  1.00 20.04           S  
ATOM    847  CE  MET A 109      31.782  -3.780 -11.453  1.00 20.01           C  
ATOM    848  N   PHE A 110      34.918  -6.351  -6.850  1.00 13.14           N  
ATOM    849  CA  PHE A 110      36.069  -6.148  -5.960  1.00 12.34           C  
ATOM    850  C   PHE A 110      37.331  -6.742  -6.489  1.00 11.88           C  
ATOM    851  O   PHE A 110      38.374  -6.082  -6.436  1.00 10.83           O  
ATOM    852  CB  PHE A 110      35.795  -6.715  -4.566  1.00 12.78           C  
ATOM    853  CG  PHE A 110      34.699  -6.002  -3.837  1.00 12.42           C  
ATOM    854  CD1 PHE A 110      34.962  -4.865  -3.105  1.00 12.26           C  
ATOM    855  CD2 PHE A 110      33.402  -6.477  -3.885  1.00 13.14           C  
ATOM    856  CE1 PHE A 110      33.948  -4.221  -2.426  1.00 12.33           C  
ATOM    857  CE2 PHE A 110      32.396  -5.832  -3.231  1.00 12.55           C  
ATOM    858  CZ  PHE A 110      32.672  -4.707  -2.491  1.00 12.39           C  
ATOM    859  N   GLY A 111      37.271  -7.974  -7.009  1.00 11.84           N  
ATOM    860  CA  GLY A 111      38.446  -8.568  -7.698  1.00 12.62           C  
ATOM    861  C   GLY A 111      38.988  -7.704  -8.855  1.00 12.66           C  
ATOM    862  O   GLY A 111      40.211  -7.378  -8.942  1.00 11.85           O  
ATOM    863  N   ALA A 112      38.068  -7.284  -9.726  1.00 13.27           N  
ATOM    864  CA  ALA A 112      38.410  -6.474 -10.901  1.00 12.81           C  
ATOM    865  C   ALA A 112      39.004  -5.104 -10.488  1.00 13.43           C  
ATOM    866  O   ALA A 112      40.047  -4.682 -11.006  1.00 13.48           O  
ATOM    867  CB  ALA A 112      37.143  -6.287 -11.753  1.00 13.54           C  
ATOM    868  N   MET A 113      38.371  -4.439  -9.515  1.00 13.59           N  
ATOM    869  CA  MET A 113      38.874  -3.144  -9.012  1.00 13.01           C  
ATOM    870  C   MET A 113      40.257  -3.267  -8.387  1.00 12.51           C  
ATOM    871  O   MET A 113      41.094  -2.393  -8.600  1.00 11.66           O  
ATOM    872  CB  MET A 113      37.895  -2.474  -8.030  1.00 14.25           C  
ATOM    873  CG  MET A 113      38.125  -0.976  -7.854  1.00 14.53           C  
ATOM    874  SD  MET A 113      37.756  -0.004  -9.323  1.00 16.74           S  
ATOM    875  CE  MET A 113      35.985  -0.005  -9.234  1.00 15.13           C  
ATOM    876  N   ASN A 114      40.535  -4.368  -7.689  1.00 11.84           N  
ATOM    877  CA  ASN A 114      41.872  -4.599  -7.179  1.00 12.16           C  
ATOM    878  C   ASN A 114      42.947  -4.645  -8.257  1.00 10.61           C  
ATOM    879  O   ASN A 114      44.066  -4.147  -8.033  1.00 10.77           O  
ATOM    880  CB  ASN A 114      41.961  -5.874  -6.327  1.00 12.04           C  
ATOM    881  CG  ASN A 114      43.289  -6.002  -5.661  1.00 13.01           C  
ATOM    882  OD1 ASN A 114      44.141  -6.761  -6.117  1.00 13.14           O  
ATOM    883  ND2 ASN A 114      43.514  -5.195  -4.576  1.00 11.84           N  
ATOM    884  N   VAL A 115      42.621  -5.196  -9.427  1.00 10.57           N  
ATOM    885  CA  VAL A 115      43.597  -5.206 -10.551  1.00  9.84           C  
ATOM    886  C   VAL A 115      44.001  -3.761 -10.910  1.00 10.34           C  
ATOM    887  O   VAL A 115      45.203  -3.419 -10.945  1.00  9.84           O  
ATOM    888  CB  VAL A 115      43.088  -5.993 -11.776  1.00 10.00           C  
ATOM    889  CG1 VAL A 115      44.112  -5.922 -12.889  1.00 10.21           C  
ATOM    890  CG2 VAL A 115      42.844  -7.451 -11.429  1.00  9.94           C  
ATOM    891  N   HIS A 116      43.009  -2.902 -11.108  1.00  9.92           N  
ATOM    892  CA  HIS A 116      43.322  -1.503 -11.389  1.00 10.74           C  
ATOM    893  C   HIS A 116      44.022  -0.805 -10.250  1.00 10.34           C  
ATOM    894  O   HIS A 116      44.931  -0.037 -10.496  1.00 10.66           O  
ATOM    895  CB  HIS A 116      42.096  -0.742 -11.663  1.00 10.98           C  
ATOM    896  CG  HIS A 116      41.540  -0.953 -13.028  1.00 11.07           C  
ATOM    897  ND1 HIS A 116      42.327  -1.279 -14.125  1.00 11.67           N  
ATOM    898  CD2 HIS A 116      40.284  -0.773 -13.490  1.00 10.83           C  
ATOM    899  CE1 HIS A 116      41.557  -1.330 -15.198  1.00 11.81           C  
ATOM    900  NE2 HIS A 116      40.315  -1.013 -14.851  1.00 11.53           N  
ATOM    901  N   ARG A 117      43.589  -1.075  -9.017  1.00 11.19           N  
ATOM    902  CA  ARG A 117      44.174  -0.422  -7.839  1.00 11.71           C  
ATOM    903  C   ARG A 117      45.650  -0.734  -7.771  1.00 11.45           C  
ATOM    904  O   ARG A 117      46.481   0.173  -7.572  1.00 12.43           O  
ATOM    905  CB  ARG A 117      43.447  -0.878  -6.552  1.00 11.73           C  
ATOM    906  CG  ARG A 117      44.042  -0.261  -5.290  1.00 10.99           C  
ATOM    907  CD  ARG A 117      43.545  -0.876  -4.017  1.00 11.06           C  
ATOM    908  NE  ARG A 117      42.080  -0.970  -3.922  1.00 11.12           N  
ATOM    909  CZ  ARG A 117      41.275   0.018  -3.581  1.00 10.29           C  
ATOM    910  NH1 ARG A 117      41.738   1.268  -3.385  1.00 11.34           N  
ATOM    911  NH2 ARG A 117      39.968  -0.206  -3.547  1.00 10.64           N  
ATOM    912  N   THR A 118      45.997  -1.997  -8.010  1.00 12.52           N  
ATOM    913  CA  THR A 118      47.395  -2.453  -7.990  1.00 13.13           C  
ATOM    914  C   THR A 118      48.233  -1.763  -9.089  1.00 13.80           C  
ATOM    915  O   THR A 118      49.288  -1.193  -8.820  1.00 13.39           O  
ATOM    916  CB  THR A 118      47.491  -4.007  -8.133  1.00 14.24           C  
ATOM    917  OG1 THR A 118      46.720  -4.668  -7.106  1.00 15.00           O  
ATOM    918  CG2 THR A 118      48.947  -4.472  -8.076  1.00 14.79           C  
ATOM    919  N   GLY A 119      47.748  -1.787 -10.334  1.00 14.29           N  
ATOM    920  CA  GLY A 119      48.466  -1.142 -11.436  1.00 14.25           C  
ATOM    921  C   GLY A 119      48.578   0.376 -11.308  1.00 13.67           C  
ATOM    922  O   GLY A 119      49.626   0.913 -11.624  1.00 13.86           O  
ATOM    923  N   LEU A 120      47.517   1.037 -10.838  1.00 14.03           N  
ATOM    924  CA  LEU A 120      47.515   2.502 -10.652  1.00 15.32           C  
ATOM    925  C   LEU A 120      48.394   2.923  -9.479  1.00 16.36           C  
ATOM    926  O   LEU A 120      49.098   3.958  -9.552  1.00 16.97           O  
ATOM    927  CB  LEU A 120      46.089   3.022 -10.482  1.00 15.37           C  
ATOM    928  CG  LEU A 120      45.272   2.945 -11.770  1.00 15.45           C  
ATOM    929  CD1 LEU A 120      43.811   3.057 -11.437  1.00 15.90           C  
ATOM    930  CD2 LEU A 120      45.715   4.031 -12.773  1.00 16.55           C  
ATOM    931  N   ALA A 121      48.438   2.101  -8.440  1.00 15.66           N  
ATOM    932  CA  ALA A 121      49.326   2.405  -7.295  1.00 16.73           C  
ATOM    933  C   ALA A 121      50.820   2.288  -7.683  1.00 17.12           C  
ATOM    934  O   ALA A 121      51.688   3.037  -7.181  1.00 16.08           O  
ATOM    935  CB  ALA A 121      48.988   1.517  -6.106  1.00 16.44           C  
ATOM    936  N   ARG A 122      51.138   1.352  -8.578  1.00 17.55           N  
ATOM    937  CA  ARG A 122      52.486   1.256  -9.107  1.00 18.75           C  
ATOM    938  C   ARG A 122      52.856   2.468  -9.964  1.00 17.59           C  
ATOM    939  O   ARG A 122      53.944   2.962  -9.849  1.00 18.47           O  
ATOM    940  CB  ARG A 122      52.652  -0.019  -9.906  1.00 21.37           C  
ATOM    941  CG  ARG A 122      54.033  -0.299 -10.472  1.00 24.32           C  
ATOM    942  CD  ARG A 122      53.955  -1.433 -11.496  1.00 29.56           C  
ATOM    943  NE  ARG A 122      52.695  -1.318 -12.274  1.00 31.03           N  
ATOM    944  CZ  ARG A 122      52.533  -0.708 -13.453  1.00 33.14           C  
ATOM    945  NH1 ARG A 122      53.564  -0.158 -14.142  1.00 33.26           N  
ATOM    946  NH2 ARG A 122      51.308  -0.665 -13.970  1.00 32.09           N  
ATOM    947  N   LEU A 123      51.949   2.901 -10.826  1.00 16.93           N  
ATOM    948  CA  LEU A 123      52.123   4.074 -11.684  1.00 17.17           C  
ATOM    949  C   LEU A 123      52.293   5.350 -10.864  1.00 16.67           C  
ATOM    950  O   LEU A 123      53.202   6.144 -11.167  1.00 15.65           O  
ATOM    951  CB  LEU A 123      50.961   4.175 -12.679  1.00 17.74           C  
ATOM    952  CG  LEU A 123      50.980   3.156 -13.840  1.00 19.57           C  
ATOM    953  CD1 LEU A 123      49.684   3.241 -14.618  1.00 20.13           C  
ATOM    954  CD2 LEU A 123      52.136   3.417 -14.794  1.00 21.32           C  
ATOM    955  N   ALA A 124      51.515   5.506  -9.785  1.00 16.51           N  
ATOM    956  CA  ALA A 124      51.664   6.685  -8.883  1.00 17.02           C  
ATOM    957  C   ALA A 124      53.015   6.678  -8.201  1.00 18.35           C  
ATOM    958  O   ALA A 124      53.667   7.722  -8.126  1.00 17.28           O  
ATOM    959  CB  ALA A 124      50.572   6.734  -7.844  1.00 17.60           C  
ATOM    960  N   TYR A 125      53.459   5.507  -7.738  1.00 18.41           N  
ATOM    961  CA  TYR A 125      54.774   5.407  -7.143  1.00 19.23           C  
ATOM    962  C   TYR A 125      55.880   5.739  -8.169  1.00 19.13           C  
ATOM    963  O   TYR A 125      56.800   6.492  -7.874  1.00 19.06           O  
ATOM    964  CB  TYR A 125      55.049   4.039  -6.468  1.00 18.37           C  
ATOM    965  CG  TYR A 125      56.491   3.973  -5.929  1.00 18.38           C  
ATOM    966  CD1 TYR A 125      57.562   3.655  -6.766  1.00 17.75           C  
ATOM    967  CD2 TYR A 125      56.773   4.325  -4.618  1.00 17.61           C  
ATOM    968  CE1 TYR A 125      58.875   3.650  -6.289  1.00 18.69           C  
ATOM    969  CE2 TYR A 125      58.076   4.327  -4.125  1.00 18.26           C  
ATOM    970  CZ  TYR A 125      59.126   3.977  -4.949  1.00 18.89           C  
ATOM    971  OH  TYR A 125      60.429   3.975  -4.452  1.00 20.11           O  
ATOM    972  N   GLU A 126      55.817   5.132  -9.340  1.00 18.31           N  
ATOM    973  CA  GLU A 126      56.762   5.424 -10.405  1.00 19.71           C  
ATOM    974  C   GLU A 126      56.881   6.924 -10.732  1.00 19.38           C  
ATOM    975  O   GLU A 126      57.983   7.436 -10.860  1.00 20.50           O  
ATOM    976  CB  GLU A 126      56.398   4.622 -11.678  1.00 22.76           C  
ATOM    977  CG  GLU A 126      56.595   3.108 -11.506  1.00 26.45           C  
ATOM    978  CD  GLU A 126      56.149   2.260 -12.703  1.00 30.13           C  
ATOM    979  OE1 GLU A 126      55.836   2.841 -13.772  1.00 30.72           O  
ATOM    980  OE2 GLU A 126      56.158   1.015 -12.555  1.00 30.12           O  
ATOM    981  N   ARG A 127      55.760   7.615 -10.850  1.00 17.69           N  
ATOM    982  CA  ARG A 127      55.769   9.044 -11.196  1.00 18.43           C  
ATOM    983  C   ARG A 127      56.204   9.890 -10.009  1.00 18.82           C  
ATOM    984  O   ARG A 127      57.039  10.779 -10.182  1.00 18.79           O  
ATOM    985  CB  ARG A 127      54.424   9.467 -11.746  1.00 19.20           C  
ATOM    986  CG  ARG A 127      54.225  10.934 -12.029  1.00 20.77           C  
ATOM    987  CD  ARG A 127      55.211  11.543 -13.037  1.00 22.83           C  
ATOM    988  NE  ARG A 127      54.917  12.968 -13.139  1.00 24.03           N  
ATOM    989  CZ  ARG A 127      55.313  13.899 -12.270  1.00 26.51           C  
ATOM    990  NH1 ARG A 127      56.084  13.577 -11.230  1.00 26.45           N  
ATOM    991  NH2 ARG A 127      54.914  15.172 -12.437  1.00 25.75           N  
ATOM    992  N   PHE A 128      55.744   9.582  -8.793  1.00 17.65           N  
ATOM    993  CA  PHE A 128      55.862  10.538  -7.697  1.00 18.20           C  
ATOM    994  C   PHE A 128      56.817  10.209  -6.570  1.00 17.15           C  
ATOM    995  O   PHE A 128      56.932  10.982  -5.646  1.00 18.82           O  
ATOM    996  CB  PHE A 128      54.456  10.816  -7.138  1.00 19.03           C  
ATOM    997  CG  PHE A 128      53.576  11.518  -8.111  1.00 19.61           C  
ATOM    998  CD1 PHE A 128      53.757  12.882  -8.366  1.00 19.29           C  
ATOM    999  CD2 PHE A 128      52.565  10.833  -8.791  1.00 19.72           C  
ATOM   1000  CE1 PHE A 128      52.958  13.542  -9.254  1.00 18.83           C  
ATOM   1001  CE2 PHE A 128      51.750  11.518  -9.691  1.00 19.15           C  
ATOM   1002  CZ  PHE A 128      51.946  12.861  -9.923  1.00 19.06           C  
ATOM   1003  N   HIS A 129      57.564   9.120  -6.666  1.00 17.85           N  
ATOM   1004  CA  HIS A 129      58.424   8.688  -5.547  1.00 19.09           C  
ATOM   1005  C   HIS A 129      59.627   9.589  -5.222  1.00 21.30           C  
ATOM   1006  O   HIS A 129      60.189   9.472  -4.128  1.00 21.08           O  
ATOM   1007  CB  HIS A 129      58.920   7.263  -5.753  1.00 18.04           C  
ATOM   1008  CG  HIS A 129      59.968   7.107  -6.820  1.00 16.84           C  
ATOM   1009  ND1 HIS A 129      59.656   6.914  -8.151  1.00 17.31           N  
ATOM   1010  CD2 HIS A 129      61.321   7.041  -6.739  1.00 17.39           C  
ATOM   1011  CE1 HIS A 129      60.775   6.752  -8.847  1.00 17.15           C  
ATOM   1012  NE2 HIS A 129      61.802   6.843  -8.015  1.00 15.98           N  
ATOM   1013  N   GLY A 130      60.025  10.463  -6.151  1.00 24.50           N  
ATOM   1014  CA  GLY A 130      61.036  11.491  -5.858  1.00 24.48           C  
ATOM   1015  C   GLY A 130      60.482  12.704  -5.100  1.00 26.08           C  
ATOM   1016  O   GLY A 130      61.237  13.626  -4.776  1.00 27.33           O  
ATOM   1017  N   ASP A 131      59.168  12.728  -4.820  1.00 24.85           N  
ATOM   1018  CA  ASP A 131      58.513  13.822  -4.069  1.00 23.12           C  
ATOM   1019  C   ASP A 131      57.523  13.195  -3.045  1.00 22.60           C  
ATOM   1020  O   ASP A 131      56.321  13.107  -3.301  1.00 23.97           O  
ATOM   1021  CB  ASP A 131      57.822  14.782  -5.050  1.00 23.65           C  
ATOM   1022  CG  ASP A 131      57.344  16.100  -4.399  1.00 26.93           C  
ATOM   1023  OD1 ASP A 131      57.394  16.225  -3.155  1.00 25.16           O  
ATOM   1024  OD2 ASP A 131      56.873  17.006  -5.149  1.00 27.37           O  
ATOM   1025  N   PRO A 132      58.024  12.766  -1.875  1.00 24.27           N  
ATOM   1026  CA  PRO A 132      57.137  11.964  -1.008  1.00 23.38           C  
ATOM   1027  C   PRO A 132      55.829  12.618  -0.572  1.00 23.44           C  
ATOM   1028  O   PRO A 132      54.805  11.911  -0.501  1.00 26.87           O  
ATOM   1029  CB  PRO A 132      58.035  11.596   0.163  1.00 23.68           C  
ATOM   1030  CG  PRO A 132      59.421  11.555  -0.460  1.00 23.17           C  
ATOM   1031  CD  PRO A 132      59.429  12.715  -1.407  1.00 23.50           C  
ATOM   1032  N   PRO A 133      55.824  13.951  -0.333  1.00 24.80           N  
ATOM   1033  CA  PRO A 133      54.543  14.620  -0.018  1.00 24.04           C  
ATOM   1034  C   PRO A 133      53.501  14.647  -1.156  1.00 23.18           C  
ATOM   1035  O   PRO A 133      52.272  14.623  -0.885  1.00 20.81           O  
ATOM   1036  CB  PRO A 133      54.979  16.054   0.367  1.00 24.10           C  
ATOM   1037  CG  PRO A 133      56.359  15.903   0.856  1.00 25.24           C  
ATOM   1038  CD  PRO A 133      56.980  14.814   0.024  1.00 24.86           C  
ATOM   1039  N   GLU A 134      53.954  14.749  -2.405  1.00 20.83           N  
ATOM   1040  CA  GLU A 134      53.040  14.628  -3.547  1.00 22.57           C  
ATOM   1041  C   GLU A 134      52.549  13.200  -3.735  1.00 18.90           C  
ATOM   1042  O   GLU A 134      51.387  12.999  -3.997  1.00 20.45           O  
ATOM   1043  CB  GLU A 134      53.682  15.145  -4.848  1.00 24.44           C  
ATOM   1044  CG  GLU A 134      52.763  15.296  -6.061  1.00 28.09           C  
ATOM   1045  CD  GLU A 134      51.569  16.241  -5.882  1.00 35.35           C  
ATOM   1046  OE1 GLU A 134      51.359  16.862  -4.795  1.00 35.97           O  
ATOM   1047  OE2 GLU A 134      50.813  16.377  -6.876  1.00 42.91           O  
ATOM   1048  N   LEU A 135      53.437  12.225  -3.636  1.00 18.86           N  
ATOM   1049  CA  LEU A 135      53.039  10.818  -3.701  1.00 17.70           C  
ATOM   1050  C   LEU A 135      51.962  10.549  -2.670  1.00 17.77           C  
ATOM   1051  O   LEU A 135      51.011   9.862  -2.982  1.00 18.09           O  
ATOM   1052  CB  LEU A 135      54.220   9.889  -3.441  1.00 17.40           C  
ATOM   1053  CG  LEU A 135      53.858   8.411  -3.264  1.00 17.20           C  
ATOM   1054  CD1 LEU A 135      53.096   7.825  -4.464  1.00 17.68           C  
ATOM   1055  CD2 LEU A 135      55.087   7.582  -2.969  1.00 18.29           C  
ATOM   1056  N   GLU A 136      52.116  11.112  -1.466  1.00 17.86           N  
ATOM   1057  CA  GLU A 136      51.144  10.970  -0.398  1.00 19.41           C  
ATOM   1058  C   GLU A 136      49.770  11.446  -0.846  1.00 18.50           C  
ATOM   1059  O   GLU A 136      48.797  10.726  -0.651  1.00 19.36           O  
ATOM   1060  CB  GLU A 136      51.587  11.702   0.892  1.00 21.13           C  
ATOM   1061  CG  GLU A 136      50.566  11.579   2.015  1.00 24.28           C  
ATOM   1062  CD  GLU A 136      51.073  12.049   3.376  1.00 27.12           C  
ATOM   1063  OE1 GLU A 136      50.872  11.308   4.349  1.00 27.05           O  
ATOM   1064  OE2 GLU A 136      51.649  13.152   3.468  1.00 28.35           O  
ATOM   1065  N   ARG A 137      49.694  12.626  -1.480  1.00 18.64           N  
ATOM   1066  CA  ARG A 137      48.422  13.217  -1.917  1.00 18.68           C  
ATOM   1067  C   ARG A 137      47.768  12.415  -3.039  1.00 17.50           C  
ATOM   1068  O   ARG A 137      46.552  12.204  -3.047  1.00 17.31           O  
ATOM   1069  CB  ARG A 137      48.622  14.679  -2.371  1.00 19.91           C  
ATOM   1070  CG  ARG A 137      49.084  15.630  -1.240  1.00 22.59           C  
ATOM   1071  CD  ARG A 137      49.057  17.099  -1.654  1.00 24.56           C  
ATOM   1072  NE  ARG A 137      50.260  17.490  -2.338  1.00 25.86           N  
ATOM   1073  CZ  ARG A 137      51.417  17.818  -1.742  1.00 31.42           C  
ATOM   1074  NH1 ARG A 137      51.553  17.849  -0.403  1.00 31.19           N  
ATOM   1075  NH2 ARG A 137      52.461  18.134  -2.504  1.00 31.47           N  
ATOM   1076  N   VAL A 138      48.597  11.978  -3.982  1.00 17.00           N  
ATOM   1077  CA  VAL A 138      48.163  11.199  -5.114  1.00 16.75           C  
ATOM   1078  C   VAL A 138      47.628   9.819  -4.668  1.00 15.85           C  
ATOM   1079  O   VAL A 138      46.533   9.397  -5.092  1.00 15.38           O  
ATOM   1080  CB  VAL A 138      49.326  11.008  -6.117  1.00 16.39           C  
ATOM   1081  CG1 VAL A 138      48.906  10.050  -7.230  1.00 16.60           C  
ATOM   1082  CG2 VAL A 138      49.732  12.331  -6.747  1.00 17.69           C  
ATOM   1083  N   ARG A 139      48.429   9.124  -3.852  1.00 15.80           N  
ATOM   1084  CA  ARG A 139      48.065   7.810  -3.281  1.00 16.82           C  
ATOM   1085  C   ARG A 139      46.784   7.892  -2.454  1.00 15.96           C  
ATOM   1086  O   ARG A 139      45.918   7.058  -2.585  1.00 16.09           O  
ATOM   1087  CB  ARG A 139      49.214   7.250  -2.436  1.00 17.74           C  
ATOM   1088  CG  ARG A 139      48.942   5.931  -1.757  1.00 19.03           C  
ATOM   1089  CD  ARG A 139      50.112   5.445  -0.886  1.00 19.67           C  
ATOM   1090  NE  ARG A 139      50.282   6.274   0.308  1.00 21.22           N  
ATOM   1091  CZ  ARG A 139      51.368   6.969   0.668  1.00 21.68           C  
ATOM   1092  NH1 ARG A 139      52.485   6.960  -0.038  1.00 22.32           N  
ATOM   1093  NH2 ARG A 139      51.325   7.720   1.768  1.00 25.94           N  
ATOM   1094  N   ASN A 140      46.662   8.908  -1.609  1.00 16.21           N  
ATOM   1095  CA  ASN A 140      45.429   9.131  -0.891  1.00 16.50           C  
ATOM   1096  C   ASN A 140      44.254   9.377  -1.816  1.00 15.43           C  
ATOM   1097  O   ASN A 140      43.217   8.785  -1.609  1.00 16.33           O  
ATOM   1098  CB  ASN A 140      45.552  10.286   0.106  1.00 17.75           C  
ATOM   1099  CG  ASN A 140      46.471   9.974   1.262  1.00 17.21           C  
ATOM   1100  OD1 ASN A 140      47.033   8.866   1.400  1.00 18.80           O  
ATOM   1101  ND2 ASN A 140      46.647  10.967   2.117  1.00 20.01           N  
ATOM   1102  N   ALA A 141      44.392  10.246  -2.823  1.00 15.49           N  
ATOM   1103  CA  ALA A 141      43.309  10.520  -3.763  1.00 14.38           C  
ATOM   1104  C   ALA A 141      42.895   9.270  -4.570  1.00 13.90           C  
ATOM   1105  O   ALA A 141      41.721   9.037  -4.795  1.00 12.79           O  
ATOM   1106  CB  ALA A 141      43.707  11.609  -4.714  1.00 15.02           C  
ATOM   1107  N   LEU A 142      43.880   8.473  -4.955  1.00 13.94           N  
ATOM   1108  CA  LEU A 142      43.640   7.235  -5.718  1.00 15.44           C  
ATOM   1109  C   LEU A 142      42.844   6.231  -4.848  1.00 14.57           C  
ATOM   1110  O   LEU A 142      41.882   5.632  -5.324  1.00 14.35           O  
ATOM   1111  CB  LEU A 142      44.979   6.628  -6.162  1.00 16.24           C  
ATOM   1112  CG  LEU A 142      44.872   5.355  -6.991  1.00 17.54           C  
ATOM   1113  CD1 LEU A 142      44.129   5.591  -8.304  1.00 17.99           C  
ATOM   1114  CD2 LEU A 142      46.257   4.780  -7.242  1.00 19.46           C  
ATOM   1115  N   GLY A 143      43.222   6.075  -3.569  1.00 12.96           N  
ATOM   1116  CA  GLY A 143      42.463   5.201  -2.670  1.00 12.73           C  
ATOM   1117  C   GLY A 143      41.034   5.629  -2.477  1.00 11.87           C  
ATOM   1118  O   GLY A 143      40.131   4.817  -2.505  1.00 12.41           O  
ATOM   1119  N   LYS A 144      40.824   6.921  -2.308  1.00 12.58           N  
ATOM   1120  CA  LYS A 144      39.499   7.526  -2.217  1.00 13.08           C  
ATOM   1121  C   LYS A 144      38.634   7.311  -3.427  1.00 12.19           C  
ATOM   1122  O   LYS A 144      37.419   6.921  -3.303  1.00 12.12           O  
ATOM   1123  CB  LYS A 144      39.621   9.052  -1.975  1.00 15.08           C  
ATOM   1124  CG  LYS A 144      40.176   9.440  -0.600  1.00 15.13           C  
ATOM   1125  CD  LYS A 144      40.256  10.953  -0.442  1.00 17.44           C  
ATOM   1126  CE  LYS A 144      41.329  11.414   0.530  1.00 17.47           C  
ATOM   1127  NZ  LYS A 144      41.019  12.831   0.887  1.00 19.54           N  
ATOM   1128  N   VAL A 145      39.184   7.589  -4.606  1.00 12.71           N  
ATOM   1129  CA  VAL A 145      38.342   7.524  -5.807  1.00 12.36           C  
ATOM   1130  C   VAL A 145      37.906   6.079  -6.080  1.00 12.04           C  
ATOM   1131  O   VAL A 145      36.745   5.848  -6.458  1.00 12.04           O  
ATOM   1132  CB  VAL A 145      38.911   8.239  -7.066  1.00 11.33           C  
ATOM   1133  CG1 VAL A 145      40.084   7.520  -7.696  1.00 11.43           C  
ATOM   1134  CG2 VAL A 145      37.818   8.450  -8.090  1.00 12.03           C  
ATOM   1135  N   LEU A 146      38.817   5.132  -5.885  1.00 11.40           N  
ATOM   1136  CA  LEU A 146      38.493   3.705  -6.094  1.00 11.36           C  
ATOM   1137  C   LEU A 146      37.517   3.206  -5.080  1.00 11.99           C  
ATOM   1138  O   LEU A 146      36.603   2.410  -5.431  1.00 12.14           O  
ATOM   1139  CB  LEU A 146      39.767   2.853  -6.073  1.00 11.61           C  
ATOM   1140  CG  LEU A 146      40.731   3.081  -7.269  1.00 11.62           C  
ATOM   1141  CD1 LEU A 146      42.008   2.354  -7.028  1.00 12.39           C  
ATOM   1142  CD2 LEU A 146      40.193   2.634  -8.611  1.00 12.10           C  
ATOM   1143  N   ASP A 147      37.663   3.676  -3.817  1.00 11.98           N  
ATOM   1144  CA  ASP A 147      36.705   3.281  -2.782  1.00 12.48           C  
ATOM   1145  C   ASP A 147      35.327   3.852  -3.024  1.00 11.76           C  
ATOM   1146  O   ASP A 147      34.331   3.166  -2.805  1.00 10.99           O  
ATOM   1147  CB  ASP A 147      37.232   3.583  -1.366  1.00 12.37           C  
ATOM   1148  CG  ASP A 147      38.289   2.587  -0.932  1.00 13.48           C  
ATOM   1149  OD1 ASP A 147      38.427   1.521  -1.608  1.00 14.45           O  
ATOM   1150  OD2 ASP A 147      39.027   2.903   0.044  1.00 14.17           O  
ATOM   1151  N   LEU A 148      35.260   5.090  -3.506  1.00 12.71           N  
