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

Should you encounter any unexpected behaviour,
please let us know.


***  TRANSFERASE 13-SEP-02 1MQ4  ***

elNémo ID: 22012923415062383

Job options:

ID        	=	 22012923415062383
JOBID     	=	 TRANSFERASE 13-SEP-02 1MQ4
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                             13-SEP-02   1MQ4              
TITLE     CRYSTAL STRUCTURE OF AURORA-A PROTEIN KINASE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AURORA-RELATED KINASE 1;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: AURORA-A PROTEIN KINASE;                                    
COMPND   6 EC: 2.7.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE STRUCTURE, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.NOWAKOWSKI,C.N.CRONIN,D.E.MCREE,M.W.KNUTH,C.NELSON,                 
AUTHOR   2 N.P.PAVLETICH,J.RODGERS,B.-C.SANG,D.N.SCHEIBE,R.V.SWANSON,           
AUTHOR   3 D.A.THOMPSON                                                         
REVDAT   2   24-FEB-09 1MQ4    1       VERSN                                    
REVDAT   1   16-SEP-03 1MQ4    0                                                
JRNL        AUTH   J.NOWAKOWSKI,C.N.CRONIN,D.E.MCREE,M.W.KNUTH,                 
JRNL        AUTH 2 C.NELSON,N.P.PAVLETICH,J.RODGERS,B.-C.SANG,                  
JRNL        AUTH 3 D.N.SCHEIBE,R.V.SWANSON,D.A.THOMPSON                         
JRNL        TITL   STRUCTURES OF THE CANCER-RELATED AURORA-A, FAK AND           
JRNL        TITL 2 EPHA2 PROTEIN KINASES FROM NANOVOLUME                        
JRNL        TITL 3 CRYSTALLOGRAPHY                                              
JRNL        REF    STRUCTURE                     V.  10  1659 2002              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12467573                                                     
JRNL        DOI    10.1016/S0969-2126(02)00907-3                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1337                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1557                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 95                           
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2105                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 72                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.14000                                             
REMARK   3    B22 (A**2) : -1.14000                                             
REMARK   3    B33 (A**2) : 1.71000                                              
REMARK   3    B12 (A**2) : -0.57000                                             
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): 0.161         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.157         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.489         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2191 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1983 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2974 ; 1.468 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4593 ; 0.839 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   259 ; 7.693 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   323 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2386 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   466 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   449 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2384 ; 0.243 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1403 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    95 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.467 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    53 ; 0.308 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.693 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1301 ; 0.821 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2091 ; 1.612 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   890 ; 2.459 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   883 ; 4.161 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1MQ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017089.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 15                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON                        
REMARK 200  OPTICS                         : SYNCHROTRON                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200   FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1FOT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME550, NACL, BICINE, PH 9.0,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.39067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      114.78133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       86.08600            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      143.47667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.69533            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.39067            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      114.78133            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      143.47667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       86.08600            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       28.69533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     MET A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     SER A   124                                                      
REMARK 465     LYS A   125                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     THR A   287                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     SER A   391                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 127    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 171    CG   CD   CE   NZ                                   
REMARK 470     GLU A 175    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 183    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 339    CG   CD   CE   NZ                                   
REMARK 470     ARG A 375    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2097     O    HOH A  3003              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  3007     O    HOH A  3007    10555     1.40            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 307   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 202     -148.70   -125.58                                   
REMARK 500    SER A 226      -48.91     70.70                                   
REMARK 500    ARG A 255       -1.39     72.48                                   
REMARK 500    ASP A 256       42.32   -143.84                                   
REMARK 500    ASP A 274       72.25     62.49                                   
REMARK 500    PRO A 282      123.62     11.91                                   
REMARK 500    ASP A 307     -152.39   -143.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  281     PRO A  282                  -96.02                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2086  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A2001   O1B                                                    
REMARK 620 2 HOH A3004   O    93.2                                              
REMARK 620 3 HOH A3022   O    85.4  76.3                                        
REMARK 620 4 ASP A 274   OD1  78.8 152.5 128.5                                  
REMARK 620 5 ASP A 274   OD2  96.9 154.1  80.8  53.4                            
REMARK 620 6 HOH A3003   O    98.3  80.1 156.2  75.2 121.6                      
REMARK 620 7 HOH A2098   O   174.0  81.2  90.9 107.2  87.3  83.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2088  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A2001   O2A                                                    
REMARK 620 2 ADP A2001   O3B  88.8                                              
REMARK 620 3 HOH A3009   O    90.9  88.5                                        
REMARK 620 4 HOH A3070   O   171.1  83.6  84.2                                  
REMARK 620 5 ASP A 274   OD1  99.8  93.9 169.1  85.5                            
REMARK 620 6 ASN A 261   OD1  97.3 170.6  84.3  89.6  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2086                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2088                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MP8   RELATED DB: PDB                                   
REMARK 900 1MP8 IS THE CRYSTAL STRUCTURE OF FOCAL ADHESION KINASE (FAK)         
REMARK 900 RELATED ID: 1MQB   RELATED DB: PDB                                   
REMARK 900 1MQB IS THE CRYSTAL STRUCTURE OF AURORA-A PROTEIN KINASE             
DBREF  1MQ4 A  125   391  UNP    O14965   STK6_HUMAN     125    391             
SEQADV 1MQ4 GLY A  120  UNP  O14965              CLONING ARTIFACT               
SEQADV 1MQ4 ALA A  121  UNP  O14965              CLONING ARTIFACT               
SEQADV 1MQ4 MET A  122  UNP  O14965              CLONING ARTIFACT               
SEQADV 1MQ4 GLY A  123  UNP  O14965              CLONING ARTIFACT               
SEQADV 1MQ4 SER A  124  UNP  O14965              CLONING ARTIFACT               
SEQRES   1 A  272  GLY ALA MET GLY SER LYS ARG GLN TRP ALA LEU GLU ASP          
SEQRES   2 A  272  PHE GLU ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY          
SEQRES   3 A  272  ASN VAL TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE          
SEQRES   4 A  272  LEU ALA LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS          
SEQRES   5 A  272  ALA GLY VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE          
SEQRES   6 A  272  GLN SER HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR          
SEQRES   7 A  272  GLY TYR PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU          
SEQRES   8 A  272  GLU TYR ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN          
SEQRES   9 A  272  LYS LEU SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR          
SEQRES  10 A  272  ILE THR GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER          
SEQRES  11 A  272  LYS ARG VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU          
SEQRES  12 A  272  LEU LEU GLY SER ALA GLY GLU LEU LYS ILE ALA ASP PHE          
SEQRES  13 A  272  GLY TRP SER VAL HIS ALA PRO SER SER ARG ARG THR THR          
SEQRES  14 A  272  LEU CYS GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE          
SEQRES  15 A  272  GLU GLY ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER          
SEQRES  16 A  272  LEU GLY VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO          
SEQRES  17 A  272  PRO PHE GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG          
SEQRES  18 A  272  ILE SER ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR          
SEQRES  19 A  272  GLU GLY ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS          
SEQRES  20 A  272  ASN PRO SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU          
SEQRES  21 A  272  HIS PRO TRP ILE THR ALA ASN SER SER LYS PRO SER              
HET     MG  A2086       1                                                       
HET     MG  A2088       1                                                       
HET    PO4  A   1       5                                                       
HET    ADP  A2001      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  HOH   *72(H2 O)                                                     
HELIX    1   1 ALA A  129  GLU A  131  5                                   3    
HELIX    2   2 LYS A  166  GLY A  173  1                                   8    
HELIX    3   3 VAL A  174  LEU A  188  1                                  15    
HELIX    4   4 THR A  217  SER A  226  1                                  10    
HELIX    5   5 ASP A  229  LYS A  250  1                                  22    
HELIX    6   6 LYS A  258  GLU A  260  5                                   3    
HELIX    7   7 ASP A  274  SER A  278  5                                   5    
HELIX    8   8 PRO A  297  GLU A  302  1                                   6    
HELIX    9   9 GLU A  308  GLY A  325  1                                  18    
HELIX   10  10 THR A  333  VAL A  344  1                                  12    
HELIX   11  11 THR A  353  LEU A  364  1                                  12    
HELIX   12  12 ASN A  367  ARG A  371  5                                   5    
HELIX   13  13 MET A  373  GLU A  379  1                                   7    
HELIX   14  14 HIS A  380  SER A  387  1                                   8    
SHEET    1   A 5 PHE A 133  LYS A 141  0                                        
SHEET    2   A 5 ASN A 146  GLU A 152 -1  O  ARG A 151   N  GLU A 134           
SHEET    3   A 5 ILE A 158  PHE A 165 -1  O  LEU A 161   N  TYR A 148           
SHEET    4   A 5 ARG A 205  LEU A 210 -1  O  LEU A 210   N  ALA A 160           
SHEET    5   A 5 LEU A 196  HIS A 201 -1  N  PHE A 200   O  TYR A 207           
SHEET    1   B 2 VAL A 252  ILE A 253  0                                        
SHEET    2   B 2 VAL A 279  HIS A 280 -1  O  VAL A 279   N  ILE A 253           
SHEET    1   C 2 LEU A 262  LEU A 264  0                                        
SHEET    2   C 2 LEU A 270  ILE A 272 -1  O  LYS A 271   N  LEU A 263           
LINK         O1B ADP A2001                MG    MG A2086     1555   1555  1.89  
LINK         O2A ADP A2001                MG    MG A2088     1555   1555  1.91  
LINK         O3B ADP A2001                MG    MG A2088     1555   1555  1.99  
LINK        MG    MG A2086                 O   HOH A3004     1555   1555  2.38  
LINK        MG    MG A2086                 O   HOH A3022     1555   1555  2.08  
LINK        MG    MG A2086                 OD1 ASP A 274     1555   1555  2.64  
LINK        MG    MG A2086                 OD2 ASP A 274     1555   1555  2.07  
LINK        MG    MG A2086                 O   HOH A3003     1555   1555  1.98  
LINK        MG    MG A2086                 O   HOH A2098     1555   1555  1.99  
LINK        MG    MG A2088                 O   HOH A3009     1555   1555  2.04  
LINK        MG    MG A2088                 O   HOH A3070     1555   1555  2.01  
LINK        MG    MG A2088                 OD1 ASP A 274     1555   1555  1.92  
LINK        MG    MG A2088                 OD1 ASN A 261     1555   1555  2.04  
SITE     1 AC1  6 ASP A 274  ADP A2001  HOH A2098  HOH A3003                    
SITE     2 AC1  6 HOH A3004  HOH A3022                                          
SITE     1 AC2  5 ASN A 261  ASP A 274  ADP A2001  HOH A3009                    
SITE     2 AC2  5 HOH A3070                                                     
SITE     1 AC3  7 HIS A 176  ARG A 180  ARG A 255  TRP A 277                    
SITE     2 AC3  7 SER A 284  ARG A 285  THR A 288                               
SITE     1 AC4 26 LEU A 139  GLY A 140  LYS A 141  GLY A 142                    
SITE     2 AC4 26 LYS A 143  VAL A 147  ALA A 160  LYS A 162                    
SITE     3 AC4 26 LEU A 194  GLU A 211  ALA A 213  THR A 217                    
SITE     4 AC4 26 GLU A 260  ASN A 261  LEU A 263  ASP A 274                    
SITE     5 AC4 26  MG A2086   MG A2088  HOH A3001  HOH A3003                    
SITE     6 AC4 26 HOH A3009  HOH A3010  HOH A3021  HOH A3022                    
SITE     7 AC4 26 HOH A3036  HOH A3070                                          
CRYST1   80.452   80.452  172.172  90.00  90.00 120.00 P 61 2 2     12          
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      0.012430  0.007176  0.000000        0.00000                         
SCALE2      0.000000  0.014353  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005808        0.00000                         
ATOM      1  N   ARG A 126      -1.532  18.014  58.995  1.00 60.64           N  
ATOM      2  CA  ARG A 126      -0.391  18.535  59.816  1.00 60.65           C  
ATOM      3  C   ARG A 126      -0.236  17.705  61.100  1.00 60.17           C  
ATOM      4  O   ARG A 126      -1.015  17.858  62.040  1.00 60.63           O  
ATOM      5  CB  ARG A 126      -0.614  20.013  60.154  1.00 60.84           C  
ATOM      6  N   GLN A 127       0.766  16.825  61.125  1.00 59.42           N  
ATOM      7  CA  GLN A 127       0.875  15.798  62.158  1.00 58.51           C  
ATOM      8  C   GLN A 127       1.891  16.183  63.221  1.00 57.57           C  
ATOM      9  O   GLN A 127       3.068  15.843  63.115  1.00 57.67           O  
ATOM     10  CB  GLN A 127       1.269  14.454  61.539  1.00 58.72           C  
ATOM     11  N   TRP A 128       1.424  16.873  64.255  1.00 55.78           N  
ATOM     12  CA  TRP A 128       2.288  17.276  65.351  1.00 54.50           C  
ATOM     13  C   TRP A 128       2.540  16.127  66.312  1.00 52.96           C  
ATOM     14  O   TRP A 128       1.768  15.181  66.384  1.00 52.61           O  
ATOM     15  CB  TRP A 128       1.660  18.445  66.109  1.00 54.78           C  
ATOM     16  CG  TRP A 128       1.508  19.641  65.256  1.00 55.74           C  
ATOM     17  CD1 TRP A 128       0.348  20.150  64.753  1.00 57.15           C  
ATOM     18  CD2 TRP A 128       2.557  20.482  64.777  1.00 56.95           C  
ATOM     19  NE1 TRP A 128       0.611  21.268  63.997  1.00 57.17           N  
ATOM     20  CE2 TRP A 128       1.963  21.490  63.991  1.00 57.87           C  
ATOM     21  CE3 TRP A 128       3.949  20.489  64.934  1.00 57.67           C  
ATOM     22  CZ2 TRP A 128       2.709  22.491  63.367  1.00 58.82           C  
ATOM     23  CZ3 TRP A 128       4.690  21.475  64.312  1.00 58.17           C  
ATOM     24  CH2 TRP A 128       4.069  22.466  63.536  1.00 58.76           C  
ATOM     25  N   ALA A 129       3.642  16.244  67.044  1.00 51.40           N  
ATOM     26  CA  ALA A 129       3.985  15.364  68.142  1.00 50.39           C  
ATOM     27  C   ALA A 129       4.616  16.211  69.266  1.00 49.55           C  
ATOM     28  O   ALA A 129       4.999  17.350  69.049  1.00 48.48           O  
ATOM     29  CB  ALA A 129       4.948  14.298  67.667  1.00 50.23           C  
ATOM     30  N   LEU A 130       4.712  15.641  70.459  1.00 49.32           N  
ATOM     31  CA  LEU A 130       5.218  16.354  71.633  1.00 49.30           C  
ATOM     32  C   LEU A 130       6.635  16.849  71.375  1.00 48.83           C  
ATOM     33  O   LEU A 130       7.002  17.952  71.801  1.00 49.04           O  
ATOM     34  CB  LEU A 130       5.190  15.446  72.877  1.00 49.53           C  
ATOM     35  CG  LEU A 130       4.685  15.955  74.240  1.00 50.85           C  
ATOM     36  CD1 LEU A 130       5.559  15.437  75.388  1.00 50.75           C  
ATOM     37  CD2 LEU A 130       4.551  17.458  74.315  1.00 50.34           C  
ATOM     38  N   GLU A 131       7.410  16.042  70.652  1.00 47.82           N  
ATOM     39  CA  GLU A 131       8.809  16.334  70.340  1.00 47.48           C  
ATOM     40  C   GLU A 131       9.007  17.596  69.506  1.00 45.45           C  
ATOM     41  O   GLU A 131      10.105  18.119  69.456  1.00 45.39           O  
ATOM     42  CB  GLU A 131       9.473  15.141  69.618  1.00 48.30           C  
ATOM     43  CG  GLU A 131       9.011  14.933  68.175  1.00 51.71           C  
ATOM     44  CD  GLU A 131       9.388  13.563  67.605  1.00 57.28           C  
ATOM     45  OE1 GLU A 131       8.520  12.950  66.926  1.00 60.71           O  
ATOM     46  OE2 GLU A 131      10.544  13.100  67.812  1.00 60.73           O  
ATOM     47  N   ASP A 132       7.953  18.081  68.852  1.00 43.38           N  
ATOM     48  CA  ASP A 132       8.030  19.327  68.100  1.00 42.17           C  
ATOM     49  C   ASP A 132       7.972  20.592  68.964  1.00 40.99           C  
ATOM     50  O   ASP A 132       8.113  21.668  68.428  1.00 39.83           O  
ATOM     51  CB  ASP A 132       6.899  19.407  67.082  1.00 42.77           C  
ATOM     52  CG  ASP A 132       6.922  18.254  66.101  1.00 43.92           C  
ATOM     53  OD1 ASP A 132       8.031  17.817  65.703  1.00 47.27           O  
ATOM     54  OD2 ASP A 132       5.874  17.723  65.708  1.00 46.05           O  
ATOM     55  N   PHE A 133       7.786  20.446  70.276  1.00 39.95           N  
ATOM     56  CA  PHE A 133       7.572  21.571  71.193  1.00 39.92           C  
ATOM     57  C   PHE A 133       8.539  21.594  72.378  1.00 40.18           C  
ATOM     58  O   PHE A 133       8.929  20.551  72.907  1.00 39.91           O  
ATOM     59  CB  PHE A 133       6.137  21.527  71.748  1.00 39.13           C  
ATOM     60  CG  PHE A 133       5.090  21.539  70.688  1.00 40.04           C  
ATOM     61  CD1 PHE A 133       4.642  22.733  70.151  1.00 40.27           C  
ATOM     62  CD2 PHE A 133       4.581  20.338  70.179  1.00 41.10           C  
ATOM     63  CE1 PHE A 133       3.684  22.738  69.151  1.00 41.21           C  
ATOM     64  CE2 PHE A 133       3.623  20.341  69.185  1.00 40.49           C  
ATOM     65  CZ  PHE A 133       3.177  21.532  68.668  1.00 41.50           C  
ATOM     66  N   GLU A 134       8.895  22.799  72.811  1.00 40.34           N  
ATOM     67  CA  GLU A 134       9.518  22.999  74.111  1.00 40.69           C  
ATOM     68  C   GLU A 134       8.430  23.467  75.038  1.00 40.16           C  
ATOM     69  O   GLU A 134       7.727  24.423  74.730  1.00 39.77           O  
ATOM     70  CB  GLU A 134      10.600  24.043  74.000  1.00 41.26           C  
ATOM     71  CG  GLU A 134      11.675  23.661  73.007  1.00 45.76           C  
ATOM     72  CD  GLU A 134      12.869  24.575  73.079  1.00 50.01           C  
ATOM     73  OE1 GLU A 134      14.001  24.084  72.848  1.00 54.64           O  
ATOM     74  OE2 GLU A 134      12.671  25.775  73.380  1.00 54.65           O  
ATOM     75  N   ILE A 135       8.274  22.804  76.168  1.00 39.17           N  
ATOM     76  CA  ILE A 135       7.201  23.126  77.062  1.00 39.84           C  
ATOM     77  C   ILE A 135       7.708  24.015  78.200  1.00 39.42           C  
ATOM     78  O   ILE A 135       8.826  23.870  78.670  1.00 38.13           O  
ATOM     79  CB  ILE A 135       6.569  21.850  77.570  1.00 40.38           C  
ATOM     80  CG1 ILE A 135       5.899  21.137  76.388  1.00 42.39           C  
ATOM     81  CG2 ILE A 135       5.579  22.134  78.672  1.00 41.21           C  
ATOM     82  CD1 ILE A 135       4.867  20.140  76.790  1.00 45.86           C  
ATOM     83  N   GLY A 136       6.846  24.920  78.632  1.00 39.63           N  
ATOM     84  CA  GLY A 136       7.207  25.937  79.587  1.00 39.49           C  
ATOM     85  C   GLY A 136       6.377  25.783  80.820  1.00 39.70           C  
ATOM     86  O   GLY A 136       6.030  24.680  81.197  1.00 40.43           O  
ATOM     87  N   ARG A 137       6.054  26.911  81.434  1.00 40.30           N  
ATOM     88  CA  ARG A 137       5.303  26.934  82.675  1.00 40.56           C  
ATOM     89  C   ARG A 137       3.842  26.592  82.441  1.00 40.14           C  
ATOM     90  O   ARG A 137       3.312  26.862  81.353  1.00 38.51           O  
ATOM     91  CB  ARG A 137       5.375  28.323  83.305  1.00 41.46           C  
ATOM     92  CG  ARG A 137       4.911  29.440  82.416  1.00 42.31           C  
ATOM     93  CD  ARG A 137       4.746  30.749  83.118  1.00 45.38           C  
ATOM     94  NE  ARG A 137       3.476  30.735  83.776  1.00 47.68           N  
ATOM     95  CZ  ARG A 137       2.441  31.512  83.510  1.00 45.04           C  
ATOM     96  NH1 ARG A 137       2.468  32.503  82.620  1.00 44.06           N  
ATOM     97  NH2 ARG A 137       1.349  31.299  84.207  1.00 46.41           N  
ATOM     98  N   PRO A 138       3.188  26.046  83.462  1.00 39.88           N  
ATOM     99  CA  PRO A 138       1.743  25.841  83.417  1.00 39.46           C  
ATOM    100  C   PRO A 138       1.056  27.198  83.366  1.00 39.24           C  
ATOM    101  O   PRO A 138       1.362  28.085  84.172  1.00 38.37           O  
ATOM    102  CB  PRO A 138       1.433  25.125  84.739  1.00 39.84           C  
ATOM    103  CG  PRO A 138       2.711  24.691  85.290  1.00 39.97           C  
ATOM    104  CD  PRO A 138       3.755  25.609  84.758  1.00 41.13           C  
ATOM    105  N   LEU A 139       0.202  27.375  82.366  1.00 38.79           N  
ATOM    106  CA  LEU A 139      -0.636  28.553  82.247  1.00 37.93           C  
ATOM    107  C   LEU A 139      -1.886  28.456  83.114  1.00 38.39           C  
ATOM    108  O   LEU A 139      -2.406  29.473  83.561  1.00 37.92           O  
ATOM    109  CB  LEU A 139      -1.026  28.756  80.797  1.00 37.45           C  
ATOM    110  CG  LEU A 139       0.141  29.165  79.905  1.00 37.06           C  
ATOM    111  CD1 LEU A 139      -0.223  29.026  78.438  1.00 37.59           C  
ATOM    112  CD2 LEU A 139       0.617  30.608  80.205  1.00 37.81           C  
