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.


***  GFP  ***

elNémo ID: 21111011211799632

Job options:

ID        	=	 21111011211799632
JOBID     	=	 GFP
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER GFP

HEADER    FLUORESCENT PROTEIN                     16-JAN-14   4OGS              
TITLE     CRYSTAL STRUCTURE OF GFP S205A/T203V AT 2.2 A RESOLUTION              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GREEN FLUORESCENT PROTEIN;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA;                              
SOURCE   3 ORGANISM_COMMON: JELLYFISH;                                          
SOURCE   4 ORGANISM_TAXID: 6100;                                                
SOURCE   5 GENE: GFP;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA-CAN, FLUORESCENT PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.REMINGTON,M.SAIF                                                  
REVDAT   2   18-JUN-14 4OGS    1       JRNL                                     
REVDAT   1   14-MAY-14 4OGS    0                                                
JRNL        AUTH   V.WINEMAN-FISHER,R.SIMKOVITCH,S.SHOMER,R.GEPSHTEIN,          
JRNL        AUTH 2 D.HUPPERT,M.SAIF,K.KALLIO,S.J.REMINGTON,Y.MILLER             
JRNL        TITL   INSIGHT INTO THE STRUCTURE AND THE MECHANISM OF THE SLOW     
JRNL        TITL 2 PROTON TRANSFER IN THE GFP DOUBLE MUTANT T203V/S205A.        
JRNL        REF    PHYS CHEM CHEM PHYS           V.  16 11211 2014              
JRNL        REFN                   ISSN 1463-9076                               
JRNL        PMID   24776960                                                     
JRNL        DOI    10.1039/C4CP00311J                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 65.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 14492                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 778                             
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) : 2.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 42                           
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 2.62                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1                            
REMARK   3   BIN FREE R VALUE                    : 0.6930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3519                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.02000                                              
REMARK   3    B22 (A**2) : 3.02000                                              
REMARK   3    B33 (A**2) : -6.03000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.381        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3611 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3275 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4906 ; 1.813 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7521 ; 0.800 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   448 ; 7.737 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;36.252 ;24.706       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   557 ;17.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;15.841 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   531 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4182 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   859 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4OGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084473.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27588                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 31.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE PRODUCED USING 1 UL        
REMARK 280  PROTEIN (26 MG/ML IN 0.1 M IMIDAZOLE, PH 7.8) MIXED WITH 1 UL       
REMARK 280  WELL SOLUTION, CRYSTALLIZATION SCREENS VARIED FROM 22% TO 32% (W:   
REMARK 280  V) POLYETHYLENE GLYCOL MONOMETHYL ETHER (PEG) 2000 AND 0.05M TO     
REMARK 280  0.2M KBR AT ROOM TEMPERATURE, FOR A RANGE OF PH VALUES NEAR         
REMARK 280  NEUTRALITY, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.61500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.30450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.30450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.80750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.30450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.30450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       89.42250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.30450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.30450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.80750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.30450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.30450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       89.42250            
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       59.61500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A     2                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     MET A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     TYR A   237                                                      
REMARK 465     LYS A   238                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     MET B   233                                                      
REMARK 465     ASP B   234                                                      
REMARK 465     GLU B   235                                                      
REMARK 465     LEU B   236                                                      
REMARK 465     TYR B   237                                                      
REMARK 465     LYS B   238                                                      
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     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     GLU A   5    CD   OE1  OE2                                       
REMARK 470     LYS A  26    NZ                                                  
REMARK 470     LYS A  52    CD   CE   NZ                                        
REMARK 470     CRO A  66    CG1                                                 
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     GLU A  90    OE2                                                 
REMARK 470     LYS A 101    CD   CE   NZ                                        
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     LYS A 131    NZ                                                  
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 156    CG   CD   CE   NZ                                   
REMARK 470     LYS A 158    CE   NZ                                             
REMARK 470     LYS A 162    CE   NZ                                             
REMARK 470     ILE A 171    CD1                                                 
REMARK 470     GLU A 172    CD   OE1  OE2                                       
REMARK 470     VAL A 193    CG1  CG2                                            
REMARK 470     LEU A 195    CD1  CD2                                            
REMARK 470     LEU A 221    CD1  CD2                                            
REMARK 470     GLU B   5    OE2                                                 
REMARK 470     LYS B  26    CD   CE   NZ                                        
REMARK 470     GLU B  32    CD   OE1  OE2                                       
REMARK 470     ILE B  47    CG1  CG2  CD1                                       
REMARK 470     CRO B  66    CG1                                                 
REMARK 470     LYS B  79    NZ                                                  
REMARK 470     ARG B  80    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B  90    CD   OE1  OE2                                       
REMARK 470     ILE B  98    CD1                                                 
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     GLU B 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 156    CG   CD   CE   NZ                                   
REMARK 470     GLN B 157    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS B 158    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     GLU B 172    CD   OE1  OE2                                       
REMARK 470     GLN B 184    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 214    CG   CD   CE   NZ                                   
REMARK 470     HIS B 231    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   305     O    HOH B   425     6555     2.06            
REMARK 500   CG   LYS A   101     O    HOH A   318     7555     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  90   CB    GLU B  90   CG      0.307                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  21      108.22   -164.43                                   
REMARK 500    PRO A  75      170.78    -55.25                                   
REMARK 500    ASP A 103     -170.49   -170.99                                   
REMARK 500    PHE A 165      162.58    177.12                                   
REMARK 500    VAL A 193      170.74    -38.67                                   
REMARK 500    SER B  86      -49.39    -25.09                                   
REMARK 500    ASP B 103     -174.33   -179.26                                   
REMARK 500    GLU B 115       77.18   -115.78                                   
REMARK 500    ASP B 129        7.93     88.25                                   
REMARK 500    HIS B 199     -177.97   -170.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 366        DISTANCE =  5.07 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QLE   RELATED DB: PDB                                   
REMARK 900 GFP S205V MUTATION                                                   
DBREF  4OGS A    1   238  UNP    P42212   GFP_AEQVI        1    238             
DBREF  4OGS B    1   238  UNP    P42212   GFP_AEQVI        1    238             
SEQADV 4OGS CRO A   66  UNP  P42212    SER    65 CHROMOPHORE                    
SEQADV 4OGS CRO A   66  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 4OGS CRO A   66  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 4OGS ARG A   80  UNP  P42212    GLN    80 ENGINEERED MUTATION            
SEQADV 4OGS VAL A  203  UNP  P42212    THR   203 ENGINEERED MUTATION            
SEQADV 4OGS ALA A  205  UNP  P42212    SER   205 ENGINEERED MUTATION            
SEQADV 4OGS CRO B   66  UNP  P42212    SER    65 CHROMOPHORE                    
SEQADV 4OGS CRO B   66  UNP  P42212    TYR    66 CHROMOPHORE                    
SEQADV 4OGS CRO B   66  UNP  P42212    GLY    67 CHROMOPHORE                    
SEQADV 4OGS ARG B   80  UNP  P42212    GLN    80 ENGINEERED MUTATION            
SEQADV 4OGS VAL B  203  UNP  P42212    THR   203 ENGINEERED MUTATION            
SEQADV 4OGS ALA B  205  UNP  P42212    SER   205 ENGINEERED MUTATION            
SEQRES   1 A  236  MET SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO          
SEQRES   2 A  236  ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS          
SEQRES   3 A  236  PHE SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR          
SEQRES   4 A  236  GLY LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS          
SEQRES   5 A  236  LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR PHE CRO          
SEQRES   6 A  236  VAL GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS ARG          
SEQRES   7 A  236  HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL          
SEQRES   8 A  236  GLN GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR          
SEQRES   9 A  236  LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU          
SEQRES  10 A  236  VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU          
SEQRES  11 A  236  ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR          
SEQRES  12 A  236  ASN SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS          
SEQRES  13 A  236  ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE          
SEQRES  14 A  236  GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN          
SEQRES  15 A  236  ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP          
SEQRES  16 A  236  ASN HIS TYR LEU SER VAL GLN ALA ALA LEU SER LYS ASP          
SEQRES  17 A  236  PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE          
SEQRES  18 A  236  VAL THR ALA ALA GLY ILE THR HIS GLY MET ASP GLU LEU          
SEQRES  19 A  236  TYR LYS                                                      
SEQRES   1 B  236  MET SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO          
SEQRES   2 B  236  ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS          
SEQRES   3 B  236  PHE SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR          
SEQRES   4 B  236  GLY LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS          
SEQRES   5 B  236  LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR PHE CRO          
SEQRES   6 B  236  VAL GLN CYS PHE SER ARG TYR PRO ASP HIS MET LYS ARG          
SEQRES   7 B  236  HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL          
SEQRES   8 B  236  GLN GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR          
SEQRES   9 B  236  LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU          
SEQRES  10 B  236  VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU          
SEQRES  11 B  236  ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR          
SEQRES  12 B  236  ASN SER HIS ASN VAL TYR ILE MET ALA ASP LYS GLN LYS          
SEQRES  13 B  236  ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE          
SEQRES  14 B  236  GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN          
SEQRES  15 B  236  ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP          
SEQRES  16 B  236  ASN HIS TYR LEU SER VAL GLN ALA ALA LEU SER LYS ASP          
SEQRES  17 B  236  PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE          
SEQRES  18 B  236  VAL THR ALA ALA GLY ILE THR HIS GLY MET ASP GLU LEU          
SEQRES  19 B  236  TYR LYS                                                      
MODRES 4OGS CRO A   66  GLY                                                     
MODRES 4OGS CRO A   66  TYR                                                     
MODRES 4OGS CRO A   66  GLY                                                     
MODRES 4OGS CRO B   66  GLY                                                     
MODRES 4OGS CRO B   66  TYR                                                     
MODRES 4OGS CRO B   66  GLY                                                     
HET    CRO  A  66      21                                                       
HET    CRO  B  66      21                                                       
HET     CL  B 301       1                                                       
HETNAM     CRO {2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-                       
HETNAM   2 CRO  HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-            
HETNAM   3 CRO  YL}ACETIC ACID                                                  
HETNAM      CL CHLORIDE ION                                                     
HETSYN     CRO PEPTIDE DERIVED CHROMOPHORE                                      
FORMUL   1  CRO    2(C15 H17 N3 O5)                                             
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *155(H2 O)                                                    
HELIX    1   1 LYS A    3  PHE A    8  5                                   6    
HELIX    2   2 PRO A   56  VAL A   61  5                                   6    
HELIX    3   3 VAL A   68  SER A   72  5                                   5    
HELIX    4   4 PRO A   75  HIS A   81  5                                   7    
HELIX    5   5 ASP A   82  ALA A   87  1                                   6    
HELIX    6   6 GLU B    6  GLY B   10  5                                   5    
HELIX    7   7 PRO B   56  VAL B   61  5                                   6    
HELIX    8   8 VAL B   68  SER B   72  5                                   5    
HELIX    9   9 PRO B   75  HIS B   81  5                                   7    
HELIX   10  10 ASP B   82  ALA B   87  1                                   6    
SHEET    1   A12 VAL A  11  VAL A  22  0                                        
SHEET    2   A12 HIS A  25  ASP A  36 -1  O  GLY A  35   N  VAL A  12           
SHEET    3   A12 LYS A  41  CYS A  48 -1  O  LYS A  41   N  ASP A  36           
SHEET    4   A12 HIS A 217  ALA A 227 -1  O  LEU A 220   N  LEU A  44           
SHEET    5   A12 HIS A 199  SER A 208 -1  N  TYR A 200   O  ALA A 227           
SHEET    6   A12 SER A 147  ASP A 155 -1  N  HIS A 148   O  VAL A 203           
SHEET    7   A12 GLY A 160  ILE A 171 -1  O  LYS A 162   N  MET A 153           
SHEET    8   A12 SER A 175  PRO A 187 -1  O  SER A 175   N  ILE A 171           
SHEET    9   A12 TYR A  92  PHE A 100 -1  N  VAL A  93   O  THR A 186           
SHEET   10   A12 ASN A 105  GLU A 115 -1  O  VAL A 112   N  TYR A  92           
SHEET   11   A12 THR A 118  ILE A 128 -1  O  GLU A 124   N  ARG A 109           
SHEET   12   A12 VAL A  11  VAL A  22  1  N  PRO A  13   O  LEU A 119           
SHEET    1   B12 VAL B  12  VAL B  22  0                                        
SHEET    2   B12 HIS B  25  ASP B  36 -1  O  GLY B  35   N  VAL B  12           
SHEET    3   B12 LYS B  41  CYS B  48 -1  O  LYS B  41   N  ASP B  36           
SHEET    4   B12 HIS B 217  ALA B 227 -1  O  GLU B 222   N  LEU B  42           
SHEET    5   B12 HIS B 199  SER B 208 -1  N  TYR B 200   O  ALA B 227           
SHEET    6   B12 HIS B 148  ASP B 155 -1  N  ILE B 152   O  HIS B 199           
SHEET    7   B12 GLY B 160  ASN B 170 -1  O  GLY B 160   N  ASP B 155           
SHEET    8   B12 VAL B 176  PRO B 187 -1  O  GLN B 177   N  HIS B 169           
SHEET    9   B12 TYR B  92  PHE B 100 -1  N  VAL B  93   O  THR B 186           
SHEET   10   B12 ASN B 105  GLU B 115 -1  O  TYR B 106   N  ILE B  98           
SHEET   11   B12 THR B 118  ILE B 128 -1  O  GLU B 124   N  ARG B 109           
SHEET   12   B12 VAL B  12  VAL B  22  1  N  LEU B  15   O  ASN B 121           
LINK         C   PHE A  64                 N1  CRO A  66     1555   1555  1.33  
LINK         C3  CRO A  66                 N   VAL A  68     1555   1555  1.43  
LINK         C   PHE B  64                 N1  CRO B  66     1555   1555  1.35  
LINK         C3  CRO B  66                 N   VAL B  68     1555   1555  1.43  
CISPEP   1 MET A   88    PRO A   89          0         5.52                     
CISPEP   2 MET B   88    PRO B   89          0         8.54                     
SITE     1 AC1  5 ASN A 146  ARG A 168  ASN B 146  ARG B 168                    
SITE     2 AC1  5 HOH B 444                                                     
CRYST1   86.609   86.609  119.230  90.00  90.00  90.00 P 41 21 2    16          
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      0.011546  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008387        0.00000                         
ATOM      1  N   LYS A   3      35.602  45.373  17.376  1.00 91.99           N  
ATOM      2  CA  LYS A   3      34.849  44.102  17.574  1.00 86.75           C  
ATOM      3  C   LYS A   3      33.337  44.380  17.694  1.00 79.59           C  
ATOM      4  O   LYS A   3      32.871  45.206  18.492  1.00 66.87           O  
ATOM      5  CB  LYS A   3      35.391  43.308  18.783  1.00 83.06           C  
ATOM      6  N   GLY A   4      32.578  43.681  16.860  1.00 75.25           N  
ATOM      7  CA  GLY A   4      31.140  43.633  16.994  1.00 69.70           C  
ATOM      8  C   GLY A   4      30.684  42.917  18.247  1.00 67.96           C  
ATOM      9  O   GLY A   4      29.486  42.827  18.498  1.00 68.79           O  
ATOM     10  N   GLU A   5      31.636  42.382  19.019  1.00 67.87           N  
ATOM     11  CA  GLU A   5      31.375  41.864  20.355  1.00 61.46           C  
ATOM     12  C   GLU A   5      30.916  42.969  21.291  1.00 62.85           C  
ATOM     13  O   GLU A   5      30.125  42.713  22.191  1.00 65.45           O  
ATOM     14  CB  GLU A   5      32.600  41.111  20.909  1.00 62.50           C  
ATOM     15  CG  GLU A   5      33.825  41.940  21.264  1.00 65.60           C  
ATOM     16  N   GLU A   6      31.384  44.197  21.034  1.00 70.83           N  
ATOM     17  CA  GLU A   6      30.947  45.423  21.749  1.00 73.09           C  
ATOM     18  C   GLU A   6      29.503  45.828  21.475  1.00 64.45           C  
ATOM     19  O   GLU A   6      28.990  46.743  22.113  1.00 64.79           O  
ATOM     20  CB  GLU A   6      31.848  46.610  21.383  1.00 80.63           C  
ATOM     21  CG  GLU A   6      33.310  46.442  21.802  1.00 93.40           C  
ATOM     22  CD  GLU A   6      34.245  47.510  21.226  1.00100.20           C  
ATOM     23  OE1 GLU A   6      33.742  48.522  20.671  1.00 92.59           O  
ATOM     24  OE2 GLU A   6      35.491  47.334  21.334  1.00105.37           O1-
ATOM     25  N   LEU A   7      28.876  45.151  20.518  1.00 57.38           N  
ATOM     26  CA  LEU A   7      27.520  45.421  20.101  1.00 54.05           C  
ATOM     27  C   LEU A   7      26.513  44.584  20.868  1.00 51.63           C  
ATOM     28  O   LEU A   7      25.346  44.920  20.934  1.00 50.48           O  
ATOM     29  CB  LEU A   7      27.365  45.134  18.614  1.00 58.44           C  
ATOM     30  CG  LEU A   7      27.711  46.220  17.594  1.00 61.50           C  
ATOM     31  CD1 LEU A   7      29.201  46.487  17.506  1.00 69.55           C  
ATOM     32  CD2 LEU A   7      27.185  45.837  16.224  1.00 61.32           C  
ATOM     33  N   PHE A   8      26.964  43.491  21.449  1.00 53.74           N  
ATOM     34  CA  PHE A   8      26.074  42.597  22.168  1.00 56.32           C  
ATOM     35  C   PHE A   8      26.256  42.740  23.666  1.00 57.13           C  
ATOM     36  O   PHE A   8      25.726  41.961  24.460  1.00 56.06           O  
ATOM     37  CB  PHE A   8      26.288  41.170  21.667  1.00 57.95           C  
ATOM     38  CG  PHE A   8      25.913  41.016  20.233  1.00 55.05           C  
ATOM     39  CD1 PHE A   8      24.592  40.846  19.875  1.00 50.66           C  
ATOM     40  CD2 PHE A   8      26.869  41.133  19.240  1.00 57.87           C  
ATOM     41  CE1 PHE A   8      24.229  40.763  18.556  1.00 52.91           C  
ATOM     42  CE2 PHE A   8      26.519  41.039  17.914  1.00 56.26           C  
ATOM     43  CZ  PHE A   8      25.192  40.858  17.574  1.00 55.98           C  
ATOM     44  N   THR A   9      26.967  43.797  24.035  1.00 60.23           N  
ATOM     45  CA  THR A   9      27.175  44.174  25.426  1.00 64.54           C  
ATOM     46  C   THR A   9      25.915  44.200  26.312  1.00 62.03           C  
ATOM     47  O   THR A   9      26.029  44.126  27.532  1.00 65.59           O  
ATOM     48  CB  THR A   9      27.927  45.547  25.538  1.00 66.71           C  
ATOM     49  OG1 THR A   9      27.537  46.473  24.496  1.00 66.81           O  
ATOM     50  CG2 THR A   9      29.386  45.316  25.426  1.00 70.13           C  
ATOM     51  N   GLY A  10      24.731  44.330  25.725  1.00 59.29           N  
ATOM     52  CA  GLY A  10      23.522  44.357  26.522  1.00 61.15           C  
ATOM     53  C   GLY A  10      22.461  43.363  26.099  1.00 61.04           C  
ATOM     54  O   GLY A  10      22.762  42.222  25.790  1.00 66.93           O  
ATOM     55  N   VAL A  11      21.213  43.816  26.123  1.00 55.56           N  
ATOM     56  CA  VAL A  11      20.088  43.069  25.663  1.00 48.87           C  
ATOM     57  C   VAL A  11      19.687  43.772  24.410  1.00 50.91           C  
ATOM     58  O   VAL A  11      19.203  44.903  24.449  1.00 53.38           O  
ATOM     59  CB  VAL A  11      18.970  43.072  26.702  1.00 45.85           C  
ATOM     60  CG1 VAL A  11      17.712  42.369  26.197  1.00 44.38           C  
ATOM     61  CG2 VAL A  11      19.477  42.396  27.946  1.00 46.61           C  
ATOM     62  N   VAL A  12      19.941  43.107  23.289  1.00 52.90           N  
ATOM     63  CA  VAL A  12      19.696  43.658  21.957  1.00 49.00           C  
ATOM     64  C   VAL A  12      18.283  43.245  21.465  1.00 51.74           C  
ATOM     65  O   VAL A  12      17.775  42.165  21.832  1.00 48.99           O  
ATOM     66  CB  VAL A  12      20.824  43.196  21.022  1.00 47.97           C  
ATOM     67  CG1 VAL A  12      20.548  43.509  19.566  1.00 50.88           C  
ATOM     68  CG2 VAL A  12      22.128  43.827  21.456  1.00 46.12           C  
ATOM     69  N   PRO A  13      17.612  44.127  20.687  1.00 54.31           N  
ATOM     70  CA  PRO A  13      16.270  43.786  20.233  1.00 55.07           C  
ATOM     71  C   PRO A  13      16.312  43.064  18.919  1.00 50.35           C  
ATOM     72  O   PRO A  13      17.193  43.324  18.101  1.00 46.55           O  
ATOM     73  CB  PRO A  13      15.566  45.145  20.081  1.00 54.67           C  
ATOM     74  CG  PRO A  13      16.638  46.155  20.014  1.00 54.25           C  
ATOM     75  CD  PRO A  13      17.968  45.499  20.296  1.00 56.14           C  
ATOM     76  N   ILE A  14      15.341  42.177  18.729  1.00 47.36           N  
ATOM     77  CA  ILE A  14      15.371  41.291  17.607  1.00 45.81           C  
ATOM     78  C   ILE A  14      14.082  41.368  16.848  1.00 44.06           C  
ATOM     79  O   ILE A  14      13.045  41.467  17.437  1.00 47.16           O  
ATOM     80  CB  ILE A  14      15.663  39.859  18.074  1.00 44.99           C  
ATOM     81  CG1 ILE A  14      17.024  39.811  18.780  1.00 40.53           C  
ATOM     82  CG2 ILE A  14      15.609  38.899  16.902  1.00 43.89           C  
ATOM     83  CD1 ILE A  14      17.266  38.506  19.471  1.00 42.60           C  
ATOM     84  N   LEU A  15      14.195  41.334  15.528  1.00 46.30           N  
ATOM     85  CA  LEU A  15      13.087  41.313  14.615  1.00 49.38           C  
ATOM     86  C   LEU A  15      13.302  40.169  13.653  1.00 46.50           C  
ATOM     87  O   LEU A  15      14.347  40.034  13.091  1.00 45.38           O  
ATOM     88  CB  LEU A  15      13.068  42.622  13.830  1.00 55.62           C  
ATOM     89  CG  LEU A  15      11.922  43.630  13.996  1.00 60.80           C  
ATOM     90  CD1 LEU A  15      10.795  43.275  13.033  1.00 66.62           C  
ATOM     91  CD2 LEU A  15      11.403  43.736  15.431  1.00 64.60           C  
ATOM     92  N   VAL A  16      12.307  39.331  13.461  1.00 51.61           N  
ATOM     93  CA  VAL A  16      12.448  38.220  12.519  1.00 53.27           C  
ATOM     94  C   VAL A  16      11.345  38.290  11.457  1.00 53.48           C  
ATOM     95  O   VAL A  16      10.178  38.330  11.789  1.00 58.19           O  
ATOM     96  CB  VAL A  16      12.360  36.847  13.229  1.00 48.86           C  
ATOM     97  CG1 VAL A  16      12.629  35.727  12.250  1.00 47.09           C  
ATOM     98  CG2 VAL A  16      13.342  36.770  14.374  1.00 51.17           C  
ATOM     99  N   GLU A  17      11.710  38.285  10.183  1.00 55.66           N  
ATOM    100  CA  GLU A  17      10.720  38.193   9.129  1.00 55.25           C  
ATOM    101  C   GLU A  17      11.045  36.981   8.263  1.00 52.09           C  
ATOM    102  O   GLU A  17      12.139  36.870   7.704  1.00 48.19           O  
ATOM    103  CB  GLU A  17      10.672  39.489   8.300  1.00 58.25           C  
ATOM    104  CG  GLU A  17      10.417  40.773   9.108  1.00 61.58           C  
ATOM    105  CD  GLU A  17       9.024  40.839   9.753  1.00 67.27           C  
ATOM    106  OE1 GLU A  17       8.054  40.282   9.173  1.00 69.69           O  
ATOM    107  OE2 GLU A  17       8.894  41.457  10.845  1.00 69.21           O1-
ATOM    108  N   LEU A  18      10.083  36.062   8.188  1.00 51.97           N  
ATOM    109  CA  LEU A  18      10.201  34.888   7.346  1.00 51.28           C  
ATOM    110  C   LEU A  18       9.109  34.806   6.312  1.00 49.40           C  
ATOM    111  O   LEU A  18       7.921  34.727   6.626  1.00 48.03           O  
ATOM    112  CB  LEU A  18      10.185  33.600   8.161  1.00 52.16           C  
ATOM    113  CG  LEU A  18      10.105  32.312   7.324  1.00 53.17           C  
ATOM    114  CD1 LEU A  18      11.122  31.279   7.769  1.00 53.68           C  
ATOM    115  CD2 LEU A  18       8.701  31.720   7.373  1.00 54.44           C  
ATOM    116  N   ASP A  19       9.574  34.756   5.072  1.00 52.10           N  
ATOM    117  CA  ASP A  19       8.793  34.411   3.905  1.00 50.06           C  
ATOM    118  C   ASP A  19       8.899  32.947   3.524  1.00 44.74           C  
ATOM    119  O   ASP A  19       9.995  32.467   3.239  1.00 40.08           O  
ATOM    120  CB  ASP A  19       9.301  35.213   2.737  1.00 53.14           C  
ATOM    121  CG  ASP A  19       8.305  35.312   1.680  1.00 56.40           C  
ATOM    122  OD1 ASP A  19       7.239  35.880   1.998  1.00 64.96           O  
ATOM    123  OD2 ASP A  19       8.572  34.812   0.569  1.00 60.29           O1-
ATOM    124  N   GLY A  20       7.746  32.285   3.441  1.00 41.84           N  
ATOM    125  CA  GLY A  20       7.687  30.850   3.323  1.00 43.14           C  
ATOM    126  C   GLY A  20       6.800  30.211   2.276  1.00 46.29           C  
ATOM    127  O   GLY A  20       5.825  30.765   1.826  1.00 47.68           O  
ATOM    128  N   ASP A  21       7.163  28.989   1.917  1.00 52.87           N  
ATOM    129  CA  ASP A  21       6.510  28.244   0.867  1.00 53.16           C  
ATOM    130  C   ASP A  21       6.953  26.803   1.044  1.00 51.19           C  
ATOM    131  O   ASP A  21       8.106  26.503   0.815  1.00 50.16           O  
ATOM    132  CB  ASP A  21       6.975  28.799  -0.475  1.00 55.28           C  
ATOM    133  CG  ASP A  21       6.323  28.146  -1.661  1.00 56.10           C  
ATOM    134  OD1 ASP A  21       5.791  27.031  -1.538  1.00 62.45           O  
ATOM    135  OD2 ASP A  21       6.376  28.766  -2.745  1.00 63.72           O1-
ATOM    136  N   VAL A  22       6.050  25.937   1.501  1.00 52.19           N  
ATOM    137  CA  VAL A  22       6.344  24.518   1.666  1.00 53.47           C  
ATOM    138  C   VAL A  22       5.341  23.713   0.907  1.00 51.16           C  
ATOM    139  O   VAL A  22       4.174  23.731   1.245  1.00 57.00           O  
ATOM    140  CB  VAL A  22       6.282  24.061   3.135  1.00 54.00           C  
ATOM    141  CG1 VAL A  22       6.555  22.551   3.235  1.00 49.62           C  
ATOM    142  CG2 VAL A  22       7.271  24.867   3.971  1.00 55.50           C  
ATOM    143  N   ASN A  23       5.789  22.979  -0.093  1.00 53.47           N  
ATOM    144  CA  ASN A  23       4.868  22.305  -0.984  1.00 56.03           C  
ATOM    145  C   ASN A  23       3.897  23.294  -1.645  1.00 55.21           C  
ATOM    146  O   ASN A  23       2.755  22.958  -1.915  1.00 56.61           O  
ATOM    147  CB  ASN A  23       4.081  21.218  -0.228  1.00 54.85           C  
ATOM    148  CG  ASN A  23       4.850  19.927  -0.082  1.00 55.21           C  
ATOM    149  OD1 ASN A  23       6.073  19.890  -0.229  1.00 55.77           O  
ATOM    150  ND2 ASN A  23       4.128  18.848   0.181  1.00 56.37           N  
ATOM    151  N   GLY A  24       4.342  24.519  -1.889  1.00 51.89           N  
ATOM    152  CA  GLY A  24       3.474  25.522  -2.478  1.00 51.37           C  
ATOM    153  C   GLY A  24       2.540  26.263  -1.552  1.00 50.12           C  
ATOM    154  O   GLY A  24       1.932  27.241  -1.951  1.00 60.34           O  
ATOM    155  N   HIS A  25       2.395  25.791  -0.329  1.00 52.88           N  
ATOM    156  CA  HIS A  25       1.653  26.502   0.687  1.00 49.83           C  
ATOM    157  C   HIS A  25       2.436  27.683   1.118  1.00 51.40           C  
ATOM    158  O   HIS A  25       3.423  27.561   1.819  1.00 50.97           O  
ATOM    159  CB  HIS A  25       1.486  25.672   1.926  1.00 51.41           C  
ATOM    160  CG  HIS A  25       0.615  24.496   1.744  1.00 51.61           C  
ATOM    161  ND1 HIS A  25       1.121  23.238   1.520  1.00 54.30           N  
ATOM    162  CD2 HIS A  25      -0.727  24.374   1.777  1.00 51.25           C  
ATOM    163  CE1 HIS A  25       0.120  22.384   1.403  1.00 55.50           C  
ATOM    164  NE2 HIS A  25      -1.011  23.050   1.557  1.00 56.28           N  
ATOM    165  N   LYS A  26       1.951  28.846   0.754  1.00 55.82           N  
ATOM    166  CA  LYS A  26       2.593  30.055   1.157  1.00 53.67           C  
ATOM    167  C   LYS A  26       2.140  30.435   2.587  1.00 55.02           C  
ATOM    168  O   LYS A  26       1.051  30.037   3.051  1.00 55.95           O  
ATOM    169  CB  LYS A  26       2.287  31.155   0.159  1.00 54.35           C  
ATOM    170  CG  LYS A  26       2.024  30.722  -1.284  1.00 53.14           C  
ATOM    171  CD  LYS A  26       3.231  30.232  -2.049  1.00 51.90           C  
ATOM    172  CE  LYS A  26       2.784  29.657  -3.390  1.00 53.44           C  
ATOM    173  N   PHE A  27       3.016  31.161   3.287  1.00 52.95           N  
ATOM    174  CA  PHE A  27       2.774  31.643   4.645  1.00 48.78           C  
ATOM    175  C   PHE A  27       3.843  32.672   4.980  1.00 49.43           C  
ATOM    176  O   PHE A  27       4.813  32.839   4.256  1.00 52.85           O  
ATOM    177  CB  PHE A  27       2.744  30.522   5.694  1.00 48.24           C  
ATOM    178  CG  PHE A  27       4.022  29.781   5.813  1.00 47.70           C  
ATOM    179  CD1 PHE A  27       4.266  28.687   5.011  1.00 47.60           C  
ATOM    180  CD2 PHE A  27       4.980  30.181   6.714  1.00 51.60           C  
ATOM    181  CE1 PHE A  27       5.444  27.999   5.086  1.00 49.19           C  
ATOM    182  CE2 PHE A  27       6.175  29.503   6.811  1.00 52.91           C  
ATOM    183  CZ  PHE A  27       6.408  28.403   5.990  1.00 53.83           C  
ATOM    184  N   SER A  28       3.626  33.404   6.056  1.00 50.36           N  
ATOM    185  CA  SER A  28       4.558  34.413   6.477  1.00 47.98           C  
ATOM    186  C   SER A  28       4.488  34.467   7.971  1.00 44.17           C  
ATOM    187  O   SER A  28       3.425  34.297   8.581  1.00 42.64           O  
ATOM    188  CB  SER A  28       4.236  35.776   5.858  1.00 49.40           C  
ATOM    189  OG  SER A  28       4.600  35.824   4.490  1.00 48.43           O  
ATOM    190  N   VAL A  29       5.656  34.661   8.553  1.00 45.99           N  
ATOM    191  CA  VAL A  29       5.762  34.784   9.971  1.00 45.38           C  
ATOM    192  C   VAL A  29       6.594  35.978  10.304  1.00 45.03           C  
ATOM    193  O   VAL A  29       7.537  36.307   9.591  1.00 43.94           O  
ATOM    194  CB  VAL A  29       6.423  33.557  10.576  1.00 47.05           C  
ATOM    195  CG1 VAL A  29       6.526  33.691  12.084  1.00 47.39           C  
ATOM    196  CG2 VAL A  29       5.626  32.316  10.206  1.00 47.11           C  
ATOM    197  N   SER A  30       6.176  36.633  11.386  1.00 47.44           N  
ATOM    198  CA ASER A  30       6.911  37.735  11.993  0.60 45.72           C  
ATOM    199  CA BSER A  30       6.928  37.728  11.982  0.40 45.93           C  
ATOM    200  C   SER A  30       7.245  37.402  13.440  1.00 45.04           C  
ATOM    201  O   SER A  30       6.418  36.827  14.157  1.00 46.06           O  
ATOM    202  CB ASER A  30       6.090  39.019  11.932  0.60 45.96           C  
ATOM    203  CB BSER A  30       6.164  39.053  11.867  0.40 46.30           C  
ATOM    204  OG ASER A  30       6.060  39.524  10.613  0.60 45.53           O  
ATOM    205  OG BSER A  30       4.927  39.014  12.553  0.40 46.57           O  
ATOM    206  N   GLY A  31       8.461  37.745  13.856  1.00 44.41           N  
ATOM    207  CA  GLY A  31       8.890  37.564  15.229  1.00 45.84           C  
ATOM    208  C   GLY A  31       9.527  38.833  15.792  1.00 49.18           C  
ATOM    209  O   GLY A  31      10.039  39.712  15.056  1.00 45.16           O  
ATOM    210  N   GLU A  32       9.486  38.918  17.117  1.00 51.25           N  
ATOM    211  CA  GLU A  32      10.140  39.992  17.838  1.00 51.12           C  
ATOM    212  C   GLU A  32      10.535  39.516  19.222  1.00 45.48           C  
ATOM    213  O   GLU A  32       9.895  38.629  19.818  1.00 46.23           O  
ATOM    214  CB  GLU A  32       9.262  41.258  17.912  1.00 58.73           C  
ATOM    215  CG  GLU A  32       7.743  41.048  18.002  1.00 67.64           C  
ATOM    216  CD  GLU A  32       7.186  40.825  19.418  1.00 76.32           C  
ATOM    217  OE1 GLU A  32       7.797  41.304  20.405  1.00 84.56           O  
ATOM    218  OE2 GLU A  32       6.105  40.179  19.544  1.00 79.26           O1-
ATOM    219  N   GLY A  33      11.598  40.102  19.737  1.00 39.58           N  
ATOM    220  CA  GLY A  33      12.056  39.730  21.062  1.00 39.51           C  
ATOM    221  C   GLY A  33      13.367  40.375  21.409  1.00 39.25           C  
ATOM    222  O   GLY A  33      13.719  41.392  20.843  1.00 44.94           O  
ATOM    223  N   GLU A  34      14.115  39.764  22.309  1.00 43.74           N  
ATOM    224  CA  GLU A  34      15.374  40.342  22.722  1.00 46.08           C  
ATOM    225  C   GLU A  34      16.461  39.311  22.953  1.00 46.14           C  
ATOM    226  O   GLU A  34      16.174  38.150  23.218  1.00 45.20           O  
ATOM    227  CB  GLU A  34      15.160  41.198  23.953  1.00 49.46           C  
ATOM    228  CG  GLU A  34      14.144  40.679  24.957  1.00 51.81           C  
ATOM    229  CD  GLU A  34      13.887  41.690  26.049  1.00 51.69           C  
ATOM    230  OE1 GLU A  34      14.505  41.592  27.122  1.00 51.58           O  
ATOM    231  OE2 GLU A  34      13.068  42.605  25.820  1.00 61.12           O1-
ATOM    232  N   GLY A  35      17.706  39.759  22.831  1.00 46.50           N  
ATOM    233  CA  GLY A  35      18.882  38.892  22.954  1.00 46.96           C  
ATOM    234  C   GLY A  35      19.983  39.374  23.897  1.00 46.52           C  
ATOM    235  O   GLY A  35      20.585  40.418  23.708  1.00 44.15           O  
ATOM    236  N   ASP A  36      20.254  38.560  24.900  1.00 48.61           N  
ATOM    237  CA  ASP A  36      21.324  38.782  25.836  1.00 52.56           C  
ATOM    238  C   ASP A  36      22.408  37.777  25.544  1.00 53.67           C  
ATOM    239  O   ASP A  36      22.311  36.641  25.979  1.00 53.79           O  
ATOM    240  CB  ASP A  36      20.807  38.550  27.254  1.00 57.48           C  
ATOM    241  CG  ASP A  36      21.796  38.968  28.343  1.00 61.34           C  
ATOM    242  OD1 ASP A  36      22.979  39.202  28.023  1.00 71.05           O  
ATOM    243  OD2 ASP A  36      21.381  39.052  29.531  1.00 62.21           O1-
ATOM    244  N   ALA A  37      23.443  38.189  24.815  1.00 53.71           N  
ATOM    245  CA  ALA A  37      24.548  37.288  24.467  1.00 52.55           C  
ATOM    246  C   ALA A  37      25.439  37.041  25.640  1.00 55.85           C  
ATOM    247  O   ALA A  37      26.120  36.018  25.723  1.00 55.99           O  
ATOM    248  CB  ALA A  37      25.365  37.864  23.345  1.00 55.43           C  
ATOM    249  N   THR A  38      25.438  38.002  26.548  1.00 60.90           N  
ATOM    250  CA  THR A  38      26.275  37.934  27.712  1.00 63.85           C  
ATOM    251  C   THR A  38      25.772  36.788  28.569  1.00 58.62           C  
ATOM    252  O   THR A  38      26.518  35.904  28.942  1.00 64.37           O  
ATOM    253  CB  THR A  38      26.284  39.301  28.430  1.00 71.70           C  
ATOM    254  OG1 THR A  38      26.873  40.278  27.554  1.00 76.19           O  
ATOM    255  CG2 THR A  38      27.079  39.257  29.729  1.00 76.18           C  
ATOM    256  N   TYR A  39      24.485  36.770  28.832  1.00 57.44           N  
ATOM    257  CA  TYR A  39      23.877  35.655  29.547  1.00 53.08           C  
ATOM    258  C   TYR A  39      23.901  34.359  28.736  1.00 53.11           C  
ATOM    259  O   TYR A  39      24.131  33.293  29.297  1.00 52.35           O  
