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.


***  1h2k_sinmut  ***

elNémo ID: 21051011164345421

Job options:

ID        	=	 21051011164345421
JOBID     	=	 1h2k_sinmut
USERID    	=	 100428742
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 1h2k_sinmut

HEADER    TRANSCRIPTION ACTIVATOR/INHIBITOR       12-AUG-02   1H2K              
TITLE     FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT    
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FACTOR INHIBITING HIF1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;                          
COMPND   7 CHAIN: S;                                                            
COMPND   8 FRAGMENT: C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES 786-  
COMPND   9 826;                                                                 
COMPND  10 SYNONYM: HIF-1 ALPHA, ARNT INTERACTING PROTEIN, MEMBER OF PAS PROTEIN
COMPND  11 1;                                                                   
COMPND  12 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A(+);                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX-GP-1                                 
KEYWDS    TRANSCRIPTION ACTIVATOR-INHIBITOR COMPLEX, FIH, HIF, DSBH, OXYGENASE, 
KEYWDS   2 TRANSCRIPTION, HYPOXIA, 2- OXOGLUTARATE, ASPARAGINYL HYDROXYLASE,    
KEYWDS   3 PHOSPHORYLATION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,I.SCHLEMMINGER,J.F.SEIBEL,        
AUTHOR   2 C.J.SCHOFIELD                                                        
REVDAT   6   21-FEB-18 1H2K    1       JRNL                                     
REVDAT   5   13-JUL-11 1H2K    1       VERSN                                    
REVDAT   4   21-JUL-09 1H2K    1       HETNAM                                   
REVDAT   3   24-FEB-09 1H2K    1       VERSN                                    
REVDAT   2   30-JAN-03 1H2K    1       JRNL                                     
REVDAT   1   28-NOV-02 1H2K    0                                                
JRNL        AUTH   J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,              
JRNL        AUTH 2 I.SCHLEMMINGER,C.PUGH,P.RATCLIFFE,C.J.SCHOFIELD              
JRNL        TITL   STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR      
JRNL        TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF         
JRNL        TITL 3 HIF-1ALPHA                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 278  1802 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12446723                                                     
JRNL        DOI    10.1074/JBC.C200644200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28171                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2340                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1906                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 152                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2875                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.156         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.588         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2973 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2561 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4044 ; 1.374 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5979 ; 0.722 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 4.018 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;17.698 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   416 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3333 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   604 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   714 ; 0.218 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2499 ; 0.204 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   259 ; 0.152 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     4 ; 0.087 ; 0.500       
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):    18 ; 0.245 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    72 ; 0.248 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.255 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     1 ; 0.052 ; 0.500       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A   349                          
REMARK   3    RESIDUE RANGE :   S   795        S   823                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6620  27.4620  28.2370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1474 T22:   0.0149                                     
REMARK   3      T33:   0.0919 T12:  -0.0099                                     
REMARK   3      T13:  -0.0455 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0098 L22:   2.2577                                     
REMARK   3      L33:   1.2037 L12:   0.6963                                     
REMARK   3      L13:   0.4840 L23:   1.0420                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.1525 S13:  -0.0400                       
REMARK   3      S21:   0.1459 S22:   0.0002 S23:   0.1021                       
REMARK   3      S31:   0.1876 S32:  -0.0468 S33:  -0.0290                       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1H2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290011170.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE, 4% PEG400,       
REMARK 280  0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM        
REMARK 280  FE(II), 2.5MM NOG AND 2.5MM PEPTIDE, PH 7.50                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.32800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.08050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.66400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.08050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      109.99200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.08050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.66400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.08050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      109.99200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.32800            
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 300 REMARK: THE PROTEIN IS A DIMERIC   FORMED BY CHAIN                   
REMARK 300   A.A HETERODIMERIC ASSOCIATION OF CHAIN A WITH                      
REMARK 300  CHAIN SPRODUCES A TETRAMER.THE BURIED SURFACE AREA                  
REMARK 300   SHOWN BELOW IS AN AVERAGECALCULATED FOR THE                        
REMARK 300  HETEROTETRAMER AND DOES NOTCORRESPOND TO THE BURIED                 
REMARK 300   SURFACE AREA FOR THEHOMODIMER OF CHAIN A                           
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       86.16100            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       86.16100            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.32800            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     SER S   786                                                      
REMARK 465     MET S   787                                                      
REMARK 465     ASP S   788                                                      
REMARK 465     GLU S   789                                                      
REMARK 465     SER S   790                                                      
REMARK 465     GLY S   791                                                      
REMARK 465     LEU S   792                                                      
REMARK 465     PRO S   793                                                      
REMARK 465     GLN S   794                                                      
REMARK 465     GLN S   807                                                      
REMARK 465     GLY S   808                                                      
REMARK 465     SER S   809                                                      
REMARK 465     ARG S   810                                                      
REMARK 465     ASN S   811                                                      
REMARK 465     GLN S   824                                                      
REMARK 465     VAL S   825                                                      
REMARK 465     ASN S   826                                                      
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     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  87    CG   OD1  ND2                                       
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 136    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 157    CD   CE   NZ                                        
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
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 347   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP S 823   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    PHE A 100       75.43   -100.76                                   
REMARK 500    ARG A 238      -10.72     79.28                                   
REMARK 500    ASN A 246       73.96   -153.19                                   
REMARK 500    TYR A 276       -8.71     73.68                                   
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                             FE2 A1350  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 104.0                                              
REMARK 620 3 HIS A 279   NE2  85.8  88.0                                        
REMARK 620 4 OGA A1351   O2  163.5  92.4  96.8                                  
REMARK 620 5 OGA A1351   O2'  86.4 168.8  97.0  77.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A 1351                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D7G   RELATED DB: PDB                                   
REMARK 900 A MODEL FOR THE COMPLEX BETWEEN THE HYPOXIA-INDUCIBLE FACTOR-1 (HIF- 
REMARK 900 1) AND ITS CONSENSUS DEOXYRIBONUCLEIC ACID SEQUENCE                  
REMARK 900 RELATED ID: 1H2L   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1H2M   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1H2N   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1L8C   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THECELLULAR       
REMARK 900 HYPOXIC RESPONSE                                                     
REMARK 900 RELATED ID: 1LM8   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A HIF-1A-PVHL-ELONGINB- ELONGINC COMPLEX                
REMARK 900 RELATED ID: 1LQB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1 ALPHA PEPTIDEBOUND TO THE  
REMARK 900 PVHL/ELONGIN-C/ ELONGIN-B COMPLEX                                    
DBREF  1H2K A    1   349  UNP    Q969Q7   Q969Q7           1    349             
DBREF  1H2K S  786   826  UNP    Q16665   HIFA_HUMAN     786    826             
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG          
SEQRES  13 A  349  LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN                  
SEQRES   1 S   41  SER MET ASP GLU SER GLY LEU PRO GLN LEU THR SER TYR          
SEQRES   2 S   41  ASP CYS GLU VAL ASN ALA PRO ILE GLN GLY SER ARG ASN          
SEQRES   3 S   41  LEU LEU GLN GLY GLU GLU LEU LEU ARG ALA LEU ASP GLN          
SEQRES   4 S   41  VAL ASN                                                      
HET    FE2  A1350       1                                                       
HET    OGA  A1351      10                                                       
HET    SO4  A1352       5                                                       
HET    SO4  A1353       5                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     OGA N-OXALYLGLYCINE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  FE2    FE 2+                                                        
FORMUL   4  OGA    C4 H5 N O5                                                   
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *194(H2 O)                                                    
HELIX    1   1 ASP A   28  LEU A   32  5                                   5    
HELIX    2   2 ASP A   49  ASN A   58  1                                  10    
HELIX    3   3 VAL A   70  TRP A   76  5                                   7    
HELIX    4   4 ASP A   77  ILE A   85  1                                   9    
HELIX    5   5 ASP A  104  GLN A  112  5                                   9    
HELIX    6   6 LYS A  124  ARG A  138  1                                  15    
HELIX    7   7 GLY A  155  GLY A  164  1                                  10    
HELIX    8   8 ASN A  166  GLY A  178  1                                  13    
HELIX    9   9 PRO A  220  ASP A  222  5                                   3    
HELIX   10  10 GLN A  223  TYR A  228  1                                   6    
HELIX   11  11 PHE A  252  VAL A  258  5                                   7    
HELIX   12  12 LYS A  311  GLY A  331  1                                  21    
HELIX   13  13 ASN A  332  GLN A  334  5                                   3    
HELIX   14  14 GLU A  335  LYS A  345  1                                  11    
HELIX   15  15 GLN S  814  ASP S  823  1                                  10    
SHEET    1  AA 5 THR A  39  PRO A  41  0                                        
SHEET    2  AA 5 GLY A 260  VAL A 265  1  O  GLY A 260   N  ARG A  40           
SHEET    3  AA 5 LYS A 214  PHE A 219 -1  O  LYS A 214   N  VAL A 265           
SHEET    4  AA 5 TRP A 278  SER A 283 -1  O  TRP A 278   N  PHE A 219           
SHEET    5  AA 5 VAL A 195  HIS A 199 -1  O  THR A 196   N  ILE A 281           
SHEET    1  AB 6 ARG A  44  LEU A  45  0                                        
SHEET    2  AB 6 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AB 6 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AB 6 GLN A 203  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AB 6 THR A 290  LYS A 298 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AB 6 LEU A 182  SER A 184 -1  N  THR A 183   O  TRP A 296           
SHEET    1  AC 9 ARG A  44  LEU A  45  0                                        
SHEET    2  AC 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AC 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AC 9 GLN A 203  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AC 9 THR A 290  LYS A 298 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AC 9 LEU A 186  GLY A 190 -1  O  LEU A 186   N  ASN A 294           
SHEET    7  AC 9 ARG A 143  THR A 149 -1  O  LEU A 146   N  ILE A 189           
SHEET    8  AC 9 PHE A  90  ALA A  95 -1  O  SER A  91   N  GLN A 147           
SHEET    9  AC 9 SER A 118  MET A 123 -1  O  ASN A 119   N  SER A  94           
LINK        FE   FE2 A1350                 NE2 HIS A 199     1555   1555  2.12  
LINK        FE   FE2 A1350                 OD2 ASP A 201     1555   1555  2.05  
LINK        FE   FE2 A1350                 NE2 HIS A 279     1555   1555  2.08  
LINK        FE   FE2 A1350                 O2  OGA A1351     1555   1555  2.13  
LINK        FE   FE2 A1350                 O2' OGA A1351     1555   1555  2.17  
CISPEP   1 TYR A  308    PRO A  309          0        -1.09                     
SITE     1 AC1  4 HIS A 199  ASP A 201  HIS A 279  OGA A1351                    
SITE     1 AC2  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC3  5 ARG A 143  GLU A 192  GLY A 193  LEU A 285                    
SITE     2 AC3  5 ASN A 286                                                     
SITE     1 AC4 12 TYR A 145  THR A 196  HIS A 199  ASP A 201                    
SITE     2 AC4 12 ASN A 205  PHE A 207  LYS A 214  HIS A 279                    
SITE     3 AC4 12 ILE A 281  ASN A 294  TRP A 296  FE2 A1350                    
CRYST1   86.161   86.161  146.656  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011606  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011606  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006819        0.00000                         
ATOM      1  N   GLU A  15       8.429  32.653   9.844  1.00 50.99           N  
ATOM      2  CA  GLU A  15       7.077  32.034   9.723  1.00 51.05           C  
ATOM      3  C   GLU A  15       7.166  30.582  10.163  1.00 50.79           C  
ATOM      4  O   GLU A  15       8.052  29.857   9.730  1.00 51.18           O  
ATOM      5  CB  GLU A  15       6.570  32.124   8.296  1.00 51.20           C  
ATOM      6  N   PRO A  16       6.254  30.150  11.022  1.00 50.50           N  
ATOM      7  CA  PRO A  16       6.301  28.781  11.549  1.00 50.12           C  
ATOM      8  C   PRO A  16       6.265  27.737  10.438  1.00 49.56           C  
ATOM      9  O   PRO A  16       5.471  27.827   9.503  1.00 49.32           O  
ATOM     10  CB  PRO A  16       5.049  28.701  12.429  1.00 50.27           C  
ATOM     11  CG  PRO A  16       4.734  30.135  12.770  1.00 50.58           C  
ATOM     12  CD  PRO A  16       5.108  30.911  11.548  1.00 50.56           C  
ATOM     13  N   ARG A  17       7.133  26.746  10.550  1.00 48.83           N  
ATOM     14  CA  ARG A  17       7.219  25.695   9.550  1.00 48.33           C  
ATOM     15  C   ARG A  17       5.967  24.832   9.561  1.00 47.48           C  
ATOM     16  O   ARG A  17       5.245  24.782  10.557  1.00 47.64           O  
ATOM     17  CB  ARG A  17       8.421  24.798   9.835  1.00 48.61           C  
ATOM     18  CG  ARG A  17       9.776  25.511   9.835  1.00 49.21           C  
ATOM     19  CD  ARG A  17      10.944  24.577  10.196  1.00 49.84           C  
ATOM     20  NE  ARG A  17      10.918  24.137  11.596  1.00 50.12           N  
ATOM     21  CZ  ARG A  17      11.455  24.809  12.623  1.00 50.99           C  
ATOM     22  NH1 ARG A  17      12.065  25.979  12.431  1.00 50.40           N  
ATOM     23  NH2 ARG A  17      11.381  24.310  13.857  1.00 50.81           N  
ATOM     24  N   GLU A  18       5.723  24.153   8.446  1.00 46.05           N  
ATOM     25  CA  GLU A  18       4.603  23.246   8.329  1.00 45.06           C  
ATOM     26  C   GLU A  18       5.096  21.830   8.607  1.00 44.00           C  
ATOM     27  O   GLU A  18       6.101  21.405   8.044  1.00 43.89           O  
ATOM     28  CB  GLU A  18       4.013  23.324   6.923  1.00 45.21           C  
ATOM     29  CG  GLU A  18       3.323  24.648   6.621  1.00 45.56           C  
ATOM     30  CD  GLU A  18       1.951  24.780   7.265  1.00 45.64           C  
ATOM     31  OE1 GLU A  18       1.342  23.749   7.641  1.00 44.14           O  
ATOM     32  OE2 GLU A  18       1.480  25.932   7.388  1.00 45.83           O  
ATOM     33  N   GLU A  19       4.396  21.113   9.484  1.00 42.49           N  
ATOM     34  CA  GLU A  19       4.734  19.728   9.795  1.00 41.55           C  
ATOM     35  C   GLU A  19       4.357  18.817   8.635  1.00 39.79           C  
ATOM     36  O   GLU A  19       3.266  18.933   8.066  1.00 39.13           O  
ATOM     37  CB  GLU A  19       4.010  19.256  11.052  1.00 41.88           C  
ATOM     38  CG  GLU A  19       4.420  19.997  12.311  1.00 44.80           C  
ATOM     39  CD  GLU A  19       4.276  19.155  13.574  1.00 49.28           C  
ATOM     40  OE1 GLU A  19       3.759  18.008  13.497  1.00 51.52           O  
ATOM     41  OE2 GLU A  19       4.695  19.643  14.656  1.00 52.76           O  
ATOM     42  N   ALA A  20       5.270  17.910   8.311  1.00 38.00           N  
ATOM     43  CA  ALA A  20       5.099  16.952   7.227  1.00 36.77           C  
ATOM     44  C   ALA A  20       3.803  16.168   7.373  1.00 35.56           C  
ATOM     45  O   ALA A  20       3.445  15.734   8.460  1.00 35.74           O  
ATOM     46  CB  ALA A  20       6.283  15.999   7.180  1.00 36.63           C  
ATOM     47  N   GLY A  21       3.082  16.020   6.279  1.00 34.05           N  
ATOM     48  CA  GLY A  21       1.860  15.242   6.307  1.00 33.24           C  
ATOM     49  C   GLY A  21       0.666  16.137   6.551  1.00 32.36           C  
ATOM     50  O   GLY A  21      -0.393  15.673   6.951  1.00 30.93           O  
ATOM     51  N   ALA A  22       0.867  17.432   6.323  1.00 32.41           N  
ATOM     52  CA  ALA A  22      -0.184  18.425   6.459  1.00 32.78           C  
ATOM     53  C   ALA A  22      -0.723  18.441   7.873  1.00 33.14           C  
ATOM     54  O   ALA A  22      -1.915  18.605   8.088  1.00 32.74           O  
ATOM     55  CB  ALA A  22      -1.304  18.139   5.462  1.00 32.61           C  
ATOM     56  N   LEU A  23       0.151  18.253   8.849  1.00 34.01           N  
ATOM     57  CA  LEU A  23      -0.297  18.275  10.232  1.00 34.91           C  
ATOM     58  C   LEU A  23      -0.342  19.694  10.757  1.00 35.27           C  
ATOM     59  O   LEU A  23      -0.528  19.918  11.943  1.00 35.72           O  
ATOM     60  CB  LEU A  23       0.565  17.366  11.097  1.00 35.27           C  
ATOM     61  CG  LEU A  23       0.384  15.910  10.653  1.00 36.36           C  
ATOM     62  CD1 LEU A  23       1.211  14.947  11.491  1.00 37.75           C  
ATOM     63  CD2 LEU A  23      -1.077  15.523  10.719  1.00 37.98           C  
ATOM     64  N   GLY A  24      -0.177  20.656   9.855  1.00 35.73           N  
ATOM     65  CA  GLY A  24      -0.332  22.053  10.194  1.00 35.66           C  
ATOM     66  C   GLY A  24       0.901  22.655  10.804  1.00 36.08           C  
ATOM     67  O   GLY A  24       1.945  22.001  10.913  1.00 36.05           O  
ATOM     68  N   PRO A  25       0.764  23.894  11.253  1.00 35.96           N  
ATOM     69  CA  PRO A  25       1.896  24.628  11.804  1.00 36.12           C  
ATOM     70  C   PRO A  25       2.327  23.980  13.108  1.00 36.32           C  
ATOM     71  O   PRO A  25       1.488  23.577  13.914  1.00 36.08           O  
ATOM     72  CB  PRO A  25       1.341  26.047  12.043  1.00 36.15           C  
ATOM     73  CG  PRO A  25      -0.162  25.942  11.982  1.00 35.84           C  
ATOM     74  CD  PRO A  25      -0.504  24.638  11.350  1.00 36.22           C  
ATOM     75  N   ALA A  26       3.632  23.848  13.285  1.00 36.64           N  
ATOM     76  CA  ALA A  26       4.178  23.274  14.499  1.00 37.19           C  
ATOM     77  C   ALA A  26       3.860  24.172  15.706  1.00 36.77           C  
ATOM     78  O   ALA A  26       3.595  23.678  16.808  1.00 37.19           O  
ATOM     79  CB  ALA A  26       5.672  23.099  14.347  1.00 37.52           C  
ATOM     80  N   TRP A  27       3.848  25.479  15.484  1.00 35.62           N  
ATOM     81  CA  TRP A  27       3.520  26.420  16.543  1.00 35.04           C  
ATOM     82  C   TRP A  27       3.029  27.729  15.933  1.00 34.20           C  
ATOM     83  O   TRP A  27       2.992  27.883  14.723  1.00 33.57           O  
ATOM     84  CB  TRP A  27       4.774  26.672  17.382  1.00 35.28           C  
ATOM     85  CG  TRP A  27       5.951  26.889  16.511  1.00 34.67           C  
ATOM     86  CD1 TRP A  27       6.761  25.930  15.955  1.00 35.52           C  
ATOM     87  CD2 TRP A  27       6.426  28.135  16.033  1.00 34.40           C  
ATOM     88  NE1 TRP A  27       7.723  26.522  15.172  1.00 35.09           N  
ATOM     89  CE2 TRP A  27       7.541  27.877  15.209  1.00 34.23           C  
ATOM     90  CE3 TRP A  27       6.038  29.452  16.232  1.00 34.31           C  
ATOM     91  CZ2 TRP A  27       8.255  28.879  14.592  1.00 35.79           C  
ATOM     92  CZ3 TRP A  27       6.750  30.442  15.629  1.00 36.35           C  
ATOM     93  CH2 TRP A  27       7.847  30.154  14.808  1.00 36.47           C  
ATOM     94  N   ASP A  28       2.638  28.672  16.766  1.00 33.77           N  
ATOM     95  CA  ASP A  28       2.259  29.970  16.249  1.00 33.48           C  
ATOM     96  C   ASP A  28       2.759  31.050  17.165  1.00 32.26           C  
ATOM     97  O   ASP A  28       3.210  30.791  18.276  1.00 32.05           O  
ATOM     98  CB  ASP A  28       0.749  30.080  16.037  1.00 34.30           C  
ATOM     99  CG  ASP A  28      -0.026  29.986  17.317  1.00 36.29           C  
ATOM    100  OD1 ASP A  28      -0.184  31.027  18.002  1.00 39.59           O  
ATOM    101  OD2 ASP A  28      -0.517  28.906  17.712  1.00 39.78           O  
ATOM    102  N   GLU A  29       2.691  32.268  16.654  1.00 31.30           N  
ATOM    103  CA  GLU A  29       3.181  33.465  17.326  1.00 30.15           C  
ATOM    104  C   GLU A  29       2.674  33.625  18.752  1.00 28.85           C  
ATOM    105  O   GLU A  29       3.407  34.036  19.621  1.00 28.58           O  
ATOM    106  CB  GLU A  29       2.791  34.682  16.503  1.00 30.32           C  
ATOM    107  N   SER A  30       1.414  33.313  18.992  1.00 27.95           N  
ATOM    108  CA  SER A  30       0.845  33.501  20.320  1.00 27.46           C  
ATOM    109  C   SER A  30       1.537  32.671  21.389  1.00 26.93           C  
ATOM    110  O   SER A  30       1.312  32.907  22.567  1.00 26.79           O  
ATOM    111  CB  SER A  30      -0.651  33.168  20.322  1.00 27.23           C  
ATOM    112  OG  SER A  30      -0.857  31.764  20.306  1.00 27.69           O  
ATOM    113  N   GLN A  31       2.360  31.703  20.984  1.00 26.55           N  
ATOM    114  CA  GLN A  31       3.071  30.837  21.926  1.00 26.63           C  
ATOM    115  C   GLN A  31       4.419  31.409  22.334  1.00 26.66           C  
ATOM    116  O   GLN A  31       5.078  30.855  23.205  1.00 26.45           O  
ATOM    117  CB  GLN A  31       3.282  29.426  21.349  1.00 26.41           C  
ATOM    118  CG  GLN A  31       1.998  28.637  21.131  1.00 26.28           C  
ATOM    119  CD  GLN A  31       2.245  27.287  20.489  1.00 26.25           C  
ATOM    120  OE1 GLN A  31       2.258  27.183  19.271  1.00 27.92           O  
ATOM    121  NE2 GLN A  31       2.465  26.258  21.305  1.00 24.36           N  
ATOM    122  N   LEU A  32       4.824  32.508  21.703  1.00 26.89           N  
ATOM    123  CA  LEU A  32       6.083  33.176  22.029  1.00 27.24           C  
ATOM    124  C   LEU A  32       5.852  34.321  23.006  1.00 26.92           C  
ATOM    125  O   LEU A  32       4.888  35.047  22.868  1.00 26.42           O  
ATOM    126  CB  LEU A  32       6.717  33.746  20.760  1.00 27.46           C  
ATOM    127  CG  LEU A  32       6.964  32.728  19.640  1.00 28.65           C  
ATOM    128  CD1 LEU A  32       7.630  33.391  18.452  1.00 29.44           C  
ATOM    129  CD2 LEU A  32       7.792  31.573  20.127  1.00 27.98           C  
ATOM    130  N   ARG A  33       6.728  34.472  23.995  1.00 26.71           N  
ATOM    131  CA  ARG A  33       6.627  35.596  24.923  1.00 26.77           C  
ATOM    132  C   ARG A  33       7.040  36.880  24.209  1.00 26.57           C  
ATOM    133  O   ARG A  33       7.719  36.844  23.203  1.00 26.30           O  
ATOM    134  CB  ARG A  33       7.492  35.357  26.163  1.00 26.67           C  
ATOM    135  CG  ARG A  33       7.052  34.141  26.983  1.00 26.29           C  
ATOM    136  CD  ARG A  33       7.937  33.837  28.181  1.00 25.85           C  
ATOM    137  NE  ARG A  33       7.381  32.778  29.018  1.00 25.80           N  
ATOM    138  CZ  ARG A  33       6.451  32.946  29.945  1.00 24.68           C  
ATOM    139  NH1 ARG A  33       5.937  34.140  30.189  1.00 23.50           N  
ATOM    140  NH2 ARG A  33       6.029  31.901  30.637  1.00 25.35           N  
ATOM    141  N   SER A  34       6.633  38.020  24.732  1.00 26.80           N  
ATOM    142  CA  SER A  34       6.903  39.280  24.061  1.00 27.15           C  
ATOM    143  C   SER A  34       7.990  40.048  24.791  1.00 26.39           C  
ATOM    144  O   SER A  34       7.964  40.140  26.005  1.00 25.87           O  
ATOM    145  CB  SER A  34       5.628  40.104  24.030  1.00 27.68           C  
ATOM    146  OG  SER A  34       5.494  40.737  25.285  1.00 32.47           O  
ATOM    147  N   TYR A  35       8.944  40.589  24.042  1.00 25.89           N  
ATOM    148  CA  TYR A  35      10.110  41.223  24.637  1.00 26.28           C  
ATOM    149  C   TYR A  35      10.353  42.558  23.970  1.00 26.85           C  
ATOM    150  O   TYR A  35       9.722  42.856  22.967  1.00 26.92           O  
ATOM    151  CB  TYR A  35      11.326  40.308  24.510  1.00 25.90           C  
ATOM    152  CG  TYR A  35      11.169  39.032  25.309  1.00 25.33           C  
ATOM    153  CD1 TYR A  35      10.975  39.073  26.685  1.00 24.99           C  
ATOM    154  CD2 TYR A  35      11.198  37.787  24.692  1.00 23.82           C  
ATOM    155  CE1 TYR A  35      10.823  37.898  27.429  1.00 24.56           C  
ATOM    156  CE2 TYR A  35      11.046  36.620  25.426  1.00 24.42           C  
ATOM    157  CZ  TYR A  35      10.862  36.682  26.793  1.00 23.48           C  
ATOM    158  OH  TYR A  35      10.696  35.524  27.513  1.00 24.75           O  
ATOM    159  N   SER A  36      11.304  43.327  24.496  1.00 27.27           N  
ATOM    160  CA  SER A  36      11.525  44.704  24.052  1.00 27.55           C  
ATOM    161  C   SER A  36      12.513  44.912  22.917  1.00 27.06           C  
ATOM    162  O   SER A  36      12.734  46.049  22.504  1.00 27.94           O  
ATOM    163  CB  SER A  36      12.082  45.498  25.226  1.00 27.88           C  
ATOM    164  OG  SER A  36      13.350  44.976  25.590  1.00 28.36           O  
ATOM    165  N   PHE A  37      13.128  43.851  22.429  1.00 25.35           N  
ATOM    166  CA  PHE A  37      14.202  44.014  21.461  1.00 24.62           C  
ATOM    167  C   PHE A  37      13.899  43.272  20.159  1.00 24.75           C  
ATOM    168  O   PHE A  37      13.130  42.335  20.135  1.00 24.25           O  
ATOM    169  CB  PHE A  37      15.487  43.462  22.071  1.00 23.87           C  
ATOM    170  CG  PHE A  37      15.318  42.069  22.635  1.00 22.53           C  
ATOM    171  CD1 PHE A  37      15.348  40.972  21.802  1.00 21.11           C  
ATOM    172  CD2 PHE A  37      15.069  41.872  23.988  1.00 21.63           C  
ATOM    173  CE1 PHE A  37      15.158  39.687  22.314  1.00 22.41           C  
ATOM    174  CE2 PHE A  37      14.900  40.612  24.505  1.00 22.29           C  
ATOM    175  CZ  PHE A  37      14.936  39.509  23.675  1.00 21.45           C  
ATOM    176  N   PRO A  38      14.489  43.715  19.067  1.00 24.94           N  
ATOM    177  CA  PRO A  38      14.322  43.017  17.793  1.00 24.67           C  
ATOM    178  C   PRO A  38      15.267  41.823  17.678  1.00 24.41           C  
ATOM    179  O   PRO A  38      16.249  41.745  18.427  1.00 23.73           O  
ATOM    180  CB  PRO A  38      14.725  44.072  16.783  1.00 24.75           C  
ATOM    181  CG  PRO A  38      15.791  44.872  17.530  1.00 26.09           C  
ATOM    182  CD  PRO A  38      15.287  44.950  18.941  1.00 25.27           C  
ATOM    183  N   THR A  39      14.981  40.927  16.734  1.00 23.30           N  
ATOM    184  CA  THR A  39      15.859  39.816  16.444  1.00 23.42           C  
ATOM    185  C   THR A  39      15.857  39.534  14.955  1.00 24.29           C  
ATOM    186  O   THR A  39      14.958  39.964  14.239  1.00 24.61           O  
ATOM    187  CB  THR A  39      15.368  38.538  17.135  1.00 23.09           C  
ATOM    188  OG1 THR A  39      14.044  38.232  16.680  1.00 19.92           O  
ATOM    189  CG2 THR A  39      15.213  38.731  18.641  1.00 23.03           C  
ATOM    190  N   ARG A  40      16.854  38.773  14.525  1.00 24.43           N  
ATOM    191  CA  ARG A  40      16.982  38.273  13.170  1.00 24.91           C  
ATOM    192  C   ARG A  40      17.061  36.751  13.268  1.00 24.49           C  
ATOM    193  O   ARG A  40      17.434  36.225  14.301  1.00 23.58           O  
ATOM    194  CB  ARG A  40      18.253  38.805  12.536  1.00 25.36           C  
ATOM    195  CG  ARG A  40      18.208  40.281  12.248  1.00 30.74           C  
ATOM    196  CD  ARG A  40      16.823  40.775  11.890  1.00 34.86           C  
ATOM    197  NE  ARG A  40      16.604  40.989  10.477  1.00 39.38           N  
ATOM    198  CZ  ARG A  40      15.403  41.229   9.971  1.00 43.86           C  
ATOM    199  NH1 ARG A  40      14.345  41.254  10.782  1.00 45.88           N  
ATOM    200  NH2 ARG A  40      15.252  41.457   8.674  1.00 44.96           N  
ATOM    201  N   PRO A  41      16.687  36.031  12.221  1.00 25.08           N  
ATOM    202  CA  PRO A  41      16.715  34.565  12.290  1.00 25.39           C  
ATOM    203  C   PRO A  41      18.095  33.913  12.282  1.00 25.10           C  
ATOM    204  O   PRO A  41      19.007  34.370  11.636  1.00 25.16           O  
ATOM    205  CB  PRO A  41      15.953  34.130  11.023  1.00 25.76           C  
ATOM    206  CG  PRO A  41      15.286  35.392  10.504  1.00 26.54           C  
ATOM    207  CD  PRO A  41      16.151  36.524  10.939  1.00 24.85           C  
ATOM    208  N   ILE A  42      18.225  32.823  13.020  1.00 25.28           N  
ATOM    209  CA  ILE A  42      19.388  31.974  12.919  1.00 24.31           C  
ATOM    210  C   ILE A  42      19.147  31.116  11.677  1.00 24.68           C  
ATOM    211  O   ILE A  42      18.043  30.614  11.466  1.00 24.72           O  
ATOM    212  CB  ILE A  42      19.481  31.104  14.163  1.00 24.80           C  
ATOM    213  CG1 ILE A  42      19.763  31.993  15.384  1.00 24.24           C  
ATOM    214  CG2 ILE A  42      20.530  30.004  13.961  1.00 23.81           C  
ATOM    215  CD1 ILE A  42      19.531  31.325  16.729  1.00 23.59           C  
ATOM    216  N   PRO A  43      20.146  30.953  10.826  1.00 24.48           N  
ATOM    217  CA  PRO A  43      19.963  30.108   9.651  1.00 24.60           C  