ATOM    113  N   GLY A 140      -2.365  27.242  83.354  1.00 38.87           N  
ATOM    114  CA  GLY A 140      -3.553  27.039  84.173  1.00 39.30           C  
ATOM    115  C   GLY A 140      -3.901  25.582  84.431  1.00 40.29           C  
ATOM    116  O   GLY A 140      -3.286  24.665  83.884  1.00 39.94           O  
ATOM    117  N   LYS A 141      -4.883  25.373  85.296  1.00 41.62           N  
ATOM    118  CA  LYS A 141      -5.302  24.041  85.690  1.00 43.20           C  
ATOM    119  C   LYS A 141      -6.624  23.816  85.000  1.00 42.99           C  
ATOM    120  O   LYS A 141      -7.546  24.579  85.207  1.00 42.41           O  
ATOM    121  CB  LYS A 141      -5.485  23.946  87.215  1.00 44.15           C  
ATOM    122  CG  LYS A 141      -4.386  23.159  87.929  1.00 48.49           C  
ATOM    123  CD  LYS A 141      -4.661  22.976  89.448  1.00 52.63           C  
ATOM    124  CE  LYS A 141      -3.934  23.998  90.361  1.00 54.60           C  
ATOM    125  NZ  LYS A 141      -3.012  24.969  89.656  1.00 57.22           N  
ATOM    126  N   GLY A 142      -6.681  22.808  84.134  1.00 43.43           N  
ATOM    127  CA  GLY A 142      -7.929  22.358  83.540  1.00 43.97           C  
ATOM    128  C   GLY A 142      -8.469  21.173  84.340  1.00 44.41           C  
ATOM    129  O   GLY A 142      -7.837  20.707  85.298  1.00 44.86           O  
ATOM    130  N   LYS A 143      -9.636  20.679  83.960  1.00 44.65           N  
ATOM    131  CA  LYS A 143     -10.243  19.553  84.660  1.00 45.08           C  
ATOM    132  C   LYS A 143      -9.457  18.258  84.448  1.00 44.30           C  
ATOM    133  O   LYS A 143      -9.252  17.506  85.392  1.00 44.12           O  
ATOM    134  CB  LYS A 143     -11.687  19.359  84.223  1.00 45.83           C  
ATOM    135  CG  LYS A 143     -12.502  18.625  85.273  1.00 49.04           C  
ATOM    136  CD  LYS A 143     -13.733  17.963  84.694  1.00 52.01           C  
ATOM    137  CE  LYS A 143     -14.633  17.447  85.807  1.00 53.96           C  
ATOM    138  NZ  LYS A 143     -15.136  16.071  85.533  1.00 56.45           N  
ATOM    139  N   PHE A 144      -8.997  18.044  83.216  1.00 43.24           N  
ATOM    140  CA  PHE A 144      -8.380  16.789  82.790  1.00 42.75           C  
ATOM    141  C   PHE A 144      -6.877  16.849  82.587  1.00 41.64           C  
ATOM    142  O   PHE A 144      -6.293  15.900  82.102  1.00 40.46           O  
ATOM    143  CB  PHE A 144      -9.070  16.307  81.516  1.00 42.89           C  
ATOM    144  CG  PHE A 144     -10.526  16.032  81.714  1.00 44.90           C  
ATOM    145  CD1 PHE A 144     -10.932  14.905  82.428  1.00 47.63           C  
ATOM    146  CD2 PHE A 144     -11.492  16.906  81.247  1.00 44.29           C  
ATOM    147  CE1 PHE A 144     -12.267  14.642  82.634  1.00 45.90           C  
ATOM    148  CE2 PHE A 144     -12.833  16.640  81.447  1.00 45.90           C  
ATOM    149  CZ  PHE A 144     -13.222  15.508  82.140  1.00 46.88           C  
ATOM    150  N   GLY A 145      -6.242  17.931  83.042  1.00 40.29           N  
ATOM    151  CA  GLY A 145      -4.824  18.154  82.831  1.00 40.17           C  
ATOM    152  C   GLY A 145      -4.544  19.641  82.812  1.00 39.73           C  
ATOM    153  O   GLY A 145      -5.469  20.425  82.855  1.00 40.11           O  
ATOM    154  N   ASN A 146      -3.282  20.033  82.747  1.00 39.71           N  
ATOM    155  CA  ASN A 146      -2.930  21.446  82.777  1.00 39.49           C  
ATOM    156  C   ASN A 146      -2.806  21.995  81.371  1.00 38.12           C  
ATOM    157  O   ASN A 146      -2.692  21.232  80.413  1.00 37.44           O  
ATOM    158  CB  ASN A 146      -1.618  21.661  83.522  1.00 39.73           C  
ATOM    159  CG  ASN A 146      -1.703  21.262  84.973  1.00 42.98           C  
ATOM    160  OD1 ASN A 146      -2.746  21.389  85.608  1.00 47.99           O  
ATOM    161  ND2 ASN A 146      -0.600  20.771  85.505  1.00 46.02           N  
ATOM    162  N   VAL A 147      -2.838  23.320  81.255  1.00 36.47           N  
ATOM    163  CA  VAL A 147      -2.467  23.986  80.014  1.00 35.07           C  
ATOM    164  C   VAL A 147      -1.048  24.531  80.180  1.00 34.57           C  
ATOM    165  O   VAL A 147      -0.717  25.115  81.237  1.00 34.01           O  
ATOM    166  CB  VAL A 147      -3.454  25.097  79.677  1.00 35.17           C  
ATOM    167  CG1 VAL A 147      -3.063  25.781  78.344  1.00 35.15           C  
ATOM    168  CG2 VAL A 147      -4.859  24.549  79.632  1.00 36.20           C  
ATOM    169  N   TYR A 148      -0.201  24.338  79.169  1.00 32.82           N  
ATOM    170  CA  TYR A 148       1.199  24.730  79.259  1.00 33.39           C  
ATOM    171  C   TYR A 148       1.536  25.741  78.195  1.00 32.87           C  
ATOM    172  O   TYR A 148       1.050  25.659  77.075  1.00 32.49           O  
ATOM    173  CB  TYR A 148       2.125  23.513  79.097  1.00 33.61           C  
ATOM    174  CG  TYR A 148       1.969  22.523  80.213  1.00 36.63           C  
ATOM    175  CD1 TYR A 148       1.056  21.486  80.116  1.00 39.01           C  
ATOM    176  CD2 TYR A 148       2.700  22.646  81.383  1.00 41.71           C  
ATOM    177  CE1 TYR A 148       0.879  20.570  81.169  1.00 42.67           C  
ATOM    178  CE2 TYR A 148       2.527  21.738  82.456  1.00 43.04           C  
ATOM    179  CZ  TYR A 148       1.625  20.706  82.337  1.00 43.53           C  
ATOM    180  OH  TYR A 148       1.450  19.813  83.381  1.00 45.65           O  
ATOM    181  N   LEU A 149       2.374  26.697  78.541  1.00 32.34           N  
ATOM    182  CA  LEU A 149       3.040  27.515  77.535  1.00 32.54           C  
ATOM    183  C   LEU A 149       3.924  26.603  76.738  1.00 31.76           C  
ATOM    184  O   LEU A 149       4.547  25.733  77.291  1.00 32.20           O  
ATOM    185  CB  LEU A 149       3.909  28.562  78.210  1.00 33.12           C  
ATOM    186  CG  LEU A 149       3.999  29.993  77.691  1.00 35.42           C  
ATOM    187  CD1 LEU A 149       5.445  30.516  77.810  1.00 36.48           C  
ATOM    188  CD2 LEU A 149       3.408  30.256  76.327  1.00 34.87           C  
ATOM    189  N   ALA A 150       4.020  26.812  75.438  1.00 32.03           N  
ATOM    190  CA  ALA A 150       4.882  25.976  74.622  1.00 31.98           C  
ATOM    191  C   ALA A 150       5.420  26.781  73.456  1.00 32.60           C  
ATOM    192  O   ALA A 150       4.839  27.781  73.041  1.00 31.94           O  
ATOM    193  CB  ALA A 150       4.108  24.734  74.115  1.00 31.93           C  
ATOM    194  N   ARG A 151       6.547  26.346  72.940  1.00 33.19           N  
ATOM    195  CA  ARG A 151       7.135  26.949  71.767  1.00 34.88           C  
ATOM    196  C   ARG A 151       7.402  25.862  70.757  1.00 35.65           C  
ATOM    197  O   ARG A 151       7.975  24.847  71.099  1.00 36.04           O  
ATOM    198  CB  ARG A 151       8.439  27.630  72.136  1.00 35.59           C  
ATOM    199  CG  ARG A 151       8.934  28.576  71.099  1.00 37.10           C  
ATOM    200  CD  ARG A 151      10.162  29.364  71.541  1.00 40.01           C  
ATOM    201  NE  ARG A 151      11.330  28.501  71.666  1.00 42.36           N  
ATOM    202  CZ  ARG A 151      12.591  28.922  71.765  1.00 45.67           C  
ATOM    203  NH1 ARG A 151      12.891  30.217  71.755  1.00 46.38           N  
ATOM    204  NH2 ARG A 151      13.564  28.030  71.863  1.00 48.08           N  
ATOM    205  N   GLU A 152       6.963  26.076  69.528  1.00 37.52           N  
ATOM    206  CA  GLU A 152       7.249  25.174  68.427  1.00 39.57           C  
ATOM    207  C   GLU A 152       8.713  25.345  68.046  1.00 40.26           C  
ATOM    208  O   GLU A 152       9.178  26.451  67.786  1.00 40.13           O  
ATOM    209  CB  GLU A 152       6.341  25.504  67.230  1.00 39.79           C  
ATOM    210  CG  GLU A 152       6.208  24.376  66.219  1.00 43.57           C  
ATOM    211  CD  GLU A 152       7.323  24.351  65.169  1.00 46.99           C  
ATOM    212  OE1 GLU A 152       7.464  25.342  64.417  1.00 50.27           O  
ATOM    213  OE2 GLU A 152       8.057  23.330  65.088  1.00 49.76           O  
ATOM    214  N   LYS A 153       9.439  24.246  67.987  1.00 41.87           N  
ATOM    215  CA  LYS A 153      10.886  24.301  67.820  1.00 43.57           C  
ATOM    216  C   LYS A 153      11.398  24.925  66.511  1.00 44.10           C  
ATOM    217  O   LYS A 153      12.403  25.602  66.506  1.00 45.13           O  
ATOM    218  CB  LYS A 153      11.472  22.897  68.008  1.00 44.27           C  
ATOM    219  CG  LYS A 153      11.890  22.607  69.428  1.00 46.46           C  
ATOM    220  CD  LYS A 153      11.404  21.262  69.974  1.00 49.37           C  
ATOM    221  CE  LYS A 153      12.421  20.159  69.772  1.00 51.83           C  
ATOM    222  NZ  LYS A 153      12.352  19.103  70.833  1.00 50.94           N  
ATOM    223  N   GLN A 154      10.733  24.692  65.397  1.00 44.87           N  
ATOM    224  CA  GLN A 154      11.248  25.169  64.104  1.00 45.36           C  
ATOM    225  C   GLN A 154      10.931  26.642  63.839  1.00 43.28           C  
ATOM    226  O   GLN A 154      11.742  27.394  63.294  1.00 44.26           O  
ATOM    227  CB  GLN A 154      10.680  24.301  62.977  1.00 46.31           C  
ATOM    228  CG  GLN A 154      11.280  22.906  62.951  1.00 51.22           C  
ATOM    229  CD  GLN A 154      11.412  22.356  61.542  1.00 56.61           C  
ATOM    230  OE1 GLN A 154      10.418  22.296  60.795  1.00 61.72           O  
ATOM    231  NE2 GLN A 154      12.634  21.964  61.165  1.00 59.80           N  
ATOM    232  N   SER A 155       9.742  27.055  64.240  1.00 40.77           N  
ATOM    233  CA  SER A 155       9.270  28.397  63.959  1.00 38.61           C  
ATOM    234  C   SER A 155       9.528  29.346  65.134  1.00 37.22           C  
ATOM    235  O   SER A 155       9.525  30.553  64.939  1.00 36.80           O  
ATOM    236  CB  SER A 155       7.778  28.348  63.676  1.00 38.33           C  
ATOM    237  OG  SER A 155       7.125  27.829  64.813  1.00 37.62           O  
ATOM    238  N   LYS A 156       9.726  28.773  66.322  1.00 36.07           N  
ATOM    239  CA  LYS A 156       9.733  29.471  67.630  1.00 36.36           C  
ATOM    240  C   LYS A 156       8.372  30.112  67.993  1.00 35.13           C  
ATOM    241  O   LYS A 156       8.287  31.045  68.822  1.00 33.61           O  
ATOM    242  CB  LYS A 156      10.875  30.497  67.712  1.00 36.98           C  
ATOM    243  CG  LYS A 156      12.296  29.913  67.482  1.00 38.64           C  
ATOM    244  CD  LYS A 156      13.387  30.938  67.890  1.00 42.47           C  
ATOM    245  CE  LYS A 156      14.557  31.096  66.890  1.00 45.84           C  
ATOM    246  NZ  LYS A 156      14.901  32.556  66.669  1.00 44.64           N  
ATOM    247  N   PHE A 157       7.310  29.571  67.406  1.00 33.58           N  
ATOM    248  CA  PHE A 157       5.956  30.072  67.609  1.00 33.37           C  
ATOM    249  C   PHE A 157       5.495  29.757  69.027  1.00 32.34           C  
ATOM    250  O   PHE A 157       5.537  28.631  69.460  1.00 31.40           O  
ATOM    251  CB  PHE A 157       5.008  29.458  66.577  1.00 33.93           C  
ATOM    252  CG  PHE A 157       3.686  30.168  66.438  1.00 36.01           C  
ATOM    253  CD1 PHE A 157       3.517  31.168  65.489  1.00 39.58           C  
ATOM    254  CD2 PHE A 157       2.599  29.795  67.210  1.00 38.12           C  
ATOM    255  CE1 PHE A 157       2.280  31.806  65.323  1.00 40.07           C  
ATOM    256  CE2 PHE A 157       1.361  30.425  67.057  1.00 36.91           C  
ATOM    257  CZ  PHE A 157       1.211  31.438  66.111  1.00 38.24           C  
ATOM    258  N   ILE A 158       5.072  30.770  69.766  1.00 31.92           N  
ATOM    259  CA  ILE A 158       4.620  30.542  71.132  1.00 32.46           C  
ATOM    260  C   ILE A 158       3.134  30.271  71.091  1.00 31.53           C  
ATOM    261  O   ILE A 158       2.384  30.908  70.340  1.00 31.82           O  
ATOM    262  CB  ILE A 158       4.946  31.739  72.060  1.00 32.57           C  
ATOM    263  CG1 ILE A 158       6.440  31.801  72.329  1.00 37.02           C  
ATOM    264  CG2 ILE A 158       4.274  31.579  73.427  1.00 34.54           C  
ATOM    265  CD1 ILE A 158       6.928  30.839  73.399  1.00 38.82           C  
ATOM    266  N   LEU A 159       2.717  29.283  71.862  1.00 31.02           N  
ATOM    267  CA  LEU A 159       1.330  28.872  71.888  1.00 30.96           C  
ATOM    268  C   LEU A 159       1.094  28.216  73.227  1.00 30.83           C  
ATOM    269  O   LEU A 159       1.972  28.227  74.072  1.00 29.77           O  
ATOM    270  CB  LEU A 159       1.049  27.925  70.721  1.00 31.62           C  
ATOM    271  CG  LEU A 159       2.057  26.851  70.374  1.00 34.57           C  
ATOM    272  CD1 LEU A 159       1.879  25.658  71.264  1.00 36.43           C  
ATOM    273  CD2 LEU A 159       1.888  26.448  68.911  1.00 38.58           C  
ATOM    274  N   ALA A 160      -0.103  27.692  73.423  1.00 31.60           N  
ATOM    275  CA  ALA A 160      -0.469  27.006  74.648  1.00 32.32           C  
ATOM    276  C   ALA A 160      -0.843  25.597  74.283  1.00 33.81           C  
ATOM    277  O   ALA A 160      -1.516  25.373  73.269  1.00 33.74           O  
ATOM    278  CB  ALA A 160      -1.633  27.687  75.286  1.00 32.17           C  
ATOM    279  N   LEU A 161      -0.416  24.652  75.115  1.00 34.78           N  
ATOM    280  CA  LEU A 161      -0.708  23.245  74.931  1.00 35.51           C  
ATOM    281  C   LEU A 161      -1.623  22.784  76.046  1.00 34.84           C  
ATOM    282  O   LEU A 161      -1.248  22.772  77.221  1.00 34.39           O  
ATOM    283  CB  LEU A 161       0.606  22.464  74.908  1.00 35.93           C  
ATOM    284  CG  LEU A 161       0.802  21.380  73.868  1.00 39.38           C  
ATOM    285  CD1 LEU A 161       0.504  21.865  72.443  1.00 38.64           C  
ATOM    286  CD2 LEU A 161       2.241  20.847  73.991  1.00 41.17           C  
ATOM    287  N   LYS A 162      -2.857  22.462  75.683  1.00 34.26           N  
ATOM    288  CA  LYS A 162      -3.842  21.992  76.629  1.00 34.93           C  
ATOM    289  C   LYS A 162      -3.760  20.454  76.678  1.00 36.18           C  
ATOM    290  O   LYS A 162      -4.058  19.789  75.701  1.00 36.02           O  
ATOM    291  CB  LYS A 162      -5.224  22.476  76.205  1.00 34.84           C  
ATOM    292  CG  LYS A 162      -6.369  21.962  77.030  1.00 33.34           C  
ATOM    293  CD  LYS A 162      -7.580  22.807  76.841  1.00 32.38           C  
ATOM    294  CE  LYS A 162      -8.763  22.183  77.561  1.00 31.38           C  
ATOM    295  NZ  LYS A 162     -10.003  22.971  77.468  1.00 33.14           N  
ATOM    296  N   VAL A 163      -3.342  19.915  77.815  1.00 37.98           N  
ATOM    297  CA  VAL A 163      -3.194  18.467  78.023  1.00 39.72           C  
ATOM    298  C   VAL A 163      -4.442  17.868  78.697  1.00 40.45           C  
ATOM    299  O   VAL A 163      -4.951  18.406  79.686  1.00 39.96           O  
ATOM    300  CB  VAL A 163      -1.948  18.181  78.877  1.00 39.85           C  
ATOM    301  CG1 VAL A 163      -1.661  16.664  78.984  1.00 41.14           C  
ATOM    302  CG2 VAL A 163      -0.717  18.916  78.309  1.00 41.29           C  
ATOM    303  N   LEU A 164      -4.958  16.775  78.130  1.00 41.79           N  
ATOM    304  CA  LEU A 164      -6.078  16.030  78.707  1.00 41.87           C  
ATOM    305  C   LEU A 164      -5.711  14.548  78.795  1.00 43.01           C  
ATOM    306  O   LEU A 164      -5.326  13.953  77.808  1.00 42.41           O  
ATOM    307  CB  LEU A 164      -7.341  16.172  77.866  1.00 42.08           C  
ATOM    308  CG  LEU A 164      -7.901  17.581  77.677  1.00 41.11           C  
ATOM    309  CD1 LEU A 164      -7.406  18.110  76.377  1.00 41.78           C  
ATOM    310  CD2 LEU A 164      -9.411  17.593  77.708  1.00 41.45           C  
ATOM    311  N   PHE A 165      -5.822  13.960  79.982  1.00 44.15           N  
ATOM    312  CA  PHE A 165      -5.471  12.556  80.178  1.00 45.50           C  
ATOM    313  C   PHE A 165      -6.635  11.702  79.711  1.00 45.87           C  
ATOM    314  O   PHE A 165      -7.738  11.840  80.208  1.00 44.85           O  
ATOM    315  CB  PHE A 165      -5.134  12.280  81.648  1.00 45.90           C  
ATOM    316  CG  PHE A 165      -3.757  12.720  82.034  1.00 48.12           C  
ATOM    317  CD1 PHE A 165      -3.547  13.926  82.686  1.00 50.10           C  
ATOM    318  CD2 PHE A 165      -2.660  11.930  81.735  1.00 50.53           C  
ATOM    319  CE1 PHE A 165      -2.272  14.327  83.043  1.00 50.63           C  
ATOM    320  CE2 PHE A 165      -1.374  12.327  82.083  1.00 51.04           C  
ATOM    321  CZ  PHE A 165      -1.181  13.518  82.744  1.00 51.95           C  
ATOM    322  N   LYS A 166      -6.385  10.870  78.705  1.00 47.23           N  
ATOM    323  CA  LYS A 166      -7.384   9.952  78.160  1.00 48.38           C  
ATOM    324  C   LYS A 166      -8.094   9.108  79.221  1.00 48.97           C  
ATOM    325  O   LYS A 166      -9.299   8.976  79.174  1.00 49.00           O  
ATOM    326  CB  LYS A 166      -6.742   9.022  77.131  1.00 48.86           C  
ATOM    327  CG  LYS A 166      -6.506   9.671  75.799  1.00 49.17           C  
ATOM    328  CD  LYS A 166      -5.539   8.847  74.975  1.00 52.05           C  
ATOM    329  CE  LYS A 166      -5.426   9.372  73.552  1.00 53.29           C  
ATOM    330  NZ  LYS A 166      -5.193   8.281  72.561  1.00 54.63           N  
ATOM    331  N   ALA A 167      -7.356   8.562  80.182  1.00 50.27           N  
ATOM    332  CA  ALA A 167      -7.977   7.721  81.215  1.00 51.07           C  
ATOM    333  C   ALA A 167      -9.123   8.463  81.902  1.00 51.57           C  
ATOM    334  O   ALA A 167     -10.239   7.949  82.024  1.00 51.51           O  
ATOM    335  CB  ALA A 167      -6.959   7.294  82.227  1.00 51.35           C  
ATOM    336  N   GLN A 168      -8.838   9.694  82.313  1.00 51.80           N  
ATOM    337  CA  GLN A 168      -9.786  10.493  83.068  1.00 51.81           C  
ATOM    338  C   GLN A 168     -10.961  10.940  82.208  1.00 51.13           C  
ATOM    339  O   GLN A 168     -12.081  11.013  82.697  1.00 50.63           O  
ATOM    340  CB  GLN A 168      -9.075  11.697  83.697  1.00 52.46           C  
ATOM    341  CG  GLN A 168      -8.476  11.414  85.089  1.00 55.32           C  
ATOM    342  CD  GLN A 168      -7.032  10.905  85.049  1.00 59.76           C  
ATOM    343  OE1 GLN A 168      -6.099  11.694  84.838  1.00 62.19           O  
ATOM    344  NE2 GLN A 168      -6.843   9.594  85.280  1.00 61.28           N  
ATOM    345  N   LEU A 169     -10.709  11.226  80.930  1.00 50.87           N  
ATOM    346  CA  LEU A 169     -11.761  11.672  80.018  1.00 51.03           C  
ATOM    347  C   LEU A 169     -12.820  10.584  79.825  1.00 51.13           C  
ATOM    348  O   LEU A 169     -14.016  10.842  79.928  1.00 51.23           O  
ATOM    349  CB  LEU A 169     -11.182  12.045  78.646  1.00 50.91           C  
ATOM    350  CG  LEU A 169     -10.616  13.451  78.432  1.00 51.20           C  
ATOM    351  CD1 LEU A 169      -9.973  13.541  77.063  1.00 51.39           C  
ATOM    352  CD2 LEU A 169     -11.699  14.492  78.542  1.00 50.55           C  
ATOM    353  N   GLU A 170     -12.366   9.378  79.519  1.00 51.59           N  
ATOM    354  CA  GLU A 170     -13.273   8.253  79.245  1.00 51.75           C  
ATOM    355  C   GLU A 170     -14.022   7.823  80.513  1.00 51.63           C  
ATOM    356  O   GLU A 170     -15.215   7.565  80.462  1.00 52.26           O  
ATOM    357  CB  GLU A 170     -12.505   7.079  78.626  1.00 52.08           C  
ATOM    358  N   LYS A 171     -13.336   7.788  81.650  1.00 51.69           N  
ATOM    359  CA  LYS A 171     -14.002   7.535  82.928  1.00 51.79           C  
ATOM    360  C   LYS A 171     -15.138   8.542  83.151  1.00 51.57           C  
ATOM    361  O   LYS A 171     -16.247   8.164  83.503  1.00 51.36           O  
ATOM    362  CB  LYS A 171     -13.005   7.567  84.103  1.00 52.01           C  
ATOM    363  N   ALA A 172     -14.856   9.821  82.902  1.00 51.30           N  
ATOM    364  CA  ALA A 172     -15.836  10.883  83.052  1.00 50.90           C  
ATOM    365  C   ALA A 172     -16.887  10.828  81.945  1.00 50.82           C  
ATOM    366  O   ALA A 172     -17.997  11.346  82.093  1.00 50.79           O  
ATOM    367  CB  ALA A 172     -15.124  12.250  83.072  1.00 51.24           C  
ATOM    368  N   GLY A 173     -16.533  10.190  80.836  1.00 50.65           N  
ATOM    369  CA  GLY A 173     -17.458   9.970  79.738  1.00 50.46           C  
ATOM    370  C   GLY A 173     -17.844  11.222  78.991  1.00 50.17           C  
ATOM    371  O   GLY A 173     -19.017  11.389  78.634  1.00 50.69           O  
ATOM    372  N   VAL A 174     -16.849  12.082  78.750  1.00 49.49           N  
ATOM    373  CA  VAL A 174     -17.004  13.344  78.029  1.00 48.81           C  
ATOM    374  C   VAL A 174     -16.056  13.433  76.826  1.00 47.67           C  
ATOM    375  O   VAL A 174     -15.651  14.528  76.417  1.00 46.93           O  
ATOM    376  CB  VAL A 174     -16.735  14.579  78.949  1.00 48.74           C  
ATOM    377  CG1 VAL A 174     -17.764  14.654  80.048  1.00 50.81           C  
ATOM    378  CG2 VAL A 174     -15.346  14.553  79.521  1.00 48.72           C  
ATOM    379  N   GLU A 175     -15.693  12.287  76.255  1.00 46.50           N  
ATOM    380  CA  GLU A 175     -14.873  12.287  75.044  1.00 45.97           C  
ATOM    381  C   GLU A 175     -15.586  13.060  73.926  1.00 45.29           C  
ATOM    382  O   GLU A 175     -14.935  13.655  73.072  1.00 45.81           O  
ATOM    383  CB  GLU A 175     -14.534  10.849  74.593  1.00 46.26           C  
ATOM    384  N   HIS A 176     -16.915  13.060  73.938  1.00 44.43           N  
ATOM    385  CA  HIS A 176     -17.706  13.821  72.959  1.00 44.54           C  
ATOM    386  C   HIS A 176     -17.511  15.351  73.096  1.00 43.44           C  
ATOM    387  O   HIS A 176     -17.576  16.074  72.112  1.00 42.50           O  
ATOM    388  CB  HIS A 176     -19.199  13.466  73.081  1.00 44.89           C  
ATOM    389  CG  HIS A 176     -19.813  13.893  74.383  1.00 46.94           C  
ATOM    390  ND1 HIS A 176     -19.630  13.191  75.561  1.00 47.61           N  
ATOM    391  CD2 HIS A 176     -20.579  14.964  74.699  1.00 48.04           C  
ATOM    392  CE1 HIS A 176     -20.271  13.804  76.541  1.00 47.96           C  
ATOM    393  NE2 HIS A 176     -20.843  14.891  76.048  1.00 48.95           N  
ATOM    394  N   GLN A 177     -17.296  15.826  74.322  1.00 42.52           N  
ATOM    395  CA  GLN A 177     -16.994  17.243  74.579  1.00 42.34           C  
ATOM    396  C   GLN A 177     -15.661  17.657  73.994  1.00 42.46           C  
ATOM    397  O   GLN A 177     -15.543  18.729  73.423  1.00 43.08           O  
ATOM    398  CB  GLN A 177     -16.983  17.527  76.075  1.00 41.70           C  
ATOM    399  CG  GLN A 177     -18.339  17.325  76.699  1.00 40.81           C  
ATOM    400  CD  GLN A 177     -18.496  17.982  78.054  1.00 39.68           C  
ATOM    401  OE1 GLN A 177     -19.595  18.406  78.397  1.00 43.96           O  
ATOM    402  NE2 GLN A 177     -17.428  18.028  78.836  1.00 36.53           N  
ATOM    403  N   LEU A 178     -14.655  16.818  74.145  1.00 42.26           N  
ATOM    404  CA  LEU A 178     -13.366  17.103  73.532  1.00 42.79           C  
ATOM    405  C   LEU A 178     -13.481  17.162  72.004  1.00 42.91           C  
ATOM    406  O   LEU A 178     -12.901  18.032  71.354  1.00 42.49           O  
ATOM    407  CB  LEU A 178     -12.325  16.070  73.945  1.00 42.53           C  
ATOM    408  CG  LEU A 178     -10.897  16.486  73.590  1.00 44.14           C  
ATOM    409  CD1 LEU A 178     -10.576  17.875  74.202  1.00 45.30           C  
ATOM    410  CD2 LEU A 178      -9.903  15.463  74.064  1.00 45.73           C  
ATOM    411  N   ARG A 179     -14.266  16.248  71.436  1.00 43.60           N  
ATOM    412  CA  ARG A 179     -14.471  16.204  69.989  1.00 43.80           C  
ATOM    413  C   ARG A 179     -15.148  17.455  69.477  1.00 43.03           C  
ATOM    414  O   ARG A 179     -14.748  18.022  68.469  1.00 42.96           O  
ATOM    415  CB  ARG A 179     -15.319  14.976  69.591  1.00 45.13           C  
ATOM    416  CG  ARG A 179     -15.046  14.472  68.157  1.00 48.18           C  
ATOM    417  CD  ARG A 179     -15.316  12.944  67.962  1.00 53.66           C  
ATOM    418  NE  ARG A 179     -16.407  12.464  68.832  1.00 54.81           N  