ATOM   1152  CA  LEU A 148      33.964   5.704  -3.892  1.00 12.76           C  
ATOM   1153  C   LEU A 148      33.304   5.020  -5.067  1.00 13.11           C  
ATOM   1154  O   LEU A 148      32.073   4.838  -5.072  1.00 13.84           O  
ATOM   1155  CB  LEU A 148      34.118   7.209  -4.160  1.00 14.19           C  
ATOM   1156  CG  LEU A 148      34.526   8.053  -2.940  1.00 15.97           C  
ATOM   1157  CD1 LEU A 148      34.985   9.437  -3.324  1.00 17.18           C  
ATOM   1158  CD2 LEU A 148      33.398   8.179  -1.990  1.00 17.54           C  
ATOM   1159  N   GLU A 149      34.101   4.669  -6.067  1.00 13.19           N  
ATOM   1160  CA  GLU A 149      33.635   3.880  -7.206  1.00 13.90           C  
ATOM   1161  C   GLU A 149      33.015   2.577  -6.780  1.00 13.34           C  
ATOM   1162  O   GLU A 149      31.946   2.254  -7.245  1.00 13.07           O  
ATOM   1163  CB  GLU A 149      34.771   3.577  -8.173  1.00 13.95           C  
ATOM   1164  CG  GLU A 149      35.231   4.750  -9.034  1.00 15.45           C  
ATOM   1165  CD  GLU A 149      34.313   5.094 -10.195  1.00 17.06           C  
ATOM   1166  OE1 GLU A 149      34.656   6.109 -10.835  1.00 16.78           O  
ATOM   1167  OE2 GLU A 149      33.341   4.342 -10.536  1.00 16.47           O  
ATOM   1168  N   LEU A 150      33.690   1.829  -5.897  1.00 14.05           N  
ATOM   1169  CA  LEU A 150      33.133   0.588  -5.361  1.00 13.14           C  
ATOM   1170  C   LEU A 150      31.828   0.823  -4.596  1.00 13.22           C  
ATOM   1171  O   LEU A 150      30.900   0.025  -4.745  1.00 12.98           O  
ATOM   1172  CB  LEU A 150      34.132  -0.151  -4.464  1.00 13.15           C  
ATOM   1173  CG  LEU A 150      35.252  -0.889  -5.202  1.00 13.97           C  
ATOM   1174  CD1 LEU A 150      36.393  -1.287  -4.263  1.00 13.86           C  
ATOM   1175  CD2 LEU A 150      34.703  -2.056  -5.986  1.00 13.87           C  
ATOM   1176  N   ALA A 151      31.781   1.881  -3.761  1.00 13.57           N  
ATOM   1177  CA  ALA A 151      30.572   2.273  -3.051  1.00 14.87           C  
ATOM   1178  C   ALA A 151      29.364   2.493  -3.983  1.00 15.95           C  
ATOM   1179  O   ALA A 151      28.302   1.908  -3.753  1.00 16.33           O  
ATOM   1180  CB  ALA A 151      30.809   3.484  -2.162  1.00 15.05           C  
ATOM   1181  N   VAL A 152      29.561   3.250  -5.062  1.00 16.46           N  
ATOM   1182  CA  VAL A 152      28.508   3.517  -6.053  1.00 18.25           C  
ATOM   1183  C   VAL A 152      28.089   2.262  -6.833  1.00 18.88           C  
ATOM   1184  O   VAL A 152      26.869   1.968  -6.992  1.00 16.32           O  
ATOM   1185  CB  VAL A 152      28.926   4.689  -6.949  1.00 18.85           C  
ATOM   1186  CG1 VAL A 152      28.037   4.791  -8.208  1.00 22.04           C  
ATOM   1187  CG2 VAL A 152      28.848   5.987  -6.151  1.00 19.14           C  
ATOM   1188  N   MET A 153      29.088   1.480  -7.262  1.00 19.69           N  
ATOM   1189  CA  MET A 153      28.829   0.204  -7.913  1.00 21.51           C  
ATOM   1190  C   MET A 153      27.989  -0.678  -7.057  1.00 19.65           C  
ATOM   1191  O   MET A 153      26.990  -1.202  -7.528  1.00 19.08           O  
ATOM   1192  CB  MET A 153      30.107  -0.599  -8.160  1.00 25.43           C  
ATOM   1193  CG  MET A 153      30.885  -0.146  -9.312  1.00 29.10           C  
ATOM   1194  SD  MET A 153      32.415  -1.090  -9.440  1.00 34.30           S  
ATOM   1195  CE  MET A 153      32.813  -0.484 -11.073  1.00 34.37           C  
ATOM   1196  N   LEU A 154      28.398  -0.877  -5.805  1.00 19.11           N  
ATOM   1197  CA  LEU A 154      27.648  -1.753  -4.938  1.00 19.49           C  
ATOM   1198  C   LEU A 154      26.322  -1.208  -4.436  1.00 19.78           C  
ATOM   1199  O   LEU A 154      25.469  -2.001  -4.061  1.00 20.12           O  
ATOM   1200  CB  LEU A 154      28.495  -2.353  -3.803  1.00 20.53           C  
ATOM   1201  CG  LEU A 154      29.118  -3.609  -4.423  1.00 21.23           C  
ATOM   1202  CD1 LEU A 154      30.559  -3.401  -4.892  1.00 21.19           C  
ATOM   1203  CD2 LEU A 154      28.874  -4.803  -3.538  1.00 21.97           C  
ATOM   1204  N   HIS A 155      26.127   0.110  -4.451  1.00 20.06           N  
ATOM   1205  CA  HIS A 155      24.785   0.668  -4.265  1.00 20.92           C  
ATOM   1206  C   HIS A 155      23.826   0.082  -5.321  1.00 20.61           C  
ATOM   1207  O   HIS A 155      22.702  -0.258  -5.006  1.00 20.57           O  
ATOM   1208  CB  HIS A 155      24.805   2.223  -4.303  1.00 23.75           C  
ATOM   1209  CG  HIS A 155      23.484   2.860  -3.957  1.00 25.08           C  
ATOM   1210  ND1 HIS A 155      23.044   3.002  -2.664  1.00 25.05           N  
ATOM   1211  CD2 HIS A 155      22.512   3.393  -4.736  1.00 28.40           C  
ATOM   1212  CE1 HIS A 155      21.857   3.591  -2.653  1.00 25.65           C  
ATOM   1213  NE2 HIS A 155      21.507   3.837  -3.899  1.00 28.32           N  
ATOM   1214  N   THR A 156      24.303  -0.139  -6.549  1.00 20.65           N  
ATOM   1215  CA  THR A 156      23.419  -0.598  -7.633  1.00 20.46           C  
ATOM   1216  C   THR A 156      22.969  -2.037  -7.523  1.00 20.96           C  
ATOM   1217  O   THR A 156      21.933  -2.398  -8.032  1.00 20.51           O  
ATOM   1218  CB  THR A 156      24.006  -0.338  -9.041  1.00 20.72           C  
ATOM   1219  OG1 THR A 156      25.126  -1.174  -9.316  1.00 21.52           O  
ATOM   1220  CG2 THR A 156      24.423   1.105  -9.214  1.00 21.52           C  
ATOM   1221  N   TYR A 157      23.777  -2.855  -6.869  1.00 21.43           N  
ATOM   1222  CA  TYR A 157      23.457  -4.226  -6.574  1.00 24.99           C  
ATOM   1223  C   TYR A 157      22.361  -4.405  -5.502  1.00 27.44           C  
ATOM   1224  O   TYR A 157      21.889  -5.522  -5.297  1.00 27.78           O  
ATOM   1225  CB  TYR A 157      24.753  -4.978  -6.178  1.00 24.90           C  
ATOM   1226  CG  TYR A 157      25.505  -5.564  -7.370  1.00 25.79           C  
ATOM   1227  CD1 TYR A 157      25.087  -6.765  -7.953  1.00 25.70           C  
ATOM   1228  CD2 TYR A 157      26.597  -4.911  -7.931  1.00 24.64           C  
ATOM   1229  CE1 TYR A 157      25.753  -7.307  -9.025  1.00 24.80           C  
ATOM   1230  CE2 TYR A 157      27.272  -5.441  -9.019  1.00 24.94           C  
ATOM   1231  CZ  TYR A 157      26.851  -6.634  -9.566  1.00 25.74           C  
ATOM   1232  OH  TYR A 157      27.510  -7.154 -10.656  1.00 26.23           O  
ATOM   1233  N   ARG A 158      21.955  -3.338  -4.817  1.00 33.00           N  
ATOM   1234  CA  ARG A 158      20.862  -3.448  -3.825  1.00 39.47           C  
ATOM   1235  C   ARG A 158      19.522  -3.552  -4.543  1.00 38.83           C  
ATOM   1236  O   ARG A 158      18.951  -2.533  -4.960  1.00 44.63           O  
ATOM   1237  CB  ARG A 158      20.886  -2.251  -2.869  1.00 42.77           C  
ATOM   1238  CG  ARG A 158      22.184  -2.142  -2.069  1.00 48.36           C  
ATOM   1239  CD  ARG A 158      22.315  -0.884  -1.206  1.00 54.78           C  
ATOM   1240  NE  ARG A 158      21.263   0.122  -1.394  1.00 60.21           N  
ATOM   1241  CZ  ARG A 158      20.123   0.214  -0.694  1.00 62.70           C  
ATOM   1242  NH1 ARG A 158      19.811  -0.659   0.272  1.00 60.87           N  
ATOM   1243  NH2 ARG A 158      19.263   1.192  -0.984  1.00 62.59           N  
TER    1244      ARG A 158                                                      
ATOM   1245  N   THR B   7      31.632 -19.609  -2.033  1.00 51.66           N  
ATOM   1246  CA  THR B   7      33.101 -19.739  -2.268  1.00 47.74           C  
ATOM   1247  C   THR B   7      33.769 -18.324  -2.406  1.00 42.41           C  
ATOM   1248  O   THR B   7      34.748 -18.189  -3.118  1.00 35.81           O  
ATOM   1249  CB  THR B   7      33.345 -20.640  -3.532  1.00 52.07           C  
ATOM   1250  OG1 THR B   7      32.381 -21.700  -3.577  1.00 55.04           O  
ATOM   1251  CG2 THR B   7      34.718 -21.294  -3.577  1.00 51.49           C  
ATOM   1252  N   VAL B   8      33.264 -17.287  -1.712  1.00 39.29           N  
ATOM   1253  CA  VAL B   8      33.649 -15.864  -2.024  1.00 34.68           C  
ATOM   1254  C   VAL B   8      35.127 -15.509  -1.772  1.00 31.60           C  
ATOM   1255  O   VAL B   8      35.793 -14.954  -2.665  1.00 26.61           O  
ATOM   1256  CB  VAL B   8      32.717 -14.803  -1.346  1.00 34.28           C  
ATOM   1257  CG1 VAL B   8      33.293 -13.378  -1.394  1.00 33.55           C  
ATOM   1258  CG2 VAL B   8      31.365 -14.787  -2.036  1.00 36.40           C  
ATOM   1259  N   PHE B   9      35.629 -15.764  -0.564  1.00 27.63           N  
ATOM   1260  CA  PHE B   9      37.046 -15.523  -0.304  1.00 26.38           C  
ATOM   1261  C   PHE B   9      37.931 -16.409  -1.183  1.00 24.78           C  
ATOM   1262  O   PHE B   9      38.988 -15.963  -1.617  1.00 21.76           O  
ATOM   1263  CB  PHE B   9      37.424 -15.660   1.186  1.00 28.84           C  
ATOM   1264  CG  PHE B   9      37.316 -17.070   1.733  1.00 31.09           C  
ATOM   1265  CD1 PHE B   9      38.403 -17.941   1.672  1.00 34.03           C  
ATOM   1266  CD2 PHE B   9      36.122 -17.521   2.318  1.00 33.75           C  
ATOM   1267  CE1 PHE B   9      38.313 -19.235   2.189  1.00 36.83           C  
ATOM   1268  CE2 PHE B   9      36.019 -18.808   2.826  1.00 35.33           C  
ATOM   1269  CZ  PHE B   9      37.115 -19.675   2.748  1.00 36.81           C  
ATOM   1270  N   GLU B  10      37.512 -17.655  -1.427  1.00 24.77           N  
ATOM   1271  CA  GLU B  10      38.302 -18.590  -2.260  1.00 27.19           C  
ATOM   1272  C   GLU B  10      38.366 -18.091  -3.719  1.00 23.98           C  
ATOM   1273  O   GLU B  10      39.438 -18.045  -4.317  1.00 22.18           O  
ATOM   1274  CB  GLU B  10      37.696 -20.018  -2.281  1.00 30.12           C  
ATOM   1275  CG  GLU B  10      37.666 -20.759  -0.939  1.00 34.48           C  
ATOM   1276  CD  GLU B  10      36.254 -20.889  -0.346  0.60 35.57           C  
ATOM   1277  OE1 GLU B  10      35.872 -22.053  -0.063  0.60 34.95           O  
ATOM   1278  OE2 GLU B  10      35.528 -19.856  -0.177  0.60 32.31           O  
ATOM   1279  N   GLU B  11      37.210 -17.754  -4.267  1.00 21.28           N  
ATOM   1280  CA  GLU B  11      37.129 -17.171  -5.633  1.00 22.56           C  
ATOM   1281  C   GLU B  11      37.942 -15.893  -5.782  1.00 19.84           C  
ATOM   1282  O   GLU B  11      38.632 -15.739  -6.794  1.00 16.07           O  
ATOM   1283  CB  GLU B  11      35.693 -16.868  -6.039  1.00 23.13           C  
ATOM   1284  CG  GLU B  11      34.963 -18.039  -6.666  1.00 25.99           C  
ATOM   1285  CD  GLU B  11      33.745 -17.592  -7.466  1.00 26.35           C  
ATOM   1286  OE1 GLU B  11      33.748 -17.769  -8.687  1.00 30.27           O  
ATOM   1287  OE2 GLU B  11      32.814 -17.015  -6.884  1.00 24.99           O  
ATOM   1288  N   LEU B  12      37.874 -14.994  -4.785  1.00 18.34           N  
ATOM   1289  CA  LEU B  12      38.617 -13.718  -4.883  1.00 19.53           C  
ATOM   1290  C   LEU B  12      40.112 -13.829  -4.610  1.00 19.38           C  
ATOM   1291  O   LEU B  12      40.889 -13.113  -5.222  1.00 21.46           O  
ATOM   1292  CB  LEU B  12      37.990 -12.633  -4.017  1.00 20.69           C  
ATOM   1293  CG  LEU B  12      36.650 -12.071  -4.477  1.00 22.47           C  
ATOM   1294  CD1 LEU B  12      36.294 -10.832  -3.685  1.00 23.17           C  
ATOM   1295  CD2 LEU B  12      36.647 -11.699  -5.956  1.00 24.56           C  
ATOM   1296  N   LYS B  13      40.552 -14.721  -3.716  1.00 19.91           N  
ATOM   1297  CA  LYS B  13      41.986 -14.989  -3.586  1.00 19.71           C  
ATOM   1298  C   LYS B  13      42.592 -15.363  -4.944  1.00 19.54           C  
ATOM   1299  O   LYS B  13      43.675 -14.918  -5.292  1.00 18.93           O  
ATOM   1300  CB  LYS B  13      42.249 -16.117  -2.589  1.00 22.40           C  
ATOM   1301  CG  LYS B  13      42.149 -15.722  -1.103  1.00 23.77           C  
ATOM   1302  CD  LYS B  13      42.370 -16.977  -0.228  1.00 23.51           C  
ATOM   1303  CE  LYS B  13      42.876 -16.642   1.152  1.00 24.58           C  
ATOM   1304  NZ  LYS B  13      43.373 -17.848   1.908  1.00 25.21           N  
ATOM   1305  N   ARG B  14      41.893 -16.188  -5.705  1.00 19.41           N  
ATOM   1306  CA  ARG B  14      42.360 -16.572  -7.026  1.00 20.77           C  
ATOM   1307  C   ARG B  14      42.371 -15.386  -7.981  1.00 18.76           C  
ATOM   1308  O   ARG B  14      43.370 -15.156  -8.672  1.00 20.95           O  
ATOM   1309  CB  ARG B  14      41.494 -17.692  -7.623  1.00 24.08           C  
ATOM   1310  CG  ARG B  14      41.794 -19.070  -7.068  1.00 25.26           C  
ATOM   1311  CD  ARG B  14      41.078 -20.129  -7.910  1.00 26.85           C  
ATOM   1312  NE  ARG B  14      39.756 -20.458  -7.379  1.00 28.68           N  
ATOM   1313  CZ  ARG B  14      38.561 -20.191  -7.935  1.00 33.10           C  
ATOM   1314  NH1 ARG B  14      38.426 -19.539  -9.098  1.00 33.87           N  
ATOM   1315  NH2 ARG B  14      37.456 -20.598  -7.302  1.00 35.66           N  
ATOM   1316  N   TYR B  15      41.292 -14.603  -7.965  1.00 16.97           N  
ATOM   1317  CA  TYR B  15      41.150 -13.442  -8.845  1.00 16.81           C  
ATOM   1318  C   TYR B  15      42.292 -12.460  -8.643  1.00 16.55           C  
ATOM   1319  O   TYR B  15      42.838 -11.921  -9.619  1.00 16.50           O  
ATOM   1320  CB  TYR B  15      39.788 -12.739  -8.615  1.00 16.90           C  
ATOM   1321  CG  TYR B  15      39.313 -11.873  -9.778  1.00 16.22           C  
ATOM   1322  CD1 TYR B  15      39.991 -10.710 -10.124  1.00 16.20           C  
ATOM   1323  CD2 TYR B  15      38.196 -12.242 -10.549  1.00 16.41           C  
ATOM   1324  CE1 TYR B  15      39.586  -9.938 -11.212  1.00 16.65           C  
ATOM   1325  CE2 TYR B  15      37.770 -11.450 -11.622  1.00 16.47           C  
ATOM   1326  CZ  TYR B  15      38.479 -10.320 -11.955  1.00 16.86           C  
ATOM   1327  OH  TYR B  15      38.078  -9.520 -12.993  1.00 18.01           O  
ATOM   1328  N   VAL B  16      42.656 -12.194  -7.384  1.00 15.10           N  
ATOM   1329  CA  VAL B  16      43.641 -11.148  -7.098  1.00 15.57           C  
ATOM   1330  C   VAL B  16      45.073 -11.696  -7.017  1.00 16.47           C  
ATOM   1331  O   VAL B  16      46.027 -10.944  -6.809  1.00 17.45           O  
ATOM   1332  CB  VAL B  16      43.289 -10.306  -5.840  1.00 15.29           C  
ATOM   1333  CG1 VAL B  16      41.882  -9.735  -5.947  1.00 15.69           C  
ATOM   1334  CG2 VAL B  16      43.428 -11.154  -4.551  1.00 16.35           C  
ATOM   1335  N   GLY B  17      45.226 -12.997  -7.190  1.00 18.28           N  
ATOM   1336  CA  GLY B  17      46.539 -13.607  -7.112  1.00 19.46           C  
ATOM   1337  C   GLY B  17      47.123 -13.674  -5.693  1.00 20.66           C  
ATOM   1338  O   GLY B  17      48.334 -13.519  -5.510  1.00 19.61           O  
ATOM   1339  N   TRP B  18      46.273 -13.980  -4.711  1.00 20.05           N  
ATOM   1340  CA  TRP B  18      46.712 -14.130  -3.302  1.00 20.67           C  
ATOM   1341  C   TRP B  18      47.691 -15.308  -3.193  1.00 21.50           C  
ATOM   1342  O   TRP B  18      47.416 -16.387  -3.705  1.00 20.94           O  
ATOM   1343  CB  TRP B  18      45.517 -14.394  -2.419  1.00 19.92           C  
ATOM   1344  CG  TRP B  18      45.827 -14.414  -0.956  1.00 20.49           C  
ATOM   1345  CD1 TRP B  18      46.311 -15.461  -0.230  1.00 19.43           C  
ATOM   1346  CD2 TRP B  18      45.647 -13.333  -0.042  1.00 19.70           C  
ATOM   1347  NE1 TRP B  18      46.444 -15.095   1.087  1.00 18.76           N  
ATOM   1348  CE2 TRP B  18      46.052 -13.793   1.230  1.00 19.31           C  
ATOM   1349  CE3 TRP B  18      45.175 -12.028  -0.176  1.00 19.39           C  
ATOM   1350  CZ2 TRP B  18      46.010 -12.983   2.369  1.00 17.95           C  
ATOM   1351  CZ3 TRP B  18      45.138 -11.231   0.935  1.00 19.82           C  
ATOM   1352  CH2 TRP B  18      45.555 -11.711   2.201  1.00 19.77           C  
ATOM   1353  N   GLY B  19      48.845 -15.075  -2.577  1.00 21.26           N  
ATOM   1354  CA  GLY B  19      49.846 -16.107  -2.399  1.00 21.53           C  
ATOM   1355  C   GLY B  19      50.604 -15.936  -1.090  1.00 23.51           C  
ATOM   1356  O   GLY B  19      50.447 -14.955  -0.375  1.00 21.43           O  
ATOM   1357  N   ASP B  20      51.412 -16.938  -0.771  1.00 25.42           N  
ATOM   1358  CA  ASP B  20      52.428 -16.842   0.284  1.00 26.20           C  
ATOM   1359  C   ASP B  20      53.169 -15.502   0.323  1.00 22.68           C  
ATOM   1360  O   ASP B  20      53.474 -15.004   1.399  1.00 22.51           O  
ATOM   1361  CB  ASP B  20      53.491 -17.946   0.066  1.00 29.73           C  
ATOM   1362  CG  ASP B  20      53.016 -19.320   0.487  1.00 31.20           C  
ATOM   1363  OD1 ASP B  20      51.833 -19.522   0.834  1.00 38.74           O  
ATOM   1364  OD2 ASP B  20      53.857 -20.230   0.448  1.00 38.14           O  
ATOM   1365  N   GLY B  21      53.484 -14.926  -0.839  1.00 21.17           N  
ATOM   1366  CA  GLY B  21      54.204 -13.645  -0.886  1.00 20.57           C  
ATOM   1367  C   GLY B  21      53.414 -12.503  -0.230  1.00 19.14           C  
ATOM   1368  O   GLY B  21      53.971 -11.659   0.483  1.00 15.97           O  
ATOM   1369  N   ASP B  22      52.099 -12.499  -0.447  1.00 19.00           N  
ATOM   1370  CA  ASP B  22      51.241 -11.470   0.180  1.00 18.55           C  
ATOM   1371  C   ASP B  22      51.177 -11.676   1.681  1.00 18.16           C  
ATOM   1372  O   ASP B  22      51.205 -10.723   2.449  1.00 16.80           O  
ATOM   1373  CB  ASP B  22      49.836 -11.532  -0.407  1.00 18.66           C  
ATOM   1374  CG  ASP B  22      49.810 -11.192  -1.881  1.00 18.68           C  
ATOM   1375  OD1 ASP B  22      50.220 -10.065  -2.259  1.00 17.86           O  
ATOM   1376  OD2 ASP B  22      49.331 -12.037  -2.657  1.00 18.49           O  
ATOM   1377  N   GLU B  23      51.116 -12.944   2.083  1.00 20.04           N  
ATOM   1378  CA  GLU B  23      51.045 -13.304   3.496  1.00 19.69           C  
ATOM   1379  C   GLU B  23      52.333 -12.876   4.262  1.00 19.80           C  
ATOM   1380  O   GLU B  23      52.240 -12.356   5.376  1.00 20.14           O  
ATOM   1381  CB  GLU B  23      50.718 -14.775   3.657  1.00 20.67           C  
ATOM   1382  CG  GLU B  23      49.397 -15.153   3.030  1.00 20.88           C  
ATOM   1383  CD  GLU B  23      48.866 -16.528   3.396  1.00 23.65           C  
ATOM   1384  OE1 GLU B  23      49.572 -17.307   4.054  1.00 27.77           O  
ATOM   1385  OE2 GLU B  23      47.700 -16.824   3.038  1.00 23.40           O  
ATOM   1386  N   ARG B  24      53.508 -13.057   3.661  1.00 19.74           N  
ATOM   1387  CA  ARG B  24      54.754 -12.564   4.248  1.00 20.52           C  
ATOM   1388  C   ARG B  24      54.760 -11.071   4.365  1.00 18.82           C  
ATOM   1389  O   ARG B  24      55.155 -10.551   5.390  1.00 18.53           O  
ATOM   1390  CB  ARG B  24      55.977 -12.982   3.437  1.00 24.11           C  
ATOM   1391  CG  ARG B  24      56.334 -14.455   3.608  1.00 26.86           C  
ATOM   1392  CD  ARG B  24      57.729 -14.759   3.067  1.00 27.82           C  
ATOM   1393  NE  ARG B  24      57.826 -14.632   1.612  1.00 28.59           N  
ATOM   1394  CZ  ARG B  24      57.417 -15.528   0.705  1.00 29.71           C  
ATOM   1395  NH1 ARG B  24      56.823 -16.669   1.052  1.00 29.62           N  
ATOM   1396  NH2 ARG B  24      57.601 -15.265  -0.585  1.00 30.89           N  
ATOM   1397  N   ALA B  25      54.337 -10.383   3.294  1.00 17.72           N  
ATOM   1398  CA  ALA B  25      54.313  -8.920   3.257  1.00 16.19           C  
ATOM   1399  C   ALA B  25      53.416  -8.325   4.334  1.00 15.40           C  
ATOM   1400  O   ALA B  25      53.814  -7.434   5.007  1.00 13.58           O  
ATOM   1401  CB  ALA B  25      53.924  -8.445   1.866  1.00 17.36           C  
ATOM   1402  N   LEU B  26      52.230  -8.891   4.528  1.00 15.16           N  
ATOM   1403  CA  LEU B  26      51.322  -8.414   5.585  1.00 15.22           C  
ATOM   1404  C   LEU B  26      51.920  -8.650   6.969  1.00 15.74           C  
ATOM   1405  O   LEU B  26      51.802  -7.768   7.840  1.00 16.66           O  
ATOM   1406  CB  LEU B  26      49.954  -9.084   5.469  1.00 13.98           C  
ATOM   1407  CG  LEU B  26      49.094  -8.688   4.250  1.00 13.97           C  
ATOM   1408  CD1 LEU B  26      47.865  -9.547   4.163  1.00 13.18           C  
ATOM   1409  CD2 LEU B  26      48.667  -7.258   4.327  1.00 14.14           C  
ATOM   1410  N   ARG B  27      52.577  -9.794   7.177  1.00 15.76           N  
ATOM   1411  CA AARG B  27      53.201 -10.072   8.481  0.50 16.78           C  
ATOM   1412  CA BARG B  27      53.222 -10.113   8.483  0.50 16.59           C  
ATOM   1413  C   ARG B  27      54.358  -9.122   8.737  1.00 17.50           C  
ATOM   1414  O   ARG B  27      54.529  -8.681   9.871  1.00 17.88           O  
ATOM   1415  CB AARG B  27      53.604 -11.543   8.602  0.50 16.70           C  
ATOM   1416  CB BARG B  27      53.732 -11.581   8.584  0.50 16.25           C  
ATOM   1417  CG AARG B  27      52.346 -12.402   8.626  0.50 17.37           C  
ATOM   1418  CG BARG B  27      52.643 -12.635   8.864  0.50 16.80           C  
ATOM   1419  CD AARG B  27      52.591 -13.884   8.747  0.50 17.03           C  
ATOM   1420  CD BARG B  27      53.208 -14.005   9.253  0.50 16.33           C  
ATOM   1421  NE AARG B  27      51.356 -14.505   9.184  0.50 17.61           N  
ATOM   1422  NE BARG B  27      53.954 -14.571   8.135  0.50 16.57           N  
ATOM   1423  CZ AARG B  27      50.771 -15.548   8.610  0.50 16.46           C  
ATOM   1424  CZ BARG B  27      53.463 -15.434   7.254  0.50 16.62           C  
ATOM   1425  NH1AARG B  27      51.309 -16.160   7.565  0.50 17.10           N  
ATOM   1426  NH1BARG B  27      52.239 -15.924   7.396  0.50 17.88           N  
ATOM   1427  NH2AARG B  27      49.653 -16.002   9.125  0.50 16.28           N  
ATOM   1428  NH2BARG B  27      54.212 -15.841   6.260  0.50 15.75           N  
ATOM   1429  N   SER B  28      55.104  -8.744   7.693  1.00 17.50           N  
ATOM   1430  CA ASER B  28      56.138  -7.698   7.819  0.50 19.50           C  
ATOM   1431  CA BSER B  28      56.138  -7.719   7.882  0.50 18.38           C  
ATOM   1432  C   SER B  28      55.503  -6.362   8.205  1.00 19.42           C  
ATOM   1433  O   SER B  28      56.058  -5.617   8.996  1.00 21.25           O  
ATOM   1434  CB ASER B  28      56.923  -7.489   6.515  0.50 20.61           C  
ATOM   1435  CB BSER B  28      57.074  -7.593   6.685  0.50 18.12           C  
ATOM   1436  OG ASER B  28      57.340  -8.714   5.935  0.50 22.17           O  
ATOM   1437  OG BSER B  28      58.225  -6.844   7.034  0.50 16.59           O  
ATOM   1438  N   LEU B  29      54.337  -6.048   7.598  1.00 19.83           N  
ATOM   1439  CA  LEU B  29      53.638  -4.803   7.871  1.00 18.93           C  
ATOM   1440  C   LEU B  29      53.056  -4.791   9.275  1.00 20.61           C  
ATOM   1441  O   LEU B  29      52.899  -3.693   9.866  1.00 21.98           O  
ATOM   1442  CB  LEU B  29      52.524  -4.508   6.817  1.00 18.74           C  
ATOM   1443  CG  LEU B  29      51.728  -3.183   6.998  1.00 17.26           C  
ATOM   1444  CD1 LEU B  29      52.618  -1.956   6.968  1.00 17.83           C  
ATOM   1445  CD2 LEU B  29      50.659  -3.044   5.918  1.00 17.02           C  
ATOM   1446  N   HIS B  30      52.695  -5.971   9.803  1.00 20.33           N  
ATOM   1447  CA  HIS B  30      52.161  -6.079  11.188  1.00 20.90           C  
ATOM   1448  C   HIS B  30      53.209  -5.544  12.158  1.00 20.30           C  
ATOM   1449  O   HIS B  30      52.900  -4.747  13.054  1.00 17.47           O  
ATOM   1450  CB  HIS B  30      51.767  -7.536  11.525  1.00 21.01           C  
ATOM   1451  CG  HIS B  30      51.234  -7.746  12.910  1.00 22.90           C  
ATOM   1452  ND1 HIS B  30      52.046  -7.765  14.031  1.00 24.02           N  
ATOM   1453  CD2 HIS B  30      49.980  -8.020  13.351  1.00 23.32           C  
ATOM   1454  CE1 HIS B  30      51.297  -7.972  15.109  1.00 24.79           C  
ATOM   1455  NE2 HIS B  30      50.045  -8.140  14.723  1.00 21.34           N  