ATOM    260  CB  TYR A  39      22.441  36.025  29.923  1.00 51.87           C  
ATOM    261  CG  TYR A  39      21.802  35.122  30.945  1.00 50.84           C  
ATOM    262  CD1 TYR A  39      21.491  33.799  30.635  1.00 47.55           C  
ATOM    263  CD2 TYR A  39      21.513  35.577  32.223  1.00 51.04           C  
ATOM    264  CE1 TYR A  39      20.908  32.954  31.556  1.00 47.88           C  
ATOM    265  CE2 TYR A  39      20.931  34.721  33.152  1.00 55.90           C  
ATOM    266  CZ  TYR A  39      20.623  33.411  32.790  1.00 50.23           C  
ATOM    267  OH  TYR A  39      20.027  32.548  33.664  1.00 59.78           O  
ATOM    268  N   GLY A  40      23.656  34.479  27.423  1.00 55.82           N  
ATOM    269  CA  GLY A  40      23.475  33.359  26.496  1.00 50.93           C  
ATOM    270  C   GLY A  40      22.012  32.981  26.340  1.00 50.46           C  
ATOM    271  O   GLY A  40      21.656  31.837  26.545  1.00 53.93           O  
ATOM    272  N   LYS A  41      21.170  33.934  25.946  1.00 52.66           N  
ATOM    273  CA  LYS A  41      19.711  33.814  26.118  1.00 48.60           C  
ATOM    274  C   LYS A  41      18.885  34.644  25.108  1.00 48.89           C  
ATOM    275  O   LYS A  41      19.151  35.824  24.891  1.00 51.87           O  
ATOM    276  CB  LYS A  41      19.364  34.188  27.561  1.00 48.93           C  
ATOM    277  CG  LYS A  41      17.940  34.627  27.789  1.00 51.86           C  
ATOM    278  CD  LYS A  41      17.509  34.545  29.224  1.00 54.30           C  
ATOM    279  CE  LYS A  41      17.495  35.914  29.855  1.00 59.91           C  
ATOM    280  NZ  LYS A  41      17.225  35.830  31.319  1.00 61.67           N  
ATOM    281  N   LEU A  42      17.897  33.999  24.489  1.00 51.39           N  
ATOM    282  CA  LEU A  42      16.937  34.636  23.576  1.00 53.44           C  
ATOM    283  C   LEU A  42      15.553  34.402  24.079  1.00 52.31           C  
ATOM    284  O   LEU A  42      15.246  33.318  24.539  1.00 53.27           O  
ATOM    285  CB  LEU A  42      16.938  34.000  22.180  1.00 54.81           C  
ATOM    286  CG  LEU A  42      18.209  34.000  21.343  1.00 54.36           C  
ATOM    287  CD1 LEU A  42      18.033  33.112  20.147  1.00 55.38           C  
ATOM    288  CD2 LEU A  42      18.560  35.387  20.852  1.00 59.08           C  
ATOM    289  N   THR A  43      14.706  35.402  23.929  1.00 52.51           N  
ATOM    290  CA  THR A  43      13.282  35.236  24.135  1.00 49.42           C  
ATOM    291  C   THR A  43      12.617  35.820  22.906  1.00 48.06           C  
ATOM    292  O   THR A  43      12.853  36.983  22.582  1.00 49.30           O  
ATOM    293  CB  THR A  43      12.852  35.944  25.416  1.00 53.98           C  
ATOM    294  OG1 THR A  43      12.851  37.361  25.210  1.00 59.12           O  
ATOM    295  CG2 THR A  43      13.826  35.589  26.565  1.00 54.57           C  
ATOM    296  N   LEU A  44      11.861  35.005  22.173  1.00 46.35           N  
ATOM    297  CA  LEU A  44      11.248  35.450  20.932  1.00 46.41           C  
ATOM    298  C   LEU A  44       9.860  34.939  20.880  1.00 44.52           C  
ATOM    299  O   LEU A  44       9.559  33.933  21.475  1.00 43.92           O  
ATOM    300  CB  LEU A  44      12.026  34.949  19.723  1.00 50.72           C  
ATOM    301  CG  LEU A  44      13.304  35.765  19.386  1.00 54.95           C  
ATOM    302  CD1 LEU A  44      14.446  34.938  18.802  1.00 56.22           C  
ATOM    303  CD2 LEU A  44      12.979  36.903  18.437  1.00 53.24           C  
ATOM    304  N   LYS A  45       9.002  35.681  20.198  1.00 47.25           N  
ATOM    305  CA  LYS A  45       7.642  35.249  19.930  1.00 44.10           C  
ATOM    306  C   LYS A  45       7.380  35.469  18.484  1.00 43.98           C  
ATOM    307  O   LYS A  45       7.823  36.471  17.902  1.00 47.81           O  
ATOM    308  CB  LYS A  45       6.632  36.030  20.740  1.00 45.54           C  
ATOM    309  CG  LYS A  45       5.208  35.806  20.286  1.00 48.30           C  
ATOM    310  CD  LYS A  45       4.196  36.557  21.113  1.00 49.28           C  
ATOM    311  CE  LYS A  45       2.831  36.549  20.427  1.00 51.37           C  
ATOM    312  NZ  LYS A  45       1.765  37.218  21.232  1.00 50.45           N  
ATOM    313  N   PHE A  46       6.651  34.522  17.906  1.00 46.92           N  
ATOM    314  CA  PHE A  46       6.354  34.491  16.473  1.00 47.41           C  
ATOM    315  C   PHE A  46       4.882  34.343  16.248  1.00 46.45           C  
ATOM    316  O   PHE A  46       4.194  33.735  17.055  1.00 44.14           O  
ATOM    317  CB  PHE A  46       7.041  33.303  15.803  1.00 46.47           C  
ATOM    318  CG  PHE A  46       8.505  33.237  16.077  1.00 44.41           C  
ATOM    319  CD1 PHE A  46       9.392  33.936  15.288  1.00 42.09           C  
ATOM    320  CD2 PHE A  46       8.985  32.493  17.155  1.00 44.41           C  
ATOM    321  CE1 PHE A  46      10.736  33.876  15.557  1.00 43.68           C  
ATOM    322  CE2 PHE A  46      10.327  32.446  17.435  1.00 43.50           C  
ATOM    323  CZ  PHE A  46      11.204  33.129  16.623  1.00 42.18           C  
ATOM    324  N   ILE A  47       4.422  34.908  15.139  1.00 52.26           N  
ATOM    325  CA  ILE A  47       3.034  34.816  14.729  1.00 56.12           C  
ATOM    326  C   ILE A  47       2.982  34.585  13.233  1.00 55.03           C  
ATOM    327  O   ILE A  47       3.652  35.327  12.472  1.00 45.90           O  
ATOM    328  CB  ILE A  47       2.246  36.121  15.034  1.00 61.30           C  
ATOM    329  CG1 ILE A  47       2.183  36.414  16.537  1.00 60.74           C  
ATOM    330  CG2 ILE A  47       0.808  36.018  14.551  1.00 62.09           C  
ATOM    331  CD1 ILE A  47       1.745  37.829  16.837  1.00 60.30           C  
ATOM    332  N   CYS A  48       2.182  33.579  12.825  1.00 55.18           N  
ATOM    333  CA  CYS A  48       1.767  33.421  11.405  1.00 54.55           C  
ATOM    334  C   CYS A  48       0.713  34.439  11.028  1.00 56.74           C  
ATOM    335  O   CYS A  48      -0.353  34.519  11.661  1.00 57.19           O  
ATOM    336  CB  CYS A  48       1.198  32.051  11.112  1.00 52.63           C  
ATOM    337  SG  CYS A  48       0.960  31.789   9.351  1.00 53.85           S  
ATOM    338  N   THR A  49       1.023  35.212   9.994  1.00 59.39           N  
ATOM    339  CA  THR A  49       0.260  36.405   9.659  1.00 57.39           C  
ATOM    340  C   THR A  49      -0.574  36.153   8.441  1.00 55.65           C  
ATOM    341  O   THR A  49      -1.215  37.042   7.926  1.00 61.62           O  
ATOM    342  CB  THR A  49       1.195  37.580   9.380  1.00 54.25           C  
ATOM    343  OG1 THR A  49       2.173  37.197   8.410  1.00 57.72           O  
ATOM    344  CG2 THR A  49       1.896  37.961  10.630  1.00 54.52           C  
ATOM    345  N   THR A  50      -0.538  34.921   7.982  1.00 55.20           N  
ATOM    346  CA  THR A  50      -1.313  34.482   6.864  1.00 52.30           C  
ATOM    347  C   THR A  50      -2.310  33.488   7.422  1.00 49.36           C  
ATOM    348  O   THR A  50      -2.858  32.688   6.715  1.00 58.98           O  
ATOM    349  CB  THR A  50      -0.374  33.813   5.843  1.00 52.39           C  
ATOM    350  OG1 THR A  50       0.091  32.533   6.352  1.00 54.90           O  
ATOM    351  CG2 THR A  50       0.802  34.741   5.554  1.00 46.77           C  
ATOM    352  N   GLY A  51      -2.513  33.524   8.717  1.00 49.97           N  
ATOM    353  CA  GLY A  51      -3.389  32.590   9.349  1.00 53.17           C  
ATOM    354  C   GLY A  51      -2.654  31.461  10.022  1.00 54.82           C  
ATOM    355  O   GLY A  51      -1.827  31.696  10.891  1.00 57.73           O  
ATOM    356  N   LYS A  52      -3.000  30.234   9.624  1.00 58.36           N  
ATOM    357  CA  LYS A  52      -2.442  29.012  10.176  1.00 55.35           C  
ATOM    358  C   LYS A  52      -1.111  28.688   9.511  1.00 57.29           C  
ATOM    359  O   LYS A  52      -0.895  28.966   8.324  1.00 53.30           O  
ATOM    360  CB  LYS A  52      -3.403  27.847   9.981  1.00 55.41           C  
ATOM    361  CG  LYS A  52      -3.129  26.630  10.864  1.00 58.18           C  
ATOM    362  N   LEU A  53      -0.213  28.100  10.302  1.00 59.12           N  
ATOM    363  CA  LEU A  53       1.099  27.768   9.813  1.00 51.09           C  
ATOM    364  C   LEU A  53       0.913  26.405   9.262  1.00 47.13           C  
ATOM    365  O   LEU A  53       0.337  25.569   9.938  1.00 50.71           O  
ATOM    366  CB  LEU A  53       2.137  27.771  10.938  1.00 51.06           C  
ATOM    367  CG  LEU A  53       3.597  27.896  10.455  1.00 50.77           C  
ATOM    368  CD1 LEU A  53       3.893  29.127   9.607  1.00 51.40           C  
ATOM    369  CD2 LEU A  53       4.501  27.908  11.648  1.00 51.98           C  
ATOM    370  N   PRO A  54       1.356  26.178   8.028  1.00 43.47           N  
ATOM    371  CA  PRO A  54       1.147  24.878   7.438  1.00 46.74           C  
ATOM    372  C   PRO A  54       2.086  23.778   7.898  1.00 48.40           C  
ATOM    373  O   PRO A  54       2.005  22.657   7.387  1.00 49.19           O  
ATOM    374  CB  PRO A  54       1.339  25.127   5.943  1.00 47.01           C  
ATOM    375  CG  PRO A  54       1.923  26.464   5.796  1.00 45.81           C  
ATOM    376  CD  PRO A  54       1.605  27.217   7.027  1.00 44.91           C  
ATOM    377  N   VAL A  55       2.971  24.099   8.839  1.00 52.55           N  
ATOM    378  CA  VAL A  55       4.014  23.182   9.288  1.00 51.17           C  
ATOM    379  C   VAL A  55       4.107  23.296  10.773  1.00 48.29           C  
ATOM    380  O   VAL A  55       3.776  24.340  11.327  1.00 55.73           O  
ATOM    381  CB  VAL A  55       5.389  23.494   8.663  1.00 51.50           C  
ATOM    382  CG1 VAL A  55       5.479  22.891   7.259  1.00 50.51           C  
ATOM    383  CG2 VAL A  55       5.662  25.000   8.659  1.00 50.81           C  
ATOM    384  N   PRO A  56       4.547  22.224  11.436  1.00 43.25           N  
ATOM    385  CA  PRO A  56       4.633  22.358  12.851  1.00 41.64           C  
ATOM    386  C   PRO A  56       5.616  23.447  13.197  1.00 42.01           C  
ATOM    387  O   PRO A  56       6.542  23.703  12.473  1.00 46.71           O  
ATOM    388  CB  PRO A  56       5.073  20.973  13.311  1.00 42.17           C  
ATOM    389  CG  PRO A  56       4.696  20.075  12.207  1.00 40.93           C  
ATOM    390  CD  PRO A  56       4.912  20.880  10.991  1.00 42.10           C  
ATOM    391  N   TRP A  57       5.347  24.143  14.277  1.00 47.11           N  
ATOM    392  CA  TRP A  57       6.157  25.265  14.677  1.00 45.10           C  
ATOM    393  C   TRP A  57       7.608  24.862  14.981  1.00 44.16           C  
ATOM    394  O   TRP A  57       8.541  25.530  14.515  1.00 43.12           O  
ATOM    395  CB  TRP A  57       5.504  25.969  15.870  1.00 44.63           C  
ATOM    396  CG  TRP A  57       4.465  26.952  15.506  1.00 42.35           C  
ATOM    397  CD1 TRP A  57       3.138  26.784  15.611  1.00 42.31           C  
ATOM    398  CD2 TRP A  57       4.668  28.278  15.019  1.00 42.09           C  
ATOM    399  NE1 TRP A  57       2.485  27.900  15.196  1.00 41.49           N  
ATOM    400  CE2 TRP A  57       3.402  28.846  14.835  1.00 41.93           C  
ATOM    401  CE3 TRP A  57       5.798  29.044  14.725  1.00 42.94           C  
ATOM    402  CZ2 TRP A  57       3.222  30.143  14.350  1.00 42.26           C  
ATOM    403  CZ3 TRP A  57       5.626  30.327  14.240  1.00 42.30           C  
ATOM    404  CH2 TRP A  57       4.343  30.865  14.053  1.00 43.87           C  
ATOM    405  N   PRO A  58       7.805  23.763  15.733  1.00 43.81           N  
ATOM    406  CA  PRO A  58       9.137  23.243  16.004  1.00 44.72           C  
ATOM    407  C   PRO A  58      10.031  23.103  14.760  1.00 46.77           C  
ATOM    408  O   PRO A  58      11.242  23.186  14.863  1.00 49.71           O  
ATOM    409  CB  PRO A  58       8.847  21.855  16.561  1.00 46.06           C  
ATOM    410  CG  PRO A  58       7.478  21.925  17.110  1.00 43.49           C  
ATOM    411  CD  PRO A  58       6.767  22.836  16.203  1.00 44.07           C  
ATOM    412  N   THR A  59       9.434  22.899  13.589  1.00 47.73           N  
ATOM    413  CA  THR A  59      10.203  22.680  12.383  1.00 41.24           C  
ATOM    414  C   THR A  59      10.859  23.961  11.893  1.00 42.27           C  
ATOM    415  O   THR A  59      11.755  23.925  11.056  1.00 44.50           O  
ATOM    416  CB  THR A  59       9.388  21.944  11.302  1.00 39.40           C  
ATOM    417  OG1 THR A  59       8.585  22.832  10.528  1.00 40.15           O  
ATOM    418  CG2 THR A  59       8.532  20.943  11.931  1.00 40.22           C  
ATOM    419  N   LEU A  60      10.482  25.099  12.460  1.00 46.60           N  
ATOM    420  CA  LEU A  60      11.139  26.349  12.088  1.00 44.31           C  
ATOM    421  C   LEU A  60      11.966  27.005  13.173  1.00 38.73           C  
ATOM    422  O   LEU A  60      12.449  28.073  12.967  1.00 38.87           O  
ATOM    423  CB  LEU A  60      10.105  27.322  11.632  1.00 46.30           C  
ATOM    424  CG  LEU A  60       9.279  26.905  10.430  1.00 44.60           C  
ATOM    425  CD1 LEU A  60       7.978  27.684  10.518  1.00 47.01           C  
ATOM    426  CD2 LEU A  60       9.994  27.217   9.144  1.00 41.63           C  
ATOM    427  N   VAL A  61      12.165  26.362  14.305  1.00 38.83           N  
ATOM    428  CA  VAL A  61      12.902  26.988  15.368  1.00 39.71           C  
ATOM    429  C   VAL A  61      14.312  27.367  14.952  1.00 42.95           C  
ATOM    430  O   VAL A  61      14.810  28.422  15.351  1.00 46.19           O  
ATOM    431  CB  VAL A  61      12.924  26.112  16.632  1.00 41.00           C  
ATOM    432  CG1 VAL A  61      13.958  26.566  17.632  1.00 41.11           C  
ATOM    433  CG2 VAL A  61      11.582  26.128  17.307  1.00 39.92           C  
ATOM    434  N   THR A  62      14.956  26.518  14.158  1.00 44.99           N  
ATOM    435  CA  THR A  62      16.386  26.700  13.815  1.00 42.08           C  
ATOM    436  C   THR A  62      16.584  27.661  12.684  1.00 41.80           C  
ATOM    437  O   THR A  62      17.658  28.178  12.445  1.00 41.29           O  
ATOM    438  CB  THR A  62      16.971  25.405  13.334  1.00 40.97           C  
ATOM    439  OG1 THR A  62      16.283  25.027  12.146  1.00 43.50           O  
ATOM    440  CG2 THR A  62      16.774  24.345  14.383  1.00 43.30           C  
ATOM    441  N   THR A  63      15.513  27.853  11.959  1.00 42.51           N  
ATOM    442  CA  THR A  63      15.472  28.794  10.908  1.00 44.45           C  
ATOM    443  C   THR A  63      15.240  30.200  11.443  1.00 42.50           C  
ATOM    444  O   THR A  63      15.959  31.102  11.069  1.00 43.61           O  
ATOM    445  CB  THR A  63      14.450  28.326   9.875  1.00 44.87           C  
ATOM    446  OG1 THR A  63      15.048  27.269   9.114  1.00 43.78           O  
ATOM    447  CG2 THR A  63      14.071  29.429   8.943  1.00 46.94           C  
ATOM    448  N   PHE A  64      14.270  30.365  12.335  1.00 43.31           N  
ATOM    449  CA  PHE A  64      14.017  31.638  13.023  1.00 42.28           C  
ATOM    450  C   PHE A  64      15.204  32.049  13.898  1.00 44.22           C  
ATOM    451  O   PHE A  64      15.659  33.195  13.879  1.00 42.46           O  
ATOM    452  CB  PHE A  64      12.828  31.501  13.982  1.00 40.72           C  
ATOM    453  CG  PHE A  64      11.518  31.273  13.334  1.00 37.30           C  
ATOM    454  CD1 PHE A  64      11.139  31.971  12.250  1.00 36.23           C  
ATOM    455  CD2 PHE A  64      10.624  30.396  13.902  1.00 39.27           C  
ATOM    456  CE1 PHE A  64       9.906  31.769  11.684  1.00 36.27           C  
ATOM    457  CE2 PHE A  64       9.390  30.180  13.339  1.00 37.47           C  
ATOM    458  CZ  PHE A  64       9.035  30.870  12.224  1.00 34.81           C  
HETATM  459  N1  CRO A  66      15.638  31.095  14.713  1.00 45.48           N  
HETATM  460  CA1 CRO A  66      16.725  31.252  15.586  1.00 45.85           C  
HETATM  461  CB1 CRO A  66      16.132  31.015  16.963  1.00 50.24           C  
HETATM  462  OG1 CRO A  66      16.899  31.776  17.894  1.00 47.21           O  
HETATM  463  C1  CRO A  66      17.809  30.280  15.279  1.00 48.05           C  
HETATM  464  N2  CRO A  66      18.012  29.061  15.940  1.00 43.04           N  
HETATM  465  N3  CRO A  66      18.756  30.545  14.333  1.00 45.53           N  
HETATM  466  C2  CRO A  66      19.539  29.494  14.360  1.00 47.98           C  
HETATM  467  O2  CRO A  66      20.564  29.329  13.607  1.00 53.47           O  
HETATM  468  CA2 CRO A  66      19.119  28.550  15.391  1.00 45.01           C  
HETATM  469  CA3 CRO A  66      18.855  31.639  13.368  1.00 46.19           C  
HETATM  470  C3  CRO A  66      19.627  32.887  13.650  1.00 46.62           C  
HETATM  471  O3  CRO A  66      19.996  33.582  12.686  1.00 47.32           O  
HETATM  472  CB2 CRO A  66      19.816  27.271  15.701  1.00 44.52           C  
HETATM  473  CG2 CRO A  66      19.455  26.199  16.653  1.00 41.34           C  
HETATM  474  CD1 CRO A  66      18.339  26.179  17.478  1.00 42.24           C  
HETATM  475  CD2 CRO A  66      20.225  25.070  16.584  1.00 41.08           C  
HETATM  476  CE1 CRO A  66      18.079  25.076  18.281  1.00 41.24           C  
HETATM  477  CE2 CRO A  66      19.957  23.958  17.377  1.00 41.24           C  
HETATM  478  CZ  CRO A  66      18.895  23.947  18.245  1.00 41.66           C  
HETATM  479  OH  CRO A  66      18.669  22.835  19.031  1.00 41.59           O  
ATOM    480  N   VAL A  68      19.855  33.181  15.034  1.00 52.10           N  
ATOM    481  CA  VAL A  68      20.587  34.415  15.496  1.00 50.72           C  
ATOM    482  C   VAL A  68      21.686  34.032  16.529  1.00 49.28           C  
ATOM    483  O   VAL A  68      21.658  34.399  17.696  1.00 47.62           O  
ATOM    484  CB  VAL A  68      19.596  35.503  15.996  1.00 46.15           C  
ATOM    485  CG1 VAL A  68      19.006  36.285  14.837  1.00 45.25           C  
ATOM    486  CG2 VAL A  68      18.468  34.897  16.807  1.00 48.84           C  
ATOM    487  N   GLN A  69      22.694  33.325  16.022  1.00 51.27           N  
ATOM    488  CA  GLN A  69      23.688  32.640  16.829  1.00 46.85           C  
ATOM    489  C   GLN A  69      24.778  33.588  17.305  1.00 50.70           C  
ATOM    490  O   GLN A  69      25.736  33.162  17.951  1.00 57.94           O  
ATOM    491  CB  GLN A  69      24.257  31.478  16.026  1.00 45.56           C  
ATOM    492  CG  GLN A  69      23.166  30.603  15.436  1.00 44.81           C  
ATOM    493  CD  GLN A  69      23.671  29.421  14.664  1.00 43.36           C  
ATOM    494  OE1 GLN A  69      24.198  29.551  13.561  1.00 47.28           O  
ATOM    495  NE2 GLN A  69      23.470  28.255  15.216  1.00 42.01           N  
ATOM    496  N   CYS A  70      24.607  34.877  16.992  1.00 51.82           N  
ATOM    497  CA  CYS A  70      25.411  35.971  17.534  1.00 48.26           C  
ATOM    498  C   CYS A  70      25.049  36.258  18.984  1.00 49.00           C  
ATOM    499  O   CYS A  70      25.749  36.996  19.660  1.00 48.22           O  
ATOM    500  CB  CYS A  70      25.231  37.233  16.671  1.00 48.40           C  
ATOM    501  SG  CYS A  70      23.559  37.545  16.051  1.00 47.91           S  
ATOM    502  N   PHE A  71      23.939  35.683  19.455  1.00 52.20           N  
ATOM    503  CA  PHE A  71      23.557  35.692  20.872  1.00 47.80           C  
ATOM    504  C   PHE A  71      23.998  34.453  21.668  1.00 45.87           C  
ATOM    505  O   PHE A  71      23.522  34.257  22.773  1.00 43.55           O  
ATOM    506  CB  PHE A  71      22.037  35.878  20.999  1.00 49.03           C  
ATOM    507  CG  PHE A  71      21.563  37.171  20.447  1.00 46.75           C  
ATOM    508  CD1 PHE A  71      21.842  38.347  21.112  1.00 50.96           C  
ATOM    509  CD2 PHE A  71      20.901  37.230  19.270  1.00 45.17           C  
ATOM    510  CE1 PHE A  71      21.458  39.566  20.618  1.00 50.01           C  
ATOM    511  CE2 PHE A  71      20.501  38.448  18.762  1.00 48.68           C  
ATOM    512  CZ  PHE A  71      20.789  39.625  19.430  1.00 47.08           C  
ATOM    513  N   SER A  72      24.889  33.630  21.102  1.00 45.54           N  
ATOM    514  CA  SER A  72      25.565  32.564  21.830  1.00 43.73           C  
ATOM    515  C   SER A  72      26.483  33.190  22.823  1.00 46.50           C  
ATOM    516  O   SER A  72      27.124  34.161  22.503  1.00 50.20           O  
ATOM    517  CB  SER A  72      26.435  31.731  20.909  1.00 44.36           C  
ATOM    518  OG  SER A  72      25.828  31.512  19.656  1.00 48.78           O  
ATOM    519  N   ARG A  73      26.557  32.629  24.026  1.00 54.48           N  
ATOM    520  CA  ARG A  73      27.545  33.026  25.029  1.00 55.39           C  
ATOM    521  C   ARG A  73      28.831  32.270  24.787  1.00 55.71           C  
ATOM    522  O   ARG A  73      28.916  31.062  25.014  1.00 50.97           O  
ATOM    523  CB  ARG A  73      27.066  32.749  26.460  1.00 63.35           C  
ATOM    524  CG  ARG A  73      28.008  33.270  27.547  1.00 69.44           C  
ATOM    525  CD  ARG A  73      27.548  32.960  28.967  1.00 74.98           C  
ATOM    526  NE  ARG A  73      27.805  31.567  29.325  1.00 88.46           N  
ATOM    527  CZ  ARG A  73      29.007  31.072  29.631  1.00102.52           C  
ATOM    528  NH1 ARG A  73      30.092  31.858  29.636  1.00110.71           N  
ATOM    529  NH2 ARG A  73      29.134  29.776  29.931  1.00 99.66           N  
ATOM    530  N   TYR A  74      29.834  33.007  24.319  1.00 62.72           N  
ATOM    531  CA  TYR A  74      31.176  32.482  24.151  1.00 60.59           C  
ATOM    532  C   TYR A  74      31.927  32.821  25.413  1.00 63.56           C  
ATOM    533  O   TYR A  74      32.115  34.006  25.697  1.00 68.87           O  
ATOM    534  CB  TYR A  74      31.858  33.111  22.942  1.00 58.42           C  
ATOM    535  CG  TYR A  74      31.583  32.365  21.670  1.00 56.89           C  
ATOM    536  CD1 TYR A  74      30.331  32.400  21.091  1.00 56.52           C  
ATOM    537  CD2 TYR A  74      32.572  31.619  21.053  1.00 53.75           C  
ATOM    538  CE1 TYR A  74      30.069  31.708  19.935  1.00 56.95           C  
ATOM    539  CE2 TYR A  74      32.320  30.938  19.890  1.00 52.44           C  
ATOM    540  CZ  TYR A  74      31.066  30.974  19.345  1.00 53.63           C  
ATOM    541  OH  TYR A  74      30.794  30.282  18.193  1.00 55.19           O  
ATOM    542  N   PRO A  75      32.349  31.793  26.186  1.00 66.44           N  
ATOM    543  CA  PRO A  75      33.110  32.082  27.399  1.00 66.76           C  
ATOM    544  C   PRO A  75      34.319  32.929  27.044  1.00 70.98           C  
ATOM    545  O   PRO A  75      34.617  33.115  25.865  1.00 72.16           O  
ATOM    546  CB  PRO A  75      33.543  30.705  27.893  1.00 63.82           C  
ATOM    547  CG  PRO A  75      32.611  29.744  27.236  1.00 65.90           C  
ATOM    548  CD  PRO A  75      32.255  30.345  25.921  1.00 63.77           C  
ATOM    549  N   ASP A  76      35.014  33.438  28.047  1.00 77.21           N  
ATOM    550  CA  ASP A  76      36.070  34.413  27.807  1.00 79.72           C  
ATOM    551  C   ASP A  76      37.230  33.867  26.947  1.00 78.52           C  
ATOM    552  O   ASP A  76      37.670  34.538  26.005  1.00 82.20           O  
ATOM    553  CB  ASP A  76      36.576  34.961  29.133  1.00 90.22           C  
ATOM    554  CG  ASP A  76      35.538  35.803  29.846  1.00102.42           C  
ATOM    555  OD1 ASP A  76      34.441  35.277  30.171  1.00112.40           O1-
ATOM    556  OD2 ASP A  76      35.831  36.995  30.090  1.00112.15           O  
ATOM    557  N   HIS A  77      37.700  32.656  27.246  1.00 67.17           N  
ATOM    558  CA  HIS A  77      38.770  32.022  26.458  1.00 67.19           C  
ATOM    559  C   HIS A  77      38.369  31.490  25.075  1.00 68.15           C  
ATOM    560  O   HIS A  77      39.164  30.852  24.375  1.00 64.98           O  
ATOM    561  CB  HIS A  77      39.357  30.879  27.250  1.00 71.18           C  
ATOM    562  CG  HIS A  77      38.496  29.671  27.269  1.00 69.02           C  
ATOM    563  ND1 HIS A  77      37.268  29.649  27.886  1.00 68.10           N  
ATOM    564  CD2 HIS A  77      38.687  28.440  26.750  1.00 72.38           C  
ATOM    565  CE1 HIS A  77      36.738  28.448  27.753  1.00 72.25           C  
ATOM    566  NE2 HIS A  77      37.579  27.697  27.066  1.00 76.54           N  
ATOM    567  N   MET A  78      37.123  31.736  24.697  1.00 71.07           N  
ATOM    568  CA  MET A  78      36.617  31.339  23.407  1.00 62.42           C  
ATOM    569  C   MET A  78      36.295  32.538  22.564  1.00 58.65           C  
ATOM    570  O   MET A  78      36.068  32.373  21.388  1.00 64.89           O  
ATOM    571  CB  MET A  78      35.344  30.496  23.567  1.00 60.98           C  
ATOM    572  CG  MET A  78      35.582  29.182  24.283  1.00 60.77           C  
ATOM    573  SD  MET A  78      34.421  27.842  23.993  1.00 60.28           S  
ATOM    574  CE  MET A  78      33.996  28.087  22.270  1.00 61.59           C  
ATOM    575  N   LYS A  79      36.298  33.739  23.140  1.00 60.53           N  
ATOM    576  CA  LYS A  79      35.631  34.899  22.511  1.00 63.67           C  
ATOM    577  C   LYS A  79      36.072  35.177  21.069  1.00 65.19           C  
ATOM    578  O   LYS A  79      35.363  35.860  20.316  1.00 64.76           O  
ATOM    579  CB  LYS A  79      35.778  36.165  23.371  1.00 61.95           C  
ATOM    580  N   ARG A  80      37.227  34.626  20.694  1.00 66.80           N  
ATOM    581  CA  ARG A  80      37.823  34.835  19.377  1.00 66.24           C  
ATOM    582  C   ARG A  80      37.483  33.755  18.353  1.00 66.66           C  
ATOM    583  O   ARG A  80      38.044  33.743  17.262  1.00 75.38           O  
ATOM    584  CB  ARG A  80      39.337  34.873  19.512  1.00 69.02           C  
ATOM    585  CG  ARG A  80      39.939  33.503  19.770  1.00 75.01           C  
ATOM    586  CD  ARG A  80      41.349  33.419  19.231  1.00 81.64           C  
ATOM    587  NE  ARG A  80      42.071  32.235  19.724  1.00 91.28           N  
ATOM    588  CZ  ARG A  80      42.413  31.152  19.009  1.00 85.33           C  
ATOM    589  NH1 ARG A  80      42.098  31.022  17.717  1.00 85.29           N  
ATOM    590  NH2 ARG A  80      43.086  30.173  19.609  1.00 79.24           N  
ATOM    591  N   HIS A  81      36.622  32.822  18.722  1.00 58.99           N  
ATOM    592  CA  HIS A  81      36.134  31.840  17.806  1.00 53.29           C  
ATOM    593  C   HIS A  81      34.745  32.252  17.420  1.00 51.47           C  
ATOM    594  O   HIS A  81      34.038  31.509  16.772  1.00 54.10           O  
ATOM    595  CB  HIS A  81      36.129  30.487  18.501  1.00 61.10           C  
ATOM    596  CG  HIS A  81      37.468  30.111  19.043  1.00 64.22           C  
ATOM    597  ND1 HIS A  81      38.460  29.586  18.252  1.00 65.18           N  
ATOM    598  CD2 HIS A  81      38.004  30.245  20.275  1.00 65.66           C  
ATOM    599  CE1 HIS A  81      39.542  29.384  18.977  1.00 62.23           C  
ATOM    600  NE2 HIS A  81      39.292  29.777  20.209  1.00 64.33           N  
ATOM    601  N   ASP A  82      34.362  33.457  17.821  1.00 54.35           N  
ATOM    602  CA  ASP A  82      33.022  33.983  17.587  1.00 56.52           C  
ATOM    603  C   ASP A  82      32.927  34.772  16.291  1.00 58.69           C  
ATOM    604  O   ASP A  82      33.084  36.001  16.255  1.00 61.04           O  
ATOM    605  CB  ASP A  82      32.566  34.851  18.762  1.00 58.63           C  
ATOM    606  CG  ASP A  82      31.097  35.148  18.720  1.00 51.74           C  
ATOM    607  OD1 ASP A  82      30.465  34.905  17.691  1.00 53.60           O  
ATOM    608  OD2 ASP A  82      30.571  35.608  19.724  1.00 54.49           O1-
ATOM    609  N   PHE A  83      32.668  34.024  15.230  1.00 57.43           N  
ATOM    610  CA  PHE A  83      32.442  34.564  13.924  1.00 53.30           C  
ATOM    611  C   PHE A  83      31.165  35.369  13.967  1.00 52.42           C  
ATOM    612  O   PHE A  83      31.101  36.477  13.477  1.00 60.69           O  
ATOM    613  CB  PHE A  83      32.330  33.398  12.926  1.00 54.98           C  
ATOM    614  CG  PHE A  83      31.689  33.759  11.624  1.00 51.82           C  
ATOM    615  CD1 PHE A  83      30.290  33.768  11.497  1.00 49.94           C  
ATOM    616  CD2 PHE A  83      32.463  34.064  10.532  1.00 46.58           C  
ATOM    617  CE1 PHE A  83      29.685  34.114  10.316  1.00 49.60           C  
ATOM    618  CE2 PHE A  83      31.864  34.413   9.348  1.00 50.85           C  
ATOM    619  CZ  PHE A  83      30.475  34.436   9.233  1.00 52.12           C  
ATOM    620  N   PHE A  84      30.142  34.823  14.584  1.00 51.51           N  
ATOM    621  CA  PHE A  84      28.821  35.417  14.479  1.00 49.46           C  
ATOM    622  C   PHE A  84      28.818  36.928  14.760  1.00 46.00           C  
ATOM    623  O   PHE A  84      28.304  37.710  13.991  1.00 48.87           O  
ATOM    624  CB  PHE A  84      27.867  34.646  15.384  1.00 48.67           C  
ATOM    625  CG  PHE A  84      27.794  33.178  15.059  1.00 44.72           C  
ATOM    626  CD1 PHE A  84      27.193  32.750  13.907  1.00 44.94           C  
ATOM    627  CD2 PHE A  84      28.326  32.238  15.902  1.00 46.71           C  
ATOM    628  CE1 PHE A  84      27.107  31.415  13.605  1.00 44.50           C  
ATOM    629  CE2 PHE A  84      28.248  30.888  15.607  1.00 43.16           C  
ATOM    630  CZ  PHE A  84      27.641  30.481  14.456  1.00 43.32           C  
ATOM    631  N   LYS A  85      29.447  37.332  15.840  1.00 53.81           N  
ATOM    632  CA  LYS A  85      29.536  38.745  16.206  1.00 55.45           C  
ATOM    633  C   LYS A  85      30.585  39.516  15.420  1.00 53.41           C  
ATOM    634  O   LYS A  85      30.332  40.637  15.053  1.00 59.91           O  
ATOM    635  CB  LYS A  85      29.865  38.897  17.682  1.00 55.30           C  
ATOM    636  CG  LYS A  85      28.846  38.293  18.626  1.00 59.51           C  
ATOM    637  CD  LYS A  85      29.166  38.677  20.062  1.00 56.77           C  
ATOM    638  CE  LYS A  85      28.246  38.023  21.074  1.00 58.26           C  
ATOM    639  NZ  LYS A  85      28.334  36.535  21.026  1.00 57.82           N  
ATOM    640  N   SER A  86      31.760  38.934  15.180  1.00 55.22           N  
ATOM    641  CA  SER A  86      32.852  39.621  14.447  1.00 52.46           C  
ATOM    642  C   SER A  86      32.405  40.118  13.083  1.00 53.81           C  
ATOM    643  O   SER A  86      32.888  41.130  12.597  1.00 61.91           O  
ATOM    644  CB  SER A  86      34.084  38.718  14.296  1.00 51.66           C  
ATOM    645  OG  SER A  86      33.960  37.825  13.211  1.00 50.88           O  
ATOM    646  N   ALA A  87      31.452  39.405  12.499  1.00 55.32           N  
ATOM    647  CA  ALA A  87      30.788  39.775  11.266  1.00 53.25           C  
ATOM    648  C   ALA A  87      29.827  40.965  11.332  1.00 53.07           C  
ATOM    649  O   ALA A  87      29.253  41.338  10.293  1.00 51.60           O  
ATOM    650  CB  ALA A  87      30.023  38.568  10.769  1.00 57.86           C  
ATOM    651  N   MET A  88      29.648  41.551  12.524  1.00 53.68           N  
ATOM    652  CA  MET A  88      28.654  42.618  12.758  1.00 53.01           C  
ATOM    653  C   MET A  88      29.274  44.007  12.786  1.00 53.66           C  
ATOM    654  O   MET A  88      30.447  44.148  13.109  1.00 59.34           O  
ATOM    655  CB  MET A  88      27.915  42.384  14.075  1.00 51.48           C  
ATOM    656  CG  MET A  88      27.002  41.176  14.084  1.00 50.32           C  
ATOM    657  SD  MET A  88      25.550  41.294  13.036  1.00 54.01           S  
ATOM    658  CE  MET A  88      25.173  39.551  13.021  1.00 52.66           C  
ATOM    659  N   PRO A  89      28.481  45.051  12.473  1.00 54.58           N  
ATOM    660  CA  PRO A  89      27.043  45.178  12.186  1.00 54.28           C  
ATOM    661  C   PRO A  89      26.660  44.980  10.735  1.00 56.46           C  
ATOM    662  O   PRO A  89      25.514  45.230  10.353  1.00 61.39           O  
ATOM    663  CB  PRO A  89      26.776  46.633  12.536  1.00 55.77           C  
ATOM    664  CG  PRO A  89      28.004  47.295  12.025  1.00 53.69           C  
ATOM    665  CD  PRO A  89      29.132  46.368  12.412  1.00 53.70           C  
ATOM    666  N   GLU A  90      27.611  44.547   9.927  1.00 59.87           N  
ATOM    667  CA  GLU A  90      27.386  44.387   8.509  1.00 60.44           C  
ATOM    668  C   GLU A  90      26.633  43.061   8.356  1.00 58.21           C  
ATOM    669  O   GLU A  90      25.711  42.926   7.538  1.00 58.73           O  
ATOM    670  CB  GLU A  90      28.720  44.396   7.754  1.00 64.57           C  
ATOM    671  CG  GLU A  90      29.760  45.375   8.295  1.00 69.16           C  
ATOM    672  CD  GLU A  90      30.641  44.787   9.396  1.00 70.92           C  
ATOM    673  OE1 GLU A  90      31.666  44.147   9.071  1.00 86.30           O  
ATOM    674  N   GLY A  91      27.045  42.102   9.173  1.00 53.77           N  
ATOM    675  CA  GLY A  91      26.288  40.908   9.400  1.00 55.25           C  
ATOM    676  C   GLY A  91      26.827  39.761   8.590  1.00 58.05           C  
ATOM    677  O   GLY A  91      28.001  39.707   8.248  1.00 53.85           O  
ATOM    678  N   TYR A  92      25.935  38.836   8.274  1.00 61.92           N  
ATOM    679  CA  TYR A  92      26.274  37.701   7.456  1.00 56.62           C  
ATOM    680  C   TYR A  92      25.028  37.150   6.847  1.00 56.24           C  
ATOM    681  O   TYR A  92      23.929  37.555   7.213  1.00 51.46           O  
ATOM    682  CB  TYR A  92      26.975  36.616   8.275  1.00 56.80           C  
ATOM    683  CG  TYR A  92      26.284  36.161   9.541  1.00 53.12           C  
ATOM    684  CD1 TYR A  92      25.296  35.200   9.516  1.00 51.62           C  
ATOM    685  CD2 TYR A  92      26.653  36.664  10.758  1.00 55.91           C  
ATOM    686  CE1 TYR A  92      24.686  34.770  10.665  1.00 47.49           C  
ATOM    687  CE2 TYR A  92      26.034  36.250  11.916  1.00 55.18           C  
ATOM    688  CZ  TYR A  92      25.069  35.289  11.858  1.00 49.52           C  
ATOM    689  OH  TYR A  92      24.500  34.892  13.017  1.00 44.19           O  
ATOM    690  N   VAL A  93      25.245  36.229   5.910  1.00 57.49           N  
ATOM    691  CA  VAL A  93      24.212  35.453   5.237  1.00 55.27           C  
ATOM    692  C   VAL A  93      24.229  34.028   5.799  1.00 53.15           C  
ATOM    693  O   VAL A  93      25.274  33.429   5.896  1.00 48.64           O  
ATOM    694  CB  VAL A  93      24.514  35.399   3.720  1.00 57.01           C  
ATOM    695  CG1 VAL A  93      23.911  34.175   3.057  1.00 58.40           C  
ATOM    696  CG2 VAL A  93      24.063  36.679   3.027  1.00 55.48           C  
ATOM    697  N   GLN A  94      23.072  33.493   6.175  1.00 56.04           N  
ATOM    698  CA  GLN A  94      22.979  32.105   6.618  1.00 50.56           C  
ATOM    699  C   GLN A  94      22.139  31.315   5.637  1.00 50.93           C  
ATOM    700  O   GLN A  94      20.979  31.643   5.376  1.00 46.92           O  
ATOM    701  CB  GLN A  94      22.399  32.012   8.026  1.00 52.24           C  
ATOM    702  CG  GLN A  94      22.295  30.609   8.629  1.00 47.14           C  
ATOM    703  CD  GLN A  94      22.011  30.666  10.117  1.00 49.85           C  
ATOM    704  OE1 GLN A  94      22.816  31.195  10.904  1.00 52.68           O  
ATOM    705  NE2 GLN A  94      20.865  30.131  10.521  1.00 51.63           N  
ATOM    706  N   GLU A  95      22.760  30.269   5.100  1.00 52.36           N  
ATOM    707  CA  GLU A  95      22.148  29.398   4.129  1.00 50.96           C  
ATOM    708  C   GLU A  95      22.130  28.010   4.679  1.00 49.14           C  
ATOM    709  O   GLU A  95      23.128  27.582   5.218  1.00 49.92           O  
ATOM    710  CB  GLU A  95      22.962  29.395   2.876  1.00 50.80           C  
ATOM    711  CG  GLU A  95      22.815  30.668   2.098  1.00 54.02           C  
ATOM    712  CD  GLU A  95      23.850  30.810   1.028  1.00 55.78           C  
ATOM    713  OE1 GLU A  95      24.860  30.090   1.106  1.00 64.65           O  
ATOM    714  OE2 GLU A  95      23.655  31.645   0.124  1.00 64.32           O1-
ATOM    715  N   ARG A  96      20.993  27.329   4.519  1.00 49.10           N  
ATOM    716  CA  ARG A  96      20.795  25.963   4.982  1.00 44.24           C  
ATOM    717  C   ARG A  96      19.971  25.117   4.061  1.00 42.79           C  
ATOM    718  O   ARG A  96      19.174  25.610   3.272  1.00 38.00           O  
ATOM    719  CB  ARG A  96      20.070  25.921   6.299  1.00 44.62           C  
ATOM    720  CG  ARG A  96      20.902  26.276   7.515  1.00 43.46           C  
ATOM    721  CD  ARG A  96      20.484  25.386   8.661  1.00 42.29           C  
ATOM    722  NE  ARG A  96      20.834  25.922   9.955  1.00 42.39           N  
ATOM    723  CZ  ARG A  96      20.088  26.764  10.648  1.00 38.25           C  
ATOM    724  NH1 ARG A  96      18.934  27.210  10.174  1.00 39.32           N  
ATOM    725  NH2 ARG A  96      20.525  27.166  11.815  1.00 39.43           N  
ATOM    726  N   THR A  97      20.207  23.815   4.210  1.00 46.18           N  
ATOM    727  CA  THR A  97      19.384  22.751   3.664  1.00 44.17           C  
ATOM    728  C   THR A  97      19.078  21.849   4.817  1.00 43.54           C  
ATOM    729  O   THR A  97      19.969  21.488   5.580  1.00 43.80           O  
ATOM    730  CB  THR A  97      20.123  21.945   2.592  1.00 43.78           C  
ATOM    731  OG1 THR A  97      21.250  22.691   2.104  1.00 48.20           O  
ATOM    732  CG2 THR A  97      19.226  21.664   1.478  1.00 40.93           C  
ATOM    733  N   ILE A  98      17.803  21.534   4.976  1.00 46.58           N  
ATOM    734  CA  ILE A  98      17.330  20.727   6.095  1.00 44.35           C  
ATOM    735  C   ILE A  98      16.589  19.562   5.499  1.00 43.56           C  
ATOM    736  O   ILE A  98      15.570  19.723   4.877  1.00 45.98           O  
ATOM    737  CB  ILE A  98      16.367  21.511   7.004  1.00 43.29           C  
ATOM    738  CG1 ILE A  98      17.067  22.725   7.579  1.00 42.02           C  
ATOM    739  CG2 ILE A  98      15.804  20.628   8.108  1.00 42.67           C  
ATOM    740  CD1 ILE A  98      16.147  23.874   7.853  1.00 41.83           C  
ATOM    741  N   PHE A  99      17.128  18.384   5.684  1.00 47.32           N  
ATOM    742  CA  PHE A  99      16.494  17.194   5.202  1.00 49.75           C  
ATOM    743  C   PHE A  99      15.765  16.500   6.328  1.00 44.92           C  
ATOM    744  O   PHE A  99      16.366  16.023   7.299  1.00 42.90           O  
ATOM    745  CB  PHE A  99      17.542  16.265   4.612  1.00 54.45           C  
ATOM    746  CG  PHE A  99      18.370  16.897   3.533  1.00 55.66           C  
ATOM    747  CD1 PHE A  99      17.836  17.128   2.290  1.00 55.69           C  
ATOM    748  CD2 PHE A  99      19.691  17.252   3.775  1.00 56.73           C  
ATOM    749  CE1 PHE A  99      18.603  17.702   1.319  1.00 56.12           C  
ATOM    750  CE2 PHE A  99      20.469  17.835   2.801  1.00 54.89           C  
ATOM    751  CZ  PHE A  99      19.919  18.063   1.576  1.00 56.18           C  
ATOM    752  N   PHE A 100      14.462  16.445   6.193  1.00 43.50           N  
ATOM    753  CA  PHE A 100      13.679  15.693   7.128  1.00 46.79           C  
ATOM    754  C   PHE A 100      13.753  14.242   6.674  1.00 50.82           C  
ATOM    755  O   PHE A 100      13.468  13.942   5.513  1.00 57.09           O  