ATOM    419  CZ  ARG A 179     -16.277  11.652  69.895  1.00 55.59           C  
ATOM    420  NH1 ARG A 179     -17.354  11.330  70.588  1.00 54.17           N  
ATOM    421  NH2 ARG A 179     -15.099  11.153  70.278  1.00 56.61           N  
ATOM    422  N   ARG A 180     -16.198  17.866  70.156  1.00 42.84           N  
ATOM    423  CA  ARG A 180     -16.901  19.100  69.830  1.00 43.68           C  
ATOM    424  C   ARG A 180     -15.986  20.320  69.925  1.00 42.67           C  
ATOM    425  O   ARG A 180     -16.012  21.171  69.051  1.00 41.68           O  
ATOM    426  CB  ARG A 180     -18.110  19.300  70.758  1.00 43.98           C  
ATOM    427  CG  ARG A 180     -19.454  19.330  70.043  1.00 48.84           C  
ATOM    428  CD  ARG A 180     -20.396  18.196  70.422  1.00 53.79           C  
ATOM    429  NE  ARG A 180     -20.852  18.286  71.805  1.00 57.58           N  
ATOM    430  CZ  ARG A 180     -21.974  17.734  72.273  1.00 60.62           C  
ATOM    431  NH1 ARG A 180     -22.306  17.893  73.551  1.00 60.52           N  
ATOM    432  NH2 ARG A 180     -22.768  17.017  71.478  1.00 62.26           N  
ATOM    433  N   GLU A 181     -15.202  20.404  70.998  1.00 41.97           N  
ATOM    434  CA  GLU A 181     -14.256  21.521  71.210  1.00 41.61           C  
ATOM    435  C   GLU A 181     -13.370  21.674  69.980  1.00 41.33           C  
ATOM    436  O   GLU A 181     -13.230  22.751  69.437  1.00 40.44           O  
ATOM    437  CB  GLU A 181     -13.375  21.257  72.454  1.00 42.23           C  
ATOM    438  CG  GLU A 181     -12.474  22.413  72.928  1.00 43.05           C  
ATOM    439  CD  GLU A 181     -11.947  22.228  74.367  1.00 46.34           C  
ATOM    440  OE1 GLU A 181     -10.995  22.951  74.764  1.00 48.48           O  
ATOM    441  OE2 GLU A 181     -12.489  21.383  75.130  1.00 46.40           O  
ATOM    442  N   VAL A 182     -12.782  20.569  69.542  1.00 40.91           N  
ATOM    443  CA  VAL A 182     -11.823  20.595  68.461  1.00 41.06           C  
ATOM    444  C   VAL A 182     -12.529  20.966  67.179  1.00 41.23           C  
ATOM    445  O   VAL A 182     -12.082  21.844  66.470  1.00 41.15           O  
ATOM    446  CB  VAL A 182     -11.099  19.241  68.306  1.00 41.21           C  
ATOM    447  CG1 VAL A 182     -10.291  19.188  67.002  1.00 41.88           C  
ATOM    448  CG2 VAL A 182     -10.194  18.988  69.500  1.00 40.72           C  
ATOM    449  N   GLU A 183     -13.659  20.318  66.905  1.00 41.83           N  
ATOM    450  CA  GLU A 183     -14.350  20.516  65.642  1.00 42.37           C  
ATOM    451  C   GLU A 183     -14.966  21.913  65.565  1.00 42.79           C  
ATOM    452  O   GLU A 183     -14.901  22.572  64.529  1.00 43.42           O  
ATOM    453  CB  GLU A 183     -15.414  19.419  65.443  1.00 43.07           C  
ATOM    454  N   ILE A 184     -15.546  22.390  66.663  1.00 42.10           N  
ATOM    455  CA  ILE A 184     -16.190  23.690  66.626  1.00 42.07           C  
ATOM    456  C   ILE A 184     -15.138  24.797  66.701  1.00 41.73           C  
ATOM    457  O   ILE A 184     -15.139  25.707  65.876  1.00 41.66           O  
ATOM    458  CB  ILE A 184     -17.255  23.835  67.733  1.00 41.88           C  
ATOM    459  CG1 ILE A 184     -18.429  22.903  67.437  1.00 43.16           C  
ATOM    460  CG2 ILE A 184     -17.758  25.263  67.794  1.00 42.41           C  
ATOM    461  CD1 ILE A 184     -19.429  22.760  68.573  1.00 43.32           C  
ATOM    462  N   GLN A 185     -14.242  24.727  67.687  1.00 41.29           N  
ATOM    463  CA  GLN A 185     -13.312  25.831  67.909  1.00 40.66           C  
ATOM    464  C   GLN A 185     -12.321  25.998  66.775  1.00 41.19           C  
ATOM    465  O   GLN A 185     -11.913  27.115  66.496  1.00 40.07           O  
ATOM    466  CB  GLN A 185     -12.558  25.679  69.227  1.00 40.40           C  
ATOM    467  CG  GLN A 185     -12.137  26.984  69.837  1.00 38.69           C  
ATOM    468  CD  GLN A 185     -11.521  26.810  71.224  1.00 37.97           C  
ATOM    469  OE1 GLN A 185     -10.728  27.629  71.647  1.00 36.44           O  
ATOM    470  NE2 GLN A 185     -11.886  25.737  71.918  1.00 35.53           N  
ATOM    471  N   SER A 186     -11.936  24.902  66.119  1.00 42.17           N  
ATOM    472  CA  SER A 186     -10.958  25.007  65.022  1.00 43.60           C  
ATOM    473  C   SER A 186     -11.497  25.721  63.778  1.00 44.44           C  
ATOM    474  O   SER A 186     -10.723  26.264  63.010  1.00 44.81           O  
ATOM    475  CB  SER A 186     -10.352  23.645  64.641  1.00 43.70           C  
ATOM    476  OG  SER A 186     -11.351  22.692  64.366  1.00 43.88           O  
ATOM    477  N   HIS A 187     -12.809  25.740  63.589  1.00 45.57           N  
ATOM    478  CA  HIS A 187     -13.409  26.375  62.405  1.00 46.86           C  
ATOM    479  C   HIS A 187     -13.818  27.839  62.628  1.00 46.48           C  
ATOM    480  O   HIS A 187     -13.926  28.618  61.672  1.00 46.57           O  
ATOM    481  CB  HIS A 187     -14.595  25.530  61.897  1.00 47.42           C  
ATOM    482  CG  HIS A 187     -14.177  24.223  61.293  1.00 51.45           C  
ATOM    483  ND1 HIS A 187     -14.353  23.926  59.956  1.00 55.36           N  
ATOM    484  CD2 HIS A 187     -13.549  23.149  61.835  1.00 54.33           C  
ATOM    485  CE1 HIS A 187     -13.864  22.723  59.707  1.00 56.26           C  
ATOM    486  NE2 HIS A 187     -13.370  22.231  60.830  1.00 55.79           N  
ATOM    487  N   LEU A 188     -14.010  28.228  63.885  1.00 46.21           N  
ATOM    488  CA  LEU A 188     -14.332  29.617  64.209  1.00 45.99           C  
ATOM    489  C   LEU A 188     -13.111  30.509  64.007  1.00 45.48           C  
ATOM    490  O   LEU A 188     -12.005  30.133  64.362  1.00 45.94           O  
ATOM    491  CB  LEU A 188     -14.829  29.736  65.661  1.00 46.05           C  
ATOM    492  CG  LEU A 188     -16.075  28.921  66.014  1.00 46.13           C  
ATOM    493  CD1 LEU A 188     -16.290  28.923  67.515  1.00 46.64           C  
ATOM    494  CD2 LEU A 188     -17.281  29.463  65.331  1.00 46.12           C  
ATOM    495  N   ARG A 189     -13.340  31.698  63.458  1.00 45.22           N  
ATOM    496  CA  ARG A 189     -12.297  32.693  63.173  1.00 45.04           C  
ATOM    497  C   ARG A 189     -12.816  34.078  63.537  1.00 43.93           C  
ATOM    498  O   ARG A 189     -13.537  34.702  62.760  1.00 44.22           O  
ATOM    499  CB  ARG A 189     -11.942  32.700  61.680  1.00 45.49           C  
ATOM    500  CG  ARG A 189     -11.247  31.468  61.222  1.00 47.57           C  
ATOM    501  CD  ARG A 189      -9.858  31.275  61.836  1.00 50.53           C  
ATOM    502  NE  ARG A 189      -9.080  30.320  61.044  1.00 53.80           N  
ATOM    503  CZ  ARG A 189      -9.320  29.017  60.991  1.00 56.47           C  
ATOM    504  NH1 ARG A 189      -8.569  28.236  60.233  1.00 57.65           N  
ATOM    505  NH2 ARG A 189     -10.304  28.474  61.700  1.00 58.68           N  
ATOM    506  N   HIS A 190     -12.446  34.558  64.714  1.00 42.55           N  
ATOM    507  CA  HIS A 190     -12.926  35.832  65.198  1.00 41.51           C  
ATOM    508  C   HIS A 190     -11.890  36.387  66.174  1.00 40.94           C  
ATOM    509  O   HIS A 190     -11.318  35.634  66.941  1.00 41.38           O  
ATOM    510  CB  HIS A 190     -14.310  35.653  65.838  1.00 41.22           C  
ATOM    511  CG  HIS A 190     -14.972  36.939  66.211  1.00 41.02           C  
ATOM    512  ND1 HIS A 190     -15.871  37.583  65.392  1.00 40.80           N  
ATOM    513  CD2 HIS A 190     -14.830  37.725  67.304  1.00 37.83           C  
ATOM    514  CE1 HIS A 190     -16.264  38.705  65.970  1.00 41.13           C  
ATOM    515  NE2 HIS A 190     -15.650  38.810  67.134  1.00 40.19           N  
ATOM    516  N   PRO A 191     -11.612  37.687  66.150  1.00 40.72           N  
ATOM    517  CA  PRO A 191     -10.560  38.242  67.016  1.00 39.66           C  
ATOM    518  C   PRO A 191     -10.823  38.026  68.522  1.00 38.34           C  
ATOM    519  O   PRO A 191      -9.890  38.094  69.311  1.00 37.77           O  
ATOM    520  CB  PRO A 191     -10.595  39.731  66.687  1.00 40.31           C  
ATOM    521  CG  PRO A 191     -11.958  39.966  66.126  1.00 41.09           C  
ATOM    522  CD  PRO A 191     -12.242  38.740  65.332  1.00 41.26           C  
ATOM    523  N   ASN A 192     -12.075  37.791  68.899  1.00 36.87           N  
ATOM    524  CA  ASN A 192     -12.455  37.558  70.303  1.00 35.82           C  
ATOM    525  C   ASN A 192     -12.849  36.127  70.615  1.00 34.58           C  
ATOM    526  O   ASN A 192     -13.542  35.874  71.610  1.00 33.90           O  
ATOM    527  CB  ASN A 192     -13.592  38.483  70.700  1.00 35.34           C  
ATOM    528  CG  ASN A 192     -13.246  39.945  70.495  1.00 36.85           C  
ATOM    529  OD1 ASN A 192     -12.314  40.485  71.118  1.00 37.08           O  
ATOM    530  ND2 ASN A 192     -13.978  40.588  69.608  1.00 32.21           N  
ATOM    531  N   ILE A 193     -12.405  35.199  69.772  1.00 33.19           N  
ATOM    532  CA  ILE A 193     -12.514  33.781  70.036  1.00 33.12           C  
ATOM    533  C   ILE A 193     -11.123  33.179  69.976  1.00 32.84           C  
ATOM    534  O   ILE A 193     -10.409  33.391  69.001  1.00 33.36           O  
ATOM    535  CB  ILE A 193     -13.459  33.081  69.020  1.00 33.28           C  
ATOM    536  CG1 ILE A 193     -14.889  33.616  69.141  1.00 34.41           C  
ATOM    537  CG2 ILE A 193     -13.457  31.572  69.240  1.00 32.81           C  
ATOM    538  CD1 ILE A 193     -15.792  33.206  68.010  1.00 36.36           C  
ATOM    539  N   LEU A 194     -10.737  32.424  71.015  1.00 31.81           N  
ATOM    540  CA  LEU A 194      -9.438  31.802  71.045  1.00 32.19           C  
ATOM    541  C   LEU A 194      -9.329  30.773  69.927  1.00 32.82           C  
ATOM    542  O   LEU A 194     -10.180  29.906  69.760  1.00 32.43           O  
ATOM    543  CB  LEU A 194      -9.177  31.120  72.383  1.00 31.87           C  
ATOM    544  CG  LEU A 194      -7.712  30.790  72.604  1.00 32.55           C  
ATOM    545  CD1 LEU A 194      -6.941  32.063  72.972  1.00 30.43           C  
ATOM    546  CD2 LEU A 194      -7.591  29.740  73.667  1.00 31.96           C  
ATOM    547  N   ARG A 195      -8.262  30.891  69.175  1.00 33.72           N  
ATOM    548  CA  ARG A 195      -7.984  29.987  68.077  1.00 34.90           C  
ATOM    549  C   ARG A 195      -7.503  28.630  68.625  1.00 34.13           C  
ATOM    550  O   ARG A 195      -6.766  28.556  69.601  1.00 31.49           O  
ATOM    551  CB  ARG A 195      -6.935  30.675  67.206  1.00 36.24           C  
ATOM    552  CG  ARG A 195      -6.711  30.112  65.863  1.00 42.21           C  
ATOM    553  CD  ARG A 195      -7.681  30.533  64.780  1.00 46.32           C  
ATOM    554  NE  ARG A 195      -7.179  29.938  63.543  1.00 50.63           N  
ATOM    555  CZ  ARG A 195      -6.229  30.471  62.778  1.00 54.26           C  
ATOM    556  NH1 ARG A 195      -5.697  31.646  63.084  1.00 55.15           N  
ATOM    557  NH2 ARG A 195      -5.815  29.834  61.682  1.00 56.52           N  
ATOM    558  N   LEU A 196      -7.983  27.557  68.030  1.00 34.43           N  
ATOM    559  CA  LEU A 196      -7.440  26.235  68.233  1.00 35.01           C  
ATOM    560  C   LEU A 196      -6.818  25.863  66.886  1.00 37.30           C  
ATOM    561  O   LEU A 196      -7.493  25.921  65.856  1.00 37.03           O  
ATOM    562  CB  LEU A 196      -8.549  25.286  68.643  1.00 35.43           C  
ATOM    563  CG  LEU A 196      -8.184  23.854  69.010  1.00 35.95           C  
ATOM    564  CD1 LEU A 196      -9.216  23.305  69.960  1.00 37.87           C  
ATOM    565  CD2 LEU A 196      -8.116  23.000  67.801  1.00 37.40           C  
ATOM    566  N   TYR A 197      -5.526  25.524  66.904  1.00 38.59           N  
ATOM    567  CA  TYR A 197      -4.750  25.267  65.696  1.00 39.75           C  
ATOM    568  C   TYR A 197      -4.721  23.811  65.311  1.00 40.45           C  
ATOM    569  O   TYR A 197      -4.454  23.475  64.162  1.00 41.04           O  
ATOM    570  CB  TYR A 197      -3.316  25.737  65.895  1.00 40.38           C  
ATOM    571  CG  TYR A 197      -3.224  27.218  66.099  1.00 41.37           C  
ATOM    572  CD1 TYR A 197      -2.734  27.750  67.275  1.00 43.01           C  
ATOM    573  CD2 TYR A 197      -3.638  28.089  65.109  1.00 43.98           C  
ATOM    574  CE1 TYR A 197      -2.654  29.104  67.457  1.00 43.41           C  
ATOM    575  CE2 TYR A 197      -3.557  29.452  65.289  1.00 44.17           C  
ATOM    576  CZ  TYR A 197      -3.074  29.948  66.462  1.00 43.30           C  
ATOM    577  OH  TYR A 197      -2.987  31.304  66.626  1.00 45.75           O  
ATOM    578  N   GLY A 198      -4.967  22.939  66.272  1.00 40.35           N  
ATOM    579  CA  GLY A 198      -5.002  21.522  65.986  1.00 40.91           C  
ATOM    580  C   GLY A 198      -4.799  20.740  67.245  1.00 41.36           C  
ATOM    581  O   GLY A 198      -4.947  21.263  68.359  1.00 40.38           O  
ATOM    582  N   TYR A 199      -4.455  19.480  67.072  1.00 41.83           N  
ATOM    583  CA  TYR A 199      -4.364  18.566  68.192  1.00 43.21           C  
ATOM    584  C   TYR A 199      -3.503  17.371  67.853  1.00 43.54           C  
ATOM    585  O   TYR A 199      -3.259  17.086  66.696  1.00 43.49           O  
ATOM    586  CB  TYR A 199      -5.759  18.107  68.624  1.00 43.10           C  
ATOM    587  CG  TYR A 199      -6.330  17.018  67.736  1.00 46.16           C  
ATOM    588  CD1 TYR A 199      -7.013  17.335  66.568  1.00 47.89           C  
ATOM    589  CD2 TYR A 199      -6.174  15.677  68.059  1.00 48.55           C  
ATOM    590  CE1 TYR A 199      -7.528  16.332  65.738  1.00 50.34           C  
ATOM    591  CE2 TYR A 199      -6.686  14.664  67.231  1.00 51.38           C  
ATOM    592  CZ  TYR A 199      -7.355  15.005  66.080  1.00 51.42           C  
ATOM    593  OH  TYR A 199      -7.863  14.013  65.267  1.00 56.81           O  
ATOM    594  N   PHE A 200      -3.023  16.683  68.877  1.00 44.50           N  
ATOM    595  CA  PHE A 200      -2.407  15.390  68.673  1.00 45.40           C  
ATOM    596  C   PHE A 200      -2.594  14.552  69.925  1.00 46.68           C  
ATOM    597  O   PHE A 200      -3.171  15.004  70.914  1.00 45.22           O  
ATOM    598  CB  PHE A 200      -0.938  15.536  68.257  1.00 45.26           C  
ATOM    599  CG  PHE A 200      -0.103  16.371  69.201  1.00 46.55           C  
ATOM    600  CD1 PHE A 200       0.650  15.765  70.200  1.00 45.38           C  
ATOM    601  CD2 PHE A 200      -0.073  17.758  69.095  1.00 46.60           C  
ATOM    602  CE1 PHE A 200       1.420  16.508  71.058  1.00 46.18           C  
ATOM    603  CE2 PHE A 200       0.714  18.511  69.968  1.00 46.32           C  
ATOM    604  CZ  PHE A 200       1.452  17.886  70.950  1.00 45.36           C  
ATOM    605  N   HIS A 201      -2.177  13.299  69.863  1.00 48.60           N  
ATOM    606  CA  HIS A 201      -2.269  12.438  71.032  1.00 50.97           C  
ATOM    607  C   HIS A 201      -1.179  11.390  71.042  1.00 51.98           C  
ATOM    608  O   HIS A 201      -0.582  11.088  70.022  1.00 51.84           O  
ATOM    609  CB  HIS A 201      -3.671  11.816  71.151  1.00 51.36           C  
ATOM    610  CG  HIS A 201      -4.039  10.892  70.029  1.00 54.19           C  
ATOM    611  ND1 HIS A 201      -3.876   9.524  70.111  1.00 57.63           N  
ATOM    612  CD2 HIS A 201      -4.607  11.131  68.822  1.00 56.87           C  
ATOM    613  CE1 HIS A 201      -4.297   8.964  68.989  1.00 58.21           C  
ATOM    614  NE2 HIS A 201      -4.750   9.916  68.192  1.00 58.22           N  
ATOM    615  N   ASP A 202      -0.880  10.900  72.233  1.00 53.98           N  
ATOM    616  CA  ASP A 202      -0.005   9.750  72.412  1.00 55.02           C  
ATOM    617  C   ASP A 202      -0.789   8.733  73.251  1.00 55.38           C  
ATOM    618  O   ASP A 202      -2.025   8.682  73.152  1.00 55.84           O  
ATOM    619  CB  ASP A 202       1.334  10.186  73.018  1.00 55.25           C  
ATOM    620  CG  ASP A 202       1.188  10.852  74.378  1.00 56.50           C  
ATOM    621  OD1 ASP A 202       0.177  10.596  75.067  1.00 56.17           O  
ATOM    622  OD2 ASP A 202       2.056  11.630  74.846  1.00 56.56           O  
ATOM    623  N   ALA A 203      -0.115   7.934  74.072  1.00 55.82           N  
ATOM    624  CA  ALA A 203      -0.781   6.793  74.721  1.00 55.79           C  
ATOM    625  C   ALA A 203      -1.769   7.210  75.809  1.00 55.44           C  
ATOM    626  O   ALA A 203      -2.904   6.709  75.869  1.00 55.33           O  
ATOM    627  CB  ALA A 203       0.271   5.820  75.300  1.00 56.12           C  
ATOM    628  N   THR A 204      -1.329   8.131  76.661  1.00 54.52           N  
ATOM    629  CA  THR A 204      -2.087   8.507  77.848  1.00 53.99           C  
ATOM    630  C   THR A 204      -2.744   9.902  77.750  1.00 52.64           C  
ATOM    631  O   THR A 204      -3.588  10.235  78.573  1.00 52.04           O  
ATOM    632  CB  THR A 204      -1.153   8.400  79.096  1.00 54.47           C  
ATOM    633  OG1 THR A 204      -1.834   8.821  80.298  1.00 56.19           O  
ATOM    634  CG2 THR A 204       0.061   9.331  78.973  1.00 54.54           C  
ATOM    635  N   ARG A 205      -2.377  10.697  76.744  1.00 51.25           N  
ATOM    636  CA  ARG A 205      -2.780  12.114  76.685  1.00 50.22           C  
ATOM    637  C   ARG A 205      -3.223  12.585  75.310  1.00 47.86           C  
ATOM    638  O   ARG A 205      -2.802  12.053  74.289  1.00 47.02           O  
ATOM    639  CB  ARG A 205      -1.641  13.021  77.146  1.00 50.55           C  
ATOM    640  CG  ARG A 205      -1.294  12.905  78.607  1.00 53.29           C  
ATOM    641  CD  ARG A 205       0.197  12.790  78.875  1.00 58.46           C  
ATOM    642  NE  ARG A 205       0.777  13.988  79.475  1.00 63.04           N  
ATOM    643  CZ  ARG A 205       2.049  14.093  79.871  1.00 67.36           C  
ATOM    644  NH1 ARG A 205       2.482  15.236  80.405  1.00 69.16           N  
ATOM    645  NH2 ARG A 205       2.894  13.067  79.738  1.00 68.58           N  
ATOM    646  N   VAL A 206      -4.118  13.570  75.328  1.00 45.39           N  
ATOM    647  CA  VAL A 206      -4.527  14.332  74.160  1.00 43.83           C  
ATOM    648  C   VAL A 206      -4.009  15.764  74.372  1.00 42.36           C  
ATOM    649  O   VAL A 206      -4.012  16.279  75.490  1.00 41.94           O  
ATOM    650  CB  VAL A 206      -6.072  14.321  73.981  1.00 43.88           C  
ATOM    651  CG1 VAL A 206      -6.489  15.128  72.748  1.00 44.67           C  
ATOM    652  CG2 VAL A 206      -6.595  12.894  73.864  1.00 44.28           C  
ATOM    653  N   TYR A 207      -3.541  16.384  73.302  1.00 40.96           N  
ATOM    654  CA  TYR A 207      -2.919  17.702  73.366  1.00 40.41           C  
ATOM    655  C   TYR A 207      -3.600  18.634  72.400  1.00 39.36           C  
ATOM    656  O   TYR A 207      -3.551  18.406  71.185  1.00 39.50           O  
ATOM    657  CB  TYR A 207      -1.465  17.626  72.967  1.00 40.13           C  
ATOM    658  CG  TYR A 207      -0.612  16.744  73.820  1.00 42.22           C  
ATOM    659  CD1 TYR A 207       0.012  17.237  74.951  1.00 43.36           C  
ATOM    660  CD2 TYR A 207      -0.394  15.412  73.471  1.00 44.38           C  
ATOM    661  CE1 TYR A 207       0.826  16.428  75.716  1.00 46.11           C  
ATOM    662  CE2 TYR A 207       0.427  14.601  74.224  1.00 45.79           C  
ATOM    663  CZ  TYR A 207       1.022  15.111  75.348  1.00 46.64           C  
ATOM    664  OH  TYR A 207       1.819  14.314  76.120  1.00 50.66           O  
ATOM    665  N   LEU A 208      -4.249  19.664  72.926  1.00 37.49           N  
ATOM    666  CA  LEU A 208      -4.819  20.703  72.088  1.00 36.07           C  
ATOM    667  C   LEU A 208      -3.834  21.862  71.940  1.00 34.75           C  
ATOM    668  O   LEU A 208      -3.321  22.409  72.930  1.00 35.32           O  
ATOM    669  CB  LEU A 208      -6.153  21.192  72.649  1.00 36.04           C  
ATOM    670  CG  LEU A 208      -7.415  20.439  72.247  1.00 38.23           C  
ATOM    671  CD1 LEU A 208      -7.179  18.941  72.127  1.00 40.62           C  
ATOM    672  CD2 LEU A 208      -8.532  20.743  73.215  1.00 38.32           C  
ATOM    673  N   ILE A 209      -3.581  22.235  70.695  1.00 32.17           N  
ATOM    674  CA  ILE A 209      -2.695  23.325  70.369  1.00 32.24           C  
ATOM    675  C   ILE A 209      -3.524  24.589  70.234  1.00 31.98           C  
ATOM    676  O   ILE A 209      -4.319  24.693  69.327  1.00 31.86           O  
ATOM    677  CB  ILE A 209      -1.965  23.049  69.058  1.00 32.18           C  
ATOM    678  CG1 ILE A 209      -1.308  21.664  69.082  1.00 34.61           C  
ATOM    679  CG2 ILE A 209      -0.960  24.116  68.806  1.00 31.66           C  
ATOM    680  CD1 ILE A 209      -0.755  21.242  67.703  1.00 37.30           C  
ATOM    681  N   LEU A 210      -3.345  25.520  71.173  1.00 30.74           N  
ATOM    682  CA  LEU A 210      -4.151  26.713  71.294  1.00 30.86           C  
ATOM    683  C   LEU A 210      -3.330  27.978  71.074  1.00 29.91           C  
ATOM    684  O   LEU A 210      -2.138  28.025  71.359  1.00 30.08           O  
ATOM    685  CB  LEU A 210      -4.778  26.768  72.704  1.00 30.59           C  
ATOM    686  CG  LEU A 210      -5.630  25.595  73.171  1.00 32.11           C  
ATOM    687  CD1 LEU A 210      -6.123  25.889  74.576  1.00 32.90           C  
ATOM    688  CD2 LEU A 210      -6.796  25.360  72.202  1.00 34.20           C  
ATOM    689  N   GLU A 211      -3.992  29.016  70.597  1.00 30.93           N  
ATOM    690  CA  GLU A 211      -3.475  30.368  70.680  1.00 31.32           C  
ATOM    691  C   GLU A 211      -3.148  30.670  72.161  1.00 30.89           C  
ATOM    692  O   GLU A 211      -3.935  30.392  73.041  1.00 30.29           O  
ATOM    693  CB  GLU A 211      -4.519  31.322  70.153  1.00 32.23           C  
ATOM    694  CG  GLU A 211      -4.150  32.774  70.276  1.00 35.92           C  
ATOM    695  CD  GLU A 211      -5.304  33.689  69.919  1.00 38.32           C  
ATOM    696  OE1 GLU A 211      -5.100  34.893  70.120  1.00 40.92           O  
ATOM    697  OE2 GLU A 211      -6.376  33.219  69.415  1.00 37.24           O  
ATOM    698  N   TYR A 212      -1.957  31.179  72.401  1.00 30.44           N  
ATOM    699  CA  TYR A 212      -1.556  31.672  73.709  1.00 30.44           C  
ATOM    700  C   TYR A 212      -2.198  33.060  73.984  1.00 30.69           C  
ATOM    701  O   TYR A 212      -2.104  33.967  73.162  1.00 29.81           O  
ATOM    702  CB  TYR A 212      -0.035  31.735  73.722  1.00 30.72           C  
ATOM    703  CG  TYR A 212       0.593  32.491  74.853  1.00 31.58           C  
ATOM    704  CD1 TYR A 212       1.535  33.480  74.598  1.00 33.90           C  
ATOM    705  CD2 TYR A 212       0.247  32.232  76.159  1.00 31.41           C  
ATOM    706  CE1 TYR A 212       2.128  34.178  75.645  1.00 36.18           C  
ATOM    707  CE2 TYR A 212       0.826  32.932  77.206  1.00 33.71           C  
ATOM    708  CZ  TYR A 212       1.778  33.901  76.921  1.00 34.64           C  
ATOM    709  OH  TYR A 212       2.379  34.610  77.932  1.00 37.86           O  
ATOM    710  N   ALA A 213      -2.860  33.183  75.144  1.00 31.22           N  
ATOM    711  CA  ALA A 213      -3.459  34.436  75.612  1.00 32.38           C  
ATOM    712  C   ALA A 213      -2.569  34.983  76.739  1.00 32.89           C  
ATOM    713  O   ALA A 213      -2.625  34.518  77.854  1.00 33.26           O  
ATOM    714  CB  ALA A 213      -4.857  34.234  76.103  1.00 32.08           C  
ATOM    715  N   PRO A 214      -1.728  35.945  76.413  1.00 34.13           N  
ATOM    716  CA  PRO A 214      -0.652  36.372  77.313  1.00 34.72           C  
ATOM    717  C   PRO A 214      -1.077  37.089  78.597  1.00 35.51           C  
ATOM    718  O   PRO A 214      -0.367  36.988  79.600  1.00 36.97           O  
ATOM    719  CB  PRO A 214       0.217  37.280  76.437  1.00 34.58           C  
ATOM    720  CG  PRO A 214      -0.377  37.295  75.092  1.00 36.26           C  
ATOM    721  CD  PRO A 214      -1.716  36.660  75.130  1.00 34.03           C  
ATOM    722  N   LEU A 215      -2.211  37.768  78.588  1.00 36.07           N  
ATOM    723  CA  LEU A 215      -2.659  38.522  79.760  1.00 36.86           C  
ATOM    724  C   LEU A 215      -3.547  37.720  80.710  1.00 36.54           C  
ATOM    725  O   LEU A 215      -4.099  38.270  81.647  1.00 36.66           O  