ATOM   1456  N   GLY B  31      54.444  -5.987  11.945  1.00 20.95           N  
ATOM   1457  CA  GLY B  31      55.594  -5.533  12.740  1.00 23.53           C  
ATOM   1458  C   GLY B  31      55.704  -4.032  12.826  1.00 23.41           C  
ATOM   1459  O   GLY B  31      55.844  -3.478  13.905  1.00 26.20           O  
ATOM   1460  N   ALA B  32      55.648  -3.370  11.680  1.00 24.47           N  
ATOM   1461  CA  ALA B  32      55.716  -1.899  11.630  1.00 24.43           C  
ATOM   1462  C   ALA B  32      54.449  -1.223  12.165  1.00 24.05           C  
ATOM   1463  O   ALA B  32      54.556  -0.196  12.793  1.00 24.41           O  
ATOM   1464  CB  ALA B  32      55.968  -1.440  10.218  1.00 26.96           C  
ATOM   1465  N   ALA B  33      53.266  -1.814  11.948  1.00 20.53           N  
ATOM   1466  CA  ALA B  33      51.989  -1.083  12.183  1.00 20.22           C  
ATOM   1467  C   ALA B  33      51.376  -1.226  13.586  1.00 19.39           C  
ATOM   1468  O   ALA B  33      50.689  -0.299  14.068  1.00 17.51           O  
ATOM   1469  CB  ALA B  33      50.956  -1.481  11.145  1.00 21.11           C  
ATOM   1470  N   ALA B  34      51.599  -2.369  14.213  1.00 18.87           N  
ATOM   1471  CA  ALA B  34      50.974  -2.714  15.502  1.00 20.89           C  
ATOM   1472  C   ALA B  34      51.202  -1.733  16.643  1.00 20.61           C  
ATOM   1473  O   ALA B  34      50.255  -1.416  17.338  1.00 21.34           O  
ATOM   1474  CB  ALA B  34      51.348  -4.132  15.947  1.00 21.85           C  
ATOM   1475  N   PRO B  35      52.430  -1.208  16.825  1.00 21.96           N  
ATOM   1476  CA  PRO B  35      52.594  -0.146  17.818  1.00 22.38           C  
ATOM   1477  C   PRO B  35      51.643   1.031  17.599  1.00 21.36           C  
ATOM   1478  O   PRO B  35      51.272   1.713  18.562  1.00 21.67           O  
ATOM   1479  CB  PRO B  35      54.034   0.301  17.589  1.00 23.33           C  
ATOM   1480  CG  PRO B  35      54.710  -0.906  17.041  1.00 24.24           C  
ATOM   1481  CD  PRO B  35      53.688  -1.451  16.102  1.00 23.06           C  
ATOM   1482  N   HIS B  36      51.251   1.250  16.335  1.00 21.15           N  
ATOM   1483  CA  HIS B  36      50.359   2.349  15.935  1.00 20.95           C  
ATOM   1484  C   HIS B  36      48.871   1.958  15.822  1.00 19.58           C  
ATOM   1485  O   HIS B  36      48.053   2.808  15.445  1.00 20.51           O  
ATOM   1486  CB  HIS B  36      50.807   2.903  14.580  1.00 24.72           C  
ATOM   1487  CG  HIS B  36      52.251   3.308  14.524  1.00 27.38           C  
ATOM   1488  ND1 HIS B  36      52.717   4.491  15.051  1.00 31.46           N  
ATOM   1489  CD2 HIS B  36      53.325   2.693  13.980  1.00 30.28           C  
ATOM   1490  CE1 HIS B  36      54.014   4.590  14.835  1.00 31.18           C  
ATOM   1491  NE2 HIS B  36      54.407   3.516  14.179  1.00 31.43           N  
ATOM   1492  N   PHE B  37      48.494   0.726  16.177  1.00 17.32           N  
ATOM   1493  CA  PHE B  37      47.080   0.361  16.130  1.00 18.15           C  
ATOM   1494  C   PHE B  37      46.179   1.265  16.990  1.00 19.30           C  
ATOM   1495  O   PHE B  37      45.060   1.571  16.563  1.00 18.38           O  
ATOM   1496  CB  PHE B  37      46.819  -1.102  16.510  1.00 17.15           C  
ATOM   1497  CG  PHE B  37      47.305  -2.141  15.519  1.00 17.22           C  
ATOM   1498  CD1 PHE B  37      47.535  -1.870  14.166  1.00 17.43           C  
ATOM   1499  CD2 PHE B  37      47.471  -3.444  15.968  1.00 17.44           C  
ATOM   1500  CE1 PHE B  37      47.991  -2.888  13.311  1.00 18.78           C  
ATOM   1501  CE2 PHE B  37      47.895  -4.462  15.113  1.00 17.99           C  
ATOM   1502  CZ  PHE B  37      48.147  -4.188  13.776  1.00 16.57           C  
ATOM   1503  N   PRO B  38      46.635   1.666  18.234  1.00 18.76           N  
ATOM   1504  CA  PRO B  38      45.785   2.554  18.991  1.00 18.00           C  
ATOM   1505  C   PRO B  38      45.523   3.874  18.257  1.00 18.06           C  
ATOM   1506  O   PRO B  38      44.367   4.384  18.284  1.00 16.74           O  
ATOM   1507  CB  PRO B  38      46.579   2.788  20.295  1.00 20.17           C  
ATOM   1508  CG  PRO B  38      47.420   1.537  20.468  1.00 19.74           C  
ATOM   1509  CD  PRO B  38      47.787   1.176  19.030  1.00 18.76           C  
ATOM   1510  N   ARG B  39      46.553   4.435  17.608  1.00 18.59           N  
ATOM   1511  CA  ARG B  39      46.365   5.678  16.835  1.00 21.32           C  
ATOM   1512  C   ARG B  39      45.444   5.500  15.594  1.00 19.85           C  
ATOM   1513  O   ARG B  39      44.561   6.327  15.333  1.00 20.04           O  
ATOM   1514  CB  ARG B  39      47.726   6.245  16.402  1.00 25.49           C  
ATOM   1515  CG  ARG B  39      47.622   7.627  15.781  1.00 28.99           C  
ATOM   1516  CD  ARG B  39      48.972   8.199  15.401  1.00 32.06           C  
ATOM   1517  NE  ARG B  39      49.831   7.324  14.584  1.00 35.52           N  
ATOM   1518  CZ  ARG B  39      49.651   7.011  13.292  1.00 37.20           C  
ATOM   1519  NH1 ARG B  39      48.587   7.421  12.614  1.00 37.70           N  
ATOM   1520  NH2 ARG B  39      50.526   6.222  12.682  1.00 38.92           N  
ATOM   1521  N   LEU B  40      45.643   4.418  14.846  1.00 19.88           N  
ATOM   1522  CA  LEU B  40      44.741   4.088  13.721  1.00 17.94           C  
ATOM   1523  C   LEU B  40      43.269   3.928  14.199  1.00 17.58           C  
ATOM   1524  O   LEU B  40      42.365   4.444  13.563  1.00 17.15           O  
ATOM   1525  CB  LEU B  40      45.225   2.840  12.988  1.00 17.77           C  
ATOM   1526  CG  LEU B  40      46.587   2.843  12.324  1.00 17.91           C  
ATOM   1527  CD1 LEU B  40      46.891   1.432  11.799  1.00 18.56           C  
ATOM   1528  CD2 LEU B  40      46.739   3.846  11.186  1.00 18.56           C  
ATOM   1529  N   ALA B  41      43.039   3.258  15.328  1.00 17.97           N  
ATOM   1530  CA  ALA B  41      41.684   3.163  15.908  1.00 17.13           C  
ATOM   1531  C   ALA B  41      41.190   4.548  16.276  1.00 18.11           C  
ATOM   1532  O   ALA B  41      40.045   4.909  15.988  1.00 17.02           O  
ATOM   1533  CB  ALA B  41      41.693   2.289  17.137  1.00 18.41           C  
ATOM   1534  N   GLU B  42      42.088   5.359  16.854  1.00 20.57           N  
ATOM   1535  CA  GLU B  42      41.757   6.756  17.205  1.00 22.92           C  
ATOM   1536  C   GLU B  42      41.299   7.554  15.981  1.00 20.97           C  
ATOM   1537  O   GLU B  42      40.262   8.164  16.039  1.00 19.28           O  
ATOM   1538  CB  GLU B  42      42.946   7.447  17.853  1.00 26.33           C  
ATOM   1539  CG  GLU B  42      42.617   8.668  18.680  1.00 30.02           C  
ATOM   1540  CD  GLU B  42      43.782   8.969  19.609  1.00 34.73           C  
ATOM   1541  OE1 GLU B  42      44.825   9.448  19.089  1.00 39.00           O  
ATOM   1542  OE2 GLU B  42      43.680   8.643  20.824  1.00 38.21           O  
ATOM   1543  N   GLU B  43      42.100   7.564  14.913  1.00 21.21           N  
ATOM   1544  CA  GLU B  43      41.702   8.231  13.635  1.00 21.79           C  
ATOM   1545  C   GLU B  43      40.382   7.698  13.079  1.00 19.04           C  
ATOM   1546  O   GLU B  43      39.568   8.462  12.588  1.00 21.03           O  
ATOM   1547  CB  GLU B  43      42.817   8.148  12.587  1.00 23.43           C  
ATOM   1548  CG  GLU B  43      44.012   9.039  12.950  1.00 27.86           C  
ATOM   1549  CD  GLU B  43      45.372   8.612  12.368  1.00 28.94           C  
ATOM   1550  OE1 GLU B  43      45.451   7.732  11.488  1.00 29.98           O  
ATOM   1551  OE2 GLU B  43      46.407   9.188  12.807  1.00 31.85           O  
ATOM   1552  N   PHE B  44      40.172   6.378  13.183  1.00 16.65           N  
ATOM   1553  CA  PHE B  44      38.938   5.732  12.689  1.00 14.71           C  
ATOM   1554  C   PHE B  44      37.676   6.245  13.415  1.00 14.98           C  
ATOM   1555  O   PHE B  44      36.673   6.609  12.775  1.00 13.71           O  
ATOM   1556  CB  PHE B  44      39.131   4.227  12.849  1.00 13.76           C  
ATOM   1557  CG  PHE B  44      38.008   3.399  12.302  1.00 13.38           C  
ATOM   1558  CD1 PHE B  44      36.944   3.062  13.084  1.00 13.20           C  
ATOM   1559  CD2 PHE B  44      38.062   2.902  11.012  1.00 12.85           C  
ATOM   1560  CE1 PHE B  44      35.924   2.269  12.590  1.00 12.87           C  
ATOM   1561  CE2 PHE B  44      37.035   2.127  10.521  1.00 11.97           C  
ATOM   1562  CZ  PHE B  44      36.010   1.784  11.289  1.00 12.05           C  
ATOM   1563  N   TYR B  45      37.699   6.275  14.765  1.00 14.36           N  
ATOM   1564  CA  TYR B  45      36.500   6.759  15.504  1.00 15.54           C  
ATOM   1565  C   TYR B  45      36.379   8.286  15.420  1.00 15.35           C  
ATOM   1566  O   TYR B  45      35.264   8.792  15.358  1.00 15.14           O  
ATOM   1567  CB  TYR B  45      36.404   6.203  16.972  1.00 14.33           C  
ATOM   1568  CG  TYR B  45      36.295   4.710  16.905  1.00 14.56           C  
ATOM   1569  CD1 TYR B  45      35.111   4.118  16.532  1.00 14.17           C  
ATOM   1570  CD2 TYR B  45      37.420   3.893  17.092  1.00 14.51           C  
ATOM   1571  CE1 TYR B  45      35.011   2.740  16.364  1.00 14.56           C  
ATOM   1572  CE2 TYR B  45      37.324   2.529  16.920  1.00 14.49           C  
ATOM   1573  CZ  TYR B  45      36.099   1.971  16.554  1.00 14.13           C  
ATOM   1574  OH  TYR B  45      35.988   0.635  16.364  1.00 15.44           O  
ATOM   1575  N   ASP B  46      37.500   8.996  15.402  1.00 17.19           N  
ATOM   1576  CA  ASP B  46      37.476  10.442  15.158  1.00 19.74           C  
ATOM   1577  C   ASP B  46      36.681  10.777  13.894  1.00 19.42           C  
ATOM   1578  O   ASP B  46      35.827  11.675  13.910  1.00 18.87           O  
ATOM   1579  CB  ASP B  46      38.893  11.019  15.013  1.00 20.83           C  
ATOM   1580  CG  ASP B  46      39.604  11.286  16.351  1.00 25.06           C  
ATOM   1581  OD1 ASP B  46      39.042  10.976  17.436  1.00 23.34           O  
ATOM   1582  OD2 ASP B  46      40.756  11.839  16.286  1.00 27.26           O  
ATOM   1583  N   ARG B  47      36.958  10.070  12.783  1.00 18.81           N  
ATOM   1584  CA  ARG B  47      36.239  10.350  11.536  1.00 17.55           C  
ATOM   1585  C   ARG B  47      34.755  10.079  11.636  1.00 17.60           C  
ATOM   1586  O   ARG B  47      33.964  10.927  11.230  1.00 17.96           O  
ATOM   1587  CB  ARG B  47      36.847   9.614  10.351  1.00 17.22           C  
ATOM   1588  CG  ARG B  47      36.446  10.221   9.000  1.00 17.73           C  
ATOM   1589  CD  ARG B  47      37.120  11.536   8.675  1.00 17.37           C  
ATOM   1590  NE  ARG B  47      38.557  11.340   8.595  1.00 18.37           N  
ATOM   1591  CZ  ARG B  47      39.211  10.803   7.546  1.00 18.38           C  
ATOM   1592  NH1 ARG B  47      38.561  10.442   6.461  1.00 18.93           N  
ATOM   1593  NH2 ARG B  47      40.541  10.623   7.603  1.00 18.46           N  
ATOM   1594  N   ILE B  48      34.363   8.936  12.225  1.00 17.68           N  
ATOM   1595  CA  ILE B  48      32.938   8.619  12.488  1.00 17.60           C  
ATOM   1596  C   ILE B  48      32.245   9.718  13.343  1.00 19.54           C  
ATOM   1597  O   ILE B  48      31.155  10.196  13.001  1.00 19.45           O  
ATOM   1598  CB  ILE B  48      32.782   7.293  13.265  1.00 18.54           C  
ATOM   1599  CG1 ILE B  48      33.177   6.089  12.390  1.00 18.74           C  
ATOM   1600  CG2 ILE B  48      31.330   7.097  13.743  1.00 18.76           C  
ATOM   1601  CD1 ILE B  48      33.207   4.742  13.094  1.00 19.64           C  
ATOM   1602  N   LEU B  49      32.893  10.091  14.442  1.00 20.80           N  
ATOM   1603  CA  LEU B  49      32.369  11.092  15.407  1.00 23.05           C  
ATOM   1604  C   LEU B  49      32.371  12.527  14.840  1.00 25.16           C  
ATOM   1605  O   LEU B  49      31.590  13.391  15.296  1.00 29.33           O  
ATOM   1606  CB  LEU B  49      33.141  11.019  16.738  1.00 23.16           C  
ATOM   1607  CG  LEU B  49      32.931   9.722  17.589  1.00 23.40           C  
ATOM   1608  CD1 LEU B  49      33.801   9.763  18.833  1.00 24.32           C  
ATOM   1609  CD2 LEU B  49      31.491   9.489  17.980  1.00 24.94           C  
ATOM   1610  N   GLY B  50      33.204  12.777  13.838  1.00 26.42           N  
ATOM   1611  CA  GLY B  50      33.194  14.056  13.104  1.00 25.83           C  
ATOM   1612  C   GLY B  50      32.134  14.211  12.018  1.00 26.21           C  
ATOM   1613  O   GLY B  50      32.028  15.266  11.449  1.00 25.67           O  
ATOM   1614  N   HIS B  51      31.377  13.163  11.697  1.00 25.48           N  
ATOM   1615  CA  HIS B  51      30.570  13.116  10.480  1.00 25.67           C  
ATOM   1616  C   HIS B  51      29.129  12.995  10.890  1.00 28.56           C  
ATOM   1617  O   HIS B  51      28.794  12.150  11.691  1.00 25.47           O  
ATOM   1618  CB  HIS B  51      30.955  11.918   9.601  1.00 24.28           C  
ATOM   1619  CG  HIS B  51      30.179  11.806   8.317  1.00 21.75           C  
ATOM   1620  ND1 HIS B  51      28.958  11.174   8.234  1.00 23.57           N  
ATOM   1621  CD2 HIS B  51      30.474  12.207   7.056  1.00 22.32           C  
ATOM   1622  CE1 HIS B  51      28.532  11.196   6.980  1.00 23.49           C  
ATOM   1623  NE2 HIS B  51      29.437  11.818   6.245  1.00 21.31           N  
ATOM   1624  N   GLU B  52      28.285  13.825  10.287  1.00 34.61           N  
ATOM   1625  CA  GLU B  52      26.912  14.066  10.768  1.00 38.50           C  
ATOM   1626  C   GLU B  52      26.045  12.816  10.669  1.00 36.81           C  
ATOM   1627  O   GLU B  52      25.286  12.506  11.569  1.00 38.83           O  
ATOM   1628  CB  GLU B  52      26.276  15.217   9.960  1.00 40.74           C  
ATOM   1629  CG  GLU B  52      24.932  15.676  10.489  1.00 46.12           C  
ATOM   1630  CD  GLU B  52      24.331  16.816   9.691  1.00 47.54           C  
ATOM   1631  OE1 GLU B  52      24.348  16.780   8.433  1.00 49.99           O  
ATOM   1632  OE2 GLU B  52      23.813  17.743  10.341  1.00 54.14           O  
ATOM   1633  N   GLY B  53      26.150  12.119   9.552  1.00 34.94           N  
ATOM   1634  CA  GLY B  53      25.417  10.889   9.341  1.00 34.98           C  
ATOM   1635  C   GLY B  53      25.947   9.696  10.123  1.00 32.42           C  
ATOM   1636  O   GLY B  53      25.165   8.909  10.671  1.00 34.69           O  
ATOM   1637  N   ALA B  54      27.266   9.555  10.178  1.00 31.21           N  
ATOM   1638  CA  ALA B  54      27.892   8.328  10.690  1.00 30.03           C  
ATOM   1639  C   ALA B  54      27.783   8.314  12.205  1.00 28.88           C  
ATOM   1640  O   ALA B  54      27.485   7.278  12.777  1.00 26.77           O  
ATOM   1641  CB  ALA B  54      29.348   8.252  10.281  1.00 29.36           C  
ATOM   1642  N   ARG B  55      28.054   9.466  12.824  1.00 28.27           N  
ATOM   1643  CA  ARG B  55      27.951   9.680  14.295  1.00 30.97           C  
ATOM   1644  C   ARG B  55      26.619   9.220  14.929  1.00 29.00           C  
ATOM   1645  O   ARG B  55      26.591   8.855  16.101  1.00 28.15           O  
ATOM   1646  CB  ARG B  55      28.192  11.167  14.592  1.00 34.72           C  
ATOM   1647  CG  ARG B  55      27.999  11.631  16.020  1.00 43.24           C  
ATOM   1648  CD  ARG B  55      28.513  13.059  16.207  1.00 48.15           C  
ATOM   1649  NE  ARG B  55      27.926  13.988  15.226  1.00 54.58           N  
ATOM   1650  CZ  ARG B  55      28.501  15.101  14.748  1.00 56.52           C  
ATOM   1651  NH1 ARG B  55      27.829  15.859  13.877  1.00 58.74           N  
ATOM   1652  NH2 ARG B  55      29.728  15.480  15.121  1.00 54.84           N  
ATOM   1653  N   THR B  56      25.539   9.203  14.158  1.00 25.17           N  
ATOM   1654  CA  THR B  56      24.247   8.732  14.657  1.00 26.25           C  
ATOM   1655  C   THR B  56      24.197   7.218  14.923  1.00 26.14           C  
ATOM   1656  O   THR B  56      23.294   6.755  15.609  1.00 24.43           O  
ATOM   1657  CB  THR B  56      23.067   9.097  13.702  1.00 27.19           C  
ATOM   1658  OG1 THR B  56      23.161   8.355  12.476  1.00 26.98           O  
ATOM   1659  CG2 THR B  56      23.032  10.599  13.389  1.00 30.23           C  
ATOM   1660  N   ALA B  57      25.143   6.462  14.363  1.00 26.47           N  
ATOM   1661  CA  ALA B  57      25.301   5.032  14.644  1.00 27.44           C  
ATOM   1662  C   ALA B  57      25.850   4.745  16.043  1.00 27.62           C  
ATOM   1663  O   ALA B  57      25.577   3.668  16.591  1.00 27.68           O  
ATOM   1664  CB  ALA B  57      26.218   4.398  13.611  1.00 26.63           C  
ATOM   1665  N   LEU B  58      26.615   5.691  16.605  1.00 25.47           N  
ATOM   1666  CA  LEU B  58      27.293   5.508  17.873  1.00 23.90           C  
ATOM   1667  C   LEU B  58      26.551   6.252  18.974  1.00 24.46           C  
ATOM   1668  O   LEU B  58      26.781   7.466  19.211  1.00 20.07           O  
ATOM   1669  CB  LEU B  58      28.743   6.000  17.801  1.00 26.08           C  
ATOM   1670  CG  LEU B  58      29.671   5.260  16.839  1.00 27.73           C  
ATOM   1671  CD1 LEU B  58      31.043   5.893  16.921  1.00 29.27           C  
ATOM   1672  CD2 LEU B  58      29.736   3.782  17.155  1.00 31.15           C  
ATOM   1673  N   VAL B  59      25.700   5.513  19.680  1.00 22.95           N  
ATOM   1674  CA  VAL B  59      24.839   6.086  20.710  1.00 24.97           C  
ATOM   1675  C   VAL B  59      25.038   5.480  22.100  1.00 27.52           C  
ATOM   1676  O   VAL B  59      24.323   5.842  23.039  1.00 28.70           O  
ATOM   1677  CB  VAL B  59      23.341   5.990  20.278  1.00 25.82           C  
ATOM   1678  CG1 VAL B  59      23.138   6.752  19.010  1.00 28.41           C  
ATOM   1679  CG2 VAL B  59      22.906   4.556  20.025  1.00 26.51           C  
ATOM   1680  N   GLY B  60      26.007   4.583  22.275  1.00 26.49           N  
ATOM   1681  CA  GLY B  60      26.304   4.047  23.598  1.00 27.13           C  
ATOM   1682  C   GLY B  60      27.149   4.924  24.494  1.00 30.10           C  
ATOM   1683  O   GLY B  60      27.432   4.521  25.618  1.00 40.32           O  
ATOM   1684  N   GLY B  61      27.622   6.078  24.016  1.00 34.18           N  
ATOM   1685  CA  GLY B  61      28.404   7.004  24.861  1.00 35.58           C  
ATOM   1686  C   GLY B  61      29.916   6.837  25.005  1.00 35.18           C  
ATOM   1687  O   GLY B  61      30.612   6.271  24.138  1.00 32.64           O  
ATOM   1688  N   GLU B  62      30.432   7.382  26.114  1.00 40.73           N  
ATOM   1689  CA  GLU B  62      31.883   7.467  26.378  1.00 39.61           C  
ATOM   1690  C   GLU B  62      32.517   6.103  26.506  1.00 31.56           C  
ATOM   1691  O   GLU B  62      33.661   5.879  26.056  1.00 38.89           O  
ATOM   1692  CB  GLU B  62      32.144   8.251  27.671  1.00 50.24           C  
ATOM   1693  CG  GLU B  62      31.651   9.695  27.675  1.00 55.69           C  
ATOM   1694  CD  GLU B  62      32.783  10.690  27.589  1.00 60.88           C  
ATOM   1695  OE1 GLU B  62      33.044  11.360  28.616  1.00 63.19           O  
ATOM   1696  OE2 GLU B  62      33.425  10.773  26.507  1.00 65.92           O  
ATOM   1697  N   SER B  63      31.767   5.167  27.070  1.00 23.90           N  
ATOM   1698  CA ASER B  63      32.347   3.832  27.189  0.50 21.37           C  
ATOM   1699  CA BSER B  63      32.170   3.763  27.214  0.50 22.72           C  
ATOM   1700  C   SER B  63      32.311   3.041  25.873  1.00 21.26           C  
ATOM   1701  O   SER B  63      33.191   2.181  25.674  1.00 17.54           O  
ATOM   1702  CB ASER B  63      31.774   3.067  28.373  0.50 19.03           C  
ATOM   1703  CB BSER B  63      31.102   3.023  28.032  0.50 22.62           C  
ATOM   1704  OG ASER B  63      32.193   3.716  29.562  0.50 16.97           O  
ATOM   1705  OG BSER B  63      29.778   3.290  27.520  0.50 21.48           O  
ATOM   1706  N   GLN B  64      31.376   3.342  24.979  1.00 21.25           N  
ATOM   1707  CA  GLN B  64      31.239   2.552  23.756  1.00 21.60           C  
ATOM   1708  C   GLN B  64      32.426   2.705  22.854  1.00 18.50           C  
ATOM   1709  O   GLN B  64      32.926   1.712  22.369  1.00 18.76           O  
ATOM   1710  CB  GLN B  64      29.945   2.846  22.999  1.00 22.32           C  
ATOM   1711  CG  GLN B  64      29.878   2.232  21.603  1.00 23.09           C  
ATOM   1712  CD  GLN B  64      28.603   2.636  20.897  1.00 22.88           C  
ATOM   1713  OE1 GLN B  64      28.291   3.842  20.819  1.00 22.09           O  
ATOM   1714  NE2 GLN B  64      27.855   1.661  20.396  1.00 21.18           N  
ATOM   1715  N   VAL B  65      32.881   3.923  22.632  1.00 18.28           N  
ATOM   1716  CA  VAL B  65      34.070   4.153  21.803  1.00 19.36           C  
ATOM   1717  C   VAL B  65      35.297   3.471  22.396  1.00 19.03           C  
ATOM   1718  O   VAL B  65      36.083   2.829  21.692  1.00 19.46           O  
ATOM   1719  CB  VAL B  65      34.270   5.649  21.577  1.00 20.30           C  
ATOM   1720  CG1 VAL B  65      35.633   5.948  20.981  1.00 21.11           C  
ATOM   1721  CG2 VAL B  65      33.157   6.184  20.676  1.00 19.56           C  
ATOM   1722  N   GLY B  66      35.453   3.544  23.716  1.00 17.45           N  
ATOM   1723  CA  GLY B  66      36.519   2.800  24.349  1.00 15.92           C  
ATOM   1724  C   GLY B  66      36.452   1.303  24.054  1.00 14.44           C  
ATOM   1725  O   GLY B  66      37.484   0.686  23.778  1.00 13.75           O  
ATOM   1726  N   HIS B  67      35.270   0.702  24.093  1.00 13.97           N  
ATOM   1727  CA  HIS B  67      35.181  -0.760  23.861  1.00 14.71           C  
ATOM   1728  C   HIS B  67      35.415  -1.091  22.364  1.00 14.76           C  
ATOM   1729  O   HIS B  67      36.154  -2.012  22.039  1.00 14.79           O  
ATOM   1730  CB  HIS B  67      33.879  -1.339  24.301  1.00 14.93           C  
ATOM   1731  CG  HIS B  67      33.753  -1.471  25.799  1.00 15.82           C  
ATOM   1732  ND1 HIS B  67      34.581  -2.282  26.541  1.00 15.46           N  
ATOM   1733  CD2 HIS B  67      32.896  -0.908  26.675  1.00 16.58           C  
ATOM   1734  CE1 HIS B  67      34.247  -2.197  27.818  1.00 16.14           C  
ATOM   1735  NE2 HIS B  67      33.226  -1.376  27.929  1.00 15.98           N  
ATOM   1736  N   LEU B  68      34.848  -0.288  21.478  1.00 14.78           N  
ATOM   1737  CA  LEU B  68      35.099  -0.458  20.036  1.00 16.06           C  
ATOM   1738  C   LEU B  68      36.576  -0.254  19.640  1.00 15.93           C  
ATOM   1739  O   LEU B  68      37.085  -0.957  18.766  1.00 15.14           O  
ATOM   1740  CB  LEU B  68      34.188   0.492  19.238  1.00 16.88           C  
ATOM   1741  CG  LEU B  68      32.678   0.237  19.316  1.00 15.20           C  
ATOM   1742  CD1 LEU B  68      31.944   1.320  18.554  1.00 16.36           C  
ATOM   1743  CD2 LEU B  68      32.237  -1.096  18.774  1.00 16.33           C  
ATOM   1744  N   LYS B  69      37.294   0.657  20.298  1.00 15.07           N  
ATOM   1745  CA  LYS B  69      38.740   0.768  20.044  1.00 15.65           C  
ATOM   1746  C   LYS B  69      39.465  -0.541  20.396  1.00 15.31           C  
ATOM   1747  O   LYS B  69      40.328  -0.994  19.638  1.00 13.07           O  
ATOM   1748  CB  LYS B  69      39.350   1.924  20.832  1.00 16.61           C  
ATOM   1749  CG  LYS B  69      38.892   3.280  20.320  1.00 18.49           C  
ATOM   1750  CD  LYS B  69      39.653   4.450  20.945  1.00 19.02           C  
ATOM   1751  CE  LYS B  69      39.135   5.780  20.417  1.00 19.95           C  
ATOM   1752  NZ  LYS B  69      39.768   6.983  21.098  1.00 20.35           N  
ATOM   1753  N   VAL B  70      39.034  -1.199  21.484  1.00 14.95           N  
ATOM   1754  CA  VAL B  70      39.638  -2.488  21.861  1.00 15.01           C  
ATOM   1755  C   VAL B  70      39.412  -3.563  20.782  1.00 14.48           C  
ATOM   1756  O   VAL B  70      40.358  -4.199  20.374  1.00 14.55           O  
ATOM   1757  CB  VAL B  70      39.134  -2.987  23.224  1.00 14.56           C  
ATOM   1758  CG1 VAL B  70      39.568  -4.426  23.475  1.00 14.40           C  
ATOM   1759  CG2 VAL B  70      39.629  -2.041  24.305  1.00 15.01           C  
ATOM   1760  N   THR B  71      38.169  -3.741  20.333  1.00 15.12           N  
