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.


***  2HAD_3umb  ***

elNémo ID: 21082211554969913

Job options:

ID        	=	 21082211554969913
JOBID     	=	 2HAD_3umb
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 2HAD_3umb

HEADER    HYDROLASE                               12-NOV-11   3UMB              
TITLE     CRYSTAL STRUCTURE OF THE L-2-HALOACID DEHALOGENASE RSC1362            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEHALOGENASE-LIKE HYDROLASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: L-2-HALOACID DEHALOGENASE RSC1362;                          
COMPND   5 EC: 3.8.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RALSTONIA SOLANACEARUM;                         
SOURCE   3 ORGANISM_TAXID: 305;                                                 
SOURCE   4 GENE: RSC1362;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P15TV-L                                   
KEYWDS    HALOACID DEHALOGENASE-LIKE HYDROLASE PROTEIN SUPERFAMILY, HYDROLASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.PETIT,P.W.Y.CHAN,A.SAVCHENKO,A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI        
REVDAT   1   14-NOV-12 3UMB    0                                                
JRNL        AUTH   P.W.Y.CHAN,T.K.W.TO,P.PETIT,C.TRAN,M.WAELTI,A.SAVCHENKO,     
JRNL        AUTH 2 A.F.YAKUNIN,E.A.EDWARDS,E.F.PAI                              
JRNL        TITL   STRUCTURAL ADAPTATIONS OF L-2-HALOACID DEHALOGENASES THAT    
JRNL        TITL 2 ENABLE HYDROLYTIC DEFLUORINATION                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12255                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 585                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 840                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 42                           
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1751                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 69                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82000                                              
REMARK   3    B22 (A**2) : -1.53000                                             
REMARK   3    B33 (A**2) : 0.71000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.334         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.250         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.208         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.389         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1799 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1203 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2454 ; 1.609 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2904 ; 0.978 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   226 ; 6.821 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    80 ;34.694 ;22.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   264 ;16.820 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;15.977 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   269 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2038 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   396 ; 0.001 ; 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):  1131 ; 0.855 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   456 ; 0.166 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1804 ; 1.573 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   668 ; 2.282 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   650 ; 3.377 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 3UMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068932.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-10                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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 FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX OPTICS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12258                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.785                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200   FOR THE DATA SET  : 26.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21400                            
REMARK 200   FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QH9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% ISOPROPANOL, 0.1 M POTASSIUM         
REMARK 280  CHLORIDE, 25 MM MAGNESIUM CHLORIDE, 2% 1,4-DIOXANE, 50 MM SODIUM    
REMARK 280  CACODYLATE, PH 6.0, CRYOPROTECTANT: PARATONE N, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.19000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       64.78500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.19000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       64.78500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.19000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       64.78500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.19000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       64.78500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       54.30000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 K      K A 234  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 306  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG A 240  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG A 241  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 255  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 248  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL A 236  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 305  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A     1                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     MSE A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  11      -80.50    -87.29                                   
REMARK 500    THR A  14      -66.27   -107.85                                   
REMARK 500    PRO A 102      -34.57    -39.68                                   
REMARK 500    ALA A 136      -10.88    139.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 240  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  42   OD1                                                    
REMARK 620 2 HOH A 301   O    68.1                                              
REMARK 620 3 ASP A  46   OD1  96.7 127.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 241  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A  77   O                                                      
REMARK 620 2 ASN A  80   OD1  91.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 239  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 285   O                                                      
REMARK 620 2 HOH A 273   O   107.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 235                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 236                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 238                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 239                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 240                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 241                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UM9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DEFLUORINATING L-2-HALOACID                 
REMARK 900 DEHALOGENASE BPRO0530                                                
REMARK 900 RELATED ID: 3UMC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE L-2-HALOACID DEHALOGENASE PA0810            
REMARK 900 RELATED ID: 3UMG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DEFLUORINATING L-2-HALOACID                 
REMARK 900 DEHALOGENASE RHA0230                                                 
DBREF  3UMB A    1   233  UNP    Q8XZN3   Q8XZN3_RALSO     1    233             
SEQRES   1 A  233  MSE THR SER ILE ARG ALA VAL VAL PHE ASP ALA TYR GLY          
SEQRES   2 A  233  THR LEU PHE ASP VAL TYR SER VAL ALA ALA ARG ALA GLU          
SEQRES   3 A  233  GLN LEU PHE PRO GLY LYS GLY GLU ALA LEU SER VAL LEU          
SEQRES   4 A  233  TRP ARG ASP ARG GLN ILE ASP TYR THR ARG ILE ARG SER          
SEQRES   5 A  233  LEU ALA GLY PRO SER GLY GLU HIS TYR LYS PRO PHE TRP          
SEQRES   6 A  233  ASP VAL THR VAL ASP ALA LEU ARG TYR ALA CYS ALA ARG          
SEQRES   7 A  233  LEU ASN LEU PRO LEU GLY ASN HIS ALA GLU ALA THR LEU          
SEQRES   8 A  233  MSE ARG GLU TYR ALA CYS LEU SER ALA PHE PRO GLU ASN          
SEQRES   9 A  233  VAL PRO VAL LEU ARG GLN LEU ARG GLU MSE GLY LEU PRO          
SEQRES  10 A  233  LEU GLY ILE LEU SER ASN GLY ASN PRO GLN MSE LEU GLU          
SEQRES  11 A  233  ILE ALA VAL LYS SER ALA GLY MSE SER GLY LEU PHE ASP          
SEQRES  12 A  233  HIS VAL LEU SER VAL ASP ALA VAL ARG LEU TYR LYS THR          
SEQRES  13 A  233  ALA PRO ALA ALA TYR ALA LEU ALA PRO ARG ALA PHE GLY          
SEQRES  14 A  233  VAL PRO ALA ALA GLN ILE LEU PHE VAL SER SER ASN GLY          
SEQRES  15 A  233  TRP ASP ALA CYS GLY ALA THR TRP HIS GLY PHE THR THR          
SEQRES  16 A  233  PHE TRP ILE ASN ARG LEU GLY HIS PRO PRO GLU ALA LEU          
SEQRES  17 A  233  ASP VAL ALA PRO ALA ALA ALA GLY HIS ASP MSE ARG ASP          
SEQRES  18 A  233  LEU LEU GLN PHE VAL GLN ALA ARG GLN SER MSE ARG              
MODRES 3UMB MSE A   92  MET  SELENOMETHIONINE                                   
MODRES 3UMB MSE A  114  MET  SELENOMETHIONINE                                   
MODRES 3UMB MSE A  128  MET  SELENOMETHIONINE                                   
MODRES 3UMB MSE A  138  MET  SELENOMETHIONINE                                   
MODRES 3UMB MSE A  219  MET  SELENOMETHIONINE                                   
HET    MSE  A  92       8                                                       
HET    MSE  A 114       8                                                       
HET    MSE  A 128       8                                                       
HET    MSE  A 138       8                                                       
HET    MSE  A 219       8                                                       
HET      K  A 234       1                                                       
HET      K  A 235       1                                                       
HET     CL  A 236       1                                                       
HET     CL  A 237       1                                                       
HET     CL  A 238       1                                                       
HET     NA  A 239       1                                                       
HET     MG  A 240       1                                                       
HET     MG  A 241       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM       K POTASSIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2    K    2(K 1+)                                                      
FORMUL   4   CL    3(CL 1-)                                                     
FORMUL   7   NA    NA 1+                                                        
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL  10  HOH   *69(H2 O)                                                     
HELIX    1   1 VAL A   18  PHE A   29  1                                  12    
HELIX    2   2 LYS A   32  GLY A   55  1                                  24    
HELIX    3   3 PRO A   63  LEU A   79  1                                  17    
HELIX    4   4 GLY A   84  CYS A   97  1                                  14    
HELIX    5   5 GLU A  103  GLU A  113  1                                  11    
HELIX    6   6 ASN A  125  SER A  135  1                                  11    
HELIX    7   7 ALA A  157  ALA A  162  1                                   6    
HELIX    8   8 ALA A  162  GLY A  169  1                                   8    
HELIX    9   9 PRO A  171  ALA A  173  5                                   3    
HELIX   10  10 ASN A  181  GLY A  192  1                                  12    
HELIX   11  11 ASP A  218  ALA A  228  1                                  11    
SHEET    1   A 6 HIS A 144  SER A 147  0                                        
SHEET    2   A 6 LEU A 118  SER A 122  1  N  ILE A 120   O  LEU A 146           
SHEET    3   A 6 ALA A   6  PHE A   9  1  N  PHE A   9   O  GLY A 119           
SHEET    4   A 6 ILE A 175  SER A 179  1  O  LEU A 176   N  ALA A   6           
SHEET    5   A 6 THR A 194  ILE A 198  1  O  THR A 194   N  PHE A 177           
SHEET    6   A 6 ALA A 214  GLY A 216  1  O  GLY A 216   N  TRP A 197           
SHEET    1   B 2 PHE A  16  ASP A  17  0                                        
SHEET    2   B 2 SER A  99  ALA A 100 -1  O  SER A  99   N  ASP A  17           
LINK         C   LEU A  91                 N   MSE A  92     1555   1555  1.32  
LINK         C   MSE A  92                 N   ARG A  93     1555   1555  1.34  
LINK         C   GLU A 113                 N   MSE A 114     1555   1555  1.34  
LINK         C   MSE A 114                 N   GLY A 115     1555   1555  1.34  
LINK         C   GLN A 127                 N   MSE A 128     1555   1555  1.34  
LINK         C   MSE A 128                 N   LEU A 129     1555   1555  1.32  
LINK         C   GLY A 137                 N   MSE A 138     1555   1555  1.33  
LINK         C   MSE A 138                 N   SER A 139     1555   1555  1.34  
LINK         C   ASP A 218                 N   MSE A 219     1555   1555  1.32  
LINK         C   MSE A 219                 N   ARG A 220     1555   1555  1.32  
LINK         OD1 ASP A  42                MG    MG A 240     1555   1555  2.30  
LINK         O   ALA A  77                MG    MG A 241     1555   1555  2.36  
LINK        MG    MG A 240                 O   HOH A 301     1555   1555  2.37  
LINK         OD1 ASN A  80                MG    MG A 241     1555   1555  2.48  
LINK         OG  SER A  57                 K     K A 235     1555   1555  2.85  
LINK        NA    NA A 239                 O   HOH A 285     1555   1555  2.93  
LINK         OD1 ASP A  46                MG    MG A 240     1555   1555  2.96  
LINK        NA    NA A 239                 O   HOH A 273     1555   1555  3.09  
CISPEP   1 LYS A  155    THR A  156          0        10.70                     
SITE     1 AC1  4 SER A  57  PRO A 158  ALA A 159  HOH A 275                    
SITE     1 AC2  2 PRO A  56  HOH A 258                                          
SITE     1 AC3  3 ASP A  46  ARG A  49  TRP A 183                               
SITE     1 AC4  4 PRO A 165  HIS A 191  HOH A 273  HOH A 285                    
SITE     1 AC5  4 ASP A  42  ASP A  46  HOH A 286  HOH A 301                    
SITE     1 AC6  2 ALA A  77  ASN A  80                                          
CRYST1   66.380  129.570   54.300  90.00  90.00  90.00 C 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015065  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007718  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018416        0.00000                         
ATOM      1  N   THR A   2      28.482   6.583  21.317  1.00 49.69           N  
ATOM      2  CA  THR A   2      28.213   5.563  20.246  1.00 49.39           C  
ATOM      3  C   THR A   2      28.059   6.216  18.860  1.00 49.31           C  
ATOM      4  O   THR A   2      27.652   7.379  18.765  1.00 49.37           O  
ATOM      5  CB  THR A   2      26.989   4.670  20.627  1.00 49.24           C  
ATOM      6  OG1 THR A   2      26.553   3.915  19.496  1.00 48.07           O  
ATOM      7  CG2 THR A   2      25.858   5.515  21.171  1.00 49.79           C  
ATOM      8  N   SER A   3      28.408   5.461  17.805  1.00 48.83           N  
ATOM      9  CA  SER A   3      28.485   5.959  16.403  1.00 48.26           C  
ATOM     10  C   SER A   3      27.143   6.221  15.692  1.00 47.50           C  
ATOM     11  O   SER A   3      26.360   5.286  15.468  1.00 48.46           O  
ATOM     12  CB  SER A   3      29.255   4.948  15.544  1.00 48.43           C  
ATOM     13  OG  SER A   3      30.603   4.845  15.950  1.00 49.38           O  
ATOM     14  N   ILE A   4      26.900   7.471  15.288  1.00 46.00           N  
ATOM     15  CA  ILE A   4      25.693   7.818  14.504  1.00 44.46           C  
ATOM     16  C   ILE A   4      25.791   7.158  13.151  1.00 43.55           C  
ATOM     17  O   ILE A   4      26.824   7.254  12.511  1.00 43.27           O  
ATOM     18  CB  ILE A   4      25.595   9.330  14.227  1.00 43.94           C  
ATOM     19  CG1 ILE A   4      25.550  10.115  15.532  1.00 45.25           C  
ATOM     20  CG2 ILE A   4      24.400   9.669  13.350  1.00 42.53           C  
ATOM     21  CD1 ILE A   4      26.529  11.306  15.547  1.00 46.17           C  
ATOM     22  N   ARG A   5      24.723   6.501  12.716  1.00 42.11           N  
ATOM     23  CA  ARG A   5      24.672   5.908  11.391  1.00 41.70           C  
ATOM     24  C   ARG A   5      23.490   6.344  10.552  1.00 39.71           C  
ATOM     25  O   ARG A   5      23.297   5.826   9.453  1.00 40.08           O  
ATOM     26  CB  ARG A   5      24.684   4.388  11.504  1.00 42.38           C  
ATOM     27  CG  ARG A   5      25.735   3.898  12.493  1.00 46.11           C  
ATOM     28  CD  ARG A   5      26.539   2.756  11.950  1.00 50.54           C  
ATOM     29  NE  ARG A   5      25.668   1.640  11.609  1.00 53.69           N  
ATOM     30  CZ  ARG A   5      25.980   0.356  11.766  1.00 57.22           C  
ATOM     31  NH1 ARG A   5      25.082  -0.577  11.428  1.00 58.59           N  
ATOM     32  NH2 ARG A   5      27.165  -0.007  12.265  1.00 57.26           N  
ATOM     33  N   ALA A   6      22.723   7.297  11.079  1.00 37.42           N  
ATOM     34  CA  ALA A   6      21.524   7.836  10.457  1.00 35.20           C  
ATOM     35  C   ALA A   6      21.046   9.059  11.258  1.00 33.50           C  
ATOM     36  O   ALA A   6      21.380   9.242  12.421  1.00 33.29           O  
ATOM     37  CB  ALA A   6      20.426   6.764  10.352  1.00 35.16           C  
ATOM     38  N   VAL A   7      20.283   9.926  10.632  1.00 31.96           N  
ATOM     39  CA  VAL A   7      19.860  11.145  11.308  1.00 31.33           C  
ATOM     40  C   VAL A   7      18.413  11.371  10.932  1.00 30.24           C  
ATOM     41  O   VAL A   7      18.072  11.415   9.747  1.00 30.70           O  
ATOM     42  CB  VAL A   7      20.767  12.354  10.926  1.00 31.64           C  
ATOM     43  CG1 VAL A   7      20.318  13.678  11.592  1.00 30.33           C  
ATOM     44  CG2 VAL A   7      22.255  12.026  11.283  1.00 32.77           C  
ATOM     45  N   VAL A   8      17.563  11.479  11.948  1.00 28.73           N  
ATOM     46  CA  VAL A   8      16.116  11.648  11.747  1.00 27.29           C  
ATOM     47  C   VAL A   8      15.659  13.013  12.310  1.00 26.41           C  
ATOM     48  O   VAL A   8      16.101  13.417  13.381  1.00 25.92           O  
ATOM     49  CB  VAL A   8      15.325  10.473  12.394  1.00 26.84           C  
ATOM     50  CG1 VAL A   8      13.821  10.716  12.332  1.00 24.59           C  
ATOM     51  CG2 VAL A   8      15.700   9.142  11.688  1.00 26.96           C  
ATOM     52  N   PHE A   9      14.800  13.688  11.553  1.00 26.02           N  
ATOM     53  CA  PHE A   9      14.289  14.995  11.886  1.00 26.59           C  
ATOM     54  C   PHE A   9      12.800  14.963  12.188  1.00 26.33           C  
ATOM     55  O   PHE A   9      12.034  14.301  11.514  1.00 26.53           O  
ATOM     56  CB  PHE A   9      14.498  15.974  10.716  1.00 27.22           C  
ATOM     57  CG  PHE A   9      15.938  16.238  10.397  1.00 28.00           C  
ATOM     58  CD1 PHE A   9      16.600  15.463   9.441  1.00 30.81           C  
ATOM     59  CD2 PHE A   9      16.619  17.263  11.020  1.00 30.51           C  
ATOM     60  CE1 PHE A   9      17.940  15.710   9.131  1.00 33.33           C  
ATOM     61  CE2 PHE A   9      17.971  17.526  10.740  1.00 32.38           C  
ATOM     62  CZ  PHE A   9      18.634  16.754   9.785  1.00 33.28           C  
ATOM     63  N   ASP A  10      12.436  15.703  13.219  1.00 26.79           N  
ATOM     64  CA  ASP A  10      11.107  16.294  13.421  1.00 27.40           C  
ATOM     65  C   ASP A  10      10.793  17.269  12.258  1.00 27.61           C  
ATOM     66  O   ASP A  10      11.690  17.808  11.610  1.00 27.09           O  
ATOM     67  CB  ASP A  10      11.207  17.072  14.730  1.00 28.78           C  
ATOM     68  CG  ASP A  10       9.916  17.683  15.163  1.00 31.71           C  
ATOM     69  OD1 ASP A  10       8.848  17.059  14.913  1.00 35.81           O  
ATOM     70  OD2 ASP A  10       9.991  18.792  15.760  1.00 35.05           O  
ATOM     71  N   ALA A  11       9.527  17.504  11.995  1.00 28.35           N  
ATOM     72  CA  ALA A  11       9.123  18.343  10.874  1.00 30.07           C  
ATOM     73  C   ALA A  11       9.049  19.881  11.220  1.00 30.95           C  
ATOM     74  O   ALA A  11       9.974  20.688  10.944  1.00 31.28           O  
ATOM     75  CB  ALA A  11       7.720  17.798  10.292  1.00 29.60           C  