ATOM    726  CB  LEU A 215      -3.351  39.812  79.312  1.00 36.74           C  
ATOM    727  CG  LEU A 215      -2.436  41.047  79.218  1.00 38.09           C  
ATOM    728  CD1 LEU A 215      -1.166  40.768  78.449  1.00 38.47           C  
ATOM    729  CD2 LEU A 215      -3.198  42.207  78.591  1.00 38.31           C  
ATOM    730  N   GLY A 216      -3.675  36.419  80.467  1.00 36.19           N  
ATOM    731  CA  GLY A 216      -4.358  35.519  81.381  1.00 35.62           C  
ATOM    732  C   GLY A 216      -5.871  35.539  81.281  1.00 34.64           C  
ATOM    733  O   GLY A 216      -6.432  35.883  80.242  1.00 34.15           O  
ATOM    734  N   THR A 217      -6.531  35.161  82.367  1.00 33.65           N  
ATOM    735  CA  THR A 217      -7.990  35.103  82.411  1.00 33.33           C  
ATOM    736  C   THR A 217      -8.635  36.343  83.030  1.00 33.38           C  
ATOM    737  O   THR A 217      -8.046  37.068  83.819  1.00 30.84           O  
ATOM    738  CB  THR A 217      -8.500  33.910  83.231  1.00 33.57           C  
ATOM    739  OG1 THR A 217      -8.059  34.035  84.591  1.00 32.62           O  
ATOM    740  CG2 THR A 217      -7.938  32.599  82.749  1.00 34.41           C  
ATOM    741  N   VAL A 218      -9.900  36.510  82.699  1.00 33.45           N  
ATOM    742  CA  VAL A 218     -10.725  37.520  83.303  1.00 34.17           C  
ATOM    743  C   VAL A 218     -10.931  37.126  84.769  1.00 34.20           C  
ATOM    744  O   VAL A 218     -10.991  37.995  85.608  1.00 33.30           O  
ATOM    745  CB  VAL A 218     -12.012  37.689  82.534  1.00 34.36           C  
ATOM    746  CG1 VAL A 218     -13.010  38.512  83.306  1.00 36.03           C  
ATOM    747  CG2 VAL A 218     -11.692  38.306  81.179  1.00 34.68           C  
ATOM    748  N   TYR A 219     -10.970  35.828  85.064  1.00 35.24           N  
ATOM    749  CA  TYR A 219     -11.048  35.341  86.447  1.00 36.52           C  
ATOM    750  C   TYR A 219      -9.911  35.909  87.320  1.00 37.02           C  
ATOM    751  O   TYR A 219     -10.160  36.411  88.404  1.00 36.65           O  
ATOM    752  CB  TYR A 219     -11.021  33.816  86.469  1.00 37.28           C  
ATOM    753  CG  TYR A 219     -11.106  33.181  87.844  1.00 38.91           C  
ATOM    754  CD1 TYR A 219     -12.325  32.792  88.370  1.00 41.94           C  
ATOM    755  CD2 TYR A 219      -9.957  32.954  88.602  1.00 42.13           C  
ATOM    756  CE1 TYR A 219     -12.415  32.200  89.621  1.00 45.92           C  
ATOM    757  CE2 TYR A 219     -10.024  32.368  89.851  1.00 44.55           C  
ATOM    758  CZ  TYR A 219     -11.258  31.984  90.359  1.00 47.05           C  
ATOM    759  OH  TYR A 219     -11.349  31.388  91.599  1.00 50.55           O  
ATOM    760  N   ARG A 220      -8.684  35.851  86.831  1.00 37.97           N  
ATOM    761  CA  ARG A 220      -7.519  36.373  87.566  1.00 39.12           C  
ATOM    762  C   ARG A 220      -7.559  37.896  87.663  1.00 39.06           C  
ATOM    763  O   ARG A 220      -7.253  38.480  88.702  1.00 38.02           O  
ATOM    764  CB  ARG A 220      -6.215  35.927  86.915  1.00 40.08           C  
ATOM    765  CG  ARG A 220      -5.093  35.624  87.927  1.00 44.61           C  
ATOM    766  CD  ARG A 220      -3.782  35.180  87.290  1.00 51.10           C  
ATOM    767  NE  ARG A 220      -3.061  36.330  86.746  1.00 55.51           N  
ATOM    768  CZ  ARG A 220      -2.578  36.432  85.500  1.00 61.06           C  
ATOM    769  NH1 ARG A 220      -1.950  37.547  85.123  1.00 62.82           N  
ATOM    770  NH2 ARG A 220      -2.707  35.442  84.622  1.00 63.13           N  
ATOM    771  N   GLU A 221      -7.978  38.519  86.577  1.00 39.65           N  
ATOM    772  CA  GLU A 221      -8.140  39.960  86.490  1.00 41.24           C  
ATOM    773  C   GLU A 221      -9.123  40.460  87.561  1.00 41.32           C  
ATOM    774  O   GLU A 221      -8.849  41.454  88.235  1.00 40.82           O  
ATOM    775  CB  GLU A 221      -8.592  40.303  85.061  1.00 42.10           C  
ATOM    776  CG  GLU A 221      -8.452  41.740  84.621  1.00 47.18           C  
ATOM    777  CD  GLU A 221      -7.073  42.306  84.874  1.00 53.76           C  
ATOM    778  OE1 GLU A 221      -6.228  42.272  83.959  1.00 58.07           O  
ATOM    779  OE2 GLU A 221      -6.842  42.800  86.003  1.00 59.85           O  
ATOM    780  N   LEU A 222     -10.217  39.724  87.761  1.00 41.23           N  
ATOM    781  CA  LEU A 222     -11.213  40.037  88.771  1.00 42.43           C  
ATOM    782  C   LEU A 222     -10.686  39.810  90.174  1.00 43.41           C  
ATOM    783  O   LEU A 222     -10.994  40.572  91.078  1.00 43.09           O  
ATOM    784  CB  LEU A 222     -12.472  39.171  88.619  1.00 42.77           C  
ATOM    785  CG  LEU A 222     -13.882  39.731  88.426  1.00 44.82           C  
ATOM    786  CD1 LEU A 222     -14.004  41.239  88.494  1.00 44.93           C  
ATOM    787  CD2 LEU A 222     -14.414  39.204  87.100  1.00 47.14           C  
ATOM    788  N   GLN A 223      -9.936  38.751  90.387  1.00 43.94           N  
ATOM    789  CA  GLN A 223      -9.432  38.531  91.732  1.00 45.78           C  
ATOM    790  C   GLN A 223      -8.332  39.565  92.072  1.00 45.49           C  
ATOM    791  O   GLN A 223      -8.198  39.955  93.221  1.00 45.97           O  
ATOM    792  CB  GLN A 223      -9.071  37.040  91.970  1.00 46.61           C  
ATOM    793  CG  GLN A 223      -7.659  36.575  91.693  1.00 49.33           C  
ATOM    794  CD  GLN A 223      -7.530  35.037  91.810  1.00 53.27           C  
ATOM    795  OE1 GLN A 223      -6.934  34.373  90.942  1.00 54.79           O  
ATOM    796  NE2 GLN A 223      -8.090  34.476  92.884  1.00 55.62           N  
ATOM    797  N   LYS A 224      -7.646  40.089  91.059  1.00 45.09           N  
ATOM    798  CA  LYS A 224      -6.642  41.137  91.234  1.00 45.46           C  
ATOM    799  C   LYS A 224      -7.318  42.473  91.596  1.00 44.99           C  
ATOM    800  O   LYS A 224      -6.957  43.094  92.586  1.00 44.79           O  
ATOM    801  CB  LYS A 224      -5.799  41.267  89.962  1.00 45.98           C  
ATOM    802  CG  LYS A 224      -4.698  42.340  89.975  1.00 48.69           C  
ATOM    803  CD  LYS A 224      -4.078  42.542  88.569  1.00 51.35           C  
ATOM    804  CE  LYS A 224      -4.722  43.698  87.808  1.00 53.73           C  
ATOM    805  NZ  LYS A 224      -4.308  43.791  86.340  1.00 54.54           N  
ATOM    806  N   LEU A 225      -8.320  42.869  90.815  1.00 43.75           N  
ATOM    807  CA  LEU A 225      -9.013  44.158  90.952  1.00 43.63           C  
ATOM    808  C   LEU A 225     -10.252  44.159  91.858  1.00 43.12           C  
ATOM    809  O   LEU A 225     -10.774  45.228  92.192  1.00 42.64           O  
ATOM    810  CB  LEU A 225      -9.455  44.640  89.571  1.00 43.17           C  
ATOM    811  CG  LEU A 225      -8.317  44.853  88.583  1.00 44.85           C  
ATOM    812  CD1 LEU A 225      -8.855  45.207  87.235  1.00 44.91           C  
ATOM    813  CD2 LEU A 225      -7.358  45.957  89.107  1.00 46.71           C  
ATOM    814  N   SER A 226     -10.725  42.974  92.230  1.00 42.71           N  
ATOM    815  CA  SER A 226     -11.989  42.785  92.954  1.00 43.12           C  
ATOM    816  C   SER A 226     -13.287  43.049  92.143  1.00 41.92           C  
ATOM    817  O   SER A 226     -14.219  42.246  92.184  1.00 41.66           O  
ATOM    818  CB  SER A 226     -11.991  43.609  94.247  1.00 43.89           C  
ATOM    819  OG  SER A 226     -12.955  43.081  95.137  1.00 48.08           O  
ATOM    820  N   LYS A 227     -13.361  44.179  91.450  1.00 40.74           N  
ATOM    821  CA  LYS A 227     -14.444  44.451  90.515  1.00 40.13           C  
ATOM    822  C   LYS A 227     -13.999  45.488  89.491  1.00 38.89           C  
ATOM    823  O   LYS A 227     -12.990  46.174  89.667  1.00 37.41           O  
ATOM    824  CB  LYS A 227     -15.703  44.907  91.239  1.00 41.16           C  
ATOM    825  CG  LYS A 227     -15.478  46.033  92.232  1.00 43.41           C  
ATOM    826  CD  LYS A 227     -16.724  46.315  93.052  1.00 46.67           C  
ATOM    827  CE  LYS A 227     -16.935  47.813  93.223  1.00 48.75           C  
ATOM    828  NZ  LYS A 227     -15.776  48.405  93.977  1.00 48.57           N  
ATOM    829  N   PHE A 228     -14.734  45.579  88.393  1.00 36.99           N  
ATOM    830  CA  PHE A 228     -14.308  46.396  87.283  1.00 36.41           C  
ATOM    831  C   PHE A 228     -15.127  47.669  87.266  1.00 37.09           C  
ATOM    832  O   PHE A 228     -16.280  47.680  87.712  1.00 36.98           O  
ATOM    833  CB  PHE A 228     -14.519  45.653  85.965  1.00 35.26           C  
ATOM    834  CG  PHE A 228     -13.708  44.384  85.814  1.00 33.98           C  
ATOM    835  CD1 PHE A 228     -12.542  44.159  86.530  1.00 32.63           C  
ATOM    836  CD2 PHE A 228     -14.106  43.428  84.892  1.00 34.23           C  
ATOM    837  CE1 PHE A 228     -11.805  43.022  86.344  1.00 35.21           C  
ATOM    838  CE2 PHE A 228     -13.386  42.275  84.725  1.00 34.00           C  
ATOM    839  CZ  PHE A 228     -12.221  42.068  85.444  1.00 34.71           C  
ATOM    840  N   ASP A 229     -14.549  48.737  86.722  1.00 38.17           N  
ATOM    841  CA  ASP A 229     -15.330  49.947  86.483  1.00 39.65           C  
ATOM    842  C   ASP A 229     -16.243  49.716  85.286  1.00 39.32           C  
ATOM    843  O   ASP A 229     -16.154  48.680  84.602  1.00 38.06           O  
ATOM    844  CB  ASP A 229     -14.442  51.208  86.341  1.00 40.69           C  
ATOM    845  CG  ASP A 229     -13.496  51.171  85.161  1.00 43.80           C  
ATOM    846  OD1 ASP A 229     -13.648  50.347  84.242  1.00 46.66           O  
ATOM    847  OD2 ASP A 229     -12.530  51.967  85.067  1.00 50.39           O  
ATOM    848  N   GLU A 230     -17.127  50.668  85.030  1.00 39.79           N  
ATOM    849  CA  GLU A 230     -18.157  50.488  84.017  1.00 40.01           C  
ATOM    850  C   GLU A 230     -17.550  50.432  82.621  1.00 39.17           C  
ATOM    851  O   GLU A 230     -18.099  49.823  81.712  1.00 37.51           O  
ATOM    852  CB  GLU A 230     -19.162  51.627  84.100  1.00 41.02           C  
ATOM    853  CG  GLU A 230     -19.947  51.635  85.395  1.00 43.66           C  
ATOM    854  CD  GLU A 230     -21.154  52.545  85.308  1.00 47.91           C  
ATOM    855  OE1 GLU A 230     -22.281  52.053  85.491  1.00 51.01           O  
ATOM    856  OE2 GLU A 230     -20.977  53.750  85.028  1.00 51.77           O  
ATOM    857  N   GLN A 231     -16.406  51.082  82.457  1.00 39.06           N  
ATOM    858  CA  GLN A 231     -15.763  51.165  81.161  1.00 38.96           C  
ATOM    859  C   GLN A 231     -15.169  49.800  80.785  1.00 38.06           C  
ATOM    860  O   GLN A 231     -15.333  49.329  79.675  1.00 38.53           O  
ATOM    861  CB  GLN A 231     -14.665  52.238  81.201  1.00 39.95           C  
ATOM    862  CG  GLN A 231     -15.218  53.698  81.305  1.00 42.31           C  
ATOM    863  CD  GLN A 231     -16.071  54.018  82.550  1.00 44.65           C  
ATOM    864  OE1 GLN A 231     -15.680  53.735  83.706  1.00 43.49           O  
ATOM    865  NE2 GLN A 231     -17.236  54.626  82.307  1.00 46.32           N  
ATOM    866  N   ARG A 232     -14.470  49.173  81.714  1.00 36.54           N  
ATOM    867  CA  ARG A 232     -13.835  47.889  81.434  1.00 36.39           C  
ATOM    868  C   ARG A 232     -14.914  46.826  81.239  1.00 34.76           C  
ATOM    869  O   ARG A 232     -14.820  46.022  80.328  1.00 33.70           O  
ATOM    870  CB  ARG A 232     -12.884  47.486  82.567  1.00 36.81           C  
ATOM    871  CG  ARG A 232     -12.221  46.114  82.366  1.00 38.96           C  
ATOM    872  CD  ARG A 232     -11.420  45.633  83.550  1.00 42.71           C  
ATOM    873  NE  ARG A 232     -10.351  46.566  83.885  1.00 47.99           N  
ATOM    874  CZ  ARG A 232      -9.144  46.607  83.327  1.00 51.03           C  
ATOM    875  NH1 ARG A 232      -8.786  45.756  82.366  1.00 52.26           N  
ATOM    876  NH2 ARG A 232      -8.278  47.519  83.755  1.00 52.63           N  
ATOM    877  N   THR A 233     -15.941  46.856  82.088  1.00 33.35           N  
ATOM    878  CA  THR A 233     -17.074  45.951  81.998  1.00 32.99           C  
ATOM    879  C   THR A 233     -17.786  46.058  80.662  1.00 33.02           C  
ATOM    880  O   THR A 233     -17.929  45.063  79.962  1.00 32.73           O  
ATOM    881  CB  THR A 233     -18.080  46.260  83.098  1.00 33.14           C  
ATOM    882  OG1 THR A 233     -17.480  45.966  84.353  1.00 29.92           O  
ATOM    883  CG2 THR A 233     -19.312  45.328  83.013  1.00 32.18           C  
ATOM    884  N   ALA A 234     -18.270  47.259  80.354  1.00 32.88           N  
ATOM    885  CA  ALA A 234     -18.953  47.533  79.088  1.00 32.84           C  
ATOM    886  C   ALA A 234     -18.120  47.108  77.897  1.00 33.17           C  
ATOM    887  O   ALA A 234     -18.661  46.583  76.918  1.00 33.66           O  
ATOM    888  CB  ALA A 234     -19.309  48.982  78.973  1.00 32.78           C  
ATOM    889  N   THR A 235     -16.813  47.339  77.968  1.00 33.35           N  
ATOM    890  CA  THR A 235     -15.905  46.920  76.895  1.00 33.94           C  
ATOM    891  C   THR A 235     -15.836  45.389  76.756  1.00 33.87           C  
ATOM    892  O   THR A 235     -15.957  44.855  75.642  1.00 34.02           O  
ATOM    893  CB  THR A 235     -14.513  47.518  77.098  1.00 33.88           C  
ATOM    894  OG1 THR A 235     -14.614  48.938  77.066  1.00 35.42           O  
ATOM    895  CG2 THR A 235     -13.577  47.186  75.938  1.00 35.38           C  
ATOM    896  N   TYR A 236     -15.722  44.679  77.875  1.00 33.24           N  
ATOM    897  CA  TYR A 236     -15.690  43.200  77.846  1.00 32.64           C  
ATOM    898  C   TYR A 236     -17.026  42.610  77.360  1.00 32.24           C  
ATOM    899  O   TYR A 236     -17.052  41.651  76.621  1.00 32.08           O  
ATOM    900  CB  TYR A 236     -15.369  42.660  79.234  1.00 32.86           C  
ATOM    901  CG  TYR A 236     -13.926  42.747  79.675  1.00 34.51           C  
ATOM    902  CD1 TYR A 236     -12.889  42.966  78.774  1.00 36.07           C  
ATOM    903  CD2 TYR A 236     -13.598  42.597  81.009  1.00 37.91           C  
ATOM    904  CE1 TYR A 236     -11.571  43.027  79.201  1.00 37.97           C  
ATOM    905  CE2 TYR A 236     -12.281  42.656  81.447  1.00 38.41           C  
ATOM    906  CZ  TYR A 236     -11.274  42.870  80.546  1.00 38.56           C  
ATOM    907  OH  TYR A 236      -9.973  42.933  80.986  1.00 38.82           O  
ATOM    908  N   ILE A 237     -18.133  43.207  77.775  1.00 32.50           N  
ATOM    909  CA  ILE A 237     -19.452  42.775  77.331  1.00 32.98           C  
ATOM    910  C   ILE A 237     -19.557  42.970  75.840  1.00 32.92           C  
ATOM    911  O   ILE A 237     -20.053  42.093  75.159  1.00 31.43           O  
ATOM    912  CB  ILE A 237     -20.570  43.508  78.063  1.00 32.56           C  
ATOM    913  CG1 ILE A 237     -20.549  43.101  79.538  1.00 33.39           C  
ATOM    914  CG2 ILE A 237     -21.938  43.144  77.501  1.00 33.85           C  
ATOM    915  CD1 ILE A 237     -20.581  41.539  79.796  1.00 35.03           C  
ATOM    916  N   THR A 238     -19.105  44.114  75.340  1.00 32.44           N  
ATOM    917  CA  THR A 238     -19.105  44.330  73.890  1.00 33.27           C  
ATOM    918  C   THR A 238     -18.300  43.286  73.135  1.00 33.51           C  
ATOM    919  O   THR A 238     -18.762  42.783  72.143  1.00 34.55           O  
ATOM    920  CB  THR A 238     -18.568  45.714  73.559  1.00 32.98           C  
ATOM    921  OG1 THR A 238     -19.435  46.690  74.142  1.00 33.76           O  
ATOM    922  CG2 THR A 238     -18.621  45.979  72.046  1.00 35.64           C  
ATOM    923  N   GLU A 239     -17.072  43.013  73.558  1.00 33.89           N  
ATOM    924  CA  GLU A 239     -16.259  41.972  72.943  1.00 35.15           C  
ATOM    925  C   GLU A 239     -16.928  40.605  72.994  1.00 34.50           C  
ATOM    926  O   GLU A 239     -16.850  39.847  72.057  1.00 33.89           O  
ATOM    927  CB  GLU A 239     -14.878  41.901  73.587  1.00 36.09           C  
ATOM    928  CG  GLU A 239     -14.053  43.158  73.299  1.00 40.96           C  
ATOM    929  CD  GLU A 239     -12.735  43.242  74.065  1.00 47.69           C  
ATOM    930  OE1 GLU A 239     -11.701  43.530  73.410  1.00 55.94           O  
ATOM    931  OE2 GLU A 239     -12.705  43.051  75.304  1.00 50.65           O  
ATOM    932  N   LEU A 240     -17.570  40.301  74.111  1.00 34.38           N  
ATOM    933  CA  LEU A 240     -18.272  39.046  74.305  1.00 34.38           C  
ATOM    934  C   LEU A 240     -19.454  38.976  73.378  1.00 34.15           C  
ATOM    935  O   LEU A 240     -19.695  37.964  72.761  1.00 33.80           O  
ATOM    936  CB  LEU A 240     -18.795  38.961  75.744  1.00 35.16           C  
ATOM    937  CG  LEU A 240     -17.808  38.339  76.707  1.00 38.92           C  
ATOM    938  CD1 LEU A 240     -18.058  38.807  78.160  1.00 41.39           C  
ATOM    939  CD2 LEU A 240     -17.951  36.832  76.579  1.00 43.93           C  
ATOM    940  N   ALA A 241     -20.206  40.059  73.300  1.00 33.97           N  
ATOM    941  CA  ALA A 241     -21.394  40.099  72.462  1.00 34.10           C  
ATOM    942  C   ALA A 241     -21.048  39.955  70.979  1.00 35.14           C  
ATOM    943  O   ALA A 241     -21.807  39.339  70.230  1.00 35.82           O  
ATOM    944  CB  ALA A 241     -22.160  41.355  72.714  1.00 33.33           C  
ATOM    945  N   ASN A 242     -19.910  40.504  70.555  1.00 36.02           N  
ATOM    946  CA  ASN A 242     -19.462  40.356  69.165  1.00 36.51           C  
ATOM    947  C   ASN A 242     -19.053  38.916  68.892  1.00 35.99           C  
ATOM    948  O   ASN A 242     -19.432  38.343  67.886  1.00 36.23           O  
ATOM    949  CB  ASN A 242     -18.282  41.273  68.854  1.00 37.06           C  
ATOM    950  CG  ASN A 242     -18.666  42.728  68.808  1.00 38.35           C  
ATOM    951  OD1 ASN A 242     -19.762  43.069  68.366  1.00 44.17           O  
ATOM    952  ND2 ASN A 242     -17.745  43.604  69.224  1.00 38.93           N  
ATOM    953  N   ALA A 243     -18.269  38.334  69.788  1.00 35.61           N  
ATOM    954  CA  ALA A 243     -17.857  36.943  69.645  1.00 35.86           C  
ATOM    955  C   ALA A 243     -19.084  36.042  69.595  1.00 35.90           C  
ATOM    956  O   ALA A 243     -19.141  35.124  68.774  1.00 36.11           O  
ATOM    957  CB  ALA A 243     -16.947  36.526  70.793  1.00 35.89           C  
ATOM    958  N   LEU A 244     -20.065  36.315  70.456  1.00 35.65           N  
ATOM    959  CA  LEU A 244     -21.290  35.500  70.502  1.00 36.45           C  
ATOM    960  C   LEU A 244     -22.167  35.694  69.271  1.00 36.97           C  
ATOM    961  O   LEU A 244     -22.822  34.752  68.834  1.00 37.00           O  
ATOM    962  CB  LEU A 244     -22.118  35.765  71.762  1.00 35.73           C  
ATOM    963  CG  LEU A 244     -21.502  35.239  73.064  1.00 36.49           C  
ATOM    964  CD1 LEU A 244     -22.406  35.626  74.192  1.00 37.00           C  
ATOM    965  CD2 LEU A 244     -21.303  33.741  73.021  1.00 37.98           C  
ATOM    966  N   SER A 245     -22.190  36.901  68.723  1.00 37.99           N  
ATOM    967  CA  SER A 245     -22.941  37.155  67.488  1.00 38.63           C  
ATOM    968  C   SER A 245     -22.380  36.280  66.387  1.00 39.10           C  
ATOM    969  O   SER A 245     -23.144  35.661  65.644  1.00 40.36           O  
ATOM    970  CB  SER A 245     -22.841  38.607  67.044  1.00 38.67           C  
ATOM    971  OG  SER A 245     -23.518  39.458  67.934  1.00 40.38           O  
ATOM    972  N   TYR A 246     -21.054  36.224  66.297  1.00 38.77           N  
ATOM    973  CA  TYR A 246     -20.374  35.388  65.316  1.00 39.08           C  
ATOM    974  C   TYR A 246     -20.727  33.906  65.516  1.00 39.19           C  
ATOM    975  O   TYR A 246     -21.125  33.232  64.575  1.00 39.03           O  
ATOM    976  CB  TYR A 246     -18.864  35.648  65.369  1.00 38.78           C  
ATOM    977  CG  TYR A 246     -18.030  34.781  64.461  1.00 39.73           C  
ATOM    978  CD1 TYR A 246     -17.783  35.141  63.139  1.00 43.20           C  
ATOM    979  CD2 TYR A 246     -17.490  33.604  64.925  1.00 40.15           C  
ATOM    980  CE1 TYR A 246     -17.015  34.334  62.321  1.00 43.10           C  
ATOM    981  CE2 TYR A 246     -16.729  32.797  64.128  1.00 42.85           C  
ATOM    982  CZ  TYR A 246     -16.483  33.165  62.822  1.00 43.49           C  
ATOM    983  OH  TYR A 246     -15.710  32.325  62.046  1.00 44.45           O  
ATOM    984  N   CYS A 247     -20.640  33.415  66.749  1.00 39.27           N  
ATOM    985  CA  CYS A 247     -21.038  32.052  67.085  1.00 39.61           C  
ATOM    986  C   CYS A 247     -22.487  31.708  66.754  1.00 39.83           C  
ATOM    987  O   CYS A 247     -22.747  30.684  66.121  1.00 39.99           O  
ATOM    988  CB  CYS A 247     -20.827  31.782  68.587  1.00 39.95           C  
ATOM    989  SG  CYS A 247     -19.097  31.615  69.006  1.00 42.55           S  
ATOM    990  N   HIS A 248     -23.420  32.522  67.238  1.00 39.50           N  
ATOM    991  CA  HIS A 248     -24.847  32.267  67.075  1.00 40.00           C  
ATOM    992  C   HIS A 248     -25.257  32.344  65.605  1.00 41.21           C  
ATOM    993  O   HIS A 248     -26.228  31.697  65.190  1.00 41.84           O  
ATOM    994  CB  HIS A 248     -25.695  33.236  67.897  1.00 40.09           C  
ATOM    995  CG  HIS A 248     -25.498  33.105  69.379  1.00 37.55           C  
ATOM    996  ND1 HIS A 248     -25.902  34.070  70.270  1.00 39.08           N  
ATOM    997  CD2 HIS A 248     -24.910  32.138  70.120  1.00 37.52           C  
ATOM    998  CE1 HIS A 248     -25.575  33.702  71.498  1.00 38.21           C  
ATOM    999  NE2 HIS A 248     -24.983  32.526  71.439  1.00 35.39           N  
ATOM   1000  N   SER A 249     -24.503  33.093  64.813  1.00 42.02           N  
ATOM   1001  CA  SER A 249     -24.775  33.174  63.382  1.00 43.10           C  
ATOM   1002  C   SER A 249     -24.641  31.785  62.772  1.00 44.22           C  
ATOM   1003  O   SER A 249     -25.321  31.471  61.802  1.00 45.22           O  
ATOM   1004  CB  SER A 249     -23.831  34.167  62.696  1.00 42.51           C  
ATOM   1005  OG  SER A 249     -22.565  33.585  62.475  1.00 42.35           O  
ATOM   1006  N   LYS A 250     -23.750  30.969  63.338  1.00 45.10           N  
ATOM   1007  CA  LYS A 250     -23.589  29.569  62.949  1.00 45.70           C  
ATOM   1008  C   LYS A 250     -24.352  28.594  63.865  1.00 45.47           C  
ATOM   1009  O   LYS A 250     -24.136  27.389  63.824  1.00 45.99           O  
ATOM   1010  CB  LYS A 250     -22.110  29.236  62.932  1.00 46.42           C  
ATOM   1011  CG  LYS A 250     -21.320  30.114  61.963  1.00 48.11           C  
ATOM   1012  CD  LYS A 250     -19.830  30.076  62.238  1.00 49.34           C  
ATOM   1013  CE  LYS A 250     -19.103  31.134  61.421  1.00 51.28           C  
ATOM   1014  NZ  LYS A 250     -17.925  30.578  60.698  1.00 54.46           N  
ATOM   1015  N   ARG A 251     -25.256  29.134  64.671  1.00 44.99           N  
ATOM   1016  CA  ARG A 251     -26.016  28.391  65.668  1.00 44.90           C  
ATOM   1017  C   ARG A 251     -25.143  27.666  66.691  1.00 43.29           C  
ATOM   1018  O   ARG A 251     -25.590  26.715  67.323  1.00 43.86           O  
ATOM   1019  CB  ARG A 251     -26.986  27.407  64.998  1.00 45.86           C  
ATOM   1020  CG  ARG A 251     -28.130  28.085  64.249  1.00 48.68           C  
ATOM   1021  CD  ARG A 251     -29.362  28.299  65.097  1.00 51.63           C  
ATOM   1022  NE  ARG A 251     -30.486  27.444  64.753  1.00 54.98           N  
ATOM   1023  CZ  ARG A 251     -31.577  27.308  65.512  1.00 56.71           C  
ATOM   1024  NH1 ARG A 251     -32.556  26.515  65.113  1.00 57.41           N  
ATOM   1025  NH2 ARG A 251     -31.693  27.954  66.677  1.00 57.40           N  
ATOM   1026  N   VAL A 252     -23.905  28.109  66.868  1.00 41.05           N  
ATOM   1027  CA  VAL A 252     -23.060  27.536  67.908  1.00 39.23           C  
ATOM   1028  C   VAL A 252     -23.379  28.292  69.190  1.00 38.12           C  
ATOM   1029  O   VAL A 252     -23.316  29.515  69.228  1.00 37.17           O  
ATOM   1030  CB  VAL A 252     -21.558  27.642  67.556  1.00 39.49           C  
ATOM   1031  CG1 VAL A 252     -20.663  27.308  68.771  1.00 39.56           C  
ATOM   1032  CG2 VAL A 252     -21.235  26.727  66.392  1.00 38.61           C  