ATOM    756  CB  PHE A 100      12.248  16.214   7.181  1.00 46.69           C  
ATOM    757  CG  PHE A 100      12.118  17.562   7.834  1.00 45.45           C  
ATOM    758  CD1 PHE A 100      11.919  17.672   9.184  1.00 44.72           C  
ATOM    759  CD2 PHE A 100      12.174  18.715   7.088  1.00 47.98           C  
ATOM    760  CE1 PHE A 100      11.781  18.904   9.776  1.00 43.42           C  
ATOM    761  CE2 PHE A 100      12.039  19.950   7.683  1.00 45.35           C  
ATOM    762  CZ  PHE A 100      11.840  20.038   9.025  1.00 41.84           C  
ATOM    763  N   LYS A 101      14.187  13.352   7.568  1.00 52.37           N  
ATOM    764  CA  LYS A 101      14.477  11.976   7.188  1.00 51.17           C  
ATOM    765  C   LYS A 101      13.208  11.344   6.656  1.00 53.68           C  
ATOM    766  O   LYS A 101      12.183  11.406   7.302  1.00 59.96           O  
ATOM    767  CB  LYS A 101      15.047  11.192   8.366  1.00 50.20           C  
ATOM    768  CG  LYS A 101      15.397   9.750   8.067  1.00 49.55           C  
ATOM    769  N   ASP A 102      13.295  10.784   5.454  1.00 57.54           N  
ATOM    770  CA  ASP A 102      12.194  10.127   4.768  1.00 62.49           C  
ATOM    771  C   ASP A 102      11.030  11.083   4.550  1.00 59.48           C  
ATOM    772  O   ASP A 102       9.865  10.704   4.738  1.00 67.32           O  
ATOM    773  CB  ASP A 102      11.707   8.879   5.529  1.00 74.49           C  
ATOM    774  CG  ASP A 102      12.819   7.867   5.796  1.00 81.78           C  
ATOM    775  OD1 ASP A 102      13.382   7.336   4.803  1.00 80.70           O  
ATOM    776  OD2 ASP A 102      13.101   7.597   7.001  1.00 84.43           O1-
ATOM    777  N   ASP A 103      11.350  12.308   4.136  1.00 51.39           N  
ATOM    778  CA  ASP A 103      10.355  13.352   3.912  1.00 45.28           C  
ATOM    779  C   ASP A 103      11.032  14.543   3.234  1.00 47.34           C  
ATOM    780  O   ASP A 103      12.198  14.473   2.826  1.00 53.50           O  
ATOM    781  CB  ASP A 103       9.762  13.765   5.254  1.00 45.82           C  
ATOM    782  CG  ASP A 103       8.291  13.972   5.206  1.00 40.46           C  
ATOM    783  OD1 ASP A 103       7.828  14.446   4.185  1.00 43.38           O  
ATOM    784  OD2 ASP A 103       7.613  13.683   6.209  1.00 41.74           O1-
ATOM    785  N   GLY A 104      10.330  15.656   3.128  1.00 46.08           N  
ATOM    786  CA  GLY A 104      10.818  16.789   2.345  1.00 43.51           C  
ATOM    787  C   GLY A 104      12.007  17.553   2.875  1.00 40.07           C  
ATOM    788  O   GLY A 104      12.626  17.159   3.825  1.00 41.51           O  
ATOM    789  N   ASN A 105      12.312  18.673   2.243  1.00 43.76           N  
ATOM    790  CA  ASN A 105      13.424  19.487   2.660  1.00 45.72           C  
ATOM    791  C   ASN A 105      13.046  20.935   2.722  1.00 47.84           C  
ATOM    792  O   ASN A 105      12.108  21.350   2.041  1.00 48.62           O  
ATOM    793  CB  ASN A 105      14.622  19.339   1.729  1.00 48.70           C  
ATOM    794  CG  ASN A 105      14.308  19.666   0.301  1.00 49.20           C  
ATOM    795  OD1 ASN A 105      14.715  20.722  -0.226  1.00 51.80           O  
ATOM    796  ND2 ASN A 105      13.620  18.739  -0.368  1.00 50.67           N  
ATOM    797  N   TYR A 106      13.792  21.671   3.553  1.00 45.80           N  
ATOM    798  CA  TYR A 106      13.740  23.124   3.625  1.00 45.06           C  
ATOM    799  C   TYR A 106      15.026  23.701   3.126  1.00 45.62           C  
ATOM    800  O   TYR A 106      16.098  23.210   3.441  1.00 43.44           O  
ATOM    801  CB  TYR A 106      13.606  23.659   5.051  1.00 41.82           C  
ATOM    802  CG  TYR A 106      12.318  23.430   5.774  1.00 37.16           C  
ATOM    803  CD1 TYR A 106      11.156  22.992   5.141  1.00 37.41           C  
ATOM    804  CD2 TYR A 106      12.262  23.681   7.093  1.00 35.58           C  
ATOM    805  CE1 TYR A 106       9.982  22.795   5.858  1.00 35.04           C  
ATOM    806  CE2 TYR A 106      11.110  23.483   7.800  1.00 39.39           C  
ATOM    807  CZ  TYR A 106       9.967  23.047   7.178  1.00 35.67           C  
ATOM    808  OH  TYR A 106       8.868  22.892   7.991  1.00 37.95           O  
ATOM    809  N   LYS A 107      14.887  24.800   2.403  1.00 49.38           N  
ATOM    810  CA  LYS A 107      15.994  25.498   1.831  1.00 55.05           C  
ATOM    811  C   LYS A 107      15.842  26.943   2.216  1.00 51.08           C  
ATOM    812  O   LYS A 107      14.892  27.574   1.816  1.00 54.72           O  
ATOM    813  CB  LYS A 107      15.952  25.361   0.322  1.00 65.60           C  
ATOM    814  CG  LYS A 107      16.124  23.939  -0.179  1.00 77.09           C  
ATOM    815  CD  LYS A 107      16.665  23.918  -1.602  1.00 89.30           C  
ATOM    816  CE  LYS A 107      18.122  24.393  -1.688  1.00 98.77           C  
ATOM    817  NZ  LYS A 107      19.152  23.319  -1.529  1.00100.71           N  
ATOM    818  N   THR A 108      16.768  27.460   3.009  1.00 48.24           N  
ATOM    819  CA  THR A 108      16.599  28.754   3.604  1.00 43.10           C  
ATOM    820  C   THR A 108      17.743  29.623   3.242  1.00 46.35           C  
ATOM    821  O   THR A 108      18.885  29.177   3.236  1.00 49.85           O  
ATOM    822  CB  THR A 108      16.503  28.686   5.151  1.00 42.60           C  
ATOM    823  OG1 THR A 108      17.806  28.747   5.788  1.00 41.49           O  
ATOM    824  CG2 THR A 108      15.731  27.464   5.585  1.00 40.13           C  
ATOM    825  N   ARG A 109      17.444  30.874   2.920  1.00 49.00           N  
ATOM    826  CA  ARG A 109      18.467  31.891   2.953  1.00 48.90           C  
ATOM    827  C   ARG A 109      18.016  33.013   3.872  1.00 48.67           C  
ATOM    828  O   ARG A 109      16.882  33.437   3.809  1.00 49.82           O  
ATOM    829  CB  ARG A 109      18.790  32.400   1.576  1.00 50.20           C  
ATOM    830  CG  ARG A 109      20.011  33.296   1.576  1.00 53.51           C  
ATOM    831  CD  ARG A 109      20.415  33.620   0.167  1.00 57.30           C  
ATOM    832  NE  ARG A 109      21.342  34.735   0.083  1.00 65.70           N  
ATOM    833  CZ  ARG A 109      21.013  36.017   0.248  1.00 73.12           C  
ATOM    834  NH1 ARG A 109      19.755  36.388   0.557  1.00 70.92           N  
ATOM    835  NH2 ARG A 109      21.968  36.939   0.112  1.00 77.29           N  
ATOM    836  N   ALA A 110      18.913  33.435   4.756  1.00 52.10           N  
ATOM    837  CA  ALA A 110      18.673  34.525   5.670  1.00 51.60           C  
ATOM    838  C   ALA A 110      19.848  35.501   5.654  1.00 54.77           C  
ATOM    839  O   ALA A 110      20.980  35.155   5.308  1.00 53.05           O  
ATOM    840  CB  ALA A 110      18.455  34.001   7.075  1.00 53.70           C  
ATOM    841  N   GLU A 111      19.536  36.738   6.006  1.00 56.56           N  
ATOM    842  CA  GLU A 111      20.520  37.746   6.276  1.00 57.89           C  
ATOM    843  C   GLU A 111      20.320  38.203   7.690  1.00 54.60           C  
ATOM    844  O   GLU A 111      19.227  38.550   8.098  1.00 58.61           O  
ATOM    845  CB  GLU A 111      20.387  38.923   5.318  1.00 64.31           C  
ATOM    846  CG  GLU A 111      21.081  38.667   3.996  1.00 69.24           C  
ATOM    847  CD  GLU A 111      20.945  39.803   3.012  1.00 75.98           C  
ATOM    848  OE1 GLU A 111      21.487  40.880   3.312  1.00 89.74           O  
ATOM    849  OE2 GLU A 111      20.328  39.612   1.931  1.00 89.60           O1-
ATOM    850  N   VAL A 112      21.400  38.183   8.436  1.00 52.49           N  
ATOM    851  CA  VAL A 112      21.369  38.524   9.814  1.00 50.37           C  
ATOM    852  C   VAL A 112      22.322  39.691   9.867  1.00 53.00           C  
ATOM    853  O   VAL A 112      23.510  39.550   9.582  1.00 54.11           O  
ATOM    854  CB  VAL A 112      21.846  37.341  10.657  1.00 45.39           C  
ATOM    855  CG1 VAL A 112      21.685  37.631  12.122  1.00 46.09           C  
ATOM    856  CG2 VAL A 112      21.071  36.094  10.306  1.00 45.33           C  
ATOM    857  N   LYS A 113      21.787  40.867  10.148  1.00 56.95           N  
ATOM    858  CA  LYS A 113      22.626  42.061  10.250  1.00 60.78           C  
ATOM    859  C   LYS A 113      21.931  43.061  11.145  1.00 57.51           C  
ATOM    860  O   LYS A 113      20.723  42.966  11.357  1.00 53.61           O  
ATOM    861  CB  LYS A 113      22.887  42.669   8.866  1.00 62.07           C  
ATOM    862  CG  LYS A 113      21.622  42.861   8.047  1.00 66.19           C  
ATOM    863  CD  LYS A 113      21.782  43.958   7.005  1.00 77.10           C  
ATOM    864  CE  LYS A 113      20.873  43.744   5.789  1.00 84.15           C  
ATOM    865  NZ  LYS A 113      19.497  43.220   6.078  1.00 83.41           N  
ATOM    866  N   PHE A 114      22.702  43.993  11.695  1.00 59.03           N  
ATOM    867  CA  PHE A 114      22.111  45.090  12.450  1.00 58.60           C  
ATOM    868  C   PHE A 114      21.458  46.066  11.507  1.00 59.14           C  
ATOM    869  O   PHE A 114      22.048  46.422  10.480  1.00 58.94           O  
ATOM    870  CB  PHE A 114      23.135  45.824  13.312  1.00 55.27           C  
ATOM    871  CG  PHE A 114      23.188  45.322  14.708  1.00 53.77           C  
ATOM    872  CD1 PHE A 114      22.109  45.513  15.557  1.00 55.66           C  
ATOM    873  CD2 PHE A 114      24.294  44.638  15.170  1.00 54.71           C  
ATOM    874  CE1 PHE A 114      22.138  45.037  16.854  1.00 57.85           C  
ATOM    875  CE2 PHE A 114      24.342  44.162  16.468  1.00 56.22           C  
ATOM    876  CZ  PHE A 114      23.264  44.361  17.313  1.00 60.53           C  
ATOM    877  N   GLU A 115      20.235  46.468  11.863  1.00 60.82           N  
ATOM    878  CA  GLU A 115      19.491  47.502  11.155  1.00 62.66           C  
ATOM    879  C   GLU A 115      19.082  48.541  12.157  1.00 62.32           C  
ATOM    880  O   GLU A 115      17.939  48.572  12.609  1.00 61.59           O  
ATOM    881  CB  GLU A 115      18.259  46.930  10.477  1.00 69.31           C  
ATOM    882  CG  GLU A 115      18.581  46.115   9.240  1.00 72.64           C  
ATOM    883  CD  GLU A 115      17.396  45.321   8.775  1.00 74.51           C  
ATOM    884  OE1 GLU A 115      16.261  45.792   8.992  1.00 73.61           O  
ATOM    885  OE2 GLU A 115      17.600  44.229   8.212  1.00 81.84           O1-
ATOM    886  N   GLY A 116      20.047  49.398  12.478  1.00 67.00           N  
ATOM    887  CA  GLY A 116      19.948  50.339  13.566  1.00 61.25           C  
ATOM    888  C   GLY A 116      20.424  49.648  14.821  1.00 62.74           C  
ATOM    889  O   GLY A 116      21.516  49.050  14.869  1.00 62.67           O  
ATOM    890  N   ASP A 117      19.586  49.743  15.841  1.00 61.37           N  
ATOM    891  CA  ASP A 117      19.853  49.136  17.112  1.00 62.36           C  
ATOM    892  C   ASP A 117      19.343  47.696  17.107  1.00 61.38           C  
ATOM    893  O   ASP A 117      19.831  46.863  17.854  1.00 64.61           O  
ATOM    894  CB  ASP A 117      19.214  49.980  18.236  1.00 65.63           C  
ATOM    895  CG  ASP A 117      20.115  51.150  18.699  1.00 71.22           C  
ATOM    896  OD1 ASP A 117      20.954  51.646  17.907  1.00 76.65           O  
ATOM    897  OD2 ASP A 117      20.002  51.569  19.877  1.00 75.30           O1-
ATOM    898  N   THR A 118      18.376  47.411  16.242  1.00 63.83           N  
ATOM    899  CA  THR A 118      17.749  46.090  16.128  1.00 62.20           C  
ATOM    900  C   THR A 118      18.578  45.059  15.345  1.00 59.36           C  
ATOM    901  O   THR A 118      19.116  45.347  14.276  1.00 57.93           O  
ATOM    902  CB  THR A 118      16.396  46.219  15.413  1.00 61.60           C  
ATOM    903  OG1 THR A 118      15.760  47.433  15.824  1.00 66.96           O  
ATOM    904  CG2 THR A 118      15.494  45.050  15.744  1.00 63.24           C  
ATOM    905  N   LEU A 119      18.662  43.849  15.877  1.00 57.28           N  
ATOM    906  CA  LEU A 119      19.263  42.747  15.140  1.00 55.81           C  
ATOM    907  C   LEU A 119      18.175  42.004  14.363  1.00 52.25           C  
ATOM    908  O   LEU A 119      17.268  41.433  14.939  1.00 49.70           O  
ATOM    909  CB  LEU A 119      20.012  41.818  16.091  1.00 56.38           C  
ATOM    910  CG  LEU A 119      20.848  40.691  15.481  1.00 53.78           C  
ATOM    911  CD1 LEU A 119      19.964  39.647  14.808  1.00 55.56           C  
ATOM    912  CD2 LEU A 119      21.903  41.211  14.522  1.00 51.95           C  
ATOM    913  N   VAL A 120      18.295  41.997  13.045  1.00 54.82           N  
ATOM    914  CA  VAL A 120      17.228  41.543  12.178  1.00 52.37           C  
ATOM    915  C   VAL A 120      17.629  40.324  11.365  1.00 52.90           C  
ATOM    916  O   VAL A 120      18.703  40.321  10.738  1.00 54.72           O  
ATOM    917  CB  VAL A 120      16.858  42.645  11.196  1.00 54.13           C  
ATOM    918  CG1 VAL A 120      15.600  42.251  10.465  1.00 56.70           C  
ATOM    919  CG2 VAL A 120      16.669  43.973  11.921  1.00 52.42           C  
ATOM    920  N   ASN A 121      16.747  39.316  11.380  1.00 50.87           N  
ATOM    921  CA  ASN A 121      16.899  38.057  10.641  1.00 48.76           C  
ATOM    922  C   ASN A 121      15.784  37.954   9.616  1.00 46.00           C  
ATOM    923  O   ASN A 121      14.621  37.795   9.950  1.00 42.25           O  
ATOM    924  CB  ASN A 121      16.850  36.884  11.624  1.00 49.78           C  
ATOM    925  CG  ASN A 121      17.238  35.535  11.015  1.00 45.46           C  
ATOM    926  OD1 ASN A 121      17.723  35.423   9.893  1.00 42.13           O  
ATOM    927  ND2 ASN A 121      17.035  34.496  11.803  1.00 43.25           N  
ATOM    928  N   ARG A 122      16.152  38.066   8.354  1.00 47.36           N  
ATOM    929  CA  ARG A 122      15.180  38.015   7.287  1.00 52.70           C  
ATOM    930  C   ARG A 122      15.345  36.771   6.443  1.00 48.29           C  
ATOM    931  O   ARG A 122      16.340  36.626   5.776  1.00 44.94           O  
ATOM    932  CB  ARG A 122      15.323  39.237   6.396  1.00 58.53           C  
ATOM    933  CG  ARG A 122      14.807  40.511   7.027  1.00 61.35           C  
ATOM    934  CD  ARG A 122      14.602  41.589   5.978  1.00 66.58           C  
ATOM    935  NE  ARG A 122      14.892  42.907   6.528  1.00 67.48           N  
ATOM    936  CZ  ARG A 122      13.999  43.757   7.013  1.00 71.18           C  
ATOM    937  NH1 ARG A 122      12.701  43.481   7.033  1.00 78.20           N  
ATOM    938  NH2 ARG A 122      14.418  44.915   7.489  1.00 82.36           N  
ATOM    939  N   ILE A 123      14.320  35.927   6.422  1.00 48.64           N  
ATOM    940  CA  ILE A 123      14.445  34.580   5.902  1.00 48.41           C  
ATOM    941  C   ILE A 123      13.605  34.315   4.680  1.00 50.41           C  
ATOM    942  O   ILE A 123      12.443  34.648   4.653  1.00 55.19           O  
ATOM    943  CB  ILE A 123      14.017  33.560   6.962  1.00 49.86           C  
ATOM    944  CG1 ILE A 123      14.689  33.883   8.309  1.00 42.74           C  
ATOM    945  CG2 ILE A 123      14.354  32.145   6.485  1.00 48.96           C  
ATOM    946  CD1 ILE A 123      13.741  33.902   9.465  1.00 41.80           C  
ATOM    947  N   GLU A 124      14.218  33.729   3.656  1.00 56.72           N  
ATOM    948  CA  GLU A 124      13.492  33.107   2.551  1.00 56.04           C  
ATOM    949  C   GLU A 124      13.550  31.607   2.836  1.00 50.42           C  
ATOM    950  O   GLU A 124      14.632  31.071   2.960  1.00 49.54           O  
ATOM    951  CB  GLU A 124      14.174  33.395   1.205  1.00 61.25           C  
ATOM    952  CG  GLU A 124      14.211  34.847   0.724  1.00 67.51           C  
ATOM    953  CD  GLU A 124      13.038  35.221  -0.193  1.00 83.14           C  
ATOM    954  OE1 GLU A 124      12.311  34.313  -0.679  1.00 89.11           O  
ATOM    955  OE2 GLU A 124      12.828  36.439  -0.435  1.00 94.44           O1-
ATOM    956  N   LEU A 125      12.404  30.946   2.962  1.00 46.38           N  
ATOM    957  CA  LEU A 125      12.341  29.491   3.073  1.00 44.16           C  
ATOM    958  C   LEU A 125      11.574  28.839   1.931  1.00 47.36           C  
ATOM    959  O   LEU A 125      10.411  29.184   1.694  1.00 53.40           O  
ATOM    960  CB  LEU A 125      11.645  29.139   4.371  1.00 43.63           C  
ATOM    961  CG  LEU A 125      11.400  27.666   4.670  1.00 41.53           C  
ATOM    962  CD1 LEU A 125      11.716  27.424   6.112  1.00 41.14           C  
ATOM    963  CD2 LEU A 125       9.967  27.233   4.385  1.00 44.87           C  
ATOM    964  N   LYS A 126      12.189  27.884   1.236  1.00 45.54           N  
ATOM    965  CA  LYS A 126      11.434  27.032   0.304  1.00 45.52           C  
ATOM    966  C   LYS A 126      11.478  25.538   0.692  1.00 45.69           C  
ATOM    967  O   LYS A 126      12.535  24.971   0.904  1.00 50.85           O  
ATOM    968  CB  LYS A 126      11.898  27.259  -1.132  1.00 47.59           C  
ATOM    969  N   GLY A 127      10.316  24.905   0.791  1.00 47.36           N  
ATOM    970  CA  GLY A 127      10.224  23.510   1.209  1.00 47.62           C  
ATOM    971  C   GLY A 127       9.512  22.585   0.223  1.00 50.91           C  
ATOM    972  O   GLY A 127       8.343  22.781  -0.130  1.00 46.04           O  
ATOM    973  N   ILE A 128      10.195  21.538  -0.219  1.00 54.86           N  
ATOM    974  CA  ILE A 128       9.552  20.661  -1.165  1.00 52.10           C  
ATOM    975  C   ILE A 128       9.542  19.177  -0.770  1.00 53.63           C  
ATOM    976  O   ILE A 128      10.216  18.756   0.152  1.00 54.47           O  
ATOM    977  CB  ILE A 128      10.097  20.962  -2.564  1.00 53.66           C  
ATOM    978  CG1 ILE A 128       9.134  20.456  -3.661  1.00 58.34           C  
ATOM    979  CG2 ILE A 128      11.514  20.455  -2.709  1.00 55.08           C  
ATOM    980  CD1 ILE A 128       7.682  20.940  -3.597  1.00 54.35           C  
ATOM    981  N   ASP A 129       8.642  18.427  -1.392  1.00 56.97           N  
ATOM    982  CA  ASP A 129       8.614  16.970  -1.341  1.00 54.37           C  
ATOM    983  C   ASP A 129       8.167  16.392  -0.009  1.00 54.24           C  
ATOM    984  O   ASP A 129       8.493  15.271   0.323  1.00 57.07           O  
ATOM    985  CB  ASP A 129       9.974  16.383  -1.760  1.00 53.88           C  
ATOM    986  CG  ASP A 129       9.999  15.900  -3.180  1.00 48.87           C  
ATOM    987  OD1 ASP A 129       9.208  16.321  -4.013  1.00 53.16           O  
ATOM    988  OD2 ASP A 129      10.849  15.075  -3.488  1.00 56.47           O1-
ATOM    989  N   PHE A 130       7.346  17.116   0.729  1.00 61.02           N  
ATOM    990  CA  PHE A 130       6.831  16.583   1.996  1.00 59.39           C  
ATOM    991  C   PHE A 130       5.695  15.640   1.692  1.00 57.82           C  
ATOM    992  O   PHE A 130       5.198  15.639   0.592  1.00 57.91           O  
ATOM    993  CB  PHE A 130       6.412  17.720   2.964  1.00 56.86           C  
ATOM    994  CG  PHE A 130       7.579  18.455   3.536  1.00 50.37           C  
ATOM    995  CD1 PHE A 130       8.138  19.512   2.860  1.00 48.50           C  
ATOM    996  CD2 PHE A 130       8.167  18.028   4.698  1.00 51.18           C  
ATOM    997  CE1 PHE A 130       9.242  20.153   3.337  1.00 49.27           C  
ATOM    998  CE2 PHE A 130       9.276  18.677   5.195  1.00 53.55           C  
ATOM    999  CZ  PHE A 130       9.806  19.755   4.517  1.00 49.20           C  
ATOM   1000  N   LYS A 131       5.301  14.831   2.662  1.00 58.36           N  
ATOM   1001  CA  LYS A 131       4.203  13.903   2.476  1.00 58.88           C  
ATOM   1002  C   LYS A 131       3.050  14.507   3.192  1.00 62.69           C  
ATOM   1003  O   LYS A 131       3.165  14.792   4.375  1.00 74.48           O  
ATOM   1004  CB  LYS A 131       4.542  12.535   3.073  1.00 58.68           C  
ATOM   1005  CG  LYS A 131       5.814  11.950   2.495  1.00 58.43           C  
ATOM   1006  CD  LYS A 131       6.204  10.647   3.148  1.00 62.71           C  
ATOM   1007  CE  LYS A 131       7.488  10.119   2.522  1.00 69.94           C  
ATOM   1008  N   GLU A 132       1.933  14.703   2.504  1.00 65.69           N  
ATOM   1009  CA  GLU A 132       0.790  15.381   3.116  1.00 66.24           C  
ATOM   1010  C   GLU A 132       0.291  14.634   4.360  1.00 67.66           C  
ATOM   1011  O   GLU A 132      -0.312  15.231   5.236  1.00 70.87           O  
ATOM   1012  CB  GLU A 132      -0.333  15.604   2.099  1.00 63.03           C  
ATOM   1013  N   ASP A 133       0.552  13.336   4.453  1.00 74.66           N  
ATOM   1014  CA  ASP A 133       0.247  12.610   5.686  1.00 83.93           C  
ATOM   1015  C   ASP A 133       1.521  12.080   6.347  1.00 81.99           C  
ATOM   1016  O   ASP A 133       1.558  10.978   6.905  1.00 83.43           O  
ATOM   1017  CB  ASP A 133      -0.808  11.507   5.461  1.00 94.94           C  
ATOM   1018  CG  ASP A 133      -0.405  10.492   4.403  1.00 94.45           C  
ATOM   1019  OD1 ASP A 133       0.776  10.068   4.397  1.00 99.94           O1-
ATOM   1020  OD2 ASP A 133      -1.289  10.108   3.597  1.00 93.27           O  
ATOM   1021  N   GLY A 134       2.560  12.905   6.285  1.00 77.94           N  
ATOM   1022  CA  GLY A 134       3.806  12.648   6.974  1.00 65.78           C  
ATOM   1023  C   GLY A 134       3.796  13.396   8.275  1.00 56.09           C  
ATOM   1024  O   GLY A 134       2.804  14.000   8.668  1.00 54.74           O  
ATOM   1025  N   ASN A 135       4.923  13.350   8.942  1.00 50.26           N  
ATOM   1026  CA  ASN A 135       5.071  13.983  10.216  1.00 47.72           C  
ATOM   1027  C   ASN A 135       5.024  15.498  10.139  1.00 45.76           C  
ATOM   1028  O   ASN A 135       4.525  16.142  11.046  1.00 48.45           O  
ATOM   1029  CB  ASN A 135       6.403  13.574  10.815  1.00 49.76           C  
ATOM   1030  CG  ASN A 135       6.440  12.124  11.259  1.00 48.55           C  
ATOM   1031  OD1 ASN A 135       5.426  11.521  11.622  1.00 49.16           O  
ATOM   1032  ND2 ASN A 135       7.636  11.574  11.281  1.00 47.48           N  
ATOM   1033  N   ILE A 136       5.546  16.069   9.062  1.00 46.85           N  
ATOM   1034  CA  ILE A 136       5.616  17.515   8.938  1.00 45.33           C  
ATOM   1035  C   ILE A 136       4.278  18.090   8.463  1.00 47.22           C  
ATOM   1036  O   ILE A 136       3.590  18.732   9.232  1.00 48.46           O  
ATOM   1037  CB  ILE A 136       6.763  17.953   8.039  1.00 41.67           C  
ATOM   1038  CG1 ILE A 136       8.090  17.733   8.734  1.00 40.43           C  
ATOM   1039  CG2 ILE A 136       6.650  19.440   7.750  1.00 44.20           C  
ATOM   1040  CD1 ILE A 136       8.436  16.315   9.067  1.00 40.91           C  
ATOM   1041  N   LEU A 137       3.897  17.831   7.218  1.00 49.64           N  
ATOM   1042  CA  LEU A 137       2.582  18.268   6.722  1.00 50.65           C  
ATOM   1043  C   LEU A 137       1.339  17.666   7.429  1.00 53.46           C  
ATOM   1044  O   LEU A 137       0.233  18.205   7.291  1.00 56.08           O  
ATOM   1045  CB  LEU A 137       2.476  18.008   5.241  1.00 45.69           C  
ATOM   1046  CG  LEU A 137       3.265  18.928   4.334  1.00 49.84           C  
ATOM   1047  CD1 LEU A 137       3.086  18.428   2.920  1.00 55.67           C  
ATOM   1048  CD2 LEU A 137       2.859  20.392   4.389  1.00 49.28           C  
ATOM   1049  N   GLY A 138       1.522  16.571   8.173  1.00 55.90           N  
ATOM   1050  CA  GLY A 138       0.455  15.967   8.989  1.00 53.67           C  
ATOM   1051  C   GLY A 138       0.399  16.409  10.447  1.00 52.93           C  
ATOM   1052  O   GLY A 138      -0.456  15.969  11.185  1.00 52.01           O  
ATOM   1053  N   HIS A 139       1.315  17.274  10.864  1.00 54.30           N  
ATOM   1054  CA  HIS A 139       1.312  17.846  12.197  1.00 54.73           C  
ATOM   1055  C   HIS A 139       1.294  16.813  13.315  1.00 53.76           C  
ATOM   1056  O   HIS A 139       0.399  16.808  14.161  1.00 53.71           O  
ATOM   1057  CB  HIS A 139       0.130  18.784  12.364  1.00 55.42           C  
ATOM   1058  CG  HIS A 139       0.188  20.013  11.514  1.00 52.32           C  
ATOM   1059  ND1 HIS A 139       0.710  21.204  11.966  1.00 57.27           N  
ATOM   1060  CD2 HIS A 139      -0.263  20.254  10.268  1.00 52.41           C  
ATOM   1061  CE1 HIS A 139       0.583  22.124  11.031  1.00 53.64           C  
ATOM   1062  NE2 HIS A 139      -0.007  21.572   9.991  1.00 53.01           N  
ATOM   1063  N   LYS A 140       2.308  15.959  13.322  1.00 52.34           N  
ATOM   1064  CA  LYS A 140       2.398  14.895  14.303  1.00 52.37           C  
ATOM   1065  C   LYS A 140       3.532  15.116  15.293  1.00 54.99           C  
ATOM   1066  O   LYS A 140       3.818  14.241  16.123  1.00 60.80           O  
ATOM   1067  CB  LYS A 140       2.571  13.558  13.596  1.00 52.54           C  
ATOM   1068  CG  LYS A 140       1.436  13.250  12.651  1.00 55.01           C  
ATOM   1069  CD  LYS A 140       1.725  12.071  11.749  1.00 57.94           C  
ATOM   1070  CE  LYS A 140       0.644  11.935  10.683  1.00 59.51           C  
ATOM   1071  NZ  LYS A 140       0.936  10.791   9.770  1.00 62.80           N  
ATOM   1072  N   LEU A 141       4.161  16.289  15.233  1.00 54.63           N  
ATOM   1073  CA  LEU A 141       5.266  16.592  16.117  1.00 50.01           C  
ATOM   1074  C   LEU A 141       4.709  17.161  17.372  1.00 52.87           C  
ATOM   1075  O   LEU A 141       3.700  17.863  17.347  1.00 60.08           O  
ATOM   1076  CB  LEU A 141       6.209  17.610  15.506  1.00 50.95           C  
ATOM   1077  CG  LEU A 141       6.922  17.174  14.236  1.00 56.80           C  
ATOM   1078  CD1 LEU A 141       7.918  18.242  13.822  1.00 56.20           C  
ATOM   1079  CD2 LEU A 141       7.574  15.810  14.437  1.00 56.98           C  
ATOM   1080  N   GLU A 142       5.402  16.873  18.466  1.00 50.50           N  
ATOM   1081  CA  GLU A 142       5.092  17.401  19.764  1.00 45.95           C  
ATOM   1082  C   GLU A 142       5.415  18.889  19.831  1.00 49.38           C  
ATOM   1083  O   GLU A 142       6.311  19.353  19.132  1.00 54.10           O  
ATOM   1084  CB  GLU A 142       5.903  16.626  20.784  1.00 46.65           C  
ATOM   1085  CG  GLU A 142       5.368  15.221  21.054  1.00 45.91           C  
ATOM   1086  CD  GLU A 142       6.219  14.492  22.041  1.00 48.04           C  
ATOM   1087  OE1 GLU A 142       6.885  15.179  22.828  1.00 55.51           O  
ATOM   1088  OE2 GLU A 142       6.262  13.249  22.021  1.00 53.50           O1-
ATOM   1089  N   TYR A 143       4.696  19.663  20.649  1.00 49.57           N  
ATOM   1090  CA  TYR A 143       4.973  21.107  20.684  1.00 46.32           C  
ATOM   1091  C   TYR A 143       6.060  21.307  21.685  1.00 43.13           C  
ATOM   1092  O   TYR A 143       5.804  21.710  22.784  1.00 44.85           O  
ATOM   1093  CB  TYR A 143       3.745  21.960  21.016  1.00 44.60           C  
ATOM   1094  CG  TYR A 143       4.005  23.447  20.919  1.00 42.80           C  
ATOM   1095  CD1 TYR A 143       4.241  24.046  19.704  1.00 42.68           C  
ATOM   1096  CD2 TYR A 143       4.049  24.240  22.047  1.00 43.40           C  
ATOM   1097  CE1 TYR A 143       4.507  25.399  19.609  1.00 45.09           C  
ATOM   1098  CE2 TYR A 143       4.298  25.602  21.964  1.00 43.62           C  
ATOM   1099  CZ  TYR A 143       4.529  26.180  20.742  1.00 42.51           C  
ATOM   1100  OH  TYR A 143       4.776  27.532  20.632  1.00 43.44           O  
ATOM   1101  N   ASN A 144       7.277  20.976  21.284  1.00 42.88           N  
ATOM   1102  CA  ASN A 144       8.384  20.903  22.202  1.00 41.87           C  
ATOM   1103  C   ASN A 144       9.714  20.799  21.464  1.00 42.48           C  
ATOM   1104  O   ASN A 144       9.723  20.794  20.234  1.00 45.29           O  
ATOM   1105  CB  ASN A 144       8.173  19.795  23.258  1.00 44.56           C  
ATOM   1106  CG  ASN A 144       8.412  18.376  22.747  1.00 45.54           C  
ATOM   1107  OD1 ASN A 144       8.787  18.140  21.609  1.00 48.08           O  
ATOM   1108  ND2 ASN A 144       8.200  17.419  23.631  1.00 48.11           N  
ATOM   1109  N   TYR A 145      10.826  20.784  22.214  1.00 41.65           N  
ATOM   1110  CA  TYR A 145      12.157  20.842  21.633  1.00 39.49           C  
ATOM   1111  C   TYR A 145      13.179  20.216  22.518  1.00 40.38           C  
ATOM   1112  O   TYR A 145      13.077  20.287  23.726  1.00 45.65           O  
ATOM   1113  CB  TYR A 145      12.556  22.284  21.356  1.00 42.20           C  
ATOM   1114  CG  TYR A 145      13.229  22.422  20.029  1.00 42.83           C  
ATOM   1115  CD1 TYR A 145      12.488  22.400  18.881  1.00 43.58           C  
ATOM   1116  CD2 TYR A 145      14.610  22.523  19.916  1.00 43.70           C  
ATOM   1117  CE1 TYR A 145      13.086  22.505  17.652  1.00 45.45           C  
ATOM   1118  CE2 TYR A 145      15.208  22.629  18.685  1.00 42.75           C  
ATOM   1119  CZ  TYR A 145      14.435  22.613  17.559  1.00 43.15           C  
ATOM   1120  OH  TYR A 145      14.967  22.707  16.305  1.00 45.68           O  
ATOM   1121  N   ASN A 146      14.197  19.619  21.925  1.00 44.16           N  
ATOM   1122  CA  ASN A 146      15.198  18.930  22.703  1.00 46.18           C  
ATOM   1123  C   ASN A 146      16.493  19.689  22.701  1.00 52.04           C  
ATOM   1124  O   ASN A 146      16.583  20.805  22.193  1.00 54.54           O  
ATOM   1125  CB  ASN A 146      15.406  17.532  22.163  1.00 46.04           C  
ATOM   1126  CG  ASN A 146      14.219  16.638  22.420  1.00 47.90           C  
ATOM   1127  OD1 ASN A 146      13.775  16.439  23.558  1.00 52.58           O  
ATOM   1128  ND2 ASN A 146      13.679  16.111  21.360  1.00 53.05           N  
ATOM   1129  N   SER A 147      17.505  19.076  23.291  1.00 56.89           N  
ATOM   1130  CA  SER A 147      18.768  19.712  23.462  1.00 51.58           C  
ATOM   1131  C   SER A 147      19.699  19.114  22.475  1.00 47.76           C  
ATOM   1132  O   SER A 147      19.688  17.901  22.296  1.00 45.66           O  
ATOM   1133  CB  SER A 147      19.258  19.437  24.844  1.00 57.37           C  
ATOM   1134  OG  SER A 147      20.176  20.436  25.171  1.00 77.18           O  
ATOM   1135  N   HIS A 148      20.478  19.979  21.826  1.00 48.25           N  
ATOM   1136  CA  HIS A 148      21.366  19.616  20.721  1.00 45.89           C  
ATOM   1137  C   HIS A 148      22.667  20.358  20.797  1.00 48.07           C  
ATOM   1138  O   HIS A 148      22.760  21.420  21.410  1.00 50.18           O  
ATOM   1139  CB  HIS A 148      20.750  19.942  19.373  1.00 45.43           C  
ATOM   1140  CG  HIS A 148      19.367  19.418  19.230  1.00 47.12           C  
ATOM   1141  ND1 HIS A 148      18.254  20.199  19.439  1.00 48.85           N  
ATOM   1142  CD2 HIS A 148      18.911  18.178  18.964  1.00 44.43           C  
ATOM   1143  CE1 HIS A 148      17.171  19.462  19.290  1.00 45.00           C  
ATOM   1144  NE2 HIS A 148      17.543  18.235  19.002  1.00 41.78           N  
ATOM   1145  N   ASN A 149      23.666  19.769  20.152  1.00 51.00           N  
ATOM   1146  CA  ASN A 149      24.914  20.422  19.872  1.00 50.48           C  
ATOM   1147  C   ASN A 149      25.005  20.806  18.401  1.00 49.66           C  
ATOM   1148  O   ASN A 149      24.613  20.068  17.486  1.00 53.10           O  
ATOM   1149  CB  ASN A 149      26.064  19.517  20.253  1.00 54.05           C  
ATOM   1150  CG  ASN A 149      26.118  19.242  21.733  1.00 52.44           C  
ATOM   1151  OD1 ASN A 149      26.341  18.124  22.157  1.00 58.07           O  
ATOM   1152  ND2 ASN A 149      25.926  20.262  22.520  1.00 55.71           N  
ATOM   1153  N   VAL A 150      25.525  21.994  18.188  1.00 49.45           N  
ATOM   1154  CA  VAL A 150      25.583  22.593  16.889  1.00 47.30           C  
ATOM   1155  C   VAL A 150      27.059  22.718  16.655  1.00 48.18           C  
ATOM   1156  O   VAL A 150      27.730  23.407  17.390  1.00 51.84           O  
ATOM   1157  CB  VAL A 150      24.925  23.981  16.942  1.00 48.11           C  
ATOM   1158  CG1 VAL A 150      25.335  24.839  15.759  1.00 49.57           C  
ATOM   1159  CG2 VAL A 150      23.413  23.850  17.060  1.00 46.63           C  
ATOM   1160  N   TYR A 151      27.569  22.045  15.640  1.00 52.12           N  
ATOM   1161  CA  TYR A 151      29.003  21.891  15.483  1.00 51.73           C  
ATOM   1162  C   TYR A 151      29.563  22.790  14.421  1.00 51.69           C  
ATOM   1163  O   TYR A 151      29.143  22.728  13.281  1.00 52.46           O  
ATOM   1164  CB  TYR A 151      29.322  20.452  15.129  1.00 53.04           C  
ATOM   1165  CG  TYR A 151      29.051  19.512  16.259  1.00 50.10           C  
ATOM   1166  CD1 TYR A 151      29.883  19.509  17.381  1.00 52.45           C  
ATOM   1167  CD2 TYR A 151      27.980  18.637  16.224  1.00 45.19           C  
ATOM   1168  CE1 TYR A 151      29.643  18.667  18.443  1.00 50.27           C  
ATOM   1169  CE2 TYR A 151      27.743  17.785  17.276  1.00 46.44           C  
ATOM   1170  CZ  TYR A 151      28.576  17.797  18.382  1.00 47.64           C  
ATOM   1171  OH  TYR A 151      28.358  16.947  19.455  1.00 54.24           O  
ATOM   1172  N   ILE A 152      30.554  23.583  14.799  1.00 52.08           N  
ATOM   1173  CA  ILE A 152      31.029  24.667  13.973  1.00 53.13           C  
ATOM   1174  C   ILE A 152      32.456  24.394  13.549  1.00 54.33           C  
ATOM   1175  O   ILE A 152      33.315  24.122  14.390  1.00 52.02           O  
ATOM   1176  CB  ILE A 152      30.948  26.001  14.747  1.00 52.12           C  
ATOM   1177  CG1 ILE A 152      29.507  26.197  15.237  1.00 51.85           C  
ATOM   1178  CG2 ILE A 152      31.459  27.163  13.904  1.00 50.50           C  
ATOM   1179  CD1 ILE A 152      29.150  27.588  15.687  1.00 52.12           C  
ATOM   1180  N   MET A 153      32.662  24.467  12.235  1.00 59.74           N  
ATOM   1181  CA  MET A 153      33.968  24.443  11.583  1.00 63.93           C  
ATOM   1182  C   MET A 153      34.203  25.721  10.828  1.00 67.28           C  
ATOM   1183  O   MET A 153      33.276  26.290  10.240  1.00 65.32           O  
ATOM   1184  CB  MET A 153      34.016  23.384  10.510  1.00 64.00           C  
ATOM   1185  CG  MET A 153      34.447  22.011  10.931  1.00 66.92           C  
ATOM   1186  SD  MET A 153      33.907  20.850   9.660  1.00 82.43           S  
ATOM   1187  CE  MET A 153      34.241  21.682   8.089  1.00 82.19           C  
ATOM   1188  N   ALA A 154      35.463  26.131  10.780  1.00 73.70           N  
ATOM   1189  CA  ALA A 154      35.869  27.200   9.876  1.00 75.13           C  
ATOM   1190  C   ALA A 154      35.935  26.689   8.413  1.00 73.36           C  
ATOM   1191  O   ALA A 154      36.303  25.532   8.132  1.00 77.89           O  
ATOM   1192  CB  ALA A 154      37.207  27.786  10.318  1.00 73.34           C  
ATOM   1193  N   ASP A 155      35.557  27.556   7.489  1.00 63.99           N  
ATOM   1194  CA  ASP A 155      35.657  27.251   6.087  1.00 60.91           C  
ATOM   1195  C   ASP A 155      36.311  28.468   5.487  1.00 61.36           C  
ATOM   1196  O   ASP A 155      35.638  29.405   5.078  1.00 64.79           O  
ATOM   1197  CB  ASP A 155      34.264  26.968   5.524  1.00 63.76           C  
ATOM   1198  CG  ASP A 155      34.253  26.655   4.046  1.00 60.00           C  
ATOM   1199  OD1 ASP A 155      34.310  25.469   3.657  1.00 61.53           O  
ATOM   1200  OD2 ASP A 155      34.121  27.614   3.284  1.00 64.62           O1-
ATOM   1201  N   LYS A 156      37.643  28.455   5.489  1.00 62.96           N  
ATOM   1202  CA  LYS A 156      38.451  29.568   4.988  1.00 66.50           C  
ATOM   1203  C   LYS A 156      38.212  29.866   3.500  1.00 72.60           C  
ATOM   1204  O   LYS A 156      38.236  31.033   3.072  1.00 65.50           O  
ATOM   1205  CB  LYS A 156      39.932  29.267   5.226  1.00 67.73           C  
ATOM   1206  N   GLN A 157      37.987  28.788   2.740  1.00 79.24           N  
ATOM   1207  CA  GLN A 157      37.638  28.816   1.317  1.00 79.76           C  
ATOM   1208  C   GLN A 157      36.625  29.920   1.028  1.00 80.93           C  
ATOM   1209  O   GLN A 157      36.862  30.777   0.182  1.00 80.75           O  
ATOM   1210  CB  GLN A 157      37.043  27.454   0.923  1.00 87.65           C  
ATOM   1211  CG  GLN A 157      37.453  26.927  -0.435  1.00100.04           C  
ATOM   1212  CD  GLN A 157      38.689  26.051  -0.383  1.00121.08           C  
ATOM   1213  OE1 GLN A 157      38.615  24.828  -0.553  1.00126.40           O  
ATOM   1214  NE2 GLN A 157      39.840  26.672  -0.147  1.00136.84           N  
ATOM   1215  N   LYS A 158      35.492  29.875   1.737  1.00 79.42           N  
ATOM   1216  CA  LYS A 158      34.429  30.875   1.612  1.00 78.64           C  
ATOM   1217  C   LYS A 158      34.604  31.981   2.686  1.00 86.70           C  
ATOM   1218  O   LYS A 158      33.905  33.016   2.656  1.00 81.43           O  
ATOM   1219  CB  LYS A 158      33.028  30.215   1.704  1.00 74.68           C  
ATOM   1220  CG  LYS A 158      32.726  29.122   0.663  1.00 69.14           C  
ATOM   1221  CD  LYS A 158      31.236  28.821   0.449  1.00 58.28           C  
ATOM   1222  N   ASN A 159      35.550  31.742   3.609  1.00 87.87           N  
ATOM   1223  CA  ASN A 159      35.912  32.640   4.730  1.00 92.03           C  
ATOM   1224  C   ASN A 159      34.716  32.981   5.627  1.00 82.52           C  
ATOM   1225  O   ASN A 159      34.340  34.136   5.877  1.00 75.82           O  
ATOM   1226  CB  ASN A 159      36.675  33.888   4.251  1.00102.72           C  
ATOM   1227  CG  ASN A 159      37.644  34.427   5.309  1.00108.92           C  
ATOM   1228  OD1 ASN A 159      38.332  33.660   5.996  1.00111.01           O  
ATOM   1229  ND2 ASN A 159      37.703  35.750   5.441  1.00110.71           N  
ATOM   1230  N   GLY A 160      34.131  31.911   6.116  1.00 74.77           N  
ATOM   1231  CA  GLY A 160      32.906  31.980   6.859  1.00 71.02           C  
ATOM   1232  C   GLY A 160      32.966  30.746   7.690  1.00 65.32           C  
ATOM   1233  O   GLY A 160      34.042  30.390   8.179  1.00 66.04           O  
ATOM   1234  N   ILE A 161      31.837  30.070   7.827  1.00 60.23           N  
ATOM   1235  CA  ILE A 161      31.828  28.843   8.588  1.00 53.05           C  
ATOM   1236  C   ILE A 161      30.956  27.815   7.980  1.00 45.43           C  
ATOM   1237  O   ILE A 161      30.261  28.080   7.034  1.00 44.27           O  
ATOM   1238  CB  ILE A 161      31.447  29.074  10.054  1.00 56.74           C  
ATOM   1239  CG1 ILE A 161      30.208  29.941  10.179  1.00 53.62           C  
ATOM   1240  CG2 ILE A 161      32.634  29.684  10.785  1.00 61.68           C  
ATOM   1241  CD1 ILE A 161      29.933  30.346  11.599  1.00 53.88           C  
ATOM   1242  N   LYS A 162      31.067  26.622   8.521  1.00 44.61           N  
ATOM   1243  CA  LYS A 162      30.397  25.469   8.004  1.00 49.07           C  
ATOM   1244  C   LYS A 162      29.851  24.818   9.223  1.00 50.44           C  
ATOM   1245  O   LYS A 162      30.619  24.328  10.054  1.00 52.71           O  
ATOM   1246  CB  LYS A 162      31.401  24.524   7.349  1.00 51.20           C  
ATOM   1247  CG  LYS A 162      30.836  23.562   6.330  1.00 49.59           C  
ATOM   1248  CD  LYS A 162      31.384  23.915   4.955  1.00 53.44           C  
ATOM   1249  N   VAL A 163      28.530  24.818   9.343  1.00 49.22           N  
ATOM   1250  CA  VAL A 163      27.893  24.305  10.518  1.00 45.81           C  