ATOM     76  N   TYR A  12       7.945  20.235  11.838  1.00 32.98           N  
ATOM     77  CA  TYR A  12       7.550  21.611  12.152  1.00 35.04           C  
ATOM     78  C   TYR A  12       8.495  22.304  13.134  1.00 35.93           C  
ATOM     79  O   TYR A  12       8.842  21.738  14.159  1.00 36.20           O  
ATOM     80  CB  TYR A  12       6.130  21.544  12.711  1.00 35.25           C  
ATOM     81  CG  TYR A  12       5.185  20.845  11.751  1.00 37.94           C  
ATOM     82  CD1 TYR A  12       5.006  21.349  10.457  1.00 41.31           C  
ATOM     83  CD2 TYR A  12       4.510  19.669  12.091  1.00 40.78           C  
ATOM     84  CE1 TYR A  12       4.149  20.730   9.516  1.00 42.69           C  
ATOM     85  CE2 TYR A  12       3.637  19.013  11.129  1.00 42.19           C  
ATOM     86  CZ  TYR A  12       3.458  19.569   9.836  1.00 42.99           C  
ATOM     87  OH  TYR A  12       2.644  19.004   8.822  1.00 40.91           O  
ATOM     88  N   GLY A  13       8.936  23.522  12.790  1.00 37.19           N  
ATOM     89  CA  GLY A  13       9.863  24.291  13.637  1.00 37.15           C  
ATOM     90  C   GLY A  13      11.310  23.827  13.502  1.00 38.32           C  
ATOM     91  O   GLY A  13      12.253  24.510  13.948  1.00 37.60           O  
ATOM     92  N   THR A  14      11.505  22.664  12.870  1.00 39.13           N  
ATOM     93  CA  THR A  14      12.827  22.062  12.748  1.00 39.91           C  
ATOM     94  C   THR A  14      13.247  22.224  11.278  1.00 40.87           C  
ATOM     95  O   THR A  14      14.173  22.975  10.926  1.00 40.37           O  
ATOM     96  CB  THR A  14      12.768  20.557  13.181  1.00 39.80           C  
ATOM     97  OG1 THR A  14      12.276  20.437  14.541  1.00 40.72           O  
ATOM     98  CG2 THR A  14      14.112  19.890  13.024  1.00 38.38           C  
ATOM     99  N   LEU A  15      12.509  21.531  10.417  1.00 42.26           N  
ATOM    100  CA  LEU A  15      12.760  21.545   8.987  1.00 42.33           C  
ATOM    101  C   LEU A  15      11.999  22.684   8.354  1.00 42.61           C  
ATOM    102  O   LEU A  15      12.538  23.375   7.468  1.00 41.65           O  
ATOM    103  CB  LEU A  15      12.315  20.222   8.370  1.00 42.46           C  
ATOM    104  CG  LEU A  15      13.212  19.055   8.757  1.00 41.35           C  
ATOM    105  CD1 LEU A  15      12.631  17.777   8.207  1.00 38.92           C  
ATOM    106  CD2 LEU A  15      14.651  19.304   8.275  1.00 39.10           C  
ATOM    107  N   PHE A  16      10.758  22.838   8.827  1.00 42.79           N  
ATOM    108  CA  PHE A  16       9.794  23.782   8.307  1.00 43.64           C  
ATOM    109  C   PHE A  16       9.472  24.947   9.262  1.00 43.89           C  
ATOM    110  O   PHE A  16       8.938  24.721  10.357  1.00 44.79           O  
ATOM    111  CB  PHE A  16       8.454  23.085   8.073  1.00 44.15           C  
ATOM    112  CG  PHE A  16       8.535  21.768   7.362  1.00 46.30           C  
ATOM    113  CD1 PHE A  16       9.476  21.526   6.374  1.00 47.64           C  
ATOM    114  CD2 PHE A  16       7.607  20.773   7.661  1.00 48.59           C  
ATOM    115  CE1 PHE A  16       9.508  20.295   5.725  1.00 49.18           C  
ATOM    116  CE2 PHE A  16       7.619  19.553   7.008  1.00 48.80           C  
ATOM    117  CZ  PHE A  16       8.573  19.309   6.041  1.00 49.57           C  
ATOM    118  N   ASP A  17       9.713  26.184   8.821  1.00 43.89           N  
ATOM    119  CA  ASP A  17       9.308  27.382   9.586  1.00 43.95           C  
ATOM    120  C   ASP A  17       7.775  27.540   9.549  1.00 44.36           C  
ATOM    121  O   ASP A  17       7.190  27.795   8.470  1.00 44.83           O  
ATOM    122  CB  ASP A  17      10.042  28.644   9.047  1.00 43.88           C  
ATOM    123  CG  ASP A  17       9.995  29.859  10.012  1.00 43.74           C  
ATOM    124  OD1 ASP A  17       9.104  29.918  10.907  1.00 43.09           O  
ATOM    125  OD2 ASP A  17      10.862  30.769   9.851  1.00 41.71           O  
ATOM    126  N   VAL A  18       7.141  27.361  10.716  1.00 44.16           N  
ATOM    127  CA  VAL A  18       5.684  27.570  10.929  1.00 44.45           C  
ATOM    128  C   VAL A  18       5.345  29.095  10.958  1.00 45.82           C  
ATOM    129  O   VAL A  18       4.171  29.513  10.941  1.00 44.75           O  
ATOM    130  CB  VAL A  18       5.266  26.847  12.281  1.00 44.47           C  
ATOM    131  CG1 VAL A  18       3.894  27.263  12.832  1.00 43.96           C  
ATOM    132  CG2 VAL A  18       5.321  25.389  12.098  1.00 44.19           C  
ATOM    133  N   TYR A  19       6.382  29.943  10.996  1.00 47.28           N  
ATOM    134  CA  TYR A  19       6.177  31.394  11.094  1.00 48.26           C  
ATOM    135  C   TYR A  19       5.020  31.904  10.207  1.00 48.18           C  
ATOM    136  O   TYR A  19       4.164  32.685  10.676  1.00 48.92           O  
ATOM    137  CB  TYR A  19       7.475  32.177  10.796  1.00 48.83           C  
ATOM    138  CG  TYR A  19       7.306  33.635  11.077  1.00 52.08           C  
ATOM    139  CD1 TYR A  19       7.737  34.176  12.289  1.00 56.00           C  
ATOM    140  CD2 TYR A  19       6.662  34.477  10.158  1.00 54.72           C  
ATOM    141  CE1 TYR A  19       7.540  35.523  12.579  1.00 58.12           C  
ATOM    142  CE2 TYR A  19       6.460  35.821  10.435  1.00 56.28           C  
ATOM    143  CZ  TYR A  19       6.897  36.338  11.644  1.00 58.30           C  
ATOM    144  OH  TYR A  19       6.707  37.678  11.929  1.00 61.09           O  
ATOM    145  N   SER A  20       4.976  31.458   8.945  1.00 47.40           N  
ATOM    146  CA  SER A  20       4.066  32.062   7.968  1.00 46.68           C  
ATOM    147  C   SER A  20       2.591  31.912   8.329  1.00 45.30           C  
ATOM    148  O   SER A  20       1.751  32.557   7.717  1.00 45.61           O  
ATOM    149  CB  SER A  20       4.338  31.532   6.549  1.00 47.04           C  
ATOM    150  OG  SER A  20       4.004  30.140   6.407  1.00 48.66           O  
ATOM    151  N   VAL A  21       2.270  31.069   9.308  1.00 44.30           N  
ATOM    152  CA  VAL A  21       0.884  30.885   9.714  1.00 43.55           C  
ATOM    153  C   VAL A  21       0.485  31.988  10.684  1.00 43.79           C  
ATOM    154  O   VAL A  21      -0.598  32.573  10.564  1.00 42.70           O  
ATOM    155  CB  VAL A  21       0.625  29.494  10.329  1.00 43.82           C  
ATOM    156  CG1 VAL A  21      -0.818  29.357  10.692  1.00 42.99           C  
ATOM    157  CG2 VAL A  21       1.033  28.366   9.357  1.00 43.15           C  
ATOM    158  N   ALA A  22       1.369  32.307  11.624  1.00 44.59           N  
ATOM    159  CA  ALA A  22       1.096  33.385  12.578  1.00 44.88           C  
ATOM    160  C   ALA A  22       0.813  34.686  11.822  1.00 45.33           C  
ATOM    161  O   ALA A  22      -0.214  35.342  12.056  1.00 45.45           O  
ATOM    162  CB  ALA A  22       2.257  33.531  13.545  1.00 45.28           C  
ATOM    163  N   ALA A  23       1.678  34.995  10.847  1.00 46.09           N  
ATOM    164  CA  ALA A  23       1.557  36.194   9.989  1.00 45.93           C  
ATOM    165  C   ALA A  23       0.252  36.303   9.180  1.00 45.80           C  
ATOM    166  O   ALA A  23      -0.283  37.389   8.977  1.00 46.32           O  
ATOM    167  CB  ALA A  23       2.756  36.259   9.052  1.00 46.16           C  
ATOM    168  N   ARG A  24      -0.246  35.180   8.709  1.00 46.02           N  
ATOM    169  CA  ARG A  24      -1.502  35.119   7.956  1.00 46.59           C  
ATOM    170  C   ARG A  24      -2.745  35.133   8.877  1.00 46.61           C  
ATOM    171  O   ARG A  24      -3.862  35.454   8.454  1.00 45.27           O  
ATOM    172  CB  ARG A  24      -1.472  33.833   7.129  1.00 47.47           C  
ATOM    173  CG  ARG A  24      -2.815  33.291   6.647  1.00 50.10           C  
ATOM    174  CD  ARG A  24      -3.401  34.153   5.578  1.00 53.88           C  
ATOM    175  NE  ARG A  24      -2.723  33.922   4.308  1.00 57.00           N  
ATOM    176  CZ  ARG A  24      -2.996  34.583   3.189  1.00 60.06           C  
ATOM    177  NH1 ARG A  24      -3.931  35.544   3.182  1.00 60.52           N  
ATOM    178  NH2 ARG A  24      -2.328  34.286   2.078  1.00 60.40           N  
ATOM    179  N   ALA A  25      -2.531  34.741  10.130  1.00 46.79           N  
ATOM    180  CA  ALA A  25      -3.557  34.818  11.167  1.00 47.47           C  
ATOM    181  C   ALA A  25      -3.858  36.297  11.434  1.00 47.40           C  
ATOM    182  O   ALA A  25      -4.986  36.733  11.277  1.00 48.11           O  
ATOM    183  CB  ALA A  25      -3.090  34.082  12.448  1.00 46.73           C  
ATOM    184  N   GLU A  26      -2.824  37.059  11.769  1.00 48.05           N  
ATOM    185  CA  GLU A  26      -2.896  38.527  11.863  1.00 48.28           C  
ATOM    186  C   GLU A  26      -3.720  39.172  10.784  1.00 48.29           C  
ATOM    187  O   GLU A  26      -4.456  40.100  11.058  1.00 49.27           O  
ATOM    188  CB  GLU A  26      -1.498  39.157  11.782  1.00 48.63           C  
ATOM    189  CG  GLU A  26      -0.752  39.313  13.116  1.00 48.99           C  
ATOM    190  CD  GLU A  26      -1.539  40.142  14.167  1.00 49.93           C  
ATOM    191  OE1 GLU A  26      -2.417  40.966  13.748  1.00 46.27           O  
ATOM    192  OE2 GLU A  26      -1.260  39.942  15.399  1.00 46.91           O  
ATOM    193  N   GLN A  27      -3.595  38.713   9.547  1.00 48.10           N  
ATOM    194  CA  GLN A  27      -4.266  39.397   8.456  1.00 47.59           C  
ATOM    195  C   GLN A  27      -5.748  39.120   8.441  1.00 46.37           C  
ATOM    196  O   GLN A  27      -6.522  39.959   7.960  1.00 46.71           O  
ATOM    197  CB  GLN A  27      -3.660  38.994   7.095  1.00 48.88           C  
ATOM    198  CG  GLN A  27      -4.191  39.803   5.867  1.00 50.66           C  
ATOM    199  CD  GLN A  27      -5.639  39.449   5.439  1.00 53.69           C  
ATOM    200  OE1 GLN A  27      -6.098  38.310   5.615  1.00 56.10           O  
ATOM    201  NE2 GLN A  27      -6.352  40.432   4.867  1.00 53.39           N  
ATOM    202  N   LEU A  28      -6.161  37.934   8.881  1.00 44.33           N  
ATOM    203  CA  LEU A  28      -7.587  37.618   8.886  1.00 43.30           C  
ATOM    204  C   LEU A  28      -8.243  38.136  10.176  1.00 41.78           C  
ATOM    205  O   LEU A  28      -9.455  38.349  10.206  1.00 40.79           O  
ATOM    206  CB  LEU A  28      -7.815  36.110   8.754  1.00 43.69           C  
ATOM    207  CG  LEU A  28      -7.349  35.391   7.470  1.00 44.60           C  
ATOM    208  CD1 LEU A  28      -6.577  34.112   7.831  1.00 44.66           C  
ATOM    209  CD2 LEU A  28      -8.505  35.083   6.466  1.00 43.30           C  
ATOM    210  N   PHE A  29      -7.411  38.324  11.207  1.00 40.11           N  
ATOM    211  CA  PHE A  29      -7.829  38.594  12.580  1.00 39.61           C  
ATOM    212  C   PHE A  29      -6.895  39.635  13.150  1.00 39.70           C  
ATOM    213  O   PHE A  29      -5.940  39.298  13.870  1.00 39.46           O  
ATOM    214  CB  PHE A  29      -7.753  37.319  13.426  1.00 38.84           C  
ATOM    215  CG  PHE A  29      -8.638  36.226  12.926  1.00 35.46           C  
ATOM    216  CD1 PHE A  29      -9.973  36.477  12.647  1.00 30.95           C  
ATOM    217  CD2 PHE A  29      -8.144  34.946  12.741  1.00 32.43           C  
ATOM    218  CE1 PHE A  29     -10.807  35.459  12.164  1.00 32.89           C  
ATOM    219  CE2 PHE A  29      -8.975  33.912  12.291  1.00 32.78           C  
ATOM    220  CZ  PHE A  29     -10.306  34.159  11.998  1.00 31.19           C  
ATOM    221  N   PRO A  30      -7.154  40.910  12.814  1.00 39.85           N  
ATOM    222  CA  PRO A  30      -6.225  41.969  13.149  1.00 40.11           C  
ATOM    223  C   PRO A  30      -6.150  42.187  14.665  1.00 40.50           C  
ATOM    224  O   PRO A  30      -7.185  42.212  15.355  1.00 39.84           O  
ATOM    225  CB  PRO A  30      -6.811  43.189  12.435  1.00 40.64           C  
ATOM    226  CG  PRO A  30      -7.853  42.676  11.518  1.00 40.37           C  
ATOM    227  CD  PRO A  30      -8.345  41.421  12.125  1.00 39.90           C  
ATOM    228  N   GLY A  31      -4.920  42.320  15.150  1.00 40.94           N  
ATOM    229  CA  GLY A  31      -4.624  42.370  16.574  1.00 41.78           C  
ATOM    230  C   GLY A  31      -4.621  41.030  17.332  1.00 42.14           C  
ATOM    231  O   GLY A  31      -4.275  41.015  18.498  1.00 41.74           O  
ATOM    232  N   LYS A  32      -4.978  39.917  16.681  1.00 42.73           N  
ATOM    233  CA  LYS A  32      -5.162  38.616  17.381  1.00 43.29           C  
ATOM    234  C   LYS A  32      -4.360  37.426  16.809  1.00 43.27           C  
ATOM    235  O   LYS A  32      -4.662  36.256  17.104  1.00 43.36           O  
ATOM    236  CB  LYS A  32      -6.661  38.266  17.419  1.00 43.29           C  
ATOM    237  CG  LYS A  32      -7.536  39.318  18.117  1.00 43.95           C  
ATOM    238  CD  LYS A  32      -7.244  39.416  19.625  1.00 45.76           C  
ATOM    239  CE  LYS A  32      -7.756  40.727  20.217  1.00 46.67           C  
ATOM    240  NZ  LYS A  32      -9.172  41.006  19.788  1.00 49.13           N  
ATOM    241  N   GLY A  33      -3.325  37.725  16.025  1.00 43.21           N  
ATOM    242  CA  GLY A  33      -2.538  36.712  15.342  1.00 42.73           C  
ATOM    243  C   GLY A  33      -1.578  35.993  16.268  1.00 42.52           C  
ATOM    244  O   GLY A  33      -1.491  34.769  16.261  1.00 42.96           O  
ATOM    245  N   GLU A  34      -0.844  36.732  17.072  1.00 41.69           N  
ATOM    246  CA  GLU A  34       0.114  36.080  17.934  1.00 41.61           C  
ATOM    247  C   GLU A  34      -0.634  35.278  19.021  1.00 40.30           C  
ATOM    248  O   GLU A  34      -0.144  34.228  19.455  1.00 39.50           O  
ATOM    249  CB  GLU A  34       1.071  37.094  18.538  1.00 42.21           C  
ATOM    250  CG  GLU A  34       2.399  36.542  19.089  1.00 45.43           C  
ATOM    251  CD  GLU A  34       3.229  37.644  19.795  1.00 49.82           C  
ATOM    252  OE1 GLU A  34       3.114  38.836  19.404  1.00 53.47           O  
ATOM    253  OE2 GLU A  34       3.995  37.335  20.739  1.00 52.19           O  
ATOM    254  N   ALA A  35      -1.816  35.771  19.436  1.00 37.65           N  
ATOM    255  CA  ALA A  35      -2.638  35.086  20.440  1.00 35.77           C  
ATOM    256  C   ALA A  35      -3.241  33.796  19.881  1.00 34.02           C  
ATOM    257  O   ALA A  35      -3.168  32.750  20.544  1.00 33.74           O  
ATOM    258  CB  ALA A  35      -3.738  35.995  20.961  1.00 35.25           C  
ATOM    259  N   LEU A  36      -3.836  33.869  18.682  1.00 31.86           N  
ATOM    260  CA  LEU A  36      -4.410  32.695  18.047  1.00 30.92           C  
ATOM    261  C   LEU A  36      -3.350  31.610  17.854  1.00 31.58           C  
ATOM    262  O   LEU A  36      -3.623  30.424  18.091  1.00 30.32           O  
ATOM    263  CB  LEU A  36      -5.028  33.026  16.684  1.00 30.24           C  
ATOM    264  CG  LEU A  36      -5.623  31.889  15.859  1.00 29.22           C  
ATOM    265  CD1 LEU A  36      -6.599  31.051  16.665  1.00 28.12           C  
ATOM    266  CD2 LEU A  36      -6.340  32.375  14.583  1.00 28.06           C  
ATOM    267  N   SER A  37      -2.162  32.038  17.404  1.00 31.14           N  
ATOM    268  CA  SER A  37      -1.179  31.114  16.892  1.00 31.40           C  
ATOM    269  C   SER A  37      -0.610  30.389  18.098  1.00 30.01           C  
ATOM    270  O   SER A  37      -0.559  29.166  18.111  1.00 29.92           O  
ATOM    271  CB  SER A  37      -0.123  31.812  16.006  1.00 31.36           C  
ATOM    272  OG  SER A  37       0.902  32.385  16.779  1.00 33.45           O  
ATOM    273  N   VAL A  38      -0.284  31.138  19.144  1.00 28.79           N  
ATOM    274  CA  VAL A  38       0.039  30.528  20.428  1.00 27.27           C  
ATOM    275  C   VAL A  38      -1.030  29.547  20.962  1.00 27.10           C  
ATOM    276  O   VAL A  38      -0.686  28.395  21.276  1.00 27.04           O  
ATOM    277  CB  VAL A  38       0.314  31.562  21.516  1.00 27.26           C  
ATOM    278  CG1 VAL A  38       0.677  30.841  22.803  1.00 25.56           C  
ATOM    279  CG2 VAL A  38       1.471  32.506  21.098  1.00 28.12           C  
ATOM    280  N   LEU A  39      -2.301  29.989  21.089  1.00 25.04           N  
ATOM    281  CA  LEU A  39      -3.354  29.130  21.647  1.00 23.92           C  
ATOM    282  C   LEU A  39      -3.554  27.892  20.793  1.00 23.37           C  
ATOM    283  O   LEU A  39      -3.758  26.813  21.310  1.00 22.33           O  
ATOM    284  CB  LEU A  39      -4.684  29.876  21.832  1.00 23.71           C  
ATOM    285  CG  LEU A  39      -5.845  29.119  22.452  1.00 22.02           C  
ATOM    286  CD1 LEU A  39      -5.423  28.480  23.771  1.00 17.33           C  
ATOM    287  CD2 LEU A  39      -7.099  30.040  22.577  1.00 16.54           C  
ATOM    288  N   TRP A  40      -3.424  28.065  19.484  1.00 23.53           N  
ATOM    289  CA  TRP A  40      -3.634  27.006  18.515  1.00 23.93           C  
ATOM    290  C   TRP A  40      -2.579  25.892  18.584  1.00 24.43           C  
ATOM    291  O   TRP A  40      -2.924  24.699  18.577  1.00 23.60           O  
ATOM    292  CB  TRP A  40      -3.619  27.633  17.151  1.00 24.14           C  
ATOM    293  CG  TRP A  40      -3.936  26.750  16.032  1.00 22.72           C  
ATOM    294  CD1 TRP A  40      -4.486  25.505  16.061  1.00 23.44           C  
ATOM    295  CD2 TRP A  40      -3.757  27.088  14.679  1.00 22.79           C  
ATOM    296  NE1 TRP A  40      -4.645  25.025  14.774  1.00 23.34           N  
ATOM    297  CE2 TRP A  40      -4.190  25.988  13.908  1.00 23.01           C  
ATOM    298  CE3 TRP A  40      -3.214  28.220  14.024  1.00 22.93           C  
ATOM    299  CZ2 TRP A  40      -4.123  25.987  12.512  1.00 23.80           C  
ATOM    300  CZ3 TRP A  40      -3.162  28.224  12.637  1.00 23.18           C  
ATOM    301  CH2 TRP A  40      -3.606  27.106  11.892  1.00 23.74           C  
ATOM    302  N   ARG A  41      -1.314  26.290  18.686  1.00 24.58           N  
ATOM    303  CA  ARG A  41      -0.208  25.344  18.860  1.00 25.31           C  
ATOM    304  C   ARG A  41      -0.331  24.607  20.200  1.00 23.98           C  
ATOM    305  O   ARG A  41      -0.208  23.384  20.247  1.00 23.39           O  
ATOM    306  CB  ARG A  41       1.137  26.063  18.729  1.00 26.08           C  
ATOM    307  CG  ARG A  41       2.403  25.192  18.916  1.00 30.51           C  
ATOM    308  CD  ARG A  41       2.503  23.995  17.909  1.00 33.15           C  
ATOM    309  NE  ARG A  41       3.697  23.176  18.179  1.00 36.57           N  
ATOM    310  CZ  ARG A  41       3.900  21.937  17.703  1.00 39.05           C  
ATOM    311  NH1 ARG A  41       2.993  21.339  16.915  1.00 38.14           N  
ATOM    312  NH2 ARG A  41       5.011  21.273  18.026  1.00 37.19           N  
ATOM    313  N   ASP A  42      -0.610  25.348  21.270  1.00 23.18           N  
ATOM    314  CA  ASP A  42      -0.882  24.753  22.574  1.00 22.27           C  
ATOM    315  C   ASP A  42      -1.935  23.661  22.475  1.00 20.54           C  
ATOM    316  O   ASP A  42      -1.700  22.531  22.883  1.00 19.68           O  
ATOM    317  CB  ASP A  42      -1.384  25.796  23.574  1.00 22.85           C  
ATOM    318  CG  ASP A  42      -1.560  25.230  25.017  1.00 25.92           C  
ATOM    319  OD1 ASP A  42      -0.518  24.893  25.662  1.00 27.83           O  
ATOM    320  OD2 ASP A  42      -2.735  25.144  25.505  1.00 26.87           O  
ATOM    321  N   ARG A  43      -3.108  23.997  21.969  1.00 18.32           N  
ATOM    322  CA  ARG A  43      -4.204  23.003  21.946  1.00 17.95           C  
ATOM    323  C   ARG A  43      -3.942  21.885  20.953  1.00 17.32           C  
ATOM    324  O   ARG A  43      -4.330  20.751  21.190  1.00 15.82           O  
ATOM    325  CB  ARG A  43      -5.596  23.640  21.765  1.00 17.44           C  
ATOM    326  CG  ARG A  43      -6.031  24.407  23.026  1.00 18.94           C  
ATOM    327  CD  ARG A  43      -6.143  23.452  24.212  1.00 18.64           C  
ATOM    328  NE  ARG A  43      -7.202  23.823  25.146  1.00 19.75           N  
ATOM    329  CZ  ARG A  43      -7.042  24.646  26.198  1.00 27.89           C  
ATOM    330  NH1 ARG A  43      -8.055  24.897  27.031  1.00 29.91           N  
ATOM    331  NH2 ARG A  43      -5.877  25.245  26.447  1.00 29.19           N  
ATOM    332  N   GLN A  44      -3.206  22.182  19.876  1.00 17.76           N  
ATOM    333  CA  GLN A  44      -2.888  21.130  18.906  1.00 18.24           C  
ATOM    334  C   GLN A  44      -2.100  20.012  19.588  1.00 17.42           C  
