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.


***  OXIDOREDUCTASE 03-OCT-07 2RGJ  ***

elNémo ID: 200125012649145318

Job options:

ID        	=	 200125012649145318
JOBID     	=	 OXIDOREDUCTASE 03-OCT-07 2RGJ
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    OXIDOREDUCTASE                          03-OCT-07   2RGJ              
TITLE     CRYSTAL STRUCTURE OF FLAVIN-CONTAINING MONOOXYGENASE PHZS             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLAVIN-CONTAINING MONOOXYGENASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.14.13.-;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 GENE: PHZS;                                                          
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);                                
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    MONOOXYGENASE, FLAVIN, FAD, PHENAZINE, PYOCYANIN, PSEUDOMONAS,        
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.LADNER,J.F.PARSONS,B.T.GREENHAGEN,H.ROBINSON                      
REVDAT   3   25-OCT-17 2RGJ    1       REMARK                                   
REVDAT   2   24-FEB-09 2RGJ    1       VERSN                                    
REVDAT   1   20-MAY-08 2RGJ    0                                                
JRNL        AUTH   B.T.GREENHAGEN,K.SHI,H.ROBINSON,S.GAMAGE,A.K.BERA,           
JRNL        AUTH 2 J.E.LADNER,J.F.PARSONS                                       
JRNL        TITL   CRYSTAL STRUCTURE OF THE PYOCYANIN BIOSYNTHETIC PROTEIN      
JRNL        TITL 2 PHZS.                                                        
JRNL        REF    BIOCHEMISTRY                  V.  47  5281 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18416536                                                     
JRNL        DOI    10.1021/BI702480T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14318                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 725                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1578                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 92                           
REMARK   3   BIN FREE R VALUE                    : 0.3740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2869                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.62000                                             
REMARK   3    B22 (A**2) : 2.94000                                              
REMARK   3    B33 (A**2) : -1.32000                                             
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): 0.655         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.208         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.863         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3009 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4105 ; 1.700 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   381 ; 6.837 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;37.132 ;23.094       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   469 ;19.605 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.321 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   448 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2323 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1315 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1960 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   155 ; 0.168 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    54 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.137 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1925 ; 1.022 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2970 ; 1.472 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1317 ; 2.145 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1132 ; 3.518 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2RGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044831.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14742                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 12.80                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 23.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXCD                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG400, 0.1M AMMONIUM NITRATE,       
REMARK 280  0.1M SODIUM ACETATE, BATCH UNDER OIL, TEMPERATURE 298K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        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       31.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.43000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       91.01000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.43000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       91.01000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       32.43000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       91.01000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       32.43000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       91.01000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     THR A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     ALA A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     LEU A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     ALA A   389                                                      
REMARK 465     ILE A   390                                                      
REMARK 465     THR A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 465     TYR A   394                                                      
REMARK 465     ARG A   395                                                      
REMARK 465     ASN A   396                                                      
REMARK 465     GLN A   397                                                      
REMARK 465     VAL A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     ARG A   400                                                      
REMARK 465     PRO A   401                                                      
REMARK 465     ARG A   402                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A  32   C     LEU A  33   N      -0.183                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  33   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  42       59.71    -66.47                                   
REMARK 500    VAL A  45     -157.42   -120.53                                   
REMARK 500    ASP A 148     -168.63   -103.63                                   
REMARK 500    ALA A 164       42.55   -109.22                                   
REMARK 500    LEU A 182      132.19    -38.70                                   
REMARK 500    LEU A 200     -135.42     46.97                                   
REMARK 500    LYS A 203       32.55   -149.00                                   
REMARK 500    ARG A 302      117.50   -167.02                                   
REMARK 500    HIS A 313       66.41   -152.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 403                 
DBREF  2RGJ A    1   402  UNP    Q9HWG9   Q9HWG9_PSEAE     1    402             
SEQRES   1 A  402  MSE SER GLU PRO ILE ASP ILE LEU ILE ALA GLY ALA GLY          
SEQRES   2 A  402  ILE GLY GLY LEU SER CYS ALA LEU ALA LEU HIS GLN ALA          
SEQRES   3 A  402  GLY ILE GLY LYS VAL THR LEU LEU GLU SER SER SER GLU          
SEQRES   4 A  402  ILE ARG PRO LEU GLY VAL GLY ILE ASN ILE GLN PRO ALA          
SEQRES   5 A  402  ALA VAL GLU ALA LEU ALA GLU LEU GLY LEU GLY PRO ALA          
SEQRES   6 A  402  LEU ALA ALA THR ALA ILE PRO THR HIS GLU LEU ARG TYR          
SEQRES   7 A  402  ILE ASP GLN SER GLY ALA THR VAL TRP SER GLU PRO ARG          
SEQRES   8 A  402  GLY VAL GLU ALA GLY ASN ALA TYR PRO GLN TYR SER ILE          
SEQRES   9 A  402  HIS ARG GLY GLU LEU GLN MSE ILE LEU LEU ALA ALA VAL          
SEQRES  10 A  402  ARG GLU ARG LEU GLY GLN GLN ALA VAL ARG THR GLY LEU          
SEQRES  11 A  402  GLY VAL GLU ARG ILE GLU GLU ARG ASP GLY ARG VAL LEU          
SEQRES  12 A  402  ILE GLY ALA ARG ASP GLY HIS GLY LYS PRO GLN ALA LEU          
SEQRES  13 A  402  GLY ALA ASP VAL LEU VAL GLY ALA ASP GLY ILE HIS SER          
SEQRES  14 A  402  ALA VAL ARG ALA HIS LEU HIS PRO ASP GLN ARG PRO LEU          
SEQRES  15 A  402  SER HIS GLY GLY ILE THR MSE TRP ARG GLY VAL THR GLU          
SEQRES  16 A  402  PHE ASP ARG PHE LEU ASP GLY LYS THR MSE ILE VAL ALA          
SEQRES  17 A  402  ASN ASP GLU HIS TRP SER ARG LEU VAL ALA TYR PRO ILE          
SEQRES  18 A  402  SER ALA ARG HIS ALA ALA GLU GLY LYS SER LEU VAL ASN          
SEQRES  19 A  402  TRP VAL CYS MSE VAL PRO SER ALA ALA VAL GLY GLN LEU          
SEQRES  20 A  402  ASP ASN GLU ALA ASP TRP ASN ARG ASP GLY ARG LEU GLU          
SEQRES  21 A  402  ASP VAL LEU PRO PHE PHE ALA ASP TRP ASP LEU GLY TRP          
SEQRES  22 A  402  PHE ASP ILE ARG ASP LEU LEU THR ARG ASN GLN LEU ILE          
SEQRES  23 A  402  LEU GLN TYR PRO MSE VAL ASP ARG ASP PRO LEU PRO HIS          
SEQRES  24 A  402  TRP GLY ARG GLY ARG ILE THR LEU LEU GLY ASP ALA ALA          
SEQRES  25 A  402  HIS LEU MSE TYR PRO MSE GLY ALA ASN GLY ALA SER GLN          
SEQRES  26 A  402  ALA ILE LEU ASP GLY ILE GLU LEU ALA ALA ALA LEU ALA          
SEQRES  27 A  402  ARG ASN ALA ASP VAL ALA ALA ALA LEU ARG GLU TYR GLU          
SEQRES  28 A  402  GLU ALA ARG ARG PRO THR ALA ASN LYS ILE ILE LEU ALA          
SEQRES  29 A  402  ASN ARG GLU ARG GLU LYS GLU GLU TRP ALA ALA ALA SER          
SEQRES  30 A  402  ARG PRO LYS THR GLU LYS SER ALA ALA LEU GLU ALA ILE          
SEQRES  31 A  402  THR GLY SER TYR ARG ASN GLN VAL GLU ARG PRO ARG              
MODRES 2RGJ MSE A  111  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  189  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  205  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  238  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  291  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  315  MET  SELENOMETHIONINE                                   
MODRES 2RGJ MSE A  318  MET  SELENOMETHIONINE                                   
HET    MSE  A 111       8                                                       
HET    MSE  A 189       8                                                       
HET    MSE  A 205       8                                                       
HET    MSE  A 238       8                                                       
HET    MSE  A 291       8                                                       
HET    MSE  A 315       8                                                       
HET    MSE  A 318       8                                                       
HET    FAD  A 403      53                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   1  MSE    7(C5 H11 N O2 SE)                                            
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  HOH   *54(H2 O)                                                     
HELIX    1   1 GLY A   13  ALA A   26  1                                  14    
HELIX    2   2 GLN A   50  LEU A   60  1                                  11    
HELIX    3   3 LEU A   62  ALA A   68  1                                   7    
HELIX    4   4 GLY A   92  GLY A   96  5                                   5    
HELIX    5   5 ARG A  106  GLY A  122  1                                  17    
HELIX    6   6 GLN A  123  VAL A  126  5                                   4    
HELIX    7   7 SER A  169  HIS A  176  1                                   8    
HELIX    8   8 SER A  222  GLU A  228  1                                   7    
HELIX    9   9 SER A  241  GLY A  245  1                                   5    
HELIX   10  10 ARG A  258  LEU A  263  1                                   6    
HELIX   11  11 PRO A  264  PHE A  266  5                                   3    
HELIX   12  12 ASP A  275  ARG A  282  1                                   8    
HELIX   13  13 GLY A  309  LEU A  314  1                                   6    
HELIX   14  14 GLY A  322  ASN A  340  1                                  19    
HELIX   15  15 ASP A  342  ARG A  378  1                                  37    
SHEET    1   A 5 ARG A 127  THR A 128  0                                        
SHEET    2   A 5 LYS A  30  GLU A  35  1  N  LEU A  33   O  ARG A 127           
SHEET    3   A 5 ASP A   6  ALA A  10  1  N  ILE A   7   O  LYS A  30           
SHEET    4   A 5 VAL A 160  GLY A 163  1  O  VAL A 162   N  LEU A   8           
SHEET    5   A 5 ILE A 305  LEU A 307  1  O  THR A 306   N  GLY A 163           
SHEET    1   B 2 GLY A  46  ILE A  49  0                                        
SHEET    2   B 2 TYR A 102  HIS A 105 -1  O  TYR A 102   N  ILE A  49           
SHEET    1   C 7 THR A  85  PRO A  90  0                                        
SHEET    2   C 7 GLU A  75  ILE A  79 -1  N  TYR A  78   O  TRP A  87           
SHEET    3   C 7 THR A 204  ASN A 209  1  O  MSE A 205   N  GLU A  75           
SHEET    4   C 7 ARG A 215  PRO A 220 -1  O  ALA A 218   N  ILE A 206           
SHEET    5   C 7 SER A 231  PRO A 240 -1  O  ASN A 234   N  TYR A 219           
SHEET    6   C 7 SER A 183  PHE A 196 -1  N  THR A 188   O  VAL A 239           
SHEET    7   C 7 ASN A 283  ASP A 293 -1  O  MSE A 291   N  GLY A 185           
SHEET    1   D 3 GLY A 131  GLU A 137  0                                        
SHEET    2   D 3 VAL A 142  ARG A 147 -1  O  GLY A 145   N  GLU A 133           
SHEET    3   D 3 PRO A 153  ALA A 158 -1  O  LEU A 156   N  ILE A 144           
LINK         C   GLN A 110                 N   MSE A 111     1555   1555  1.34  
LINK         C   MSE A 111                 N   ILE A 112     1555   1555  1.33  
LINK         C   THR A 188                 N   MSE A 189     1555   1555  1.32  
LINK         C   MSE A 189                 N   TRP A 190     1555   1555  1.33  
LINK         C   THR A 204                 N   MSE A 205     1555   1555  1.32  
LINK         C   MSE A 205                 N   ILE A 206     1555   1555  1.33  
LINK         C   CYS A 237                 N   MSE A 238     1555   1555  1.33  
LINK         C   MSE A 238                 N   VAL A 239     1555   1555  1.34  
LINK         C   PRO A 290                 N   MSE A 291     1555   1555  1.31  
LINK         C   MSE A 291                 N   VAL A 292     1555   1555  1.33  
LINK         C   LEU A 314                 N   MSE A 315     1555   1555  1.33  
LINK         C   MSE A 315                 N   TYR A 316     1555   1555  1.33  
LINK         C   PRO A 317                 N   MSE A 318     1555   1555  1.32  
LINK         C   MSE A 318                 N   GLY A 319     1555   1555  1.33  
SITE     1 AC1 27 GLY A  11  GLY A  13  ILE A  14  GLY A  15                    
SITE     2 AC1 27 LEU A  34  GLU A  35  SER A  36  LEU A  43                    
SITE     3 AC1 27 GLY A  44  ILE A  47  ARG A 106  GLY A 131                    
SITE     4 AC1 27 ALA A 164  ASP A 165  GLY A 166  ARG A 191                    
SITE     5 AC1 27 TRP A 253  ASN A 254  GLY A 309  ASP A 310                    
SITE     6 AC1 27 GLY A 322  ALA A 323  HOH A 407  HOH A 408                    
SITE     7 AC1 27 HOH A 409  HOH A 423  HOH A 437                               
CRYST1   63.500   64.860  182.020  90.00  90.00  90.00 I 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      0.015748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015418  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005494        0.00000                         
ATOM      1  N   PRO A   4      20.735  18.863  98.135  1.00 50.90           N  
ATOM      2  CA  PRO A   4      21.285  17.643  97.519  1.00 50.73           C  
ATOM      3  C   PRO A   4      20.305  16.963  96.526  1.00 50.23           C  
ATOM      4  O   PRO A   4      19.609  16.021  96.906  1.00 50.38           O  
ATOM      5  CB  PRO A   4      21.538  16.736  98.735  1.00 50.65           C  
ATOM      6  CG  PRO A   4      20.534  17.234  99.791  1.00 50.75           C  
ATOM      7  CD  PRO A   4      20.484  18.711  99.585  1.00 50.86           C  
ATOM      8  N   ILE A   5      20.241  17.425  95.274  1.00 49.39           N  
ATOM      9  CA  ILE A   5      19.304  16.806  94.291  1.00 48.59           C  
ATOM     10  C   ILE A   5      19.873  15.642  93.453  1.00 47.22           C  
ATOM     11  O   ILE A   5      21.064  15.639  93.095  1.00 46.58           O  
ATOM     12  CB  ILE A   5      18.577  17.829  93.360  1.00 48.86           C  
ATOM     13  CG1 ILE A   5      19.539  18.913  92.812  1.00 50.15           C  
ATOM     14  CG2 ILE A   5      17.330  18.377  94.058  1.00 48.87           C  
ATOM     15  CD1 ILE A   5      20.001  20.027  93.824  1.00 51.66           C  
ATOM     16  N   ASP A   6      19.021  14.654  93.168  1.00 45.46           N  
ATOM     17  CA  ASP A   6      19.434  13.568  92.290  1.00 44.43           C  
ATOM     18  C   ASP A   6      18.780  13.649  90.917  1.00 43.20           C  
ATOM     19  O   ASP A   6      17.543  13.724  90.757  1.00 42.94           O  
ATOM     20  CB  ASP A   6      19.327  12.180  92.926  1.00 44.89           C  
ATOM     21  CG  ASP A   6      17.923  11.764  93.173  1.00 46.50           C  
ATOM     22  OD1 ASP A   6      17.181  12.545  93.796  1.00 51.63           O  
ATOM     23  OD2 ASP A   6      17.551  10.655  92.756  1.00 47.55           O  
ATOM     24  N   ILE A   7      19.659  13.647  89.929  1.00 41.37           N  
ATOM     25  CA  ILE A   7      19.298  13.961  88.565  1.00 40.02           C  
ATOM     26  C   ILE A   7      19.413  12.720  87.710  1.00 38.55           C  
ATOM     27  O   ILE A   7      20.419  12.012  87.744  1.00 38.23           O  
ATOM     28  CB  ILE A   7      20.139  15.150  88.045  1.00 40.08           C  
ATOM     29  CG1 ILE A   7      19.741  16.406  88.844  1.00 39.88           C  
ATOM     30  CG2 ILE A   7      19.935  15.351  86.547  1.00 39.83           C  
ATOM     31  CD1 ILE A   7      20.699  17.566  88.748  1.00 39.55           C  
ATOM     32  N   LEU A   8      18.342  12.434  86.988  1.00 37.00           N  
ATOM     33  CA  LEU A   8      18.366  11.355  86.014  1.00 36.15           C  
ATOM     34  C   LEU A   8      18.452  11.949  84.606  1.00 34.34           C  
ATOM     35  O   LEU A   8      17.707  12.857  84.270  1.00 33.71           O  
ATOM     36  CB  LEU A   8      17.140  10.455  86.178  1.00 36.61           C  
ATOM     37  CG  LEU A   8      17.305   8.982  85.765  1.00 39.35           C  
ATOM     38  CD1 LEU A   8      18.671   8.415  86.157  1.00 41.05           C  
ATOM     39  CD2 LEU A   8      16.211   8.133  86.410  1.00 42.13           C  
ATOM     40  N   ILE A   9      19.399  11.482  83.807  1.00 32.87           N  
ATOM     41  CA  ILE A   9      19.479  11.931  82.424  1.00 31.59           C  
ATOM     42  C   ILE A   9      19.226  10.730  81.518  1.00 31.03           C  
ATOM     43  O   ILE A   9      19.962   9.752  81.599  1.00 31.73           O  
ATOM     44  CB  ILE A   9      20.862  12.525  82.057  1.00 31.68           C  
ATOM     45  CG1 ILE A   9      21.211  13.775  82.886  1.00 31.02           C  
ATOM     46  CG2 ILE A   9      20.905  12.866  80.570  1.00 32.12           C  
ATOM     47  CD1 ILE A   9      22.753  14.152  82.823  1.00 30.32           C  
ATOM     48  N   ALA A  10      18.198  10.813  80.669  1.00 29.69           N  
ATOM     49  CA  ALA A  10      17.896   9.799  79.649  1.00 28.70           C  
ATOM     50  C   ALA A  10      18.730  10.054  78.391  1.00 28.30           C  
ATOM     51  O   ALA A  10      18.557  11.071  77.713  1.00 28.43           O  
ATOM     52  CB  ALA A  10      16.413   9.811  79.302  1.00 27.90           C  
ATOM     53  N   GLY A  11      19.653   9.150  78.109  1.00 27.07           N  
ATOM     54  CA  GLY A  11      20.486   9.253  76.931  1.00 26.52           C  
ATOM     55  C   GLY A  11      21.906   9.657  77.258  1.00 26.36           C  
ATOM     56  O   GLY A  11      22.150  10.709  77.872  1.00 26.51           O  
ATOM     57  N   ALA A  12      22.856   8.833  76.827  1.00 25.78           N  
ATOM     58  CA  ALA A  12      24.284   9.115  77.071  1.00 25.30           C  
ATOM     59  C   ALA A  12      25.017   9.501  75.771  1.00 24.92           C  
ATOM     60  O   ALA A  12      26.173   9.158  75.569  1.00 24.29           O  
ATOM     61  CB  ALA A  12      24.945   7.919  77.772  1.00 24.75           C  
ATOM     62  N   GLY A  13      24.313  10.205  74.887  1.00 24.70           N  
ATOM     63  CA  GLY A  13      24.882  10.660  73.648  1.00 24.83           C  
ATOM     64  C   GLY A  13      25.701  11.893  73.974  1.00 25.13           C  
ATOM     65  O   GLY A  13      26.214  12.034  75.069  1.00 26.03           O  
ATOM     66  N   ILE A  14      25.797  12.812  73.041  1.00 24.55           N  
ATOM     67  CA  ILE A  14      26.727  13.876  73.188  1.00 24.81           C  
ATOM     68  C   ILE A  14      26.219  14.894  74.184  1.00 25.23           C  
ATOM     69  O   ILE A  14      26.986  15.380  75.014  1.00 25.02           O  
ATOM     70  CB  ILE A  14      27.132  14.439  71.784  1.00 25.43           C  
ATOM     71  CG1 ILE A  14      28.236  13.522  71.237  1.00 24.75           C  
ATOM     72  CG2 ILE A  14      27.555  15.911  71.870  1.00 23.54           C  
ATOM     73  CD1 ILE A  14      28.402  13.558  69.817  1.00 29.26           C  
ATOM     74  N   GLY A  15      24.917  15.185  74.093  1.00 25.44           N  
ATOM     75  CA  GLY A  15      24.213  16.108  74.979  1.00 24.82           C  
ATOM     76  C   GLY A  15      24.159  15.611  76.404  1.00 25.44           C  
ATOM     77  O   GLY A  15      24.369  16.394  77.345  1.00 25.09           O  
ATOM     78  N   GLY A  16      23.895  14.313  76.568  1.00 25.26           N  
ATOM     79  CA  GLY A  16      23.718  13.721  77.883  1.00 25.42           C  
ATOM     80  C   GLY A  16      25.013  13.687  78.672  1.00 26.30           C  
ATOM     81  O   GLY A  16      25.061  14.147  79.820  1.00 26.07           O  
ATOM     82  N   LEU A  17      26.071  13.146  78.069  1.00 26.47           N  
ATOM     83  CA  LEU A  17      27.370  13.056  78.750  1.00 26.78           C  
ATOM     84  C   LEU A  17      27.921  14.425  79.112  1.00 27.53           C  
ATOM     85  O   LEU A  17      28.399  14.655  80.200  1.00 27.86           O  
ATOM     86  CB  LEU A  17      28.364  12.306  77.884  1.00 27.13           C  
ATOM     87  CG  LEU A  17      28.125  10.788  77.845  1.00 26.53           C  
ATOM     88  CD1 LEU A  17      28.908  10.119  76.733  1.00 23.76           C  
ATOM     89  CD2 LEU A  17      28.423  10.177  79.211  1.00 25.56           C  
ATOM     90  N   SER A  18      27.789  15.356  78.195  1.00 28.27           N  
ATOM     91  CA  SER A  18      28.344  16.673  78.363  1.00 28.87           C  
ATOM     92  C   SER A  18      27.587  17.448  79.455  1.00 28.91           C  
ATOM     93  O   SER A  18      28.179  18.116  80.278  1.00 28.82           O  
ATOM     94  CB  SER A  18      28.295  17.364  76.996  1.00 28.18           C  
ATOM     95  OG  SER A  18      28.647  18.702  77.128  1.00 31.06           O  
ATOM     96  N   CYS A  19      26.267  17.315  79.472  1.00 30.32           N  
ATOM     97  CA  CYS A  19      25.428  17.853  80.526  1.00 30.28           C  
ATOM     98  C   CYS A  19      25.826  17.335  81.917  1.00 30.79           C  
ATOM     99  O   CYS A  19      25.915  18.119  82.873  1.00 30.95           O  
ATOM    100  CB  CYS A  19      23.988  17.473  80.254  1.00 30.46           C  
ATOM    101  SG  CYS A  19      22.832  18.115  81.462  1.00 32.41           S  
ATOM    102  N   ALA A  20      26.074  16.025  82.011  1.00 30.69           N  
ATOM    103  CA  ALA A  20      26.478  15.380  83.235  1.00 31.30           C  
ATOM    104  C   ALA A  20      27.760  16.049  83.702  1.00 32.47           C  
ATOM    105  O   ALA A  20      27.875  16.442  84.870  1.00 33.31           O  
ATOM    106  CB  ALA A  20      26.684  13.905  83.001  1.00 30.84           C  
ATOM    107  N   LEU A  21      28.704  16.227  82.778  1.00 33.09           N  
ATOM    108  CA  LEU A  21      29.937  16.967  83.060  1.00 33.55           C  
ATOM    109  C   LEU A  21      29.671  18.407  83.511  1.00 33.88           C  
ATOM    110  O   LEU A  21      30.270  18.865  84.463  1.00 34.07           O  
ATOM    111  CB  LEU A  21      30.845  16.973  81.835  1.00 33.87           C  
ATOM    112  CG  LEU A  21      32.051  16.048  81.653  1.00 33.82           C  
ATOM    113  CD1 LEU A  21      32.137  14.976  82.709  1.00 32.37           C  
ATOM    114  CD2 LEU A  21      32.143  15.487  80.196  1.00 32.92           C  
ATOM    115  N   ALA A  22      28.779  19.124  82.846  1.00 34.26           N  
ATOM    116  CA  ALA A  22      28.508  20.519  83.256  1.00 35.06           C  
ATOM    117  C   ALA A  22      27.920  20.570  84.676  1.00 35.87           C  
ATOM    118  O   ALA A  22      28.314  21.394  85.493  1.00 34.71           O  
ATOM    119  CB  ALA A  22      27.589  21.218  82.264  1.00 33.90           C  
ATOM    120  N   LEU A  23      26.971  19.671  84.934  1.00 37.21           N  
ATOM    121  CA  LEU A  23      26.343  19.527  86.222  1.00 38.43           C  
ATOM    122  C   LEU A  23      27.441  19.341  87.282  1.00 40.19           C  
ATOM    123  O   LEU A  23      27.569  20.167  88.186  1.00 40.21           O  
ATOM    124  CB  LEU A  23      25.371  18.333  86.179  1.00 37.76           C  
ATOM    125  CG  LEU A  23      23.850  18.500  85.941  1.00 36.81           C  
ATOM    126  CD1 LEU A  23      23.374  19.937  85.759  1.00 34.25           C  
ATOM    127  CD2 LEU A  23      23.280  17.567  84.823  1.00 33.74           C  
ATOM    128  N   HIS A  24      28.230  18.270  87.141  1.00 42.05           N  
ATOM    129  CA  HIS A  24      29.413  17.987  87.970  1.00 44.07           C  
ATOM    130  C   HIS A  24      30.301  19.203  88.271  1.00 44.84           C  
ATOM    131  O   HIS A  24      30.569  19.509  89.427  1.00 45.67           O  
ATOM    132  CB  HIS A  24      30.251  16.918  87.301  1.00 43.96           C  
ATOM    133  CG  HIS A  24      31.249  16.274  88.208  1.00 47.36           C  
ATOM    134  ND1 HIS A  24      32.529  16.765  88.378  1.00 49.75           N  
ATOM    135  CD2 HIS A  24      31.168  15.158  88.975  1.00 48.28           C  