ATOM   1251  C   VAL A 163      27.047  23.094  10.206  1.00 46.69           C  
ATOM   1252  O   VAL A 163      26.444  23.042   9.172  1.00 44.36           O  
ATOM   1253  CB  VAL A 163      27.005  25.358  11.122  1.00 46.55           C  
ATOM   1254  CG1 VAL A 163      26.532  24.912  12.489  1.00 47.55           C  
ATOM   1255  CG2 VAL A 163      27.746  26.683  11.183  1.00 50.03           C  
ATOM   1256  N   ASN A 164      27.009  22.137  11.135  1.00 52.04           N  
ATOM   1257  CA  ASN A 164      26.186  20.953  11.006  1.00 56.05           C  
ATOM   1258  C   ASN A 164      25.660  20.467  12.354  1.00 51.97           C  
ATOM   1259  O   ASN A 164      26.256  20.742  13.395  1.00 52.99           O  
ATOM   1260  CB  ASN A 164      26.992  19.837  10.384  1.00 62.79           C  
ATOM   1261  CG  ASN A 164      27.928  19.193  11.381  1.00 67.11           C  
ATOM   1262  OD1 ASN A 164      28.893  19.810  11.820  1.00 74.76           O  
ATOM   1263  ND2 ASN A 164      27.639  17.959  11.759  1.00 68.55           N  
ATOM   1264  N   PHE A 165      24.533  19.753  12.302  1.00 48.93           N  
ATOM   1265  CA  PHE A 165      23.860  19.174  13.462  1.00 44.84           C  
ATOM   1266  C   PHE A 165      22.588  18.512  12.960  1.00 48.74           C  
ATOM   1267  O   PHE A 165      22.143  18.784  11.869  1.00 47.87           O  
ATOM   1268  CB  PHE A 165      23.525  20.226  14.513  1.00 45.63           C  
ATOM   1269  CG  PHE A 165      22.766  21.441  13.965  1.00 45.62           C  
ATOM   1270  CD1 PHE A 165      23.430  22.471  13.291  1.00 45.58           C  
ATOM   1271  CD2 PHE A 165      21.407  21.564  14.140  1.00 40.43           C  
ATOM   1272  CE1 PHE A 165      22.754  23.558  12.784  1.00 41.03           C  
ATOM   1273  CE2 PHE A 165      20.742  22.650  13.644  1.00 39.13           C  
ATOM   1274  CZ  PHE A 165      21.414  23.647  12.970  1.00 40.24           C  
ATOM   1275  N   LYS A 166      22.009  17.632  13.764  1.00 55.89           N  
ATOM   1276  CA  LYS A 166      20.703  17.045  13.470  1.00 52.26           C  
ATOM   1277  C   LYS A 166      19.724  17.361  14.570  1.00 47.02           C  
ATOM   1278  O   LYS A 166      20.033  17.185  15.717  1.00 47.74           O  
ATOM   1279  CB  LYS A 166      20.773  15.529  13.418  1.00 52.62           C  
ATOM   1280  CG  LYS A 166      21.951  14.974  12.701  1.00 55.58           C  
ATOM   1281  CD  LYS A 166      21.615  13.577  12.230  1.00 63.27           C  
ATOM   1282  CE  LYS A 166      22.870  12.878  11.739  1.00 69.78           C  
ATOM   1283  NZ  LYS A 166      22.518  11.823  10.752  1.00 74.69           N  
ATOM   1284  N   ILE A 167      18.521  17.766  14.215  1.00 46.77           N  
ATOM   1285  CA  ILE A 167      17.481  17.956  15.206  1.00 43.89           C  
ATOM   1286  C   ILE A 167      16.700  16.652  15.348  1.00 42.10           C  
ATOM   1287  O   ILE A 167      16.540  15.909  14.405  1.00 43.25           O  
ATOM   1288  CB  ILE A 167      16.571  19.164  14.868  1.00 41.36           C  
ATOM   1289  CG1 ILE A 167      17.411  20.425  14.677  1.00 42.88           C  
ATOM   1290  CG2 ILE A 167      15.552  19.454  15.954  1.00 39.35           C  
ATOM   1291  CD1 ILE A 167      17.939  21.048  15.935  1.00 43.81           C  
ATOM   1292  N   ARG A 168      16.272  16.390  16.577  1.00 46.21           N  
ATOM   1293  CA  ARG A 168      15.539  15.221  16.977  1.00 46.89           C  
ATOM   1294  C   ARG A 168      14.162  15.690  17.290  1.00 47.17           C  
ATOM   1295  O   ARG A 168      13.894  16.070  18.427  1.00 48.87           O  
ATOM   1296  CB  ARG A 168      16.091  14.652  18.272  1.00 47.69           C  
ATOM   1297  CG  ARG A 168      17.180  13.620  18.179  1.00 50.65           C  
ATOM   1298  CD  ARG A 168      17.728  13.382  19.586  1.00 53.66           C  
ATOM   1299  NE  ARG A 168      18.914  14.220  19.877  1.00 58.55           N  
ATOM   1300  CZ  ARG A 168      19.030  15.146  20.836  1.00 56.99           C  
ATOM   1301  NH1 ARG A 168      18.041  15.427  21.665  1.00 61.14           N  
ATOM   1302  NH2 ARG A 168      20.172  15.804  20.971  1.00 62.45           N  
ATOM   1303  N   HIS A 169      13.280  15.662  16.301  1.00 50.67           N  
ATOM   1304  CA  HIS A 169      11.886  16.064  16.525  1.00 48.87           C  
ATOM   1305  C   HIS A 169      11.125  14.870  17.126  1.00 49.57           C  
ATOM   1306  O   HIS A 169      11.115  13.790  16.566  1.00 49.86           O  
ATOM   1307  CB  HIS A 169      11.245  16.572  15.227  1.00 47.32           C  
ATOM   1308  CG  HIS A 169      11.809  17.876  14.731  1.00 43.35           C  
ATOM   1309  ND1 HIS A 169      11.934  18.989  15.531  1.00 42.48           N  
ATOM   1310  CD2 HIS A 169      12.230  18.256  13.503  1.00 44.74           C  
ATOM   1311  CE1 HIS A 169      12.421  19.992  14.824  1.00 41.33           C  
ATOM   1312  NE2 HIS A 169      12.604  19.577  13.587  1.00 43.34           N  
ATOM   1313  N   ASN A 170      10.551  15.050  18.307  1.00 50.90           N  
ATOM   1314  CA  ASN A 170       9.725  14.010  18.883  1.00 51.68           C  
ATOM   1315  C   ASN A 170       8.367  13.942  18.225  1.00 51.08           C  
ATOM   1316  O   ASN A 170       7.747  14.980  17.979  1.00 52.75           O  
ATOM   1317  CB  ASN A 170       9.479  14.249  20.352  1.00 50.71           C  
ATOM   1318  CG  ASN A 170      10.643  13.921  21.197  1.00 47.13           C  
ATOM   1319  OD1 ASN A 170      10.567  14.040  22.409  1.00 48.51           O  
ATOM   1320  ND2 ASN A 170      11.721  13.510  20.589  1.00 50.51           N  
ATOM   1321  N   ILE A 171       7.905  12.711  18.017  1.00 49.74           N  
ATOM   1322  CA  ILE A 171       6.667  12.432  17.360  1.00 53.33           C  
ATOM   1323  C   ILE A 171       5.670  11.938  18.405  1.00 56.25           C  
ATOM   1324  O   ILE A 171       6.043  11.225  19.347  1.00 53.37           O  
ATOM   1325  CB  ILE A 171       6.891  11.392  16.246  1.00 58.21           C  
ATOM   1326  CG1 ILE A 171       7.930  11.898  15.237  1.00 56.11           C  
ATOM   1327  CG2 ILE A 171       5.611  11.107  15.497  1.00 57.97           C  
ATOM   1328  N   GLU A 172       4.417  12.384  18.252  1.00 61.33           N  
ATOM   1329  CA  GLU A 172       3.261  11.915  19.032  1.00 62.86           C  
ATOM   1330  C   GLU A 172       3.366  10.450  19.473  1.00 64.40           C  
ATOM   1331  O   GLU A 172       3.280  10.164  20.664  1.00 74.86           O  
ATOM   1332  CB  GLU A 172       1.975  12.055  18.206  1.00 65.90           C  
ATOM   1333  CG  GLU A 172       1.546  13.473  17.889  1.00 66.87           C  
ATOM   1334  N   ASP A 173       3.563   9.540  18.509  1.00 66.67           N  
ATOM   1335  CA  ASP A 173       3.565   8.074  18.754  1.00 62.65           C  
ATOM   1336  C   ASP A 173       4.748   7.506  19.532  1.00 61.81           C  
ATOM   1337  O   ASP A 173       4.852   6.293  19.711  1.00 62.90           O  
ATOM   1338  CB  ASP A 173       3.368   7.265  17.454  1.00 64.07           C  
ATOM   1339  CG  ASP A 173       4.520   7.394  16.455  1.00 64.51           C  
ATOM   1340  OD1 ASP A 173       5.471   8.174  16.687  1.00 66.11           O1-
ATOM   1341  OD2 ASP A 173       4.437   6.715  15.407  1.00 59.45           O  
ATOM   1342  N   GLY A 174       5.610   8.381  20.025  1.00 61.55           N  
ATOM   1343  CA  GLY A 174       6.761   7.960  20.794  1.00 63.69           C  
ATOM   1344  C   GLY A 174       7.981   7.763  19.920  1.00 61.71           C  
ATOM   1345  O   GLY A 174       8.869   7.003  20.268  1.00 72.52           O  
ATOM   1346  N   SER A 175       8.042   8.483  18.809  1.00 58.55           N  
ATOM   1347  CA  SER A 175       8.981   8.192  17.750  1.00 54.03           C  
ATOM   1348  C   SER A 175       9.779   9.446  17.522  1.00 51.71           C  
ATOM   1349  O   SER A 175       9.357  10.491  17.977  1.00 51.96           O  
ATOM   1350  CB  SER A 175       8.203   7.796  16.502  1.00 50.99           C  
ATOM   1351  OG  SER A 175       9.055   7.346  15.482  1.00 56.76           O  
ATOM   1352  N   VAL A 176      10.920   9.341  16.829  1.00 52.76           N  
ATOM   1353  CA  VAL A 176      11.722  10.509  16.462  1.00 46.42           C  
ATOM   1354  C   VAL A 176      11.889  10.683  14.980  1.00 44.70           C  
ATOM   1355  O   VAL A 176      12.176   9.762  14.241  1.00 47.49           O  
ATOM   1356  CB  VAL A 176      13.103  10.512  17.120  1.00 48.47           C  
ATOM   1357  CG1 VAL A 176      13.873  11.758  16.750  1.00 50.59           C  
ATOM   1358  CG2 VAL A 176      12.957  10.517  18.617  1.00 49.89           C  
ATOM   1359  N   GLN A 177      11.713  11.927  14.582  1.00 45.14           N  
ATOM   1360  CA  GLN A 177      11.863  12.381  13.246  1.00 43.75           C  
ATOM   1361  C   GLN A 177      13.101  13.218  13.206  1.00 44.53           C  
ATOM   1362  O   GLN A 177      13.172  14.281  13.779  1.00 47.70           O  
ATOM   1363  CB  GLN A 177      10.688  13.269  12.909  1.00 45.78           C  
ATOM   1364  CG  GLN A 177      10.939  14.183  11.745  1.00 45.41           C  
ATOM   1365  CD  GLN A 177      10.870  13.451  10.426  1.00 47.65           C  
ATOM   1366  OE1 GLN A 177       9.814  12.930  10.059  1.00 51.74           O  
ATOM   1367  NE2 GLN A 177      11.966  13.455   9.679  1.00 45.71           N  
ATOM   1368  N   LEU A 178      14.105  12.744  12.527  1.00 49.11           N  
ATOM   1369  CA  LEU A 178      15.332  13.477  12.515  1.00 48.52           C  
ATOM   1370  C   LEU A 178      15.269  14.533  11.449  1.00 45.88           C  
ATOM   1371  O   LEU A 178      14.566  14.352  10.464  1.00 46.85           O  
ATOM   1372  CB  LEU A 178      16.478  12.530  12.260  1.00 50.54           C  
ATOM   1373  CG  LEU A 178      16.770  11.619  13.449  1.00 49.81           C  
ATOM   1374  CD1 LEU A 178      17.534  10.432  12.911  1.00 51.42           C  
ATOM   1375  CD2 LEU A 178      17.544  12.306  14.568  1.00 48.97           C  
ATOM   1376  N   ALA A 179      15.998  15.631  11.652  1.00 43.26           N  
ATOM   1377  CA  ALA A 179      16.092  16.680  10.651  1.00 42.12           C  
ATOM   1378  C   ALA A 179      17.514  17.133  10.564  1.00 39.28           C  
ATOM   1379  O   ALA A 179      18.028  17.674  11.487  1.00 37.98           O  
ATOM   1380  CB  ALA A 179      15.173  17.842  10.990  1.00 43.66           C  
ATOM   1381  N   ASP A 180      18.132  16.930   9.410  1.00 45.97           N  
ATOM   1382  CA  ASP A 180      19.588  17.001   9.271  1.00 46.40           C  
ATOM   1383  C   ASP A 180      19.993  18.320   8.626  1.00 45.67           C  
ATOM   1384  O   ASP A 180      19.623  18.605   7.497  1.00 38.86           O  
ATOM   1385  CB  ASP A 180      20.051  15.805   8.431  1.00 50.28           C  
ATOM   1386  CG  ASP A 180      21.548  15.509   8.550  1.00 51.01           C  
ATOM   1387  OD1 ASP A 180      22.269  16.224   9.275  1.00 51.74           O  
ATOM   1388  OD2 ASP A 180      21.999  14.535   7.896  1.00 52.15           O1-
ATOM   1389  N   HIS A 181      20.743  19.136   9.365  1.00 49.04           N  
ATOM   1390  CA  HIS A 181      20.973  20.514   8.974  1.00 46.56           C  
ATOM   1391  C   HIS A 181      22.344  20.664   8.409  1.00 48.46           C  
ATOM   1392  O   HIS A 181      23.341  20.342   9.065  1.00 53.05           O  
ATOM   1393  CB  HIS A 181      20.837  21.436  10.169  1.00 45.77           C  
ATOM   1394  CG  HIS A 181      19.431  21.689  10.577  1.00 44.16           C  
ATOM   1395  ND1 HIS A 181      18.607  20.698  11.041  1.00 45.73           N  
ATOM   1396  CD2 HIS A 181      18.710  22.832  10.630  1.00 48.37           C  
ATOM   1397  CE1 HIS A 181      17.426  21.210  11.339  1.00 45.83           C  
ATOM   1398  NE2 HIS A 181      17.462  22.504  11.097  1.00 48.56           N  
ATOM   1399  N   TYR A 182      22.395  21.152   7.178  1.00 49.92           N  
ATOM   1400  CA  TYR A 182      23.645  21.560   6.586  1.00 46.04           C  
ATOM   1401  C   TYR A 182      23.656  23.056   6.463  1.00 42.82           C  
ATOM   1402  O   TYR A 182      22.833  23.626   5.791  1.00 43.26           O  
ATOM   1403  CB  TYR A 182      23.803  20.924   5.240  1.00 43.69           C  
ATOM   1404  CG  TYR A 182      23.795  19.445   5.333  1.00 45.90           C  
ATOM   1405  CD1 TYR A 182      24.972  18.742   5.517  1.00 46.39           C  
ATOM   1406  CD2 TYR A 182      22.612  18.745   5.275  1.00 45.43           C  
ATOM   1407  CE1 TYR A 182      24.969  17.379   5.619  1.00 46.86           C  
ATOM   1408  CE2 TYR A 182      22.601  17.385   5.384  1.00 46.36           C  
ATOM   1409  CZ  TYR A 182      23.776  16.704   5.546  1.00 50.49           C  
ATOM   1410  OH  TYR A 182      23.727  15.325   5.622  1.00 62.06           O  
ATOM   1411  N   GLN A 183      24.618  23.684   7.103  1.00 43.83           N  
ATOM   1412  CA  GLN A 183      24.629  25.122   7.206  1.00 47.17           C  
ATOM   1413  C   GLN A 183      25.961  25.812   6.891  1.00 47.96           C  
ATOM   1414  O   GLN A 183      27.033  25.364   7.269  1.00 51.41           O  
ATOM   1415  CB  GLN A 183      24.206  25.459   8.625  1.00 44.65           C  
ATOM   1416  CG  GLN A 183      24.102  26.924   8.922  1.00 42.95           C  
ATOM   1417  CD  GLN A 183      24.046  27.140  10.373  1.00 40.39           C  
ATOM   1418  OE1 GLN A 183      23.566  26.301  11.098  1.00 43.82           O  
ATOM   1419  NE2 GLN A 183      24.565  28.247  10.819  1.00 44.44           N  
ATOM   1420  N   GLN A 184      25.866  26.943   6.224  1.00 51.67           N  
ATOM   1421  CA  GLN A 184      27.017  27.802   6.059  1.00 54.89           C  
ATOM   1422  C   GLN A 184      26.630  29.261   6.259  1.00 52.67           C  
ATOM   1423  O   GLN A 184      25.557  29.690   5.830  1.00 45.14           O  
ATOM   1424  CB  GLN A 184      27.690  27.575   4.689  1.00 59.78           C  
ATOM   1425  CG  GLN A 184      27.257  28.485   3.547  1.00 59.83           C  
ATOM   1426  CD  GLN A 184      27.729  27.984   2.201  1.00 59.12           C  
ATOM   1427  OE1 GLN A 184      28.698  27.220   2.096  1.00 60.37           O  
ATOM   1428  NE2 GLN A 184      27.039  28.407   1.160  1.00 56.42           N  
ATOM   1429  N   ASN A 185      27.521  29.976   6.953  1.00 54.19           N  
ATOM   1430  CA  ASN A 185      27.473  31.417   7.114  1.00 51.57           C  
ATOM   1431  C   ASN A 185      28.703  32.067   6.473  1.00 53.89           C  
ATOM   1432  O   ASN A 185      29.844  31.589   6.580  1.00 53.61           O  
ATOM   1433  CB  ASN A 185      27.405  31.815   8.586  1.00 49.84           C  
ATOM   1434  CG  ASN A 185      26.476  30.939   9.390  1.00 48.43           C  
ATOM   1435  OD1 ASN A 185      26.545  29.715   9.343  1.00 47.27           O  
ATOM   1436  ND2 ASN A 185      25.613  31.567  10.156  1.00 53.40           N  
ATOM   1437  N   THR A 186      28.432  33.178   5.809  1.00 57.29           N  
ATOM   1438  CA  THR A 186      29.407  33.928   5.054  1.00 54.53           C  
ATOM   1439  C   THR A 186      29.175  35.419   5.284  1.00 51.71           C  
ATOM   1440  O   THR A 186      28.034  35.859   5.435  1.00 45.84           O  
ATOM   1441  CB  THR A 186      29.302  33.587   3.565  1.00 53.25           C  
ATOM   1442  OG1 THR A 186      27.964  33.137   3.281  1.00 54.15           O  
ATOM   1443  CG2 THR A 186      30.337  32.475   3.198  1.00 49.28           C  
ATOM   1444  N   PRO A 187      30.267  36.195   5.331  1.00 54.30           N  
ATOM   1445  CA  PRO A 187      30.189  37.590   5.755  1.00 54.71           C  
ATOM   1446  C   PRO A 187      29.609  38.500   4.718  1.00 52.26           C  
ATOM   1447  O   PRO A 187      29.833  38.278   3.544  1.00 54.68           O  
ATOM   1448  CB  PRO A 187      31.642  37.968   6.020  1.00 55.23           C  
ATOM   1449  CG  PRO A 187      32.357  36.663   6.125  1.00 58.96           C  
ATOM   1450  CD  PRO A 187      31.661  35.765   5.169  1.00 56.05           C  
ATOM   1451  N   ILE A 188      28.850  39.503   5.161  1.00 53.53           N  
ATOM   1452  CA  ILE A 188      28.333  40.524   4.266  1.00 54.92           C  
ATOM   1453  C   ILE A 188      29.391  41.594   4.043  1.00 58.97           C  
ATOM   1454  O   ILE A 188      29.664  41.967   2.913  1.00 66.29           O  
ATOM   1455  CB  ILE A 188      27.035  41.148   4.787  1.00 52.82           C  
ATOM   1456  CG1 ILE A 188      25.839  40.282   4.374  1.00 54.08           C  
ATOM   1457  CG2 ILE A 188      26.844  42.541   4.226  1.00 53.47           C  
ATOM   1458  CD1 ILE A 188      24.543  40.600   5.108  1.00 54.40           C  
ATOM   1459  N   GLY A 189      29.997  42.076   5.112  1.00 63.48           N  
ATOM   1460  CA  GLY A 189      31.029  43.096   4.988  1.00 71.60           C  
ATOM   1461  C   GLY A 189      32.363  42.625   4.424  1.00 75.60           C  
ATOM   1462  O   GLY A 189      32.636  41.409   4.359  1.00 73.04           O  
ATOM   1463  N   ASP A 190      33.182  43.605   4.009  1.00 81.81           N  
ATOM   1464  CA  ASP A 190      34.573  43.387   3.545  1.00 87.58           C  
ATOM   1465  C   ASP A 190      35.517  43.247   4.744  1.00 90.62           C  
ATOM   1466  O   ASP A 190      36.573  42.614   4.634  1.00 82.62           O  
ATOM   1467  CB  ASP A 190      35.086  44.564   2.685  1.00 93.02           C  
ATOM   1468  CG  ASP A 190      34.350  44.726   1.346  1.00 93.58           C  
ATOM   1469  OD1 ASP A 190      34.323  43.760   0.546  1.00 94.48           O  
ATOM   1470  OD2 ASP A 190      33.853  45.851   1.076  1.00 91.18           O1-
ATOM   1471  N   GLY A 191      35.119  43.855   5.874  1.00100.62           N  
ATOM   1472  CA  GLY A 191      35.930  43.941   7.099  1.00 95.90           C  
ATOM   1473  C   GLY A 191      35.899  42.665   7.918  1.00 93.08           C  
ATOM   1474  O   GLY A 191      34.847  42.306   8.471  1.00 97.36           O  
ATOM   1475  N   PRO A 192      37.076  42.021   8.066  1.00 88.17           N  
ATOM   1476  CA  PRO A 192      37.262  40.579   8.286  1.00 87.75           C  
ATOM   1477  C   PRO A 192      36.495  39.928   9.445  1.00 87.59           C  
ATOM   1478  O   PRO A 192      36.705  40.254  10.622  1.00 78.45           O  
ATOM   1479  CB  PRO A 192      38.771  40.452   8.526  1.00 87.65           C  
ATOM   1480  CG  PRO A 192      39.154  41.770   9.102  1.00 87.72           C  
ATOM   1481  CD  PRO A 192      38.323  42.760   8.336  1.00 88.82           C  
ATOM   1482  N   VAL A 193      35.605  39.012   9.072  1.00 83.73           N  
ATOM   1483  CA  VAL A 193      35.179  37.931   9.934  1.00 74.87           C  
ATOM   1484  C   VAL A 193      36.347  37.387  10.744  1.00 72.70           C  
ATOM   1485  O   VAL A 193      37.511  37.708  10.495  1.00 70.50           O  
ATOM   1486  CB  VAL A 193      34.651  36.751   9.099  1.00 75.00           C  
ATOM   1487  N   LEU A 194      36.019  36.529  11.696  1.00 70.72           N  
ATOM   1488  CA  LEU A 194      36.996  35.950  12.576  1.00 70.30           C  
ATOM   1489  C   LEU A 194      36.840  34.452  12.495  1.00 65.87           C  
ATOM   1490  O   LEU A 194      35.918  33.913  13.078  1.00 77.57           O  
ATOM   1491  CB  LEU A 194      36.728  36.471  13.988  1.00 72.12           C  
ATOM   1492  CG  LEU A 194      37.425  35.893  15.216  1.00 68.85           C  
ATOM   1493  CD1 LEU A 194      38.943  35.911  15.104  1.00 73.97           C  
ATOM   1494  CD2 LEU A 194      36.956  36.680  16.434  1.00 68.65           C  
ATOM   1495  N   LEU A 195      37.723  33.784  11.760  1.00 60.85           N  
ATOM   1496  CA  LEU A 195      37.613  32.340  11.559  1.00 58.57           C  
ATOM   1497  C   LEU A 195      38.028  31.563  12.808  1.00 58.21           C  
ATOM   1498  O   LEU A 195      39.110  31.773  13.344  1.00 68.20           O  
ATOM   1499  CB  LEU A 195      38.417  31.878  10.333  1.00 61.20           C  
ATOM   1500  CG  LEU A 195      37.826  32.202   8.948  1.00 56.25           C  
ATOM   1501  N   PRO A 196      37.156  30.668  13.287  1.00 58.80           N  
ATOM   1502  CA  PRO A 196      37.388  29.901  14.502  1.00 61.19           C  
ATOM   1503  C   PRO A 196      38.029  28.514  14.345  1.00 62.90           C  
ATOM   1504  O   PRO A 196      37.938  27.873  13.293  1.00 63.31           O  
ATOM   1505  CB  PRO A 196      35.967  29.695  15.008  1.00 64.30           C  
ATOM   1506  CG  PRO A 196      35.194  29.471  13.748  1.00 60.18           C  
ATOM   1507  CD  PRO A 196      35.766  30.500  12.814  1.00 59.44           C  
ATOM   1508  N   ASP A 197      38.657  28.055  15.421  1.00 67.75           N  
ATOM   1509  CA  ASP A 197      38.969  26.649  15.584  1.00 69.15           C  
ATOM   1510  C   ASP A 197      37.646  25.987  15.810  1.00 66.16           C  
ATOM   1511  O   ASP A 197      36.680  26.621  16.191  1.00 66.99           O  
ATOM   1512  CB  ASP A 197      39.835  26.353  16.820  1.00 72.23           C  
ATOM   1513  CG  ASP A 197      41.216  27.023  16.801  1.00 69.14           C  
ATOM   1514  OD1 ASP A 197      41.569  27.803  15.884  1.00 62.17           O  
ATOM   1515  OD2 ASP A 197      41.947  26.755  17.776  1.00 68.50           O1-
ATOM   1516  N   ASN A 198      37.621  24.688  15.617  1.00 68.82           N  
ATOM   1517  CA  ASN A 198      36.405  23.944  15.762  1.00 70.09           C  
ATOM   1518  C   ASN A 198      35.868  24.028  17.175  1.00 74.66           C  
ATOM   1519  O   ASN A 198      36.617  23.896  18.142  1.00 88.10           O  
ATOM   1520  CB  ASN A 198      36.646  22.487  15.387  1.00 70.27           C  
ATOM   1521  CG  ASN A 198      37.026  22.319  13.925  1.00 73.68           C  
ATOM   1522  OD1 ASN A 198      37.431  23.280  13.242  1.00 76.88           O  
ATOM   1523  ND2 ASN A 198      36.895  21.094  13.431  1.00 73.68           N  
ATOM   1524  N   HIS A 199      34.564  24.256  17.293  1.00 69.22           N  
ATOM   1525  CA  HIS A 199      33.905  24.137  18.568  1.00 58.66           C  
ATOM   1526  C   HIS A 199      32.473  23.759  18.329  1.00 57.99           C  
ATOM   1527  O   HIS A 199      32.122  23.335  17.244  1.00 59.44           O  
ATOM   1528  CB  HIS A 199      34.025  25.429  19.340  1.00 55.85           C  
ATOM   1529  CG  HIS A 199      33.425  26.602  18.650  1.00 49.81           C  
ATOM   1530  ND1 HIS A 199      33.861  27.045  17.429  1.00 48.70           N  
ATOM   1531  CD2 HIS A 199      32.483  27.481  19.053  1.00 49.48           C  
ATOM   1532  CE1 HIS A 199      33.189  28.124  17.084  1.00 47.69           C  
ATOM   1533  NE2 HIS A 199      32.344  28.407  18.053  1.00 48.58           N  
ATOM   1534  N   TYR A 200      31.662  23.855  19.366  1.00 59.08           N  
ATOM   1535  CA  TYR A 200      30.264  23.563  19.252  1.00 57.85           C  
ATOM   1536  C   TYR A 200      29.483  24.528  20.130  1.00 53.94           C  
ATOM   1537  O   TYR A 200      30.031  25.111  21.044  1.00 55.92           O  
ATOM   1538  CB  TYR A 200      29.992  22.072  19.570  1.00 62.05           C  
ATOM   1539  CG  TYR A 200      30.048  21.624  21.024  1.00 63.53           C  
ATOM   1540  CD1 TYR A 200      29.133  22.084  21.948  1.00 69.74           C  
ATOM   1541  CD2 TYR A 200      30.978  20.685  21.456  1.00 65.44           C  
ATOM   1542  CE1 TYR A 200      29.165  21.667  23.278  1.00 70.52           C  
ATOM   1543  CE2 TYR A 200      31.017  20.257  22.781  1.00 66.08           C  
ATOM   1544  CZ  TYR A 200      30.104  20.757  23.694  1.00 68.66           C  
ATOM   1545  OH  TYR A 200      30.089  20.360  25.021  1.00 70.62           O  
ATOM   1546  N   LEU A 201      28.218  24.748  19.785  1.00 54.85           N  
ATOM   1547  CA  LEU A 201      27.282  25.456  20.646  1.00 46.97           C  
ATOM   1548  C   LEU A 201      26.305  24.469  21.233  1.00 45.84           C  
ATOM   1549  O   LEU A 201      25.790  23.611  20.543  1.00 48.20           O  
ATOM   1550  CB  LEU A 201      26.509  26.511  19.888  1.00 43.40           C  
ATOM   1551  CG  LEU A 201      27.332  27.470  19.034  1.00 47.09           C  
ATOM   1552  CD1 LEU A 201      26.416  28.321  18.154  1.00 46.53           C  
ATOM   1553  CD2 LEU A 201      28.222  28.335  19.901  1.00 47.57           C  
ATOM   1554  N   SER A 202      26.050  24.631  22.522  1.00 51.00           N  
ATOM   1555  CA  SER A 202      25.084  23.860  23.244  1.00 47.95           C  
ATOM   1556  C   SER A 202      23.767  24.625  23.315  1.00 49.25           C  
ATOM   1557  O   SER A 202      23.708  25.694  23.920  1.00 48.34           O  
ATOM   1558  CB  SER A 202      25.608  23.622  24.628  1.00 45.98           C  
ATOM   1559  OG  SER A 202      24.634  22.992  25.413  1.00 51.15           O  
ATOM   1560  N   VAL A 203      22.714  24.036  22.731  1.00 51.30           N  
ATOM   1561  CA  VAL A 203      21.437  24.710  22.533  1.00 47.12           C  
ATOM   1562  C   VAL A 203      20.246  23.971  23.116  1.00 44.83           C  
ATOM   1563  O   VAL A 203      19.879  22.907  22.658  1.00 45.20           O  
ATOM   1564  CB  VAL A 203      21.141  24.876  21.039  1.00 46.88           C  
ATOM   1565  CG1 VAL A 203      20.008  25.856  20.844  1.00 48.27           C  
ATOM   1566  CG2 VAL A 203      22.374  25.304  20.262  1.00 44.18           C  
ATOM   1567  N   GLN A 204      19.634  24.591  24.108  1.00 43.44           N  
ATOM   1568  CA  GLN A 204      18.366  24.182  24.646  1.00 43.96           C  
ATOM   1569  C   GLN A 204      17.304  25.214  24.297  1.00 49.32           C  
ATOM   1570  O   GLN A 204      17.485  26.404  24.536  1.00 49.41           O  
ATOM   1571  CB  GLN A 204      18.450  24.158  26.142  1.00 47.35           C  
ATOM   1572  CG  GLN A 204      19.532  23.285  26.658  1.00 47.92           C  
ATOM   1573  CD  GLN A 204      19.655  23.418  28.119  1.00 50.14           C  
ATOM   1574  OE1 GLN A 204      18.886  22.820  28.866  1.00 52.31           O  
ATOM   1575  NE2 GLN A 204      20.615  24.225  28.558  1.00 57.58           N  
ATOM   1576  N   ALA A 205      16.184  24.751  23.757  1.00 50.17           N  
ATOM   1577  CA  ALA A 205      15.131  25.634  23.283  1.00 47.68           C  
ATOM   1578  C   ALA A 205      13.901  25.181  23.998  1.00 45.84           C  
ATOM   1579  O   ALA A 205      13.742  23.997  24.170  1.00 44.09           O  
ATOM   1580  CB  ALA A 205      14.956  25.486  21.778  1.00 46.78           C  
ATOM   1581  N   ALA A 206      13.060  26.113  24.451  1.00 46.24           N  
ATOM   1582  CA  ALA A 206      11.808  25.766  25.121  1.00 42.28           C  
ATOM   1583  C   ALA A 206      10.645  26.554  24.562  1.00 41.87           C  
ATOM   1584  O   ALA A 206      10.721  27.767  24.429  1.00 40.19           O  
ATOM   1585  CB  ALA A 206      11.917  25.972  26.604  1.00 43.04           C  
ATOM   1586  N   LEU A 207       9.566  25.820  24.263  1.00 45.26           N  
ATOM   1587  CA  LEU A 207       8.463  26.256  23.412  1.00 42.83           C  
ATOM   1588  C   LEU A 207       7.185  26.359  24.185  1.00 43.25           C  
ATOM   1589  O   LEU A 207       6.864  25.449  24.943  1.00 44.26           O  
ATOM   1590  CB  LEU A 207       8.202  25.221  22.331  1.00 42.39           C  
ATOM   1591  CG  LEU A 207       9.222  24.794  21.299  1.00 37.40           C  
ATOM   1592  CD1 LEU A 207       8.451  24.189  20.166  1.00 36.99           C  
ATOM   1593  CD2 LEU A 207      10.038  25.965  20.805  1.00 39.21           C  
ATOM   1594  N   SER A 208       6.438  27.435  23.933  1.00 47.49           N  
ATOM   1595  CA  SER A 208       5.263  27.817  24.752  1.00 50.04           C  
ATOM   1596  C   SER A 208       4.151  28.571  23.989  1.00 50.77           C  
ATOM   1597  O   SER A 208       4.219  28.722  22.760  1.00 50.10           O  
ATOM   1598  CB  SER A 208       5.720  28.663  25.940  1.00 53.21           C  
ATOM   1599  OG  SER A 208       6.824  29.494  25.582  1.00 63.56           O  
ATOM   1600  N   LYS A 209       3.117  29.002  24.719  1.00 49.97           N  
ATOM   1601  CA  LYS A 209       2.046  29.806  24.147  1.00 50.81           C  
ATOM   1602  C   LYS A 209       1.668  30.945  25.078  1.00 49.64           C  
ATOM   1603  O   LYS A 209       1.580  30.767  26.275  1.00 52.84           O  
ATOM   1604  CB  LYS A 209       0.803  28.954  23.909  1.00 53.59           C  
ATOM   1605  CG  LYS A 209       0.944  27.758  22.965  1.00 51.38           C  
ATOM   1606  CD  LYS A 209       1.101  28.211  21.528  1.00 48.99           C  
ATOM   1607  CE  LYS A 209       1.078  27.045  20.568  1.00 44.98           C  
ATOM   1608  NZ  LYS A 209       1.354  27.547  19.210  1.00 43.54           N  
ATOM   1609  N   ASP A 210       1.478  32.119  24.492  1.00 55.54           N  
ATOM   1610  CA  ASP A 210       0.804  33.263  25.100  1.00 58.68           C  
ATOM   1611  C   ASP A 210      -0.700  32.971  25.257  1.00 58.03           C  
ATOM   1612  O   ASP A 210      -1.416  32.957  24.282  1.00 57.07           O  
ATOM   1613  CB  ASP A 210       1.016  34.472  24.176  1.00 60.54           C  
ATOM   1614  CG  ASP A 210       0.282  35.706  24.629  1.00 68.30           C  
ATOM   1615  OD1 ASP A 210      -0.410  35.665  25.671  1.00 75.87           O  
ATOM   1616  OD2 ASP A 210       0.406  36.732  23.934  1.00 68.14           O1-
ATOM   1617  N   PRO A 211      -1.194  32.762  26.487  1.00 63.76           N  
ATOM   1618  CA  PRO A 211      -2.618  32.374  26.675  1.00 65.44           C  
ATOM   1619  C   PRO A 211      -3.668  33.405  26.182  1.00 68.63           C  
ATOM   1620  O   PRO A 211      -4.862  33.100  26.048  1.00 65.83           O  
ATOM   1621  CB  PRO A 211      -2.729  32.192  28.192  1.00 64.79           C  
ATOM   1622  CG  PRO A 211      -1.327  32.131  28.715  1.00 63.30           C  
ATOM   1623  CD  PRO A 211      -0.479  32.904  27.769  1.00 63.39           C  
ATOM   1624  N   ASN A 212      -3.186  34.606  25.893  1.00 74.92           N  
ATOM   1625  CA  ASN A 212      -3.990  35.739  25.490  1.00 75.04           C  
ATOM   1626  C   ASN A 212      -3.915  36.002  23.997  1.00 78.19           C  
ATOM   1627  O   ASN A 212      -4.578  36.901  23.491  1.00 84.83           O  
ATOM   1628  CB  ASN A 212      -3.431  36.969  26.192  1.00 81.63           C  
ATOM   1629  CG  ASN A 212      -3.047  36.690  27.638  1.00 87.73           C  
ATOM   1630  OD1 ASN A 212      -3.920  36.572  28.501  1.00 89.99           O  
ATOM   1631  ND2 ASN A 212      -1.736  36.577  27.909  1.00 83.97           N  
ATOM   1632  N   GLU A 213      -3.064  35.257  23.294  1.00 80.84           N  
ATOM   1633  CA  GLU A 213      -2.851  35.467  21.864  1.00 73.56           C  
ATOM   1634  C   GLU A 213      -3.696  34.476  21.109  1.00 72.16           C  
ATOM   1635  O   GLU A 213      -3.657  33.281  21.384  1.00 64.43           O  
ATOM   1636  CB  GLU A 213      -1.378  35.294  21.496  1.00 65.69           C  
ATOM   1637  CG  GLU A 213      -1.086  35.432  20.018  1.00 59.44           C  
ATOM   1638  CD  GLU A 213      -1.273  36.838  19.516  1.00 57.00           C  
ATOM   1639  OE1 GLU A 213      -0.638  37.737  20.055  1.00 57.11           O  
ATOM   1640  OE2 GLU A 213      -2.020  37.054  18.558  1.00 58.22           O1-
ATOM   1641  N   LYS A 214      -4.455  34.990  20.149  1.00 78.86           N  
ATOM   1642  CA  LYS A 214      -5.412  34.176  19.403  1.00 83.09           C  
ATOM   1643  C   LYS A 214      -4.839  33.693  18.077  1.00 75.44           C  
ATOM   1644  O   LYS A 214      -5.169  32.588  17.624  1.00 73.05           O  
ATOM   1645  CB  LYS A 214      -6.714  34.953  19.173  1.00 86.91           C  
ATOM   1646  CG  LYS A 214      -7.580  35.076  20.420  1.00 89.10           C  
ATOM   1647  CD  LYS A 214      -7.221  36.298  21.248  1.00 89.57           C  
ATOM   1648  CE  LYS A 214      -8.108  36.384  22.476  1.00 91.60           C  
ATOM   1649  NZ  LYS A 214      -7.822  37.591  23.297  1.00 93.39           N  
ATOM   1650  N   ARG A 215      -3.982  34.515  17.470  1.00 64.38           N  
ATOM   1651  CA  ARG A 215      -3.332  34.151  16.228  1.00 61.88           C  
ATOM   1652  C   ARG A 215      -2.371  32.994  16.437  1.00 60.40           C  
ATOM   1653  O   ARG A 215      -1.997  32.676  17.561  1.00 63.32           O  
ATOM   1654  CB  ARG A 215      -2.600  35.345  15.649  1.00 64.19           C  
ATOM   1655  CG  ARG A 215      -3.524  36.393  15.067  1.00 69.00           C  
ATOM   1656  CD  ARG A 215      -2.803  37.717  14.856  1.00 75.74           C  
ATOM   1657  NE  ARG A 215      -2.574  38.431  16.113  1.00 78.74           N  
ATOM   1658  CZ  ARG A 215      -1.795  39.501  16.259  1.00 80.32           C  
ATOM   1659  NH1 ARG A 215      -1.129  40.018  15.224  1.00 80.21           N  
ATOM   1660  NH2 ARG A 215      -1.680  40.052  17.463  1.00 84.21           N  
ATOM   1661  N   ASP A 216      -1.985  32.348  15.348  1.00 60.66           N  
ATOM   1662  CA  ASP A 216      -1.063  31.225  15.429  1.00 60.22           C  
ATOM   1663  C   ASP A 216       0.326  31.791  15.777  1.00 57.28           C  
ATOM   1664  O   ASP A 216       0.911  32.554  14.999  1.00 63.33           O  
ATOM   1665  CB  ASP A 216      -1.056  30.444  14.102  1.00 58.75           C  
ATOM   1666  CG  ASP A 216      -0.773  28.948  14.284  1.00 55.32           C  
ATOM   1667  OD1 ASP A 216      -0.778  28.429  15.423  1.00 51.82           O  
ATOM   1668  OD2 ASP A 216      -0.559  28.287  13.256  1.00 57.29           O1-
ATOM   1669  N   HIS A 217       0.829  31.438  16.955  1.00 52.64           N  
ATOM   1670  CA  HIS A 217       2.068  32.020  17.472  1.00 53.62           C  
ATOM   1671  C   HIS A 217       2.897  30.930  18.117  1.00 48.76           C  
ATOM   1672  O   HIS A 217       2.406  29.822  18.341  1.00 48.40           O  
ATOM   1673  CB  HIS A 217       1.769  33.121  18.520  1.00 55.78           C  
ATOM   1674  CG  HIS A 217       1.012  32.611  19.704  1.00 54.89           C  
ATOM   1675  ND1 HIS A 217      -0.341  32.359  19.662  1.00 54.11           N  
ATOM   1676  CD2 HIS A 217       1.428  32.224  20.930  1.00 53.10           C  
ATOM   1677  CE1 HIS A 217      -0.730  31.854  20.815  1.00 51.09           C  
ATOM   1678  NE2 HIS A 217       0.327  31.746  21.597  1.00 53.18           N  
ATOM   1679  N   MET A 218       4.148  31.250  18.418  1.00 43.72           N  
ATOM   1680  CA  MET A 218       4.986  30.364  19.180  1.00 42.86           C  
ATOM   1681  C   MET A 218       5.894  31.243  19.958  1.00 40.40           C  
ATOM   1682  O   MET A 218       6.488  32.138  19.429  1.00 41.40           O  
ATOM   1683  CB  MET A 218       5.817  29.454  18.273  1.00 49.90           C  
ATOM   1684  CG  MET A 218       6.965  28.696  18.958  1.00 50.71           C  
ATOM   1685  SD  MET A 218       8.093  27.860  17.840  1.00 46.65           S  
ATOM   1686  CE  MET A 218       9.233  29.117  17.267  1.00 45.85           C  
ATOM   1687  N   VAL A 219       6.016  30.937  21.226  1.00 44.78           N  
ATOM   1688  CA  VAL A 219       6.895  31.628  22.133  1.00 45.21           C  
ATOM   1689  C   VAL A 219       8.141  30.771  22.223  1.00 45.89           C  
ATOM   1690  O   VAL A 219       8.045  29.550  22.305  1.00 48.42           O  
ATOM   1691  CB  VAL A 219       6.224  31.728  23.513  1.00 46.53           C  
ATOM   1692  CG1 VAL A 219       7.105  32.453  24.498  1.00 50.83           C  
ATOM   1693  CG2 VAL A 219       4.896  32.446  23.412  1.00 46.65           C  
ATOM   1694  N   LEU A 220       9.305  31.396  22.205  1.00 43.54           N  
ATOM   1695  CA  LEU A 220      10.525  30.647  22.251  1.00 43.03           C  
ATOM   1696  C   LEU A 220      11.468  31.229  23.266  1.00 44.33           C  
ATOM   1697  O   LEU A 220      11.714  32.414  23.233  1.00 48.07           O  
ATOM   1698  CB  LEU A 220      11.181  30.693  20.900  1.00 44.40           C  
ATOM   1699  CG  LEU A 220      12.476  29.913  20.823  1.00 42.90           C  
ATOM   1700  CD1 LEU A 220      12.183  28.426  20.827  1.00 44.99           C  
ATOM   1701  CD2 LEU A 220      13.194  30.300  19.572  1.00 41.43           C  
ATOM   1702  N   LEU A 221      11.971  30.382  24.166  1.00 43.88           N  
ATOM   1703  CA  LEU A 221      13.104  30.682  25.014  1.00 44.36           C  
ATOM   1704  C   LEU A 221      14.279  29.822  24.565  1.00 45.47           C  
ATOM   1705  O   LEU A 221      14.193  28.611  24.557  1.00 45.23           O  
ATOM   1706  CB  LEU A 221      12.819  30.361  26.498  1.00 48.87           C  
ATOM   1707  CG  LEU A 221      11.956  31.280  27.381  1.00 50.78           C  
ATOM   1708  N   GLU A 222      15.395  30.460  24.245  1.00 51.11           N  
ATOM   1709  CA  GLU A 222      16.615  29.771  23.804  1.00 53.51           C  
ATOM   1710  C   GLU A 222      17.753  30.056  24.783  1.00 51.16           C  
ATOM   1711  O   GLU A 222      17.910  31.178  25.220  1.00 48.36           O  
ATOM   1712  CB  GLU A 222      16.999  30.248  22.388  1.00 56.54           C  
ATOM   1713  CG  GLU A 222      17.936  29.329  21.603  1.00 60.38           C  
ATOM   1714  CD  GLU A 222      17.995  29.622  20.095  1.00 65.58           C  
ATOM   1715  OE1 GLU A 222      16.932  29.880  19.474  1.00 64.47           O  
ATOM   1716  OE2 GLU A 222      19.114  29.574  19.504  1.00 78.95           O1-
ATOM   1717  N   PHE A 223      18.519  29.025  25.129  1.00 53.30           N  
ATOM   1718  CA  PHE A 223      19.699  29.146  25.955  1.00 51.48           C  
ATOM   1719  C   PHE A 223      20.862  28.565  25.184  1.00 50.56           C  
ATOM   1720  O   PHE A 223      20.830  27.404  24.813  1.00 56.17           O  
ATOM   1721  CB  PHE A 223      19.502  28.370  27.249  1.00 57.30           C  
ATOM   1722  CG  PHE A 223      18.501  28.993  28.176  1.00 64.30           C  
ATOM   1723  CD1 PHE A 223      18.882  29.991  29.052  1.00 67.81           C  
ATOM   1724  CD2 PHE A 223      17.165  28.592  28.161  1.00 72.25           C  
ATOM   1725  CE1 PHE A 223      17.964  30.573  29.893  1.00 67.15           C  
ATOM   1726  CE2 PHE A 223      16.233  29.176  28.998  1.00 68.79           C  
ATOM   1727  CZ  PHE A 223      16.641  30.167  29.860  1.00 71.17           C  
ATOM   1728  N   VAL A 224      21.885  29.363  24.913  1.00 52.94           N  
ATOM   1729  CA  VAL A 224      23.025  28.875  24.128  1.00 52.46           C  
ATOM   1730  C   VAL A 224      24.329  29.286  24.736  1.00 49.28           C  
ATOM   1731  O   VAL A 224      24.485  30.393  25.163  1.00 46.52           O  
ATOM   1732  CB  VAL A 224      23.042  29.438  22.709  1.00 53.06           C  
ATOM   1733  CG1 VAL A 224      24.061  28.704  21.849  1.00 54.15           C  
ATOM   1734  CG2 VAL A 224      21.685  29.331  22.077  1.00 54.57           C  
ATOM   1735  N   THR A 225      25.281  28.386  24.735  1.00 52.16           N  
ATOM   1736  CA  THR A 225      26.589  28.708  25.236  1.00 53.17           C  
ATOM   1737  C   THR A 225      27.615  27.897  24.464  1.00 54.58           C  
ATOM   1738  O   THR A 225      27.377  26.713  24.215  1.00 53.19           O  
ATOM   1739  CB  THR A 225      26.656  28.439  26.724  1.00 54.53           C  
ATOM   1740  OG1 THR A 225      27.948  27.934  27.058  1.00 53.32           O  
ATOM   1741  CG2 THR A 225      25.620  27.430  27.104  1.00 59.03           C  
ATOM   1742  N   ALA A 226      28.716  28.545  24.049  1.00 55.85           N  
ATOM   1743  CA  ALA A 226      29.751  27.905  23.189  1.00 56.53           C  
ATOM   1744  C   ALA A 226      30.680  27.039  23.999  1.00 56.69           C  
ATOM   1745  O   ALA A 226      30.798  27.220  25.190  1.00 60.16           O  
ATOM   1746  CB  ALA A 226      30.549  28.926  22.409  1.00 53.14           C  