ATOM    335  O   GLN A  44      -2.454  18.850  19.522  1.00 17.91           O  
ATOM    336  CB  GLN A  44      -2.166  21.722  17.693  1.00 18.72           C  
ATOM    337  CG  GLN A  44      -1.600  20.735  16.719  1.00 20.56           C  
ATOM    338  CD  GLN A  44      -0.604  21.383  15.768  1.00 20.98           C  
ATOM    339  OE1 GLN A  44       0.345  22.020  16.216  1.00 21.54           O  
ATOM    340  NE2 GLN A  44      -0.860  21.277  14.444  1.00 17.29           N  
ATOM    341  N   ILE A  45      -1.075  20.403  20.312  1.00 18.23           N  
ATOM    342  CA  ILE A  45      -0.270  19.482  21.035  1.00 18.47           C  
ATOM    343  C   ILE A  45      -1.019  18.896  22.232  1.00 16.80           C  
ATOM    344  O   ILE A  45      -0.988  17.717  22.432  1.00 15.55           O  
ATOM    345  CB  ILE A  45       1.066  20.124  21.353  1.00 19.94           C  
ATOM    346  CG1 ILE A  45       1.856  20.265  20.058  1.00 22.59           C  
ATOM    347  CG2 ILE A  45       1.891  19.267  22.316  1.00 22.27           C  
ATOM    348  CD1 ILE A  45       2.165  18.871  19.363  1.00 24.80           C  
ATOM    349  N   ASP A  46      -1.728  19.706  22.996  1.00 15.84           N  
ATOM    350  CA  ASP A  46      -2.490  19.193  24.100  1.00 15.38           C  
ATOM    351  C   ASP A  46      -3.389  18.063  23.632  1.00 15.24           C  
ATOM    352  O   ASP A  46      -3.475  17.040  24.307  1.00 13.96           O  
ATOM    353  CB  ASP A  46      -3.368  20.276  24.695  1.00 16.50           C  
ATOM    354  CG  ASP A  46      -2.593  21.260  25.522  1.00 19.05           C  
ATOM    355  OD1 ASP A  46      -1.361  21.029  25.689  1.00 18.10           O  
ATOM    356  OD2 ASP A  46      -3.237  22.259  25.964  1.00 21.30           O  
ATOM    357  N   TYR A  47      -4.079  18.261  22.491  1.00 14.82           N  
ATOM    358  CA  TYR A  47      -5.034  17.285  21.988  1.00 14.00           C  
ATOM    359  C   TYR A  47      -4.377  15.991  21.552  1.00 13.32           C  
ATOM    360  O   TYR A  47      -4.936  14.939  21.784  1.00 12.71           O  
ATOM    361  CB  TYR A  47      -5.919  17.854  20.869  1.00 13.13           C  
ATOM    362  CG  TYR A  47      -6.952  18.911  21.299  1.00 15.15           C  
ATOM    363  CD1 TYR A  47      -7.221  19.195  22.661  1.00 15.80           C  
ATOM    364  CD2 TYR A  47      -7.709  19.590  20.357  1.00 16.95           C  
ATOM    365  CE1 TYR A  47      -8.181  20.184  23.046  1.00 13.56           C  
ATOM    366  CE2 TYR A  47      -8.675  20.576  20.736  1.00 13.90           C  
ATOM    367  CZ  TYR A  47      -8.907  20.845  22.070  1.00 15.86           C  
ATOM    368  OH  TYR A  47      -9.864  21.778  22.413  1.00 14.07           O  
ATOM    369  N   THR A  48      -3.183  16.036  20.970  1.00 13.56           N  
ATOM    370  CA  THR A  48      -2.497  14.770  20.597  1.00 12.80           C  
ATOM    371  C   THR A  48      -2.150  13.959  21.857  1.00 13.92           C  
ATOM    372  O   THR A  48      -2.312  12.763  21.878  1.00 13.91           O  
ATOM    373  CB  THR A  48      -1.208  15.023  19.821  1.00 12.58           C  
ATOM    374  OG1 THR A  48      -0.297  15.740  20.636  1.00 11.21           O  
ATOM    375  CG2 THR A  48      -1.465  15.801  18.518  1.00  9.73           C  
ATOM    376  N   ARG A  49      -1.668  14.630  22.901  1.00 13.35           N  
ATOM    377  CA  ARG A  49      -1.366  13.967  24.151  1.00 14.19           C  
ATOM    378  C   ARG A  49      -2.584  13.457  24.902  1.00 14.91           C  
ATOM    379  O   ARG A  49      -2.579  12.355  25.392  1.00 15.29           O  
ATOM    380  CB  ARG A  49      -0.630  14.907  25.057  1.00 13.82           C  
ATOM    381  CG  ARG A  49       0.727  15.278  24.514  1.00 14.08           C  
ATOM    382  CD  ARG A  49       1.290  16.387  25.307  1.00 13.68           C  
ATOM    383  NE  ARG A  49       2.629  16.739  24.878  1.00 12.33           N  
ATOM    384  CZ  ARG A  49       3.271  17.825  25.294  1.00 15.21           C  
ATOM    385  NH1 ARG A  49       2.686  18.702  26.143  1.00 19.72           N  
ATOM    386  NH2 ARG A  49       4.490  18.062  24.843  1.00 15.86           N  
ATOM    387  N   ILE A  50      -3.625  14.271  25.001  1.00 14.66           N  
ATOM    388  CA  ILE A  50      -4.834  13.864  25.684  1.00 14.43           C  
ATOM    389  C   ILE A  50      -5.347  12.569  25.052  1.00 14.91           C  
ATOM    390  O   ILE A  50      -5.653  11.596  25.754  1.00 16.37           O  
ATOM    391  CB  ILE A  50      -5.930  14.974  25.600  1.00 13.58           C  
ATOM    392  CG1 ILE A  50      -5.561  16.148  26.465  1.00 10.93           C  
ATOM    393  CG2 ILE A  50      -7.342  14.420  25.995  1.00 14.44           C  
ATOM    394  CD1 ILE A  50      -6.469  17.326  26.261  1.00  6.52           C  
ATOM    395  N   ARG A  51      -5.463  12.574  23.730  1.00 14.76           N  
ATOM    396  CA  ARG A  51      -5.881  11.394  22.967  1.00 14.54           C  
ATOM    397  C   ARG A  51      -5.024  10.142  23.144  1.00 14.55           C  
ATOM    398  O   ARG A  51      -5.567   9.042  23.312  1.00 15.95           O  
ATOM    399  CB  ARG A  51      -5.933  11.736  21.469  1.00 14.28           C  
ATOM    400  CG  ARG A  51      -7.067  12.728  21.130  1.00 15.30           C  
ATOM    401  CD  ARG A  51      -7.190  13.034  19.626  1.00 17.05           C  
ATOM    402  NE  ARG A  51      -8.398  13.796  19.309  1.00 17.21           N  
ATOM    403  CZ  ARG A  51      -9.621  13.288  19.223  1.00 19.59           C  
ATOM    404  NH1 ARG A  51      -9.819  11.988  19.380  1.00 20.81           N  
ATOM    405  NH2 ARG A  51     -10.655  14.087  18.958  1.00 20.82           N  
ATOM    406  N   SER A  52      -3.706  10.266  23.051  1.00 13.75           N  
ATOM    407  CA  SER A  52      -2.859   9.073  23.061  1.00 13.97           C  
ATOM    408  C   SER A  52      -2.746   8.525  24.478  1.00 15.11           C  
ATOM    409  O   SER A  52      -2.670   7.299  24.646  1.00 15.92           O  
ATOM    410  CB  SER A  52      -1.484   9.378  22.418  1.00 14.24           C  
ATOM    411  OG  SER A  52      -1.632   9.545  20.978  1.00 13.42           O  
ATOM    412  N   LEU A  53      -2.735   9.430  25.475  1.00 14.31           N  
ATOM    413  CA  LEU A  53      -2.740   9.073  26.882  1.00 15.59           C  
ATOM    414  C   LEU A  53      -4.010   8.364  27.242  1.00 15.51           C  
ATOM    415  O   LEU A  53      -3.927   7.425  28.023  1.00 15.07           O  
ATOM    416  CB  LEU A  53      -2.490  10.293  27.816  1.00 16.30           C  
ATOM    417  CG  LEU A  53      -1.991  10.085  29.274  1.00 18.57           C  
ATOM    418  CD1 LEU A  53      -0.904   9.033  29.366  1.00 17.57           C  
ATOM    419  CD2 LEU A  53      -1.444  11.426  29.904  1.00 20.43           C  
ATOM    420  N   ALA A  54      -5.138   8.735  26.620  1.00 15.88           N  
ATOM    421  CA  ALA A  54      -6.474   8.186  26.931  1.00 16.54           C  
ATOM    422  C   ALA A  54      -6.706   6.816  26.323  1.00 17.58           C  
ATOM    423  O   ALA A  54      -7.580   6.086  26.798  1.00 17.58           O  
ATOM    424  CB  ALA A  54      -7.663   9.130  26.438  1.00 15.98           C  
ATOM    425  N   GLY A  55      -6.007   6.539  25.214  1.00 17.31           N  
ATOM    426  CA  GLY A  55      -6.113   5.306  24.500  1.00 16.51           C  
ATOM    427  C   GLY A  55      -4.741   4.857  24.118  1.00 17.09           C  
ATOM    428  O   GLY A  55      -4.277   5.156  23.029  1.00 15.46           O  
ATOM    429  N   PRO A  56      -4.053   4.164  25.034  1.00 18.55           N  
ATOM    430  CA  PRO A  56      -2.643   3.775  24.817  1.00 19.22           C  
ATOM    431  C   PRO A  56      -2.472   2.785  23.650  1.00 20.43           C  
ATOM    432  O   PRO A  56      -1.350   2.544  23.205  1.00 19.89           O  
ATOM    433  CB  PRO A  56      -2.261   3.101  26.114  1.00 19.44           C  
ATOM    434  CG  PRO A  56      -3.304   3.390  27.061  1.00 19.11           C  
ATOM    435  CD  PRO A  56      -4.538   3.749  26.353  1.00 18.65           C  
ATOM    436  N   SER A  57      -3.576   2.225  23.159  1.00 21.49           N  
ATOM    437  CA  SER A  57      -3.559   1.420  21.938  1.00 22.23           C  
ATOM    438  C   SER A  57      -4.283   2.095  20.763  1.00 22.31           C  
ATOM    439  O   SER A  57      -4.723   1.427  19.851  1.00 23.39           O  
ATOM    440  CB  SER A  57      -4.219   0.049  22.177  1.00 22.37           C  
ATOM    441  OG  SER A  57      -4.043  -0.444  23.507  1.00 23.83           O  
ATOM    442  N   GLY A  58      -4.432   3.402  20.785  1.00 21.83           N  
ATOM    443  CA  GLY A  58      -4.966   4.101  19.647  1.00 21.61           C  
ATOM    444  C   GLY A  58      -6.468   4.289  19.660  1.00 21.68           C  
ATOM    445  O   GLY A  58      -7.016   4.741  18.667  1.00 21.88           O  
ATOM    446  N   GLU A  59      -7.109   4.000  20.786  1.00 21.33           N  
ATOM    447  CA  GLU A  59      -8.547   4.089  20.909  1.00 22.70           C  
ATOM    448  C   GLU A  59      -9.114   5.465  20.571  1.00 22.14           C  
ATOM    449  O   GLU A  59     -10.255   5.568  20.159  1.00 21.50           O  
ATOM    450  CB  GLU A  59      -8.962   3.764  22.337  1.00 24.23           C  
ATOM    451  CG  GLU A  59      -8.776   2.308  22.716  1.00 28.22           C  
ATOM    452  CD  GLU A  59      -7.367   1.949  23.196  1.00 31.38           C  
ATOM    453  OE1 GLU A  59      -6.388   2.727  22.971  1.00 30.60           O  
ATOM    454  OE2 GLU A  59      -7.273   0.853  23.799  1.00 35.60           O  
ATOM    455  N   HIS A  60      -8.323   6.516  20.755  1.00 21.60           N  
ATOM    456  CA  HIS A  60      -8.812   7.866  20.506  1.00 20.71           C  
ATOM    457  C   HIS A  60      -7.981   8.600  19.492  1.00 20.00           C  
ATOM    458  O   HIS A  60      -8.019   9.805  19.436  1.00 21.63           O  
ATOM    459  CB  HIS A  60      -8.965   8.645  21.819  1.00 20.05           C  
ATOM    460  CG  HIS A  60      -9.913   7.996  22.770  1.00 18.11           C  
ATOM    461  ND1 HIS A  60     -11.276   7.942  22.549  1.00 17.57           N  
ATOM    462  CD2 HIS A  60      -9.699   7.342  23.937  1.00 20.06           C  
ATOM    463  CE1 HIS A  60     -11.856   7.286  23.539  1.00 16.59           C  
ATOM    464  NE2 HIS A  60     -10.924   6.926  24.406  1.00 15.79           N  
ATOM    465  N   TYR A  61      -7.314   7.871  18.622  1.00 19.00           N  
ATOM    466  CA  TYR A  61      -6.487   8.466  17.618  1.00 18.96           C  
ATOM    467  C   TYR A  61      -7.335   9.207  16.587  1.00 19.47           C  
ATOM    468  O   TYR A  61      -8.408   8.800  16.238  1.00 19.09           O  
ATOM    469  CB  TYR A  61      -5.625   7.400  16.910  1.00 18.83           C  
ATOM    470  CG  TYR A  61      -4.789   7.975  15.779  1.00 19.01           C  
ATOM    471  CD1 TYR A  61      -3.614   8.672  16.042  1.00 17.99           C  
ATOM    472  CD2 TYR A  61      -5.204   7.870  14.439  1.00 20.39           C  
ATOM    473  CE1 TYR A  61      -2.887   9.239  15.042  1.00 16.77           C  
ATOM    474  CE2 TYR A  61      -4.428   8.414  13.391  1.00 16.82           C  
ATOM    475  CZ  TYR A  61      -3.296   9.109  13.697  1.00 19.09           C  
ATOM    476  OH  TYR A  61      -2.533   9.678  12.684  1.00 18.27           O  
ATOM    477  N   LYS A  62      -6.779  10.285  16.070  1.00 20.44           N  
ATOM    478  CA  LYS A  62      -7.318  10.995  14.946  1.00 20.70           C  
ATOM    479  C   LYS A  62      -6.122  11.633  14.259  1.00 19.93           C  
ATOM    480  O   LYS A  62      -5.185  12.081  14.952  1.00 19.26           O  
ATOM    481  CB  LYS A  62      -8.279  12.043  15.478  1.00 21.06           C  
ATOM    482  CG  LYS A  62      -8.963  12.922  14.490  1.00 25.37           C  
ATOM    483  CD  LYS A  62      -9.806  13.987  15.301  1.00 28.12           C  
ATOM    484  CE  LYS A  62     -10.910  14.672  14.489  1.00 30.15           C  
ATOM    485  NZ  LYS A  62     -12.101  15.007  15.331  1.00 30.57           N  
ATOM    486  N   PRO A  63      -6.130  11.678  12.908  1.00 19.78           N  
ATOM    487  CA  PRO A  63      -4.911  12.166  12.233  1.00 19.94           C  
ATOM    488  C   PRO A  63      -4.642  13.620  12.546  1.00 19.44           C  
ATOM    489  O   PRO A  63      -5.573  14.362  12.828  1.00 20.18           O  
ATOM    490  CB  PRO A  63      -5.172  11.952  10.713  1.00 20.07           C  
ATOM    491  CG  PRO A  63      -6.456  11.182  10.599  1.00 20.40           C  
ATOM    492  CD  PRO A  63      -7.175  11.204  11.971  1.00 20.43           C  
ATOM    493  N   PHE A  64      -3.372  13.990  12.479  1.00 19.44           N  
ATOM    494  CA  PHE A  64      -2.855  15.252  12.951  1.00 19.91           C  
ATOM    495  C   PHE A  64      -3.539  16.436  12.291  1.00 21.77           C  
ATOM    496  O   PHE A  64      -3.625  17.523  12.894  1.00 22.71           O  
ATOM    497  CB  PHE A  64      -1.369  15.308  12.664  1.00 18.84           C  
ATOM    498  CG  PHE A  64      -0.605  16.402  13.401  1.00 18.41           C  
ATOM    499  CD1 PHE A  64      -0.711  16.563  14.791  1.00 17.53           C  
ATOM    500  CD2 PHE A  64       0.240  17.254  12.724  1.00 17.48           C  
ATOM    501  CE1 PHE A  64       0.016  17.514  15.453  1.00 14.61           C  
ATOM    502  CE2 PHE A  64       0.964  18.272  13.410  1.00 14.13           C  
ATOM    503  CZ  PHE A  64       0.864  18.363  14.768  1.00 16.50           C  
ATOM    504  N   TRP A  65      -4.001  16.217  11.063  1.00 22.51           N  
ATOM    505  CA  TRP A  65      -4.652  17.226  10.266  1.00 23.32           C  
ATOM    506  C   TRP A  65      -5.929  17.601  10.917  1.00 22.92           C  
ATOM    507  O   TRP A  65      -6.194  18.775  11.165  1.00 23.82           O  
ATOM    508  CB  TRP A  65      -4.978  16.691   8.862  1.00 23.88           C  
ATOM    509  CG  TRP A  65      -5.791  17.684   8.030  1.00 24.61           C  
ATOM    510  CD1 TRP A  65      -7.159  17.725   7.887  1.00 27.43           C  
ATOM    511  CD2 TRP A  65      -5.278  18.759   7.244  1.00 22.63           C  
ATOM    512  NE1 TRP A  65      -7.520  18.767   7.065  1.00 24.17           N  
ATOM    513  CE2 TRP A  65      -6.377  19.412   6.655  1.00 23.05           C  
ATOM    514  CE3 TRP A  65      -3.991  19.221   6.962  1.00 23.65           C  
ATOM    515  CZ2 TRP A  65      -6.224  20.506   5.809  1.00 22.66           C  
ATOM    516  CZ3 TRP A  65      -3.838  20.317   6.144  1.00 23.85           C  
ATOM    517  CH2 TRP A  65      -4.951  20.936   5.552  1.00 22.86           C  
ATOM    518  N   ASP A  66      -6.718  16.585  11.188  1.00 23.44           N  
ATOM    519  CA  ASP A  66      -8.022  16.781  11.791  1.00 23.60           C  
ATOM    520  C   ASP A  66      -7.897  17.296  13.234  1.00 22.83           C  
ATOM    521  O   ASP A  66      -8.756  18.077  13.698  1.00 23.17           O  
ATOM    522  CB  ASP A  66      -8.838  15.483  11.710  1.00 24.11           C  
ATOM    523  CG  ASP A  66      -8.804  14.843  10.286  1.00 26.86           C  
ATOM    524  OD1 ASP A  66      -9.532  15.288   9.379  1.00 30.81           O  
ATOM    525  OD2 ASP A  66      -8.030  13.912  10.068  1.00 28.08           O  
ATOM    526  N   VAL A  67      -6.855  16.849  13.952  1.00 21.26           N  
ATOM    527  CA  VAL A  67      -6.558  17.401  15.273  1.00 19.51           C  
ATOM    528  C   VAL A  67      -6.208  18.883  15.150  1.00 19.40           C  
ATOM    529  O   VAL A  67      -6.504  19.655  16.057  1.00 17.88           O  
ATOM    530  CB  VAL A  67      -5.416  16.629  16.044  1.00 19.56           C  
ATOM    531  CG1 VAL A  67      -4.978  17.413  17.316  1.00 17.10           C  
ATOM    532  CG2 VAL A  67      -5.863  15.130  16.377  1.00 17.48           C  
ATOM    533  N   THR A  68      -5.558  19.276  14.041  1.00 19.25           N  
ATOM    534  CA  THR A  68      -5.107  20.660  13.867  1.00 19.12           C  
ATOM    535  C   THR A  68      -6.356  21.555  13.594  1.00 20.74           C  
ATOM    536  O   THR A  68      -6.447  22.670  14.036  1.00 21.97           O  
ATOM    537  CB  THR A  68      -3.999  20.765  12.800  1.00 19.00           C  
ATOM    538  OG1 THR A  68      -2.814  20.122  13.275  1.00 18.37           O  
ATOM    539  CG2 THR A  68      -3.663  22.213  12.458  1.00 14.05           C  
ATOM    540  N   VAL A  69      -7.330  21.025  12.888  1.00 22.50           N  
ATOM    541  CA  VAL A  69      -8.592  21.727  12.640  1.00 22.81           C  
ATOM    542  C   VAL A  69      -9.321  21.918  13.983  1.00 22.02           C  
ATOM    543  O   VAL A  69      -9.632  23.039  14.353  1.00 22.03           O  
ATOM    544  CB  VAL A  69      -9.421  20.927  11.592  1.00 23.12           C  
ATOM    545  CG1 VAL A  69     -10.859  21.425  11.492  1.00 23.46           C  
ATOM    546  CG2 VAL A  69      -8.696  20.969  10.213  1.00 24.57           C  
ATOM    547  N   ASP A  70      -9.496  20.821  14.734  1.00 21.02           N  
ATOM    548  CA  ASP A  70     -10.072  20.874  16.082  1.00 20.03           C  
ATOM    549  C   ASP A  70      -9.421  21.962  16.939  1.00 19.81           C  
ATOM    550  O   ASP A  70     -10.105  22.766  17.559  1.00 18.99           O  
ATOM    551  CB  ASP A  70      -9.913  19.542  16.795  1.00 20.70           C  
ATOM    552  CG  ASP A  70     -10.649  18.433  16.127  1.00 20.98           C  
ATOM    553  OD1 ASP A  70     -11.537  18.773  15.337  1.00 24.29           O  
ATOM    554  OD2 ASP A  70     -10.314  17.237  16.356  1.00 23.45           O  
ATOM    555  N   ALA A  71      -8.105  21.960  17.017  1.00 18.52           N  
ATOM    556  CA  ALA A  71      -7.412  22.929  17.864  1.00 18.60           C  
ATOM    557  C   ALA A  71      -7.667  24.351  17.358  1.00 18.67           C  
ATOM    558  O   ALA A  71      -7.824  25.276  18.158  1.00 18.52           O  
ATOM    559  CB  ALA A  71      -5.892  22.658  17.942  1.00 16.83           C  
ATOM    560  N   LEU A  72      -7.655  24.535  16.040  1.00 18.97           N  
ATOM    561  CA  LEU A  72      -7.838  25.864  15.460  1.00 19.05           C  
ATOM    562  C   LEU A  72      -9.240  26.398  15.770  1.00 18.51           C  
ATOM    563  O   LEU A  72      -9.413  27.576  16.083  1.00 18.32           O  
ATOM    564  CB  LEU A  72      -7.668  25.809  13.939  1.00 19.58           C  
ATOM    565  CG  LEU A  72      -8.077  27.079  13.162  1.00 18.44           C  
ATOM    566  CD1 LEU A  72      -7.081  28.183  13.527  1.00 18.64           C  
ATOM    567  CD2 LEU A  72      -8.128  26.821  11.681  1.00 16.01           C  
ATOM    568  N   ARG A  73     -10.225  25.522  15.591  1.00 18.99           N  
ATOM    569  CA  ARG A  73     -11.603  25.777  15.976  1.00 19.84           C  
ATOM    570  C   ARG A  73     -11.806  26.101  17.443  1.00 19.58           C  
ATOM    571  O   ARG A  73     -12.510  27.085  17.783  1.00 18.53           O  
ATOM    572  CB  ARG A  73     -12.482  24.597  15.632  1.00 20.47           C  
ATOM    573  CG  ARG A  73     -12.699  24.445  14.138  1.00 25.47           C  
ATOM    574  CD  ARG A  73     -13.541  23.234  13.765  1.00 29.26           C  
ATOM    575  NE  ARG A  73     -13.706  23.173  12.292  1.00 34.88           N  
ATOM    576  CZ  ARG A  73     -14.061  22.094  11.588  1.00 36.51           C  
ATOM    577  NH1 ARG A  73     -14.295  20.927  12.180  1.00 38.89           N  
ATOM    578  NH2 ARG A  73     -14.165  22.176  10.272  1.00 38.90           N  
ATOM    579  N   TYR A  74     -11.245  25.279  18.337  1.00 18.83           N  
ATOM    580  CA  TYR A  74     -11.336  25.628  19.757  1.00 17.84           C  
ATOM    581  C   TYR A  74     -10.706  27.027  19.965  1.00 18.72           C  
ATOM    582  O   TYR A  74     -11.286  27.888  20.648  1.00 17.49           O  
ATOM    583  CB  TYR A  74     -10.648  24.622  20.671  1.00 17.78           C  
ATOM    584  CG  TYR A  74     -10.597  25.123  22.083  1.00 15.16           C  
ATOM    585  CD1 TYR A  74     -11.595  24.788  22.977  1.00 15.59           C  
ATOM    586  CD2 TYR A  74      -9.554  25.914  22.520  1.00 14.93           C  
ATOM    587  CE1 TYR A  74     -11.596  25.250  24.273  1.00 14.58           C  
ATOM    588  CE2 TYR A  74      -9.514  26.392  23.827  1.00 17.58           C  
ATOM    589  CZ  TYR A  74     -10.572  26.052  24.706  1.00 16.74           C  
ATOM    590  OH  TYR A  74     -10.610  26.504  26.010  1.00 16.42           O  
ATOM    591  N   ALA A  75      -9.516  27.247  19.403  1.00 18.95           N  
ATOM    592  CA  ALA A  75      -8.784  28.507  19.700  1.00 19.91           C  
ATOM    593  C   ALA A  75      -9.611  29.740  19.228  1.00 20.68           C  
ATOM    594  O   ALA A  75      -9.654  30.774  19.880  1.00 20.41           O  