ATOM    218  C   PRO A  43      19.611  28.650  10.001  1.00 24.85           C  
ATOM    219  O   PRO A  43      20.148  28.130  10.989  1.00 24.38           O  
ATOM    220  CB  PRO A  43      21.320  30.192   8.937  1.00 24.87           C  
ATOM    221  CG  PRO A  43      22.040  31.372   9.541  1.00 25.04           C  
ATOM    222  CD  PRO A  43      21.475  31.583  10.886  1.00 24.37           C  
ATOM    223  N   ARG A  44      18.686  28.032   9.248  1.00 24.70           N  
ATOM    224  CA  ARG A  44      18.367  26.608   9.391  1.00 25.53           C  
ATOM    225  C   ARG A  44      18.910  25.943   8.152  1.00 25.00           C  
ATOM    226  O   ARG A  44      18.505  26.265   7.030  1.00 24.62           O  
ATOM    227  CB  ARG A  44      16.873  26.287   9.452  1.00 26.51           C  
ATOM    228  CG  ARG A  44      16.044  27.133  10.378  1.00 29.49           C  
ATOM    229  CD  ARG A  44      14.683  26.485  10.813  1.00 31.03           C  
ATOM    230  NE  ARG A  44      14.401  25.120  10.323  1.00 32.36           N  
ATOM    231  CZ  ARG A  44      14.174  24.057  11.126  1.00 33.85           C  
ATOM    232  NH1 ARG A  44      14.239  24.170  12.451  1.00 30.71           N  
ATOM    233  NH2 ARG A  44      13.898  22.863  10.613  1.00 35.56           N  
ATOM    234  N   LEU A  45      19.815  25.006   8.337  1.00 23.91           N  
ATOM    235  CA  LEU A  45      20.500  24.444   7.202  1.00 23.40           C  
ATOM    236  C   LEU A  45      20.684  22.967   7.352  1.00 23.52           C  
ATOM    237  O   LEU A  45      20.559  22.423   8.446  1.00 22.50           O  
ATOM    238  CB  LEU A  45      21.888  25.064   7.093  1.00 22.62           C  
ATOM    239  CG  LEU A  45      21.911  26.563   6.819  1.00 23.96           C  
ATOM    240  CD1 LEU A  45      23.317  27.111   6.947  1.00 24.52           C  
ATOM    241  CD2 LEU A  45      21.366  26.845   5.423  1.00 24.63           C  
ATOM    242  N   SER A  46      21.018  22.347   6.227  1.00 23.57           N  
ATOM    243  CA  SER A  46      21.382  20.975   6.221  1.00 24.12           C  
ATOM    244  C   SER A  46      22.820  20.888   6.668  1.00 24.81           C  
ATOM    245  O   SER A  46      23.640  21.757   6.398  1.00 23.76           O  
ATOM    246  CB  SER A  46      21.236  20.354   4.830  1.00 23.80           C  
ATOM    247  OG  SER A  46      21.744  19.020   4.830  1.00 24.09           O  
ATOM    248  N   GLN A  47      23.089  19.804   7.366  1.00 25.92           N  
ATOM    249  CA  GLN A  47      24.399  19.444   7.844  1.00 27.25           C  
ATOM    250  C   GLN A  47      25.379  19.326   6.674  1.00 27.54           C  
ATOM    251  O   GLN A  47      26.563  19.564   6.836  1.00 27.97           O  
ATOM    252  CB  GLN A  47      24.245  18.088   8.554  1.00 28.46           C  
ATOM    253  CG  GLN A  47      25.487  17.279   8.705  1.00 31.10           C  
ATOM    254  CD  GLN A  47      25.776  16.372   7.570  1.00 33.17           C  
ATOM    255  OE1 GLN A  47      24.881  15.970   6.803  1.00 36.23           O  
ATOM    256  NE2 GLN A  47      27.041  16.000   7.458  1.00 36.17           N  
ATOM    257  N   SER A  48      24.884  18.951   5.498  1.00 27.72           N  
ATOM    258  CA  SER A  48      25.736  18.809   4.323  1.00 28.35           C  
ATOM    259  C   SER A  48      26.016  20.150   3.629  1.00 28.86           C  
ATOM    260  O   SER A  48      26.825  20.235   2.711  1.00 28.96           O  
ATOM    261  CB  SER A  48      25.092  17.839   3.324  1.00 28.65           C  
ATOM    262  OG  SER A  48      23.798  18.276   2.918  1.00 28.51           O  
ATOM    263  N   ASP A  49      25.347  21.203   4.065  1.00 29.16           N  
ATOM    264  CA  ASP A  49      25.515  22.496   3.442  1.00 29.28           C  
ATOM    265  C   ASP A  49      26.800  23.163   3.913  1.00 29.71           C  
ATOM    266  O   ASP A  49      26.981  23.398   5.101  1.00 29.02           O  
ATOM    267  CB  ASP A  49      24.325  23.369   3.783  1.00 29.35           C  
ATOM    268  CG  ASP A  49      24.316  24.667   3.010  1.00 29.93           C  
ATOM    269  OD1 ASP A  49      25.398  25.183   2.666  1.00 28.14           O  
ATOM    270  OD2 ASP A  49      23.259  25.247   2.731  1.00 30.49           O  
ATOM    271  N   PRO A  50      27.693  23.483   2.976  1.00 30.34           N  
ATOM    272  CA  PRO A  50      28.964  24.134   3.315  1.00 30.54           C  
ATOM    273  C   PRO A  50      28.783  25.354   4.186  1.00 30.38           C  
ATOM    274  O   PRO A  50      29.661  25.651   4.990  1.00 30.53           O  
ATOM    275  CB  PRO A  50      29.520  24.573   1.952  1.00 30.39           C  
ATOM    276  CG  PRO A  50      28.926  23.667   0.988  1.00 30.96           C  
ATOM    277  CD  PRO A  50      27.574  23.243   1.531  1.00 30.51           C  
ATOM    278  N   ARG A  51      27.683  26.072   4.008  1.00 30.50           N  
ATOM    279  CA  ARG A  51      27.439  27.253   4.817  1.00 30.94           C  
ATOM    280  C   ARG A  51      27.341  26.875   6.299  1.00 30.49           C  
ATOM    281  O   ARG A  51      27.744  27.646   7.161  1.00 29.74           O  
ATOM    282  CB  ARG A  51      26.171  27.979   4.370  1.00 30.97           C  
ATOM    283  CG  ARG A  51      26.337  28.781   3.099  1.00 33.47           C  
ATOM    284  CD  ARG A  51      25.029  29.321   2.521  1.00 34.80           C  
ATOM    285  NE  ARG A  51      24.071  28.252   2.221  1.00 36.68           N  
ATOM    286  CZ  ARG A  51      22.766  28.448   2.081  1.00 37.94           C  
ATOM    287  NH1 ARG A  51      22.260  29.677   2.208  1.00 39.10           N  
ATOM    288  NH2 ARG A  51      21.967  27.436   1.794  1.00 36.51           N  
ATOM    289  N   ALA A  52      26.831  25.684   6.596  1.00 30.03           N  
ATOM    290  CA  ALA A  52      26.697  25.288   7.993  1.00 29.96           C  
ATOM    291  C   ALA A  52      28.079  25.101   8.593  1.00 30.07           C  
ATOM    292  O   ALA A  52      28.345  25.518   9.710  1.00 29.00           O  
ATOM    293  CB  ALA A  52      25.901  24.028   8.119  1.00 29.81           C  
ATOM    294  N   GLU A  53      28.958  24.455   7.845  1.00 30.12           N  
ATOM    295  CA  GLU A  53      30.290  24.213   8.347  1.00 31.08           C  
ATOM    296  C   GLU A  53      30.999  25.550   8.579  1.00 30.37           C  
ATOM    297  O   GLU A  53      31.683  25.730   9.580  1.00 29.89           O  
ATOM    298  CB  GLU A  53      31.086  23.362   7.379  1.00 31.41           C  
ATOM    299  CG  GLU A  53      32.189  22.603   8.081  1.00 35.02           C  
ATOM    300  CD  GLU A  53      31.785  21.185   8.507  1.00 37.87           C  
ATOM    301  OE1 GLU A  53      30.614  20.929   8.887  1.00 39.16           O  
ATOM    302  OE2 GLU A  53      32.674  20.313   8.463  1.00 40.43           O  
ATOM    303  N   GLU A  54      30.811  26.479   7.652  1.00 29.84           N  
ATOM    304  CA  GLU A  54      31.413  27.796   7.757  1.00 30.22           C  
ATOM    305  C   GLU A  54      30.975  28.486   9.045  1.00 29.05           C  
ATOM    306  O   GLU A  54      31.780  29.102   9.719  1.00 28.03           O  
ATOM    307  CB  GLU A  54      31.026  28.680   6.573  1.00 30.53           C  
ATOM    308  CG  GLU A  54      31.635  28.276   5.243  1.00 34.66           C  
ATOM    309  CD  GLU A  54      30.993  29.002   4.058  1.00 38.49           C  
ATOM    310  OE1 GLU A  54      30.651  30.208   4.214  1.00 42.20           O  
ATOM    311  OE2 GLU A  54      30.829  28.368   2.975  1.00 41.54           O  
ATOM    312  N   LEU A  55      29.696  28.366   9.387  1.00 28.24           N  
ATOM    313  CA  LEU A  55      29.177  29.029  10.571  1.00 27.28           C  
ATOM    314  C   LEU A  55      29.774  28.448  11.827  1.00 26.43           C  
ATOM    315  O   LEU A  55      30.212  29.199  12.695  1.00 25.20           O  
ATOM    316  CB  LEU A  55      27.655  28.975  10.597  1.00 27.25           C  
ATOM    317  CG  LEU A  55      27.027  29.829   9.502  1.00 27.43           C  
ATOM    318  CD1 LEU A  55      25.568  29.452   9.322  1.00 28.83           C  
ATOM    319  CD2 LEU A  55      27.173  31.318   9.821  1.00 26.98           C  
ATOM    320  N   ILE A  56      29.829  27.116  11.915  1.00 25.75           N  
ATOM    321  CA  ILE A  56      30.382  26.473  13.107  1.00 25.50           C  
ATOM    322  C   ILE A  56      31.874  26.815  13.254  1.00 26.26           C  
ATOM    323  O   ILE A  56      32.346  27.134  14.349  1.00 25.55           O  
ATOM    324  CB  ILE A  56      30.192  24.955  13.059  1.00 25.63           C  
ATOM    325  CG1 ILE A  56      28.698  24.574  13.034  1.00 24.00           C  
ATOM    326  CG2 ILE A  56      30.848  24.321  14.263  1.00 25.48           C  
ATOM    327  CD1 ILE A  56      28.439  23.170  12.531  1.00 24.10           C  
ATOM    328  N   GLU A  57      32.597  26.781  12.135  1.00 27.04           N  
ATOM    329  CA  GLU A  57      34.023  27.082  12.107  1.00 28.01           C  
ATOM    330  C   GLU A  57      34.232  28.491  12.625  1.00 28.49           C  
ATOM    331  O   GLU A  57      35.183  28.770  13.344  1.00 28.92           O  
ATOM    332  CB  GLU A  57      34.561  26.977  10.676  1.00 28.61           C  
ATOM    333  CG  GLU A  57      36.053  27.224  10.509  1.00 30.77           C  
ATOM    334  CD  GLU A  57      36.902  26.322  11.394  1.00 35.15           C  
ATOM    335  OE1 GLU A  57      36.556  25.127  11.591  1.00 37.11           O  
ATOM    336  OE2 GLU A  57      37.924  26.818  11.909  1.00 40.88           O  
ATOM    337  N   ASN A  58      33.321  29.378  12.270  1.00 28.34           N  
ATOM    338  CA  ASN A  58      33.424  30.758  12.701  1.00 28.81           C  
ATOM    339  C   ASN A  58      32.770  31.079  14.025  1.00 27.23           C  
ATOM    340  O   ASN A  58      32.630  32.233  14.374  1.00 26.07           O  
ATOM    341  CB  ASN A  58      32.792  31.641  11.656  1.00 29.66           C  
ATOM    342  CG  ASN A  58      33.789  32.386  10.913  1.00 33.61           C  
ATOM    343  OD1 ASN A  58      34.280  31.901   9.893  1.00 38.81           O  
ATOM    344  ND2 ASN A  58      34.160  33.582  11.429  1.00 36.72           N  
ATOM    345  N   GLU A  59      32.343  30.053  14.735  1.00 26.39           N  
ATOM    346  CA  GLU A  59      31.712  30.241  16.030  1.00 26.36           C  
ATOM    347  C   GLU A  59      30.495  31.144  15.926  1.00 25.39           C  
ATOM    348  O   GLU A  59      30.325  32.100  16.668  1.00 24.14           O  
ATOM    349  CB  GLU A  59      32.753  30.697  17.059  1.00 26.80           C  
ATOM    350  CG  GLU A  59      33.717  29.537  17.316  1.00 29.10           C  
ATOM    351  CD  GLU A  59      34.722  29.791  18.407  1.00 32.85           C  
ATOM    352  OE1 GLU A  59      35.790  30.330  18.080  1.00 37.47           O  
ATOM    353  OE2 GLU A  59      34.466  29.432  19.572  1.00 34.14           O  
ATOM    354  N   GLU A  60      29.641  30.799  14.970  1.00 24.88           N  
ATOM    355  CA  GLU A  60      28.366  31.465  14.801  1.00 25.20           C  
ATOM    356  C   GLU A  60      27.262  30.414  14.822  1.00 24.07           C  
ATOM    357  O   GLU A  60      27.420  29.320  14.293  1.00 22.49           O  
ATOM    358  CB  GLU A  60      28.343  32.249  13.505  1.00 25.69           C  
ATOM    359  CG  GLU A  60      29.354  33.363  13.536  1.00 30.40           C  
ATOM    360  CD  GLU A  60      28.962  34.516  12.657  1.00 37.91           C  
ATOM    361  OE1 GLU A  60      29.009  34.377  11.414  1.00 38.24           O  
ATOM    362  OE2 GLU A  60      28.595  35.566  13.236  1.00 46.50           O  
ATOM    363  N   PRO A  61      26.124  30.779  15.386  1.00 22.90           N  
ATOM    364  CA  PRO A  61      25.045  29.816  15.571  1.00 22.19           C  
ATOM    365  C   PRO A  61      24.448  29.371  14.267  1.00 21.47           C  
ATOM    366  O   PRO A  61      24.419  30.104  13.266  1.00 20.48           O  
ATOM    367  CB  PRO A  61      23.996  30.583  16.368  1.00 22.29           C  
ATOM    368  CG  PRO A  61      24.315  32.053  16.148  1.00 22.67           C  
ATOM    369  CD  PRO A  61      25.764  32.140  15.798  1.00 22.92           C  
ATOM    370  N   VAL A  62      23.957  28.142  14.283  1.00 20.87           N  
ATOM    371  CA  VAL A  62      23.248  27.591  13.146  1.00 20.94           C  
ATOM    372  C   VAL A  62      22.353  26.475  13.655  1.00 21.15           C  
ATOM    373  O   VAL A  62      22.714  25.761  14.605  1.00 21.21           O  
ATOM    374  CB  VAL A  62      24.214  27.052  12.073  1.00 21.30           C  
ATOM    375  CG1 VAL A  62      25.061  25.912  12.608  1.00 22.10           C  
ATOM    376  CG2 VAL A  62      23.440  26.587  10.825  1.00 21.19           C  
ATOM    377  N   VAL A  63      21.158  26.366  13.084  1.00 21.48           N  
ATOM    378  CA  VAL A  63      20.302  25.231  13.374  1.00 21.87           C  
ATOM    379  C   VAL A  63      20.526  24.212  12.270  1.00 22.00           C  
ATOM    380  O   VAL A  63      20.366  24.528  11.109  1.00 22.54           O  
ATOM    381  CB  VAL A  63      18.793  25.574  13.421  1.00 22.02           C  
ATOM    382  CG1 VAL A  63      17.955  24.277  13.612  1.00 21.90           C  
ATOM    383  CG2 VAL A  63      18.494  26.522  14.546  1.00 21.22           C  
ATOM    384  N   LEU A  64      20.911  23.002  12.643  1.00 22.48           N  
ATOM    385  CA  LEU A  64      21.067  21.902  11.710  1.00 23.08           C  
ATOM    386  C   LEU A  64      19.826  21.014  11.775  1.00 22.19           C  
ATOM    387  O   LEU A  64      19.423  20.558  12.843  1.00 21.85           O  
ATOM    388  CB  LEU A  64      22.327  21.107  12.032  1.00 24.00           C  
ATOM    389  CG  LEU A  64      23.614  21.930  11.984  1.00 27.02           C  
ATOM    390  CD1 LEU A  64      24.791  21.080  12.303  1.00 31.61           C  
ATOM    391  CD2 LEU A  64      23.827  22.540  10.640  1.00 29.86           C  
ATOM    392  N   THR A  65      19.222  20.757  10.628  1.00 21.50           N  
ATOM    393  CA  THR A  65      17.943  20.056  10.613  1.00 21.95           C  
ATOM    394  C   THR A  65      18.022  18.561  10.389  1.00 21.35           C  
ATOM    395  O   THR A  65      17.028  17.870  10.581  1.00 21.37           O  
ATOM    396  CB  THR A  65      17.062  20.592   9.478  1.00 22.08           C  
ATOM    397  OG1 THR A  65      17.725  20.351   8.230  1.00 22.38           O  
ATOM    398  CG2 THR A  65      16.919  22.099   9.553  1.00 24.00           C  
ATOM    399  N   ASP A  66      19.168  18.062   9.961  1.00 21.50           N  
ATOM    400  CA  ASP A  66      19.259  16.650   9.604  1.00 21.86           C  
ATOM    401  C   ASP A  66      20.513  15.899  10.069  1.00 21.61           C  
ATOM    402  O   ASP A  66      21.070  15.088   9.316  1.00 21.82           O  
ATOM    403  CB  ASP A  66      19.152  16.553   8.084  1.00 22.20           C  
ATOM    404  CG  ASP A  66      20.199  17.355   7.390  1.00 21.49           C  
ATOM    405  OD1 ASP A  66      21.065  17.936   8.070  1.00 21.14           O  
ATOM    406  OD2 ASP A  66      20.240  17.477   6.159  1.00 25.40           O  
ATOM    407  N   THR A  67      20.967  16.158  11.287  1.00 21.05           N  
ATOM    408  CA  THR A  67      22.154  15.491  11.768  1.00 20.85           C  
ATOM    409  C   THR A  67      21.858  14.084  12.231  1.00 20.12           C  
ATOM    410  O   THR A  67      22.757  13.281  12.283  1.00 20.45           O  
ATOM    411  CB  THR A  67      22.747  16.207  12.977  1.00 20.77           C  
ATOM    412  OG1 THR A  67      21.782  16.210  14.039  1.00 20.61           O  
ATOM    413  CG2 THR A  67      23.054  17.671  12.682  1.00 22.44           C  
ATOM    414  N   ASN A  68      20.614  13.815  12.618  1.00 19.51           N  
ATOM    415  CA  ASN A  68      20.269  12.555  13.267  1.00 19.09           C  
ATOM    416  C   ASN A  68      21.116  12.349  14.517  1.00 18.40           C  
ATOM    417  O   ASN A  68      21.383  11.212  14.928  1.00 17.67           O  
ATOM    418  CB  ASN A  68      20.455  11.362  12.325  1.00 19.63           C  
ATOM    419  CG  ASN A  68      19.453  11.344  11.209  1.00 19.93           C  
ATOM    420  OD1 ASN A  68      18.253  11.236  11.442  1.00 19.76           O  
ATOM    421  ND2 ASN A  68      19.941  11.423   9.987  1.00 19.96           N  
ATOM    422  N   LEU A  69      21.532  13.448  15.134  1.00 18.28           N  
ATOM    423  CA  LEU A  69      22.378  13.382  16.326  1.00 17.98           C  
ATOM    424  C   LEU A  69      21.773  12.542  17.447  1.00 17.59           C  
ATOM    425  O   LEU A  69      22.478  11.725  18.039  1.00 17.61           O  
ATOM    426  CB  LEU A  69      22.693  14.772  16.844  1.00 18.38           C  
ATOM    427  CG  LEU A  69      23.636  14.859  18.035  1.00 18.31           C  
ATOM    428  CD1 LEU A  69      24.936  14.144  17.744  1.00 20.68           C  
ATOM    429  CD2 LEU A  69      23.907  16.299  18.399  1.00 19.25           C  
ATOM    430  N   VAL A  70      20.489  12.741  17.740  1.00 17.27           N  
ATOM    431  CA  VAL A  70      19.811  11.989  18.794  1.00 17.72           C  
ATOM    432  C   VAL A  70      18.588  11.253  18.257  1.00 18.11           C  
ATOM    433  O   VAL A  70      17.557  11.148  18.927  1.00 17.23           O  
ATOM    434  CB  VAL A  70      19.395  12.866  19.999  1.00 17.54           C  
ATOM    435  CG1 VAL A  70      20.624  13.402  20.704  1.00 19.07           C  
ATOM    436  CG2 VAL A  70      18.451  13.994  19.599  1.00 17.50           C  
ATOM    437  N   TYR A  71      18.715  10.764  17.028  1.00 19.22           N  
ATOM    438  CA  TYR A  71      17.615  10.071  16.367  1.00 19.79           C  
ATOM    439  C   TYR A  71      16.934   9.072  17.306  1.00 19.62           C  
ATOM    440  O   TYR A  71      15.726   9.120  17.457  1.00 18.64           O  
ATOM    441  CB  TYR A  71      18.082   9.406  15.055  1.00 20.19           C  
ATOM    442  CG  TYR A  71      17.156   8.320  14.554  1.00 22.29           C  
ATOM    443  CD1 TYR A  71      15.938   8.619  13.948  1.00 25.33           C  
ATOM    444  CD2 TYR A  71      17.503   6.986  14.691  1.00 23.31           C  
ATOM    445  CE1 TYR A  71      15.080   7.555  13.480  1.00 24.74           C  
ATOM    446  CE2 TYR A  71      16.684   5.968  14.252  1.00 23.57           C  
ATOM    447  CZ  TYR A  71      15.479   6.244  13.650  1.00 24.07           C  
ATOM    448  OH  TYR A  71      14.686   5.159  13.266  1.00 27.86           O  
ATOM    449  N   PRO A  72      17.688   8.200  17.960  1.00 20.27           N  
ATOM    450  CA  PRO A  72      17.074   7.196  18.840  1.00 21.30           C  
ATOM    451  C   PRO A  72      16.307   7.794  20.008  1.00 21.82           C  
ATOM    452  O   PRO A  72      15.463   7.120  20.535  1.00 21.13           O  
ATOM    453  CB  PRO A  72      18.267   6.377  19.351  1.00 21.33           C  
ATOM    454  CG  PRO A  72      19.362   6.650  18.386  1.00 21.75           C  
ATOM    455  CD  PRO A  72      19.151   8.065  17.905  1.00 20.71           C  
ATOM    456  N   ALA A  73      16.588   9.038  20.391  1.00 22.47           N  
ATOM    457  CA  ALA A  73      15.892   9.658  21.522  1.00 23.20           C  
ATOM    458  C   ALA A  73      14.567  10.293  21.103  1.00 23.47           C  
ATOM    459  O   ALA A  73      13.801  10.765  21.938  1.00 23.46           O  
ATOM    460  CB  ALA A  73      16.783  10.718  22.173  1.00 23.27           C  
ATOM    461  N   LEU A  74      14.297  10.322  19.808  1.00 23.79           N  
ATOM    462  CA  LEU A  74      13.086  10.967  19.329  1.00 24.10           C  
ATOM    463  C   LEU A  74      11.797  10.301  19.801  1.00 24.55           C  
ATOM    464  O   LEU A  74      10.732  10.903  19.746  1.00 23.83           O  
ATOM    465  CB  LEU A  74      13.114  11.076  17.810  1.00 24.16           C  
ATOM    466  CG  LEU A  74      14.185  12.061  17.296  1.00 24.67           C  
ATOM    467  CD1 LEU A  74      13.988  12.320  15.820  1.00 26.73           C  
ATOM    468  CD2 LEU A  74      14.225  13.371  18.077  1.00 23.39           C  
ATOM    469  N   LYS A  75      11.897   9.053  20.244  1.00 24.97           N  
ATOM    470  CA  LYS A  75      10.741   8.317  20.738  1.00 25.16           C  
ATOM    471  C   LYS A  75      10.589   8.519  22.245  1.00 25.37           C  
ATOM    472  O   LYS A  75       9.612   8.082  22.822  1.00 25.23           O  
ATOM    473  CB  LYS A  75      10.885   6.819  20.428  1.00 25.16           C  
ATOM    474  CG  LYS A  75      12.079   6.163  21.097  1.00 25.17           C  
ATOM    475  CD  LYS A  75      12.178   4.653  20.765  1.00 27.19           C  
ATOM    476  CE  LYS A  75      13.646   4.220  20.609  1.00 26.95           C  
ATOM    477  NZ  LYS A  75      14.348   4.123  21.868  1.00 26.22           N  
ATOM    478  N   TRP A  76      11.552   9.179  22.882  1.00 25.25           N  
ATOM    479  CA  TRP A  76      11.486   9.389  24.319  1.00 25.56           C  
ATOM    480  C   TRP A  76      10.268  10.201  24.749  1.00 26.35           C  
ATOM    481  O   TRP A  76       9.920  11.198  24.130  1.00 26.71           O  
ATOM    482  CB  TRP A  76      12.719  10.139  24.816  1.00 25.19           C  
ATOM    483  CG  TRP A  76      13.975   9.338  24.816  1.00 24.32           C  
ATOM    484  CD1 TRP A  76      14.129   8.059  24.393  1.00 22.72           C  
ATOM    485  CD2 TRP A  76      15.258   9.762  25.271  1.00 22.34           C  
ATOM    486  NE1 TRP A  76      15.431   7.658  24.552  1.00 20.61           N  
ATOM    487  CE2 TRP A  76      16.145   8.685  25.096  1.00 20.28           C  
ATOM    488  CE3 TRP A  76      15.750  10.944  25.817  1.00 22.65           C  
ATOM    489  CZ2 TRP A  76      17.481   8.756  25.437  1.00 20.18           C  
ATOM    490  CZ3 TRP A  76      17.088  11.012  26.163  1.00 21.43           C  
ATOM    491  CH2 TRP A  76      17.932   9.934  25.970  1.00 21.94           C  
ATOM    492  N   ASP A  77       9.643   9.772  25.836  1.00 26.46           N  
ATOM    493  CA  ASP A  77       8.583  10.530  26.467  1.00 26.47           C  
ATOM    494  C   ASP A  77       8.618  10.116  27.931  1.00 26.16           C  
ATOM    495  O   ASP A  77       9.405   9.264  28.291  1.00 26.44           O  
ATOM    496  CB  ASP A  77       7.230  10.276  25.810  1.00 26.51           C  
ATOM    497  CG  ASP A  77       6.795   8.835  25.885  1.00 27.32           C  
ATOM    498  OD1 ASP A  77       7.388   8.015  26.638  1.00 26.02           O  
ATOM    499  OD2 ASP A  77       5.832   8.439  25.211  1.00 29.97           O  
ATOM    500  N   LEU A  78       7.790  10.705  28.775  1.00 25.96           N  
ATOM    501  CA  LEU A  78       7.893  10.441  30.201  1.00 26.27           C  
ATOM    502  C   LEU A  78       7.716   8.965  30.539  1.00 26.14           C  
ATOM    503  O   LEU A  78       8.446   8.438  31.374  1.00 25.51           O  
ATOM    504  CB  LEU A  78       6.905  11.301  30.979  1.00 26.32           C  
ATOM    505  CG  LEU A  78       7.155  12.802  30.860  1.00 27.35           C  
ATOM    506  CD1 LEU A  78       6.098  13.579  31.623  1.00 28.05           C  
ATOM    507  CD2 LEU A  78       8.536  13.165  31.379  1.00 28.39           C  
ATOM    508  N   GLU A  79       6.775   8.297  29.874  1.00 26.56           N  
ATOM    509  CA  GLU A  79       6.526   6.876  30.123  1.00 27.00           C  
ATOM    510  C   GLU A  79       7.754   6.029  29.780  1.00 26.63           C  
ATOM    511  O   GLU A  79       8.220   5.231  30.583  1.00 25.94           O  
ATOM    512  CB  GLU A  79       5.302   6.371  29.333  1.00 27.39           C  
ATOM    513  CG  GLU A  79       4.963   4.919  29.657  1.00 29.75           C  
ATOM    514  CD  GLU A  79       3.803   4.347  28.854  1.00 33.15           C  
ATOM    515  OE1 GLU A  79       3.361   4.976  27.863  1.00 35.39           O  
ATOM    516  OE2 GLU A  79       3.338   3.245  29.224  1.00 35.44           O  
ATOM    517  N   TYR A  80       8.279   6.205  28.575  1.00 26.53           N  
ATOM    518  CA  TYR A  80       9.466   5.465  28.169  1.00 26.29           C  
ATOM    519  C   TYR A  80      10.669   5.763  29.072  1.00 25.83           C  
ATOM    520  O   TYR A  80      11.418   4.863  29.435  1.00 25.75           O  
ATOM    521  CB  TYR A  80       9.812   5.802  26.728  1.00 26.53           C  
ATOM    522  CG  TYR A  80      11.047   5.106  26.210  1.00 26.94           C  
ATOM    523  CD1 TYR A  80      10.971   3.836  25.637  1.00 26.53           C  
ATOM    524  CD2 TYR A  80      12.287   5.721  26.291  1.00 25.32           C  
ATOM    525  CE1 TYR A  80      12.113   3.208  25.142  1.00 26.28           C  
ATOM    526  CE2 TYR A  80      13.416   5.109  25.823  1.00 25.73           C  
ATOM    527  CZ  TYR A  80      13.331   3.861  25.240  1.00 25.94           C  
ATOM    528  OH  TYR A  80      14.478   3.294  24.758  1.00 25.55           O  
ATOM    529  N   LEU A  81      10.859   7.016  29.448  1.00 25.62           N  
ATOM    530  CA  LEU A  81      12.000   7.350  30.309  1.00 25.87           C  
ATOM    531  C   LEU A  81      11.821   6.794  31.733  1.00 26.06           C  
ATOM    532  O   LEU A  81      12.763   6.263  32.327  1.00 26.00           O  
ATOM    533  CB  LEU A  81      12.250   8.863  30.340  1.00 25.81           C  
ATOM    534  CG  LEU A  81      12.748   9.501  29.030  1.00 25.65           C  
ATOM    535  CD1 LEU A  81      12.828  11.010  29.174  1.00 26.40           C  
ATOM    536  CD2 LEU A  81      14.102   8.959  28.592  1.00 25.79           C  
ATOM    537  N   GLN A  82      10.617   6.913  32.274  1.00 26.27           N  
ATOM    538  CA  GLN A  82      10.338   6.388  33.602  1.00 26.77           C  
ATOM    539  C   GLN A  82      10.640   4.897  33.623  1.00 26.51           C  
ATOM    540  O   GLN A  82      11.232   4.384  34.552  1.00 26.60           O  
ATOM    541  CB  GLN A  82       8.877   6.611  33.974  1.00 26.90           C  
ATOM    542  CG  GLN A  82       8.466   5.856  35.236  1.00 28.41           C  
ATOM    543  CD  GLN A  82       7.315   6.501  35.987  1.00 30.63           C  
ATOM    544  OE1 GLN A  82       6.755   7.501  35.551  1.00 32.13           O  
ATOM    545  NE2 GLN A  82       6.944   5.907  37.116  1.00 34.12           N  
ATOM    546  N   GLU A  83      10.252   4.216  32.561  1.00 26.68           N  
ATOM    547  CA  GLU A  83      10.429   2.773  32.456  1.00 26.90           C  
ATOM    548  C   GLU A  83      11.893   2.359  32.295  1.00 26.42           C  
ATOM    549  O   GLU A  83      12.285   1.294  32.764  1.00 25.50           O  
ATOM    550  CB  GLU A  83       9.604   2.257  31.273  1.00 26.84           C  
ATOM    551  CG  GLU A  83       9.607   0.753  31.080  1.00 29.20           C  
ATOM    552  CD  GLU A  83       8.902   0.014  32.205  1.00 31.92           C  
ATOM    553  OE1 GLU A  83       8.258   0.666  33.060  1.00 34.06           O  
ATOM    554  OE2 GLU A  83       9.008  -1.221  32.243  1.00 33.78           O  
ATOM    555  N   ASN A  84      12.711   3.223  31.700  1.00 25.79           N  
ATOM    556  CA  ASN A  84      14.063   2.824  31.312  1.00 25.87           C  
ATOM    557  C   ASN A  84      15.273   3.607  31.810  1.00 26.08           C  
ATOM    558  O   ASN A  84      16.392   3.138  31.628  1.00 26.05           O  
ATOM    559  CB  ASN A  84      14.137   2.844  29.784  1.00 25.74           C  
ATOM    560  CG  ASN A  84      13.262   1.799  29.152  1.00 25.67           C  
ATOM    561  OD1 ASN A  84      13.402   0.608  29.439  1.00 24.26           O  
ATOM    562  ND2 ASN A  84      12.354   2.231  28.288  1.00 22.66           N  
ATOM    563  N   ILE A  85      15.087   4.773  32.422  1.00 26.02           N  
ATOM    564  CA  ILE A  85      16.240   5.599  32.763  1.00 26.74           C  
ATOM    565  C   ILE A  85      16.930   5.307  34.099  1.00 26.89           C  
ATOM    566  O   ILE A  85      17.820   6.054  34.519  1.00 26.93           O  
ATOM    567  CB  ILE A  85      15.846   7.076  32.688  1.00 26.70           C  
ATOM    568  CG1 ILE A  85      17.049   7.923  32.270  1.00 27.99           C  
ATOM    569  CG2 ILE A  85      15.232   7.535  33.988  1.00 26.50           C  
ATOM    570  CD1 ILE A  85      16.696   9.389  32.000  1.00 28.77           C  
ATOM    571  N   GLY A  86      16.503   4.253  34.773  1.00 27.27           N  
ATOM    572  CA  GLY A  86      17.130   3.834  36.018  1.00 27.51           C  
ATOM    573  C   GLY A  86      16.573   4.453  37.289  1.00 27.73           C  
ATOM    574  O   GLY A  86      15.563   5.163  37.268  1.00 27.80           O  
ATOM    575  N   ASN A  87      17.273   4.186  38.392  1.00 27.70           N  
ATOM    576  CA  ASN A  87      16.864   4.603  39.726  1.00 27.53           C  
ATOM    577  C   ASN A  87      17.849   5.602  40.320  1.00 27.33           C  
ATOM    578  O   ASN A  87      17.932   5.762  41.539  1.00 26.97           O  
ATOM    579  CB  ASN A  87      16.726   3.367  40.644  1.00 27.60           C  
ATOM    580  N   GLY A  88      18.601   6.273  39.455  1.00 27.41           N  
ATOM    581  CA  GLY A  88      19.528   7.307  39.888  1.00 27.29           C  
ATOM    582  C   GLY A  88      18.762   8.549  40.288  1.00 27.18           C  
ATOM    583  O   GLY A  88      17.570   8.654  40.001  1.00 27.43           O  
ATOM    584  N   ASP A  89      19.437   9.489  40.945  1.00 27.04           N  
ATOM    585  CA  ASP A  89      18.808  10.739  41.366  1.00 26.88           C  
ATOM    586  C   ASP A  89      18.761  11.755  40.227  1.00 26.69           C  
ATOM    587  O   ASP A  89      19.697  11.848  39.446  1.00 26.91           O  
ATOM    588  CB  ASP A  89      19.596  11.372  42.504  1.00 26.95           C  
ATOM    589  CG  ASP A  89      19.375  10.688  43.834  1.00 27.28           C  
ATOM    590  OD1 ASP A  89      18.499   9.811  43.939  1.00 29.31           O  
ATOM    591  OD2 ASP A  89      20.040  10.983  44.839  1.00 27.32           O  
ATOM    592  N   PHE A  90      17.687  12.531  40.152  1.00 26.24           N  
ATOM    593  CA  PHE A  90      17.598  13.594  39.165  1.00 26.10           C  
ATOM    594  C   PHE A  90      17.407  14.931  39.866  1.00 26.23           C  
ATOM    595  O   PHE A  90      16.629  15.037  40.811  1.00 26.48           O  
ATOM    596  CB  PHE A  90      16.460  13.322  38.184  1.00 25.91           C  
ATOM    597  CG  PHE A  90      16.747  12.201  37.241  1.00 25.26           C  
ATOM    598  CD1 PHE A  90      16.601  10.886  37.640  1.00 25.32           C  
ATOM    599  CD2 PHE A  90      17.190  12.459  35.958  1.00 26.02           C  
ATOM    600  CE1 PHE A  90      16.872   9.856  36.777  1.00 24.09           C  
ATOM    601  CE2 PHE A  90      17.460  11.427  35.091  1.00 25.07           C  
ATOM    602  CZ  PHE A  90      17.308  10.117  35.512  1.00 24.67           C  
ATOM    603  N   SER A  91      18.149  15.941  39.430  1.00 26.33           N  
ATOM    604  CA  SER A  91      17.985  17.280  39.973  1.00 26.48           C  
ATOM    605  C   SER A  91      16.777  17.923  39.310  1.00 26.71           C  
ATOM    606  O   SER A  91      16.696  18.029  38.077  1.00 26.09           O  
ATOM    607  CB  SER A  91      19.226  18.152  39.763  1.00 26.25           C  
ATOM    608  OG  SER A  91      20.364  17.543  40.326  1.00 26.61           O  
ATOM    609  N   VAL A  92      15.835  18.327  40.150  1.00 27.06           N  
ATOM    610  CA  VAL A  92      14.629  18.971  39.695  1.00 27.44           C  
ATOM    611  C   VAL A  92      14.468  20.295  40.405  1.00 27.57           C  
ATOM    612  O   VAL A  92      14.475  20.376  41.642  1.00 26.69           O  
ATOM    613  CB  VAL A  92      13.407  18.132  40.004  1.00 27.60           C  
ATOM    614  CG1 VAL A  92      12.164  18.800  39.432  1.00 28.15           C  
ATOM    615  CG2 VAL A  92      13.584  16.731  39.457  1.00 27.84           C  
ATOM    616  N   TYR A  93      14.312  21.334  39.598  1.00 27.77           N  
ATOM    617  CA  TYR A  93      14.120  22.661  40.108  1.00 27.91           C  
ATOM    618  C   TYR A  93      12.654  22.940  40.172  1.00 28.16           C  
ATOM    619  O   TYR A  93      11.894  22.525  39.303  1.00 28.02           O  
ATOM    620  CB  TYR A  93      14.810  23.673  39.216  1.00 27.94           C  
ATOM    621  CG  TYR A  93      16.291  23.593  39.368  1.00 29.53           C  
ATOM    622  CD1 TYR A  93      16.929  24.258  40.395  1.00 29.48           C  
ATOM    623  CD2 TYR A  93      17.046  22.815  38.522  1.00 30.95           C  
ATOM    624  CE1 TYR A  93      18.266  24.169  40.553  1.00 29.93           C  
ATOM    625  CE2 TYR A  93      18.386  22.726  38.679  1.00 31.90           C  
ATOM    626  CZ  TYR A  93      18.985  23.402  39.704  1.00 31.56           C  
ATOM    627  OH  TYR A  93      20.327  23.306  39.878  1.00 35.47           O  
ATOM    628  N   SER A  94      12.282  23.669  41.208  1.00 28.70           N  
ATOM    629  CA  SER A  94      10.913  24.037  41.459  1.00 29.47           C  
ATOM    630  C   SER A  94      10.856  25.547  41.554  1.00 29.69           C  
ATOM    631  O   SER A  94      11.705  26.167  42.187  1.00 29.50           O  
ATOM    632  CB  SER A  94      10.456  23.411  42.774  1.00 29.32           C  