ATOM   1761  CA  THR B  71      37.870  -4.666  19.255  1.00 15.01           C  
ATOM   1762  C   THR B  71      38.466  -4.285  17.892  1.00 13.35           C  
ATOM   1763  O   THR B  71      38.787  -5.186  17.118  1.00 12.77           O  
ATOM   1764  CB  THR B  71      36.381  -4.907  19.074  1.00 16.50           C  
ATOM   1765  OG1 THR B  71      35.713  -3.650  19.108  1.00 20.56           O  
ATOM   1766  CG2 THR B  71      35.845  -5.819  20.145  1.00 17.88           C  
ATOM   1767  N   MET B  72      38.615  -2.987  17.596  1.00 13.01           N  
ATOM   1768  CA  MET B  72      39.225  -2.524  16.340  1.00 13.12           C  
ATOM   1769  C   MET B  72      40.723  -2.813  16.361  1.00 12.75           C  
ATOM   1770  O   MET B  72      41.299  -3.143  15.325  1.00 12.02           O  
ATOM   1771  CB  MET B  72      39.010  -1.041  16.095  1.00 12.84           C  
ATOM   1772  CG  MET B  72      39.436  -0.569  14.683  1.00 13.84           C  
ATOM   1773  SD  MET B  72      38.599  -1.509  13.366  1.00 12.56           S  
ATOM   1774  CE  MET B  72      36.957  -0.977  13.613  1.00 12.23           C  
ATOM   1775  N   ILE B  73      41.366  -2.643  17.524  1.00 13.01           N  
ATOM   1776  CA  ILE B  73      42.785  -3.051  17.699  1.00 12.98           C  
ATOM   1777  C   ILE B  73      42.968  -4.539  17.415  1.00 11.90           C  
ATOM   1778  O   ILE B  73      43.917  -4.918  16.701  1.00 13.02           O  
ATOM   1779  CB  ILE B  73      43.343  -2.623  19.093  1.00 14.08           C  
ATOM   1780  CG1 ILE B  73      43.595  -1.103  19.094  1.00 15.35           C  
ATOM   1781  CG2 ILE B  73      44.697  -3.279  19.355  1.00 14.80           C  
ATOM   1782  CD1 ILE B  73      43.805  -0.496  20.465  1.00 17.31           C  
ATOM   1783  N   ALA B  74      42.076  -5.385  17.922  1.00 11.15           N  
ATOM   1784  CA  ALA B  74      42.107  -6.852  17.629  1.00 10.82           C  
ATOM   1785  C   ALA B  74      41.784  -7.127  16.160  1.00 10.59           C  
ATOM   1786  O   ALA B  74      42.418  -7.948  15.573  1.00 10.99           O  
ATOM   1787  CB  ALA B  74      41.138  -7.633  18.476  1.00 10.49           C  
ATOM   1788  N   TRP B  75      40.872  -6.371  15.567  1.00 10.66           N  
ATOM   1789  CA  TRP B  75      40.592  -6.507  14.126  1.00 11.38           C  
ATOM   1790  C   TRP B  75      41.822  -6.278  13.233  1.00 11.35           C  
ATOM   1791  O   TRP B  75      42.153  -7.082  12.321  1.00 10.56           O  
ATOM   1792  CB  TRP B  75      39.416  -5.572  13.760  1.00 11.89           C  
ATOM   1793  CG  TRP B  75      38.946  -5.791  12.345  1.00 11.29           C  
ATOM   1794  CD1 TRP B  75      37.972  -6.658  11.946  1.00 11.07           C  
ATOM   1795  CD2 TRP B  75      39.418  -5.137  11.169  1.00 11.06           C  
ATOM   1796  NE1 TRP B  75      37.815  -6.590  10.590  1.00 10.88           N  
ATOM   1797  CE2 TRP B  75      38.697  -5.668  10.085  1.00 10.66           C  
ATOM   1798  CE3 TRP B  75      40.367  -4.157  10.924  1.00 10.73           C  
ATOM   1799  CZ2 TRP B  75      38.917  -5.276   8.786  1.00 10.73           C  
ATOM   1800  CZ3 TRP B  75      40.590  -3.788   9.646  1.00 10.79           C  
ATOM   1801  CH2 TRP B  75      39.862  -4.332   8.575  1.00 10.45           C  
ATOM   1802  N   LEU B  76      42.524  -5.201  13.532  1.00 11.80           N  
ATOM   1803  CA  LEU B  76      43.753  -4.851  12.867  1.00 12.24           C  
ATOM   1804  C   LEU B  76      44.820  -5.875  13.043  1.00 13.68           C  
ATOM   1805  O   LEU B  76      45.541  -6.195  12.086  1.00 13.39           O  
ATOM   1806  CB  LEU B  76      44.277  -3.507  13.349  1.00 12.32           C  
ATOM   1807  CG  LEU B  76      43.499  -2.294  12.832  1.00 11.56           C  
ATOM   1808  CD1 LEU B  76      43.852  -1.024  13.604  1.00 12.21           C  
ATOM   1809  CD2 LEU B  76      43.733  -2.060  11.357  1.00 11.43           C  
ATOM   1810  N   ASP B  77      44.974  -6.353  14.263  1.00 13.99           N  
ATOM   1811  CA  ASP B  77      45.976  -7.349  14.589  1.00 15.48           C  
ATOM   1812  C   ASP B  77      45.779  -8.659  13.792  1.00 15.52           C  
ATOM   1813  O   ASP B  77      46.750  -9.221  13.251  1.00 14.86           O  
ATOM   1814  CB  ASP B  77      45.934  -7.607  16.098  1.00 17.07           C  
ATOM   1815  CG  ASP B  77      47.006  -8.553  16.557  1.00 20.68           C  
ATOM   1816  OD1 ASP B  77      48.189  -8.203  16.447  1.00 22.23           O  
ATOM   1817  OD2 ASP B  77      46.656  -9.637  17.073  1.00 26.44           O  
ATOM   1818  N   GLU B  78      44.535  -9.109  13.692  1.00 15.79           N  
ATOM   1819  CA  GLU B  78      44.191 -10.244  12.825  1.00 17.69           C  
ATOM   1820  C   GLU B  78      44.352  -9.934  11.312  1.00 16.21           C  
ATOM   1821  O   GLU B  78      44.767 -10.796  10.551  1.00 16.97           O  
ATOM   1822  CB  GLU B  78      42.756 -10.642  13.025  1.00 20.89           C  
ATOM   1823  CG  GLU B  78      42.426 -11.236  14.369  1.00 26.06           C  
ATOM   1824  CD  GLU B  78      40.939 -11.534  14.420  1.00 31.29           C  
ATOM   1825  OE1 GLU B  78      40.604 -12.739  14.286  1.00 38.50           O  
ATOM   1826  OE2 GLU B  78      40.131 -10.555  14.504  1.00 31.25           O  
ATOM   1827  N   LEU B  79      43.982  -8.731  10.892  1.00 14.79           N  
ATOM   1828  CA  LEU B  79      44.088  -8.308   9.496  1.00 15.14           C  
ATOM   1829  C   LEU B  79      45.496  -8.532   8.987  1.00 15.06           C  
ATOM   1830  O   LEU B  79      45.692  -9.098   7.901  1.00 13.60           O  
ATOM   1831  CB  LEU B  79      43.733  -6.821   9.315  1.00 14.85           C  
ATOM   1832  CG  LEU B  79      43.754  -6.259   7.909  1.00 13.98           C  
ATOM   1833  CD1 LEU B  79      42.493  -6.714   7.188  1.00 14.35           C  
ATOM   1834  CD2 LEU B  79      43.867  -4.742   7.914  1.00 13.32           C  
ATOM   1835  N   LEU B  80      46.468  -8.037   9.746  1.00 15.57           N  
ATOM   1836  CA  LEU B  80      47.881  -8.095   9.330  1.00 15.15           C  
ATOM   1837  C   LEU B  80      48.642  -9.368   9.711  1.00 16.80           C  
ATOM   1838  O   LEU B  80      49.652  -9.707   9.056  1.00 17.29           O  
ATOM   1839  CB  LEU B  80      48.597  -6.861   9.769  1.00 15.12           C  
ATOM   1840  CG  LEU B  80      47.993  -5.518   9.356  1.00 14.63           C  
ATOM   1841  CD1 LEU B  80      48.920  -4.347   9.687  1.00 15.78           C  
ATOM   1842  CD2 LEU B  80      47.718  -5.514   7.869  1.00 15.86           C  
ATOM   1843  N   GLY B  81      48.178 -10.077  10.730  1.00 18.13           N  
ATOM   1844  CA  GLY B  81      48.882 -11.252  11.261  1.00 18.26           C  
ATOM   1845  C   GLY B  81      48.394 -12.565  10.704  1.00 19.31           C  
ATOM   1846  O   GLY B  81      49.192 -13.466  10.459  1.00 21.72           O  
ATOM   1847  N   GLY B  82      47.088 -12.686  10.520  1.00 19.96           N  
ATOM   1848  CA  GLY B  82      46.478 -13.865   9.904  1.00 21.75           C  
ATOM   1849  C   GLY B  82      46.442 -15.070  10.857  1.00 23.63           C  
ATOM   1850  O   GLY B  82      46.618 -14.890  12.041  1.00 27.28           O  
ATOM   1851  N   PRO B  83      46.256 -16.291  10.365  1.00 24.80           N  
ATOM   1852  CA  PRO B  83      46.202 -16.608   8.939  1.00 23.27           C  
ATOM   1853  C   PRO B  83      44.901 -16.147   8.327  1.00 22.78           C  
ATOM   1854  O   PRO B  83      44.009 -15.661   9.044  1.00 22.01           O  
ATOM   1855  CB  PRO B  83      46.316 -18.165   8.917  1.00 25.15           C  
ATOM   1856  CG  PRO B  83      45.790 -18.577  10.228  1.00 24.56           C  
ATOM   1857  CD  PRO B  83      46.227 -17.515  11.196  1.00 25.24           C  
ATOM   1858  N   TRP B  84      44.812 -16.303   7.019  1.00 22.00           N  
ATOM   1859  CA  TRP B  84      43.683 -15.840   6.215  1.00 21.25           C  
ATOM   1860  C   TRP B  84      42.991 -17.010   5.561  1.00 22.62           C  
ATOM   1861  O   TRP B  84      42.750 -17.005   4.342  1.00 22.73           O  
ATOM   1862  CB  TRP B  84      44.226 -14.901   5.175  1.00 20.54           C  
ATOM   1863  CG  TRP B  84      44.825 -13.659   5.792  1.00 19.33           C  
ATOM   1864  CD1 TRP B  84      44.153 -12.508   6.118  1.00 18.19           C  
ATOM   1865  CD2 TRP B  84      46.189 -13.426   6.126  1.00 17.94           C  
ATOM   1866  NE1 TRP B  84      45.011 -11.603   6.627  1.00 17.36           N  
ATOM   1867  CE2 TRP B  84      46.268 -12.134   6.666  1.00 17.70           C  
ATOM   1868  CE3 TRP B  84      47.357 -14.184   6.034  1.00 20.13           C  
ATOM   1869  CZ2 TRP B  84      47.483 -11.568   7.109  1.00 17.17           C  
ATOM   1870  CZ3 TRP B  84      48.565 -13.641   6.512  1.00 17.86           C  
ATOM   1871  CH2 TRP B  84      48.612 -12.351   7.043  1.00 17.32           C  
ATOM   1872  N   ASP B  85      42.655 -17.991   6.408  1.00 24.55           N  
ATOM   1873  CA  ASP B  85      42.021 -19.273   6.028  1.00 26.54           C  
ATOM   1874  C   ASP B  85      40.526 -19.134   6.176  1.00 24.26           C  
ATOM   1875  O   ASP B  85      40.064 -18.062   6.485  1.00 22.27           O  
ATOM   1876  CB  ASP B  85      42.584 -20.459   6.898  1.00 29.21           C  
ATOM   1877  CG  ASP B  85      42.432 -20.237   8.459  1.00 31.23           C  
ATOM   1878  OD1 ASP B  85      42.103 -19.111   8.905  1.00 30.46           O  
ATOM   1879  OD2 ASP B  85      42.642 -21.203   9.261  1.00 31.99           O  
ATOM   1880  N   GLU B  86      39.778 -20.217   5.981  1.00 25.60           N  
ATOM   1881  CA  GLU B  86      38.326 -20.212   6.094  1.00 26.47           C  
ATOM   1882  C   GLU B  86      37.811 -19.734   7.441  1.00 24.55           C  
ATOM   1883  O   GLU B  86      36.802 -19.022   7.505  1.00 22.89           O  
ATOM   1884  CB  GLU B  86      37.719 -21.585   5.750  1.00 29.24           C  
ATOM   1885  CG  GLU B  86      36.186 -21.588   5.732  1.00 33.71           C  
ATOM   1886  CD  GLU B  86      35.549 -22.930   5.357  1.00 38.96           C  
ATOM   1887  OE1 GLU B  86      35.841 -23.953   6.025  1.00 46.58           O  
ATOM   1888  OE2 GLU B  86      34.737 -22.955   4.408  1.00 39.48           O  
ATOM   1889  N   ALA B  87      38.486 -20.118   8.520  1.00 24.34           N  
ATOM   1890  CA  ALA B  87      38.036 -19.708   9.853  1.00 21.85           C  
ATOM   1891  C   ALA B  87      38.045 -18.176   9.948  1.00 19.25           C  
ATOM   1892  O   ALA B  87      37.049 -17.566  10.395  1.00 18.54           O  
ATOM   1893  CB  ALA B  87      38.913 -20.351  10.937  1.00 22.53           C  
ATOM   1894  N   TYR B  88      39.126 -17.562   9.464  1.00 17.05           N  
ATOM   1895  CA  TYR B  88      39.283 -16.089   9.488  1.00 16.22           C  
ATOM   1896  C   TYR B  88      38.152 -15.429   8.714  1.00 14.78           C  
ATOM   1897  O   TYR B  88      37.514 -14.510   9.208  1.00 14.41           O  
ATOM   1898  CB  TYR B  88      40.633 -15.695   8.897  1.00 15.48           C  
ATOM   1899  CG  TYR B  88      40.893 -14.237   8.638  1.00 15.03           C  
ATOM   1900  CD1 TYR B  88      40.407 -13.610   7.454  1.00 14.67           C  
ATOM   1901  CD2 TYR B  88      41.747 -13.498   9.459  1.00 14.49           C  
ATOM   1902  CE1 TYR B  88      40.670 -12.265   7.186  1.00 14.71           C  
ATOM   1903  CE2 TYR B  88      42.008 -12.153   9.189  1.00 14.69           C  
ATOM   1904  CZ  TYR B  88      41.478 -11.547   8.037  1.00 14.72           C  
ATOM   1905  OH  TYR B  88      41.751 -10.260   7.720  1.00 14.30           O  
ATOM   1906  N   TRP B  89      37.909 -15.892   7.496  1.00 15.46           N  
ATOM   1907  CA  TRP B  89      36.887 -15.258   6.634  1.00 15.78           C  
ATOM   1908  C   TRP B  89      35.464 -15.476   7.157  1.00 16.10           C  
ATOM   1909  O   TRP B  89      34.630 -14.599   7.032  1.00 16.01           O  
ATOM   1910  CB  TRP B  89      37.089 -15.632   5.146  1.00 15.40           C  
ATOM   1911  CG  TRP B  89      38.415 -15.063   4.572  1.00 16.03           C  
ATOM   1912  CD1 TRP B  89      39.545 -15.771   4.249  1.00 16.09           C  
ATOM   1913  CD2 TRP B  89      38.749 -13.682   4.348  1.00 16.64           C  
ATOM   1914  NE1 TRP B  89      40.536 -14.931   3.825  1.00 16.83           N  
ATOM   1915  CE2 TRP B  89      40.072 -13.644   3.865  1.00 16.58           C  
ATOM   1916  CE3 TRP B  89      38.044 -12.470   4.481  1.00 16.17           C  
ATOM   1917  CZ2 TRP B  89      40.702 -12.457   3.499  1.00 17.06           C  
ATOM   1918  CZ3 TRP B  89      38.687 -11.295   4.136  1.00 17.17           C  
ATOM   1919  CH2 TRP B  89      40.004 -11.296   3.673  1.00 16.63           C  
ATOM   1920  N   ASP B  90      35.194 -16.620   7.788  1.00 17.93           N  
ATOM   1921  CA  ASP B  90      33.897 -16.872   8.417  1.00 20.69           C  
ATOM   1922  C   ASP B  90      33.718 -15.886   9.562  1.00 19.35           C  
ATOM   1923  O   ASP B  90      32.609 -15.352   9.728  1.00 19.22           O  
ATOM   1924  CB  ASP B  90      33.762 -18.310   8.972  1.00 22.61           C  
ATOM   1925  CG  ASP B  90      33.607 -19.373   7.880  1.00 26.85           C  
ATOM   1926  OD1 ASP B  90      33.211 -19.095   6.709  1.00 27.21           O  
ATOM   1927  OD2 ASP B  90      33.895 -20.545   8.224  1.00 31.73           O  
ATOM   1928  N   ARG B  91      34.773 -15.634  10.349  1.00 17.33           N  
ATOM   1929  CA  ARG B  91      34.697 -14.541  11.364  1.00 19.23           C  
ATOM   1930  C   ARG B  91      34.398 -13.150  10.733  1.00 16.29           C  
ATOM   1931  O   ARG B  91      33.611 -12.350  11.293  1.00 16.02           O  
ATOM   1932  CB  ARG B  91      35.974 -14.435  12.246  1.00 21.38           C  
ATOM   1933  CG  ARG B  91      36.208 -15.617  13.198  1.00 25.76           C  
ATOM   1934  CD  ARG B  91      37.362 -15.425  14.201  1.00 27.16           C  
ATOM   1935  NE  ARG B  91      38.662 -15.651  13.562  1.00 29.48           N  
ATOM   1936  CZ  ARG B  91      39.230 -16.850  13.346  1.00 33.28           C  
ATOM   1937  NH1 ARG B  91      40.415 -16.919  12.738  1.00 35.38           N  
ATOM   1938  NH2 ARG B  91      38.632 -17.987  13.722  1.00 35.88           N  
ATOM   1939  N   ARG B  92      35.050 -12.837   9.617  1.00 14.49           N  
ATOM   1940  CA  ARG B  92      34.745 -11.579   8.926  1.00 14.38           C  
ATOM   1941  C   ARG B  92      33.306 -11.453   8.437  1.00 14.92           C  
ATOM   1942  O   ARG B  92      32.770 -10.351   8.453  1.00 15.35           O  
ATOM   1943  CB  ARG B  92      35.677 -11.305   7.773  1.00 13.79           C  
ATOM   1944  CG  ARG B  92      37.156 -11.107   8.127  1.00 12.84           C  
ATOM   1945  CD  ARG B  92      37.448 -10.586   9.529  1.00 13.38           C  
ATOM   1946  NE  ARG B  92      38.677  -9.813   9.539  1.00 12.42           N  
ATOM   1947  CZ  ARG B  92      39.355  -9.450  10.614  1.00 12.87           C  
ATOM   1948  NH1 ARG B  92      40.444  -8.687  10.472  1.00 11.73           N  
ATOM   1949  NH2 ARG B  92      38.976  -9.844  11.833  1.00 13.20           N  
ATOM   1950  N   TYR B  93      32.719 -12.565   8.001  1.00 16.39           N  
ATOM   1951  CA  TYR B  93      31.291 -12.666   7.672  1.00 19.74           C  
ATOM   1952  C   TYR B  93      30.445 -12.273   8.859  1.00 19.83           C  
ATOM   1953  O   TYR B  93      29.574 -11.416   8.724  1.00 19.65           O  
ATOM   1954  CB  TYR B  93      30.907 -14.110   7.255  1.00 24.01           C  
ATOM   1955  CG  TYR B  93      29.541 -14.226   6.603  1.00 30.98           C  
ATOM   1956  CD1 TYR B  93      29.357 -13.830   5.282  1.00 33.52           C  
ATOM   1957  CD2 TYR B  93      28.421 -14.739   7.306  1.00 36.46           C  
ATOM   1958  CE1 TYR B  93      28.113 -13.914   4.676  1.00 37.38           C  
ATOM   1959  CE2 TYR B  93      27.163 -14.846   6.693  1.00 37.64           C  
ATOM   1960  CZ  TYR B  93      27.020 -14.427   5.375  1.00 38.32           C  
ATOM   1961  OH  TYR B  93      25.816 -14.498   4.714  1.00 39.15           O  
ATOM   1962  N   ARG B  94      30.661 -12.897  10.023  1.00 18.31           N  
ATOM   1963  CA  ARG B  94      29.873 -12.499  11.214  1.00 20.62           C  
ATOM   1964  C   ARG B  94      30.006 -11.016  11.560  1.00 18.58           C  
ATOM   1965  O   ARG B  94      29.075 -10.418  12.003  1.00 18.11           O  
ATOM   1966  CB  ARG B  94      30.270 -13.332  12.409  1.00 23.80           C  
ATOM   1967  CG  ARG B  94      29.704 -14.735  12.331  1.00 28.14           C  
ATOM   1968  CD  ARG B  94      30.090 -15.586  13.537  1.00 30.57           C  
ATOM   1969  NE  ARG B  94      31.035 -16.581  13.054  1.00 35.47           N  
ATOM   1970  CZ  ARG B  94      32.259 -16.806  13.518  1.00 35.68           C  
ATOM   1971  NH1 ARG B  94      32.774 -16.145  14.577  1.00 33.11           N  
ATOM   1972  NH2 ARG B  94      32.964 -17.750  12.909  1.00 33.93           N  
ATOM   1973  N   ILE B  95      31.206 -10.460  11.392  1.00 18.81           N  
ATOM   1974  CA  ILE B  95      31.452  -9.037  11.628  1.00 18.20           C  
ATOM   1975  C   ILE B  95      30.611  -8.185  10.668  1.00 17.64           C  
ATOM   1976  O   ILE B  95      30.054  -7.172  11.068  1.00 19.54           O  
ATOM   1977  CB  ILE B  95      32.965  -8.690  11.514  1.00 17.42           C  
ATOM   1978  CG1 ILE B  95      33.698  -9.211  12.749  1.00 17.77           C  
ATOM   1979  CG2 ILE B  95      33.142  -7.168  11.408  1.00 17.79           C  
ATOM   1980  CD1 ILE B  95      35.199  -9.387  12.634  1.00 17.69           C  
ATOM   1981  N   GLY B  96      30.504  -8.602   9.411  1.00 18.26           N  
ATOM   1982  CA  GLY B  96      29.632  -7.931   8.452  1.00 18.48           C  
ATOM   1983  C   GLY B  96      28.195  -7.928   8.893  1.00 19.01           C  
ATOM   1984  O   GLY B  96      27.558  -6.848   8.947  1.00 16.42           O  
ATOM   1985  N   ARG B  97      27.692  -9.117   9.225  1.00 19.00           N  
ATOM   1986  CA  ARG B  97      26.312  -9.244   9.745  1.00 22.60           C  
ATOM   1987  C   ARG B  97      26.003  -8.387  10.964  1.00 21.02           C  
ATOM   1988  O   ARG B  97      24.857  -7.970  11.090  1.00 22.26           O  
ATOM   1989  CB  ARG B  97      25.933 -10.695  10.081  1.00 25.04           C  
ATOM   1990  CG  ARG B  97      25.784 -11.643   8.903  1.00 28.82           C  
ATOM   1991  CD  ARG B  97      25.144 -12.970   9.317  1.00 33.62           C  
ATOM   1992  NE  ARG B  97      25.503 -13.403  10.688  1.00 38.61           N  
ATOM   1993  CZ  ARG B  97      26.016 -14.588  11.073  1.00 43.09           C  
ATOM   1994  NH1 ARG B  97      26.287 -15.562  10.197  1.00 42.41           N  
ATOM   1995  NH2 ARG B  97      26.274 -14.796  12.390  1.00 40.29           N  
ATOM   1996  N   VAL B  98      26.971  -8.143  11.859  1.00 19.16           N  
ATOM   1997  CA  VAL B  98      26.737  -7.248  13.017  1.00 21.92           C  
ATOM   1998  C   VAL B  98      26.252  -5.857  12.546  1.00 21.47           C  
ATOM   1999  O   VAL B  98      25.253  -5.335  13.073  1.00 23.47           O  
ATOM   2000  CB  VAL B  98      27.983  -7.033  13.919  1.00 22.45           C  
ATOM   2001  CG1 VAL B  98      27.682  -5.976  14.962  1.00 22.53           C  
ATOM   2002  CG2 VAL B  98      28.422  -8.314  14.611  1.00 22.08           C  
ATOM   2003  N   HIS B  99      26.919  -5.311  11.516  1.00 19.30           N  
ATOM   2004  CA  HIS B  99      26.629  -3.980  10.964  1.00 18.74           C  
ATOM   2005  C   HIS B  99      25.326  -3.994  10.175  1.00 20.69           C  
ATOM   2006  O   HIS B  99      24.568  -3.013  10.183  1.00 20.61           O  
ATOM   2007  CB  HIS B  99      27.777  -3.494  10.104  1.00 17.50           C  
ATOM   2008  CG  HIS B  99      29.038  -3.368  10.879  1.00 16.07           C  
ATOM   2009  ND1 HIS B  99      29.862  -4.438  11.114  1.00 15.44           N  
ATOM   2010  CD2 HIS B  99      29.543  -2.332  11.584  1.00 15.71           C  
ATOM   2011  CE1 HIS B  99      30.870  -4.037  11.864  1.00 16.23           C  
ATOM   2012  NE2 HIS B  99      30.662  -2.783  12.221  1.00 14.85           N  
ATOM   2013  N   VAL B 100      25.047  -5.124   9.539  1.00 20.99           N  
ATOM   2014  CA  VAL B 100      23.763  -5.310   8.876  1.00 23.41           C  
ATOM   2015  C   VAL B 100      22.630  -5.214   9.923  1.00 22.52           C  
ATOM   2016  O   VAL B 100      21.708  -4.412   9.779  1.00 21.74           O  
ATOM   2017  CB  VAL B 100      23.704  -6.654   8.106  1.00 22.84           C  
ATOM   2018  CG1 VAL B 100      22.279  -6.953   7.611  1.00 24.29           C  
ATOM   2019  CG2 VAL B 100      24.644  -6.606   6.939  1.00 23.66           C  
ATOM   2020  N   ARG B 101      22.752  -5.978  10.998  1.00 22.99           N  
ATOM   2021  CA  ARG B 101      21.727  -6.014  12.053  1.00 24.34           C  
ATOM   2022  C   ARG B 101      21.506  -4.713  12.848  1.00 24.81           C  
ATOM   2023  O   ARG B 101      20.378  -4.447  13.303  1.00 25.03           O  
ATOM   2024  CB  ARG B 101      22.022  -7.145  13.024  1.00 27.59           C  
ATOM   2025  CG  ARG B 101      21.935  -8.528  12.400  1.00 31.06           C  
ATOM   2026  CD  ARG B 101      22.726  -9.501  13.225  1.00 34.61           C  
ATOM   2027  NE  ARG B 101      22.543 -10.884  12.786  1.00 40.64           N  
ATOM   2028  CZ  ARG B 101      23.248 -11.912  13.254  1.00 44.84           C  
ATOM   2029  NH1 ARG B 101      24.202 -11.725  14.174  1.00 46.53           N  
ATOM   2030  NH2 ARG B 101      23.009 -13.145  12.796  1.00 48.68           N  
ATOM   2031  N   ILE B 102      22.545  -3.887  13.018  1.00 22.86           N  
ATOM   2032  CA  ILE B 102      22.325  -2.552  13.597  1.00 21.45           C  
ATOM   2033  C   ILE B 102      21.746  -1.563  12.575  1.00 21.19           C  
ATOM   2034  O   ILE B 102      21.518  -0.390  12.907  1.00 21.86           O  
ATOM   2035  CB  ILE B 102      23.569  -1.995  14.317  1.00 20.41           C  
ATOM   2036  CG1 ILE B 102      24.721  -1.732  13.354  1.00 20.02           C  
ATOM   2037  CG2 ILE B 102      24.019  -2.963  15.425  1.00 21.38           C  
ATOM   2038  CD1 ILE B 102      25.973  -1.131  14.015  1.00 18.78           C  
ATOM   2039  N   GLY B 103      21.481  -2.028  11.349  1.00 21.21           N  
ATOM   2040  CA  GLY B 103      20.957  -1.184  10.285  1.00 20.51           C  
ATOM   2041  C   GLY B 103      21.900  -0.076   9.820  1.00 18.94           C  
ATOM   2042  O   GLY B 103      21.448   0.959   9.389  1.00 17.85           O  
ATOM   2043  N   LEU B 104      23.208  -0.281   9.885  1.00 19.40           N  
ATOM   2044  CA  LEU B 104      24.165   0.735   9.412  1.00 19.08           C  
ATOM   2045  C   LEU B 104      24.088   0.765   7.886  1.00 18.27           C  
ATOM   2046  O   LEU B 104      24.126  -0.281   7.272  1.00 19.41           O  
ATOM   2047  CB  LEU B 104      25.595   0.397   9.828  1.00 18.97           C  
ATOM   2048  CG  LEU B 104      26.691   1.362   9.387  1.00 18.87           C  
ATOM   2049  CD1 LEU B 104      26.584   2.683  10.107  1.00 19.74           C  
ATOM   2050  CD2 LEU B 104      28.050   0.755   9.659  1.00 19.52           C  
ATOM   2051  N   PRO B 105      23.963   1.952   7.277  1.00 19.44           N  
ATOM   2052  CA  PRO B 105      23.944   1.989   5.819  1.00 19.90           C  
ATOM   2053  C   PRO B 105      25.256   1.462   5.200  1.00 20.20           C  
ATOM   2054  O   PRO B 105      26.329   1.780   5.668  1.00 18.06           O  
ATOM   2055  CB  PRO B 105      23.729   3.469   5.514  1.00 21.97           C  
ATOM   2056  CG  PRO B 105      22.969   4.006   6.685  1.00 20.54           C  
ATOM   2057  CD  PRO B 105      23.512   3.236   7.870  1.00 20.08           C  
ATOM   2058  N   GLN B 106      25.161   0.627   4.169  1.00 20.29           N  
ATOM   2059  CA  GLN B 106      26.349  -0.094   3.695  1.00 19.70           C  
ATOM   2060  C   GLN B 106      27.444   0.832   3.217  1.00 19.01           C  
ATOM   2061  O   GLN B 106      28.623   0.514   3.358  1.00 16.54           O  
ATOM   2062  CB  GLN B 106      26.004  -1.122   2.625  1.00 20.17           C  
ATOM   2063  CG  GLN B 106      25.692  -0.556   1.259  1.00 21.21           C  
ATOM   2064  CD  GLN B 106      25.306  -1.611   0.264  1.00 20.15           C  
ATOM   2065  OE1 GLN B 106      24.626  -2.561   0.602  1.00 24.07           O  