ATOM    595  CB  ALA A  75      -7.429  28.495  19.058  1.00 18.71           C  
ATOM    596  N   CYS A  76     -10.311  29.596  18.111  1.00 22.02           N  
ATOM    597  CA  CYS A  76     -11.088  30.723  17.594  1.00 23.41           C  
ATOM    598  C   CYS A  76     -12.325  31.011  18.448  1.00 23.05           C  
ATOM    599  O   CYS A  76     -12.582  32.166  18.710  1.00 23.43           O  
ATOM    600  CB  CYS A  76     -11.445  30.515  16.125  1.00 23.88           C  
ATOM    601  SG  CYS A  76      -9.990  30.828  15.055  1.00 28.13           S  
ATOM    602  N   ALA A  77     -13.023  29.960  18.886  1.00 22.28           N  
ATOM    603  CA  ALA A  77     -14.173  30.035  19.765  1.00 21.90           C  
ATOM    604  C   ALA A  77     -13.793  30.706  21.051  1.00 21.68           C  
ATOM    605  O   ALA A  77     -14.461  31.639  21.471  1.00 22.11           O  
ATOM    606  CB  ALA A  77     -14.772  28.604  20.059  1.00 22.10           C  
ATOM    607  N   ARG A  78     -12.689  30.264  21.647  1.00 21.50           N  
ATOM    608  CA  ARG A  78     -12.163  30.819  22.913  1.00 20.71           C  
ATOM    609  C   ARG A  78     -11.775  32.291  22.801  1.00 20.51           C  
ATOM    610  O   ARG A  78     -11.939  33.059  23.722  1.00 17.44           O  
ATOM    611  CB  ARG A  78     -10.960  29.977  23.344  1.00 21.44           C  
ATOM    612  CG  ARG A  78     -10.012  30.504  24.413  1.00 22.75           C  
ATOM    613  CD  ARG A  78     -10.398  30.116  25.860  1.00 29.51           C  
ATOM    614  NE  ARG A  78      -9.278  30.421  26.767  1.00 33.42           N  
ATOM    615  CZ  ARG A  78      -8.320  29.546  27.154  1.00 33.32           C  
ATOM    616  NH1 ARG A  78      -8.328  28.253  26.805  1.00 31.30           N  
ATOM    617  NH2 ARG A  78      -7.343  29.977  27.943  1.00 31.88           N  
ATOM    618  N   LEU A  79     -11.214  32.664  21.652  1.00 21.99           N  
ATOM    619  CA  LEU A  79     -10.644  33.973  21.452  1.00 22.54           C  
ATOM    620  C   LEU A  79     -11.662  34.872  20.766  1.00 23.56           C  
ATOM    621  O   LEU A  79     -11.339  36.007  20.389  1.00 24.98           O  
ATOM    622  CB  LEU A  79      -9.375  33.866  20.584  1.00 23.37           C  
ATOM    623  CG  LEU A  79      -8.033  33.471  21.221  1.00 23.83           C  
ATOM    624  CD1 LEU A  79      -6.970  33.388  20.142  1.00 22.12           C  
ATOM    625  CD2 LEU A  79      -7.650  34.473  22.332  1.00 23.80           C  
ATOM    626  N   ASN A  80     -12.875  34.363  20.589  1.00 24.20           N  
ATOM    627  CA  ASN A  80     -13.996  35.106  19.980  1.00 25.35           C  
ATOM    628  C   ASN A  80     -13.742  35.656  18.576  1.00 26.66           C  
ATOM    629  O   ASN A  80     -14.248  36.730  18.246  1.00 27.13           O  
ATOM    630  CB  ASN A  80     -14.451  36.235  20.916  1.00 24.86           C  
ATOM    631  CG  ASN A  80     -15.035  35.699  22.182  1.00 22.61           C  
ATOM    632  OD1 ASN A  80     -15.842  34.759  22.132  1.00 19.97           O  
ATOM    633  ND2 ASN A  80     -14.647  36.278  23.329  1.00 19.79           N  
ATOM    634  N   LEU A  81     -13.035  34.872  17.754  1.00 27.50           N  
ATOM    635  CA  LEU A  81     -12.702  35.215  16.367  1.00 28.35           C  
ATOM    636  C   LEU A  81     -13.657  34.628  15.302  1.00 29.77           C  
ATOM    637  O   LEU A  81     -14.002  33.445  15.375  1.00 29.98           O  
ATOM    638  CB  LEU A  81     -11.283  34.734  16.070  1.00 27.97           C  
ATOM    639  CG  LEU A  81     -10.205  35.155  17.061  1.00 26.57           C  
ATOM    640  CD1 LEU A  81      -8.857  34.510  16.642  1.00 28.93           C  
ATOM    641  CD2 LEU A  81     -10.090  36.668  17.135  1.00 25.50           C  
ATOM    642  N   PRO A  82     -14.066  35.444  14.289  1.00 31.42           N  
ATOM    643  CA  PRO A  82     -14.978  35.002  13.207  1.00 33.10           C  
ATOM    644  C   PRO A  82     -14.409  33.992  12.152  1.00 35.28           C  
ATOM    645  O   PRO A  82     -14.179  34.348  10.984  1.00 36.44           O  
ATOM    646  CB  PRO A  82     -15.392  36.320  12.538  1.00 32.42           C  
ATOM    647  CG  PRO A  82     -14.316  37.243  12.811  1.00 31.66           C  
ATOM    648  CD  PRO A  82     -13.795  36.889  14.184  1.00 31.24           C  
ATOM    649  N   LEU A  83     -14.250  32.737  12.575  1.00 37.35           N  
ATOM    650  CA  LEU A  83     -13.696  31.668  11.749  1.00 38.55           C  
ATOM    651  C   LEU A  83     -14.814  30.822  11.144  1.00 39.55           C  
ATOM    652  O   LEU A  83     -15.309  29.891  11.764  1.00 39.84           O  
ATOM    653  CB  LEU A  83     -12.758  30.767  12.576  1.00 38.67           C  
ATOM    654  CG  LEU A  83     -12.065  29.610  11.830  1.00 39.07           C  
ATOM    655  CD1 LEU A  83     -10.607  29.978  11.496  1.00 36.82           C  
ATOM    656  CD2 LEU A  83     -12.136  28.327  12.642  1.00 36.33           C  
ATOM    657  N   GLY A  84     -15.204  31.161   9.926  1.00 40.61           N  
ATOM    658  CA  GLY A  84     -16.084  30.300   9.143  1.00 41.88           C  
ATOM    659  C   GLY A  84     -15.263  29.538   8.094  1.00 42.52           C  
ATOM    660  O   GLY A  84     -14.038  29.503   8.162  1.00 42.25           O  
ATOM    661  N   ASN A  85     -15.943  28.969   7.104  1.00 43.21           N  
ATOM    662  CA  ASN A  85     -15.286  28.103   6.142  1.00 44.20           C  
ATOM    663  C   ASN A  85     -14.094  28.766   5.407  1.00 43.72           C  
ATOM    664  O   ASN A  85     -13.007  28.185   5.361  1.00 44.20           O  
ATOM    665  CB  ASN A  85     -16.308  27.511   5.169  1.00 44.47           C  
ATOM    666  CG  ASN A  85     -17.329  26.636   5.869  1.00 45.57           C  
ATOM    667  OD1 ASN A  85     -16.973  25.759   6.667  1.00 46.48           O  
ATOM    668  ND2 ASN A  85     -18.614  26.868   5.576  1.00 45.68           N  
ATOM    669  N   HIS A  86     -14.257  29.981   4.883  1.00 43.29           N  
ATOM    670  CA  HIS A  86     -13.158  30.594   4.128  1.00 42.34           C  
ATOM    671  C   HIS A  86     -11.944  30.761   5.025  1.00 40.66           C  
ATOM    672  O   HIS A  86     -10.877  30.301   4.653  1.00 40.15           O  
ATOM    673  CB  HIS A  86     -13.531  31.940   3.439  1.00 43.24           C  
ATOM    674  CG  HIS A  86     -12.346  32.659   2.839  1.00 45.84           C  
ATOM    675  ND1 HIS A  86     -11.891  32.417   1.555  1.00 48.42           N  
ATOM    676  CD2 HIS A  86     -11.502  33.587   3.365  1.00 47.87           C  
ATOM    677  CE1 HIS A  86     -10.832  33.176   1.307  1.00 49.18           C  
ATOM    678  NE2 HIS A  86     -10.566  33.886   2.393  1.00 49.66           N  
ATOM    679  N   ALA A  87     -12.075  31.399   6.195  1.00 38.92           N  
ATOM    680  CA  ALA A  87     -10.855  31.740   6.981  1.00 37.99           C  
ATOM    681  C   ALA A  87     -10.156  30.465   7.522  1.00 36.72           C  
ATOM    682  O   ALA A  87      -8.937  30.414   7.654  1.00 35.61           O  
ATOM    683  CB  ALA A  87     -11.154  32.721   8.106  1.00 37.23           C  
ATOM    684  N   GLU A  88     -10.971  29.467   7.841  1.00 36.19           N  
ATOM    685  CA  GLU A  88     -10.512  28.122   8.179  1.00 36.30           C  
ATOM    686  C   GLU A  88      -9.750  27.485   7.011  1.00 36.45           C  
ATOM    687  O   GLU A  88      -8.587  27.151   7.152  1.00 36.37           O  
ATOM    688  CB  GLU A  88     -11.709  27.243   8.526  1.00 35.92           C  
ATOM    689  CG  GLU A  88     -11.359  25.810   8.780  1.00 36.13           C  
ATOM    690  CD  GLU A  88     -12.370  25.135   9.624  1.00 35.40           C  
ATOM    691  OE1 GLU A  88     -12.708  25.682  10.683  1.00 37.26           O  
ATOM    692  OE2 GLU A  88     -12.831  24.049   9.249  1.00 36.37           O  
ATOM    693  N   ALA A  89     -10.410  27.332   5.858  1.00 36.40           N  
ATOM    694  CA  ALA A  89      -9.726  26.818   4.661  1.00 36.40           C  
ATOM    695  C   ALA A  89      -8.410  27.571   4.435  1.00 35.37           C  
ATOM    696  O   ALA A  89      -7.370  26.969   4.277  1.00 36.08           O  
ATOM    697  CB  ALA A  89     -10.650  26.866   3.419  1.00 36.49           C  
ATOM    698  N   THR A  90      -8.425  28.886   4.507  1.00 35.45           N  
ATOM    699  CA  THR A  90      -7.212  29.677   4.262  1.00 34.92           C  
ATOM    700  C   THR A  90      -6.079  29.368   5.194  1.00 34.91           C  
ATOM    701  O   THR A  90      -4.907  29.432   4.807  1.00 33.99           O  
ATOM    702  CB  THR A  90      -7.479  31.188   4.391  1.00 35.15           C  
ATOM    703  OG1 THR A  90      -8.429  31.577   3.407  1.00 34.63           O  
ATOM    704  CG2 THR A  90      -6.197  31.992   4.181  1.00 35.21           C  
ATOM    705  N   LEU A  91      -6.399  29.082   6.452  1.00 35.59           N  
ATOM    706  CA  LEU A  91      -5.323  28.928   7.443  1.00 35.95           C  
ATOM    707  C   LEU A  91      -4.768  27.542   7.361  1.00 35.32           C  
ATOM    708  O   LEU A  91      -3.597  27.335   7.572  1.00 35.05           O  
ATOM    709  CB  LEU A  91      -5.795  29.242   8.866  1.00 36.25           C  
ATOM    710  CG  LEU A  91      -5.741  30.736   9.224  1.00 37.42           C  
ATOM    711  CD1 LEU A  91      -6.294  30.940  10.638  1.00 37.26           C  
ATOM    712  CD2 LEU A  91      -4.299  31.265   9.099  1.00 35.85           C  
HETATM  713  N   MSE A  92      -5.651  26.601   7.070  1.00 35.81           N  
HETATM  714  CA  MSE A  92      -5.280  25.212   6.844  1.00 36.32           C  
HETATM  715  C   MSE A  92      -4.393  25.086   5.557  1.00 37.46           C  
HETATM  716  O   MSE A  92      -3.277  24.541   5.651  1.00 37.59           O  
HETATM  717  CB  MSE A  92      -6.545  24.299   6.873  1.00 36.33           C  
HETATM  718  CG  MSE A  92      -7.194  24.046   8.345  1.00 34.22           C  
HETATM  719 SE   MSE A  92      -5.844  23.797   9.770  1.00 37.71          SE  
HETATM  720  CE  MSE A  92      -5.323  21.929   9.272  1.00 34.44           C  
ATOM    721  N   ARG A  93      -4.819  25.659   4.419  1.00 37.85           N  
ATOM    722  CA  ARG A  93      -3.941  25.800   3.236  1.00 38.70           C  
ATOM    723  C   ARG A  93      -2.576  26.286   3.626  1.00 39.40           C  
ATOM    724  O   ARG A  93      -1.554  25.697   3.282  1.00 38.83           O  
ATOM    725  CB  ARG A  93      -4.495  26.802   2.213  1.00 39.13           C  
ATOM    726  CG  ARG A  93      -5.711  26.291   1.444  1.00 40.84           C  
ATOM    727  CD  ARG A  93      -6.036  27.118   0.200  1.00 43.62           C  
ATOM    728  NE  ARG A  93      -7.128  28.085   0.397  1.00 46.21           N  
ATOM    729  CZ  ARG A  93      -8.440  27.810   0.356  1.00 46.96           C  
ATOM    730  NH1 ARG A  93      -8.892  26.567   0.155  1.00 48.05           N  
ATOM    731  NH2 ARG A  93      -9.318  28.798   0.538  1.00 45.86           N  
ATOM    732  N   GLU A  94      -2.553  27.375   4.369  1.00 40.45           N  
ATOM    733  CA  GLU A  94      -1.307  27.893   4.823  1.00 41.28           C  
ATOM    734  C   GLU A  94      -0.542  26.814   5.541  1.00 42.55           C  
ATOM    735  O   GLU A  94       0.674  26.734   5.406  1.00 42.46           O  
ATOM    736  CB  GLU A  94      -1.525  29.080   5.752  1.00 41.25           C  
ATOM    737  CG  GLU A  94      -0.323  29.939   5.826  1.00 40.51           C  
ATOM    738  CD  GLU A  94      -0.148  30.797   4.607  1.00 41.71           C  
ATOM    739  OE1 GLU A  94      -1.174  31.159   3.968  1.00 42.72           O  
ATOM    740  OE2 GLU A  94       1.022  31.105   4.302  1.00 40.34           O  
ATOM    741  N   TYR A  95      -1.259  25.986   6.303  1.00 44.46           N  
ATOM    742  CA  TYR A  95      -0.621  24.945   7.139  1.00 46.48           C  
ATOM    743  C   TYR A  95      -0.069  23.826   6.266  1.00 47.02           C  
ATOM    744  O   TYR A  95       1.022  23.329   6.519  1.00 46.80           O  
ATOM    745  CB  TYR A  95      -1.580  24.362   8.227  1.00 46.75           C  
ATOM    746  CG  TYR A  95      -0.860  23.945   9.522  1.00 48.95           C  
ATOM    747  CD1 TYR A  95      -1.176  24.528  10.739  1.00 50.05           C  
ATOM    748  CD2 TYR A  95       0.161  23.005   9.513  1.00 51.56           C  
ATOM    749  CE1 TYR A  95      -0.501  24.181  11.912  1.00 51.42           C  
ATOM    750  CE2 TYR A  95       0.835  22.654  10.680  1.00 52.66           C  
ATOM    751  CZ  TYR A  95       0.495  23.244  11.872  1.00 52.65           C  
ATOM    752  OH  TYR A  95       1.161  22.891  13.022  1.00 55.61           O  
ATOM    753  N   ALA A  96      -0.834  23.442   5.244  1.00 48.37           N  
ATOM    754  CA  ALA A  96      -0.407  22.398   4.307  1.00 49.38           C  
ATOM    755  C   ALA A  96       0.945  22.692   3.713  1.00 50.09           C  
ATOM    756  O   ALA A  96       1.763  21.799   3.617  1.00 50.74           O  
ATOM    757  CB  ALA A  96      -1.435  22.189   3.209  1.00 48.86           C  
ATOM    758  N   CYS A  97       1.202  23.947   3.375  1.00 51.76           N  
ATOM    759  CA  CYS A  97       2.342  24.284   2.535  1.00 53.45           C  
ATOM    760  C   CYS A  97       3.300  25.342   3.077  1.00 53.71           C  
ATOM    761  O   CYS A  97       3.141  26.534   2.813  1.00 54.40           O  
ATOM    762  CB  CYS A  97       1.832  24.689   1.162  1.00 53.81           C  
ATOM    763  SG  CYS A  97       2.182  23.398  -0.061  1.00 59.92           S  
ATOM    764  N   LEU A  98       4.345  24.877   3.757  1.00 53.98           N  
ATOM    765  CA  LEU A  98       5.240  25.745   4.509  1.00 54.01           C  
ATOM    766  C   LEU A  98       6.636  25.784   3.917  1.00 54.00           C  
ATOM    767  O   LEU A  98       6.981  24.945   3.107  1.00 53.96           O  
ATOM    768  CB  LEU A  98       5.281  25.264   5.959  1.00 54.06           C  
ATOM    769  CG  LEU A  98       4.049  25.781   6.709  1.00 54.35           C  
ATOM    770  CD1 LEU A  98       3.579  24.896   7.860  1.00 53.38           C  
ATOM    771  CD2 LEU A  98       4.377  27.176   7.173  1.00 55.20           C  
ATOM    772  N   SER A  99       7.448  26.754   4.331  1.00 53.78           N  
ATOM    773  CA  SER A  99       8.802  26.856   3.795  1.00 53.69           C  
ATOM    774  C   SER A  99       9.864  26.535   4.854  1.00 53.49           C  
ATOM    775  O   SER A  99       9.626  26.603   6.067  1.00 52.86           O  
ATOM    776  CB  SER A  99       9.043  28.211   3.060  1.00 53.90           C  
ATOM    777  OG  SER A  99       9.474  29.275   3.897  1.00 53.98           O  
ATOM    778  N   ALA A 100      11.031  26.145   4.351  1.00 53.43           N  
ATOM    779  CA  ALA A 100      12.145  25.698   5.167  1.00 53.37           C  
ATOM    780  C   ALA A 100      12.899  26.879   5.750  1.00 53.44           C  
ATOM    781  O   ALA A 100      12.770  28.018   5.272  1.00 53.56           O  
ATOM    782  CB  ALA A 100      13.109  24.839   4.327  1.00 53.42           C  
ATOM    783  N   PHE A 101      13.692  26.588   6.774  1.00 52.99           N  
ATOM    784  CA  PHE A 101      14.694  27.514   7.237  1.00 53.27           C  
ATOM    785  C   PHE A 101      15.855  27.427   6.215  1.00 53.76           C  
ATOM    786  O   PHE A 101      16.495  26.377   6.066  1.00 54.12           O  
ATOM    787  CB  PHE A 101      15.137  27.188   8.680  1.00 53.35           C  
ATOM    788  CG  PHE A 101      14.005  27.260   9.715  1.00 51.71           C  
ATOM    789  CD1 PHE A 101      13.806  28.408  10.475  1.00 51.21           C  
ATOM    790  CD2 PHE A 101      13.174  26.180   9.940  1.00 50.90           C  
ATOM    791  CE1 PHE A 101      12.783  28.478  11.445  1.00 50.30           C  
ATOM    792  CE2 PHE A 101      12.159  26.241  10.908  1.00 50.71           C  
ATOM    793  CZ  PHE A 101      11.959  27.394  11.653  1.00 50.91           C  
ATOM    794  N   PRO A 102      16.095  28.521   5.477  1.00 53.76           N  
ATOM    795  CA  PRO A 102      17.049  28.670   4.361  1.00 53.86           C  
ATOM    796  C   PRO A 102      18.407  27.966   4.541  1.00 53.56           C  
ATOM    797  O   PRO A 102      19.021  27.492   3.582  1.00 52.64           O  
ATOM    798  CB  PRO A 102      17.245  30.195   4.308  1.00 54.18           C  
ATOM    799  CG  PRO A 102      15.887  30.731   4.721  1.00 54.07           C  
ATOM    800  CD  PRO A 102      15.386  29.789   5.764  1.00 54.07           C  
ATOM    801  N   GLU A 103      18.856  27.947   5.783  1.00 53.58           N  
ATOM    802  CA  GLU A 103      20.029  27.197   6.219  1.00 54.14           C  
ATOM    803  C   GLU A 103      19.922  25.662   6.061  1.00 53.77           C  
ATOM    804  O   GLU A 103      20.935  24.976   5.925  1.00 53.95           O  
ATOM    805  CB  GLU A 103      20.284  27.520   7.705  1.00 54.44           C  
ATOM    806  CG  GLU A 103      18.979  27.556   8.557  1.00 56.16           C  
ATOM    807  CD  GLU A 103      19.170  27.171  10.012  1.00 57.90           C  
ATOM    808  OE1 GLU A 103      20.339  27.151  10.468  1.00 60.07           O  
ATOM    809  OE2 GLU A 103      18.147  26.880  10.693  1.00 57.75           O  
ATOM    810  N   ASN A 104      18.710  25.122   6.110  1.00 52.97           N  
ATOM    811  CA  ASN A 104      18.532  23.665   6.152  1.00 52.81           C  
ATOM    812  C   ASN A 104      19.134  22.886   4.950  1.00 52.70           C  
ATOM    813  O   ASN A 104      19.997  21.990   5.115  1.00 51.86           O  
ATOM    814  CB  ASN A 104      17.025  23.338   6.324  1.00 52.56           C  
ATOM    815  CG  ASN A 104      16.498  23.677   7.735  1.00 51.55           C  
ATOM    816  OD1 ASN A 104      17.285  23.919   8.637  1.00 48.75           O  
ATOM    817  ND2 ASN A 104      15.167  23.673   7.920  1.00 49.86           N  
ATOM    818  N   VAL A 105      18.674  23.241   3.749  1.00 52.67           N  
ATOM    819  CA  VAL A 105      18.874  22.394   2.578  1.00 52.28           C  
ATOM    820  C   VAL A 105      20.361  22.121   2.251  1.00 52.38           C  
ATOM    821  O   VAL A 105      20.678  21.033   1.750  1.00 52.51           O  
ATOM    822  CB  VAL A 105      18.095  22.905   1.344  1.00 52.25           C  
ATOM    823  CG1 VAL A 105      17.913  21.777   0.360  1.00 52.04           C  
ATOM    824  CG2 VAL A 105      16.721  23.461   1.737  1.00 52.43           C  
ATOM    825  N   PRO A 106      21.276  23.093   2.528  1.00 52.02           N  
ATOM    826  CA  PRO A 106      22.722  22.810   2.348  1.00 51.78           C  
ATOM    827  C   PRO A 106      23.306  21.884   3.400  1.00 51.84           C  
ATOM    828  O   PRO A 106      24.116  20.986   3.068  1.00 51.11           O  
ATOM    829  CB  PRO A 106      23.398  24.188   2.479  1.00 51.95           C  
ATOM    830  CG  PRO A 106      22.313  25.170   2.831  1.00 52.45           C  
ATOM    831  CD  PRO A 106      20.989  24.541   2.596  1.00 51.84           C  
ATOM    832  N   VAL A 107      22.919  22.156   4.665  1.00 52.07           N  
ATOM    833  CA  VAL A 107      23.322  21.370   5.854  1.00 51.65           C  
ATOM    834  C   VAL A 107      22.904  19.918   5.660  1.00 51.73           C  
ATOM    835  O   VAL A 107      23.657  19.018   5.993  1.00 51.46           O  
ATOM    836  CB  VAL A 107      22.674  21.870   7.218  1.00 51.95           C  
ATOM    837  CG1 VAL A 107      23.342  21.174   8.384  1.00 51.14           C  
ATOM    838  CG2 VAL A 107      22.746  23.399   7.403  1.00 49.95           C  
ATOM    839  N   LEU A 108      21.709  19.696   5.120  1.00 51.99           N  
ATOM    840  CA  LEU A 108      21.279  18.337   4.813  1.00 52.78           C  
ATOM    841  C   LEU A 108      22.288  17.717   3.830  1.00 53.86           C  
ATOM    842  O   LEU A 108      22.668  16.547   3.957  1.00 53.61           O  
ATOM    843  CB  LEU A 108      19.828  18.315   4.285  1.00 52.55           C  
ATOM    844  CG  LEU A 108      18.729  18.660   5.325  1.00 51.86           C  
ATOM    845  CD1 LEU A 108      17.315  18.886   4.738  1.00 49.94           C  
ATOM    846  CD2 LEU A 108      18.657  17.580   6.387  1.00 50.54           C  
ATOM    847  N   ARG A 109      22.786  18.524   2.899  1.00 55.19           N  
ATOM    848  CA  ARG A 109      23.754  18.029   1.922  1.00 56.25           C  
ATOM    849  C   ARG A 109      25.113  17.707   2.530  1.00 56.41           C  
ATOM    850  O   ARG A 109      25.626  16.627   2.274  1.00 56.77           O  
ATOM    851  CB  ARG A 109      23.849  18.969   0.730  1.00 56.81           C  
ATOM    852  CG  ARG A 109      22.623  18.818  -0.155  1.00 59.42           C  
ATOM    853  CD  ARG A 109      22.280  20.064  -0.978  1.00 63.62           C  
ATOM    854  NE  ARG A 109      21.129  19.784  -1.847  1.00 67.38           N  