ATOM    136  CE1 HIS A  24      33.189  15.985  89.217  1.00 50.25           C  
ATOM    137  NE2 HIS A  24      32.388  15.000  89.588  1.00 49.87           N  
ATOM    138  N   GLN A  25      30.753  19.892  87.237  1.00 45.63           N  
ATOM    139  CA  GLN A  25      31.559  21.091  87.415  1.00 47.27           C  
ATOM    140  C   GLN A  25      30.820  22.149  88.260  1.00 47.72           C  
ATOM    141  O   GLN A  25      31.426  22.757  89.158  1.00 48.67           O  
ATOM    142  CB  GLN A  25      31.959  21.672  86.053  1.00 47.47           C  
ATOM    143  CG  GLN A  25      33.066  22.739  86.086  1.00 50.96           C  
ATOM    144  CD  GLN A  25      34.474  22.159  85.870  1.00 53.84           C  
ATOM    145  OE1 GLN A  25      34.631  21.046  85.355  1.00 55.33           O  
ATOM    146  NE2 GLN A  25      35.499  22.919  86.267  1.00 53.41           N  
ATOM    147  N   ALA A  26      29.530  22.356  87.977  1.00 47.57           N  
ATOM    148  CA  ALA A  26      28.694  23.335  88.676  1.00 47.69           C  
ATOM    149  C   ALA A  26      28.391  22.915  90.117  1.00 48.08           C  
ATOM    150  O   ALA A  26      27.769  23.667  90.861  1.00 47.46           O  
ATOM    151  CB  ALA A  26      27.407  23.575  87.919  1.00 47.54           C  
ATOM    152  N   GLY A  27      28.843  21.711  90.477  1.00 48.75           N  
ATOM    153  CA  GLY A  27      28.767  21.166  91.829  1.00 49.76           C  
ATOM    154  C   GLY A  27      27.413  20.584  92.181  1.00 50.61           C  
ATOM    155  O   GLY A  27      27.003  20.646  93.345  1.00 50.95           O  
ATOM    156  N   ILE A  28      26.741  19.982  91.192  1.00 50.83           N  
ATOM    157  CA  ILE A  28      25.301  19.708  91.266  1.00 50.85           C  
ATOM    158  C   ILE A  28      24.895  18.376  91.883  1.00 51.29           C  
ATOM    159  O   ILE A  28      23.701  18.135  92.125  1.00 51.34           O  
ATOM    160  CB  ILE A  28      24.625  19.873  89.901  1.00 51.07           C  
ATOM    161  CG1 ILE A  28      23.710  21.118  89.888  1.00 50.74           C  
ATOM    162  CG2 ILE A  28      23.817  18.625  89.575  1.00 50.44           C  
ATOM    163  CD1 ILE A  28      24.336  22.405  90.382  1.00 48.77           C  
ATOM    164  N   GLY A  29      25.875  17.503  92.120  1.00 51.28           N  
ATOM    165  CA  GLY A  29      25.673  16.410  93.085  1.00 50.36           C  
ATOM    166  C   GLY A  29      25.480  15.019  92.533  1.00 49.47           C  
ATOM    167  O   GLY A  29      26.437  14.398  92.066  1.00 49.65           O  
ATOM    168  N   LYS A  30      24.266  14.492  92.641  1.00 48.19           N  
ATOM    169  CA  LYS A  30      24.043  13.167  92.106  1.00 47.16           C  
ATOM    170  C   LYS A  30      23.368  13.202  90.743  1.00 46.05           C  
ATOM    171  O   LYS A  30      22.242  13.688  90.583  1.00 45.76           O  
ATOM    172  CB  LYS A  30      23.335  12.206  93.057  1.00 47.20           C  
ATOM    173  CG  LYS A  30      23.755  10.770  92.715  1.00 48.85           C  
ATOM    174  CD  LYS A  30      22.927   9.707  93.423  1.00 52.57           C  
ATOM    175  CE  LYS A  30      23.479   8.322  93.131  1.00 53.43           C  
ATOM    176  NZ  LYS A  30      23.286   7.456  94.331  1.00 55.15           N  
ATOM    177  N   VAL A  31      24.117  12.685  89.777  1.00 44.18           N  
ATOM    178  CA  VAL A  31      23.722  12.588  88.403  1.00 42.30           C  
ATOM    179  C   VAL A  31      23.898  11.130  88.037  1.00 41.14           C  
ATOM    180  O   VAL A  31      24.947  10.538  88.251  1.00 40.21           O  
ATOM    181  CB  VAL A  31      24.635  13.431  87.486  1.00 42.29           C  
ATOM    182  CG1 VAL A  31      24.221  13.258  86.032  1.00 41.68           C  
ATOM    183  CG2 VAL A  31      24.590  14.909  87.882  1.00 42.19           C  
ATOM    184  N   THR A  32      22.948  10.436  87.366  1.00 39.91           N  
ATOM    185  CA  THR A  32      22.919   9.119  86.776  1.00 39.55           C  
ATOM    186  C   THR A  32      22.407   9.252  85.352  1.00 38.29           C  
ATOM    187  O   THR A  32      21.585  10.136  85.043  1.00 38.06           O  
ATOM    188  CB  THR A  32      22.153   8.089  87.637  1.00 39.02           C  
ATOM    189  OG1 THR A  32      22.793   7.961  88.911  1.00 41.20           O  
ATOM    190  CG2 THR A  32      22.087   6.738  86.946  1.00 40.77           C  
ATOM    191  N   LEU A  33      22.928   8.606  84.552  1.00 37.24           N  
ATOM    192  CA  LEU A  33      22.372   8.617  83.208  1.00 36.56           C  
ATOM    193  C   LEU A  33      22.004   7.249  82.683  1.00 35.83           C  
ATOM    194  O   LEU A  33      22.658   6.246  82.989  1.00 35.78           O  
ATOM    195  CB  LEU A  33      23.200   9.454  82.210  1.00 36.49           C  
ATOM    196  CG  LEU A  33      24.708   9.660  82.034  1.00 36.10           C  
ATOM    197  CD1 LEU A  33      24.900  10.683  80.881  1.00 34.65           C  
ATOM    198  CD2 LEU A  33      25.463  10.127  83.302  1.00 34.92           C  
ATOM    199  N   LEU A  34      20.921   7.228  81.918  1.00 35.16           N  
ATOM    200  CA  LEU A  34      20.350   5.993  81.400  1.00 35.22           C  
ATOM    201  C   LEU A  34      20.431   5.954  79.876  1.00 35.48           C  
ATOM    202  O   LEU A  34      19.935   6.840  79.211  1.00 36.11           O  
ATOM    203  CB  LEU A  34      18.903   5.908  81.848  1.00 34.85           C  
ATOM    204  CG  LEU A  34      18.440   5.295  83.180  1.00 34.63           C  
ATOM    205  CD1 LEU A  34      19.450   5.282  84.322  1.00 33.72           C  
ATOM    206  CD2 LEU A  34      17.148   5.980  83.602  1.00 35.84           C  
ATOM    207  N   GLU A  35      21.067   4.929  79.332  1.00 35.98           N  
ATOM    208  CA  GLU A  35      21.275   4.812  77.888  1.00 36.40           C  
ATOM    209  C   GLU A  35      20.724   3.485  77.377  1.00 37.03           C  
ATOM    210  O   GLU A  35      21.175   2.416  77.813  1.00 36.55           O  
ATOM    211  CB  GLU A  35      22.761   4.911  77.558  1.00 36.17           C  
ATOM    212  CG  GLU A  35      23.153   4.490  76.143  1.00 36.74           C  
ATOM    213  CD  GLU A  35      22.558   5.380  75.049  1.00 38.26           C  
ATOM    214  OE1 GLU A  35      22.550   6.637  75.198  1.00 35.85           O  
ATOM    215  OE2 GLU A  35      22.114   4.792  74.029  1.00 38.59           O  
ATOM    216  N   SER A  36      19.772   3.562  76.442  1.00 37.57           N  
ATOM    217  CA  SER A  36      19.114   2.381  75.915  1.00 38.68           C  
ATOM    218  C   SER A  36      20.054   1.399  75.201  1.00 39.83           C  
ATOM    219  O   SER A  36      19.772   0.208  75.180  1.00 40.64           O  
ATOM    220  CB  SER A  36      17.942   2.765  75.020  1.00 38.44           C  
ATOM    221  OG  SER A  36      18.398   3.333  73.805  1.00 39.10           O  
ATOM    222  N   SER A  37      21.165   1.875  74.635  1.00 40.86           N  
ATOM    223  CA  SER A  37      22.136   0.984  73.976  1.00 41.76           C  
ATOM    224  C   SER A  37      22.892   0.119  74.984  1.00 42.81           C  
ATOM    225  O   SER A  37      23.312   0.606  76.036  1.00 42.28           O  
ATOM    226  CB  SER A  37      23.124   1.780  73.106  1.00 41.45           C  
ATOM    227  OG  SER A  37      22.503   2.155  71.900  1.00 40.77           O  
ATOM    228  N   SER A  38      23.065  -1.156  74.640  1.00 44.75           N  
ATOM    229  CA  SER A  38      23.609  -2.171  75.551  1.00 46.90           C  
ATOM    230  C   SER A  38      25.027  -1.817  75.951  1.00 48.37           C  
ATOM    231  O   SER A  38      25.365  -1.881  77.131  1.00 49.21           O  
ATOM    232  CB  SER A  38      23.596  -3.559  74.906  1.00 47.13           C  
ATOM    233  OG  SER A  38      22.707  -3.621  73.792  1.00 48.58           O  
ATOM    234  N   GLU A  39      25.860  -1.460  74.967  1.00 49.51           N  
ATOM    235  CA  GLU A  39      27.185  -0.873  75.238  1.00 50.66           C  
ATOM    236  C   GLU A  39      27.313   0.443  74.467  1.00 50.68           C  
ATOM    237  O   GLU A  39      26.557   0.676  73.531  1.00 50.57           O  
ATOM    238  CB  GLU A  39      28.322  -1.850  74.898  1.00 51.00           C  
ATOM    239  CG  GLU A  39      28.245  -3.207  75.659  1.00 53.78           C  
ATOM    240  CD  GLU A  39      28.681  -3.138  77.143  1.00 56.35           C  
ATOM    241  OE1 GLU A  39      29.374  -2.166  77.524  1.00 56.65           O  
ATOM    242  OE2 GLU A  39      28.349  -4.073  77.918  0.50 55.61           O  
ATOM    243  N   ILE A  40      28.237   1.314  74.873  1.00 51.10           N  
ATOM    244  CA  ILE A  40      28.379   2.628  74.220  1.00 51.14           C  
ATOM    245  C   ILE A  40      29.487   2.593  73.191  1.00 50.92           C  
ATOM    246  O   ILE A  40      30.642   2.267  73.497  1.00 51.38           O  
ATOM    247  CB  ILE A  40      28.530   3.814  75.226  1.00 51.34           C  
ATOM    248  CG1 ILE A  40      27.139   4.316  75.642  1.00 50.86           C  
ATOM    249  CG2 ILE A  40      29.363   4.983  74.627  1.00 51.03           C  
ATOM    250  CD1 ILE A  40      27.161   5.298  76.786  1.00 50.26           C  
ATOM    251  N   ARG A  41      29.106   2.944  71.970  1.00 50.66           N  
ATOM    252  CA  ARG A  41      29.932   2.736  70.781  1.00 50.54           C  
ATOM    253  C   ARG A  41      30.330   4.046  70.090  1.00 49.32           C  
ATOM    254  O   ARG A  41      29.501   4.946  69.928  1.00 49.01           O  
ATOM    255  CB  ARG A  41      29.138   1.892  69.795  1.00 51.02           C  
ATOM    256  CG  ARG A  41      29.925   0.859  69.061  1.00 53.68           C  
ATOM    257  CD  ARG A  41      29.004  -0.282  68.791  1.00 57.58           C  
ATOM    258  NE  ARG A  41      28.496  -0.836  70.052  1.00 60.31           N  
ATOM    259  CZ  ARG A  41      27.233  -0.754  70.465  1.00 62.80           C  
ATOM    260  NH1 ARG A  41      26.318  -0.127  69.725  1.00 63.33           N  
ATOM    261  NH2 ARG A  41      26.881  -1.312  71.619  1.00 63.78           N  
ATOM    262  N   PRO A  42      31.598   4.145  69.661  1.00 48.34           N  
ATOM    263  CA  PRO A  42      32.055   5.282  68.840  1.00 47.17           C  
ATOM    264  C   PRO A  42      31.412   5.314  67.455  1.00 45.44           C  
ATOM    265  O   PRO A  42      32.114   5.268  66.452  1.00 45.15           O  
ATOM    266  CB  PRO A  42      33.579   5.064  68.712  1.00 47.27           C  
ATOM    267  CG  PRO A  42      33.928   4.008  69.745  1.00 48.67           C  
ATOM    268  CD  PRO A  42      32.681   3.188  69.946  1.00 48.35           C  
ATOM    269  N   LEU A  43      30.087   5.404  67.397  1.00 43.87           N  
ATOM    270  CA  LEU A  43      29.403   5.467  66.092  1.00 42.27           C  
ATOM    271  C   LEU A  43      29.256   6.912  65.592  1.00 41.36           C  
ATOM    272  O   LEU A  43      29.280   7.864  66.394  1.00 40.95           O  
ATOM    273  CB  LEU A  43      28.058   4.728  66.126  1.00 41.24           C  
ATOM    274  CG  LEU A  43      28.152   3.212  66.382  1.00 41.15           C  
ATOM    275  CD1 LEU A  43      26.789   2.603  66.626  1.00 39.29           C  
ATOM    276  CD2 LEU A  43      28.863   2.480  65.237  1.00 39.85           C  
ATOM    277  N   GLY A  44      29.110   7.049  64.269  1.00 40.23           N  
ATOM    278  CA  GLY A  44      28.908   8.329  63.605  1.00 38.02           C  
ATOM    279  C   GLY A  44      30.135   8.760  62.825  1.00 37.14           C  
ATOM    280  O   GLY A  44      31.177   8.109  62.846  1.00 37.40           O  
ATOM    281  N   VAL A  45      30.023   9.896  62.166  1.00 35.73           N  
ATOM    282  CA  VAL A  45      31.037  10.327  61.243  1.00 34.30           C  
ATOM    283  C   VAL A  45      31.543  11.688  61.771  1.00 33.16           C  
ATOM    284  O   VAL A  45      31.431  11.943  62.967  1.00 31.99           O  
ATOM    285  CB  VAL A  45      30.463  10.226  59.774  1.00 34.45           C  
ATOM    286  CG1 VAL A  45      29.992  11.532  59.208  1.00 33.60           C  
ATOM    287  CG2 VAL A  45      31.422   9.510  58.867  1.00 35.36           C  
ATOM    288  N   GLY A  46      32.131  12.533  60.933  1.00 31.96           N  
ATOM    289  CA  GLY A  46      32.673  13.789  61.415  1.00 31.13           C  
ATOM    290  C   GLY A  46      31.590  14.697  61.933  1.00 31.20           C  
ATOM    291  O   GLY A  46      30.472  14.654  61.454  1.00 31.42           O  
ATOM    292  N   ILE A  47      31.910  15.507  62.938  1.00 31.34           N  
ATOM    293  CA  ILE A  47      31.048  16.623  63.341  1.00 31.57           C  
ATOM    294  C   ILE A  47      31.918  17.837  63.587  1.00 31.21           C  
ATOM    295  O   ILE A  47      33.145  17.711  63.700  1.00 31.80           O  
ATOM    296  CB  ILE A  47      30.125  16.341  64.597  1.00 31.12           C  
ATOM    297  CG1 ILE A  47      30.941  15.994  65.824  1.00 31.61           C  
ATOM    298  CG2 ILE A  47      29.099  15.216  64.332  1.00 31.65           C  
ATOM    299  CD1 ILE A  47      30.093  15.969  67.108  1.00 32.68           C  
ATOM    300  N   ASN A  48      31.273  18.999  63.656  1.00 30.52           N  
ATOM    301  CA  ASN A  48      31.927  20.258  63.939  1.00 29.92           C  
ATOM    302  C   ASN A  48      31.545  20.823  65.296  1.00 29.00           C  
ATOM    303  O   ASN A  48      30.350  20.974  65.611  1.00 29.08           O  
ATOM    304  CB  ASN A  48      31.606  21.286  62.844  1.00 30.41           C  
ATOM    305  CG  ASN A  48      32.504  21.129  61.638  1.00 31.85           C  
ATOM    306  OD1 ASN A  48      33.682  21.509  61.670  1.00 31.82           O  
ATOM    307  ND2 ASN A  48      31.967  20.524  60.572  1.00 34.44           N  
ATOM    308  N   ILE A  49      32.566  21.132  66.093  1.00 27.25           N  
ATOM    309  CA  ILE A  49      32.374  21.848  67.344  1.00 25.83           C  
ATOM    310  C   ILE A  49      32.763  23.347  67.185  1.00 25.47           C  
ATOM    311  O   ILE A  49      33.915  23.696  66.955  1.00 24.91           O  
ATOM    312  CB  ILE A  49      33.091  21.175  68.541  1.00 25.27           C  
ATOM    313  CG1 ILE A  49      32.975  19.646  68.482  1.00 24.42           C  
ATOM    314  CG2 ILE A  49      32.560  21.732  69.857  1.00 24.16           C  
ATOM    315  CD1 ILE A  49      31.552  19.083  68.412  1.00 23.62           C  
ATOM    316  N   GLN A  50      31.763  24.218  67.266  1.00 25.22           N  
ATOM    317  CA AGLN A  50      32.022  25.633  67.109  0.50 24.87           C  
ATOM    318  CA BGLN A  50      31.949  25.663  67.147  0.50 25.53           C  
ATOM    319  C   GLN A  50      32.834  26.195  68.289  1.00 24.69           C  
ATOM    320  O   GLN A  50      32.829  25.629  69.380  1.00 24.46           O  
ATOM    321  CB AGLN A  50      30.729  26.409  66.848  0.50 24.59           C  
ATOM    322  CB BGLN A  50      30.591  26.394  67.105  0.50 25.27           C  
ATOM    323  CG AGLN A  50      29.997  25.993  65.559  0.50 23.71           C  
ATOM    324  CG BGLN A  50      30.198  27.137  68.385  0.50 26.61           C  
ATOM    325  CD AGLN A  50      30.864  25.921  64.292  0.50 22.55           C  
ATOM    326  CD BGLN A  50      29.056  28.121  68.187  0.50 26.76           C  
ATOM    327  OE1AGLN A  50      30.753  24.963  63.534  0.50 22.28           O  
ATOM    328  OE1BGLN A  50      29.154  29.050  67.380  0.50 30.04           O  
ATOM    329  NE2AGLN A  50      31.706  26.931  64.054  0.50 20.45           N  
ATOM    330  NE2BGLN A  50      27.969  27.927  68.930  0.50 27.56           N  
ATOM    331  N   PRO A  51      33.591  27.287  68.038  1.00 23.98           N  
ATOM    332  CA  PRO A  51      34.460  27.817  69.087  1.00 23.54           C  
ATOM    333  C   PRO A  51      33.839  27.952  70.500  1.00 23.46           C  
ATOM    334  O   PRO A  51      34.480  27.542  71.485  1.00 22.52           O  
ATOM    335  CB  PRO A  51      34.904  29.160  68.497  1.00 23.65           C  
ATOM    336  CG  PRO A  51      34.994  28.852  66.992  1.00 22.62           C  
ATOM    337  CD  PRO A  51      33.736  28.058  66.776  1.00 23.14           C  
ATOM    338  N   ALA A  52      32.604  28.460  70.591  1.00 23.13           N  
ATOM    339  CA  ALA A  52      31.933  28.651  71.898  1.00 22.85           C  
ATOM    340  C   ALA A  52      31.678  27.330  72.647  1.00 22.72           C  
ATOM    341  O   ALA A  52      31.747  27.289  73.869  1.00 22.46           O  
ATOM    342  CB  ALA A  52      30.627  29.435  71.726  1.00 22.27           C  
ATOM    343  N   ALA A  53      31.396  26.256  71.906  1.00 22.46           N  
ATOM    344  CA  ALA A  53      31.215  24.939  72.520  1.00 22.47           C  
ATOM    345  C   ALA A  53      32.575  24.333  72.916  1.00 22.98           C  
ATOM    346  O   ALA A  53      32.670  23.668  73.949  1.00 23.58           O  
ATOM    347  CB  ALA A  53      30.409  24.003  71.589  1.00 21.25           C  
ATOM    348  N   VAL A  54      33.618  24.573  72.114  1.00 23.48           N  
ATOM    349  CA  VAL A  54      34.992  24.146  72.437  1.00 24.56           C  
ATOM    350  C   VAL A  54      35.421  24.891  73.708  1.00 26.56           C  
ATOM    351  O   VAL A  54      36.040  24.321  74.619  1.00 27.27           O  
ATOM    352  CB  VAL A  54      35.984  24.482  71.287  1.00 24.17           C  
ATOM    353  CG1 VAL A  54      37.447  24.235  71.686  1.00 22.89           C  
ATOM    354  CG2 VAL A  54      35.627  23.740  70.017  1.00 21.87           C  
ATOM    355  N   GLU A  55      35.071  26.169  73.773  1.00 28.08           N  
ATOM    356  CA  GLU A  55      35.299  26.950  74.975  1.00 29.95           C  
ATOM    357  C   GLU A  55      34.694  26.228  76.197  1.00 30.06           C  
ATOM    358  O   GLU A  55      35.349  26.075  77.216  1.00 30.33           O  
ATOM    359  CB  GLU A  55      34.719  28.345  74.790  1.00 29.87           C  
ATOM    360  CG  GLU A  55      35.267  29.396  75.723  1.00 34.31           C  
ATOM    361  CD  GLU A  55      35.073  30.819  75.181  1.00 41.36           C  
ATOM    362  OE1 GLU A  55      35.356  31.053  73.969  1.00 42.40           O  
ATOM    363  OE2 GLU A  55      34.623  31.703  75.968  1.00 44.13           O  
ATOM    364  N   ALA A  56      33.452  25.772  76.078  1.00 30.14           N  
ATOM    365  CA  ALA A  56      32.793  25.051  77.164  1.00 30.06           C  
ATOM    366  C   ALA A  56      33.496  23.741  77.455  1.00 30.33           C  
ATOM    367  O   ALA A  56      33.744  23.421  78.602  1.00 30.17           O  
ATOM    368  CB  ALA A  56      31.323  24.815  76.854  1.00 29.05           C  
ATOM    369  N   LEU A  57      33.815  22.972  76.423  1.00 30.87           N  
ATOM    370  CA  LEU A  57      34.519  21.695  76.658  1.00 31.52           C  
ATOM    371  C   LEU A  57      35.901  21.871  77.302  1.00 31.60           C  
ATOM    372  O   LEU A  57      36.285  21.073  78.157  1.00 31.12           O  
ATOM    373  CB  LEU A  57      34.591  20.843  75.391  1.00 31.01           C  
ATOM    374  CG  LEU A  57      33.241  20.474  74.772  1.00 31.45           C  
ATOM    375  CD1 LEU A  57      33.508  19.752  73.493  1.00 32.50           C  
ATOM    376  CD2 LEU A  57      32.428  19.587  75.695  1.00 31.27           C  
ATOM    377  N   ALA A  58      36.620  22.924  76.902  1.00 32.51           N  
ATOM    378  CA  ALA A  58      37.897  23.297  77.525  1.00 33.29           C  
ATOM    379  C   ALA A  58      37.715  23.706  78.985  1.00 34.09           C  
ATOM    380  O   ALA A  58      38.540  23.364  79.843  1.00 34.10           O  
ATOM    381  CB  ALA A  58      38.563  24.417  76.764  1.00 33.46           C  
ATOM    382  N   GLU A  59      36.627  24.418  79.263  1.00 34.44           N  
ATOM    383  CA  GLU A  59      36.322  24.869  80.612  1.00 35.13           C  
ATOM    384  C   GLU A  59      36.088  23.657  81.515  1.00 34.21           C  
ATOM    385  O   GLU A  59      36.391  23.687  82.717  1.00 34.28           O  
ATOM    386  CB  GLU A  59      35.084  25.774  80.604  1.00 35.77           C  
ATOM    387  CG  GLU A  59      35.296  27.142  81.231  1.00 39.31           C  
ATOM    388  CD  GLU A  59      35.207  28.287  80.236  1.00 44.53           C  
ATOM    389  OE1 GLU A  59      35.821  28.202  79.153  1.00 48.84           O  
ATOM    390  OE2 GLU A  59      34.522  29.294  80.532  1.00 47.05           O  
ATOM    391  N   LEU A  60      35.558  22.595  80.922  1.00 32.83           N  
ATOM    392  CA  LEU A  60      35.287  21.356  81.622  1.00 31.77           C  
ATOM    393  C   LEU A  60      36.498  20.451  81.621  1.00 31.70           C  
ATOM    394  O   LEU A  60      36.377  19.289  81.968  1.00 32.37           O  
ATOM    395  CB  LEU A  60      34.128  20.611  80.959  1.00 31.98           C  
ATOM    396  CG  LEU A  60      32.704  21.171  81.040  1.00 30.92           C  
ATOM    397  CD1 LEU A  60      31.788  20.503  80.014  1.00 27.95           C  
ATOM    398  CD2 LEU A  60      32.168  20.986  82.440  1.00 31.45           C  
ATOM    399  N   GLY A  61      37.653  20.963  81.198  1.00 31.24           N  
ATOM    400  CA  GLY A  61      38.915  20.214  81.244  1.00 30.44           C  
ATOM    401  C   GLY A  61      39.173  19.234  80.103  1.00 30.45           C  
ATOM    402  O   GLY A  61      39.963  18.291  80.250  1.00 30.17           O  
ATOM    403  N   LEU A  62      38.537  19.461  78.952  1.00 29.87           N  
ATOM    404  CA  LEU A  62      38.662  18.532  77.835  1.00 29.28           C  
ATOM    405  C   LEU A  62      39.614  19.026  76.742  1.00 29.27           C  
ATOM    406  O   LEU A  62      39.843  18.328  75.741  1.00 29.06           O  
ATOM    407  CB  LEU A  62      37.270  18.179  77.276  1.00 28.98           C  
ATOM    408  CG  LEU A  62      36.386  17.378  78.247  1.00 28.81           C  
ATOM    409  CD1 LEU A  62      34.946  17.179  77.773  1.00 27.56           C  
ATOM    410  CD2 LEU A  62      37.025  16.044  78.562  1.00 29.32           C  
ATOM    411  N   GLY A  63      40.178  20.221  76.951  1.00 29.26           N  
ATOM    412  CA  GLY A  63      41.077  20.858  75.985  1.00 29.06           C  
ATOM    413  C   GLY A  63      42.128  19.984  75.317  1.00 29.38           C  
ATOM    414  O   GLY A  63      42.231  19.950  74.098  1.00 29.78           O  
ATOM    415  N   PRO A  64      42.958  19.302  76.104  1.00 29.60           N  
ATOM    416  CA  PRO A  64      43.998  18.484  75.508  1.00 29.73           C  
ATOM    417  C   PRO A  64      43.493  17.169  74.914  1.00 29.72           C  
ATOM    418  O   PRO A  64      44.151  16.606  74.019  1.00 30.74           O  
ATOM    419  CB  PRO A  64      44.929  18.190  76.700  1.00 29.83           C  
ATOM    420  CG  PRO A  64      44.519  19.133  77.767  1.00 28.66           C  
ATOM    421  CD  PRO A  64      43.060  19.295  77.567  1.00 29.97           C  
ATOM    422  N   ALA A  65      42.381  16.651  75.422  1.00 28.41           N  
ATOM    423  CA  ALA A  65      41.861  15.432  74.852  1.00 28.22           C  
ATOM    424  C   ALA A  65      41.393  15.769  73.440  1.00 28.01           C  
ATOM    425  O   ALA A  65      41.656  15.011  72.488  1.00 28.13           O  
ATOM    426  CB  ALA A  65      40.731  14.853  75.704  1.00 28.26           C  
ATOM    427  N   LEU A  66      40.746  16.930  73.301  1.00 27.43           N  
ATOM    428  CA  LEU A  66      40.327  17.434  71.992  1.00 26.98           C  
ATOM    429  C   LEU A  66      41.497  17.704  71.089  1.00 27.04           C  
ATOM    430  O   LEU A  66      41.432  17.394  69.901  1.00 26.45           O  
ATOM    431  CB  LEU A  66      39.541  18.710  72.131  1.00 26.72           C  
ATOM    432  CG  LEU A  66      38.197  18.578  72.829  1.00 27.40           C  
ATOM    433  CD1 LEU A  66      37.650  20.014  73.046  1.00 24.69           C  
ATOM    434  CD2 LEU A  66      37.238  17.680  72.002  1.00 25.10           C  
ATOM    435  N   ALA A  67      42.573  18.256  71.663  1.00 27.31           N  
ATOM    436  CA  ALA A  67      43.740  18.676  70.881  1.00 27.81           C  
ATOM    437  C   ALA A  67      44.433  17.467  70.325  1.00 28.46           C  
ATOM    438  O   ALA A  67      44.980  17.539  69.259  1.00 29.24           O  
ATOM    439  CB  ALA A  67      44.726  19.512  71.717  1.00 27.43           C  
ATOM    440  N   ALA A  68      44.402  16.358  71.051  1.00 28.90           N  
ATOM    441  CA  ALA A  68      45.013  15.129  70.578  1.00 29.56           C  
ATOM    442  C   ALA A  68      44.119  14.261  69.660  1.00 29.66           C  
ATOM    443  O   ALA A  68      44.561  13.175  69.262  1.00 29.43           O  
ATOM    444  CB  ALA A  68      45.458  14.297  71.772  1.00 29.86           C  
ATOM    445  N   THR A  69      42.892  14.712  69.351  1.00 29.11           N  
ATOM    446  CA  THR A  69      41.926  13.920  68.557  1.00 29.21           C  
ATOM    447  C   THR A  69      41.380  14.639  67.318  1.00 27.97           C  
ATOM    448  O   THR A  69      41.258  14.062  66.226  1.00 27.57           O  
ATOM    449  CB  THR A  69      40.666  13.591  69.369  1.00 29.79           C  
ATOM    450  OG1 THR A  69      41.023  12.998  70.624  1.00 34.35           O  
ATOM    451  CG2 THR A  69      39.805  12.596  68.592  1.00 32.38           C  
ATOM    452  N   ALA A  70      41.035  15.904  67.518  1.00 26.59           N  
ATOM    453  CA  ALA A  70      40.257  16.650  66.582  1.00 25.63           C  
ATOM    454  C   ALA A  70      41.176  17.537  65.772  1.00 25.57           C  
ATOM    455  O   ALA A  70      42.340  17.748  66.149  1.00 25.23           O  
ATOM    456  CB  ALA A  70      39.213  17.459  67.332  1.00 24.94           C  
ATOM    457  N   ILE A  71      40.657  18.033  64.643  1.00 25.42           N  
ATOM    458  CA  ILE A  71      41.407  18.967  63.777  1.00 24.65           C  
ATOM    459  C   ILE A  71      40.986  20.413  64.048  1.00 24.34           C  
ATOM    460  O   ILE A  71      39.816  20.698  64.089  1.00 23.22           O  
ATOM    461  CB  ILE A  71      41.251  18.606  62.265  1.00 24.56           C  