ATOM   1033  N   ILE A 253     -23.768  27.549  70.216  1.00 37.17           N  
ATOM   1034  CA  ILE A 253     -23.975  28.103  71.554  1.00 36.09           C  
ATOM   1035  C   ILE A 253     -22.846  27.597  72.441  1.00 34.78           C  
ATOM   1036  O   ILE A 253     -22.447  26.436  72.355  1.00 34.01           O  
ATOM   1037  CB  ILE A 253     -25.424  27.807  72.073  1.00 37.52           C  
ATOM   1038  CG1 ILE A 253     -25.741  26.324  72.234  1.00 37.90           C  
ATOM   1039  CG2 ILE A 253     -26.423  28.319  71.065  1.00 38.38           C  
ATOM   1040  CD1 ILE A 253     -27.232  26.026  72.523  1.00 37.93           C  
ATOM   1041  N   HIS A 254     -22.276  28.480  73.265  1.00 33.64           N  
ATOM   1042  CA  HIS A 254     -21.060  28.137  74.013  1.00 32.50           C  
ATOM   1043  C   HIS A 254     -21.413  27.358  75.284  1.00 32.43           C  
ATOM   1044  O   HIS A 254     -20.842  26.305  75.562  1.00 31.88           O  
ATOM   1045  CB  HIS A 254     -20.255  29.404  74.345  1.00 32.70           C  
ATOM   1046  CG  HIS A 254     -18.974  29.125  75.056  1.00 30.61           C  
ATOM   1047  ND1 HIS A 254     -18.929  28.684  76.361  1.00 32.04           N  
ATOM   1048  CD2 HIS A 254     -17.687  29.239  74.650  1.00 30.31           C  
ATOM   1049  CE1 HIS A 254     -17.664  28.539  76.727  1.00 32.26           C  
ATOM   1050  NE2 HIS A 254     -16.894  28.872  75.707  1.00 32.68           N  
ATOM   1051  N   ARG A 255     -22.365  27.895  76.034  1.00 32.96           N  
ATOM   1052  CA  ARG A 255     -22.918  27.260  77.226  1.00 32.87           C  
ATOM   1053  C   ARG A 255     -22.022  27.225  78.461  1.00 33.50           C  
ATOM   1054  O   ARG A 255     -22.455  26.714  79.489  1.00 34.41           O  
ATOM   1055  CB  ARG A 255     -23.402  25.836  76.906  1.00 32.76           C  
ATOM   1056  CG  ARG A 255     -24.359  25.747  75.732  1.00 33.34           C  
ATOM   1057  CD  ARG A 255     -25.209  24.492  75.737  1.00 33.55           C  
ATOM   1058  NE  ARG A 255     -24.370  23.313  75.654  1.00 32.88           N  
ATOM   1059  CZ  ARG A 255     -24.801  22.065  75.671  1.00 33.10           C  
ATOM   1060  NH1 ARG A 255     -26.073  21.788  75.795  1.00 33.87           N  
ATOM   1061  NH2 ARG A 255     -23.929  21.080  75.570  1.00 33.86           N  
ATOM   1062  N   ASP A 256     -20.796  27.737  78.389  1.00 33.58           N  
ATOM   1063  CA  ASP A 256     -19.874  27.721  79.532  1.00 34.12           C  
ATOM   1064  C   ASP A 256     -19.048  28.995  79.546  1.00 33.97           C  
ATOM   1065  O   ASP A 256     -17.833  28.991  79.767  1.00 33.89           O  
ATOM   1066  CB  ASP A 256     -18.998  26.461  79.466  1.00 34.58           C  
ATOM   1067  CG  ASP A 256     -18.291  26.142  80.754  1.00 36.24           C  
ATOM   1068  OD1 ASP A 256     -18.807  26.474  81.863  1.00 40.16           O  
ATOM   1069  OD2 ASP A 256     -17.202  25.529  80.747  1.00 36.69           O  
ATOM   1070  N   ILE A 257     -19.730  30.094  79.277  1.00 33.66           N  
ATOM   1071  CA  ILE A 257     -19.150  31.415  79.371  1.00 34.64           C  
ATOM   1072  C   ILE A 257     -19.053  31.716  80.870  1.00 34.85           C  
ATOM   1073  O   ILE A 257     -20.072  31.823  81.579  1.00 35.96           O  
ATOM   1074  CB  ILE A 257     -20.046  32.376  78.659  1.00 34.77           C  
ATOM   1075  CG1 ILE A 257     -19.980  32.085  77.142  1.00 36.34           C  
ATOM   1076  CG2 ILE A 257     -19.683  33.783  78.945  1.00 36.49           C  
ATOM   1077  CD1 ILE A 257     -21.170  32.559  76.427  1.00 40.00           C  
ATOM   1078  N   LYS A 258     -17.824  31.727  81.350  1.00 33.63           N  
ATOM   1079  CA  LYS A 258     -17.526  32.182  82.702  1.00 33.29           C  
ATOM   1080  C   LYS A 258     -16.107  32.733  82.735  1.00 32.53           C  
ATOM   1081  O   LYS A 258     -15.319  32.516  81.811  1.00 29.58           O  
ATOM   1082  CB  LYS A 258     -17.733  31.065  83.707  1.00 33.48           C  
ATOM   1083  CG  LYS A 258     -16.996  29.806  83.437  1.00 36.37           C  
ATOM   1084  CD  LYS A 258     -17.658  28.621  84.209  1.00 39.19           C  
ATOM   1085  CE  LYS A 258     -16.771  27.390  84.223  1.00 42.19           C  
ATOM   1086  NZ  LYS A 258     -17.573  26.126  84.337  1.00 42.62           N  
ATOM   1087  N   PRO A 259     -15.791  33.512  83.759  1.00 31.39           N  
ATOM   1088  CA  PRO A 259     -14.508  34.205  83.789  1.00 31.31           C  
ATOM   1089  C   PRO A 259     -13.292  33.325  83.589  1.00 30.59           C  
ATOM   1090  O   PRO A 259     -12.348  33.793  82.993  1.00 31.68           O  
ATOM   1091  CB  PRO A 259     -14.508  34.871  85.158  1.00 30.62           C  
ATOM   1092  CG  PRO A 259     -15.943  35.135  85.394  1.00 31.55           C  
ATOM   1093  CD  PRO A 259     -16.640  33.880  84.902  1.00 32.34           C  
ATOM   1094  N   GLU A 260     -13.308  32.084  84.045  1.00 30.97           N  
ATOM   1095  CA  GLU A 260     -12.162  31.205  83.870  1.00 31.37           C  
ATOM   1096  C   GLU A 260     -11.990  30.731  82.426  1.00 30.45           C  
ATOM   1097  O   GLU A 260     -10.922  30.223  82.092  1.00 31.35           O  
ATOM   1098  CB  GLU A 260     -12.195  30.003  84.823  1.00 32.94           C  
ATOM   1099  CG  GLU A 260     -13.547  29.320  84.953  1.00 35.56           C  
ATOM   1100  CD  GLU A 260     -14.401  29.886  86.112  1.00 40.94           C  
ATOM   1101  OE1 GLU A 260     -14.562  29.172  87.147  1.00 46.03           O  
ATOM   1102  OE2 GLU A 260     -14.909  31.030  86.010  1.00 36.64           O  
ATOM   1103  N   ASN A 261     -12.998  30.927  81.580  1.00 29.20           N  
ATOM   1104  CA  ASN A 261     -12.911  30.585  80.166  1.00 29.48           C  
ATOM   1105  C   ASN A 261     -12.835  31.806  79.238  1.00 30.03           C  
ATOM   1106  O   ASN A 261     -13.035  31.669  78.033  1.00 30.31           O  
ATOM   1107  CB  ASN A 261     -14.124  29.729  79.763  1.00 29.17           C  
ATOM   1108  CG  ASN A 261     -14.139  28.393  80.429  1.00 28.65           C  
ATOM   1109  OD1 ASN A 261     -13.085  27.828  80.759  1.00 29.82           O  
ATOM   1110  ND2 ASN A 261     -15.339  27.830  80.576  1.00 26.16           N  
ATOM   1111  N   LEU A 262     -12.560  32.986  79.806  1.00 30.27           N  
ATOM   1112  CA  LEU A 262     -12.433  34.232  79.068  1.00 30.25           C  
ATOM   1113  C   LEU A 262     -11.004  34.676  79.275  1.00 30.66           C  
ATOM   1114  O   LEU A 262     -10.589  34.887  80.412  1.00 31.20           O  
ATOM   1115  CB  LEU A 262     -13.357  35.303  79.627  1.00 30.58           C  
ATOM   1116  CG  LEU A 262     -14.847  35.008  79.615  1.00 29.87           C  
ATOM   1117  CD1 LEU A 262     -15.594  36.157  80.177  1.00 31.11           C  
ATOM   1118  CD2 LEU A 262     -15.301  34.740  78.166  1.00 29.85           C  
ATOM   1119  N   LEU A 263     -10.253  34.756  78.189  1.00 29.76           N  
ATOM   1120  CA  LEU A 263      -8.825  34.997  78.217  1.00 30.10           C  
ATOM   1121  C   LEU A 263      -8.549  36.378  77.643  1.00 31.32           C  
ATOM   1122  O   LEU A 263      -9.399  36.977  76.981  1.00 31.33           O  
ATOM   1123  CB  LEU A 263      -8.082  33.945  77.399  1.00 29.71           C  
ATOM   1124  CG  LEU A 263      -8.424  32.471  77.645  1.00 30.92           C  
ATOM   1125  CD1 LEU A 263      -7.493  31.550  76.893  1.00 32.75           C  
ATOM   1126  CD2 LEU A 263      -8.272  32.186  79.116  1.00 33.92           C  
ATOM   1127  N   LEU A 264      -7.356  36.874  77.899  1.00 32.33           N  
ATOM   1128  CA  LEU A 264      -6.971  38.218  77.478  1.00 32.53           C  
ATOM   1129  C   LEU A 264      -5.765  38.152  76.544  1.00 32.79           C  
ATOM   1130  O   LEU A 264      -4.757  37.530  76.858  1.00 31.86           O  
ATOM   1131  CB  LEU A 264      -6.706  39.089  78.716  1.00 32.85           C  
ATOM   1132  CG  LEU A 264      -7.923  39.276  79.632  1.00 32.35           C  
ATOM   1133  CD1 LEU A 264      -7.499  39.988  80.932  1.00 34.18           C  
ATOM   1134  CD2 LEU A 264      -9.036  40.052  78.960  1.00 34.12           C  
ATOM   1135  N   GLY A 265      -5.907  38.747  75.364  1.00 33.34           N  
ATOM   1136  CA  GLY A 265      -4.834  38.840  74.400  1.00 34.66           C  
ATOM   1137  C   GLY A 265      -3.838  39.931  74.752  1.00 36.35           C  
ATOM   1138  O   GLY A 265      -3.987  40.595  75.772  1.00 36.34           O  
ATOM   1139  N   SER A 266      -2.818  40.133  73.920  1.00 38.19           N  
ATOM   1140  CA  SER A 266      -1.725  41.047  74.283  1.00 40.09           C  
ATOM   1141  C   SER A 266      -2.141  42.517  74.315  1.00 40.61           C  
ATOM   1142  O   SER A 266      -1.499  43.314  74.980  1.00 42.38           O  
ATOM   1143  CB  SER A 266      -0.507  40.865  73.378  1.00 40.67           C  
ATOM   1144  OG  SER A 266      -0.907  40.778  72.039  1.00 44.18           O  
ATOM   1145  N   ALA A 267      -3.219  42.878  73.631  1.00 41.21           N  
ATOM   1146  CA  ALA A 267      -3.794  44.221  73.763  1.00 41.70           C  
ATOM   1147  C   ALA A 267      -4.868  44.301  74.847  1.00 41.54           C  
ATOM   1148  O   ALA A 267      -5.549  45.317  74.970  1.00 42.45           O  
ATOM   1149  CB  ALA A 267      -4.371  44.682  72.410  1.00 42.04           C  
ATOM   1150  N   GLY A 268      -5.025  43.235  75.625  1.00 40.93           N  
ATOM   1151  CA  GLY A 268      -6.081  43.147  76.624  1.00 41.10           C  
ATOM   1152  C   GLY A 268      -7.460  42.805  76.094  1.00 40.59           C  
ATOM   1153  O   GLY A 268      -8.432  42.895  76.831  1.00 40.95           O  
ATOM   1154  N   GLU A 269      -7.548  42.404  74.829  1.00 39.52           N  
ATOM   1155  CA  GLU A 269      -8.827  42.066  74.216  1.00 39.15           C  
ATOM   1156  C   GLU A 269      -9.296  40.700  74.729  1.00 37.26           C  
ATOM   1157  O   GLU A 269      -8.509  39.808  74.982  1.00 34.98           O  
ATOM   1158  CB  GLU A 269      -8.749  42.059  72.683  1.00 39.77           C  
ATOM   1159  CG  GLU A 269      -7.938  40.919  72.074  1.00 43.44           C  
ATOM   1160  CD  GLU A 269      -6.447  41.220  71.937  1.00 48.48           C  
ATOM   1161  OE1 GLU A 269      -5.821  41.691  72.911  1.00 50.45           O  
ATOM   1162  OE2 GLU A 269      -5.884  40.951  70.854  1.00 53.18           O  
ATOM   1163  N   LEU A 270     -10.595  40.580  74.888  1.00 36.12           N  
ATOM   1164  CA  LEU A 270     -11.187  39.424  75.507  1.00 36.14           C  
ATOM   1165  C   LEU A 270     -11.307  38.368  74.436  1.00 35.71           C  
ATOM   1166  O   LEU A 270     -11.610  38.681  73.260  1.00 36.12           O  
ATOM   1167  CB  LEU A 270     -12.548  39.796  76.069  1.00 36.50           C  
ATOM   1168  CG  LEU A 270     -13.414  38.717  76.719  1.00 37.31           C  
ATOM   1169  CD1 LEU A 270     -14.330  39.367  77.746  1.00 39.66           C  
ATOM   1170  CD2 LEU A 270     -14.277  37.995  75.694  1.00 38.39           C  
ATOM   1171  N   LYS A 271     -11.113  37.121  74.845  1.00 33.89           N  
ATOM   1172  CA  LYS A 271     -11.181  35.972  73.946  1.00 33.56           C  
ATOM   1173  C   LYS A 271     -11.975  34.845  74.626  1.00 32.70           C  
ATOM   1174  O   LYS A 271     -11.628  34.416  75.701  1.00 32.97           O  
ATOM   1175  CB  LYS A 271      -9.776  35.521  73.559  1.00 33.99           C  
ATOM   1176  CG  LYS A 271      -9.172  36.476  72.475  1.00 37.13           C  
ATOM   1177  CD  LYS A 271      -7.808  36.083  71.965  1.00 40.02           C  
ATOM   1178  CE  LYS A 271      -7.172  37.223  71.144  1.00 41.14           C  
ATOM   1179  NZ  LYS A 271      -7.498  37.169  69.696  1.00 41.84           N  
ATOM   1180  N   ILE A 272     -13.068  34.422  74.025  1.00 32.48           N  
ATOM   1181  CA  ILE A 272     -13.780  33.259  74.517  1.00 33.16           C  
ATOM   1182  C   ILE A 272     -12.962  32.007  74.198  1.00 32.18           C  
ATOM   1183  O   ILE A 272     -12.495  31.829  73.096  1.00 30.99           O  
ATOM   1184  CB  ILE A 272     -15.234  33.180  73.987  1.00 34.01           C  
ATOM   1185  CG1 ILE A 272     -15.930  31.962  74.578  1.00 36.29           C  
ATOM   1186  CG2 ILE A 272     -15.331  33.050  72.480  1.00 36.92           C  
ATOM   1187  CD1 ILE A 272     -17.058  32.303  75.458  1.00 40.48           C  
ATOM   1188  N   ALA A 273     -12.804  31.148  75.197  1.00 31.50           N  
ATOM   1189  CA  ALA A 273     -12.080  29.912  75.069  1.00 30.85           C  
ATOM   1190  C   ALA A 273     -12.897  28.764  75.675  1.00 31.09           C  
ATOM   1191  O   ALA A 273     -13.996  28.969  76.194  1.00 31.63           O  
ATOM   1192  CB  ALA A 273     -10.734  30.045  75.776  1.00 30.31           C  
ATOM   1193  N   ASP A 274     -12.343  27.563  75.608  1.00 31.18           N  
ATOM   1194  CA  ASP A 274     -12.923  26.369  76.228  1.00 31.58           C  
ATOM   1195  C   ASP A 274     -14.303  25.991  75.658  1.00 31.43           C  
ATOM   1196  O   ASP A 274     -15.340  26.168  76.302  1.00 31.01           O  
ATOM   1197  CB  ASP A 274     -12.988  26.523  77.746  1.00 30.93           C  
ATOM   1198  CG  ASP A 274     -13.240  25.219  78.427  1.00 31.80           C  
ATOM   1199  OD1 ASP A 274     -13.317  25.206  79.676  1.00 29.38           O  
ATOM   1200  OD2 ASP A 274     -13.383  24.143  77.781  1.00 32.56           O  
ATOM   1201  N   PHE A 275     -14.307  25.483  74.436  1.00 31.66           N  
ATOM   1202  CA  PHE A 275     -15.555  25.167  73.752  1.00 32.62           C  
ATOM   1203  C   PHE A 275     -16.038  23.733  73.978  1.00 32.95           C  
ATOM   1204  O   PHE A 275     -16.847  23.237  73.209  1.00 34.63           O  
ATOM   1205  CB  PHE A 275     -15.436  25.443  72.235  1.00 32.10           C  
ATOM   1206  CG  PHE A 275     -15.593  26.861  71.887  1.00 31.53           C  
ATOM   1207  CD1 PHE A 275     -14.605  27.777  72.235  1.00 31.80           C  
ATOM   1208  CD2 PHE A 275     -16.702  27.304  71.185  1.00 30.40           C  
ATOM   1209  CE1 PHE A 275     -14.746  29.125  71.895  1.00 32.17           C  
ATOM   1210  CE2 PHE A 275     -16.868  28.629  70.871  1.00 30.09           C  
ATOM   1211  CZ  PHE A 275     -15.884  29.554  71.220  1.00 31.92           C  
ATOM   1212  N   GLY A 276     -15.585  23.092  75.045  1.00 34.41           N  
ATOM   1213  CA  GLY A 276     -15.998  21.721  75.381  1.00 34.95           C  
ATOM   1214  C   GLY A 276     -17.480  21.523  75.648  1.00 35.13           C  
ATOM   1215  O   GLY A 276     -18.018  20.450  75.406  1.00 36.99           O  
ATOM   1216  N   TRP A 277     -18.161  22.555  76.108  1.00 34.79           N  
ATOM   1217  CA  TRP A 277     -19.600  22.482  76.352  1.00 34.96           C  
ATOM   1218  C   TRP A 277     -20.405  22.949  75.155  1.00 34.36           C  
ATOM   1219  O   TRP A 277     -21.605  22.881  75.171  1.00 34.22           O  
ATOM   1220  CB  TRP A 277     -19.983  23.324  77.571  1.00 34.68           C  
ATOM   1221  CG  TRP A 277     -19.890  22.553  78.840  1.00 36.40           C  
ATOM   1222  CD1 TRP A 277     -18.928  22.650  79.785  1.00 38.63           C  
ATOM   1223  CD2 TRP A 277     -20.812  21.566  79.306  1.00 38.52           C  
ATOM   1224  NE1 TRP A 277     -19.184  21.785  80.819  1.00 40.43           N  
ATOM   1225  CE2 TRP A 277     -20.336  21.099  80.544  1.00 40.30           C  
ATOM   1226  CE3 TRP A 277     -21.993  21.013  78.790  1.00 39.09           C  
ATOM   1227  CZ2 TRP A 277     -21.002  20.120  81.289  1.00 41.86           C  
ATOM   1228  CZ3 TRP A 277     -22.649  20.032  79.521  1.00 41.66           C  
ATOM   1229  CH2 TRP A 277     -22.152  19.600  80.762  1.00 40.36           C  
ATOM   1230  N   SER A 278     -19.741  23.431  74.120  1.00 34.27           N  
ATOM   1231  CA  SER A 278     -20.443  24.033  73.020  1.00 34.97           C  
ATOM   1232  C   SER A 278     -21.188  22.977  72.196  1.00 35.88           C  
ATOM   1233  O   SER A 278     -20.839  21.805  72.206  1.00 36.24           O  
ATOM   1234  CB  SER A 278     -19.478  24.803  72.144  1.00 35.35           C  
ATOM   1235  OG  SER A 278     -18.601  23.915  71.491  1.00 38.13           O  
ATOM   1236  N   VAL A 279     -22.222  23.436  71.504  1.00 36.64           N  
ATOM   1237  CA  VAL A 279     -23.098  22.584  70.736  1.00 37.91           C  
ATOM   1238  C   VAL A 279     -23.809  23.441  69.720  1.00 38.07           C  
ATOM   1239  O   VAL A 279     -23.894  24.649  69.871  1.00 37.16           O  
ATOM   1240  CB  VAL A 279     -24.127  21.880  71.672  1.00 37.69           C  
ATOM   1241  CG1 VAL A 279     -25.185  22.850  72.147  1.00 38.00           C  
ATOM   1242  CG2 VAL A 279     -24.751  20.664  71.003  1.00 40.12           C  
ATOM   1243  N   HIS A 280     -24.349  22.807  68.683  1.00 39.74           N  
ATOM   1244  CA  HIS A 280     -25.206  23.520  67.758  1.00 40.27           C  
ATOM   1245  C   HIS A 280     -26.597  23.565  68.350  1.00 40.63           C  
ATOM   1246  O   HIS A 280     -27.061  22.580  68.934  1.00 40.91           O  
ATOM   1247  CB  HIS A 280     -25.164  22.847  66.391  1.00 41.32           C  
ATOM   1248  CG  HIS A 280     -23.814  22.910  65.753  1.00 41.92           C  
ATOM   1249  ND1 HIS A 280     -22.899  21.884  65.842  1.00 46.33           N  
ATOM   1250  CD2 HIS A 280     -23.224  23.880  65.015  1.00 45.50           C  
ATOM   1251  CE1 HIS A 280     -21.798  22.222  65.190  1.00 46.78           C  
ATOM   1252  NE2 HIS A 280     -21.970  23.428  64.678  1.00 46.26           N  
ATOM   1253  N   ALA A 281     -27.235  24.723  68.238  1.00 40.87           N  
ATOM   1254  CA  ALA A 281     -28.513  24.975  68.861  1.00 41.97           C  
ATOM   1255  C   ALA A 281     -29.593  24.207  68.137  1.00 43.72           C  
ATOM   1256  O   ALA A 281     -29.384  23.814  66.989  1.00 43.97           O  
ATOM   1257  CB  ALA A 281     -28.836  26.454  68.893  1.00 41.84           C  
ATOM   1258  N   PRO A 282     -30.811  24.316  68.646  1.00 44.38           N  
ATOM   1259  CA  PRO A 282     -31.477  23.410  69.570  1.00 43.92           C  
ATOM   1260  C   PRO A 282     -30.607  22.341  70.234  1.00 43.35           C  
ATOM   1261  O   PRO A 282     -29.967  21.558  69.549  1.00 42.85           O  
ATOM   1262  CB  PRO A 282     -32.567  22.805  68.674  1.00 44.49           C  
ATOM   1263  CG  PRO A 282     -32.607  23.764  67.473  1.00 44.37           C  
ATOM   1264  CD  PRO A 282     -31.834  25.050  67.908  1.00 45.78           C  
ATOM   1265  N   SER A 283     -30.587  22.300  71.564  1.00 42.44           N  
ATOM   1266  CA  SER A 283     -29.945  21.180  72.234  1.00 42.42           C  
ATOM   1267  C   SER A 283     -30.547  20.874  73.583  1.00 42.59           C  
ATOM   1268  O   SER A 283     -31.152  21.731  74.218  1.00 42.69           O  
ATOM   1269  CB  SER A 283     -28.450  21.415  72.384  1.00 42.42           C  
ATOM   1270  OG  SER A 283     -27.809  20.295  72.990  1.00 43.35           O  
ATOM   1271  N   SER A 284     -30.364  19.633  74.007  1.00 42.94           N  
ATOM   1272  CA  SER A 284     -30.573  19.250  75.390  1.00 44.04           C  
ATOM   1273  C   SER A 284     -29.206  19.190  76.033  1.00 44.69           C  
ATOM   1274  O   SER A 284     -28.195  19.617  75.442  1.00 44.91           O  
ATOM   1275  CB  SER A 284     -31.258  17.884  75.477  1.00 44.95           C  
ATOM   1276  OG  SER A 284     -32.360  17.947  76.372  1.00 46.46           O  
ATOM   1277  N   ARG A 285     -29.172  18.666  77.249  1.00 45.35           N  
ATOM   1278  CA  ARG A 285     -27.927  18.407  77.950  1.00 46.13           C  
ATOM   1279  C   ARG A 285     -27.877  16.923  78.323  1.00 45.93           C  
ATOM   1280  O   ARG A 285     -28.818  16.433  78.950  1.00 46.11           O  
ATOM   1281  CB  ARG A 285     -27.856  19.264  79.213  1.00 46.32           C  
ATOM   1282  CG  ARG A 285     -26.538  19.164  79.962  1.00 47.51           C  
ATOM   1283  CD  ARG A 285     -26.403  20.161  81.093  1.00 49.10           C  
ATOM   1284  NE  ARG A 285     -27.592  20.198  81.941  1.00 50.95           N  
ATOM   1285  CZ  ARG A 285     -27.824  19.381  82.960  1.00 53.25           C  
ATOM   1286  NH1 ARG A 285     -28.940  19.517  83.670  1.00 54.23           N  
ATOM   1287  NH2 ARG A 285     -26.965  18.415  83.272  1.00 54.19           N  
ATOM   1288  N   THR A 288     -25.055  15.549  79.599  1.00 53.03           N  
ATOM   1289  CA  THR A 288     -23.843  15.551  80.428  1.00 53.36           C  
ATOM   1290  C   THR A 288     -24.083  16.198  81.806  1.00 53.77           C  
ATOM   1291  O   THR A 288     -24.851  17.148  81.924  1.00 52.68           O  
ATOM   1292  CB  THR A 288     -22.691  16.304  79.711  1.00 53.31           C  
ATOM   1293  OG1 THR A 288     -22.462  15.762  78.407  1.00 54.15           O  
ATOM   1294  CG2 THR A 288     -21.358  16.087  80.412  1.00 53.01           C  
ATOM   1295  N   LEU A 289     -23.393  15.684  82.826  1.00 54.63           N  
ATOM   1296  CA  LEU A 289     -23.414  16.241  84.193  1.00 55.91           C  
ATOM   1297  C   LEU A 289     -22.670  17.597  84.331  1.00 55.92           C  
ATOM   1298  O   LEU A 289     -21.715  17.844  83.602  1.00 56.28           O  
ATOM   1299  CB  LEU A 289     -22.786  15.226  85.158  1.00 56.32           C  
ATOM   1300  CG  LEU A 289     -23.733  14.499  86.104  1.00 58.73           C  
ATOM   1301  CD1 LEU A 289     -24.247  15.459  87.173  1.00 59.71           C  
ATOM   1302  CD2 LEU A 289     -24.892  13.830  85.345  1.00 60.31           C  
ATOM   1303  N   CYS A 290     -23.070  18.411  85.322  1.00 56.70           N  
ATOM   1304  CA  CYS A 290     -22.628  19.826  85.505  1.00 56.87           C  
ATOM   1305  C   CYS A 290     -21.448  20.097  86.525  1.00 55.76           C  
ATOM   1306  O   CYS A 290     -20.716  19.167  86.879  1.00 55.81           O  
ATOM   1307  CB  CYS A 290     -23.872  20.668  85.867  1.00 57.14           C  
ATOM   1308  SG  CYS A 290     -25.016  21.026  84.496  1.00 61.63           S  
ATOM   1309  N   GLY A 291     -21.253  21.379  86.933  1.00 54.41           N  
ATOM   1310  CA  GLY A 291     -20.232  21.846  87.910  1.00 52.54           C  
ATOM   1311  C   GLY A 291     -20.727  23.040  88.773  1.00 50.54           C  
ATOM   1312  O   GLY A 291     -21.794  22.931  89.355  1.00 50.32           O  
ATOM   1313  N   THR A 292     -19.999  24.162  88.873  1.00 48.37           N  
ATOM   1314  CA  THR A 292     -20.605  25.391  89.426  1.00 46.46           C  
ATOM   1315  C   THR A 292     -21.781  25.818  88.533  1.00 44.09           C  
ATOM   1316  O   THR A 292     -21.637  25.898  87.311  1.00 43.82           O  
ATOM   1317  CB  THR A 292     -19.620  26.598  89.563  1.00 47.49           C  
ATOM   1318  OG1 THR A 292     -20.334  27.746  90.069  1.00 47.12           O  
ATOM   1319  CG2 THR A 292     -19.126  27.103  88.182  1.00 48.30           C  
ATOM   1320  N   LEU A 293     -22.928  26.107  89.144  1.00 40.37           N  
ATOM   1321  CA  LEU A 293     -24.115  26.507  88.390  1.00 39.25           C  
ATOM   1322  C   LEU A 293     -24.180  28.010  88.102  1.00 37.01           C  
ATOM   1323  O   LEU A 293     -25.064  28.463  87.387  1.00 36.32           O  
ATOM   1324  CB  LEU A 293     -25.372  26.119  89.169  1.00 39.41           C  
ATOM   1325  CG  LEU A 293     -26.193  24.874  88.829  1.00 42.28           C  
ATOM   1326  CD1 LEU A 293     -25.410  23.768  88.148  1.00 42.29           C  
ATOM   1327  CD2 LEU A 293     -26.889  24.380  90.099  1.00 42.87           C  
ATOM   1328  N   ASP A 294     -23.254  28.778  88.660  1.00 35.11           N  
ATOM   1329  CA  ASP A 294     -23.403  30.229  88.771  1.00 34.22           C  
ATOM   1330  C   ASP A 294     -23.760  30.963  87.479  1.00 33.10           C  
ATOM   1331  O   ASP A 294     -24.475  31.952  87.498  1.00 31.38           O  
ATOM   1332  CB  ASP A 294     -22.130  30.807  89.366  1.00 34.80           C  
ATOM   1333  CG  ASP A 294     -22.139  30.751  90.870  1.00 38.14           C  
ATOM   1334  OD1 ASP A 294     -21.168  30.218  91.434  1.00 41.99           O  
ATOM   1335  OD2 ASP A 294     -23.105  31.195  91.544  1.00 40.73           O  
ATOM   1336  N   TYR A 295     -23.242  30.481  86.367  1.00 31.84           N  
ATOM   1337  CA  TYR A 295     -23.408  31.162  85.084  1.00 31.85           C  
ATOM   1338  C   TYR A 295     -24.453  30.582  84.131  1.00 32.26           C  