ATOM    633  OG  SER A  94       9.093  23.701  43.009  1.00 30.85           O  
ATOM    634  N   ALA A  95       9.858  26.146  40.928  1.00 30.39           N  
ATOM    635  CA  ALA A  95       9.760  27.591  40.929  1.00 31.04           C  
ATOM    636  C   ALA A  95       8.330  28.064  40.932  1.00 31.76           C  
ATOM    637  O   ALA A  95       7.425  27.386  40.452  1.00 31.87           O  
ATOM    638  CB  ALA A  95      10.480  28.165  39.716  1.00 31.12           C  
ATOM    639  N   SER A  96       8.147  29.258  41.467  1.00 32.54           N  
ATOM    640  CA  SER A  96       6.848  29.891  41.489  1.00 33.42           C  
ATOM    641  C   SER A  96       6.708  30.869  40.326  1.00 33.15           C  
ATOM    642  O   SER A  96       5.662  31.487  40.163  1.00 34.35           O  
ATOM    643  CB  SER A  96       6.673  30.661  42.787  1.00 33.88           C  
ATOM    644  OG  SER A  96       5.380  31.217  42.815  1.00 35.79           O  
ATOM    645  N   THR A  97       7.775  31.031  39.554  1.00 32.09           N  
ATOM    646  CA  THR A  97       7.797  31.920  38.397  1.00 31.44           C  
ATOM    647  C   THR A  97       8.185  31.095  37.191  1.00 30.26           C  
ATOM    648  O   THR A  97       8.693  30.003  37.348  1.00 29.72           O  
ATOM    649  CB  THR A  97       8.857  33.031  38.582  1.00 31.64           C  
ATOM    650  OG1 THR A  97       9.147  33.656  37.323  1.00 32.17           O  
ATOM    651  CG2 THR A  97      10.227  32.455  38.978  1.00 31.73           C  
ATOM    652  N   HIS A  98       7.974  31.623  35.996  1.00 29.35           N  
ATOM    653  CA  HIS A  98       8.379  30.915  34.780  1.00 28.83           C  
ATOM    654  C   HIS A  98       9.899  30.969  34.589  1.00 28.37           C  
ATOM    655  O   HIS A  98      10.467  30.189  33.824  1.00 27.53           O  
ATOM    656  CB  HIS A  98       7.671  31.490  33.548  1.00 28.76           C  
ATOM    657  CG  HIS A  98       7.936  32.942  33.309  1.00 28.53           C  
ATOM    658  ND1 HIS A  98       7.271  33.944  33.984  1.00 29.18           N  
ATOM    659  CD2 HIS A  98       8.793  33.566  32.463  1.00 29.68           C  
ATOM    660  CE1 HIS A  98       7.708  35.120  33.568  1.00 29.42           C  
ATOM    661  NE2 HIS A  98       8.638  34.919  32.650  1.00 29.10           N  
ATOM    662  N   LYS A  99      10.562  31.874  35.299  1.00 27.85           N  
ATOM    663  CA  LYS A  99      11.997  32.041  35.124  1.00 28.24           C  
ATOM    664  C   LYS A  99      12.878  31.143  35.997  1.00 27.69           C  
ATOM    665  O   LYS A  99      12.892  31.278  37.216  1.00 29.10           O  
ATOM    666  CB  LYS A  99      12.366  33.498  35.349  1.00 28.47           C  
ATOM    667  CG  LYS A  99      11.836  34.410  34.255  1.00 30.42           C  
ATOM    668  CD  LYS A  99      12.431  35.791  34.347  1.00 32.66           C  
ATOM    669  CE  LYS A  99      11.757  36.624  35.421  1.00 34.45           C  
ATOM    670  NZ  LYS A  99      10.569  37.347  34.884  1.00 35.39           N  
ATOM    671  N   PHE A 100      13.621  30.237  35.376  1.00 26.40           N  
ATOM    672  CA  PHE A 100      14.551  29.397  36.127  1.00 25.95           C  
ATOM    673  C   PHE A 100      15.978  29.920  35.995  1.00 25.87           C  
ATOM    674  O   PHE A 100      16.809  29.386  35.247  1.00 25.86           O  
ATOM    675  CB  PHE A 100      14.469  27.945  35.686  1.00 25.48           C  
ATOM    676  CG  PHE A 100      13.211  27.267  36.109  1.00 25.06           C  
ATOM    677  CD1 PHE A 100      12.047  27.436  35.388  1.00 24.80           C  
ATOM    678  CD2 PHE A 100      13.191  26.472  37.238  1.00 25.18           C  
ATOM    679  CE1 PHE A 100      10.886  26.805  35.772  1.00 25.96           C  
ATOM    680  CE2 PHE A 100      12.030  25.835  37.631  1.00 25.79           C  
ATOM    681  CZ  PHE A 100      10.878  26.004  36.898  1.00 26.05           C  
ATOM    682  N   LEU A 101      16.237  30.997  36.709  1.00 25.77           N  
ATOM    683  CA  LEU A 101      17.549  31.589  36.747  1.00 25.85           C  
ATOM    684  C   LEU A 101      18.527  30.605  37.381  1.00 25.87           C  
ATOM    685  O   LEU A 101      18.319  30.136  38.503  1.00 24.99           O  
ATOM    686  CB  LEU A 101      17.488  32.876  37.559  1.00 25.84           C  
ATOM    687  CG  LEU A 101      18.795  33.656  37.708  1.00 26.07           C  
ATOM    688  CD1 LEU A 101      19.244  34.200  36.377  1.00 25.11           C  
ATOM    689  CD2 LEU A 101      18.609  34.800  38.710  1.00 27.75           C  
ATOM    690  N   TYR A 102      19.582  30.274  36.644  1.00 26.56           N  
ATOM    691  CA  TYR A 102      20.611  29.380  37.159  1.00 26.99           C  
ATOM    692  C   TYR A 102      21.430  30.072  38.260  1.00 27.10           C  
ATOM    693  O   TYR A 102      21.711  31.264  38.174  1.00 27.00           O  
ATOM    694  CB  TYR A 102      21.562  28.939  36.053  1.00 27.26           C  
ATOM    695  CG  TYR A 102      22.667  28.088  36.620  1.00 28.93           C  
ATOM    696  CD1 TYR A 102      22.457  26.750  36.914  1.00 29.52           C  
ATOM    697  CD2 TYR A 102      23.906  28.636  36.909  1.00 31.11           C  
ATOM    698  CE1 TYR A 102      23.463  25.979  37.480  1.00 32.23           C  
ATOM    699  CE2 TYR A 102      24.913  27.872  37.470  1.00 32.52           C  
ATOM    700  CZ  TYR A 102      24.693  26.549  37.750  1.00 33.88           C  
ATOM    701  OH  TYR A 102      25.727  25.794  38.314  1.00 38.68           O  
ATOM    702  N   TYR A 103      21.793  29.322  39.296  1.00 26.83           N  
ATOM    703  CA  TYR A 103      22.667  29.840  40.343  1.00 27.22           C  
ATOM    704  C   TYR A 103      23.613  28.750  40.834  1.00 26.77           C  
ATOM    705  O   TYR A 103      23.287  27.556  40.853  1.00 25.60           O  
ATOM    706  CB  TYR A 103      21.880  30.440  41.517  1.00 27.38           C  
ATOM    707  CG  TYR A 103      20.909  29.493  42.154  1.00 29.11           C  
ATOM    708  CD1 TYR A 103      19.639  29.340  41.639  1.00 30.58           C  
ATOM    709  CD2 TYR A 103      21.257  28.759  43.279  1.00 32.13           C  
ATOM    710  CE1 TYR A 103      18.734  28.469  42.212  1.00 32.78           C  
ATOM    711  CE2 TYR A 103      20.357  27.887  43.877  1.00 33.15           C  
ATOM    712  CZ  TYR A 103      19.096  27.745  43.329  1.00 34.41           C  
ATOM    713  OH  TYR A 103      18.187  26.888  43.892  1.00 37.44           O  
ATOM    714  N   ASP A 104      24.798  29.182  41.225  1.00 26.36           N  
ATOM    715  CA  ASP A 104      25.832  28.273  41.673  1.00 26.28           C  
ATOM    716  C   ASP A 104      25.802  28.239  43.184  1.00 26.21           C  
ATOM    717  O   ASP A 104      26.163  29.212  43.845  1.00 25.45           O  
ATOM    718  CB  ASP A 104      27.174  28.765  41.154  1.00 25.92           C  
ATOM    719  CG  ASP A 104      28.330  27.889  41.575  1.00 27.39           C  
ATOM    720  OD1 ASP A 104      28.161  26.973  42.437  1.00 27.13           O  
ATOM    721  OD2 ASP A 104      29.459  28.068  41.075  1.00 27.68           O  
ATOM    722  N   GLU A 105      25.358  27.114  43.724  1.00 26.46           N  
ATOM    723  CA  GLU A 105      25.218  26.962  45.162  1.00 27.02           C  
ATOM    724  C   GLU A 105      26.540  27.199  45.916  1.00 26.91           C  
ATOM    725  O   GLU A 105      26.523  27.718  47.026  1.00 26.51           O  
ATOM    726  CB  GLU A 105      24.602  25.587  45.481  1.00 27.45           C  
ATOM    727  CG  GLU A 105      23.088  25.556  45.254  1.00 29.46           C  
ATOM    728  CD  GLU A 105      22.527  24.158  45.025  1.00 32.85           C  
ATOM    729  OE1 GLU A 105      22.908  23.234  45.765  1.00 32.90           O  
ATOM    730  OE2 GLU A 105      21.703  23.980  44.085  1.00 35.16           O  
ATOM    731  N   LYS A 106      27.680  26.874  45.305  1.00 27.12           N  
ATOM    732  CA  LYS A 106      28.979  27.041  45.983  1.00 27.54           C  
ATOM    733  C   LYS A 106      29.331  28.493  46.258  1.00 27.70           C  
ATOM    734  O   LYS A 106      30.164  28.769  47.099  1.00 27.61           O  
ATOM    735  CB  LYS A 106      30.127  26.441  45.163  1.00 27.58           C  
ATOM    736  CG  LYS A 106      30.038  24.928  44.918  1.00 28.61           C  
ATOM    737  N   LYS A 107      28.713  29.420  45.537  1.00 27.99           N  
ATOM    738  CA  LYS A 107      29.020  30.826  45.694  1.00 28.30           C  
ATOM    739  C   LYS A 107      28.034  31.513  46.631  1.00 29.21           C  
ATOM    740  O   LYS A 107      28.175  32.701  46.917  1.00 29.08           O  
ATOM    741  CB  LYS A 107      29.040  31.524  44.324  1.00 28.30           C  
ATOM    742  CG  LYS A 107      30.344  31.291  43.516  1.00 28.07           C  
ATOM    743  CD  LYS A 107      30.242  31.737  42.034  1.00 27.29           C  
ATOM    744  CE  LYS A 107      31.584  31.518  41.315  1.00 26.86           C  
ATOM    745  NZ  LYS A 107      31.642  31.889  39.870  1.00 24.80           N  
ATOM    746  N   MET A 108      27.041  30.781  47.125  1.00 30.08           N  
ATOM    747  CA  MET A 108      26.031  31.405  47.982  1.00 31.53           C  
ATOM    748  C   MET A 108      26.581  31.952  49.309  1.00 32.44           C  
ATOM    749  O   MET A 108      26.102  32.972  49.812  1.00 32.47           O  
ATOM    750  CB  MET A 108      24.862  30.452  48.218  1.00 31.81           C  
ATOM    751  CG  MET A 108      24.072  30.193  46.932  1.00 33.07           C  
ATOM    752  SD  MET A 108      22.625  29.140  47.064  1.00 35.76           S  
ATOM    753  CE  MET A 108      21.540  30.140  48.050  1.00 35.99           C  
ATOM    754  N   ALA A 109      27.603  31.315  49.860  1.00 33.56           N  
ATOM    755  CA  ALA A 109      28.154  31.769  51.138  1.00 34.94           C  
ATOM    756  C   ALA A 109      28.651  33.212  51.060  1.00 35.81           C  
ATOM    757  O   ALA A 109      28.483  33.989  51.991  1.00 36.23           O  
ATOM    758  CB  ALA A 109      29.279  30.838  51.606  1.00 34.82           C  
ATOM    759  N   ASN A 110      29.236  33.575  49.929  1.00 37.05           N  
ATOM    760  CA  ASN A 110      29.774  34.918  49.748  1.00 37.94           C  
ATOM    761  C   ASN A 110      28.731  35.992  49.413  1.00 38.13           C  
ATOM    762  O   ASN A 110      29.064  37.167  49.293  1.00 37.92           O  
ATOM    763  CB  ASN A 110      30.855  34.878  48.669  1.00 38.16           C  
ATOM    764  CG  ASN A 110      32.050  34.035  49.079  1.00 39.37           C  
ATOM    765  OD1 ASN A 110      32.407  33.964  50.265  1.00 40.12           O  
ATOM    766  ND2 ASN A 110      32.670  33.377  48.103  1.00 39.46           N  
ATOM    767  N   PHE A 111      27.480  35.588  49.234  1.00 38.71           N  
ATOM    768  CA  PHE A 111      26.408  36.539  48.966  1.00 39.02           C  
ATOM    769  C   PHE A 111      25.180  36.135  49.773  1.00 39.71           C  
ATOM    770  O   PHE A 111      24.143  35.747  49.232  1.00 39.45           O  
ATOM    771  CB  PHE A 111      26.091  36.603  47.471  1.00 38.97           C  
ATOM    772  CG  PHE A 111      27.110  37.362  46.672  1.00 38.04           C  
ATOM    773  CD1 PHE A 111      28.329  36.791  46.363  1.00 37.99           C  
ATOM    774  CD2 PHE A 111      26.851  38.642  46.235  1.00 36.83           C  
ATOM    775  CE1 PHE A 111      29.269  37.493  45.635  1.00 37.68           C  
ATOM    776  CE2 PHE A 111      27.788  39.339  45.500  1.00 36.08           C  
ATOM    777  CZ  PHE A 111      28.994  38.768  45.208  1.00 35.84           C  
ATOM    778  N   GLN A 112      25.315  36.267  51.085  1.00 40.62           N  
ATOM    779  CA  GLN A 112      24.286  35.852  52.029  1.00 41.31           C  
ATOM    780  C   GLN A 112      22.915  36.430  51.721  1.00 41.10           C  
ATOM    781  O   GLN A 112      21.906  35.827  52.060  1.00 41.31           O  
ATOM    782  CB  GLN A 112      24.701  36.236  53.451  1.00 41.65           C  
ATOM    783  CG  GLN A 112      26.058  35.694  53.882  1.00 43.80           C  
ATOM    784  CD  GLN A 112      26.104  34.177  53.938  1.00 46.42           C  
ATOM    785  OE1 GLN A 112      25.394  33.501  53.191  1.00 48.56           O  
ATOM    786  NE2 GLN A 112      26.951  33.637  54.816  1.00 46.94           N  
ATOM    787  N   ASN A 113      22.876  37.588  51.074  1.00 41.02           N  
ATOM    788  CA  ASN A 113      21.606  38.229  50.749  1.00 40.98           C  
ATOM    789  C   ASN A 113      20.954  37.760  49.440  1.00 40.71           C  
ATOM    790  O   ASN A 113      19.889  38.251  49.071  1.00 40.77           O  
ATOM    791  CB  ASN A 113      21.778  39.753  50.737  1.00 41.09           C  
ATOM    792  CG  ASN A 113      22.129  40.314  52.123  1.00 41.51           C  
ATOM    793  OD1 ASN A 113      21.717  39.772  53.158  1.00 40.60           O  
ATOM    794  ND2 ASN A 113      22.892  41.401  52.141  1.00 41.19           N  
ATOM    795  N   PHE A 114      21.571  36.826  48.725  1.00 40.34           N  
ATOM    796  CA  PHE A 114      20.934  36.321  47.515  1.00 39.86           C  
ATOM    797  C   PHE A 114      19.908  35.266  47.902  1.00 39.46           C  
ATOM    798  O   PHE A 114      20.235  34.299  48.584  1.00 38.82           O  
ATOM    799  CB  PHE A 114      21.940  35.714  46.552  1.00 39.96           C  
ATOM    800  CG  PHE A 114      21.298  35.059  45.362  1.00 40.54           C  
ATOM    801  CD1 PHE A 114      20.670  35.828  44.395  1.00 40.29           C  
ATOM    802  CD2 PHE A 114      21.295  33.679  45.224  1.00 40.62           C  
ATOM    803  CE1 PHE A 114      20.061  35.237  43.307  1.00 40.20           C  
ATOM    804  CE2 PHE A 114      20.684  33.082  44.126  1.00 40.36           C  
ATOM    805  CZ  PHE A 114      20.066  33.866  43.172  1.00 40.52           C  
ATOM    806  N   LYS A 115      18.669  35.457  47.461  1.00 39.11           N  
ATOM    807  CA  LYS A 115      17.596  34.529  47.787  1.00 39.02           C  
ATOM    808  C   LYS A 115      17.042  33.938  46.497  1.00 38.71           C  
ATOM    809  O   LYS A 115      16.285  34.590  45.787  1.00 39.00           O  
ATOM    810  CB  LYS A 115      16.498  35.251  48.578  1.00 39.14           C  
ATOM    811  N   PRO A 116      17.389  32.691  46.213  1.00 38.17           N  
ATOM    812  CA  PRO A 116      17.027  32.060  44.938  1.00 37.95           C  
ATOM    813  C   PRO A 116      15.532  31.889  44.783  1.00 37.38           C  
ATOM    814  O   PRO A 116      14.865  31.506  45.733  1.00 37.36           O  
ATOM    815  CB  PRO A 116      17.684  30.679  45.004  1.00 38.15           C  
ATOM    816  CG  PRO A 116      18.416  30.604  46.297  1.00 38.40           C  
ATOM    817  CD  PRO A 116      18.079  31.775  47.125  1.00 38.19           C  
ATOM    818  N   ARG A 117      15.027  32.161  43.590  1.00 36.84           N  
ATOM    819  CA  ARG A 117      13.611  32.028  43.293  1.00 36.61           C  
ATOM    820  C   ARG A 117      13.259  30.581  42.984  1.00 36.38           C  
ATOM    821  O   ARG A 117      12.084  30.230  42.913  1.00 36.44           O  
ATOM    822  CB  ARG A 117      13.235  32.913  42.122  1.00 36.62           C  
ATOM    823  N   SER A 118      14.271  29.745  42.777  1.00 35.79           N  
ATOM    824  CA  SER A 118      14.025  28.339  42.538  1.00 35.51           C  
ATOM    825  C   SER A 118      14.844  27.491  43.512  1.00 35.35           C  
ATOM    826  O   SER A 118      15.888  27.923  43.991  1.00 35.16           O  
ATOM    827  CB  SER A 118      14.330  27.976  41.086  1.00 35.26           C  
ATOM    828  OG  SER A 118      15.689  28.164  40.795  1.00 35.14           O  
ATOM    829  N   ASN A 119      14.329  26.306  43.824  1.00 35.11           N  
ATOM    830  CA  ASN A 119      14.997  25.373  44.715  1.00 35.21           C  
ATOM    831  C   ASN A 119      15.233  24.049  44.022  1.00 34.26           C  
ATOM    832  O   ASN A 119      14.401  23.595  43.244  1.00 34.11           O  
ATOM    833  CB  ASN A 119      14.145  25.110  45.957  1.00 35.95           C  
ATOM    834  CG  ASN A 119      13.636  26.382  46.592  1.00 38.47           C  
ATOM    835  OD1 ASN A 119      14.417  27.245  47.025  1.00 41.76           O  
ATOM    836  ND2 ASN A 119      12.314  26.511  46.657  1.00 42.21           N  
ATOM    837  N   ARG A 120      16.368  23.434  44.326  1.00 33.75           N  
ATOM    838  CA  ARG A 120      16.750  22.149  43.761  1.00 33.33           C  
ATOM    839  C   ARG A 120      16.327  21.045  44.699  1.00 33.26           C  
ATOM    840  O   ARG A 120      16.523  21.138  45.910  1.00 33.07           O  
ATOM    841  CB  ARG A 120      18.270  22.075  43.592  1.00 33.37           C  
ATOM    842  CG  ARG A 120      18.759  20.889  42.771  1.00 32.70           C  
ATOM    843  CD  ARG A 120      20.277  20.732  42.743  1.00 31.64           C  
ATOM    844  NE  ARG A 120      20.892  21.165  43.992  1.00 31.16           N  
ATOM    845  CZ  ARG A 120      21.233  20.357  44.993  1.00 31.33           C  
ATOM    846  NH1 ARG A 120      21.027  19.047  44.920  1.00 30.77           N  
ATOM    847  NH2 ARG A 120      21.789  20.867  46.077  1.00 31.01           N  
ATOM    848  N   GLU A 121      15.735  20.001  44.137  1.00 32.98           N  
ATOM    849  CA  GLU A 121      15.379  18.827  44.904  1.00 32.85           C  
ATOM    850  C   GLU A 121      15.846  17.630  44.095  1.00 32.17           C  
ATOM    851  O   GLU A 121      15.744  17.612  42.864  1.00 32.36           O  
ATOM    852  CB  GLU A 121      13.874  18.767  45.179  1.00 33.21           C  
ATOM    853  CG  GLU A 121      13.420  17.468  45.826  1.00 35.39           C  
ATOM    854  CD  GLU A 121      12.189  17.629  46.699  1.00 38.11           C  
ATOM    855  OE1 GLU A 121      12.326  18.152  47.830  1.00 41.26           O  
ATOM    856  OE2 GLU A 121      11.091  17.221  46.270  1.00 39.55           O  
ATOM    857  N   GLU A 122      16.400  16.648  44.786  1.00 31.28           N  
ATOM    858  CA  GLU A 122      16.886  15.448  44.150  1.00 30.61           C  
ATOM    859  C   GLU A 122      15.814  14.392  44.298  1.00 30.31           C  
ATOM    860  O   GLU A 122      15.328  14.165  45.395  1.00 30.07           O  
ATOM    861  CB  GLU A 122      18.163  14.980  44.833  1.00 30.52           C  
ATOM    862  CG  GLU A 122      19.293  15.983  44.771  1.00 29.67           C  
ATOM    863  CD  GLU A 122      19.747  16.253  43.348  1.00 29.79           C  
ATOM    864  OE1 GLU A 122      20.120  15.280  42.667  1.00 28.28           O  
ATOM    865  OE2 GLU A 122      19.734  17.439  42.914  1.00 27.93           O  
ATOM    866  N   MET A 123      15.432  13.751  43.202  1.00 29.74           N  
ATOM    867  CA  MET A 123      14.407  12.728  43.277  1.00 29.77           C  
ATOM    868  C   MET A 123      14.594  11.683  42.202  1.00 29.31           C  
ATOM    869  O   MET A 123      15.408  11.842  41.294  1.00 29.42           O  
ATOM    870  CB  MET A 123      13.016  13.354  43.165  1.00 29.81           C  
ATOM    871  CG  MET A 123      12.749  14.057  41.865  1.00 30.27           C  
ATOM    872  SD  MET A 123      11.181  14.960  41.871  1.00 31.65           S  
ATOM    873  CE  MET A 123      11.582  16.371  42.804  1.00 31.47           C  
ATOM    874  N   LYS A 124      13.835  10.604  42.332  1.00 28.82           N  
ATOM    875  CA  LYS A 124      13.841   9.535  41.352  1.00 28.33           C  
ATOM    876  C   LYS A 124      12.959   9.976  40.191  1.00 27.51           C  
ATOM    877  O   LYS A 124      12.077  10.817  40.361  1.00 26.52           O  
ATOM    878  CB  LYS A 124      13.330   8.242  41.984  1.00 28.45           C  
ATOM    879  CG  LYS A 124      14.153   7.783  43.204  1.00 29.42           C  
ATOM    880  CD  LYS A 124      15.597   7.442  42.804  1.00 30.46           C  
ATOM    881  CE  LYS A 124      16.479   7.067  43.992  1.00 30.52           C  
ATOM    882  NZ  LYS A 124      17.928   7.324  43.699  1.00 30.05           N  
ATOM    883  N   PHE A 125      13.188   9.407  39.014  1.00 26.98           N  
ATOM    884  CA  PHE A 125      12.477   9.871  37.826  1.00 26.83           C  
ATOM    885  C   PHE A 125      10.974   9.762  37.972  1.00 26.77           C  
ATOM    886  O   PHE A 125      10.245  10.673  37.585  1.00 26.38           O  
ATOM    887  CB  PHE A 125      12.927   9.138  36.568  1.00 26.71           C  
ATOM    888  CG  PHE A 125      12.613   9.891  35.316  1.00 26.32           C  
ATOM    889  CD1 PHE A 125      13.476  10.876  34.849  1.00 26.29           C  
ATOM    890  CD2 PHE A 125      11.438   9.657  34.635  1.00 26.06           C  
ATOM    891  CE1 PHE A 125      13.183  11.594  33.715  1.00 25.70           C  
ATOM    892  CE2 PHE A 125      11.140  10.368  33.483  1.00 26.70           C  
ATOM    893  CZ  PHE A 125      12.018  11.341  33.025  1.00 26.87           C  
ATOM    894  N   HIS A 126      10.527   8.649  38.550  1.00 26.77           N  
ATOM    895  CA  HIS A 126       9.113   8.396  38.753  1.00 26.82           C  
ATOM    896  C   HIS A 126       8.517   9.390  39.734  1.00 26.68           C  
ATOM    897  O   HIS A 126       7.326   9.670  39.687  1.00 26.03           O  
ATOM    898  CB  HIS A 126       8.882   6.951  39.238  1.00 27.07           C  
ATOM    899  CG  HIS A 126       9.028   6.767  40.717  1.00 27.39           C  
ATOM    900  ND1 HIS A 126       7.959   6.836  41.582  1.00 28.48           N  
ATOM    901  CD2 HIS A 126      10.115   6.505  41.484  1.00 28.33           C  
ATOM    902  CE1 HIS A 126       8.382   6.636  42.819  1.00 28.68           C  
ATOM    903  NE2 HIS A 126       9.687   6.439  42.788  1.00 27.97           N  
ATOM    904  N   GLU A 127       9.342   9.918  40.630  1.00 27.00           N  
ATOM    905  CA  GLU A 127       8.876  10.930  41.572  1.00 27.34           C  
ATOM    906  C   GLU A 127       8.683  12.259  40.838  1.00 27.36           C  
ATOM    907  O   GLU A 127       7.761  13.026  41.126  1.00 26.86           O  
ATOM    908  CB  GLU A 127       9.862  11.084  42.728  1.00 27.31           C  
ATOM    909  CG  GLU A 127      10.018   9.821  43.552  1.00 28.69           C  
ATOM    910  CD  GLU A 127      10.959   9.992  44.722  1.00 29.65           C  
ATOM    911  OE1 GLU A 127      12.139  10.318  44.485  1.00 29.56           O  
ATOM    912  OE2 GLU A 127      10.509   9.787  45.876  1.00 30.92           O  
ATOM    913  N   PHE A 128       9.554  12.519  39.876  1.00 27.91           N  
ATOM    914  CA  PHE A 128       9.453  13.736  39.068  1.00 28.21           C  
ATOM    915  C   PHE A 128       8.149  13.658  38.282  1.00 29.04           C  
ATOM    916  O   PHE A 128       7.354  14.600  38.255  1.00 29.03           O  
ATOM    917  CB  PHE A 128      10.643  13.838  38.115  1.00 27.74           C  
ATOM    918  CG  PHE A 128      10.427  14.792  36.959  1.00 27.06           C  
ATOM    919  CD1 PHE A 128      10.189  16.138  37.185  1.00 25.41           C  
ATOM    920  CD2 PHE A 128      10.480  14.343  35.657  1.00 25.60           C  
ATOM    921  CE1 PHE A 128       9.985  17.000  36.144  1.00 25.41           C  
ATOM    922  CE2 PHE A 128      10.281  15.215  34.604  1.00 26.59           C  
ATOM    923  CZ  PHE A 128      10.032  16.540  34.846  1.00 25.61           C  
ATOM    924  N   VAL A 129       7.925  12.500  37.677  1.00 29.90           N  
ATOM    925  CA  VAL A 129       6.756  12.285  36.847  1.00 30.82           C  
ATOM    926  C   VAL A 129       5.476  12.447  37.669  1.00 31.61           C  
ATOM    927  O   VAL A 129       4.515  13.091  37.234  1.00 31.39           O  
ATOM    928  CB  VAL A 129       6.793  10.883  36.213  1.00 30.92           C  
ATOM    929  CG1 VAL A 129       5.479  10.582  35.503  1.00 31.15           C  
ATOM    930  CG2 VAL A 129       7.975  10.751  35.253  1.00 30.61           C  
ATOM    931  N   GLU A 130       5.475  11.858  38.861  1.00 32.42           N  
ATOM    932  CA  GLU A 130       4.332  11.946  39.761  1.00 33.13           C  
ATOM    933  C   GLU A 130       4.070  13.403  40.126  1.00 33.42           C  
ATOM    934  O   GLU A 130       2.930  13.867  40.081  1.00 33.01           O  
ATOM    935  CB  GLU A 130       4.587  11.108  41.017  1.00 33.20           C  
ATOM    936  CG  GLU A 130       4.537   9.609  40.755  1.00 34.22           C  
ATOM    937  CD  GLU A 130       5.294   8.792  41.789  1.00 35.55           C  
ATOM    938  OE1 GLU A 130       5.630   9.339  42.861  1.00 37.02           O  
ATOM    939  OE2 GLU A 130       5.558   7.598  41.525  1.00 35.99           O  
ATOM    940  N   LYS A 131       5.128  14.120  40.486  1.00 34.00           N  
ATOM    941  CA  LYS A 131       4.994  15.538  40.800  1.00 34.79           C  
ATOM    942  C   LYS A 131       4.354  16.286  39.637  1.00 35.25           C  
ATOM    943  O   LYS A 131       3.449  17.089  39.835  1.00 34.81           O  
ATOM    944  CB  LYS A 131       6.345  16.171  41.100  1.00 34.89           C  
ATOM    945  CG  LYS A 131       6.597  16.477  42.554  1.00 35.57           C  
ATOM    946  CD  LYS A 131       7.191  17.868  42.694  1.00 36.25           C  
ATOM    947  CE  LYS A 131       7.862  18.072  44.034  1.00 37.30           C  
ATOM    948  NZ  LYS A 131       8.108  19.526  44.332  1.00 37.49           N  
ATOM    949  N   LEU A 132       4.829  16.038  38.422  1.00 36.00           N  
ATOM    950  CA  LEU A 132       4.243  16.701  37.268  1.00 37.05           C  
ATOM    951  C   LEU A 132       2.755  16.406  37.170  1.00 37.67           C  
ATOM    952  O   LEU A 132       1.963  17.300  36.870  1.00 37.77           O  
ATOM    953  CB  LEU A 132       4.919  16.260  35.979  1.00 37.39           C  
ATOM    954  CG  LEU A 132       6.310  16.803  35.710  1.00 38.29           C  
ATOM    955  CD1 LEU A 132       6.783  16.289  34.363  1.00 39.35           C  
ATOM    956  CD2 LEU A 132       6.306  18.314  35.721  1.00 39.70           C  
ATOM    957  N   GLN A 133       2.386  15.151  37.417  1.00 38.34           N  
ATOM    958  CA  GLN A 133       0.989  14.730  37.373  1.00 39.11           C  
ATOM    959  C   GLN A 133       0.132  15.434  38.427  1.00 39.73           C  
ATOM    960  O   GLN A 133      -0.966  15.897  38.126  1.00 39.61           O  
ATOM    961  CB  GLN A 133       0.886  13.213  37.538  1.00 39.05           C  
ATOM    962  N   ASP A 134       0.629  15.507  39.658  1.00 40.61           N  
ATOM    963  CA  ASP A 134      -0.108  16.149  40.747  1.00 41.70           C  
ATOM    964  C   ASP A 134      -0.398  17.626  40.451  1.00 41.68           C  
ATOM    965  O   ASP A 134      -1.470  18.137  40.770  1.00 41.28           O  
ATOM    966  CB  ASP A 134       0.678  16.030  42.056  1.00 42.32           C  
ATOM    967  CG  ASP A 134      -0.165  16.351  43.286  1.00 44.92           C  
ATOM    968  OD1 ASP A 134      -1.235  16.991  43.152  1.00 48.33           O  
ATOM    969  OD2 ASP A 134       0.164  15.991  44.442  1.00 48.64           O  
ATOM    970  N   ILE A 135       0.563  18.312  39.842  1.00 41.92           N  
ATOM    971  CA  ILE A 135       0.383  19.717  39.512  1.00 42.18           C  
ATOM    972  C   ILE A 135      -0.715  19.862  38.471  1.00 42.41           C  
ATOM    973  O   ILE A 135      -1.635  20.664  38.634  1.00 42.49           O  
ATOM    974  CB  ILE A 135       1.696  20.324  38.997  1.00 42.17           C  
ATOM    975  CG1 ILE A 135       2.720  20.399  40.131  1.00 42.25           C  
ATOM    976  CG2 ILE A 135       1.451  21.708  38.437  1.00 42.11           C  
ATOM    977  CD1 ILE A 135       4.151  20.438  39.653  1.00 42.91           C  
ATOM    978  N   GLN A 136      -0.614  19.075  37.407  1.00 42.71           N  
ATOM    979  CA  GLN A 136      -1.593  19.114  36.333  1.00 43.09           C  
ATOM    980  C   GLN A 136      -2.991  18.935  36.900  1.00 43.56           C  
ATOM    981  O   GLN A 136      -3.863  19.785  36.707  1.00 43.93           O  
ATOM    982  CB  GLN A 136      -1.298  18.031  35.317  1.00 43.10           C  
ATOM    983  N   GLN A 137      -3.181  17.844  37.635  1.00 43.82           N  
ATOM    984  CA  GLN A 137      -4.486  17.493  38.182  1.00 44.02           C  
ATOM    985  C   GLN A 137      -5.023  18.540  39.144  1.00 44.08           C  
ATOM    986  O   GLN A 137      -6.202  18.891  39.080  1.00 44.46           O  
ATOM    987  CB  GLN A 137      -4.425  16.124  38.868  1.00 44.00           C  
ATOM    988  N   ARG A 138      -4.169  19.043  40.031  1.00 43.93           N  
ATOM    989  CA  ARG A 138      -4.606  20.022  41.024  1.00 43.76           C  
ATOM    990  C   ARG A 138      -4.578  21.445  40.463  1.00 43.34           C  
ATOM    991  O   ARG A 138      -4.681  22.415  41.214  1.00 43.54           O  
ATOM    992  CB  ARG A 138      -3.751  19.919  42.299  1.00 43.84           C  
ATOM    993  CG  ARG A 138      -2.420  20.679  42.279  1.00 44.85           C  
ATOM    994  CD  ARG A 138      -1.493  20.279  43.420  1.00 45.82           C  
ATOM    995  NE  ARG A 138      -0.372  21.197  43.620  1.00 46.44           N  
ATOM    996  CZ  ARG A 138       0.914  20.863  43.499  1.00 47.95           C  
ATOM    997  NH1 ARG A 138       1.262  19.627  43.162  1.00 49.02           N  
ATOM    998  NH2 ARG A 138       1.864  21.767  43.709  1.00 47.70           N  
ATOM    999  N   GLY A 139      -4.450  21.569  39.143  1.00 42.62           N  
ATOM   1000  CA  GLY A 139      -4.371  22.871  38.504  1.00 41.93           C  
ATOM   1001  C   GLY A 139      -3.389  23.820  39.174  1.00 41.28           C  
ATOM   1002  O   GLY A 139      -3.607  25.030  39.196  1.00 41.58           O  
ATOM   1003  N   GLY A 140      -2.291  23.292  39.703  1.00 40.31           N  
ATOM   1004  CA  GLY A 140      -1.329  24.119  40.410  1.00 39.43           C  
ATOM   1005  C   GLY A 140      -0.563  25.070  39.512  1.00 38.71           C  
ATOM   1006  O   GLY A 140      -0.495  24.871  38.294  1.00 38.40           O  
ATOM   1007  N   GLU A 141       0.003  26.117  40.110  1.00 37.82           N  
ATOM   1008  CA  GLU A 141       0.829  27.066  39.363  1.00 37.20           C  
ATOM   1009  C   GLU A 141       2.320  26.726  39.491  1.00 35.94           C  
ATOM   1010  O   GLU A 141       3.160  27.356  38.845  1.00 35.76           O  
ATOM   1011  CB  GLU A 141       0.590  28.510  39.828  1.00 37.63           C  
ATOM   1012  CG  GLU A 141      -0.729  29.146  39.379  1.00 39.51           C  
ATOM   1013  CD  GLU A 141      -0.936  29.164  37.866  1.00 41.63           C  
ATOM   1014  OE1 GLU A 141       0.056  29.147  37.102  1.00 42.42           O  
ATOM   1015  OE2 GLU A 141      -2.115  29.202  37.434  1.00 43.77           O  
ATOM   1016  N   GLU A 142       2.652  25.742  40.326  1.00 34.29           N  
ATOM   1017  CA  GLU A 142       4.045  25.351  40.510  1.00 33.08           C  
ATOM   1018  C   GLU A 142       4.655  24.938  39.170  1.00 31.87           C  
ATOM   1019  O   GLU A 142       3.958  24.443  38.296  1.00 31.87           O  
ATOM   1020  CB  GLU A 142       4.170  24.201  41.519  1.00 32.96           C  
ATOM   1021  CG  GLU A 142       5.610  23.914  41.942  1.00 32.71           C  
ATOM   1022  CD  GLU A 142       5.761  22.730  42.896  1.00 33.55           C  
ATOM   1023  OE1 GLU A 142       4.778  22.001  43.146  1.00 32.41           O  
ATOM   1024  OE2 GLU A 142       6.888  22.520  43.398  1.00 34.13           O  
ATOM   1025  N   ARG A 143       5.954  25.156  39.017  1.00 30.56           N  
ATOM   1026  CA  ARG A 143       6.662  24.766  37.803  1.00 29.79           C  
ATOM   1027  C   ARG A 143       7.878  23.939  38.142  1.00 28.70           C  
ATOM   1028  O   ARG A 143       8.565  24.210  39.127  1.00 28.88           O  
ATOM   1029  CB  ARG A 143       7.142  25.991  37.040  1.00 29.90           C  
ATOM   1030  CG  ARG A 143       6.043  26.832  36.441  1.00 30.80           C  
ATOM   1031  CD  ARG A 143       6.591  27.992  35.636  1.00 30.70           C  
ATOM   1032  NE  ARG A 143       5.538  28.715  34.935  1.00 30.86           N  
ATOM   1033  CZ  ARG A 143       5.168  28.487  33.682  1.00 29.53           C  
ATOM   1034  NH1 ARG A 143       5.763  27.547  32.941  1.00 27.51           N  
ATOM   1035  NH2 ARG A 143       4.196  29.216  33.168  1.00 30.04           N  
ATOM   1036  N   LEU A 144       8.156  22.943  37.315  1.00 27.27           N  
ATOM   1037  CA  LEU A 144       9.319  22.102  37.518  1.00 26.47           C  
ATOM   1038  C   LEU A 144      10.220  22.148  36.297  1.00 25.40           C  
ATOM   1039  O   LEU A 144       9.755  22.330  35.172  1.00 25.39           O  
ATOM   1040  CB  LEU A 144       8.893  20.652  37.753  1.00 26.70           C  
ATOM   1041  CG  LEU A 144       7.922  20.416  38.915  1.00 27.15           C  
ATOM   1042  CD1 LEU A 144       7.575  18.921  39.059  1.00 27.40           C  
ATOM   1043  CD2 LEU A 144       8.488  20.956  40.221  1.00 27.42           C  
ATOM   1044  N   TYR A 145      11.511  21.974  36.527  1.00 23.90           N  
ATOM   1045  CA  TYR A 145      12.458  21.871  35.441  1.00 23.15           C  
ATOM   1046  C   TYR A 145      13.516  20.857  35.868  1.00 23.04           C  