ATOM    855  CZ  ARG A 109      20.493  20.680  -2.605  1.00 69.48           C  
ATOM    856  NH1 ARG A 109      20.886  21.958  -2.618  1.00 69.55           N  
ATOM    857  NH2 ARG A 109      19.449  20.291  -3.354  1.00 69.27           N  
ATOM    858  N   GLN A 110      25.676  18.578   3.373  1.00 56.58           N  
ATOM    859  CA  GLN A 110      26.947  18.240   4.068  1.00 56.74           C  
ATOM    860  C   GLN A 110      26.876  16.944   4.933  1.00 56.65           C  
ATOM    861  O   GLN A 110      27.898  16.401   5.339  1.00 55.72           O  
ATOM    862  CB  GLN A 110      27.434  19.425   4.917  1.00 57.18           C  
ATOM    863  CG  GLN A 110      28.225  20.503   4.128  1.00 58.45           C  
ATOM    864  CD  GLN A 110      27.996  21.935   4.657  1.00 60.26           C  
ATOM    865  OE1 GLN A 110      28.839  22.483   5.370  1.00 61.58           O  
ATOM    866  NE2 GLN A 110      26.848  22.538   4.306  1.00 60.45           N  
ATOM    867  N   LEU A 111      25.652  16.480   5.212  1.00 57.01           N  
ATOM    868  CA  LEU A 111      25.380  15.215   5.934  1.00 56.83           C  
ATOM    869  C   LEU A 111      25.165  14.049   4.958  1.00 56.98           C  
ATOM    870  O   LEU A 111      25.732  12.980   5.153  1.00 56.54           O  
ATOM    871  CB  LEU A 111      24.137  15.344   6.836  1.00 56.70           C  
ATOM    872  CG  LEU A 111      24.092  16.456   7.891  1.00 55.48           C  
ATOM    873  CD1 LEU A 111      22.651  16.647   8.382  1.00 54.36           C  
ATOM    874  CD2 LEU A 111      25.048  16.142   9.028  1.00 55.18           C  
ATOM    875  N   ARG A 112      24.318  14.254   3.942  1.00 57.39           N  
ATOM    876  CA  ARG A 112      24.123  13.272   2.873  1.00 58.19           C  
ATOM    877  C   ARG A 112      25.472  12.916   2.279  1.00 58.92           C  
ATOM    878  O   ARG A 112      25.763  11.742   2.019  1.00 58.65           O  
ATOM    879  CB  ARG A 112      23.245  13.828   1.746  1.00 58.29           C  
ATOM    880  CG  ARG A 112      21.783  13.886   2.056  1.00 58.68           C  
ATOM    881  CD  ARG A 112      20.993  13.129   1.020  1.00 60.32           C  
ATOM    882  NE  ARG A 112      21.195  11.678   1.158  1.00 61.97           N  
ATOM    883  CZ  ARG A 112      20.707  10.755   0.325  1.00 62.52           C  
ATOM    884  NH1 ARG A 112      20.954   9.464   0.555  1.00 63.22           N  
ATOM    885  NH2 ARG A 112      19.973  11.109  -0.735  1.00 61.46           N  
ATOM    886  N   GLU A 113      26.299  13.952   2.087  1.00 59.69           N  
ATOM    887  CA  GLU A 113      27.605  13.787   1.469  1.00 60.05           C  
ATOM    888  C   GLU A 113      28.575  13.078   2.421  1.00 59.36           C  
ATOM    889  O   GLU A 113      29.387  12.270   1.959  1.00 59.82           O  
ATOM    890  CB  GLU A 113      28.155  15.133   0.931  1.00 60.73           C  
ATOM    891  CG  GLU A 113      27.238  15.913  -0.098  1.00 62.31           C  
ATOM    892  CD  GLU A 113      25.935  15.170  -0.545  1.00 64.71           C  
ATOM    893  OE1 GLU A 113      24.825  15.797  -0.555  1.00 63.99           O  
ATOM    894  OE2 GLU A 113      26.025  13.964  -0.900  1.00 65.92           O  
HETATM  895  N   MSE A 114      28.479  13.315   3.733  1.00 58.36           N  
HETATM  896  CA  MSE A 114      29.293  12.517   4.698  1.00 57.50           C  
HETATM  897  C   MSE A 114      28.693  11.125   5.032  1.00 54.82           C  
HETATM  898  O   MSE A 114      28.982  10.548   6.087  1.00 53.84           O  
HETATM  899  CB  MSE A 114      29.658  13.314   5.971  1.00 58.71           C  
HETATM  900  CG  MSE A 114      28.509  14.019   6.659  1.00 62.27           C  
HETATM  901 SE   MSE A 114      29.052  15.171   8.146  1.00 73.58          SE  
HETATM  902  CE  MSE A 114      30.129  13.887   9.223  1.00 69.87           C  
ATOM    903  N   GLY A 115      27.868  10.607   4.109  1.00 52.15           N  
ATOM    904  CA  GLY A 115      27.472   9.184   4.061  1.00 50.05           C  
ATOM    905  C   GLY A 115      26.330   8.800   4.992  1.00 48.06           C  
ATOM    906  O   GLY A 115      26.272   7.651   5.486  1.00 46.67           O  
ATOM    907  N   LEU A 116      25.431   9.772   5.220  1.00 45.60           N  
ATOM    908  CA  LEU A 116      24.389   9.656   6.252  1.00 43.24           C  
ATOM    909  C   LEU A 116      23.001   9.589   5.642  1.00 41.32           C  
ATOM    910  O   LEU A 116      22.569  10.511   4.950  1.00 41.25           O  
ATOM    911  CB  LEU A 116      24.512  10.758   7.318  1.00 42.66           C  
ATOM    912  CG  LEU A 116      25.656  10.571   8.332  1.00 41.99           C  
ATOM    913  CD1 LEU A 116      25.706  11.735   9.307  1.00 40.28           C  
ATOM    914  CD2 LEU A 116      25.626   9.223   9.099  1.00 41.08           C  
ATOM    915  N   PRO A 117      22.316   8.453   5.853  1.00 39.53           N  
ATOM    916  CA  PRO A 117      20.889   8.382   5.495  1.00 38.88           C  
ATOM    917  C   PRO A 117      20.064   9.359   6.367  1.00 37.04           C  
ATOM    918  O   PRO A 117      20.439   9.644   7.496  1.00 35.71           O  
ATOM    919  CB  PRO A 117      20.500   6.930   5.767  1.00 39.13           C  
ATOM    920  CG  PRO A 117      21.670   6.303   6.565  1.00 40.35           C  
ATOM    921  CD  PRO A 117      22.836   7.227   6.497  1.00 39.73           C  
ATOM    922  N   LEU A 118      18.981   9.884   5.808  1.00 35.52           N  
ATOM    923  CA  LEU A 118      18.231  10.956   6.446  1.00 34.29           C  
ATOM    924  C   LEU A 118      16.788  10.574   6.442  1.00 33.70           C  
ATOM    925  O   LEU A 118      16.305  10.020   5.450  1.00 33.75           O  
ATOM    926  CB  LEU A 118      18.399  12.298   5.713  1.00 33.68           C  
ATOM    927  CG  LEU A 118      19.807  12.894   5.601  1.00 32.10           C  
ATOM    928  CD1 LEU A 118      19.744  14.326   5.035  1.00 30.40           C  
ATOM    929  CD2 LEU A 118      20.613  12.830   6.920  1.00 30.38           C  
ATOM    930  N   GLY A 119      16.114  10.841   7.561  1.00 32.63           N  
ATOM    931  CA  GLY A 119      14.668  10.658   7.632  1.00 32.24           C  
ATOM    932  C   GLY A 119      13.930  11.761   8.370  1.00 31.14           C  
ATOM    933  O   GLY A 119      14.542  12.556   9.122  1.00 30.37           O  
ATOM    934  N   ILE A 120      12.619  11.792   8.138  1.00 30.58           N  
ATOM    935  CA  ILE A 120      11.663  12.568   8.931  1.00 31.18           C  
ATOM    936  C   ILE A 120      10.788  11.635   9.779  1.00 31.26           C  
ATOM    937  O   ILE A 120      10.276  10.612   9.270  1.00 31.90           O  
ATOM    938  CB  ILE A 120      10.701  13.326   8.041  1.00 31.28           C  
ATOM    939  CG1 ILE A 120      11.464  14.241   7.094  1.00 31.34           C  
ATOM    940  CG2 ILE A 120       9.717  14.149   8.879  1.00 32.17           C  
ATOM    941  CD1 ILE A 120      10.553  15.108   6.234  1.00 31.57           C  
ATOM    942  N   LEU A 121      10.615  11.984  11.054  1.00 30.76           N  
ATOM    943  CA  LEU A 121       9.608  11.353  11.933  1.00 30.27           C  
ATOM    944  C   LEU A 121       8.705  12.426  12.536  1.00 30.41           C  
ATOM    945  O   LEU A 121       9.182  13.274  13.290  1.00 30.42           O  
ATOM    946  CB  LEU A 121      10.234  10.510  13.036  1.00 29.89           C  
ATOM    947  CG  LEU A 121       9.227   9.718  13.886  1.00 30.82           C  
ATOM    948  CD1 LEU A 121       8.506   8.653  13.029  1.00 28.76           C  
ATOM    949  CD2 LEU A 121       9.903   9.081  15.094  1.00 30.90           C  
ATOM    950  N   SER A 122       7.416  12.384  12.172  1.00 30.48           N  
ATOM    951  CA  SER A 122       6.501  13.480  12.383  1.00 31.08           C  
ATOM    952  C   SER A 122       5.144  13.056  12.918  1.00 31.25           C  
ATOM    953  O   SER A 122       4.606  12.010  12.557  1.00 30.44           O  
ATOM    954  CB  SER A 122       6.288  14.216  11.070  1.00 31.30           C  
ATOM    955  OG  SER A 122       5.269  15.209  11.210  1.00 32.43           O  
ATOM    956  N   ASN A 123       4.582  13.897  13.777  1.00 32.10           N  
ATOM    957  CA  ASN A 123       3.226  13.698  14.281  1.00 32.37           C  
ATOM    958  C   ASN A 123       2.305  13.830  13.055  1.00 33.39           C  
ATOM    959  O   ASN A 123       1.179  13.298  13.002  1.00 32.07           O  
ATOM    960  CB  ASN A 123       2.884  14.740  15.384  1.00 31.97           C  
ATOM    961  CG  ASN A 123       3.255  14.282  16.818  1.00 30.52           C  
ATOM    962  OD1 ASN A 123       3.520  13.107  17.095  1.00 27.49           O  
ATOM    963  ND2 ASN A 123       3.251  15.237  17.746  1.00 29.18           N  
ATOM    964  N   GLY A 124       2.823  14.520  12.041  1.00 35.18           N  
ATOM    965  CA  GLY A 124       2.093  14.732  10.804  1.00 36.60           C  
ATOM    966  C   GLY A 124       1.586  13.462  10.177  1.00 38.21           C  
ATOM    967  O   GLY A 124       2.348  12.533   9.947  1.00 38.84           O  
ATOM    968  N   ASN A 125       0.285  13.389   9.923  1.00 39.87           N  
ATOM    969  CA  ASN A 125      -0.247  12.329   9.048  1.00 41.00           C  
ATOM    970  C   ASN A 125       0.477  12.402   7.671  1.00 43.44           C  
ATOM    971  O   ASN A 125       0.984  13.469   7.298  1.00 44.00           O  
ATOM    972  CB  ASN A 125      -1.800  12.349   8.932  1.00 40.47           C  
ATOM    973  CG  ASN A 125      -2.394  13.763   8.774  1.00 38.54           C  
ATOM    974  OD1 ASN A 125      -3.538  13.927   8.402  1.00 38.15           O  
ATOM    975  ND2 ASN A 125      -1.621  14.761   9.074  1.00 38.31           N  
ATOM    976  N   PRO A 126       0.603  11.261   6.961  1.00 45.79           N  
ATOM    977  CA  PRO A 126       1.500  11.312   5.800  1.00 47.67           C  
ATOM    978  C   PRO A 126       0.927  12.206   4.692  1.00 49.21           C  
ATOM    979  O   PRO A 126       1.657  13.030   4.176  1.00 50.14           O  
ATOM    980  CB  PRO A 126       1.643   9.835   5.355  1.00 47.34           C  
ATOM    981  CG  PRO A 126       0.436   9.129   5.899  1.00 47.43           C  
ATOM    982  CD  PRO A 126      -0.042   9.938   7.127  1.00 46.29           C  
ATOM    983  N   GLN A 127      -0.363  12.075   4.364  1.00 50.93           N  
ATOM    984  CA  GLN A 127      -0.991  12.989   3.391  1.00 52.07           C  
ATOM    985  C   GLN A 127      -0.535  14.453   3.539  1.00 52.55           C  
ATOM    986  O   GLN A 127      -0.240  15.109   2.524  1.00 52.65           O  
ATOM    987  CB  GLN A 127      -2.525  12.882   3.387  1.00 52.33           C  
ATOM    988  CG  GLN A 127      -3.062  11.922   2.334  1.00 53.56           C  
ATOM    989  CD  GLN A 127      -4.568  11.707   2.455  1.00 57.10           C  
ATOM    990  OE1 GLN A 127      -5.271  12.512   3.072  1.00 58.32           O  
ATOM    991  NE2 GLN A 127      -5.065  10.606   1.882  1.00 58.38           N  
HETATM  992  N   MSE A 128      -0.431  14.961   4.769  1.00 53.09           N  
HETATM  993  CA  MSE A 128      -0.002  16.372   4.965  1.00 53.57           C  
HETATM  994  C   MSE A 128       1.526  16.515   4.990  1.00 54.30           C  
HETATM  995  O   MSE A 128       2.083  17.581   4.700  1.00 54.17           O  
HETATM  996  CB  MSE A 128      -0.691  17.021   6.201  1.00 53.17           C  
HETATM  997  CG  MSE A 128       0.030  16.885   7.549  1.00 51.41           C  
HETATM  998 SE   MSE A 128      -1.139  17.418   9.077  1.00 48.67          SE  
HETATM  999  CE  MSE A 128      -0.469  19.226   9.447  1.00 44.97           C  
ATOM   1000  N   LEU A 129       2.192  15.425   5.332  1.00 55.68           N  
ATOM   1001  CA  LEU A 129       3.636  15.407   5.477  1.00 56.90           C  
ATOM   1002  C   LEU A 129       4.354  15.426   4.124  1.00 57.68           C  
ATOM   1003  O   LEU A 129       5.487  15.897   4.025  1.00 57.24           O  
ATOM   1004  CB  LEU A 129       4.012  14.154   6.270  1.00 57.07           C  
ATOM   1005  CG  LEU A 129       5.471  13.874   6.635  1.00 57.81           C  
ATOM   1006  CD1 LEU A 129       6.289  15.154   6.919  1.00 58.42           C  
ATOM   1007  CD2 LEU A 129       5.497  12.908   7.831  1.00 57.86           C  
ATOM   1008  N   GLU A 130       3.668  14.912   3.106  1.00 59.11           N  
ATOM   1009  CA  GLU A 130       4.256  14.588   1.802  1.00 60.61           C  
ATOM   1010  C   GLU A 130       4.361  15.812   0.882  1.00 61.24           C  
ATOM   1011  O   GLU A 130       5.419  16.082   0.279  1.00 60.70           O  
ATOM   1012  CB  GLU A 130       3.379  13.542   1.109  1.00 61.00           C  
ATOM   1013  CG  GLU A 130       3.190  12.171   1.856  1.00 62.73           C  
ATOM   1014  CD  GLU A 130       1.957  11.390   1.325  1.00 64.18           C  
ATOM   1015  OE1 GLU A 130       1.008  12.055   0.865  1.00 63.88           O  
ATOM   1016  OE2 GLU A 130       1.931  10.132   1.349  1.00 65.01           O  
ATOM   1017  N   ILE A 131       3.230  16.515   0.760  1.00 62.38           N  
ATOM   1018  CA  ILE A 131       3.174  17.830   0.097  1.00 63.12           C  
ATOM   1019  C   ILE A 131       3.994  18.828   0.882  1.00 62.90           C  
ATOM   1020  O   ILE A 131       4.843  19.521   0.300  1.00 63.28           O  
ATOM   1021  CB  ILE A 131       1.712  18.392  -0.064  1.00 63.49           C  
ATOM   1022  CG1 ILE A 131       1.375  18.601  -1.549  1.00 64.75           C  
ATOM   1023  CG2 ILE A 131       1.560  19.760   0.590  1.00 63.23           C  
ATOM   1024  CD1 ILE A 131       1.628  17.398  -2.418  1.00 65.20           C  
ATOM   1025  N   ALA A 132       3.754  18.882   2.197  1.00 62.02           N  
ATOM   1026  CA  ALA A 132       4.553  19.733   3.070  1.00 61.26           C  
ATOM   1027  C   ALA A 132       6.016  19.649   2.650  1.00 60.29           C  
ATOM   1028  O   ALA A 132       6.673  20.657   2.538  1.00 60.24           O  
ATOM   1029  CB  ALA A 132       4.368  19.347   4.544  1.00 61.32           C  
ATOM   1030  N   VAL A 133       6.503  18.449   2.354  1.00 59.81           N  
ATOM   1031  CA  VAL A 133       7.905  18.256   1.948  1.00 59.49           C  
ATOM   1032  C   VAL A 133       8.247  18.877   0.583  1.00 59.29           C  
ATOM   1033  O   VAL A 133       9.358  19.398   0.379  1.00 58.43           O  
ATOM   1034  CB  VAL A 133       8.253  16.769   1.870  1.00 59.45           C  
ATOM   1035  CG1 VAL A 133       9.764  16.602   1.634  1.00 59.42           C  
ATOM   1036  CG2 VAL A 133       7.780  16.044   3.132  1.00 59.13           C  
ATOM   1037  N   LYS A 134       7.288  18.765  -0.342  1.00 59.21           N  
ATOM   1038  CA  LYS A 134       7.398  19.312  -1.688  1.00 59.44           C  
ATOM   1039  C   LYS A 134       7.375  20.862  -1.734  1.00 59.42           C  
ATOM   1040  O   LYS A 134       7.920  21.484  -2.654  1.00 59.04           O  
ATOM   1041  CB  LYS A 134       6.295  18.717  -2.559  1.00 59.81           C  
ATOM   1042  CG  LYS A 134       6.619  17.306  -3.060  1.00 60.62           C  
ATOM   1043  CD  LYS A 134       5.376  16.402  -3.119  1.00 62.32           C  
ATOM   1044  CE  LYS A 134       4.336  16.887  -4.132  1.00 62.65           C  
ATOM   1045  NZ  LYS A 134       3.025  16.236  -3.902  1.00 61.99           N  
ATOM   1046  N   SER A 135       6.756  21.481  -0.736  1.00 59.24           N  
ATOM   1047  CA  SER A 135       6.985  22.899  -0.456  1.00 58.95           C  
ATOM   1048  C   SER A 135       8.326  23.064   0.260  1.00 58.97           C  
ATOM   1049  O   SER A 135       8.381  22.964   1.474  1.00 59.53           O  
ATOM   1050  CB  SER A 135       5.872  23.414   0.441  1.00 58.72           C  
ATOM   1051  OG  SER A 135       4.628  23.057  -0.108  1.00 57.97           O  
ATOM   1052  N   ALA A 136       9.415  23.303  -0.461  1.00 58.75           N  
ATOM   1053  CA  ALA A 136      10.715  23.460   0.210  1.00 58.57           C  
ATOM   1054  C   ALA A 136      11.896  22.811  -0.500  1.00 58.53           C  
ATOM   1055  O   ALA A 136      13.035  23.041  -0.096  1.00 58.89           O  
ATOM   1056  CB  ALA A 136      10.648  22.933   1.618  1.00 58.12           C  
ATOM   1057  N   GLY A 137      11.646  21.988  -1.515  1.00 58.26           N  
ATOM   1058  CA  GLY A 137      12.731  21.461  -2.348  1.00 58.42           C  
ATOM   1059  C   GLY A 137      13.599  20.396  -1.698  1.00 58.50           C  
ATOM   1060  O   GLY A 137      14.779  20.241  -2.049  1.00 58.47           O  
HETATM 1061  N   MSE A 138      13.029  19.652  -0.754  1.00 58.46           N  
HETATM 1062  CA  MSE A 138      13.820  18.624  -0.051  1.00 58.64           C  
HETATM 1063  C   MSE A 138      13.485  17.195  -0.504  1.00 58.30           C  
HETATM 1064  O   MSE A 138      13.983  16.215   0.094  1.00 58.32           O  
HETATM 1065  CB  MSE A 138      13.628  18.738   1.456  1.00 58.76           C  
HETATM 1066  CG  MSE A 138      14.093  20.047   2.054  1.00 58.75           C  
HETATM 1067 SE   MSE A 138      13.655  20.030   3.936  1.00 61.99          SE  
HETATM 1068  CE  MSE A 138      11.674  20.227   3.937  1.00 45.67           C  
ATOM   1069  N   SER A 139      12.651  17.079  -1.551  1.00 57.56           N  
ATOM   1070  CA  SER A 139      12.377  15.783  -2.199  1.00 56.36           C  
ATOM   1071  C   SER A 139      13.731  15.133  -2.620  1.00 55.02           C  
ATOM   1072  O   SER A 139      14.625  15.821  -3.123  1.00 54.38           O  
ATOM   1073  CB  SER A 139      11.410  15.973  -3.387  1.00 56.55           C  
ATOM   1074  OG  SER A 139      10.306  16.846  -3.078  1.00 57.15           O  
ATOM   1075  N   GLY A 140      13.897  13.838  -2.330  1.00 53.12           N  
ATOM   1076  CA  GLY A 140      15.147  13.114  -2.623  1.00 51.84           C  
ATOM   1077  C   GLY A 140      16.166  12.971  -1.489  1.00 50.86           C  
ATOM   1078  O   GLY A 140      16.974  12.016  -1.469  1.00 50.18           O  
ATOM   1079  N   LEU A 141      16.133  13.906  -0.532  1.00 49.63           N  
ATOM   1080  CA  LEU A 141      17.128  13.951   0.558  1.00 48.01           C  
ATOM   1081  C   LEU A 141      16.823  12.925   1.632  1.00 45.99           C  
ATOM   1082  O   LEU A 141      17.735  12.402   2.266  1.00 45.27           O  
ATOM   1083  CB  LEU A 141      17.241  15.368   1.162  1.00 48.42           C  
ATOM   1084  CG  LEU A 141      17.854  16.445   0.229  1.00 49.35           C  
ATOM   1085  CD1 LEU A 141      16.795  17.050  -0.705  1.00 50.00           C  
ATOM   1086  CD2 LEU A 141      18.547  17.551   1.012  1.00 50.11           C  
ATOM   1087  N   PHE A 142      15.541  12.629   1.817  1.00 44.69           N  
ATOM   1088  CA  PHE A 142      15.116  11.618   2.796  1.00 43.56           C  
ATOM   1089  C   PHE A 142      14.834  10.231   2.191  1.00 42.56           C  
ATOM   1090  O   PHE A 142      13.949  10.032   1.346  1.00 41.96           O  
ATOM   1091  CB  PHE A 142      13.887  12.092   3.580  1.00 43.55           C  
ATOM   1092  CG  PHE A 142      14.081  13.408   4.248  1.00 42.90           C  
ATOM   1093  CD1 PHE A 142      15.077  13.579   5.175  1.00 45.09           C  
ATOM   1094  CD2 PHE A 142      13.278  14.472   3.943  1.00 44.65           C  
ATOM   1095  CE1 PHE A 142      15.285  14.799   5.788  1.00 44.91           C  
ATOM   1096  CE2 PHE A 142      13.471  15.701   4.550  1.00 45.12           C  
ATOM   1097  CZ  PHE A 142      14.474  15.864   5.472  1.00 44.65           C  
ATOM   1098  N   ASP A 143      15.592   9.269   2.689  1.00 41.98           N  
ATOM   1099  CA  ASP A 143      15.268   7.860   2.531  1.00 41.23           C  
ATOM   1100  C   ASP A 143      13.863   7.515   3.083  1.00 39.98           C  
ATOM   1101  O   ASP A 143      13.043   6.932   2.365  1.00 40.19           O  
ATOM   1102  CB  ASP A 143      16.338   7.019   3.212  1.00 41.09           C  
ATOM   1103  CG  ASP A 143      17.692   7.157   2.545  1.00 43.37           C  
ATOM   1104  OD1 ASP A 143      17.918   8.172   1.840  1.00 47.87           O  
ATOM   1105  OD2 ASP A 143      18.540   6.248   2.726  1.00 46.05           O  
ATOM   1106  N   HIS A 144      13.570   7.899   4.333  1.00 38.04           N  
ATOM   1107  CA  HIS A 144      12.268   7.569   4.950  1.00 35.93           C  
ATOM   1108  C   HIS A 144      11.560   8.816   5.460  1.00 33.28           C  
ATOM   1109  O   HIS A 144      12.164   9.668   6.068  1.00 32.81           O  
ATOM   1110  CB  HIS A 144      12.450   6.566   6.090  1.00 36.19           C  
ATOM   1111  CG  HIS A 144      13.259   5.347   5.729  1.00 39.29           C  
ATOM   1112  ND1 HIS A 144      12.707   4.240   5.108  1.00 40.26           N  
ATOM   1113  CD2 HIS A 144      14.569   5.049   5.935  1.00 39.78           C  