ATOM   1339  O   TYR A 295     -24.594  31.054  82.994  1.00 31.40           O  
ATOM   1340  CB  TYR A 295     -22.056  31.229  84.401  1.00 32.25           C  
ATOM   1341  CG  TYR A 295     -21.038  31.914  85.264  1.00 31.74           C  
ATOM   1342  CD1 TYR A 295     -20.263  31.184  86.138  1.00 34.17           C  
ATOM   1343  CD2 TYR A 295     -20.879  33.291  85.234  1.00 34.30           C  
ATOM   1344  CE1 TYR A 295     -19.334  31.784  86.961  1.00 36.10           C  
ATOM   1345  CE2 TYR A 295     -19.958  33.919  86.080  1.00 35.27           C  
ATOM   1346  CZ  TYR A 295     -19.191  33.145  86.942  1.00 34.48           C  
ATOM   1347  OH  TYR A 295     -18.248  33.670  87.796  1.00 37.58           O  
ATOM   1348  N   LEU A 296     -25.206  29.587  84.590  1.00 32.66           N  
ATOM   1349  CA  LEU A 296     -26.131  28.845  83.722  1.00 33.08           C  
ATOM   1350  C   LEU A 296     -27.540  29.271  83.976  1.00 33.04           C  
ATOM   1351  O   LEU A 296     -27.913  29.481  85.139  1.00 32.00           O  
ATOM   1352  CB  LEU A 296     -26.026  27.360  83.990  1.00 33.81           C  
ATOM   1353  CG  LEU A 296     -24.662  26.739  83.752  1.00 36.62           C  
ATOM   1354  CD1 LEU A 296     -24.727  25.257  84.071  1.00 38.71           C  
ATOM   1355  CD2 LEU A 296     -24.212  26.998  82.330  1.00 38.52           C  
ATOM   1356  N   PRO A 297     -28.332  29.384  82.902  1.00 32.68           N  
ATOM   1357  CA  PRO A 297     -29.728  29.786  82.993  1.00 33.07           C  
ATOM   1358  C   PRO A 297     -30.592  28.625  83.497  1.00 34.06           C  
ATOM   1359  O   PRO A 297     -30.127  27.487  83.485  1.00 33.36           O  
ATOM   1360  CB  PRO A 297     -30.085  30.117  81.539  1.00 33.37           C  
ATOM   1361  CG  PRO A 297     -29.262  29.217  80.774  1.00 32.82           C  
ATOM   1362  CD  PRO A 297     -27.943  29.129  81.501  1.00 33.03           C  
ATOM   1363  N   PRO A 298     -31.800  28.924  83.946  1.00 35.53           N  
ATOM   1364  CA  PRO A 298     -32.723  27.905  84.461  1.00 37.48           C  
ATOM   1365  C   PRO A 298     -32.923  26.733  83.485  1.00 39.07           C  
ATOM   1366  O   PRO A 298     -32.803  25.582  83.897  1.00 39.76           O  
ATOM   1367  CB  PRO A 298     -34.021  28.683  84.659  1.00 37.08           C  
ATOM   1368  CG  PRO A 298     -33.601  30.090  84.867  1.00 37.39           C  
ATOM   1369  CD  PRO A 298     -32.375  30.273  84.017  1.00 36.05           C  
ATOM   1370  N   GLU A 299     -33.136  27.017  82.207  1.00 40.50           N  
ATOM   1371  CA  GLU A 299     -33.420  25.959  81.239  1.00 41.84           C  
ATOM   1372  C   GLU A 299     -32.293  24.945  81.159  1.00 43.16           C  
ATOM   1373  O   GLU A 299     -32.532  23.733  81.079  1.00 42.66           O  
ATOM   1374  CB  GLU A 299     -33.775  26.519  79.844  1.00 41.84           C  
ATOM   1375  CG  GLU A 299     -32.661  27.239  79.098  1.00 41.97           C  
ATOM   1376  CD  GLU A 299     -32.602  28.741  79.347  1.00 41.80           C  
ATOM   1377  OE1 GLU A 299     -33.159  29.236  80.360  1.00 40.60           O  
ATOM   1378  OE2 GLU A 299     -31.989  29.436  78.503  1.00 39.83           O  
ATOM   1379  N   MET A 300     -31.064  25.436  81.234  1.00 44.55           N  
ATOM   1380  CA  MET A 300     -29.905  24.576  81.210  1.00 45.99           C  
ATOM   1381  C   MET A 300     -29.796  23.703  82.456  1.00 47.00           C  
ATOM   1382  O   MET A 300     -29.593  22.489  82.336  1.00 46.97           O  
ATOM   1383  CB  MET A 300     -28.645  25.403  81.071  1.00 46.58           C  
ATOM   1384  CG  MET A 300     -27.392  24.596  81.070  1.00 49.64           C  
ATOM   1385  SD  MET A 300     -26.666  24.557  79.466  1.00 56.71           S  
ATOM   1386  CE  MET A 300     -25.323  23.426  79.753  1.00 55.08           C  
ATOM   1387  N   ILE A 301     -29.890  24.294  83.640  1.00 48.07           N  
ATOM   1388  CA  ILE A 301     -29.743  23.494  84.862  1.00 49.44           C  
ATOM   1389  C   ILE A 301     -30.869  22.444  84.971  1.00 50.60           C  
ATOM   1390  O   ILE A 301     -30.606  21.287  85.301  1.00 50.93           O  
ATOM   1391  CB  ILE A 301     -29.641  24.371  86.130  1.00 49.73           C  
ATOM   1392  CG1 ILE A 301     -30.988  25.024  86.492  1.00 51.17           C  
ATOM   1393  CG2 ILE A 301     -28.551  25.467  85.962  1.00 49.33           C  
ATOM   1394  CD1 ILE A 301     -30.901  26.035  87.639  1.00 52.42           C  
ATOM   1395  N   GLU A 302     -32.099  22.844  84.633  1.00 51.61           N  
ATOM   1396  CA  GLU A 302     -33.273  21.961  84.660  1.00 52.52           C  
ATOM   1397  C   GLU A 302     -33.296  20.905  83.552  1.00 52.67           C  
ATOM   1398  O   GLU A 302     -34.188  20.062  83.535  1.00 53.11           O  
ATOM   1399  CB  GLU A 302     -34.553  22.784  84.560  1.00 52.92           C  
ATOM   1400  CG  GLU A 302     -34.908  23.528  85.833  1.00 55.30           C  
ATOM   1401  CD  GLU A 302     -35.717  24.784  85.562  1.00 57.90           C  
ATOM   1402  OE1 GLU A 302     -35.654  25.735  86.376  1.00 59.96           O  
ATOM   1403  OE2 GLU A 302     -36.425  24.820  84.534  1.00 59.81           O  
ATOM   1404  N   GLY A 303     -32.350  20.969  82.620  1.00 52.29           N  
ATOM   1405  CA  GLY A 303     -32.227  19.981  81.565  1.00 52.08           C  
ATOM   1406  C   GLY A 303     -33.292  20.090  80.480  1.00 51.64           C  
ATOM   1407  O   GLY A 303     -33.597  19.097  79.818  1.00 52.27           O  
ATOM   1408  N   ARG A 304     -33.870  21.276  80.305  1.00 50.45           N  
ATOM   1409  CA  ARG A 304     -34.813  21.529  79.215  1.00 49.76           C  
ATOM   1410  C   ARG A 304     -34.083  21.783  77.895  1.00 48.52           C  
ATOM   1411  O   ARG A 304     -32.855  21.946  77.868  1.00 47.55           O  
ATOM   1412  CB  ARG A 304     -35.708  22.726  79.553  1.00 50.31           C  
ATOM   1413  CG  ARG A 304     -36.692  22.460  80.715  1.00 52.45           C  
ATOM   1414  CD  ARG A 304     -37.231  23.731  81.401  1.00 56.21           C  
ATOM   1415  NE  ARG A 304     -37.371  24.858  80.462  1.00 58.64           N  
ATOM   1416  CZ  ARG A 304     -37.319  26.154  80.797  1.00 60.72           C  
ATOM   1417  NH1 ARG A 304     -37.452  27.092  79.848  1.00 61.53           N  
ATOM   1418  NH2 ARG A 304     -37.134  26.526  82.064  1.00 60.77           N  
ATOM   1419  N   MET A 305     -34.841  21.794  76.802  1.00 46.97           N  
ATOM   1420  CA  MET A 305     -34.287  22.132  75.486  1.00 46.74           C  
ATOM   1421  C   MET A 305     -33.928  23.606  75.523  1.00 44.01           C  
ATOM   1422  O   MET A 305     -34.637  24.385  76.126  1.00 44.15           O  
ATOM   1423  CB  MET A 305     -35.305  21.896  74.352  1.00 47.30           C  
ATOM   1424  CG  MET A 305     -35.362  20.463  73.770  1.00 52.05           C  
ATOM   1425  SD  MET A 305     -34.024  19.350  74.327  1.00 61.22           S  
ATOM   1426  CE  MET A 305     -33.518  18.604  73.015  1.00 59.82           C  
ATOM   1427  N   HIS A 306     -32.836  23.983  74.875  1.00 41.95           N  
ATOM   1428  CA  HIS A 306     -32.357  25.366  74.929  1.00 40.25           C  
ATOM   1429  C   HIS A 306     -31.580  25.718  73.677  1.00 40.27           C  
ATOM   1430  O   HIS A 306     -31.156  24.847  72.918  1.00 39.94           O  
ATOM   1431  CB  HIS A 306     -31.461  25.563  76.162  1.00 39.40           C  
ATOM   1432  CG  HIS A 306     -30.333  24.589  76.232  1.00 36.12           C  
ATOM   1433  ND1 HIS A 306     -30.444  23.369  76.859  1.00 33.06           N  
ATOM   1434  CD2 HIS A 306     -29.083  24.640  75.727  1.00 34.38           C  
ATOM   1435  CE1 HIS A 306     -29.306  22.715  76.745  1.00 34.27           C  
ATOM   1436  NE2 HIS A 306     -28.467  23.460  76.051  1.00 33.99           N  
ATOM   1437  N   ASP A 307     -31.358  27.011  73.494  1.00 40.26           N  
ATOM   1438  CA  ASP A 307     -30.775  27.511  72.267  1.00 40.57           C  
ATOM   1439  C   ASP A 307     -29.842  28.687  72.588  1.00 40.07           C  
ATOM   1440  O   ASP A 307     -29.317  28.778  73.689  1.00 39.60           O  
ATOM   1441  CB  ASP A 307     -31.908  27.888  71.313  1.00 41.15           C  
ATOM   1442  CG  ASP A 307     -32.760  29.061  71.824  1.00 44.39           C  
ATOM   1443  OD1 ASP A 307     -33.697  29.473  71.095  1.00 49.45           O  
ATOM   1444  OD2 ASP A 307     -32.579  29.652  72.916  1.00 46.69           O  
ATOM   1445  N   GLU A 308     -29.675  29.594  71.637  1.00 39.53           N  
ATOM   1446  CA  GLU A 308     -28.726  30.687  71.745  1.00 39.42           C  
ATOM   1447  C   GLU A 308     -28.962  31.591  72.949  1.00 38.10           C  
ATOM   1448  O   GLU A 308     -28.031  32.227  73.430  1.00 37.66           O  
ATOM   1449  CB  GLU A 308     -28.790  31.529  70.477  1.00 39.71           C  
ATOM   1450  CG  GLU A 308     -28.160  30.863  69.273  1.00 41.63           C  
ATOM   1451  CD  GLU A 308     -29.117  30.034  68.442  1.00 44.93           C  
ATOM   1452  OE1 GLU A 308     -30.162  29.579  68.948  1.00 44.30           O  
ATOM   1453  OE2 GLU A 308     -28.796  29.826  67.249  1.00 47.57           O  
ATOM   1454  N   LYS A 309     -30.199  31.666  73.422  1.00 37.16           N  
ATOM   1455  CA  LYS A 309     -30.520  32.540  74.553  1.00 36.82           C  
ATOM   1456  C   LYS A 309     -29.806  32.156  75.840  1.00 35.79           C  
ATOM   1457  O   LYS A 309     -29.717  32.964  76.740  1.00 35.11           O  
ATOM   1458  CB  LYS A 309     -32.031  32.620  74.790  1.00 37.16           C  
ATOM   1459  CG  LYS A 309     -32.802  33.221  73.615  1.00 39.14           C  
ATOM   1460  CD  LYS A 309     -32.329  34.638  73.306  1.00 41.67           C  
ATOM   1461  CE  LYS A 309     -33.290  35.371  72.372  1.00 45.35           C  
ATOM   1462  NZ  LYS A 309     -34.661  35.440  72.967  1.00 47.46           N  
ATOM   1463  N   VAL A 310     -29.270  30.953  75.904  1.00 34.75           N  
ATOM   1464  CA  VAL A 310     -28.483  30.518  77.047  1.00 34.99           C  
ATOM   1465  C   VAL A 310     -27.317  31.473  77.284  1.00 34.78           C  
ATOM   1466  O   VAL A 310     -27.103  31.920  78.402  1.00 34.16           O  
ATOM   1467  CB  VAL A 310     -27.996  29.088  76.835  1.00 35.18           C  
ATOM   1468  CG1 VAL A 310     -26.783  28.763  77.685  1.00 37.47           C  
ATOM   1469  CG2 VAL A 310     -29.137  28.107  77.157  1.00 35.80           C  
ATOM   1470  N   ASP A 311     -26.587  31.800  76.222  1.00 33.74           N  
ATOM   1471  CA  ASP A 311     -25.432  32.683  76.323  1.00 33.84           C  
ATOM   1472  C   ASP A 311     -25.829  34.110  76.698  1.00 33.13           C  
ATOM   1473  O   ASP A 311     -25.024  34.826  77.272  1.00 33.00           O  
ATOM   1474  CB  ASP A 311     -24.610  32.664  75.010  1.00 34.34           C  
ATOM   1475  CG  ASP A 311     -23.931  31.295  74.737  1.00 35.54           C  
ATOM   1476  OD1 ASP A 311     -23.586  30.546  75.682  1.00 36.08           O  
ATOM   1477  OD2 ASP A 311     -23.681  30.879  73.595  1.00 36.37           O  
ATOM   1478  N   LEU A 312     -27.048  34.534  76.373  1.00 32.71           N  
ATOM   1479  CA  LEU A 312     -27.512  35.861  76.755  1.00 32.65           C  
ATOM   1480  C   LEU A 312     -27.649  35.950  78.260  1.00 32.21           C  
ATOM   1481  O   LEU A 312     -27.231  36.921  78.858  1.00 31.79           O  
ATOM   1482  CB  LEU A 312     -28.840  36.219  76.099  1.00 34.35           C  
ATOM   1483  CG  LEU A 312     -28.737  36.822  74.690  1.00 34.12           C  
ATOM   1484  CD1 LEU A 312     -28.017  38.152  74.756  1.00 37.03           C  
ATOM   1485  CD2 LEU A 312     -28.030  35.858  73.749  1.00 37.69           C  
ATOM   1486  N   TRP A 313     -28.181  34.905  78.876  1.00 31.51           N  
ATOM   1487  CA  TRP A 313     -28.250  34.884  80.332  1.00 31.26           C  
ATOM   1488  C   TRP A 313     -26.858  35.007  80.944  1.00 31.86           C  
ATOM   1489  O   TRP A 313     -26.633  35.836  81.811  1.00 30.22           O  
ATOM   1490  CB  TRP A 313     -28.904  33.619  80.775  1.00 31.60           C  
ATOM   1491  CG  TRP A 313     -28.837  33.359  82.201  1.00 29.94           C  
ATOM   1492  CD1 TRP A 313     -27.802  32.833  82.874  1.00 28.48           C  
ATOM   1493  CD2 TRP A 313     -29.879  33.553  83.136  1.00 29.35           C  
ATOM   1494  NE1 TRP A 313     -28.129  32.691  84.203  1.00 29.78           N  
ATOM   1495  CE2 TRP A 313     -29.416  33.112  84.377  1.00 29.48           C  
ATOM   1496  CE3 TRP A 313     -31.182  34.025  83.046  1.00 29.32           C  
ATOM   1497  CZ2 TRP A 313     -30.201  33.164  85.530  1.00 28.44           C  
ATOM   1498  CZ3 TRP A 313     -31.955  34.061  84.182  1.00 31.79           C  
ATOM   1499  CH2 TRP A 313     -31.462  33.639  85.398  1.00 28.39           C  
ATOM   1500  N   SER A 314     -25.931  34.183  80.470  1.00 32.25           N  
ATOM   1501  CA  SER A 314     -24.558  34.178  80.943  1.00 32.51           C  
ATOM   1502  C   SER A 314     -23.887  35.558  80.836  1.00 33.04           C  
ATOM   1503  O   SER A 314     -23.150  35.960  81.716  1.00 31.21           O  
ATOM   1504  CB  SER A 314     -23.770  33.106  80.179  1.00 32.93           C  
ATOM   1505  OG  SER A 314     -24.292  31.802  80.465  1.00 34.07           O  
ATOM   1506  N   LEU A 315     -24.150  36.267  79.746  1.00 33.01           N  
ATOM   1507  CA  LEU A 315     -23.731  37.639  79.566  1.00 33.60           C  
ATOM   1508  C   LEU A 315     -24.234  38.535  80.687  1.00 33.12           C  
ATOM   1509  O   LEU A 315     -23.522  39.412  81.150  1.00 33.22           O  
ATOM   1510  CB  LEU A 315     -24.279  38.175  78.237  1.00 34.24           C  
ATOM   1511  CG  LEU A 315     -23.481  39.246  77.532  1.00 36.29           C  
ATOM   1512  CD1 LEU A 315     -22.009  38.863  77.449  1.00 36.20           C  
ATOM   1513  CD2 LEU A 315     -24.067  39.409  76.145  1.00 36.36           C  
ATOM   1514  N   GLY A 316     -25.465  38.303  81.116  1.00 33.08           N  
ATOM   1515  CA  GLY A 316     -26.057  39.033  82.217  1.00 31.72           C  
ATOM   1516  C   GLY A 316     -25.347  38.736  83.513  1.00 31.46           C  
ATOM   1517  O   GLY A 316     -25.011  39.645  84.263  1.00 30.74           O  
ATOM   1518  N   VAL A 317     -25.111  37.458  83.784  1.00 31.52           N  
ATOM   1519  CA  VAL A 317     -24.390  37.048  84.983  1.00 31.55           C  
ATOM   1520  C   VAL A 317     -22.988  37.695  84.989  1.00 31.68           C  
ATOM   1521  O   VAL A 317     -22.541  38.213  86.010  1.00 30.71           O  
ATOM   1522  CB  VAL A 317     -24.294  35.499  85.079  1.00 31.58           C  
ATOM   1523  CG1 VAL A 317     -23.453  35.067  86.231  1.00 33.21           C  
ATOM   1524  CG2 VAL A 317     -25.645  34.905  85.183  1.00 31.72           C  
ATOM   1525  N   LEU A 318     -22.300  37.674  83.856  1.00 31.47           N  
ATOM   1526  CA  LEU A 318     -20.967  38.235  83.768  1.00 31.67           C  
ATOM   1527  C   LEU A 318     -20.985  39.733  83.955  1.00 31.64           C  
ATOM   1528  O   LEU A 318     -20.103  40.265  84.579  1.00 31.27           O  
ATOM   1529  CB  LEU A 318     -20.321  37.955  82.408  1.00 31.81           C  
ATOM   1530  CG  LEU A 318     -19.785  36.581  82.107  1.00 34.14           C  
ATOM   1531  CD1 LEU A 318     -19.331  36.600  80.633  1.00 35.37           C  
ATOM   1532  CD2 LEU A 318     -18.623  36.184  83.004  1.00 31.33           C  
ATOM   1533  N   CYS A 319     -21.989  40.425  83.441  1.00 32.16           N  
ATOM   1534  CA  CYS A 319     -22.026  41.864  83.613  1.00 33.38           C  
ATOM   1535  C   CYS A 319     -22.137  42.202  85.112  1.00 32.91           C  
ATOM   1536  O   CYS A 319     -21.426  43.053  85.648  1.00 32.14           O  
ATOM   1537  CB  CYS A 319     -23.182  42.464  82.843  1.00 33.82           C  
ATOM   1538  SG  CYS A 319     -22.993  44.257  82.698  1.00 41.00           S  
ATOM   1539  N   TYR A 320     -22.988  41.466  85.793  1.00 31.55           N  
ATOM   1540  CA  TYR A 320     -23.150  41.660  87.219  1.00 30.93           C  
ATOM   1541  C   TYR A 320     -21.836  41.371  87.953  1.00 31.40           C  
ATOM   1542  O   TYR A 320     -21.352  42.204  88.733  1.00 30.94           O  
ATOM   1543  CB  TYR A 320     -24.291  40.789  87.716  1.00 30.97           C  
ATOM   1544  CG  TYR A 320     -24.592  40.928  89.191  1.00 29.59           C  
ATOM   1545  CD1 TYR A 320     -23.741  40.408  90.150  1.00 31.18           C  
ATOM   1546  CD2 TYR A 320     -25.730  41.572  89.610  1.00 29.23           C  
ATOM   1547  CE1 TYR A 320     -24.040  40.543  91.505  1.00 31.58           C  
ATOM   1548  CE2 TYR A 320     -26.047  41.682  90.959  1.00 30.32           C  
ATOM   1549  CZ  TYR A 320     -25.212  41.202  91.878  1.00 29.77           C  
ATOM   1550  OH  TYR A 320     -25.585  41.341  93.200  1.00 35.29           O  
ATOM   1551  N   GLU A 321     -21.235  40.215  87.692  1.00 31.08           N  
ATOM   1552  CA  GLU A 321     -20.014  39.840  88.378  1.00 31.25           C  
ATOM   1553  C   GLU A 321     -18.868  40.820  88.153  1.00 31.32           C  
ATOM   1554  O   GLU A 321     -18.137  41.128  89.078  1.00 30.42           O  
ATOM   1555  CB  GLU A 321     -19.567  38.449  87.987  1.00 31.25           C  
ATOM   1556  CG  GLU A 321     -18.337  38.042  88.771  1.00 33.90           C  
ATOM   1557  CD  GLU A 321     -17.971  36.605  88.631  1.00 38.26           C  
ATOM   1558  OE1 GLU A 321     -17.030  36.179  89.353  1.00 40.65           O  
ATOM   1559  OE2 GLU A 321     -18.594  35.917  87.792  1.00 40.59           O  
ATOM   1560  N   PHE A 322     -18.715  41.307  86.924  1.00 31.13           N  
ATOM   1561  CA  PHE A 322     -17.689  42.287  86.608  1.00 31.53           C  
ATOM   1562  C   PHE A 322     -17.889  43.549  87.433  1.00 32.24           C  
ATOM   1563  O   PHE A 322     -16.938  44.034  88.025  1.00 33.50           O  
ATOM   1564  CB  PHE A 322     -17.740  42.646  85.125  1.00 31.91           C  
ATOM   1565  CG  PHE A 322     -17.264  41.554  84.200  1.00 31.39           C  
ATOM   1566  CD1 PHE A 322     -16.721  40.375  84.670  1.00 31.59           C  
ATOM   1567  CD2 PHE A 322     -17.361  41.731  82.835  1.00 32.01           C  
ATOM   1568  CE1 PHE A 322     -16.292  39.398  83.791  1.00 33.14           C  
ATOM   1569  CE2 PHE A 322     -16.934  40.749  81.953  1.00 33.51           C  
ATOM   1570  CZ  PHE A 322     -16.404  39.602  82.426  1.00 33.16           C  
ATOM   1571  N   LEU A 323     -19.130  44.007  87.536  1.00 32.51           N  
ATOM   1572  CA  LEU A 323     -19.468  45.221  88.289  1.00 33.32           C  
ATOM   1573  C   LEU A 323     -19.435  45.037  89.779  1.00 34.29           C  
ATOM   1574  O   LEU A 323     -19.027  45.950  90.513  1.00 34.86           O  
ATOM   1575  CB  LEU A 323     -20.845  45.747  87.892  1.00 33.33           C  
ATOM   1576  CG  LEU A 323     -20.950  46.287  86.467  1.00 32.84           C  
ATOM   1577  CD1 LEU A 323     -22.350  46.669  86.173  1.00 33.45           C  
ATOM   1578  CD2 LEU A 323     -20.010  47.459  86.257  1.00 36.43           C  
ATOM   1579  N   VAL A 324     -19.824  43.853  90.241  1.00 34.64           N  
ATOM   1580  CA  VAL A 324     -20.080  43.645  91.658  1.00 34.88           C  
ATOM   1581  C   VAL A 324     -18.932  42.918  92.329  1.00 36.21           C  
ATOM   1582  O   VAL A 324     -18.654  43.154  93.487  1.00 36.64           O  
ATOM   1583  CB  VAL A 324     -21.433  42.944  91.860  1.00 34.82           C  
ATOM   1584  CG1 VAL A 324     -21.694  42.625  93.338  1.00 35.02           C  
ATOM   1585  CG2 VAL A 324     -22.558  43.800  91.305  1.00 35.32           C  
ATOM   1586  N   GLY A 325     -18.240  42.044  91.608  1.00 36.47           N  
ATOM   1587  CA  GLY A 325     -17.174  41.239  92.176  1.00 36.68           C  
ATOM   1588  C   GLY A 325     -17.562  39.809  92.517  1.00 36.99           C  
ATOM   1589  O   GLY A 325     -16.706  38.977  92.803  1.00 37.80           O  
ATOM   1590  N   LYS A 326     -18.855  39.523  92.465  1.00 36.97           N  
ATOM   1591  CA  LYS A 326     -19.345  38.177  92.650  1.00 37.42           C  
ATOM   1592  C   LYS A 326     -20.555  37.951  91.755  1.00 36.17           C  
ATOM   1593  O   LYS A 326     -21.289  38.882  91.465  1.00 35.12           O  
ATOM   1594  CB  LYS A 326     -19.712  37.964  94.126  1.00 37.92           C  
ATOM   1595  CG  LYS A 326     -20.976  38.691  94.543  1.00 41.38           C  
ATOM   1596  CD  LYS A 326     -21.226  38.633  96.068  1.00 46.42           C  
ATOM   1597  CE  LYS A 326     -22.227  39.722  96.509  1.00 49.50           C  
ATOM   1598  NZ  LYS A 326     -21.621  40.758  97.377  1.00 49.79           N  
ATOM   1599  N   PRO A 327     -20.793  36.711  91.338  1.00 35.54           N  
ATOM   1600  CA  PRO A 327     -21.962  36.434  90.491  1.00 35.07           C  
ATOM   1601  C   PRO A 327     -23.275  36.588  91.281  1.00 33.74           C  
ATOM   1602  O   PRO A 327     -23.301  36.384  92.493  1.00 33.77           O  
ATOM   1603  CB  PRO A 327     -21.718  34.996  90.019  1.00 35.80           C  
ATOM   1604  CG  PRO A 327     -20.859  34.377  91.099  1.00 36.41           C  
ATOM   1605  CD  PRO A 327     -20.003  35.496  91.620  1.00 35.77           C  
ATOM   1606  N   PRO A 328     -24.353  36.970  90.616  1.00 32.77           N  
ATOM   1607  CA  PRO A 328     -25.591  37.330  91.317  1.00 32.55           C  
ATOM   1608  C   PRO A 328     -26.326  36.207  92.084  1.00 33.80           C  
ATOM   1609  O   PRO A 328     -27.149  36.534  92.930  1.00 33.66           O  
ATOM   1610  CB  PRO A 328     -26.461  37.872  90.212  1.00 31.86           C  
ATOM   1611  CG  PRO A 328     -25.906  37.272  88.943  1.00 32.85           C  
ATOM   1612  CD  PRO A 328     -24.470  37.147  89.164  1.00 32.29           C  
ATOM   1613  N   PHE A 329     -26.045  34.936  91.780  1.00 33.66           N  
ATOM   1614  CA  PHE A 329     -26.762  33.821  92.386  1.00 34.49           C  
ATOM   1615  C   PHE A 329     -25.846  33.000  93.281  1.00 36.17           C  
ATOM   1616  O   PHE A 329     -26.250  31.952  93.767  1.00 37.14           O  
ATOM   1617  CB  PHE A 329     -27.407  32.941  91.293  1.00 33.42           C  
ATOM   1618  CG  PHE A 329     -28.243  33.712  90.310  1.00 31.25           C  
ATOM   1619  CD1 PHE A 329     -29.411  34.324  90.698  1.00 29.14           C  
ATOM   1620  CD2 PHE A 329     -27.835  33.856  88.989  1.00 29.84           C  
ATOM   1621  CE1 PHE A 329     -30.168  35.046  89.811  1.00 27.68           C  
ATOM   1622  CE2 PHE A 329     -28.570  34.611  88.110  1.00 28.69           C  
ATOM   1623  CZ  PHE A 329     -29.749  35.201  88.504  1.00 29.08           C  
ATOM   1624  N   GLU A 330     -24.632  33.494  93.500  1.00 38.38           N  
ATOM   1625  CA  GLU A 330     -23.667  32.919  94.425  1.00 40.68           C  
ATOM   1626  C   GLU A 330     -24.355  32.542  95.735  1.00 41.08           C  
ATOM   1627  O   GLU A 330     -25.183  33.274  96.254  1.00 40.97           O  
ATOM   1628  CB  GLU A 330     -22.554  33.924  94.741  1.00 41.65           C  
ATOM   1629  CG  GLU A 330     -21.232  33.307  95.164  1.00 44.96           C  
ATOM   1630  CD  GLU A 330     -20.295  34.328  95.811  1.00 51.12           C  
ATOM   1631  OE1 GLU A 330     -20.650  34.895  96.886  1.00 53.46           O  
ATOM   1632  OE2 GLU A 330     -19.204  34.573  95.237  1.00 55.83           O  
ATOM   1633  N   ALA A 331     -24.006  31.368  96.226  1.00 42.05           N  
ATOM   1634  CA  ALA A 331     -24.587  30.811  97.434  1.00 42.11           C  
ATOM   1635  C   ALA A 331     -23.589  29.771  97.904  1.00 42.49           C  
ATOM   1636  O   ALA A 331     -22.731  29.359  97.135  1.00 42.13           O  
ATOM   1637  CB  ALA A 331     -25.917  30.215  97.116  1.00 42.66           C  
ATOM   1638  N   ASN A 332     -23.648  29.370  99.173  1.00 42.88           N  
ATOM   1639  CA  ASN A 332     -22.656  28.439  99.709  1.00 42.41           C  
ATOM   1640  C   ASN A 332     -22.965  26.996  99.326  1.00 40.42           C  
ATOM   1641  O   ASN A 332     -22.182  26.119  99.576  1.00 40.67           O  
ATOM   1642  CB  ASN A 332     -22.510  28.594 101.242  1.00 43.79           C  
ATOM   1643  CG  ASN A 332     -21.660  29.815 101.630  1.00 47.07           C  
ATOM   1644  OD1 ASN A 332     -20.429  29.825 101.467  1.00 52.59           O  
ATOM   1645  ND2 ASN A 332     -22.320  30.854 102.127  1.00 52.17           N  