ATOM   1747  N   ALA A 227      31.338  26.091  23.349  1.00 63.14           N  
ATOM   1748  CA  ALA A 227      32.051  25.042  24.084  1.00 68.58           C  
ATOM   1749  C   ALA A 227      32.857  24.113  23.170  1.00 73.19           C  
ATOM   1750  O   ALA A 227      32.624  24.060  21.968  1.00 79.15           O  
ATOM   1751  CB  ALA A 227      31.053  24.240  24.905  1.00 68.64           C  
ATOM   1752  N   GLY A 228      33.809  23.388  23.744  1.00 78.64           N  
ATOM   1753  CA  GLY A 228      34.670  22.483  22.963  1.00 87.67           C  
ATOM   1754  C   GLY A 228      36.164  22.768  23.054  1.00 90.08           C  
ATOM   1755  O   GLY A 228      36.988  21.852  22.921  1.00 99.85           O  
ATOM   1756  N   ILE A 229      36.504  24.034  23.299  1.00 90.06           N  
ATOM   1757  CA  ILE A 229      37.892  24.500  23.361  1.00 90.71           C  
ATOM   1758  C   ILE A 229      38.402  24.650  24.809  1.00 94.68           C  
ATOM   1759  O   ILE A 229      37.723  25.193  25.676  1.00 87.36           O  
ATOM   1760  CB  ILE A 229      38.040  25.829  22.588  1.00 87.63           C  
ATOM   1761  CG1 ILE A 229      37.734  25.606  21.100  1.00 85.20           C  
ATOM   1762  CG2 ILE A 229      39.439  26.397  22.745  1.00 90.11           C  
ATOM   1763  CD1 ILE A 229      37.548  26.879  20.308  1.00 83.00           C  
ATOM   1764  N   THR A 230      39.611  24.156  25.056  1.00110.59           N  
ATOM   1765  CA  THR A 230      40.236  24.223  26.376  1.00116.67           C  
ATOM   1766  C   THR A 230      40.887  25.592  26.604  1.00119.60           C  
ATOM   1767  O   THR A 230      40.776  26.178  27.682  1.00118.88           O  
ATOM   1768  CB  THR A 230      41.303  23.127  26.509  1.00117.38           C  
ATOM   1769  OG1 THR A 230      42.289  23.296  25.478  1.00119.37           O  
ATOM   1770  CG2 THR A 230      40.656  21.743  26.381  1.00117.65           C  
TER    1771      THR A 230                                                      
ATOM   1772  N   GLY B   4      -6.912  25.023  46.625  1.00 95.12           N  
ATOM   1773  CA  GLY B   4      -6.220  24.793  45.310  1.00 89.97           C  
ATOM   1774  C   GLY B   4      -6.090  25.958  44.329  1.00 82.10           C  
ATOM   1775  O   GLY B   4      -5.254  26.847  44.499  1.00 79.06           O  
ATOM   1776  N   GLU B   5      -6.916  25.940  43.287  1.00 75.33           N  
ATOM   1777  CA  GLU B   5      -6.674  26.730  42.078  1.00 75.27           C  
ATOM   1778  C   GLU B   5      -6.708  28.243  42.208  1.00 81.35           C  
ATOM   1779  O   GLU B   5      -6.031  28.945  41.446  1.00 87.46           O  
ATOM   1780  CB  GLU B   5      -7.652  26.313  40.983  1.00 73.98           C  
ATOM   1781  CG  GLU B   5      -7.292  26.859  39.612  1.00 72.17           C  
ATOM   1782  CD  GLU B   5      -7.939  26.080  38.499  1.00 69.13           C  
ATOM   1783  OE1 GLU B   5      -9.170  25.917  38.555  1.00 65.49           O  
ATOM   1784  N   GLU B   6      -7.497  28.745  43.151  1.00 87.48           N  
ATOM   1785  CA  GLU B   6      -7.575  30.188  43.386  1.00 86.30           C  
ATOM   1786  C   GLU B   6      -6.290  30.684  44.054  1.00 77.21           C  
ATOM   1787  O   GLU B   6      -6.013  31.891  44.035  1.00 77.18           O  
ATOM   1788  CB  GLU B   6      -8.781  30.569  44.250  1.00 93.22           C  
ATOM   1789  CG  GLU B   6      -9.960  29.597  44.229  1.00 98.25           C  
ATOM   1790  CD  GLU B   6     -10.001  28.680  45.448  1.00 99.32           C  
ATOM   1791  OE1 GLU B   6     -11.044  27.992  45.619  1.00 96.59           O  
ATOM   1792  OE2 GLU B   6      -9.011  28.662  46.235  1.00 86.26           O  
ATOM   1793  N   LEU B   7      -5.525  29.749  44.639  1.00 69.10           N  
ATOM   1794  CA  LEU B   7      -4.199  30.035  45.205  1.00 66.09           C  
ATOM   1795  C   LEU B   7      -3.172  30.271  44.118  1.00 63.81           C  
ATOM   1796  O   LEU B   7      -2.277  31.092  44.268  1.00 66.34           O  
ATOM   1797  CB  LEU B   7      -3.704  28.889  46.090  1.00 66.30           C  
ATOM   1798  CG  LEU B   7      -4.417  28.680  47.422  1.00 62.50           C  
ATOM   1799  CD1 LEU B   7      -5.574  27.743  47.263  1.00 65.59           C  
ATOM   1800  CD2 LEU B   7      -3.484  28.098  48.452  1.00 62.17           C  
ATOM   1801  N   PHE B   8      -3.327  29.545  43.017  1.00 66.75           N  
ATOM   1802  CA  PHE B   8      -2.422  29.626  41.882  1.00 66.32           C  
ATOM   1803  C   PHE B   8      -2.903  30.584  40.816  1.00 69.04           C  
ATOM   1804  O   PHE B   8      -2.515  30.454  39.649  1.00 66.09           O  
ATOM   1805  CB  PHE B   8      -2.224  28.234  41.275  1.00 65.75           C  
ATOM   1806  CG  PHE B   8      -1.481  27.304  42.172  1.00 59.12           C  
ATOM   1807  CD1 PHE B   8      -0.108  27.317  42.209  1.00 58.73           C  
ATOM   1808  CD2 PHE B   8      -2.158  26.457  43.006  1.00 57.45           C  
ATOM   1809  CE1 PHE B   8       0.580  26.485  43.059  1.00 60.79           C  
ATOM   1810  CE2 PHE B   8      -1.482  25.620  43.864  1.00 59.48           C  
ATOM   1811  CZ  PHE B   8      -0.107  25.634  43.892  1.00 60.49           C  
ATOM   1812  N   THR B   9      -3.726  31.555  41.210  1.00 73.50           N  
ATOM   1813  CA  THR B   9      -4.169  32.577  40.276  1.00 75.18           C  
ATOM   1814  C   THR B   9      -2.947  33.392  39.842  1.00 75.76           C  
ATOM   1815  O   THR B   9      -2.766  33.672  38.644  1.00 78.86           O  
ATOM   1816  CB  THR B   9      -5.334  33.470  40.816  1.00 77.36           C  
ATOM   1817  OG1 THR B   9      -5.308  33.572  42.252  1.00 77.39           O  
ATOM   1818  CG2 THR B   9      -6.670  32.886  40.405  1.00 80.93           C  
ATOM   1819  N   GLY B  10      -2.077  33.729  40.791  1.00 67.20           N  
ATOM   1820  CA  GLY B  10      -1.009  34.656  40.479  1.00 67.38           C  
ATOM   1821  C   GLY B  10       0.261  33.988  40.017  1.00 68.81           C  
ATOM   1822  O   GLY B  10       0.286  32.797  39.714  1.00 70.33           O  
ATOM   1823  N   VAL B  11       1.317  34.791  39.937  1.00 68.71           N  
ATOM   1824  CA  VAL B  11       2.673  34.282  40.078  1.00 66.57           C  
ATOM   1825  C   VAL B  11       2.875  33.973  41.562  1.00 64.88           C  
ATOM   1826  O   VAL B  11       2.629  34.814  42.429  1.00 60.62           O  
ATOM   1827  CB  VAL B  11       3.737  35.287  39.597  1.00 65.82           C  
ATOM   1828  CG1 VAL B  11       5.111  34.930  40.151  1.00 66.34           C  
ATOM   1829  CG2 VAL B  11       3.763  35.336  38.077  1.00 65.06           C  
ATOM   1830  N   VAL B  12       3.326  32.758  41.843  1.00 62.56           N  
ATOM   1831  CA  VAL B  12       3.485  32.303  43.199  1.00 56.30           C  
ATOM   1832  C   VAL B  12       4.974  32.179  43.487  1.00 55.70           C  
ATOM   1833  O   VAL B  12       5.740  31.808  42.613  1.00 59.05           O  
ATOM   1834  CB  VAL B  12       2.731  30.983  43.398  1.00 52.61           C  
ATOM   1835  CG1 VAL B  12       2.848  30.490  44.836  1.00 53.28           C  
ATOM   1836  CG2 VAL B  12       1.268  31.168  42.992  1.00 49.78           C  
ATOM   1837  N   PRO B  13       5.396  32.536  44.705  1.00 55.08           N  
ATOM   1838  CA  PRO B  13       6.780  32.303  45.032  1.00 55.30           C  
ATOM   1839  C   PRO B  13       7.037  30.874  45.461  1.00 55.56           C  
ATOM   1840  O   PRO B  13       6.141  30.145  45.895  1.00 57.66           O  
ATOM   1841  CB  PRO B  13       7.048  33.278  46.175  1.00 56.79           C  
ATOM   1842  CG  PRO B  13       5.719  33.635  46.743  1.00 56.28           C  
ATOM   1843  CD  PRO B  13       4.652  33.153  45.816  1.00 54.28           C  
ATOM   1844  N   ILE B  14       8.281  30.470  45.337  1.00 59.31           N  
ATOM   1845  CA  ILE B  14       8.608  29.087  45.570  1.00 63.28           C  
ATOM   1846  C   ILE B  14       9.878  28.941  46.421  1.00 65.94           C  
ATOM   1847  O   ILE B  14      10.923  29.603  46.181  1.00 59.29           O  
ATOM   1848  CB  ILE B  14       8.718  28.322  44.224  1.00 62.24           C  
ATOM   1849  CG1 ILE B  14       7.383  28.385  43.465  1.00 57.30           C  
ATOM   1850  CG2 ILE B  14       9.129  26.876  44.465  1.00 63.76           C  
ATOM   1851  CD1 ILE B  14       7.362  27.592  42.190  1.00 55.59           C  
ATOM   1852  N   LEU B  15       9.754  28.083  47.433  1.00 65.58           N  
ATOM   1853  CA  LEU B  15      10.904  27.597  48.169  1.00 68.29           C  
ATOM   1854  C   LEU B  15      11.132  26.099  47.968  1.00 61.90           C  
ATOM   1855  O   LEU B  15      10.216  25.271  48.075  1.00 59.03           O  
ATOM   1856  CB  LEU B  15      10.796  27.924  49.665  1.00 78.08           C  
ATOM   1857  CG  LEU B  15      11.800  28.976  50.184  1.00 85.51           C  
ATOM   1858  CD1 LEU B  15      11.185  30.369  50.289  1.00 87.31           C  
ATOM   1859  CD2 LEU B  15      12.392  28.564  51.529  1.00 87.83           C  
ATOM   1860  N   VAL B  16      12.383  25.782  47.668  1.00 58.68           N  
ATOM   1861  CA  VAL B  16      12.839  24.414  47.528  1.00 61.00           C  
ATOM   1862  C   VAL B  16      13.964  24.195  48.526  1.00 58.29           C  
ATOM   1863  O   VAL B  16      14.904  24.965  48.575  1.00 63.05           O  
ATOM   1864  CB  VAL B  16      13.345  24.129  46.090  1.00 57.10           C  
ATOM   1865  CG1 VAL B  16      13.596  22.650  45.885  1.00 54.42           C  
ATOM   1866  CG2 VAL B  16      12.347  24.629  45.061  1.00 58.94           C  
ATOM   1867  N   GLU B  17      13.853  23.169  49.349  1.00 62.53           N  
ATOM   1868  CA  GLU B  17      14.967  22.756  50.189  1.00 66.43           C  
ATOM   1869  C   GLU B  17      15.150  21.247  50.021  1.00 65.87           C  
ATOM   1870  O   GLU B  17      14.176  20.482  50.020  1.00 60.44           O  
ATOM   1871  CB  GLU B  17      14.714  23.112  51.657  1.00 71.87           C  
ATOM   1872  CG  GLU B  17      14.433  24.587  51.947  1.00 76.35           C  
ATOM   1873  CD  GLU B  17      15.685  25.433  52.155  1.00 86.52           C  
ATOM   1874  OE1 GLU B  17      16.814  24.877  52.080  1.00 87.20           O  
ATOM   1875  OE2 GLU B  17      15.529  26.663  52.403  1.00 89.47           O  
ATOM   1876  N   LEU B  18      16.400  20.833  49.850  1.00 64.14           N  
ATOM   1877  CA  LEU B  18      16.722  19.435  49.694  1.00 66.11           C  
ATOM   1878  C   LEU B  18      17.977  19.076  50.466  1.00 66.76           C  
ATOM   1879  O   LEU B  18      19.069  19.507  50.099  1.00 67.41           O  
ATOM   1880  CB  LEU B  18      16.937  19.115  48.210  1.00 67.58           C  
ATOM   1881  CG  LEU B  18      17.538  17.727  47.905  1.00 67.53           C  
ATOM   1882  CD1 LEU B  18      16.837  17.076  46.729  1.00 71.25           C  
ATOM   1883  CD2 LEU B  18      19.047  17.773  47.661  1.00 68.67           C  
ATOM   1884  N   ASP B  19      17.834  18.285  51.525  1.00 67.29           N  
ATOM   1885  CA  ASP B  19      18.998  17.625  52.115  1.00 67.00           C  
ATOM   1886  C   ASP B  19      19.088  16.311  51.410  1.00 64.17           C  
ATOM   1887  O   ASP B  19      18.077  15.705  51.110  1.00 59.28           O  
ATOM   1888  CB  ASP B  19      18.872  17.431  53.622  1.00 65.76           C  
ATOM   1889  CG  ASP B  19      18.884  18.744  54.371  1.00 67.12           C  
ATOM   1890  OD1 ASP B  19      19.706  19.615  54.036  1.00 68.64           O  
ATOM   1891  OD2 ASP B  19      18.059  18.926  55.284  1.00 71.35           O  
ATOM   1892  N   GLY B  20      20.303  15.884  51.115  1.00 69.24           N  
ATOM   1893  CA  GLY B  20      20.491  14.704  50.297  1.00 68.40           C  
ATOM   1894  C   GLY B  20      21.768  13.981  50.639  1.00 71.36           C  
ATOM   1895  O   GLY B  20      22.688  14.550  51.246  1.00 72.31           O  
ATOM   1896  N   ASP B  21      21.808  12.723  50.212  1.00 71.79           N  
ATOM   1897  CA  ASP B  21      22.821  11.772  50.618  1.00 72.81           C  
ATOM   1898  C   ASP B  21      22.961  10.776  49.512  1.00 70.14           C  
ATOM   1899  O   ASP B  21      22.005  10.079  49.184  1.00 76.71           O  
ATOM   1900  CB  ASP B  21      22.360  11.039  51.872  1.00 77.99           C  
ATOM   1901  CG  ASP B  21      23.410  10.128  52.427  1.00 81.15           C  
ATOM   1902  OD1 ASP B  21      23.978   9.315  51.654  1.00 86.48           O  
ATOM   1903  OD2 ASP B  21      23.656  10.234  53.650  1.00 83.78           O  
ATOM   1904  N   VAL B  22      24.146  10.696  48.939  1.00 64.17           N  
ATOM   1905  CA  VAL B  22      24.323   9.878  47.785  1.00 68.91           C  
ATOM   1906  C   VAL B  22      25.566   9.073  47.959  1.00 70.48           C  
ATOM   1907  O   VAL B  22      26.639   9.645  48.058  1.00 74.60           O  
ATOM   1908  CB  VAL B  22      24.399  10.741  46.511  1.00 75.96           C  
ATOM   1909  CG1 VAL B  22      24.963   9.944  45.328  1.00 75.14           C  
ATOM   1910  CG2 VAL B  22      23.005  11.287  46.179  1.00 76.18           C  
ATOM   1911  N   ASN B  23      25.421   7.748  47.983  1.00 71.65           N  
ATOM   1912  CA  ASN B  23      26.542   6.860  48.246  1.00 71.97           C  
ATOM   1913  C   ASN B  23      27.290   7.343  49.461  1.00 70.17           C  
ATOM   1914  O   ASN B  23      28.515   7.328  49.472  1.00 71.95           O  
ATOM   1915  CB  ASN B  23      27.502   6.811  47.047  1.00 74.96           C  
ATOM   1916  CG  ASN B  23      27.331   5.563  46.193  1.00 76.70           C  
ATOM   1917  OD1 ASN B  23      26.405   4.772  46.367  1.00 81.86           O  
ATOM   1918  ND2 ASN B  23      28.239   5.388  45.254  1.00 73.70           N  
ATOM   1919  N   GLY B  24      26.553   7.803  50.467  1.00 71.43           N  
ATOM   1920  CA  GLY B  24      27.164   8.481  51.604  1.00 78.10           C  
ATOM   1921  C   GLY B  24      27.565   9.937  51.367  1.00 80.29           C  
ATOM   1922  O   GLY B  24      27.316  10.776  52.230  1.00 86.50           O  
ATOM   1923  N   HIS B  25      28.191  10.246  50.224  1.00 82.75           N  
ATOM   1924  CA  HIS B  25      28.553  11.641  49.874  1.00 85.53           C  
ATOM   1925  C   HIS B  25      27.339  12.562  49.994  1.00 77.94           C  
ATOM   1926  O   HIS B  25      26.389  12.422  49.244  1.00 88.20           O  
ATOM   1927  CB  HIS B  25      29.130  11.748  48.455  1.00 89.95           C  
ATOM   1928  CG  HIS B  25      30.392  10.966  48.240  1.00 95.41           C  
ATOM   1929  ND1 HIS B  25      30.477   9.925  47.339  1.00 97.18           N  
ATOM   1930  CD2 HIS B  25      31.619  11.078  48.801  1.00102.46           C  
ATOM   1931  CE1 HIS B  25      31.700   9.428  47.357  1.00100.63           C  
ATOM   1932  NE2 HIS B  25      32.413  10.106  48.239  1.00104.40           N  
ATOM   1933  N   LYS B  26      27.379  13.493  50.939  1.00 70.78           N  
ATOM   1934  CA  LYS B  26      26.191  14.206  51.366  1.00 71.46           C  
ATOM   1935  C   LYS B  26      26.269  15.660  50.989  1.00 75.32           C  
ATOM   1936  O   LYS B  26      27.358  16.234  50.952  1.00 89.01           O  
ATOM   1937  CB  LYS B  26      26.044  14.103  52.878  1.00 71.56           C  
ATOM   1938  CG  LYS B  26      25.428  12.801  53.348  1.00 73.64           C  
ATOM   1939  N   PHE B  27      25.106  16.265  50.754  1.00 72.59           N  
ATOM   1940  CA  PHE B  27      25.018  17.652  50.287  1.00 63.09           C  
ATOM   1941  C   PHE B  27      23.667  18.270  50.632  1.00 59.72           C  
ATOM   1942  O   PHE B  27      22.717  17.583  51.025  1.00 56.98           O  
ATOM   1943  CB  PHE B  27      25.218  17.693  48.774  1.00 60.84           C  
ATOM   1944  CG  PHE B  27      24.239  16.839  48.028  1.00 61.48           C  
ATOM   1945  CD1 PHE B  27      24.458  15.482  47.891  1.00 60.76           C  
ATOM   1946  CD2 PHE B  27      23.074  17.377  47.516  1.00 61.04           C  
ATOM   1947  CE1 PHE B  27      23.554  14.685  47.233  1.00 57.77           C  
ATOM   1948  CE2 PHE B  27      22.157  16.584  46.862  1.00 61.93           C  
ATOM   1949  CZ  PHE B  27      22.400  15.231  46.723  1.00 60.90           C  
ATOM   1950  N   SER B  28      23.601  19.586  50.495  1.00 61.85           N  
ATOM   1951  CA  SER B  28      22.344  20.304  50.597  1.00 63.38           C  
ATOM   1952  C   SER B  28      22.240  21.412  49.544  1.00 61.42           C  
ATOM   1953  O   SER B  28      23.240  21.993  49.127  1.00 56.49           O  
ATOM   1954  CB  SER B  28      22.146  20.849  52.002  1.00 68.31           C  
ATOM   1955  OG  SER B  28      22.359  19.821  52.959  1.00 73.63           O  
ATOM   1956  N   VAL B  29      21.005  21.622  49.088  1.00 64.56           N  
ATOM   1957  CA  VAL B  29      20.658  22.570  48.024  1.00 63.66           C  
ATOM   1958  C   VAL B  29      19.450  23.399  48.498  1.00 63.97           C  
ATOM   1959  O   VAL B  29      18.475  22.876  49.079  1.00 56.59           O  
ATOM   1960  CB  VAL B  29      20.265  21.887  46.670  1.00 59.38           C  
ATOM   1961  CG1 VAL B  29      20.059  22.934  45.597  1.00 56.35           C  
ATOM   1962  CG2 VAL B  29      21.296  20.863  46.196  1.00 59.06           C  
ATOM   1963  N   SER B  30      19.527  24.695  48.228  1.00 64.06           N  
ATOM   1964  CA  SER B  30      18.447  25.612  48.511  1.00 63.56           C  
ATOM   1965  C   SER B  30      18.013  26.230  47.188  1.00 56.71           C  
ATOM   1966  O   SER B  30      18.803  26.309  46.257  1.00 54.71           O  
ATOM   1967  CB  SER B  30      18.913  26.669  49.521  1.00 72.46           C  
ATOM   1968  OG  SER B  30      18.997  26.120  50.841  1.00 74.00           O  
ATOM   1969  N   GLY B  31      16.749  26.621  47.102  1.00 51.92           N  
ATOM   1970  CA  GLY B  31      16.175  27.113  45.859  1.00 56.00           C  
ATOM   1971  C   GLY B  31      15.011  28.074  46.023  1.00 56.57           C  
ATOM   1972  O   GLY B  31      14.238  28.003  46.982  1.00 58.17           O  
ATOM   1973  N   GLU B  32      14.899  28.996  45.080  1.00 58.15           N  
ATOM   1974  CA  GLU B  32      13.841  29.986  45.115  1.00 62.22           C  
ATOM   1975  C   GLU B  32      13.513  30.409  43.703  1.00 61.92           C  
ATOM   1976  O   GLU B  32      14.344  30.321  42.801  1.00 55.76           O  
ATOM   1977  CB  GLU B  32      14.252  31.216  45.939  1.00 68.11           C  
ATOM   1978  CG  GLU B  32      14.899  32.359  45.154  1.00 67.99           C  
ATOM   1979  N   GLY B  33      12.288  30.871  43.526  1.00 60.99           N  
ATOM   1980  CA  GLY B  33      11.841  31.332  42.239  1.00 60.95           C  
ATOM   1981  C   GLY B  33      10.361  31.506  42.297  1.00 56.46           C  
ATOM   1982  O   GLY B  33       9.829  31.693  43.374  1.00 57.53           O  
ATOM   1983  N   GLU B  34       9.698  31.432  41.146  1.00 59.64           N  
ATOM   1984  CA  GLU B  34       8.254  31.676  41.086  1.00 61.09           C  
ATOM   1985  C   GLU B  34       7.600  30.816  40.061  1.00 52.77           C  
ATOM   1986  O   GLU B  34       8.183  30.552  39.048  1.00 56.04           O  
ATOM   1987  CB  GLU B  34       7.928  33.143  40.789  1.00 65.30           C  
ATOM   1988  CG  GLU B  34       9.104  33.954  40.281  1.00 70.72           C  
ATOM   1989  CD  GLU B  34       8.676  35.178  39.512  1.00 78.57           C  
ATOM   1990  OE1 GLU B  34       7.743  35.051  38.696  1.00 92.43           O  
ATOM   1991  OE2 GLU B  34       9.286  36.252  39.693  1.00 80.97           O  
ATOM   1992  N   GLY B  35       6.378  30.397  40.343  1.00 51.75           N  
ATOM   1993  CA  GLY B  35       5.602  29.615  39.418  1.00 51.96           C  
ATOM   1994  C   GLY B  35       4.367  30.356  38.965  1.00 54.57           C  
ATOM   1995  O   GLY B  35       3.780  31.109  39.715  1.00 59.70           O  
ATOM   1996  N   ASP B  36       3.974  30.137  37.725  1.00 56.80           N  
ATOM   1997  CA  ASP B  36       2.861  30.832  37.147  1.00 57.73           C  
ATOM   1998  C   ASP B  36       2.030  29.786  36.424  1.00 62.89           C  
ATOM   1999  O   ASP B  36       2.108  29.655  35.208  1.00 75.82           O  
ATOM   2000  CB  ASP B  36       3.429  31.886  36.205  1.00 62.44           C  
ATOM   2001  CG  ASP B  36       2.373  32.654  35.451  1.00 65.18           C  
ATOM   2002  OD1 ASP B  36       1.168  32.442  35.693  1.00 71.86           O  
ATOM   2003  OD2 ASP B  36       2.766  33.477  34.596  1.00 61.18           O  
ATOM   2004  N   ALA B  37       1.223  29.044  37.188  1.00 62.99           N  
ATOM   2005  CA  ALA B  37       0.448  27.891  36.684  1.00 54.49           C  
ATOM   2006  C   ALA B  37      -0.548  28.216  35.580  1.00 55.94           C  
ATOM   2007  O   ALA B  37      -1.160  27.321  34.985  1.00 58.29           O  
ATOM   2008  CB  ALA B  37      -0.275  27.213  37.832  1.00 53.27           C  
ATOM   2009  N   THR B  38      -0.708  29.496  35.293  1.00 56.44           N  
ATOM   2010  CA  THR B  38      -1.663  29.933  34.311  1.00 60.57           C  
ATOM   2011  C   THR B  38      -1.053  29.868  32.949  1.00 60.37           C  
ATOM   2012  O   THR B  38      -1.679  29.476  31.959  1.00 58.13           O  
ATOM   2013  CB  THR B  38      -2.036  31.393  34.575  1.00 67.78           C  
ATOM   2014  OG1 THR B  38      -1.927  31.658  35.982  1.00 72.61           O  
ATOM   2015  CG2 THR B  38      -3.455  31.684  34.073  1.00 70.51           C  
ATOM   2016  N   TYR B  39       0.183  30.323  32.913  1.00 63.70           N  
ATOM   2017  CA  TYR B  39       0.956  30.355  31.711  1.00 64.08           C  
ATOM   2018  C   TYR B  39       1.629  29.000  31.585  1.00 59.26           C  
ATOM   2019  O   TYR B  39       1.993  28.610  30.483  1.00 61.38           O  
ATOM   2020  CB  TYR B  39       1.962  31.508  31.805  1.00 69.02           C  
ATOM   2021  CG  TYR B  39       2.733  31.762  30.546  1.00 76.68           C  
ATOM   2022  CD1 TYR B  39       3.835  30.969  30.217  1.00 80.80           C  
ATOM   2023  CD2 TYR B  39       2.377  32.785  29.676  1.00 79.30           C  
ATOM   2024  CE1 TYR B  39       4.561  31.184  29.060  1.00 76.87           C  
ATOM   2025  CE2 TYR B  39       3.100  33.005  28.509  1.00 83.56           C  
ATOM   2026  CZ  TYR B  39       4.198  32.198  28.214  1.00 80.08           C  
ATOM   2027  OH  TYR B  39       4.941  32.390  27.078  1.00 80.89           O  
ATOM   2028  N   GLY B  40       1.764  28.294  32.716  1.00 57.05           N  
ATOM   2029  CA  GLY B  40       2.350  26.957  32.788  1.00 57.44           C  
ATOM   2030  C   GLY B  40       3.860  27.029  32.866  1.00 59.70           C  
ATOM   2031  O   GLY B  40       4.563  26.373  32.093  1.00 53.78           O  
ATOM   2032  N   LYS B  41       4.356  27.836  33.806  1.00 61.54           N  
ATOM   2033  CA  LYS B  41       5.770  28.215  33.823  1.00 56.58           C  
ATOM   2034  C   LYS B  41       6.324  28.377  35.233  1.00 50.54           C  
ATOM   2035  O   LYS B  41       5.644  28.856  36.118  1.00 52.69           O  
ATOM   2036  CB  LYS B  41       5.987  29.494  33.003  1.00 58.39           C  
ATOM   2037  CG  LYS B  41       7.338  30.156  33.248  1.00 62.06           C  
ATOM   2038  CD  LYS B  41       7.673  31.251  32.257  1.00 60.47           C  
ATOM   2039  CE  LYS B  41       6.661  32.372  32.333  1.00 64.20           C  
ATOM   2040  NZ  LYS B  41       7.108  33.585  31.602  1.00 68.06           N  
ATOM   2041  N   LEU B  42       7.563  27.921  35.409  1.00 52.91           N  
ATOM   2042  CA  LEU B  42       8.404  28.171  36.582  1.00 55.09           C  
ATOM   2043  C   LEU B  42       9.734  28.782  36.149  1.00 58.04           C  
ATOM   2044  O   LEU B  42      10.360  28.294  35.200  1.00 57.05           O  
ATOM   2045  CB  LEU B  42       8.789  26.874  37.286  1.00 55.36           C  
ATOM   2046  CG  LEU B  42       7.700  25.919  37.737  1.00 56.67           C  
ATOM   2047  CD1 LEU B  42       8.316  24.557  37.973  1.00 57.50           C  
ATOM   2048  CD2 LEU B  42       7.039  26.431  38.992  1.00 58.93           C  
ATOM   2049  N   THR B  43      10.183  29.813  36.866  1.00 58.43           N  
ATOM   2050  CA  THR B  43      11.610  30.128  36.911  1.00 55.56           C  
ATOM   2051  C   THR B  43      12.104  29.891  38.328  1.00 52.28           C  
ATOM   2052  O   THR B  43      11.435  30.213  39.304  1.00 51.73           O  
ATOM   2053  CB  THR B  43      11.905  31.555  36.500  1.00 58.54           C  
ATOM   2054  OG1 THR B  43      11.737  32.395  37.637  1.00 65.82           O  
ATOM   2055  CG2 THR B  43      10.968  32.003  35.356  1.00 63.04           C  
ATOM   2056  N   LEU B  44      13.278  29.295  38.418  1.00 56.92           N  
ATOM   2057  CA  LEU B  44      13.847  28.827  39.669  1.00 55.93           C  
ATOM   2058  C   LEU B  44      15.366  28.868  39.553  1.00 53.29           C  
ATOM   2059  O   LEU B  44      15.919  28.780  38.464  1.00 53.77           O  
ATOM   2060  CB  LEU B  44      13.401  27.389  39.930  1.00 59.79           C  
ATOM   2061  CG  LEU B  44      12.078  27.105  40.636  1.00 61.84           C  
ATOM   2062  CD1 LEU B  44      11.721  25.622  40.571  1.00 62.86           C  
ATOM   2063  CD2 LEU B  44      12.207  27.537  42.081  1.00 62.66           C  
ATOM   2064  N   LYS B  45      16.031  28.986  40.691  1.00 57.59           N  
ATOM   2065  CA  LYS B  45      17.484  28.992  40.768  1.00 55.31           C  
ATOM   2066  C   LYS B  45      17.894  28.235  42.010  1.00 54.54           C  
ATOM   2067  O   LYS B  45      17.282  28.420  43.045  1.00 59.51           O  
ATOM   2068  CB  LYS B  45      17.973  30.428  40.856  1.00 56.68           C  
ATOM   2069  CG  LYS B  45      19.473  30.609  40.940  1.00 56.97           C  
ATOM   2070  CD  LYS B  45      19.769  32.090  41.082  1.00 60.22           C  
ATOM   2071  CE  LYS B  45      21.227  32.365  41.419  1.00 63.27           C  
ATOM   2072  NZ  LYS B  45      21.584  33.784  41.139  1.00 64.03           N  
ATOM   2073  N   PHE B  46      18.936  27.409  41.908  1.00 57.43           N  
ATOM   2074  CA  PHE B  46      19.397  26.565  43.015  1.00 55.97           C  
ATOM   2075  C   PHE B  46      20.860  26.778  43.399  1.00 59.75           C  
ATOM   2076  O   PHE B  46      21.730  26.747  42.519  1.00 56.81           O  
ATOM   2077  CB  PHE B  46      19.204  25.129  42.611  1.00 53.33           C  
ATOM   2078  CG  PHE B  46      17.797  24.816  42.288  1.00 52.17           C  
ATOM   2079  CD1 PHE B  46      16.900  24.515  43.297  1.00 53.94           C  
ATOM   2080  CD2 PHE B  46      17.353  24.869  40.992  1.00 53.41           C  
ATOM   2081  CE1 PHE B  46      15.588  24.231  43.018  1.00 53.72           C  
ATOM   2082  CE2 PHE B  46      16.033  24.587  40.694  1.00 57.06           C  
ATOM   2083  CZ  PHE B  46      15.146  24.270  41.707  1.00 56.72           C  
ATOM   2084  N   ILE B  47      21.113  26.984  44.707  1.00 59.86           N  
ATOM   2085  CA  ILE B  47      22.472  27.089  45.283  1.00 58.35           C  
ATOM   2086  C   ILE B  47      22.764  25.847  46.076  1.00 56.92           C  
ATOM   2087  O   ILE B  47      21.915  25.406  46.836  1.00 59.99           O  
ATOM   2088  CB  ILE B  47      22.599  28.261  46.286  1.00 54.68           C  
ATOM   2089  N   CYS B  48      23.948  25.275  45.912  1.00 58.94           N  
ATOM   2090  CA  CYS B  48      24.379  24.200  46.810  1.00 63.66           C  
ATOM   2091  C   CYS B  48      24.933  24.854  48.065  1.00 71.66           C  
ATOM   2092  O   CYS B  48      26.030  25.406  48.049  1.00 97.46           O  
ATOM   2093  CB  CYS B  48      25.438  23.313  46.159  1.00 63.01           C  
ATOM   2094  SG  CYS B  48      26.058  21.999  47.225  1.00 66.05           S  
ATOM   2095  N   THR B  49      24.175  24.802  49.152  1.00 67.96           N  
ATOM   2096  CA  THR B  49      24.541  25.467  50.389  1.00 64.70           C  
ATOM   2097  C   THR B  49      25.677  24.769  51.169  1.00 68.43           C  
ATOM   2098  O   THR B  49      26.012  25.158  52.291  1.00 67.40           O  
ATOM   2099  CB  THR B  49      23.293  25.576  51.277  1.00 67.93           C  
ATOM   2100  OG1 THR B  49      22.667  24.288  51.417  1.00 69.35           O  
ATOM   2101  CG2 THR B  49      22.311  26.521  50.651  1.00 66.21           C  
ATOM   2102  N   THR B  50      26.268  23.741  50.561  1.00 77.17           N  
ATOM   2103  CA  THR B  50      27.272  22.892  51.201  1.00 77.42           C  
ATOM   2104  C   THR B  50      28.458  22.659  50.260  1.00 81.65           C  
ATOM   2105  O   THR B  50      28.975  21.545  50.156  1.00 93.03           O  
ATOM   2106  CB  THR B  50      26.661  21.521  51.623  1.00 76.03           C  
ATOM   2107  OG1 THR B  50      26.325  20.736  50.469  1.00 77.01           O  
ATOM   2108  CG2 THR B  50      25.411  21.715  52.486  1.00 74.10           C  
ATOM   2109  N   GLY B  51      28.882  23.712  49.569  1.00 80.98           N  
ATOM   2110  CA  GLY B  51      30.008  23.627  48.641  1.00 77.77           C  
ATOM   2111  C   GLY B  51      29.506  23.354  47.249  1.00 74.30           C  
ATOM   2112  O   GLY B  51      28.490  23.909  46.844  1.00 80.99           O  
ATOM   2113  N   LYS B  52      30.228  22.522  46.509  1.00 70.29           N  
ATOM   2114  CA  LYS B  52      29.734  22.003  45.235  1.00 69.99           C  
ATOM   2115  C   LYS B  52      28.730  20.879  45.428  1.00 65.66           C  
ATOM   2116  O   LYS B  52      28.589  20.342  46.516  1.00 64.37           O  
ATOM   2117  CB  LYS B  52      30.866  21.438  44.395  1.00 74.98           C  
ATOM   2118  CG  LYS B  52      31.502  20.206  45.006  1.00 79.84           C  
ATOM   2119  CD  LYS B  52      32.394  19.524  43.996  1.00 79.47           C  
ATOM   2120  CE  LYS B  52      33.785  19.254  44.529  1.00 74.80           C  
ATOM   2121  NZ  LYS B  52      34.019  17.838  44.200  1.00 74.44           N  
ATOM   2122  N   LEU B  53      28.067  20.521  44.336  1.00 61.22           N  
ATOM   2123  CA  LEU B  53      27.177  19.395  44.311  1.00 56.13           C  
ATOM   2124  C   LEU B  53      28.026  18.175  43.911  1.00 56.55           C  
ATOM   2125  O   LEU B  53      28.854  18.276  43.013  1.00 56.72           O  
ATOM   2126  CB  LEU B  53      26.054  19.654  43.310  1.00 52.64           C  
ATOM   2127  CG  LEU B  53      24.708  18.952  43.517  1.00 48.38           C  
ATOM   2128  CD1 LEU B  53      23.914  19.545  44.671  1.00 48.87           C  
ATOM   2129  CD2 LEU B  53      23.907  19.023  42.234  1.00 46.79           C  
ATOM   2130  N   PRO B  54      27.866  17.046  44.616  1.00 56.32           N  
ATOM   2131  CA  PRO B  54      28.499  15.785  44.260  1.00 59.65           C  
ATOM   2132  C   PRO B  54      27.848  15.009  43.138  1.00 66.85           C  
ATOM   2133  O   PRO B  54      28.416  14.001  42.687  1.00 75.91           O  
ATOM   2134  CB  PRO B  54      28.369  14.957  45.533  1.00 62.43           C  
ATOM   2135  CG  PRO B  54      27.284  15.586  46.310  1.00 60.80           C  
ATOM   2136  CD  PRO B  54      27.411  17.033  46.015  1.00 60.88           C  
ATOM   2137  N   VAL B  55      26.661  15.440  42.715  1.00 67.45           N  
ATOM   2138  CA  VAL B  55      25.953  14.823  41.575  1.00 65.02           C  
ATOM   2139  C   VAL B  55      25.820  15.845  40.435  1.00 60.73           C  
ATOM   2140  O   VAL B  55      26.006  17.034  40.669  1.00 66.11           O  
ATOM   2141  CB  VAL B  55      24.568  14.278  42.000  1.00 65.38           C  
ATOM   2142  CG1 VAL B  55      24.733  13.005  42.815  1.00 62.36           C  
ATOM   2143  CG2 VAL B  55      23.782  15.312  42.793  1.00 63.95           C  
ATOM   2144  N   PRO B  56      25.562  15.394  39.197  1.00 55.00           N  
ATOM   2145  CA  PRO B  56      25.242  16.376  38.182  1.00 56.59           C  
ATOM   2146  C   PRO B  56      23.861  17.066  38.390  1.00 59.17           C  
ATOM   2147  O   PRO B  56      22.868  16.401  38.687  1.00 60.99           O  
ATOM   2148  CB  PRO B  56      25.299  15.571  36.880  1.00 55.32           C  
ATOM   2149  CG  PRO B  56      26.136  14.388  37.180  1.00 54.35           C  
ATOM   2150  CD  PRO B  56      25.861  14.079  38.609  1.00 55.01           C  
ATOM   2151  N   TRP B  57      23.831  18.393  38.221  1.00 56.32           N  
ATOM   2152  CA  TRP B  57      22.653  19.198  38.472  1.00 54.71           C  
ATOM   2153  C   TRP B  57      21.427  18.720  37.718  1.00 53.72           C  
ATOM   2154  O   TRP B  57      20.324  18.839  38.221  1.00 61.44           O  
ATOM   2155  CB  TRP B  57      22.914  20.652  38.077  1.00 58.30           C  
ATOM   2156  CG  TRP B  57      23.572  21.507  39.104  1.00 54.90           C  
ATOM   2157  CD1 TRP B  57      24.856  21.928  39.102  1.00 53.48           C  
ATOM   2158  CD2 TRP B  57      22.955  22.097  40.251  1.00 56.40           C  
ATOM   2159  NE1 TRP B  57      25.095  22.731  40.185  1.00 52.89           N  
ATOM   2160  CE2 TRP B  57      23.944  22.849  40.913  1.00 55.07           C  
ATOM   2161  CE3 TRP B  57      21.661  22.068  40.782  1.00 55.13           C  
ATOM   2162  CZ2 TRP B  57      23.692  23.535  42.095  1.00 54.37           C  
ATOM   2163  CZ3 TRP B  57      21.401  22.779  41.937  1.00 55.36           C  
ATOM   2164  CH2 TRP B  57      22.413  23.494  42.588  1.00 56.41           C  
ATOM   2165  N   PRO B  58      21.598  18.214  36.492  1.00 53.16           N  
ATOM   2166  CA  PRO B  58      20.432  17.671  35.801  1.00 53.03           C  
ATOM   2167  C   PRO B  58      19.800  16.452  36.483  1.00 52.09           C  
ATOM   2168  O   PRO B  58      18.612  16.261  36.374  1.00 55.69           O  
ATOM   2169  CB  PRO B  58      20.999  17.278  34.428  1.00 54.94           C  
ATOM   2170  CG  PRO B  58      22.179  18.156  34.233  1.00 51.01           C  
ATOM   2171  CD  PRO B  58      22.775  18.247  35.601  1.00 55.26           C  
ATOM   2172  N   THR B  59      20.588  15.659  37.208  1.00 53.06           N  
ATOM   2173  CA  THR B  59      20.084  14.448  37.852  1.00 49.25           C  
ATOM   2174  C   THR B  59      19.068  14.780  38.940  1.00 50.44           C  
ATOM   2175  O   THR B  59      18.338  13.898  39.384  1.00 56.07           O  
ATOM   2176  CB  THR B  59      21.207  13.578  38.475  1.00 49.09           C  
ATOM   2177  OG1 THR B  59      21.876  14.277  39.526  1.00 50.77           O  
ATOM   2178  CG2 THR B  59      22.239  13.165  37.464  1.00 49.54           C  
ATOM   2179  N   LEU B  60      19.017  16.045  39.358  1.00 48.52           N  
ATOM   2180  CA  LEU B  60      18.115  16.487  40.410  1.00 46.30           C  
ATOM   2181  C   LEU B  60      16.933  17.260  39.904  1.00 43.78           C  
ATOM   2182  O   LEU B  60      16.074  17.643  40.664  1.00 45.13           O  
ATOM   2183  CB  LEU B  60      18.872  17.373  41.388  1.00 47.29           C  
ATOM   2184  CG  LEU B  60      20.030  16.692  42.105  1.00 47.18           C  
ATOM   2185  CD1 LEU B  60      20.587  17.619  43.160  1.00 48.08           C  
ATOM   2186  CD2 LEU B  60      19.607  15.371  42.742  1.00 46.85           C  
ATOM   2187  N   VAL B  61      16.877  17.482  38.611  1.00 48.80           N  
ATOM   2188  CA  VAL B  61      15.885  18.376  38.082  1.00 49.78           C  
ATOM   2189  C   VAL B  61      14.494  17.872  38.421  1.00 50.35           C  
ATOM   2190  O   VAL B  61      13.665  18.618  38.914  1.00 56.57           O  
ATOM   2191  CB  VAL B  61      16.049  18.571  36.570  1.00 52.17           C  
ATOM   2192  CG1 VAL B  61      14.911  19.419  36.028  1.00 52.27           C  
ATOM   2193  CG2 VAL B  61      17.401  19.209  36.250  1.00 49.50           C  
ATOM   2194  N   THR B  62      14.251  16.598  38.190  1.00 48.74           N  
ATOM   2195  CA  THR B  62      12.940  16.026  38.434  1.00 47.91           C  
ATOM   2196  C   THR B  62      12.556  16.148  39.875  1.00 48.67           C  
ATOM   2197  O   THR B  62      11.391  16.235  40.200  1.00 50.34           O  
ATOM   2198  CB  THR B  62      12.948  14.548  38.077  1.00 50.47           C  
ATOM   2199  OG1 THR B  62      14.242  14.012  38.397  1.00 55.87           O  
ATOM   2200  CG2 THR B  62      12.672  14.359  36.597  1.00 48.57           C  
ATOM   2201  N   THR B  63      13.559  16.156  40.736  1.00 53.17           N  
ATOM   2202  CA  THR B  63      13.376  16.167  42.181  1.00 52.46           C  
ATOM   2203  C   THR B  63      13.111  17.573  42.719  1.00 51.57           C  
ATOM   2204  O   THR B  63      12.287  17.739  43.592  1.00 55.58           O  
ATOM   2205  CB  THR B  63      14.621  15.571  42.895  1.00 56.09           C  
ATOM   2206  OG1 THR B  63      14.802  14.184  42.540  1.00 53.91           O  
ATOM   2207  CG2 THR B  63      14.505  15.691  44.407  1.00 55.05           C  
ATOM   2208  N   PHE B  64      13.815  18.583  42.231  1.00 51.52           N  
ATOM   2209  CA  PHE B  64      13.553  19.947  42.670  1.00 47.27           C  
ATOM   2210  C   PHE B  64      12.218  20.459  42.116  1.00 49.07           C  
ATOM   2211  O   PHE B  64      11.506  21.219  42.780  1.00 48.81           O  
ATOM   2212  CB  PHE B  64      14.605  20.921  42.141  1.00 49.58           C  
ATOM   2213  CG  PHE B  64      16.002  20.675  42.597  1.00 47.01           C  
ATOM   2214  CD1 PHE B  64      16.279  20.204  43.844  1.00 48.49           C  
ATOM   2215  CD2 PHE B  64      17.050  21.005  41.754  1.00 47.55           C  
ATOM   2216  CE1 PHE B  64      17.585  19.999  44.226  1.00 52.47           C  
ATOM   2217  CE2 PHE B  64      18.359  20.811  42.122  1.00 46.40           C  
ATOM   2218  CZ  PHE B  64      18.632  20.313  43.364  1.00 50.30           C  
HETATM 2219  N1  CRO B  66      11.920  20.094  40.853  1.00 53.56           N  
HETATM 2220  CA1 CRO B  66      10.734  20.519  40.158  1.00 52.87           C  
HETATM 2221  CB1 CRO B  66      11.221  21.383  39.005  1.00 54.36           C  
HETATM 2222  OG1 CRO B  66      10.128  21.931  38.273  1.00 56.81           O  
HETATM 2223  C1  CRO B  66      10.041  19.289  39.714  1.00 55.05           C  
HETATM 2224  N2  CRO B  66      10.159  18.783  38.430  1.00 55.88           N  
HETATM 2225  N3  CRO B  66       9.236  18.518  40.512  1.00 53.30           N  
HETATM 2226  C2  CRO B  66       8.878  17.532  39.742  1.00 57.96           C  
HETATM 2227  O2  CRO B  66       8.114  16.566  40.074  1.00 62.24           O  
HETATM 2228  CA2 CRO B  66       9.419  17.684  38.407  1.00 55.63           C  
HETATM 2229  CA3 CRO B  66       8.867  18.616  41.918  1.00 55.85           C  
HETATM 2230  C3  CRO B  66       7.605  19.345  42.296  1.00 59.88           C  
HETATM 2231  O3  CRO B  66       6.751  18.800  43.016  1.00 62.63           O  
HETATM 2232  CB2 CRO B  66       9.203  16.717  37.319  1.00 53.78           C  
HETATM 2233  CG2 CRO B  66       9.723  16.738  35.954  1.00 51.07           C  
HETATM 2234  CD1 CRO B  66      10.686  17.648  35.535  1.00 49.06           C  
HETATM 2235  CD2 CRO B  66       9.254  15.727  35.093  1.00 48.45           C  
HETATM 2236  CE1 CRO B  66      11.121  17.592  34.202  1.00 49.00           C  
HETATM 2237  CE2 CRO B  66       9.699  15.676  33.770  1.00 49.67           C  
HETATM 2238  CZ  CRO B  66      10.634  16.617  33.336  1.00 48.79           C  
HETATM 2239  OH  CRO B  66      11.073  16.600  32.064  1.00 52.78           O  
ATOM   2240  N   VAL B  68       7.507  20.683  41.816  1.00 63.32           N  
ATOM   2241  CA  VAL B  68       6.342  21.583  42.111  1.00 58.51           C  