ATOM   1114  CE1 HIS A 144      13.642   3.317   4.951  1.00 41.19           C  
ATOM   1115  NE2 HIS A 144      14.780   3.781   5.443  1.00 40.74           N  
ATOM   1116  N   VAL A 145      10.275   8.919   5.163  1.00 30.96           N  
ATOM   1117  CA  VAL A 145       9.432  10.004   5.621  1.00 29.02           C  
ATOM   1118  C   VAL A 145       8.323   9.287   6.420  1.00 27.90           C  
ATOM   1119  O   VAL A 145       7.418   8.647   5.840  1.00 28.32           O  
ATOM   1120  CB  VAL A 145       8.918  10.856   4.437  1.00 29.39           C  
ATOM   1121  CG1 VAL A 145       7.744  11.762   4.840  1.00 29.64           C  
ATOM   1122  CG2 VAL A 145      10.054  11.709   3.850  1.00 28.39           C  
ATOM   1123  N   LEU A 146       8.447   9.353   7.749  1.00 25.55           N  
ATOM   1124  CA  LEU A 146       7.651   8.538   8.668  1.00 24.24           C  
ATOM   1125  C   LEU A 146       6.608   9.372   9.460  1.00 23.51           C  
ATOM   1126  O   LEU A 146       6.841  10.502   9.860  1.00 23.45           O  
ATOM   1127  CB  LEU A 146       8.590   7.759   9.612  1.00 22.67           C  
ATOM   1128  CG  LEU A 146       9.745   6.976   8.932  1.00 22.14           C  
ATOM   1129  CD1 LEU A 146      10.801   6.654   9.896  1.00 18.36           C  
ATOM   1130  CD2 LEU A 146       9.245   5.672   8.271  1.00 21.91           C  
ATOM   1131  N   SER A 147       5.437   8.787   9.636  1.00 23.20           N  
ATOM   1132  CA  SER A 147       4.329   9.396  10.339  1.00 22.27           C  
ATOM   1133  C   SER A 147       3.879   8.484  11.447  1.00 20.84           C  
ATOM   1134  O   SER A 147       3.760   7.279  11.254  1.00 21.38           O  
ATOM   1135  CB  SER A 147       3.175   9.577   9.384  1.00 22.95           C  
ATOM   1136  OG  SER A 147       1.979   9.931  10.051  1.00 23.58           O  
ATOM   1137  N   VAL A 148       3.567   9.070  12.585  1.00 19.08           N  
ATOM   1138  CA  VAL A 148       2.987   8.336  13.697  1.00 18.28           C  
ATOM   1139  C   VAL A 148       1.634   7.760  13.353  1.00 17.38           C  
ATOM   1140  O   VAL A 148       1.040   7.045  14.127  1.00 15.68           O  
ATOM   1141  CB  VAL A 148       2.811   9.252  14.914  1.00 18.49           C  
ATOM   1142  CG1 VAL A 148       4.129   9.933  15.258  1.00 15.57           C  
ATOM   1143  CG2 VAL A 148       1.656  10.292  14.643  1.00 19.57           C  
ATOM   1144  N   ASP A 149       1.115   8.083  12.184  1.00 18.84           N  
ATOM   1145  CA  ASP A 149      -0.134   7.501  11.758  1.00 20.32           C  
ATOM   1146  C   ASP A 149      -0.095   5.953  11.601  1.00 20.46           C  
ATOM   1147  O   ASP A 149      -1.119   5.286  11.660  1.00 21.31           O  
ATOM   1148  CB  ASP A 149      -0.531   8.126  10.427  1.00 21.68           C  
ATOM   1149  CG  ASP A 149      -1.908   7.717   9.998  1.00 21.43           C  
ATOM   1150  OD1 ASP A 149      -2.924   8.271  10.503  1.00 20.71           O  
ATOM   1151  OD2 ASP A 149      -1.954   6.856   9.135  1.00 23.62           O  
ATOM   1152  N   ALA A 150       1.084   5.413  11.359  1.00 20.75           N  
ATOM   1153  CA  ALA A 150       1.315   3.964  11.219  1.00 20.93           C  
ATOM   1154  C   ALA A 150       0.985   3.255  12.522  1.00 21.61           C  
ATOM   1155  O   ALA A 150       0.545   2.098  12.505  1.00 22.81           O  
ATOM   1156  CB  ALA A 150       2.804   3.727  10.842  1.00 20.50           C  
ATOM   1157  N   VAL A 151       1.186   3.948  13.661  1.00 20.26           N  
ATOM   1158  CA  VAL A 151       0.947   3.334  14.925  1.00 19.16           C  
ATOM   1159  C   VAL A 151      -0.248   3.942  15.666  1.00 19.72           C  
ATOM   1160  O   VAL A 151      -0.600   3.458  16.717  1.00 19.51           O  
ATOM   1161  CB  VAL A 151       2.211   3.365  15.760  1.00 19.26           C  
ATOM   1162  CG1 VAL A 151       3.352   2.546  15.022  1.00 17.92           C  
ATOM   1163  CG2 VAL A 151       2.680   4.839  15.989  1.00 17.74           C  
ATOM   1164  N   ARG A 152      -0.872   5.007  15.145  1.00 19.88           N  
ATOM   1165  CA  ARG A 152      -2.053   5.569  15.762  1.00 18.86           C  
ATOM   1166  C   ARG A 152      -1.773   6.105  17.163  1.00 18.10           C  
ATOM   1167  O   ARG A 152      -2.650   6.154  17.990  1.00 16.88           O  
ATOM   1168  CB  ARG A 152      -3.195   4.537  15.769  1.00 19.08           C  
ATOM   1169  CG  ARG A 152      -3.618   4.054  14.302  1.00 20.97           C  
ATOM   1170  CD  ARG A 152      -4.729   3.001  14.273  1.00 22.59           C  
ATOM   1171  NE  ARG A 152      -5.836   3.305  15.182  1.00 25.03           N  
ATOM   1172  CZ  ARG A 152      -6.826   4.130  14.905  1.00 28.29           C  
ATOM   1173  NH1 ARG A 152      -6.879   4.739  13.708  1.00 31.78           N  
ATOM   1174  NH2 ARG A 152      -7.777   4.337  15.813  1.00 26.75           N  
ATOM   1175  N   LEU A 153      -0.555   6.568  17.382  1.00 17.10           N  
ATOM   1176  CA  LEU A 153      -0.149   7.091  18.694  1.00 17.47           C  
ATOM   1177  C   LEU A 153       0.872   8.216  18.504  1.00 17.44           C  
ATOM   1178  O   LEU A 153       1.846   8.077  17.688  1.00 19.33           O  
ATOM   1179  CB  LEU A 153       0.483   5.997  19.556  1.00 16.57           C  
ATOM   1180  CG  LEU A 153      -0.459   4.898  20.099  1.00 16.83           C  
ATOM   1181  CD1 LEU A 153       0.346   3.689  20.423  1.00 15.36           C  
ATOM   1182  CD2 LEU A 153      -1.315   5.333  21.339  1.00 15.24           C  
ATOM   1183  N   TYR A 154       0.684   9.304  19.234  1.00 16.22           N  
ATOM   1184  CA  TYR A 154       1.554  10.472  19.093  1.00 15.69           C  
ATOM   1185  C   TYR A 154       2.737  10.372  20.025  1.00 15.95           C  
ATOM   1186  O   TYR A 154       2.676   9.731  21.067  1.00 15.35           O  
ATOM   1187  CB  TYR A 154       0.756  11.727  19.392  1.00 16.02           C  
ATOM   1188  CG  TYR A 154      -0.200  12.073  18.302  1.00 14.55           C  
ATOM   1189  CD1 TYR A 154      -1.533  11.829  18.435  1.00 11.70           C  
ATOM   1190  CD2 TYR A 154       0.248  12.649  17.105  1.00 17.50           C  
ATOM   1191  CE1 TYR A 154      -2.431  12.127  17.403  1.00 15.23           C  
ATOM   1192  CE2 TYR A 154      -0.641  12.925  16.042  1.00 17.94           C  
ATOM   1193  CZ  TYR A 154      -1.988  12.709  16.221  1.00 17.77           C  
ATOM   1194  OH  TYR A 154      -2.906  13.020  15.208  1.00 17.44           O  
ATOM   1195  N   LYS A 155       3.831  11.019  19.667  1.00 16.70           N  
ATOM   1196  CA  LYS A 155       4.901  11.272  20.621  1.00 16.89           C  
ATOM   1197  C   LYS A 155       4.276  11.881  21.839  1.00 16.32           C  
ATOM   1198  O   LYS A 155       3.357  12.707  21.701  1.00 17.95           O  
ATOM   1199  CB  LYS A 155       5.915  12.280  20.084  1.00 17.46           C  
ATOM   1200  CG  LYS A 155       6.631  11.843  18.801  1.00 20.80           C  
ATOM   1201  CD  LYS A 155       7.045  13.091  18.019  1.00 23.40           C  
ATOM   1202  CE  LYS A 155       8.204  12.882  17.065  1.00 23.81           C  
ATOM   1203  NZ  LYS A 155       8.476  14.197  16.311  1.00 24.40           N  
ATOM   1204  N   THR A 156       4.773  11.555  23.029  1.00 15.68           N  
ATOM   1205  CA  THR A 156       6.034  10.815  23.255  1.00 15.27           C  
ATOM   1206  C   THR A 156       5.921   9.281  23.358  1.00 15.84           C  
ATOM   1207  O   THR A 156       6.796   8.642  23.930  1.00 16.45           O  
ATOM   1208  CB  THR A 156       6.649  11.299  24.547  1.00 15.25           C  
ATOM   1209  OG1 THR A 156       5.610  11.407  25.512  1.00 14.69           O  
ATOM   1210  CG2 THR A 156       7.270  12.720  24.380  1.00 13.34           C  
ATOM   1211  N   ALA A 157       4.837   8.708  22.834  1.00 14.50           N  
ATOM   1212  CA  ALA A 157       4.554   7.295  22.915  1.00 14.39           C  
ATOM   1213  C   ALA A 157       5.686   6.442  22.346  1.00 14.79           C  
ATOM   1214  O   ALA A 157       6.151   6.747  21.255  1.00 15.34           O  
ATOM   1215  CB  ALA A 157       3.211   7.018  22.113  1.00 14.12           C  
ATOM   1216  N   PRO A 158       6.134   5.379  23.069  1.00 15.17           N  
ATOM   1217  CA  PRO A 158       7.248   4.544  22.546  1.00 15.54           C  
ATOM   1218  C   PRO A 158       7.037   4.052  21.099  1.00 16.11           C  
ATOM   1219  O   PRO A 158       7.985   3.984  20.335  1.00 12.57           O  
ATOM   1220  CB  PRO A 158       7.291   3.342  23.489  1.00 15.29           C  
ATOM   1221  CG  PRO A 158       6.793   3.867  24.812  1.00 14.10           C  
ATOM   1222  CD  PRO A 158       5.864   5.078  24.494  1.00 16.10           C  
ATOM   1223  N   ALA A 159       5.783   3.740  20.754  1.00 17.95           N  
ATOM   1224  CA  ALA A 159       5.477   3.139  19.455  1.00 18.53           C  
ATOM   1225  C   ALA A 159       5.793   4.153  18.348  1.00 18.56           C  
ATOM   1226  O   ALA A 159       6.086   3.741  17.222  1.00 18.04           O  
ATOM   1227  CB  ALA A 159       3.997   2.697  19.366  1.00 18.75           C  
ATOM   1228  N   ALA A 160       5.680   5.451  18.660  1.00 18.78           N  
ATOM   1229  CA  ALA A 160       6.008   6.531  17.692  1.00 18.97           C  
ATOM   1230  C   ALA A 160       7.501   6.624  17.501  1.00 19.27           C  
ATOM   1231  O   ALA A 160       7.966   6.634  16.381  1.00 19.44           O  
ATOM   1232  CB  ALA A 160       5.470   7.883  18.130  1.00 19.16           C  
ATOM   1233  N   TYR A 161       8.255   6.689  18.593  1.00 20.02           N  
ATOM   1234  CA  TYR A 161       9.722   6.731  18.507  1.00 20.55           C  
ATOM   1235  C   TYR A 161      10.248   5.455  17.808  1.00 20.82           C  
ATOM   1236  O   TYR A 161      11.113   5.523  16.907  1.00 20.90           O  
ATOM   1237  CB  TYR A 161      10.371   6.948  19.883  1.00 21.14           C  
ATOM   1238  CG  TYR A 161      10.156   8.356  20.449  1.00 19.74           C  
ATOM   1239  CD1 TYR A 161      10.565   9.506  19.728  1.00 19.84           C  
ATOM   1240  CD2 TYR A 161       9.580   8.541  21.691  1.00 18.55           C  
ATOM   1241  CE1 TYR A 161      10.348  10.817  20.224  1.00 15.84           C  
ATOM   1242  CE2 TYR A 161       9.364   9.854  22.213  1.00 19.17           C  
ATOM   1243  CZ  TYR A 161       9.752  10.983  21.468  1.00 18.77           C  
ATOM   1244  OH  TYR A 161       9.549  12.246  22.000  1.00 20.46           O  
ATOM   1245  N   ALA A 162       9.644   4.314  18.135  1.00 19.75           N  
ATOM   1246  CA  ALA A 162      10.106   3.062  17.593  1.00 19.81           C  
ATOM   1247  C   ALA A 162      10.062   2.994  16.088  1.00 19.98           C  
ATOM   1248  O   ALA A 162      10.746   2.153  15.534  1.00 21.10           O  
ATOM   1249  CB  ALA A 162       9.371   1.868  18.178  1.00 18.76           C  
ATOM   1250  N   LEU A 163       9.279   3.834  15.431  1.00 20.44           N  
ATOM   1251  CA  LEU A 163       9.210   3.776  13.979  1.00 22.31           C  
ATOM   1252  C   LEU A 163      10.600   3.961  13.316  1.00 22.81           C  
ATOM   1253  O   LEU A 163      10.857   3.381  12.267  1.00 23.49           O  
ATOM   1254  CB  LEU A 163       8.161   4.767  13.379  1.00 21.61           C  
ATOM   1255  CG  LEU A 163       6.658   4.502  13.597  1.00 20.52           C  
ATOM   1256  CD1 LEU A 163       5.792   5.745  13.312  1.00 16.49           C  
ATOM   1257  CD2 LEU A 163       6.172   3.328  12.791  1.00 20.41           C  
ATOM   1258  N   ALA A 164      11.488   4.745  13.915  1.00 23.83           N  
ATOM   1259  CA  ALA A 164      12.706   5.131  13.188  1.00 24.26           C  
ATOM   1260  C   ALA A 164      13.761   4.037  13.234  1.00 24.42           C  
ATOM   1261  O   ALA A 164      14.273   3.668  12.192  1.00 24.27           O  
ATOM   1262  CB  ALA A 164      13.241   6.455  13.632  1.00 24.27           C  
ATOM   1263  N   PRO A 165      14.036   3.455  14.409  1.00 24.96           N  
ATOM   1264  CA  PRO A 165      14.875   2.262  14.340  1.00 26.01           C  
ATOM   1265  C   PRO A 165      14.371   1.231  13.323  1.00 27.94           C  
ATOM   1266  O   PRO A 165      15.189   0.715  12.553  1.00 27.96           O  
ATOM   1267  CB  PRO A 165      14.844   1.742  15.758  1.00 25.74           C  
ATOM   1268  CG  PRO A 165      14.779   3.042  16.568  1.00 24.64           C  
ATOM   1269  CD  PRO A 165      13.777   3.846  15.804  1.00 25.41           C  
ATOM   1270  N   ARG A 166      13.051   1.000  13.250  1.00 29.11           N  
ATOM   1271  CA  ARG A 166      12.511  -0.018  12.339  1.00 29.96           C  
ATOM   1272  C   ARG A 166      12.794   0.263  10.936  1.00 30.42           C  
ATOM   1273  O   ARG A 166      13.256  -0.614  10.244  1.00 31.22           O  
ATOM   1274  CB  ARG A 166      10.997  -0.174  12.405  1.00 29.83           C  
ATOM   1275  CG  ARG A 166      10.593  -1.312  13.303  1.00 32.56           C  
ATOM   1276  CD  ARG A 166       9.303  -2.017  12.825  1.00 32.38           C  
ATOM   1277  NE  ARG A 166       8.154  -1.133  12.812  1.00 28.42           N  
ATOM   1278  CZ  ARG A 166       7.684  -0.533  13.879  1.00 27.75           C  
ATOM   1279  NH1 ARG A 166       8.266  -0.710  15.062  1.00 31.45           N  
ATOM   1280  NH2 ARG A 166       6.603   0.212  13.780  1.00 28.56           N  
ATOM   1281  N   ALA A 167      12.442   1.465  10.484  1.00 31.18           N  
ATOM   1282  CA  ALA A 167      12.656   1.856   9.079  1.00 31.42           C  
ATOM   1283  C   ALA A 167      14.155   1.846   8.650  1.00 32.26           C  
ATOM   1284  O   ALA A 167      14.459   1.491   7.521  1.00 30.94           O  
ATOM   1285  CB  ALA A 167      12.040   3.208   8.799  1.00 30.61           C  
ATOM   1286  N   PHE A 168      15.055   2.219   9.564  1.00 33.99           N  
ATOM   1287  CA  PHE A 168      16.482   2.370   9.241  1.00 36.25           C  
ATOM   1288  C   PHE A 168      17.319   1.100   9.427  1.00 37.42           C  
ATOM   1289  O   PHE A 168      18.460   1.068   8.982  1.00 38.19           O  
ATOM   1290  CB  PHE A 168      17.095   3.558  10.018  1.00 36.33           C  
ATOM   1291  CG  PHE A 168      16.766   4.891   9.384  1.00 39.00           C  
ATOM   1292  CD1 PHE A 168      17.608   5.451   8.445  1.00 39.90           C  
ATOM   1293  CD2 PHE A 168      15.545   5.509   9.637  1.00 38.76           C  
ATOM   1294  CE1 PHE A 168      17.266   6.638   7.820  1.00 41.61           C  
ATOM   1295  CE2 PHE A 168      15.197   6.682   9.008  1.00 40.00           C  
ATOM   1296  CZ  PHE A 168      16.054   7.252   8.099  1.00 41.03           C  
ATOM   1297  N   GLY A 169      16.748   0.091  10.090  1.00 37.98           N  
ATOM   1298  CA  GLY A 169      17.404  -1.162  10.340  1.00 38.39           C  
ATOM   1299  C   GLY A 169      18.542  -1.026  11.321  1.00 39.43           C  
ATOM   1300  O   GLY A 169      19.406  -1.896  11.357  1.00 40.00           O  
ATOM   1301  N   VAL A 170      18.538   0.046  12.129  1.00 39.71           N  
ATOM   1302  CA  VAL A 170      19.557   0.283  13.167  1.00 39.52           C  
ATOM   1303  C   VAL A 170      18.926   0.549  14.550  1.00 39.03           C  
ATOM   1304  O   VAL A 170      17.795   1.014  14.629  1.00 38.53           O  
ATOM   1305  CB  VAL A 170      20.504   1.467  12.792  1.00 39.99           C  
ATOM   1306  CG1 VAL A 170      21.178   1.202  11.426  1.00 41.40           C  
ATOM   1307  CG2 VAL A 170      19.762   2.794  12.760  1.00 39.44           C  
ATOM   1308  N   PRO A 171      19.654   0.221  15.640  1.00 38.19           N  
ATOM   1309  CA  PRO A 171      19.216   0.536  16.986  1.00 37.53           C  
ATOM   1310  C   PRO A 171      19.082   2.024  17.127  1.00 36.53           C  
ATOM   1311  O   PRO A 171      19.768   2.749  16.424  1.00 37.35           O  
ATOM   1312  CB  PRO A 171      20.386   0.070  17.871  1.00 37.43           C  
ATOM   1313  CG  PRO A 171      21.066  -0.930  17.103  1.00 38.03           C  
ATOM   1314  CD  PRO A 171      20.884  -0.591  15.648  1.00 38.55           C  
ATOM   1315  N   ALA A 172      18.225   2.455  18.045  1.00 35.84           N  
ATOM   1316  CA  ALA A 172      18.087   3.864  18.471  1.00 34.69           C  
ATOM   1317  C   ALA A 172      19.446   4.551  18.758  1.00 33.87           C  
ATOM   1318  O   ALA A 172      19.676   5.700  18.346  1.00 32.38           O  
ATOM   1319  CB  ALA A 172      17.198   3.940  19.716  1.00 33.44           C  
ATOM   1320  N   ALA A 173      20.334   3.847  19.457  1.00 34.05           N  
ATOM   1321  CA  ALA A 173      21.631   4.443  19.857  1.00 34.22           C  
ATOM   1322  C   ALA A 173      22.449   4.942  18.676  1.00 33.69           C  
ATOM   1323  O   ALA A 173      23.270   5.859  18.826  1.00 34.24           O  
ATOM   1324  CB  ALA A 173      22.442   3.489  20.684  1.00 34.89           C  
ATOM   1325  N   GLN A 174      22.195   4.386  17.503  1.00 32.47           N  
ATOM   1326  CA  GLN A 174      22.959   4.752  16.317  1.00 32.71           C  
ATOM   1327  C   GLN A 174      22.230   5.727  15.388  1.00 31.27           C  
ATOM   1328  O   GLN A 174      22.694   5.980  14.281  1.00 30.49           O  
ATOM   1329  CB  GLN A 174      23.323   3.471  15.529  1.00 33.12           C  
ATOM   1330  CG  GLN A 174      24.239   2.504  16.315  1.00 35.43           C  
ATOM   1331  CD  GLN A 174      24.390   1.130  15.639  1.00 39.10           C  
ATOM   1332  OE1 GLN A 174      24.242   0.993  14.411  1.00 38.54           O  
ATOM   1333  NE2 GLN A 174      24.693   0.104  16.452  1.00 40.99           N  
ATOM   1334  N   ILE A 175      21.075   6.233  15.807  1.00 29.60           N  
ATOM   1335  CA  ILE A 175      20.365   7.264  15.046  1.00 28.52           C  
ATOM   1336  C   ILE A 175      20.530   8.559  15.819  1.00 27.14           C  
ATOM   1337  O   ILE A 175      20.434   8.571  17.042  1.00 26.38           O  
ATOM   1338  CB  ILE A 175      18.873   6.899  14.831  1.00 28.33           C  
ATOM   1339  CG1 ILE A 175      18.773   5.572  14.058  1.00 28.17           C  
ATOM   1340  CG2 ILE A 175      18.123   7.998  14.072  1.00 28.17           C  
ATOM   1341  CD1 ILE A 175      17.350   5.141  13.685  1.00 25.29           C  
ATOM   1342  N   LEU A 176      20.865   9.636  15.110  1.00 26.83           N  
ATOM   1343  CA  LEU A 176      20.811  10.969  15.704  1.00 25.68           C  
ATOM   1344  C   LEU A 176      19.406  11.530  15.485  1.00 24.24           C  
ATOM   1345  O   LEU A 176      18.927  11.682  14.346  1.00 22.76           O  
ATOM   1346  CB  LEU A 176      21.858  11.928  15.136  1.00 26.34           C  
ATOM   1347  CG  LEU A 176      21.800  13.339  15.752  1.00 27.07           C  
ATOM   1348  CD1 LEU A 176      22.100  13.344  17.267  1.00 28.04           C  
ATOM   1349  CD2 LEU A 176      22.743  14.277  15.004  1.00 29.52           C  
ATOM   1350  N   PHE A 177      18.763  11.844  16.603  1.00 22.80           N  
ATOM   1351  CA  PHE A 177      17.408  12.350  16.591  1.00 21.99           C  
ATOM   1352  C   PHE A 177      17.448  13.854  16.806  1.00 21.97           C  
ATOM   1353  O   PHE A 177      17.948  14.338  17.821  1.00 22.70           O  
ATOM   1354  CB  PHE A 177      16.592  11.676  17.687  1.00 21.79           C  
ATOM   1355  CG  PHE A 177      15.167  12.096  17.678  1.00 22.65           C  
ATOM   1356  CD1 PHE A 177      14.245  11.434  16.885  1.00 23.67           C  
ATOM   1357  CD2 PHE A 177      14.758  13.228  18.395  1.00 19.76           C  
ATOM   1358  CE1 PHE A 177      12.911  11.881  16.837  1.00 28.27           C  
ATOM   1359  CE2 PHE A 177      13.456  13.678  18.353  1.00 21.82           C  
ATOM   1360  CZ  PHE A 177      12.506  13.001  17.593  1.00 23.49           C  
ATOM   1361  N   VAL A 178      16.882  14.583  15.858  1.00 22.05           N  
ATOM   1362  CA  VAL A 178      16.884  16.039  15.861  1.00 21.28           C  
ATOM   1363  C   VAL A 178      15.475  16.600  15.956  1.00 20.29           C  
ATOM   1364  O   VAL A 178      14.604  16.254  15.159  1.00 20.35           O  
ATOM   1365  CB  VAL A 178      17.526  16.576  14.566  1.00 21.65           C  
ATOM   1366  CG1 VAL A 178      17.529  18.125  14.562  1.00 19.83           C  
ATOM   1367  CG2 VAL A 178      18.946  16.003  14.419  1.00 18.84           C  
ATOM   1368  N   SER A 179      15.256  17.440  16.966  1.00 20.16           N  
ATOM   1369  CA  SER A 179      13.959  18.159  17.158  1.00 18.73           C  
ATOM   1370  C   SER A 179      14.141  19.588  17.632  1.00 18.74           C  
ATOM   1371  O   SER A 179      15.103  19.891  18.297  1.00 17.08           O  
ATOM   1372  CB  SER A 179      13.103  17.469  18.215  1.00 17.66           C  
ATOM   1373  OG  SER A 179      11.782  18.023  18.135  1.00 17.10           O  