ATOM   1047  O   TYR A 145      14.328  21.130  36.740  1.00 22.58           O  
ATOM   1048  CB  TYR A 145      13.080  23.235  35.107  1.00 23.01           C  
ATOM   1049  CG  TYR A 145      13.522  23.419  33.666  1.00 21.34           C  
ATOM   1050  CD1 TYR A 145      13.824  22.333  32.863  1.00 20.11           C  
ATOM   1051  CD2 TYR A 145      13.662  24.691  33.119  1.00 21.14           C  
ATOM   1052  CE1 TYR A 145      14.219  22.494  31.563  1.00 20.22           C  
ATOM   1053  CE2 TYR A 145      14.075  24.866  31.807  1.00 19.81           C  
ATOM   1054  CZ  TYR A 145      14.349  23.764  31.027  1.00 19.19           C  
ATOM   1055  OH  TYR A 145      14.736  23.903  29.699  1.00 18.36           O  
ATOM   1056  N   LEU A 146      13.461  19.666  35.287  1.00 22.75           N  
ATOM   1057  CA  LEU A 146      14.490  18.661  35.516  1.00 23.17           C  
ATOM   1058  C   LEU A 146      15.720  19.005  34.679  1.00 22.99           C  
ATOM   1059  O   LEU A 146      15.604  19.264  33.490  1.00 22.81           O  
ATOM   1060  CB  LEU A 146      13.980  17.282  35.115  1.00 23.33           C  
ATOM   1061  CG  LEU A 146      14.992  16.141  35.274  1.00 24.98           C  
ATOM   1062  CD1 LEU A 146      14.276  14.846  35.622  1.00 24.56           C  
ATOM   1063  CD2 LEU A 146      15.849  15.946  34.016  1.00 26.13           C  
ATOM   1064  N   GLN A 147      16.891  18.983  35.299  1.00 23.05           N  
ATOM   1065  CA  GLN A 147      18.135  19.314  34.619  1.00 23.65           C  
ATOM   1066  C   GLN A 147      19.158  18.394  35.231  1.00 23.86           C  
ATOM   1067  O   GLN A 147      19.573  18.597  36.364  1.00 24.61           O  
ATOM   1068  CB  GLN A 147      18.516  20.793  34.821  1.00 23.53           C  
ATOM   1069  CG  GLN A 147      17.386  21.770  34.461  1.00 24.34           C  
ATOM   1070  CD  GLN A 147      17.800  23.238  34.482  1.00 26.20           C  
ATOM   1071  OE1 GLN A 147      17.034  24.114  34.035  1.00 29.67           O  
ATOM   1072  NE2 GLN A 147      18.979  23.514  34.988  1.00 21.33           N  
ATOM   1073  N   GLN A 148      19.542  17.369  34.485  1.00 24.35           N  
ATOM   1074  CA  GLN A 148      20.393  16.314  35.006  1.00 24.70           C  
ATOM   1075  C   GLN A 148      21.319  15.753  33.964  1.00 25.16           C  
ATOM   1076  O   GLN A 148      20.898  15.378  32.866  1.00 24.21           O  
ATOM   1077  CB  GLN A 148      19.525  15.172  35.526  1.00 24.97           C  
ATOM   1078  CG  GLN A 148      20.317  13.940  35.953  1.00 25.54           C  
ATOM   1079  CD  GLN A 148      21.275  14.256  37.085  1.00 26.98           C  
ATOM   1080  OE1 GLN A 148      20.892  14.941  38.042  1.00 26.73           O  
ATOM   1081  NE2 GLN A 148      22.522  13.786  36.976  1.00 26.37           N  
ATOM   1082  N   THR A 149      22.592  15.704  34.321  1.00 25.94           N  
ATOM   1083  CA  THR A 149      23.603  15.134  33.466  1.00 27.43           C  
ATOM   1084  C   THR A 149      23.369  13.632  33.324  1.00 27.29           C  
ATOM   1085  O   THR A 149      23.081  12.965  34.303  1.00 27.40           O  
ATOM   1086  CB  THR A 149      24.990  15.430  34.075  1.00 27.91           C  
ATOM   1087  OG1 THR A 149      25.282  16.829  33.901  1.00 30.41           O  
ATOM   1088  CG2 THR A 149      26.078  14.776  33.276  1.00 30.12           C  
ATOM   1089  N   LEU A 150      23.461  13.117  32.100  1.00 27.79           N  
ATOM   1090  CA  LEU A 150      23.321  11.690  31.832  1.00 28.02           C  
ATOM   1091  C   LEU A 150      24.549  10.935  32.364  1.00 28.42           C  
ATOM   1092  O   LEU A 150      25.682  11.261  32.002  1.00 28.86           O  
ATOM   1093  CB  LEU A 150      23.194  11.435  30.326  1.00 28.08           C  
ATOM   1094  CG  LEU A 150      21.929  11.937  29.622  1.00 28.70           C  
ATOM   1095  CD1 LEU A 150      22.016  11.725  28.117  1.00 28.62           C  
ATOM   1096  CD2 LEU A 150      20.697  11.260  30.175  1.00 29.47           C  
ATOM   1097  N   ASN A 151      24.332   9.928  33.203  1.00 28.58           N  
ATOM   1098  CA  ASN A 151      25.434   9.156  33.781  1.00 28.79           C  
ATOM   1099  C   ASN A 151      25.194   7.636  33.782  1.00 29.24           C  
ATOM   1100  O   ASN A 151      24.197   7.163  33.238  1.00 29.60           O  
ATOM   1101  CB  ASN A 151      25.657   9.631  35.208  1.00 28.77           C  
ATOM   1102  CG  ASN A 151      24.459   9.367  36.084  1.00 28.05           C  
ATOM   1103  OD1 ASN A 151      23.936   8.246  36.126  1.00 29.02           O  
ATOM   1104  ND2 ASN A 151      24.000  10.396  36.772  1.00 26.99           N  
ATOM   1105  N   ASP A 152      26.083   6.885  34.437  1.00 29.71           N  
ATOM   1106  CA  ASP A 152      26.039   5.410  34.448  1.00 30.06           C  
ATOM   1107  C   ASP A 152      24.850   4.733  35.075  1.00 29.51           C  
ATOM   1108  O   ASP A 152      24.771   3.503  35.026  1.00 28.98           O  
ATOM   1109  CB  ASP A 152      27.199   4.829  35.250  1.00 30.99           C  
ATOM   1110  CG  ASP A 152      28.447   5.561  35.048  1.00 33.80           C  
ATOM   1111  OD1 ASP A 152      28.636   6.071  33.918  1.00 40.13           O  
ATOM   1112  OD2 ASP A 152      29.274   5.719  35.960  1.00 35.65           O  
ATOM   1113  N   THR A 153      23.959   5.468  35.722  1.00 28.96           N  
ATOM   1114  CA  THR A 153      22.831   4.792  36.359  1.00 28.42           C  
ATOM   1115  C   THR A 153      21.685   4.594  35.387  1.00 27.75           C  
ATOM   1116  O   THR A 153      20.730   3.909  35.712  1.00 27.68           O  
ATOM   1117  CB  THR A 153      22.330   5.552  37.584  1.00 28.53           C  
ATOM   1118  OG1 THR A 153      21.833   6.836  37.193  1.00 28.91           O  
ATOM   1119  CG2 THR A 153      23.473   5.855  38.540  1.00 29.18           C  
ATOM   1120  N   VAL A 154      21.766   5.171  34.194  1.00 26.76           N  
ATOM   1121  CA  VAL A 154      20.671   4.996  33.246  1.00 26.61           C  
ATOM   1122  C   VAL A 154      20.583   3.531  32.895  1.00 26.77           C  
ATOM   1123  O   VAL A 154      21.592   2.832  32.923  1.00 27.36           O  
ATOM   1124  CB  VAL A 154      20.838   5.826  31.964  1.00 26.05           C  
ATOM   1125  CG1 VAL A 154      20.914   7.279  32.312  1.00 26.14           C  
ATOM   1126  CG2 VAL A 154      22.071   5.383  31.182  1.00 25.62           C  
ATOM   1127  N   GLY A 155      19.379   3.072  32.568  1.00 26.71           N  
ATOM   1128  CA  GLY A 155      19.147   1.674  32.252  1.00 26.42           C  
ATOM   1129  C   GLY A 155      19.531   1.266  30.840  1.00 26.67           C  
ATOM   1130  O   GLY A 155      19.894   2.093  29.983  1.00 26.52           O  
ATOM   1131  N   ARG A 156      19.390  -0.028  30.599  1.00 26.49           N  
ATOM   1132  CA  ARG A 156      19.811  -0.684  29.364  1.00 26.54           C  
ATOM   1133  C   ARG A 156      19.305  -0.053  28.068  1.00 25.95           C  
ATOM   1134  O   ARG A 156      20.089   0.194  27.160  1.00 26.26           O  
ATOM   1135  CB  ARG A 156      19.429  -2.165  29.418  1.00 26.28           C  
ATOM   1136  N   LYS A 157      18.004   0.175  27.964  1.00 25.43           N  
ATOM   1137  CA  LYS A 157      17.460   0.777  26.756  1.00 25.11           C  
ATOM   1138  C   LYS A 157      18.026   2.198  26.517  1.00 25.50           C  
ATOM   1139  O   LYS A 157      18.249   2.595  25.372  1.00 25.14           O  
ATOM   1140  CB  LYS A 157      15.927   0.796  26.809  1.00 24.88           C  
ATOM   1141  CG  LYS A 157      15.255  -0.572  26.516  1.00 24.25           C  
ATOM   1142  N   ILE A 158      18.257   2.956  27.585  1.00 25.35           N  
ATOM   1143  CA  ILE A 158      18.766   4.326  27.432  1.00 25.61           C  
ATOM   1144  C   ILE A 158      20.205   4.250  26.971  1.00 25.76           C  
ATOM   1145  O   ILE A 158      20.661   5.058  26.166  1.00 25.39           O  
ATOM   1146  CB  ILE A 158      18.662   5.107  28.740  1.00 25.41           C  
ATOM   1147  CG1 ILE A 158      17.202   5.245  29.162  1.00 25.92           C  
ATOM   1148  CG2 ILE A 158      19.297   6.475  28.601  1.00 25.61           C  
ATOM   1149  CD1 ILE A 158      16.331   5.924  28.174  1.00 27.88           C  
ATOM   1150  N   VAL A 159      20.909   3.251  27.481  1.00 26.10           N  
ATOM   1151  CA  VAL A 159      22.276   3.010  27.079  1.00 26.57           C  
ATOM   1152  C   VAL A 159      22.279   2.703  25.585  1.00 26.40           C  
ATOM   1153  O   VAL A 159      23.074   3.248  24.840  1.00 26.32           O  
ATOM   1154  CB  VAL A 159      22.895   1.850  27.883  1.00 26.94           C  
ATOM   1155  CG1 VAL A 159      24.136   1.310  27.193  1.00 27.73           C  
ATOM   1156  CG2 VAL A 159      23.223   2.308  29.298  1.00 26.73           C  
ATOM   1157  N   MET A 160      21.363   1.852  25.145  1.00 26.48           N  
ATOM   1158  CA  MET A 160      21.270   1.518  23.721  1.00 26.52           C  
ATOM   1159  C   MET A 160      20.985   2.771  22.880  1.00 25.02           C  
ATOM   1160  O   MET A 160      21.600   2.986  21.845  1.00 24.31           O  
ATOM   1161  CB  MET A 160      20.183   0.476  23.485  1.00 27.05           C  
ATOM   1162  CG  MET A 160      20.540  -0.900  24.001  1.00 30.45           C  
ATOM   1163  SD  MET A 160      21.843  -1.730  23.058  1.00 34.87           S  
ATOM   1164  CE  MET A 160      20.957  -2.028  21.496  1.00 36.94           C  
ATOM   1165  N   ASP A 161      20.047   3.589  23.342  1.00 23.96           N  
ATOM   1166  CA  ASP A 161      19.699   4.831  22.665  1.00 23.14           C  
ATOM   1167  C   ASP A 161      20.890   5.781  22.550  1.00 21.93           C  
ATOM   1168  O   ASP A 161      21.167   6.323  21.480  1.00 21.41           O  
ATOM   1169  CB  ASP A 161      18.549   5.528  23.402  1.00 23.13           C  
ATOM   1170  CG  ASP A 161      17.250   4.762  23.293  1.00 24.08           C  
ATOM   1171  OD1 ASP A 161      17.182   3.812  22.478  1.00 21.27           O  
ATOM   1172  OD2 ASP A 161      16.248   5.035  23.980  1.00 25.87           O  
ATOM   1173  N   PHE A 162      21.575   5.973  23.671  1.00 20.59           N  
ATOM   1174  CA  PHE A 162      22.712   6.859  23.765  1.00 19.97           C  
ATOM   1175  C   PHE A 162      23.802   6.409  22.809  1.00 19.19           C  
ATOM   1176  O   PHE A 162      24.410   7.213  22.160  1.00 18.98           O  
ATOM   1177  CB  PHE A 162      23.223   6.859  25.220  1.00 20.44           C  
ATOM   1178  CG  PHE A 162      24.386   7.755  25.470  1.00 20.78           C  
ATOM   1179  CD1 PHE A 162      24.206   9.107  25.673  1.00 25.50           C  
ATOM   1180  CD2 PHE A 162      25.662   7.245  25.542  1.00 23.71           C  
ATOM   1181  CE1 PHE A 162      25.290   9.930  25.935  1.00 25.85           C  
ATOM   1182  CE2 PHE A 162      26.755   8.072  25.795  1.00 24.89           C  
ATOM   1183  CZ  PHE A 162      26.572   9.394  26.001  1.00 23.50           C  
ATOM   1184  N   LEU A 163      24.062   5.115  22.744  1.00 19.25           N  
ATOM   1185  CA  LEU A 163      25.084   4.597  21.838  1.00 19.42           C  
ATOM   1186  C   LEU A 163      24.715   4.804  20.361  1.00 18.63           C  
ATOM   1187  O   LEU A 163      25.585   4.831  19.493  1.00 18.21           O  
ATOM   1188  CB  LEU A 163      25.297   3.115  22.104  1.00 19.49           C  
ATOM   1189  CG  LEU A 163      25.988   2.812  23.422  1.00 20.88           C  
ATOM   1190  CD1 LEU A 163      25.980   1.319  23.651  1.00 22.44           C  
ATOM   1191  CD2 LEU A 163      27.407   3.368  23.396  1.00 21.73           C  
ATOM   1192  N   GLY A 164      23.419   4.917  20.104  1.00 18.01           N  
ATOM   1193  CA  GLY A 164      22.889   5.158  18.779  1.00 18.55           C  
ATOM   1194  C   GLY A 164      22.873   6.622  18.355  1.00 18.40           C  
ATOM   1195  O   GLY A 164      22.406   6.921  17.256  1.00 19.24           O  
ATOM   1196  N   PHE A 165      23.365   7.521  19.209  1.00 17.50           N  
ATOM   1197  CA  PHE A 165      23.493   8.913  18.831  1.00 17.67           C  
ATOM   1198  C   PHE A 165      24.497   8.955  17.663  1.00 17.49           C  
ATOM   1199  O   PHE A 165      25.293   8.028  17.497  1.00 16.10           O  
ATOM   1200  CB  PHE A 165      23.984   9.753  20.018  1.00 17.47           C  
ATOM   1201  CG  PHE A 165      22.932  10.004  21.098  1.00 18.51           C  
ATOM   1202  CD1 PHE A 165      21.645   9.479  21.009  1.00 19.26           C  
ATOM   1203  CD2 PHE A 165      23.242  10.784  22.203  1.00 18.52           C  
ATOM   1204  CE1 PHE A 165      20.697   9.730  21.996  1.00 18.44           C  
ATOM   1205  CE2 PHE A 165      22.303  11.030  23.199  1.00 18.52           C  
ATOM   1206  CZ  PHE A 165      21.032  10.500  23.100  1.00 18.90           C  
ATOM   1207  N   ASN A 166      24.466  10.009  16.854  1.00 17.77           N  
ATOM   1208  CA  ASN A 166      25.393  10.110  15.712  1.00 18.29           C  
ATOM   1209  C   ASN A 166      26.787  10.622  16.129  1.00 18.73           C  
ATOM   1210  O   ASN A 166      27.156  11.795  15.897  1.00 19.54           O  
ATOM   1211  CB  ASN A 166      24.793  10.972  14.598  1.00 17.92           C  
ATOM   1212  CG  ASN A 166      25.571  10.861  13.293  1.00 17.28           C  
ATOM   1213  OD1 ASN A 166      26.679  10.289  13.262  1.00 16.53           O  
ATOM   1214  ND2 ASN A 166      24.994  11.395  12.204  1.00 12.92           N  
ATOM   1215  N   TRP A 167      27.527   9.739  16.789  1.00 19.26           N  
ATOM   1216  CA  TRP A 167      28.867  10.035  17.264  1.00 19.76           C  
ATOM   1217  C   TRP A 167      29.785  10.266  16.084  1.00 19.88           C  
ATOM   1218  O   TRP A 167      30.731  11.031  16.169  1.00 19.35           O  
ATOM   1219  CB  TRP A 167      29.384   8.864  18.130  1.00 19.92           C  
ATOM   1220  CG  TRP A 167      28.556   8.728  19.351  1.00 20.39           C  
ATOM   1221  CD1 TRP A 167      27.686   7.727  19.656  1.00 20.85           C  
ATOM   1222  CD2 TRP A 167      28.445   9.686  20.400  1.00 20.99           C  
ATOM   1223  NE1 TRP A 167      27.059   7.995  20.851  1.00 21.18           N  
ATOM   1224  CE2 TRP A 167      27.509   9.194  21.325  1.00 20.70           C  
ATOM   1225  CE3 TRP A 167      29.065  10.916  20.664  1.00 21.55           C  
ATOM   1226  CZ2 TRP A 167      27.183   9.871  22.488  1.00 22.63           C  
ATOM   1227  CZ3 TRP A 167      28.731  11.589  21.804  1.00 21.78           C  
ATOM   1228  CH2 TRP A 167      27.789  11.071  22.706  1.00 22.79           C  
ATOM   1229  N   ASN A 168      29.529   9.577  14.979  1.00 20.07           N  
ATOM   1230  CA  ASN A 168      30.374   9.759  13.818  1.00 20.50           C  
ATOM   1231  C   ASN A 168      30.396  11.237  13.421  1.00 20.67           C  
ATOM   1232  O   ASN A 168      31.465  11.806  13.207  1.00 19.54           O  
ATOM   1233  CB  ASN A 168      29.917   8.930  12.628  1.00 20.87           C  
ATOM   1234  CG  ASN A 168      30.818   9.129  11.423  1.00 22.96           C  
ATOM   1235  OD1 ASN A 168      32.027   8.923  11.522  1.00 25.54           O  
ATOM   1236  ND2 ASN A 168      30.247   9.578  10.295  1.00 23.09           N  
ATOM   1237  N   TRP A 169      29.211  11.844  13.338  1.00 20.57           N  
ATOM   1238  CA  TRP A 169      29.106  13.226  12.917  1.00 20.23           C  
ATOM   1239  C   TRP A 169      29.653  14.188  13.972  1.00 20.59           C  
ATOM   1240  O   TRP A 169      30.367  15.118  13.634  1.00 20.09           O  
ATOM   1241  CB  TRP A 169      27.662  13.618  12.570  1.00 20.35           C  
ATOM   1242  CG  TRP A 169      27.542  15.101  12.238  1.00 19.49           C  
ATOM   1243  CD1 TRP A 169      27.769  15.693  11.026  1.00 19.03           C  
ATOM   1244  CD2 TRP A 169      27.203  16.157  13.137  1.00 20.25           C  
ATOM   1245  NE1 TRP A 169      27.578  17.052  11.117  1.00 20.36           N  
ATOM   1246  CE2 TRP A 169      27.244  17.366  12.406  1.00 19.45           C  
ATOM   1247  CE3 TRP A 169      26.874  16.207  14.492  1.00 20.60           C  
ATOM   1248  CZ2 TRP A 169      26.964  18.600  12.975  1.00 21.03           C  
ATOM   1249  CZ3 TRP A 169      26.614  17.433  15.064  1.00 23.09           C  
ATOM   1250  CH2 TRP A 169      26.649  18.621  14.297  1.00 23.61           C  
ATOM   1251  N   ILE A 170      29.326  13.979  15.239  1.00 20.47           N  
ATOM   1252  CA  ILE A 170      29.759  14.926  16.241  1.00 20.67           C  
ATOM   1253  C   ILE A 170      31.262  14.772  16.567  1.00 21.18           C  
ATOM   1254  O   ILE A 170      31.943  15.758  16.836  1.00 21.20           O  
ATOM   1255  CB  ILE A 170      28.842  14.892  17.483  1.00 20.61           C  
ATOM   1256  CG1 ILE A 170      28.900  16.231  18.221  1.00 20.05           C  
ATOM   1257  CG2 ILE A 170      29.191  13.755  18.402  1.00 19.89           C  
ATOM   1258  CD1 ILE A 170      27.865  16.353  19.329  1.00 21.00           C  
ATOM   1259  N   ASN A 171      31.780  13.556  16.527  1.00 20.74           N  
ATOM   1260  CA  ASN A 171      33.214  13.355  16.715  1.00 21.80           C  
ATOM   1261  C   ASN A 171      34.024  14.093  15.634  1.00 22.34           C  
ATOM   1262  O   ASN A 171      35.093  14.652  15.916  1.00 21.98           O  
ATOM   1263  CB  ASN A 171      33.581  11.857  16.718  1.00 21.55           C  
ATOM   1264  CG  ASN A 171      33.111  11.124  17.981  1.00 21.20           C  
ATOM   1265  OD1 ASN A 171      32.637  11.724  18.963  1.00 21.35           O  
ATOM   1266  ND2 ASN A 171      33.263   9.830  17.962  1.00 19.36           N  
ATOM   1267  N   LYS A 172      33.529  14.097  14.400  1.00 22.97           N  
ATOM   1268  CA  LYS A 172      34.218  14.847  13.353  1.00 24.09           C  
ATOM   1269  C   LYS A 172      34.167  16.342  13.656  1.00 23.61           C  
ATOM   1270  O   LYS A 172      35.166  17.041  13.511  1.00 23.54           O  
ATOM   1271  CB  LYS A 172      33.669  14.529  11.961  1.00 24.58           C  
ATOM   1272  CG  LYS A 172      34.087  13.163  11.491  1.00 27.56           C  
ATOM   1273  CD  LYS A 172      33.653  12.852  10.034  1.00 31.03           C  
ATOM   1274  CE  LYS A 172      34.323  11.576   9.565  1.00 33.01           C  
ATOM   1275  NZ  LYS A 172      34.357  11.406   8.070  1.00 36.89           N  
ATOM   1276  N   GLN A 173      33.019  16.834  14.109  1.00 23.74           N  
ATOM   1277  CA  GLN A 173      32.914  18.245  14.482  1.00 23.87           C  
ATOM   1278  C   GLN A 173      33.960  18.578  15.547  1.00 23.86           C  
ATOM   1279  O   GLN A 173      34.739  19.500  15.374  1.00 24.25           O  
ATOM   1280  CB  GLN A 173      31.517  18.590  14.993  1.00 23.63           C  
ATOM   1281  CG  GLN A 173      30.451  18.619  13.916  1.00 24.53           C  
ATOM   1282  CD  GLN A 173      30.753  19.634  12.851  1.00 25.08           C  
ATOM   1283  OE1 GLN A 173      31.194  20.740  13.157  1.00 26.69           O  
ATOM   1284  NE2 GLN A 173      30.512  19.273  11.601  1.00 23.36           N  
ATOM   1285  N   GLN A 174      33.963  17.822  16.635  1.00 23.63           N  
ATOM   1286  CA  GLN A 174      34.925  17.995  17.717  1.00 23.91           C  
ATOM   1287  C   GLN A 174      36.365  18.053  17.161  1.00 24.01           C  
ATOM   1288  O   GLN A 174      37.133  18.962  17.480  1.00 23.39           O  
ATOM   1289  CB  GLN A 174      34.783  16.840  18.717  1.00 23.67           C  
ATOM   1290  CG  GLN A 174      35.688  16.913  19.934  1.00 24.07           C  
ATOM   1291  CD  GLN A 174      35.595  15.668  20.799  1.00 25.12           C  
ATOM   1292  OE1 GLN A 174      35.229  14.602  20.312  1.00 25.70           O  
ATOM   1293  NE2 GLN A 174      35.901  15.803  22.084  1.00 23.63           N  
ATOM   1294  N   GLY A 175      36.706  17.080  16.334  1.00 23.75           N  
ATOM   1295  CA  GLY A 175      38.005  17.028  15.696  1.00 24.73           C  
ATOM   1296  C   GLY A 175      38.268  18.209  14.768  1.00 25.21           C  
ATOM   1297  O   GLY A 175      39.310  18.842  14.854  1.00 25.60           O  
ATOM   1298  N   LYS A 176      37.327  18.518  13.888  1.00 25.81           N  
ATOM   1299  CA  LYS A 176      37.491  19.634  12.961  1.00 26.88           C  
ATOM   1300  C   LYS A 176      37.719  20.997  13.638  1.00 26.95           C  
ATOM   1301  O   LYS A 176      38.490  21.803  13.136  1.00 26.74           O  
ATOM   1302  CB  LYS A 176      36.256  19.778  12.077  1.00 27.35           C  
ATOM   1303  CG  LYS A 176      36.093  18.716  11.009  1.00 29.87           C  
ATOM   1304  CD  LYS A 176      34.894  19.085  10.137  1.00 33.21           C  
ATOM   1305  CE  LYS A 176      33.948  17.932   9.961  1.00 35.30           C  
ATOM   1306  NZ  LYS A 176      32.558  18.388   9.643  1.00 37.22           N  
ATOM   1307  N   ARG A 177      37.031  21.257  14.749  1.00 26.93           N  
ATOM   1308  CA  ARG A 177      37.153  22.539  15.435  1.00 27.36           C  
ATOM   1309  C   ARG A 177      38.241  22.611  16.509  1.00 26.63           C  
ATOM   1310  O   ARG A 177      38.402  23.650  17.135  1.00 25.85           O  
ATOM   1311  CB  ARG A 177      35.832  22.902  16.114  1.00 27.86           C  
ATOM   1312  CG  ARG A 177      34.625  22.712  15.267  1.00 29.88           C  
ATOM   1313  CD  ARG A 177      34.653  23.460  13.973  1.00 32.39           C  
ATOM   1314  NE  ARG A 177      33.683  22.854  13.084  1.00 34.54           N  
ATOM   1315  CZ  ARG A 177      33.841  22.701  11.790  1.00 37.31           C  
ATOM   1316  NH1 ARG A 177      34.952  23.110  11.189  1.00 38.34           N  
ATOM   1317  NH2 ARG A 177      32.877  22.126  11.088  1.00 38.88           N  
ATOM   1318  N   GLY A 178      38.950  21.510  16.743  1.00 26.35           N  
ATOM   1319  CA  GLY A 178      39.998  21.470  17.753  1.00 25.46           C  
ATOM   1320  C   GLY A 178      39.473  21.514  19.176  1.00 25.27           C  
ATOM   1321  O   GLY A 178      40.213  21.818  20.123  1.00 25.46           O  
ATOM   1322  N   TRP A 179      38.199  21.202  19.359  1.00 24.30           N  
ATOM   1323  CA  TRP A 179      37.639  21.260  20.692  1.00 24.02           C  
ATOM   1324  C   TRP A 179      38.290  20.266  21.638  1.00 23.85           C  
ATOM   1325  O   TRP A 179      38.958  19.333  21.226  1.00 22.62           O  
ATOM   1326  CB  TRP A 179      36.136  21.011  20.674  1.00 23.73           C  
ATOM   1327  CG  TRP A 179      35.346  22.061  19.962  1.00 23.92           C  
ATOM   1328  CD1 TRP A 179      35.787  23.291  19.531  1.00 22.69           C  
ATOM   1329  CD2 TRP A 179      33.968  21.981  19.594  1.00 23.74           C  
ATOM   1330  NE1 TRP A 179      34.765  23.968  18.912  1.00 24.45           N  
ATOM   1331  CE2 TRP A 179      33.636  23.183  18.929  1.00 24.47           C  
ATOM   1332  CE3 TRP A 179      32.984  21.002  19.730  1.00 23.10           C  
ATOM   1333  CZ2 TRP A 179      32.379  23.422  18.414  1.00 23.69           C  
ATOM   1334  CZ3 TRP A 179      31.733  21.241  19.211  1.00 21.89           C  
ATOM   1335  CH2 TRP A 179      31.435  22.445  18.573  1.00 23.90           C  
ATOM   1336  N   GLY A 180      38.080  20.499  22.925  1.00 24.08           N  
ATOM   1337  CA  GLY A 180      38.488  19.558  23.941  1.00 24.08           C  
ATOM   1338  C   GLY A 180      37.437  18.476  24.103  1.00 24.64           C  
ATOM   1339  O   GLY A 180      36.618  18.234  23.202  1.00 24.66           O  
ATOM   1340  N   GLN A 181      37.437  17.830  25.261  1.00 24.77           N  
ATOM   1341  CA  GLN A 181      36.575  16.682  25.471  1.00 25.23           C  
ATOM   1342  C   GLN A 181      35.117  17.039  25.725  1.00 24.50           C  
ATOM   1343  O   GLN A 181      34.779  18.151  26.149  1.00 24.42           O  
ATOM   1344  CB  GLN A 181      37.094  15.847  26.646  1.00 25.76           C  
ATOM   1345  CG  GLN A 181      36.720  16.409  28.025  1.00 28.85           C  
ATOM   1346  CD  GLN A 181      37.046  15.434  29.156  1.00 33.38           C  
ATOM   1347  OE1 GLN A 181      38.186  15.003  29.293  1.00 36.10           O  
ATOM   1348  NE2 GLN A 181      36.044  15.085  29.958  1.00 36.04           N  
ATOM   1349  N   LEU A 182      34.262  16.078  25.423  1.00 23.71           N  
ATOM   1350  CA  LEU A 182      32.857  16.110  25.792  1.00 23.70           C  
ATOM   1351  C   LEU A 182      32.876  16.040  27.317  1.00 22.68           C  
ATOM   1352  O   LEU A 182      33.406  15.079  27.849  1.00 21.72           O  
ATOM   1353  CB  LEU A 182      32.179  14.836  25.273  1.00 23.82           C  
ATOM   1354  CG  LEU A 182      30.661  14.693  25.199  1.00 26.38           C  
ATOM   1355  CD1 LEU A 182      30.243  13.231  25.368  1.00 26.04           C  
ATOM   1356  CD2 LEU A 182      29.977  15.501  26.192  1.00 29.73           C  
ATOM   1357  N   THR A 183      32.323  17.031  28.021  1.00 21.93           N  
ATOM   1358  CA  THR A 183      32.300  16.971  29.484  1.00 21.44           C  
ATOM   1359  C   THR A 183      31.004  16.388  29.984  1.00 21.27           C  
ATOM   1360  O   THR A 183      30.972  15.766  31.032  1.00 21.29           O  
ATOM   1361  CB  THR A 183      32.490  18.362  30.150  1.00 21.73           C  
ATOM   1362  OG1 THR A 183      31.463  19.257  29.715  1.00 20.35           O  
ATOM   1363  CG2 THR A 183      33.796  19.015  29.725  1.00 20.91           C  
ATOM   1364  N   SER A 184      29.918  16.590  29.251  1.00 21.42           N  
ATOM   1365  CA  SER A 184      28.649  16.053  29.689  1.00 21.45           C  
ATOM   1366  C   SER A 184      27.537  16.272  28.714  1.00 21.46           C  
ATOM   1367  O   SER A 184      27.672  17.031  27.753  1.00 21.17           O  
ATOM   1368  CB  SER A 184      28.243  16.687  31.006  1.00 21.74           C  
ATOM   1369  OG  SER A 184      27.919  18.049  30.845  1.00 23.24           O  
ATOM   1370  N   ASN A 185      26.445  15.575  28.982  1.00 21.21           N  
ATOM   1371  CA  ASN A 185      25.216  15.712  28.245  1.00 22.29           C  
ATOM   1372  C   ASN A 185      24.154  16.005  29.273  1.00 22.08           C  
ATOM   1373  O   ASN A 185      23.886  15.184  30.135  1.00 22.25           O  
ATOM   1374  CB  ASN A 185      24.856  14.416  27.497  1.00 22.67           C  
ATOM   1375  CG  ASN A 185      25.885  14.037  26.454  1.00 23.57           C  
ATOM   1376  OD1 ASN A 185      26.646  13.097  26.655  1.00 27.51           O  
ATOM   1377  ND2 ASN A 185      25.905  14.754  25.329  1.00 24.27           N  
ATOM   1378  N   LEU A 186      23.574  17.189  29.202  1.00 22.01           N  
ATOM   1379  CA  LEU A 186      22.529  17.563  30.135  1.00 22.03           C  
ATOM   1380  C   LEU A 186      21.170  17.219  29.558  1.00 22.00           C  
ATOM   1381  O   LEU A 186      20.844  17.592  28.435  1.00 22.34           O  
ATOM   1382  CB  LEU A 186      22.578  19.065  30.423  1.00 21.68           C  
ATOM   1383  CG  LEU A 186      21.707  19.538  31.588  1.00 22.25           C  
ATOM   1384  CD1 LEU A 186      22.252  18.985  32.891  1.00 22.43           C  
ATOM   1385  CD2 LEU A 186      21.643  21.098  31.648  1.00 23.35           C  
ATOM   1386  N   LEU A 187      20.377  16.518  30.344  1.00 22.19           N  
ATOM   1387  CA  LEU A 187      19.009  16.198  29.979  1.00 21.95           C  
ATOM   1388  C   LEU A 187      18.149  17.286  30.603  1.00 21.91           C  
ATOM   1389  O   LEU A 187      18.232  17.521  31.823  1.00 21.61           O  
ATOM   1390  CB  LEU A 187      18.616  14.830  30.527  1.00 21.55           C  
ATOM   1391  CG  LEU A 187      17.129  14.488  30.477  1.00 22.78           C  
ATOM   1392  CD1 LEU A 187      16.616  14.429  29.054  1.00 23.66           C  
ATOM   1393  CD2 LEU A 187      16.866  13.143  31.174  1.00 22.84           C  
ATOM   1394  N   LEU A 188      17.348  17.956  29.770  1.00 21.56           N  
ATOM   1395  CA  LEU A 188      16.461  19.000  30.227  1.00 22.26           C  
ATOM   1396  C   LEU A 188      14.993  18.662  29.920  1.00 22.55           C  
ATOM   1397  O   LEU A 188      14.588  18.517  28.760  1.00 23.16           O  
ATOM   1398  CB  LEU A 188      16.827  20.327  29.562  1.00 22.84           C  
ATOM   1399  CG  LEU A 188      18.244  20.840  29.821  1.00 22.60           C  
ATOM   1400  CD1 LEU A 188      18.967  21.111  28.523  1.00 23.92           C  
ATOM   1401  CD2 LEU A 188      18.177  22.088  30.655  1.00 24.56           C  
ATOM   1402  N   ILE A 189      14.181  18.577  30.958  1.00 22.15           N  
ATOM   1403  CA  ILE A 189      12.769  18.315  30.756  1.00 22.34           C  
ATOM   1404  C   ILE A 189      11.996  19.395  31.460  1.00 22.37           C  
ATOM   1405  O   ILE A 189      12.072  19.528  32.692  1.00 22.77           O  
ATOM   1406  CB  ILE A 189      12.377  16.953  31.281  1.00 21.60           C  
ATOM   1407  CG1 ILE A 189      13.254  15.888  30.638  1.00 21.85           C  
ATOM   1408  CG2 ILE A 189      10.928  16.708  30.958  1.00 22.51           C  
ATOM   1409  CD1 ILE A 189      12.918  14.425  31.075  1.00 23.06           C  
ATOM   1410  N   GLY A 190      11.276  20.186  30.673  1.00 22.37           N  
ATOM   1411  CA  GLY A 190      10.587  21.336  31.206  1.00 22.29           C  
ATOM   1412  C   GLY A 190       9.124  21.342  30.902  1.00 22.48           C  
ATOM   1413  O   GLY A 190       8.652  20.633  30.007  1.00 22.39           O  
ATOM   1414  N   MET A 191       8.402  22.134  31.687  1.00 22.74           N  
ATOM   1415  CA  MET A 191       6.991  22.339  31.467  1.00 23.16           C  
ATOM   1416  C   MET A 191       6.838  23.482  30.478  1.00 22.94           C  
ATOM   1417  O   MET A 191       7.738  24.329  30.338  1.00 23.03           O  
ATOM   1418  CB  MET A 191       6.283  22.673  32.784  1.00 23.69           C  
ATOM   1419  CG  MET A 191       6.224  21.513  33.741  1.00 25.02           C  
ATOM   1420  SD  MET A 191       5.664  21.927  35.415  1.00 28.11           S  
ATOM   1421  CE  MET A 191       4.016  22.460  35.097  1.00 28.35           C  
ATOM   1422  N   GLU A 192       5.712  23.492  29.773  1.00 22.60           N  
ATOM   1423  CA  GLU A 192       5.410  24.544  28.810  1.00 22.83           C  
ATOM   1424  C   GLU A 192       5.495  25.895  29.490  1.00 22.51           C  
ATOM   1425  O   GLU A 192       5.062  26.046  30.614  1.00 22.41           O  
ATOM   1426  CB  GLU A 192       4.005  24.342  28.249  1.00 22.86           C  
ATOM   1427  CG  GLU A 192       2.925  24.367  29.315  1.00 24.36           C  
ATOM   1428  CD  GLU A 192       1.572  23.891  28.814  1.00 25.71           C  
ATOM   1429  OE1 GLU A 192       1.503  23.294  27.718  1.00 25.51           O  
ATOM   1430  OE2 GLU A 192       0.582  24.128  29.525  1.00 26.30           O  
ATOM   1431  N   GLY A 193       6.069  26.888  28.828  1.00 22.95           N  
ATOM   1432  CA  GLY A 193       6.185  28.199  29.444  1.00 22.50           C  
ATOM   1433  C   GLY A 193       7.465  28.414  30.254  1.00 22.36           C  
ATOM   1434  O   GLY A 193       7.756  29.544  30.602  1.00 23.08           O  
ATOM   1435  N   ASN A 194       8.219  27.361  30.566  1.00 21.60           N  
ATOM   1436  CA  ASN A 194       9.456  27.506  31.341  1.00 21.44           C  
ATOM   1437  C   ASN A 194      10.489  28.320  30.581  1.00 21.19           C  
ATOM   1438  O   ASN A 194      10.635  28.134  29.372  1.00 22.08           O  
ATOM   1439  CB  ASN A 194      10.099  26.147  31.629  1.00 21.05           C  
ATOM   1440  CG  ASN A 194       9.494  25.435  32.801  1.00 20.86           C  
ATOM   1441  OD1 ASN A 194       8.509  25.883  33.385  1.00 22.48           O  
ATOM   1442  ND2 ASN A 194      10.092  24.312  33.167  1.00 17.74           N  
ATOM   1443  N   VAL A 195      11.213  29.183  31.290  1.00 20.69           N  
ATOM   1444  CA  VAL A 195      12.268  29.993  30.701  1.00 20.84           C  
ATOM   1445  C   VAL A 195      13.572  29.854  31.450  1.00 20.06           C  
ATOM   1446  O   VAL A 195      13.601  29.874  32.681  1.00 20.75           O  
ATOM   1447  CB  VAL A 195      11.903  31.502  30.686  1.00 21.41           C  
ATOM   1448  CG1 VAL A 195      13.081  32.357  30.219  1.00 22.24           C  
ATOM   1449  CG2 VAL A 195      10.666  31.767  29.843  1.00 22.30           C  
ATOM   1450  N   THR A 196      14.651  29.673  30.702  1.00 19.51           N  
ATOM   1451  CA  THR A 196      15.993  29.737  31.257  1.00 19.52           C  
ATOM   1452  C   THR A 196      16.487  31.117  30.820  1.00 19.98           C  
ATOM   1453  O   THR A 196      16.653  31.352  29.620  1.00 19.56           O  
ATOM   1454  CB  THR A 196      16.896  28.677  30.675  1.00 19.26           C  
ATOM   1455  OG1 THR A 196      16.526  27.366  31.162  1.00 21.13           O  
ATOM   1456  CG2 THR A 196      18.309  28.886  31.185  1.00 19.85           C  
ATOM   1457  N   PRO A 197      16.627  32.043  31.767  1.00 20.27           N  
ATOM   1458  CA  PRO A 197      17.046  33.412  31.463  1.00 20.52           C  
ATOM   1459  C   PRO A 197      18.431  33.497  30.836  1.00 20.89           C  
ATOM   1460  O   PRO A 197      19.277  32.609  31.025  1.00 20.66           O  
ATOM   1461  CB  PRO A 197      17.018  34.099  32.825  1.00 21.22           C  