ATOM    462  CG1 ILE A  71      42.000  17.309  61.916  1.00 22.80           C  
ATOM    463  CG2 ILE A  71      41.709  19.746  61.394  1.00 24.42           C  
ATOM    464  CD1 ILE A  71      43.528  17.364  62.140  1.00 20.83           C  
ATOM    465  N   PRO A  72      41.961  21.323  64.289  1.00 25.35           N  
ATOM    466  CA  PRO A  72      41.621  22.738  64.420  1.00 25.14           C  
ATOM    467  C   PRO A  72      41.488  23.394  63.047  1.00 25.19           C  
ATOM    468  O   PRO A  72      42.344  24.157  62.624  1.00 25.55           O  
ATOM    469  CB  PRO A  72      42.805  23.313  65.206  1.00 24.79           C  
ATOM    470  CG  PRO A  72      43.957  22.463  64.862  1.00 24.20           C  
ATOM    471  CD  PRO A  72      43.417  21.091  64.484  1.00 25.48           C  
ATOM    472  N   THR A  73      40.393  23.078  62.366  1.00 25.69           N  
ATOM    473  CA  THR A  73      39.980  23.718  61.111  1.00 25.08           C  
ATOM    474  C   THR A  73      40.184  25.246  61.122  1.00 25.09           C  
ATOM    475  O   THR A  73      39.610  25.970  61.943  1.00 24.85           O  
ATOM    476  CB  THR A  73      38.521  23.365  60.834  1.00 25.35           C  
ATOM    477  OG1 THR A  73      38.374  21.932  60.947  1.00 25.83           O  
ATOM    478  CG2 THR A  73      38.066  23.866  59.435  1.00 24.03           C  
ATOM    479  N   HIS A  74      41.027  25.721  60.215  1.00 24.93           N  
ATOM    480  CA  HIS A  74      41.432  27.117  60.224  1.00 25.59           C  
ATOM    481  C   HIS A  74      40.864  27.849  58.999  1.00 26.13           C  
ATOM    482  O   HIS A  74      40.879  29.081  58.941  1.00 26.50           O  
ATOM    483  CB  HIS A  74      42.960  27.213  60.337  1.00 25.18           C  
ATOM    484  CG  HIS A  74      43.689  26.975  59.051  1.00 25.93           C  
ATOM    485  ND1 HIS A  74      44.771  27.736  58.662  1.00 28.12           N  
ATOM    486  CD2 HIS A  74      43.491  26.070  58.060  1.00 27.24           C  
ATOM    487  CE1 HIS A  74      45.198  27.317  57.480  1.00 28.40           C  
ATOM    488  NE2 HIS A  74      44.431  26.316  57.088  1.00 28.09           N  
ATOM    489  N   GLU A  75      40.305  27.082  58.064  1.00 25.77           N  
ATOM    490  CA  GLU A  75      39.845  27.627  56.803  1.00 27.07           C  
ATOM    491  C   GLU A  75      38.650  26.920  56.147  1.00 26.18           C  
ATOM    492  O   GLU A  75      38.538  25.715  56.187  1.00 25.53           O  
ATOM    493  CB  GLU A  75      40.991  27.760  55.796  1.00 27.36           C  
ATOM    494  CG  GLU A  75      40.634  28.669  54.611  1.00 32.15           C  
ATOM    495  CD  GLU A  75      41.773  28.825  53.651  1.00 40.81           C  
ATOM    496  OE1 GLU A  75      42.825  29.379  54.074  1.00 46.04           O  
ATOM    497  OE2 GLU A  75      41.629  28.396  52.476  1.00 43.94           O  
ATOM    498  N   LEU A  76      37.764  27.717  55.574  1.00 26.22           N  
ATOM    499  CA  LEU A  76      36.695  27.221  54.756  1.00 28.08           C  
ATOM    500  C   LEU A  76      36.830  27.851  53.366  1.00 28.50           C  
ATOM    501  O   LEU A  76      36.837  29.087  53.253  1.00 28.98           O  
ATOM    502  CB  LEU A  76      35.332  27.547  55.401  1.00 27.54           C  
ATOM    503  CG  LEU A  76      34.000  27.496  54.622  1.00 29.36           C  
ATOM    504  CD1 LEU A  76      33.869  26.328  53.654  1.00 31.03           C  
ATOM    505  CD2 LEU A  76      32.861  27.413  55.618  1.00 29.81           C  
ATOM    506  N   ARG A  77      36.987  26.998  52.340  1.00 28.92           N  
ATOM    507  CA  ARG A  77      36.957  27.379  50.903  1.00 29.92           C  
ATOM    508  C   ARG A  77      35.684  26.900  50.220  1.00 28.91           C  
ATOM    509  O   ARG A  77      35.331  25.731  50.318  1.00 29.36           O  
ATOM    510  CB  ARG A  77      38.118  26.750  50.120  1.00 28.83           C  
ATOM    511  CG  ARG A  77      39.497  27.300  50.435  1.00 33.40           C  
ATOM    512  CD  ARG A  77      40.597  26.684  49.533  1.00 33.02           C  
ATOM    513  NE  ARG A  77      41.949  26.917  50.061  1.00 40.30           N  
ATOM    514  CZ  ARG A  77      43.083  26.473  49.498  1.00 41.22           C  
ATOM    515  NH1 ARG A  77      43.065  25.754  48.370  1.00 41.12           N  
ATOM    516  NH2 ARG A  77      44.249  26.743  50.071  1.00 42.49           N  
ATOM    517  N   TYR A  78      35.023  27.785  49.489  1.00 29.23           N  
ATOM    518  CA  TYR A  78      33.956  27.385  48.569  1.00 29.22           C  
ATOM    519  C   TYR A  78      34.573  27.441  47.190  1.00 29.51           C  
ATOM    520  O   TYR A  78      35.143  28.457  46.804  1.00 29.07           O  
ATOM    521  CB  TYR A  78      32.753  28.337  48.682  1.00 29.45           C  
ATOM    522  CG  TYR A  78      31.692  28.166  47.629  1.00 29.29           C  
ATOM    523  CD1 TYR A  78      30.964  26.980  47.525  1.00 30.67           C  
ATOM    524  CD2 TYR A  78      31.404  29.188  46.745  1.00 31.47           C  
ATOM    525  CE1 TYR A  78      29.999  26.810  46.543  1.00 31.50           C  
ATOM    526  CE2 TYR A  78      30.436  29.036  45.752  1.00 31.75           C  
ATOM    527  CZ  TYR A  78      29.730  27.850  45.659  1.00 32.72           C  
ATOM    528  OH  TYR A  78      28.753  27.698  44.685  1.00 31.17           O  
ATOM    529  N   ILE A  79      34.485  26.334  46.466  1.00 30.22           N  
ATOM    530  CA  ILE A  79      35.129  26.212  45.165  1.00 31.74           C  
ATOM    531  C   ILE A  79      34.111  26.031  44.033  1.00 32.42           C  
ATOM    532  O   ILE A  79      33.113  25.325  44.211  1.00 32.94           O  
ATOM    533  CB  ILE A  79      36.170  25.054  45.148  1.00 31.70           C  
ATOM    534  CG1 ILE A  79      35.466  23.695  45.058  1.00 32.33           C  
ATOM    535  CG2 ILE A  79      37.184  25.182  46.370  1.00 30.76           C  
ATOM    536  CD1 ILE A  79      36.378  22.472  45.379  1.00 32.44           C  
ATOM    537  N   ASP A  80      34.363  26.647  42.871  1.00 32.50           N  
ATOM    538  CA  ASP A  80      33.439  26.504  41.736  1.00 32.40           C  
ATOM    539  C   ASP A  80      33.565  25.136  41.064  1.00 32.54           C  
ATOM    540  O   ASP A  80      34.352  24.292  41.500  1.00 31.84           O  
ATOM    541  CB  ASP A  80      33.540  27.661  40.727  1.00 32.42           C  
ATOM    542  CG  ASP A  80      34.885  27.728  40.017  1.00 34.21           C  
ATOM    543  OD1 ASP A  80      35.369  26.687  39.487  1.00 36.42           O  
ATOM    544  OD2 ASP A  80      35.453  28.847  39.973  1.00 35.06           O  
ATOM    545  N   GLN A  81      32.767  24.921  40.019  1.00 32.93           N  
ATOM    546  CA  GLN A  81      32.703  23.626  39.360  1.00 33.57           C  
ATOM    547  C   GLN A  81      33.956  23.246  38.536  1.00 33.94           C  
ATOM    548  O   GLN A  81      34.111  22.103  38.098  1.00 33.30           O  
ATOM    549  CB  GLN A  81      31.402  23.501  38.557  1.00 34.11           C  
ATOM    550  CG  GLN A  81      30.204  23.190  39.465  1.00 33.12           C  
ATOM    551  CD  GLN A  81      30.486  21.976  40.316  1.00 32.30           C  
ATOM    552  OE1 GLN A  81      30.684  20.886  39.797  1.00 35.70           O  
ATOM    553  NE2 GLN A  81      30.546  22.162  41.618  1.00 33.28           N  
ATOM    554  N   SER A  82      34.863  24.195  38.379  1.00 33.75           N  
ATOM    555  CA  SER A  82      36.122  23.906  37.713  1.00 34.47           C  
ATOM    556  C   SER A  82      37.278  23.735  38.732  1.00 33.99           C  
ATOM    557  O   SER A  82      38.414  23.514  38.358  1.00 34.06           O  
ATOM    558  CB  SER A  82      36.421  25.016  36.688  1.00 34.56           C  
ATOM    559  OG  SER A  82      36.600  26.266  37.338  1.00 34.67           O  
ATOM    560  N   GLY A  83      36.970  23.830  40.021  1.00 33.88           N  
ATOM    561  CA  GLY A  83      37.961  23.689  41.081  1.00 32.54           C  
ATOM    562  C   GLY A  83      38.454  25.004  41.648  1.00 32.64           C  
ATOM    563  O   GLY A  83      39.194  25.021  42.612  1.00 33.23           O  
ATOM    564  N   ALA A  84      38.059  26.129  41.078  1.00 32.51           N  
ATOM    565  CA  ALA A  84      38.637  27.381  41.568  1.00 32.38           C  
ATOM    566  C   ALA A  84      38.030  27.820  42.912  1.00 32.57           C  
ATOM    567  O   ALA A  84      36.822  27.650  43.165  1.00 33.01           O  
ATOM    568  CB  ALA A  84      38.530  28.504  40.502  1.00 31.30           C  
ATOM    569  N   THR A  85      38.870  28.390  43.760  1.00 32.45           N  
ATOM    570  CA  THR A  85      38.412  28.993  45.006  1.00 32.85           C  
ATOM    571  C   THR A  85      37.686  30.291  44.693  1.00 33.69           C  
ATOM    572  O   THR A  85      38.285  31.261  44.213  1.00 34.13           O  
ATOM    573  CB  THR A  85      39.587  29.217  46.015  1.00 32.54           C  
ATOM    574  OG1 THR A  85      40.310  27.978  46.179  1.00 32.81           O  
ATOM    575  CG2 THR A  85      39.072  29.673  47.366  1.00 29.65           C  
ATOM    576  N   VAL A  86      36.382  30.293  44.938  1.00 34.49           N  
ATOM    577  CA  VAL A  86      35.576  31.497  44.771  1.00 35.22           C  
ATOM    578  C   VAL A  86      35.570  32.313  46.067  1.00 35.04           C  
ATOM    579  O   VAL A  86      35.909  33.483  46.070  1.00 35.09           O  
ATOM    580  CB  VAL A  86      34.150  31.154  44.461  1.00 35.40           C  
ATOM    581  CG1 VAL A  86      33.424  32.410  44.176  1.00 37.71           C  
ATOM    582  CG2 VAL A  86      34.076  30.225  43.270  1.00 36.65           C  
ATOM    583  N   TRP A  87      35.180  31.672  47.165  1.00 34.96           N  
ATOM    584  CA  TRP A  87      35.138  32.314  48.487  1.00 34.62           C  
ATOM    585  C   TRP A  87      36.003  31.568  49.493  1.00 34.05           C  
ATOM    586  O   TRP A  87      36.045  30.322  49.520  1.00 33.85           O  
ATOM    587  CB  TRP A  87      33.699  32.359  49.012  1.00 34.73           C  
ATOM    588  CG  TRP A  87      33.587  32.837  50.426  1.00 35.07           C  
ATOM    589  CD1 TRP A  87      33.391  32.066  51.547  1.00 34.65           C  
ATOM    590  CD2 TRP A  87      33.687  34.193  50.883  1.00 33.83           C  
ATOM    591  NE1 TRP A  87      33.339  32.874  52.672  1.00 33.99           N  
ATOM    592  CE2 TRP A  87      33.524  34.176  52.295  1.00 33.45           C  
ATOM    593  CE3 TRP A  87      33.904  35.413  50.243  1.00 33.14           C  
ATOM    594  CZ2 TRP A  87      33.577  35.330  53.069  1.00 33.31           C  
ATOM    595  CZ3 TRP A  87      33.935  36.570  51.017  1.00 34.35           C  
ATOM    596  CH2 TRP A  87      33.779  36.514  52.418  1.00 34.37           C  
ATOM    597  N   SER A  88      36.662  32.349  50.335  1.00 32.72           N  
ATOM    598  CA  SER A  88      37.509  31.808  51.354  1.00 32.22           C  
ATOM    599  C   SER A  88      37.330  32.552  52.673  1.00 31.50           C  
ATOM    600  O   SER A  88      37.173  33.757  52.707  1.00 32.42           O  
ATOM    601  CB  SER A  88      38.951  31.871  50.877  1.00 31.63           C  
ATOM    602  OG  SER A  88      39.802  31.381  51.867  1.00 32.96           O  
ATOM    603  N   GLU A  89      37.355  31.826  53.772  1.00 31.05           N  
ATOM    604  CA  GLU A  89      37.261  32.452  55.079  1.00 30.17           C  
ATOM    605  C   GLU A  89      38.051  31.724  56.134  1.00 29.66           C  
ATOM    606  O   GLU A  89      38.141  30.478  56.110  1.00 30.20           O  
ATOM    607  CB  GLU A  89      35.809  32.586  55.535  1.00 29.58           C  
ATOM    608  CG  GLU A  89      35.038  31.294  55.722  1.00 30.19           C  
ATOM    609  CD  GLU A  89      33.599  31.597  56.151  1.00 31.10           C  
ATOM    610  OE1 GLU A  89      32.915  32.274  55.368  1.00 31.74           O  
ATOM    611  OE2 GLU A  89      33.175  31.221  57.272  1.00 30.68           O  
ATOM    612  N   PRO A  90      38.608  32.494  57.080  1.00 28.98           N  
ATOM    613  CA  PRO A  90      39.294  31.915  58.216  1.00 28.47           C  
ATOM    614  C   PRO A  90      38.282  31.240  59.131  1.00 28.29           C  
ATOM    615  O   PRO A  90      37.119  31.651  59.152  1.00 28.23           O  
ATOM    616  CB  PRO A  90      39.882  33.144  58.914  1.00 28.36           C  
ATOM    617  CG  PRO A  90      38.910  34.264  58.539  1.00 28.21           C  
ATOM    618  CD  PRO A  90      38.603  33.975  57.126  1.00 28.76           C  
ATOM    619  N   ARG A  91      38.739  30.234  59.879  1.00 27.59           N  
ATOM    620  CA  ARG A  91      37.963  29.582  60.908  1.00 27.85           C  
ATOM    621  C   ARG A  91      38.763  29.496  62.224  1.00 28.47           C  
ATOM    622  O   ARG A  91      40.009  29.598  62.204  1.00 28.67           O  
ATOM    623  CB  ARG A  91      37.596  28.180  60.432  1.00 28.08           C  
ATOM    624  CG  ARG A  91      36.541  28.156  59.321  1.00 30.00           C  
ATOM    625  CD  ARG A  91      35.208  27.975  59.962  1.00 34.72           C  
ATOM    626  NE  ARG A  91      34.234  28.904  59.459  1.00 38.14           N  
ATOM    627  CZ  ARG A  91      33.009  29.032  59.954  1.00 39.53           C  
ATOM    628  NH1 ARG A  91      32.619  28.295  60.995  1.00 36.91           N  
ATOM    629  NH2 ARG A  91      32.180  29.917  59.413  1.00 39.24           N  
ATOM    630  N   GLY A  92      38.049  29.323  63.348  1.00 27.99           N  
ATOM    631  CA  GLY A  92      38.650  29.066  64.645  1.00 28.43           C  
ATOM    632  C   GLY A  92      39.499  30.216  65.133  1.00 29.25           C  
ATOM    633  O   GLY A  92      39.098  31.368  64.991  1.00 30.25           O  
ATOM    634  N   VAL A  93      40.665  29.925  65.712  1.00 29.52           N  
ATOM    635  CA  VAL A  93      41.487  30.991  66.299  1.00 30.57           C  
ATOM    636  C   VAL A  93      41.836  32.092  65.297  1.00 31.85           C  
ATOM    637  O   VAL A  93      41.748  33.275  65.614  1.00 32.49           O  
ATOM    638  CB  VAL A  93      42.770  30.459  67.002  1.00 30.27           C  
ATOM    639  CG1 VAL A  93      43.722  31.596  67.268  1.00 28.62           C  
ATOM    640  CG2 VAL A  93      42.401  29.745  68.330  1.00 28.55           C  
ATOM    641  N   GLU A  94      42.184  31.692  64.076  1.00 33.01           N  
ATOM    642  CA  GLU A  94      42.608  32.633  63.026  1.00 33.93           C  
ATOM    643  C   GLU A  94      41.522  33.625  62.607  1.00 33.26           C  
ATOM    644  O   GLU A  94      41.815  34.659  62.011  1.00 32.95           O  
ATOM    645  CB  GLU A  94      43.157  31.873  61.811  1.00 33.70           C  
ATOM    646  CG  GLU A  94      44.480  31.175  62.141  1.00 36.61           C  
ATOM    647  CD  GLU A  94      44.954  30.291  61.016  1.00 38.86           C  
ATOM    648  OE1 GLU A  94      44.408  30.426  59.895  1.00 41.58           O  
ATOM    649  OE2 GLU A  94      45.849  29.455  61.260  1.00 39.88           O  
ATOM    650  N   ALA A  95      40.284  33.286  62.934  1.00 32.86           N  
ATOM    651  CA  ALA A  95      39.139  34.073  62.557  1.00 32.94           C  
ATOM    652  C   ALA A  95      38.761  35.018  63.685  1.00 32.99           C  
ATOM    653  O   ALA A  95      37.817  35.801  63.543  1.00 33.77           O  
ATOM    654  CB  ALA A  95      37.940  33.154  62.190  1.00 32.42           C  
ATOM    655  N   GLY A  96      39.471  34.925  64.808  1.00 32.83           N  
ATOM    656  CA  GLY A  96      39.267  35.830  65.934  1.00 32.33           C  
ATOM    657  C   GLY A  96      38.639  35.201  67.157  1.00 32.75           C  
ATOM    658  O   GLY A  96      38.251  35.908  68.110  1.00 34.31           O  
ATOM    659  N   ASN A  97      38.498  33.885  67.153  1.00 31.58           N  
ATOM    660  CA  ASN A  97      37.912  33.219  68.293  1.00 30.78           C  
ATOM    661  C   ASN A  97      38.970  32.870  69.287  1.00 30.39           C  
ATOM    662  O   ASN A  97      40.101  32.530  68.914  1.00 31.43           O  
ATOM    663  CB  ASN A  97      37.175  31.947  67.864  1.00 31.00           C  
ATOM    664  CG  ASN A  97      36.079  32.233  66.896  1.00 30.40           C  
ATOM    665  OD1 ASN A  97      35.028  32.752  67.278  1.00 32.03           O  
ATOM    666  ND2 ASN A  97      36.326  31.951  65.621  1.00 26.98           N  
ATOM    667  N   ALA A  98      38.605  32.898  70.556  1.00 29.79           N  
ATOM    668  CA  ALA A  98      39.564  32.575  71.602  1.00 28.99           C  
ATOM    669  C   ALA A  98      39.932  31.094  71.562  1.00 28.85           C  
ATOM    670  O   ALA A  98      41.019  30.723  71.986  1.00 28.93           O  
ATOM    671  CB  ALA A  98      39.016  32.997  72.990  1.00 29.08           C  
ATOM    672  N   TYR A  99      39.035  30.259  71.030  1.00 28.65           N  
ATOM    673  CA  TYR A  99      39.275  28.811  70.910  1.00 28.35           C  
ATOM    674  C   TYR A  99      39.108  28.303  69.491  1.00 27.51           C  
ATOM    675  O   TYR A  99      38.494  28.967  68.662  1.00 28.28           O  
ATOM    676  CB  TYR A  99      38.344  28.027  71.845  1.00 29.73           C  
ATOM    677  CG  TYR A  99      38.710  28.185  73.282  1.00 29.56           C  
ATOM    678  CD1 TYR A  99      39.676  27.362  73.872  1.00 31.79           C  
ATOM    679  CD2 TYR A  99      38.140  29.179  74.039  1.00 30.30           C  
ATOM    680  CE1 TYR A  99      40.038  27.522  75.209  1.00 32.54           C  
ATOM    681  CE2 TYR A  99      38.494  29.364  75.376  1.00 31.67           C  
ATOM    682  CZ  TYR A  99      39.435  28.537  75.958  1.00 32.55           C  
ATOM    683  OH  TYR A  99      39.782  28.731  77.293  1.00 33.80           O  
ATOM    684  N   PRO A 100      39.683  27.130  69.191  1.00 26.68           N  
ATOM    685  CA  PRO A 100      39.457  26.583  67.861  1.00 25.65           C  
ATOM    686  C   PRO A 100      38.010  26.137  67.637  1.00 25.10           C  
ATOM    687  O   PRO A 100      37.307  25.805  68.582  1.00 25.56           O  
ATOM    688  CB  PRO A 100      40.361  25.342  67.825  1.00 24.77           C  
ATOM    689  CG  PRO A 100      41.264  25.461  68.978  1.00 25.86           C  
ATOM    690  CD  PRO A 100      40.587  26.282  70.001  1.00 26.05           C  
ATOM    691  N   GLN A 101      37.583  26.137  66.387  1.00 23.81           N  
ATOM    692  CA  GLN A 101      36.565  25.206  65.955  1.00 23.71           C  
ATOM    693  C   GLN A 101      37.257  23.842  65.832  1.00 22.30           C  
ATOM    694  O   GLN A 101      38.367  23.746  65.335  1.00 22.81           O  
ATOM    695  CB  GLN A 101      35.991  25.652  64.602  1.00 23.57           C  
ATOM    696  CG  GLN A 101      35.182  24.579  63.871  1.00 25.09           C  
ATOM    697  CD  GLN A 101      34.778  25.030  62.498  1.00 24.14           C  
ATOM    698  OE1 GLN A 101      34.672  26.230  62.251  1.00 30.12           O  
ATOM    699  NE2 GLN A 101      34.573  24.102  61.601  1.00 19.14           N  
ATOM    700  N   TYR A 102      36.617  22.789  66.304  1.00 21.91           N  
ATOM    701  CA  TYR A 102      37.194  21.445  66.193  1.00 21.64           C  
ATOM    702  C   TYR A 102      36.311  20.584  65.299  1.00 21.56           C  
ATOM    703  O   TYR A 102      35.095  20.497  65.490  1.00 20.93           O  
ATOM    704  CB  TYR A 102      37.413  20.787  67.575  1.00 21.28           C  
ATOM    705  CG  TYR A 102      38.745  21.123  68.236  1.00 21.85           C  
ATOM    706  CD1 TYR A 102      39.939  21.004  67.540  1.00 24.17           C  
ATOM    707  CD2 TYR A 102      38.811  21.571  69.570  1.00 23.57           C  
ATOM    708  CE1 TYR A 102      41.186  21.315  68.144  1.00 24.66           C  
ATOM    709  CE2 TYR A 102      40.051  21.905  70.181  1.00 22.29           C  
ATOM    710  CZ  TYR A 102      41.227  21.770  69.459  1.00 23.25           C  
ATOM    711  OH  TYR A 102      42.451  22.069  70.026  1.00 21.97           O  
ATOM    712  N   SER A 103      36.929  19.971  64.300  1.00 22.02           N  
ATOM    713  CA  SER A 103      36.244  19.014  63.455  1.00 22.78           C  
ATOM    714  C   SER A 103      36.678  17.652  63.940  1.00 23.24           C  
ATOM    715  O   SER A 103      37.878  17.339  63.993  1.00 24.35           O  
ATOM    716  CB  SER A 103      36.575  19.254  61.981  1.00 22.81           C  
ATOM    717  OG  SER A 103      36.238  20.600  61.601  1.00 24.34           O  
ATOM    718  N   ILE A 104      35.709  16.831  64.320  1.00 23.27           N  
ATOM    719  CA  ILE A 104      36.041  15.636  65.085  1.00 23.08           C  
ATOM    720  C   ILE A 104      35.130  14.482  64.706  1.00 23.19           C  
ATOM    721  O   ILE A 104      33.994  14.687  64.316  1.00 22.90           O  
ATOM    722  CB  ILE A 104      35.948  15.935  66.623  1.00 22.98           C  
ATOM    723  CG1 ILE A 104      36.426  14.740  67.476  1.00 23.66           C  
ATOM    724  CG2 ILE A 104      34.528  16.380  67.002  1.00 22.16           C  
ATOM    725  CD1 ILE A 104      36.747  15.103  68.901  1.00 22.28           C  
ATOM    726  N   HIS A 105      35.638  13.267  64.835  1.00 24.00           N  
ATOM    727  CA  HIS A 105      34.815  12.085  64.692  1.00 25.26           C  
ATOM    728  C   HIS A 105      33.796  12.007  65.861  1.00 24.99           C  
ATOM    729  O   HIS A 105      34.167  12.103  67.024  1.00 25.51           O  
ATOM    730  CB  HIS A 105      35.735  10.874  64.657  1.00 25.51           C  
ATOM    731  CG  HIS A 105      35.032   9.613  64.268  1.00 28.87           C  
ATOM    732  ND1 HIS A 105      34.213   8.919  65.135  1.00 29.13           N  
ATOM    733  CD2 HIS A 105      35.000   8.938  63.098  1.00 29.89           C  
ATOM    734  CE1 HIS A 105      33.704   7.876  64.513  1.00 30.73           C  
ATOM    735  NE2 HIS A 105      34.177   7.856  63.281  1.00 32.26           N  
ATOM    736  N   ARG A 106      32.518  11.872  65.570  1.00 24.91           N  
ATOM    737  CA  ARG A 106      31.520  11.884  66.629  1.00 25.44           C  
ATOM    738  C   ARG A 106      31.776  10.867  67.747  1.00 26.04           C  
ATOM    739  O   ARG A 106      31.636  11.191  68.927  1.00 26.51           O  
ATOM    740  CB  ARG A 106      30.120  11.641  66.061  1.00 25.87           C  
ATOM    741  CG  ARG A 106      29.015  11.907  67.085  1.00 27.13           C  
ATOM    742  CD  ARG A 106      27.845  11.032  66.852  1.00 24.43           C  
ATOM    743  NE  ARG A 106      26.969  10.956  68.004  1.00 21.65           N  
ATOM    744  CZ  ARG A 106      26.888   9.909  68.833  1.00 23.87           C  
ATOM    745  NH1 ARG A 106      27.674   8.835  68.663  1.00 22.34           N  
ATOM    746  NH2 ARG A 106      26.006   9.928  69.842  1.00 23.09           N  
ATOM    747  N   GLY A 107      32.130   9.641  67.376  1.00 26.19           N  
ATOM    748  CA  GLY A 107      32.341   8.583  68.334  1.00 26.82           C  
ATOM    749  C   GLY A 107      33.618   8.737  69.127  1.00 28.27           C  
ATOM    750  O   GLY A 107      33.669   8.412  70.323  1.00 28.32           O  
ATOM    751  N   GLU A 108      34.666   9.231  68.481  1.00 28.66           N  
ATOM    752  CA  GLU A 108      35.791   9.711  69.252  1.00 29.65           C  
ATOM    753  C   GLU A 108      35.389  10.801  70.291  1.00 29.50           C  
ATOM    754  O   GLU A 108      35.773  10.673  71.457  1.00 30.64           O  
ATOM    755  CB  GLU A 108      36.932  10.127  68.348  1.00 29.75           C  
ATOM    756  CG  GLU A 108      38.264   9.789  68.984  1.00 36.40           C  
ATOM    757  CD  GLU A 108      39.325   9.281  67.998  1.00 41.89           C  
ATOM    758  OE1 GLU A 108      39.052   9.278  66.774  1.00 44.34           O  
ATOM    759  OE2 GLU A 108      40.440   8.907  68.462  1.00 43.06           O  
ATOM    760  N   LEU A 109      34.586  11.815  69.917  1.00 28.42           N  
ATOM    761  CA  LEU A 109      34.065  12.782  70.909  1.00 28.38           C  
ATOM    762  C   LEU A 109      33.227  12.125  72.015  1.00 28.99           C  
ATOM    763  O   LEU A 109      33.377  12.414  73.197  1.00 28.03           O  
ATOM    764  CB  LEU A 109      33.266  13.944  70.275  1.00 28.07           C  
ATOM    765  CG  LEU A 109      32.631  14.933  71.291  1.00 27.57           C  
ATOM    766  CD1 LEU A 109      33.688  15.669  72.138  1.00 22.96           C  
ATOM    767  CD2 LEU A 109      31.700  15.950  70.653  1.00 27.52           C  
ATOM    768  N   GLN A 110      32.338  11.233  71.632  1.00 30.31           N  
ATOM    769  CA  GLN A 110      31.607  10.481  72.637  1.00 32.26           C  
ATOM    770  C   GLN A 110      32.452   9.680  73.660  1.00 33.13           C  
ATOM    771  O   GLN A 110      32.079   9.636  74.842  1.00 33.52           O  
ATOM    772  CB  GLN A 110      30.612   9.574  71.978  1.00 32.28           C  
ATOM    773  CG  GLN A 110      29.764   8.876  72.978  1.00 34.46           C  
ATOM    774  CD  GLN A 110      28.638   8.210  72.325  1.00 36.83           C  
ATOM    775  OE1 GLN A 110      28.792   7.610  71.242  1.00 37.93           O  
ATOM    776  NE2 GLN A 110      27.470   8.325  72.933  1.00 35.28           N  
HETATM  777  N   MSE A 111      33.554   9.065  73.205  1.00 33.95           N  
HETATM  778  CA  MSE A 111      34.494   8.335  74.063  1.00 35.23           C  
HETATM  779  C   MSE A 111      35.226   9.249  75.045  1.00 35.50           C  
HETATM  780  O   MSE A 111      35.396   8.901  76.221  1.00 35.72           O  
HETATM  781  CB  MSE A 111      35.526   7.567  73.234  1.00 36.25           C  
HETATM  782  CG  MSE A 111      35.006   6.333  72.463  1.00 39.48           C  
HETATM  783 SE   MSE A 111      33.562   5.216  73.281  0.50 49.69          SE  
HETATM  784  CE  MSE A 111      31.995   5.963  72.414  1.00 41.10           C  
ATOM    785  N   ILE A 112      35.663  10.410  74.562  1.00 35.25           N  
ATOM    786  CA  ILE A 112      36.253  11.438  75.416  1.00 35.06           C  
ATOM    787  C   ILE A 112      35.269  11.860  76.511  1.00 34.84           C  
ATOM    788  O   ILE A 112      35.632  11.970  77.695  1.00 34.82           O  