ATOM   1374  N   SER A 180      13.205  20.453  17.273  1.00 19.86           N  
ATOM   1375  CA  SER A 180      13.105  21.768  17.891  1.00 21.51           C  
ATOM   1376  C   SER A 180      12.400  21.820  19.225  1.00 21.70           C  
ATOM   1377  O   SER A 180      12.470  22.819  19.941  1.00 21.85           O  
ATOM   1378  CB  SER A 180      12.329  22.683  16.994  1.00 21.08           C  
ATOM   1379  OG  SER A 180      13.262  23.182  16.099  1.00 26.41           O  
ATOM   1380  N   ASN A 181      11.675  20.777  19.549  1.00 22.24           N  
ATOM   1381  CA  ASN A 181      10.810  20.841  20.694  1.00 21.78           C  
ATOM   1382  C   ASN A 181      11.580  20.159  21.807  1.00 21.80           C  
ATOM   1383  O   ASN A 181      11.984  18.990  21.698  1.00 21.57           O  
ATOM   1384  CB  ASN A 181       9.497  20.172  20.367  1.00 22.35           C  
ATOM   1385  CG  ASN A 181       8.696  20.942  19.341  1.00 23.17           C  
ATOM   1386  OD1 ASN A 181       8.579  22.133  19.445  1.00 25.52           O  
ATOM   1387  ND2 ASN A 181       8.123  20.256  18.369  1.00 22.72           N  
ATOM   1388  N   GLY A 182      11.855  20.916  22.853  1.00 20.45           N  
ATOM   1389  CA  GLY A 182      12.573  20.376  24.006  1.00 20.80           C  
ATOM   1390  C   GLY A 182      11.961  19.102  24.544  1.00 20.80           C  
ATOM   1391  O   GLY A 182      12.686  18.162  24.866  1.00 21.23           O  
ATOM   1392  N   TRP A 183      10.633  19.044  24.618  1.00 20.58           N  
ATOM   1393  CA  TRP A 183       9.980  17.853  25.167  1.00 20.24           C  
ATOM   1394  C   TRP A 183      10.323  16.627  24.311  1.00 21.03           C  
ATOM   1395  O   TRP A 183      10.517  15.527  24.814  1.00 22.54           O  
ATOM   1396  CB  TRP A 183       8.461  18.042  25.313  1.00 19.07           C  
ATOM   1397  CG  TRP A 183       7.715  18.418  24.045  1.00 18.39           C  
ATOM   1398  CD1 TRP A 183       7.378  19.684  23.653  1.00 15.36           C  
ATOM   1399  CD2 TRP A 183       7.221  17.537  23.024  1.00 15.64           C  
ATOM   1400  NE1 TRP A 183       6.765  19.650  22.413  1.00 17.98           N  
ATOM   1401  CE2 TRP A 183       6.622  18.342  22.030  1.00 17.41           C  
ATOM   1402  CE3 TRP A 183       7.250  16.151  22.842  1.00 18.50           C  
ATOM   1403  CZ2 TRP A 183       6.006  17.803  20.882  1.00 16.60           C  
ATOM   1404  CZ3 TRP A 183       6.683  15.604  21.671  1.00 13.64           C  
ATOM   1405  CH2 TRP A 183       6.071  16.442  20.706  1.00 16.04           C  
ATOM   1406  N   ASP A 184      10.404  16.824  23.008  1.00 21.53           N  
ATOM   1407  CA  ASP A 184      10.649  15.745  22.076  1.00 21.45           C  
ATOM   1408  C   ASP A 184      12.118  15.320  22.123  1.00 22.01           C  
ATOM   1409  O   ASP A 184      12.403  14.119  22.125  1.00 23.06           O  
ATOM   1410  CB  ASP A 184      10.240  16.206  20.681  1.00 21.84           C  
ATOM   1411  CG  ASP A 184      10.053  15.066  19.694  1.00 22.91           C  
ATOM   1412  OD1 ASP A 184      10.055  13.857  20.074  1.00 22.14           O  
ATOM   1413  OD2 ASP A 184       9.880  15.423  18.516  1.00 26.71           O  
ATOM   1414  N   ALA A 185      13.057  16.263  22.230  1.00 21.79           N  
ATOM   1415  CA  ALA A 185      14.503  15.859  22.382  1.00 21.64           C  
ATOM   1416  C   ALA A 185      14.622  14.985  23.600  1.00 21.93           C  
ATOM   1417  O   ALA A 185      15.326  13.961  23.595  1.00 23.20           O  
ATOM   1418  CB  ALA A 185      15.454  17.062  22.501  1.00 19.60           C  
ATOM   1419  N   CYS A 186      13.917  15.377  24.646  1.00 21.96           N  
ATOM   1420  CA  CYS A 186      13.958  14.672  25.932  1.00 22.41           C  
ATOM   1421  C   CYS A 186      13.293  13.293  25.862  1.00 22.44           C  
ATOM   1422  O   CYS A 186      13.789  12.314  26.424  1.00 21.49           O  
ATOM   1423  CB  CYS A 186      13.239  15.521  26.980  1.00 22.11           C  
ATOM   1424  SG  CYS A 186      14.218  16.953  27.568  1.00 23.66           S  
ATOM   1425  N   GLY A 187      12.145  13.233  25.191  1.00 22.91           N  
ATOM   1426  CA  GLY A 187      11.449  11.958  25.015  1.00 23.59           C  
ATOM   1427  C   GLY A 187      12.307  11.002  24.189  1.00 24.45           C  
ATOM   1428  O   GLY A 187      12.348   9.785  24.472  1.00 25.38           O  
ATOM   1429  N   ALA A 188      12.983  11.538  23.161  1.00 23.72           N  
ATOM   1430  CA  ALA A 188      13.839  10.714  22.310  1.00 23.28           C  
ATOM   1431  C   ALA A 188      15.039  10.194  23.053  1.00 23.07           C  
ATOM   1432  O   ALA A 188      15.456   9.068  22.830  1.00 23.54           O  
ATOM   1433  CB  ALA A 188      14.246  11.449  21.098  1.00 23.86           C  
ATOM   1434  N   THR A 189      15.578  10.986  23.961  1.00 22.63           N  
ATOM   1435  CA  THR A 189      16.701  10.561  24.751  1.00 22.59           C  
ATOM   1436  C   THR A 189      16.321   9.412  25.666  1.00 23.23           C  
ATOM   1437  O   THR A 189      17.128   8.500  25.908  1.00 23.96           O  
ATOM   1438  CB  THR A 189      17.234  11.732  25.602  1.00 22.81           C  
ATOM   1439  OG1 THR A 189      17.415  12.887  24.763  1.00 24.51           O  
ATOM   1440  CG2 THR A 189      18.549  11.381  26.301  1.00 21.22           C  
ATOM   1441  N   TRP A 190      15.104   9.455  26.214  1.00 23.81           N  
ATOM   1442  CA  TRP A 190      14.554   8.354  27.027  1.00 22.64           C  
ATOM   1443  C   TRP A 190      14.458   7.096  26.162  1.00 22.89           C  
ATOM   1444  O   TRP A 190      14.740   6.024  26.585  1.00 23.58           O  
ATOM   1445  CB  TRP A 190      13.118   8.696  27.541  1.00 22.15           C  
ATOM   1446  CG  TRP A 190      13.011   9.548  28.786  1.00 19.54           C  
ATOM   1447  CD1 TRP A 190      13.935   9.677  29.796  1.00 19.22           C  
ATOM   1448  CD2 TRP A 190      11.881  10.346  29.190  1.00 18.61           C  
ATOM   1449  NE1 TRP A 190      13.474  10.539  30.762  1.00 19.01           N  
ATOM   1450  CE2 TRP A 190      12.207  10.941  30.426  1.00 19.89           C  
ATOM   1451  CE3 TRP A 190      10.640  10.640  28.609  1.00 17.41           C  
ATOM   1452  CZ2 TRP A 190      11.346  11.802  31.076  1.00 17.48           C  
ATOM   1453  CZ3 TRP A 190       9.789  11.501  29.262  1.00 15.38           C  
ATOM   1454  CH2 TRP A 190      10.143  12.067  30.482  1.00 14.64           C  
ATOM   1455  N   HIS A 191      14.032   7.220  24.939  1.00 24.55           N  
ATOM   1456  CA  HIS A 191      13.904   6.024  24.109  1.00 25.90           C  
ATOM   1457  C   HIS A 191      15.261   5.387  23.767  1.00 26.52           C  
ATOM   1458  O   HIS A 191      15.334   4.216  23.442  1.00 26.68           O  
ATOM   1459  CB  HIS A 191      13.150   6.368  22.841  1.00 25.92           C  
ATOM   1460  CG  HIS A 191      12.762   5.179  22.009  1.00 25.73           C  
ATOM   1461  ND1 HIS A 191      11.772   4.298  22.388  1.00 24.36           N  
ATOM   1462  CD2 HIS A 191      13.216   4.740  20.813  1.00 25.42           C  
ATOM   1463  CE1 HIS A 191      11.621   3.381  21.449  1.00 26.24           C  
ATOM   1464  NE2 HIS A 191      12.488   3.622  20.484  1.00 25.42           N  
ATOM   1465  N   GLY A 192      16.329   6.168  23.869  1.00 27.43           N  
ATOM   1466  CA  GLY A 192      17.698   5.687  23.646  1.00 27.95           C  
ATOM   1467  C   GLY A 192      18.407   6.254  22.409  1.00 27.07           C  
ATOM   1468  O   GLY A 192      19.438   5.713  22.019  1.00 28.10           O  
ATOM   1469  N   PHE A 193      17.867   7.288  21.768  1.00 25.84           N  
ATOM   1470  CA  PHE A 193      18.570   7.933  20.639  1.00 25.84           C  
ATOM   1471  C   PHE A 193      19.676   8.824  21.133  1.00 25.79           C  
ATOM   1472  O   PHE A 193      19.661   9.288  22.265  1.00 25.06           O  
ATOM   1473  CB  PHE A 193      17.678   8.856  19.809  1.00 25.49           C  
ATOM   1474  CG  PHE A 193      16.533   8.175  19.135  1.00 25.64           C  
ATOM   1475  CD1 PHE A 193      16.662   7.665  17.851  1.00 23.89           C  
ATOM   1476  CD2 PHE A 193      15.290   8.072  19.776  1.00 25.22           C  
ATOM   1477  CE1 PHE A 193      15.587   7.041  17.219  1.00 22.90           C  
ATOM   1478  CE2 PHE A 193      14.225   7.479  19.145  1.00 23.05           C  
ATOM   1479  CZ  PHE A 193      14.369   6.960  17.851  1.00 22.39           C  
ATOM   1480  N   THR A 194      20.625   9.097  20.251  1.00 26.18           N  
ATOM   1481  CA  THR A 194      21.504  10.247  20.441  1.00 26.66           C  
ATOM   1482  C   THR A 194      20.669  11.396  19.942  1.00 26.26           C  
ATOM   1483  O   THR A 194      20.186  11.363  18.813  1.00 26.62           O  
ATOM   1484  CB  THR A 194      22.797  10.197  19.561  1.00 26.95           C  
ATOM   1485  OG1 THR A 194      23.477   8.955  19.768  1.00 28.21           O  
ATOM   1486  CG2 THR A 194      23.726  11.375  19.910  1.00 27.62           C  
ATOM   1487  N   THR A 195      20.479  12.419  20.758  1.00 26.18           N  
ATOM   1488  CA  THR A 195      19.610  13.487  20.333  1.00 25.45           C  
ATOM   1489  C   THR A 195      20.302  14.860  20.312  1.00 25.12           C  
ATOM   1490  O   THR A 195      21.150  15.166  21.148  1.00 24.35           O  
ATOM   1491  CB  THR A 195      18.388  13.563  21.263  1.00 25.05           C  
ATOM   1492  OG1 THR A 195      18.838  13.959  22.544  1.00 26.55           O  
ATOM   1493  CG2 THR A 195      17.701  12.231  21.387  1.00 23.86           C  
ATOM   1494  N   PHE A 196      19.853  15.694  19.386  1.00 25.02           N  
ATOM   1495  CA  PHE A 196      20.273  17.059  19.304  1.00 26.12           C  
ATOM   1496  C   PHE A 196      19.029  17.952  19.334  1.00 25.53           C  
ATOM   1497  O   PHE A 196      18.099  17.740  18.569  1.00 25.35           O  
ATOM   1498  CB  PHE A 196      21.023  17.284  17.984  1.00 27.29           C  
ATOM   1499  CG  PHE A 196      21.590  18.667  17.843  1.00 30.00           C  
ATOM   1500  CD1 PHE A 196      22.902  18.941  18.272  1.00 33.22           C  
ATOM   1501  CD2 PHE A 196      20.826  19.697  17.295  1.00 32.81           C  
ATOM   1502  CE1 PHE A 196      23.434  20.215  18.176  1.00 33.60           C  
ATOM   1503  CE2 PHE A 196      21.372  21.006  17.186  1.00 35.45           C  
ATOM   1504  CZ  PHE A 196      22.681  21.248  17.629  1.00 34.11           C  
ATOM   1505  N   TRP A 197      19.052  18.994  20.163  1.00 24.45           N  
ATOM   1506  CA  TRP A 197      17.935  19.908  20.291  1.00 23.49           C  
ATOM   1507  C   TRP A 197      18.240  21.243  19.612  1.00 24.10           C  
ATOM   1508  O   TRP A 197      19.121  21.987  20.069  1.00 23.70           O  
ATOM   1509  CB  TRP A 197      17.641  20.116  21.789  1.00 22.75           C  
ATOM   1510  CG  TRP A 197      16.528  21.083  22.086  1.00 20.28           C  
ATOM   1511  CD1 TRP A 197      15.411  21.321  21.338  1.00 19.69           C  
ATOM   1512  CD2 TRP A 197      16.411  21.916  23.251  1.00 19.55           C  
ATOM   1513  NE1 TRP A 197      14.608  22.285  21.955  1.00 16.79           N  
ATOM   1514  CE2 TRP A 197      15.211  22.659  23.129  1.00 17.51           C  
ATOM   1515  CE3 TRP A 197      17.204  22.105  24.386  1.00 20.75           C  
ATOM   1516  CZ2 TRP A 197      14.800  23.557  24.091  1.00 17.52           C  
ATOM   1517  CZ3 TRP A 197      16.788  23.020  25.332  1.00 19.89           C  
ATOM   1518  CH2 TRP A 197      15.592  23.712  25.184  1.00 18.50           C  
ATOM   1519  N   ILE A 198      17.488  21.562  18.560  1.00 23.97           N  
ATOM   1520  CA  ILE A 198      17.566  22.865  17.929  1.00 24.55           C  
ATOM   1521  C   ILE A 198      16.673  23.788  18.723  1.00 24.52           C  
ATOM   1522  O   ILE A 198      15.495  23.897  18.485  1.00 25.53           O  
ATOM   1523  CB  ILE A 198      17.222  22.868  16.393  1.00 24.28           C  
ATOM   1524  CG1 ILE A 198      18.027  21.790  15.667  1.00 26.01           C  
ATOM   1525  CG2 ILE A 198      17.566  24.262  15.771  1.00 24.70           C  
ATOM   1526  CD1 ILE A 198      17.899  21.748  14.156  1.00 22.31           C  
ATOM   1527  N   ASN A 199      17.272  24.428  19.712  1.00 25.53           N  
ATOM   1528  CA  ASN A 199      16.589  25.339  20.591  1.00 26.47           C  
ATOM   1529  C   ASN A 199      16.563  26.753  19.970  1.00 27.73           C  
ATOM   1530  O   ASN A 199      17.367  27.632  20.321  1.00 27.55           O  
ATOM   1531  CB  ASN A 199      17.307  25.304  21.964  1.00 26.75           C  
ATOM   1532  CG  ASN A 199      16.658  26.186  22.992  1.00 25.52           C  
ATOM   1533  OD1 ASN A 199      15.537  26.660  22.794  1.00 25.84           O  
ATOM   1534  ND2 ASN A 199      17.371  26.434  24.100  1.00 19.96           N  
ATOM   1535  N   ARG A 200      15.617  26.961  19.058  1.00 28.88           N  
ATOM   1536  CA  ARG A 200      15.568  28.193  18.260  1.00 30.49           C  
ATOM   1537  C   ARG A 200      15.241  29.469  19.049  1.00 30.16           C  
ATOM   1538  O   ARG A 200      15.667  30.557  18.677  1.00 30.44           O  
ATOM   1539  CB  ARG A 200      14.550  28.046  17.116  1.00 30.94           C  
ATOM   1540  CG  ARG A 200      15.042  27.131  16.024  1.00 34.71           C  
ATOM   1541  CD  ARG A 200      14.137  27.189  14.800  1.00 38.86           C  
ATOM   1542  NE  ARG A 200      14.460  26.145  13.825  1.00 42.09           N  
ATOM   1543  CZ  ARG A 200      15.568  26.116  13.087  1.00 46.20           C  
ATOM   1544  NH1 ARG A 200      16.499  27.079  13.219  1.00 48.13           N  
ATOM   1545  NH2 ARG A 200      15.765  25.113  12.218  1.00 46.76           N  
ATOM   1546  N   LEU A 201      14.452  29.340  20.111  1.00 29.77           N  
ATOM   1547  CA  LEU A 201      14.031  30.504  20.866  1.00 29.06           C  
ATOM   1548  C   LEU A 201      14.881  30.712  22.125  1.00 27.63           C  
ATOM   1549  O   LEU A 201      14.597  31.580  22.912  1.00 28.08           O  
ATOM   1550  CB  LEU A 201      12.538  30.389  21.184  1.00 29.74           C  
ATOM   1551  CG  LEU A 201      11.521  30.228  20.025  1.00 31.62           C  
ATOM   1552  CD1 LEU A 201      10.068  30.402  20.568  1.00 32.34           C  
ATOM   1553  CD2 LEU A 201      11.783  31.189  18.856  1.00 30.35           C  
ATOM   1554  N   GLY A 202      15.939  29.930  22.292  1.00 26.85           N  
ATOM   1555  CA  GLY A 202      16.849  30.080  23.430  1.00 26.58           C  
ATOM   1556  C   GLY A 202      16.225  29.805  24.791  1.00 26.30           C  
ATOM   1557  O   GLY A 202      16.541  30.456  25.754  1.00 26.58           O  
ATOM   1558  N   HIS A 203      15.349  28.806  24.864  1.00 25.84           N  
ATOM   1559  CA  HIS A 203      14.626  28.506  26.094  1.00 24.44           C  
ATOM   1560  C   HIS A 203      15.460  27.665  27.045  1.00 22.89           C  
ATOM   1561  O   HIS A 203      16.488  27.115  26.637  1.00 23.05           O  
ATOM   1562  CB  HIS A 203      13.321  27.792  25.733  1.00 24.94           C  
ATOM   1563  CG  HIS A 203      12.283  28.712  25.172  1.00 25.76           C  
ATOM   1564  ND1 HIS A 203      11.156  28.255  24.531  1.00 30.53           N  
ATOM   1565  CD2 HIS A 203      12.201  30.066  25.165  1.00 29.19           C  
ATOM   1566  CE1 HIS A 203      10.419  29.284  24.152  1.00 31.99           C  
ATOM   1567  NE2 HIS A 203      11.024  30.396  24.536  1.00 32.56           N  
ATOM   1568  N   PRO A 204      15.039  27.554  28.319  1.00 21.01           N  
ATOM   1569  CA  PRO A 204      15.788  26.641  29.210  1.00 21.02           C  
ATOM   1570  C   PRO A 204      15.526  25.188  28.844  1.00 21.26           C  
ATOM   1571  O   PRO A 204      14.566  24.932  28.109  1.00 21.33           O  
ATOM   1572  CB  PRO A 204      15.256  26.970  30.605  1.00 21.59           C  
ATOM   1573  CG  PRO A 204      14.370  28.193  30.444  1.00 20.60           C  
ATOM   1574  CD  PRO A 204      13.976  28.287  29.015  1.00 20.83           C  
ATOM   1575  N   PRO A 205      16.396  24.251  29.278  1.00 21.41           N  
ATOM   1576  CA  PRO A 205      16.021  22.857  29.149  1.00 21.28           C  
ATOM   1577  C   PRO A 205      14.782  22.510  29.966  1.00 20.44           C  
ATOM   1578  O   PRO A 205      14.567  23.039  31.027  1.00 18.96           O  
ATOM   1579  CB  PRO A 205      17.240  22.091  29.680  1.00 21.95           C  
ATOM   1580  CG  PRO A 205      18.392  23.008  29.475  1.00 22.97           C  
ATOM   1581  CD  PRO A 205      17.818  24.400  29.671  1.00 22.31           C  
ATOM   1582  N   GLU A 206      13.977  21.604  29.445  1.00 20.58           N  
ATOM   1583  CA  GLU A 206      12.815  21.109  30.169  1.00 20.39           C  
ATOM   1584  C   GLU A 206      13.293  20.427  31.438  1.00 20.23           C  
ATOM   1585  O   GLU A 206      14.323  19.777  31.449  1.00 18.76           O  
ATOM   1586  CB  GLU A 206      11.995  20.140  29.321  1.00 19.94           C  
ATOM   1587  CG  GLU A 206      11.377  20.754  28.102  1.00 21.39           C  
ATOM   1588  CD  GLU A 206      10.329  21.842  28.380  1.00 21.26           C  
ATOM   1589  OE1 GLU A 206       9.918  22.107  29.513  1.00 20.53           O  
ATOM   1590  OE2 GLU A 206       9.879  22.451  27.420  1.00 25.52           O  
ATOM   1591  N   ALA A 207      12.527  20.598  32.517  1.00 21.01           N  
ATOM   1592  CA  ALA A 207      12.875  20.003  33.793  1.00 21.35           C  
ATOM   1593  C   ALA A 207      12.260  18.591  33.794  1.00 21.48           C  
ATOM   1594  O   ALA A 207      11.249  18.346  34.411  1.00 21.31           O  
ATOM   1595  CB  ALA A 207      12.357  20.897  34.981  1.00 20.56           C  
ATOM   1596  N   LEU A 208      12.893  17.684  33.052  1.00 23.15           N  
ATOM   1597  CA  LEU A 208      12.441  16.291  32.890  1.00 23.91           C  
ATOM   1598  C   LEU A 208      13.460  15.275  33.414  1.00 25.25           C  
ATOM   1599  O   LEU A 208      13.283  14.087  33.205  1.00 26.02           O  
ATOM   1600  CB  LEU A 208      12.064  15.986  31.427  1.00 22.38           C  
ATOM   1601  CG  LEU A 208      10.754  16.639  30.892  1.00 21.48           C  
ATOM   1602  CD1 LEU A 208      10.685  16.567  29.358  1.00 16.65           C  
ATOM   1603  CD2 LEU A 208       9.493  16.089  31.464  1.00 17.80           C  
ATOM   1604  N   ASP A 209      14.505  15.733  34.104  1.00 27.13           N  
ATOM   1605  CA  ASP A 209      15.584  14.850  34.636  1.00 28.87           C  
ATOM   1606  C   ASP A 209      16.345  14.080  33.547  1.00 28.91           C  
ATOM   1607  O   ASP A 209      16.878  12.989  33.773  1.00 29.49           O  
ATOM   1608  CB  ASP A 209      15.038  13.864  35.679  1.00 29.50           C  
ATOM   1609  CG  ASP A 209      14.435  14.559  36.862  1.00 31.38           C  
ATOM   1610  OD1 ASP A 209      15.204  15.170  37.629  1.00 36.89           O  
ATOM   1611  OD2 ASP A 209      13.194  14.503  37.023  1.00 34.02           O  
ATOM   1612  N   VAL A 210      16.382  14.655  32.358  1.00 29.06           N  
ATOM   1613  CA  VAL A 210      17.067  14.050  31.214  1.00 28.85           C  
ATOM   1614  C   VAL A 210      17.448  15.225  30.322  1.00 28.49           C  
ATOM   1615  O   VAL A 210      16.807  16.271  30.363  1.00 27.98           O  
ATOM   1616  CB  VAL A 210      16.154  13.047  30.472  1.00 29.16           C  
ATOM   1617  CG1 VAL A 210      14.916  13.755  29.873  1.00 28.67           C  
ATOM   1618  CG2 VAL A 210      16.918  12.280  29.386  1.00 30.08           C  
ATOM   1619  N   ALA A 211      18.524  15.068  29.562  1.00 28.86           N  
ATOM   1620  CA  ALA A 211      18.989  16.113  28.625  1.00 28.47           C  
ATOM   1621  C   ALA A 211      19.467  15.481  27.306  1.00 28.30           C  
ATOM   1622  O   ALA A 211      20.082  14.443  27.282  1.00 27.95           O  
ATOM   1623  CB  ALA A 211      20.100  17.009  29.286  1.00 27.88           C  
ATOM   1624  N   PRO A 212      19.173  16.116  26.193  1.00 28.75           N  
ATOM   1625  CA  PRO A 212      19.737  15.633  24.953  1.00 29.41           C  
ATOM   1626  C   PRO A 212      21.285  15.623  24.947  1.00 30.15           C  
ATOM   1627  O   PRO A 212      21.908  16.223  25.811  1.00 30.01           O  
ATOM   1628  CB  PRO A 212      19.224  16.639  23.941  1.00 29.35           C  
ATOM   1629  CG  PRO A 212      19.020  17.890  24.730  1.00 29.19           C  
ATOM   1630  CD  PRO A 212      18.517  17.419  26.033  1.00 29.68           C  
ATOM   1631  N   ALA A 213      21.875  14.944  23.973  1.00 30.57           N  
ATOM   1632  CA  ALA A 213      23.309  14.805  23.900  1.00 31.73           C  
ATOM   1633  C   ALA A 213      23.932  16.202  23.761  1.00 32.09           C  