ATOM   1462  CG  PRO A 197      16.144  33.263  33.657  1.00 21.01           C  
ATOM   1463  CD  PRO A 197      16.309  31.872  33.189  1.00 20.28           C  
ATOM   1464  N   ALA A 198      18.633  34.577  30.089  1.00 20.28           N  
ATOM   1465  CA  ALA A 198      19.841  34.817  29.341  1.00 20.22           C  
ATOM   1466  C   ALA A 198      21.130  34.634  30.146  1.00 20.58           C  
ATOM   1467  O   ALA A 198      21.284  35.186  31.235  1.00 19.91           O  
ATOM   1468  CB  ALA A 198      19.791  36.222  28.759  1.00 20.52           C  
ATOM   1469  N   HIS A 199      22.062  33.891  29.563  1.00 20.87           N  
ATOM   1470  CA  HIS A 199      23.371  33.646  30.158  1.00 21.41           C  
ATOM   1471  C   HIS A 199      24.281  33.168  29.063  1.00 21.82           C  
ATOM   1472  O   HIS A 199      23.826  32.892  27.943  1.00 21.80           O  
ATOM   1473  CB  HIS A 199      23.305  32.534  31.198  1.00 21.44           C  
ATOM   1474  CG  HIS A 199      22.915  31.220  30.617  1.00 22.21           C  
ATOM   1475  ND1 HIS A 199      21.619  30.940  30.253  1.00 21.93           N  
ATOM   1476  CD2 HIS A 199      23.644  30.120  30.296  1.00 22.04           C  
ATOM   1477  CE1 HIS A 199      21.561  29.721  29.749  1.00 23.76           C  
ATOM   1478  NE2 HIS A 199      22.777  29.214  29.737  1.00 22.57           N  
ATOM   1479  N   TYR A 200      25.568  33.060  29.384  1.00 22.40           N  
ATOM   1480  CA  TYR A 200      26.536  32.456  28.469  1.00 22.34           C  
ATOM   1481  C   TYR A 200      27.225  31.316  29.197  1.00 22.03           C  
ATOM   1482  O   TYR A 200      27.328  31.330  30.425  1.00 21.90           O  
ATOM   1483  CB  TYR A 200      27.544  33.458  27.924  1.00 22.22           C  
ATOM   1484  CG  TYR A 200      28.517  34.051  28.924  1.00 22.16           C  
ATOM   1485  CD1 TYR A 200      29.746  33.454  29.171  1.00 21.36           C  
ATOM   1486  CD2 TYR A 200      28.236  35.246  29.565  1.00 22.58           C  
ATOM   1487  CE1 TYR A 200      30.638  33.997  30.052  1.00 21.48           C  
ATOM   1488  CE2 TYR A 200      29.128  35.806  30.462  1.00 21.46           C  
ATOM   1489  CZ  TYR A 200      30.334  35.189  30.695  1.00 22.03           C  
ATOM   1490  OH  TYR A 200      31.230  35.733  31.593  1.00 20.69           O  
ATOM   1491  N   ASP A 201      27.681  30.310  28.444  1.00 22.42           N  
ATOM   1492  CA  ASP A 201      28.381  29.152  29.048  1.00 22.10           C  
ATOM   1493  C   ASP A 201      29.801  29.142  28.531  1.00 21.96           C  
ATOM   1494  O   ASP A 201      30.018  29.601  27.433  1.00 22.26           O  
ATOM   1495  CB  ASP A 201      27.722  27.840  28.661  1.00 21.97           C  
ATOM   1496  CG  ASP A 201      26.311  27.714  29.181  1.00 21.99           C  
ATOM   1497  OD1 ASP A 201      26.126  27.649  30.421  1.00 22.61           O  
ATOM   1498  OD2 ASP A 201      25.330  27.624  28.412  1.00 19.35           O  
ATOM   1499  N   GLU A 202      30.769  28.620  29.283  1.00 21.66           N  
ATOM   1500  CA  GLU A 202      32.146  28.612  28.773  1.00 23.16           C  
ATOM   1501  C   GLU A 202      32.515  27.334  28.035  1.00 23.38           C  
ATOM   1502  O   GLU A 202      33.684  26.951  28.049  1.00 25.48           O  
ATOM   1503  CB  GLU A 202      33.178  28.774  29.897  1.00 23.46           C  
ATOM   1504  CG  GLU A 202      33.110  30.064  30.681  1.00 26.52           C  
ATOM   1505  CD  GLU A 202      34.233  30.132  31.704  1.00 28.11           C  
ATOM   1506  OE1 GLU A 202      34.207  29.387  32.698  1.00 29.06           O  
ATOM   1507  OE2 GLU A 202      35.148  30.920  31.490  1.00 31.04           O  
ATOM   1508  N   GLN A 203      31.538  26.632  27.476  1.00 22.70           N  
ATOM   1509  CA  GLN A 203      31.808  25.451  26.685  1.00 22.01           C  
ATOM   1510  C   GLN A 203      31.049  25.576  25.373  1.00 21.93           C  
ATOM   1511  O   GLN A 203      30.113  26.378  25.253  1.00 22.49           O  
ATOM   1512  CB  GLN A 203      31.409  24.169  27.427  1.00 22.02           C  
ATOM   1513  CG  GLN A 203      32.287  23.822  28.657  1.00 22.33           C  
ATOM   1514  CD  GLN A 203      32.103  22.379  29.165  1.00 23.14           C  
ATOM   1515  OE1 GLN A 203      31.948  21.448  28.370  1.00 21.46           O  
ATOM   1516  NE2 GLN A 203      32.138  22.203  30.489  1.00 21.21           N  
ATOM   1517  N   GLN A 204      31.486  24.807  24.380  1.00 21.81           N  
ATOM   1518  CA  GLN A 204      30.806  24.720  23.092  1.00 21.45           C  
ATOM   1519  C   GLN A 204      29.610  23.799  23.295  1.00 21.12           C  
ATOM   1520  O   GLN A 204      29.673  22.862  24.088  1.00 20.29           O  
ATOM   1521  CB  GLN A 204      31.740  24.140  22.040  1.00 21.75           C  
ATOM   1522  CG  GLN A 204      33.033  24.928  21.852  1.00 21.56           C  
ATOM   1523  CD  GLN A 204      32.856  26.198  21.000  1.00 21.57           C  
ATOM   1524  OE1 GLN A 204      31.741  26.609  20.692  1.00 20.30           O  
ATOM   1525  NE2 GLN A 204      33.966  26.776  20.594  1.00 18.60           N  
ATOM   1526  N   ASN A 205      28.522  24.060  22.580  1.00 21.25           N  
ATOM   1527  CA  ASN A 205      27.291  23.316  22.795  1.00 21.04           C  
ATOM   1528  C   ASN A 205      26.529  22.977  21.526  1.00 21.25           C  
ATOM   1529  O   ASN A 205      26.160  23.880  20.747  1.00 20.22           O  
ATOM   1530  CB  ASN A 205      26.387  24.194  23.654  1.00 21.95           C  
ATOM   1531  CG  ASN A 205      25.116  23.507  24.098  1.00 21.98           C  
ATOM   1532  OD1 ASN A 205      24.759  22.418  23.643  1.00 21.21           O  
ATOM   1533  ND2 ASN A 205      24.400  24.178  24.979  1.00 17.72           N  
ATOM   1534  N   PHE A 206      26.314  21.677  21.319  1.00 19.90           N  
ATOM   1535  CA  PHE A 206      25.339  21.230  20.354  1.00 19.77           C  
ATOM   1536  C   PHE A 206      24.085  20.869  21.150  1.00 19.25           C  
ATOM   1537  O   PHE A 206      24.094  19.939  21.959  1.00 19.15           O  
ATOM   1538  CB  PHE A 206      25.849  20.049  19.545  1.00 20.09           C  
ATOM   1539  CG  PHE A 206      26.786  20.442  18.454  1.00 19.77           C  
ATOM   1540  CD1 PHE A 206      26.371  21.294  17.453  1.00 22.21           C  
ATOM   1541  CD2 PHE A 206      28.079  19.973  18.435  1.00 20.21           C  
ATOM   1542  CE1 PHE A 206      27.213  21.643  16.434  1.00 22.06           C  
ATOM   1543  CE2 PHE A 206      28.941  20.336  17.418  1.00 20.66           C  
ATOM   1544  CZ  PHE A 206      28.504  21.190  16.427  1.00 22.18           C  
ATOM   1545  N   PHE A 207      23.009  21.596  20.869  1.00 18.42           N  
ATOM   1546  CA  PHE A 207      21.760  21.590  21.620  1.00 18.78           C  
ATOM   1547  C   PHE A 207      20.732  20.841  20.804  1.00 19.36           C  
ATOM   1548  O   PHE A 207      20.241  21.359  19.818  1.00 19.26           O  
ATOM   1549  CB  PHE A 207      21.366  23.063  21.836  1.00 18.70           C  
ATOM   1550  CG  PHE A 207      20.120  23.301  22.635  1.00 17.94           C  
ATOM   1551  CD1 PHE A 207      18.899  23.404  22.007  1.00 17.78           C  
ATOM   1552  CD2 PHE A 207      20.188  23.548  23.989  1.00 18.50           C  
ATOM   1553  CE1 PHE A 207      17.772  23.684  22.713  1.00 19.52           C  
ATOM   1554  CE2 PHE A 207      19.052  23.823  24.705  1.00 20.66           C  
ATOM   1555  CZ  PHE A 207      17.836  23.909  24.053  1.00 19.44           C  
ATOM   1556  N   ALA A 208      20.435  19.618  21.234  1.00 19.90           N  
ATOM   1557  CA  ALA A 208      19.628  18.670  20.469  1.00 20.17           C  
ATOM   1558  C   ALA A 208      18.210  18.541  20.991  1.00 20.52           C  
ATOM   1559  O   ALA A 208      17.971  17.946  22.047  1.00 20.61           O  
ATOM   1560  CB  ALA A 208      20.294  17.308  20.494  1.00 19.33           C  
ATOM   1561  N   GLN A 209      17.270  19.076  20.219  1.00 20.94           N  
ATOM   1562  CA  GLN A 209      15.880  19.062  20.627  1.00 20.82           C  
ATOM   1563  C   GLN A 209      15.227  17.712  20.323  1.00 20.75           C  
ATOM   1564  O   GLN A 209      15.401  17.129  19.224  1.00 19.59           O  
ATOM   1565  CB  GLN A 209      15.141  20.216  19.961  1.00 20.91           C  
ATOM   1566  CG  GLN A 209      13.735  20.431  20.463  1.00 20.52           C  
ATOM   1567  CD  GLN A 209      13.673  20.840  21.928  1.00 20.69           C  
ATOM   1568  OE1 GLN A 209      14.702  21.155  22.562  1.00 19.72           O  
ATOM   1569  NE2 GLN A 209      12.460  20.852  22.473  1.00 19.21           N  
ATOM   1570  N   ILE A 210      14.442  17.248  21.296  1.00 20.72           N  
ATOM   1571  CA  ILE A 210      13.853  15.922  21.252  1.00 21.43           C  
ATOM   1572  C   ILE A 210      12.334  15.911  21.292  1.00 21.72           C  
ATOM   1573  O   ILE A 210      11.728  15.195  20.534  1.00 22.12           O  
ATOM   1574  CB  ILE A 210      14.396  15.095  22.424  1.00 21.84           C  
ATOM   1575  CG1 ILE A 210      15.859  14.733  22.156  1.00 22.48           C  
ATOM   1576  CG2 ILE A 210      13.581  13.832  22.622  1.00 21.83           C  
ATOM   1577  CD1 ILE A 210      16.631  14.354  23.382  1.00 24.34           C  
ATOM   1578  N   LYS A 211      11.728  16.677  22.188  1.00 22.08           N  
ATOM   1579  CA  LYS A 211      10.279  16.715  22.319  1.00 21.72           C  
ATOM   1580  C   LYS A 211       9.858  18.130  22.564  1.00 21.67           C  
ATOM   1581  O   LYS A 211      10.468  18.841  23.372  1.00 20.87           O  
ATOM   1582  CB  LYS A 211       9.797  15.856  23.487  1.00 22.44           C  
ATOM   1583  CG  LYS A 211       8.267  15.562  23.479  1.00 23.29           C  
ATOM   1584  CD  LYS A 211       7.791  15.022  24.824  1.00 25.02           C  
ATOM   1585  CE  LYS A 211       6.494  14.215  24.757  1.00 26.00           C  
ATOM   1586  NZ  LYS A 211       5.561  14.522  23.634  1.00 26.43           N  
ATOM   1587  N   GLY A 212       8.798  18.541  21.875  1.00 21.35           N  
ATOM   1588  CA  GLY A 212       8.306  19.891  21.994  1.00 21.71           C  
ATOM   1589  C   GLY A 212       9.195  20.906  21.297  1.00 21.63           C  
ATOM   1590  O   GLY A 212      10.150  20.572  20.591  1.00 21.32           O  
ATOM   1591  N   TYR A 213       8.871  22.166  21.522  1.00 22.35           N  
ATOM   1592  CA  TYR A 213       9.533  23.279  20.862  1.00 22.42           C  
ATOM   1593  C   TYR A 213      10.028  24.293  21.868  1.00 22.33           C  
ATOM   1594  O   TYR A 213       9.340  24.589  22.853  1.00 21.55           O  
ATOM   1595  CB  TYR A 213       8.556  23.951  19.916  1.00 23.46           C  
ATOM   1596  CG  TYR A 213       8.114  23.034  18.815  1.00 24.81           C  
ATOM   1597  CD1 TYR A 213       7.100  22.112  19.020  1.00 28.16           C  
ATOM   1598  CD2 TYR A 213       8.751  23.051  17.589  1.00 26.74           C  
ATOM   1599  CE1 TYR A 213       6.716  21.237  18.011  1.00 28.91           C  
ATOM   1600  CE2 TYR A 213       8.378  22.193  16.585  1.00 28.63           C  
ATOM   1601  CZ  TYR A 213       7.366  21.295  16.795  1.00 29.44           C  
ATOM   1602  OH  TYR A 213       7.013  20.456  15.756  1.00 33.67           O  
ATOM   1603  N   LYS A 214      11.239  24.788  21.609  1.00 21.60           N  
ATOM   1604  CA  LYS A 214      11.875  25.793  22.414  1.00 21.89           C  
ATOM   1605  C   LYS A 214      12.312  26.947  21.528  1.00 21.62           C  
ATOM   1606  O   LYS A 214      12.878  26.747  20.442  1.00 22.07           O  
ATOM   1607  CB  LYS A 214      13.103  25.239  23.140  1.00 22.10           C  
ATOM   1608  CG  LYS A 214      12.796  24.385  24.338  1.00 22.63           C  
ATOM   1609  CD  LYS A 214      14.103  23.893  24.964  1.00 24.24           C  
ATOM   1610  CE  LYS A 214      13.923  23.478  26.402  1.00 23.54           C  
ATOM   1611  NZ  LYS A 214      15.169  22.872  26.951  1.00 22.10           N  
ATOM   1612  N   ARG A 215      12.007  28.156  21.974  1.00 20.97           N  
ATOM   1613  CA  ARG A 215      12.447  29.347  21.277  1.00 20.73           C  
ATOM   1614  C   ARG A 215      13.778  29.724  21.900  1.00 20.03           C  
ATOM   1615  O   ARG A 215      13.885  29.828  23.113  1.00 19.70           O  
ATOM   1616  CB  ARG A 215      11.461  30.470  21.493  1.00 21.30           C  
ATOM   1617  CG  ARG A 215      11.754  31.760  20.726  1.00 22.21           C  
ATOM   1618  CD  ARG A 215      11.177  32.925  21.473  1.00 24.71           C  
ATOM   1619  NE  ARG A 215      11.122  34.156  20.715  1.00 25.47           N  
ATOM   1620  CZ  ARG A 215      10.479  35.235  21.130  1.00 26.28           C  
ATOM   1621  NH1 ARG A 215       9.844  35.245  22.299  1.00 26.07           N  
ATOM   1622  NH2 ARG A 215      10.483  36.314  20.384  1.00 28.83           N  
ATOM   1623  N   CYS A 216      14.794  29.877  21.074  1.00 19.45           N  
ATOM   1624  CA  CYS A 216      16.116  30.219  21.554  1.00 19.58           C  
ATOM   1625  C   CYS A 216      16.503  31.587  20.993  1.00 19.92           C  
ATOM   1626  O   CYS A 216      16.503  31.774  19.789  1.00 20.16           O  
ATOM   1627  CB  CYS A 216      17.110  29.186  21.073  1.00 20.01           C  
ATOM   1628  SG  CYS A 216      16.693  27.450  21.462  1.00 21.39           S  
ATOM   1629  N   ILE A 217      16.812  32.530  21.878  1.00 19.28           N  
ATOM   1630  CA  ILE A 217      17.286  33.845  21.504  1.00 19.58           C  
ATOM   1631  C   ILE A 217      18.742  33.961  21.937  1.00 19.21           C  
ATOM   1632  O   ILE A 217      19.055  33.849  23.126  1.00 19.05           O  
ATOM   1633  CB  ILE A 217      16.424  34.943  22.168  1.00 19.88           C  
ATOM   1634  CG1 ILE A 217      14.926  34.687  21.878  1.00 20.56           C  
ATOM   1635  CG2 ILE A 217      16.803  36.312  21.627  1.00 20.25           C  
ATOM   1636  CD1 ILE A 217      13.984  35.692  22.488  1.00 20.99           C  
ATOM   1637  N   LEU A 218      19.620  34.176  20.965  1.00 19.01           N  
ATOM   1638  CA  LEU A 218      21.048  34.271  21.222  1.00 19.61           C  
ATOM   1639  C   LEU A 218      21.568  35.682  20.970  1.00 20.43           C  
ATOM   1640  O   LEU A 218      21.018  36.414  20.136  1.00 19.76           O  
ATOM   1641  CB  LEU A 218      21.816  33.329  20.308  1.00 19.66           C  
ATOM   1642  CG  LEU A 218      21.906  31.881  20.778  1.00 19.74           C  
ATOM   1643  CD1 LEU A 218      20.549  31.237  20.905  1.00 20.56           C  
ATOM   1644  CD2 LEU A 218      22.733  31.099  19.798  1.00 21.32           C  
ATOM   1645  N   PHE A 219      22.626  36.046  21.700  1.00 20.11           N  
ATOM   1646  CA  PHE A 219      23.282  37.324  21.524  1.00 20.96           C  
ATOM   1647  C   PHE A 219      24.805  37.078  21.453  1.00 21.19           C  
ATOM   1648  O   PHE A 219      25.351  36.313  22.257  1.00 21.20           O  
ATOM   1649  CB  PHE A 219      22.942  38.304  22.678  1.00 20.97           C  
ATOM   1650  CG  PHE A 219      21.463  38.456  22.954  1.00 20.44           C  
ATOM   1651  CD1 PHE A 219      20.821  37.637  23.846  1.00 21.46           C  
ATOM   1652  CD2 PHE A 219      20.724  39.447  22.334  1.00 22.49           C  
ATOM   1653  CE1 PHE A 219      19.472  37.790  24.108  1.00 22.33           C  
ATOM   1654  CE2 PHE A 219      19.387  39.605  22.605  1.00 21.32           C  
ATOM   1655  CZ  PHE A 219      18.760  38.773  23.480  1.00 21.50           C  
ATOM   1656  N   PRO A 220      25.485  37.705  20.498  1.00 21.20           N  
ATOM   1657  CA  PRO A 220      26.936  37.541  20.368  1.00 21.72           C  
ATOM   1658  C   PRO A 220      27.683  38.108  21.569  1.00 21.31           C  
ATOM   1659  O   PRO A 220      27.165  38.972  22.280  1.00 20.90           O  
ATOM   1660  CB  PRO A 220      27.302  38.341  19.120  1.00 21.41           C  
ATOM   1661  CG  PRO A 220      26.020  38.781  18.510  1.00 23.12           C  
ATOM   1662  CD  PRO A 220      24.938  38.637  19.508  1.00 22.22           C  
ATOM   1663  N   PRO A 221      28.884  37.594  21.806  1.00 21.46           N  
ATOM   1664  CA  PRO A 221      29.721  38.053  22.918  1.00 21.33           C  
ATOM   1665  C   PRO A 221      29.961  39.556  22.940  1.00 21.04           C  
ATOM   1666  O   PRO A 221      30.220  40.096  24.009  1.00 20.68           O  
ATOM   1667  CB  PRO A 221      31.032  37.325  22.681  1.00 21.42           C  
ATOM   1668  CG  PRO A 221      30.656  36.134  21.939  1.00 22.42           C  
ATOM   1669  CD  PRO A 221      29.522  36.510  21.041  1.00 21.53           C  
ATOM   1670  N   ASP A 222      29.877  40.225  21.792  1.00 21.47           N  
ATOM   1671  CA  ASP A 222      30.128  41.669  21.749  1.00 21.80           C  
ATOM   1672  C   ASP A 222      28.946  42.464  22.271  1.00 21.74           C  
ATOM   1673  O   ASP A 222      28.970  43.685  22.261  1.00 22.16           O  
ATOM   1674  CB  ASP A 222      30.568  42.148  20.355  1.00 21.85           C  
ATOM   1675  CG  ASP A 222      29.433  42.151  19.325  1.00 24.83           C  
ATOM   1676  OD1 ASP A 222      28.311  41.668  19.585  1.00 25.32           O  
ATOM   1677  OD2 ASP A 222      29.595  42.607  18.186  1.00 29.30           O  
ATOM   1678  N   GLN A 223      27.916  41.775  22.748  1.00 21.94           N  
ATOM   1679  CA  GLN A 223      26.794  42.453  23.388  1.00 22.17           C  
ATOM   1680  C   GLN A 223      26.897  42.388  24.928  1.00 21.93           C  
ATOM   1681  O   GLN A 223      25.926  42.681  25.660  1.00 21.70           O  
ATOM   1682  CB  GLN A 223      25.456  41.911  22.832  1.00 22.84           C  
ATOM   1683  CG  GLN A 223      25.149  42.508  21.412  1.00 25.34           C  
ATOM   1684  CD  GLN A 223      23.728  42.283  20.965  1.00 27.81           C  
ATOM   1685  OE1 GLN A 223      22.801  42.473  21.750  1.00 30.00           O  
ATOM   1686  NE2 GLN A 223      23.543  41.850  19.709  1.00 29.69           N  
ATOM   1687  N   PHE A 224      28.079  42.027  25.417  1.00 21.04           N  
ATOM   1688  CA  PHE A 224      28.363  42.035  26.860  1.00 21.41           C  
ATOM   1689  C   PHE A 224      27.886  43.350  27.527  1.00 21.57           C  
ATOM   1690  O   PHE A 224      27.240  43.315  28.561  1.00 21.34           O  
ATOM   1691  CB  PHE A 224      29.883  41.874  27.076  1.00 20.95           C  
ATOM   1692  CG  PHE A 224      30.304  41.773  28.529  1.00 21.82           C  
ATOM   1693  CD1 PHE A 224      30.452  42.912  29.319  1.00 19.33           C  
ATOM   1694  CD2 PHE A 224      30.595  40.552  29.089  1.00 20.01           C  
ATOM   1695  CE1 PHE A 224      30.870  42.807  30.630  1.00 20.89           C  
ATOM   1696  CE2 PHE A 224      31.025  40.449  30.397  1.00 20.59           C  
ATOM   1697  CZ  PHE A 224      31.151  41.579  31.171  1.00 20.99           C  
ATOM   1698  N   GLU A 225      28.195  44.495  26.916  1.00 22.10           N  
ATOM   1699  CA  GLU A 225      27.823  45.800  27.466  1.00 23.01           C  
ATOM   1700  C   GLU A 225      26.337  46.042  27.574  1.00 22.26           C  
ATOM   1701  O   GLU A 225      25.928  46.946  28.311  1.00 21.91           O  
ATOM   1702  CB  GLU A 225      28.401  46.935  26.624  1.00 24.27           C  
ATOM   1703  CG  GLU A 225      29.886  47.133  26.857  1.00 29.26           C  
ATOM   1704  CD  GLU A 225      30.312  48.579  27.062  1.00 35.91           C  
ATOM   1705  OE1 GLU A 225      29.745  49.317  27.942  1.00 39.92           O  
ATOM   1706  OE2 GLU A 225      31.281  48.958  26.368  1.00 40.78           O  
ATOM   1707  N   CYS A 226      25.539  45.258  26.836  1.00 21.15           N  
ATOM   1708  CA  CYS A 226      24.081  45.396  26.851  1.00 21.01           C  
ATOM   1709  C   CYS A 226      23.359  44.417  27.768  1.00 20.67           C  
ATOM   1710  O   CYS A 226      22.159  44.601  28.043  1.00 18.85           O  
ATOM   1711  CB  CYS A 226      23.520  45.190  25.447  1.00 20.88           C  
ATOM   1712  SG  CYS A 226      24.194  46.296  24.190  1.00 22.39           S  
ATOM   1713  N   LEU A 227      24.085  43.399  28.256  1.00 20.56           N  
ATOM   1714  CA  LEU A 227      23.461  42.304  28.985  1.00 20.48           C  
ATOM   1715  C   LEU A 227      23.795  42.185  30.466  1.00 20.42           C  
ATOM   1716  O   LEU A 227      23.180  41.398  31.187  1.00 20.78           O  
ATOM   1717  CB  LEU A 227      23.737  41.003  28.232  1.00 21.20           C  
ATOM   1718  CG  LEU A 227      22.865  40.993  26.963  1.00 22.96           C  
ATOM   1719  CD1 LEU A 227      23.373  40.023  25.929  1.00 24.99           C  
ATOM   1720  CD2 LEU A 227      21.420  40.655  27.323  1.00 24.79           C  
ATOM   1721  N   TYR A 228      24.793  42.939  30.901  1.00 20.08           N  
ATOM   1722  CA  TYR A 228      25.060  43.127  32.303  1.00 19.66           C  
ATOM   1723  C   TYR A 228      25.061  41.858  33.165  1.00 19.95           C  
ATOM   1724  O   TYR A 228      24.229  41.697  34.058  1.00 19.69           O  
ATOM   1725  CB  TYR A 228      24.050  44.137  32.857  1.00 19.77           C  
ATOM   1726  CG  TYR A 228      24.028  45.481  32.119  1.00 19.37           C  
ATOM   1727  CD1 TYR A 228      24.836  46.513  32.515  1.00 18.65           C  
ATOM   1728  CD2 TYR A 228      23.180  45.697  31.036  1.00 19.82           C  
ATOM   1729  CE1 TYR A 228      24.819  47.759  31.862  1.00 20.56           C  
ATOM   1730  CE2 TYR A 228      23.143  46.920  30.380  1.00 20.78           C  
ATOM   1731  CZ  TYR A 228      23.962  47.956  30.801  1.00 20.88           C  
ATOM   1732  OH  TYR A 228      23.944  49.174  30.152  1.00 19.73           O  
ATOM   1733  N   PRO A 229      26.028  40.981  32.941  1.00 19.99           N  
ATOM   1734  CA  PRO A 229      26.140  39.781  33.768  1.00 20.44           C  
ATOM   1735  C   PRO A 229      26.481  40.141  35.196  1.00 19.99           C  
ATOM   1736  O   PRO A 229      27.130  41.166  35.451  1.00 20.03           O  
ATOM   1737  CB  PRO A 229      27.334  39.043  33.157  1.00 20.11           C  
ATOM   1738  CG  PRO A 229      28.125  40.130  32.541  1.00 21.04           C  
ATOM   1739  CD  PRO A 229      27.099  41.050  31.935  1.00 19.79           C  
ATOM   1740  N   TYR A 230      26.044  39.294  36.115  1.00 19.50           N  
ATOM   1741  CA  TYR A 230      26.348  39.458  37.511  1.00 19.17           C  
ATOM   1742  C   TYR A 230      27.860  39.464  37.704  1.00 19.14           C  
ATOM   1743  O   TYR A 230      28.598  39.060  36.832  1.00 18.83           O  
ATOM   1744  CB  TYR A 230      25.746  38.313  38.320  1.00 18.51           C  
ATOM   1745  CG  TYR A 230      24.253  38.411  38.531  1.00 18.95           C  
ATOM   1746  CD1 TYR A 230      23.368  37.949  37.560  1.00 18.39           C  
ATOM   1747  CD2 TYR A 230      23.719  38.969  39.707  1.00 18.65           C  
ATOM   1748  CE1 TYR A 230      22.001  38.006  37.751  1.00 17.34           C  
ATOM   1749  CE2 TYR A 230      22.337  39.043  39.903  1.00 17.05           C  
ATOM   1750  CZ  TYR A 230      21.492  38.550  38.909  1.00 17.79           C  
ATOM   1751  OH  TYR A 230      20.127  38.601  39.051  1.00 19.77           O  
ATOM   1752  N   PRO A 231      28.316  39.963  38.843  1.00 19.95           N  
ATOM   1753  CA  PRO A 231      29.722  39.829  39.213  1.00 20.42           C  
ATOM   1754  C   PRO A 231      30.157  38.339  39.187  1.00 20.93           C  
ATOM   1755  O   PRO A 231      29.345  37.463  39.506  1.00 20.71           O  
ATOM   1756  CB  PRO A 231      29.755  40.369  40.642  1.00 20.70           C  
ATOM   1757  CG  PRO A 231      28.588  41.341  40.716  1.00 20.76           C  
ATOM   1758  CD  PRO A 231      27.528  40.701  39.845  1.00 19.53           C  
ATOM   1759  N   VAL A 232      31.413  38.067  38.831  1.00 20.93           N  
ATOM   1760  CA  VAL A 232      31.906  36.685  38.742  1.00 21.31           C  
ATOM   1761  C   VAL A 232      31.722  35.843  40.014  1.00 20.95           C  
ATOM   1762  O   VAL A 232      31.431  34.650  39.934  1.00 20.50           O  
ATOM   1763  CB  VAL A 232      33.398  36.655  38.304  1.00 21.35           C  
ATOM   1764  CG1 VAL A 232      34.029  35.280  38.552  1.00 22.23           C  
ATOM   1765  CG2 VAL A 232      33.533  37.031  36.850  1.00 21.71           C  
ATOM   1766  N   HIS A 233      31.872  36.455  41.181  1.00 21.10           N  
ATOM   1767  CA  HIS A 233      31.742  35.721  42.438  1.00 21.01           C  
ATOM   1768  C   HIS A 233      30.302  35.571  42.944  1.00 20.95           C  
ATOM   1769  O   HIS A 233      30.045  34.864  43.914  1.00 19.92           O  
ATOM   1770  CB  HIS A 233      32.606  36.363  43.501  1.00 21.12           C  
ATOM   1771  CG  HIS A 233      34.063  36.342  43.174  1.00 21.52           C  
ATOM   1772  ND1 HIS A 233      34.720  37.424  42.625  1.00 22.78           N  
ATOM   1773  CD2 HIS A 233      34.993  35.368  43.318  1.00 22.27           C  
ATOM   1774  CE1 HIS A 233      35.994  37.114  42.446  1.00 24.00           C  
ATOM   1775  NE2 HIS A 233      36.186  35.870  42.857  1.00 23.34           N  
ATOM   1776  N   HIS A 234      29.364  36.236  42.288  1.00 20.94           N  
ATOM   1777  CA  HIS A 234      27.959  36.081  42.630  1.00 21.27           C  
ATOM   1778  C   HIS A 234      27.493  34.722  42.103  1.00 21.28           C  
ATOM   1779  O   HIS A 234      28.022  34.233  41.107  1.00 21.02           O  
ATOM   1780  CB  HIS A 234      27.169  37.203  41.989  1.00 21.52           C  
ATOM   1781  CG  HIS A 234      25.730  37.253  42.374  1.00 21.54           C  
ATOM   1782  ND1 HIS A 234      24.769  36.498  41.740  1.00 21.95           N  
ATOM   1783  CD2 HIS A 234      25.073  38.028  43.269  1.00 22.67           C  
ATOM   1784  CE1 HIS A 234      23.585  36.779  42.254  1.00 22.38           C  
ATOM   1785  NE2 HIS A 234      23.743  37.700  43.187  1.00 21.91           N  
ATOM   1786  N   PRO A 235      26.551  34.087  42.792  1.00 21.11           N  
ATOM   1787  CA  PRO A 235      25.999  32.809  42.338  1.00 21.46           C  
ATOM   1788  C   PRO A 235      25.461  32.835  40.916  1.00 21.10           C  
ATOM   1789  O   PRO A 235      25.517  31.802  40.244  1.00 20.37           O  
ATOM   1790  CB  PRO A 235      24.860  32.551  43.325  1.00 21.90           C  
ATOM   1791  CG  PRO A 235      25.316  33.240  44.574  1.00 22.00           C  
ATOM   1792  CD  PRO A 235      26.007  34.485  44.100  1.00 21.41           C  
ATOM   1793  N   CYS A 236      24.997  33.989  40.452  1.00 20.41           N  
ATOM   1794  CA  CYS A 236      24.456  34.077  39.110  1.00 20.17           C  
ATOM   1795  C   CYS A 236      25.503  34.554  38.107  1.00 20.00           C  
ATOM   1796  O   CYS A 236      25.180  35.111  37.061  1.00 20.30           O  
ATOM   1797  CB  CYS A 236      23.195  34.924  39.090  1.00 19.66           C  
ATOM   1798  SG  CYS A 236      21.914  34.209  40.133  1.00 20.71           S  
ATOM   1799  N   ASP A 237      26.768  34.311  38.433  1.00 19.87           N  
ATOM   1800  CA  ASP A 237      27.857  34.498  37.485  1.00 19.60           C  
ATOM   1801  C   ASP A 237      27.459  33.915  36.105  1.00 19.48           C  
ATOM   1802  O   ASP A 237      26.883  32.834  36.020  1.00 18.94           O  
ATOM   1803  CB  ASP A 237      29.075  33.789  38.031  1.00 19.20           C  
ATOM   1804  CG  ASP A 237      30.268  33.842  37.107  1.00 20.58           C  
ATOM   1805  OD1 ASP A 237      30.477  34.871  36.373  1.00 18.56           O  
ATOM   1806  OD2 ASP A 237      31.070  32.868  37.077  1.00 19.51           O  
ATOM   1807  N   ARG A 238      27.749  34.675  35.056  1.00 19.85           N  
ATOM   1808  CA  ARG A 238      27.459  34.332  33.664  1.00 20.90           C  
ATOM   1809  C   ARG A 238      26.002  34.572  33.247  1.00 20.67           C  
ATOM   1810  O   ARG A 238      25.709  34.491  32.059  1.00 21.20           O  
ATOM   1811  CB  ARG A 238      27.854  32.876  33.319  1.00 21.44           C  
ATOM   1812  CG  ARG A 238      29.330  32.585  33.482  1.00 21.04           C  
ATOM   1813  CD  ARG A 238      29.710  31.150  33.145  1.00 22.38           C  
ATOM   1814  NE  ARG A 238      29.080  30.243  34.085  1.00 23.86           N  
ATOM   1815  CZ  ARG A 238      27.937  29.584  33.874  1.00 25.81           C  
ATOM   1816  NH1 ARG A 238      27.262  29.686  32.712  1.00 24.18           N  
ATOM   1817  NH2 ARG A 238      27.471  28.810  34.849  1.00 27.18           N  
ATOM   1818  N   GLN A 239      25.105  34.845  34.190  1.00 19.94           N  
ATOM   1819  CA  GLN A 239      23.722  35.141  33.833  1.00 20.58           C  
ATOM   1820  C   GLN A 239      23.535  36.661  33.740  1.00 20.50           C  
ATOM   1821  O   GLN A 239      24.219  37.402  34.446  1.00 20.63           O  
ATOM   1822  CB  GLN A 239      22.735  34.591  34.863  1.00 20.32           C  
ATOM   1823  CG  GLN A 239      23.159  33.314  35.594  1.00 20.84           C  
ATOM   1824  CD  GLN A 239      23.367  32.137  34.673  1.00 21.23           C  
ATOM   1825  OE1 GLN A 239      22.434  31.675  34.014  1.00 21.22           O  
ATOM   1826  NE2 GLN A 239      24.591  31.655  34.616  1.00 20.93           N  
ATOM   1827  N   SER A 240      22.600  37.112  32.900  1.00 20.07           N  
ATOM   1828  CA  SER A 240      22.282  38.533  32.768  1.00 20.18           C  
ATOM   1829  C   SER A 240      21.498  39.027  33.969  1.00 20.71           C  
ATOM   1830  O   SER A 240      20.619  38.316  34.467  1.00 20.85           O  
ATOM   1831  CB  SER A 240      21.405  38.776  31.539  1.00 20.29           C  
ATOM   1832  OG  SER A 240      21.007  40.137  31.454  1.00 21.43           O  
ATOM   1833  N   GLN A 241      21.793  40.246  34.426  1.00 20.46           N  
ATOM   1834  CA  GLN A 241      21.013  40.839  35.496  1.00 20.42           C  
ATOM   1835  C   GLN A 241      19.711  41.433  34.965  1.00 20.26           C  
ATOM   1836  O   GLN A 241      18.839  41.767  35.726  1.00 19.62           O  
ATOM   1837  CB  GLN A 241      21.770  41.949  36.201  1.00 20.32           C  
ATOM   1838  CG  GLN A 241      23.019  41.544  36.912  1.00 20.58           C  
ATOM   1839  CD  GLN A 241      23.771  42.767  37.423  1.00 21.94           C  
ATOM   1840  OE1 GLN A 241      23.524  43.210  38.514  1.00 23.52           O  
ATOM   1841  NE2 GLN A 241      24.670  43.304  36.624  1.00 20.84           N  
ATOM   1842  N   VAL A 242      19.557  41.563  33.659  1.00 20.57           N  
ATOM   1843  CA  VAL A 242      18.361  42.229  33.182  1.00 20.73           C  
ATOM   1844  C   VAL A 242      17.173  41.309  33.246  1.00 20.69           C  
ATOM   1845  O   VAL A 242      17.244  40.190  32.757  1.00 21.13           O  
ATOM   1846  CB  VAL A 242      18.498  42.667  31.712  1.00 21.03           C  
ATOM   1847  CG1 VAL A 242      17.204  43.377  31.250  1.00 20.85           C  
ATOM   1848  CG2 VAL A 242      19.723  43.527  31.498  1.00 20.71           C  
ATOM   1849  N   ASP A 243      16.071  41.786  33.813  1.00 20.62           N  
ATOM   1850  CA  ASP A 243      14.807  41.042  33.788  1.00 20.64           C  
ATOM   1851  C   ASP A 243      14.148  41.348  32.448  1.00 20.94           C  
ATOM   1852  O   ASP A 243      13.591  42.438  32.230  1.00 19.75           O  
ATOM   1853  CB  ASP A 243      13.916  41.471  34.963  1.00 20.88           C  
ATOM   1854  CG  ASP A 243      12.526  40.894  34.898  1.00 21.39           C  
ATOM   1855  OD1 ASP A 243      12.209  40.153  33.941  1.00 23.25           O  
ATOM   1856  OD2 ASP A 243      11.672  41.130  35.784  1.00 23.49           O  
ATOM   1857  N   PHE A 244      14.238  40.385  31.541  1.00 21.19           N  
ATOM   1858  CA  PHE A 244      13.717  40.549  30.197  1.00 21.56           C  
ATOM   1859  C   PHE A 244      12.225  40.916  30.204  1.00 22.49           C  
ATOM   1860  O   PHE A 244      11.734  41.521  29.260  1.00 21.85           O  
ATOM   1861  CB  PHE A 244      13.940  39.275  29.378  1.00 21.85           C  
ATOM   1862  CG  PHE A 244      15.316  39.152  28.743  1.00 20.87           C  
ATOM   1863  CD1 PHE A 244      16.457  39.540  29.399  1.00 20.74           C  
ATOM   1864  CD2 PHE A 244      15.446  38.617  27.483  1.00 21.00           C  
ATOM   1865  CE1 PHE A 244      17.691  39.407  28.810  1.00 19.77           C  
ATOM   1866  CE2 PHE A 244      16.687  38.470  26.890  1.00 20.94           C  
ATOM   1867  CZ  PHE A 244      17.805  38.881  27.551  1.00 20.34           C  
ATOM   1868  N   ASP A 245      11.500  40.554  31.259  1.00 23.56           N  
ATOM   1869  CA  ASP A 245      10.072  40.831  31.311  1.00 24.26           C  
ATOM   1870  C   ASP A 245       9.794  42.256  31.814  1.00 24.66           C  
ATOM   1871  O   ASP A 245       8.711  42.762  31.607  1.00 24.21           O  
ATOM   1872  CB  ASP A 245       9.353  39.841  32.222  1.00 24.74           C  
ATOM   1873  CG  ASP A 245       9.408  38.427  31.721  1.00 26.56           C  
ATOM   1874  OD1 ASP A 245       9.368  38.210  30.493  1.00 28.81           O  
ATOM   1875  OD2 ASP A 245       9.489  37.455  32.498  1.00 28.39           O  