ATOM   2242  C   VAL B  68       5.289  21.517  40.984  1.00 53.38           C  
ATOM   2243  O   VAL B  68       4.938  22.497  40.353  1.00 50.39           O  
ATOM   2244  CB  VAL B  68       6.859  22.998  42.441  1.00 60.89           C  
ATOM   2245  CG1 VAL B  68       7.699  22.957  43.714  1.00 63.46           C  
ATOM   2246  CG2 VAL B  68       7.698  23.576  41.314  1.00 62.30           C  
ATOM   2247  N   GLN B  69       4.762  20.313  40.778  1.00 54.71           N  
ATOM   2248  CA  GLN B  69       3.930  20.006  39.628  1.00 50.61           C  
ATOM   2249  C   GLN B  69       2.563  20.659  39.720  1.00 47.92           C  
ATOM   2250  O   GLN B  69       1.819  20.696  38.753  1.00 46.56           O  
ATOM   2251  CB  GLN B  69       3.822  18.487  39.443  1.00 53.71           C  
ATOM   2252  CG  GLN B  69       5.155  17.811  39.135  1.00 56.07           C  
ATOM   2253  CD  GLN B  69       5.039  16.327  38.809  1.00 55.77           C  
ATOM   2254  OE1 GLN B  69       4.727  15.512  39.667  1.00 56.35           O  
ATOM   2255  NE2 GLN B  69       5.330  15.973  37.569  1.00 57.52           N  
ATOM   2256  N   CYS B  70       2.238  21.202  40.873  1.00 48.85           N  
ATOM   2257  CA  CYS B  70       1.126  22.118  40.958  1.00 53.68           C  
ATOM   2258  C   CYS B  70       1.218  23.284  39.990  1.00 55.36           C  
ATOM   2259  O   CYS B  70       0.173  23.859  39.686  1.00 55.92           O  
ATOM   2260  CB  CYS B  70       0.989  22.648  42.364  1.00 57.18           C  
ATOM   2261  SG  CYS B  70       2.548  23.067  43.133  1.00 57.40           S  
ATOM   2262  N   PHE B  71       2.422  23.596  39.473  1.00 52.17           N  
ATOM   2263  CA  PHE B  71       2.609  24.686  38.483  1.00 49.19           C  
ATOM   2264  C   PHE B  71       2.412  24.384  36.999  1.00 49.14           C  
ATOM   2265  O   PHE B  71       2.580  25.261  36.148  1.00 44.97           O  
ATOM   2266  CB  PHE B  71       3.935  25.389  38.724  1.00 49.40           C  
ATOM   2267  CG  PHE B  71       3.912  26.178  39.971  1.00 47.31           C  
ATOM   2268  CD1 PHE B  71       3.244  27.384  40.007  1.00 46.51           C  
ATOM   2269  CD2 PHE B  71       4.434  25.663  41.138  1.00 48.90           C  
ATOM   2270  CE1 PHE B  71       3.136  28.093  41.179  1.00 47.31           C  
ATOM   2271  CE2 PHE B  71       4.335  26.363  42.320  1.00 50.96           C  
ATOM   2272  CZ  PHE B  71       3.688  27.592  42.337  1.00 50.94           C  
ATOM   2273  N   SER B  72       1.991  23.161  36.707  1.00 53.20           N  
ATOM   2274  CA  SER B  72       1.585  22.779  35.362  1.00 53.23           C  
ATOM   2275  C   SER B  72       0.354  23.549  34.982  1.00 52.75           C  
ATOM   2276  O   SER B  72      -0.531  23.702  35.798  1.00 56.21           O  
ATOM   2277  CB  SER B  72       1.243  21.286  35.303  1.00 52.09           C  
ATOM   2278  OG  SER B  72       1.723  20.626  36.449  1.00 55.91           O  
ATOM   2279  N   ARG B  73       0.284  23.998  33.737  1.00 54.34           N  
ATOM   2280  CA  ARG B  73      -0.927  24.566  33.215  1.00 53.68           C  
ATOM   2281  C   ARG B  73      -1.879  23.463  32.800  1.00 57.06           C  
ATOM   2282  O   ARG B  73      -1.601  22.740  31.852  1.00 53.35           O  
ATOM   2283  CB  ARG B  73      -0.623  25.425  32.009  1.00 54.27           C  
ATOM   2284  CG  ARG B  73      -1.865  26.061  31.435  1.00 56.38           C  
ATOM   2285  CD  ARG B  73      -1.580  26.857  30.181  1.00 60.42           C  
ATOM   2286  NE  ARG B  73      -2.052  26.184  28.974  1.00 62.26           N  
ATOM   2287  CZ  ARG B  73      -3.295  26.238  28.503  1.00 66.14           C  
ATOM   2288  NH1 ARG B  73      -4.246  26.925  29.132  1.00 66.88           N  
ATOM   2289  NH2 ARG B  73      -3.594  25.579  27.387  1.00 78.47           N  
ATOM   2290  N   TYR B  74      -3.011  23.352  33.498  1.00 62.44           N  
ATOM   2291  CA  TYR B  74      -4.107  22.462  33.079  1.00 59.91           C  
ATOM   2292  C   TYR B  74      -5.131  23.237  32.217  1.00 66.72           C  
ATOM   2293  O   TYR B  74      -5.720  24.221  32.681  1.00 76.83           O  
ATOM   2294  CB  TYR B  74      -4.789  21.835  34.295  1.00 56.05           C  
ATOM   2295  CG  TYR B  74      -4.145  20.555  34.762  1.00 54.82           C  
ATOM   2296  CD1 TYR B  74      -3.038  20.568  35.594  1.00 53.96           C  
ATOM   2297  CD2 TYR B  74      -4.641  19.313  34.348  1.00 54.76           C  
ATOM   2298  CE1 TYR B  74      -2.440  19.383  35.996  1.00 54.83           C  
ATOM   2299  CE2 TYR B  74      -4.058  18.123  34.749  1.00 49.57           C  
ATOM   2300  CZ  TYR B  74      -2.961  18.159  35.568  1.00 50.23           C  
ATOM   2301  OH  TYR B  74      -2.406  16.977  35.997  1.00 47.83           O  
ATOM   2302  N   PRO B  75      -5.310  22.833  30.942  1.00 63.53           N  
ATOM   2303  CA  PRO B  75      -6.349  23.367  30.083  1.00 63.81           C  
ATOM   2304  C   PRO B  75      -7.765  23.326  30.675  1.00 66.14           C  
ATOM   2305  O   PRO B  75      -8.169  22.322  31.255  1.00 68.57           O  
ATOM   2306  CB  PRO B  75      -6.279  22.452  28.871  1.00 66.42           C  
ATOM   2307  CG  PRO B  75      -4.862  22.044  28.783  1.00 67.01           C  
ATOM   2308  CD  PRO B  75      -4.303  22.089  30.166  1.00 65.45           C  
ATOM   2309  N   ASP B  76      -8.520  24.401  30.487  1.00 71.19           N  
ATOM   2310  CA  ASP B  76      -9.867  24.527  31.047  1.00 77.67           C  
ATOM   2311  C   ASP B  76     -10.670  23.241  31.155  1.00 76.61           C  
ATOM   2312  O   ASP B  76     -11.315  23.014  32.182  1.00 79.94           O  
ATOM   2313  CB  ASP B  76     -10.683  25.516  30.225  1.00 83.50           C  
ATOM   2314  CG  ASP B  76     -10.433  26.941  30.618  1.00 88.07           C  
ATOM   2315  OD1 ASP B  76      -9.419  27.222  31.296  1.00 97.89           O  
ATOM   2316  OD2 ASP B  76     -11.266  27.780  30.241  1.00 92.91           O  
ATOM   2317  N   HIS B  77     -10.653  22.424  30.097  1.00 77.73           N  
ATOM   2318  CA  HIS B  77     -11.452  21.191  30.077  1.00 72.61           C  
ATOM   2319  C   HIS B  77     -10.865  20.131  30.985  1.00 66.29           C  
ATOM   2320  O   HIS B  77     -11.570  19.216  31.420  1.00 71.71           O  
ATOM   2321  CB  HIS B  77     -11.703  20.658  28.650  1.00 72.02           C  
ATOM   2322  CG  HIS B  77     -10.483  20.187  27.929  1.00 75.81           C  
ATOM   2323  ND1 HIS B  77      -9.735  21.011  27.118  1.00 85.07           N  
ATOM   2324  CD2 HIS B  77      -9.908  18.964  27.853  1.00 80.42           C  
ATOM   2325  CE1 HIS B  77      -8.730  20.323  26.600  1.00 85.00           C  
ATOM   2326  NE2 HIS B  77      -8.808  19.079  27.037  1.00 79.94           N  
ATOM   2327  N   MET B  78      -9.594  20.287  31.321  1.00 59.40           N  
ATOM   2328  CA  MET B  78      -8.909  19.305  32.129  1.00 57.06           C  
ATOM   2329  C   MET B  78      -8.698  19.781  33.530  1.00 57.97           C  
ATOM   2330  O   MET B  78      -7.924  19.189  34.274  1.00 55.48           O  
ATOM   2331  CB  MET B  78      -7.554  18.989  31.519  1.00 57.85           C  
ATOM   2332  CG  MET B  78      -7.611  18.589  30.057  1.00 54.84           C  
ATOM   2333  SD  MET B  78      -6.036  18.061  29.423  1.00 52.58           S  
ATOM   2334  CE  MET B  78      -5.465  16.977  30.712  1.00 48.74           C  
ATOM   2335  N   LYS B  79      -9.390  20.841  33.918  1.00 63.76           N  
ATOM   2336  CA  LYS B  79      -9.113  21.427  35.216  1.00 62.51           C  
ATOM   2337  C   LYS B  79      -9.573  20.549  36.370  1.00 61.73           C  
ATOM   2338  O   LYS B  79      -9.094  20.739  37.478  1.00 59.70           O  
ATOM   2339  CB  LYS B  79      -9.634  22.868  35.305  1.00 66.98           C  
ATOM   2340  CG  LYS B  79      -8.630  23.882  34.733  1.00 69.74           C  
ATOM   2341  CD  LYS B  79      -9.102  25.336  34.750  1.00 69.56           C  
ATOM   2342  CE  LYS B  79      -8.201  26.215  33.888  1.00 65.57           C  
ATOM   2343  N   ARG B  80     -10.433  19.554  36.093  1.00 63.18           N  
ATOM   2344  CA  ARG B  80     -10.885  18.561  37.101  1.00 59.19           C  
ATOM   2345  C   ARG B  80     -10.020  17.322  37.233  1.00 63.41           C  
ATOM   2346  O   ARG B  80     -10.405  16.397  37.942  1.00 73.53           O  
ATOM   2347  CB  ARG B  80     -12.300  18.078  36.800  1.00 55.93           C  
ATOM   2348  CG  ARG B  80     -12.399  17.087  35.667  1.00 54.29           C  
ATOM   2349  N   HIS B  81      -8.873  17.287  36.552  1.00 67.74           N  
ATOM   2350  CA  HIS B  81      -7.957  16.132  36.577  1.00 62.55           C  
ATOM   2351  C   HIS B  81      -6.654  16.479  37.294  1.00 63.53           C  
ATOM   2352  O   HIS B  81      -5.691  15.722  37.271  1.00 64.47           O  
ATOM   2353  CB  HIS B  81      -7.675  15.693  35.151  1.00 59.60           C  
ATOM   2354  CG  HIS B  81      -8.883  15.179  34.444  1.00 58.35           C  
ATOM   2355  ND1 HIS B  81      -9.584  14.079  34.887  1.00 57.36           N  
ATOM   2356  CD2 HIS B  81      -9.523  15.609  33.335  1.00 59.94           C  
ATOM   2357  CE1 HIS B  81     -10.608  13.855  34.085  1.00 58.45           C  
ATOM   2358  NE2 HIS B  81     -10.596  14.770  33.136  1.00 62.03           N  
ATOM   2359  N   ASP B  82      -6.674  17.626  37.966  1.00 60.40           N  
ATOM   2360  CA  ASP B  82      -5.506  18.267  38.525  1.00 53.92           C  
ATOM   2361  C   ASP B  82      -5.325  17.928  39.992  1.00 53.53           C  
ATOM   2362  O   ASP B  82      -5.666  18.722  40.864  1.00 61.96           O  
ATOM   2363  CB  ASP B  82      -5.698  19.763  38.366  1.00 52.91           C  
ATOM   2364  CG  ASP B  82      -4.478  20.525  38.655  1.00 51.27           C  
ATOM   2365  OD1 ASP B  82      -3.665  20.039  39.441  1.00 54.91           O  
ATOM   2366  OD2 ASP B  82      -4.328  21.605  38.079  1.00 54.25           O  
ATOM   2367  N   PHE B  83      -4.772  16.761  40.270  1.00 46.42           N  
ATOM   2368  CA  PHE B  83      -4.572  16.355  41.630  1.00 45.52           C  
ATOM   2369  C   PHE B  83      -3.667  17.320  42.395  1.00 45.90           C  
ATOM   2370  O   PHE B  83      -3.676  17.374  43.622  1.00 50.39           O  
ATOM   2371  CB  PHE B  83      -3.996  14.929  41.661  1.00 48.03           C  
ATOM   2372  CG  PHE B  83      -3.295  14.570  42.951  1.00 49.54           C  
ATOM   2373  CD1 PHE B  83      -1.936  14.857  43.125  1.00 50.04           C  
ATOM   2374  CD2 PHE B  83      -3.980  13.944  43.984  1.00 47.82           C  
ATOM   2375  CE1 PHE B  83      -1.282  14.541  44.306  1.00 52.79           C  
ATOM   2376  CE2 PHE B  83      -3.329  13.612  45.164  1.00 49.83           C  
ATOM   2377  CZ  PHE B  83      -1.977  13.909  45.330  1.00 52.51           C  
ATOM   2378  N   PHE B  84      -2.861  18.086  41.694  1.00 48.21           N  
ATOM   2379  CA  PHE B  84      -1.813  18.832  42.389  1.00 51.76           C  
ATOM   2380  C   PHE B  84      -2.304  20.081  43.115  1.00 48.99           C  
ATOM   2381  O   PHE B  84      -1.871  20.368  44.231  1.00 48.72           O  
ATOM   2382  CB  PHE B  84      -0.681  19.190  41.418  1.00 51.88           C  
ATOM   2383  CG  PHE B  84      -0.035  17.997  40.782  1.00 47.70           C  
ATOM   2384  CD1 PHE B  84       0.865  17.232  41.486  1.00 48.35           C  
ATOM   2385  CD2 PHE B  84      -0.333  17.643  39.482  1.00 48.63           C  
ATOM   2386  CE1 PHE B  84       1.468  16.129  40.904  1.00 49.63           C  
ATOM   2387  CE2 PHE B  84       0.263  16.550  38.891  1.00 48.61           C  
ATOM   2388  CZ  PHE B  84       1.165  15.785  39.605  1.00 48.18           C  
ATOM   2389  N   LYS B  85      -3.162  20.838  42.444  1.00 53.18           N  
ATOM   2390  CA  LYS B  85      -3.736  22.041  43.000  1.00 53.04           C  
ATOM   2391  C   LYS B  85      -4.784  21.547  43.951  1.00 57.50           C  
ATOM   2392  O   LYS B  85      -4.698  21.804  45.146  1.00 58.60           O  
ATOM   2393  CB  LYS B  85      -4.316  22.937  41.907  1.00 51.98           C  
ATOM   2394  CG  LYS B  85      -3.229  23.552  41.018  1.00 55.72           C  
ATOM   2395  CD  LYS B  85      -3.777  24.290  39.787  1.00 58.70           C  
ATOM   2396  CE  LYS B  85      -2.712  24.772  38.777  1.00 59.71           C  
ATOM   2397  NZ  LYS B  85      -1.656  23.786  38.375  1.00 56.31           N  
ATOM   2398  N   SER B  86      -5.727  20.761  43.435  1.00 65.14           N  
ATOM   2399  CA  SER B  86      -6.789  20.159  44.261  1.00 65.18           C  
ATOM   2400  C   SER B  86      -6.404  19.990  45.736  1.00 62.93           C  
ATOM   2401  O   SER B  86      -7.150  20.405  46.613  1.00 70.04           O  
ATOM   2402  CB  SER B  86      -7.229  18.807  43.684  1.00 61.45           C  
ATOM   2403  OG  SER B  86      -6.382  17.770  44.120  1.00 60.07           O  
ATOM   2404  N   ALA B  87      -5.231  19.409  45.987  1.00 62.11           N  
ATOM   2405  CA  ALA B  87      -4.776  19.038  47.330  1.00 60.91           C  
ATOM   2406  C   ALA B  87      -4.023  20.134  48.074  1.00 62.81           C  
ATOM   2407  O   ALA B  87      -3.229  19.833  48.968  1.00 62.98           O  
ATOM   2408  CB  ALA B  87      -3.893  17.790  47.239  1.00 62.77           C  
ATOM   2409  N   MET B  88      -4.279  21.392  47.714  1.00 67.67           N  
ATOM   2410  CA  MET B  88      -3.579  22.555  48.282  1.00 66.11           C  
ATOM   2411  C   MET B  88      -4.565  23.437  49.035  1.00 66.45           C  
ATOM   2412  O   MET B  88      -5.736  23.505  48.643  1.00 66.57           O  
ATOM   2413  CB  MET B  88      -2.925  23.393  47.165  1.00 67.31           C  
ATOM   2414  CG  MET B  88      -1.649  22.810  46.579  1.00 67.85           C  
ATOM   2415  SD  MET B  88      -0.296  22.845  47.758  1.00 67.58           S  
ATOM   2416  CE  MET B  88       0.864  21.698  47.049  1.00 73.97           C  
ATOM   2417  N   PRO B  89      -4.087  24.176  50.066  1.00 63.44           N  
ATOM   2418  CA  PRO B  89      -2.707  24.406  50.500  1.00 63.84           C  
ATOM   2419  C   PRO B  89      -2.206  23.415  51.523  1.00 59.29           C  
ATOM   2420  O   PRO B  89      -1.026  23.379  51.826  1.00 59.45           O  
ATOM   2421  CB  PRO B  89      -2.775  25.788  51.113  1.00 63.54           C  
ATOM   2422  CG  PRO B  89      -4.112  25.824  51.712  1.00 64.86           C  
ATOM   2423  CD  PRO B  89      -5.013  24.910  50.927  1.00 62.77           C  
ATOM   2424  N   GLU B  90      -3.099  22.601  52.038  1.00 62.67           N  
ATOM   2425  CA  GLU B  90      -2.699  21.432  52.795  1.00 70.20           C  
ATOM   2426  C   GLU B  90      -1.447  20.753  52.169  1.00 60.08           C  
ATOM   2427  O   GLU B  90      -0.466  20.537  52.857  1.00 60.75           O  
ATOM   2428  CB  GLU B  90      -3.900  20.461  52.894  1.00 78.93           C  
ATOM   2429  CG  GLU B  90      -5.528  21.228  52.597  1.00 87.10           C  
ATOM   2430  N   GLY B  91      -1.511  20.423  50.880  1.00 55.82           N  
ATOM   2431  CA  GLY B  91      -0.401  19.846  50.135  1.00 56.03           C  
ATOM   2432  C   GLY B  91      -0.435  18.338  49.987  1.00 59.01           C  
ATOM   2433  O   GLY B  91      -1.430  17.691  50.300  1.00 57.60           O  
ATOM   2434  N   TYR B  92       0.675  17.788  49.496  1.00 64.77           N  
ATOM   2435  CA  TYR B  92       0.836  16.339  49.263  1.00 67.22           C  
ATOM   2436  C   TYR B  92       2.297  15.884  49.486  1.00 68.72           C  
ATOM   2437  O   TYR B  92       3.200  16.689  49.695  1.00 68.71           O  
ATOM   2438  CB  TYR B  92       0.367  15.942  47.845  1.00 68.57           C  
ATOM   2439  CG  TYR B  92       1.018  16.754  46.739  1.00 67.00           C  
ATOM   2440  CD1 TYR B  92       2.295  16.457  46.299  1.00 63.15           C  
ATOM   2441  CD2 TYR B  92       0.363  17.829  46.160  1.00 67.14           C  
ATOM   2442  CE1 TYR B  92       2.902  17.196  45.318  1.00 62.54           C  
ATOM   2443  CE2 TYR B  92       0.964  18.576  45.170  1.00 68.88           C  
ATOM   2444  CZ  TYR B  92       2.239  18.255  44.757  1.00 66.81           C  
ATOM   2445  OH  TYR B  92       2.856  18.992  43.771  1.00 69.68           O  
ATOM   2446  N   VAL B  93       2.502  14.579  49.447  1.00 70.80           N  
ATOM   2447  CA  VAL B  93       3.820  13.970  49.558  1.00 72.58           C  
ATOM   2448  C   VAL B  93       4.170  13.376  48.183  1.00 72.52           C  
ATOM   2449  O   VAL B  93       3.320  12.784  47.527  1.00 73.22           O  
ATOM   2450  CB  VAL B  93       3.805  12.864  50.655  1.00 74.63           C  
ATOM   2451  CG1 VAL B  93       4.973  11.897  50.528  1.00 70.03           C  
ATOM   2452  CG2 VAL B  93       3.782  13.485  52.045  1.00 77.36           C  
ATOM   2453  N   GLN B  94       5.414  13.543  47.749  1.00 68.44           N  
ATOM   2454  CA  GLN B  94       5.871  12.990  46.488  1.00 61.86           C  
ATOM   2455  C   GLN B  94       7.039  12.102  46.817  1.00 60.10           C  
ATOM   2456  O   GLN B  94       8.045  12.568  47.333  1.00 62.44           O  
ATOM   2457  CB  GLN B  94       6.297  14.122  45.558  1.00 65.78           C  
ATOM   2458  CG  GLN B  94       6.370  13.766  44.079  1.00 64.21           C  
ATOM   2459  CD  GLN B  94       6.479  14.991  43.176  1.00 59.53           C  
ATOM   2460  OE1 GLN B  94       5.506  15.731  42.923  1.00 51.64           O  
ATOM   2461  NE2 GLN B  94       7.678  15.202  42.676  1.00 60.33           N  
ATOM   2462  N   GLU B  95       6.886  10.809  46.576  1.00 60.55           N  
ATOM   2463  CA  GLU B  95       7.964   9.868  46.773  1.00 57.03           C  
ATOM   2464  C   GLU B  95       8.266   9.376  45.430  1.00 55.47           C  
ATOM   2465  O   GLU B  95       7.360   9.193  44.658  1.00 56.64           O  
ATOM   2466  CB  GLU B  95       7.520   8.671  47.568  1.00 64.26           C  
ATOM   2467  CG  GLU B  95       7.045   9.003  48.960  1.00 74.41           C  
ATOM   2468  CD  GLU B  95       5.927   8.100  49.407  1.00 80.16           C  
ATOM   2469  OE1 GLU B  95       4.996   7.853  48.599  1.00 80.26           O  
ATOM   2470  OE2 GLU B  95       5.985   7.655  50.572  1.00 92.49           O  
ATOM   2471  N   ARG B  96       9.536   9.137  45.152  1.00 63.47           N  
ATOM   2472  CA  ARG B  96       9.956   8.577  43.870  1.00 64.55           C  
ATOM   2473  C   ARG B  96      11.026   7.531  44.056  1.00 59.61           C  
ATOM   2474  O   ARG B  96      11.617   7.437  45.113  1.00 65.28           O  
ATOM   2475  CB  ARG B  96      10.518   9.669  42.951  1.00 67.17           C  
ATOM   2476  CG  ARG B  96       9.476  10.406  42.116  1.00 68.50           C  
ATOM   2477  CD  ARG B  96      10.089  11.005  40.850  1.00 63.80           C  
ATOM   2478  NE  ARG B  96       9.212  11.927  40.118  1.00 57.50           N  
ATOM   2479  CZ  ARG B  96       9.299  13.252  40.148  1.00 54.67           C  
ATOM   2480  NH1 ARG B  96      10.202  13.858  40.902  1.00 55.30           N  
ATOM   2481  NH2 ARG B  96       8.460  13.983  39.430  1.00 53.68           N  
ATOM   2482  N   THR B  97      11.242   6.739  43.013  1.00 62.66           N  
ATOM   2483  CA  THR B  97      12.453   5.942  42.841  1.00 61.31           C  
ATOM   2484  C   THR B  97      12.975   6.175  41.429  1.00 59.87           C  
ATOM   2485  O   THR B  97      12.321   5.827  40.434  1.00 59.37           O  
ATOM   2486  CB  THR B  97      12.203   4.441  43.024  1.00 64.86           C  
ATOM   2487  OG1 THR B  97      11.491   4.207  44.237  1.00 65.14           O  
ATOM   2488  CG2 THR B  97      13.510   3.718  43.114  1.00 69.53           C  
ATOM   2489  N   ILE B  98      14.144   6.790  41.335  1.00 57.59           N  
ATOM   2490  CA  ILE B  98      14.724   7.104  40.043  1.00 56.58           C  
ATOM   2491  C   ILE B  98      15.774   6.026  39.781  1.00 57.80           C  
ATOM   2492  O   ILE B  98      16.629   5.805  40.612  1.00 65.20           O  
ATOM   2493  CB  ILE B  98      15.335   8.525  40.044  1.00 55.00           C  
ATOM   2494  CG1 ILE B  98      14.307   9.584  40.461  1.00 51.38           C  
ATOM   2495  CG2 ILE B  98      15.847   8.887  38.672  1.00 57.91           C  
ATOM   2496  N   PHE B  99      15.688   5.319  38.661  1.00 62.60           N  
ATOM   2497  CA  PHE B  99      16.649   4.252  38.375  1.00 59.92           C  
ATOM   2498  C   PHE B  99      17.519   4.656  37.263  1.00 57.88           C  
ATOM   2499  O   PHE B  99      17.062   4.752  36.111  1.00 53.77           O  
ATOM   2500  CB  PHE B  99      15.985   2.969  37.947  1.00 57.50           C  
ATOM   2501  CG  PHE B  99      15.240   2.332  39.022  1.00 60.95           C  
ATOM   2502  CD1 PHE B  99      15.904   1.588  39.962  1.00 66.13           C  
ATOM   2503  CD2 PHE B  99      13.875   2.516  39.131  1.00 65.62           C  
ATOM   2504  CE1 PHE B  99      15.211   0.999  40.990  1.00 71.06           C  
ATOM   2505  CE2 PHE B  99      13.165   1.933  40.154  1.00 67.91           C  
ATOM   2506  CZ  PHE B  99      13.832   1.165  41.081  1.00 72.62           C  
ATOM   2507  N   PHE B 100      18.783   4.848  37.613  1.00 57.80           N  
ATOM   2508  CA  PHE B 100      19.773   5.131  36.626  1.00 58.23           C  
ATOM   2509  C   PHE B 100      20.197   3.783  36.116  1.00 57.39           C  
ATOM   2510  O   PHE B 100      20.464   2.880  36.892  1.00 61.69           O  
ATOM   2511  CB  PHE B 100      20.905   5.970  37.209  1.00 60.58           C  
ATOM   2512  CG  PHE B 100      20.470   7.374  37.600  1.00 60.00           C  
ATOM   2513  CD1 PHE B 100      19.890   7.618  38.855  1.00 55.50           C  
ATOM   2514  CD2 PHE B 100      20.609   8.440  36.704  1.00 54.46           C  
ATOM   2515  CE1 PHE B 100      19.472   8.885  39.216  1.00 50.64           C  
ATOM   2516  CE2 PHE B 100      20.197   9.703  37.067  1.00 53.85           C  
ATOM   2517  CZ  PHE B 100      19.626   9.928  38.325  1.00 52.31           C  
ATOM   2518  N   LYS B 101      20.142   3.656  34.797  1.00 59.33           N  
ATOM   2519  CA  LYS B 101      20.387   2.425  34.110  1.00 59.75           C  
ATOM   2520  C   LYS B 101      21.859   2.098  34.176  1.00 67.42           C  
ATOM   2521  O   LYS B 101      22.719   2.928  33.834  1.00 64.52           O  
ATOM   2522  CB  LYS B 101      19.948   2.513  32.654  1.00 59.08           C  
ATOM   2523  CG  LYS B 101      19.273   1.247  32.184  1.00 63.94           C  
ATOM   2524  CD  LYS B 101      19.231   1.129  30.673  1.00 70.44           C  
ATOM   2525  CE  LYS B 101      20.597   0.762  30.104  1.00 75.18           C  
ATOM   2526  NZ  LYS B 101      20.521  -0.204  28.969  1.00 74.79           N  
ATOM   2527  N   ASP B 102      22.138   0.872  34.608  1.00 71.53           N  
ATOM   2528  CA  ASP B 102      23.490   0.421  34.811  1.00 71.67           C  
ATOM   2529  C   ASP B 102      24.191   1.449  35.652  1.00 71.48           C  
ATOM   2530  O   ASP B 102      25.204   2.005  35.224  1.00 79.66           O  
ATOM   2531  CB  ASP B 102      24.212   0.255  33.471  1.00 72.60           C  
ATOM   2532  CG  ASP B 102      23.703  -0.917  32.687  1.00 74.30           C  
ATOM   2533  OD1 ASP B 102      23.612  -2.005  33.284  1.00 85.59           O  
ATOM   2534  OD2 ASP B 102      23.417  -0.771  31.483  1.00 76.77           O  
ATOM   2535  N   ASP B 103      23.618   1.737  36.822  1.00 65.08           N  
ATOM   2536  CA  ASP B 103      24.228   2.647  37.803  1.00 61.92           C  
ATOM   2537  C   ASP B 103      23.251   2.648  38.946  1.00 57.80           C  
ATOM   2538  O   ASP B 103      22.291   1.887  38.906  1.00 64.28           O  
ATOM   2539  CB  ASP B 103      24.424   4.055  37.217  1.00 67.39           C  
ATOM   2540  CG  ASP B 103      25.685   4.743  37.711  1.00 66.73           C  
ATOM   2541  OD1 ASP B 103      25.862   4.822  38.937  1.00 72.61           O  
ATOM   2542  OD2 ASP B 103      26.465   5.250  36.873  1.00 67.66           O  
ATOM   2543  N   GLY B 104      23.470   3.478  39.956  1.00 52.13           N  
ATOM   2544  CA  GLY B 104      22.622   3.453  41.144  1.00 55.70           C  
ATOM   2545  C   GLY B 104      21.273   4.139  41.039  1.00 56.78           C  
ATOM   2546  O   GLY B 104      20.819   4.466  39.958  1.00 59.91           O  
ATOM   2547  N   ASN B 105      20.638   4.373  42.183  1.00 62.44           N  
ATOM   2548  CA  ASN B 105      19.290   4.938  42.212  1.00 68.42           C  
ATOM   2549  C   ASN B 105      19.077   6.011  43.275  1.00 67.14           C  
ATOM   2550  O   ASN B 105      19.620   5.917  44.369  1.00 68.98           O  
ATOM   2551  CB  ASN B 105      18.273   3.833  42.451  1.00 70.88           C  
ATOM   2552  CG  ASN B 105      18.411   3.216  43.819  1.00 79.42           C  
ATOM   2553  OD1 ASN B 105      18.063   3.823  44.828  1.00 81.15           O  
ATOM   2554  ND2 ASN B 105      18.931   2.000  43.861  1.00 92.74           N  
ATOM   2555  N   TYR B 106      18.278   7.021  42.946  1.00 64.18           N  
ATOM   2556  CA  TYR B 106      17.784   7.936  43.944  1.00 66.13           C  
ATOM   2557  C   TYR B 106      16.455   7.449  44.480  1.00 68.17           C  
ATOM   2558  O   TYR B 106      15.602   6.993  43.731  1.00 75.46           O  
ATOM   2559  CB  TYR B 106      17.561   9.322  43.366  1.00 67.45           C  
ATOM   2560  CG  TYR B 106      18.774  10.043  42.849  1.00 63.44           C  
ATOM   2561  CD1 TYR B 106      20.050   9.754  43.295  1.00 59.09           C  
ATOM   2562  CD2 TYR B 106      18.619  11.075  41.942  1.00 66.10           C  
ATOM   2563  CE1 TYR B 106      21.139  10.449  42.809  1.00 60.22           C  
ATOM   2564  CE2 TYR B 106      19.701  11.774  41.455  1.00 63.54           C  
ATOM   2565  CZ  TYR B 106      20.958  11.466  41.888  1.00 58.96           C  
ATOM   2566  OH  TYR B 106      22.000  12.192  41.368  1.00 55.83           O  
ATOM   2567  N   LYS B 107      16.292   7.549  45.788  1.00 72.84           N  
ATOM   2568  CA  LYS B 107      15.010   7.368  46.428  1.00 73.52           C  
ATOM   2569  C   LYS B 107      14.693   8.664  47.158  1.00 67.85           C  
ATOM   2570  O   LYS B 107      15.512   9.170  47.906  1.00 63.67           O  
ATOM   2571  CB  LYS B 107      15.055   6.180  47.382  1.00 79.13           C  
ATOM   2572  CG  LYS B 107      14.749   4.862  46.682  1.00 89.01           C  
ATOM   2573  CD  LYS B 107      14.670   3.672  47.642  1.00 95.11           C  
ATOM   2574  CE  LYS B 107      13.987   2.449  47.016  1.00 94.61           C  
ATOM   2575  NZ  LYS B 107      14.871   1.556  46.207  1.00 94.83           N  
ATOM   2576  N   THR B 108      13.512   9.214  46.910  1.00 66.50           N  
ATOM   2577  CA  THR B 108      13.163  10.527  47.424  1.00 60.61           C  
ATOM   2578  C   THR B 108      11.785  10.546  47.984  1.00 59.76           C  
ATOM   2579  O   THR B 108      10.869   9.942  47.442  1.00 59.36           O  
ATOM   2580  CB  THR B 108      13.180  11.611  46.335  1.00 59.96           C  
ATOM   2581  OG1 THR B 108      12.028  11.485  45.491  1.00 60.60           O  
ATOM   2582  CG2 THR B 108      14.435  11.514  45.516  1.00 61.55           C  
ATOM   2583  N   ARG B 109      11.658  11.253  49.088  1.00 61.85           N  
ATOM   2584  CA  ARG B 109      10.377  11.696  49.556  1.00 67.41           C  
ATOM   2585  C   ARG B 109      10.511  13.188  49.761  1.00 65.07           C  
ATOM   2586  O   ARG B 109      11.546  13.659  50.239  1.00 63.63           O  
ATOM   2587  CB  ARG B 109       9.983  10.990  50.859  1.00 71.62           C  
ATOM   2588  CG  ARG B 109       8.609  11.381  51.433  1.00 76.33           C  
ATOM   2589  CD  ARG B 109       8.371  10.801  52.838  1.00 76.32           C  
ATOM   2590  NE  ARG B 109       7.338  11.502  53.613  1.00 70.96           N  
ATOM   2591  CZ  ARG B 109       7.513  12.657  54.252  1.00 72.65           C  
ATOM   2592  NH1 ARG B 109       8.686  13.292  54.217  1.00 78.90           N  
ATOM   2593  NH2 ARG B 109       6.503  13.196  54.922  1.00 70.90           N  
ATOM   2594  N   ALA B 110       9.464  13.908  49.371  1.00 62.43           N  
ATOM   2595  CA  ALA B 110       9.373  15.335  49.558  1.00 62.99           C  
ATOM   2596  C   ALA B 110       7.958  15.726  49.985  1.00 67.82           C  
ATOM   2597  O   ALA B 110       6.995  14.997  49.721  1.00 72.89           O  
ATOM   2598  CB  ALA B 110       9.734  16.035  48.262  1.00 62.95           C  
ATOM   2599  N   GLU B 111       7.830  16.881  50.632  1.00 64.35           N  
ATOM   2600  CA  GLU B 111       6.534  17.361  51.054  1.00 65.22           C  
ATOM   2601  C   GLU B 111       6.310  18.698  50.418  1.00 63.20           C  
ATOM   2602  O   GLU B 111       7.114  19.603  50.592  1.00 65.81           O  
ATOM   2603  CB  GLU B 111       6.458  17.476  52.579  1.00 77.38           C  
ATOM   2604  CG  GLU B 111       5.803  16.279  53.282  1.00 81.26           C  
ATOM   2605  CD  GLU B 111       5.679  16.465  54.792  1.00 82.23           C  
ATOM   2606  OE1 GLU B 111       4.567  16.786  55.259  1.00 86.33           O  
ATOM   2607  OE2 GLU B 111       6.689  16.293  55.514  1.00 85.11           O  
ATOM   2608  N   VAL B 112       5.220  18.808  49.670  1.00 63.26           N  
ATOM   2609  CA  VAL B 112       4.894  20.019  48.959  1.00 65.34           C  
ATOM   2610  C   VAL B 112       3.577  20.526  49.463  1.00 64.10           C  
ATOM   2611  O   VAL B 112       2.585  19.814  49.453  1.00 63.63           O  
ATOM   2612  CB  VAL B 112       4.768  19.796  47.439  1.00 70.07           C  
ATOM   2613  CG1 VAL B 112       4.420  21.102  46.722  1.00 67.68           C  
ATOM   2614  CG2 VAL B 112       6.058  19.219  46.885  1.00 69.85           C  
ATOM   2615  N   LYS B 113       3.589  21.783  49.867  1.00 68.00           N  
ATOM   2616  CA  LYS B 113       2.452  22.419  50.472  1.00 69.08           C  
ATOM   2617  C   LYS B 113       2.773  23.884  50.605  1.00 65.67           C  
ATOM   2618  O   LYS B 113       3.947  24.272  50.570  1.00 59.91           O  
ATOM   2619  CB  LYS B 113       2.225  21.860  51.866  1.00 75.68           C  
ATOM   2620  CG  LYS B 113       3.440  22.006  52.771  1.00 83.45           C  
ATOM   2621  CD  LYS B 113       3.204  21.372  54.131  1.00 90.29           C  
ATOM   2622  CE  LYS B 113       4.495  20.855  54.737  1.00 95.45           C  
ATOM   2623  NZ  LYS B 113       5.591  21.860  54.692  1.00102.47           N  
ATOM   2624  N   PHE B 114       1.717  24.666  50.796  1.00 65.14           N  
ATOM   2625  CA  PHE B 114       1.800  26.094  51.054  1.00 66.52           C  
ATOM   2626  C   PHE B 114       2.153  26.393  52.513  1.00 72.97           C  
ATOM   2627  O   PHE B 114       1.547  25.849  53.436  1.00 73.99           O  
ATOM   2628  CB  PHE B 114       0.465  26.770  50.731  1.00 66.46           C  
ATOM   2629  CG  PHE B 114       0.396  27.381  49.351  1.00 66.01           C  
ATOM   2630  CD1 PHE B 114       1.117  28.526  49.042  1.00 64.84           C  
ATOM   2631  CD2 PHE B 114      -0.418  26.828  48.370  1.00 63.33           C  
ATOM   2632  CE1 PHE B 114       1.033  29.096  47.779  1.00 65.27           C  
ATOM   2633  CE2 PHE B 114      -0.492  27.396  47.107  1.00 62.35           C  
ATOM   2634  CZ  PHE B 114       0.231  28.528  46.813  1.00 59.56           C  
ATOM   2635  N   GLU B 115       3.146  27.267  52.690  1.00 77.75           N  
ATOM   2636  CA  GLU B 115       3.519  27.833  53.978  1.00 73.68           C  
ATOM   2637  C   GLU B 115       3.256  29.343  53.907  1.00 73.09           C  
ATOM   2638  O   GLU B 115       4.159  30.161  53.725  1.00 69.77           O  
ATOM   2639  CB  GLU B 115       4.978  27.535  54.290  1.00 71.42           C  
ATOM   2640  CG  GLU B 115       5.281  26.054  54.482  1.00 71.05           C  
ATOM   2641  CD  GLU B 115       6.733  25.812  54.865  1.00 72.67           C  
ATOM   2642  OE1 GLU B 115       7.530  26.775  54.842  1.00 77.25           O  
ATOM   2643  OE2 GLU B 115       7.110  24.669  55.185  1.00 74.81           O  
ATOM   2644  N   GLY B 116       1.977  29.668  54.024  1.00 74.72           N  
ATOM   2645  CA  GLY B 116       1.489  31.015  53.989  1.00 75.02           C  
ATOM   2646  C   GLY B 116       1.300  31.464  52.565  1.00 77.80           C  
ATOM   2647  O   GLY B 116       0.204  31.418  52.005  1.00 94.16           O  
ATOM   2648  N   ASP B 117       2.406  31.873  51.985  1.00 74.52           N  
ATOM   2649  CA  ASP B 117       2.430  32.662  50.778  1.00 74.27           C  
ATOM   2650  C   ASP B 117       3.181  31.881  49.694  1.00 73.27           C  
ATOM   2651  O   ASP B 117       2.773  31.811  48.521  1.00 70.86           O  
ATOM   2652  CB  ASP B 117       3.195  33.946  51.126  1.00 78.83           C  
ATOM   2653  CG  ASP B 117       2.766  35.133  50.318  1.00 85.59           C  
ATOM   2654  OD1 ASP B 117       1.548  35.319  50.159  1.00 98.47           O  
ATOM   2655  OD2 ASP B 117       3.647  35.904  49.869  1.00 92.62           O  
ATOM   2656  N   THR B 118       4.288  31.292  50.131  1.00 69.42           N  
ATOM   2657  CA  THR B 118       5.251  30.652  49.286  1.00 65.67           C  
ATOM   2658  C   THR B 118       4.922  29.189  49.187  1.00 63.99           C  
ATOM   2659  O   THR B 118       4.714  28.529  50.201  1.00 58.33           O  
ATOM   2660  CB  THR B 118       6.647  30.812  49.902  1.00 67.65           C  
ATOM   2661  OG1 THR B 118       6.972  32.207  49.927  1.00 63.80           O  
ATOM   2662  CG2 THR B 118       7.718  30.004  49.128  1.00 66.60           C  
ATOM   2663  N   LEU B 119       4.856  28.698  47.956  1.00 62.50           N  
ATOM   2664  CA  LEU B 119       4.693  27.293  47.732  1.00 62.32           C  
ATOM   2665  C   LEU B 119       6.045  26.661  47.996  1.00 61.02           C  
ATOM   2666  O   LEU B 119       7.044  27.047  47.405  1.00 62.45           O  
ATOM   2667  CB  LEU B 119       4.240  27.041  46.307  1.00 63.35           C  
ATOM   2668  CG  LEU B 119       3.939  25.584  45.942  1.00 61.30           C  
ATOM   2669  CD1 LEU B 119       5.204  24.738  45.830  1.00 58.85           C  
ATOM   2670  CD2 LEU B 119       2.945  24.969  46.913  1.00 58.88           C  
ATOM   2671  N   VAL B 120       6.062  25.683  48.882  1.00 61.15           N  
ATOM   2672  CA  VAL B 120       7.297  25.161  49.406  1.00 63.24           C  
ATOM   2673  C   VAL B 120       7.446  23.693  49.140  1.00 65.20           C  
ATOM   2674  O   VAL B 120       6.505  22.926  49.367  1.00 64.93           O  
ATOM   2675  CB  VAL B 120       7.329  25.285  50.924  1.00 67.03           C  
ATOM   2676  CG1 VAL B 120       8.749  25.071  51.438  1.00 65.84           C  
ATOM   2677  CG2 VAL B 120       6.784  26.637  51.335  1.00 72.04           C  
ATOM   2678  N   ASN B 121       8.658  23.313  48.732  1.00 61.45           N  
ATOM   2679  CA  ASN B 121       9.001  21.937  48.442  1.00 58.43           C  
ATOM   2680  C   ASN B 121      10.239  21.558  49.240  1.00 57.74           C  
ATOM   2681  O   ASN B 121      11.294  22.119  49.021  1.00 56.72           O  
ATOM   2682  CB  ASN B 121       9.223  21.807  46.931  1.00 60.68           C  
ATOM   2683  CG  ASN B 121       9.650  20.414  46.492  1.00 58.09           C  
ATOM   2684  OD1 ASN B 121       9.264  19.411  47.069  1.00 63.02           O  
ATOM   2685  ND2 ASN B 121      10.433  20.357  45.440  1.00 56.16           N  
ATOM   2686  N   ARG B 122      10.088  20.635  50.192  1.00 59.68           N  
ATOM   2687  CA  ARG B 122      11.198  20.161  51.017  1.00 62.46           C  
ATOM   2688  C   ARG B 122      11.392  18.672  50.784  1.00 60.04           C  
ATOM   2689  O   ARG B 122      10.407  17.949  50.769  1.00 57.36           O  
ATOM   2690  CB  ARG B 122      10.911  20.409  52.499  1.00 68.98           C  
ATOM   2691  CG  ARG B 122      10.542  21.847  52.862  1.00 71.12           C  
ATOM   2692  CD  ARG B 122      10.479  22.028  54.380  1.00 73.77           C  
ATOM   2693  NE  ARG B 122       9.874  23.301  54.782  1.00 75.39           N  
ATOM   2694  CZ  ARG B 122      10.513  24.473  54.844  1.00 77.45           C  
ATOM   2695  NH1 ARG B 122      11.805  24.587  54.529  1.00 78.43           N  
ATOM   2696  NH2 ARG B 122       9.848  25.554  55.224  1.00 77.67           N  
ATOM   2697  N   ILE B 123      12.652  18.230  50.630  1.00 61.02           N  
ATOM   2698  CA  ILE B 123      13.001  16.906  50.034  1.00 61.78           C  
ATOM   2699  C   ILE B 123      14.112  16.156  50.768  1.00 60.57           C  
ATOM   2700  O   ILE B 123      15.095  16.766  51.158  1.00 59.89           O  
ATOM   2701  CB  ILE B 123      13.537  17.030  48.571  1.00 59.14           C  
ATOM   2702  CG1 ILE B 123      12.661  17.943  47.704  1.00 58.07           C  
ATOM   2703  CG2 ILE B 123      13.631  15.659  47.911  1.00 56.80           C  
ATOM   2704  CD1 ILE B 123      13.434  18.755  46.703  1.00 55.44           C  
ATOM   2705  N   GLU B 124      13.956  14.836  50.905  1.00 63.89           N  
ATOM   2706  CA  GLU B 124      15.018  13.934  51.381  1.00 71.91           C  
ATOM   2707  C   GLU B 124      15.468  13.002  50.241  1.00 70.95           C  
ATOM   2708  O   GLU B 124      14.631  12.336  49.643  1.00 71.27           O  
ATOM   2709  CB  GLU B 124      14.523  13.065  52.548  1.00 77.89           C  
ATOM   2710  CG  GLU B 124      14.406  13.751  53.902  1.00 84.99           C  
ATOM   2711  CD  GLU B 124      15.744  14.192  54.501  1.00 97.26           C  
ATOM   2712  OE1 GLU B 124      16.766  13.472  54.382  1.00100.62           O  
ATOM   2713  OE2 GLU B 124      15.775  15.281  55.120  1.00116.94           O  
ATOM   2714  N   LEU B 125      16.772  12.945  49.956  1.00 66.28           N  
ATOM   2715  CA  LEU B 125      17.295  12.108  48.881  1.00 67.73           C  
ATOM   2716  C   LEU B 125      18.374  11.122  49.365  1.00 71.60           C  
ATOM   2717  O   LEU B 125      19.428  11.517  49.881  1.00 71.07           O  
ATOM   2718  CB  LEU B 125      17.844  12.972  47.737  1.00 69.14           C  
ATOM   2719  CG  LEU B 125      18.340  12.227  46.474  1.00 72.12           C  
ATOM   2720  CD1 LEU B 125      17.951  12.948  45.192  1.00 73.74           C  
ATOM   2721  CD2 LEU B 125      19.845  11.952  46.479  1.00 72.48           C  
ATOM   2722  N   LYS B 126      18.089   9.834  49.186  1.00 70.04           N  
ATOM   2723  CA  LYS B 126      19.036   8.773  49.451  1.00 67.23           C  
ATOM   2724  C   LYS B 126      19.347   8.149  48.128  1.00 65.14           C  
ATOM   2725  O   LYS B 126      18.465   7.627  47.462  1.00 66.38           O  
ATOM   2726  CB  LYS B 126      18.460   7.705  50.400  1.00 64.62           C  
ATOM   2727  N   GLY B 127      20.612   8.201  47.756  1.00 68.02           N  
ATOM   2728  CA  GLY B 127      21.076   7.510  46.582  1.00 70.36           C  
ATOM   2729  C   GLY B 127      22.244   6.589  46.885  1.00 72.29           C  
ATOM   2730  O   GLY B 127      23.148   6.942  47.646  1.00 61.87           O  
ATOM   2731  N   ILE B 128      22.222   5.416  46.249  1.00 78.77           N  
ATOM   2732  CA  ILE B 128      23.199   4.361  46.480  1.00 82.14           C  
ATOM   2733  C   ILE B 128      23.370   3.493  45.236  1.00 79.58           C  
ATOM   2734  O   ILE B 128      22.498   3.448  44.366  1.00 80.18           O  
ATOM   2735  CB  ILE B 128      22.779   3.467  47.680  1.00 85.44           C  
ATOM   2736  CG1 ILE B 128      23.934   2.580  48.180  1.00 92.72           C  
ATOM   2737  CG2 ILE B 128      21.596   2.581  47.311  1.00 84.82           C  