ATOM   1634  O   ALA A 213      24.849  16.539  24.524  1.00 32.06           O  
ATOM   1635  CB  ALA A 213      23.706  13.891  22.710  1.00 31.79           C  
ATOM   1636  N   ALA A 214      23.395  17.009  22.829  1.00 32.08           N  
ATOM   1637  CA  ALA A 214      23.749  18.413  22.721  1.00 31.56           C  
ATOM   1638  C   ALA A 214      22.562  19.214  22.188  1.00 31.45           C  
ATOM   1639  O   ALA A 214      21.595  18.654  21.744  1.00 32.03           O  
ATOM   1640  CB  ALA A 214      24.973  18.575  21.816  1.00 31.87           C  
ATOM   1641  N   ALA A 215      22.640  20.528  22.272  1.00 31.13           N  
ATOM   1642  CA  ALA A 215      21.623  21.444  21.748  1.00 30.97           C  
ATOM   1643  C   ALA A 215      22.331  22.656  21.072  1.00 31.16           C  
ATOM   1644  O   ALA A 215      23.479  22.961  21.372  1.00 30.69           O  
ATOM   1645  CB  ALA A 215      20.701  21.940  22.881  1.00 30.56           C  
ATOM   1646  N   GLY A 216      21.640  23.320  20.163  1.00 30.95           N  
ATOM   1647  CA  GLY A 216      22.161  24.499  19.535  1.00 31.78           C  
ATOM   1648  C   GLY A 216      21.004  25.375  19.139  1.00 32.56           C  
ATOM   1649  O   GLY A 216      19.866  25.113  19.498  1.00 32.30           O  
ATOM   1650  N   HIS A 217      21.309  26.395  18.355  1.00 33.62           N  
ATOM   1651  CA  HIS A 217      20.364  27.452  18.032  1.00 34.32           C  
ATOM   1652  C   HIS A 217      19.728  27.253  16.688  1.00 34.30           C  
ATOM   1653  O   HIS A 217      18.636  27.753  16.439  1.00 33.37           O  
ATOM   1654  CB  HIS A 217      21.079  28.803  18.084  1.00 34.78           C  
ATOM   1655  CG  HIS A 217      20.264  29.941  17.569  1.00 38.08           C  
ATOM   1656  ND1 HIS A 217      20.597  30.634  16.420  1.00 42.11           N  
ATOM   1657  CD2 HIS A 217      19.119  30.507  18.038  1.00 41.58           C  
ATOM   1658  CE1 HIS A 217      19.682  31.569  16.199  1.00 43.75           C  
ATOM   1659  NE2 HIS A 217      18.783  31.522  17.174  1.00 41.87           N  
ATOM   1660  N   ASP A 218      20.402  26.505  15.820  1.00 35.78           N  
ATOM   1661  CA  ASP A 218      19.936  26.287  14.456  1.00 36.68           C  
ATOM   1662  C   ASP A 218      20.560  25.048  13.840  1.00 37.40           C  
ATOM   1663  O   ASP A 218      21.376  24.356  14.463  1.00 37.03           O  
ATOM   1664  CB  ASP A 218      20.236  27.517  13.600  1.00 37.55           C  
ATOM   1665  CG  ASP A 218      21.722  27.872  13.559  1.00 38.88           C  
ATOM   1666  OD1 ASP A 218      22.558  27.159  14.194  1.00 37.67           O  
ATOM   1667  OD2 ASP A 218      22.022  28.906  12.911  1.00 40.42           O  
HETATM 1668  N   MSE A 219      20.145  24.764  12.617  1.00 38.49           N  
HETATM 1669  CA  MSE A 219      20.556  23.564  11.903  1.00 39.68           C  
HETATM 1670  C   MSE A 219      22.033  23.437  11.626  1.00 40.61           C  
HETATM 1671  O   MSE A 219      22.606  22.325  11.535  1.00 41.01           O  
HETATM 1672  CB  MSE A 219      19.789  23.524  10.615  1.00 39.78           C  
HETATM 1673  CG  MSE A 219      18.425  22.988  10.881  1.00 42.08           C  
HETATM 1674 SE   MSE A 219      18.498  21.031  10.806  1.00 49.72          SE  
HETATM 1675  CE  MSE A 219      17.912  20.880   8.921  1.00 37.34           C  
ATOM   1676  N   ARG A 220      22.654  24.599  11.503  1.00 41.92           N  
ATOM   1677  CA  ARG A 220      24.059  24.693  11.220  1.00 42.40           C  
ATOM   1678  C   ARG A 220      24.824  24.390  12.481  1.00 42.39           C  
ATOM   1679  O   ARG A 220      25.900  23.817  12.413  1.00 42.83           O  
ATOM   1680  CB  ARG A 220      24.368  26.077  10.658  1.00 43.39           C  
ATOM   1681  CG  ARG A 220      23.612  26.352   9.344  1.00 46.21           C  
ATOM   1682  CD  ARG A 220      23.781  27.789   8.782  1.00 49.82           C  
ATOM   1683  NE  ARG A 220      23.038  28.783   9.563  1.00 50.73           N  
ATOM   1684  CZ  ARG A 220      22.825  30.046   9.195  1.00 52.13           C  
ATOM   1685  NH1 ARG A 220      23.263  30.494   8.013  1.00 53.80           N  
ATOM   1686  NH2 ARG A 220      22.163  30.867  10.010  1.00 50.98           N  
ATOM   1687  N   ASP A 221      24.278  24.703  13.653  1.00 42.25           N  
ATOM   1688  CA  ASP A 221      24.902  24.163  14.861  1.00 42.55           C  
ATOM   1689  C   ASP A 221      24.858  22.641  14.877  1.00 42.21           C  
ATOM   1690  O   ASP A 221      25.777  22.015  15.418  1.00 42.48           O  
ATOM   1691  CB  ASP A 221      24.295  24.729  16.146  1.00 42.70           C  
ATOM   1692  CG  ASP A 221      24.660  26.187  16.375  1.00 43.70           C  
ATOM   1693  OD1 ASP A 221      25.802  26.605  16.041  1.00 45.25           O  
ATOM   1694  OD2 ASP A 221      23.787  26.916  16.888  1.00 44.28           O  
ATOM   1695  N   LEU A 222      23.808  22.048  14.298  1.00 41.91           N  
ATOM   1696  CA  LEU A 222      23.664  20.578  14.276  1.00 41.94           C  
ATOM   1697  C   LEU A 222      24.769  19.935  13.436  1.00 43.29           C  
ATOM   1698  O   LEU A 222      25.397  18.957  13.858  1.00 42.95           O  
ATOM   1699  CB  LEU A 222      22.290  20.140  13.741  1.00 40.74           C  
ATOM   1700  CG  LEU A 222      22.291  18.675  13.244  1.00 38.73           C  
ATOM   1701  CD1 LEU A 222      22.393  17.679  14.366  1.00 31.09           C  
ATOM   1702  CD2 LEU A 222      21.106  18.376  12.403  1.00 37.53           C  
ATOM   1703  N   LEU A 223      24.971  20.494  12.238  1.00 45.39           N  
ATOM   1704  CA  LEU A 223      26.123  20.169  11.371  1.00 46.43           C  
ATOM   1705  C   LEU A 223      27.435  20.248  12.145  1.00 47.35           C  
ATOM   1706  O   LEU A 223      28.226  19.297  12.107  1.00 47.78           O  
ATOM   1707  CB  LEU A 223      26.165  21.115  10.169  1.00 46.61           C  
ATOM   1708  CG  LEU A 223      26.969  20.686   8.932  1.00 47.81           C  
ATOM   1709  CD1 LEU A 223      26.732  19.229   8.500  1.00 46.25           C  
ATOM   1710  CD2 LEU A 223      26.673  21.656   7.763  1.00 49.77           C  
ATOM   1711  N   GLN A 224      27.657  21.362  12.855  1.00 48.08           N  
ATOM   1712  CA  GLN A 224      28.875  21.535  13.662  1.00 48.89           C  
ATOM   1713  C   GLN A 224      29.088  20.228  14.424  1.00 48.89           C  
ATOM   1714  O   GLN A 224      30.135  19.599  14.332  1.00 48.94           O  
ATOM   1715  CB  GLN A 224      28.743  22.685  14.689  1.00 49.45           C  
ATOM   1716  CG  GLN A 224      29.429  24.044  14.413  1.00 51.75           C  
ATOM   1717  CD  GLN A 224      29.456  24.999  15.684  1.00 55.36           C  
ATOM   1718  OE1 GLN A 224      28.446  25.640  16.051  1.00 55.33           O  
ATOM   1719  NE2 GLN A 224      30.628  25.085  16.331  1.00 55.04           N  
ATOM   1720  N   PHE A 225      28.038  19.821  15.141  1.00 48.79           N  
ATOM   1721  CA  PHE A 225      28.101  18.774  16.172  1.00 48.19           C  
ATOM   1722  C   PHE A 225      28.391  17.386  15.623  1.00 48.72           C  
ATOM   1723  O   PHE A 225      29.153  16.621  16.231  1.00 48.53           O  
ATOM   1724  CB  PHE A 225      26.779  18.784  16.973  1.00 47.93           C  
ATOM   1725  CG  PHE A 225      26.449  17.490  17.665  1.00 45.00           C  
ATOM   1726  CD1 PHE A 225      26.820  17.276  18.985  1.00 42.96           C  
ATOM   1727  CD2 PHE A 225      25.728  16.507  17.011  1.00 44.28           C  
ATOM   1728  CE1 PHE A 225      26.504  16.096  19.627  1.00 42.77           C  
ATOM   1729  CE2 PHE A 225      25.399  15.314  17.662  1.00 43.11           C  
ATOM   1730  CZ  PHE A 225      25.791  15.115  18.961  1.00 42.49           C  
ATOM   1731  N   VAL A 226      27.757  17.059  14.502  1.00 48.98           N  
ATOM   1732  CA  VAL A 226      27.985  15.779  13.841  1.00 49.89           C  
ATOM   1733  C   VAL A 226      29.482  15.690  13.442  1.00 50.78           C  
ATOM   1734  O   VAL A 226      30.229  14.808  13.918  1.00 50.40           O  
ATOM   1735  CB  VAL A 226      27.070  15.612  12.568  1.00 49.96           C  
ATOM   1736  CG1 VAL A 226      27.227  14.208  11.975  1.00 49.76           C  
ATOM   1737  CG2 VAL A 226      25.602  15.875  12.892  1.00 48.38           C  
ATOM   1738  N   GLN A 227      29.905  16.650  12.607  1.00 51.66           N  
ATOM   1739  CA  GLN A 227      31.294  16.737  12.120  1.00 52.31           C  
ATOM   1740  C   GLN A 227      32.329  16.537  13.254  1.00 52.45           C  
ATOM   1741  O   GLN A 227      33.309  15.827  13.060  1.00 52.81           O  
ATOM   1742  CB  GLN A 227      31.511  18.037  11.314  1.00 52.52           C  
ATOM   1743  CG  GLN A 227      30.942  17.954   9.872  1.00 52.83           C  
ATOM   1744  CD  GLN A 227      30.648  19.318   9.211  1.00 55.21           C  
ATOM   1745  OE1 GLN A 227      30.622  20.363   9.869  1.00 57.38           O  
ATOM   1746  NE2 GLN A 227      30.422  19.299   7.892  1.00 55.74           N  
ATOM   1747  N   ALA A 228      32.076  17.085  14.445  1.00 52.47           N  
ATOM   1748  CA  ALA A 228      32.936  16.818  15.613  1.00 52.63           C  
ATOM   1749  C   ALA A 228      33.076  15.312  15.954  1.00 53.03           C  
ATOM   1750  O   ALA A 228      32.247  14.700  16.646  1.00 53.34           O  
ATOM   1751  CB  ALA A 228      32.453  17.607  16.828  1.00 52.26           C  
TER    1752      ALA A 228                                                      
HETATM 1753  K     K A 234       0.000  28.759   0.000  0.50 57.89           K  
HETATM 1754  K     K A 235      -3.263  -3.118  22.898  1.00 35.55           K  
HETATM 1755 CL    CL A 236       0.009   0.002  23.031  0.50 23.41          CL  
HETATM 1756 CL    CL A 237       0.725  26.813  14.822  1.00 40.43          CL  
HETATM 1757 CL    CL A 238      -5.240  21.120  28.029  1.00 27.88          CL  
HETATM 1758 NA    NA A 239      13.103   1.094  18.926  1.00 26.72          NA  
HETATM 1759 MG    MG A 240       0.001  23.212  27.149  0.50 33.08          MG  
HETATM 1760 MG    MG A 241     -16.594  32.395  22.131  0.50 30.39          MG  
HETATM 1761  O   HOH A 242      -5.393   6.984  21.616  1.00 17.66           O  
HETATM 1762  O   HOH A 243      -3.699   8.024  19.850  1.00 10.88           O  
HETATM 1763  O   HOH A 244       9.764  21.636  25.055  1.00 13.14           O  
HETATM 1764  O   HOH A 245       2.478  14.973  20.558  1.00 18.66           O  
HETATM 1765  O   HOH A 246      -8.999  16.637  18.647  1.00 22.54           O  
HETATM 1766  O   HOH A 247      16.479  18.943  29.918  1.00 32.62           O  
HETATM 1767  O   HOH A 248      -0.006   0.004  10.616  0.50 21.02           O  
HETATM 1768  O   HOH A 249      -5.340  -0.209  25.686  1.00 28.75           O  
HETATM 1769  O   HOH A 250     -14.354  32.614  25.012  1.00 27.23           O  
HETATM 1770  O   HOH A 251       6.615   6.114   5.406  1.00 29.31           O  
HETATM 1771  O   HOH A 252       2.318   5.974   7.641  1.00 17.67           O  
HETATM 1772  O   HOH A 253     -12.275  24.408  27.570  1.00 31.62           O  
HETATM 1773  O   HOH A 254       6.306   1.152  16.566  1.00 18.25           O  
HETATM 1774  O   HOH A 255       0.003  19.151  27.146  0.50 27.26           O  
HETATM 1775  O   HOH A 256      -1.163  11.865  12.021  1.00 24.54           O  
HETATM 1776  O   HOH A 257     -11.772  17.731  12.699  1.00 39.23           O  
HETATM 1777  O   HOH A 258      -1.488  -0.997  25.278  1.00 19.28           O  
HETATM 1778  O   HOH A 259      14.412  11.204  33.421  1.00 32.63           O  
HETATM 1779  O   HOH A 260       5.470  22.085  21.282  1.00 17.00           O  
HETATM 1780  O   HOH A 261      14.479  21.093  26.598  1.00 26.00           O  
HETATM 1781  O   HOH A 262      11.171  23.824  22.977  1.00 19.05           O  
HETATM 1782  O   HOH A 263      -9.841   3.100  25.956  1.00 39.21           O  
HETATM 1783  O   HOH A 264      16.552  19.635  27.294  1.00 23.03           O  
HETATM 1784  O   HOH A 265       4.637   0.480  11.341  1.00 26.47           O  
HETATM 1785  O   HOH A 266      28.954  12.915  18.945  1.00 45.59           O  
HETATM 1786  O   HOH A 267      24.045   0.502  19.066  1.00 23.04           O  
HETATM 1787  O   HOH A 268      -0.031   5.310   7.927  1.00 41.60           O  
HETATM 1788  O   HOH A 269      10.446   4.695  24.612  1.00 28.66           O  
HETATM 1789  O   HOH A 270     -14.455  33.579   7.105  1.00 27.48           O  
HETATM 1790  O   HOH A 271     -17.131  31.912   5.162  0.50 17.83           O  
HETATM 1791  O   HOH A 272       8.446   6.788  25.121  1.00 28.17           O  
HETATM 1792  O   HOH A 273      16.138   0.555  19.136  1.00 23.33           O  
HETATM 1793  O   HOH A 274      -5.279   4.141  11.176  1.00 37.70           O  
HETATM 1794  O   HOH A 275       1.091   3.441  24.310  1.00 21.21           O  
HETATM 1795  O   HOH A 276     -11.246   5.309  26.416  1.00 36.99           O  
HETATM 1796  O   HOH A 277      -2.446   3.169  10.998  1.00 27.62           O  
HETATM 1797  O   HOH A 278      17.355  29.282  14.832  1.00 41.51           O  
HETATM 1798  O   HOH A 279      -2.244   0.602  12.479  1.00 29.55           O  
HETATM 1799  O   HOH A 280       3.894  15.572  22.776  1.00 25.42           O  
HETATM 1800  O   HOH A 281       6.664  28.878   5.701  1.00 44.70           O  
HETATM 1801  O   HOH A 282      -8.295  41.345   8.019  1.00 37.20           O  
HETATM 1802  O   HOH A 283      -4.104   0.608  17.298  1.00 31.27           O  
HETATM 1803  O   HOH A 284       8.210  17.639  18.158  1.00 38.56           O  
HETATM 1804  O   HOH A 285      12.164  -0.238  16.497  1.00 29.63           O  
HETATM 1805  O   HOH A 286       0.726  22.006  24.388  1.00 28.64           O  
HETATM 1806  O   HOH A 287      19.814  28.552  21.273  1.00 33.39           O  
HETATM 1807  O   HOH A 288       8.906   2.174  10.405  1.00 42.76           O  
HETATM 1808  O   HOH A 289      13.017  25.740  19.264  1.00 33.41           O  
HETATM 1809  O   HOH A 290       6.441   3.199   9.328  1.00 25.46           O  
HETATM 1810  O   HOH A 291      -2.969  10.401   5.621  1.00 25.78           O  
HETATM 1811  O   HOH A 292      20.436  12.560  30.882  1.00 23.49           O  
HETATM 1812  O   HOH A 293     -12.179   9.411  19.907  1.00 19.54           O  
HETATM 1813  O   HOH A 294      10.125  20.032  -3.181  1.00 40.10           O  
HETATM 1814  O   HOH A 295      15.207  18.326  36.027  1.00 29.94           O  
HETATM 1815  O   HOH A 296      -9.839  11.774   9.059  1.00 33.35           O  
HETATM 1816  O   HOH A 297       4.150  18.258  16.495  1.00 22.70           O  
HETATM 1817  O   HOH A 298      11.009   9.354   0.834  1.00 36.02           O  
HETATM 1818  O   HOH A 299     -10.209  38.032  21.009  1.00 34.22           O  
HETATM 1819  O   HOH A 300     -12.741  38.788  22.865  1.00 30.54           O  
HETATM 1820  O   HOH A 301       1.924  24.407  26.463  1.00 33.13           O  
HETATM 1821  O   HOH A 302      -9.553   1.763  17.937  1.00 19.39           O  
HETATM 1822  O   HOH A 303     -11.283   4.681  13.052  1.00 35.87           O  
HETATM 1823  O   HOH A 304       3.862  29.838  13.692  1.00 38.99           O  
HETATM 1824  O   HOH A 305     -16.568  32.433  18.991  0.50 24.76           O  
HETATM 1825  O   HOH A 306       0.000   0.000  27.157  0.25 19.48           O  
HETATM 1826  O   HOH A 307      -0.268   5.996  25.838  1.00 36.42           O  
HETATM 1827  O   HOH A 308       6.912  17.510  13.339  1.00 26.92           O  
HETATM 1828  O   HOH A 309      19.701  20.867  27.026  1.00 14.80           O  
HETATM 1829  O   HOH A 310      20.412  25.617  23.825  1.00 22.04           O  
CONECT  319 1759                                                                
CONECT  355 1759                                                                
CONECT  441 1754                                                                
CONECT  605 1760                                                                
CONECT  632 1760                                                                
CONECT  707  713                                                                
CONECT  713  707  714                                                           
CONECT  714  713  715  717                                                      
CONECT  715  714  716  721                                                      
CONECT  716  715                                                                
CONECT  717  714  718                                                           
CONECT  718  717  719                                                           
CONECT  719  718  720                                                           
CONECT  720  719                                                                
CONECT  721  715                                                                
CONECT  888  895                                                                
CONECT  895  888  896                                                           
CONECT  896  895  897  899                                                      
CONECT  897  896  898  903                                                      
CONECT  898  897                                                                
CONECT  899  896  900                                                           
CONECT  900  899  901                                                           
CONECT  901  900  902                                                           
CONECT  902  901                                                                
CONECT  903  897                                                                
CONECT  985  992                                                                
CONECT  992  985  993                                                           
CONECT  993  992  994  996                                                      
CONECT  994  993  995 1000                                                      
CONECT  995  994                                                                
CONECT  996  993  997                                                           
CONECT  997  996  998                                                           
CONECT  998  997  999                                                           
CONECT  999  998                                                                
CONECT 1000  994                                                                
CONECT 1059 1061                                                                
CONECT 1061 1059 1062                                                           
CONECT 1062 1061 1063 1065                                                      
CONECT 1063 1062 1064 1069                                                      
CONECT 1064 1063                                                                
CONECT 1065 1062 1066                                                           
CONECT 1066 1065 1067                                                           
CONECT 1067 1066 1068                                                           
CONECT 1068 1067                                                                
CONECT 1069 1063                                                                
CONECT 1662 1668                                                                
CONECT 1668 1662 1669                                                           
CONECT 1669 1668 1670 1672                                                      
CONECT 1670 1669 1671 1676                                                      
CONECT 1671 1670                                                                
CONECT 1672 1669 1673                                                           
CONECT 1673 1672 1674                                                           
CONECT 1674 1673 1675                                                           
CONECT 1675 1674                                                                
CONECT 1676 1670                                                                
CONECT 1754  441                                                                
CONECT 1758 1792 1804                                                           
CONECT 1759  319  355 1820                                                      
CONECT 1760  605  632                                                           
CONECT 1792 1758                                                                
CONECT 1804 1758                                                                
CONECT 1820 1759                                                                
MASTER      365    0   13   11    8    0    6    6 1828    1   62   18          
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.