ATOM   1646  N   THR A 333     -24.096  26.767  98.693  1.00 39.04           N  
ATOM   1647  CA  THR A 333     -24.503  25.444  98.307  1.00 38.65           C  
ATOM   1648  C   THR A 333     -24.986  25.448  96.866  1.00 37.24           C  
ATOM   1649  O   THR A 333     -25.622  26.396  96.412  1.00 35.69           O  
ATOM   1650  CB  THR A 333     -25.607  25.007  99.286  1.00 39.48           C  
ATOM   1651  OG1 THR A 333     -24.996  24.710 100.566  1.00 40.50           O  
ATOM   1652  CG2 THR A 333     -26.229  23.776  98.887  1.00 40.79           C  
ATOM   1653  N   TYR A 334     -24.716  24.354  96.169  1.00 36.78           N  
ATOM   1654  CA  TYR A 334     -25.211  24.121  94.816  1.00 36.70           C  
ATOM   1655  C   TYR A 334     -26.715  24.166  94.789  1.00 36.75           C  
ATOM   1656  O   TYR A 334     -27.328  24.696  93.871  1.00 36.36           O  
ATOM   1657  CB  TYR A 334     -24.763  22.730  94.404  1.00 37.01           C  
ATOM   1658  CG  TYR A 334     -25.238  22.190  93.096  1.00 38.83           C  
ATOM   1659  CD1 TYR A 334     -24.370  22.115  92.014  1.00 41.43           C  
ATOM   1660  CD2 TYR A 334     -26.513  21.634  92.958  1.00 42.62           C  
ATOM   1661  CE1 TYR A 334     -24.768  21.567  90.825  1.00 43.30           C  
ATOM   1662  CE2 TYR A 334     -26.917  21.084  91.762  1.00 43.73           C  
ATOM   1663  CZ  TYR A 334     -26.031  21.058  90.704  1.00 45.81           C  
ATOM   1664  OH  TYR A 334     -26.382  20.503  89.498  1.00 52.11           O  
ATOM   1665  N   GLN A 335     -27.314  23.541  95.788  1.00 37.09           N  
ATOM   1666  CA  GLN A 335     -28.755  23.408  95.852  1.00 37.17           C  
ATOM   1667  C   GLN A 335     -29.409  24.807  96.017  1.00 36.68           C  
ATOM   1668  O   GLN A 335     -30.375  25.124  95.344  1.00 36.90           O  
ATOM   1669  CB  GLN A 335     -29.128  22.399  96.962  1.00 38.20           C  
ATOM   1670  CG  GLN A 335     -28.833  20.894  96.567  1.00 39.40           C  
ATOM   1671  CD  GLN A 335     -27.511  20.316  97.126  1.00 40.63           C  
ATOM   1672  OE1 GLN A 335     -27.465  19.143  97.565  1.00 40.09           O  
ATOM   1673  NE2 GLN A 335     -26.450  21.111  97.111  1.00 37.30           N  
ATOM   1674  N   GLU A 336     -28.859  25.619  96.895  1.00 35.75           N  
ATOM   1675  CA  GLU A 336     -29.284  26.997  97.127  1.00 36.41           C  
ATOM   1676  C   GLU A 336     -29.060  27.867  95.843  1.00 35.44           C  
ATOM   1677  O   GLU A 336     -29.918  28.641  95.451  1.00 34.15           O  
ATOM   1678  CB  GLU A 336     -28.496  27.429  98.354  1.00 37.35           C  
ATOM   1679  CG  GLU A 336     -28.426  28.841  98.883  1.00 40.69           C  
ATOM   1680  CD  GLU A 336     -27.178  28.952  99.797  1.00 47.40           C  
ATOM   1681  OE1 GLU A 336     -26.141  28.362  99.410  1.00 54.73           O  
ATOM   1682  OE2 GLU A 336     -27.172  29.586 100.879  1.00 41.89           O  
ATOM   1683  N   THR A 337     -27.948  27.656  95.147  1.00 33.96           N  
ATOM   1684  CA  THR A 337     -27.685  28.388  93.909  1.00 33.37           C  
ATOM   1685  C   THR A 337     -28.726  28.065  92.882  1.00 32.18           C  
ATOM   1686  O   THR A 337     -29.250  28.945  92.234  1.00 31.44           O  
ATOM   1687  CB  THR A 337     -26.278  28.057  93.393  1.00 32.55           C  
ATOM   1688  OG1 THR A 337     -25.334  28.477  94.371  1.00 34.24           O  
ATOM   1689  CG2 THR A 337     -25.928  28.871  92.162  1.00 31.75           C  
ATOM   1690  N   TYR A 338     -29.043  26.776  92.748  1.00 32.89           N  
ATOM   1691  CA  TYR A 338     -30.067  26.302  91.848  1.00 33.61           C  
ATOM   1692  C   TYR A 338     -31.400  26.989  92.134  1.00 33.01           C  
ATOM   1693  O   TYR A 338     -32.086  27.431  91.236  1.00 32.05           O  
ATOM   1694  CB  TYR A 338     -30.229  24.798  92.050  1.00 35.13           C  
ATOM   1695  CG  TYR A 338     -31.227  24.155  91.141  1.00 39.78           C  
ATOM   1696  CD1 TYR A 338     -30.810  23.443  90.024  1.00 43.93           C  
ATOM   1697  CD2 TYR A 338     -32.595  24.213  91.417  1.00 43.30           C  
ATOM   1698  CE1 TYR A 338     -31.733  22.826  89.184  1.00 46.78           C  
ATOM   1699  CE2 TYR A 338     -33.525  23.616  90.576  1.00 45.92           C  
ATOM   1700  CZ  TYR A 338     -33.088  22.924  89.467  1.00 48.35           C  
ATOM   1701  OH  TYR A 338     -34.001  22.320  88.639  1.00 51.80           O  
ATOM   1702  N   LYS A 339     -31.767  27.053  93.397  1.00 32.86           N  
ATOM   1703  CA  LYS A 339     -33.023  27.731  93.778  1.00 33.16           C  
ATOM   1704  C   LYS A 339     -33.007  29.189  93.344  1.00 32.07           C  
ATOM   1705  O   LYS A 339     -33.947  29.677  92.740  1.00 33.47           O  
ATOM   1706  CB  LYS A 339     -33.233  27.659  95.296  1.00 33.30           C  
ATOM   1707  N   ARG A 340     -31.913  29.860  93.637  1.00 31.85           N  
ATOM   1708  CA  ARG A 340     -31.756  31.270  93.338  1.00 31.84           C  
ATOM   1709  C   ARG A 340     -31.882  31.537  91.844  1.00 31.33           C  
ATOM   1710  O   ARG A 340     -32.629  32.423  91.420  1.00 31.30           O  
ATOM   1711  CB  ARG A 340     -30.429  31.758  93.894  1.00 32.42           C  
ATOM   1712  CG  ARG A 340     -30.429  31.747  95.444  1.00 36.23           C  
ATOM   1713  CD  ARG A 340     -31.032  32.952  96.029  1.00 40.79           C  
ATOM   1714  NE  ARG A 340     -30.382  34.105  95.413  1.00 46.15           N  
ATOM   1715  CZ  ARG A 340     -29.204  34.578  95.802  1.00 48.02           C  
ATOM   1716  NH1 ARG A 340     -28.656  35.605  95.157  1.00 49.44           N  
ATOM   1717  NH2 ARG A 340     -28.594  34.056  96.863  1.00 49.82           N  
ATOM   1718  N   ILE A 341     -31.232  30.707  91.045  1.00 30.93           N  
ATOM   1719  CA  ILE A 341     -31.287  30.841  89.577  1.00 30.25           C  
ATOM   1720  C   ILE A 341     -32.670  30.580  89.069  1.00 30.91           C  
ATOM   1721  O   ILE A 341     -33.210  31.315  88.246  1.00 31.84           O  
ATOM   1722  CB  ILE A 341     -30.299  29.870  88.925  1.00 29.54           C  
ATOM   1723  CG1 ILE A 341     -28.862  30.261  89.255  1.00 28.44           C  
ATOM   1724  CG2 ILE A 341     -30.519  29.818  87.391  1.00 29.38           C  
ATOM   1725  CD1 ILE A 341     -27.832  29.210  88.865  1.00 29.75           C  
ATOM   1726  N   SER A 342     -33.278  29.502  89.551  1.00 32.95           N  
ATOM   1727  CA  SER A 342     -34.595  29.124  89.099  1.00 34.03           C  
ATOM   1728  C   SER A 342     -35.635  30.212  89.423  1.00 34.45           C  
ATOM   1729  O   SER A 342     -36.534  30.431  88.656  1.00 35.51           O  
ATOM   1730  CB  SER A 342     -34.980  27.779  89.718  1.00 34.91           C  
ATOM   1731  OG  SER A 342     -36.366  27.589  89.626  1.00 40.73           O  
ATOM   1732  N   ARG A 343     -35.511  30.891  90.561  1.00 34.36           N  
ATOM   1733  CA  ARG A 343     -36.447  31.953  90.927  1.00 35.07           C  
ATOM   1734  C   ARG A 343     -35.974  33.323  90.412  1.00 34.74           C  
ATOM   1735  O   ARG A 343     -36.699  34.297  90.502  1.00 34.16           O  
ATOM   1736  CB  ARG A 343     -36.610  32.012  92.460  1.00 35.66           C  
ATOM   1737  CG  ARG A 343     -37.275  30.784  93.083  1.00 38.85           C  
ATOM   1738  CD  ARG A 343     -36.911  30.603  94.579  1.00 43.25           C  
ATOM   1739  NE  ARG A 343     -37.685  29.638  95.393  1.00 49.05           N  
ATOM   1740  CZ  ARG A 343     -38.198  28.453  95.005  1.00 52.83           C  
ATOM   1741  NH1 ARG A 343     -38.079  27.983  93.766  1.00 54.52           N  
ATOM   1742  NH2 ARG A 343     -38.854  27.709  95.901  1.00 53.95           N  
ATOM   1743  N   VAL A 344     -34.763  33.356  89.841  1.00 35.23           N  
ATOM   1744  CA  VAL A 344     -34.070  34.571  89.408  1.00 35.04           C  
ATOM   1745  C   VAL A 344     -34.012  35.578  90.542  1.00 34.63           C  
ATOM   1746  O   VAL A 344     -34.400  36.722  90.398  1.00 34.06           O  
ATOM   1747  CB  VAL A 344     -34.677  35.160  88.136  1.00 34.89           C  
ATOM   1748  CG1 VAL A 344     -33.714  36.118  87.478  1.00 36.09           C  
ATOM   1749  CG2 VAL A 344     -35.015  34.047  87.136  1.00 36.00           C  
ATOM   1750  N   GLU A 345     -33.534  35.147  91.697  1.00 35.68           N  
ATOM   1751  CA  GLU A 345     -33.513  36.051  92.830  1.00 37.17           C  
ATOM   1752  C   GLU A 345     -32.122  36.618  92.986  1.00 36.33           C  
ATOM   1753  O   GLU A 345     -31.174  35.933  93.354  1.00 36.07           O  
ATOM   1754  CB  GLU A 345     -34.017  35.434  94.131  1.00 38.35           C  
ATOM   1755  CG  GLU A 345     -33.890  33.958  94.248  1.00 42.71           C  
ATOM   1756  CD  GLU A 345     -34.321  33.456  95.622  1.00 48.70           C  
ATOM   1757  OE1 GLU A 345     -34.384  34.268  96.591  1.00 51.82           O  
ATOM   1758  OE2 GLU A 345     -34.570  32.242  95.733  1.00 54.58           O  
ATOM   1759  N   PHE A 346     -32.020  37.893  92.659  1.00 35.57           N  
ATOM   1760  CA  PHE A 346     -30.803  38.640  92.865  1.00 35.46           C  
ATOM   1761  C   PHE A 346     -31.147  40.096  93.160  1.00 35.57           C  
ATOM   1762  O   PHE A 346     -32.228  40.593  92.788  1.00 35.24           O  
ATOM   1763  CB  PHE A 346     -29.898  38.529  91.629  1.00 35.77           C  
ATOM   1764  CG  PHE A 346     -30.424  39.239  90.446  1.00 35.47           C  
ATOM   1765  CD1 PHE A 346     -31.314  38.627  89.596  1.00 36.72           C  
ATOM   1766  CD2 PHE A 346     -30.028  40.534  90.171  1.00 38.59           C  
ATOM   1767  CE1 PHE A 346     -31.801  39.284  88.496  1.00 36.14           C  
ATOM   1768  CE2 PHE A 346     -30.546  41.208  89.101  1.00 37.83           C  
ATOM   1769  CZ  PHE A 346     -31.420  40.586  88.252  1.00 38.38           C  
ATOM   1770  N   THR A 347     -30.245  40.751  93.875  1.00 35.44           N  
ATOM   1771  CA  THR A 347     -30.333  42.190  94.116  1.00 35.96           C  
ATOM   1772  C   THR A 347     -28.985  42.807  93.852  1.00 35.80           C  
ATOM   1773  O   THR A 347     -27.962  42.122  93.862  1.00 36.60           O  
ATOM   1774  CB  THR A 347     -30.736  42.489  95.579  1.00 35.80           C  
ATOM   1775  OG1 THR A 347     -29.790  41.882  96.456  1.00 36.80           O  
ATOM   1776  CG2 THR A 347     -32.055  41.838  95.955  1.00 35.85           C  
ATOM   1777  N   PHE A 348     -29.000  44.114  93.651  1.00 36.00           N  
ATOM   1778  CA  PHE A 348     -27.823  44.888  93.277  1.00 36.01           C  
ATOM   1779  C   PHE A 348     -27.328  45.646  94.488  1.00 37.66           C  
ATOM   1780  O   PHE A 348     -28.135  46.173  95.252  1.00 37.17           O  
ATOM   1781  CB  PHE A 348     -28.201  45.955  92.267  1.00 35.83           C  
ATOM   1782  CG  PHE A 348     -28.630  45.430  90.947  1.00 33.98           C  
ATOM   1783  CD1 PHE A 348     -29.956  45.503  90.555  1.00 34.85           C  
ATOM   1784  CD2 PHE A 348     -27.702  44.915  90.067  1.00 33.17           C  
ATOM   1785  CE1 PHE A 348     -30.348  45.049  89.323  1.00 34.24           C  
ATOM   1786  CE2 PHE A 348     -28.093  44.449  88.831  1.00 33.79           C  
ATOM   1787  CZ  PHE A 348     -29.413  44.518  88.460  1.00 33.29           C  
ATOM   1788  N   PRO A 349     -26.016  45.758  94.660  1.00 39.03           N  
ATOM   1789  CA  PRO A 349     -25.502  46.735  95.627  1.00 39.91           C  
ATOM   1790  C   PRO A 349     -25.852  48.134  95.148  1.00 40.59           C  
ATOM   1791  O   PRO A 349     -26.141  48.339  93.971  1.00 39.37           O  
ATOM   1792  CB  PRO A 349     -23.987  46.477  95.648  1.00 40.36           C  
ATOM   1793  CG  PRO A 349     -23.680  45.623  94.481  1.00 39.83           C  
ATOM   1794  CD  PRO A 349     -24.950  45.010  93.991  1.00 39.20           C  
ATOM   1795  N   ASP A 350     -25.849  49.101  96.056  1.00 42.26           N  
ATOM   1796  CA  ASP A 350     -26.244  50.469  95.706  1.00 43.43           C  
ATOM   1797  C   ASP A 350     -25.367  51.108  94.650  1.00 42.95           C  
ATOM   1798  O   ASP A 350     -25.850  51.929  93.871  1.00 43.53           O  
ATOM   1799  CB  ASP A 350     -26.232  51.369  96.947  1.00 44.45           C  
ATOM   1800  CG  ASP A 350     -27.332  51.022  97.920  1.00 47.92           C  
ATOM   1801  OD1 ASP A 350     -27.236  51.491  99.092  1.00 53.00           O  
ATOM   1802  OD2 ASP A 350     -28.312  50.279  97.611  1.00 51.14           O  
ATOM   1803  N   PHE A 351     -24.087  50.763  94.616  1.00 42.71           N  
ATOM   1804  CA  PHE A 351     -23.184  51.424  93.671  1.00 42.38           C  
ATOM   1805  C   PHE A 351     -23.495  51.125  92.199  1.00 42.92           C  
ATOM   1806  O   PHE A 351     -23.101  51.897  91.324  1.00 42.84           O  
ATOM   1807  CB  PHE A 351     -21.707  51.177  94.001  1.00 42.53           C  
ATOM   1808  CG  PHE A 351     -21.294  49.735  93.967  1.00 42.72           C  
ATOM   1809  CD1 PHE A 351     -21.236  48.993  95.141  1.00 41.80           C  
ATOM   1810  CD2 PHE A 351     -20.963  49.115  92.761  1.00 42.44           C  
ATOM   1811  CE1 PHE A 351     -20.859  47.666  95.122  1.00 42.21           C  
ATOM   1812  CE2 PHE A 351     -20.590  47.793  92.735  1.00 41.33           C  
ATOM   1813  CZ  PHE A 351     -20.542  47.058  93.912  1.00 42.59           C  
ATOM   1814  N   VAL A 352     -24.227  50.046  91.910  1.00 42.20           N  
ATOM   1815  CA  VAL A 352     -24.554  49.718  90.523  1.00 41.89           C  
ATOM   1816  C   VAL A 352     -25.526  50.718  89.919  1.00 42.12           C  
ATOM   1817  O   VAL A 352     -26.602  50.954  90.466  1.00 41.72           O  
ATOM   1818  CB  VAL A 352     -25.131  48.294  90.373  1.00 41.59           C  
ATOM   1819  CG1 VAL A 352     -25.430  47.997  88.915  1.00 41.10           C  
ATOM   1820  CG2 VAL A 352     -24.147  47.275  90.913  1.00 41.60           C  
ATOM   1821  N   THR A 353     -25.167  51.271  88.759  1.00 42.58           N  
ATOM   1822  CA  THR A 353     -25.951  52.336  88.128  1.00 42.97           C  
ATOM   1823  C   THR A 353     -27.214  51.853  87.436  1.00 43.58           C  
ATOM   1824  O   THR A 353     -27.354  50.671  87.135  1.00 43.31           O  
ATOM   1825  CB  THR A 353     -25.082  53.102  87.115  1.00 43.24           C  
ATOM   1826  OG1 THR A 353     -24.651  52.214  86.074  1.00 41.77           O  
ATOM   1827  CG2 THR A 353     -23.808  53.604  87.772  1.00 42.99           C  
ATOM   1828  N   GLU A 354     -28.131  52.774  87.149  1.00 44.02           N  
ATOM   1829  CA  GLU A 354     -29.427  52.373  86.611  1.00 45.14           C  
ATOM   1830  C   GLU A 354     -29.305  51.791  85.210  1.00 43.81           C  
ATOM   1831  O   GLU A 354     -30.112  50.954  84.818  1.00 43.39           O  
ATOM   1832  CB  GLU A 354     -30.436  53.535  86.603  1.00 46.69           C  
ATOM   1833  CG  GLU A 354     -31.129  53.831  87.946  1.00 51.39           C  
ATOM   1834  CD  GLU A 354     -31.020  52.713  88.983  1.00 56.89           C  
ATOM   1835  OE1 GLU A 354     -31.990  51.910  89.117  1.00 58.42           O  
ATOM   1836  OE2 GLU A 354     -29.962  52.653  89.666  1.00 60.80           O  
ATOM   1837  N   GLY A 355     -28.297  52.229  84.463  1.00 42.56           N  
ATOM   1838  CA  GLY A 355     -28.061  51.714  83.128  1.00 41.52           C  
ATOM   1839  C   GLY A 355     -27.601  50.271  83.197  1.00 40.44           C  
ATOM   1840  O   GLY A 355     -28.067  49.422  82.433  1.00 40.22           O  
ATOM   1841  N   ALA A 356     -26.677  49.995  84.112  1.00 39.77           N  
ATOM   1842  CA  ALA A 356     -26.176  48.640  84.302  1.00 39.30           C  
ATOM   1843  C   ALA A 356     -27.303  47.757  84.793  1.00 38.61           C  
ATOM   1844  O   ALA A 356     -27.481  46.668  84.298  1.00 38.02           O  
ATOM   1845  CB  ALA A 356     -25.036  48.628  85.272  1.00 39.15           C  
ATOM   1846  N   ARG A 357     -28.093  48.243  85.750  1.00 38.79           N  
ATOM   1847  CA  ARG A 357     -29.227  47.479  86.272  1.00 38.78           C  
ATOM   1848  C   ARG A 357     -30.212  47.143  85.186  1.00 39.17           C  
ATOM   1849  O   ARG A 357     -30.763  46.054  85.164  1.00 39.68           O  
ATOM   1850  CB  ARG A 357     -29.975  48.256  87.331  1.00 38.77           C  
ATOM   1851  CG  ARG A 357     -29.195  48.483  88.569  1.00 37.59           C  
ATOM   1852  CD  ARG A 357     -29.984  49.272  89.588  1.00 39.15           C  
ATOM   1853  NE  ARG A 357     -29.132  49.611  90.716  1.00 37.26           N  
ATOM   1854  CZ  ARG A 357     -29.447  49.458  91.986  1.00 37.25           C  
ATOM   1855  NH1 ARG A 357     -30.625  48.969  92.353  1.00 39.86           N  
ATOM   1856  NH2 ARG A 357     -28.553  49.787  92.904  1.00 37.49           N  
ATOM   1857  N   ASP A 358     -30.441  48.093  84.295  1.00 39.45           N  
ATOM   1858  CA  ASP A 358     -31.383  47.901  83.218  1.00 39.97           C  
ATOM   1859  C   ASP A 358     -30.921  46.806  82.269  1.00 39.03           C  
ATOM   1860  O   ASP A 358     -31.715  45.958  81.877  1.00 39.25           O  
ATOM   1861  CB  ASP A 358     -31.597  49.191  82.452  1.00 40.72           C  
ATOM   1862  CG  ASP A 358     -32.649  49.043  81.378  1.00 43.32           C  
ATOM   1863  OD1 ASP A 358     -33.855  49.131  81.707  1.00 47.28           O  
ATOM   1864  OD2 ASP A 358     -32.366  48.809  80.181  1.00 45.61           O  
ATOM   1865  N   LEU A 359     -29.638  46.817  81.914  1.00 38.06           N  
ATOM   1866  CA  LEU A 359     -29.073  45.818  81.013  1.00 37.32           C  
ATOM   1867  C   LEU A 359     -29.157  44.437  81.640  1.00 36.22           C  
ATOM   1868  O   LEU A 359     -29.589  43.479  80.997  1.00 35.85           O  
ATOM   1869  CB  LEU A 359     -27.600  46.125  80.699  1.00 37.34           C  
ATOM   1870  CG  LEU A 359     -27.017  45.803  79.317  1.00 39.18           C  
ATOM   1871  CD1 LEU A 359     -25.526  45.533  79.400  1.00 38.97           C  
ATOM   1872  CD2 LEU A 359     -27.725  44.723  78.565  1.00 38.40           C  
ATOM   1873  N   ILE A 360     -28.708  44.344  82.889  1.00 34.88           N  
ATOM   1874  CA  ILE A 360     -28.628  43.069  83.594  1.00 34.31           C  
ATOM   1875  C   ILE A 360     -30.021  42.483  83.820  1.00 34.58           C  
ATOM   1876  O   ILE A 360     -30.225  41.281  83.611  1.00 33.53           O  
ATOM   1877  CB  ILE A 360     -27.852  43.239  84.927  1.00 34.44           C  
ATOM   1878  CG1 ILE A 360     -26.375  43.532  84.632  1.00 33.45           C  
ATOM   1879  CG2 ILE A 360     -27.993  41.989  85.806  1.00 34.31           C  
ATOM   1880  CD1 ILE A 360     -25.647  44.151  85.745  1.00 33.13           C  
ATOM   1881  N   SER A 361     -30.971  43.336  84.200  1.00 34.76           N  
ATOM   1882  CA  SER A 361     -32.341  42.910  84.428  1.00 36.55           C  
ATOM   1883  C   SER A 361     -32.978  42.412  83.135  1.00 36.74           C  
ATOM   1884  O   SER A 361     -33.772  41.497  83.160  1.00 36.62           O  
ATOM   1885  CB  SER A 361     -33.183  44.031  85.053  1.00 37.10           C  
ATOM   1886  OG  SER A 361     -32.789  44.235  86.410  1.00 39.71           O  
ATOM   1887  N   ARG A 362     -32.597  42.985  82.000  1.00 37.39           N  
ATOM   1888  CA  ARG A 362     -33.128  42.532  80.708  1.00 38.22           C  
ATOM   1889  C   ARG A 362     -32.552  41.176  80.281  1.00 37.77           C  
ATOM   1890  O   ARG A 362     -33.243  40.383  79.633  1.00 38.13           O  
ATOM   1891  CB  ARG A 362     -32.865  43.575  79.622  1.00 38.95           C  
ATOM   1892  CG  ARG A 362     -33.811  44.760  79.655  1.00 43.39           C  
ATOM   1893  CD  ARG A 362     -33.320  45.967  78.861  1.00 48.17           C  
ATOM   1894  NE  ARG A 362     -34.238  47.106  78.981  1.00 53.54           N  
ATOM   1895  CZ  ARG A 362     -35.269  47.349  78.166  1.00 57.89           C  
ATOM   1896  NH1 ARG A 362     -35.543  46.539  77.142  1.00 59.51           N  
ATOM   1897  NH2 ARG A 362     -36.040  48.416  78.379  1.00 58.78           N  
ATOM   1898  N   LEU A 363     -31.299  40.913  80.656  1.00 36.51           N  
ATOM   1899  CA  LEU A 363     -30.611  39.683  80.286  1.00 36.21           C  
ATOM   1900  C   LEU A 363     -31.015  38.523  81.187  1.00 35.85           C  
ATOM   1901  O   LEU A 363     -31.098  37.386  80.737  1.00 35.64           O  
ATOM   1902  CB  LEU A 363     -29.094  39.890  80.362  1.00 36.14           C  
ATOM   1903  CG  LEU A 363     -28.210  40.281  79.159  1.00 37.73           C  
ATOM   1904  CD1 LEU A 363     -28.899  40.534  77.875  1.00 39.03           C  
ATOM   1905  CD2 LEU A 363     -27.257  41.403  79.515  1.00 37.54           C  
ATOM   1906  N   LEU A 364     -31.282  38.803  82.455  1.00 35.26           N  
ATOM   1907  CA  LEU A 364     -31.573  37.755  83.429  1.00 35.47           C  
ATOM   1908  C   LEU A 364     -33.077  37.549  83.522  1.00 36.60           C  
ATOM   1909  O   LEU A 364     -33.693  37.805  84.536  1.00 36.57           O  
ATOM   1910  CB  LEU A 364     -30.956  38.099  84.786  1.00 35.19           C  
ATOM   1911  CG  LEU A 364     -29.428  38.111  84.794  1.00 33.42           C  
ATOM   1912  CD1 LEU A 364     -28.889  38.382  86.194  1.00 34.74           C  
ATOM   1913  CD2 LEU A 364     -28.896  36.788  84.279  1.00 32.98           C  
ATOM   1914  N   LYS A 365     -33.665  37.101  82.424  1.00 37.27           N  
ATOM   1915  CA  LYS A 365     -35.081  36.785  82.388  1.00 38.49           C  
ATOM   1916  C   LYS A 365     -35.204  35.281  82.376  1.00 38.71           C  
ATOM   1917  O   LYS A 365     -34.480  34.618  81.646  1.00 38.18           O  
ATOM   1918  CB  LYS A 365     -35.734  37.370  81.145  1.00 38.52           C  
ATOM   1919  CG  LYS A 365     -35.973  38.861  81.174  1.00 41.29           C  
ATOM   1920  CD  LYS A 365     -36.776  39.287  82.396  1.00 45.60           C  
ATOM   1921  CE  LYS A 365     -37.740  40.412  82.074  1.00 47.05           C  
ATOM   1922  NZ  LYS A 365     -37.029  41.562  81.481  1.00 49.71           N  
ATOM   1923  N   HIS A 366     -36.096  34.745  83.204  1.00 39.01           N  
ATOM   1924  CA  HIS A 366     -36.333  33.317  83.261  1.00 39.97           C  
ATOM   1925  C   HIS A 366     -36.741  32.787  81.884  1.00 40.49           C  
ATOM   1926  O   HIS A 366     -36.268  31.754  81.443  1.00 39.75           O  
ATOM   1927  CB  HIS A 366     -37.432  32.973  84.291  1.00 40.30           C  
ATOM   1928  CG  HIS A 366     -37.555  31.505  84.556  1.00 41.68           C  
ATOM   1929  ND1 HIS A 366     -38.154  30.634  83.669  1.00 43.97           N  
ATOM   1930  CD2 HIS A 366     -37.141  30.751  85.602  1.00 42.42           C  
ATOM   1931  CE1 HIS A 366     -38.098  29.406  84.157  1.00 44.34           C  
ATOM   1932  NE2 HIS A 366     -37.484  29.448  85.327  1.00 44.02           N  
ATOM   1933  N   ASN A 367     -37.634  33.494  81.216  1.00 41.29           N  
ATOM   1934  CA  ASN A 367     -38.083  33.061  79.900  1.00 42.43           C  
ATOM   1935  C   ASN A 367     -37.065  33.516  78.853  1.00 41.96           C  
ATOM   1936  O   ASN A 367     -36.896  34.710  78.675  1.00 41.25           O  
ATOM   1937  CB  ASN A 367     -39.466  33.653  79.625  1.00 43.01           C  
ATOM   1938  CG  ASN A 367     -40.141  33.061  78.399  1.00 45.32           C  
ATOM   1939  OD1 ASN A 367     -41.327  33.303  78.170  1.00 50.00           O  
ATOM   1940  ND2 ASN A 367     -39.401  32.302  77.603  1.00 47.06           N  
ATOM   1941  N   PRO A 368     -36.398  32.576  78.177  1.00 42.41           N  
ATOM   1942  CA  PRO A 368     -35.347  32.908  77.204  1.00 42.86           C  
ATOM   1943  C   PRO A 368     -35.816  33.813  76.073  1.00 43.36           C  
ATOM   1944  O   PRO A 368     -35.061  34.677  75.645  1.00 42.76           O  
ATOM   1945  CB  PRO A 368     -34.937  31.550  76.624  1.00 42.47           C  
ATOM   1946  CG  PRO A 368     -35.418  30.538  77.543  1.00 43.05           C  
ATOM   1947  CD  PRO A 368     -36.592  31.118  78.274  1.00 42.88           C  
ATOM   1948  N   SER A 369     -37.042  33.602  75.601  1.00 44.67           N  
ATOM   1949  CA  SER A 369     -37.643  34.441  74.554  1.00 45.54           C  
ATOM   1950  C   SER A 369     -37.792  35.911  74.947  1.00 45.79           C  
ATOM   1951  O   SER A 369     -37.916  36.765  74.077  1.00 45.91           O  
ATOM   1952  CB  SER A 369     -39.018  33.896  74.165  1.00 45.85           C  