ATOM   1876  N   ASN A 246      10.758  42.876  32.492  1.00 24.80           N  
ATOM   1877  CA  ASN A 246      10.605  44.244  32.989  1.00 25.56           C  
ATOM   1878  C   ASN A 246      11.960  44.902  33.106  1.00 25.31           C  
ATOM   1879  O   ASN A 246      12.500  45.064  34.205  1.00 25.43           O  
ATOM   1880  CB  ASN A 246       9.912  44.285  34.345  1.00 26.09           C  
ATOM   1881  CG  ASN A 246       9.555  45.716  34.765  1.00 29.59           C  
ATOM   1882  OD1 ASN A 246       9.366  46.598  33.912  1.00 32.67           O  
ATOM   1883  ND2 ASN A 246       9.468  45.954  36.075  1.00 33.42           N  
ATOM   1884  N   PRO A 247      12.525  45.257  31.961  1.00 25.08           N  
ATOM   1885  CA  PRO A 247      13.885  45.782  31.911  1.00 24.89           C  
ATOM   1886  C   PRO A 247      13.992  47.144  32.579  1.00 24.95           C  
ATOM   1887  O   PRO A 247      13.217  48.049  32.297  1.00 24.55           O  
ATOM   1888  CB  PRO A 247      14.182  45.899  30.413  1.00 25.05           C  
ATOM   1889  CG  PRO A 247      13.016  45.325  29.702  1.00 25.39           C  
ATOM   1890  CD  PRO A 247      11.890  45.184  30.640  1.00 25.02           C  
ATOM   1891  N   ASP A 248      14.976  47.267  33.460  1.00 24.53           N  
ATOM   1892  CA  ASP A 248      15.216  48.489  34.167  1.00 24.65           C  
ATOM   1893  C   ASP A 248      16.271  49.284  33.389  1.00 24.54           C  
ATOM   1894  O   ASP A 248      17.472  49.077  33.552  1.00 23.15           O  
ATOM   1895  CB  ASP A 248      15.706  48.144  35.564  1.00 24.64           C  
ATOM   1896  CG  ASP A 248      15.787  49.343  36.454  1.00 26.02           C  
ATOM   1897  OD1 ASP A 248      16.035  50.466  35.944  1.00 26.95           O  
ATOM   1898  OD2 ASP A 248      15.609  49.249  37.684  1.00 27.69           O  
ATOM   1899  N   TYR A 249      15.812  50.181  32.525  1.00 24.81           N  
ATOM   1900  CA  TYR A 249      16.720  50.936  31.673  1.00 25.45           C  
ATOM   1901  C   TYR A 249      17.573  51.954  32.426  1.00 25.90           C  
ATOM   1902  O   TYR A 249      18.585  52.421  31.897  1.00 25.80           O  
ATOM   1903  CB  TYR A 249      15.948  51.615  30.544  1.00 25.57           C  
ATOM   1904  CG  TYR A 249      15.244  50.651  29.630  1.00 24.58           C  
ATOM   1905  CD1 TYR A 249      15.930  49.624  29.003  1.00 25.44           C  
ATOM   1906  CD2 TYR A 249      13.890  50.764  29.404  1.00 24.48           C  
ATOM   1907  CE1 TYR A 249      15.276  48.731  28.173  1.00 25.01           C  
ATOM   1908  CE2 TYR A 249      13.234  49.892  28.583  1.00 24.43           C  
ATOM   1909  CZ  TYR A 249      13.927  48.883  27.969  1.00 24.47           C  
ATOM   1910  OH  TYR A 249      13.252  48.043  27.142  1.00 25.97           O  
ATOM   1911  N   GLU A 250      17.195  52.278  33.660  1.00 26.10           N  
ATOM   1912  CA  GLU A 250      17.999  53.190  34.458  1.00 26.93           C  
ATOM   1913  C   GLU A 250      19.259  52.492  34.929  1.00 25.85           C  
ATOM   1914  O   GLU A 250      20.329  53.086  34.964  1.00 25.90           O  
ATOM   1915  CB  GLU A 250      17.219  53.740  35.661  1.00 27.56           C  
ATOM   1916  CG  GLU A 250      16.021  54.576  35.246  1.00 32.34           C  
ATOM   1917  CD  GLU A 250      15.420  55.366  36.385  1.00 36.85           C  
ATOM   1918  OE1 GLU A 250      15.945  55.309  37.516  1.00 42.35           O  
ATOM   1919  OE2 GLU A 250      14.422  56.057  36.142  1.00 40.82           O  
ATOM   1920  N   ARG A 251      19.136  51.233  35.315  1.00 24.58           N  
ATOM   1921  CA  ARG A 251      20.297  50.502  35.756  1.00 23.76           C  
ATOM   1922  C   ARG A 251      21.030  49.909  34.568  1.00 22.91           C  
ATOM   1923  O   ARG A 251      22.242  49.773  34.602  1.00 22.42           O  
ATOM   1924  CB  ARG A 251      19.896  49.374  36.696  1.00 24.55           C  
ATOM   1925  CG  ARG A 251      19.421  49.802  38.077  1.00 25.88           C  
ATOM   1926  CD  ARG A 251      18.894  48.629  38.921  1.00 29.50           C  
ATOM   1927  NE  ARG A 251      19.993  47.764  39.349  1.00 31.63           N  
ATOM   1928  CZ  ARG A 251      19.894  46.467  39.623  1.00 33.13           C  
ATOM   1929  NH1 ARG A 251      18.736  45.826  39.521  1.00 33.12           N  
ATOM   1930  NH2 ARG A 251      20.978  45.805  39.998  1.00 33.93           N  
ATOM   1931  N   PHE A 252      20.300  49.560  33.515  1.00 21.47           N  
ATOM   1932  CA  PHE A 252      20.898  48.863  32.379  1.00 21.32           C  
ATOM   1933  C   PHE A 252      20.576  49.552  31.056  1.00 20.68           C  
ATOM   1934  O   PHE A 252      19.934  48.984  30.187  1.00 20.79           O  
ATOM   1935  CB  PHE A 252      20.355  47.434  32.344  1.00 21.09           C  
ATOM   1936  CG  PHE A 252      20.373  46.738  33.690  1.00 20.96           C  
ATOM   1937  CD1 PHE A 252      21.555  46.560  34.376  1.00 19.28           C  
ATOM   1938  CD2 PHE A 252      19.207  46.238  34.247  1.00 21.43           C  
ATOM   1939  CE1 PHE A 252      21.571  45.891  35.609  1.00 20.54           C  
ATOM   1940  CE2 PHE A 252      19.217  45.588  35.488  1.00 22.13           C  
ATOM   1941  CZ  PHE A 252      20.403  45.414  36.156  1.00 20.96           C  
ATOM   1942  N   PRO A 253      21.057  50.767  30.884  1.00 20.56           N  
ATOM   1943  CA  PRO A 253      20.658  51.566  29.714  1.00 20.38           C  
ATOM   1944  C   PRO A 253      20.984  50.916  28.361  1.00 20.20           C  
ATOM   1945  O   PRO A 253      20.191  51.053  27.428  1.00 19.48           O  
ATOM   1946  CB  PRO A 253      21.383  52.903  29.928  1.00 19.77           C  
ATOM   1947  CG  PRO A 253      22.562  52.555  30.895  1.00 20.60           C  
ATOM   1948  CD  PRO A 253      21.986  51.484  31.782  1.00 20.69           C  
ATOM   1949  N   ASN A 254      22.091  50.187  28.240  1.00 20.32           N  
ATOM   1950  CA  ASN A 254      22.409  49.613  26.938  1.00 20.12           C  
ATOM   1951  C   ASN A 254      21.572  48.393  26.554  1.00 19.96           C  
ATOM   1952  O   ASN A 254      21.675  47.892  25.441  1.00 19.16           O  
ATOM   1953  CB  ASN A 254      23.893  49.336  26.784  1.00 20.06           C  
ATOM   1954  CG  ASN A 254      24.706  50.601  26.697  1.00 21.51           C  
ATOM   1955  OD1 ASN A 254      25.502  50.896  27.598  1.00 23.96           O  
ATOM   1956  ND2 ASN A 254      24.514  51.373  25.614  1.00 20.38           N  
ATOM   1957  N   PHE A 255      20.724  47.922  27.455  1.00 19.81           N  
ATOM   1958  CA  PHE A 255      19.807  46.858  27.063  1.00 19.54           C  
ATOM   1959  C   PHE A 255      18.855  47.384  25.977  1.00 19.69           C  
ATOM   1960  O   PHE A 255      18.194  46.606  25.274  1.00 19.77           O  
ATOM   1961  CB  PHE A 255      19.023  46.330  28.252  1.00 19.22           C  
ATOM   1962  CG  PHE A 255      18.269  45.105  27.940  1.00 20.47           C  
ATOM   1963  CD1 PHE A 255      18.928  43.922  27.736  1.00 20.23           C  
ATOM   1964  CD2 PHE A 255      16.909  45.148  27.758  1.00 20.13           C  
ATOM   1965  CE1 PHE A 255      18.243  42.786  27.416  1.00 21.65           C  
ATOM   1966  CE2 PHE A 255      16.227  44.023  27.432  1.00 20.73           C  
ATOM   1967  CZ  PHE A 255      16.886  42.842  27.257  1.00 22.63           C  
ATOM   1968  N   GLN A 256      18.790  48.707  25.841  1.00 19.89           N  
ATOM   1969  CA  GLN A 256      17.969  49.345  24.794  1.00 20.24           C  
ATOM   1970  C   GLN A 256      18.595  49.160  23.403  1.00 19.74           C  
ATOM   1971  O   GLN A 256      17.969  49.443  22.384  1.00 19.92           O  
ATOM   1972  CB  GLN A 256      17.778  50.849  25.095  1.00 20.01           C  
ATOM   1973  CG  GLN A 256      16.736  51.095  26.197  1.00 21.20           C  
ATOM   1974  CD  GLN A 256      16.741  52.513  26.764  1.00 22.14           C  
ATOM   1975  OE1 GLN A 256      15.711  53.195  26.741  1.00 23.01           O  
ATOM   1976  NE2 GLN A 256      17.874  52.943  27.298  1.00 21.42           N  
ATOM   1977  N   ASN A 257      19.845  48.716  23.385  1.00 19.66           N  
ATOM   1978  CA  ASN A 257      20.580  48.485  22.155  1.00 20.07           C  
ATOM   1979  C   ASN A 257      20.757  47.005  21.811  1.00 20.73           C  
ATOM   1980  O   ASN A 257      21.416  46.694  20.823  1.00 20.96           O  
ATOM   1981  CB  ASN A 257      21.969  49.100  22.232  1.00 19.17           C  
ATOM   1982  CG  ASN A 257      21.941  50.550  22.635  1.00 20.82           C  
ATOM   1983  OD1 ASN A 257      22.413  50.902  23.722  1.00 21.51           O  
ATOM   1984  ND2 ASN A 257      21.396  51.407  21.763  1.00 16.92           N  
ATOM   1985  N   VAL A 258      20.190  46.098  22.596  1.00 21.59           N  
ATOM   1986  CA  VAL A 258      20.410  44.660  22.347  1.00 23.34           C  
ATOM   1987  C   VAL A 258      19.671  44.172  21.112  1.00 23.85           C  
ATOM   1988  O   VAL A 258      18.549  44.611  20.818  1.00 24.10           O  
ATOM   1989  CB  VAL A 258      20.015  43.806  23.573  1.00 23.68           C  
ATOM   1990  CG1 VAL A 258      18.507  43.720  23.685  1.00 24.12           C  
ATOM   1991  CG2 VAL A 258      20.570  42.436  23.445  1.00 28.30           C  
ATOM   1992  N   VAL A 259      20.314  43.286  20.360  1.00 24.47           N  
ATOM   1993  CA  VAL A 259      19.705  42.721  19.154  1.00 24.91           C  
ATOM   1994  C   VAL A 259      20.004  41.215  19.140  1.00 24.93           C  
ATOM   1995  O   VAL A 259      21.152  40.829  19.119  1.00 25.32           O  
ATOM   1996  CB  VAL A 259      20.281  43.362  17.895  1.00 24.88           C  
ATOM   1997  CG1 VAL A 259      19.667  42.738  16.670  1.00 26.38           C  
ATOM   1998  CG2 VAL A 259      20.051  44.869  17.909  1.00 24.83           C  
ATOM   1999  N   GLY A 260      18.974  40.381  19.186  1.00 25.06           N  
ATOM   2000  CA  GLY A 260      19.166  38.944  19.232  1.00 25.64           C  
ATOM   2001  C   GLY A 260      19.076  38.221  17.887  1.00 25.42           C  
ATOM   2002  O   GLY A 260      18.679  38.796  16.869  1.00 25.77           O  
ATOM   2003  N   TYR A 261      19.497  36.965  17.907  1.00 25.04           N  
ATOM   2004  CA  TYR A 261      19.380  36.049  16.792  1.00 25.30           C  
ATOM   2005  C   TYR A 261      18.428  34.973  17.328  1.00 24.63           C  
ATOM   2006  O   TYR A 261      18.676  34.417  18.392  1.00 24.77           O  
ATOM   2007  CB  TYR A 261      20.729  35.414  16.482  1.00 25.84           C  
ATOM   2008  CG  TYR A 261      21.750  36.315  15.825  1.00 28.57           C  
ATOM   2009  CD1 TYR A 261      21.821  36.423  14.447  1.00 34.41           C  
ATOM   2010  CD2 TYR A 261      22.631  37.049  16.574  1.00 29.87           C  
ATOM   2011  CE1 TYR A 261      22.752  37.255  13.838  1.00 35.64           C  
ATOM   2012  CE2 TYR A 261      23.576  37.852  15.986  1.00 32.26           C  
ATOM   2013  CZ  TYR A 261      23.644  37.949  14.623  1.00 34.92           C  
ATOM   2014  OH  TYR A 261      24.582  38.772  14.047  1.00 38.39           O  
ATOM   2015  N   GLU A 262      17.325  34.698  16.658  1.00 23.64           N  
ATOM   2016  CA  GLU A 262      16.376  33.758  17.244  1.00 24.03           C  
ATOM   2017  C   GLU A 262      15.933  32.660  16.306  1.00 23.15           C  
ATOM   2018  O   GLU A 262      16.063  32.766  15.078  1.00 22.51           O  
ATOM   2019  CB  GLU A 262      15.172  34.482  17.861  1.00 24.11           C  
ATOM   2020  CG  GLU A 262      13.899  34.502  17.057  1.00 26.35           C  
ATOM   2021  CD  GLU A 262      12.744  35.177  17.785  1.00 27.98           C  
ATOM   2022  OE1 GLU A 262      12.743  36.415  17.872  1.00 27.19           O  
ATOM   2023  OE2 GLU A 262      11.818  34.476  18.254  1.00 29.21           O  
ATOM   2024  N   THR A 263      15.455  31.587  16.917  1.00 22.58           N  
ATOM   2025  CA  THR A 263      14.939  30.458  16.170  1.00 22.52           C  
ATOM   2026  C   THR A 263      14.047  29.617  17.076  1.00 22.48           C  
ATOM   2027  O   THR A 263      14.107  29.712  18.313  1.00 22.14           O  
ATOM   2028  CB  THR A 263      16.117  29.607  15.659  1.00 22.55           C  
ATOM   2029  OG1 THR A 263      15.665  28.666  14.675  1.00 22.25           O  
ATOM   2030  CG2 THR A 263      16.693  28.743  16.770  1.00 22.79           C  
ATOM   2031  N   VAL A 264      13.208  28.797  16.472  1.00 21.62           N  
ATOM   2032  CA  VAL A 264      12.453  27.860  17.263  1.00 22.45           C  
ATOM   2033  C   VAL A 264      12.871  26.474  16.837  1.00 22.76           C  
ATOM   2034  O   VAL A 264      12.779  26.134  15.673  1.00 22.77           O  
ATOM   2035  CB  VAL A 264      10.964  28.027  17.087  1.00 23.08           C  
ATOM   2036  CG1 VAL A 264      10.234  26.805  17.643  1.00 23.67           C  
ATOM   2037  CG2 VAL A 264      10.499  29.344  17.767  1.00 22.75           C  
ATOM   2038  N   VAL A 265      13.389  25.695  17.777  1.00 22.93           N  
ATOM   2039  CA  VAL A 265      13.779  24.329  17.458  1.00 23.08           C  
ATOM   2040  C   VAL A 265      12.738  23.317  17.886  1.00 22.86           C  
ATOM   2041  O   VAL A 265      12.105  23.473  18.932  1.00 23.06           O  
ATOM   2042  CB  VAL A 265      15.143  23.937  18.075  1.00 22.94           C  
ATOM   2043  CG1 VAL A 265      16.243  24.745  17.404  1.00 23.66           C  
ATOM   2044  CG2 VAL A 265      15.169  24.122  19.592  1.00 22.99           C  
ATOM   2045  N   GLY A 266      12.574  22.290  17.056  1.00 21.77           N  
ATOM   2046  CA  GLY A 266      11.683  21.178  17.355  1.00 21.98           C  
ATOM   2047  C   GLY A 266      12.376  19.826  17.263  1.00 20.97           C  
ATOM   2048  O   GLY A 266      13.562  19.757  16.999  1.00 20.63           O  
ATOM   2049  N   PRO A 267      11.643  18.737  17.461  1.00 21.23           N  
ATOM   2050  CA  PRO A 267      12.253  17.403  17.427  1.00 20.68           C  
ATOM   2051  C   PRO A 267      13.126  17.183  16.203  1.00 20.04           C  
ATOM   2052  O   PRO A 267      12.666  17.371  15.081  1.00 19.35           O  
ATOM   2053  CB  PRO A 267      11.039  16.463  17.379  1.00 21.29           C  
ATOM   2054  CG  PRO A 267       9.970  17.202  18.037  1.00 22.85           C  
ATOM   2055  CD  PRO A 267      10.188  18.676  17.710  1.00 21.61           C  
ATOM   2056  N   GLY A 268      14.376  16.787  16.411  1.00 20.31           N  
ATOM   2057  CA  GLY A 268      15.278  16.518  15.305  1.00 19.95           C  
ATOM   2058  C   GLY A 268      16.256  17.627  14.993  1.00 20.50           C  
ATOM   2059  O   GLY A 268      17.277  17.400  14.311  1.00 21.62           O  
ATOM   2060  N   ASP A 269      15.965  18.831  15.477  1.00 19.81           N  
ATOM   2061  CA  ASP A 269      16.818  19.977  15.217  1.00 19.75           C  
ATOM   2062  C   ASP A 269      17.970  20.003  16.215  1.00 19.67           C  
ATOM   2063  O   ASP A 269      17.811  19.625  17.377  1.00 18.76           O  
ATOM   2064  CB  ASP A 269      16.032  21.288  15.386  1.00 19.99           C  
ATOM   2065  CG  ASP A 269      14.916  21.464  14.374  1.00 20.91           C  
ATOM   2066  OD1 ASP A 269      14.935  20.842  13.287  1.00 22.13           O  
ATOM   2067  OD2 ASP A 269      13.987  22.259  14.576  1.00 23.27           O  
ATOM   2068  N   VAL A 270      19.116  20.481  15.746  1.00 19.56           N  
ATOM   2069  CA  VAL A 270      20.276  20.700  16.595  1.00 19.57           C  
ATOM   2070  C   VAL A 270      20.747  22.137  16.444  1.00 19.33           C  
ATOM   2071  O   VAL A 270      21.033  22.594  15.352  1.00 19.78           O  
ATOM   2072  CB  VAL A 270      21.404  19.776  16.215  1.00 19.55           C  
ATOM   2073  CG1 VAL A 270      22.646  20.154  16.966  1.00 20.05           C  
ATOM   2074  CG2 VAL A 270      21.001  18.342  16.535  1.00 19.44           C  
ATOM   2075  N   LEU A 271      20.786  22.870  17.539  1.00 19.33           N  
ATOM   2076  CA  LEU A 271      21.263  24.229  17.501  1.00 19.02           C  
ATOM   2077  C   LEU A 271      22.677  24.272  18.036  1.00 19.15           C  
ATOM   2078  O   LEU A 271      22.961  23.787  19.130  1.00 18.74           O  
ATOM   2079  CB  LEU A 271      20.376  25.120  18.331  1.00 19.93           C  
ATOM   2080  CG  LEU A 271      20.892  26.549  18.573  1.00 20.11           C  
ATOM   2081  CD1 LEU A 271      21.011  27.358  17.296  1.00 19.41           C  
ATOM   2082  CD2 LEU A 271      19.979  27.245  19.555  1.00 20.25           C  
ATOM   2083  N   TYR A 272      23.582  24.818  17.244  1.00 19.15           N  
ATOM   2084  CA  TYR A 272      24.924  25.051  17.718  1.00 19.70           C  
ATOM   2085  C   TYR A 272      24.914  26.360  18.483  1.00 19.63           C  
ATOM   2086  O   TYR A 272      24.646  27.395  17.897  1.00 20.44           O  
ATOM   2087  CB  TYR A 272      25.908  25.172  16.547  1.00 19.86           C  
ATOM   2088  CG  TYR A 272      27.293  25.654  16.962  1.00 21.59           C  
ATOM   2089  CD1 TYR A 272      27.952  25.093  18.048  1.00 22.02           C  
ATOM   2090  CD2 TYR A 272      27.936  26.668  16.278  1.00 20.87           C  
ATOM   2091  CE1 TYR A 272      29.214  25.522  18.421  1.00 19.87           C  
ATOM   2092  CE2 TYR A 272      29.200  27.098  16.649  1.00 20.88           C  
ATOM   2093  CZ  TYR A 272      29.834  26.517  17.721  1.00 21.07           C  
ATOM   2094  OH  TYR A 272      31.091  26.937  18.104  1.00 18.93           O  
ATOM   2095  N   ILE A 273      25.210  26.308  19.776  1.00 19.80           N  
ATOM   2096  CA  ILE A 273      25.342  27.500  20.598  1.00 20.12           C  
ATOM   2097  C   ILE A 273      26.837  27.683  20.883  1.00 20.39           C  
ATOM   2098  O   ILE A 273      27.393  27.000  21.760  1.00 19.88           O  
ATOM   2099  CB  ILE A 273      24.576  27.366  21.901  1.00 19.72           C  
ATOM   2100  CG1 ILE A 273      23.111  27.045  21.624  1.00 20.57           C  
ATOM   2101  CG2 ILE A 273      24.661  28.695  22.696  1.00 20.99           C  
ATOM   2102  CD1 ILE A 273      22.296  26.797  22.876  1.00 20.93           C  
ATOM   2103  N   PRO A 274      27.487  28.611  20.182  1.00 20.23           N  
ATOM   2104  CA  PRO A 274      28.938  28.743  20.326  1.00 21.16           C  
ATOM   2105  C   PRO A 274      29.289  29.264  21.704  1.00 21.39           C  
ATOM   2106  O   PRO A 274      28.520  30.027  22.317  1.00 20.89           O  
ATOM   2107  CB  PRO A 274      29.353  29.757  19.230  1.00 21.62           C  
ATOM   2108  CG  PRO A 274      28.089  30.056  18.410  1.00 21.22           C  
ATOM   2109  CD  PRO A 274      26.919  29.621  19.282  1.00 20.51           C  
ATOM   2110  N   MET A 275      30.450  28.831  22.180  1.00 21.53           N  
ATOM   2111  CA  MET A 275      30.953  29.207  23.479  1.00 22.30           C  
ATOM   2112  C   MET A 275      30.920  30.734  23.636  1.00 21.94           C  
ATOM   2113  O   MET A 275      31.160  31.442  22.675  1.00 20.78           O  
ATOM   2114  CB  MET A 275      32.367  28.695  23.589  1.00 23.06           C  
ATOM   2115  CG  MET A 275      32.937  28.734  24.966  1.00 27.00           C  
ATOM   2116  SD  MET A 275      34.545  27.926  24.991  1.00 33.74           S  
ATOM   2117  CE  MET A 275      35.263  28.479  23.499  1.00 32.50           C  
ATOM   2118  N   TYR A 276      30.583  31.211  24.832  1.00 21.96           N  
ATOM   2119  CA  TYR A 276      30.485  32.656  25.138  1.00 23.15           C  
ATOM   2120  C   TYR A 276      29.256  33.365  24.546  1.00 22.39           C  
ATOM   2121  O   TYR A 276      28.989  34.496  24.899  1.00 22.58           O  
ATOM   2122  CB  TYR A 276      31.776  33.409  24.760  1.00 23.80           C  
ATOM   2123  CG  TYR A 276      32.904  33.136  25.729  1.00 28.82           C  
ATOM   2124  CD1 TYR A 276      32.940  33.756  26.951  1.00 32.73           C  
ATOM   2125  CD2 TYR A 276      33.935  32.246  25.415  1.00 35.83           C  
ATOM   2126  CE1 TYR A 276      33.956  33.507  27.864  1.00 35.96           C  
ATOM   2127  CE2 TYR A 276      34.975  31.992  26.336  1.00 38.59           C  
ATOM   2128  CZ  TYR A 276      34.958  32.628  27.562  1.00 38.60           C  
ATOM   2129  OH  TYR A 276      35.951  32.421  28.513  1.00 45.18           O  
ATOM   2130  N   TRP A 277      28.488  32.709  23.684  1.00 21.71           N  
ATOM   2131  CA  TRP A 277      27.281  33.350  23.149  1.00 21.24           C  
ATOM   2132  C   TRP A 277      26.184  33.278  24.152  1.00 20.90           C  
ATOM   2133  O   TRP A 277      25.914  32.217  24.708  1.00 21.96           O  
ATOM   2134  CB  TRP A 277      26.790  32.711  21.856  1.00 21.01           C  
ATOM   2135  CG  TRP A 277      27.547  33.166  20.670  1.00 19.98           C  
ATOM   2136  CD1 TRP A 277      28.875  33.013  20.462  1.00 17.90           C  
ATOM   2137  CD2 TRP A 277      27.030  33.832  19.519  1.00 19.76           C  
ATOM   2138  NE1 TRP A 277      29.218  33.533  19.247  1.00 18.64           N  
ATOM   2139  CE2 TRP A 277      28.106  34.071  18.662  1.00 18.29           C  
ATOM   2140  CE3 TRP A 277      25.764  34.305  19.151  1.00 20.56           C  
ATOM   2141  CZ2 TRP A 277      27.963  34.716  17.442  1.00 19.63           C  
ATOM   2142  CZ3 TRP A 277      25.624  34.950  17.943  1.00 21.16           C  
ATOM   2143  CH2 TRP A 277      26.720  35.137  17.095  1.00 19.92           C  
ATOM   2144  N   TRP A 278      25.574  34.426  24.405  1.00 20.32           N  
ATOM   2145  CA  TRP A 278      24.452  34.533  25.316  1.00 20.13           C  
ATOM   2146  C   TRP A 278      23.268  33.787  24.741  1.00 19.99           C  
ATOM   2147  O   TRP A 278      23.083  33.758  23.538  1.00 20.42           O  
ATOM   2148  CB  TRP A 278      24.025  35.999  25.441  1.00 20.65           C  
ATOM   2149  CG  TRP A 278      25.031  36.864  26.107  1.00 20.56           C  
ATOM   2150  CD1 TRP A 278      26.078  37.526  25.519  1.00 19.63           C  
ATOM   2151  CD2 TRP A 278      25.096  37.160  27.501  1.00 19.59           C  
ATOM   2152  NE1 TRP A 278      26.772  38.233  26.469  1.00 20.70           N  
ATOM   2153  CE2 TRP A 278      26.191  38.012  27.699  1.00 20.10           C  
ATOM   2154  CE3 TRP A 278      24.318  36.811  28.601  1.00 20.98           C  
ATOM   2155  CZ2 TRP A 278      26.527  38.516  28.951  1.00 20.24           C  
ATOM   2156  CZ3 TRP A 278      24.668  37.299  29.849  1.00 23.26           C  
ATOM   2157  CH2 TRP A 278      25.759  38.146  30.011  1.00 20.41           C  
ATOM   2158  N   HIS A 279      22.463  33.194  25.591  1.00 19.84           N  
ATOM   2159  CA  HIS A 279      21.269  32.530  25.122  1.00 20.78           C  
ATOM   2160  C   HIS A 279      20.202  32.495  26.192  1.00 20.37           C  
ATOM   2161  O   HIS A 279      20.479  32.275  27.370  1.00 20.66           O  
ATOM   2162  CB  HIS A 279      21.540  31.098  24.604  1.00 20.86           C  
ATOM   2163  CG  HIS A 279      22.349  30.238  25.528  1.00 21.83           C  
ATOM   2164  ND1 HIS A 279      23.720  30.324  25.608  1.00 23.19           N  
ATOM   2165  CD2 HIS A 279      21.988  29.240  26.371  1.00 23.96           C  
ATOM   2166  CE1 HIS A 279      24.175  29.411  26.449  1.00 22.20           C  
ATOM   2167  NE2 HIS A 279      23.144  28.747  26.940  1.00 23.84           N  
ATOM   2168  N   HIS A 280      18.994  32.718  25.711  1.00 20.90           N  
ATOM   2169  CA  HIS A 280      17.742  32.758  26.441  1.00 21.22           C  
ATOM   2170  C   HIS A 280      16.910  31.676  25.793  1.00 21.42           C  
ATOM   2171  O   HIS A 280      16.749  31.685  24.580  1.00 21.70           O  
ATOM   2172  CB  HIS A 280      17.099  34.124  26.224  1.00 21.04           C  
ATOM   2173  CG  HIS A 280      15.632  34.168  26.489  1.00 21.54           C  
ATOM   2174  ND1 HIS A 280      15.096  34.836  27.571  1.00 22.76           N  
ATOM   2175  CD2 HIS A 280      14.581  33.660  25.802  1.00 22.74           C  
ATOM   2176  CE1 HIS A 280      13.779  34.721  27.546  1.00 23.23           C  
ATOM   2177  NE2 HIS A 280      13.441  34.014  26.482  1.00 23.05           N  
ATOM   2178  N   ILE A 281      16.367  30.755  26.584  1.00 22.31           N  
ATOM   2179  CA  ILE A 281      15.649  29.599  26.040  1.00 22.39           C  
ATOM   2180  C   ILE A 281      14.304  29.443  26.722  1.00 22.72           C  
ATOM   2181  O   ILE A 281      14.216  29.419  27.945  1.00 22.70           O  
ATOM   2182  CB  ILE A 281      16.527  28.336  26.189  1.00 22.98           C  
ATOM   2183  CG1 ILE A 281      17.771  28.504  25.305  1.00 24.90           C  
ATOM   2184  CG2 ILE A 281      15.770  27.059  25.771  1.00 21.60           C  
ATOM   2185  CD1 ILE A 281      18.795  27.556  25.554  1.00 27.31           C  
ATOM   2186  N   GLU A 282      13.252  29.350  25.920  1.00 22.93           N  
ATOM   2187  CA  GLU A 282      11.903  29.205  26.458  1.00 23.35           C  
ATOM   2188  C   GLU A 282      11.101  28.105  25.769  1.00 22.59           C  
ATOM   2189  O   GLU A 282      11.092  27.982  24.549  1.00 21.77           O  
ATOM   2190  CB  GLU A 282      11.144  30.538  26.393  1.00 23.47           C  
ATOM   2191  CG  GLU A 282      10.830  31.055  25.009  1.00 25.70           C  
ATOM   2192  CD  GLU A 282      10.281  32.483  25.023  1.00 25.79           C  
ATOM   2193  OE1 GLU A 282      10.898  33.356  25.665  1.00 27.49           O  
ATOM   2194  OE2 GLU A 282       9.241  32.740  24.391  1.00 26.03           O  
ATOM   2195  N   SER A 283      10.456  27.293  26.588  1.00 22.44           N  
ATOM   2196  CA  SER A 283       9.570  26.246  26.103  1.00 23.00           C  
ATOM   2197  C   SER A 283       8.256  26.916  25.753  1.00 23.56           C  
ATOM   2198  O   SER A 283       7.685  27.615  26.584  1.00 24.14           O  
ATOM   2199  CB  SER A 283       9.346  25.204  27.188  1.00 22.59           C  
ATOM   2200  OG  SER A 283      10.496  24.400  27.345  1.00 22.67           O  
ATOM   2201  N   LEU A 284       7.763  26.694  24.541  1.00 24.07           N  
ATOM   2202  CA  LEU A 284       6.581  27.412  24.070  1.00 24.80           C  
ATOM   2203  C   LEU A 284       5.386  27.324  25.004  1.00 24.51           C  
ATOM   2204  O   LEU A 284       5.098  26.271  25.602  1.00 23.93           O  
ATOM   2205  CB  LEU A 284       6.161  26.947  22.682  1.00 25.09           C  
ATOM   2206  CG  LEU A 284       7.185  27.083  21.555  1.00 26.46           C  
ATOM   2207  CD1 LEU A 284       6.475  27.236  20.215  1.00 28.29           C  
ATOM   2208  CD2 LEU A 284       8.123  28.188  21.775  1.00 26.10           C  
ATOM   2209  N   LEU A 285       4.718  28.463  25.136  1.00 24.41           N  
ATOM   2210  CA  LEU A 285       3.506  28.554  25.930  1.00 24.83           C  
ATOM   2211  C   LEU A 285       2.526  27.583  25.323  1.00 24.68           C  
ATOM   2212  O   LEU A 285       2.393  27.516  24.110  1.00 24.08           O  
ATOM   2213  CB  LEU A 285       2.927  29.961  25.872  1.00 24.79           C  
ATOM   2214  CG  LEU A 285       3.825  31.078  26.397  1.00 25.19           C  
ATOM   2215  CD1 LEU A 285       3.298  32.434  25.954  1.00 26.02           C  
ATOM   2216  CD2 LEU A 285       3.925  30.999  27.898  1.00 26.27           C  
ATOM   2217  N   ASN A 286       1.867  26.815  26.173  1.00 25.20           N  
ATOM   2218  CA  ASN A 286       0.867  25.848  25.730  1.00 25.85           C  
ATOM   2219  C   ASN A 286       1.371  24.791  24.742  1.00 25.23           C  
ATOM   2220  O   ASN A 286       0.594  24.267  23.965  1.00 24.38           O  
ATOM   2221  CB  ASN A 286      -0.319  26.599  25.124  1.00 26.54           C  
ATOM   2222  CG  ASN A 286      -0.957  27.546  26.109  1.00 29.40           C  
ATOM   2223  OD1 ASN A 286      -1.478  27.118  27.140  1.00 33.49           O  
ATOM   2224  ND2 ASN A 286      -0.893  28.843  25.821  1.00 33.58           N  
ATOM   2225  N   GLY A 287       2.669  24.487  24.774  1.00 24.55           N  
ATOM   2226  CA  GLY A 287       3.243  23.518  23.863  1.00 24.10           C  
ATOM   2227  C   GLY A 287       3.524  22.167  24.487  1.00 23.80           C  
ATOM   2228  O   GLY A 287       4.110  21.301  23.838  1.00 24.10           O  
ATOM   2229  N   GLY A 288       3.100  21.971  25.734  1.00 23.32           N  
ATOM   2230  CA  GLY A 288       3.360  20.730  26.439  1.00 23.24           C  
ATOM   2231  C   GLY A 288       4.808  20.673  26.903  1.00 23.49           C  
ATOM   2232  O   GLY A 288       5.548  21.646  26.741  1.00 22.86           O  
ATOM   2233  N   ILE A 289       5.220  19.539  27.462  1.00 23.36           N  
ATOM   2234  CA  ILE A 289       6.571  19.406  27.983  1.00 23.99           C  
ATOM   2235  C   ILE A 289       7.601  19.374  26.874  1.00 23.28           C  
ATOM   2236  O   ILE A 289       7.324  18.958  25.755  1.00 23.68           O  
ATOM   2237  CB  ILE A 289       6.750  18.123  28.817  1.00 24.68           C  
ATOM   2238  CG1 ILE A 289       6.819  16.912  27.901  1.00 26.90           C  
ATOM   2239  CG2 ILE A 289       5.648  17.983  29.885  1.00 25.75           C  
ATOM   2240  CD1 ILE A 289       7.294  15.640  28.613  1.00 29.37           C  
ATOM   2241  N   THR A 290       8.811  19.790  27.210  1.00 22.42           N  
ATOM   2242  CA  THR A 290       9.904  19.768  26.264  1.00 21.38           C  
ATOM   2243  C   THR A 290      11.030  18.880  26.774  1.00 20.56           C  
ATOM   2244  O   THR A 290      11.243  18.743  27.986  1.00 19.81           O  
ATOM   2245  CB  THR A 290      10.461  21.175  26.053  1.00 21.70           C  
ATOM   2246  OG1 THR A 290      10.823  21.761  27.308  1.00 20.15           O  
ATOM   2247  CG2 THR A 290       9.405  22.108  25.460  1.00 21.76           C  
ATOM   2248  N   ILE A 291      11.757  18.296  25.841  1.00 19.36           N  
ATOM   2249  CA  ILE A 291      12.903  17.503  26.190  1.00 19.73           C  
ATOM   2250  C   ILE A 291      14.044  17.865  25.286  1.00 19.29           C  
ATOM   2251  O   ILE A 291      13.862  17.976  24.083  1.00 19.81           O  
ATOM   2252  CB  ILE A 291      12.598  15.992  26.085  1.00 20.08           C  
ATOM   2253  CG1 ILE A 291      11.467  15.609  27.044  1.00 20.06           C  
ATOM   2254  CG2 ILE A 291      13.873  15.214  26.378  1.00 20.21           C  
ATOM   2255  CD1 ILE A 291      11.028  14.131  26.931  1.00 21.77           C  
ATOM   2256  N   THR A 292      15.215  18.070  25.882  1.00 18.95           N  
ATOM   2257  CA  THR A 292      16.406  18.407  25.156  1.00 19.17           C  
ATOM   2258  C   THR A 292      17.589  17.691  25.753  1.00 19.18           C  
ATOM   2259  O   THR A 292      17.671  17.497  26.965  1.00 19.21           O  
ATOM   2260  CB  THR A 292      16.703  19.937  25.259  1.00 19.83           C  
ATOM   2261  OG1 THR A 292      15.559  20.724  24.879  1.00 20.23           O  
ATOM   2262  CG2 THR A 292      17.787  20.350  24.270  1.00 20.15           C  
ATOM   2263  N   VAL A 293      18.530  17.314  24.903  1.00 19.25           N  
ATOM   2264  CA  VAL A 293      19.809  16.824  25.387  1.00 19.51           C  
ATOM   2265  C   VAL A 293      20.912  17.667  24.749  1.00 19.58           C  
ATOM   2266  O   VAL A 293      20.962  17.792  23.535  1.00 18.47           O  
ATOM   2267  CB  VAL A 293      20.024  15.345  25.063  1.00 19.73           C  
ATOM   2268  CG1 VAL A 293      21.490  14.951  25.250  1.00 20.24           C  
ATOM   2269  CG2 VAL A 293      19.146  14.478  25.968  1.00 20.65           C  
ATOM   2270  N   ASN A 294      21.766  18.277  25.569  1.00 19.85           N  
ATOM   2271  CA  ASN A 294      22.882  19.057  25.039  1.00 20.26           C  
ATOM   2272  C   ASN A 294      24.179  18.232  25.052  1.00 20.35           C  
ATOM   2273  O   ASN A 294      24.233  17.131  25.634  1.00 21.82           O  
ATOM   2274  CB  ASN A 294      23.008  20.443  25.727  1.00 20.82           C  
ATOM   2275  CG  ASN A 294      23.676  20.388  27.102  1.00 21.84           C  
ATOM   2276  OD1 ASN A 294      24.209  19.354  27.495  1.00 21.66           O  
ATOM   2277  ND2 ASN A 294      23.630  21.519  27.849  1.00 21.23           N  
ATOM   2278  N   PHE A 295      25.186  18.729  24.346  1.00 20.69           N  
ATOM   2279  CA  PHE A 295      26.490  18.095  24.233  1.00 20.46           C  
ATOM   2280  C   PHE A 295      27.452  19.240  24.494  1.00 21.42           C  
ATOM   2281  O   PHE A 295      27.573  20.167  23.653  1.00 20.85           O  
ATOM   2282  CB  PHE A 295      26.728  17.569  22.814  1.00 20.62           C  
ATOM   2283  CG  PHE A 295      25.898  16.366  22.440  1.00 21.15           C  
ATOM   2284  CD1 PHE A 295      24.526  16.468  22.247  1.00 21.98           C  
ATOM   2285  CD2 PHE A 295      26.498  15.130  22.256  1.00 19.31           C  
ATOM   2286  CE1 PHE A 295      23.791  15.343  21.902  1.00 19.77           C  
ATOM   2287  CE2 PHE A 295      25.762  14.037  21.885  1.00 17.96           C  
ATOM   2288  CZ  PHE A 295      24.424  14.138  21.720  1.00 17.87           C  
ATOM   2289  N   TRP A 296      28.123  19.196  25.645  1.00 21.19           N  
ATOM   2290  CA  TRP A 296      29.023  20.275  26.050  1.00 21.46           C  