ATOM   2738  CD1 ILE B 128      25.218   3.301  48.569  1.00 92.99           C  
ATOM   2739  N   ASP B 129      24.509   2.812  45.182  1.00 77.61           N  
ATOM   2740  CA  ASP B 129      24.845   1.857  44.148  1.00 76.01           C  
ATOM   2741  C   ASP B 129      25.505   2.575  43.008  1.00 72.39           C  
ATOM   2742  O   ASP B 129      25.747   1.971  41.965  1.00 75.57           O  
ATOM   2743  CB  ASP B 129      23.623   1.083  43.631  1.00 81.36           C  
ATOM   2744  CG  ASP B 129      23.228  -0.059  44.532  1.00 86.19           C  
ATOM   2745  OD1 ASP B 129      23.495   0.006  45.762  1.00 79.43           O  
ATOM   2746  OD2 ASP B 129      22.652  -1.031  43.980  1.00 91.25           O  
ATOM   2747  N   PHE B 130      25.813   3.854  43.182  1.00 68.21           N  
ATOM   2748  CA  PHE B 130      26.400   4.589  42.071  1.00 72.71           C  
ATOM   2749  C   PHE B 130      27.875   4.247  41.918  1.00 76.59           C  
ATOM   2750  O   PHE B 130      28.566   3.981  42.888  1.00 79.22           O  
ATOM   2751  CB  PHE B 130      26.193   6.098  42.187  1.00 70.25           C  
ATOM   2752  CG  PHE B 130      24.780   6.516  41.968  1.00 65.45           C  
ATOM   2753  CD1 PHE B 130      24.266   6.594  40.702  1.00 64.26           C  
ATOM   2754  CD2 PHE B 130      23.959   6.806  43.041  1.00 65.79           C  
ATOM   2755  CE1 PHE B 130      22.953   6.963  40.508  1.00 68.30           C  
ATOM   2756  CE2 PHE B 130      22.645   7.183  42.852  1.00 64.53           C  
ATOM   2757  CZ  PHE B 130      22.141   7.260  41.583  1.00 65.05           C  
ATOM   2758  N   LYS B 131      28.325   4.243  40.672  1.00 77.10           N  
ATOM   2759  CA  LYS B 131      29.690   3.957  40.335  1.00 73.17           C  
ATOM   2760  C   LYS B 131      30.485   5.252  40.476  1.00 81.59           C  
ATOM   2761  O   LYS B 131      30.063   6.315  40.004  1.00 83.10           O  
ATOM   2762  CB  LYS B 131      29.767   3.418  38.904  1.00 72.79           C  
ATOM   2763  CG  LYS B 131      28.851   2.226  38.637  1.00 71.08           C  
ATOM   2764  CD  LYS B 131      28.798   1.858  37.161  1.00 70.10           C  
ATOM   2765  CE  LYS B 131      27.835   0.700  36.921  1.00 71.44           C  
ATOM   2766  NZ  LYS B 131      27.773   0.235  35.495  1.00 71.41           N  
ATOM   2767  N   GLU B 132      31.637   5.148  41.136  1.00 90.62           N  
ATOM   2768  CA  GLU B 132      32.558   6.264  41.309  1.00 86.45           C  
ATOM   2769  C   GLU B 132      33.121   6.674  39.955  1.00 88.89           C  
ATOM   2770  O   GLU B 132      33.766   7.720  39.830  1.00 91.56           O  
ATOM   2771  CB  GLU B 132      33.691   5.875  42.267  1.00 79.86           C  
ATOM   2772  N   ASP B 133      32.868   5.840  38.946  1.00 90.01           N  
ATOM   2773  CA  ASP B 133      33.232   6.133  37.563  1.00 95.04           C  
ATOM   2774  C   ASP B 133      32.024   5.958  36.619  1.00 85.07           C  
ATOM   2775  O   ASP B 133      32.190   5.773  35.418  1.00 84.03           O  
ATOM   2776  CB  ASP B 133      34.388   5.223  37.149  1.00101.94           C  
ATOM   2777  CG  ASP B 133      34.131   3.764  37.506  1.00114.07           C  
ATOM   2778  OD1 ASP B 133      33.732   3.492  38.667  1.00114.41           O  
ATOM   2779  OD2 ASP B 133      34.311   2.894  36.625  1.00124.56           O  
ATOM   2780  N   GLY B 134      30.812   6.033  37.164  1.00 78.67           N  
ATOM   2781  CA  GLY B 134      29.604   6.054  36.352  1.00 77.05           C  
ATOM   2782  C   GLY B 134      29.490   7.439  35.758  1.00 79.96           C  
ATOM   2783  O   GLY B 134      30.374   8.282  35.977  1.00 82.25           O  
ATOM   2784  N   ASN B 135      28.423   7.692  35.000  1.00 75.98           N  
ATOM   2785  CA  ASN B 135      28.207   9.034  34.449  1.00 68.74           C  
ATOM   2786  C   ASN B 135      27.681   9.941  35.514  1.00 64.37           C  
ATOM   2787  O   ASN B 135      27.812  11.152  35.411  1.00 69.63           O  
ATOM   2788  CB  ASN B 135      27.199   9.055  33.316  1.00 67.72           C  
ATOM   2789  CG  ASN B 135      27.570   8.148  32.176  1.00 68.93           C  
ATOM   2790  OD1 ASN B 135      28.656   8.256  31.580  1.00 79.65           O  
ATOM   2791  ND2 ASN B 135      26.648   7.263  31.831  1.00 67.66           N  
ATOM   2792  N   ILE B 136      27.060   9.359  36.531  1.00 64.14           N  
ATOM   2793  CA  ILE B 136      26.565  10.159  37.628  1.00 65.51           C  
ATOM   2794  C   ILE B 136      27.758  10.608  38.470  1.00 65.85           C  
ATOM   2795  O   ILE B 136      28.066  11.793  38.520  1.00 59.54           O  
ATOM   2796  CB  ILE B 136      25.447   9.453  38.449  1.00 62.38           C  
ATOM   2797  CG1 ILE B 136      24.141   9.343  37.628  1.00 60.24           C  
ATOM   2798  CG2 ILE B 136      25.123  10.255  39.693  1.00 60.32           C  
ATOM   2799  CD1 ILE B 136      23.894   8.010  36.959  1.00 55.51           C  
ATOM   2800  N   LEU B 137      28.467   9.677  39.089  1.00 73.05           N  
ATOM   2801  CA  LEU B 137      29.545  10.099  39.992  1.00 77.71           C  
ATOM   2802  C   LEU B 137      30.868  10.509  39.324  1.00 71.71           C  
ATOM   2803  O   LEU B 137      31.701  11.173  39.958  1.00 69.96           O  
ATOM   2804  CB  LEU B 137      29.759   9.079  41.109  1.00 80.91           C  
ATOM   2805  CG  LEU B 137      29.135   9.627  42.393  1.00 85.55           C  
ATOM   2806  CD1 LEU B 137      28.839   8.519  43.388  1.00 85.71           C  
ATOM   2807  CD2 LEU B 137      30.039  10.705  42.993  1.00 91.17           C  
ATOM   2808  N   GLY B 138      31.038  10.143  38.056  1.00 63.93           N  
ATOM   2809  CA  GLY B 138      32.116  10.671  37.234  1.00 60.76           C  
ATOM   2810  C   GLY B 138      31.811  12.020  36.594  1.00 60.37           C  
ATOM   2811  O   GLY B 138      32.688  12.594  35.961  1.00 66.03           O  
ATOM   2812  N   HIS B 139      30.574  12.515  36.755  1.00 60.75           N  
ATOM   2813  CA  HIS B 139      30.069  13.762  36.150  1.00 54.53           C  
ATOM   2814  C   HIS B 139      30.221  13.811  34.632  1.00 58.21           C  
ATOM   2815  O   HIS B 139      30.796  14.757  34.084  1.00 64.45           O  
ATOM   2816  CB  HIS B 139      30.733  14.986  36.776  1.00 53.25           C  
ATOM   2817  CG  HIS B 139      30.525  15.116  38.250  1.00 53.42           C  
ATOM   2818  ND1 HIS B 139      29.979  16.241  38.822  1.00 54.78           N  
ATOM   2819  CD2 HIS B 139      30.809  14.275  39.275  1.00 56.20           C  
ATOM   2820  CE1 HIS B 139      29.918  16.081  40.133  1.00 52.72           C  
ATOM   2821  NE2 HIS B 139      30.406  14.891  40.432  1.00 53.18           N  
ATOM   2822  N   LYS B 140      29.695  12.804  33.941  1.00 60.04           N  
ATOM   2823  CA  LYS B 140      29.868  12.718  32.484  1.00 61.63           C  
ATOM   2824  C   LYS B 140      28.602  13.181  31.793  1.00 57.96           C  
ATOM   2825  O   LYS B 140      28.444  13.031  30.583  1.00 55.41           O  
ATOM   2826  CB  LYS B 140      30.245  11.291  32.053  1.00 67.14           C  
ATOM   2827  CG  LYS B 140      31.599  10.818  32.569  1.00 68.75           C  
ATOM   2828  CD  LYS B 140      31.754   9.301  32.522  1.00 74.72           C  
ATOM   2829  CE  LYS B 140      32.910   8.848  33.405  1.00 78.15           C  
ATOM   2830  NZ  LYS B 140      33.353   7.452  33.136  1.00 77.34           N  
ATOM   2831  N   LEU B 141      27.716  13.753  32.598  1.00 61.02           N  
ATOM   2832  CA  LEU B 141      26.473  14.358  32.155  1.00 58.98           C  
ATOM   2833  C   LEU B 141      26.685  15.713  31.520  1.00 55.24           C  
ATOM   2834  O   LEU B 141      27.330  16.567  32.098  1.00 64.30           O  
ATOM   2835  CB  LEU B 141      25.586  14.564  33.372  1.00 60.24           C  
ATOM   2836  CG  LEU B 141      24.614  13.440  33.732  1.00 65.75           C  
ATOM   2837  CD1 LEU B 141      23.318  13.714  32.999  1.00 63.84           C  
ATOM   2838  CD2 LEU B 141      25.133  12.032  33.435  1.00 63.56           C  
ATOM   2839  N   GLU B 142      26.128  15.918  30.339  1.00 53.96           N  
ATOM   2840  CA  GLU B 142      26.021  17.255  29.775  1.00 50.43           C  
ATOM   2841  C   GLU B 142      25.021  18.128  30.527  1.00 48.17           C  
ATOM   2842  O   GLU B 142      24.055  17.624  31.062  1.00 50.75           O  
ATOM   2843  CB  GLU B 142      25.571  17.148  28.340  1.00 55.84           C  
ATOM   2844  CG  GLU B 142      26.662  16.792  27.369  1.00 60.26           C  
ATOM   2845  CD  GLU B 142      26.227  16.998  25.932  1.00 65.66           C  
ATOM   2846  OE1 GLU B 142      25.027  16.818  25.639  1.00 67.81           O  
ATOM   2847  OE2 GLU B 142      27.092  17.331  25.094  1.00 78.77           O  
ATOM   2848  N   TYR B 143      25.235  19.443  30.530  1.00 49.40           N  
ATOM   2849  CA  TYR B 143      24.339  20.410  31.213  1.00 47.62           C  
ATOM   2850  C   TYR B 143      23.238  20.947  30.294  1.00 51.19           C  
ATOM   2851  O   TYR B 143      23.337  22.042  29.701  1.00 52.85           O  
ATOM   2852  CB  TYR B 143      25.145  21.590  31.731  1.00 45.10           C  
ATOM   2853  CG  TYR B 143      24.439  22.529  32.699  1.00 37.36           C  
ATOM   2854  CD1 TYR B 143      24.061  22.099  33.924  1.00 34.78           C  
ATOM   2855  CD2 TYR B 143      24.208  23.853  32.366  1.00 35.22           C  
ATOM   2856  CE1 TYR B 143      23.464  22.944  34.811  1.00 37.24           C  
ATOM   2857  CE2 TYR B 143      23.595  24.701  33.236  1.00 34.46           C  
ATOM   2858  CZ  TYR B 143      23.224  24.248  34.464  1.00 35.69           C  
ATOM   2859  OH  TYR B 143      22.622  25.101  35.373  1.00 38.09           O  
ATOM   2860  N   ASN B 144      22.170  20.170  30.208  1.00 52.01           N  
ATOM   2861  CA  ASN B 144      21.081  20.473  29.324  1.00 52.15           C  
ATOM   2862  C   ASN B 144      19.894  19.630  29.763  1.00 51.81           C  
ATOM   2863  O   ASN B 144      20.027  18.818  30.676  1.00 53.15           O  
ATOM   2864  CB  ASN B 144      21.491  20.190  27.863  1.00 52.44           C  
ATOM   2865  CG  ASN B 144      21.753  18.712  27.588  1.00 54.42           C  
ATOM   2866  OD1 ASN B 144      21.188  17.827  28.231  1.00 63.38           O  
ATOM   2867  ND2 ASN B 144      22.610  18.438  26.621  1.00 60.06           N  
ATOM   2868  N   TYR B 145      18.744  19.815  29.123  1.00 51.29           N  
ATOM   2869  CA  TYR B 145      17.613  18.945  29.369  1.00 49.87           C  
ATOM   2870  C   TYR B 145      16.761  18.804  28.096  1.00 47.95           C  
ATOM   2871  O   TYR B 145      16.714  19.714  27.268  1.00 49.62           O  
ATOM   2872  CB  TYR B 145      16.810  19.481  30.568  1.00 49.50           C  
ATOM   2873  CG  TYR B 145      16.333  18.444  31.583  1.00 46.63           C  
ATOM   2874  CD1 TYR B 145      17.153  18.011  32.602  1.00 45.22           C  
ATOM   2875  CD2 TYR B 145      15.061  17.921  31.523  1.00 45.77           C  
ATOM   2876  CE1 TYR B 145      16.715  17.084  33.521  1.00 45.35           C  
ATOM   2877  CE2 TYR B 145      14.624  16.998  32.446  1.00 46.25           C  
ATOM   2878  CZ  TYR B 145      15.450  16.594  33.438  1.00 43.77           C  
ATOM   2879  OH  TYR B 145      14.999  15.702  34.348  1.00 45.71           O  
ATOM   2880  N   ASN B 146      16.136  17.632  27.957  1.00 47.82           N  
ATOM   2881  CA  ASN B 146      15.258  17.290  26.853  1.00 44.19           C  
ATOM   2882  C   ASN B 146      13.779  17.230  27.262  1.00 44.50           C  
ATOM   2883  O   ASN B 146      13.445  17.362  28.432  1.00 48.19           O  
ATOM   2884  CB  ASN B 146      15.621  15.906  26.394  1.00 47.01           C  
ATOM   2885  CG  ASN B 146      16.957  15.836  25.726  1.00 44.52           C  
ATOM   2886  OD1 ASN B 146      17.334  16.699  24.944  1.00 42.65           O  
ATOM   2887  ND2 ASN B 146      17.660  14.761  25.994  1.00 45.87           N  
ATOM   2888  N   SER B 147      12.888  17.005  26.304  1.00 43.15           N  
ATOM   2889  CA  SER B 147      11.473  17.074  26.578  1.00 42.24           C  
ATOM   2890  C   SER B 147      10.949  15.726  26.857  1.00 46.60           C  
ATOM   2891  O   SER B 147      11.306  14.816  26.170  1.00 58.65           O  
ATOM   2892  CB  SER B 147      10.783  17.584  25.377  1.00 45.46           C  
ATOM   2893  OG  SER B 147      11.377  18.798  25.022  1.00 52.62           O  
ATOM   2894  N   HIS B 148      10.103  15.576  27.864  1.00 51.07           N  
ATOM   2895  CA  HIS B 148       9.501  14.273  28.172  1.00 50.38           C  
ATOM   2896  C   HIS B 148       8.019  14.419  28.518  1.00 47.73           C  
ATOM   2897  O   HIS B 148       7.554  15.498  28.865  1.00 42.34           O  
ATOM   2898  CB  HIS B 148      10.240  13.561  29.326  1.00 50.22           C  
ATOM   2899  CG  HIS B 148      11.733  13.682  29.265  1.00 53.08           C  
ATOM   2900  ND1 HIS B 148      12.411  14.782  29.753  1.00 52.98           N  
ATOM   2901  CD2 HIS B 148      12.681  12.840  28.789  1.00 52.90           C  
ATOM   2902  CE1 HIS B 148      13.708  14.616  29.571  1.00 52.37           C  
ATOM   2903  NE2 HIS B 148      13.900  13.445  28.993  1.00 51.93           N  
ATOM   2904  N   ASN B 149       7.289  13.312  28.429  1.00 49.25           N  
ATOM   2905  CA  ASN B 149       5.949  13.262  28.980  1.00 46.64           C  
ATOM   2906  C   ASN B 149       5.909  12.515  30.286  1.00 48.63           C  
ATOM   2907  O   ASN B 149       6.601  11.510  30.448  1.00 49.87           O  
ATOM   2908  CB  ASN B 149       4.991  12.607  28.035  1.00 45.48           C  
ATOM   2909  CG  ASN B 149       5.049  13.180  26.668  1.00 41.07           C  
ATOM   2910  OD1 ASN B 149       5.315  12.458  25.719  1.00 48.04           O  
ATOM   2911  ND2 ASN B 149       4.793  14.472  26.541  1.00 41.46           N  
ATOM   2912  N   VAL B 150       5.061  13.027  31.184  1.00 50.20           N  
ATOM   2913  CA  VAL B 150       4.906  12.583  32.550  1.00 49.78           C  
ATOM   2914  C   VAL B 150       3.513  12.036  32.586  1.00 50.51           C  
ATOM   2915  O   VAL B 150       2.543  12.751  32.385  1.00 51.32           O  
ATOM   2916  CB  VAL B 150       5.022  13.759  33.544  1.00 48.72           C  
ATOM   2917  CG1 VAL B 150       4.691  13.344  34.955  1.00 51.42           C  
ATOM   2918  CG2 VAL B 150       6.422  14.308  33.536  1.00 50.86           C  
ATOM   2919  N   TYR B 151       3.417  10.758  32.851  1.00 52.60           N  
ATOM   2920  CA  TYR B 151       2.161  10.090  32.762  1.00 52.29           C  
ATOM   2921  C   TYR B 151       1.564  10.013  34.113  1.00 50.72           C  
ATOM   2922  O   TYR B 151       2.227   9.621  35.054  1.00 49.35           O  
ATOM   2923  CB  TYR B 151       2.357   8.719  32.133  1.00 52.61           C  
ATOM   2924  CG  TYR B 151       2.793   8.912  30.714  1.00 51.94           C  
ATOM   2925  CD1 TYR B 151       1.940   9.498  29.804  1.00 50.03           C  
ATOM   2926  CD2 TYR B 151       4.096   8.604  30.300  1.00 54.70           C  
ATOM   2927  CE1 TYR B 151       2.331   9.728  28.500  1.00 52.35           C  
ATOM   2928  CE2 TYR B 151       4.506   8.837  28.994  1.00 50.28           C  
ATOM   2929  CZ  TYR B 151       3.612   9.388  28.099  1.00 48.76           C  
ATOM   2930  OH  TYR B 151       3.982   9.635  26.814  1.00 46.89           O  
ATOM   2931  N   ILE B 152       0.300  10.423  34.186  1.00 55.94           N  
ATOM   2932  CA  ILE B 152      -0.467  10.457  35.431  1.00 59.38           C  
ATOM   2933  C   ILE B 152      -1.705   9.562  35.319  1.00 58.75           C  
ATOM   2934  O   ILE B 152      -2.440   9.618  34.348  1.00 58.36           O  
ATOM   2935  CB  ILE B 152      -0.892  11.904  35.804  1.00 58.71           C  
ATOM   2936  CG1 ILE B 152       0.339  12.799  36.053  1.00 53.27           C  
ATOM   2937  CG2 ILE B 152      -1.786  11.905  37.039  1.00 59.38           C  
ATOM   2938  CD1 ILE B 152       0.083  14.275  35.912  1.00 47.19           C  
ATOM   2939  N   MET B 153      -1.903   8.724  36.327  1.00 65.04           N  
ATOM   2940  CA  MET B 153      -3.118   7.932  36.454  1.00 72.51           C  
ATOM   2941  C   MET B 153      -3.555   7.821  37.921  1.00 64.59           C  
ATOM   2942  O   MET B 153      -2.731   7.905  38.829  1.00 56.20           O  
ATOM   2943  CB  MET B 153      -2.920   6.549  35.830  1.00 84.47           C  
ATOM   2944  CG  MET B 153      -1.797   5.720  36.441  1.00 91.14           C  
ATOM   2945  SD  MET B 153      -2.182   3.956  36.440  1.00 98.09           S  
ATOM   2946  CE  MET B 153      -2.281   3.675  34.669  1.00 98.75           C  
ATOM   2947  N   ALA B 154      -4.855   7.645  38.146  1.00 68.13           N  
ATOM   2948  CA  ALA B 154      -5.383   7.667  39.511  1.00 70.62           C  
ATOM   2949  C   ALA B 154      -5.004   6.412  40.260  1.00 74.56           C  
ATOM   2950  O   ALA B 154      -4.837   5.350  39.665  1.00 77.00           O  
ATOM   2951  CB  ALA B 154      -6.895   7.852  39.525  1.00 71.71           C  
ATOM   2952  N   ASP B 155      -4.853   6.566  41.573  1.00 87.73           N  
ATOM   2953  CA  ASP B 155      -4.602   5.468  42.501  1.00 93.55           C  
ATOM   2954  C   ASP B 155      -5.692   5.568  43.557  1.00 92.86           C  
ATOM   2955  O   ASP B 155      -5.488   6.179  44.621  1.00 89.67           O  
ATOM   2956  CB  ASP B 155      -3.207   5.605  43.132  1.00 96.53           C  
ATOM   2957  CG  ASP B 155      -2.774   4.367  43.908  1.00 99.04           C  
ATOM   2958  OD1 ASP B 155      -3.615   3.463  44.148  1.00102.22           O  
ATOM   2959  OD2 ASP B 155      -1.573   4.306  44.270  1.00 93.16           O  
ATOM   2960  N   LYS B 156      -6.854   4.987  43.235  1.00 86.27           N  
ATOM   2961  CA  LYS B 156      -8.029   5.049  44.108  1.00 84.13           C  
ATOM   2962  C   LYS B 156      -7.697   4.477  45.484  1.00 85.92           C  
ATOM   2963  O   LYS B 156      -8.022   5.095  46.499  1.00 83.49           O  
ATOM   2964  CB  LYS B 156      -9.215   4.314  43.482  1.00 81.60           C  
ATOM   2965  N   GLN B 157      -7.022   3.321  45.499  1.00 90.29           N  
ATOM   2966  CA  GLN B 157      -6.472   2.724  46.720  1.00 86.10           C  
ATOM   2967  C   GLN B 157      -5.805   3.754  47.636  1.00 93.40           C  
ATOM   2968  O   GLN B 157      -6.113   3.804  48.830  1.00101.18           O  
ATOM   2969  N   LYS B 158      -4.925   4.589  47.073  1.00 93.50           N  
ATOM   2970  CA  LYS B 158      -4.105   5.523  47.858  1.00 84.63           C  
ATOM   2971  C   LYS B 158      -4.642   6.954  48.024  1.00 88.66           C  
ATOM   2972  O   LYS B 158      -3.952   7.808  48.597  1.00 85.97           O  
ATOM   2973  N   ASN B 159      -5.871   7.215  47.573  1.00 83.02           N  
ATOM   2974  CA  ASN B 159      -6.371   8.596  47.463  1.00 83.15           C  
ATOM   2975  C   ASN B 159      -5.241   9.429  46.899  1.00 80.56           C  
ATOM   2976  O   ASN B 159      -4.689  10.270  47.587  1.00 72.30           O  
ATOM   2977  CB  ASN B 159      -6.848   9.187  48.817  1.00 84.35           C  
ATOM   2978  CG  ASN B 159      -7.723  10.457  48.654  1.00 80.55           C  
ATOM   2979  OD1 ASN B 159      -8.612  10.504  47.804  1.00 89.65           O  
ATOM   2980  ND2 ASN B 159      -7.491  11.471  49.493  1.00 72.63           N  
ATOM   2981  N   GLY B 160      -4.861   9.147  45.658  1.00 86.78           N  
ATOM   2982  CA  GLY B 160      -3.762   9.867  45.020  1.00 81.80           C  
ATOM   2983  C   GLY B 160      -3.528   9.482  43.574  1.00 77.18           C  
ATOM   2984  O   GLY B 160      -4.462   9.060  42.887  1.00 74.92           O  
ATOM   2985  N   ILE B 161      -2.270   9.647  43.137  1.00 73.23           N  
ATOM   2986  CA  ILE B 161      -1.804   9.317  41.778  1.00 63.97           C  
ATOM   2987  C   ILE B 161      -0.453   8.564  41.756  1.00 65.55           C  
ATOM   2988  O   ILE B 161       0.421   8.734  42.640  1.00 61.06           O  
ATOM   2989  CB  ILE B 161      -1.684  10.567  40.910  1.00 56.86           C  
ATOM   2990  CG1 ILE B 161      -0.732  11.561  41.577  1.00 59.91           C  
ATOM   2991  CG2 ILE B 161      -3.061  11.158  40.678  1.00 54.49           C  
ATOM   2992  CD1 ILE B 161      -0.581  12.890  40.857  1.00 63.08           C  
ATOM   2993  N   LYS B 162      -0.332   7.703  40.746  1.00 62.06           N  
ATOM   2994  CA  LYS B 162       0.878   6.961  40.453  1.00 59.62           C  
ATOM   2995  C   LYS B 162       1.394   7.571  39.151  1.00 60.19           C  
ATOM   2996  O   LYS B 162       0.678   7.641  38.169  1.00 60.47           O  
ATOM   2997  CB  LYS B 162       0.557   5.473  40.286  1.00 57.92           C  
ATOM   2998  N   VAL B 163       2.619   8.065  39.161  1.00 56.68           N  
ATOM   2999  CA  VAL B 163       3.129   8.795  38.033  1.00 53.03           C  
ATOM   3000  C   VAL B 163       4.316   8.047  37.496  1.00 57.65           C  
ATOM   3001  O   VAL B 163       5.038   7.392  38.237  1.00 63.98           O  
ATOM   3002  CB  VAL B 163       3.500  10.203  38.458  1.00 50.40           C  
ATOM   3003  CG1 VAL B 163       4.200  10.980  37.357  1.00 51.03           C  
ATOM   3004  CG2 VAL B 163       2.243  10.913  38.862  1.00 52.04           C  
ATOM   3005  N   ASN B 164       4.514   8.171  36.197  1.00 59.21           N  
ATOM   3006  CA  ASN B 164       5.342   7.272  35.449  1.00 62.94           C  
ATOM   3007  C   ASN B 164       6.095   8.036  34.365  1.00 57.26           C  
ATOM   3008  O   ASN B 164       5.477   8.708  33.560  1.00 59.88           O  
ATOM   3009  CB  ASN B 164       4.390   6.265  34.815  1.00 73.10           C  
ATOM   3010  CG  ASN B 164       5.102   5.157  34.102  1.00 86.64           C  
ATOM   3011  OD1 ASN B 164       5.333   5.229  32.892  1.00 88.68           O  
ATOM   3012  ND2 ASN B 164       5.467   4.113  34.850  1.00101.42           N  
ATOM   3013  N   PHE B 165       7.421   7.979  34.357  1.00 56.38           N  
ATOM   3014  CA  PHE B 165       8.182   8.493  33.215  1.00 53.36           C  
ATOM   3015  C   PHE B 165       9.664   8.148  33.230  1.00 51.78           C  
ATOM   3016  O   PHE B 165      10.162   7.603  34.191  1.00 53.41           O  
ATOM   3017  CB  PHE B 165       8.022   9.987  33.102  1.00 53.16           C  
ATOM   3018  CG  PHE B 165       8.397  10.719  34.325  1.00 52.21           C  
ATOM   3019  CD1 PHE B 165       7.473  10.904  35.333  1.00 49.51           C  
ATOM   3020  CD2 PHE B 165       9.654  11.262  34.447  1.00 53.20           C  
ATOM   3021  CE1 PHE B 165       7.794  11.590  36.458  1.00 49.12           C  
ATOM   3022  CE2 PHE B 165       9.989  11.968  35.574  1.00 56.15           C  
ATOM   3023  CZ  PHE B 165       9.057  12.128  36.585  1.00 55.85           C  
ATOM   3024  N   LYS B 166      10.339   8.462  32.129  1.00 55.63           N  
ATOM   3025  CA  LYS B 166      11.752   8.169  31.946  1.00 54.52           C  
ATOM   3026  C   LYS B 166      12.479   9.343  31.318  1.00 51.13           C  
ATOM   3027  O   LYS B 166      12.067   9.826  30.265  1.00 52.73           O  
ATOM   3028  CB  LYS B 166      11.892   6.976  31.019  1.00 57.60           C  
ATOM   3029  CG  LYS B 166      13.265   6.316  31.030  1.00 63.30           C  
ATOM   3030  CD  LYS B 166      13.408   5.283  29.917  1.00 68.87           C  
ATOM   3031  CE  LYS B 166      12.522   4.048  30.125  1.00 75.50           C  
ATOM   3032  NZ  LYS B 166      12.048   3.449  28.839  1.00 77.07           N  
ATOM   3033  N   ILE B 167      13.575   9.762  31.947  1.00 52.33           N  
ATOM   3034  CA  ILE B 167      14.403  10.883  31.476  1.00 51.80           C  
ATOM   3035  C   ILE B 167      15.655  10.433  30.703  1.00 51.51           C  
ATOM   3036  O   ILE B 167      16.470   9.691  31.200  1.00 57.89           O  
ATOM   3037  CB  ILE B 167      14.828  11.786  32.657  1.00 49.05           C  
ATOM   3038  CG1 ILE B 167      13.596  12.340  33.397  1.00 50.46           C  
ATOM   3039  CG2 ILE B 167      15.711  12.929  32.199  1.00 50.11           C  
ATOM   3040  CD1 ILE B 167      12.774  13.374  32.653  1.00 49.53           C  
ATOM   3041  N   ARG B 168      15.774  10.884  29.468  1.00 53.05           N  
ATOM   3042  CA  ARG B 168      17.008  10.799  28.697  1.00 53.92           C  
ATOM   3043  C   ARG B 168      18.004  11.930  29.015  1.00 51.84           C  
ATOM   3044  O   ARG B 168      17.889  13.061  28.513  1.00 47.84           O  
ATOM   3045  CB  ARG B 168      16.704  10.934  27.206  1.00 57.47           C  
ATOM   3046  CG  ARG B 168      15.855   9.880  26.538  1.00 57.91           C  
ATOM   3047  CD  ARG B 168      15.302  10.461  25.234  1.00 55.90           C  
ATOM   3048  NE  ARG B 168      14.027  11.144  25.492  1.00 60.79           N  
ATOM   3049  CZ  ARG B 168      13.726  12.424  25.260  1.00 59.78           C  
ATOM   3050  NH1 ARG B 168      14.569  13.267  24.693  1.00 61.16           N  
ATOM   3051  NH2 ARG B 168      12.521  12.857  25.578  1.00 63.73           N  
ATOM   3052  N   HIS B 169      19.005  11.617  29.813  1.00 52.56           N  
ATOM   3053  CA  HIS B 169      20.058  12.566  30.072  1.00 51.81           C  
ATOM   3054  C   HIS B 169      21.140  12.352  29.030  1.00 49.71           C  
ATOM   3055  O   HIS B 169      21.730  11.305  28.996  1.00 52.49           O  
ATOM   3056  CB  HIS B 169      20.639  12.361  31.472  1.00 51.19           C  
ATOM   3057  CG  HIS B 169      19.704  12.671  32.616  1.00 49.22           C  
ATOM   3058  ND1 HIS B 169      19.546  13.939  33.132  1.00 50.71           N  
ATOM   3059  CD2 HIS B 169      18.947  11.859  33.393  1.00 51.92           C  
ATOM   3060  CE1 HIS B 169      18.719  13.898  34.163  1.00 54.71           C  
ATOM   3061  NE2 HIS B 169      18.330  12.648  34.336  1.00 53.52           N  
ATOM   3062  N   ASN B 170      21.396  13.333  28.170  1.00 55.67           N  
ATOM   3063  CA  ASN B 170      22.505  13.238  27.210  1.00 53.53           C  
ATOM   3064  C   ASN B 170      23.828  13.255  27.916  1.00 53.57           C  
ATOM   3065  O   ASN B 170      23.954  13.751  29.021  1.00 53.37           O  
ATOM   3066  CB  ASN B 170      22.528  14.393  26.236  1.00 55.29           C  
ATOM   3067  CG  ASN B 170      21.360  14.399  25.298  1.00 59.81           C  
ATOM   3068  OD1 ASN B 170      21.184  15.369  24.557  1.00 68.83           O  
ATOM   3069  ND2 ASN B 170      20.546  13.333  25.308  1.00 58.80           N  
ATOM   3070  N   ILE B 171      24.828  12.725  27.243  1.00 59.06           N  
ATOM   3071  CA  ILE B 171      26.112  12.467  27.865  1.00 64.30           C  
ATOM   3072  C   ILE B 171      27.151  13.059  26.945  1.00 61.05           C  
ATOM   3073  O   ILE B 171      26.880  13.229  25.762  1.00 59.61           O  
ATOM   3074  CB  ILE B 171      26.288  10.951  28.125  1.00 66.13           C  
ATOM   3075  CG1 ILE B 171      25.475  10.568  29.356  1.00 63.98           C  
ATOM   3076  CG2 ILE B 171      27.740  10.567  28.348  1.00 66.81           C  
ATOM   3077  CD1 ILE B 171      25.305   9.088  29.492  1.00 69.58           C  
ATOM   3078  N   GLU B 172      28.302  13.424  27.514  1.00 66.35           N  
ATOM   3079  CA  GLU B 172      29.362  14.141  26.787  1.00 66.63           C  
ATOM   3080  C   GLU B 172      29.857  13.329  25.585  1.00 68.38           C  
ATOM   3081  O   GLU B 172      30.132  13.899  24.534  1.00 72.14           O  
ATOM   3082  CB  GLU B 172      30.518  14.530  27.736  1.00 66.66           C  
ATOM   3083  CG  GLU B 172      30.168  15.577  28.795  1.00 60.46           C  
ATOM   3084  N   ASP B 173      29.896  12.000  25.721  1.00 73.66           N  
ATOM   3085  CA  ASP B 173      30.304  11.083  24.627  1.00 76.99           C  
ATOM   3086  C   ASP B 173      29.315  10.920  23.437  1.00 77.88           C  
ATOM   3087  O   ASP B 173      29.579  10.138  22.515  1.00 81.74           O  
ATOM   3088  CB  ASP B 173      30.728   9.699  25.207  1.00 79.07           C  
ATOM   3089  CG  ASP B 173      29.585   8.668  25.272  1.00 83.84           C  
ATOM   3090  OD1 ASP B 173      28.511   8.956  25.855  1.00 97.57           O  
ATOM   3091  OD2 ASP B 173      29.784   7.540  24.760  1.00 83.57           O  
ATOM   3092  N   GLY B 174      28.202  11.654  23.443  1.00 79.11           N  
ATOM   3093  CA  GLY B 174      27.143  11.483  22.433  1.00 80.00           C  
ATOM   3094  C   GLY B 174      26.092  10.420  22.775  1.00 79.42           C  
ATOM   3095  O   GLY B 174      25.160  10.165  21.989  1.00 76.07           O  
ATOM   3096  N   SER B 175      26.235   9.796  23.943  1.00 75.46           N  
ATOM   3097  CA  SER B 175      25.280   8.815  24.384  1.00 71.48           C  
ATOM   3098  C   SER B 175      24.237   9.434  25.295  1.00 68.73           C  
ATOM   3099  O   SER B 175      24.219  10.642  25.503  1.00 69.31           O  
ATOM   3100  CB  SER B 175      25.975   7.687  25.105  1.00 72.78           C  
ATOM   3101  OG  SER B 175      25.164   6.534  24.989  1.00 88.88           O  
ATOM   3102  N   VAL B 176      23.364   8.582  25.818  1.00 64.25           N  
ATOM   3103  CA  VAL B 176      22.254   8.989  26.665  1.00 60.99           C  
ATOM   3104  C   VAL B 176      22.206   8.106  27.892  1.00 60.70           C  
ATOM   3105  O   VAL B 176      22.467   6.913  27.810  1.00 62.74           O  
ATOM   3106  CB  VAL B 176      20.906   8.808  25.945  1.00 54.39           C  
ATOM   3107  CG1 VAL B 176      19.747   9.058  26.893  1.00 52.40           C  
ATOM   3108  CG2 VAL B 176      20.847   9.702  24.736  1.00 52.08           C  
ATOM   3109  N   GLN B 177      21.859   8.706  29.019  1.00 62.17           N  
ATOM   3110  CA  GLN B 177      21.587   7.982  30.235  1.00 63.34           C  
ATOM   3111  C   GLN B 177      20.092   8.006  30.445  1.00 63.36           C  
ATOM   3112  O   GLN B 177      19.462   9.039  30.310  1.00 68.92           O  
ATOM   3113  CB  GLN B 177      22.291   8.643  31.410  1.00 66.79           C  
ATOM   3114  CG  GLN B 177      21.879   8.116  32.775  1.00 71.32           C  
ATOM   3115  CD  GLN B 177      22.454   6.747  33.072  1.00 71.78           C  
ATOM   3116  OE1 GLN B 177      23.663   6.605  33.192  1.00 74.14           O  
ATOM   3117  NE2 GLN B 177      21.593   5.738  33.200  1.00 72.87           N  
ATOM   3118  N   LEU B 178      19.520   6.869  30.788  1.00 62.41           N  
ATOM   3119  CA  LEU B 178      18.112   6.821  31.042  1.00 58.75           C  
ATOM   3120  C   LEU B 178      17.931   6.733  32.510  1.00 56.86           C  
ATOM   3121  O   LEU B 178      18.583   5.929  33.165  1.00 56.77           O  
ATOM   3122  CB  LEU B 178      17.508   5.627  30.359  1.00 63.61           C  
ATOM   3123  CG  LEU B 178      17.676   5.809  28.858  1.00 64.94           C  
ATOM   3124  CD1 LEU B 178      17.693   4.445  28.199  1.00 69.41           C  
ATOM   3125  CD2 LEU B 178      16.577   6.711  28.306  1.00 67.38           C  
ATOM   3126  N   ALA B 179      17.074   7.611  33.024  1.00 56.53           N  
ATOM   3127  CA  ALA B 179      16.652   7.591  34.402  1.00 53.84           C  
ATOM   3128  C   ALA B 179      15.154   7.311  34.458  1.00 55.20           C  
ATOM   3129  O   ALA B 179      14.336   8.014  33.868  1.00 51.51           O  
ATOM   3130  CB  ALA B 179      16.982   8.907  35.066  1.00 57.52           C  
ATOM   3131  N   ASP B 180      14.809   6.262  35.177  1.00 59.42           N  
ATOM   3132  CA  ASP B 180      13.486   5.720  35.112  1.00 60.03           C  
ATOM   3133  C   ASP B 180      12.781   6.104  36.388  1.00 58.47           C  
ATOM   3134  O   ASP B 180      13.180   5.699  37.466  1.00 59.46           O  
ATOM   3135  CB  ASP B 180      13.585   4.209  34.960  1.00 62.55           C  
ATOM   3136  CG  ASP B 180      12.273   3.560  34.605  1.00 65.32           C  
ATOM   3137  OD1 ASP B 180      11.298   4.264  34.267  1.00 70.46           O  
ATOM   3138  OD2 ASP B 180      12.225   2.318  34.659  1.00 67.08           O  
ATOM   3139  N   HIS B 181      11.721   6.888  36.248  1.00 60.06           N  
ATOM   3140  CA  HIS B 181      11.023   7.487  37.379  1.00 58.94           C  
ATOM   3141  C   HIS B 181       9.722   6.793  37.745  1.00 60.16           C  
ATOM   3142  O   HIS B 181       8.774   6.724  36.959  1.00 64.22           O  
ATOM   3143  CB  HIS B 181      10.727   8.953  37.081  1.00 58.25           C  
ATOM   3144  CG  HIS B 181      11.940   9.814  37.090  1.00 55.66           C  
ATOM   3145  ND1 HIS B 181      12.988   9.622  36.224  1.00 61.79           N  
ATOM   3146  CD2 HIS B 181      12.284  10.857  37.875  1.00 59.20           C  
ATOM   3147  CE1 HIS B 181      13.929  10.514  36.475  1.00 61.50           C  
ATOM   3148  NE2 HIS B 181      13.523  11.277  37.470  1.00 60.89           N  
ATOM   3149  N   TYR B 182       9.700   6.295  38.968  1.00 62.00           N  
ATOM   3150  CA  TYR B 182       8.510   5.755  39.567  1.00 64.12           C  
ATOM   3151  C   TYR B 182       8.133   6.715  40.698  1.00 60.75           C  
ATOM   3152  O   TYR B 182       8.960   7.096  41.500  1.00 60.18           O  
ATOM   3153  CB  TYR B 182       8.763   4.299  40.000  1.00 68.65           C  
ATOM   3154  CG  TYR B 182       8.877   3.375  38.782  1.00 77.54           C  
ATOM   3155  CD1 TYR B 182       7.730   2.938  38.107  1.00 86.23           C  
ATOM   3156  CD2 TYR B 182      10.117   2.987  38.263  1.00 78.13           C  
ATOM   3157  CE1 TYR B 182       7.811   2.132  36.981  1.00 82.22           C  
ATOM   3158  CE2 TYR B 182      10.201   2.183  37.127  1.00 74.25           C  
ATOM   3159  CZ  TYR B 182       9.044   1.759  36.496  1.00 77.86           C  
ATOM   3160  OH  TYR B 182       9.081   0.956  35.382  1.00 78.40           O  
ATOM   3161  N   GLN B 183       6.881   7.153  40.696  1.00 59.39           N  
ATOM   3162  CA  GLN B 183       6.439   8.246  41.523  1.00 54.99           C  
ATOM   3163  C   GLN B 183       5.041   7.986  42.073  1.00 58.50           C  
ATOM   3164  O   GLN B 183       4.180   7.419  41.388  1.00 59.93           O  
ATOM   3165  CB  GLN B 183       6.439   9.517  40.692  1.00 56.15           C  
ATOM   3166  CG  GLN B 183       5.975  10.766  41.412  1.00 55.24           C  
ATOM   3167  CD  GLN B 183       5.780  11.914  40.473  1.00 54.37           C  
ATOM   3168  OE1 GLN B 183       6.397  11.977  39.428  1.00 58.67           O  
ATOM   3169  NE2 GLN B 183       4.910  12.829  40.838  1.00 59.28           N  
ATOM   3170  N   GLN B 184       4.845   8.412  43.321  1.00 62.37           N  
ATOM   3171  CA  GLN B 184       3.594   8.278  44.035  1.00 61.84           C  
ATOM   3172  C   GLN B 184       3.354   9.611  44.725  1.00 59.93           C  
ATOM   3173  O   GLN B 184       4.307  10.261  45.154  1.00 54.94           O  
ATOM   3174  CB  GLN B 184       3.692   7.137  45.055  1.00 64.02           C  
ATOM   3175  N   ASN B 185       2.085  10.008  44.816  1.00 58.55           N  
ATOM   3176  CA  ASN B 185       1.709  11.287  45.384  1.00 58.66           C  
ATOM   3177  C   ASN B 185       0.473  11.183  46.261  1.00 64.37           C  
ATOM   3178  O   ASN B 185      -0.602  10.885  45.770  1.00 68.02           O  
ATOM   3179  CB  ASN B 185       1.384  12.276  44.274  1.00 61.64           C  
ATOM   3180  CG  ASN B 185       2.596  12.934  43.692  1.00 57.20           C  
ATOM   3181  OD1 ASN B 185       3.022  12.582  42.613  1.00 61.07           O  
ATOM   3182  ND2 ASN B 185       3.142  13.907  44.391  1.00 57.38           N  
ATOM   3183  N   THR B 186       0.613  11.488  47.547  1.00 71.46           N  
ATOM   3184  CA  THR B 186      -0.465  11.308  48.525  1.00 71.10           C  
ATOM   3185  C   THR B 186      -0.754  12.649  49.208  1.00 74.16           C  
ATOM   3186  O   THR B 186       0.183  13.393  49.515  1.00 72.09           O  
ATOM   3187  CB  THR B 186      -0.061  10.287  49.617  1.00 72.00           C  
ATOM   3188  OG1 THR B 186       0.845   9.311  49.088  1.00 75.54           O  
ATOM   3189  CG2 THR B 186      -1.257   9.574  50.159  1.00 78.73           C  
ATOM   3190  N   PRO B 187      -2.044  12.959  49.466  1.00 73.28           N  
ATOM   3191  CA  PRO B 187      -2.375  14.244  50.044  1.00 76.00           C  
ATOM   3192  C   PRO B 187      -2.111  14.237  51.518  1.00 77.14           C  
ATOM   3193  O   PRO B 187      -2.157  13.184  52.135  1.00 80.09           O  
ATOM   3194  CB  PRO B 187      -3.883  14.361  49.812  1.00 74.77           C  
ATOM   3195  CG  PRO B 187      -4.308  13.099  49.156  1.00 70.61           C  
ATOM   3196  CD  PRO B 187      -3.234  12.113  49.413  1.00 69.84           C  
ATOM   3197  N   ILE B 188      -1.851  15.407  52.076  1.00 82.97           N  
ATOM   3198  CA  ILE B 188      -1.650  15.533  53.508  1.00 91.04           C  
ATOM   3199  C   ILE B 188      -3.005  15.832  54.128  1.00 99.01           C  
ATOM   3200  O   ILE B 188      -3.459  15.122  55.028  1.00 99.22           O  
ATOM   3201  CB  ILE B 188      -0.678  16.678  53.861  1.00 95.41           C  
ATOM   3202  CG1 ILE B 188       0.599  16.594  53.002  1.00 96.77           C  
ATOM   3203  CG2 ILE B 188      -0.374  16.655  55.359  1.00 91.10           C  
ATOM   3204  CD1 ILE B 188       1.310  17.914  52.786  1.00 96.21           C  
ATOM   3205  N   GLY B 189      -3.651  16.885  53.626  1.00100.99           N  
ATOM   3206  CA  GLY B 189      -4.941  17.303  54.143  1.00109.75           C  
ATOM   3207  C   GLY B 189      -5.977  16.202  54.001  1.00116.02           C  
ATOM   3208  O   GLY B 189      -6.243  15.732  52.892  1.00138.79           O  
ATOM   3209  N   ASP B 190      -6.570  15.792  55.119  1.00106.07           N  
ATOM   3210  CA  ASP B 190      -7.653  14.817  55.088  1.00 99.19           C  
ATOM   3211  C   ASP B 190      -8.790  15.263  54.151  1.00 94.12           C  
ATOM   3212  O   ASP B 190      -9.696  14.485  53.835  1.00 87.71           O  
ATOM   3213  CB  ASP B 190      -8.171  14.553  56.505  1.00 99.22           C  
ATOM   3214  CG  ASP B 190      -7.195  13.731  57.333  1.00104.56           C  
ATOM   3215  OD1 ASP B 190      -5.976  13.993  57.253  1.00111.89           O  
ATOM   3216  OD2 ASP B 190      -7.642  12.821  58.060  1.00102.33           O  
ATOM   3217  N   GLY B 191      -8.735  16.517  53.706  1.00 87.53           N  
ATOM   3218  CA  GLY B 191      -9.613  16.994  52.660  1.00 86.14           C  
ATOM   3219  C   GLY B 191      -9.554  16.116  51.420  1.00 89.74           C  
ATOM   3220  O   GLY B 191      -8.707  15.204  51.332  1.00 90.07           O  
ATOM   3221  N   PRO B 192     -10.458  16.383  50.448  1.00 84.88           N  
ATOM   3222  CA  PRO B 192     -10.546  15.599  49.221  1.00 82.63           C  
ATOM   3223  C   PRO B 192      -9.596  16.112  48.146  1.00 80.04           C  
ATOM   3224  O   PRO B 192      -9.281  17.312  48.104  1.00 74.56           O  
ATOM   3225  CB  PRO B 192     -11.998  15.802  48.793  1.00 77.10           C  
ATOM   3226  CG  PRO B 192     -12.362  17.139  49.323  1.00 74.75           C  
ATOM   3227  CD  PRO B 192     -11.417  17.501  50.430  1.00 76.33           C  
ATOM   3228  N   VAL B 193      -9.149  15.192  47.295  1.00 79.69           N  
ATOM   3229  CA  VAL B 193      -8.304  15.523  46.151  1.00 77.90           C  
ATOM   3230  C   VAL B 193      -8.975  15.020  44.891  1.00 76.36           C  
ATOM   3231  O   VAL B 193      -9.887  14.183  44.974  1.00 85.57           O  
ATOM   3232  CB  VAL B 193      -6.899  14.900  46.277  1.00 77.29           C  