ATOM    789  CB  ILE A 112      36.666  12.688  74.605  1.00 35.33           C  
ATOM    790  CG1 ILE A 112      37.824  12.360  73.667  1.00 34.62           C  
ATOM    791  CG2 ILE A 112      37.068  13.825  75.544  1.00 36.20           C  
ATOM    792  CD1 ILE A 112      38.069  13.428  72.640  1.00 35.58           C  
ATOM    793  N   LEU A 113      34.024  12.079  76.111  1.00 34.04           N  
ATOM    794  CA  LEU A 113      32.980  12.426  77.053  1.00 33.54           C  
ATOM    795  C   LEU A 113      32.683  11.287  78.031  1.00 33.55           C  
ATOM    796  O   LEU A 113      32.519  11.504  79.226  1.00 33.39           O  
ATOM    797  CB  LEU A 113      31.724  12.803  76.290  1.00 33.31           C  
ATOM    798  CG  LEU A 113      31.390  14.256  75.967  1.00 32.89           C  
ATOM    799  CD1 LEU A 113      32.592  15.168  76.053  1.00 35.40           C  
ATOM    800  CD2 LEU A 113      30.731  14.315  74.586  1.00 30.19           C  
ATOM    801  N   LEU A 114      32.628  10.068  77.516  1.00 33.65           N  
ATOM    802  CA  LEU A 114      32.307   8.922  78.338  1.00 33.72           C  
ATOM    803  C   LEU A 114      33.391   8.670  79.406  1.00 33.72           C  
ATOM    804  O   LEU A 114      33.064   8.458  80.588  1.00 33.82           O  
ATOM    805  CB  LEU A 114      32.081   7.689  77.464  1.00 33.59           C  
ATOM    806  CG  LEU A 114      31.651   6.462  78.264  1.00 34.33           C  
ATOM    807  CD1 LEU A 114      30.359   6.741  79.044  1.00 35.28           C  
ATOM    808  CD2 LEU A 114      31.522   5.230  77.379  1.00 33.86           C  
ATOM    809  N   ALA A 115      34.659   8.733  78.990  1.00 32.80           N  
ATOM    810  CA  ALA A 115      35.791   8.627  79.910  1.00 32.46           C  
ATOM    811  C   ALA A 115      35.784   9.718  80.980  1.00 32.47           C  
ATOM    812  O   ALA A 115      35.947   9.415  82.151  1.00 33.03           O  
ATOM    813  CB  ALA A 115      37.126   8.621  79.157  1.00 32.22           C  
ATOM    814  N   ALA A 116      35.598  10.976  80.591  1.00 32.19           N  
ATOM    815  CA  ALA A 116      35.482  12.062  81.567  1.00 32.25           C  
ATOM    816  C   ALA A 116      34.417  11.797  82.647  1.00 32.96           C  
ATOM    817  O   ALA A 116      34.742  11.824  83.830  1.00 32.39           O  
ATOM    818  CB  ALA A 116      35.242  13.402  80.879  1.00 31.18           C  
ATOM    819  N   VAL A 117      33.170  11.533  82.231  1.00 34.33           N  
ATOM    820  CA  VAL A 117      32.074  11.156  83.139  1.00 35.77           C  
ATOM    821  C   VAL A 117      32.415   9.937  84.033  1.00 37.48           C  
ATOM    822  O   VAL A 117      32.232   9.981  85.266  1.00 37.18           O  
ATOM    823  CB  VAL A 117      30.751  10.868  82.385  1.00 35.56           C  
ATOM    824  CG1 VAL A 117      29.705  10.266  83.339  1.00 35.22           C  
ATOM    825  CG2 VAL A 117      30.187  12.142  81.759  1.00 35.31           C  
ATOM    826  N   ARG A 118      32.899   8.858  83.412  1.00 38.78           N  
ATOM    827  CA  ARG A 118      33.323   7.683  84.182  1.00 40.51           C  
ATOM    828  C   ARG A 118      34.384   7.966  85.246  1.00 41.31           C  
ATOM    829  O   ARG A 118      34.217   7.562  86.396  1.00 41.43           O  
ATOM    830  CB  ARG A 118      33.732   6.517  83.280  1.00 40.25           C  
ATOM    831  CG  ARG A 118      32.574   5.587  83.063  1.00 40.85           C  
ATOM    832  CD  ARG A 118      32.879   4.455  82.105  1.00 42.67           C  
ATOM    833  NE  ARG A 118      31.606   3.910  81.634  1.00 43.67           N  
ATOM    834  CZ  ARG A 118      31.462   3.113  80.584  1.00 43.27           C  
ATOM    835  NH1 ARG A 118      32.523   2.732  79.882  1.00 43.53           N  
ATOM    836  NH2 ARG A 118      30.246   2.702  80.236  1.00 44.20           N  
ATOM    837  N   GLU A 119      35.439   8.684  84.864  1.00 42.08           N  
ATOM    838  CA  GLU A 119      36.499   9.094  85.797  1.00 43.24           C  
ATOM    839  C   GLU A 119      36.044   9.994  86.932  1.00 42.97           C  
ATOM    840  O   GLU A 119      36.507   9.822  88.066  1.00 43.55           O  
ATOM    841  CB  GLU A 119      37.644   9.797  85.057  1.00 43.38           C  
ATOM    842  CG  GLU A 119      38.800   8.876  84.698  1.00 46.96           C  
ATOM    843  CD  GLU A 119      39.474   9.286  83.407  1.00 52.96           C  
ATOM    844  OE1 GLU A 119      39.490  10.515  83.112  1.00 54.10           O  
ATOM    845  OE2 GLU A 119      39.972   8.376  82.683  1.00 54.54           O  
ATOM    846  N   ARG A 120      35.172  10.957  86.616  1.00 42.51           N  
ATOM    847  CA  ARG A 120      34.771  12.019  87.545  1.00 41.98           C  
ATOM    848  C   ARG A 120      33.561  11.724  88.425  1.00 41.93           C  
ATOM    849  O   ARG A 120      33.395  12.355  89.470  1.00 41.64           O  
ATOM    850  CB  ARG A 120      34.495  13.317  86.804  1.00 42.11           C  
ATOM    851  CG  ARG A 120      35.697  13.934  86.167  1.00 41.90           C  
ATOM    852  CD  ARG A 120      35.274  15.122  85.355  1.00 41.20           C  
ATOM    853  NE  ARG A 120      36.200  15.327  84.245  1.00 41.89           N  
ATOM    854  CZ  ARG A 120      36.276  16.439  83.515  1.00 41.83           C  
ATOM    855  NH1 ARG A 120      35.466  17.473  83.756  1.00 39.45           N  
ATOM    856  NH2 ARG A 120      37.171  16.511  82.534  1.00 42.41           N  
ATOM    857  N   LEU A 121      32.695  10.810  88.016  1.00 41.84           N  
ATOM    858  CA  LEU A 121      31.635  10.434  88.923  1.00 42.40           C  
ATOM    859  C   LEU A 121      31.448   8.943  89.122  1.00 42.47           C  
ATOM    860  O   LEU A 121      30.455   8.498  89.690  1.00 42.68           O  
ATOM    861  CB  LEU A 121      30.323  11.206  88.660  1.00 42.93           C  
ATOM    862  CG  LEU A 121      29.703  11.613  87.314  1.00 44.01           C  
ATOM    863  CD1 LEU A 121      28.379  12.274  87.598  1.00 45.33           C  
ATOM    864  CD2 LEU A 121      30.544  12.581  86.523  1.00 45.82           C  
ATOM    865  N   GLY A 122      32.438   8.171  88.710  1.00 42.69           N  
ATOM    866  CA  GLY A 122      32.415   6.736  88.926  1.00 43.56           C  
ATOM    867  C   GLY A 122      31.683   5.992  87.827  1.00 44.13           C  
ATOM    868  O   GLY A 122      30.703   6.501  87.279  1.00 43.74           O  
ATOM    869  N   GLN A 123      32.167   4.782  87.539  1.00 44.77           N  
ATOM    870  CA  GLN A 123      31.719   3.921  86.436  1.00 46.15           C  
ATOM    871  C   GLN A 123      30.212   3.676  86.510  1.00 46.31           C  
ATOM    872  O   GLN A 123      29.540   3.412  85.503  1.00 46.22           O  
ATOM    873  CB  GLN A 123      32.456   2.578  86.552  1.00 46.86           C  
ATOM    874  CG  GLN A 123      32.563   1.732  85.279  1.00 50.40           C  
ATOM    875  CD  GLN A 123      33.861   1.961  84.505  1.00 53.13           C  
ATOM    876  OE1 GLN A 123      34.726   2.741  84.923  1.00 55.44           O  
ATOM    877  NE2 GLN A 123      33.994   1.288  83.364  1.00 53.54           N  
ATOM    878  N   GLN A 124      29.703   3.817  87.730  1.00 46.53           N  
ATOM    879  CA  GLN A 124      28.342   3.507  88.100  1.00 47.10           C  
ATOM    880  C   GLN A 124      27.360   4.540  87.557  1.00 46.24           C  
ATOM    881  O   GLN A 124      26.163   4.244  87.420  1.00 45.39           O  
ATOM    882  CB  GLN A 124      28.250   3.469  89.631  1.00 47.41           C  
ATOM    883  CG  GLN A 124      29.466   2.793  90.314  1.00 49.60           C  
ATOM    884  CD  GLN A 124      29.259   2.560  91.812  1.00 49.55           C  
ATOM    885  OE1 GLN A 124      29.403   3.489  92.634  1.00 51.20           O  
ATOM    886  NE2 GLN A 124      28.926   1.305  92.177  1.00 51.19           N  
ATOM    887  N   ALA A 125      27.868   5.748  87.272  1.00 45.63           N  
ATOM    888  CA  ALA A 125      27.049   6.863  86.755  1.00 45.59           C  
ATOM    889  C   ALA A 125      26.312   6.581  85.421  1.00 45.13           C  
ATOM    890  O   ALA A 125      25.198   7.070  85.213  1.00 45.03           O  
ATOM    891  CB  ALA A 125      27.876   8.144  86.655  1.00 45.26           C  
ATOM    892  N   VAL A 126      26.927   5.779  84.551  1.00 44.88           N  
ATOM    893  CA  VAL A 126      26.386   5.492  83.227  1.00 44.56           C  
ATOM    894  C   VAL A 126      25.759   4.106  83.196  1.00 44.69           C  
ATOM    895  O   VAL A 126      26.458   3.099  83.060  1.00 44.20           O  
ATOM    896  CB  VAL A 126      27.475   5.593  82.126  1.00 44.53           C  
ATOM    897  CG1 VAL A 126      26.843   5.570  80.726  1.00 44.62           C  
ATOM    898  CG2 VAL A 126      28.341   6.847  82.305  1.00 45.21           C  
ATOM    899  N   ARG A 127      24.433   4.055  83.329  1.00 45.37           N  
ATOM    900  CA  ARG A 127      23.705   2.770  83.273  1.00 45.55           C  
ATOM    901  C   ARG A 127      23.323   2.435  81.847  1.00 44.93           C  
ATOM    902  O   ARG A 127      22.352   2.954  81.269  1.00 44.72           O  
ATOM    903  CB  ARG A 127      22.514   2.713  84.231  1.00 45.80           C  
ATOM    904  CG  ARG A 127      22.966   2.768  85.690  1.00 49.64           C  
ATOM    905  CD  ARG A 127      22.096   1.876  86.569  1.00 56.22           C  
ATOM    906  NE  ARG A 127      21.779   2.523  87.850  1.00 59.56           N  
ATOM    907  CZ  ARG A 127      20.641   2.350  88.529  1.00 59.99           C  
ATOM    908  NH1 ARG A 127      19.689   1.545  88.061  1.00 60.33           N  
ATOM    909  NH2 ARG A 127      20.457   2.987  89.679  1.00 60.15           N  
ATOM    910  N   THR A 128      24.140   1.563  81.289  1.00 43.98           N  
ATOM    911  CA  THR A 128      24.037   1.162  79.916  1.00 43.45           C  
ATOM    912  C   THR A 128      23.001   0.025  79.855  1.00 42.57           C  
ATOM    913  O   THR A 128      22.787  -0.646  80.844  1.00 42.62           O  
ATOM    914  CB  THR A 128      25.464   0.783  79.432  1.00 43.68           C  
ATOM    915  OG1 THR A 128      25.649   1.151  78.058  1.00 44.36           O  
ATOM    916  CG2 THR A 128      25.810  -0.705  79.708  1.00 43.90           C  
ATOM    917  N   GLY A 129      22.336  -0.154  78.719  1.00 41.98           N  
ATOM    918  CA  GLY A 129      21.290  -1.168  78.557  1.00 40.70           C  
ATOM    919  C   GLY A 129      19.955  -0.819  79.198  1.00 40.54           C  
ATOM    920  O   GLY A 129      19.125  -1.697  79.435  1.00 40.65           O  
ATOM    921  N   LEU A 130      19.733   0.462  79.478  1.00 39.86           N  
ATOM    922  CA  LEU A 130      18.531   0.887  80.184  1.00 39.02           C  
ATOM    923  C   LEU A 130      17.827   2.022  79.475  1.00 38.93           C  
ATOM    924  O   LEU A 130      18.171   3.197  79.649  1.00 38.78           O  
ATOM    925  CB  LEU A 130      18.848   1.290  81.631  1.00 38.75           C  
ATOM    926  CG  LEU A 130      18.464   0.397  82.823  1.00 38.52           C  
ATOM    927  CD1 LEU A 130      18.843   1.074  84.130  1.00 37.81           C  
ATOM    928  CD2 LEU A 130      16.998   0.094  82.856  1.00 36.35           C  
ATOM    929  N   GLY A 131      16.816   1.672  78.691  1.00 38.98           N  
ATOM    930  CA  GLY A 131      16.019   2.677  77.997  1.00 38.75           C  
ATOM    931  C   GLY A 131      14.832   3.110  78.816  1.00 38.63           C  
ATOM    932  O   GLY A 131      14.134   2.274  79.366  1.00 39.17           O  
ATOM    933  N   VAL A 132      14.629   4.422  78.911  1.00 38.28           N  
ATOM    934  CA  VAL A 132      13.449   5.019  79.502  1.00 37.72           C  
ATOM    935  C   VAL A 132      12.236   4.682  78.634  1.00 38.60           C  
ATOM    936  O   VAL A 132      12.249   4.925  77.425  1.00 38.49           O  
ATOM    937  CB  VAL A 132      13.629   6.559  79.621  1.00 37.62           C  
ATOM    938  CG1 VAL A 132      12.311   7.275  79.803  1.00 35.40           C  
ATOM    939  CG2 VAL A 132      14.599   6.910  80.753  1.00 37.52           C  
ATOM    940  N   GLU A 133      11.195   4.128  79.253  1.00 39.25           N  
ATOM    941  CA  GLU A 133       9.947   3.831  78.557  1.00 40.84           C  
ATOM    942  C   GLU A 133       8.725   4.541  79.142  1.00 40.72           C  
ATOM    943  O   GLU A 133       7.909   5.069  78.395  1.00 40.63           O  
ATOM    944  CB  GLU A 133       9.708   2.324  78.499  1.00 40.67           C  
ATOM    945  CG  GLU A 133      10.660   1.571  77.537  1.00 43.21           C  
ATOM    946  CD  GLU A 133      10.569   0.039  77.647  1.00 44.20           C  
ATOM    947  OE1 GLU A 133       9.632  -0.495  78.302  1.00 48.06           O  
ATOM    948  OE2 GLU A 133      11.453  -0.643  77.063  1.00 49.82           O  
ATOM    949  N   ARG A 134       8.579   4.539  80.465  1.00 40.83           N  
ATOM    950  CA  ARG A 134       7.433   5.190  81.098  1.00 41.88           C  
ATOM    951  C   ARG A 134       7.922   6.328  81.989  1.00 40.40           C  
ATOM    952  O   ARG A 134       8.955   6.201  82.632  1.00 39.69           O  
ATOM    953  CB  ARG A 134       6.632   4.197  81.965  1.00 41.95           C  
ATOM    954  CG  ARG A 134       5.980   2.988  81.273  1.00 44.24           C  
ATOM    955  CD  ARG A 134       5.579   1.965  82.384  1.00 45.39           C  
ATOM    956  NE  ARG A 134       4.649   0.907  81.963  1.00 52.60           N  
ATOM    957  CZ  ARG A 134       3.315   1.014  81.967  1.00 55.90           C  
ATOM    958  NH1 ARG A 134       2.717   2.147  82.343  1.00 56.73           N  
ATOM    959  NH2 ARG A 134       2.569  -0.017  81.579  1.00 57.75           N  
ATOM    960  N   ILE A 135       7.156   7.409  82.050  1.00 40.02           N  
ATOM    961  CA  ILE A 135       7.498   8.581  82.853  1.00 40.59           C  
ATOM    962  C   ILE A 135       6.239   9.154  83.525  1.00 41.52           C  
ATOM    963  O   ILE A 135       5.172   9.139  82.939  1.00 40.74           O  
ATOM    964  CB  ILE A 135       8.163   9.686  81.976  1.00 40.61           C  
ATOM    965  CG1 ILE A 135       9.406   9.165  81.217  1.00 41.04           C  
ATOM    966  CG2 ILE A 135       8.558  10.847  82.796  1.00 40.45           C  
ATOM    967  CD1 ILE A 135       9.929  10.112  80.098  1.00 39.88           C  
ATOM    968  N   GLU A 136       6.383   9.662  84.755  1.00 43.52           N  
ATOM    969  CA  GLU A 136       5.293  10.296  85.528  1.00 45.61           C  
ATOM    970  C   GLU A 136       5.858  11.282  86.584  1.00 45.84           C  
ATOM    971  O   GLU A 136       6.816  10.954  87.289  1.00 46.39           O  
ATOM    972  CB  GLU A 136       4.444   9.202  86.193  1.00 44.96           C  
ATOM    973  CG  GLU A 136       3.285   9.675  87.073  1.00 47.53           C  
ATOM    974  CD  GLU A 136       2.599   8.529  87.903  1.00 48.31           C  
ATOM    975  OE1 GLU A 136       2.898   7.317  87.706  1.00 50.40           O  
ATOM    976  OE2 GLU A 136       1.745   8.858  88.767  1.00 51.70           O  
ATOM    977  N   GLU A 137       5.285  12.479  86.705  1.00 46.27           N  
ATOM    978  CA  GLU A 137       5.695  13.371  87.797  1.00 46.80           C  
ATOM    979  C   GLU A 137       4.683  13.401  88.949  1.00 47.74           C  
ATOM    980  O   GLU A 137       3.554  13.880  88.789  1.00 47.34           O  
ATOM    981  CB  GLU A 137       5.996  14.806  87.342  1.00 46.42           C  
ATOM    982  CG  GLU A 137       6.613  15.623  88.492  1.00 45.31           C  
ATOM    983  CD  GLU A 137       6.798  17.098  88.191  1.00 46.32           C  
ATOM    984  OE1 GLU A 137       7.205  17.449  87.055  1.00 45.86           O  
ATOM    985  OE2 GLU A 137       6.553  17.916  89.111  1.00 44.41           O  
ATOM    986  N   ARG A 138       5.121  12.936  90.117  1.00 48.43           N  
ATOM    987  CA  ARG A 138       4.208  12.659  91.228  1.00 49.70           C  
ATOM    988  C   ARG A 138       4.801  13.188  92.539  1.00 49.09           C  
ATOM    989  O   ARG A 138       5.788  12.652  93.036  1.00 49.11           O  
ATOM    990  CB  ARG A 138       3.968  11.141  91.288  1.00 49.36           C  
ATOM    991  CG  ARG A 138       2.592  10.681  91.706  1.00 51.13           C  
ATOM    992  CD  ARG A 138       2.575   9.143  91.851  1.00 52.22           C  
ATOM    993  NE  ARG A 138       1.441   8.643  92.642  1.00 58.32           N  
ATOM    994  CZ  ARG A 138       1.523   8.121  93.876  1.00 59.57           C  
ATOM    995  NH1 ARG A 138       2.692   8.006  94.508  1.00 58.78           N  
ATOM    996  NH2 ARG A 138       0.416   7.707  94.488  1.00 60.79           N  
ATOM    997  N   ASP A 139       4.221  14.263  93.071  1.00 49.45           N  
ATOM    998  CA  ASP A 139       4.648  14.858  94.358  1.00 50.01           C  
ATOM    999  C   ASP A 139       6.135  15.253  94.449  1.00 49.11           C  
ATOM   1000  O   ASP A 139       6.852  14.761  95.321  1.00 49.41           O  
ATOM   1001  CB  ASP A 139       4.291  13.931  95.547  1.00 50.55           C  
ATOM   1002  CG  ASP A 139       2.802  13.618  95.627  1.00 53.62           C  
ATOM   1003  OD1 ASP A 139       1.962  14.503  95.325  1.00 56.33           O  
ATOM   1004  OD2 ASP A 139       2.464  12.474  95.996  1.00 57.28           O  
ATOM   1005  N   GLY A 140       6.597  16.138  93.568  1.00 48.14           N  
ATOM   1006  CA  GLY A 140       7.990  16.628  93.636  1.00 46.48           C  
ATOM   1007  C   GLY A 140       9.039  15.600  93.247  1.00 45.16           C  
ATOM   1008  O   GLY A 140      10.219  15.749  93.555  1.00 45.07           O  
ATOM   1009  N   ARG A 141       8.602  14.568  92.532  1.00 44.23           N  
ATOM   1010  CA  ARG A 141       9.426  13.413  92.250  1.00 43.35           C  
ATOM   1011  C   ARG A 141       9.113  12.845  90.861  1.00 42.68           C  
ATOM   1012  O   ARG A 141       7.944  12.626  90.523  1.00 42.55           O  
ATOM   1013  CB  ARG A 141       9.192  12.364  93.342  1.00 43.56           C  
ATOM   1014  CG  ARG A 141      10.099  11.172  93.254  1.00 44.22           C  
ATOM   1015  CD  ARG A 141      10.847  10.967  94.573  1.00 45.25           C  
ATOM   1016  NE  ARG A 141      11.966  10.047  94.386  1.00 44.08           N  
ATOM   1017  CZ  ARG A 141      13.230  10.425  94.216  1.00 44.11           C  
ATOM   1018  NH1 ARG A 141      13.559  11.716  94.237  1.00 43.22           N  
ATOM   1019  NH2 ARG A 141      14.176   9.500  94.044  1.00 43.51           N  
ATOM   1020  N   VAL A 142      10.155  12.624  90.057  1.00 41.60           N  
ATOM   1021  CA  VAL A 142       9.977  11.966  88.760  1.00 40.73           C  
ATOM   1022  C   VAL A 142      10.253  10.464  88.860  1.00 40.50           C  
ATOM   1023  O   VAL A 142      11.291  10.034  89.375  1.00 40.37           O  
ATOM   1024  CB  VAL A 142      10.812  12.603  87.586  1.00 40.84           C  
ATOM   1025  CG1 VAL A 142      10.444  11.930  86.252  1.00 39.64           C  
ATOM   1026  CG2 VAL A 142      10.615  14.115  87.502  1.00 38.74           C  
ATOM   1027  N   LEU A 143       9.299   9.698  88.338  1.00 40.45           N  
ATOM   1028  CA  LEU A 143       9.216   8.256  88.476  1.00 40.36           C  
ATOM   1029  C   LEU A 143       9.295   7.661  87.094  1.00 40.36           C  
ATOM   1030  O   LEU A 143       8.481   7.996  86.210  1.00 40.69           O  
ATOM   1031  CB  LEU A 143       7.879   7.860  89.120  1.00 40.80           C  
ATOM   1032  CG  LEU A 143       7.456   8.453  90.487  1.00 41.62           C  
ATOM   1033  CD1 LEU A 143       5.993   8.148  90.749  1.00 43.95           C  
ATOM   1034  CD2 LEU A 143       8.293   7.928  91.643  1.00 42.77           C  
ATOM   1035  N   ILE A 144      10.262   6.766  86.918  1.00 39.60           N  
ATOM   1036  CA  ILE A 144      10.613   6.247  85.611  1.00 39.71           C  
ATOM   1037  C   ILE A 144      10.472   4.730  85.511  1.00 40.26           C  
ATOM   1038  O   ILE A 144      10.958   3.982  86.365  1.00 40.58           O  
ATOM   1039  CB  ILE A 144      12.048   6.720  85.188  1.00 39.24           C  
ATOM   1040  CG1 ILE A 144      11.960   8.116  84.624  1.00 38.60           C  
ATOM   1041  CG2 ILE A 144      12.621   5.870  84.100  1.00 38.10           C  
ATOM   1042  CD1 ILE A 144      12.949   9.030  85.183  1.00 40.42           C  
ATOM   1043  N   GLY A 145       9.782   4.297  84.462  1.00 40.41           N  
ATOM   1044  CA  GLY A 145       9.812   2.919  84.045  1.00 40.71           C  
ATOM   1045  C   GLY A 145      10.908   2.769  83.011  1.00 41.31           C  
ATOM   1046  O   GLY A 145      10.976   3.541  82.051  1.00 41.41           O  
ATOM   1047  N   ALA A 146      11.774   1.786  83.217  1.00 41.68           N  
ATOM   1048  CA  ALA A 146      12.806   1.463  82.264  1.00 42.82           C  
ATOM   1049  C   ALA A 146      12.781  -0.033  82.007  1.00 43.79           C  
ATOM   1050  O   ALA A 146      12.155  -0.786  82.742  1.00 43.40           O  
ATOM   1051  CB  ALA A 146      14.161   1.903  82.800  1.00 42.54           C  
ATOM   1052  N   ARG A 147      13.454  -0.459  80.950  1.00 45.87           N  
ATOM   1053  CA  ARG A 147      13.516  -1.871  80.588  1.00 47.87           C  
ATOM   1054  C   ARG A 147      14.964  -2.165  80.320  1.00 48.96           C  
ATOM   1055  O   ARG A 147      15.636  -1.359  79.673  1.00 49.34           O  
ATOM   1056  CB  ARG A 147      12.688  -2.130  79.337  1.00 47.92           C  
ATOM   1057  CG  ARG A 147      12.664  -3.580  78.891  1.00 49.91           C  
ATOM   1058  CD  ARG A 147      11.374  -3.953  78.133  1.00 53.78           C  
ATOM   1059  NE  ARG A 147      10.140  -3.385  78.712  1.00 55.93           N  
ATOM   1060  CZ  ARG A 147       9.444  -3.902  79.724  1.00 55.79           C  
ATOM   1061  NH1 ARG A 147       9.834  -5.019  80.333  1.00 56.09           N  
ATOM   1062  NH2 ARG A 147       8.349  -3.283  80.136  1.00 55.70           N  
ATOM   1063  N   ASP A 148      15.459  -3.293  80.816  1.00 50.29           N  
ATOM   1064  CA  ASP A 148      16.883  -3.563  80.704  1.00 51.98           C  
ATOM   1065  C   ASP A 148      17.245  -4.583  79.620  1.00 52.94           C  
ATOM   1066  O   ASP A 148      16.410  -4.922  78.776  1.00 52.71           O  
ATOM   1067  CB  ASP A 148      17.512  -3.881  82.086  1.00 52.43           C  
ATOM   1068  CG  ASP A 148      17.195  -5.298  82.596  1.00 53.07           C  
ATOM   1069  OD1 ASP A 148      17.867  -5.749  83.548  1.00 53.86           O  
ATOM   1070  OD2 ASP A 148      16.300  -5.963  82.052  1.00 53.43           O  
ATOM   1071  N   GLY A 149      18.507  -5.032  79.645  1.00 54.68           N  
ATOM   1072  CA  GLY A 149      19.059  -6.014  78.692  1.00 56.14           C  
ATOM   1073  C   GLY A 149      18.549  -7.408  79.005  1.00 57.13           C  
ATOM   1074  O   GLY A 149      18.692  -7.905  80.140  1.00 57.86           O  
ATOM   1075  N   HIS A 150      17.957  -8.045  78.001  1.00 57.42           N  
ATOM   1076  CA  HIS A 150      17.167  -9.268  78.220  1.00 57.77           C  
ATOM   1077  C   HIS A 150      15.851  -8.987  79.005  1.00 57.05           C  
ATOM   1078  O   HIS A 150      15.372  -9.826  79.771  1.00 57.15           O  
ATOM   1079  CB  HIS A 150      18.018 -10.444  78.796  1.00 58.25           C  
ATOM   1080  CG  HIS A 150      18.218 -11.592  77.835  1.00 59.54           C  
ATOM   1081  ND1 HIS A 150      19.387 -11.785  77.125  1.00 61.58           N  
ATOM   1082  CD2 HIS A 150      17.394 -12.611  77.476  1.00 60.48           C  
ATOM   1083  CE1 HIS A 150      19.272 -12.865  76.367  1.00 60.90           C  
ATOM   1084  NE2 HIS A 150      18.072 -13.384  76.559  1.00 60.01           N  
ATOM   1085  N   GLY A 151      15.298  -7.783  78.809  1.00 56.09           N  
ATOM   1086  CA  GLY A 151      13.851  -7.544  78.915  1.00 54.55           C  
ATOM   1087  C   GLY A 151      13.141  -7.172  80.204  1.00 53.49           C  
ATOM   1088  O   GLY A 151      11.982  -6.759  80.157  1.00 53.03           O  
ATOM   1089  N   LYS A 152      13.807  -7.317  81.348  1.00 52.73           N  
ATOM   1090  CA  LYS A 152      13.182  -7.018  82.656  1.00 52.04           C  
ATOM   1091  C   LYS A 152      12.847  -5.524  82.812  1.00 51.10           C  
ATOM   1092  O   LYS A 152      13.645  -4.675  82.425  1.00 51.13           O  
ATOM   1093  CB  LYS A 152      14.079  -7.476  83.832  1.00 52.18           C  
ATOM   1094  CG  LYS A 152      14.535  -8.944  83.812  1.00 52.51           C  
ATOM   1095  CD  LYS A 152      13.320  -9.907  83.788  1.00 54.90           C  
ATOM   1096  CE  LYS A 152      13.673 -11.293  83.211  1.00 53.04           C  
ATOM   1097  NZ  LYS A 152      13.919 -12.297  84.282  1.00 51.75           N  
ATOM   1098  N   PRO A 153      11.658  -5.200  83.361  1.00 50.32           N  
ATOM   1099  CA  PRO A 153      11.342  -3.807  83.745  1.00 49.25           C  
ATOM   1100  C   PRO A 153      12.054  -3.317  85.024  1.00 48.23           C  
ATOM   1101  O   PRO A 153      12.366  -4.110  85.910  1.00 48.21           O  
ATOM   1102  CB  PRO A 153       9.826  -3.834  83.952  1.00 49.34           C  
ATOM   1103  CG  PRO A 153       9.525  -5.220  84.368  1.00 50.04           C  
ATOM   1104  CD  PRO A 153      10.517  -6.104  83.608  1.00 50.63           C  
ATOM   1105  N   GLN A 154      12.300  -2.012  85.098  1.00 46.60           N  
ATOM   1106  CA  GLN A 154      13.007  -1.411  86.208  1.00 45.33           C  
ATOM   1107  C   GLN A 154      12.339  -0.093  86.579  1.00 44.24           C  
ATOM   1108  O   GLN A 154      11.933   0.659  85.707  1.00 44.34           O  
ATOM   1109  CB  GLN A 154      14.445  -1.164  85.801  1.00 45.77           C  
ATOM   1110  CG  GLN A 154      15.472  -1.548  86.848  1.00 48.36           C  
ATOM   1111  CD  GLN A 154      15.497  -3.050  87.119  1.00 50.87           C  
ATOM   1112  OE1 GLN A 154      15.466  -3.870  86.181  1.00 52.45           O  
ATOM   1113  NE2 GLN A 154      15.550  -3.417  88.405  1.00 48.37           N  
ATOM   1114  N   ALA A 155      12.178   0.165  87.873  1.00 43.03           N  