ATOM   2066  NE2 GLN B 106      25.723  -1.439  -0.977  1.00 20.65           N  
ATOM   2067  N   HIS B 107      27.034   1.965   2.652  1.00 18.64           N  
ATOM   2068  CA  HIS B 107      27.970   2.901   2.077  1.00 19.02           C  
ATOM   2069  C   HIS B 107      28.988   3.375   3.133  1.00 16.40           C  
ATOM   2070  O   HIS B 107      30.128   3.545   2.786  1.00 16.34           O  
ATOM   2071  CB  HIS B 107      27.244   4.004   1.290  1.00 21.16           C  
ATOM   2072  CG  HIS B 107      26.527   5.014   2.133  1.00 24.46           C  
ATOM   2073  ND1 HIS B 107      25.276   4.799   2.668  1.00 28.51           N  
ATOM   2074  CD2 HIS B 107      26.889   6.255   2.520  1.00 28.54           C  
ATOM   2075  CE1 HIS B 107      24.908   5.858   3.364  1.00 27.72           C  
ATOM   2076  NE2 HIS B 107      25.872   6.758   3.293  1.00 27.20           N  
ATOM   2077  N   TYR B 108      28.611   3.483   4.425  1.00 15.81           N  
ATOM   2078  CA  TYR B 108      29.572   3.811   5.469  1.00 16.43           C  
ATOM   2079  C   TYR B 108      30.742   2.831   5.601  1.00 14.21           C  
ATOM   2080  O   TYR B 108      31.829   3.247   5.988  1.00 13.22           O  
ATOM   2081  CB  TYR B 108      28.927   4.068   6.843  1.00 18.19           C  
ATOM   2082  CG  TYR B 108      28.050   5.309   6.890  1.00 21.85           C  
ATOM   2083  CD1 TYR B 108      28.571   6.571   6.643  1.00 25.44           C  
ATOM   2084  CD2 TYR B 108      26.702   5.209   7.204  1.00 25.07           C  
ATOM   2085  CE1 TYR B 108      27.773   7.695   6.688  1.00 27.60           C  
ATOM   2086  CE2 TYR B 108      25.890   6.328   7.257  1.00 26.80           C  
ATOM   2087  CZ  TYR B 108      26.424   7.556   7.004  1.00 29.31           C  
ATOM   2088  OH  TYR B 108      25.589   8.636   7.057  1.00 34.80           O  
ATOM   2089  N   MET B 109      30.536   1.569   5.277  1.00 13.62           N  
ATOM   2090  CA  MET B 109      31.646   0.600   5.298  1.00 14.81           C  
ATOM   2091  C   MET B 109      32.786   1.019   4.371  1.00 13.42           C  
ATOM   2092  O   MET B 109      33.928   0.857   4.729  1.00 11.93           O  
ATOM   2093  CB  MET B 109      31.205  -0.857   5.017  1.00 16.18           C  
ATOM   2094  CG  MET B 109      30.136  -1.433   5.905  1.00 19.25           C  
ATOM   2095  SD  MET B 109      30.455  -1.298   7.697  1.00 25.38           S  
ATOM   2096  CE  MET B 109      31.424  -2.803   7.845  1.00 23.25           C  
ATOM   2097  N   PHE B 110      32.488   1.624   3.201  1.00 14.12           N  
ATOM   2098  CA  PHE B 110      33.570   2.028   2.273  1.00 13.40           C  
ATOM   2099  C   PHE B 110      34.324   3.234   2.809  1.00 12.30           C  
ATOM   2100  O   PHE B 110      35.554   3.339   2.718  1.00 11.91           O  
ATOM   2101  CB  PHE B 110      33.011   2.324   0.875  1.00 13.61           C  
ATOM   2102  CG  PHE B 110      32.378   1.160   0.226  1.00 13.23           C  
ATOM   2103  CD1 PHE B 110      33.120   0.332  -0.587  1.00 12.90           C  
ATOM   2104  CD2 PHE B 110      31.022   0.915   0.383  1.00 13.70           C  
ATOM   2105  CE1 PHE B 110      32.543  -0.744  -1.200  1.00 13.08           C  
ATOM   2106  CE2 PHE B 110      30.436  -0.154  -0.227  1.00 14.07           C  
ATOM   2107  CZ  PHE B 110      31.194  -1.000  -1.007  1.00 14.33           C  
ATOM   2108  N   GLY B 111      33.589   4.146   3.392  1.00 12.69           N  
ATOM   2109  CA  GLY B 111      34.163   5.353   4.017  1.00 12.69           C  
ATOM   2110  C   GLY B 111      35.107   4.946   5.156  1.00 12.58           C  
ATOM   2111  O   GLY B 111      36.259   5.418   5.230  1.00 12.07           O  
ATOM   2112  N   ALA B 112      34.619   4.063   6.032  1.00 12.54           N  
ATOM   2113  CA  ALA B 112      35.372   3.663   7.219  1.00 12.11           C  
ATOM   2114  C   ALA B 112      36.662   2.912   6.771  1.00 12.80           C  
ATOM   2115  O   ALA B 112      37.761   3.225   7.206  1.00 11.22           O  
ATOM   2116  CB  ALA B 112      34.485   2.806   8.092  1.00 13.06           C  
ATOM   2117  N   MET B 113      36.518   1.974   5.828  1.00 13.07           N  
ATOM   2118  CA  MET B 113      37.665   1.208   5.309  1.00 12.39           C  
ATOM   2119  C   MET B 113      38.649   2.142   4.650  1.00 12.12           C  
ATOM   2120  O   MET B 113      39.842   1.956   4.847  1.00 11.64           O  
ATOM   2121  CB  MET B 113      37.217   0.125   4.367  1.00 12.55           C  
ATOM   2122  CG  MET B 113      38.229  -0.937   4.069  1.00 13.28           C  
ATOM   2123  SD  MET B 113      38.623  -1.930   5.487  1.00 14.72           S  
ATOM   2124  CE  MET B 113      37.205  -2.987   5.504  1.00 14.38           C  
ATOM   2125  N   ASN B 114      38.179   3.190   3.957  1.00 11.84           N  
ATOM   2126  CA  ASN B 114      39.119   4.183   3.414  1.00 11.97           C  
ATOM   2127  C   ASN B 114      40.012   4.873   4.476  1.00 11.00           C  
ATOM   2128  O   ASN B 114      41.192   5.187   4.201  1.00 11.13           O  
ATOM   2129  CB  ASN B 114      38.438   5.228   2.540  1.00 12.23           C  
ATOM   2130  CG  ASN B 114      39.432   6.094   1.839  1.00 12.56           C  
ATOM   2131  OD1 ASN B 114      39.755   7.173   2.309  1.00 15.16           O  
ATOM   2132  ND2 ASN B 114      39.989   5.600   0.774  1.00 12.16           N  
ATOM   2133  N   VAL B 115      39.504   5.072   5.689  1.00 11.71           N  
ATOM   2134  CA  VAL B 115      40.360   5.678   6.752  1.00 13.30           C  
ATOM   2135  C   VAL B 115      41.493   4.721   7.075  1.00 12.53           C  
ATOM   2136  O   VAL B 115      42.653   5.087   6.982  1.00 12.62           O  
ATOM   2137  CB  VAL B 115      39.580   6.030   8.030  1.00 13.79           C  
ATOM   2138  CG1 VAL B 115      40.515   6.723   8.967  1.00 14.08           C  
ATOM   2139  CG2 VAL B 115      38.402   6.936   7.678  1.00 15.11           C  
ATOM   2140  N   HIS B 116      41.162   3.466   7.365  1.00 12.66           N  
ATOM   2141  CA  HIS B 116      42.228   2.448   7.578  1.00 12.51           C  
ATOM   2142  C   HIS B 116      43.181   2.321   6.369  1.00 11.41           C  
ATOM   2143  O   HIS B 116      44.386   2.248   6.562  1.00 10.45           O  
ATOM   2144  CB  HIS B 116      41.648   1.078   7.892  1.00 13.11           C  
ATOM   2145  CG  HIS B 116      41.118   0.919   9.287  1.00 12.93           C  
ATOM   2146  ND1 HIS B 116      41.637   1.586  10.385  1.00 12.65           N  
ATOM   2147  CD2 HIS B 116      40.142   0.103   9.762  1.00 12.84           C  
ATOM   2148  CE1 HIS B 116      40.972   1.213  11.471  1.00 12.94           C  
ATOM   2149  NE2 HIS B 116      40.066   0.306  11.126  1.00 12.75           N  
ATOM   2150  N   ARG B 117      42.632   2.334   5.125  1.00 11.39           N  
ATOM   2151  CA  ARG B 117      43.451   2.206   3.933  1.00 11.27           C  
ATOM   2152  C   ARG B 117      44.488   3.327   3.909  1.00 11.83           C  
ATOM   2153  O   ARG B 117      45.636   3.038   3.685  1.00 11.27           O  
ATOM   2154  CB  ARG B 117      42.613   2.263   2.648  1.00 11.34           C  
ATOM   2155  CG  ARG B 117      43.413   1.965   1.384  1.00 10.96           C  
ATOM   2156  CD  ARG B 117      42.641   2.102   0.068  1.00 10.87           C  
ATOM   2157  NE  ARG B 117      41.382   1.361   0.052  1.00 10.90           N  
ATOM   2158  CZ  ARG B 117      41.279   0.074  -0.256  1.00 10.15           C  
ATOM   2159  NH1 ARG B 117      42.339  -0.646  -0.544  1.00  9.63           N  
ATOM   2160  NH2 ARG B 117      40.109  -0.489  -0.234  1.00 10.85           N  
ATOM   2161  N   THR B 118      44.068   4.566   4.152  1.00 12.18           N  
ATOM   2162  CA  THR B 118      44.936   5.721   4.086  1.00 14.75           C  
ATOM   2163  C   THR B 118      46.037   5.655   5.173  1.00 15.08           C  
ATOM   2164  O   THR B 118      47.222   5.800   4.856  1.00 14.10           O  
ATOM   2165  CB  THR B 118      44.111   7.057   4.167  1.00 16.93           C  
ATOM   2166  OG1 THR B 118      43.130   7.043   3.118  1.00 17.82           O  
ATOM   2167  CG2 THR B 118      45.015   8.282   4.019  1.00 17.80           C  
ATOM   2168  N   GLY B 119      45.658   5.393   6.433  1.00 15.55           N  
ATOM   2169  CA  GLY B 119      46.663   5.303   7.507  1.00 15.83           C  
ATOM   2170  C   GLY B 119      47.633   4.147   7.305  1.00 17.04           C  
ATOM   2171  O   GLY B 119      48.826   4.303   7.542  1.00 16.90           O  
ATOM   2172  N   LEU B 120      47.127   2.989   6.860  1.00 16.09           N  
ATOM   2173  CA  LEU B 120      47.970   1.795   6.700  1.00 16.75           C  
ATOM   2174  C   LEU B 120      48.909   1.947   5.516  1.00 18.09           C  
ATOM   2175  O   LEU B 120      50.087   1.588   5.636  1.00 16.30           O  
ATOM   2176  CB  LEU B 120      47.123   0.521   6.576  1.00 17.28           C  
ATOM   2177  CG  LEU B 120      46.450   0.065   7.881  1.00 17.22           C  
ATOM   2178  CD1 LEU B 120      45.459  -1.079   7.636  1.00 17.37           C  
ATOM   2179  CD2 LEU B 120      47.482  -0.432   8.905  1.00 17.60           C  
ATOM   2180  N   ALA B 121      48.416   2.535   4.412  1.00 19.28           N  
ATOM   2181  CA  ALA B 121      49.294   2.919   3.266  1.00 19.81           C  
ATOM   2182  C   ALA B 121      50.401   3.879   3.676  1.00 19.91           C  
ATOM   2183  O   ALA B 121      51.523   3.796   3.154  1.00 23.00           O  
ATOM   2184  CB  ALA B 121      48.484   3.538   2.136  1.00 19.44           C  
ATOM   2185  N   ARG B 122      50.101   4.793   4.594  1.00 21.03           N  
ATOM   2186  CA  ARG B 122      51.108   5.773   5.082  1.00 23.82           C  
ATOM   2187  C   ARG B 122      52.200   5.047   5.919  1.00 21.95           C  
ATOM   2188  O   ARG B 122      53.389   5.210   5.651  1.00 20.07           O  
ATOM   2189  CB  ARG B 122      50.394   6.870   5.873  1.00 26.13           C  
ATOM   2190  CG  ARG B 122      51.215   8.108   6.105  1.00 32.22           C  
ATOM   2191  CD  ARG B 122      50.749   8.943   7.300  1.00 34.56           C  
ATOM   2192  NE  ARG B 122      51.950   9.346   8.035  1.00 42.57           N  
ATOM   2193  CZ  ARG B 122      52.796  10.322   7.673  1.00 43.30           C  
ATOM   2194  NH1 ARG B 122      52.578  11.095   6.594  1.00 43.01           N  
ATOM   2195  NH2 ARG B 122      53.875  10.547   8.421  1.00 42.77           N  
ATOM   2196  N   LEU B 123      51.791   4.215   6.891  1.00 19.98           N  
ATOM   2197  CA  LEU B 123      52.731   3.422   7.692  1.00 21.06           C  
ATOM   2198  C   LEU B 123      53.631   2.549   6.830  1.00 22.77           C  
ATOM   2199  O   LEU B 123      54.854   2.474   7.084  1.00 24.69           O  
ATOM   2200  CB  LEU B 123      52.007   2.563   8.728  1.00 22.05           C  
ATOM   2201  CG  LEU B 123      51.465   3.335   9.934  1.00 23.03           C  
ATOM   2202  CD1 LEU B 123      50.398   2.558  10.699  1.00 21.27           C  
ATOM   2203  CD2 LEU B 123      52.603   3.707  10.870  1.00 23.74           C  
ATOM   2204  N   ALA B 124      53.055   1.914   5.798  1.00 21.09           N  
ATOM   2205  CA  ALA B 124      53.806   1.075   4.880  1.00 21.01           C  
ATOM   2206  C   ALA B 124      54.872   1.869   4.131  1.00 20.77           C  
ATOM   2207  O   ALA B 124      56.014   1.432   4.021  1.00 21.08           O  
ATOM   2208  CB  ALA B 124      52.868   0.393   3.877  1.00 21.49           C  
ATOM   2209  N   TYR B 125      54.499   3.022   3.593  1.00 21.21           N  
ATOM   2210  CA  TYR B 125      55.470   3.889   2.911  1.00 20.84           C  
ATOM   2211  C   TYR B 125      56.611   4.247   3.881  1.00 24.01           C  
ATOM   2212  O   TYR B 125      57.818   4.124   3.560  1.00 21.60           O  
ATOM   2213  CB  TYR B 125      54.803   5.141   2.337  1.00 21.89           C  
ATOM   2214  CG  TYR B 125      55.843   6.040   1.725  1.00 21.09           C  
ATOM   2215  CD1 TYR B 125      56.256   5.876   0.401  1.00 21.22           C  
ATOM   2216  CD2 TYR B 125      56.473   6.975   2.496  1.00 20.61           C  
ATOM   2217  CE1 TYR B 125      57.276   6.641  -0.129  1.00 20.61           C  
ATOM   2218  CE2 TYR B 125      57.494   7.738   1.985  1.00 21.19           C  
ATOM   2219  CZ  TYR B 125      57.882   7.588   0.681  1.00 22.21           C  
ATOM   2220  OH  TYR B 125      58.895   8.406   0.238  1.00 21.84           O  
ATOM   2221  N   GLU B 126      56.231   4.686   5.071  1.00 24.46           N  
ATOM   2222  CA  GLU B 126      57.206   5.182   6.041  1.00 26.54           C  
ATOM   2223  C   GLU B 126      58.262   4.159   6.413  1.00 26.51           C  
ATOM   2224  O   GLU B 126      59.431   4.537   6.535  1.00 27.66           O  
ATOM   2225  CB  GLU B 126      56.517   5.694   7.286  1.00 28.48           C  
ATOM   2226  CG  GLU B 126      55.835   7.026   7.070  1.00 32.44           C  
ATOM   2227  CD  GLU B 126      55.288   7.580   8.360  0.50 33.75           C  
ATOM   2228  OE1 GLU B 126      54.697   6.809   9.159  0.50 36.07           O  
ATOM   2229  OE2 GLU B 126      55.475   8.786   8.575  0.50 36.48           O  
ATOM   2230  N   ARG B 127      57.838   2.891   6.549  1.00 24.36           N  
ATOM   2231  CA AARG B 127      58.723   1.798   6.899  0.50 24.52           C  
ATOM   2232  CA BARG B 127      58.715   1.769   6.903  0.50 24.92           C  
ATOM   2233  C   ARG B 127      59.481   1.204   5.725  1.00 25.22           C  
ATOM   2234  O   ARG B 127      60.610   0.739   5.899  1.00 28.46           O  
ATOM   2235  CB AARG B 127      57.931   0.675   7.561  0.50 23.78           C  
ATOM   2236  CB BARG B 127      57.913   0.626   7.576  0.50 24.76           C  
ATOM   2237  CG AARG B 127      58.782  -0.435   8.177  0.50 24.16           C  
ATOM   2238  CG BARG B 127      58.527  -0.798   7.617  0.50 25.27           C  
ATOM   2239  CD AARG B 127      59.655   0.075   9.322  0.50 23.39           C  
ATOM   2240  CD BARG B 127      59.689  -0.987   8.594  0.50 26.36           C  
ATOM   2241  NE AARG B 127      59.639  -0.915  10.392  0.50 24.82           N  
ATOM   2242  NE BARG B 127      59.775  -2.392   9.035  0.50 26.66           N  
ATOM   2243  CZ AARG B 127      59.256  -0.690  11.643  0.50 24.32           C  
ATOM   2244  CZ BARG B 127      60.559  -3.316   8.479  0.50 25.98           C  
ATOM   2245  NH1AARG B 127      59.272  -1.680  12.485  0.50 28.05           N  
ATOM   2246  NH1BARG B 127      60.546  -4.556   8.925  0.50 25.90           N  
ATOM   2247  NH2AARG B 127      58.908   0.499  12.075  0.50 24.25           N  
ATOM   2248  NH2BARG B 127      61.361  -3.004   7.471  0.50 27.01           N  
ATOM   2249  N   PHE B 128      58.868   1.169   4.543  1.00 23.93           N  
ATOM   2250  CA  PHE B 128      59.441   0.383   3.451  1.00 23.38           C  
ATOM   2251  C   PHE B 128      59.980   1.235   2.305  1.00 22.75           C  
ATOM   2252  O   PHE B 128      60.539   0.692   1.372  1.00 22.94           O  
ATOM   2253  CB  PHE B 128      58.419  -0.665   2.960  1.00 22.13           C  
ATOM   2254  CG  PHE B 128      58.121  -1.740   3.969  1.00 23.75           C  
ATOM   2255  CD1 PHE B 128      59.033  -2.801   4.188  1.00 23.99           C  
ATOM   2256  CD2 PHE B 128      56.929  -1.729   4.700  1.00 21.83           C  
ATOM   2257  CE1 PHE B 128      58.767  -3.785   5.110  1.00 21.52           C  
ATOM   2258  CE2 PHE B 128      56.664  -2.721   5.621  1.00 23.29           C  
ATOM   2259  CZ  PHE B 128      57.577  -3.756   5.823  1.00 23.00           C  
ATOM   2260  N   HIS B 129      59.865   2.561   2.372  1.00 24.44           N  
ATOM   2261  CA  HIS B 129      60.297   3.405   1.223  1.00 26.78           C  
ATOM   2262  C   HIS B 129      61.736   3.179   0.783  1.00 27.27           C  
ATOM   2263  O   HIS B 129      62.049   3.336  -0.396  1.00 27.38           O  
ATOM   2264  CB  HIS B 129      60.020   4.901   1.425  1.00 28.94           C  
ATOM   2265  CG  HIS B 129      60.912   5.585   2.422  1.00 30.51           C  
ATOM   2266  ND1 HIS B 129      60.545   5.785   3.735  1.00 31.88           N  
ATOM   2267  CD2 HIS B 129      62.104   6.205   2.268  1.00 30.99           C  
ATOM   2268  CE1 HIS B 129      61.506   6.437   4.366  1.00 32.76           C  
ATOM   2269  NE2 HIS B 129      62.454   6.721   3.493  1.00 31.97           N  
ATOM   2270  N   GLY B 130      62.605   2.812   1.724  1.00 29.42           N  
ATOM   2271  CA  GLY B 130      64.019   2.569   1.434  1.00 29.28           C  
ATOM   2272  C   GLY B 130      64.334   1.292   0.676  1.00 29.01           C  
ATOM   2273  O   GLY B 130      65.445   1.129   0.150  1.00 29.54           O  
ATOM   2274  N   ASP B 131      63.372   0.377   0.638  1.00 25.93           N  
ATOM   2275  CA  ASP B 131      63.472  -0.833  -0.123  1.00 25.49           C  
ATOM   2276  C   ASP B 131      62.267  -0.874  -1.055  1.00 25.35           C  
ATOM   2277  O   ASP B 131      61.274  -1.540  -0.741  1.00 25.86           O  
ATOM   2278  CB  ASP B 131      63.511  -2.040   0.835  1.00 25.28           C  
ATOM   2279  CG  ASP B 131      63.870  -3.345   0.138  1.00 27.60           C  
ATOM   2280  OD1 ASP B 131      64.283  -3.297  -1.047  1.00 27.68           O  
ATOM   2281  OD2 ASP B 131      63.744  -4.433   0.780  1.00 27.16           O  
ATOM   2282  N   PRO B 132      62.340  -0.171  -2.211  1.00 24.22           N  
ATOM   2283  CA  PRO B 132      61.137  -0.074  -3.076  1.00 24.09           C  
ATOM   2284  C   PRO B 132      60.455  -1.389  -3.476  1.00 22.65           C  
ATOM   2285  O   PRO B 132      59.218  -1.403  -3.535  1.00 22.69           O  
ATOM   2286  CB  PRO B 132      61.643   0.668  -4.294  1.00 23.51           C  
ATOM   2287  CG  PRO B 132      62.728   1.540  -3.757  1.00 24.32           C  
ATOM   2288  CD  PRO B 132      63.378   0.787  -2.645  1.00 25.10           C  
ATOM   2289  N   PRO B 133      61.223  -2.478  -3.708  1.00 21.12           N  
ATOM   2290  CA  PRO B 133      60.553  -3.722  -4.095  1.00 21.21           C  
ATOM   2291  C   PRO B 133      59.788  -4.391  -2.972  1.00 21.04           C  
ATOM   2292  O   PRO B 133      58.824  -5.141  -3.246  1.00 21.57           O  
ATOM   2293  CB  PRO B 133      61.704  -4.616  -4.595  1.00 22.42           C  
ATOM   2294  CG  PRO B 133      62.930  -4.043  -4.017  1.00 21.09           C  
ATOM   2295  CD  PRO B 133      62.688  -2.587  -3.871  1.00 22.60           C  
ATOM   2296  N   GLU B 134      60.185  -4.131  -1.728  1.00 19.71           N  
ATOM   2297  CA  GLU B 134      59.432  -4.606  -0.589  1.00 19.95           C  
ATOM   2298  C   GLU B 134      58.229  -3.682  -0.307  1.00 19.71           C  
ATOM   2299  O   GLU B 134      57.160  -4.181   0.051  1.00 20.63           O  
ATOM   2300  CB  GLU B 134      60.370  -4.785   0.621  1.00 22.25           C  
ATOM   2301  CG  GLU B 134      59.741  -5.381   1.859  1.00 23.08           C  
ATOM   2302  CD  GLU B 134      59.397  -6.857   1.748  1.00 25.82           C  
ATOM   2303  OE1 GLU B 134      58.824  -7.377   2.733  1.00 31.47           O  
ATOM   2304  OE2 GLU B 134      59.654  -7.516   0.709  1.00 28.69           O  
ATOM   2305  N   LEU B 135      58.368  -2.362  -0.483  1.00 18.67           N  
ATOM   2306  CA  LEU B 135      57.221  -1.481  -0.434  1.00 18.55           C  
ATOM   2307  C   LEU B 135      56.122  -1.890  -1.446  1.00 19.23           C  
ATOM   2308  O   LEU B 135      54.927  -1.819  -1.126  1.00 19.04           O  
ATOM   2309  CB  LEU B 135      57.591  -0.004  -0.604  1.00 19.59           C  
ATOM   2310  CG  LEU B 135      56.418   0.996  -0.701  1.00 18.11           C  
ATOM   2311  CD1 LEU B 135      55.484   0.884   0.481  1.00 18.19           C  
ATOM   2312  CD2 LEU B 135      56.862   2.449  -0.797  1.00 19.10           C  
ATOM   2313  N   GLU B 136      56.530  -2.289  -2.646  1.00 19.02           N  
ATOM   2314  CA  GLU B 136      55.597  -2.740  -3.668  1.00 19.82           C  
ATOM   2315  C   GLU B 136      54.878  -3.998  -3.231  1.00 18.75           C  
ATOM   2316  O   GLU B 136      53.670  -4.046  -3.313  1.00 17.31           O  
ATOM   2317  CB  GLU B 136      56.314  -2.982  -4.999  1.00 22.49           C  
ATOM   2318  CG  GLU B 136      55.381  -3.412  -6.115  1.00 24.71           C  
ATOM   2319  CD  GLU B 136      56.045  -3.407  -7.481  1.00 28.37           C  
ATOM   2320  OE1 GLU B 136      55.464  -2.843  -8.435  1.00 30.67           O  
ATOM   2321  OE2 GLU B 136      57.143  -3.979  -7.616  1.00 28.10           O  
ATOM   2322  N   ARG B 137      55.608  -5.001  -2.748  1.00 17.54           N  
ATOM   2323  CA  ARG B 137      54.963  -6.223  -2.210  1.00 18.58           C  
ATOM   2324  C   ARG B 137      53.987  -5.949  -1.058  1.00 17.76           C  
ATOM   2325  O   ARG B 137      52.873  -6.497  -1.046  1.00 18.39           O  
ATOM   2326  CB  ARG B 137      56.000  -7.294  -1.793  1.00 17.80           C  
ATOM   2327  CG  ARG B 137      56.663  -7.953  -3.000  1.00 19.51           C  
ATOM   2328  CD  ARG B 137      57.614  -9.056  -2.540  1.00 21.45           C  
ATOM   2329  NE  ARG B 137      58.779  -8.420  -1.937  1.00 23.39           N  
ATOM   2330  CZ  ARG B 137      59.927  -8.132  -2.562  1.00 25.46           C  
ATOM   2331  NH1 ARG B 137      60.860  -7.506  -1.881  1.00 26.35           N  
ATOM   2332  NH2 ARG B 137      60.170  -8.463  -3.840  1.00 27.62           N  
ATOM   2333  N   VAL B 138      54.372  -5.074  -0.145  1.00 17.34           N  
ATOM   2334  CA  VAL B 138      53.540  -4.698   1.009  1.00 17.28           C  
ATOM   2335  C   VAL B 138      52.301  -3.860   0.626  1.00 17.45           C  
ATOM   2336  O   VAL B 138      51.178  -4.208   0.966  1.00 19.79           O  
ATOM   2337  CB  VAL B 138      54.397  -3.974   2.067  1.00 16.69           C  
ATOM   2338  CG1 VAL B 138      53.553  -3.442   3.217  1.00 16.62           C  
ATOM   2339  CG2 VAL B 138      55.468  -4.938   2.617  1.00 17.33           C  
ATOM   2340  N   ARG B 139      52.509  -2.780  -0.099  1.00 17.40           N  
ATOM   2341  CA  ARG B 139      51.414  -2.040  -0.775  1.00 17.43           C  
ATOM   2342  C   ARG B 139      50.437  -2.938  -1.525  1.00 16.10           C  
ATOM   2343  O   ARG B 139      49.212  -2.810  -1.343  1.00 15.72           O  
ATOM   2344  CB  ARG B 139      52.015  -1.061  -1.758  1.00 18.66           C  
ATOM   2345  CG  ARG B 139      51.053  -0.094  -2.332  1.00 20.09           C  
ATOM   2346  CD  ARG B 139      51.791   0.985  -3.108  1.00 20.74           C  
ATOM   2347  NE  ARG B 139      52.298   0.474  -4.360  1.00 19.53           N  
ATOM   2348  CZ  ARG B 139      53.527   0.659  -4.843  1.00 20.74           C  
ATOM   2349  NH1 ARG B 139      54.444   1.388  -4.206  1.00 20.83           N  
ATOM   2350  NH2 ARG B 139      53.850   0.085  -5.988  1.00 22.88           N  
ATOM   2351  N   ASN B 140      50.939  -3.899  -2.304  1.00 15.92           N  
ATOM   2352  CA  ASN B 140      50.045  -4.791  -3.075  1.00 15.31           C  
ATOM   2353  C   ASN B 140      49.225  -5.713  -2.185  1.00 14.83           C  
ATOM   2354  O   ASN B 140      48.000  -5.806  -2.340  1.00 12.59           O  
ATOM   2355  CB  ASN B 140      50.806  -5.596  -4.126  1.00 16.01           C  
ATOM   2356  CG  ASN B 140      51.308  -4.750  -5.281  1.00 17.60           C  
ATOM   2357  OD1 ASN B 140      51.012  -3.542  -5.406  1.00 19.90           O  
ATOM   2358  ND2 ASN B 140      52.068  -5.389  -6.145  1.00 17.61           N  
ATOM   2359  N   ALA B 141      49.862  -6.328  -1.179  1.00 14.19           N  
ATOM   2360  CA  ALA B 141      49.128  -7.170  -0.227  1.00 14.05           C  
ATOM   2361  C   ALA B 141      48.051  -6.436   0.582  1.00 13.20           C  
ATOM   2362  O   ALA B 141      46.925  -6.947   0.777  1.00 11.67           O  
ATOM   2363  CB  ALA B 141      50.082  -7.873   0.711  1.00 15.71           C  
ATOM   2364  N   LEU B 142      48.415  -5.265   1.063  1.00 13.99           N  
ATOM   2365  CA  LEU B 142      47.487  -4.379   1.775  1.00 13.55           C  
ATOM   2366  C   LEU B 142      46.267  -4.085   0.958  1.00 12.12           C  
ATOM   2367  O   LEU B 142      45.162  -4.224   1.445  1.00 11.48           O  
ATOM   2368  CB  LEU B 142      48.172  -3.069   2.178  1.00 13.62           C  
ATOM   2369  CG  LEU B 142      47.329  -2.074   2.947  1.00 14.52           C  
ATOM   2370  CD1 LEU B 142      46.779  -2.652   4.246  1.00 14.56           C  