ATOM   3233  CG1 VAL B 193      -6.324  15.208  47.646  1.00 76.77           C  
ATOM   3234  CG2 VAL B 193      -6.924  13.394  46.037  1.00 75.21           C  
ATOM   3235  N   LEU B 194      -8.517  15.519  43.740  1.00 70.30           N  
ATOM   3236  CA  LEU B 194      -9.077  15.136  42.434  1.00 64.61           C  
ATOM   3237  C   LEU B 194      -8.368  13.914  41.950  1.00 61.08           C  
ATOM   3238  O   LEU B 194      -7.166  13.960  41.800  1.00 71.67           O  
ATOM   3239  CB  LEU B 194      -8.901  16.259  41.407  1.00 66.32           C  
ATOM   3240  CG  LEU B 194     -10.028  17.297  41.210  1.00 68.42           C  
ATOM   3241  CD1 LEU B 194     -10.987  17.378  42.383  1.00 71.14           C  
ATOM   3242  CD2 LEU B 194      -9.458  18.680  40.915  1.00 68.37           C  
ATOM   3243  N   LEU B 195      -9.093  12.824  41.717  1.00 59.36           N  
ATOM   3244  CA  LEU B 195      -8.489  11.599  41.205  1.00 62.53           C  
ATOM   3245  C   LEU B 195      -8.675  11.578  39.734  1.00 60.28           C  
ATOM   3246  O   LEU B 195      -9.770  11.375  39.247  1.00 65.19           O  
ATOM   3247  CB  LEU B 195      -9.085  10.327  41.810  1.00 69.80           C  
ATOM   3248  CG  LEU B 195      -8.592   9.962  43.213  1.00 72.11           C  
ATOM   3249  CD1 LEU B 195      -8.942   8.512  43.479  1.00 79.83           C  
ATOM   3250  CD2 LEU B 195      -7.096  10.174  43.390  1.00 72.22           C  
ATOM   3251  N   PRO B 196      -7.585  11.767  39.008  1.00 65.43           N  
ATOM   3252  CA  PRO B 196      -7.722  12.121  37.624  1.00 61.85           C  
ATOM   3253  C   PRO B 196      -7.884  10.936  36.700  1.00 57.48           C  
ATOM   3254  O   PRO B 196      -7.429   9.834  37.014  1.00 56.07           O  
ATOM   3255  CB  PRO B 196      -6.393  12.796  37.342  1.00 65.80           C  
ATOM   3256  CG  PRO B 196      -5.418  12.008  38.155  1.00 66.80           C  
ATOM   3257  CD  PRO B 196      -6.166  11.650  39.408  1.00 65.56           C  
ATOM   3258  N   ASP B 197      -8.553  11.176  35.577  1.00 54.04           N  
ATOM   3259  CA  ASP B 197      -8.511  10.278  34.458  1.00 56.25           C  
ATOM   3260  C   ASP B 197      -7.175  10.450  33.788  1.00 57.04           C  
ATOM   3261  O   ASP B 197      -6.524  11.486  33.893  1.00 64.02           O  
ATOM   3262  CB  ASP B 197      -9.598  10.595  33.442  1.00 58.22           C  
ATOM   3263  CG  ASP B 197     -10.962  10.153  33.872  1.00 58.38           C  
ATOM   3264  OD1 ASP B 197     -11.185   9.811  35.047  1.00 63.10           O  
ATOM   3265  OD2 ASP B 197     -11.832  10.158  32.998  1.00 66.42           O  
ATOM   3266  N   ASN B 198      -6.784   9.434  33.054  1.00 57.20           N  
ATOM   3267  CA  ASN B 198      -5.422   9.326  32.641  1.00 55.12           C  
ATOM   3268  C   ASN B 198      -5.117  10.386  31.644  1.00 52.48           C  
ATOM   3269  O   ASN B 198      -5.947  10.723  30.824  1.00 49.98           O  
ATOM   3270  CB  ASN B 198      -5.142   7.932  32.120  1.00 57.79           C  
ATOM   3271  CG  ASN B 198      -5.394   6.858  33.180  1.00 66.11           C  
ATOM   3272  OD1 ASN B 198      -5.639   7.150  34.364  1.00 67.55           O  
ATOM   3273  ND2 ASN B 198      -5.343   5.602  32.753  1.00 76.72           N  
ATOM   3274  N   HIS B 199      -3.914  10.934  31.781  1.00 56.49           N  
ATOM   3275  CA  HIS B 199      -3.414  12.046  30.987  1.00 52.09           C  
ATOM   3276  C   HIS B 199      -1.939  12.169  31.335  1.00 50.57           C  
ATOM   3277  O   HIS B 199      -1.421  11.406  32.140  1.00 49.66           O  
ATOM   3278  CB  HIS B 199      -4.157  13.344  31.351  1.00 49.54           C  
ATOM   3279  CG  HIS B 199      -3.911  13.799  32.748  1.00 47.87           C  
ATOM   3280  ND1 HIS B 199      -4.495  13.197  33.840  1.00 48.73           N  
ATOM   3281  CD2 HIS B 199      -3.118  14.777  33.235  1.00 47.30           C  
ATOM   3282  CE1 HIS B 199      -4.067  13.784  34.941  1.00 48.84           C  
ATOM   3283  NE2 HIS B 199      -3.230  14.747  34.601  1.00 48.79           N  
ATOM   3284  N   TYR B 200      -1.276  13.150  30.759  1.00 50.34           N  
ATOM   3285  CA  TYR B 200       0.109  13.403  31.089  1.00 52.07           C  
ATOM   3286  C   TYR B 200       0.429  14.884  30.952  1.00 50.09           C  
ATOM   3287  O   TYR B 200      -0.399  15.691  30.553  1.00 47.49           O  
ATOM   3288  CB  TYR B 200       0.990  12.618  30.130  1.00 53.06           C  
ATOM   3289  CG  TYR B 200       0.784  13.094  28.736  1.00 51.06           C  
ATOM   3290  CD1 TYR B 200      -0.257  12.611  27.991  1.00 55.06           C  
ATOM   3291  CD2 TYR B 200       1.559  14.092  28.191  1.00 47.51           C  
ATOM   3292  CE1 TYR B 200      -0.493  13.062  26.709  1.00 49.67           C  
ATOM   3293  CE2 TYR B 200       1.328  14.541  26.917  1.00 43.89           C  
ATOM   3294  CZ  TYR B 200       0.295  14.010  26.184  1.00 46.00           C  
ATOM   3295  OH  TYR B 200       0.007  14.405  24.900  1.00 50.51           O  
ATOM   3296  N   LEU B 201       1.667  15.216  31.254  1.00 51.16           N  
ATOM   3297  CA  LEU B 201       2.147  16.568  31.125  1.00 51.13           C  
ATOM   3298  C   LEU B 201       3.226  16.544  30.074  1.00 49.77           C  
ATOM   3299  O   LEU B 201       3.963  15.592  30.017  1.00 51.51           O  
ATOM   3300  CB  LEU B 201       2.716  17.027  32.471  1.00 52.11           C  
ATOM   3301  CG  LEU B 201       1.822  16.756  33.691  1.00 52.83           C  
ATOM   3302  CD1 LEU B 201       2.448  17.220  35.012  1.00 51.41           C  
ATOM   3303  CD2 LEU B 201       0.465  17.410  33.471  1.00 52.93           C  
ATOM   3304  N   SER B 202       3.288  17.556  29.213  1.00 50.44           N  
ATOM   3305  CA  SER B 202       4.452  17.747  28.361  1.00 49.53           C  
ATOM   3306  C   SER B 202       5.368  18.746  29.014  1.00 45.85           C  
ATOM   3307  O   SER B 202       5.041  19.900  29.092  1.00 49.77           O  
ATOM   3308  CB  SER B 202       4.088  18.250  26.982  1.00 50.44           C  
ATOM   3309  OG  SER B 202       5.250  18.192  26.173  1.00 56.62           O  
ATOM   3310  N   VAL B 203       6.520  18.293  29.467  1.00 43.92           N  
ATOM   3311  CA  VAL B 203       7.410  19.099  30.247  1.00 42.93           C  
ATOM   3312  C   VAL B 203       8.645  19.455  29.456  1.00 41.93           C  
ATOM   3313  O   VAL B 203       9.290  18.605  28.903  1.00 38.93           O  
ATOM   3314  CB  VAL B 203       7.891  18.294  31.454  1.00 46.32           C  
ATOM   3315  CG1 VAL B 203       8.595  19.197  32.458  1.00 47.15           C  
ATOM   3316  CG2 VAL B 203       6.728  17.556  32.104  1.00 46.16           C  
ATOM   3317  N   GLN B 204       8.990  20.722  29.423  1.00 46.71           N  
ATOM   3318  CA  GLN B 204      10.286  21.131  28.902  1.00 47.27           C  
ATOM   3319  C   GLN B 204      11.077  21.831  29.988  1.00 45.36           C  
ATOM   3320  O   GLN B 204      10.547  22.591  30.711  1.00 43.57           O  
ATOM   3321  CB  GLN B 204      10.113  22.057  27.730  1.00 45.27           C  
ATOM   3322  CG  GLN B 204       9.416  21.408  26.586  1.00 47.00           C  
ATOM   3323  CD  GLN B 204       8.664  22.412  25.772  1.00 50.17           C  
ATOM   3324  OE1 GLN B 204       9.224  23.056  24.880  1.00 50.85           O  
ATOM   3325  NE2 GLN B 204       7.378  22.555  26.069  1.00 52.32           N  
ATOM   3326  N   ALA B 205      12.360  21.536  30.094  1.00 51.73           N  
ATOM   3327  CA  ALA B 205      13.240  22.184  31.049  1.00 49.13           C  
ATOM   3328  C   ALA B 205      14.457  22.693  30.318  1.00 49.49           C  
ATOM   3329  O   ALA B 205      15.054  21.979  29.513  1.00 50.32           O  
ATOM   3330  CB  ALA B 205      13.665  21.203  32.117  1.00 50.59           C  
ATOM   3331  N   ALA B 206      14.813  23.941  30.582  1.00 50.57           N  
ATOM   3332  CA  ALA B 206      16.047  24.493  30.071  1.00 49.15           C  
ATOM   3333  C   ALA B 206      16.916  24.956  31.238  1.00 45.36           C  
ATOM   3334  O   ALA B 206      16.441  25.569  32.158  1.00 45.52           O  
ATOM   3335  CB  ALA B 206      15.743  25.621  29.113  1.00 52.36           C  
ATOM   3336  N   LEU B 207      18.188  24.596  31.211  1.00 49.56           N  
ATOM   3337  CA  LEU B 207      19.126  24.912  32.281  1.00 44.84           C  
ATOM   3338  C   LEU B 207      20.043  25.992  31.838  1.00 45.17           C  
ATOM   3339  O   LEU B 207      20.523  25.958  30.719  1.00 52.60           O  
ATOM   3340  CB  LEU B 207      20.016  23.729  32.573  1.00 41.10           C  
ATOM   3341  CG  LEU B 207      19.395  22.374  32.689  1.00 37.53           C  
ATOM   3342  CD1 LEU B 207      20.394  21.495  33.386  1.00 35.64           C  
ATOM   3343  CD2 LEU B 207      18.112  22.489  33.476  1.00 39.22           C  
ATOM   3344  N   SER B 208      20.339  26.918  32.734  1.00 51.85           N  
ATOM   3345  CA  SER B 208      21.359  27.926  32.481  1.00 50.94           C  
ATOM   3346  C   SER B 208      22.132  28.340  33.747  1.00 51.12           C  
ATOM   3347  O   SER B 208      22.032  27.713  34.816  1.00 49.79           O  
ATOM   3348  CB  SER B 208      20.721  29.133  31.789  1.00 55.20           C  
ATOM   3349  OG  SER B 208      19.560  29.588  32.471  1.00 59.70           O  
ATOM   3350  N   LYS B 209      22.946  29.379  33.584  1.00 53.63           N  
ATOM   3351  CA  LYS B 209      23.737  29.951  34.642  1.00 49.74           C  
ATOM   3352  C   LYS B 209      23.507  31.434  34.584  1.00 51.01           C  
ATOM   3353  O   LYS B 209      23.697  32.047  33.530  1.00 49.98           O  
ATOM   3354  CB  LYS B 209      25.222  29.694  34.402  1.00 47.54           C  
ATOM   3355  CG  LYS B 209      25.634  28.246  34.332  1.00 46.63           C  
ATOM   3356  CD  LYS B 209      25.394  27.507  35.635  1.00 47.84           C  
ATOM   3357  CE  LYS B 209      26.027  26.117  35.612  1.00 45.76           C  
ATOM   3358  NZ  LYS B 209      25.936  25.440  36.921  1.00 45.63           N  
ATOM   3359  N   ASP B 210      23.066  31.994  35.706  1.00 57.80           N  
ATOM   3360  CA  ASP B 210      23.245  33.405  35.981  1.00 58.89           C  
ATOM   3361  C   ASP B 210      24.717  33.721  35.843  1.00 63.35           C  
ATOM   3362  O   ASP B 210      25.529  33.148  36.562  1.00 59.04           O  
ATOM   3363  CB  ASP B 210      22.790  33.754  37.379  1.00 55.71           C  
ATOM   3364  CG  ASP B 210      22.995  35.206  37.696  1.00 60.10           C  
ATOM   3365  OD1 ASP B 210      23.692  35.917  36.930  1.00 54.26           O  
ATOM   3366  OD2 ASP B 210      22.450  35.643  38.727  1.00 71.99           O  
ATOM   3367  N   PRO B 211      25.069  34.619  34.899  1.00 73.67           N  
ATOM   3368  CA  PRO B 211      26.486  34.860  34.660  1.00 74.85           C  
ATOM   3369  C   PRO B 211      27.208  35.631  35.802  1.00 77.00           C  
ATOM   3370  O   PRO B 211      28.413  35.449  35.968  1.00 83.89           O  
ATOM   3371  CB  PRO B 211      26.491  35.619  33.319  1.00 73.08           C  
ATOM   3372  CG  PRO B 211      25.152  36.271  33.231  1.00 69.50           C  
ATOM   3373  CD  PRO B 211      24.208  35.364  33.951  1.00 70.95           C  
ATOM   3374  N   ASN B 212      26.493  36.443  36.591  1.00 75.16           N  
ATOM   3375  CA  ASN B 212      27.087  37.152  37.755  1.00 72.82           C  
ATOM   3376  C   ASN B 212      27.030  36.336  39.040  1.00 68.26           C  
ATOM   3377  O   ASN B 212      27.024  36.913  40.127  1.00 65.01           O  
ATOM   3378  CB  ASN B 212      26.378  38.494  38.041  1.00 80.43           C  
ATOM   3379  CG  ASN B 212      26.654  39.558  36.989  1.00 85.77           C  
ATOM   3380  OD1 ASN B 212      27.530  39.400  36.125  1.00 93.44           O  
ATOM   3381  ND2 ASN B 212      25.904  40.664  37.063  1.00 84.05           N  
ATOM   3382  N   GLU B 213      26.979  35.011  38.903  1.00 68.60           N  
ATOM   3383  CA  GLU B 213      26.884  34.086  40.028  1.00 70.37           C  
ATOM   3384  C   GLU B 213      27.981  33.017  39.925  1.00 71.31           C  
ATOM   3385  O   GLU B 213      27.978  32.193  39.009  1.00 78.57           O  
ATOM   3386  CB  GLU B 213      25.485  33.453  40.090  1.00 67.80           C  
ATOM   3387  CG  GLU B 213      25.253  32.434  41.215  1.00 68.96           C  
ATOM   3388  CD  GLU B 213      25.539  32.954  42.621  1.00 67.85           C  
ATOM   3389  OE1 GLU B 213      24.748  33.748  43.177  1.00 70.43           O  
ATOM   3390  OE2 GLU B 213      26.567  32.552  43.187  1.00 68.44           O  
ATOM   3391  N   LYS B 214      28.892  33.048  40.900  1.00 78.11           N  
ATOM   3392  CA  LYS B 214      30.155  32.300  40.888  1.00 82.63           C  
ATOM   3393  C   LYS B 214      30.106  31.016  41.734  1.00 80.36           C  
ATOM   3394  O   LYS B 214      31.070  30.225  41.742  1.00 76.52           O  
ATOM   3395  CB  LYS B 214      31.291  33.213  41.384  1.00 77.34           C  
ATOM   3396  N   ARG B 215      28.991  30.835  42.446  1.00 74.61           N  
ATOM   3397  CA  ARG B 215      28.708  29.603  43.161  1.00 72.73           C  
ATOM   3398  C   ARG B 215      28.187  28.534  42.242  1.00 67.06           C  
ATOM   3399  O   ARG B 215      27.783  28.803  41.124  1.00 73.03           O  
ATOM   3400  CB  ARG B 215      27.658  29.824  44.237  1.00 79.09           C  
ATOM   3401  CG  ARG B 215      28.229  30.005  45.621  1.00 87.60           C  
ATOM   3402  CD  ARG B 215      27.125  30.136  46.655  1.00 93.32           C  
ATOM   3403  NE  ARG B 215      26.224  31.246  46.347  1.00 97.68           N  
ATOM   3404  CZ  ARG B 215      25.296  31.717  47.176  1.00111.39           C  
ATOM   3405  NH1 ARG B 215      25.142  31.191  48.392  1.00113.22           N  
ATOM   3406  NH2 ARG B 215      24.525  32.737  46.791  1.00119.71           N  
ATOM   3407  N   ASP B 216      28.196  27.306  42.740  1.00 66.40           N  
ATOM   3408  CA  ASP B 216      27.623  26.201  42.014  1.00 64.79           C  
ATOM   3409  C   ASP B 216      26.143  26.423  42.098  1.00 64.28           C  
ATOM   3410  O   ASP B 216      25.592  26.451  43.194  1.00 65.62           O  
ATOM   3411  CB  ASP B 216      27.992  24.849  42.644  1.00 64.96           C  
ATOM   3412  CG  ASP B 216      27.922  23.687  41.654  1.00 61.92           C  
ATOM   3413  OD1 ASP B 216      28.187  23.885  40.446  1.00 69.25           O  
ATOM   3414  OD2 ASP B 216      27.619  22.560  42.088  1.00 61.50           O  
ATOM   3415  N   HIS B 217      25.504  26.603  40.948  1.00 60.82           N  
ATOM   3416  CA  HIS B 217      24.076  26.773  40.920  1.00 54.80           C  
ATOM   3417  C   HIS B 217      23.543  26.251  39.635  1.00 52.06           C  
ATOM   3418  O   HIS B 217      24.293  25.869  38.748  1.00 53.48           O  
ATOM   3419  CB  HIS B 217      23.702  28.241  41.054  1.00 56.35           C  
ATOM   3420  CG  HIS B 217      24.056  29.065  39.862  1.00 55.94           C  
ATOM   3421  ND1 HIS B 217      25.350  29.176  39.390  1.00 60.06           N  
ATOM   3422  CD2 HIS B 217      23.293  29.837  39.059  1.00 53.47           C  
ATOM   3423  CE1 HIS B 217      25.369  29.972  38.339  1.00 57.89           C  
ATOM   3424  NE2 HIS B 217      24.132  30.383  38.116  1.00 60.86           N  
ATOM   3425  N   MET B 218      22.224  26.247  39.565  1.00 49.29           N  
ATOM   3426  CA  MET B 218      21.495  25.951  38.372  1.00 45.59           C  
ATOM   3427  C   MET B 218      20.372  26.956  38.254  1.00 45.33           C  
ATOM   3428  O   MET B 218      19.721  27.239  39.225  1.00 48.81           O  
ATOM   3429  CB  MET B 218      20.916  24.556  38.504  1.00 47.04           C  
ATOM   3430  CG  MET B 218      20.226  24.021  37.271  1.00 46.96           C  
ATOM   3431  SD  MET B 218      19.728  22.324  37.501  1.00 49.13           S  
ATOM   3432  CE  MET B 218      18.209  22.407  38.428  1.00 45.52           C  
ATOM   3433  N   VAL B 219      20.153  27.516  37.073  1.00 48.04           N  
ATOM   3434  CA  VAL B 219      18.879  28.171  36.781  1.00 47.31           C  
ATOM   3435  C   VAL B 219      18.039  27.211  35.925  1.00 45.97           C  
ATOM   3436  O   VAL B 219      18.548  26.546  35.042  1.00 47.49           O  
ATOM   3437  CB  VAL B 219      19.065  29.533  36.071  1.00 46.84           C  
ATOM   3438  CG1 VAL B 219      17.786  30.352  36.100  1.00 48.40           C  
ATOM   3439  CG2 VAL B 219      20.156  30.329  36.745  1.00 49.50           C  
ATOM   3440  N   LEU B 220      16.749  27.165  36.204  1.00 46.08           N  
ATOM   3441  CA  LEU B 220      15.820  26.321  35.522  1.00 46.07           C  
ATOM   3442  C   LEU B 220      14.699  27.212  35.061  1.00 46.81           C  
ATOM   3443  O   LEU B 220      14.009  27.778  35.862  1.00 51.62           O  
ATOM   3444  CB  LEU B 220      15.281  25.286  36.530  1.00 52.02           C  
ATOM   3445  CG  LEU B 220      14.457  24.056  36.095  1.00 53.32           C  
ATOM   3446  CD1 LEU B 220      15.246  23.290  35.047  1.00 56.31           C  
ATOM   3447  CD2 LEU B 220      14.095  23.124  37.242  1.00 50.36           C  
ATOM   3448  N   LEU B 221      14.536  27.378  33.769  1.00 50.77           N  
ATOM   3449  CA  LEU B 221      13.279  27.869  33.245  1.00 55.17           C  
ATOM   3450  C   LEU B 221      12.515  26.642  32.823  1.00 54.19           C  
ATOM   3451  O   LEU B 221      13.012  25.835  32.059  1.00 56.94           O  
ATOM   3452  CB  LEU B 221      13.484  28.820  32.052  1.00 63.33           C  
ATOM   3453  CG  LEU B 221      13.435  30.335  32.398  1.00 71.69           C  
ATOM   3454  CD1 LEU B 221      14.559  30.824  33.322  1.00 73.67           C  
ATOM   3455  CD2 LEU B 221      13.386  31.198  31.145  1.00 71.08           C  
ATOM   3456  N   GLU B 222      11.314  26.464  33.331  1.00 52.22           N  
ATOM   3457  CA  GLU B 222      10.551  25.306  32.936  1.00 51.06           C  
ATOM   3458  C   GLU B 222       9.169  25.682  32.450  1.00 51.57           C  
ATOM   3459  O   GLU B 222       8.619  26.685  32.871  1.00 51.21           O  
ATOM   3460  CB  GLU B 222      10.490  24.318  34.076  1.00 54.42           C  
ATOM   3461  CG  GLU B 222       9.495  23.186  33.877  1.00 58.45           C  
ATOM   3462  CD  GLU B 222       9.550  22.146  34.986  1.00 61.24           C  
ATOM   3463  OE1 GLU B 222      10.522  22.113  35.767  1.00 60.29           O  
ATOM   3464  OE2 GLU B 222       8.593  21.350  35.089  1.00 73.74           O  
ATOM   3465  N   PHE B 223       8.663  24.876  31.514  1.00 54.94           N  
ATOM   3466  CA  PHE B 223       7.331  25.003  30.915  1.00 56.18           C  
ATOM   3467  C   PHE B 223       6.597  23.651  30.941  1.00 52.73           C  
ATOM   3468  O   PHE B 223       7.127  22.633  30.527  1.00 52.47           O  
ATOM   3469  CB  PHE B 223       7.416  25.490  29.471  1.00 57.26           C  
ATOM   3470  CG  PHE B 223       8.112  26.823  29.292  1.00 57.63           C  
ATOM   3471  CD1 PHE B 223       9.504  26.918  29.330  1.00 63.97           C  
ATOM   3472  CD2 PHE B 223       7.385  27.965  29.039  1.00 52.03           C  
ATOM   3473  CE1 PHE B 223      10.143  28.136  29.140  1.00 62.36           C  
ATOM   3474  CE2 PHE B 223       8.012  29.175  28.842  1.00 52.77           C  
ATOM   3475  CZ  PHE B 223       9.387  29.264  28.886  1.00 60.32           C  
ATOM   3476  N   VAL B 224       5.371  23.661  31.449  1.00 55.18           N  
ATOM   3477  CA  VAL B 224       4.541  22.450  31.531  1.00 52.95           C  
ATOM   3478  C   VAL B 224       3.061  22.711  31.167  1.00 52.21           C  
ATOM   3479  O   VAL B 224       2.398  23.545  31.774  1.00 51.20           O  
ATOM   3480  CB  VAL B 224       4.608  21.799  32.923  1.00 49.20           C  
ATOM   3481  CG1 VAL B 224       4.227  20.331  32.843  1.00 46.04           C  
ATOM   3482  CG2 VAL B 224       5.987  21.972  33.532  1.00 48.94           C  
ATOM   3483  N   THR B 225       2.587  22.011  30.139  1.00 53.51           N  
ATOM   3484  CA  THR B 225       1.192  21.979  29.790  1.00 54.61           C  
ATOM   3485  C   THR B 225       0.692  20.559  29.826  1.00 55.21           C  
ATOM   3486  O   THR B 225       1.338  19.647  29.328  1.00 57.81           O  
ATOM   3487  CB  THR B 225       0.952  22.544  28.400  1.00 54.87           C  
ATOM   3488  OG1 THR B 225       1.252  23.947  28.415  1.00 63.89           O  
ATOM   3489  CG2 THR B 225      -0.483  22.357  28.010  1.00 55.73           C  
ATOM   3490  N   ALA B 226      -0.482  20.392  30.418  1.00 60.70           N  
ATOM   3491  CA  ALA B 226      -1.086  19.087  30.611  1.00 57.39           C  
ATOM   3492  C   ALA B 226      -1.922  18.764  29.421  1.00 52.81           C  
ATOM   3493  O   ALA B 226      -2.412  19.648  28.725  1.00 52.96           O  
ATOM   3494  CB  ALA B 226      -1.932  19.059  31.877  1.00 57.97           C  
ATOM   3495  N   ALA B 227      -2.091  17.481  29.187  1.00 53.56           N  
ATOM   3496  CA  ALA B 227      -2.750  17.054  27.986  1.00 52.00           C  
ATOM   3497  C   ALA B 227      -3.180  15.623  28.102  1.00 51.28           C  
ATOM   3498  O   ALA B 227      -3.000  15.004  29.154  1.00 49.95           O  
ATOM   3499  CB  ALA B 227      -1.811  17.222  26.819  1.00 53.89           C  
ATOM   3500  N   GLY B 228      -3.770  15.118  27.020  1.00 53.00           N  
ATOM   3501  CA  GLY B 228      -4.107  13.686  26.893  1.00 60.78           C  
ATOM   3502  C   GLY B 228      -5.583  13.348  27.022  1.00 59.51           C  
ATOM   3503  O   GLY B 228      -5.997  12.163  26.984  1.00 54.67           O  
ATOM   3504  N   ILE B 229      -6.362  14.405  27.201  1.00 56.17           N  
ATOM   3505  CA  ILE B 229      -7.758  14.285  27.388  1.00 56.33           C  
ATOM   3506  C   ILE B 229      -8.345  15.275  26.408  1.00 63.93           C  
ATOM   3507  O   ILE B 229      -8.109  16.475  26.500  1.00 72.47           O  
ATOM   3508  CB  ILE B 229      -8.095  14.513  28.850  1.00 52.77           C  
ATOM   3509  CG1 ILE B 229      -7.825  13.226  29.621  1.00 52.68           C  
ATOM   3510  CG2 ILE B 229      -9.530  14.920  29.027  1.00 55.66           C  
ATOM   3511  CD1 ILE B 229      -7.658  13.427  31.104  1.00 52.26           C  
ATOM   3512  N   THR B 230      -9.062  14.710  25.435  1.00 75.44           N  
ATOM   3513  CA  THR B 230      -9.624  15.399  24.280  1.00 78.89           C  
ATOM   3514  C   THR B 230     -11.036  15.872  24.561  1.00 84.83           C  
ATOM   3515  O   THR B 230     -11.445  16.935  24.090  1.00 87.68           O  
ATOM   3516  CB  THR B 230      -9.706  14.421  23.110  1.00 85.15           C  
ATOM   3517  OG1 THR B 230     -10.680  13.405  23.404  1.00 84.82           O  
ATOM   3518  CG2 THR B 230      -8.332  13.763  22.871  1.00 89.31           C  
ATOM   3519  N   HIS B 231     -11.774  15.048  25.314  1.00 93.89           N  
ATOM   3520  CA  HIS B 231     -13.106  15.372  25.825  1.00 94.93           C  
ATOM   3521  C   HIS B 231     -13.024  16.227  27.098  1.00 91.39           C  
ATOM   3522  O   HIS B 231     -13.845  17.121  27.327  1.00 82.16           O  
ATOM   3523  CB  HIS B 231     -13.863  14.085  26.110  1.00 99.34           C  
TER    3524      HIS B 231                                                      
HETATM 3525 CL    CL B 301      16.200  13.898  22.996  1.00 65.45          CL  
HETATM 3526  O   HOH A 301      13.974  25.342  10.742  1.00 40.69           O  
HETATM 3527  O   HOH A 302      24.764  17.236   9.306  1.00 46.17           O  
HETATM 3528  O   HOH A 303      20.983   9.848  14.097  1.00 51.16           O  
HETATM 3529  O   HOH A 304      22.054  28.632  18.034  1.00 63.25           O  
HETATM 3530  O   HOH A 305      38.170  31.765  31.001  1.00 85.09           O  
HETATM 3531  O   HOH A 306      42.505  29.093  26.988  1.00 74.30           O  
HETATM 3532  O   HOH A 307      17.964  39.040  29.481  1.00 52.52           O  
HETATM 3533  O   HOH A 308      -3.422  36.111  11.672  1.00 57.50           O  
HETATM 3534  O   HOH A 309      -0.941  25.508  12.824  1.00 66.38           O  
HETATM 3535  O   HOH A 310       1.455  21.691  14.510  1.00 44.89           O  
HETATM 3536  O   HOH A 311      13.602  23.113  14.109  1.00 35.01           O  
HETATM 3537  O   HOH A 312      22.868  33.224  12.674  1.00 55.46           O  
HETATM 3538  O   HOH A 313      15.071  14.811   3.069  1.00 43.09           O  
HETATM 3539  O   HOH A 314      18.175  31.206   9.403  1.00 47.19           O  
HETATM 3540  O   HOH A 315      13.976   6.361   9.687  1.00 73.37           O  
HETATM 3541  O   HOH A 316      14.090  10.134  11.798  1.00 64.58           O  
HETATM 3542  O   HOH A 317       5.849  18.341  -3.339  1.00 47.58           O  
HETATM 3543  O   HOH A 318       8.741  16.901  -6.906  1.00 45.38           O  
HETATM 3544  O   HOH A 319      12.691  16.890  -3.533  1.00 44.90           O  
HETATM 3545  O   HOH A 320      -1.569  12.963   7.866  1.00 60.97           O  
HETATM 3546  O   HOH A 321      -0.519   5.587   3.239  1.00 86.23           O  
HETATM 3547  O   HOH A 322       9.616  12.188   0.568  1.00 80.28           O  
HETATM 3548  O   HOH A 323       9.262  11.417  26.074  1.00 56.89           O  
HETATM 3549  O   HOH A 324       2.066  11.231  23.171  1.00 55.13           O  
HETATM 3550  O   HOH A 325       3.123   8.365  23.113  1.00 61.42           O  
HETATM 3551  O   HOH A 326      22.395  21.625  24.468  1.00 54.98           O  
HETATM 3552  O   HOH A 327      22.659  25.718  26.585  1.00 49.04           O  
HETATM 3553  O   HOH A 328      30.476  26.371  18.226  1.00148.87           O  
HETATM 3554  O   HOH A 329      24.511  25.177   2.716  1.00 60.50           O  
HETATM 3555  O   HOH A 330      32.556  26.586   0.133  1.00 63.55           O  
HETATM 3556  O   HOH A 331      35.697  27.853  -1.571  1.00 50.85           O  
HETATM 3557  O   HOH A 332      24.752  35.015  -0.314  1.00 68.39           O  
HETATM 3558  O   HOH A 333       5.698  15.369   5.623  1.00 48.94           O  
HETATM 3559  O   HOH A 334      40.594  32.778  22.397  1.00 63.05           O  
HETATM 3560  O   HOH A 335      33.403  36.561  25.299  1.00 59.60           O  
HETATM 3561  O   HOH A 336      23.463  40.415  23.495  1.00 51.32           O  
HETATM 3562  O   HOH A 337      24.407  40.842  26.536  1.00 53.75           O  
HETATM 3563  O   HOH A 338      -0.128   7.844  17.932  1.00 70.84           O  
HETATM 3564  O   HOH A 339       4.529   9.171  12.635  1.00 65.61           O  
HETATM 3565  O   HOH A 340      20.274  31.684  17.589  1.00 42.62           O  
HETATM 3566  O   HOH A 341      14.087  21.471  12.140  1.00 42.12           O  
HETATM 3567  O   HOH A 342      17.595  22.699  21.246  1.00 54.09           O  
HETATM 3568  O   HOH A 343      24.020  17.744  16.224  1.00 48.36           O  
HETATM 3569  O   HOH A 344      31.259  27.945   4.271  1.00 75.72           O  
HETATM 3570  O   HOH A 345      28.079  34.087  18.796  1.00 61.45           O  
HETATM 3571  O   HOH A 346      24.319  43.985  30.424  1.00 63.38           O  
HETATM 3572  O   HOH A 347      15.980  21.863  24.719  1.00 51.75           O  
HETATM 3573  O   HOH A 348      31.633  31.387  15.236  1.00 55.89           O  
HETATM 3574  O   HOH A 349      11.976  43.820  21.145  1.00 74.63           O  
HETATM 3575  O   HOH A 350       8.843  25.524  -3.013  1.00 44.66           O  
HETATM 3576  O   HOH A 351      17.438  33.266  32.980  1.00 44.79           O  
HETATM 3577  O   HOH A 352       2.658  19.141  14.716  1.00 56.21           O  
HETATM 3578  O   HOH A 353       8.308  41.688  13.652  1.00 61.02           O  
HETATM 3579  O   HOH A 354      11.781  10.047   9.985  1.00 58.83           O  
HETATM 3580  O   HOH A 355      19.361  12.221   9.960  1.00 49.28           O  
HETATM 3581  O   HOH A 356       2.933  23.253  15.856  1.00 51.75           O  
HETATM 3582  O   HOH A 357      -0.522  28.801  17.950  1.00 44.99           O  
HETATM 3583  O   HOH A 358      33.071  20.896  16.292  1.00 61.83           O  
HETATM 3584  O   HOH A 359       3.662  21.122  -3.897  1.00 77.83           O  
HETATM 3585  O   HOH A 360       1.388  16.387  18.730  1.00 54.84           O  
HETATM 3586  O   HOH A 361      -5.031  38.153  19.979  1.00 61.14           O  
HETATM 3587  O   HOH A 362      29.961  21.391   9.706  1.00 62.38           O  
HETATM 3588  O   HOH A 363      24.339  47.252  19.831  1.00 52.31           O  
HETATM 3589  O   HOH A 364      24.249  45.944  23.052  1.00 56.16           O  
HETATM 3590  O   HOH A 365      -1.664  38.927  11.783  1.00 67.74           O  
HETATM 3591  O   HOH A 366      44.900  27.557  24.596  1.00 63.57           O  
HETATM 3592  O   HOH A 367       8.901  13.990  24.456  1.00 65.66           O  
HETATM 3593  O   HOH A 368      10.937  19.260  18.197  1.00 37.82           O  
HETATM 3594  O   HOH A 369      18.787  45.853   4.080  1.00 66.03           O  
HETATM 3595  O   HOH A 370      20.835  47.353  20.510  1.00 62.66           O  
HETATM 3596  O   HOH A 371       4.854  33.347   1.302  1.00 49.51           O  
HETATM 3597  O   HOH A 372      33.454  32.570  31.060  1.00 67.47           O  
HETATM 3598  O   HOH A 373       2.299  13.912  22.299  1.00 68.12           O  
HETATM 3599  O   HOH A 374      10.901  17.387  20.244  1.00 46.44           O  
HETATM 3600  O   HOH A 375      40.121  36.940   8.653  1.00 58.56           O  
HETATM 3601  O   HOH A 376      15.879  28.935  -0.635  1.00 45.84           O  
HETATM 3602  O   HOH A 377      19.216  28.671  -0.313  1.00 55.94           O  
HETATM 3603  O   HOH A 378      -0.093  25.587  15.704  1.00 67.65           O  
HETATM 3604  O   HOH A 379      21.377  32.364  23.099  1.00 61.11           O  
HETATM 3605  O   HOH A 380      41.533  29.188  23.764  1.00 71.61           O  
HETATM 3606  O   HOH A 381      14.244  30.942  -1.476  1.00 65.63           O  
HETATM 3607  O   HOH A 382       7.911  11.387  21.686  1.00 74.66           O  
HETATM 3608  O   HOH A 383      27.520  42.339  29.030  1.00 65.06           O  
HETATM 3609  O   HOH A 384      13.805  18.809  19.206  1.00 49.95           O  
HETATM 3610  O   HOH A 385       8.724  18.318  17.963  1.00 58.88           O  
HETATM 3611  O   HOH A 386      23.082  14.020   2.421  1.00 71.39           O  
HETATM 3612  O   HOH A 387       8.344  45.033  11.040  1.00 71.16           O  
HETATM 3613  O   HOH A 388       9.326  38.331  22.360  1.00 62.79           O  
HETATM 3614  O   HOH A 389      -2.904  38.863  22.240  1.00 75.93           O  
HETATM 3615  O   HOH B 401      -3.020  14.531  59.383  1.00 56.69           O  
HETATM 3616  O   HOH B 402       4.344  20.777  25.205  1.00 44.09           O  
HETATM 3617  O   HOH B 403      -8.927  18.480  22.075  1.00 62.22           O  
HETATM 3618  O   HOH B 404      -7.464  26.803  29.072  1.00 58.26           O  
HETATM 3619  O   HOH B 405      -6.124  23.187  37.338  1.00 50.30           O  
HETATM 3620  O   HOH B 406      -1.222  21.012  38.532  1.00 46.10           O  
HETATM 3621  O   HOH B 407       0.067  30.380  39.603  1.00 68.09           O  
HETATM 3622  O   HOH B 408       4.775  22.380  27.620  1.00 51.39           O  
HETATM 3623  O   HOH B 409      11.375  18.113  29.996  1.00 51.97           O  
HETATM 3624  O   HOH B 410      13.284  20.276  27.618  1.00 48.41           O  
HETATM 3625  O   HOH B 411      19.643  15.735  28.407  1.00 49.55           O  
HETATM 3626  O   HOH B 412      17.112  15.103  29.945  1.00 40.75           O  
HETATM 3627  O   HOH B 413      -9.073   6.674  33.230  1.00 55.59           O  
HETATM 3628  O   HOH B 414       1.660   5.650  36.322  1.00 51.09           O  
HETATM 3629  O   HOH B 415      -2.871  21.073  26.379  1.00 59.14           O  
HETATM 3630  O   HOH B 416      22.955  17.517  23.776  1.00 49.86           O  
HETATM 3631  O   HOH B 417     -11.135  25.006  42.770  1.00 67.07           O  
HETATM 3632  O   HOH B 418     -10.972  24.667  48.142  1.00 79.25           O  
HETATM 3633  O   HOH B 419     -13.117  27.467  39.954  1.00 62.06           O  
HETATM 3634  O   HOH B 420     -12.242  18.782  53.876  1.00 48.05           O  
HETATM 3635  O   HOH B 421      11.033  32.690  46.855  1.00 57.08           O  
HETATM 3636  O   HOH B 422       9.846  34.689  44.933  1.00 62.42           O  
HETATM 3637  O   HOH B 423      15.960   2.672  31.714  1.00 36.73           O  
HETATM 3638  O   HOH B 424      32.786   6.207  44.648  1.00 51.57           O  
HETATM 3639  O   HOH B 425      -6.212  11.924  60.138  1.00 61.61           O  
HETATM 3640  O   HOH B 426      31.538  23.999  44.339  1.00 60.56           O  
HETATM 3641  O   HOH B 427      15.884  14.003  40.256  1.00 54.38           O  
HETATM 3642  O   HOH B 428      16.003  15.395  36.377  1.00 44.12           O  
HETATM 3643  O   HOH B 429       5.495  22.295  36.885  1.00 64.56           O  
HETATM 3644  O   HOH B 430       7.220  20.471  37.973  1.00 54.75           O  
HETATM 3645  O   HOH B 431      27.576  19.437  48.777  1.00 77.87           O  
HETATM 3646  O   HOH B 432      27.129  23.043  35.915  1.00 43.26           O  
HETATM 3647  O   HOH B 433      27.293  26.653  38.876  1.00 58.32           O  
HETATM 3648  O   HOH B 434      -8.695  28.297  49.261  1.00 64.70           O  
HETATM 3649  O   HOH B 435       7.857  32.525  36.506  1.00 48.20           O  
HETATM 3650  O   HOH B 436      27.980   8.761  54.907  1.00 72.98           O  
HETATM 3651  O   HOH B 437      10.292  29.636  32.599  1.00 54.11           O  
HETATM 3652  O   HOH B 438      23.723  12.634  23.359  1.00 51.48           O  
HETATM 3653  O   HOH B 439      22.408  15.619  30.873  1.00 46.35           O  
HETATM 3654  O   HOH B 440      16.897  12.664  36.458  1.00 49.57           O  
HETATM 3655  O   HOH B 441      -1.551   8.549  32.068  1.00 47.24           O  
HETATM 3656  O   HOH B 442      12.213  33.738  39.475  1.00 54.93           O  
HETATM 3657  O   HOH B 443      17.036  28.743  32.200  1.00 53.88           O  
HETATM 3658  O   HOH B 444      18.625  12.224  23.770  1.00 47.74           O  
HETATM 3659  O   HOH B 445      27.996  32.396  36.121  1.00 55.27           O  
HETATM 3660  O   HOH B 446      -0.124   7.008  45.162  1.00 59.02           O  
HETATM 3661  O   HOH B 447     -11.156   9.292  38.979  1.00 65.21           O  
HETATM 3662  O   HOH B 448     -11.344  13.657  38.585  1.00 61.88           O  
HETATM 3663  O   HOH B 449      12.063   8.734  27.314  1.00 59.14           O  
HETATM 3664  O   HOH B 450      25.709  -0.374  39.476  1.00 64.42           O  
HETATM 3665  O   HOH B 451      19.712  15.920  31.166  1.00 78.62           O  
HETATM 3666  O   HOH B 452       9.751  16.389  44.479  1.00 48.22           O  
HETATM 3667  O   HOH B 453      21.944  34.317  44.115  1.00 65.23           O  
HETATM 3668  O   HOH B 454       6.136  18.464  36.018  1.00 57.84           O  
HETATM 3669  O   HOH B 455      -2.433   3.318  47.144  1.00 65.86           O  
HETATM 3670  O   HOH B 456      -3.009  15.096  37.521  1.00 69.90           O  
HETATM 3671  O   HOH B 457     -12.088  21.051  34.575  1.00 63.06           O  
HETATM 3672  O   HOH B 458      22.613  30.173  44.700  1.00 56.89           O  
HETATM 3673  O   HOH B 459      -9.803  20.287  47.426  1.00 65.58           O  
HETATM 3674  O   HOH B 460      29.536  29.304  38.388  1.00 77.08           O  
HETATM 3675  O   HOH B 461     -11.992  12.622  42.356  1.00 56.80           O  
HETATM 3676  O   HOH B 462      25.637  14.634  23.793  1.00 56.11           O  
HETATM 3677  O   HOH B 463      34.585  10.291  41.809  1.00 83.48           O  
HETATM 3678  O   HOH B 464       7.048  22.238  52.161  1.00 57.50           O  
HETATM 3679  O   HOH B 465       5.612   8.147  53.410  1.00 72.44           O  
HETATM 3680  O   HOH B 466       7.914   5.578  45.180  1.00 60.02           O  
CONECT  450  459                                                                
CONECT  459  450  460                                                           
CONECT  460  459  461  463                                                      
CONECT  461  460  462                                                           
CONECT  462  461                                                                
CONECT  463  460  464  465                                                      
CONECT  464  463  468                                                           
CONECT  465  463  466  469                                                      
CONECT  466  465  467  468                                                      
CONECT  467  466                                                                
CONECT  468  464  466  472                                                      
CONECT  469  465  470                                                           
CONECT  470  469  471  480                                                      
CONECT  471  470                                                                
CONECT  472  468  473                                                           
CONECT  473  472  474  475                                                      
CONECT  474  473  476                                                           
CONECT  475  473  477                                                           
CONECT  476  474  478                                                           
CONECT  477  475  478                                                           
CONECT  478  476  477  479                                                      
CONECT  479  478                                                                
CONECT  480  470                                                                
CONECT 2210 2219                                                                
CONECT 2219 2210 2220                                                           
CONECT 2220 2219 2221 2223                                                      
CONECT 2221 2220 2222                                                           
CONECT 2222 2221                                                                
CONECT 2223 2220 2224 2225                                                      
CONECT 2224 2223 2228                                                           
CONECT 2225 2223 2226 2229                                                      
CONECT 2226 2225 2227 2228                                                      
CONECT 2227 2226                                                                
CONECT 2228 2224 2226 2232                                                      
CONECT 2229 2225 2230                                                           
CONECT 2230 2229 2231 2240                                                      
CONECT 2231 2230                                                                
CONECT 2232 2228 2233                                                           
CONECT 2233 2232 2234 2235                                                      
CONECT 2234 2233 2236                                                           
CONECT 2235 2233 2237                                                           
CONECT 2236 2234 2238                                                           
CONECT 2237 2235 2238                                                           
CONECT 2238 2236 2237 2239                                                      
CONECT 2239 2238                                                                
CONECT 2240 2230                                                                
MASTER      423    0    3   10   24    0    2    6 3675    2   46   38          
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.