ATOM   1115  CA  ALA A 155      11.599   1.418  88.339  1.00 41.71           C  
ATOM   1116  C   ALA A 155      12.705   2.259  88.936  1.00 41.33           C  
ATOM   1117  O   ALA A 155      13.526   1.756  89.723  1.00 40.57           O  
ATOM   1118  CB  ALA A 155      10.515   1.173  89.361  1.00 41.77           C  
ATOM   1119  N   LEU A 156      12.744   3.529  88.537  1.00 40.43           N  
ATOM   1120  CA  LEU A 156      13.711   4.473  89.076  1.00 40.12           C  
ATOM   1121  C   LEU A 156      12.993   5.767  89.426  1.00 39.33           C  
ATOM   1122  O   LEU A 156      11.891   6.013  88.920  1.00 39.85           O  
ATOM   1123  CB  LEU A 156      14.841   4.717  88.073  1.00 40.86           C  
ATOM   1124  CG  LEU A 156      15.734   3.499  87.782  1.00 42.60           C  
ATOM   1125  CD1 LEU A 156      16.919   3.858  86.881  1.00 44.21           C  
ATOM   1126  CD2 LEU A 156      16.246   2.875  89.089  1.00 44.96           C  
ATOM   1127  N   GLY A 157      13.585   6.563  90.316  1.00 37.50           N  
ATOM   1128  CA  GLY A 157      13.010   7.825  90.723  1.00 35.46           C  
ATOM   1129  C   GLY A 157      14.092   8.876  90.717  1.00 35.04           C  
ATOM   1130  O   GLY A 157      15.272   8.547  90.799  1.00 34.83           O  
ATOM   1131  N   ALA A 158      13.705  10.147  90.621  1.00 34.12           N  
ATOM   1132  CA  ALA A 158      14.675  11.238  90.635  1.00 33.37           C  
ATOM   1133  C   ALA A 158      14.015  12.581  90.954  1.00 32.69           C  
ATOM   1134  O   ALA A 158      12.808  12.715  90.887  1.00 33.16           O  
ATOM   1135  CB  ALA A 158      15.406  11.302  89.277  1.00 33.18           C  
ATOM   1136  N   ASP A 159      14.818  13.582  91.280  1.00 32.62           N  
ATOM   1137  CA  ASP A 159      14.315  14.934  91.515  1.00 32.16           C  
ATOM   1138  C   ASP A 159      14.126  15.738  90.217  1.00 31.14           C  
ATOM   1139  O   ASP A 159      13.238  16.623  90.132  1.00 30.55           O  
ATOM   1140  CB  ASP A 159      15.279  15.677  92.424  1.00 32.70           C  
ATOM   1141  CG  ASP A 159      15.381  15.056  93.792  1.00 35.35           C  
ATOM   1142  OD1 ASP A 159      14.362  14.500  94.257  1.00 39.75           O  
ATOM   1143  OD2 ASP A 159      16.476  15.126  94.408  1.00 38.41           O  
ATOM   1144  N   VAL A 160      15.008  15.465  89.241  1.00 29.58           N  
ATOM   1145  CA  VAL A 160      14.956  16.076  87.897  1.00 27.16           C  
ATOM   1146  C   VAL A 160      15.134  14.955  86.909  1.00 25.83           C  
ATOM   1147  O   VAL A 160      15.926  14.063  87.154  1.00 25.87           O  
ATOM   1148  CB  VAL A 160      16.081  17.120  87.644  1.00 27.20           C  
ATOM   1149  CG1 VAL A 160      15.849  17.885  86.314  1.00 26.15           C  
ATOM   1150  CG2 VAL A 160      16.211  18.118  88.781  1.00 26.67           C  
ATOM   1151  N   LEU A 161      14.378  14.996  85.821  1.00 24.26           N  
ATOM   1152  CA  LEU A 161      14.629  14.169  84.662  1.00 23.62           C  
ATOM   1153  C   LEU A 161      14.989  15.085  83.479  1.00 24.38           C  
ATOM   1154  O   LEU A 161      14.218  15.983  83.107  1.00 24.90           O  
ATOM   1155  CB  LEU A 161      13.415  13.278  84.319  1.00 23.00           C  
ATOM   1156  CG  LEU A 161      13.472  12.557  82.948  1.00 20.96           C  
ATOM   1157  CD1 LEU A 161      14.627  11.573  82.781  1.00 22.48           C  
ATOM   1158  CD2 LEU A 161      12.188  11.881  82.594  1.00 22.19           C  
ATOM   1159  N   VAL A 162      16.167  14.852  82.909  1.00 24.30           N  
ATOM   1160  CA  VAL A 162      16.654  15.573  81.739  1.00 23.95           C  
ATOM   1161  C   VAL A 162      16.591  14.633  80.577  1.00 23.97           C  
ATOM   1162  O   VAL A 162      17.337  13.646  80.550  1.00 23.60           O  
ATOM   1163  CB  VAL A 162      18.148  15.947  81.849  1.00 23.63           C  
ATOM   1164  CG1 VAL A 162      18.607  16.633  80.578  1.00 21.07           C  
ATOM   1165  CG2 VAL A 162      18.417  16.816  83.069  1.00 22.73           C  
ATOM   1166  N   GLY A 163      15.730  14.966  79.617  1.00 24.32           N  
ATOM   1167  CA  GLY A 163      15.569  14.192  78.376  1.00 24.24           C  
ATOM   1168  C   GLY A 163      16.585  14.575  77.329  1.00 24.21           C  
ATOM   1169  O   GLY A 163      16.379  15.503  76.542  1.00 26.10           O  
ATOM   1170  N   ALA A 164      17.696  13.863  77.322  1.00 23.92           N  
ATOM   1171  CA  ALA A 164      18.754  14.086  76.360  1.00 23.44           C  
ATOM   1172  C   ALA A 164      18.780  12.895  75.376  1.00 23.60           C  
ATOM   1173  O   ALA A 164      19.843  12.371  75.024  1.00 24.58           O  
ATOM   1174  CB  ALA A 164      20.050  14.231  77.091  1.00 22.12           C  
ATOM   1175  N   ASP A 165      17.610  12.451  74.943  1.00 23.32           N  
ATOM   1176  CA  ASP A 165      17.544  11.149  74.275  1.00 24.26           C  
ATOM   1177  C   ASP A 165      17.355  11.231  72.721  1.00 24.30           C  
ATOM   1178  O   ASP A 165      16.727  10.373  72.127  1.00 23.25           O  
ATOM   1179  CB  ASP A 165      16.576  10.177  74.998  1.00 23.91           C  
ATOM   1180  CG  ASP A 165      15.157  10.761  75.215  1.00 26.48           C  
ATOM   1181  OD1 ASP A 165      14.953  12.015  75.159  1.00 25.73           O  
ATOM   1182  OD2 ASP A 165      14.229   9.937  75.431  1.00 27.67           O  
ATOM   1183  N   GLY A 166      17.932  12.290  72.116  1.00 24.01           N  
ATOM   1184  CA  GLY A 166      18.104  12.430  70.677  1.00 23.24           C  
ATOM   1185  C   GLY A 166      16.850  12.518  69.817  1.00 23.22           C  
ATOM   1186  O   GLY A 166      15.756  12.674  70.312  1.00 22.42           O  
ATOM   1187  N   ILE A 167      17.055  12.428  68.514  1.00 23.14           N  
ATOM   1188  CA  ILE A 167      16.006  12.352  67.519  1.00 24.99           C  
ATOM   1189  C   ILE A 167      14.683  11.634  67.882  1.00 26.33           C  
ATOM   1190  O   ILE A 167      13.594  12.166  67.586  1.00 27.00           O  
ATOM   1191  CB  ILE A 167      16.567  11.761  66.179  1.00 25.51           C  
ATOM   1192  CG1 ILE A 167      15.486  11.721  65.095  1.00 25.43           C  
ATOM   1193  CG2 ILE A 167      17.264  10.412  66.395  1.00 22.42           C  
ATOM   1194  CD1 ILE A 167      16.053  12.017  63.708  1.00 25.21           C  
ATOM   1195  N   HIS A 168      14.776  10.445  68.482  1.00 26.61           N  
ATOM   1196  CA  HIS A 168      13.597   9.627  68.764  1.00 27.47           C  
ATOM   1197  C   HIS A 168      13.217   9.660  70.226  1.00 27.90           C  
ATOM   1198  O   HIS A 168      12.653   8.696  70.751  1.00 27.39           O  
ATOM   1199  CB  HIS A 168      13.843   8.200  68.344  1.00 28.02           C  
ATOM   1200  CG  HIS A 168      14.155   8.072  66.897  1.00 28.88           C  
ATOM   1201  ND1 HIS A 168      13.270   8.475  65.913  1.00 28.65           N  
ATOM   1202  CD2 HIS A 168      15.270   7.641  66.265  1.00 27.98           C  
ATOM   1203  CE1 HIS A 168      13.825   8.278  64.734  1.00 28.19           C  
ATOM   1204  NE2 HIS A 168      15.036   7.776  64.920  1.00 30.36           N  
ATOM   1205  N   SER A 169      13.509  10.809  70.838  1.00 27.80           N  
ATOM   1206  CA  SER A 169      13.307  11.066  72.233  1.00 27.95           C  
ATOM   1207  C   SER A 169      11.974  10.599  72.784  1.00 28.43           C  
ATOM   1208  O   SER A 169      10.893  11.102  72.387  1.00 28.97           O  
ATOM   1209  CB  SER A 169      13.425  12.561  72.513  1.00 27.40           C  
ATOM   1210  OG  SER A 169      13.301  12.769  73.908  1.00 26.35           O  
ATOM   1211  N   ALA A 170      12.064   9.685  73.746  1.00 28.31           N  
ATOM   1212  CA  ALA A 170      10.888   9.259  74.488  1.00 28.26           C  
ATOM   1213  C   ALA A 170      10.380  10.317  75.486  1.00 28.11           C  
ATOM   1214  O   ALA A 170       9.179  10.374  75.769  1.00 28.32           O  
ATOM   1215  CB  ALA A 170      11.152   7.914  75.175  1.00 28.68           C  
ATOM   1216  N   VAL A 171      11.279  11.160  76.011  1.00 27.70           N  
ATOM   1217  CA  VAL A 171      10.876  12.177  77.009  1.00 26.43           C  
ATOM   1218  C   VAL A 171      10.092  13.291  76.330  1.00 25.97           C  
ATOM   1219  O   VAL A 171       9.036  13.722  76.837  1.00 26.02           O  
ATOM   1220  CB  VAL A 171      12.051  12.738  77.878  1.00 26.45           C  
ATOM   1221  CG1 VAL A 171      11.538  13.747  78.866  1.00 26.30           C  
ATOM   1222  CG2 VAL A 171      12.787  11.622  78.646  1.00 25.65           C  
ATOM   1223  N   ARG A 172      10.601  13.728  75.174  1.00 25.31           N  
ATOM   1224  CA  ARG A 172       9.876  14.607  74.255  1.00 25.19           C  
ATOM   1225  C   ARG A 172       8.488  14.058  73.897  1.00 25.14           C  
ATOM   1226  O   ARG A 172       7.512  14.759  74.004  1.00 24.73           O  
ATOM   1227  CB  ARG A 172      10.681  14.825  72.968  1.00 24.92           C  
ATOM   1228  CG  ARG A 172      10.130  15.931  72.097  1.00 25.65           C  
ATOM   1229  CD  ARG A 172      10.706  15.967  70.694  1.00 25.39           C  
ATOM   1230  NE  ARG A 172      10.056  17.028  69.896  1.00 29.86           N  
ATOM   1231  CZ  ARG A 172      10.476  18.297  69.788  1.00 31.47           C  
ATOM   1232  NH1 ARG A 172      11.572  18.712  70.430  1.00 32.66           N  
ATOM   1233  NH2 ARG A 172       9.802  19.161  69.030  1.00 28.80           N  
ATOM   1234  N   ALA A 173       8.410  12.804  73.468  1.00 26.00           N  
ATOM   1235  CA  ALA A 173       7.115  12.199  73.130  1.00 27.32           C  
ATOM   1236  C   ALA A 173       6.149  12.177  74.329  1.00 28.17           C  
ATOM   1237  O   ALA A 173       4.950  12.371  74.144  1.00 27.88           O  
ATOM   1238  CB  ALA A 173       7.293  10.787  72.527  1.00 26.88           C  
ATOM   1239  N   HIS A 174       6.677  11.961  75.541  1.00 28.79           N  
ATOM   1240  CA  HIS A 174       5.857  11.998  76.749  1.00 29.94           C  
ATOM   1241  C   HIS A 174       5.324  13.400  76.936  1.00 30.21           C  
ATOM   1242  O   HIS A 174       4.139  13.586  77.173  1.00 31.34           O  
ATOM   1243  CB  HIS A 174       6.653  11.567  77.999  1.00 29.77           C  
ATOM   1244  CG  HIS A 174       5.991  11.932  79.303  1.00 31.05           C  
ATOM   1245  ND1 HIS A 174       5.022  11.144  79.899  1.00 33.47           N  
ATOM   1246  CD2 HIS A 174       6.165  12.995  80.129  1.00 30.74           C  
ATOM   1247  CE1 HIS A 174       4.629  11.708  81.030  1.00 32.06           C  
ATOM   1248  NE2 HIS A 174       5.304  12.835  81.189  1.00 31.94           N  
ATOM   1249  N   LEU A 175       6.209  14.386  76.834  1.00 30.91           N  
ATOM   1250  CA  LEU A 175       5.854  15.773  77.099  1.00 31.29           C  
ATOM   1251  C   LEU A 175       5.029  16.428  76.011  1.00 32.25           C  
ATOM   1252  O   LEU A 175       4.284  17.354  76.284  1.00 32.30           O  
ATOM   1253  CB  LEU A 175       7.106  16.602  77.306  1.00 30.84           C  
ATOM   1254  CG  LEU A 175       7.857  16.384  78.606  1.00 31.07           C  
ATOM   1255  CD1 LEU A 175       9.239  16.926  78.439  1.00 29.90           C  
ATOM   1256  CD2 LEU A 175       7.132  17.060  79.775  1.00 31.80           C  
ATOM   1257  N   HIS A 176       5.189  15.979  74.775  1.00 33.73           N  
ATOM   1258  CA  HIS A 176       4.529  16.611  73.643  1.00 35.63           C  
ATOM   1259  C   HIS A 176       3.837  15.551  72.816  1.00 37.28           C  
ATOM   1260  O   HIS A 176       4.266  15.257  71.702  1.00 37.37           O  
ATOM   1261  CB  HIS A 176       5.541  17.411  72.838  1.00 35.35           C  
ATOM   1262  CG  HIS A 176       6.100  18.566  73.602  1.00 37.14           C  
ATOM   1263  ND1 HIS A 176       5.505  19.809  73.608  1.00 35.68           N  
ATOM   1264  CD2 HIS A 176       7.164  18.654  74.436  1.00 38.67           C  
ATOM   1265  CE1 HIS A 176       6.199  20.624  74.379  1.00 37.77           C  
ATOM   1266  NE2 HIS A 176       7.203  19.946  74.906  1.00 38.97           N  
ATOM   1267  N   PRO A 177       2.768  14.948  73.381  1.00 39.08           N  
ATOM   1268  CA  PRO A 177       2.097  13.848  72.712  1.00 40.24           C  
ATOM   1269  C   PRO A 177       1.420  14.320  71.435  1.00 41.85           C  
ATOM   1270  O   PRO A 177       1.109  13.502  70.572  1.00 42.49           O  
ATOM   1271  CB  PRO A 177       1.035  13.411  73.734  1.00 40.34           C  
ATOM   1272  CG  PRO A 177       1.491  13.972  75.033  1.00 39.88           C  
ATOM   1273  CD  PRO A 177       2.130  15.260  74.678  1.00 38.98           C  
ATOM   1274  N   ASP A 178       1.210  15.627  71.291  1.00 42.99           N  
ATOM   1275  CA  ASP A 178       0.569  16.118  70.070  1.00 44.17           C  
ATOM   1276  C   ASP A 178       1.523  16.602  69.007  1.00 43.84           C  
ATOM   1277  O   ASP A 178       1.122  17.284  68.072  1.00 44.12           O  
ATOM   1278  CB  ASP A 178      -0.491  17.154  70.405  1.00 44.57           C  
ATOM   1279  CG  ASP A 178      -1.697  16.516  71.062  1.00 47.80           C  
ATOM   1280  OD1 ASP A 178      -1.877  15.275  70.887  1.00 48.08           O  
ATOM   1281  OD2 ASP A 178      -2.464  17.251  71.743  1.00 52.55           O  
ATOM   1282  N   GLN A 179       2.791  16.242  69.159  1.00 43.58           N  
ATOM   1283  CA  GLN A 179       3.818  16.684  68.235  1.00 43.02           C  
ATOM   1284  C   GLN A 179       3.618  16.140  66.815  1.00 43.42           C  
ATOM   1285  O   GLN A 179       3.160  15.004  66.602  1.00 43.44           O  
ATOM   1286  CB  GLN A 179       5.225  16.373  68.777  1.00 43.01           C  
ATOM   1287  CG  GLN A 179       5.560  14.887  69.045  1.00 41.94           C  
ATOM   1288  CD  GLN A 179       7.015  14.710  69.453  1.00 42.50           C  
ATOM   1289  OE1 GLN A 179       7.823  15.593  69.221  1.00 41.40           O  
ATOM   1290  NE2 GLN A 179       7.350  13.571  70.057  1.00 40.73           N  
ATOM   1291  N   ARG A 180       3.945  16.992  65.855  1.00 43.67           N  
ATOM   1292  CA  ARG A 180       4.060  16.644  64.451  1.00 43.77           C  
ATOM   1293  C   ARG A 180       5.134  15.560  64.308  1.00 42.69           C  
ATOM   1294  O   ARG A 180       6.061  15.509  65.134  1.00 42.59           O  
ATOM   1295  CB  ARG A 180       4.520  17.912  63.731  1.00 44.46           C  
ATOM   1296  CG  ARG A 180       4.115  18.026  62.275  1.00 48.25           C  
ATOM   1297  CD  ARG A 180       5.276  18.601  61.470  1.00 52.47           C  
ATOM   1298  NE  ARG A 180       5.104  18.398  60.035  1.00 57.34           N  
ATOM   1299  CZ  ARG A 180       5.591  17.368  59.341  1.00 59.39           C  
ATOM   1300  NH1 ARG A 180       5.368  17.296  58.034  1.00 61.66           N  
ATOM   1301  NH2 ARG A 180       6.300  16.415  59.934  1.00 58.78           N  
ATOM   1302  N   PRO A 181       5.042  14.696  63.261  1.00 41.87           N  
ATOM   1303  CA  PRO A 181       6.159  13.754  63.023  1.00 40.78           C  
ATOM   1304  C   PRO A 181       7.401  14.556  62.636  1.00 39.41           C  
ATOM   1305  O   PRO A 181       7.282  15.774  62.383  1.00 39.49           O  
ATOM   1306  CB  PRO A 181       5.681  12.918  61.820  1.00 40.97           C  
ATOM   1307  CG  PRO A 181       4.192  13.127  61.747  1.00 41.11           C  
ATOM   1308  CD  PRO A 181       3.978  14.535  62.247  1.00 42.21           C  
ATOM   1309  N   LEU A 182       8.576  13.923  62.633  1.00 37.09           N  
ATOM   1310  CA  LEU A 182       9.759  14.541  62.037  1.00 35.52           C  
ATOM   1311  C   LEU A 182       9.385  15.294  60.762  1.00 34.88           C  
ATOM   1312  O   LEU A 182       8.686  14.749  59.900  1.00 35.52           O  
ATOM   1313  CB  LEU A 182      10.769  13.471  61.650  1.00 35.32           C  
ATOM   1314  CG  LEU A 182      11.399  12.660  62.762  1.00 35.22           C  
ATOM   1315  CD1 LEU A 182      12.068  11.471  62.167  1.00 32.75           C  
ATOM   1316  CD2 LEU A 182      12.369  13.540  63.548  1.00 35.53           C  
ATOM   1317  N   SER A 183       9.855  16.528  60.633  1.00 33.58           N  
ATOM   1318  CA  SER A 183       9.677  17.299  59.407  1.00 32.99           C  
ATOM   1319  C   SER A 183      10.817  17.114  58.385  1.00 32.98           C  
ATOM   1320  O   SER A 183      11.992  17.329  58.696  1.00 33.24           O  
ATOM   1321  CB  SER A 183       9.505  18.774  59.742  1.00 32.62           C  
ATOM   1322  OG  SER A 183       8.395  18.978  60.598  1.00 33.48           O  
ATOM   1323  N   HIS A 184      10.464  16.745  57.156  1.00 32.80           N  
ATOM   1324  CA  HIS A 184      11.467  16.480  56.111  1.00 33.25           C  
ATOM   1325  C   HIS A 184      11.845  17.769  55.485  1.00 31.86           C  
ATOM   1326  O   HIS A 184      10.988  18.469  55.002  1.00 31.70           O  
ATOM   1327  CB  HIS A 184      10.945  15.532  55.020  1.00 33.52           C  
ATOM   1328  CG  HIS A 184      10.772  14.115  55.483  1.00 37.52           C  
ATOM   1329  ND1 HIS A 184      11.600  13.090  55.070  1.00 40.63           N  
ATOM   1330  CD2 HIS A 184       9.870  13.552  56.327  1.00 39.79           C  
ATOM   1331  CE1 HIS A 184      11.218  11.958  55.645  1.00 41.34           C  
ATOM   1332  NE2 HIS A 184      10.179  12.214  56.420  1.00 41.64           N  
ATOM   1333  N   GLY A 185      13.136  18.073  55.475  1.00 31.48           N  
ATOM   1334  CA  GLY A 185      13.627  19.302  54.860  1.00 30.88           C  
ATOM   1335  C   GLY A 185      13.648  19.258  53.334  1.00 31.05           C  
ATOM   1336  O   GLY A 185      13.779  20.310  52.700  1.00 31.10           O  
ATOM   1337  N   GLY A 186      13.536  18.058  52.741  1.00 29.78           N  
ATOM   1338  CA  GLY A 186      13.567  17.919  51.286  1.00 29.20           C  
ATOM   1339  C   GLY A 186      14.956  17.748  50.666  1.00 28.32           C  
ATOM   1340  O   GLY A 186      15.142  17.991  49.483  1.00 28.29           O  
ATOM   1341  N   ILE A 187      15.929  17.321  51.466  1.00 27.42           N  
ATOM   1342  CA  ILE A 187      17.320  17.116  50.994  1.00 26.83           C  
ATOM   1343  C   ILE A 187      17.770  15.736  51.492  1.00 26.43           C  
ATOM   1344  O   ILE A 187      17.531  15.409  52.644  1.00 26.68           O  
ATOM   1345  CB  ILE A 187      18.282  18.295  51.481  1.00 26.32           C  
ATOM   1346  CG1 ILE A 187      17.813  19.674  50.960  1.00 25.19           C  
ATOM   1347  CG2 ILE A 187      19.770  18.002  51.196  1.00 25.73           C  
ATOM   1348  CD1 ILE A 187      18.176  20.016  49.511  1.00 23.67           C  
ATOM   1349  N   THR A 188      18.352  14.918  50.617  1.00 26.44           N  
ATOM   1350  CA  THR A 188      18.882  13.593  50.975  1.00 27.17           C  
ATOM   1351  C   THR A 188      20.376  13.730  51.191  1.00 28.63           C  
ATOM   1352  O   THR A 188      21.084  14.340  50.385  1.00 28.69           O  
ATOM   1353  CB  THR A 188      18.636  12.504  49.860  1.00 26.92           C  
ATOM   1354  OG1 THR A 188      17.252  12.427  49.569  1.00 25.63           O  
ATOM   1355  CG2 THR A 188      19.124  11.075  50.290  1.00 26.31           C  
HETATM 1356  N   MSE A 189      20.852  13.165  52.289  1.00 30.31           N  
HETATM 1357  CA  MSE A 189      22.259  13.230  52.638  1.00 34.34           C  
HETATM 1358  C   MSE A 189      22.901  11.869  52.635  1.00 30.47           C  
HETATM 1359  O   MSE A 189      22.282  10.898  53.044  1.00 30.55           O  
HETATM 1360  CB  MSE A 189      22.408  13.826  54.020  1.00 32.68           C  
HETATM 1361  CG  MSE A 189      21.734  15.155  54.137  1.00 39.06           C  
HETATM 1362 SE   MSE A 189      21.951  15.995  55.911  1.00 51.57          SE  
HETATM 1363  CE  MSE A 189      23.880  15.663  56.223  1.00 46.94           C  
ATOM   1364  N   TRP A 190      24.142  11.814  52.152  1.00 28.86           N  
ATOM   1365  CA  TRP A 190      25.059  10.698  52.386  1.00 26.37           C  
ATOM   1366  C   TRP A 190      26.306  11.238  53.054  1.00 25.49           C  
ATOM   1367  O   TRP A 190      26.778  12.315  52.735  1.00 23.65           O  
ATOM   1368  CB  TRP A 190      25.463  10.028  51.090  1.00 26.34           C  
ATOM   1369  CG  TRP A 190      24.356   9.329  50.377  1.00 26.21           C  
ATOM   1370  CD1 TRP A 190      24.051   7.998  50.443  1.00 24.98           C  
ATOM   1371  CD2 TRP A 190      23.420   9.916  49.468  1.00 25.83           C  
ATOM   1372  NE1 TRP A 190      22.979   7.715  49.620  1.00 26.23           N  
ATOM   1373  CE2 TRP A 190      22.579   8.877  49.003  1.00 27.32           C  
ATOM   1374  CE3 TRP A 190      23.230  11.214  48.968  1.00 28.02           C  
ATOM   1375  CZ2 TRP A 190      21.544   9.104  48.070  1.00 26.40           C  
ATOM   1376  CZ3 TRP A 190      22.191  11.441  48.044  1.00 26.78           C  
ATOM   1377  CH2 TRP A 190      21.368  10.387  47.609  1.00 26.45           C  
ATOM   1378  N   ARG A 191      26.845  10.439  53.961  1.00 24.92           N  
ATOM   1379  CA  ARG A 191      27.890  10.845  54.877  1.00 24.31           C  
ATOM   1380  C   ARG A 191      28.940   9.765  54.795  1.00 23.53           C  
ATOM   1381  O   ARG A 191      28.606   8.582  54.650  1.00 22.39           O  
ATOM   1382  CB  ARG A 191      27.351  10.770  56.318  1.00 24.40           C  
ATOM   1383  CG  ARG A 191      26.791  11.978  56.932  1.00 24.41           C  
ATOM   1384  CD  ARG A 191      26.510  11.691  58.429  1.00 25.73           C  
ATOM   1385  NE  ARG A 191      25.403  10.758  58.603  1.00 31.71           N  
ATOM   1386  CZ  ARG A 191      25.219   9.989  59.661  1.00 33.02           C  
ATOM   1387  NH1 ARG A 191      26.062  10.012  60.679  1.00 35.24           N  
ATOM   1388  NH2 ARG A 191      24.185   9.180  59.689  1.00 36.63           N  
ATOM   1389  N   GLY A 192      30.197  10.147  54.953  1.00 22.77           N  
ATOM   1390  CA  GLY A 192      31.232   9.143  55.019  1.00 23.91           C  
ATOM   1391  C   GLY A 192      32.591   9.678  55.393  1.00 24.24           C  
ATOM   1392  O   GLY A 192      32.756  10.897  55.564  1.00 24.22           O  
ATOM   1393  N   VAL A 193      33.550   8.749  55.512  1.00 24.14           N  
ATOM   1394  CA  VAL A 193      34.967   9.060  55.725  1.00 24.34           C  
ATOM   1395  C   VAL A 193      35.813   8.361  54.666  1.00 25.12           C  
ATOM   1396  O   VAL A 193      35.555   7.205  54.308  1.00 25.43           O  
ATOM   1397  CB  VAL A 193      35.494   8.715  57.162  1.00 24.04           C  
ATOM   1398  CG1 VAL A 193      34.820   9.563  58.215  1.00 21.94           C  
ATOM   1399  CG2 VAL A 193      35.317   7.224  57.491  1.00 24.42           C  
ATOM   1400  N   THR A 194      36.798   9.082  54.136  1.00 25.46           N  
ATOM   1401  CA  THR A 194      37.723   8.503  53.187  1.00 26.19           C  
ATOM   1402  C   THR A 194      39.148   8.856  53.647  1.00 27.08           C  
ATOM   1403  O   THR A 194      39.403   9.953  54.166  1.00 26.57           O  
ATOM   1404  CB  THR A 194      37.413   8.981  51.739  1.00 26.31           C  
ATOM   1405  OG1 THR A 194      36.017   8.776  51.457  1.00 25.30           O  
ATOM   1406  CG2 THR A 194      38.274   8.211  50.679  1.00 25.59           C  
ATOM   1407  N   GLU A 195      40.065   7.906  53.508  1.00 28.34           N  
ATOM   1408  CA  GLU A 195      41.462   8.177  53.823  1.00 30.22           C  
ATOM   1409  C   GLU A 195      42.207   8.842  52.662  1.00 30.51           C  
ATOM   1410  O   GLU A 195      42.102   8.398  51.507  1.00 30.28           O  
ATOM   1411  CB  GLU A 195      42.172   6.913  54.223  1.00 30.63           C  
ATOM   1412  CG  GLU A 195      43.347   7.194  55.119  1.00 36.89           C  
ATOM   1413  CD  GLU A 195      42.906   7.557  56.534  1.00 43.23           C  
ATOM   1414  OE1 GLU A 195      42.007   6.836  57.059  1.00 45.79           O  
ATOM   1415  OE2 GLU A 195      43.458   8.551  57.106  1.00 44.00           O  
ATOM   1416  N   PHE A 196      42.950   9.900  53.002  1.00 30.95           N  
ATOM   1417  CA  PHE A 196      43.824  10.644  52.088  1.00 31.74           C  
ATOM   1418  C   PHE A 196      45.258  10.683  52.610  1.00 32.64           C  
ATOM   1419  O   PHE A 196      45.468  10.618  53.826  1.00 32.42           O  
ATOM   1420  CB  PHE A 196      43.319  12.086  51.934  1.00 31.79           C  
ATOM   1421  CG  PHE A 196      42.245  12.231  50.902  1.00 31.09           C  
ATOM   1422  CD1 PHE A 196      42.558  12.694  49.622  1.00 29.45           C  
ATOM   1423  CD2 PHE A 196      40.923  11.872  51.195  1.00 31.00           C  
ATOM   1424  CE1 PHE A 196      41.583  12.805  48.643  1.00 28.53           C  
ATOM   1425  CE2 PHE A 196      39.929  11.970  50.219  1.00 31.46           C  
ATOM   1426  CZ  PHE A 196      40.259  12.426  48.935  1.00 30.81           C  
ATOM   1427  N   ASP A 197      46.258  10.785  51.721  1.00 34.02           N  
ATOM   1428  CA  ASP A 197      47.593  11.057  52.250  1.00 34.95           C  
ATOM   1429  C   ASP A 197      47.636  12.498  52.689  1.00 34.80           C  
ATOM   1430  O   ASP A 197      47.792  12.806  53.881  1.00 35.58           O  
ATOM   1431  CB  ASP A 197      48.758  10.789  51.308  1.00 35.80           C  
ATOM   1432  CG  ASP A 197      50.109  11.011  52.028  1.00 37.61           C  
ATOM   1433  OD1 ASP A 197      50.564  12.177  52.105  1.00 36.32           O  
ATOM   1434  OD2 ASP A 197      50.659  10.027  52.596  1.00 38.32           O  
ATOM   1435  N   ARG A 198      47.480  13.376  51.712  1.00 34.19           N  
ATOM   1436  CA  ARG A 198      47.296  14.781  51.984  1.00 33.21           C  
ATOM   1437  C   ARG A 198      45.997  15.273  51.404  1.00 31.51           C  
ATOM   1438  O   ARG A 198      45.601  14.868  50.332  1.00 31.88           O  
ATOM   1439  CB  ARG A 198      48.508  15.610  51.558  1.00 33.42           C  
ATOM   1440  CG  ARG A 198      49.549  15.549  52.666  1.00 35.74           C  