ATOM   2291  C   TRP A 296      30.481  19.834  25.873  1.00 21.42           C  
ATOM   2292  O   TRP A 296      30.898  18.795  26.387  1.00 21.96           O  
ATOM   2293  CB  TRP A 296      28.760  20.669  27.498  1.00 21.13           C  
ATOM   2294  CG  TRP A 296      27.853  21.859  27.710  1.00 21.95           C  
ATOM   2295  CD1 TRP A 296      27.797  22.987  26.955  1.00 23.23           C  
ATOM   2296  CD2 TRP A 296      26.935  22.067  28.797  1.00 22.27           C  
ATOM   2297  NE1 TRP A 296      26.882  23.869  27.478  1.00 22.26           N  
ATOM   2298  CE2 TRP A 296      26.336  23.329  28.607  1.00 22.53           C  
ATOM   2299  CE3 TRP A 296      26.531  21.298  29.894  1.00 24.83           C  
ATOM   2300  CZ2 TRP A 296      25.362  23.840  29.463  1.00 22.34           C  
ATOM   2301  CZ3 TRP A 296      25.557  21.810  30.754  1.00 24.59           C  
ATOM   2302  CH2 TRP A 296      24.993  23.075  30.531  1.00 23.75           C  
ATOM   2303  N   TYR A 297      31.235  20.632  25.126  1.00 21.64           N  
ATOM   2304  CA  TYR A 297      32.633  20.361  24.845  1.00 21.81           C  
ATOM   2305  C   TYR A 297      33.482  21.523  25.320  1.00 22.41           C  
ATOM   2306  O   TYR A 297      33.110  22.682  25.146  1.00 21.78           O  
ATOM   2307  CB  TYR A 297      32.862  20.198  23.344  1.00 21.49           C  
ATOM   2308  CG  TYR A 297      32.287  18.943  22.761  1.00 21.77           C  
ATOM   2309  CD1 TYR A 297      30.934  18.870  22.415  1.00 21.68           C  
ATOM   2310  CD2 TYR A 297      33.083  17.841  22.526  1.00 19.80           C  
ATOM   2311  CE1 TYR A 297      30.405  17.734  21.890  1.00 22.16           C  
ATOM   2312  CE2 TYR A 297      32.555  16.690  21.993  1.00 20.99           C  
ATOM   2313  CZ  TYR A 297      31.215  16.637  21.686  1.00 21.46           C  
ATOM   2314  OH  TYR A 297      30.673  15.494  21.159  1.00 22.11           O  
ATOM   2315  N   LYS A 298      34.632  21.220  25.899  1.00 23.17           N  
ATOM   2316  CA  LYS A 298      35.566  22.273  26.288  1.00 24.45           C  
ATOM   2317  C   LYS A 298      36.074  22.912  25.021  1.00 24.21           C  
ATOM   2318  O   LYS A 298      36.264  22.228  24.025  1.00 23.35           O  
ATOM   2319  CB  LYS A 298      36.748  21.699  27.085  1.00 24.85           C  
ATOM   2320  CG  LYS A 298      36.436  21.416  28.552  1.00 28.00           C  
ATOM   2321  CD  LYS A 298      37.657  20.865  29.298  1.00 31.59           C  
ATOM   2322  CE  LYS A 298      37.309  20.447  30.730  1.00 33.77           C  
ATOM   2323  NZ  LYS A 298      38.406  19.627  31.367  1.00 36.02           N  
ATOM   2324  N   GLY A 299      36.317  24.216  25.056  1.00 25.28           N  
ATOM   2325  CA  GLY A 299      36.818  24.909  23.886  1.00 26.38           C  
ATOM   2326  C   GLY A 299      38.254  24.542  23.547  1.00 27.78           C  
ATOM   2327  O   GLY A 299      38.935  23.895  24.315  1.00 27.16           O  
ATOM   2328  N   ALA A 300      38.690  24.949  22.366  1.00 30.42           N  
ATOM   2329  CA  ALA A 300      40.062  24.762  21.918  1.00 32.93           C  
ATOM   2330  C   ALA A 300      41.021  25.544  22.819  1.00 35.12           C  
ATOM   2331  O   ALA A 300      40.597  26.337  23.646  1.00 34.87           O  
ATOM   2332  CB  ALA A 300      40.199  25.249  20.472  1.00 32.98           C  
ATOM   2333  N   PRO A 301      42.318  25.355  22.615  1.00 38.54           N  
ATOM   2334  CA  PRO A 301      43.347  26.012  23.440  1.00 40.37           C  
ATOM   2335  C   PRO A 301      43.548  27.484  23.102  1.00 41.99           C  
ATOM   2336  O   PRO A 301      43.379  27.853  21.950  1.00 42.88           O  
ATOM   2337  CB  PRO A 301      44.615  25.246  23.061  1.00 40.42           C  
ATOM   2338  CG  PRO A 301      44.397  24.879  21.638  1.00 39.87           C  
ATOM   2339  CD  PRO A 301      42.919  24.544  21.535  1.00 38.98           C  
ATOM   2340  N   THR A 302      43.915  28.293  24.090  1.00 44.60           N  
ATOM   2341  CA  THR A 302      44.209  29.725  23.912  1.00 46.30           C  
ATOM   2342  C   THR A 302      45.593  29.790  23.315  1.00 47.41           C  
ATOM   2343  O   THR A 302      46.534  29.388  23.992  1.00 47.96           O  
ATOM   2344  CB  THR A 302      44.242  30.391  25.294  1.00 46.57           C  
ATOM   2345  OG1 THR A 302      42.941  30.320  25.895  1.00 48.00           O  
ATOM   2346  CG2 THR A 302      44.526  31.869  25.199  1.00 47.24           C  
ATOM   2347  N   PRO A 303      45.782  30.336  22.112  1.00 48.55           N  
ATOM   2348  CA  PRO A 303      47.090  30.170  21.473  1.00 48.80           C  
ATOM   2349  C   PRO A 303      48.210  30.717  22.341  1.00 48.76           C  
ATOM   2350  O   PRO A 303      47.874  31.450  23.269  1.00 49.07           O  
ATOM   2351  CB  PRO A 303      46.967  30.980  20.185  1.00 49.07           C  
ATOM   2352  CG  PRO A 303      45.504  31.101  19.952  1.00 48.93           C  
ATOM   2353  CD  PRO A 303      44.916  31.243  21.330  1.00 48.62           C  
ATOM   2354  N   GLU A 307      46.795  36.776  18.436  1.00 52.62           N  
ATOM   2355  CA  GLU A 307      46.885  37.814  17.415  1.00 52.76           C  
ATOM   2356  C   GLU A 307      45.865  38.906  17.636  1.00 52.00           C  
ATOM   2357  O   GLU A 307      44.757  38.658  18.096  1.00 52.48           O  
ATOM   2358  CB  GLU A 307      46.686  37.246  15.996  1.00 53.32           C  
ATOM   2359  CG  GLU A 307      46.893  38.307  14.908  1.00 54.63           C  
ATOM   2360  CD  GLU A 307      46.862  37.764  13.487  1.00 56.43           C  
ATOM   2361  OE1 GLU A 307      46.527  36.574  13.290  1.00 57.49           O  
ATOM   2362  OE2 GLU A 307      47.173  38.543  12.558  1.00 57.89           O  
ATOM   2363  N   TYR A 308      46.255  40.125  17.303  1.00 51.19           N  
ATOM   2364  CA  TYR A 308      45.367  41.267  17.405  1.00 50.55           C  
ATOM   2365  C   TYR A 308      44.747  41.494  16.039  1.00 49.51           C  
ATOM   2366  O   TYR A 308      45.300  41.053  15.028  1.00 49.70           O  
ATOM   2367  CB  TYR A 308      46.151  42.485  17.867  1.00 50.82           C  
ATOM   2368  CG  TYR A 308      46.702  42.286  19.259  1.00 52.47           C  
ATOM   2369  CD1 TYR A 308      45.949  42.632  20.373  1.00 53.15           C  
ATOM   2370  CD2 TYR A 308      47.948  41.696  19.462  1.00 53.79           C  
ATOM   2371  CE1 TYR A 308      46.426  42.426  21.643  1.00 54.22           C  
ATOM   2372  CE2 TYR A 308      48.437  41.487  20.736  1.00 54.76           C  
ATOM   2373  CZ  TYR A 308      47.670  41.857  21.824  1.00 55.10           C  
ATOM   2374  OH  TYR A 308      48.146  41.659  23.101  1.00 56.68           O  
ATOM   2375  N   PRO A 309      43.584  42.135  15.987  1.00 47.88           N  
ATOM   2376  CA  PRO A 309      42.843  42.621  17.169  1.00 46.21           C  
ATOM   2377  C   PRO A 309      42.139  41.503  17.952  1.00 43.75           C  
ATOM   2378  O   PRO A 309      41.768  40.503  17.369  1.00 44.10           O  
ATOM   2379  CB  PRO A 309      41.804  43.566  16.562  1.00 46.39           C  
ATOM   2380  CG  PRO A 309      41.610  43.069  15.128  1.00 47.65           C  
ATOM   2381  CD  PRO A 309      42.899  42.431  14.716  1.00 48.06           C  
ATOM   2382  N   LEU A 310      41.973  41.672  19.256  1.00 40.94           N  
ATOM   2383  CA  LEU A 310      41.349  40.650  20.093  1.00 38.75           C  
ATOM   2384  C   LEU A 310      39.863  40.491  19.817  1.00 36.87           C  
ATOM   2385  O   LEU A 310      39.148  41.474  19.610  1.00 37.02           O  
ATOM   2386  CB  LEU A 310      41.499  41.017  21.566  1.00 38.63           C  
ATOM   2387  CG  LEU A 310      42.571  40.351  22.435  1.00 37.97           C  
ATOM   2388  CD1 LEU A 310      43.840  40.049  21.711  1.00 37.27           C  
ATOM   2389  CD2 LEU A 310      42.836  41.234  23.637  1.00 37.27           C  
ATOM   2390  N   LYS A 311      39.392  39.254  19.847  1.00 34.04           N  
ATOM   2391  CA  LYS A 311      37.972  38.998  19.702  1.00 32.20           C  
ATOM   2392  C   LYS A 311      37.208  39.376  20.968  1.00 30.33           C  
ATOM   2393  O   LYS A 311      37.760  39.421  22.072  1.00 29.17           O  
ATOM   2394  CB  LYS A 311      37.733  37.564  19.371  1.00 32.59           C  
ATOM   2395  N   ALA A 312      35.924  39.641  20.788  1.00 28.23           N  
ATOM   2396  CA  ALA A 312      35.074  40.011  21.895  1.00 27.38           C  
ATOM   2397  C   ALA A 312      35.148  38.973  23.005  1.00 26.28           C  
ATOM   2398  O   ALA A 312      35.271  39.334  24.172  1.00 24.54           O  
ATOM   2399  CB  ALA A 312      33.641  40.205  21.421  1.00 27.09           C  
ATOM   2400  N   HIS A 313      35.101  37.689  22.649  1.00 25.72           N  
ATOM   2401  CA  HIS A 313      35.086  36.669  23.674  1.00 25.82           C  
ATOM   2402  C   HIS A 313      36.399  36.609  24.428  1.00 24.79           C  
ATOM   2403  O   HIS A 313      36.428  36.183  25.557  1.00 24.19           O  
ATOM   2404  CB  HIS A 313      34.688  35.293  23.129  1.00 26.92           C  
ATOM   2405  CG  HIS A 313      35.741  34.641  22.303  1.00 29.84           C  
ATOM   2406  ND1 HIS A 313      35.896  34.903  20.954  1.00 35.52           N  
ATOM   2407  CD2 HIS A 313      36.702  33.746  22.627  1.00 33.54           C  
ATOM   2408  CE1 HIS A 313      36.921  34.208  20.489  1.00 35.03           C  
ATOM   2409  NE2 HIS A 313      37.424  33.491  21.481  1.00 35.78           N  
ATOM   2410  N   GLN A 314      37.479  37.042  23.803  1.00 24.43           N  
ATOM   2411  CA  GLN A 314      38.762  37.092  24.465  1.00 24.34           C  
ATOM   2412  C   GLN A 314      38.762  38.226  25.510  1.00 24.39           C  
ATOM   2413  O   GLN A 314      39.327  38.081  26.590  1.00 24.82           O  
ATOM   2414  CB  GLN A 314      39.882  37.290  23.439  1.00 24.47           C  
ATOM   2415  CG  GLN A 314      40.032  36.106  22.472  1.00 25.49           C  
ATOM   2416  CD  GLN A 314      41.036  36.362  21.366  1.00 25.52           C  
ATOM   2417  OE1 GLN A 314      40.878  37.287  20.563  1.00 27.59           O  
ATOM   2418  NE2 GLN A 314      42.078  35.553  21.330  1.00 28.22           N  
ATOM   2419  N   LYS A 315      38.113  39.337  25.196  1.00 23.51           N  
ATOM   2420  CA  LYS A 315      38.000  40.423  26.154  1.00 23.79           C  
ATOM   2421  C   LYS A 315      37.125  39.979  27.325  1.00 23.05           C  
ATOM   2422  O   LYS A 315      37.373  40.347  28.465  1.00 21.38           O  
ATOM   2423  CB  LYS A 315      37.421  41.667  25.504  1.00 24.09           C  
ATOM   2424  CG  LYS A 315      38.382  42.286  24.533  1.00 26.96           C  
ATOM   2425  CD  LYS A 315      37.849  43.552  23.947  1.00 31.28           C  
ATOM   2426  CE  LYS A 315      38.856  44.156  22.977  1.00 34.34           C  
ATOM   2427  NZ  LYS A 315      38.207  45.098  22.005  1.00 36.25           N  
ATOM   2428  N   VAL A 316      36.109  39.177  27.041  1.00 22.30           N  
ATOM   2429  CA  VAL A 316      35.276  38.673  28.113  1.00 22.39           C  
ATOM   2430  C   VAL A 316      36.124  37.800  29.063  1.00 22.29           C  
ATOM   2431  O   VAL A 316      36.040  37.932  30.274  1.00 21.27           O  
ATOM   2432  CB  VAL A 316      34.065  37.887  27.595  1.00 22.03           C  
ATOM   2433  CG1 VAL A 316      33.309  37.282  28.750  1.00 21.64           C  
ATOM   2434  CG2 VAL A 316      33.123  38.796  26.802  1.00 22.46           C  
ATOM   2435  N   ALA A 317      36.964  36.941  28.499  1.00 22.09           N  
ATOM   2436  CA  ALA A 317      37.848  36.086  29.295  1.00 21.98           C  
ATOM   2437  C   ALA A 317      38.783  36.916  30.164  1.00 21.61           C  
ATOM   2438  O   ALA A 317      39.042  36.573  31.300  1.00 21.05           O  
ATOM   2439  CB  ALA A 317      38.668  35.147  28.380  1.00 22.01           C  
ATOM   2440  N   ILE A 318      39.273  38.016  29.606  1.00 21.45           N  
ATOM   2441  CA  ILE A 318      40.162  38.917  30.318  1.00 21.24           C  
ATOM   2442  C   ILE A 318      39.431  39.511  31.524  1.00 21.38           C  
ATOM   2443  O   ILE A 318      39.937  39.462  32.646  1.00 20.76           O  
ATOM   2444  CB  ILE A 318      40.709  40.023  29.377  1.00 20.58           C  
ATOM   2445  CG1 ILE A 318      41.715  39.434  28.400  1.00 21.19           C  
ATOM   2446  CG2 ILE A 318      41.354  41.167  30.185  1.00 20.20           C  
ATOM   2447  CD1 ILE A 318      42.223  40.419  27.353  1.00 21.35           C  
ATOM   2448  N   MET A 319      38.234  40.030  31.287  1.00 20.83           N  
ATOM   2449  CA  MET A 319      37.446  40.622  32.355  1.00 21.31           C  
ATOM   2450  C   MET A 319      37.154  39.617  33.454  1.00 21.52           C  
ATOM   2451  O   MET A 319      37.326  39.911  34.651  1.00 21.13           O  
ATOM   2452  CB  MET A 319      36.177  41.260  31.818  1.00 21.01           C  
ATOM   2453  CG  MET A 319      36.423  42.519  30.971  1.00 21.17           C  
ATOM   2454  SD  MET A 319      34.860  43.346  30.459  1.00 22.71           S  
ATOM   2455  CE  MET A 319      34.204  42.152  29.206  1.00 22.13           C  
ATOM   2456  N   ARG A 320      36.767  38.408  33.068  1.00 21.34           N  
ATOM   2457  CA  ARG A 320      36.532  37.399  34.075  1.00 21.12           C  
ATOM   2458  C   ARG A 320      37.801  37.186  34.898  1.00 21.25           C  
ATOM   2459  O   ARG A 320      37.747  37.064  36.122  1.00 21.48           O  
ATOM   2460  CB  ARG A 320      36.102  36.095  33.427  1.00 21.01           C  
ATOM   2461  CG  ARG A 320      34.723  36.145  32.741  1.00 20.63           C  
ATOM   2462  CD  ARG A 320      34.324  34.795  32.142  1.00 18.73           C  
ATOM   2463  NE  ARG A 320      34.225  33.824  33.225  1.00 19.25           N  
ATOM   2464  CZ  ARG A 320      33.247  33.809  34.115  1.00 19.86           C  
ATOM   2465  NH1 ARG A 320      32.259  34.689  34.062  1.00 21.08           N  
ATOM   2466  NH2 ARG A 320      33.263  32.923  35.081  1.00 23.29           N  
ATOM   2467  N   ASN A 321      38.947  37.123  34.231  1.00 20.94           N  
ATOM   2468  CA  ASN A 321      40.184  36.855  34.939  1.00 20.88           C  
ATOM   2469  C   ASN A 321      40.535  37.981  35.916  1.00 20.93           C  
ATOM   2470  O   ASN A 321      40.962  37.716  37.047  1.00 21.77           O  
ATOM   2471  CB  ASN A 321      41.324  36.552  33.958  1.00 21.04           C  
ATOM   2472  CG  ASN A 321      41.288  35.099  33.447  1.00 22.80           C  
ATOM   2473  OD1 ASN A 321      40.924  34.193  34.185  1.00 23.97           O  
ATOM   2474  ND2 ASN A 321      41.666  34.887  32.193  1.00 21.35           N  
ATOM   2475  N   ILE A 322      40.355  39.233  35.505  1.00 20.14           N  
ATOM   2476  CA  ILE A 322      40.633  40.336  36.408  1.00 20.06           C  
ATOM   2477  C   ILE A 322      39.742  40.196  37.650  1.00 19.42           C  
ATOM   2478  O   ILE A 322      40.207  40.345  38.767  1.00 18.73           O  
ATOM   2479  CB  ILE A 322      40.372  41.690  35.715  1.00 20.21           C  
ATOM   2480  CG1 ILE A 322      41.320  41.894  34.535  1.00 21.54           C  
ATOM   2481  CG2 ILE A 322      40.504  42.823  36.699  1.00 20.53           C  
ATOM   2482  CD1 ILE A 322      42.806  41.798  34.868  1.00 24.56           C  
ATOM   2483  N   GLU A 323      38.458  39.904  37.454  1.00 18.94           N  
ATOM   2484  CA  GLU A 323      37.553  39.757  38.576  1.00 18.98           C  
ATOM   2485  C   GLU A 323      38.027  38.651  39.492  1.00 19.33           C  
ATOM   2486  O   GLU A 323      38.084  38.832  40.707  1.00 19.05           O  
ATOM   2487  CB  GLU A 323      36.113  39.538  38.106  1.00 19.25           C  
ATOM   2488  CG  GLU A 323      35.518  40.803  37.484  1.00 19.34           C  
ATOM   2489  CD  GLU A 323      34.143  40.616  36.855  1.00 18.71           C  
ATOM   2490  OE1 GLU A 323      33.183  40.332  37.573  1.00 19.19           O  
ATOM   2491  OE2 GLU A 323      34.024  40.805  35.636  1.00 19.56           O  
ATOM   2492  N   LYS A 324      38.425  37.528  38.908  1.00 19.55           N  
ATOM   2493  CA  LYS A 324      38.874  36.379  39.693  1.00 20.24           C  
ATOM   2494  C   LYS A 324      40.115  36.707  40.513  1.00 20.68           C  
ATOM   2495  O   LYS A 324      40.157  36.405  41.699  1.00 20.83           O  
ATOM   2496  CB  LYS A 324      39.175  35.175  38.789  1.00 20.07           C  
ATOM   2497  CG  LYS A 324      37.924  34.507  38.212  1.00 20.57           C  
ATOM   2498  CD  LYS A 324      38.331  33.318  37.350  1.00 20.28           C  
ATOM   2499  CE  LYS A 324      37.137  32.689  36.621  1.00 19.29           C  
ATOM   2500  NZ  LYS A 324      37.596  31.460  35.876  1.00 17.17           N  
ATOM   2501  N   MET A 325      41.112  37.320  39.885  1.00 21.21           N  
ATOM   2502  CA  MET A 325      42.366  37.657  40.568  1.00 22.87           C  
ATOM   2503  C   MET A 325      42.162  38.665  41.699  1.00 22.44           C  
ATOM   2504  O   MET A 325      42.763  38.560  42.771  1.00 22.08           O  
ATOM   2505  CB  MET A 325      43.380  38.232  39.572  1.00 23.32           C  
ATOM   2506  CG  MET A 325      43.993  37.195  38.671  1.00 27.47           C  
ATOM   2507  SD  MET A 325      44.795  37.924  37.197  1.00 35.56           S  
ATOM   2508  CE  MET A 325      45.664  39.189  38.009  1.00 34.71           C  
ATOM   2509  N   LEU A 326      41.309  39.641  41.452  1.00 22.71           N  
ATOM   2510  CA  LEU A 326      41.043  40.670  42.449  1.00 23.24           C  
ATOM   2511  C   LEU A 326      40.385  40.073  43.679  1.00 23.15           C  
ATOM   2512  O   LEU A 326      40.735  40.417  44.795  1.00 22.40           O  
ATOM   2513  CB  LEU A 326      40.151  41.735  41.865  1.00 23.01           C  
ATOM   2514  CG  LEU A 326      40.677  43.139  41.625  1.00 25.86           C  
ATOM   2515  CD1 LEU A 326      42.187  43.277  41.529  1.00 26.53           C  
ATOM   2516  CD2 LEU A 326      39.986  43.672  40.377  1.00 25.54           C  
ATOM   2517  N   GLY A 327      39.441  39.164  43.460  1.00 23.29           N  
ATOM   2518  CA  GLY A 327      38.760  38.489  44.547  1.00 23.97           C  
ATOM   2519  C   GLY A 327      39.728  37.723  45.418  1.00 24.63           C  
ATOM   2520  O   GLY A 327      39.659  37.783  46.649  1.00 24.75           O  
ATOM   2521  N   GLU A 328      40.644  37.002  44.778  1.00 25.03           N  
ATOM   2522  CA  GLU A 328      41.671  36.265  45.506  1.00 26.08           C  
ATOM   2523  C   GLU A 328      42.661  37.180  46.223  1.00 25.43           C  
ATOM   2524  O   GLU A 328      43.029  36.926  47.367  1.00 25.16           O  
ATOM   2525  CB  GLU A 328      42.442  35.368  44.546  1.00 26.76           C  
ATOM   2526  CG  GLU A 328      41.576  34.278  43.947  1.00 30.36           C  
ATOM   2527  CD  GLU A 328      41.719  32.957  44.676  1.00 35.76           C  
ATOM   2528  OE1 GLU A 328      42.091  32.986  45.878  1.00 38.79           O  
ATOM   2529  OE2 GLU A 328      41.483  31.896  44.034  1.00 38.82           O  
ATOM   2530  N   ALA A 329      43.094  38.240  45.552  1.00 24.91           N  
ATOM   2531  CA  ALA A 329      44.102  39.119  46.134  1.00 24.95           C  
ATOM   2532  C   ALA A 329      43.535  39.929  47.285  1.00 24.94           C  
ATOM   2533  O   ALA A 329      44.197  40.147  48.276  1.00 24.57           O  
ATOM   2534  CB  ALA A 329      44.682  40.022  45.088  1.00 24.88           C  
ATOM   2535  N   LEU A 330      42.290  40.354  47.161  1.00 25.47           N  
ATOM   2536  CA  LEU A 330      41.672  41.133  48.219  1.00 26.16           C  
ATOM   2537  C   LEU A 330      41.212  40.265  49.379  1.00 26.80           C  
ATOM   2538  O   LEU A 330      40.994  40.761  50.471  1.00 27.00           O  
ATOM   2539  CB  LEU A 330      40.504  41.930  47.669  1.00 26.08           C  
ATOM   2540  CG  LEU A 330      40.954  42.981  46.653  1.00 26.04           C  
ATOM   2541  CD1 LEU A 330      39.760  43.489  45.888  1.00 26.16           C  
ATOM   2542  CD2 LEU A 330      41.688  44.134  47.353  1.00 26.65           C  
ATOM   2543  N   GLY A 331      41.037  38.977  49.126  1.00 27.87           N  
ATOM   2544  CA  GLY A 331      40.645  38.039  50.158  1.00 28.89           C  
ATOM   2545  C   GLY A 331      39.176  38.086  50.526  1.00 29.43           C  
ATOM   2546  O   GLY A 331      38.763  37.435  51.478  1.00 30.62           O  
ATOM   2547  N   ASN A 332      38.400  38.887  49.808  1.00 29.59           N  
ATOM   2548  CA  ASN A 332      36.963  38.995  50.023  1.00 29.64           C  
ATOM   2549  C   ASN A 332      36.367  39.500  48.718  1.00 29.00           C  
ATOM   2550  O   ASN A 332      36.649  40.605  48.303  1.00 28.70           O  
ATOM   2551  CB  ASN A 332      36.656  39.973  51.156  1.00 30.15           C  
ATOM   2552  CG  ASN A 332      35.162  40.094  51.441  1.00 31.82           C  
ATOM   2553  OD1 ASN A 332      34.335  39.531  50.734  1.00 34.71           O  
ATOM   2554  ND2 ASN A 332      34.818  40.818  52.504  1.00 35.11           N  
ATOM   2555  N   PRO A 333      35.528  38.706  48.081  1.00 28.53           N  
ATOM   2556  CA  PRO A 333      35.001  39.075  46.771  1.00 28.25           C  
ATOM   2557  C   PRO A 333      34.176  40.343  46.807  1.00 27.91           C  
ATOM   2558  O   PRO A 333      34.033  40.984  45.776  1.00 26.99           O  
ATOM   2559  CB  PRO A 333      34.120  37.893  46.368  1.00 28.16           C  
ATOM   2560  CG  PRO A 333      34.137  36.938  47.468  1.00 28.91           C  
ATOM   2561  CD  PRO A 333      35.022  37.415  48.561  1.00 28.96           C  
ATOM   2562  N   GLN A 334      33.638  40.701  47.965  1.00 27.80           N  
ATOM   2563  CA  GLN A 334      32.814  41.896  48.039  1.00 27.97           C  
ATOM   2564  C   GLN A 334      33.665  43.155  47.975  1.00 26.77           C  
ATOM   2565  O   GLN A 334      33.144  44.245  47.764  1.00 26.51           O  
ATOM   2566  CB  GLN A 334      31.906  41.867  49.278  1.00 28.98           C  
ATOM   2567  CG  GLN A 334      30.675  40.969  49.038  1.00 32.17           C  
ATOM   2568  CD  GLN A 334      29.661  40.962  50.175  1.00 35.54           C  
ATOM   2569  OE1 GLN A 334      29.682  41.840  51.048  1.00 37.92           O  
ATOM   2570  NE2 GLN A 334      28.760  39.961  50.163  1.00 36.72           N  
ATOM   2571  N   GLU A 335      34.974  43.007  48.132  1.00 25.19           N  
ATOM   2572  CA  GLU A 335      35.860  44.151  48.018  1.00 24.41           C  
ATOM   2573  C   GLU A 335      36.170  44.466  46.537  1.00 22.68           C  
ATOM   2574  O   GLU A 335      36.700  45.521  46.228  1.00 21.42           O  
ATOM   2575  CB  GLU A 335      37.150  43.928  48.835  1.00 24.98           C  
ATOM   2576  CG  GLU A 335      36.974  44.148  50.343  1.00 27.94           C  
ATOM   2577  CD  GLU A 335      38.264  44.055  51.139  1.00 31.85           C  
ATOM   2578  OE1 GLU A 335      39.248  44.736  50.777  1.00 34.79           O  
ATOM   2579  OE2 GLU A 335      38.298  43.312  52.158  1.00 36.87           O  
ATOM   2580  N   VAL A 336      35.809  43.566  45.625  1.00 21.32           N  
ATOM   2581  CA  VAL A 336      36.113  43.751  44.201  1.00 20.37           C  
ATOM   2582  C   VAL A 336      35.541  45.034  43.603  1.00 20.01           C  
ATOM   2583  O   VAL A 336      36.247  45.798  42.954  1.00 19.07           O  
ATOM   2584  CB  VAL A 336      35.647  42.554  43.371  1.00 20.60           C  
ATOM   2585  CG1 VAL A 336      35.785  42.841  41.883  1.00 21.06           C  
ATOM   2586  CG2 VAL A 336      36.463  41.316  43.743  1.00 20.68           C  
ATOM   2587  N   GLY A 337      34.260  45.275  43.842  1.00 19.61           N  
ATOM   2588  CA  GLY A 337      33.593  46.437  43.317  1.00 19.45           C  
ATOM   2589  C   GLY A 337      34.205  47.760  43.731  1.00 19.51           C  
ATOM   2590  O   GLY A 337      34.522  48.576  42.871  1.00 18.93           O  
ATOM   2591  N   PRO A 338      34.333  48.010  45.032  1.00 20.41           N  
ATOM   2592  CA  PRO A 338      34.959  49.253  45.503  1.00 20.40           C  
ATOM   2593  C   PRO A 338      36.368  49.500  44.923  1.00 20.13           C  
ATOM   2594  O   PRO A 338      36.674  50.630  44.548  1.00 19.20           O  
ATOM   2595  CB  PRO A 338      34.960  49.092  47.035  1.00 20.63           C  
ATOM   2596  CG  PRO A 338      33.749  48.261  47.298  1.00 21.17           C  
ATOM   2597  CD  PRO A 338      33.782  47.221  46.151  1.00 20.95           C  
ATOM   2598  N   LEU A 339      37.199  48.470  44.831  1.00 20.34           N  
ATOM   2599  CA  LEU A 339      38.518  48.655  44.234  1.00 20.55           C  
ATOM   2600  C   LEU A 339      38.382  49.060  42.768  1.00 20.06           C  
ATOM   2601  O   LEU A 339      39.020  50.019  42.330  1.00 19.61           O  
ATOM   2602  CB  LEU A 339      39.383  47.408  44.358  1.00 20.81           C  
ATOM   2603  CG  LEU A 339      40.855  47.618  43.943  1.00 22.54           C  
ATOM   2604  CD1 LEU A 339      41.809  46.817  44.786  1.00 25.30           C  
ATOM   2605  CD2 LEU A 339      41.035  47.209  42.496  1.00 23.17           C  
ATOM   2606  N   LEU A 340      37.526  48.361  42.023  1.00 19.51           N  
ATOM   2607  CA  LEU A 340      37.327  48.687  40.600  1.00 19.36           C  
ATOM   2608  C   LEU A 340      36.827  50.120  40.427  1.00 19.30           C  
ATOM   2609  O   LEU A 340      37.318  50.861  39.566  1.00 17.55           O  
ATOM   2610  CB  LEU A 340      36.361  47.721  39.952  1.00 19.31           C  
ATOM   2611  CG  LEU A 340      36.929  46.333  39.637  1.00 21.99           C  
ATOM   2612  CD1 LEU A 340      35.842  45.506  39.069  1.00 22.03           C  
ATOM   2613  CD2 LEU A 340      38.140  46.390  38.673  1.00 21.20           C  
ATOM   2614  N   ASN A 341      35.879  50.521  41.270  1.00 19.17           N  
ATOM   2615  CA  ASN A 341      35.369  51.887  41.232  1.00 20.20           C  
ATOM   2616  C   ASN A 341      36.465  52.914  41.530  1.00 19.98           C  
ATOM   2617  O   ASN A 341      36.598  53.920  40.848  1.00 19.61           O  
ATOM   2618  CB  ASN A 341      34.181  52.043  42.196  1.00 20.66           C  
ATOM   2619  CG  ASN A 341      32.898  51.459  41.619  1.00 24.17           C  
ATOM   2620  OD1 ASN A 341      32.484  51.843  40.531  1.00 30.93           O  
ATOM   2621  ND2 ASN A 341      32.294  50.499  42.317  1.00 26.37           N  
ATOM   2622  N   THR A 342      37.245  52.633  42.558  1.00 20.07           N  
ATOM   2623  CA  THR A 342      38.351  53.489  42.939  1.00 20.49           C  
ATOM   2624  C   THR A 342      39.322  53.613  41.763  1.00 20.27           C  
ATOM   2625  O   THR A 342      39.835  54.688  41.502  1.00 19.66           O  
ATOM   2626  CB  THR A 342      39.001  52.909  44.189  1.00 20.82           C  
ATOM   2627  OG1 THR A 342      38.123  53.124  45.320  1.00 22.13           O  
ATOM   2628  CG2 THR A 342      40.308  53.625  44.545  1.00 21.01           C  
ATOM   2629  N   MET A 343      39.517  52.525  41.024  1.00 20.30           N  
ATOM   2630  CA  MET A 343      40.402  52.543  39.873  1.00 20.66           C  
ATOM   2631  C   MET A 343      39.932  53.445  38.758  1.00 20.29           C  
ATOM   2632  O   MET A 343      40.750  54.119  38.129  1.00 19.31           O  
ATOM   2633  CB  MET A 343      40.560  51.157  39.270  1.00 20.76           C  
ATOM   2634  CG  MET A 343      41.810  50.453  39.625  1.00 23.39           C  
ATOM   2635  SD  MET A 343      42.247  49.059  38.524  1.00 25.69           S  
ATOM   2636  CE  MET A 343      41.161  48.058  38.968  1.00 26.74           C  
ATOM   2637  N   ILE A 344      38.631  53.438  38.466  1.00 20.76           N  
ATOM   2638  CA  ILE A 344      38.167  54.187  37.312  1.00 21.23           C  
ATOM   2639  C   ILE A 344      37.648  55.577  37.565  1.00 20.71           C  
ATOM   2640  O   ILE A 344      37.763  56.403  36.666  1.00 20.65           O  
ATOM   2641  CB  ILE A 344      37.109  53.400  36.458  1.00 22.07           C  
ATOM   2642  CG1 ILE A 344      35.710  53.613  36.992  1.00 23.91           C  
ATOM   2643  CG2 ILE A 344      37.482  51.943  36.352  1.00 24.35           C  
ATOM   2644  CD1 ILE A 344      34.650  53.199  36.033  1.00 28.26           C  
ATOM   2645  N   LYS A 345      37.069  55.886  38.726  1.00 20.84           N  
ATOM   2646  CA  LYS A 345      36.482  57.231  38.817  1.00 21.15           C  
ATOM   2647  C   LYS A 345      37.464  58.376  38.784  1.00 19.86           C  
ATOM   2648  O   LYS A 345      38.459  58.429  39.517  1.00 19.23           O  
ATOM   2649  CB  LYS A 345      35.438  57.451  39.922  1.00 22.66           C  
ATOM   2650  CG  LYS A 345      35.562  56.714  41.190  1.00 27.82           C  
ATOM   2651  CD  LYS A 345      34.214  56.021  41.489  1.00 30.51           C  
ATOM   2652  CE  LYS A 345      33.398  56.782  42.502  1.00 32.51           C  
ATOM   2653  NZ  LYS A 345      34.069  56.806  43.829  1.00 37.63           N  
ATOM   2654  N   GLY A 346      37.143  59.307  37.899  1.00 18.18           N  
ATOM   2655  CA  GLY A 346      37.978  60.453  37.644  1.00 17.22           C  
ATOM   2656  C   GLY A 346      39.303  60.105  36.978  1.00 16.31           C  
ATOM   2657  O   GLY A 346      40.172  60.949  36.889  1.00 16.63           O  
ATOM   2658  N   ARG A 347      39.453  58.872  36.531  1.00 16.85           N  
ATOM   2659  CA  ARG A 347      40.697  58.413  35.904  1.00 17.52           C  
ATOM   2660  C   ARG A 347      40.469  57.811  34.502  1.00 17.57           C  
ATOM   2661  O   ARG A 347      41.178  58.143  33.559  1.00 17.10           O  
ATOM   2662  CB  ARG A 347      41.379  57.384  36.812  1.00 17.20           C  
ATOM   2663  CG  ARG A 347      41.822  57.949  38.181  1.00 16.77           C  
ATOM   2664  CD  ARG A 347      43.287  57.491  38.583  1.00 18.88           C  
ATOM   2665  NE  ARG A 347      43.254  56.087  38.618  1.00 17.77           N  
ATOM   2666  CZ  ARG A 347      44.115  55.220  38.149  1.00 16.11           C  
ATOM   2667  NH1 ARG A 347      45.323  55.512  37.658  1.00 16.59           N  
ATOM   2668  NH2 ARG A 347      43.734  53.978  38.276  1.00 13.22           N  
ATOM   2669  N   TYR A 348      39.472  56.954  34.375  1.00 18.74           N  
ATOM   2670  CA  TYR A 348      39.138  56.317  33.091  1.00 20.48           C  
ATOM   2671  C   TYR A 348      37.674  56.499  32.671  1.00 21.75           C  
ATOM   2672  O   TYR A 348      37.296  56.047  31.596  1.00 22.39           O  
ATOM   2673  CB  TYR A 348      39.411  54.800  33.124  1.00 19.97           C  
ATOM   2674  CG  TYR A 348      40.874  54.384  33.199  1.00 19.65           C  
ATOM   2675  CD1 TYR A 348      41.661  54.310  32.054  1.00 18.48           C  
ATOM   2676  CD2 TYR A 348      41.458  54.051  34.414  1.00 17.73           C  
ATOM   2677  CE1 TYR A 348      42.986  53.921  32.122  1.00 19.00           C  
ATOM   2678  CE2 TYR A 348      42.775  53.667  34.494  1.00 18.72           C  
ATOM   2679  CZ  TYR A 348      43.543  53.600  33.339  1.00 18.96           C  
ATOM   2680  OH  TYR A 348      44.856  53.203  33.419  1.00 17.77           O  
ATOM   2681  N   ASN A 349      36.837  57.123  33.488  1.00 23.99           N  
ATOM   2682  CA  ASN A 349      35.429  57.244  33.089  1.00 26.57           C  
ATOM   2683  C   ASN A 349      34.947  58.611  32.689  1.00 27.62           C  
ATOM   2684  O   ASN A 349      35.646  59.606  32.655  1.00 28.49           O  
ATOM   2685  CB  ASN A 349      34.496  56.720  34.150  1.00 26.11           C  
ATOM   2686  CG  ASN A 349      34.511  57.552  35.386  1.00 28.01           C  
ATOM   2687  OD1 ASN A 349      35.282  58.518  35.517  1.00 29.49           O  
ATOM   2688  ND2 ASN A 349      33.658  57.173  36.342  1.00 31.84           N  
ATOM   2689  OXT ASN A 349      33.761  58.686  32.399  1.00 31.04           O  
TER    2690      ASN A 349                                                      
ATOM   2691  N   LEU S 795      45.837  35.555  30.600  1.00 35.49           N  
ATOM   2692  CA  LEU S 795      44.757  36.539  30.946  1.00 35.77           C  
ATOM   2693  C   LEU S 795      43.580  36.250  30.030  1.00 35.54           C  
ATOM   2694  O   LEU S 795      42.418  36.338  30.412  1.00 34.79           O  
ATOM   2695  CB  LEU S 795      45.257  37.967  30.787  1.00 36.01           C  
ATOM   2696  CG  LEU S 795      44.695  38.978  31.791  1.00 37.16           C  
ATOM   2697  CD1 LEU S 795      44.761  38.459  33.204  1.00 37.65           C  
ATOM   2698  CD2 LEU S 795      45.450  40.289  31.718  1.00 38.07           C  
ATOM   2699  N   THR S 796      43.936  35.940  28.796  1.00 35.47           N  
ATOM   2700  CA  THR S 796      43.060  35.351  27.800  1.00 36.25           C  
ATOM   2701  C   THR S 796      42.644  33.888  28.079  1.00 35.84           C  
ATOM   2702  O   THR S 796      41.819  33.331  27.365  1.00 36.38           O  
ATOM   2703  CB  THR S 796      43.817  35.429  26.457  1.00 36.63           C  
ATOM   2704  OG1 THR S 796      43.251  34.528  25.524  1.00 38.48           O  