ATOM   2371  CD2 LEU B 142      48.225  -0.881   3.243  1.00 15.94           C  
ATOM   2372  N   GLY B 143      46.449  -3.665  -0.299  1.00 11.73           N  
ATOM   2373  CA  GLY B 143      45.282  -3.452  -1.162  1.00 11.58           C  
ATOM   2374  C   GLY B 143      44.385  -4.678  -1.306  1.00 11.60           C  
ATOM   2375  O   GLY B 143      43.124  -4.577  -1.256  1.00 11.86           O  
ATOM   2376  N   LYS B 144      45.005  -5.838  -1.498  1.00 10.70           N  
ATOM   2377  CA  LYS B 144      44.268  -7.088  -1.622  1.00 11.84           C  
ATOM   2378  C   LYS B 144      43.489  -7.426  -0.393  1.00 10.99           C  
ATOM   2379  O   LYS B 144      42.263  -7.689  -0.494  1.00 10.09           O  
ATOM   2380  CB  LYS B 144      45.166  -8.299  -1.951  1.00 12.39           C  
ATOM   2381  CG  LYS B 144      45.813  -8.260  -3.321  1.00 13.51           C  
ATOM   2382  CD  LYS B 144      46.762  -9.433  -3.485  1.00 14.10           C  
ATOM   2383  CE  LYS B 144      47.758  -9.165  -4.593  1.00 15.77           C  
ATOM   2384  NZ  LYS B 144      48.530 -10.394  -4.943  1.00 15.61           N  
ATOM   2385  N   VAL B 145      44.127  -7.381   0.800  1.00 10.85           N  
ATOM   2386  CA  VAL B 145      43.368  -7.794   2.010  1.00 10.41           C  
ATOM   2387  C   VAL B 145      42.193  -6.856   2.300  1.00 10.80           C  
ATOM   2388  O   VAL B 145      41.089  -7.311   2.671  1.00 10.61           O  
ATOM   2389  CB  VAL B 145      44.259  -8.090   3.248  1.00 10.89           C  
ATOM   2390  CG1 VAL B 145      44.828  -6.838   3.845  1.00 11.52           C  
ATOM   2391  CG2 VAL B 145      43.462  -8.847   4.294  1.00 11.47           C  
ATOM   2392  N   LEU B 146      42.396  -5.547   2.106  1.00 11.13           N  
ATOM   2393  CA  LEU B 146      41.320  -4.573   2.316  1.00 10.98           C  
ATOM   2394  C   LEU B 146      40.195  -4.685   1.274  1.00 10.42           C  
ATOM   2395  O   LEU B 146      39.059  -4.563   1.629  1.00 11.15           O  
ATOM   2396  CB  LEU B 146      41.866  -3.144   2.414  1.00 11.43           C  
ATOM   2397  CG  LEU B 146      42.873  -2.807   3.535  1.00 12.21           C  
ATOM   2398  CD1 LEU B 146      43.211  -1.343   3.422  1.00 12.13           C  
ATOM   2399  CD2 LEU B 146      42.295  -3.085   4.893  1.00 12.86           C  
ATOM   2400  N   ASP B 147      40.490  -4.996   0.011  1.00 10.29           N  
ATOM   2401  CA  ASP B 147      39.439  -5.199  -0.970  1.00 10.19           C  
ATOM   2402  C   ASP B 147      38.656  -6.473  -0.714  1.00  9.92           C  
ATOM   2403  O   ASP B 147      37.455  -6.449  -0.861  1.00  9.50           O  
ATOM   2404  CB  ASP B 147      39.992  -5.151  -2.395  1.00 11.12           C  
ATOM   2405  CG  ASP B 147      40.411  -3.714  -2.817  1.00 11.04           C  
ATOM   2406  OD1 ASP B 147      39.969  -2.721  -2.124  1.00 12.09           O  
ATOM   2407  OD2 ASP B 147      41.167  -3.584  -3.820  1.00 10.74           O  
ATOM   2408  N   LEU B 148      39.312  -7.543  -0.264  1.00 10.22           N  
ATOM   2409  CA  LEU B 148      38.610  -8.792   0.110  1.00 11.83           C  
ATOM   2410  C   LEU B 148      37.739  -8.620   1.379  1.00 11.61           C  
ATOM   2411  O   LEU B 148      36.646  -9.183   1.461  1.00 12.17           O  
ATOM   2412  CB  LEU B 148      39.609  -9.954   0.288  1.00 13.72           C  
ATOM   2413  CG  LEU B 148      39.960 -10.805  -0.954  1.00 14.97           C  
ATOM   2414  CD1 LEU B 148      40.242  -9.966  -2.174  1.00 15.94           C  
ATOM   2415  CD2 LEU B 148      41.182 -11.681  -0.669  1.00 16.68           C  
ATOM   2416  N   GLU B 149      38.192  -7.842   2.357  1.00 12.19           N  
ATOM   2417  CA  GLU B 149      37.369  -7.510   3.562  1.00 12.52           C  
ATOM   2418  C   GLU B 149      36.090  -6.794   3.152  1.00 12.35           C  
ATOM   2419  O   GLU B 149      35.002  -7.147   3.581  1.00 11.88           O  
ATOM   2420  CB  GLU B 149      38.124  -6.625   4.556  1.00 13.11           C  
ATOM   2421  CG  GLU B 149      39.253  -7.327   5.307  1.00 13.28           C  
ATOM   2422  CD  GLU B 149      38.801  -8.164   6.483  1.00 13.53           C  
ATOM   2423  OE1 GLU B 149      39.671  -8.890   7.053  1.00 13.60           O  
ATOM   2424  OE2 GLU B 149      37.577  -8.135   6.799  1.00 14.78           O  
ATOM   2425  N   LEU B 150      36.230  -5.802   2.296  1.00 12.87           N  
ATOM   2426  CA  LEU B 150      35.053  -5.132   1.728  1.00 13.33           C  
ATOM   2427  C   LEU B 150      34.132  -6.104   0.991  1.00 13.00           C  
ATOM   2428  O   LEU B 150      32.914  -6.098   1.191  1.00 12.97           O  
ATOM   2429  CB  LEU B 150      35.476  -4.009   0.797  1.00 13.42           C  
ATOM   2430  CG  LEU B 150      35.930  -2.726   1.449  1.00 12.76           C  
ATOM   2431  CD1 LEU B 150      36.507  -1.855   0.386  1.00 13.10           C  
ATOM   2432  CD2 LEU B 150      34.767  -2.096   2.199  1.00 13.02           C  
ATOM   2433  N   ALA B 151      34.723  -6.962   0.160  1.00 13.99           N  
ATOM   2434  CA  ALA B 151      33.946  -7.980  -0.577  1.00 13.58           C  
ATOM   2435  C   ALA B 151      33.144  -8.886   0.350  1.00 14.62           C  
ATOM   2436  O   ALA B 151      31.935  -9.110   0.112  1.00 13.18           O  
ATOM   2437  CB  ALA B 151      34.858  -8.814  -1.463  1.00 13.69           C  
ATOM   2438  N   VAL B 152      33.813  -9.403   1.390  1.00 15.00           N  
ATOM   2439  CA  VAL B 152      33.157 -10.281   2.353  1.00 17.06           C  
ATOM   2440  C   VAL B 152      32.097  -9.569   3.184  1.00 18.55           C  
ATOM   2441  O   VAL B 152      31.008 -10.109   3.369  1.00 19.40           O  
ATOM   2442  CB  VAL B 152      34.148 -11.021   3.263  1.00 17.74           C  
ATOM   2443  CG1 VAL B 152      33.405 -11.779   4.379  1.00 17.79           C  
ATOM   2444  CG2 VAL B 152      34.982 -11.984   2.430  1.00 17.74           C  
ATOM   2445  N   MET B 153      32.398  -8.364   3.659  1.00 20.49           N  
ATOM   2446  CA  MET B 153      31.422  -7.607   4.470  1.00 22.95           C  
ATOM   2447  C   MET B 153      30.192  -7.186   3.634  1.00 20.85           C  
ATOM   2448  O   MET B 153      29.079  -7.213   4.121  1.00 19.30           O  
ATOM   2449  CB  MET B 153      32.103  -6.435   5.216  1.00 24.65           C  
ATOM   2450  CG  MET B 153      32.622  -6.875   6.613  1.00 28.76           C  
ATOM   2451  SD  MET B 153      33.559  -5.714   7.649  1.00 33.32           S  
ATOM   2452  CE  MET B 153      34.096  -4.532   6.366  1.00 32.04           C  
ATOM   2453  N   LEU B 154      30.385  -6.867   2.365  1.00 20.32           N  
ATOM   2454  CA  LEU B 154      29.286  -6.454   1.521  1.00 21.05           C  
ATOM   2455  C   LEU B 154      28.455  -7.650   1.036  1.00 20.06           C  
ATOM   2456  O   LEU B 154      27.301  -7.490   0.763  1.00 19.76           O  
ATOM   2457  CB  LEU B 154      29.745  -5.570   0.355  1.00 22.09           C  
ATOM   2458  CG  LEU B 154      29.731  -4.047   0.530  1.00 21.91           C  
ATOM   2459  CD1 LEU B 154      28.324  -3.483   0.600  1.00 25.24           C  
ATOM   2460  CD2 LEU B 154      30.571  -3.597   1.710  1.00 23.30           C  
ATOM   2461  N   HIS B 155      29.047  -8.836   0.966  1.00 19.92           N  
ATOM   2462  CA  HIS B 155      28.302 -10.071   0.770  1.00 21.55           C  
ATOM   2463  C   HIS B 155      27.206 -10.193   1.829  1.00 22.75           C  
ATOM   2464  O   HIS B 155      26.069 -10.523   1.489  1.00 21.31           O  
ATOM   2465  CB  HIS B 155      29.273 -11.275   0.803  1.00 22.25           C  
ATOM   2466  CG  HIS B 155      28.648 -12.597   0.492  1.00 25.48           C  
ATOM   2467  ND1 HIS B 155      27.802 -12.799  -0.577  1.00 27.47           N  
ATOM   2468  CD2 HIS B 155      28.800 -13.807   1.085  1.00 28.80           C  
ATOM   2469  CE1 HIS B 155      27.408 -14.062  -0.590  1.00 29.52           C  
ATOM   2470  NE2 HIS B 155      28.013 -14.702   0.399  1.00 29.42           N  
ATOM   2471  N   THR B 156      27.527  -9.856   3.088  1.00 21.97           N  
ATOM   2472  CA  THR B 156      26.536 -10.007   4.186  1.00 22.53           C  
ATOM   2473  C   THR B 156      25.346  -9.094   4.047  1.00 22.09           C  
ATOM   2474  O   THR B 156      24.287  -9.445   4.526  1.00 19.33           O  
ATOM   2475  CB  THR B 156      27.121  -9.847   5.605  1.00 21.30           C  
ATOM   2476  OG1 THR B 156      27.548  -8.494   5.861  1.00 19.36           O  
ATOM   2477  CG2 THR B 156      28.260 -10.809   5.804  1.00 21.25           C  
ATOM   2478  N   TYR B 157      25.514  -7.959   3.357  1.00 21.92           N  
ATOM   2479  CA  TYR B 157      24.382  -7.049   3.070  1.00 24.74           C  
ATOM   2480  C   TYR B 157      23.416  -7.581   2.005  1.00 26.73           C  
ATOM   2481  O   TYR B 157      22.342  -7.010   1.856  1.00 31.23           O  
ATOM   2482  CB  TYR B 157      24.875  -5.646   2.687  1.00 23.00           C  
ATOM   2483  CG  TYR B 157      25.224  -4.729   3.860  1.00 23.36           C  
ATOM   2484  CD1 TYR B 157      26.509  -4.708   4.421  1.00 21.71           C  
ATOM   2485  CD2 TYR B 157      24.264  -3.846   4.375  1.00 23.34           C  
ATOM   2486  CE1 TYR B 157      26.825  -3.831   5.463  1.00 23.28           C  
ATOM   2487  CE2 TYR B 157      24.570  -2.957   5.408  1.00 25.23           C  
ATOM   2488  CZ  TYR B 157      25.847  -2.950   5.956  1.00 23.86           C  
ATOM   2489  OH  TYR B 157      26.133  -2.080   6.998  1.00 23.77           O  
ATOM   2490  N   ARG B 158      23.808  -8.628   1.260  1.00 30.04           N  
ATOM   2491  CA  ARG B 158      22.915  -9.403   0.360  1.00 35.42           C  
ATOM   2492  C   ARG B 158      22.472 -10.714   1.015  1.00 38.17           C  
ATOM   2493  O   ARG B 158      21.335 -10.847   1.446  1.00 42.77           O  
ATOM   2494  CB  ARG B 158      23.627  -9.771  -0.941  1.00 36.89           C  
ATOM   2495  CG  ARG B 158      24.336  -8.616  -1.632  1.00 40.77           C  
ATOM   2496  CD  ARG B 158      23.359  -7.613  -2.238  1.00 43.73           C  
ATOM   2497  NE  ARG B 158      24.062  -6.415  -2.702  1.00 46.67           N  
ATOM   2498  CZ  ARG B 158      24.218  -5.262  -2.027  1.00 49.65           C  
ATOM   2499  NH1 ARG B 158      23.699  -5.054  -0.804  1.00 45.09           N  
ATOM   2500  NH2 ARG B 158      24.907  -4.280  -2.606  1.00 46.70           N  
TER    2501      ARG B 158                                                      
HETATM 9991  CHA HEM A 200      30.511  -3.317 -19.462  1.00 16.28           C  
HETATM 9992  CHB HEM A 200      33.479  -1.017 -16.411  1.00 15.83           C  
HETATM 9993  CHC HEM A 200      33.995  -5.255 -14.038  1.00 14.76           C  
HETATM 9994  CHD HEM A 200      32.085  -7.593 -17.787  1.00 15.63           C  
HETATM 9995  C1A HEM A 200      31.234  -2.333 -18.820  1.00 16.79           C  
HETATM 9996  C2A HEM A 200      31.262  -0.973 -19.177  1.00 17.46           C  
HETATM 9997  C3A HEM A 200      32.130  -0.335 -18.360  1.00 16.72           C  
HETATM 9998  C4A HEM A 200      32.618  -1.293 -17.448  1.00 15.56           C  
HETATM 9999  CMA HEM A 200      32.497   1.138 -18.414  1.00 16.92           C  
HETATM10000  CAA HEM A 200      30.555  -0.332 -20.355  1.00 21.36           C  
HETATM10001  CBA HEM A 200      29.071  -0.111 -20.163  1.00 23.37           C  
HETATM10002  CGA HEM A 200      28.546   0.493 -21.455  1.00 28.34           C  
HETATM10003  O1A HEM A 200      27.817   1.517 -21.397  1.00 33.51           O  
HETATM10004  O2A HEM A 200      28.875  -0.009 -22.582  1.00 31.90           O  
HETATM10005  C1B HEM A 200      33.850  -1.979 -15.445  1.00 15.67           C  
HETATM10006  C2B HEM A 200      34.574  -1.680 -14.252  1.00 16.50           C  
HETATM10007  C3B HEM A 200      34.728  -2.860 -13.543  1.00 15.67           C  
HETATM10008  C4B HEM A 200      34.062  -3.897 -14.358  1.00 15.18           C  
HETATM10009  CMB HEM A 200      35.068  -0.286 -13.888  1.00 17.15           C  
HETATM10010  CAB HEM A 200      35.420  -3.189 -12.271  1.00 16.53           C  
HETATM10011  CBB HEM A 200      36.288  -2.392 -11.642  1.00 19.50           C  
HETATM10012  C1C HEM A 200      33.557  -6.299 -14.860  1.00 14.65           C  
HETATM10013  C2C HEM A 200      33.766  -7.685 -14.642  1.00 14.94           C  
HETATM10014  C3C HEM A 200      33.242  -8.377 -15.706  1.00 14.69           C  
HETATM10015  C4C HEM A 200      32.736  -7.364 -16.602  1.00 14.90           C  
HETATM10016  CMC HEM A 200      34.431  -8.284 -13.413  1.00 15.75           C  
HETATM10017  CAC HEM A 200      33.164  -9.841 -16.018  1.00 16.28           C  
HETATM10018  CBC HEM A 200      33.747 -10.868 -15.410  1.00 17.80           C  
HETATM10019  C1D HEM A 200      31.467  -6.583 -18.517  1.00 16.72           C  
HETATM10020  C2D HEM A 200      30.585  -6.891 -19.651  1.00 19.26           C  
HETATM10021  C3D HEM A 200      30.120  -5.712 -20.110  1.00 19.87           C  
HETATM10022  C4D HEM A 200      30.745  -4.676 -19.240  1.00 17.58           C  
HETATM10023  CMD HEM A 200      30.292  -8.261 -20.210  1.00 18.70           C  
HETATM10024  CAD HEM A 200      29.222  -5.511 -21.316  1.00 21.74           C  
HETATM10025  CBD HEM A 200      27.796  -5.959 -21.069  1.00 25.33           C  
HETATM10026  CGD HEM A 200      26.980  -5.718 -22.322  1.00 31.00           C  
HETATM10027  O1D HEM A 200      27.220  -6.379 -23.364  1.00 34.07           O  
HETATM10028  O2D HEM A 200      26.079  -4.837 -22.335  1.00 36.42           O  
HETATM10029  NA  HEM A 200      32.097  -2.532 -17.749  1.00 16.03           N  
HETATM10030  NB  HEM A 200      33.551  -3.293 -15.453  1.00 16.15           N  
HETATM10031  NC  HEM A 200      33.005  -6.137 -16.076  1.00 15.24           N  
HETATM10032  ND  HEM A 200      31.534  -5.245 -18.303  1.00 17.19           N  
HETATM10033 FE   HEM A 200      32.497  -4.319 -16.938  1.00 14.45          FE  
HETATM10034  C   CYN A 201      34.060  -4.478 -18.204  1.00 15.79           C  
HETATM10035  N   CYN A 201      34.933  -4.212 -19.114  1.00 18.33           N  
HETATM10036 CL    CL B 202      53.425   4.062  -2.003  1.00 23.34          CL  
HETATM10037  CHA HEM B 200      30.909  -3.588  15.940  1.00 17.86           C  
HETATM10038  CHB HEM B 200      34.630  -3.694  12.773  1.00 15.08           C  
HETATM10039  CHC HEM B 200      32.565   0.044  10.408  1.00 15.12           C  
HETATM10040  CHD HEM B 200      29.717   0.838  14.290  1.00 16.39           C  
HETATM10041  C1A HEM B 200      32.065  -3.974  15.270  1.00 16.94           C  
HETATM10042  C2A HEM B 200      32.928  -5.036  15.633  1.00 18.27           C  
HETATM10043  C3A HEM B 200      33.994  -5.030  14.763  1.00 16.79           C  
HETATM10044  C4A HEM B 200      33.792  -3.970  13.846  1.00 15.59           C  
HETATM10045  CMA HEM B 200      35.175  -5.969  14.722  1.00 16.48           C  
HETATM10046  CAA HEM B 200      32.712  -5.956  16.811  1.00 21.63           C  
HETATM10047  CBA HEM B 200      31.710  -7.059  16.486  1.00 23.83           C  
HETATM10048  CGA HEM B 200      31.832  -8.076  17.597  1.00 29.46           C  
HETATM10049  O1A HEM B 200      32.466  -9.144  17.401  1.00 30.10           O  
HETATM10050  O2A HEM B 200      31.351  -7.833  18.733  1.00 32.05           O  
HETATM10051  C1B HEM B 200      34.368  -2.713  11.818  1.00 14.89           C  
HETATM10052  C2B HEM B 200      35.131  -2.562  10.630  1.00 15.22           C  
HETATM10053  C3B HEM B 200      34.565  -1.542   9.930  1.00 15.56           C  
HETATM10054  C4B HEM B 200      33.396  -1.050  10.748  1.00 15.42           C  
HETATM10055  CMB HEM B 200      36.359  -3.382  10.236  1.00 15.44           C  
HETATM10056  CAB HEM B 200      34.994  -0.910   8.665  1.00 15.53           C  
HETATM10057  CBB HEM B 200      36.211  -1.022   8.142  1.00 17.45           C  
HETATM10058  C1C HEM B 200      31.639   0.630  11.291  1.00 15.73           C  
HETATM10059  C2C HEM B 200      30.994   1.890  11.110  1.00 16.28           C  
HETATM10060  C3C HEM B 200      30.204   2.116  12.220  1.00 16.07           C  
HETATM10061  C4C HEM B 200      30.368   1.006  13.089  1.00 16.14           C  
HETATM10062  CMC HEM B 200      31.181   2.796   9.911  1.00 14.30           C  
HETATM10063  CAC HEM B 200      29.371   3.307  12.524  1.00 17.82           C  
HETATM10064  CBC HEM B 200      29.465   4.482  11.915  1.00 18.88           C  
HETATM10065  C1D HEM B 200      29.796  -0.354  15.022  1.00 17.24           C  
HETATM10066  C2D HEM B 200      28.911  -0.607  16.176  1.00 18.30           C  
HETATM10067  C3D HEM B 200      29.236  -1.832  16.631  1.00 20.02           C  
HETATM10068  C4D HEM B 200      30.315  -2.339  15.737  1.00 17.66           C  
HETATM10069  CMD HEM B 200      27.873   0.299  16.802  1.00 17.65           C  
HETATM10070  CAD HEM B 200      28.592  -2.504  17.821  1.00 25.86           C  
HETATM10071  CBD HEM B 200      27.298  -3.219  17.423  1.00 31.66           C  
HETATM10072  CGD HEM B 200      26.580  -3.838  18.625  1.00 37.50           C  
HETATM10073  O1D HEM B 200      25.349  -3.651  18.867  1.00 42.19           O  
HETATM10074  O2D HEM B 200      27.218  -4.575  19.389  1.00 40.73           O  
HETATM10075  NA  HEM B 200      32.644  -3.303  14.192  1.00 15.54           N  
HETATM10076  NB  HEM B 200      33.333  -1.812  11.841  1.00 15.46           N  
HETATM10077  NC  HEM B 200      31.272   0.147  12.510  1.00 15.70           N  
HETATM10078  ND  HEM B 200      30.632  -1.411  14.807  1.00 17.10           N  
HETATM10079 FE   HEM B 200      31.920  -1.609  13.399  1.00 15.65          FE  
HETATM10080  C   CYN B 201      33.386  -0.460  14.329  1.00 13.82           C  
HETATM10081  N   CYN B 201      33.947  -0.173  15.453  1.00 14.35           N  
HETATM10352  O   HOH A 301      21.083  -1.078 -17.462  0.50 26.73           O  
HETATM10353  O   HOH A 302      38.745  20.235  -9.574  1.00 23.36           O  
HETATM10354  O   HOH A 303      21.433  -7.504  -6.700  1.00 31.03           O  
HETATM10355  O   HOH A 304      28.681  -8.063 -24.484  1.00 41.03           O  
HETATM10356  O   HOH A 305      46.630  17.893  -4.742  1.00 30.24           O  
HETATM10357  O   HOH A 306      51.593  15.087   1.843  1.00 29.51           O  
HETATM10358  O   HOH A 307      44.807  13.738  -1.679  1.00 24.49           O  
HETATM10359  O   HOH A 308      40.436 -19.760 -16.600  1.00 35.89           O  
HETATM10360  O   HOH A 309      59.021  11.474  -8.650  1.00 18.26           O  
HETATM10361  O   HOH A 310      27.946 -15.538 -20.013  1.00 30.60           O  
HETATM10362  O   HOH A 311      56.746   5.016 -14.882  1.00 34.28           O  
HETATM10363  O   HOH A 312      44.827  -3.002 -24.167  1.00 21.39           O  
HETATM10364  O   HOH A 313      29.136  15.410   7.664  1.00 37.70           O  
HETATM10365  O   HOH A 314      63.840  13.873  -4.839  1.00 25.79           O  
HETATM10366  O   HOH A 315      61.327   5.332  -2.402  1.00 26.13           O  
HETATM10367  O   HOH A 316      48.790   7.475   2.773  1.00 32.96           O  
HETATM10368  O   HOH A 317      46.183   4.493  -3.126  1.00 25.47           O  
HETATM10369  O   HOH A 318      45.450  -8.159  -7.947  1.00 23.64           O  
HETATM10370  O   HOH A 319      40.133  -8.904 -28.982  1.00 23.17           O  
HETATM10371  O   HOH A 320      31.091   3.350  -9.542  1.00 21.57           O  
HETATM10372  O   HOH A 321      28.489 -11.282 -19.790  1.00 25.51           O  
HETATM10373  O   HOH A 322      45.919  13.412   1.326  1.00 28.61           O  
HETATM10374  O   HOH A 323      44.465 -18.269 -13.931  1.00 39.21           O  
HETATM10375  O   HOH A 324      38.607  17.789 -13.906  1.00 29.72           O  
HETATM10376  O   HOH A 325      39.707 -17.995 -20.947  1.00 16.02           O  
HETATM10377  O   HOH A 326      30.112   1.834 -11.464  1.00 40.68           O  
HETATM10378  O   HOH A 327      44.565  -2.912 -14.712  1.00 14.55           O  
HETATM10379  O   HOH A 328      62.311  10.473  -2.758  1.00 34.25           O  
HETATM10380  O   HOH A 329      44.749 -14.949 -18.696  1.00 19.81           O  
HETATM10381  O   HOH A 330      50.178   4.268 -25.104  1.00 24.92           O  
HETATM10382  O   HOH A 331      29.937  -9.683 -29.612  1.00 35.78           O  
HETATM10383  O   HOH A 332      33.515   3.917 -20.864  1.00 17.37           O  
HETATM10384  O   HOH A 333      38.863  12.821 -18.189  1.00 27.85           O  
HETATM10385  O   HOH A 334      35.646  18.092 -10.735  1.00 30.06           O  
HETATM10386  O   HOH A 335      34.843  -1.425 -20.359  1.00 17.45           O  
HETATM10387  O   HOH A 336      29.501 -12.338 -23.098  1.00 25.15           O  
HETATM10388  O   HOH A 337      24.351 -13.112 -18.418  1.00 33.37           O  
HETATM10389  O   HOH A 338      41.403  16.701 -16.781  1.00 23.66           O  
HETATM10390  O   HOH A 339      24.704   2.131  -0.642  1.00 24.95           O  
HETATM10391  O   HOH A 340      47.031  -3.361 -13.431  1.00 14.54           O  
HETATM10392  O   HOH A 341      33.050  -9.546 -34.678  1.00 39.66           O  
HETATM10393  O   HOH A 342      41.972  -7.017 -27.780  1.00 18.46           O  
HETATM10394  O   HOH A 343      36.171   5.674  10.142  1.00 18.94           O  
HETATM10395  O   HOH A 344      47.400  -7.284  -9.651  1.00 23.19           O  
HETATM10396  O   HOH A 345      56.780  -0.962 -14.397  1.00 41.11           O  
HETATM10397  O   HOH A 346      45.176   5.964 -22.821  1.00 32.50           O  
HETATM10398  O   HOH A 347      31.030  10.364 -20.213  1.00 31.83           O  
HETATM10399  O   HOH A 348      46.546  18.998 -11.305  1.00 17.93           O  
HETATM10400  O   HOH A 349      48.190  -8.440 -19.431  1.00 32.17           O  
HETATM10401  O   HOH A 350      29.912 -15.061 -29.503  1.00 24.38           O  
HETATM10402  O   HOH A 351      31.505  20.181 -13.101  1.00 35.28           O  
HETATM10403  O   HOH A 352      22.107  -9.595 -10.974  1.00 36.60           O  
HETATM10404  O   HOH A 353      32.235   2.693 -12.516  1.00 16.55           O  
HETATM10405  O   HOH A 354      43.159 -14.727 -13.608  1.00 21.45           O  
HETATM10406  O   HOH A 355      31.448  -4.849 -33.246  1.00 22.82           O  
HETATM10407  O   HOH A 356      19.446   3.985  -6.407  1.00 41.92           O  
HETATM10408  O   HOH A 357      46.662  -9.447 -15.177  1.00 31.89           O  
HETATM10409  O   HOH A 358      44.352   2.330  -3.294  1.00 14.41           O  
HETATM10410  O   HOH A 359      40.502  -2.193 -28.388  1.00 15.13           O  
HETATM10411  O   HOH A 360      35.888  19.067  -5.059  1.00 43.51           O  
HETATM10412  O   HOH A 361      57.513  -0.016 -10.293  1.00 45.82           O  
HETATM10413  O   HOH A 362      49.635  11.837 -21.081  1.00 22.95           O  
HETATM10414  O   HOH A 363      48.156  10.466   4.646  1.00 28.90           O  
HETATM10415  O   HOH A 364      38.744   4.964 -25.313  1.00 18.75           O  
HETATM10416  O   HOH A 365      34.947 -12.156 -25.330  1.00 39.96           O  
HETATM10417  O   HOH A 366      33.397  13.519   7.633  1.00 32.11           O  
HETATM10418  O   HOH A 367      40.575 -11.284 -27.454  0.50 12.41           O  
HETATM10419  O   HOH A 368      46.557  -4.179  -4.267  1.00 10.08           O  
HETATM10420  O   HOH A 369      41.552  19.787  -0.683  1.00 35.77           O  
HETATM10421  O   HOH A 370      59.837   8.122 -12.976  1.00 33.05           O  
HETATM10422  O   HOH A 371      27.956 -17.321 -16.253  1.00 34.49           O  
HETATM10423  O   HOH A 372      45.728  16.349 -16.610  1.00 43.28           O  
HETATM10424  O   HOH A 373      48.405  16.289 -16.167  1.00 46.35           O  
HETATM10425  O   HOH A 374      54.561   8.668 -18.077  1.00 35.93           O  
HETATM10426  O   HOH A 375      22.593   1.072 -17.245  1.00 32.33           O  
HETATM10427  O   HOH A 376      30.667 -14.882 -14.396  1.00 47.80           O  
HETATM10428  O   HOH A 377      23.974   8.926   0.974  1.00 42.98           O  
HETATM10429  O   HOH A 378      24.305 -10.965  -9.860  1.00 45.76           O  
HETATM10430  O   HOH A 379      50.128   0.910 -22.392  1.00 19.92           O  
HETATM10431  O   HOH A 380      54.682   9.131   0.468  1.00 23.84           O  
HETATM10432  O   HOH A 381      57.255  15.688  -9.512  1.00 27.21           O  
HETATM10433  O   HOH A 382      53.499   9.137   3.200  1.00 29.54           O  
HETATM10434  O   HOH A 383      28.045  18.398  -9.441  1.00 38.28           O  