ATOM   1441  CD  ARG A 198      50.969  15.665  52.173  1.00 41.35           C  
ATOM   1442  NE  ARG A 198      51.639  16.842  52.707  1.00 43.55           N  
ATOM   1443  CZ  ARG A 198      52.955  16.948  52.840  1.00 46.78           C  
ATOM   1444  NH1 ARG A 198      53.752  15.947  52.485  1.00 45.80           N  
ATOM   1445  NH2 ARG A 198      53.474  18.062  53.337  1.00 48.62           N  
ATOM   1446  N   PHE A 199      45.296  16.081  52.191  1.00 30.23           N  
ATOM   1447  CA  PHE A 199      44.137  16.801  51.717  1.00 28.17           C  
ATOM   1448  C   PHE A 199      44.363  18.239  52.087  1.00 26.99           C  
ATOM   1449  O   PHE A 199      44.144  18.641  53.239  1.00 26.26           O  
ATOM   1450  CB  PHE A 199      42.860  16.286  52.354  1.00 27.28           C  
ATOM   1451  CG  PHE A 199      41.620  17.020  51.878  1.00 27.52           C  
ATOM   1452  CD1 PHE A 199      41.243  16.980  50.529  1.00 26.99           C  
ATOM   1453  CD2 PHE A 199      40.826  17.743  52.772  1.00 24.14           C  
ATOM   1454  CE1 PHE A 199      40.081  17.628  50.089  1.00 24.74           C  
ATOM   1455  CE2 PHE A 199      39.675  18.371  52.329  1.00 24.67           C  
ATOM   1456  CZ  PHE A 199      39.308  18.317  50.991  1.00 23.89           C  
ATOM   1457  N   LEU A 200      44.804  19.005  51.099  1.00 25.83           N  
ATOM   1458  CA  LEU A 200      45.310  20.341  51.345  1.00 25.54           C  
ATOM   1459  C   LEU A 200      46.300  20.348  52.531  1.00 25.16           C  
ATOM   1460  O   LEU A 200      47.156  19.467  52.618  1.00 24.61           O  
ATOM   1461  CB  LEU A 200      44.160  21.354  51.477  1.00 24.87           C  
ATOM   1462  CG  LEU A 200      43.240  21.487  50.251  1.00 25.32           C  
ATOM   1463  CD1 LEU A 200      42.012  22.372  50.579  1.00 24.91           C  
ATOM   1464  CD2 LEU A 200      43.971  22.003  48.936  1.00 21.85           C  
ATOM   1465  N   ASP A 201      46.180  21.319  53.436  1.00 25.56           N  
ATOM   1466  CA  ASP A 201      47.105  21.423  54.573  1.00 25.72           C  
ATOM   1467  C   ASP A 201      46.659  20.613  55.780  1.00 25.63           C  
ATOM   1468  O   ASP A 201      47.223  20.766  56.899  1.00 25.88           O  
ATOM   1469  CB  ASP A 201      47.270  22.886  54.989  1.00 26.26           C  
ATOM   1470  CG  ASP A 201      45.955  23.524  55.476  1.00 28.65           C  
ATOM   1471  OD1 ASP A 201      44.848  22.926  55.332  1.00 30.71           O  
ATOM   1472  OD2 ASP A 201      46.039  24.649  56.004  1.00 31.85           O  
ATOM   1473  N   GLY A 202      45.628  19.798  55.571  1.00 24.83           N  
ATOM   1474  CA  GLY A 202      45.096  18.905  56.599  1.00 24.63           C  
ATOM   1475  C   GLY A 202      44.125  19.547  57.585  1.00 24.57           C  
ATOM   1476  O   GLY A 202      43.681  18.884  58.530  1.00 24.69           O  
ATOM   1477  N   LYS A 203      43.784  20.821  57.383  1.00 23.73           N  
ATOM   1478  CA  LYS A 203      42.897  21.508  58.318  1.00 23.72           C  
ATOM   1479  C   LYS A 203      42.008  22.597  57.672  1.00 23.14           C  
ATOM   1480  O   LYS A 203      41.628  23.633  58.288  1.00 22.13           O  
ATOM   1481  CB  LYS A 203      43.697  21.999  59.551  1.00 24.33           C  
ATOM   1482  CG  LYS A 203      44.905  22.860  59.255  1.00 26.07           C  
ATOM   1483  CD  LYS A 203      45.641  23.115  60.534  1.00 30.53           C  
ATOM   1484  CE  LYS A 203      46.135  24.567  60.634  1.00 33.72           C  
ATOM   1485  NZ  LYS A 203      47.526  24.770  60.156  1.00 32.96           N  
ATOM   1486  N   THR A 204      41.658  22.317  56.424  1.00 23.02           N  
ATOM   1487  CA  THR A 204      40.844  23.194  55.602  1.00 23.57           C  
ATOM   1488  C   THR A 204      39.614  22.422  55.161  1.00 24.04           C  
ATOM   1489  O   THR A 204      39.702  21.305  54.641  1.00 23.70           O  
ATOM   1490  CB  THR A 204      41.643  23.713  54.364  1.00 23.90           C  
ATOM   1491  OG1 THR A 204      42.771  24.480  54.827  1.00 26.56           O  
ATOM   1492  CG2 THR A 204      40.765  24.571  53.411  1.00 21.95           C  
HETATM 1493  N   MSE A 205      38.479  23.060  55.380  1.00 24.98           N  
HETATM 1494  CA  MSE A 205      37.183  22.598  54.968  1.00 27.70           C  
HETATM 1495  C   MSE A 205      36.872  23.095  53.552  1.00 26.18           C  
HETATM 1496  O   MSE A 205      37.032  24.293  53.241  1.00 25.05           O  
HETATM 1497  CB  MSE A 205      36.127  23.132  55.948  1.00 27.11           C  
HETATM 1498  CG  MSE A 205      34.726  22.861  55.487  1.00 29.60           C  
HETATM 1499 SE   MSE A 205      33.520  23.058  56.988  0.70 35.31          SE  
HETATM 1500  CE  MSE A 205      31.833  23.310  56.073  1.00 33.29           C  
ATOM   1501  N   ILE A 206      36.403  22.158  52.726  1.00 25.52           N  
ATOM   1502  CA  ILE A 206      35.979  22.392  51.350  1.00 24.92           C  
ATOM   1503  C   ILE A 206      34.428  22.338  51.221  1.00 25.10           C  
ATOM   1504  O   ILE A 206      33.780  21.417  51.725  1.00 23.48           O  
ATOM   1505  CB  ILE A 206      36.667  21.313  50.417  1.00 25.40           C  
ATOM   1506  CG1 ILE A 206      38.183  21.516  50.375  1.00 26.34           C  
ATOM   1507  CG2 ILE A 206      36.173  21.357  49.027  1.00 23.72           C  
ATOM   1508  CD1 ILE A 206      38.625  22.647  49.474  1.00 28.47           C  
ATOM   1509  N   VAL A 207      33.851  23.323  50.522  1.00 25.68           N  
ATOM   1510  CA  VAL A 207      32.445  23.309  50.145  1.00 26.42           C  
ATOM   1511  C   VAL A 207      32.325  23.533  48.616  1.00 27.14           C  
ATOM   1512  O   VAL A 207      33.144  24.246  48.027  1.00 26.50           O  
ATOM   1513  CB  VAL A 207      31.636  24.349  51.020  1.00 27.02           C  
ATOM   1514  CG1 VAL A 207      30.239  24.679  50.452  1.00 27.42           C  
ATOM   1515  CG2 VAL A 207      31.488  23.838  52.468  1.00 27.68           C  
ATOM   1516  N   ALA A 208      31.312  22.908  47.983  1.00 27.67           N  
ATOM   1517  CA  ALA A 208      31.004  23.077  46.539  1.00 27.44           C  
ATOM   1518  C   ALA A 208      29.555  22.714  46.216  1.00 28.28           C  
ATOM   1519  O   ALA A 208      28.919  21.968  46.958  1.00 28.45           O  
ATOM   1520  CB  ALA A 208      31.930  22.226  45.691  1.00 27.22           C  
ATOM   1521  N   ASN A 209      29.039  23.233  45.101  1.00 29.32           N  
ATOM   1522  CA  ASN A 209      27.778  22.754  44.540  1.00 30.40           C  
ATOM   1523  C   ASN A 209      27.618  22.810  43.026  1.00 31.19           C  
ATOM   1524  O   ASN A 209      28.214  23.635  42.345  1.00 31.61           O  
ATOM   1525  CB  ASN A 209      26.540  23.390  45.208  1.00 29.97           C  
ATOM   1526  CG  ASN A 209      26.452  24.854  44.968  1.00 31.79           C  
ATOM   1527  OD1 ASN A 209      27.159  25.624  45.603  1.00 35.00           O  
ATOM   1528  ND2 ASN A 209      25.583  25.267  44.050  1.00 32.62           N  
ATOM   1529  N   ASP A 210      26.791  21.884  42.549  1.00 32.05           N  
ATOM   1530  CA  ASP A 210      26.177  21.840  41.236  1.00 32.87           C  
ATOM   1531  C   ASP A 210      25.340  23.033  40.868  1.00 33.11           C  
ATOM   1532  O   ASP A 210      24.852  23.770  41.729  1.00 32.85           O  
ATOM   1533  CB  ASP A 210      25.153  20.676  41.202  1.00 32.88           C  
ATOM   1534  CG  ASP A 210      25.710  19.476  40.580  1.00 34.58           C  
ATOM   1535  OD1 ASP A 210      26.723  19.668  39.893  1.00 37.15           O  
ATOM   1536  OD2 ASP A 210      25.181  18.356  40.778  1.00 38.68           O  
ATOM   1537  N   GLU A 211      25.115  23.124  39.557  1.00 33.08           N  
ATOM   1538  CA  GLU A 211      24.062  23.906  38.937  1.00 33.88           C  
ATOM   1539  C   GLU A 211      22.706  23.239  39.223  1.00 32.64           C  
ATOM   1540  O   GLU A 211      21.663  23.868  39.073  1.00 32.51           O  
ATOM   1541  CB  GLU A 211      24.292  23.983  37.415  1.00 34.51           C  
ATOM   1542  CG  GLU A 211      25.733  24.369  36.981  1.00 38.88           C  
ATOM   1543  CD  GLU A 211      26.823  23.282  37.239  1.00 43.14           C  
ATOM   1544  OE1 GLU A 211      26.518  22.088  37.517  1.00 43.46           O  
ATOM   1545  OE2 GLU A 211      28.014  23.649  37.147  1.00 45.56           O  
ATOM   1546  N   HIS A 212      22.756  21.965  39.613  1.00 31.52           N  
ATOM   1547  CA  HIS A 212      21.614  21.200  40.098  1.00 30.50           C  
ATOM   1548  C   HIS A 212      21.486  21.182  41.630  1.00 30.03           C  
ATOM   1549  O   HIS A 212      20.768  20.320  42.180  1.00 29.90           O  
ATOM   1550  CB  HIS A 212      21.768  19.759  39.661  1.00 30.52           C  
ATOM   1551  CG  HIS A 212      22.035  19.588  38.200  1.00 33.64           C  
ATOM   1552  ND1 HIS A 212      21.035  19.645  37.248  1.00 35.12           N  
ATOM   1553  CD2 HIS A 212      23.183  19.323  37.527  1.00 34.25           C  
ATOM   1554  CE1 HIS A 212      21.558  19.424  36.052  1.00 35.53           C  
ATOM   1555  NE2 HIS A 212      22.858  19.226  36.194  1.00 35.68           N  
ATOM   1556  N   TRP A 213      22.222  22.066  42.321  1.00 28.91           N  
ATOM   1557  CA  TRP A 213      22.212  22.120  43.791  1.00 27.84           C  
ATOM   1558  C   TRP A 213      22.502  20.733  44.493  1.00 26.57           C  
ATOM   1559  O   TRP A 213      21.908  20.373  45.515  1.00 26.51           O  
ATOM   1560  CB  TRP A 213      20.898  22.788  44.224  1.00 29.11           C  
ATOM   1561  CG  TRP A 213      20.833  23.343  45.585  1.00 29.22           C  
ATOM   1562  CD1 TRP A 213      19.874  23.083  46.513  1.00 30.24           C  
ATOM   1563  CD2 TRP A 213      21.723  24.292  46.180  1.00 31.98           C  
ATOM   1564  NE1 TRP A 213      20.121  23.783  47.662  1.00 31.10           N  
ATOM   1565  CE2 TRP A 213      21.254  24.535  47.489  1.00 31.67           C  
ATOM   1566  CE3 TRP A 213      22.885  24.954  45.739  1.00 34.06           C  
ATOM   1567  CZ2 TRP A 213      21.904  25.421  48.382  1.00 32.99           C  
ATOM   1568  CZ3 TRP A 213      23.540  25.850  46.630  1.00 33.25           C  
ATOM   1569  CH2 TRP A 213      23.040  26.068  47.939  1.00 31.88           C  
ATOM   1570  N   SER A 214      23.395  19.949  43.907  1.00 24.58           N  
ATOM   1571  CA  SER A 214      24.102  18.950  44.650  1.00 23.85           C  
ATOM   1572  C   SER A 214      25.292  19.639  45.317  1.00 24.27           C  
ATOM   1573  O   SER A 214      26.122  20.265  44.655  1.00 23.08           O  
ATOM   1574  CB  SER A 214      24.581  17.801  43.763  1.00 23.64           C  
ATOM   1575  OG  SER A 214      23.489  17.154  43.113  1.00 22.49           O  
ATOM   1576  N   ARG A 215      25.342  19.526  46.644  1.00 24.51           N  
ATOM   1577  CA  ARG A 215      26.382  20.134  47.444  1.00 24.22           C  
ATOM   1578  C   ARG A 215      27.312  19.099  48.046  1.00 23.39           C  
ATOM   1579  O   ARG A 215      26.947  17.955  48.240  1.00 22.51           O  
ATOM   1580  CB  ARG A 215      25.755  20.989  48.539  1.00 24.85           C  
ATOM   1581  CG  ARG A 215      24.863  22.135  48.037  1.00 24.46           C  
ATOM   1582  CD  ARG A 215      24.121  22.806  49.206  1.00 24.47           C  
ATOM   1583  NE  ARG A 215      22.898  22.057  49.516  1.00 24.15           N  
ATOM   1584  CZ  ARG A 215      22.038  22.332  50.496  1.00 22.40           C  
ATOM   1585  NH1 ARG A 215      22.255  23.333  51.332  1.00 21.90           N  
ATOM   1586  NH2 ARG A 215      20.962  21.565  50.660  1.00 21.86           N  
ATOM   1587  N   LEU A 216      28.542  19.535  48.298  1.00 23.97           N  
ATOM   1588  CA  LEU A 216      29.610  18.736  48.897  1.00 22.69           C  
ATOM   1589  C   LEU A 216      30.233  19.533  50.024  1.00 22.44           C  
ATOM   1590  O   LEU A 216      30.470  20.734  49.905  1.00 21.06           O  
ATOM   1591  CB  LEU A 216      30.705  18.529  47.879  1.00 23.11           C  
ATOM   1592  CG  LEU A 216      31.637  17.318  47.785  1.00 23.23           C  
ATOM   1593  CD1 LEU A 216      32.979  17.893  47.450  1.00 22.16           C  
ATOM   1594  CD2 LEU A 216      31.720  16.443  49.020  1.00 20.80           C  
ATOM   1595  N   VAL A 217      30.536  18.825  51.105  1.00 22.57           N  
ATOM   1596  CA  VAL A 217      31.308  19.332  52.199  1.00 22.12           C  
ATOM   1597  C   VAL A 217      32.331  18.262  52.491  1.00 22.13           C  
ATOM   1598  O   VAL A 217      31.962  17.135  52.716  1.00 23.85           O  
ATOM   1599  CB  VAL A 217      30.438  19.542  53.489  1.00 23.00           C  
ATOM   1600  CG1 VAL A 217      31.293  20.228  54.610  1.00 21.54           C  
ATOM   1601  CG2 VAL A 217      29.125  20.341  53.180  1.00 21.33           C  
ATOM   1602  N   ALA A 218      33.610  18.608  52.515  1.00 21.85           N  
ATOM   1603  CA  ALA A 218      34.656  17.679  52.913  1.00 21.14           C  
ATOM   1604  C   ALA A 218      35.668  18.425  53.798  1.00 21.34           C  
ATOM   1605  O   ALA A 218      36.038  19.579  53.516  1.00 20.50           O  
ATOM   1606  CB  ALA A 218      35.343  17.073  51.685  1.00 20.84           C  
ATOM   1607  N   TYR A 219      36.082  17.769  54.882  1.00 20.78           N  
ATOM   1608  CA  TYR A 219      37.037  18.360  55.816  1.00 20.23           C  
ATOM   1609  C   TYR A 219      37.656  17.267  56.631  1.00 20.45           C  
ATOM   1610  O   TYR A 219      36.980  16.263  56.918  1.00 21.44           O  
ATOM   1611  CB  TYR A 219      36.358  19.380  56.740  1.00 19.56           C  
ATOM   1612  CG  TYR A 219      35.142  18.866  57.488  1.00 19.45           C  
ATOM   1613  CD1 TYR A 219      33.873  18.872  56.908  1.00 16.98           C  
ATOM   1614  CD2 TYR A 219      35.267  18.396  58.794  1.00 19.48           C  
ATOM   1615  CE1 TYR A 219      32.736  18.409  57.627  1.00 19.26           C  
ATOM   1616  CE2 TYR A 219      34.175  17.943  59.506  1.00 18.88           C  
ATOM   1617  CZ  TYR A 219      32.916  17.953  58.940  1.00 20.20           C  
ATOM   1618  OH  TYR A 219      31.871  17.496  59.710  1.00 20.48           O  
ATOM   1619  N   PRO A 220      38.943  17.431  56.995  1.00 20.53           N  
ATOM   1620  CA  PRO A 220      39.651  16.491  57.860  1.00 20.32           C  
ATOM   1621  C   PRO A 220      39.150  16.566  59.290  1.00 20.89           C  
ATOM   1622  O   PRO A 220      38.787  17.673  59.754  1.00 20.86           O  
ATOM   1623  CB  PRO A 220      41.104  16.963  57.773  1.00 20.30           C  
ATOM   1624  CG  PRO A 220      41.168  17.789  56.499  1.00 20.42           C  
ATOM   1625  CD  PRO A 220      39.837  18.506  56.535  1.00 20.69           C  
ATOM   1626  N   ILE A 221      39.128  15.409  59.969  1.00 20.96           N  
ATOM   1627  CA  ILE A 221      38.538  15.274  61.319  1.00 22.87           C  
ATOM   1628  C   ILE A 221      39.432  14.541  62.341  1.00 24.63           C  
ATOM   1629  O   ILE A 221      39.037  14.407  63.498  1.00 25.84           O  
ATOM   1630  CB  ILE A 221      37.137  14.513  61.301  1.00 22.97           C  
ATOM   1631  CG1 ILE A 221      37.293  13.115  60.716  1.00 22.90           C  
ATOM   1632  CG2 ILE A 221      36.070  15.259  60.508  1.00 20.02           C  
ATOM   1633  CD1 ILE A 221      36.095  12.261  60.922  1.00 26.53           C  
ATOM   1634  N   SER A 222      40.621  14.078  61.938  1.00 25.83           N  
ATOM   1635  CA  SER A 222      41.452  13.240  62.814  1.00 27.07           C  
ATOM   1636  C   SER A 222      42.915  13.691  63.037  1.00 27.59           C  
ATOM   1637  O   SER A 222      43.766  13.612  62.121  1.00 27.27           O  
ATOM   1638  CB  SER A 222      41.450  11.814  62.281  1.00 27.25           C  
ATOM   1639  OG  SER A 222      42.246  10.980  63.109  1.00 31.28           O  
ATOM   1640  N   ALA A 223      43.195  14.138  64.259  1.00 28.22           N  
ATOM   1641  CA  ALA A 223      44.546  14.486  64.703  1.00 29.99           C  
ATOM   1642  C   ALA A 223      45.526  13.287  64.686  1.00 31.27           C  
ATOM   1643  O   ALA A 223      46.697  13.448  64.339  1.00 30.72           O  
ATOM   1644  CB  ALA A 223      44.490  15.135  66.118  1.00 29.59           C  
ATOM   1645  N   ARG A 224      45.025  12.098  65.044  1.00 33.26           N  
ATOM   1646  CA  ARG A 224      45.797  10.858  65.054  1.00 36.06           C  
ATOM   1647  C   ARG A 224      46.329  10.575  63.675  1.00 35.99           C  
ATOM   1648  O   ARG A 224      47.512  10.280  63.521  1.00 36.75           O  
ATOM   1649  CB  ARG A 224      44.943   9.662  65.518  1.00 36.60           C  
ATOM   1650  CG  ARG A 224      44.682   9.543  67.054  1.00 39.72           C  
ATOM   1651  CD  ARG A 224      43.574   8.477  67.401  1.00 40.34           C  
ATOM   1652  NE  ARG A 224      43.818   7.165  66.769  1.00 49.46           N  
ATOM   1653  CZ  ARG A 224      43.085   6.605  65.787  1.00 52.12           C  
ATOM   1654  NH1 ARG A 224      41.997   7.196  65.278  1.00 53.69           N  
ATOM   1655  NH2 ARG A 224      43.443   5.422  65.304  1.00 52.98           N  
ATOM   1656  N   HIS A 225      45.466  10.680  62.662  1.00 36.28           N  
ATOM   1657  CA  HIS A 225      45.882  10.480  61.261  1.00 35.81           C  
ATOM   1658  C   HIS A 225      46.888  11.520  60.832  1.00 36.22           C  
ATOM   1659  O   HIS A 225      47.912  11.184  60.234  1.00 36.73           O  
ATOM   1660  CB  HIS A 225      44.678  10.486  60.310  1.00 35.59           C  
ATOM   1661  CG  HIS A 225      43.807   9.278  60.440  1.00 34.76           C  
ATOM   1662  ND1 HIS A 225      43.649   8.360  59.425  1.00 34.40           N  
ATOM   1663  CD2 HIS A 225      43.082   8.812  61.482  1.00 35.07           C  
ATOM   1664  CE1 HIS A 225      42.856   7.383  59.831  1.00 33.34           C  
ATOM   1665  NE2 HIS A 225      42.490   7.638  61.074  1.00 35.91           N  
ATOM   1666  N   ALA A 226      46.596  12.787  61.124  1.00 36.69           N  
ATOM   1667  CA  ALA A 226      47.506  13.893  60.800  1.00 37.22           C  
ATOM   1668  C   ALA A 226      48.898  13.687  61.416  1.00 38.21           C  
ATOM   1669  O   ALA A 226      49.894  14.074  60.820  1.00 37.79           O  
ATOM   1670  CB  ALA A 226      46.922  15.210  61.246  1.00 36.08           C  
ATOM   1671  N   ALA A 227      48.951  13.078  62.604  1.00 39.62           N  
ATOM   1672  CA  ALA A 227      50.214  12.881  63.314  1.00 41.51           C  
ATOM   1673  C   ALA A 227      51.024  11.746  62.682  1.00 42.41           C  
ATOM   1674  O   ALA A 227      52.237  11.661  62.864  1.00 42.78           O  
ATOM   1675  CB  ALA A 227      49.970  12.623  64.811  1.00 41.83           C  
ATOM   1676  N   GLU A 228      50.331  10.885  61.942  1.00 43.10           N  
ATOM   1677  CA  GLU A 228      50.956   9.871  61.093  1.00 43.45           C  
ATOM   1678  C   GLU A 228      51.224  10.316  59.639  1.00 42.74           C  
ATOM   1679  O   GLU A 228      51.604   9.485  58.834  1.00 43.33           O  
ATOM   1680  CB  GLU A 228      50.104   8.599  61.093  1.00 43.70           C  
ATOM   1681  CG  GLU A 228      50.341   7.735  62.327  1.00 48.33           C  
ATOM   1682  CD  GLU A 228      49.155   6.828  62.685  1.00 54.12           C  
ATOM   1683  OE1 GLU A 228      48.314   6.507  61.789  1.00 54.99           O  
ATOM   1684  OE2 GLU A 228      49.070   6.440  63.883  1.00 55.86           O  
ATOM   1685  N   GLY A 229      51.036  11.596  59.309  1.00 41.98           N  
ATOM   1686  CA  GLY A 229      51.171  12.091  57.922  1.00 41.00           C  
ATOM   1687  C   GLY A 229      49.859  12.134  57.122  1.00 40.91           C  
ATOM   1688  O   GLY A 229      49.661  13.019  56.236  1.00 41.09           O  
ATOM   1689  N   LYS A 230      48.952  11.210  57.473  1.00 39.17           N  
ATOM   1690  CA  LYS A 230      47.672  10.987  56.784  1.00 37.81           C  
ATOM   1691  C   LYS A 230      46.549  11.976  57.100  1.00 36.44           C  
ATOM   1692  O   LYS A 230      46.626  12.789  58.028  1.00 36.64           O  
ATOM   1693  CB  LYS A 230      47.135   9.574  57.083  1.00 37.63           C  
ATOM   1694  CG  LYS A 230      48.052   8.421  56.682  1.00 39.22           C  
ATOM   1695  CD  LYS A 230      48.492   8.480  55.223  1.00 40.65           C  
ATOM   1696  CE  LYS A 230      49.727   7.595  55.001  1.00 39.51           C  
ATOM   1697  NZ  LYS A 230      50.438   8.004  53.764  1.00 39.06           N  
ATOM   1698  N   SER A 231      45.476  11.867  56.333  1.00 34.49           N  
ATOM   1699  CA  SER A 231      44.304  12.659  56.586  1.00 33.18           C  
ATOM   1700  C   SER A 231      43.021  11.805  56.538  1.00 31.89           C  
ATOM   1701  O   SER A 231      42.785  11.090  55.569  1.00 31.93           O  
ATOM   1702  CB  SER A 231      44.260  13.828  55.596  1.00 33.13           C  
ATOM   1703  OG  SER A 231      43.356  14.819  56.030  1.00 34.61           O  
ATOM   1704  N   LEU A 232      42.217  11.850  57.602  1.00 30.13           N  
ATOM   1705  CA  LEU A 232      40.850  11.305  57.535  1.00 28.45           C  
ATOM   1706  C   LEU A 232      39.875  12.410  57.134  1.00 27.61           C  
ATOM   1707  O   LEU A 232      39.568  13.294  57.924  1.00 27.90           O  
ATOM   1708  CB  LEU A 232      40.415  10.670  58.848  1.00 27.87           C  
ATOM   1709  CG  LEU A 232      39.135   9.847  58.745  1.00 28.11           C  
ATOM   1710  CD1 LEU A 232      39.257   8.806  57.627  1.00 27.41           C  
ATOM   1711  CD2 LEU A 232      38.778   9.213  60.103  1.00 28.22           C  
ATOM   1712  N   VAL A 233      39.422  12.350  55.885  1.00 26.07           N  
ATOM   1713  CA  VAL A 233      38.515  13.327  55.335  1.00 23.92           C  
ATOM   1714  C   VAL A 233      37.041  12.899  55.489  1.00 23.47           C  
ATOM   1715  O   VAL A 233      36.601  11.863  54.957  1.00 22.82           O  
ATOM   1716  CB  VAL A 233      38.825  13.559  53.871  1.00 23.82           C  
ATOM   1717  CG1 VAL A 233      37.806  14.502  53.249  1.00 22.47           C  
ATOM   1718  CG2 VAL A 233      40.241  14.071  53.718  1.00 22.31           C  
ATOM   1719  N   ASN A 234      36.290  13.706  56.234  1.00 22.18           N  
ATOM   1720  CA  ASN A 234      34.854  13.502  56.356  1.00 21.23           C  
ATOM   1721  C   ASN A 234      34.173  14.168  55.150  1.00 20.84           C  
ATOM   1722  O   ASN A 234      34.626  15.210  54.666  1.00 21.59           O  
ATOM   1723  CB  ASN A 234      34.334  14.090  57.673  1.00 20.06           C  
ATOM   1724  CG  ASN A 234      32.877  13.813  57.885  1.00 20.68           C  
ATOM   1725  OD1 ASN A 234      32.472  12.675  58.070  1.00 16.31           O  
ATOM   1726  ND2 ASN A 234      32.062  14.854  57.802  1.00 23.99           N  
ATOM   1727  N   TRP A 235      33.124  13.553  54.632  1.00 19.93           N  
ATOM   1728  CA  TRP A 235      32.413  14.164  53.547  1.00 20.16           C  
ATOM   1729  C   TRP A 235      30.885  14.035  53.689  1.00 21.40           C  
ATOM   1730  O   TRP A 235      30.366  13.062  54.258  1.00 20.73           O  
ATOM   1731  CB  TRP A 235      32.902  13.642  52.186  1.00 18.44           C  
ATOM   1732  CG  TRP A 235      32.913  12.170  52.095  1.00 18.42           C  
ATOM   1733  CD1 TRP A 235      33.984  11.330  52.335  1.00 16.88           C  
ATOM   1734  CD2 TRP A 235      31.815  11.324  51.722  1.00 16.67           C  
ATOM   1735  NE1 TRP A 235      33.603  10.023  52.138  1.00 16.15           N  
ATOM   1736  CE2 TRP A 235      32.284   9.993  51.757  1.00 18.11           C  
ATOM   1737  CE3 TRP A 235      30.477  11.561  51.389  1.00 15.08           C  
ATOM   1738  CZ2 TRP A 235      31.450   8.898  51.467  1.00 18.42           C  
ATOM   1739  CZ3 TRP A 235      29.667  10.490  51.114  1.00 16.14           C  
ATOM   1740  CH2 TRP A 235      30.160   9.171  51.139  1.00 17.32           C  
ATOM   1741  N   VAL A 236      30.186  15.033  53.161  1.00 22.30           N  
ATOM   1742  CA  VAL A 236      28.748  15.039  53.189  1.00 23.86           C  
ATOM   1743  C   VAL A 236      28.285  15.426  51.791  1.00 24.84           C  
ATOM   1744  O   VAL A 236      28.727  16.449  51.242  1.00 24.78           O  
ATOM   1745  CB  VAL A 236      28.221  16.053  54.245  1.00 24.38           C  
ATOM   1746  CG1 VAL A 236      26.717  16.061  54.262  1.00 23.74           C  
ATOM   1747  CG2 VAL A 236      28.857  15.808  55.702  1.00 23.41           C  
ATOM   1748  N   CYS A 237      27.428  14.590  51.218  1.00 25.43           N  
ATOM   1749  CA  CYS A 237      26.791  14.854  49.939  1.00 27.21           C  
ATOM   1750  C   CYS A 237      25.332  15.152  50.155  1.00 27.72           C  
ATOM   1751  O   CYS A 237      24.618  14.318  50.722  1.00 27.90           O  
ATOM   1752  CB  CYS A 237      26.878  13.618  49.061  1.00 27.35           C  
ATOM   1753  SG  CYS A 237      28.498  13.376  48.434  1.00 30.81           S  
HETATM 1754  N   MSE A 238      24.882  16.317  49.690  1.00 27.71           N  
HETATM 1755  CA  MSE A 238      23.512  16.754  49.911  1.00 28.24           C  
HETATM 1756  C   MSE A 238      22.781  16.933  48.581  1.00 28.17           C  
HETATM 1757  O   MSE A 238      23.143  17.832  47.782  1.00 28.24           O  
HETATM 1758  CB  MSE A 238      23.497  18.068  50.694  1.00 28.26           C  
HETATM 1759  CG  MSE A 238      24.349  18.011  51.969  1.00 31.00           C  
HETATM 1760 SE   MSE A 238      24.300  19.645  53.012  0.50 30.10          SE  
HETATM 1761  CE  MSE A 238      22.432  19.737  53.431  1.00 32.81           C  
ATOM   1762  N   VAL A 239      21.739  16.120  48.364  1.00 26.73           N  
ATOM   1763  CA  VAL A 239      21.017  16.119  47.089  1.00 26.50           C  
ATOM   1764  C   VAL A 239      19.511  16.343  47.303  1.00 26.89           C  
ATOM   1765  O   VAL A 239      18.878  15.648  48.115  1.00 25.90           O  
ATOM   1766  CB  VAL A 239      21.246  14.755  46.305  1.00 27.05           C  
ATOM   1767  CG1 VAL A 239      20.286  14.601  45.114  1.00 25.22           C  