ATOM   2705  CG2 THR S 796      45.257  34.907  26.593  1.00 37.07           C  
ATOM   2706  N   SER S 797      43.197  33.251  29.101  1.00 35.44           N  
ATOM   2707  CA  SER S 797      42.835  31.860  29.377  1.00 35.29           C  
ATOM   2708  C   SER S 797      41.426  31.760  29.984  1.00 35.18           C  
ATOM   2709  O   SER S 797      40.925  32.701  30.611  1.00 33.96           O  
ATOM   2710  CB  SER S 797      43.856  31.189  30.291  1.00 35.17           C  
ATOM   2711  OG  SER S 797      43.716  31.654  31.624  1.00 36.65           O  
ATOM   2712  N   TYR S 798      40.789  30.611  29.790  1.00 35.36           N  
ATOM   2713  CA  TYR S 798      39.427  30.430  30.256  1.00 35.94           C  
ATOM   2714  C   TYR S 798      39.148  29.075  30.890  1.00 35.14           C  
ATOM   2715  O   TYR S 798      39.845  28.095  30.657  1.00 35.54           O  
ATOM   2716  CB  TYR S 798      38.440  30.707  29.120  1.00 36.37           C  
ATOM   2717  CG  TYR S 798      38.554  29.794  27.920  1.00 39.89           C  
ATOM   2718  CD1 TYR S 798      39.587  29.934  26.996  1.00 42.41           C  
ATOM   2719  CD2 TYR S 798      37.606  28.808  27.697  1.00 43.13           C  
ATOM   2720  CE1 TYR S 798      39.681  29.095  25.893  1.00 43.97           C  
ATOM   2721  CE2 TYR S 798      37.687  27.963  26.597  1.00 44.94           C  
ATOM   2722  CZ  TYR S 798      38.723  28.109  25.698  1.00 44.95           C  
ATOM   2723  OH  TYR S 798      38.781  27.270  24.613  1.00 44.37           O  
ATOM   2724  N   ASP S 799      38.108  29.046  31.709  1.00 34.54           N  
ATOM   2725  CA  ASP S 799      37.685  27.840  32.392  1.00 33.87           C  
ATOM   2726  C   ASP S 799      36.600  27.187  31.545  1.00 32.58           C  
ATOM   2727  O   ASP S 799      36.465  27.501  30.366  1.00 32.32           O  
ATOM   2728  CB  ASP S 799      37.140  28.208  33.770  1.00 34.50           C  
ATOM   2729  CG  ASP S 799      37.299  27.104  34.773  1.00 36.07           C  
ATOM   2730  OD1 ASP S 799      36.790  25.986  34.551  1.00 37.15           O  
ATOM   2731  OD2 ASP S 799      37.918  27.279  35.833  1.00 41.54           O  
ATOM   2732  N   CYS S 800      35.812  26.301  32.141  1.00 30.83           N  
ATOM   2733  CA  CYS S 800      34.798  25.586  31.392  1.00 29.83           C  
ATOM   2734  C   CYS S 800      33.490  25.511  32.161  1.00 29.15           C  
ATOM   2735  O   CYS S 800      32.794  24.502  32.092  1.00 28.68           O  
ATOM   2736  CB  CYS S 800      35.273  24.167  31.092  1.00 29.46           C  
ATOM   2737  SG  CYS S 800      35.576  23.194  32.601  1.00 30.36           S  
ATOM   2738  N   GLU S 801      33.152  26.578  32.874  1.00 28.36           N  
ATOM   2739  CA  GLU S 801      31.936  26.605  33.670  1.00 28.63           C  
ATOM   2740  C   GLU S 801      30.667  26.793  32.829  1.00 28.34           C  
ATOM   2741  O   GLU S 801      30.626  27.562  31.867  1.00 27.30           O  
ATOM   2742  CB  GLU S 801      32.038  27.688  34.751  1.00 28.61           C  
ATOM   2743  CG  GLU S 801      33.252  27.501  35.655  1.00 30.83           C  
ATOM   2744  CD  GLU S 801      33.188  28.346  36.907  1.00 32.58           C  
ATOM   2745  OE1 GLU S 801      32.414  27.985  37.805  1.00 33.57           O  
ATOM   2746  OE2 GLU S 801      33.910  29.362  36.989  1.00 33.97           O  
ATOM   2747  N   VAL S 802      29.627  26.062  33.212  1.00 28.85           N  
ATOM   2748  CA  VAL S 802      28.350  26.079  32.515  1.00 29.03           C  
ATOM   2749  C   VAL S 802      27.233  26.056  33.546  1.00 29.80           C  
ATOM   2750  O   VAL S 802      27.505  25.948  34.726  1.00 29.92           O  
ATOM   2751  CB  VAL S 802      28.221  24.834  31.606  1.00 28.44           C  
ATOM   2752  CG1 VAL S 802      29.288  24.856  30.523  1.00 26.99           C  
ATOM   2753  CG2 VAL S 802      28.333  23.551  32.428  1.00 29.08           C  
ATOM   2754  N   ASN S 803      25.978  26.135  33.111  1.00 31.09           N  
ATOM   2755  CA  ASN S 803      24.853  26.053  34.042  1.00 32.53           C  
ATOM   2756  C   ASN S 803      24.550  24.641  34.497  1.00 33.81           C  
ATOM   2757  O   ASN S 803      23.456  24.143  34.270  1.00 34.27           O  
ATOM   2758  CB  ASN S 803      23.575  26.659  33.463  1.00 32.29           C  
ATOM   2759  CG  ASN S 803      23.640  28.146  33.367  1.00 31.77           C  
ATOM   2760  OD1 ASN S 803      24.688  28.741  33.616  1.00 33.47           O  
ATOM   2761  ND2 ASN S 803      22.525  28.772  33.005  1.00 29.83           N  
ATOM   2762  N   ALA S 804      25.521  24.015  35.147  1.00 35.23           N  
ATOM   2763  CA  ALA S 804      25.365  22.689  35.740  1.00 36.86           C  
ATOM   2764  C   ALA S 804      26.577  22.452  36.638  1.00 37.98           C  
ATOM   2765  O   ALA S 804      27.660  22.949  36.360  1.00 37.44           O  
ATOM   2766  CB  ALA S 804      25.285  21.610  34.676  1.00 36.63           C  
ATOM   2767  N   PRO S 805      26.394  21.694  37.711  1.00 40.20           N  
ATOM   2768  CA  PRO S 805      27.495  21.381  38.635  1.00 41.46           C  
ATOM   2769  C   PRO S 805      28.572  20.511  37.983  1.00 42.51           C  
ATOM   2770  O   PRO S 805      28.342  19.931  36.938  1.00 43.07           O  
ATOM   2771  CB  PRO S 805      26.799  20.615  39.774  1.00 41.54           C  
ATOM   2772  CG  PRO S 805      25.506  20.116  39.185  1.00 41.29           C  
ATOM   2773  CD  PRO S 805      25.117  21.076  38.115  1.00 40.40           C  
ATOM   2774  N   ILE S 806      29.728  20.406  38.622  1.00 44.25           N  
ATOM   2775  CA  ILE S 806      30.854  19.627  38.099  1.00 44.96           C  
ATOM   2776  C   ILE S 806      30.770  18.169  38.532  1.00 45.18           C  
ATOM   2777  O   ILE S 806      29.902  17.801  39.323  1.00 45.78           O  
ATOM   2778  CB  ILE S 806      32.197  20.246  38.569  1.00 45.19           C  
ATOM   2779  CG1 ILE S 806      32.412  20.018  40.070  1.00 46.10           C  
ATOM   2780  CG2 ILE S 806      32.230  21.743  38.246  1.00 46.08           C  
ATOM   2781  CD1 ILE S 806      33.740  20.574  40.597  1.00 46.98           C  
ATOM   2782  N   LEU S 812      29.934   8.629  39.561  1.00 43.80           N  
ATOM   2783  CA  LEU S 812      29.027   8.736  38.425  1.00 43.90           C  
ATOM   2784  C   LEU S 812      29.761   9.243  37.182  1.00 43.45           C  
ATOM   2785  O   LEU S 812      30.160  10.410  37.114  1.00 43.36           O  
ATOM   2786  CB  LEU S 812      27.862   9.678  38.757  1.00 44.22           C  
ATOM   2787  CG  LEU S 812      26.979   9.292  39.951  1.00 45.50           C  
ATOM   2788  CD1 LEU S 812      25.871  10.341  40.144  1.00 46.20           C  
ATOM   2789  CD2 LEU S 812      26.385   7.894  39.793  1.00 45.08           C  
ATOM   2790  N   LEU S 813      29.928   8.375  36.190  1.00 42.70           N  
ATOM   2791  CA  LEU S 813      30.620   8.776  34.969  1.00 42.21           C  
ATOM   2792  C   LEU S 813      29.711   9.604  34.057  1.00 41.46           C  
ATOM   2793  O   LEU S 813      28.492   9.438  34.062  1.00 41.23           O  
ATOM   2794  CB  LEU S 813      31.167   7.554  34.225  1.00 42.30           C  
ATOM   2795  CG  LEU S 813      32.093   6.644  35.046  1.00 42.35           C  
ATOM   2796  CD1 LEU S 813      32.494   5.419  34.233  1.00 42.48           C  
ATOM   2797  CD2 LEU S 813      33.322   7.398  35.527  1.00 41.80           C  
ATOM   2798  N   GLN S 814      30.326  10.492  33.283  1.00 40.74           N  
ATOM   2799  CA  GLN S 814      29.603  11.385  32.378  1.00 40.26           C  
ATOM   2800  C   GLN S 814      30.475  11.775  31.190  1.00 39.82           C  
ATOM   2801  O   GLN S 814      31.674  11.514  31.176  1.00 39.19           O  
ATOM   2802  CB  GLN S 814      29.173  12.649  33.122  1.00 40.24           C  
ATOM   2803  CG  GLN S 814      30.336  13.501  33.615  1.00 40.51           C  
ATOM   2804  CD  GLN S 814      29.879  14.725  34.406  1.00 41.88           C  
ATOM   2805  OE1 GLN S 814      29.200  14.590  35.419  1.00 41.86           O  
ATOM   2806  NE2 GLN S 814      30.253  15.919  33.940  1.00 40.63           N  
ATOM   2807  N   GLY S 815      29.864  12.416  30.200  1.00 39.81           N  
ATOM   2808  CA  GLY S 815      30.568  12.851  29.012  1.00 39.53           C  
ATOM   2809  C   GLY S 815      31.402  11.755  28.365  1.00 39.85           C  
ATOM   2810  O   GLY S 815      30.962  10.609  28.210  1.00 38.55           O  
ATOM   2811  N   GLU S 816      32.624  12.123  27.995  1.00 40.44           N  
ATOM   2812  CA  GLU S 816      33.553  11.208  27.352  1.00 41.24           C  
ATOM   2813  C   GLU S 816      33.744   9.926  28.154  1.00 41.73           C  
ATOM   2814  O   GLU S 816      33.895   8.852  27.577  1.00 41.11           O  
ATOM   2815  CB  GLU S 816      34.909  11.884  27.148  1.00 41.24           C  
ATOM   2816  CG  GLU S 816      35.752  11.238  26.063  1.00 42.19           C  
ATOM   2817  CD  GLU S 816      37.161  11.790  26.019  1.00 43.70           C  
ATOM   2818  OE1 GLU S 816      37.985  11.311  26.814  1.00 45.25           O  
ATOM   2819  OE2 GLU S 816      37.447  12.696  25.201  1.00 44.50           O  
ATOM   2820  N   GLU S 817      33.724  10.039  29.479  1.00 42.66           N  
ATOM   2821  CA  GLU S 817      33.925   8.877  30.340  1.00 43.73           C  
ATOM   2822  C   GLU S 817      32.744   7.917  30.268  1.00 44.19           C  
ATOM   2823  O   GLU S 817      32.930   6.699  30.252  1.00 43.99           O  
ATOM   2824  CB  GLU S 817      34.167   9.308  31.788  1.00 43.81           C  
ATOM   2825  CG  GLU S 817      35.463  10.077  31.989  1.00 44.98           C  
ATOM   2826  CD  GLU S 817      35.337  11.569  31.688  1.00 46.95           C  
ATOM   2827  OE1 GLU S 817      34.221  12.052  31.394  1.00 48.87           O  
ATOM   2828  OE2 GLU S 817      36.362  12.277  31.748  1.00 49.02           O  
ATOM   2829  N   LEU S 818      31.536   8.470  30.231  1.00 44.93           N  
ATOM   2830  CA  LEU S 818      30.335   7.663  30.149  1.00 45.78           C  
ATOM   2831  C   LEU S 818      30.359   6.882  28.846  1.00 46.89           C  
ATOM   2832  O   LEU S 818      30.163   5.663  28.833  1.00 46.50           O  
ATOM   2833  CB  LEU S 818      29.077   8.537  30.219  1.00 45.65           C  
ATOM   2834  CG  LEU S 818      27.741   7.788  30.147  1.00 45.58           C  
ATOM   2835  CD1 LEU S 818      27.612   6.809  31.318  1.00 45.36           C  
ATOM   2836  CD2 LEU S 818      26.551   8.719  30.133  1.00 43.95           C  
ATOM   2837  N   LEU S 819      30.654   7.588  27.760  1.00 48.01           N  
ATOM   2838  CA  LEU S 819      30.607   7.014  26.420  1.00 49.24           C  
ATOM   2839  C   LEU S 819      31.559   5.829  26.247  1.00 50.32           C  
ATOM   2840  O   LEU S 819      31.169   4.777  25.731  1.00 50.11           O  
ATOM   2841  CB  LEU S 819      30.903   8.105  25.380  1.00 49.22           C  
ATOM   2842  CG  LEU S 819      30.848   7.724  23.901  1.00 49.32           C  
ATOM   2843  CD1 LEU S 819      29.495   7.178  23.497  1.00 48.73           C  
ATOM   2844  CD2 LEU S 819      31.205   8.940  23.058  1.00 49.85           C  
ATOM   2845  N   ARG S 820      32.801   6.005  26.684  1.00 51.33           N  
ATOM   2846  CA  ARG S 820      33.807   4.966  26.550  1.00 52.53           C  
ATOM   2847  C   ARG S 820      33.471   3.748  27.414  1.00 52.95           C  
ATOM   2848  O   ARG S 820      33.534   2.606  26.942  1.00 53.06           O  
ATOM   2849  CB  ARG S 820      35.185   5.529  26.898  1.00 52.91           C  
ATOM   2850  CG  ARG S 820      35.620   6.583  25.904  1.00 54.20           C  
ATOM   2851  CD  ARG S 820      37.044   7.046  26.040  1.00 55.94           C  
ATOM   2852  NE  ARG S 820      37.320   8.113  25.081  1.00 58.09           N  
ATOM   2853  CZ  ARG S 820      38.453   8.808  25.022  1.00 59.82           C  
ATOM   2854  NH1 ARG S 820      39.448   8.555  25.867  1.00 60.28           N  
ATOM   2855  NH2 ARG S 820      38.590   9.765  24.108  1.00 60.61           N  
ATOM   2856  N   ALA S 821      33.106   3.994  28.670  1.00 53.36           N  
ATOM   2857  CA  ALA S 821      32.698   2.920  29.561  1.00 53.67           C  
ATOM   2858  C   ALA S 821      31.598   2.094  28.892  1.00 54.08           C  
ATOM   2859  O   ALA S 821      31.648   0.862  28.897  1.00 54.01           O  
ATOM   2860  CB  ALA S 821      32.215   3.479  30.883  1.00 53.55           C  
ATOM   2861  N   LEU S 822      30.616   2.777  28.308  1.00 54.44           N  
ATOM   2862  CA  LEU S 822      29.516   2.110  27.622  1.00 54.93           C  
ATOM   2863  C   LEU S 822      30.007   1.342  26.398  1.00 55.41           C  
ATOM   2864  O   LEU S 822      29.557   0.230  26.143  1.00 55.60           O  
ATOM   2865  CB  LEU S 822      28.445   3.117  27.212  1.00 54.90           C  
ATOM   2866  CG  LEU S 822      27.667   3.756  28.361  1.00 54.80           C  
ATOM   2867  CD1 LEU S 822      26.531   4.601  27.801  1.00 54.39           C  
ATOM   2868  CD2 LEU S 822      27.139   2.702  29.335  1.00 54.48           C  
ATOM   2869  N   ASP S 823      30.911   1.949  25.634  1.00 55.82           N  
ATOM   2870  CA  ASP S 823      31.525   1.282  24.492  1.00 56.04           C  
ATOM   2871  C   ASP S 823      32.893   0.735  24.901  1.00 56.10           C  
ATOM   2872  O   ASP S 823      33.186  -0.451  24.731  1.00 56.09           O  
ATOM   2873  CB  ASP S 823      31.688   2.252  23.320  1.00 56.21           C  
ATOM   2874  CG  ASP S 823      31.858   1.535  21.997  1.00 56.45           C  
ATOM   2875  OD1 ASP S 823      32.245   0.351  22.028  1.00 58.65           O  
ATOM   2876  OD2 ASP S 823      31.628   2.056  20.885  1.00 56.19           O  
TER    2877      ASP S 823                                                      
HETATM 2878 FE   FE2 A1350      23.294  27.501  28.594  1.00 20.46          FE  
HETATM 2879  C1  OGA A1351      22.091  25.173  27.594  1.00 24.79           C  
HETATM 2880  C2  OGA A1351      21.066  25.829  28.202  1.00 24.27           C  
HETATM 2881  C4  OGA A1351      18.756  25.714  29.004  1.00 23.09           C  
HETATM 2882  C5  OGA A1351      17.415  25.241  28.495  1.00 23.17           C  
HETATM 2883  O1  OGA A1351      21.909  24.061  27.090  1.00 25.24           O  
HETATM 2884  O2  OGA A1351      23.219  25.658  27.531  1.00 24.40           O  
HETATM 2885  O2' OGA A1351      21.192  26.959  28.711  1.00 21.19           O  
HETATM 2886  O3  OGA A1351      16.416  25.662  29.055  1.00 23.03           O  
HETATM 2887  N1  OGA A1351      19.886  25.203  28.228  1.00 21.70           N  
HETATM 2888  O4  OGA A1351      17.332  24.475  27.537  1.00 23.98           O  
HETATM 2889  S   SO4 A1352       0.316  25.182  43.602  1.00 77.77           S  
HETATM 2890  O1  SO4 A1352       1.239  25.980  44.403  1.00 77.64           O  
HETATM 2891  O2  SO4 A1352       1.075  24.260  42.760  1.00 77.88           O  
HETATM 2892  O3  SO4 A1352      -0.525  24.416  44.514  1.00 78.38           O  
HETATM 2893  O4  SO4 A1352      -0.507  26.042  42.757  1.00 76.90           O  
HETATM 2894  S   SO4 A1353       1.990  28.487  29.834  1.00 69.20           S  
HETATM 2895  O1  SO4 A1353       3.243  29.065  30.309  1.00 68.34           O  
HETATM 2896  O2  SO4 A1353       2.236  27.438  28.847  1.00 67.90           O  
HETATM 2897  O3  SO4 A1353       1.298  27.948  31.009  1.00 70.32           O  
HETATM 2898  O4  SO4 A1353       1.162  29.517  29.203  1.00 69.63           O  
HETATM 2899  O   HOH A2001       9.466  21.720  12.039  1.00 63.79           O  
HETATM 2900  O   HOH A2002       1.367  21.270   7.724  1.00 60.01           O  
HETATM 2901  O   HOH A2003       3.426  13.325   8.811  1.00 43.04           O  
HETATM 2902  O   HOH A2004      -0.760  13.029   7.574  1.00 47.08           O  
HETATM 2903  O   HOH A2005       2.515  19.304   5.195  1.00 46.76           O  
HETATM 2904  O   HOH A2006       4.861  33.534  13.331  1.00 75.60           O  
HETATM 2905  O   HOH A2007       1.403  29.250  13.007  1.00 46.80           O  
HETATM 2906  O   HOH A2008      13.563  35.806  31.131  1.00 39.09           O  
HETATM 2907  O   HOH A2009       1.614  32.100  13.758  1.00 66.18           O  
HETATM 2908  O   HOH A2010      12.671  34.540  13.968  1.00 43.83           O  
HETATM 2909  O   HOH A2011      11.399   2.867  17.750  1.00 68.06           O  
HETATM 2910  O   HOH A2012      -1.220  30.205  22.820  1.00 80.54           O  
HETATM 2911  O   HOH A2013       6.576  36.529  29.511  1.00 43.88           O  
HETATM 2912  O   HOH A2014       3.525  32.513  31.866  1.00 65.87           O  
HETATM 2913  O   HOH A2015       5.033  37.447  27.566  1.00 54.03           O  
HETATM 2914  O   HOH A2016      10.981  35.615  30.196  1.00 36.24           O  
HETATM 2915  O   HOH A2017      12.816  42.461  26.787  1.00 37.83           O  
HETATM 2916  O   HOH A2018      13.508  37.138  13.905  1.00 50.79           O  
HETATM 2917  O   HOH A2019      11.439   7.927  15.708  1.00 63.10           O  
HETATM 2918  O   HOH A2020      16.409   3.305  16.425  1.00 59.87           O  
HETATM 2919  O   HOH A2021      14.424   4.598  17.530  1.00 54.39           O  
HETATM 2920  O   HOH A2022      15.821  30.360  12.573  1.00 43.61           O  
HETATM 2921  O   HOH A2023      13.496  22.189   7.246  1.00 57.93           O  
HETATM 2922  O   HOH A2024      17.591  29.863   7.160  1.00 49.97           O  
HETATM 2923  O   HOH A2025      14.617  26.200  13.898  1.00 48.56           O  
HETATM 2924  O   HOH A2026      20.840  23.785   3.695  1.00 38.79           O  
HETATM 2925  O   HOH A2027      27.946  19.151   9.101  1.00 43.14           O  
HETATM 2926  O   HOH A2028      23.279  21.788   0.672  1.00 62.23           O  
HETATM 2927  O   HOH A2029      27.443  22.009  43.177  1.00 68.81           O  
HETATM 2928  O   HOH A2030      27.326  30.900   5.769  1.00 84.31           O  
HETATM 2929  O   HOH A2031      16.938  35.662  41.749  1.00 51.88           O  
HETATM 2930  O   HOH A2032      36.792  29.262  21.033  1.00 42.38           O  
HETATM 2931  O   HOH A2033      26.719  37.403  13.167  1.00 60.20           O  
HETATM 2932  O   HOH A2034      29.797  37.021  10.379  1.00 60.24           O  
HETATM 2933  O   HOH A2035      28.365  37.713  15.023  1.00 68.08           O  
HETATM 2934  O   HOH A2036      27.471  34.815   9.298  1.00 63.90           O  
HETATM 2935  O   HOH A2037      24.262  32.919  12.792  1.00 45.02           O  
HETATM 2936  O   HOH A2038      19.704  17.909  13.178  1.00 28.78           O  
HETATM 2937  O   HOH A2039      22.022  12.870   8.792  1.00 48.37           O  
HETATM 2938  O   HOH A2040      18.151  14.971  12.982  1.00 36.76           O  
HETATM 2939  O   HOH A2041      29.160   5.439  16.977  1.00 44.05           O  
HETATM 2940  O   HOH A2042      18.863  14.590  16.204  1.00 30.84           O  
HETATM 2941  O   HOH A2043      12.149   5.293  13.385  1.00 72.13           O  
HETATM 2942  O   HOH A2044      15.651   2.782  13.845  1.00 41.52           O  
HETATM 2943  O   HOH A2045      14.014   7.467  18.234  1.00 52.22           O  
HETATM 2944  O   HOH A2046      40.791  21.415  26.920  1.00 58.98           O  
HETATM 2945  O   HOH A2047       5.548  12.548  27.846  1.00 38.03           O  
HETATM 2946  O   HOH A2048      12.742   5.782  36.187  1.00 51.07           O  
HETATM 2947  O   HOH A2049      19.063   6.567  36.600  1.00 49.16           O  
HETATM 2948  O   HOH A2050       7.710  14.276  19.473  1.00 48.41           O  
HETATM 2949  O   HOH A2051      19.545   2.633  38.104  1.00 67.28           O  
HETATM 2950  O   HOH A2052      15.732   7.234  38.833  1.00 54.12           O  
HETATM 2951  O   HOH A2053      21.932  13.291  44.351  1.00 62.49           O  
HETATM 2952  O   HOH A2054      33.998  44.086  25.334  1.00 53.56           O  
HETATM 2953  O   HOH A2055      12.673  21.178  43.612  1.00 63.01           O  
HETATM 2954  O   HOH A2056       8.172  26.738  44.107  1.00 61.46           O  
HETATM 2955  O   HOH A2057       9.613  30.854  42.520  1.00 54.56           O  
HETATM 2956  O   HOH A2058      15.688  37.473  35.304  1.00 47.58           O  
HETATM 2957  O   HOH A2059       7.422  43.868  25.982  1.00 75.57           O  
HETATM 2958  O   HOH A2060       7.978  38.223  34.865  1.00 59.51           O  
HETATM 2959  O   HOH A2061      17.035  27.760  38.288  1.00 52.22           O  
HETATM 2960  O   HOH A2062      16.338  30.836  40.223  1.00 38.80           O  
HETATM 2961  O   HOH A2063      22.131  25.023  41.390  1.00 55.16           O  
HETATM 2962  O   HOH A2064      31.794  27.570  41.962  1.00 48.59           O  
HETATM 2963  O   HOH A2065      29.869  29.910  39.122  1.00 47.28           O  
HETATM 2964  O   HOH A2066      28.353  24.399  41.766  1.00 60.35           O  
HETATM 2965  O   HOH A2067      24.838  24.783  42.190  1.00 52.90           O  
HETATM 2966  O   HOH A2068      28.058  28.695  48.927  1.00 65.95           O  
HETATM 2967  O   HOH A2069      11.541  32.183  15.082  1.00 63.99           O  
HETATM 2968  O   HOH A2070      31.599  33.767  45.823  1.00 44.28           O  
HETATM 2969  O   HOH A2071      24.728  38.721  49.282  1.00 48.25           O  
HETATM 2970  O   HOH A2072      17.845  37.716  46.244  1.00 57.93           O  
HETATM 2971  O   HOH A2073      16.271  36.399  44.087  1.00 58.46           O  
HETATM 2972  O   HOH A2074      16.480  33.117  41.520  1.00 59.15           O  
HETATM 2973  O   HOH A2075      21.842  17.819  48.106  1.00 67.11           O  
HETATM 2974  O   HOH A2076       8.791  17.468  46.626  1.00 63.28           O  
HETATM 2975  O   HOH A2077      21.626  14.804  40.702  1.00 53.91           O  
HETATM 2976  O   HOH A2078      17.141  16.914  47.607  1.00 52.87           O  
HETATM 2977  O   HOH A2079      39.117  50.091  47.735  1.00 57.17           O  
HETATM 2978  O   HOH A2080      10.617  19.257  44.587  1.00 69.00           O  
HETATM 2979  O   HOH A2081       1.682  24.435  36.842  1.00 55.40           O  
HETATM 2980  O   HOH A2082       4.627  30.781  36.487  1.00 53.38           O  
HETATM 2981  O   HOH A2083      18.429  25.785  36.464  1.00 54.65           O  
HETATM 2982  O   HOH A2084      17.463  26.906  33.818  1.00 38.64           O  
HETATM 2983  O   HOH A2085      23.466  17.336  36.578  1.00 41.94           O  
HETATM 2984  O   HOH A2086      26.890  12.949  30.365  1.00 49.34           O  
HETATM 2985  O   HOH A2087      21.694  10.405  34.333  1.00 45.95           O  
HETATM 2986  O   HOH A2088      20.030   9.589  36.847  1.00 52.33           O  
HETATM 2987  O   HOH A2089      18.447  -1.706  32.981  1.00 66.29           O  
HETATM 2988  O   HOH A2090      16.300  -0.205  30.017  1.00 50.70           O  
HETATM 2989  O   HOH A2091      17.950   1.645  20.589  1.00 51.55           O  
HETATM 2990  O   HOH A2092      26.301   5.439  16.918  1.00 36.67           O  
HETATM 2991  O   HOH A2093      33.944  10.218  13.383  1.00 51.60           O  
HETATM 2992  O   HOH A2094      30.893  16.371  11.174  1.00 40.00           O  
HETATM 2993  O   HOH A2095      32.606  13.689  20.709  1.00 45.01           O  
HETATM 2994  O   HOH A2096      36.957  10.422   7.614  1.00 76.91           O  
HETATM 2995  O   HOH A2097      31.860  10.158   7.765  1.00 58.55           O  
HETATM 2996  O   HOH A2098      35.951  16.836  31.735  1.00 59.28           O  
HETATM 2997  O   HOH A2099      39.867  18.412  27.150  1.00 50.38           O  
HETATM 2998  O   HOH A2100      13.436  20.952  28.355  1.00 27.89           O  
HETATM 2999  O   HOH A2101       3.992  21.265  30.540  1.00 43.76           O  
HETATM 3000  O   HOH A2102      30.735  37.910  33.103  1.00 30.45           O  
HETATM 3001  O   HOH A2103      25.986  26.303  26.047  1.00 26.08           O  
HETATM 3002  O   HOH A2104      35.845  25.360  27.653  1.00 33.53           O  
HETATM 3003  O   HOH A2105      36.837  32.025  33.001  1.00 37.86           O  
HETATM 3004  O   HOH A2106      31.874  20.474  33.040  1.00 55.47           O  
HETATM 3005  O   HOH A2107      36.793  26.619  20.918  1.00 34.57           O  
HETATM 3006  O   HOH A2108      17.114  16.909  17.862  1.00 35.83           O  
HETATM 3007  O   HOH A2109       9.968  13.510  19.464  1.00 37.10           O  
HETATM 3008  O   HOH A2110       5.274  16.717  22.023  1.00 44.26           O  
HETATM 3009  O   HOH A2111       7.041  16.862  20.149  1.00 37.71           O  
HETATM 3010  O   HOH A2112       6.517  22.763  22.963  1.00 38.94           O  
HETATM 3011  O   HOH A2113      32.253  43.121  24.229  1.00 53.95           O  
HETATM 3012  O   HOH A2114      29.471  38.812  26.249  1.00 22.19           O  
HETATM 3013  O   HOH A2115      30.645  39.042  18.925  1.00 33.21           O  
HETATM 3014  O   HOH A2116      28.797  40.227  16.136  1.00 64.15           O  
HETATM 3015  O   HOH A2117      25.466  42.302  17.883  1.00 64.00           O  
HETATM 3016  O   HOH A2118      27.698  44.486  31.068  1.00 26.13           O  
HETATM 3017  O   HOH A2119      27.635  48.525  29.776  1.00 35.59           O  
HETATM 3018  O   HOH A2120      30.274  44.879  25.031  1.00 38.32           O  
HETATM 3019  O   HOH A2121      25.933  50.527  30.463  1.00 35.79           O  
HETATM 3020  O   HOH A2122      26.614  31.094  38.158  1.00 32.11           O  
HETATM 3021  O   HOH A2123      29.486  36.934  35.226  1.00 27.40           O  
HETATM 3022  O   HOH A2124      30.510  30.229  36.300  1.00 31.99           O  
HETATM 3023  O   HOH A2125      19.859  31.575  33.786  1.00 31.77           O  
HETATM 3024  O   HOH A2126      19.538  36.155  33.217  1.00 30.91           O  
HETATM 3025  O   HOH A2127      18.490  38.301  36.415  1.00 43.54           O  
HETATM 3026  O   HOH A2128      21.227  42.704  39.938  1.00 38.88           O  
HETATM 3027  O   HOH A2129      25.386  44.358  40.124  1.00 54.33           O  
HETATM 3028  O   HOH A2130      17.603  37.763  31.961  1.00 35.39           O  
HETATM 3029  O   HOH A2131       9.290  41.007  35.589  1.00 51.53           O  
HETATM 3030  O   HOH A2132      15.089  37.816  32.481  1.00 32.05           O  
HETATM 3031  O   HOH A2133       9.348  43.374  27.752  1.00 61.17           O  
HETATM 3032  O   HOH A2134      10.824  48.278  31.295  1.00 52.52           O  
HETATM 3033  O   HOH A2135      15.962  46.870  38.981  1.00 51.42           O  
HETATM 3034  O   HOH A2136      15.691  44.668  34.824  1.00 31.47           O  
HETATM 3035  O   HOH A2137      14.202  48.658  24.558  1.00 43.59           O  
HETATM 3036  O   HOH A2138      13.481  51.613  32.894  1.00 45.77           O  
HETATM 3037  O   HOH A2139      16.193  44.497  37.574  1.00 58.87           O  
HETATM 3038  O   HOH A2140      15.573  46.265  24.419  1.00 39.51           O  
HETATM 3039  O   HOH A2141      15.284  50.258  22.000  1.00 32.96           O  
HETATM 3040  O   HOH A2142      14.817  55.477  27.388  1.00 52.87           O  
HETATM 3041  O   HOH A2143      18.684  55.873  28.304  1.00 58.28           O  
HETATM 3042  O   HOH A2144      23.651  46.151  19.718  1.00 33.04           O  
HETATM 3043  O   HOH A2145      16.751  46.565  21.800  1.00 33.97           O  
HETATM 3044  O   HOH A2146      12.595  29.171  13.536  1.00 39.79           O  
HETATM 3045  O   HOH A2147      10.812  19.188  14.084  1.00 50.88           O  
HETATM 3046  O   HOH A2148      14.521  18.471  12.156  1.00 37.16           O  
HETATM 3047  O   HOH A2149      11.495  21.508  13.792  1.00 44.23           O  
HETATM 3048  O   HOH A2150      33.566  26.082  16.801  1.00 38.34           O  
HETATM 3049  O   HOH A2151      27.798  27.494  24.390  1.00 25.11           O  
HETATM 3050  O   HOH A2152      30.253  36.176  26.688  1.00 27.79           O  
HETATM 3051  O   HOH A2153      27.363  30.094  25.612  1.00 23.74           O  
HETATM 3052  O   HOH A2154      32.762  34.069  19.065  1.00 47.61           O  
HETATM 3053  O   HOH A2155      16.282  36.168  29.566  1.00 33.13           O  
HETATM 3054  O   HOH A2156      13.289  26.522  28.472  1.00 47.17           O  
HETATM 3055  O   HOH A2157       7.556  30.888  24.716  1.00 44.35           O  
HETATM 3056  O   HOH A2158       7.790  30.392  27.265  1.00 37.71           O  
HETATM 3057  O   HOH A2159       3.910  21.360  21.198  1.00 60.23           O  
HETATM 3058  O   HOH A2160       6.411  23.837  25.422  1.00 40.51           O  
HETATM 3059  O   HOH A2161       5.352  18.754  24.064  1.00 42.17           O  
HETATM 3060  O   HOH A2162       3.001  17.561  27.759  1.00 55.61           O  
HETATM 3061  O   HOH A2163      40.897  21.985  24.633  1.00 54.83           O  
HETATM 3062  O   HOH A2164      42.626  37.977  17.732  1.00 71.69           O  
HETATM 3063  O   HOH A2165      42.463  44.114  19.559  1.00 54.59           O  
HETATM 3064  O   HOH A2166      33.754  36.855  19.984  1.00 36.17           O  
HETATM 3065  O   HOH A2167      33.194  39.271  33.406  1.00 28.26           O  
HETATM 3066  O   HOH A2168      38.789  34.566  42.752  1.00 40.46           O  
HETATM 3067  O   HOH A2169      37.482  29.751  37.743  1.00 57.74           O  
HETATM 3068  O   HOH A2170      32.020  40.390  44.008  1.00 38.46           O  
HETATM 3069  O   HOH A2171      31.865  44.151  45.174  1.00 45.64           O  
HETATM 3070  O   HOH A2172      38.498  47.344  48.085  1.00 60.19           O  
HETATM 3071  O   HOH A2173      41.427  43.475  51.164  1.00 50.64           O  
HETATM 3072  O   HOH A2174      35.239  52.784  45.826  1.00 54.63           O  
HETATM 3073  O   HOH A2175      32.343  51.933  45.286  1.00 58.03           O  
HETATM 3074  O   HOH A2176      39.267  57.239  41.745  1.00 26.45           O  
HETATM 3075  O   HOH A2177      32.755  59.287  44.804  1.00 60.46           O  
HETATM 3076  O   HOH A2178      37.840  55.111  29.241  1.00 44.20           O  
HETATM 3077  O   HOH A2179      46.839  53.182  31.757  1.00 31.38           O  
HETATM 3078  O   HOH S2001      35.955  31.618  40.285  1.00 80.01           O  
HETATM 3079  O   HOH S2002      38.513  33.804  31.613  1.00 33.04           O  
HETATM 3080  O   HOH S2003      38.106  25.337  29.179  1.00 54.79           O  
HETATM 3081  O   HOH S2004      36.648  25.786  38.779  1.00 76.96           O  
HETATM 3082  O   HOH S2005      30.766  25.787  37.613  1.00 54.75           O  
HETATM 3083  O   HOH S2006      33.667  28.867  40.196  1.00 59.66           O  
HETATM 3084  O   HOH S2007      33.934  31.237  38.711  1.00 40.66           O  
HETATM 3085  O   HOH S2008      34.990  30.561  34.967  1.00 30.13           O  
HETATM 3086  O   HOH S2009      28.622  27.043  37.556  1.00 57.58           O  
HETATM 3087  O   HOH S2010      19.894  26.655  33.706  1.00 54.88           O  
HETATM 3088  O   HOH S2011      30.052  24.213  35.628  1.00 41.23           O  
HETATM 3089  O   HOH S2012      28.737  12.960  37.083  1.00 59.80           O  
HETATM 3090  O   HOH S2013      35.568  13.822  23.888  1.00 38.00           O  
HETATM 3091  O   HOH S2014      32.110   2.136  17.673  1.00 69.92           O  
HETATM 3092  O   HOH S2015      30.722  -1.323  21.296  1.00 48.92           O  
CONECT 1478 2878                                                                
CONECT 1498 2878                                                                
CONECT 2167 2878                                                                
CONECT 2878 1478 1498 2167 2884                                                 
CONECT 2878 2885                                                                
CONECT 2879 2880 2883 2884                                                      
CONECT 2880 2879 2885 2887                                                      
CONECT 2881 2882 2887                                                           
CONECT 2882 2881 2886 2888                                                      
CONECT 2883 2879                                                                
CONECT 2884 2878 2879                                                           
CONECT 2885 2878 2880                                                           
CONECT 2886 2882                                                                
CONECT 2887 2880 2881                                                           
CONECT 2888 2882                                                                
CONECT 2889 2890 2891 2892 2893                                                 
CONECT 2890 2889                                                                
CONECT 2891 2889                                                                
CONECT 2892 2889                                                                
CONECT 2893 2889                                                                
CONECT 2894 2895 2896 2897 2898                                                 
CONECT 2895 2894                                                                
CONECT 2896 2894                                                                
CONECT 2897 2894                                                                
CONECT 2898 2894                                                                
MASTER      440    0    4   15   20    0    7    6 3090    2   25   31          
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.