HETATM10435  O   HOH A 384      44.718 -13.643 -23.241  1.00 34.11           O  
HETATM10436  O   HOH A 385      31.834  -5.147 -25.596  1.00 30.28           O  
HETATM10437  O   HOH A 386      25.430 -10.710  -7.065  1.00 22.63           O  
HETATM10438  O   HOH A 387      43.358  15.181 -16.898  1.00 44.96           O  
HETATM10439  O   HOH A 388      35.131 -11.010 -33.207  1.00 37.09           O  
HETATM10440  O   HOH A 389      41.005  20.838  -8.324  1.00 36.89           O  
HETATM10441  O   HOH A 390      51.045   4.188  -4.466  1.00 18.66           O  
HETATM10442  O   HOH A 391      42.995  -9.147 -22.976  1.00 35.05           O  
HETATM10443  O   HOH A 392      33.468  13.481 -16.158  1.00 28.09           O  
HETATM10444  O   HOH A 393      43.127 -10.154 -25.421  0.50 20.61           O  
HETATM10445  O   HOH A 394      47.075  20.136  -3.054  1.00 35.77           O  
HETATM10446  O   HOH A 395      32.131  -1.816 -24.653  1.00 26.48           O  
HETATM10447  O   HOH A 396      37.482  21.619  -1.603  1.00 29.31           O  
HETATM10448  O   HOH A 397      43.496   8.093 -22.813  1.00 28.48           O  
HETATM10449  O   HOH A 398      32.881  -6.605 -35.235  1.00 35.49           O  
HETATM10450  O   HOH A 399      32.232  11.064 -16.656  1.00 25.89           O  
HETATM10451  O   HOH A 400      44.601  20.587 -11.812  1.00 28.53           O  
HETATM10452  O   HOH A 401      27.060  17.656 -13.458  1.00 45.31           O  
HETATM10453  O   HOH A 402      52.708   0.216 -20.899  1.00 33.39           O  
HETATM10454  O   HOH A 403      47.844  -5.271 -11.597  1.00 29.95           O  
HETATM10455  O   HOH A 404      56.430  19.015  -1.684  1.00 30.49           O  
HETATM10456  O   HOH A 405      51.053  -4.013 -11.252  1.00 24.76           O  
HETATM10457  O   HOH A 406      19.121  -8.356 -12.648  1.00 43.19           O  
HETATM10458  O   HOH A 407      52.895  13.748 -17.193  1.00 40.23           O  
HETATM10459  O   HOH A 408      55.974  12.530 -16.317  1.00 40.54           O  
HETATM10460  O   HOH A 409      47.030  15.342 -18.786  1.00 35.51           O  
HETATM10461  O   HOH A 410      37.395  14.144   6.371  1.00 40.08           O  
HETATM10462  O   HOH A 411      45.325   5.291   0.280  1.00 24.01           O  
HETATM10463  O   HOH A 412      42.810 -18.715 -11.410  1.00 34.80           O  
HETATM10464  O   HOH A 413      39.717  -7.267 -31.868  1.00 28.39           O  
HETATM10465  O   HOH A 414      47.719 -12.647 -10.917  1.00 29.56           O  
HETATM10466  O   HOH A 415      23.411  -9.153  -5.239  1.00 42.11           O  
HETATM10467  O   HOH A 416      45.097  16.496  -1.278  1.00 26.13           O  
HETATM10468  O   HOH A 417      46.576 -12.258 -15.500  1.00 38.63           O  
HETATM10469  O   HOH A 418      27.985 -12.064 -25.393  1.00 36.87           O  
HETATM10470  O   HOH A 419      51.017  -6.822 -19.394  1.00 39.78           O  
HETATM10471  O   HOH A 420      41.516  -0.215 -26.679  1.00 17.32           O  
HETATM10472  O   HOH A 421      39.455   7.385 -23.927  1.00 24.29           O  
HETATM10473  O   HOH A 422      30.350  12.484 -17.276  1.00 32.97           O  
HETATM10474  O   HOH A 423      40.560 -10.993 -34.359  1.00 21.67           O  
HETATM10475  O   HOH A 424      44.060 -14.046 -27.953  1.00 33.03           O  
HETATM10476  O   HOH A 425      18.811  -5.617 -13.806  1.00 40.16           O  
HETATM10477  O   HOH A 426      45.953  20.426  -0.520  1.00 40.83           O  
HETATM10478  O   HOH A 427      45.562 -14.748 -14.734  1.00 25.02           O  
HETATM10479  O   HOH A 428      30.895  -8.906 -33.102  1.00 40.57           O  
HETATM10480  O   HOH A 429      56.405   8.361 -14.829  1.00 30.91           O  
HETATM10481  O   HOH A 430      28.321 -14.182 -15.370  1.00 29.08           O  
HETATM10482  O   HOH A 431      49.668  -8.569  -8.814  1.00 31.59           O  
HETATM10483  O   HOH A 432      41.675 -11.474 -25.843  0.50 12.44           O  
HETATM10484  O   HOH A 433      45.607   9.435 -23.370  1.00 37.63           O  
HETATM10485  O   HOH A 434      23.797 -11.534 -20.656  1.00 37.67           O  
HETATM10486  O   HOH A 435      33.832  17.671   6.758  1.00 41.71           O  
HETATM10487  O   HOH A 436      41.812  -4.501 -28.832  1.00 22.34           O  
HETATM10488  O   HOH A 437      60.559   3.703 -11.083  1.00 30.82           O  
HETATM10489  O   HOH A 438      26.340 -10.320 -21.445  1.00 44.16           O  
HETATM10490  O   HOH A 439      44.634  -7.939 -29.285  1.00 26.85           O  
HETATM10491  O   HOH A 440      33.301  19.697 -10.916  1.00 30.27           O  
HETATM10492  O   HOH A 441      51.008  -0.089 -24.776  1.00 28.00           O  
HETATM10493  O   HOH A 442      25.250 -13.384  -6.945  1.00 30.85           O  
HETATM10494  O   HOH A 443      20.536   2.702 -15.940  1.00 34.20           O  
HETATM10495  O   HOH A 444      48.812 -13.086 -17.183  1.00 31.84           O  
HETATM10496  O   HOH A 445      47.420 -14.408 -24.000  1.00 34.15           O  
HETATM10497  O   HOH A 446      41.826  -9.057 -32.727  1.00 35.20           O  
HETATM10498  O   HOH A 447      44.346  -3.581 -28.488  1.00 26.64           O  
HETATM10499  O   HOH A 448      43.954  -1.410 -26.450  1.00 35.30           O  
HETATM10500  O   HOH A 449      45.095   4.873 -25.446  1.00 32.49           O  
HETATM10501  O   HOH A 450      41.829   2.295 -27.563  1.00 27.75           O  
HETATM10502  O   HOH A 451      51.323 -13.242 -21.467  1.00 37.03           O  
HETATM10503  O   HOH A 452      44.592   3.048 -27.228  1.00 28.21           O  
HETATM10504  O   HOH A 453      45.656   0.357 -27.643  1.00 31.49           O  
HETATM10505  O   HOH B 301      58.327  -1.879  14.500  1.00 30.38           O  
HETATM10506  O   HOH B 302      41.988   6.584  21.375  1.00 31.47           O  
HETATM10507  O   HOH B 303      63.580  -2.496   8.249  1.00 30.39           O  
HETATM10508  O   HOH B 304      60.756  -9.649   1.221  1.00 31.52           O  
HETATM10509  O   HOH B 305      58.765  -4.129  12.384  1.00 31.09           O  
HETATM10510  O   HOH B 306      57.792  -9.632   3.222  1.00 38.28           O  
HETATM10511  O   HOH B 307      21.474   6.460  12.380  1.00 48.54           O  
HETATM10512  O   HOH B 308      56.460 -17.749   3.339  1.00 34.24           O  
HETATM10513  O   HOH B 309      59.717   7.719  -2.117  1.00 24.72           O  
HETATM10514  O   HOH B 310      41.335 -14.491  16.056  1.00 37.51           O  
HETATM10515  O   HOH B 311      56.503 -14.435   7.622  1.00 26.65           O  
HETATM10516  O   HOH B 312      24.915  -1.136  19.418  1.00 41.83           O  
HETATM10517  O   HOH B 313      52.001   7.356   9.733  1.00 25.24           O  
HETATM10518  O   HOH B 314      34.976  -8.645   5.731  1.00 34.31           O  
HETATM10519  O   HOH B 315      35.252  -2.466  16.801  1.00 19.07           O  
HETATM10520  O   HOH B 316      49.125 -17.541   7.010  1.00 31.14           O  
HETATM10521  O   HOH B 317      52.911  -3.551  -8.422  1.00 26.17           O  
HETATM10522  O   HOH B 318      30.102   4.574  30.961  1.00 31.87           O  
HETATM10523  O   HOH B 319      29.139  -6.164  18.465  1.00 37.30           O  
HETATM10524  O   HOH B 320      52.498  -8.730  -2.573  1.00 16.06           O  
HETATM10525  O   HOH B 321      48.001  -0.499  -0.788  1.00 29.29           O  
HETATM10526  O   HOH B 322      39.719  -7.647 -13.955  1.00 11.18           O  
HETATM10527  O   HOH B 323      65.321  -5.611  -1.898  1.00 39.59           O  
HETATM10528  O   HOH B 324      26.355  10.314  18.339  1.00 35.47           O  
HETATM10529  O   HOH B 325      24.347   1.597  15.396  1.00 20.88           O  
HETATM10530  O   HOH B 326      55.731   2.772   9.610  1.00 28.61           O  
HETATM10531  O   HOH B 327      23.492 -11.409   6.204  1.00 39.22           O  
HETATM10532  O   HOH B 328      29.700   6.217  21.594  1.00 25.19           O  
HETATM10533  O   HOH B 329      57.386  -4.257  16.003  1.00 39.17           O  
HETATM10534  O   HOH B 330      67.550  -0.555  -0.213  1.00 32.26           O  
HETATM10535  O   HOH B 331      28.564  -0.920  20.901  1.00 44.24           O  
HETATM10536  O   HOH B 332      42.992   4.424  20.638  1.00 25.64           O  
HETATM10537  O   HOH B 333      37.945 -12.101  13.986  1.00 29.59           O  
HETATM10538  O   HOH B 334      27.156   0.863  -1.302  1.00 25.25           O  
HETATM10539  O   HOH B 335      57.118 -11.616   6.962  1.00 17.55           O  
HETATM10540  O   HOH B 336      51.606  -1.321  -6.884  1.00 30.78           O  
HETATM10541  O   HOH B 337      48.495  -2.679  19.011  1.00 25.76           O  
HETATM10542  O   HOH B 338      44.127   6.176   9.663  1.00 14.88           O  
HETATM10543  O   HOH B 339      42.220   9.519   5.740  1.00 25.38           O  
HETATM10544  O   HOH B 340      54.548  -8.884  14.103  1.00 34.05           O  
HETATM10545  O   HOH B 341      34.809   4.347  30.108  1.00 14.51           O  
HETATM10546  O   HOH B 342      43.086   6.717   0.391  1.00 12.74           O  
HETATM10547  O   HOH B 343      25.454   2.565  19.113  1.00 24.36           O  
HETATM10548  O   HOH B 344      58.263  -5.931  -6.026  1.00 24.77           O  
HETATM10549  O   HOH B 345      40.237 -19.548 -11.178  1.00 26.12           O  
HETATM10550  O   HOH B 346      34.592  13.392  10.149  1.00 27.16           O  
HETATM10551  O   HOH B 347      52.131 -17.873   4.933  1.00 29.65           O  
HETATM10552  O   HOH B 348      40.008   9.224   4.149  1.00 22.53           O  
HETATM10553  O   HOH B 349      56.500 -10.535   0.482  1.00 27.68           O  
HETATM10554  O   HOH B 350      46.060 -13.094  14.076  1.00 31.33           O  
HETATM10555  O   HOH B 351      34.012  17.120  10.850  1.00 43.56           O  
HETATM10556  O   HOH B 352      42.655   4.429  10.795  1.00 12.30           O  
HETATM10557  O   HOH B 353      35.721  -7.601   8.806  1.00 12.66           O  
HETATM10558  O   HOH B 354      42.481  -5.534  21.602  1.00 11.66           O  
HETATM10559  O   HOH B 355      20.426  -3.475   7.479  1.00 25.09           O  
HETATM10560  O   HOH B 356      18.897   0.606  13.020  1.00 32.88           O  
HETATM10561  O   HOH B 357      51.536   5.691  17.297  1.00 29.05           O  
HETATM10562  O   HOH B 358      35.475 -19.776  -9.632  1.00 41.87           O  
HETATM10563  O   HOH B 359      62.791   1.658   4.380  1.00 42.03           O  
HETATM10564  O   HOH B 360      51.475 -12.537  -4.411  1.00 42.09           O  
HETATM10565  O   HOH B 361      30.428  -8.847  -2.251  1.00 14.37           O  
HETATM10566  O   HOH B 362      67.079   3.423   0.320  1.00 25.37           O  
HETATM10567  O   HOH B 363      40.031   1.584  24.600  1.00 17.81           O  
HETATM10568  O   HOH B 364      53.072  -7.923  -5.400  1.00 28.81           O  
HETATM10569  O   HOH B 365      51.881 -18.792  -2.853  1.00 32.07           O  
HETATM10570  O   HOH B 366      27.034 -11.613  13.564  1.00 39.14           O  
HETATM10571  O   HOH B 367      33.104 -12.772  14.049  1.00 30.57           O  
HETATM10572  O   HOH B 368      43.339 -15.983  11.780  1.00 32.90           O  
HETATM10573  O   HOH B 369      49.372   6.302   9.489  1.00 18.76           O  
HETATM10574  O   HOH B 370      29.169 -11.550  -2.746  1.00 23.95           O  
HETATM10575  O   HOH B 371      24.901  14.170  13.861  1.00 35.78           O  
HETATM10576  O   HOH B 372      47.575   8.235   9.630  1.00 32.72           O  
HETATM10577  O   HOH B 373      37.472  -7.734  17.294  1.00 15.69           O  
HETATM10578  O   HOH B 374      51.288 -13.464  12.424  1.00 26.84           O  
HETATM10579  O   HOH B 375      40.514  10.701  11.043  1.00 28.29           O  
HETATM10580  O   HOH B 376      53.545 -15.325  -3.703  1.00 35.52           O  
HETATM10581  O   HOH B 377      57.619   0.811  -4.488  1.00 26.42           O  
HETATM10582  O   HOH B 378      22.509  -0.393   3.619  1.00 23.62           O  
HETATM10583  O   HOH B 379      36.266 -19.301  14.772  1.00 37.55           O  
HETATM10584  O   HOH B 380      45.193  -0.088  -0.637  1.00 17.45           O  
HETATM10585  O   HOH B 381      40.998 -22.371   4.448  1.00 42.57           O  
HETATM10586  O   HOH B 382      30.975  -0.592  29.614  1.00 16.98           O  
HETATM10587  O   HOH B 383      21.446   5.971  23.527  1.00 27.43           O  
HETATM10588  O   HOH B 384      41.406 -20.030  -3.425  1.00 42.02           O  
HETATM10589  O   HOH B 385      23.340   1.914  12.983  1.00 23.49           O  
HETATM10590  O   HOH B 386      21.838  -2.638   1.578  1.00 31.61           O  
HETATM10591  O   HOH B 387      23.791  -3.805  21.376  1.00 52.57           O  
HETATM10592  O   HOH B 388      66.527  -1.802  -2.266  1.00 36.45           O  
HETATM10593  O   HOH B 389      31.569   1.284  31.151  1.00 44.48           O  
HETATM10594  O   HOH B 390      19.706   2.992  10.717  1.00 36.50           O  
HETATM10595  O   HOH B 391      42.381 -16.070 -11.340  1.00 21.38           O  
HETATM10596  O   HOH B 392      38.184   8.738  19.222  1.00 34.47           O  
HETATM10597  O   HOH B 393      60.950   9.382   2.198  1.00 32.42           O  
HETATM10598  O   HOH B 394      49.497   4.164  18.680  1.00 25.33           O  
HETATM10599  O   HOH B 395      50.718 -17.827  11.306  1.00 35.99           O  
HETATM10600  O   HOH B 396      30.009 -16.890   9.398  1.00 33.41           O  
HETATM10601  O   HOH B 397      43.153 -10.244  17.424  1.00 32.89           O  
HETATM10602  O   HOH B 398      51.676   2.558   0.380  1.00 16.42           O  
HETATM10603  O   HOH B 399      56.541  -0.110  -7.621  1.00 27.94           O  
HETATM10604  O   HOH B 400      39.935  11.248  20.350  1.00 36.04           O  
HETATM10605  O   HOH B 401      40.191 -22.874   8.417  1.00 37.38           O  
HETATM10606  O   HOH B 402      31.204 -17.642   0.584  1.00 40.62           O  
HETATM10607  O   HOH B 403      58.035  -9.428  -5.915  1.00 33.43           O  
HETATM10608  O   HOH B 404      40.628 -20.382  14.162  1.00 26.57           O  
HETATM10609  O   HOH B 405      23.629   5.937  10.511  1.00 49.21           O  
HETATM10610  O   HOH B 406      34.664 -17.832  16.470  1.00 32.67           O  
HETATM10611  O   HOH B 407      31.709 -16.866   5.027  1.00 43.16           O  
HETATM10612  O   HOH B 408      22.995   7.645   8.645  1.00 36.89           O  
HETATM10613  O   HOH B 409      38.235   6.469  23.879  1.00 21.94           O  
HETATM10614  O   HOH B 410      35.514  -9.631  16.448  1.00 33.55           O  
HETATM10615  O   HOH B 411      47.998 -11.869  14.665  1.00 36.18           O  
HETATM10616  O   HOH B 412      63.573  -7.664  -3.741  1.00 28.63           O  
HETATM10617  O   HOH B 413      62.424  -8.070  -6.230  1.00 35.25           O  
HETATM10618  O   HOH B 414      58.959   3.115  10.013  1.00 42.33           O  
HETATM10619  O   HOH B 415      32.983  -3.902  21.085  1.00 25.39           O  
HETATM10620  O   HOH B 416      44.283  -9.494  19.511  1.00 32.59           O  
HETATM10621  O   HOH B 417      29.889 -18.348   6.606  1.00 41.22           O  
HETATM10622  O   HOH B 418      47.612  -1.850  -4.285  1.00 20.57           O  
HETATM10623  O   HOH B 419      44.241  -6.857  20.222  1.00 24.22           O  
HETATM10624  O   HOH B 420      40.823 -18.581  16.427  1.00 32.52           O  
HETATM10625  O   HOH B 421      36.550   5.624  28.103  1.00 19.37           O  
HETATM10626  O   HOH B 422      43.932   8.292   7.838  1.00 20.74           O  
HETATM10627  O   HOH B 423      29.375  -6.391  21.595  1.00 39.97           O  
HETATM10628  O   HOH B 424      62.552  -2.809   4.100  1.00 34.24           O  
HETATM10629  O   HOH B 425      31.819  15.836   7.891  1.00 45.79           O  
HETATM10630  O   HOH B 426      53.138 -15.515  12.285  1.00 36.78           O  
HETATM10631  O   HOH B 427      54.359 -10.818  -3.188  1.00 26.19           O  
HETATM10632  O   HOH B 428      46.817   9.068   7.246  1.00 32.24           O  
HETATM10633  O   HOH B 429      41.988   0.888  23.050  1.00 29.69           O  
HETATM10634  O   HOH B 430      32.477  -4.841  29.658  1.00 34.24           O  
HETATM10635  O   HOH B 431      64.178  -0.935   5.006  1.00 35.53           O  
HETATM10636  O   HOH B 432      67.208  -2.584   1.737  1.00 42.12           O  
HETATM10637  O   HOH B 433      35.315   8.961  31.058  1.00 34.58           O  
HETATM10638  O   HOH B 434      43.471  11.961   5.025  1.00 33.10           O  
HETATM10639  O   HOH B 435      30.913  -1.904  21.842  1.00 52.26           O  
HETATM10640  O   HOH B 436      42.036 -20.721  -0.807  1.00 38.38           O  
HETATM10641  O   HOH B 437      60.657  -6.844  -7.669  1.00 28.07           O  
HETATM10642  O   HOH B 438      36.891  10.050  20.979  1.00 29.48           O  
HETATM10643  O   HOH B 439      22.405   4.111  12.150  1.00 38.20           O  
HETATM10644  O   HOH B 440      32.096 -19.168   2.207  1.00 40.28           O  
HETATM10645  O   HOH B 441      29.061 -11.751  16.077  1.00 35.63           O  
HETATM10646  O   HOH B 442      36.843  14.638  10.919  1.00 31.06           O  
HETATM10647  O   HOH B 443      35.319 -11.711  15.238  1.00 28.27           O  
HETATM10648  O   HOH B 444      39.983   8.713  25.089  1.00 33.34           O  
HETATM10649  O   HOH B 445      51.345 -17.184  -5.472  1.00 47.11           O  
HETATM10650  O   HOH B 446      22.101  10.023  18.280  1.00 34.91           O  
HETATM10651  O   HOH B 447      55.581  -8.106  -6.260  1.00 38.11           O  
HETATM10652  O   HOH B 448      48.803   3.023  -3.282  1.00 27.69           O  
HETATM10653  O   HOH B 449      34.790   9.047  22.494  1.00 41.81           O  
HETATM10654  O   HOH B 450      29.769  -1.064  24.417  1.00 37.52           O  
HETATM10655  O   HOH B 451      40.081   4.379  25.019  1.00 17.80           O  
HETATM10656  O   HOH B 452      49.079   1.848  -0.734  1.00 26.66           O  
HETATM10657  O   HOH B 453      21.329   9.098  21.168  1.00 25.56           O  
HETATM10658  O   HOH B 454      47.693  -2.232  21.381  1.00 31.66           O  
HETATM10659  O   HOH B 455      42.410   4.986  24.739  1.00 21.50           O  
HETATM10660  O   HOH B 456      37.268   8.167  28.725  1.00 34.60           O  
HETATM10661  O   HOH B 457      43.805  -1.052  23.911  1.00 20.16           O  
HETATM10662  O   HOH B 458      46.420  -0.458  23.414  1.00 32.47           O  
HETATM10663  O   HOH B 459      45.814   2.165  23.833  1.00 33.33           O  
CONECT  76310033                                                                
CONECT 201210079                                                                
CONECT 324810124                                                                
CONECT 449810170                                                                
CONECT 538310217                                                                
CONECT 540610217                                                                
CONECT 574710213                                                                
CONECT 699910260                                                                
CONECT 825710303                                                                
CONECT 950910349                                                                
CONECT 9991 999510022                                                           
CONECT 9992 999810005                                                           
CONECT 99931000810012                                                           
CONECT 99941001510019                                                           
CONECT 9995 9991 999610029                                                      
CONECT 9996 9995 999710000                                                      
CONECT 9997 9996 9998 9999                                                      
CONECT 9998 9992 999710029                                                      
CONECT 9999 9997                                                                
CONECT10000 999610001                                                           
CONECT100011000010002                                                           
CONECT10002100011000310004                                                      
CONECT1000310002                                                                
CONECT1000410002                                                                
CONECT10005 99921000610030                                                      
CONECT10006100051000710009                                                      
CONECT10007100061000810010                                                      
CONECT10008 99931000710030                                                      
CONECT1000910006                                                                
CONECT100101000710011                                                           
CONECT1001110010                                                                
CONECT10012 99931001310031                                                      
CONECT10013100121001410016                                                      
CONECT10014100131001510017                                                      
CONECT10015 99941001410031                                                      
CONECT1001610013                                                                
CONECT100171001410018                                                           
CONECT1001810017                                                                
CONECT10019 99941002010032                                                      
CONECT10020100191002110023                                                      
CONECT10021100201002210024                                                      
CONECT10022 99911002110032                                                      
CONECT1002310020                                                                
CONECT100241002110025                                                           
CONECT100251002410026                                                           
CONECT10026100251002710028                                                      
CONECT1002710026                                                                
CONECT1002810026                                                                
CONECT10029 9995 999810033                                                      
CONECT10030100051000810033                                                      
CONECT10031100121001510033                                                      
CONECT10032100191002210033                                                      
CONECT10033  763100291003010031                                                 
CONECT100331003210034                                                           
CONECT100341003310035                                                           
CONECT1003510034                                                                
CONECT100371004110068                                                           
CONECT100381004410051                                                           
CONECT100391005410058                                                           
CONECT100401006110065                                                           
CONECT10041100371004210075                                                      
CONECT10042100411004310046                                                      
CONECT10043100421004410045                                                      
CONECT10044100381004310075                                                      
CONECT1004510043                                                                
CONECT100461004210047                                                           
CONECT100471004610048                                                           
CONECT10048100471004910050                                                      
CONECT1004910048                                                                
CONECT1005010048                                                                
CONECT10051100381005210076                                                      
CONECT10052100511005310055                                                      
CONECT10053100521005410056                                                      
CONECT10054100391005310076                                                      
CONECT1005510052                                                                
CONECT100561005310057                                                           