ATOM   1768  CG2 VAL A 239      22.738  14.570  45.877  1.00 24.84           C  
ATOM   1769  N   PRO A 240      18.911  17.275  46.537  1.00 27.16           N  
ATOM   1770  CA  PRO A 240      17.448  17.442  46.609  1.00 27.09           C  
ATOM   1771  C   PRO A 240      16.704  16.110  46.516  1.00 27.24           C  
ATOM   1772  O   PRO A 240      16.996  15.266  45.651  1.00 27.32           O  
ATOM   1773  CB  PRO A 240      17.140  18.338  45.412  1.00 26.77           C  
ATOM   1774  CG  PRO A 240      18.377  19.186  45.285  1.00 28.25           C  
ATOM   1775  CD  PRO A 240      19.514  18.196  45.551  1.00 27.49           C  
ATOM   1776  N   SER A 241      15.785  15.898  47.448  1.00 27.07           N  
ATOM   1777  CA  SER A 241      15.055  14.645  47.517  1.00 26.73           C  
ATOM   1778  C   SER A 241      14.127  14.490  46.323  1.00 26.58           C  
ATOM   1779  O   SER A 241      13.784  13.372  45.921  1.00 26.53           O  
ATOM   1780  CB  SER A 241      14.285  14.587  48.815  1.00 26.49           C  
ATOM   1781  OG  SER A 241      15.219  14.526  49.866  1.00 27.41           O  
ATOM   1782  N   ALA A 242      13.743  15.623  45.748  1.00 26.74           N  
ATOM   1783  CA  ALA A 242      12.945  15.631  44.523  1.00 27.49           C  
ATOM   1784  C   ALA A 242      13.681  14.870  43.399  1.00 27.64           C  
ATOM   1785  O   ALA A 242      13.045  14.155  42.621  1.00 27.23           O  
ATOM   1786  CB  ALA A 242      12.599  17.087  44.112  1.00 26.94           C  
ATOM   1787  N   ALA A 243      15.015  15.003  43.355  1.00 28.00           N  
ATOM   1788  CA  ALA A 243      15.863  14.191  42.458  1.00 29.28           C  
ATOM   1789  C   ALA A 243      15.926  12.694  42.793  1.00 30.53           C  
ATOM   1790  O   ALA A 243      16.065  11.854  41.902  1.00 31.50           O  
ATOM   1791  CB  ALA A 243      17.287  14.766  42.382  1.00 29.13           C  
ATOM   1792  N   VAL A 244      15.796  12.349  44.066  1.00 31.66           N  
ATOM   1793  CA  VAL A 244      16.188  11.042  44.526  1.00 32.40           C  
ATOM   1794  C   VAL A 244      15.031  10.061  44.605  1.00 33.59           C  
ATOM   1795  O   VAL A 244      15.198   8.880  44.287  1.00 33.30           O  
ATOM   1796  CB  VAL A 244      16.921  11.145  45.895  1.00 32.84           C  
ATOM   1797  CG1 VAL A 244      17.440   9.757  46.398  1.00 31.26           C  
ATOM   1798  CG2 VAL A 244      18.068  12.108  45.770  1.00 32.45           C  
ATOM   1799  N   GLY A 245      13.863  10.534  45.027  1.00 34.44           N  
ATOM   1800  CA  GLY A 245      12.796   9.616  45.406  1.00 35.83           C  
ATOM   1801  C   GLY A 245      13.051   9.138  46.818  1.00 37.03           C  
ATOM   1802  O   GLY A 245      13.981   9.587  47.467  1.00 36.16           O  
ATOM   1803  N   GLN A 246      12.207   8.247  47.320  1.00 39.15           N  
ATOM   1804  CA  GLN A 246      12.308   7.886  48.734  1.00 41.50           C  
ATOM   1805  C   GLN A 246      13.301   6.757  48.907  1.00 42.27           C  
ATOM   1806  O   GLN A 246      13.094   5.652  48.407  1.00 42.11           O  
ATOM   1807  CB  GLN A 246      10.949   7.550  49.383  1.00 41.42           C  
ATOM   1808  CG  GLN A 246      11.086   7.253  50.884  1.00 41.97           C  
ATOM   1809  CD  GLN A 246       9.778   7.301  51.669  1.00 42.80           C  
ATOM   1810  OE1 GLN A 246       9.248   6.253  52.100  1.00 43.08           O  
ATOM   1811  NE2 GLN A 246       9.266   8.521  51.893  1.00 43.03           N  
ATOM   1812  N   LEU A 247      14.385   7.075  49.605  1.00 43.68           N  
ATOM   1813  CA  LEU A 247      15.457   6.146  49.852  1.00 45.43           C  
ATOM   1814  C   LEU A 247      15.140   5.203  50.987  1.00 46.49           C  
ATOM   1815  O   LEU A 247      15.625   4.069  51.002  1.00 47.04           O  
ATOM   1816  CB  LEU A 247      16.743   6.893  50.176  1.00 45.62           C  
ATOM   1817  CG  LEU A 247      17.635   7.166  48.981  1.00 45.78           C  
ATOM   1818  CD1 LEU A 247      19.071   7.106  49.467  1.00 46.17           C  
ATOM   1819  CD2 LEU A 247      17.396   6.129  47.883  1.00 46.60           C  
ATOM   1820  N   ASP A 248      14.331   5.671  51.934  1.00 47.12           N  
ATOM   1821  CA  ASP A 248      14.069   4.907  53.145  1.00 48.12           C  
ATOM   1822  C   ASP A 248      12.843   5.423  53.864  1.00 47.47           C  
ATOM   1823  O   ASP A 248      12.457   6.563  53.697  1.00 48.09           O  
ATOM   1824  CB  ASP A 248      15.270   5.029  54.082  1.00 48.99           C  
ATOM   1825  CG  ASP A 248      15.582   3.739  54.799  1.00 51.43           C  
ATOM   1826  OD1 ASP A 248      15.487   2.658  54.162  1.00 53.84           O  
ATOM   1827  OD2 ASP A 248      15.947   3.822  56.000  1.00 54.76           O  
ATOM   1828  N   ASN A 249      12.254   4.575  54.682  1.00 46.95           N  
ATOM   1829  CA  ASN A 249      11.080   4.915  55.468  1.00 47.18           C  
ATOM   1830  C   ASN A 249      11.501   5.414  56.846  1.00 46.87           C  
ATOM   1831  O   ASN A 249      10.660   5.694  57.697  1.00 46.65           O  
ATOM   1832  CB  ASN A 249      10.252   3.647  55.642  1.00 47.48           C  
ATOM   1833  CG  ASN A 249      11.124   2.444  55.917  1.00 48.01           C  
ATOM   1834  OD1 ASN A 249      11.445   1.669  55.000  1.00 49.10           O  
ATOM   1835  ND2 ASN A 249      11.566   2.306  57.172  1.00 48.41           N  
ATOM   1836  N   GLU A 250      12.816   5.505  57.042  1.00 46.47           N  
ATOM   1837  CA  GLU A 250      13.423   5.690  58.353  1.00 45.94           C  
ATOM   1838  C   GLU A 250      14.322   6.909  58.382  1.00 44.25           C  
ATOM   1839  O   GLU A 250      14.844   7.320  57.357  1.00 44.43           O  
ATOM   1840  CB  GLU A 250      14.268   4.456  58.722  1.00 46.98           C  
ATOM   1841  CG  GLU A 250      14.448   4.233  60.239  1.00 48.99           C  
ATOM   1842  CD  GLU A 250      13.148   4.487  61.030  1.00 52.45           C  
ATOM   1843  OE1 GLU A 250      12.856   5.675  61.374  1.00 51.03           O  
ATOM   1844  OE2 GLU A 250      12.437   3.484  61.310  1.00 52.68           O  
ATOM   1845  N   ALA A 251      14.474   7.486  59.564  1.00 42.36           N  
ATOM   1846  CA  ALA A 251      15.504   8.464  59.849  1.00 40.32           C  
ATOM   1847  C   ALA A 251      16.290   7.876  61.020  1.00 39.28           C  
ATOM   1848  O   ALA A 251      15.763   7.738  62.127  1.00 39.42           O  
ATOM   1849  CB  ALA A 251      14.878   9.796  60.215  1.00 40.52           C  
ATOM   1850  N   ASP A 252      17.534   7.493  60.752  1.00 37.64           N  
ATOM   1851  CA  ASP A 252      18.370   6.745  61.681  1.00 36.25           C  
ATOM   1852  C   ASP A 252      19.809   7.209  61.439  1.00 34.73           C  
ATOM   1853  O   ASP A 252      20.277   7.228  60.308  1.00 33.61           O  
ATOM   1854  CB  ASP A 252      18.150   5.230  61.424  1.00 37.30           C  
ATOM   1855  CG  ASP A 252      19.242   4.293  62.048  1.00 39.85           C  
ATOM   1856  OD1 ASP A 252      19.985   4.678  62.985  1.00 39.83           O  
ATOM   1857  OD2 ASP A 252      19.337   3.128  61.560  1.00 41.77           O  
ATOM   1858  N   TRP A 253      20.494   7.614  62.508  1.00 33.50           N  
ATOM   1859  CA  TRP A 253      21.890   8.060  62.444  1.00 32.22           C  
ATOM   1860  C   TRP A 253      22.910   6.984  61.994  1.00 32.73           C  
ATOM   1861  O   TRP A 253      24.016   7.332  61.611  1.00 33.05           O  
ATOM   1862  CB  TRP A 253      22.311   8.686  63.778  1.00 30.99           C  
ATOM   1863  CG  TRP A 253      21.688  10.042  64.061  1.00 29.11           C  
ATOM   1864  CD1 TRP A 253      20.809  10.344  65.052  1.00 28.15           C  
ATOM   1865  CD2 TRP A 253      21.904  11.265  63.331  1.00 27.74           C  
ATOM   1866  NE1 TRP A 253      20.467  11.686  64.997  1.00 28.15           N  
ATOM   1867  CE2 TRP A 253      21.119  12.266  63.944  1.00 27.40           C  
ATOM   1868  CE3 TRP A 253      22.703  11.614  62.236  1.00 27.87           C  
ATOM   1869  CZ2 TRP A 253      21.112  13.594  63.502  1.00 28.76           C  
ATOM   1870  CZ3 TRP A 253      22.699  12.947  61.796  1.00 28.16           C  
ATOM   1871  CH2 TRP A 253      21.900  13.911  62.424  1.00 28.34           C  
ATOM   1872  N   ASN A 254      22.518   5.703  62.009  1.00 32.96           N  
ATOM   1873  CA AASN A 254      23.403   4.617  61.597  0.50 33.04           C  
ATOM   1874  CA BASN A 254      23.382   4.585  61.609  0.50 33.85           C  
ATOM   1875  C   ASN A 254      22.841   3.814  60.395  1.00 33.79           C  
ATOM   1876  O   ASN A 254      22.952   2.591  60.338  1.00 33.85           O  
ATOM   1877  CB AASN A 254      23.678   3.715  62.816  0.50 32.61           C  
ATOM   1878  CB BASN A 254      23.554   3.556  62.750  0.50 34.17           C  
ATOM   1879  CG AASN A 254      24.948   2.883  62.685  0.50 31.21           C  
ATOM   1880  CG BASN A 254      23.986   4.168  64.065  0.50 35.88           C  
ATOM   1881  OD1AASN A 254      25.951   3.310  62.114  0.50 28.64           O  
ATOM   1882  OD1BASN A 254      24.493   5.284  64.116  0.50 39.77           O  
ATOM   1883  ND2AASN A 254      24.907   1.679  63.252  0.50 31.20           N  
ATOM   1884  ND2BASN A 254      23.797   3.421  65.145  0.50 37.14           N  
ATOM   1885  N   ARG A 255      22.227   4.490  59.427  1.00 34.09           N  
ATOM   1886  CA  ARG A 255      21.743   3.762  58.234  1.00 34.94           C  
ATOM   1887  C   ARG A 255      22.780   3.703  57.106  1.00 34.57           C  
ATOM   1888  O   ARG A 255      23.123   4.732  56.520  1.00 34.30           O  
ATOM   1889  CB  ARG A 255      20.431   4.336  57.712  1.00 35.11           C  
ATOM   1890  CG  ARG A 255      19.222   3.506  58.082  1.00 40.55           C  
ATOM   1891  CD  ARG A 255      18.678   2.712  56.866  1.00 45.54           C  
ATOM   1892  NE  ARG A 255      17.755   1.631  57.252  1.00 49.69           N  
ATOM   1893  CZ  ARG A 255      18.034   0.323  57.165  1.00 53.62           C  
ATOM   1894  NH1 ARG A 255      19.211  -0.109  56.695  1.00 55.63           N  
ATOM   1895  NH2 ARG A 255      17.136  -0.576  57.543  1.00 54.97           N  
ATOM   1896  N   ASP A 256      23.271   2.501  56.813  1.00 34.60           N  
ATOM   1897  CA  ASP A 256      24.207   2.297  55.701  1.00 35.89           C  
ATOM   1898  C   ASP A 256      23.602   2.729  54.353  1.00 34.95           C  
ATOM   1899  O   ASP A 256      22.444   2.386  54.026  1.00 34.11           O  
ATOM   1900  CB  ASP A 256      24.706   0.843  55.637  1.00 36.83           C  
ATOM   1901  CG  ASP A 256      23.574  -0.160  55.450  1.00 42.24           C  
ATOM   1902  OD1 ASP A 256      22.749  -0.342  56.390  1.00 47.63           O  
ATOM   1903  OD2 ASP A 256      23.500  -0.778  54.354  1.00 47.25           O  
ATOM   1904  N   GLY A 257      24.384   3.511  53.606  1.00 33.57           N  
ATOM   1905  CA  GLY A 257      23.962   4.027  52.312  1.00 32.78           C  
ATOM   1906  C   GLY A 257      24.664   3.256  51.217  1.00 32.70           C  
ATOM   1907  O   GLY A 257      25.466   2.353  51.504  1.00 31.59           O  
ATOM   1908  N   ARG A 258      24.385   3.633  49.969  1.00 32.88           N  
ATOM   1909  CA  ARG A 258      24.860   2.909  48.787  1.00 33.39           C  
ATOM   1910  C   ARG A 258      25.631   3.791  47.840  1.00 33.03           C  
ATOM   1911  O   ARG A 258      25.146   4.830  47.404  1.00 32.93           O  
ATOM   1912  CB  ARG A 258      23.693   2.315  48.002  1.00 34.38           C  
ATOM   1913  CG  ARG A 258      23.005   1.140  48.622  1.00 37.18           C  
ATOM   1914  CD  ARG A 258      21.659   0.990  47.935  1.00 44.24           C  
ATOM   1915  NE  ARG A 258      21.747   0.154  46.731  1.00 49.04           N  
ATOM   1916  CZ  ARG A 258      21.213   0.437  45.537  1.00 49.27           C  
ATOM   1917  NH1 ARG A 258      20.530   1.558  45.331  1.00 45.67           N  
ATOM   1918  NH2 ARG A 258      21.367  -0.432  44.541  1.00 49.51           N  
ATOM   1919  N   LEU A 259      26.834   3.359  47.497  1.00 33.56           N  
ATOM   1920  CA  LEU A 259      27.642   4.062  46.508  1.00 33.94           C  
ATOM   1921  C   LEU A 259      26.851   4.328  45.223  1.00 34.11           C  
ATOM   1922  O   LEU A 259      26.914   5.419  44.659  1.00 34.27           O  
ATOM   1923  CB  LEU A 259      28.935   3.295  46.245  1.00 33.81           C  
ATOM   1924  CG  LEU A 259      29.941   3.885  45.258  1.00 33.69           C  
ATOM   1925  CD1 LEU A 259      30.258   5.352  45.577  1.00 30.84           C  
ATOM   1926  CD2 LEU A 259      31.182   3.036  45.327  1.00 31.89           C  
ATOM   1927  N   GLU A 260      26.043   3.358  44.818  1.00 34.70           N  
ATOM   1928  CA  GLU A 260      25.269   3.464  43.578  1.00 35.96           C  
ATOM   1929  C   GLU A 260      24.160   4.531  43.626  1.00 35.34           C  
ATOM   1930  O   GLU A 260      23.793   5.076  42.589  1.00 35.30           O  
ATOM   1931  CB  GLU A 260      24.733   2.086  43.103  1.00 37.01           C  
ATOM   1932  CG  GLU A 260      24.687   0.945  44.186  1.00 39.40           C  
ATOM   1933  CD  GLU A 260      26.090   0.527  44.700  1.00 42.66           C  
ATOM   1934  OE1 GLU A 260      27.003   0.307  43.853  1.00 43.23           O  
ATOM   1935  OE2 GLU A 260      26.273   0.423  45.946  1.00 40.94           O  
ATOM   1936  N   ASP A 261      23.642   4.841  44.816  1.00 34.80           N  
ATOM   1937  CA  ASP A 261      22.636   5.911  44.953  1.00 33.56           C  
ATOM   1938  C   ASP A 261      23.196   7.326  44.874  1.00 33.07           C  
ATOM   1939  O   ASP A 261      22.528   8.237  44.356  1.00 32.35           O  
ATOM   1940  CB  ASP A 261      21.897   5.784  46.269  1.00 33.71           C  
ATOM   1941  CG  ASP A 261      21.074   4.559  46.336  1.00 34.15           C  
ATOM   1942  OD1 ASP A 261      20.657   4.112  45.256  1.00 35.93           O  
ATOM   1943  OD2 ASP A 261      20.856   4.037  47.451  1.00 33.54           O  
ATOM   1944  N   VAL A 262      24.395   7.524  45.430  1.00 32.14           N  
ATOM   1945  CA  VAL A 262      24.950   8.890  45.534  1.00 31.74           C  
ATOM   1946  C   VAL A 262      25.842   9.259  44.339  1.00 31.31           C  
ATOM   1947  O   VAL A 262      25.693  10.338  43.773  1.00 30.71           O  
ATOM   1948  CB  VAL A 262      25.613   9.192  46.944  1.00 31.31           C  
ATOM   1949  CG1 VAL A 262      26.581   8.110  47.363  1.00 30.61           C  
ATOM   1950  CG2 VAL A 262      26.257  10.561  46.972  1.00 30.31           C  
ATOM   1951  N   LEU A 263      26.710   8.329  43.937  1.00 31.44           N  
ATOM   1952  CA  LEU A 263      27.666   8.557  42.843  1.00 31.55           C  
ATOM   1953  C   LEU A 263      27.062   9.176  41.577  1.00 31.71           C  
ATOM   1954  O   LEU A 263      27.595  10.191  41.095  1.00 31.82           O  
ATOM   1955  CB  LEU A 263      28.463   7.298  42.498  1.00 31.14           C  
ATOM   1956  CG  LEU A 263      29.717   7.488  41.634  1.00 31.42           C  
ATOM   1957  CD1 LEU A 263      30.500   8.769  41.940  1.00 30.45           C  
ATOM   1958  CD2 LEU A 263      30.622   6.279  41.824  1.00 32.13           C  
ATOM   1959  N   PRO A 264      25.939   8.605  41.053  1.00 31.48           N  
ATOM   1960  CA  PRO A 264      25.403   9.152  39.815  1.00 31.14           C  
ATOM   1961  C   PRO A 264      25.298  10.659  39.875  1.00 31.17           C  
ATOM   1962  O   PRO A 264      25.466  11.307  38.850  1.00 31.78           O  
ATOM   1963  CB  PRO A 264      24.011   8.547  39.738  1.00 31.56           C  
ATOM   1964  CG  PRO A 264      24.161   7.238  40.415  1.00 31.53           C  
ATOM   1965  CD  PRO A 264      25.119   7.482  41.542  1.00 30.90           C  
ATOM   1966  N   PHE A 265      25.061  11.215  41.064  1.00 31.08           N  
ATOM   1967  CA  PHE A 265      24.880  12.671  41.225  1.00 30.42           C  
ATOM   1968  C   PHE A 265      26.158  13.483  41.164  1.00 30.50           C  
ATOM   1969  O   PHE A 265      26.123  14.710  40.989  1.00 30.27           O  
ATOM   1970  CB  PHE A 265      24.131  12.981  42.526  1.00 30.08           C  
ATOM   1971  CG  PHE A 265      22.698  12.522  42.510  1.00 29.49           C  
ATOM   1972  CD1 PHE A 265      21.724  13.244  41.798  1.00 27.81           C  
ATOM   1973  CD2 PHE A 265      22.325  11.365  43.184  1.00 27.77           C  
ATOM   1974  CE1 PHE A 265      20.394  12.822  41.757  1.00 25.93           C  
ATOM   1975  CE2 PHE A 265      20.992  10.936  43.165  1.00 28.20           C  
ATOM   1976  CZ  PHE A 265      20.024  11.669  42.447  1.00 27.98           C  
ATOM   1977  N   PHE A 266      27.287  12.804  41.305  1.00 30.42           N  
ATOM   1978  CA  PHE A 266      28.543  13.506  41.399  1.00 31.24           C  
ATOM   1979  C   PHE A 266      29.505  13.157  40.269  1.00 32.33           C  
ATOM   1980  O   PHE A 266      30.575  13.757  40.154  1.00 32.55           O  
ATOM   1981  CB  PHE A 266      29.153  13.308  42.791  1.00 29.89           C  
ATOM   1982  CG  PHE A 266      28.422  14.069  43.860  1.00 29.58           C  
ATOM   1983  CD1 PHE A 266      27.297  13.519  44.486  1.00 26.50           C  
ATOM   1984  CD2 PHE A 266      28.820  15.363  44.203  1.00 26.18           C  
ATOM   1985  CE1 PHE A 266      26.603  14.250  45.435  1.00 25.43           C  
ATOM   1986  CE2 PHE A 266      28.151  16.079  45.166  1.00 22.68           C  
ATOM   1987  CZ  PHE A 266      27.044  15.528  45.789  1.00 26.16           C  
ATOM   1988  N   ALA A 267      29.070  12.234  39.417  1.00 33.34           N  
ATOM   1989  CA  ALA A 267      29.906  11.582  38.419  1.00 34.43           C  
ATOM   1990  C   ALA A 267      30.377  12.536  37.334  1.00 35.28           C  
ATOM   1991  O   ALA A 267      31.482  12.356  36.809  1.00 35.99           O  
ATOM   1992  CB  ALA A 267      29.147  10.404  37.792  1.00 34.36           C  
ATOM   1993  N   ASP A 268      29.548  13.525  36.997  1.00 35.61           N  
ATOM   1994  CA  ASP A 268      29.877  14.536  35.979  1.00 37.33           C  
ATOM   1995  C   ASP A 268      30.873  15.603  36.480  1.00 36.98           C  
ATOM   1996  O   ASP A 268      31.235  16.517  35.729  1.00 36.46           O  
ATOM   1997  CB  ASP A 268      28.608  15.302  35.513  1.00 38.50           C  
ATOM   1998  CG  ASP A 268      27.724  14.510  34.503  1.00 42.24           C  
ATOM   1999  OD1 ASP A 268      28.174  13.510  33.887  1.00 46.14           O  
ATOM   2000  OD2 ASP A 268      26.549  14.926  34.307  1.00 45.49           O  
ATOM   2001  N   TRP A 269      31.270  15.527  37.752  1.00 36.63           N  
ATOM   2002  CA  TRP A 269      32.061  16.598  38.340  1.00 36.02           C  
ATOM   2003  C   TRP A 269      33.477  16.488  37.815  1.00 35.94           C  
ATOM   2004  O   TRP A 269      34.012  15.396  37.647  1.00 35.93           O  
ATOM   2005  CB  TRP A 269      32.014  16.577  39.881  1.00 35.26           C  
ATOM   2006  CG  TRP A 269      30.705  17.119  40.458  1.00 36.51           C  
ATOM   2007  CD1 TRP A 269      29.437  16.982  39.917  1.00 35.13           C  
ATOM   2008  CD2 TRP A 269      30.526  17.845  41.692  1.00 35.68           C  
ATOM   2009  NE1 TRP A 269      28.508  17.577  40.739  1.00 34.93           N  
ATOM   2010  CE2 TRP A 269      29.147  18.121  41.824  1.00 35.41           C  
ATOM   2011  CE3 TRP A 269      31.392  18.287  42.691  1.00 34.58           C  
ATOM   2012  CZ2 TRP A 269      28.627  18.834  42.909  1.00 34.97           C  
ATOM   2013  CZ3 TRP A 269      30.868  18.991  43.769  1.00 34.67           C  
ATOM   2014  CH2 TRP A 269      29.500  19.255  43.866  1.00 34.96           C  
ATOM   2015  N   ASP A 270      34.075  17.628  37.534  1.00 36.18           N  
ATOM   2016  CA  ASP A 270      35.465  17.660  37.148  1.00 36.31           C  
ATOM   2017  C   ASP A 270      36.086  18.847  37.849  1.00 35.27           C  
ATOM   2018  O   ASP A 270      36.184  19.928  37.297  1.00 35.61           O  
ATOM   2019  CB  ASP A 270      35.612  17.719  35.614  1.00 36.94           C  
ATOM   2020  CG  ASP A 270      37.085  17.542  35.132  1.00 39.51           C  
ATOM   2021  OD1 ASP A 270      38.017  17.470  35.968  1.00 40.37           O  
ATOM   2022  OD2 ASP A 270      37.305  17.489  33.890  1.00 42.10           O  
ATOM   2023  N   LEU A 271      36.500  18.632  39.089  1.00 34.48           N  
ATOM   2024  CA  LEU A 271      37.091  19.702  39.883  1.00 33.99           C  
ATOM   2025  C   LEU A 271      38.606  19.893  39.566  1.00 33.83           C  
ATOM   2026  O   LEU A 271      39.222  20.913  39.927  1.00 33.25           O  
ATOM   2027  CB  LEU A 271      36.803  19.464  41.371  1.00 33.58           C  
ATOM   2028  CG  LEU A 271      35.467  19.940  41.997  1.00 33.98           C  
ATOM   2029  CD1 LEU A 271      34.249  19.966  41.074  1.00 33.18           C  
ATOM   2030  CD2 LEU A 271      35.144  19.140  43.230  1.00 34.06           C  
ATOM   2031  N   GLY A 272      39.187  18.923  38.860  1.00 33.12           N  
ATOM   2032  CA  GLY A 272      40.590  19.003  38.476  1.00 32.49           C  
ATOM   2033  C   GLY A 272      41.537  18.565  39.586  1.00 31.90           C  
ATOM   2034  O   GLY A 272      42.122  17.480  39.512  1.00 31.88           O  
ATOM   2035  N   TRP A 273      41.679  19.392  40.622  1.00 31.37           N  
ATOM   2036  CA  TRP A 273      42.582  19.077  41.728  1.00 31.06           C  
ATOM   2037  C   TRP A 273      42.015  18.050  42.734  1.00 31.28           C  
ATOM   2038  O   TRP A 273      42.771  17.287  43.321  1.00 30.44           O  
ATOM   2039  CB  TRP A 273      43.057  20.346  42.408  1.00 30.57           C  
ATOM   2040  CG  TRP A 273      41.997  21.048  43.188  1.00 31.13           C  
ATOM   2041  CD1 TRP A 273      41.161  22.037  42.748  1.00 30.02           C  
ATOM   2042  CD2 TRP A 273      41.665  20.827  44.560  1.00 31.51           C  
ATOM   2043  NE1 TRP A 273      40.329  22.443  43.758  1.00 29.66           N  
ATOM   2044  CE2 TRP A 273      40.622  21.726  44.888  1.00 30.91           C  
ATOM   2045  CE3 TRP A 273      42.145  19.953  45.547  1.00 31.35           C  
ATOM   2046  CZ2 TRP A 273      40.044  21.773  46.162  1.00 30.63           C  
ATOM   2047  CZ3 TRP A 273      41.566  19.998  46.820  1.00 31.00           C  
ATOM   2048  CH2 TRP A 273      40.528  20.904  47.113  1.00 30.64           C  
ATOM   2049  N   PHE A 274      40.689  18.014  42.882  1.00 32.13           N  
ATOM   2050  CA  PHE A 274      39.986  17.161  43.842  1.00 32.20           C  
ATOM   2051  C   PHE A 274      39.076  16.206  43.056  1.00 33.10           C  
ATOM   2052  O   PHE A 274      38.232  16.665  42.282  1.00 33.37           O  
ATOM   2053  CB  PHE A 274      39.168  18.063  44.770  1.00 32.35           C  
ATOM   2054  CG  PHE A 274      38.577  17.381  45.982  1.00 32.22           C  
ATOM   2055  CD1 PHE A 274      38.909  16.081  46.339  1.00 32.94           C  
ATOM   2056  CD2 PHE A 274      37.685  18.085  46.801  1.00 35.23           C  
ATOM   2057  CE1 PHE A 274      38.348  15.460  47.495  1.00 32.83           C  
ATOM   2058  CE2 PHE A 274      37.110  17.483  47.966  1.00 34.02           C  
ATOM   2059  CZ  PHE A 274      37.448  16.161  48.306  1.00 33.12           C  
ATOM   2060  N   ASP A 275      39.257  14.893  43.249  1.00 33.20           N  
ATOM   2061  CA  ASP A 275      38.453  13.854  42.574  1.00 33.44           C  
ATOM   2062  C   ASP A 275      37.300  13.291  43.447  1.00 32.73           C  
ATOM   2063  O   ASP A 275      37.503  12.400  44.295  1.00 32.54           O  
ATOM   2064  CB  ASP A 275      39.367  12.716  42.073  1.00 33.68           C  
ATOM   2065  CG  ASP A 275      38.599  11.626  41.314  1.00 36.12           C  
ATOM   2066  OD1 ASP A 275      37.383  11.778  41.071  1.00 39.59           O  
ATOM   2067  OD2 ASP A 275      39.204  10.588  40.976  1.00 38.89           O  
ATOM   2068  N   ILE A 276      36.094  13.801  43.213  1.00 32.35           N  
ATOM   2069  CA  ILE A 276      34.887  13.403  43.981  1.00 31.88           C  
ATOM   2070  C   ILE A 276      34.474  11.953  43.777  1.00 31.84           C  
ATOM   2071  O   ILE A 276      34.075  11.278  44.733  1.00 31.92           O  
ATOM   2072  CB  ILE A 276      33.688  14.342  43.717  1.00 31.91           C  
ATOM   2073  CG1 ILE A 276      34.110  15.807  43.909  1.00 31.99           C  
ATOM   2074  CG2 ILE A 276      32.485  13.972  44.621  1.00 31.02           C  
ATOM   2075  CD1 ILE A 276      35.071  16.086  45.143  1.00 33.52           C  
ATOM   2076  N   ARG A 277      34.589  11.464  42.545  1.00 31.86           N  
ATOM   2077  CA  ARG A 277      34.393  10.051  42.292  1.00 32.41           C  
ATOM   2078  C   ARG A 277      35.313   9.249  43.215  1.00 30.94           C  
ATOM   2079  O   ARG A 277      34.844   8.387  43.940  1.00 30.28           O  
ATOM   2080  CB  ARG A 277      34.621   9.693  40.826  1.00 32.30           C  
ATOM   2081  CG  ARG A 277      34.375   8.202  40.540  1.00 34.83           C  
ATOM   2082  CD  ARG A 277      34.721   7.794  39.074  1.00 35.80           C  
ATOM   2083  NE  ARG A 277      33.659   8.159  38.126  1.00 41.62           N  
ATOM   2084  CZ  ARG A 277      32.565   7.430  37.917  1.00 43.15           C  
ATOM   2085  NH1 ARG A 277      32.390   6.291  38.587  1.00 43.10           N  
ATOM   2086  NH2 ARG A 277      31.649   7.841  37.042  1.00 43.64           N  
ATOM   2087  N   ASP A 278      36.604   9.567  43.221  1.00 30.10           N  
ATOM   2088  CA  ASP A 278      37.571   8.838  44.084  1.00 29.53           C  
ATOM   2089  C   ASP A 278      37.182   8.919  45.566  1.00 28.60           C  
ATOM   2090  O   ASP A 278      37.237   7.925  46.297  1.00 28.17           O  
ATOM   2091  CB  ASP A 278      38.997   9.376  43.836  1.00 29.95           C  
ATOM   2092  CG  ASP A 278      39.972   9.037  44.936  1.00 30.22           C  
ATOM   2093  OD1 ASP A 278      40.381   7.853  45.004  1.00 32.26           O  