ATOM   1953  OG  SER A 369     -38.922  32.527  73.778  1.00 47.49           O  
ATOM   1954  N   GLN A 370     -37.796  36.210  76.247  1.00 46.32           N  
ATOM   1955  CA  GLN A 370     -37.801  37.608  76.710  1.00 46.83           C  
ATOM   1956  C   GLN A 370     -36.406  38.236  76.821  1.00 46.10           C  
ATOM   1957  O   GLN A 370     -36.285  39.430  77.080  1.00 46.07           O  
ATOM   1958  CB  GLN A 370     -38.524  37.724  78.051  1.00 47.34           C  
ATOM   1959  CG  GLN A 370     -40.020  37.362  77.966  1.00 50.29           C  
ATOM   1960  CD  GLN A 370     -40.710  37.322  79.324  1.00 54.07           C  
ATOM   1961  OE1 GLN A 370     -41.804  36.734  79.462  1.00 57.16           O  
ATOM   1962  NE2 GLN A 370     -40.085  37.939  80.329  1.00 54.47           N  
ATOM   1963  N   ARG A 371     -35.358  37.432  76.665  1.00 45.66           N  
ATOM   1964  CA  ARG A 371     -33.985  37.950  76.666  1.00 44.90           C  
ATOM   1965  C   ARG A 371     -33.719  38.680  75.361  1.00 45.18           C  
ATOM   1966  O   ARG A 371     -34.189  38.241  74.319  1.00 45.54           O  
ATOM   1967  CB  ARG A 371     -32.974  36.824  76.857  1.00 44.25           C  
ATOM   1968  CG  ARG A 371     -33.008  36.260  78.256  1.00 40.59           C  
ATOM   1969  CD  ARG A 371     -32.165  35.058  78.460  1.00 37.58           C  
ATOM   1970  NE  ARG A 371     -32.776  34.194  79.454  1.00 35.66           N  
ATOM   1971  CZ  ARG A 371     -32.600  32.889  79.550  1.00 34.82           C  
ATOM   1972  NH1 ARG A 371     -33.259  32.219  80.486  1.00 35.43           N  
ATOM   1973  NH2 ARG A 371     -31.757  32.243  78.752  1.00 34.10           N  
ATOM   1974  N   PRO A 372     -32.984  39.788  75.399  1.00 45.56           N  
ATOM   1975  CA  PRO A 372     -32.735  40.548  74.172  1.00 45.64           C  
ATOM   1976  C   PRO A 372     -31.830  39.805  73.204  1.00 45.96           C  
ATOM   1977  O   PRO A 372     -31.141  38.840  73.555  1.00 46.26           O  
ATOM   1978  CB  PRO A 372     -32.071  41.832  74.674  1.00 45.69           C  
ATOM   1979  CG  PRO A 372     -31.487  41.494  75.993  1.00 45.72           C  
ATOM   1980  CD  PRO A 372     -32.369  40.429  76.578  1.00 45.74           C  
ATOM   1981  N   MET A 373     -31.864  40.236  71.955  1.00 46.13           N  
ATOM   1982  CA  MET A 373     -30.897  39.778  70.980  1.00 46.43           C  
ATOM   1983  C   MET A 373     -29.587  40.504  71.254  1.00 45.28           C  
ATOM   1984  O   MET A 373     -29.563  41.520  71.928  1.00 43.75           O  
ATOM   1985  CB  MET A 373     -31.369  40.100  69.573  1.00 47.51           C  
ATOM   1986  CG  MET A 373     -32.672  39.427  69.186  1.00 51.60           C  
ATOM   1987  SD  MET A 373     -33.126  39.934  67.531  1.00 59.96           S  
ATOM   1988  CE  MET A 373     -33.178  41.814  67.691  1.00 58.92           C  
ATOM   1989  N   LEU A 374     -28.500  39.977  70.715  1.00 44.80           N  
ATOM   1990  CA  LEU A 374     -27.188  40.531  70.985  1.00 44.91           C  
ATOM   1991  C   LEU A 374     -27.093  41.942  70.410  1.00 44.98           C  
ATOM   1992  O   LEU A 374     -26.437  42.788  70.987  1.00 44.02           O  
ATOM   1993  CB  LEU A 374     -26.099  39.636  70.424  1.00 44.85           C  
ATOM   1994  CG  LEU A 374     -25.802  38.385  71.263  1.00 45.55           C  
ATOM   1995  CD1 LEU A 374     -24.931  37.406  70.480  1.00 46.34           C  
ATOM   1996  CD2 LEU A 374     -25.128  38.763  72.557  1.00 44.97           C  
ATOM   1997  N   ARG A 375     -27.774  42.180  69.288  1.00 45.10           N  
ATOM   1998  CA  ARG A 375     -27.823  43.505  68.658  1.00 45.47           C  
ATOM   1999  C   ARG A 375     -28.328  44.543  69.646  1.00 45.29           C  
ATOM   2000  O   ARG A 375     -27.787  45.641  69.754  1.00 46.09           O  
ATOM   2001  CB  ARG A 375     -28.756  43.480  67.440  1.00 45.40           C  
ATOM   2002  N   GLU A 376     -29.360  44.164  70.385  1.00 45.31           N  
ATOM   2003  CA  GLU A 376     -29.957  45.028  71.391  1.00 45.29           C  
ATOM   2004  C   GLU A 376     -29.026  45.318  72.570  1.00 44.18           C  
ATOM   2005  O   GLU A 376     -29.126  46.366  73.180  1.00 44.79           O  
ATOM   2006  CB  GLU A 376     -31.275  44.424  71.868  1.00 45.76           C  
ATOM   2007  CG  GLU A 376     -32.280  44.241  70.741  1.00 48.98           C  
ATOM   2008  CD  GLU A 376     -33.623  43.720  71.228  1.00 53.16           C  
ATOM   2009  OE1 GLU A 376     -33.738  42.499  71.450  1.00 53.55           O  
ATOM   2010  OE2 GLU A 376     -34.566  44.539  71.378  1.00 56.84           O  
ATOM   2011  N   VAL A 377     -28.127  44.389  72.885  1.00 42.89           N  
ATOM   2012  CA  VAL A 377     -27.115  44.596  73.925  1.00 41.86           C  
ATOM   2013  C   VAL A 377     -26.040  45.547  73.427  1.00 41.74           C  
ATOM   2014  O   VAL A 377     -25.616  46.436  74.143  1.00 41.08           O  
ATOM   2015  CB  VAL A 377     -26.428  43.269  74.339  1.00 41.34           C  
ATOM   2016  CG1 VAL A 377     -25.302  43.519  75.339  1.00 40.95           C  
ATOM   2017  CG2 VAL A 377     -27.449  42.289  74.898  1.00 41.77           C  
ATOM   2018  N   LEU A 378     -25.595  45.344  72.193  1.00 41.95           N  
ATOM   2019  CA  LEU A 378     -24.539  46.161  71.613  1.00 43.01           C  
ATOM   2020  C   LEU A 378     -24.935  47.634  71.450  1.00 43.84           C  
ATOM   2021  O   LEU A 378     -24.061  48.518  71.432  1.00 44.40           O  
ATOM   2022  CB  LEU A 378     -24.093  45.555  70.286  1.00 43.21           C  
ATOM   2023  CG  LEU A 378     -23.330  44.248  70.518  1.00 43.34           C  
ATOM   2024  CD1 LEU A 378     -23.182  43.432  69.241  1.00 45.22           C  
ATOM   2025  CD2 LEU A 378     -21.983  44.538  71.130  1.00 42.98           C  
ATOM   2026  N   GLU A 379     -26.242  47.890  71.381  1.00 44.15           N  
ATOM   2027  CA  GLU A 379     -26.789  49.226  71.184  1.00 44.97           C  
ATOM   2028  C   GLU A 379     -27.514  49.722  72.424  1.00 44.66           C  
ATOM   2029  O   GLU A 379     -28.221  50.735  72.384  1.00 44.80           O  
ATOM   2030  CB  GLU A 379     -27.741  49.221  69.985  1.00 46.09           C  
ATOM   2031  CG  GLU A 379     -27.018  49.065  68.652  1.00 48.66           C  
ATOM   2032  CD  GLU A 379     -27.932  48.691  67.492  1.00 54.48           C  
ATOM   2033  OE1 GLU A 379     -29.186  48.754  67.638  1.00 57.34           O  
ATOM   2034  OE2 GLU A 379     -27.382  48.327  66.418  1.00 58.52           O  
ATOM   2035  N   HIS A 380     -27.340  49.020  73.544  1.00 43.66           N  
ATOM   2036  CA  HIS A 380     -27.891  49.479  74.797  1.00 42.87           C  
ATOM   2037  C   HIS A 380     -27.183  50.779  75.185  1.00 42.54           C  
ATOM   2038  O   HIS A 380     -25.985  50.852  75.025  1.00 42.24           O  
ATOM   2039  CB  HIS A 380     -27.688  48.421  75.890  1.00 42.68           C  
ATOM   2040  CG  HIS A 380     -28.350  48.775  77.173  1.00 41.48           C  
ATOM   2041  ND1 HIS A 380     -29.607  48.326  77.511  1.00 42.47           N  
ATOM   2042  CD2 HIS A 380     -27.941  49.559  78.193  1.00 39.05           C  
ATOM   2043  CE1 HIS A 380     -29.937  48.816  78.692  1.00 41.50           C  
ATOM   2044  NE2 HIS A 380     -28.943  49.567  79.130  1.00 41.46           N  
ATOM   2045  N   PRO A 381     -27.906  51.794  75.672  1.00 42.72           N  
ATOM   2046  CA  PRO A 381     -27.294  53.090  75.996  1.00 42.52           C  
ATOM   2047  C   PRO A 381     -26.151  53.034  77.010  1.00 42.11           C  
ATOM   2048  O   PRO A 381     -25.219  53.804  76.875  1.00 41.36           O  
ATOM   2049  CB  PRO A 381     -28.456  53.902  76.591  1.00 42.95           C  
ATOM   2050  CG  PRO A 381     -29.682  53.268  76.114  1.00 43.70           C  
ATOM   2051  CD  PRO A 381     -29.364  51.818  75.902  1.00 43.17           C  
ATOM   2052  N   TRP A 382     -26.255  52.189  78.038  1.00 40.59           N  
ATOM   2053  CA  TRP A 382     -25.169  51.991  78.990  1.00 40.49           C  
ATOM   2054  C   TRP A 382     -23.893  51.436  78.343  1.00 40.49           C  
ATOM   2055  O   TRP A 382     -22.790  51.871  78.675  1.00 40.78           O  
ATOM   2056  CB  TRP A 382     -25.604  51.067  80.127  1.00 39.95           C  
ATOM   2057  CG  TRP A 382     -24.588  50.955  81.174  1.00 39.49           C  
ATOM   2058  CD1 TRP A 382     -24.318  51.860  82.139  1.00 39.96           C  
ATOM   2059  CD2 TRP A 382     -23.684  49.869  81.370  1.00 38.32           C  
ATOM   2060  NE1 TRP A 382     -23.301  51.402  82.943  1.00 41.25           N  
ATOM   2061  CE2 TRP A 382     -22.889  50.180  82.484  1.00 39.16           C  
ATOM   2062  CE3 TRP A 382     -23.459  48.659  80.710  1.00 39.28           C  
ATOM   2063  CZ2 TRP A 382     -21.894  49.332  82.954  1.00 36.67           C  
ATOM   2064  CZ3 TRP A 382     -22.472  47.818  81.183  1.00 38.32           C  
ATOM   2065  CH2 TRP A 382     -21.702  48.161  82.287  1.00 37.58           C  
ATOM   2066  N   ILE A 383     -24.046  50.466  77.452  1.00 41.06           N  
ATOM   2067  CA  ILE A 383     -22.911  49.916  76.700  1.00 41.54           C  
ATOM   2068  C   ILE A 383     -22.313  50.980  75.776  1.00 42.87           C  
ATOM   2069  O   ILE A 383     -21.106  51.139  75.691  1.00 43.20           O  
ATOM   2070  CB  ILE A 383     -23.343  48.671  75.864  1.00 41.42           C  
ATOM   2071  CG1 ILE A 383     -23.756  47.493  76.775  1.00 40.38           C  
ATOM   2072  CG2 ILE A 383     -22.219  48.223  74.928  1.00 40.90           C  
ATOM   2073  CD1 ILE A 383     -22.602  46.886  77.552  1.00 40.32           C  
ATOM   2074  N   THR A 384     -23.173  51.710  75.088  1.00 44.13           N  
ATOM   2075  CA  THR A 384     -22.741  52.751  74.159  1.00 45.35           C  
ATOM   2076  C   THR A 384     -21.933  53.854  74.836  1.00 45.00           C  
ATOM   2077  O   THR A 384     -20.898  54.274  74.325  1.00 46.00           O  
ATOM   2078  CB  THR A 384     -23.986  53.324  73.473  1.00 45.39           C  
ATOM   2079  OG1 THR A 384     -24.455  52.354  72.532  1.00 47.37           O  
ATOM   2080  CG2 THR A 384     -23.651  54.537  72.635  1.00 48.54           C  
ATOM   2081  N   ALA A 385     -22.400  54.300  75.992  1.00 44.53           N  
ATOM   2082  CA  ALA A 385     -21.765  55.382  76.715  1.00 44.56           C  
ATOM   2083  C   ALA A 385     -20.499  54.955  77.426  1.00 44.55           C  
ATOM   2084  O   ALA A 385     -19.643  55.805  77.708  1.00 44.84           O  
ATOM   2085  CB  ALA A 385     -22.730  55.962  77.723  1.00 44.81           C  
ATOM   2086  N   ASN A 386     -20.354  53.659  77.725  1.00 43.32           N  
ATOM   2087  CA  ASN A 386     -19.207  53.203  78.496  1.00 42.81           C  
ATOM   2088  C   ASN A 386     -18.157  52.377  77.767  1.00 42.63           C  
ATOM   2089  O   ASN A 386     -17.031  52.329  78.207  1.00 41.88           O  
ATOM   2090  CB  ASN A 386     -19.675  52.465  79.746  1.00 42.66           C  
ATOM   2091  CG  ASN A 386     -20.340  53.393  80.745  1.00 42.33           C  
ATOM   2092  OD1 ASN A 386     -19.666  54.071  81.521  1.00 43.25           O  
ATOM   2093  ND2 ASN A 386     -21.665  53.430  80.726  1.00 43.46           N  
ATOM   2094  N   SER A 387     -18.516  51.741  76.668  1.00 43.45           N  
ATOM   2095  CA  SER A 387     -17.598  50.863  75.962  1.00 44.67           C  
ATOM   2096  C   SER A 387     -16.559  51.628  75.167  1.00 45.71           C  
ATOM   2097  O   SER A 387     -16.906  52.587  74.484  1.00 46.05           O  
ATOM   2098  CB  SER A 387     -18.342  49.976  74.968  1.00 44.25           C  
ATOM   2099  OG  SER A 387     -17.414  49.113  74.316  1.00 44.78           O  
ATOM   2100  N   SER A 388     -15.321  51.131  75.198  1.00 46.80           N  
ATOM   2101  CA  SER A 388     -14.223  51.615  74.358  1.00 47.66           C  
ATOM   2102  C   SER A 388     -14.302  51.126  72.912  1.00 47.92           C  
ATOM   2103  O   SER A 388     -15.090  50.232  72.574  1.00 49.14           O  
ATOM   2104  CB  SER A 388     -12.885  51.187  74.951  1.00 47.85           C  
ATOM   2105  OG  SER A 388     -12.776  51.649  76.286  1.00 49.51           O  
TER    2106      SER A 388                                                      
HETATM 2107 MG    MG A2086     -13.491  22.622  79.173  1.00 29.85          MG  
HETATM 2108 MG    MG A2088     -12.339  25.972  81.136  1.00 29.40          MG  
HETATM 2109  P   PO4 A   1     -24.757  17.645  76.266  1.00 63.09           P  
HETATM 2110  O1  PO4 A   1     -24.862  18.289  74.906  1.00 64.88           O  
HETATM 2111  O2  PO4 A   1     -25.925  16.697  76.425  1.00 67.98           O  
HETATM 2112  O3  PO4 A   1     -23.476  16.852  76.383  1.00 64.06           O  
HETATM 2113  O4  PO4 A   1     -24.809  18.689  77.344  1.00 64.75           O  
HETATM 2114  PB  ADP A2001     -10.922  23.177  81.000  1.00 32.94           P  
HETATM 2115  O1B ADP A2001     -11.708  22.755  79.793  1.00 30.32           O  
HETATM 2116  O2B ADP A2001     -10.446  22.008  81.842  1.00 35.66           O  
HETATM 2117  O3B ADP A2001     -11.704  24.214  81.811  1.00 30.64           O  
HETATM 2118  PA  ADP A2001      -9.492  25.355  79.860  1.00 31.65           P  
HETATM 2119  O1A ADP A2001      -9.338  25.363  78.374  1.00 30.48           O  
HETATM 2120  O2A ADP A2001     -10.643  26.217  80.297  1.00 29.26           O  
HETATM 2121  O3A ADP A2001      -9.568  23.870  80.508  1.00 32.35           O  
HETATM 2122  O5' ADP A2001      -8.152  25.875  80.518  1.00 31.77           O  
HETATM 2123  C5' ADP A2001      -7.997  25.879  81.925  1.00 32.00           C  
HETATM 2124  C4' ADP A2001      -7.210  27.120  82.337  1.00 31.28           C  
HETATM 2125  O4' ADP A2001      -5.956  27.180  81.667  1.00 29.26           O  
HETATM 2126  C3' ADP A2001      -7.926  28.411  81.989  1.00 32.01           C  
HETATM 2127  O3' ADP A2001      -8.955  28.733  82.907  1.00 33.25           O  
HETATM 2128  C2' ADP A2001      -6.772  29.374  81.920  1.00 30.14           C  
HETATM 2129  O2' ADP A2001      -6.406  29.720  83.239  1.00 34.66           O  
HETATM 2130  C1' ADP A2001      -5.671  28.537  81.320  1.00 30.76           C  
HETATM 2131  N9  ADP A2001      -5.607  28.641  79.863  1.00 30.69           N  
HETATM 2132  C8  ADP A2001      -6.342  27.878  78.987  1.00 31.98           C  
HETATM 2133  N7  ADP A2001      -6.041  28.235  77.706  1.00 30.56           N  
HETATM 2134  C5  ADP A2001      -5.126  29.207  77.787  1.00 28.06           C  
HETATM 2135  C6  ADP A2001      -4.499  29.902  76.794  1.00 30.48           C  
HETATM 2136  N6  ADP A2001      -4.700  29.586  75.497  1.00 27.18           N  
HETATM 2137  N1  ADP A2001      -3.609  30.863  77.166  1.00 30.36           N  
HETATM 2138  C2  ADP A2001      -3.341  31.141  78.492  1.00 32.40           C  
HETATM 2139  N3  ADP A2001      -3.970  30.432  79.483  1.00 31.40           N  
HETATM 2140  C4  ADP A2001      -4.835  29.467  79.126  1.00 29.64           C  
HETATM 2141  O   HOH A2089      -4.571  33.208  84.057  1.00 48.82           O  
HETATM 2142  O   HOH A2090      -9.928  27.057  74.333  1.00 29.14           O  
HETATM 2143  O   HOH A2091      -0.166  31.714  70.176  1.00 29.81           O  
HETATM 2144  O   HOH A2092      -1.165  31.947  83.775  1.00 47.75           O  
HETATM 2145  O   HOH A2093     -25.254  41.198  66.837  1.00 58.44           O  
HETATM 2146  O   HOH A2094     -25.220  43.504  65.772  1.00 64.28           O  
HETATM 2147  O   HOH A2095     -32.361  31.438  69.131  1.00 67.16           O  
HETATM 2148  O   HOH A2096     -24.386  33.329  89.917  1.00 33.52           O  
HETATM 2149  O   HOH A2097     -14.829  21.612  82.482  1.00 41.81           O  
HETATM 2150  O   HOH A2098     -15.339  22.274  78.509  1.00 38.03           O  
HETATM 2151  O   HOH A2099     -11.273  29.832  67.169  1.00 49.34           O  
HETATM 2152  O   HOH A2100      -9.663  28.249  65.542  1.00 46.75           O  
HETATM 2153  O   HOH A3001      -9.997  28.791  79.016  1.00 32.88           O  
HETATM 2154  O   HOH A3003     -14.414  22.864  80.902  1.00 29.56           O  
HETATM 2155  O   HOH A3004     -13.699  20.346  79.851  1.00 44.01           O  
HETATM 2156  O   HOH A3005     -26.940  31.609  86.565  1.00 30.10           O  
HETATM 2157  O   HOH A3006     -23.042  30.476  78.316  1.00 36.19           O  
HETATM 2158  O   HOH A3007     -30.325  16.914  72.212  1.00 45.73           O  
HETATM 2159  O   HOH A3008     -18.158  25.393  75.593  1.00 33.60           O  
HETATM 2160  O   HOH A3009     -11.647  26.821  82.855  1.00 35.75           O  
HETATM 2161  O   HOH A3010      -8.648  27.328  76.760  1.00 35.52           O  
HETATM 2162  O   HOH A3011     -37.918  36.605  85.015  1.00 39.45           O  
HETATM 2163  O   HOH A3012     -27.834  38.822  94.258  1.00 37.56           O  
HETATM 2164  O   HOH A3013     -16.624  24.721  78.298  1.00 32.30           O  
HETATM 2165  O   HOH A3014      -8.268  34.963  68.266  1.00 33.39           O  
HETATM 2166  O   HOH A3015      -0.914  17.915  82.937  1.00 36.13           O  
HETATM 2167  O   HOH A3017     -14.990  34.898  89.024  1.00 48.09           O  
HETATM 2168  O   HOH A3018     -22.784  25.728  92.261  1.00 48.49           O  
HETATM 2169  O   HOH A3021     -11.885  23.583  84.346  1.00 41.15           O  
HETATM 2170  O   HOH A3022     -12.683  21.558  77.583  1.00 39.34           O  
HETATM 2171  O   HOH A3023     -37.539  43.161  79.820  1.00 60.11           O  
HETATM 2172  O   HOH A3024      -5.587  15.241  86.171  1.00 62.42           O  
HETATM 2173  O   HOH A3026      -8.315  43.708  79.381  1.00 46.98           O  
HETATM 2174  O   HOH A3027     -23.128  19.803  67.838  1.00 48.20           O  
HETATM 2175  O   HOH A3028     -10.865  32.558  66.324  1.00 36.12           O  
HETATM 2176  O   HOH A3029     -15.756  32.230  88.220  1.00 43.18           O  
HETATM 2177  O   HOH A3030      -0.215  34.786  71.367  1.00 53.01           O  
HETATM 2178  O   HOH A3031     -20.448  50.270  89.114  1.00 49.98           O  
HETATM 2179  O   HOH A3032      -4.366  26.030  61.599  1.00 59.54           O  
HETATM 2180  O   HOH A3033      -6.531  20.531  80.247  1.00 41.41           O  
HETATM 2181  O   HOH A3034     -26.982  54.704  81.117  1.00 45.84           O  
HETATM 2182  O   HOH A3036      -3.564  31.869  81.788  1.00 46.46           O  
HETATM 2183  O   HOH A3037     -28.203  35.404  69.891  1.00 50.38           O  
HETATM 2184  O   HOH A3038     -26.204  36.250  65.291  1.00 48.42           O  
HETATM 2185  O   HOH A3039      14.101  34.471  65.206  1.00 53.95           O  
HETATM 2186  O   HOH A3040     -34.949  43.492  76.787  1.00 52.43           O  
HETATM 2187  O   HOH A3041     -39.255  35.975  82.265  1.00 47.57           O  
HETATM 2188  O   HOH A3043     -14.187  39.778  92.753  1.00 39.49           O  
HETATM 2189  O   HOH A3044     -17.824  51.055  95.240  1.00 60.32           O  
HETATM 2190  O   HOH A3045     -17.693  46.693  68.499  1.00 54.11           O  
HETATM 2191  O   HOH A3046     -21.076  27.932  83.122  1.00 43.07           O  
HETATM 2192  O   HOH A3047     -32.442  28.686  75.920  1.00 38.37           O  
HETATM 2193  O   HOH A3048     -26.649  54.628  84.283  1.00 55.31           O  
HETATM 2194  O   HOH A3049     -29.092  37.609  69.072  1.00 47.86           O  
HETATM 2195  O   HOH A3050       1.014  35.033  80.609  1.00 42.94           O  
HETATM 2196  O   HOH A3051     -18.079  48.206  89.552  1.00 34.12           O  
HETATM 2197  O   HOH A3052     -22.751  50.248  87.681  1.00 40.21           O  
HETATM 2198  O   HOH A3054     -28.314  40.064  67.231  1.00 38.79           O  
HETATM 2199  O   HOH A3055      -5.721  27.801  86.501  1.00 44.26           O  
HETATM 2200  O   HOH A3056     -22.079  29.548  81.264  1.00 50.54           O  
HETATM 2201  O   HOH A3057     -21.807  27.959  85.787  1.00 32.36           O  
HETATM 2202  O   HOH A3058     -19.292  55.436  84.167  1.00 64.31           O  
HETATM 2203  O   HOH A3059     -16.900  53.292  86.785  1.00 64.01           O  
HETATM 2204  O   HOH A3060     -11.588  48.408  86.239  1.00 44.19           O  
HETATM 2205  O   HOH A3061     -35.183  41.431  78.433  1.00 44.40           O  
HETATM 2206  O   HOH A3062     -35.795  29.258  81.313  1.00 46.48           O  
HETATM 2207  O   HOH A3063     -20.407  19.988  74.156  1.00 51.42           O  
HETATM 2208  O   HOH A3064      -5.455  37.936  83.995  1.00 38.30           O  
HETATM 2209  O   HOH A3066      -2.664  38.075  71.632  1.00 47.20           O  
HETATM 2210  O   HOH A3067      -3.947  35.799  72.232  1.00 37.68           O  
HETATM 2211  O   HOH A3068     -29.794  38.986  96.825  1.00 57.62           O  
HETATM 2212  O   HOH A3070     -13.968  25.556  82.240  1.00 32.05           O  
CONECT 1109 2108                                                                
CONECT 1199 2107 2108                                                           
CONECT 1200 2107                                                                
CONECT 2107 1199 1200 2115 2150                                                 
CONECT 2107 2154 2155 2170                                                      
CONECT 2108 1109 1199 2117 2120                                                 
CONECT 2108 2160 2212                                                           
CONECT 2109 2110 2111 2112 2113                                                 
CONECT 2110 2109                                                                
CONECT 2111 2109                                                                
CONECT 2112 2109                                                                
CONECT 2113 2109                                                                
CONECT 2114 2115 2116 2117 2121                                                 
CONECT 2115 2107 2114                                                           
CONECT 2116 2114                                                                
CONECT 2117 2108 2114                                                           
CONECT 2118 2119 2120 2121 2122                                                 
CONECT 2119 2118                                                                
CONECT 2120 2108 2118                                                           
CONECT 2121 2114 2118                                                           
CONECT 2122 2118 2123                                                           
CONECT 2123 2122 2124                                                           
CONECT 2124 2123 2125 2126                                                      
CONECT 2125 2124 2130                                                           
CONECT 2126 2124 2127 2128                                                      
CONECT 2127 2126                                                                
CONECT 2128 2126 2129 2130                                                      
CONECT 2129 2128                                                                
CONECT 2130 2125 2128 2131                                                      
CONECT 2131 2130 2132 2140                                                      
CONECT 2132 2131 2133                                                           
CONECT 2133 2132 2134                                                           
CONECT 2134 2133 2135 2140                                                      
CONECT 2135 2134 2136 2137                                                      
CONECT 2136 2135                                                                
CONECT 2137 2135 2138                                                           
CONECT 2138 2137 2139                                                           
CONECT 2139 2138 2140                                                           
CONECT 2140 2131 2134 2139                                                      
CONECT 2150 2107                                                                
CONECT 2154 2107                                                                
CONECT 2155 2107                                                                
CONECT 2160 2108                                                                
CONECT 2170 2107                                                                
CONECT 2212 2108                                                                
MASTER      426    0    4   14    9    0   13    6 2211    1   45   21          
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.