CONECT1005710056                                                                
CONECT10058100391005910077                                                      
CONECT10059100581006010062                                                      
CONECT10060100591006110063                                                      
CONECT10061100401006010077                                                      
CONECT1006210059                                                                
CONECT100631006010064                                                           
CONECT1006410063                                                                
CONECT10065100401006610078                                                      
CONECT10066100651006710069                                                      
CONECT10067100661006810070                                                      
CONECT10068100371006710078                                                      
CONECT1006910066                                                                
CONECT100701006710071                                                           
CONECT100711007010072                                                           
CONECT10072100711007310074                                                      
CONECT1007310072                                                                
CONECT1007410072                                                                
CONECT10075100411004410079                                                      
CONECT10076100511005410079                                                      
CONECT10077100581006110079                                                      
CONECT10078100651006810079                                                      
CONECT10079 2012100751007610077                                                 
CONECT100791007810080                                                           
CONECT100801007910081                                                           
CONECT1008110080                                                                
CONECT100821008610113                                                           
CONECT100831008910096                                                           
CONECT100841009910103                                                           
CONECT100851010610110                                                           
CONECT10086100821008710120                                                      
CONECT10087100861008810091                                                      
CONECT10088100871008910090                                                      
CONECT10089100831008810120                                                      
CONECT1009010088                                                                
CONECT100911008710092                                                           
CONECT100921009110093                                                           
CONECT10093100921009410095                                                      
CONECT1009410093                                                                
CONECT1009510093                                                                
CONECT10096100831009710121                                                      
CONECT10097100961009810100                                                      
CONECT10098100971009910101                                                      
CONECT10099100841009810121                                                      
CONECT1010010097                                                                
CONECT101011009810102                                                           
CONECT1010210101                                                                
CONECT10103100841010410122                                                      
CONECT10104101031010510107                                                      
CONECT10105101041010610108                                                      
CONECT10106100851010510122                                                      
CONECT1010710104                                                                
CONECT101081010510109                                                           
CONECT1010910108                                                                
CONECT10110100851011110123                                                      
CONECT10111101101011210114                                                      
CONECT10112101111011310115                                                      
CONECT10113100821011210123                                                      
CONECT1011410111                                                                
CONECT101151011210116                                                           
CONECT101161011510117                                                           
CONECT10117101161011810119                                                      
CONECT1011810117                                                                
CONECT1011910117                                                                
CONECT10120100861008910124                                                      
CONECT10121100961009910124                                                      
CONECT10122101031010610124                                                      
CONECT10123101101011310124                                                      
CONECT10124 3248101201012110122                                                 
CONECT101241012310125                                                           
CONECT101251012410126                                                           
CONECT1012610125                                                                
CONECT101281013210159                                                           
CONECT101291013510142                                                           
CONECT101301014510149                                                           
CONECT101311015210156                                                           
CONECT10132101281013310166                                                      
CONECT10133101321013410137                                                      
CONECT10134101331013510136                                                      
CONECT10135101291013410166                                                      
CONECT1013610134                                                                
CONECT101371013310138                                                           
CONECT101381013710139                                                           
CONECT10139101381014010141                                                      
CONECT1014010139                                                                
CONECT1014110139                                                                
CONECT10142101291014310167                                                      
CONECT10143101421014410146                                                      
CONECT10144101431014510147                                                      
CONECT10145101301014410167                                                      
CONECT1014610143                                                                
CONECT101471014410148                                                           
CONECT1014810147                                                                
CONECT10149101301015010168                                                      
CONECT10150101491015110153                                                      
CONECT10151101501015210154                                                      
CONECT10152101311015110168                                                      
CONECT1015310150                                                                
CONECT101541015110155                                                           
CONECT1015510154                                                                
CONECT10156101311015710169                                                      
CONECT10157101561015810160                                                      
CONECT10158101571015910161                                                      
CONECT10159101281015810169                                                      
CONECT1016010157                                                                
CONECT101611015810162                                                           
CONECT101621016110163                                                           
CONECT10163101621016410165                                                      
CONECT1016410163                                                                
CONECT1016510163                                                                
CONECT10166101321013510170                                                      
CONECT10167101421014510170                                                      
CONECT10168101491015210170                                                      
CONECT10169101561015910170                                                      
CONECT10170 4498101661016710168                                                 
CONECT101701016910854                                                           
CONECT101711017510202                                                           
CONECT101721017810185                                                           
CONECT101731018810192                                                           
CONECT101741019510199                                                           
CONECT10175101711017610209                                                      
CONECT10176101751017710180                                                      
CONECT10177101761017810179                                                      
CONECT10178101721017710209                                                      
CONECT1017910177                                                                
CONECT101801017610181                                                           
CONECT101811018010182                                                           
CONECT10182101811018310184                                                      
CONECT1018310182                                                                
CONECT1018410182                                                                
CONECT10185101721018610210                                                      
CONECT10186101851018710189                                                      
CONECT10187101861018810190                                                      
CONECT10188101731018710210                                                      
CONECT1018910186                                                                
CONECT101901018710191                                                           
CONECT1019110190                                                                
CONECT10192101731019310211                                                      
CONECT10193101921019410196                                                      
CONECT10194101931019510197                                                      
CONECT10195101741019410211                                                      
CONECT1019610193                                                                
CONECT101971019410198                                                           
CONECT1019810197                                                                
CONECT10199101741020010212                                                      
CONECT10200101991020110203                                                      
CONECT10201102001020210204                                                      
CONECT10202101711020110212                                                      
CONECT1020310200                                                                
CONECT102041020110205                                                           
CONECT102051020410206                                                           
CONECT10206102051020710208                                                      
CONECT1020710206                                                                
CONECT1020810206                                                                
CONECT10209101751017810213                                                      
CONECT10210101851018810213                                                      
CONECT10211101921019510213                                                      
CONECT10212101991020210213                                                      
CONECT10213 5747102091021010211                                                 
CONECT102131021210214                                                           
CONECT102141021310215                                                           
CONECT1021510214                                                                
CONECT10217 5383 54061102311040                                                 
CONECT102181022210249                                                           
CONECT102191022510232                                                           
CONECT102201023510239                                                           
CONECT102211024210246                                                           
CONECT10222102181022310256                                                      
CONECT10223102221022410227                                                      
CONECT10224102231022510226                                                      
CONECT10225102191022410256                                                      
CONECT1022610224                                                                
CONECT102271022310228                                                           
CONECT102281022710229                                                           
CONECT10229102281023010231                                                      
CONECT1023010229                                                                
CONECT1023110229                                                                
CONECT10232102191023310257                                                      
CONECT10233102321023410236                                                      
CONECT10234102331023510237                                                      
CONECT10235102201023410257                                                      
CONECT1023610233                                                                
CONECT102371023410238                                                           
CONECT1023810237                                                                
CONECT10239102201024010258                                                      
CONECT10240102391024110243                                                      
CONECT10241102401024210244                                                      
CONECT10242102211024110258                                                      
CONECT1024310240                                                                
CONECT102441024110245                                                           
CONECT1024510244                                                                
CONECT10246102211024710259                                                      
CONECT10247102461024810250                                                      
CONECT10248102471024910251                                                      
CONECT10249102181024810259                                                      
CONECT1025010247                                                                
CONECT102511024810252                                                           
CONECT102521025110253                                                           
CONECT10253102521025410255                                                      
CONECT1025410253                                                                
CONECT1025510253                                                                
CONECT10256102221022510260                                                      
CONECT10257102321023510260                                                      
CONECT10258102391024210260                                                      
CONECT10259102461024910260                                                      
CONECT10260 6999102561025710258                                                 
CONECT102601025911144                                                           
CONECT102611026510292                                                           
CONECT102621026810275                                                           
CONECT102631027810282                                                           
CONECT102641028510289                                                           
CONECT10265102611026610299                                                      
CONECT10266102651026710270                                                      
CONECT10267102661026810269                                                      
CONECT10268102621026710299                                                      
CONECT1026910267                                                                
CONECT102701026610271                                                           
CONECT102711027010272                                                           
CONECT10272102711027310274                                                      
CONECT1027310272                                                                
CONECT1027410272                                                                
CONECT10275102621027610300                                                      
CONECT10276102751027710279                                                      
CONECT10277102761027810280                                                      
CONECT10278102631027710300                                                      
CONECT1027910276                                                                
CONECT102801027710281                                                           
CONECT1028110280                                                                
CONECT10282102631028310301                                                      
CONECT10283102821028410286                                                      
CONECT10284102831028510287                                                      
CONECT10285102641028410301                                                      
CONECT1028610283                                                                
CONECT102871028410288                                                           
CONECT1028810287                                                                
CONECT10289102641029010302                                                      
CONECT10290102891029110293                                                      
CONECT10291102901029210294                                                      
CONECT10292102611029110302                                                      
CONECT1029310290                                                                
CONECT102941029110295                                                           
CONECT102951029410296                                                           
CONECT10296102951029710298                                                      
CONECT1029710296                                                                
CONECT1029810296                                                                
CONECT10299102651026810303                                                      
CONECT10300102751027810303                                                      
CONECT10301102821028510303                                                      
CONECT10302102891029210303                                                      
CONECT10303 8257102991030010301                                                 
CONECT103031030210304                                                           
CONECT103041030310305                                                           
CONECT1030510304                                                                
CONECT103071031110338                                                           
CONECT103081031410321                                                           
CONECT103091032410328                                                           
CONECT103101033110335                                                           
CONECT10311103071031210345                                                      
CONECT10312103111031310316                                                      
CONECT10313103121031410315                                                      
CONECT10314103081031310345                                                      
CONECT1031510313                                                                
CONECT103161031210317                                                           
CONECT103171031610318                                                           
CONECT10318103171031910320                                                      
CONECT1031910318                                                                
CONECT1032010318                                                                
CONECT10321103081032210346                                                      
CONECT10322103211032310325                                                      
CONECT10323103221032410326                                                      
CONECT10324103091032310346                                                      
CONECT1032510322                                                                
CONECT103261032310327                                                           
CONECT1032710326                                                                
CONECT10328103091032910347                                                      
CONECT10329103281033010332                                                      
CONECT10330103291033110333                                                      
CONECT10331103101033010347                                                      
CONECT1033210329                                                                
CONECT103331033010334                                                           
CONECT1033410333                                                                
CONECT10335103101033610348                                                      
CONECT10336103351033710339                                                      
CONECT10337103361033810340                                                      
CONECT10338103071033710348                                                      
CONECT1033910336                                                                
CONECT103401033710341                                                           
CONECT103411034010342                                                           
CONECT10342103411034310344                                                      
CONECT1034310342                                                                
CONECT1034410342                                                                
CONECT10345103111031410349                                                      
CONECT10346103211032410349                                                      
CONECT10347103281033110349                                                      
CONECT10348103351033810349                                                      
CONECT10349 9509103451034610347                                                 
CONECT103491034810350                                                           
CONECT103501034910351                                                           
CONECT1035110350                                                                
CONECT1085410170                                                                
CONECT1102310217                                                                
CONECT1104010217                                                                
CONECT1114410260                                                                
MASTER      619    0   19   63    0    0   41    611369    8  379  104          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.