ATOM   2094  OD2 ASP A 278      40.346   9.965  45.705  1.00 29.55           O  
ATOM   2095  N   LEU A 279      36.752  10.112  45.981  1.00 27.90           N  
ATOM   2096  CA  LEU A 279      36.390  10.388  47.364  1.00 26.82           C  
ATOM   2097  C   LEU A 279      35.248   9.473  47.837  1.00 27.19           C  
ATOM   2098  O   LEU A 279      35.342   8.848  48.910  1.00 27.10           O  
ATOM   2099  CB  LEU A 279      36.062  11.875  47.526  1.00 26.22           C  
ATOM   2100  CG  LEU A 279      35.419  12.333  48.844  1.00 27.66           C  
ATOM   2101  CD1 LEU A 279      36.467  12.353  49.982  1.00 22.39           C  
ATOM   2102  CD2 LEU A 279      34.660  13.717  48.680  1.00 25.54           C  
ATOM   2103  N   LEU A 280      34.197   9.368  47.023  1.00 27.24           N  
ATOM   2104  CA  LEU A 280      33.061   8.476  47.319  1.00 27.24           C  
ATOM   2105  C   LEU A 280      33.421   7.018  47.189  1.00 27.24           C  
ATOM   2106  O   LEU A 280      32.955   6.183  47.973  1.00 27.92           O  
ATOM   2107  CB  LEU A 280      31.870   8.764  46.391  1.00 27.31           C  
ATOM   2108  CG  LEU A 280      31.213  10.159  46.462  1.00 26.75           C  
ATOM   2109  CD1 LEU A 280      29.845  10.177  45.786  1.00 23.87           C  
ATOM   2110  CD2 LEU A 280      31.060  10.556  47.893  1.00 27.25           C  
ATOM   2111  N   THR A 281      34.236   6.713  46.182  1.00 27.07           N  
ATOM   2112  CA  THR A 281      34.561   5.342  45.797  1.00 26.68           C  
ATOM   2113  C   THR A 281      35.463   4.685  46.823  1.00 26.92           C  
ATOM   2114  O   THR A 281      35.378   3.484  47.050  1.00 27.55           O  
ATOM   2115  CB  THR A 281      35.213   5.294  44.368  1.00 26.57           C  
ATOM   2116  OG1 THR A 281      34.324   5.904  43.433  1.00 26.56           O  
ATOM   2117  CG2 THR A 281      35.455   3.878  43.900  1.00 25.33           C  
ATOM   2118  N   ARG A 282      36.329   5.457  47.462  1.00 27.45           N  
ATOM   2119  CA  ARG A 282      37.235   4.844  48.430  1.00 27.62           C  
ATOM   2120  C   ARG A 282      36.742   5.014  49.874  1.00 28.18           C  
ATOM   2121  O   ARG A 282      37.525   4.906  50.825  1.00 28.66           O  
ATOM   2122  CB  ARG A 282      38.669   5.364  48.251  1.00 27.45           C  
ATOM   2123  CG  ARG A 282      39.430   4.803  47.051  1.00 26.81           C  
ATOM   2124  CD  ARG A 282      40.881   5.315  47.010  1.00 27.21           C  
ATOM   2125  NE  ARG A 282      40.963   6.777  47.140  1.00 25.04           N  
ATOM   2126  CZ  ARG A 282      41.318   7.413  48.261  1.00 26.11           C  
ATOM   2127  NH1 ARG A 282      41.630   6.720  49.352  1.00 24.13           N  
ATOM   2128  NH2 ARG A 282      41.336   8.745  48.307  1.00 26.56           N  
ATOM   2129  N   ASN A 283      35.446   5.266  50.030  1.00 28.30           N  
ATOM   2130  CA  ASN A 283      34.867   5.472  51.331  1.00 28.99           C  
ATOM   2131  C   ASN A 283      35.207   4.264  52.177  1.00 30.20           C  
ATOM   2132  O   ASN A 283      35.537   3.212  51.638  1.00 31.02           O  
ATOM   2133  CB  ASN A 283      33.350   5.699  51.245  1.00 28.52           C  
ATOM   2134  CG  ASN A 283      32.584   4.417  51.019  1.00 26.75           C  
ATOM   2135  OD1 ASN A 283      32.316   3.664  51.961  1.00 26.82           O  
ATOM   2136  ND2 ASN A 283      32.239   4.149  49.769  1.00 23.24           N  
ATOM   2137  N   GLN A 284      35.187   4.438  53.493  1.00 30.93           N  
ATOM   2138  CA  GLN A 284      35.348   3.343  54.420  1.00 32.37           C  
ATOM   2139  C   GLN A 284      33.981   3.030  54.966  1.00 32.52           C  
ATOM   2140  O   GLN A 284      33.776   2.002  55.621  1.00 33.48           O  
ATOM   2141  CB  GLN A 284      36.268   3.757  55.564  1.00 32.89           C  
ATOM   2142  CG  GLN A 284      37.657   4.087  55.090  1.00 37.15           C  
ATOM   2143  CD  GLN A 284      38.626   4.112  56.214  1.00 42.34           C  
ATOM   2144  OE1 GLN A 284      38.615   5.034  57.046  1.00 43.81           O  
ATOM   2145  NE2 GLN A 284      39.481   3.089  56.270  1.00 42.74           N  
ATOM   2146  N   LEU A 285      33.045   3.930  54.667  1.00 32.37           N  
ATOM   2147  CA  LEU A 285      31.712   3.968  55.261  1.00 31.56           C  
ATOM   2148  C   LEU A 285      30.913   4.973  54.444  1.00 30.26           C  
ATOM   2149  O   LEU A 285      31.403   6.058  54.144  1.00 29.80           O  
ATOM   2150  CB  LEU A 285      31.791   4.451  56.722  1.00 31.58           C  
ATOM   2151  CG  LEU A 285      30.478   4.363  57.502  1.00 33.92           C  
ATOM   2152  CD1 LEU A 285      30.133   2.869  57.824  1.00 35.72           C  
ATOM   2153  CD2 LEU A 285      30.479   5.202  58.783  1.00 32.00           C  
ATOM   2154  N   ILE A 286      29.710   4.567  54.054  1.00 29.51           N  
ATOM   2155  CA  ILE A 286      28.654   5.447  53.577  1.00 28.89           C  
ATOM   2156  C   ILE A 286      27.438   5.251  54.455  1.00 27.64           C  
ATOM   2157  O   ILE A 286      27.000   4.120  54.686  1.00 27.08           O  
ATOM   2158  CB  ILE A 286      28.206   5.170  52.108  1.00 29.41           C  
ATOM   2159  CG1 ILE A 286      29.381   5.199  51.157  1.00 30.49           C  
ATOM   2160  CG2 ILE A 286      27.236   6.253  51.641  1.00 27.95           C  
ATOM   2161  CD1 ILE A 286      28.956   5.403  49.716  1.00 32.59           C  
ATOM   2162  N   LEU A 287      26.900   6.365  54.928  1.00 27.34           N  
ATOM   2163  CA  LEU A 287      25.618   6.397  55.611  1.00 27.45           C  
ATOM   2164  C   LEU A 287      24.642   7.328  54.889  1.00 27.45           C  
ATOM   2165  O   LEU A 287      25.054   8.330  54.295  1.00 28.45           O  
ATOM   2166  CB  LEU A 287      25.803   6.852  57.063  1.00 27.89           C  
ATOM   2167  CG  LEU A 287      26.763   6.073  57.969  1.00 27.42           C  
ATOM   2168  CD1 LEU A 287      27.155   6.928  59.179  1.00 26.96           C  
ATOM   2169  CD2 LEU A 287      26.194   4.702  58.384  1.00 25.85           C  
ATOM   2170  N   GLN A 288      23.354   7.012  54.943  1.00 26.60           N  
ATOM   2171  CA  GLN A 288      22.351   7.887  54.349  1.00 26.70           C  
ATOM   2172  C   GLN A 288      21.457   8.406  55.466  1.00 26.82           C  
ATOM   2173  O   GLN A 288      21.228   7.713  56.480  1.00 26.82           O  
ATOM   2174  CB  GLN A 288      21.496   7.181  53.267  1.00 26.12           C  
ATOM   2175  CG  GLN A 288      20.783   5.909  53.787  1.00 27.15           C  
ATOM   2176  CD  GLN A 288      20.177   5.049  52.698  1.00 28.19           C  
ATOM   2177  OE1 GLN A 288      20.721   4.921  51.590  1.00 29.88           O  
ATOM   2178  NE2 GLN A 288      19.040   4.449  53.003  1.00 28.96           N  
ATOM   2179  N   TYR A 289      20.942   9.613  55.253  1.00 26.43           N  
ATOM   2180  CA  TYR A 289      20.083  10.276  56.188  1.00 26.30           C  
ATOM   2181  C   TYR A 289      19.268  11.372  55.473  1.00 26.41           C  
ATOM   2182  O   TYR A 289      19.844  12.208  54.791  1.00 25.44           O  
ATOM   2183  CB  TYR A 289      20.964  10.880  57.259  1.00 26.25           C  
ATOM   2184  CG  TYR A 289      20.242  11.491  58.443  1.00 27.25           C  
ATOM   2185  CD1 TYR A 289      19.563  10.682  59.376  1.00 23.21           C  
ATOM   2186  CD2 TYR A 289      20.278  12.876  58.650  1.00 26.16           C  
ATOM   2187  CE1 TYR A 289      18.931  11.231  60.467  1.00 25.39           C  
ATOM   2188  CE2 TYR A 289      19.642  13.443  59.749  1.00 27.72           C  
ATOM   2189  CZ  TYR A 289      18.976  12.612  60.655  1.00 27.05           C  
ATOM   2190  OH  TYR A 289      18.370  13.173  61.744  1.00 27.11           O  
ATOM   2191  N   PRO A 290      17.927  11.378  55.653  1.00 27.11           N  
ATOM   2192  CA  PRO A 290      17.117  12.460  55.100  1.00 28.18           C  
ATOM   2193  C   PRO A 290      17.187  13.675  56.033  1.00 29.61           C  
ATOM   2194  O   PRO A 290      17.025  13.551  57.248  1.00 30.24           O  
ATOM   2195  CB  PRO A 290      15.696  11.867  55.074  1.00 28.00           C  
ATOM   2196  CG  PRO A 290      15.668  10.863  56.198  1.00 27.87           C  
ATOM   2197  CD  PRO A 290      17.112  10.413  56.429  1.00 27.27           C  
HETATM 2198  N   MSE A 291      17.423  14.841  55.476  1.00 31.11           N  
HETATM 2199  CA  MSE A 291      17.588  16.029  56.278  1.00 34.82           C  
HETATM 2200  C   MSE A 291      16.282  16.425  56.985  1.00 31.33           C  
HETATM 2201  O   MSE A 291      15.354  16.960  56.372  1.00 31.51           O  
HETATM 2202  CB  MSE A 291      18.087  17.144  55.386  1.00 33.84           C  
HETATM 2203  CG  MSE A 291      18.950  18.130  56.084  1.00 38.55           C  
HETATM 2204 SE   MSE A 291      19.183  19.737  54.991  1.00 50.16          SE  
HETATM 2205  CE  MSE A 291      17.289  20.164  54.662  1.00 46.24           C  
ATOM   2206  N   VAL A 292      16.224  16.151  58.280  1.00 28.91           N  
ATOM   2207  CA  VAL A 292      15.003  16.344  59.046  1.00 26.89           C  
ATOM   2208  C   VAL A 292      15.205  17.248  60.247  1.00 25.33           C  
ATOM   2209  O   VAL A 292      16.291  17.347  60.798  1.00 24.82           O  
ATOM   2210  CB  VAL A 292      14.329  14.981  59.510  1.00 27.01           C  
ATOM   2211  CG1 VAL A 292      13.815  14.166  58.325  1.00 25.83           C  
ATOM   2212  CG2 VAL A 292      15.280  14.150  60.394  1.00 26.86           C  
ATOM   2213  N   ASP A 293      14.140  17.934  60.618  1.00 24.04           N  
ATOM   2214  CA  ASP A 293      14.096  18.675  61.843  1.00 23.61           C  
ATOM   2215  C   ASP A 293      12.733  18.443  62.493  1.00 23.80           C  
ATOM   2216  O   ASP A 293      11.946  17.614  62.036  1.00 22.28           O  
ATOM   2217  CB  ASP A 293      14.343  20.168  61.589  1.00 23.27           C  
ATOM   2218  CG  ASP A 293      13.204  20.848  60.811  1.00 24.38           C  
ATOM   2219  OD1 ASP A 293      12.195  20.189  60.496  1.00 23.54           O  
ATOM   2220  OD2 ASP A 293      13.320  22.055  60.516  1.00 24.99           O  
ATOM   2221  N   ARG A 294      12.469  19.210  63.550  1.00 24.01           N  
ATOM   2222  CA  ARG A 294      11.163  19.265  64.176  1.00 24.54           C  
ATOM   2223  C   ARG A 294      10.732  20.710  64.306  1.00 25.43           C  
ATOM   2224  O   ARG A 294      11.576  21.622  64.513  1.00 25.89           O  
ATOM   2225  CB  ARG A 294      11.213  18.641  65.567  1.00 24.01           C  
ATOM   2226  CG  ARG A 294      11.383  17.158  65.559  1.00 21.68           C  
ATOM   2227  CD  ARG A 294      11.110  16.631  66.946  1.00 21.43           C  
ATOM   2228  NE  ARG A 294      11.514  15.238  67.086  1.00 22.84           N  
ATOM   2229  CZ  ARG A 294      10.765  14.203  66.704  1.00 23.10           C  
ATOM   2230  NH1 ARG A 294       9.571  14.408  66.157  1.00 22.69           N  
ATOM   2231  NH2 ARG A 294      11.221  12.963  66.859  1.00 22.33           N  
ATOM   2232  N   ASP A 295       9.423  20.919  64.187  1.00 25.68           N  
ATOM   2233  CA  ASP A 295       8.824  22.231  64.378  1.00 26.32           C  
ATOM   2234  C   ASP A 295       9.231  22.881  65.720  1.00 26.41           C  
ATOM   2235  O   ASP A 295       9.445  22.195  66.727  1.00 25.53           O  
ATOM   2236  CB  ASP A 295       7.299  22.110  64.259  1.00 27.26           C  
ATOM   2237  CG  ASP A 295       6.826  21.839  62.794  1.00 30.47           C  
ATOM   2238  OD1 ASP A 295       7.638  21.924  61.809  1.00 29.87           O  
ATOM   2239  OD2 ASP A 295       5.616  21.537  62.644  1.00 34.17           O  
ATOM   2240  N   PRO A 296       9.419  24.212  65.716  1.00 26.46           N  
ATOM   2241  CA  PRO A 296       9.577  25.003  66.950  1.00 26.39           C  
ATOM   2242  C   PRO A 296       8.466  24.713  67.956  1.00 26.48           C  
ATOM   2243  O   PRO A 296       7.293  24.803  67.599  1.00 27.42           O  
ATOM   2244  CB  PRO A 296       9.450  26.445  66.455  1.00 26.34           C  
ATOM   2245  CG  PRO A 296       9.873  26.386  65.012  1.00 26.82           C  
ATOM   2246  CD  PRO A 296       9.559  25.019  64.496  1.00 25.86           C  
ATOM   2247  N   LEU A 297       8.828  24.371  69.188  1.00 26.64           N  
ATOM   2248  CA  LEU A 297       7.877  24.254  70.291  1.00 26.88           C  
ATOM   2249  C   LEU A 297       7.775  25.609  71.022  1.00 28.06           C  
ATOM   2250  O   LEU A 297       8.761  26.350  71.080  1.00 28.16           O  
ATOM   2251  CB  LEU A 297       8.317  23.168  71.267  1.00 26.43           C  
ATOM   2252  CG  LEU A 297       8.360  21.692  70.834  1.00 26.22           C  
ATOM   2253  CD1 LEU A 297       8.988  20.813  71.895  1.00 24.66           C  
ATOM   2254  CD2 LEU A 297       6.969  21.166  70.506  1.00 27.83           C  
ATOM   2255  N   PRO A 298       6.577  25.956  71.547  1.00 28.35           N  
ATOM   2256  CA  PRO A 298       6.451  27.130  72.417  1.00 28.97           C  
ATOM   2257  C   PRO A 298       6.952  26.876  73.841  1.00 29.22           C  
ATOM   2258  O   PRO A 298       7.127  27.817  74.603  1.00 29.65           O  
ATOM   2259  CB  PRO A 298       4.931  27.402  72.439  1.00 29.25           C  
ATOM   2260  CG  PRO A 298       4.294  26.057  72.169  1.00 28.75           C  
ATOM   2261  CD  PRO A 298       5.278  25.288  71.310  1.00 28.80           C  
ATOM   2262  N   HIS A 299       7.135  25.608  74.206  1.00 29.34           N  
ATOM   2263  CA AHIS A 299       7.708  25.241  75.497  0.50 28.91           C  
ATOM   2264  CA BHIS A 299       7.700  25.236  75.506  0.50 29.04           C  
ATOM   2265  C   HIS A 299       8.326  23.860  75.401  1.00 28.51           C  
ATOM   2266  O   HIS A 299       7.885  23.026  74.600  1.00 28.70           O  
ATOM   2267  CB AHIS A 299       6.646  25.293  76.605  0.50 28.91           C  
ATOM   2268  CB BHIS A 299       6.671  25.357  76.670  0.50 29.15           C  
ATOM   2269  CG AHIS A 299       7.203  25.576  77.965  0.50 30.24           C  
ATOM   2270  CG BHIS A 299       5.750  24.180  76.829  0.50 30.97           C  
ATOM   2271  ND1AHIS A 299       7.856  26.753  78.274  0.50 31.49           N  
ATOM   2272  ND1BHIS A 299       6.131  23.010  77.455  0.50 32.37           N  
ATOM   2273  CD2AHIS A 299       7.191  24.843  79.104  0.50 30.38           C  
ATOM   2274  CD2BHIS A 299       4.449  24.010  76.479  0.50 32.29           C  
ATOM   2275  CE1AHIS A 299       8.223  26.731  79.543  0.50 31.39           C  
ATOM   2276  CE1BHIS A 299       5.117  22.160  77.457  0.50 32.18           C  
ATOM   2277  NE2AHIS A 299       7.834  25.582  80.068  0.50 31.61           N  
ATOM   2278  NE2BHIS A 299       4.085  22.743  76.871  0.50 32.50           N  
ATOM   2279  N   TRP A 300       9.362  23.632  76.195  1.00 27.98           N  
ATOM   2280  CA  TRP A 300      10.026  22.347  76.228  1.00 27.30           C  
ATOM   2281  C   TRP A 300       9.568  21.442  77.360  1.00 27.96           C  
ATOM   2282  O   TRP A 300       9.159  20.308  77.119  1.00 28.65           O  
ATOM   2283  CB  TRP A 300      11.547  22.501  76.265  1.00 25.71           C  
ATOM   2284  CG  TRP A 300      12.129  23.020  74.963  1.00 25.58           C  
ATOM   2285  CD1 TRP A 300      11.481  23.133  73.741  1.00 23.26           C  
ATOM   2286  CD2 TRP A 300      13.478  23.492  74.748  1.00 22.79           C  
ATOM   2287  NE1 TRP A 300      12.341  23.645  72.808  1.00 23.82           N  
ATOM   2288  CE2 TRP A 300      13.570  23.873  73.385  1.00 22.43           C  
ATOM   2289  CE3 TRP A 300      14.604  23.643  75.577  1.00 19.46           C  
ATOM   2290  CZ2 TRP A 300      14.741  24.382  72.833  1.00 21.45           C  
ATOM   2291  CZ3 TRP A 300      15.768  24.127  75.030  1.00 21.85           C  
ATOM   2292  CH2 TRP A 300      15.829  24.497  73.665  1.00 22.56           C  
ATOM   2293  N   GLY A 301       9.654  21.908  78.596  1.00 28.39           N  
ATOM   2294  CA  GLY A 301       9.452  20.987  79.705  1.00 29.21           C  
ATOM   2295  C   GLY A 301       8.206  21.265  80.495  1.00 30.05           C  
ATOM   2296  O   GLY A 301       7.353  22.053  80.094  1.00 31.37           O  
ATOM   2297  N   ARG A 302       8.102  20.616  81.633  1.00 30.84           N  
ATOM   2298  CA  ARG A 302       6.930  20.720  82.462  1.00 31.85           C  
ATOM   2299  C   ARG A 302       7.283  20.120  83.811  1.00 31.40           C  
ATOM   2300  O   ARG A 302       7.606  18.919  83.919  1.00 30.81           O  
ATOM   2301  CB  ARG A 302       5.780  19.942  81.831  1.00 32.84           C  
ATOM   2302  CG  ARG A 302       4.605  19.759  82.759  1.00 36.74           C  
ATOM   2303  CD  ARG A 302       3.298  19.630  81.985  1.00 43.99           C  
ATOM   2304  NE  ARG A 302       2.230  19.238  82.903  1.00 49.84           N  
ATOM   2305  CZ  ARG A 302       1.839  17.979  83.088  1.00 51.42           C  
ATOM   2306  NH1 ARG A 302       2.408  16.993  82.374  1.00 50.94           N  
ATOM   2307  NH2 ARG A 302       0.870  17.717  83.966  1.00 50.02           N  
ATOM   2308  N   GLY A 303       7.227  20.964  84.836  1.00 30.72           N  
ATOM   2309  CA  GLY A 303       7.537  20.522  86.180  1.00 29.83           C  
ATOM   2310  C   GLY A 303       9.029  20.301  86.341  1.00 28.98           C  
ATOM   2311  O   GLY A 303       9.823  21.229  86.176  1.00 28.60           O  
ATOM   2312  N   ARG A 304       9.389  19.068  86.662  1.00 28.52           N  
ATOM   2313  CA  ARG A 304      10.753  18.697  86.962  1.00 29.31           C  
ATOM   2314  C   ARG A 304      11.392  17.856  85.844  1.00 28.91           C  
ATOM   2315  O   ARG A 304      12.406  17.191  86.053  1.00 28.13           O  
ATOM   2316  CB  ARG A 304      10.778  17.930  88.280  1.00 30.02           C  
ATOM   2317  CG  ARG A 304      10.565  18.790  89.529  1.00 32.21           C  
ATOM   2318  CD  ARG A 304      10.139  17.934  90.719  1.00 35.84           C  
ATOM   2319  NE  ARG A 304      10.121  18.699  91.961  1.00 37.73           N  
ATOM   2320  CZ  ARG A 304      11.136  18.744  92.823  1.00 37.67           C  
ATOM   2321  NH1 ARG A 304      12.258  18.070  92.580  1.00 38.80           N  
ATOM   2322  NH2 ARG A 304      11.026  19.464  93.926  1.00 35.07           N  
ATOM   2323  N   ILE A 305      10.767  17.897  84.669  1.00 28.96           N  
ATOM   2324  CA  ILE A 305      11.231  17.196  83.485  1.00 28.78           C  
ATOM   2325  C   ILE A 305      11.535  18.224  82.433  1.00 28.72           C  
ATOM   2326  O   ILE A 305      10.666  19.000  82.053  1.00 28.43           O  
ATOM   2327  CB  ILE A 305      10.137  16.301  82.837  1.00 29.07           C  
ATOM   2328  CG1 ILE A 305       9.572  15.283  83.815  1.00 28.00           C  
ATOM   2329  CG2 ILE A 305      10.693  15.635  81.570  1.00 26.54           C  
ATOM   2330  CD1 ILE A 305       8.675  14.259  83.127  1.00 29.12           C  
ATOM   2331  N   THR A 306      12.753  18.196  81.917  1.00 28.61           N  
ATOM   2332  CA  THR A 306      13.086  19.085  80.832  1.00 28.54           C  
ATOM   2333  C   THR A 306      13.679  18.329  79.628  1.00 27.43           C  
ATOM   2334  O   THR A 306      13.821  17.091  79.654  1.00 26.84           O  
ATOM   2335  CB  THR A 306      13.993  20.251  81.348  1.00 28.86           C  
ATOM   2336  OG1 THR A 306      13.804  21.409  80.519  1.00 33.06           O  
ATOM   2337  CG2 THR A 306      15.470  19.854  81.399  1.00 28.01           C  
ATOM   2338  N   LEU A 307      14.020  19.094  78.590  1.00 26.33           N  
ATOM   2339  CA  LEU A 307      14.591  18.570  77.343  1.00 25.77           C  
ATOM   2340  C   LEU A 307      15.928  19.261  77.012  1.00 25.43           C  
ATOM   2341  O   LEU A 307      16.119  20.436  77.335  1.00 24.52           O  
ATOM   2342  CB  LEU A 307      13.608  18.754  76.186  1.00 24.74           C  
ATOM   2343  CG  LEU A 307      12.495  17.742  75.787  1.00 25.43           C  
ATOM   2344  CD1 LEU A 307      12.267  16.556  76.713  1.00 22.79           C  
ATOM   2345  CD2 LEU A 307      11.168  18.454  75.440  1.00 25.12           C  
ATOM   2346  N   LEU A 308      16.827  18.519  76.360  1.00 24.30           N  
ATOM   2347  CA  LEU A 308      18.144  19.006  76.012  1.00 24.35           C  
ATOM   2348  C   LEU A 308      18.586  18.365  74.687  1.00 24.28           C  
ATOM   2349  O   LEU A 308      18.132  17.256  74.364  1.00 26.25           O  
ATOM   2350  CB  LEU A 308      19.093  18.619  77.146  1.00 24.39           C  
ATOM   2351  CG  LEU A 308      20.588  18.942  77.064  1.00 25.51           C  
ATOM   2352  CD1 LEU A 308      21.137  19.284  78.485  1.00 25.92           C  
ATOM   2353  CD2 LEU A 308      21.379  17.807  76.367  1.00 22.03           C  
ATOM   2354  N   GLY A 309      19.470  19.019  73.937  1.00 22.87           N  
ATOM   2355  CA  GLY A 309      19.985  18.470  72.669  1.00 21.76           C  
ATOM   2356  C   GLY A 309      18.910  18.241  71.614  1.00 21.43           C  
ATOM   2357  O   GLY A 309      17.871  18.912  71.633  1.00 21.54           O  
ATOM   2358  N   ASP A 310      19.148  17.288  70.709  1.00 20.72           N  
ATOM   2359  CA  ASP A 310      18.181  16.915  69.668  1.00 20.45           C  
ATOM   2360  C   ASP A 310      16.771  16.682  70.201  1.00 20.41           C  
ATOM   2361  O   ASP A 310      15.801  16.996  69.499  1.00 19.17           O  
ATOM   2362  CB  ASP A 310      18.605  15.653  68.904  1.00 20.97           C  
ATOM   2363  CG  ASP A 310      19.777  15.881  67.990  1.00 21.60           C  
ATOM   2364  OD1 ASP A 310      20.263  14.890  67.349  1.00 23.43           O  
ATOM   2365  OD2 ASP A 310      20.230  17.037  67.925  1.00 17.15           O  
ATOM   2366  N   ALA A 311      16.665  16.135  71.426  1.00 20.25           N  
ATOM   2367  CA  ALA A 311      15.358  15.930  72.110  1.00 19.93           C  
ATOM   2368  C   ALA A 311      14.564  17.236  72.252  1.00 20.26           C  
ATOM   2369  O   ALA A 311      13.322  17.243  72.146  1.00 21.82           O  
ATOM   2370  CB  ALA A 311      15.564  15.290  73.480  1.00 19.22           C  
ATOM   2371  N   ALA A 312      15.288  18.330  72.484  1.00 20.12           N  
ATOM   2372  CA  ALA A 312      14.723  19.676  72.648  1.00 20.16           C  
ATOM   2373  C   ALA A 312      14.488  20.325  71.311  1.00 20.39           C  
ATOM   2374  O   ALA A 312      13.432  20.900  71.090  1.00 21.76           O  
ATOM   2375  CB  ALA A 312      15.691  20.567  73.486  1.00 18.89           C  
ATOM   2376  N   HIS A 313      15.478  20.241  70.417  1.00 21.06           N  
ATOM   2377  CA  HIS A 313      15.523  21.070  69.185  1.00 20.70           C  
ATOM   2378  C   HIS A 313      16.290  20.391  68.048  1.00 21.05           C  
ATOM   2379  O   HIS A 313      17.359  20.864  67.659  1.00 22.59           O  
ATOM   2380  CB  HIS A 313      16.195  22.424  69.507  1.00 19.72           C  
ATOM   2381  CG  HIS A 313      17.517  22.299  70.219  1.00 17.56           C  
ATOM   2382  ND1 HIS A 313      18.653  21.808  69.609  1.00 18.66           N  
ATOM   2383  CD2 HIS A 313      17.884  22.603  71.491  1.00 17.38           C  
ATOM   2384  CE1 HIS A 313      19.664  21.819  70.466  1.00 17.20           C  
ATOM   2385  NE2 HIS A 313      19.219  22.275  71.625  1.00 16.34           N  
ATOM   2386  N   LEU A 314      15.784  19.282  67.509  1.00 21.09           N  
ATOM   2387  CA  LEU A 314      16.466  18.619  66.371  1.00 20.25           C  
ATOM   2388  C   LEU A 314      16.525  19.592  65.191  1.00 20.69           C  
ATOM   2389  O   LEU A 314      15.505  20.180  64.788  1.00 19.48           O  
ATOM   2390  CB  LEU A 314      15.742  17.335  65.953  1.00 19.76           C  
ATOM   2391  CG  LEU A 314      16.278  16.549  64.741  1.00 20.46           C  
ATOM   2392  CD1 LEU A 314      17.636  15.845  64.987  1.00 16.80           C  
ATOM   2393  CD2 LEU A 314      15.247  15.558  64.227  1.00 19.09           C  
HETATM 2394  N   MSE A 315      17.726  19.752  64.655  1.00 21.34           N  
HETATM 2395  CA  MSE A 315      17.986  20.633  63.524  1.00 23.09           C  
HETATM 2396  C   MSE A 315      18.654  19.878  62.361  1.00 22.76           C  
HETATM 2397  O   MSE A 315      19.234  18.785  62.549  1.00 22.31           O  
HETATM 2398  CB  MSE A 315      18.924  21.772  63.977  1.00 21.71           C  
HETATM 2399  CG  MSE A 315      18.282  22.783  64.862  1.00 22.58           C  
HETATM 2400 SE   MSE A 315      19.664  23.839  65.725  0.50 28.17          SE  
HETATM 2401  CE  MSE A 315      18.621  24.566  67.173  1.00 22.25           C  
ATOM   2402  N   TYR A 316      18.629  20.483  61.177  1.00 23.48           N  
ATOM   2403  CA  TYR A 316      19.447  19.976  60.063  1.00 25.09           C  
ATOM   2404  C   TYR A 316      20.923  19.916  60.454  1.00 26.35           C  
ATOM   2405  O   TYR A 316      21.482  20.898  60.922  1.00 25.32           O  
ATOM   2406  CB  TYR A 316      19.308  20.833  58.794  1.00 24.48           C  
ATOM   2407  CG  TYR A 316      17.918  21.050  58.328  1.00 22.79           C  
ATOM   2408  CD1 TYR A 316      16.940  20.069  58.509  1.00 22.69           C  
ATOM   2409  CD2 TYR A 316      17.563  22.227  57.691  1.00 20.17           C  
ATOM   2410  CE1 TYR A 316      15.635  20.280  58.084  1.00 21.36           C  
ATOM   2411  CE2 TYR A 316      16.269  22.437  57.240  1.00 18.64           C  
ATOM   2412  CZ  TYR A 316      15.319  21.465  57.446  1.00 22.47           C  
ATOM   2413  OH  TYR A 316      14.037  21.648  56.994  1.00 26.22           O  
ATOM   2414  N   PRO A 317      21.559  18.757  60.238  1.00 29.04           N  
ATOM   2415  CA  PRO A 317      22.980  18.608  60.605  1.00 30.83           C  
ATOM   2416  C   PRO A 317      23.944  19.411  59.714  1.00 32.65           C  
ATOM   2417  O   PRO A 317      24.620  18.846  58.866  1.00 34.61           O  
ATOM   2418  CB  PRO A 317      23.221  17.101  60.488  1.00 30.39           C  
ATOM   2419  CG  PRO A 317      22.161  16.616  59.496  1.00 29.95           C  
ATOM   2420  CD  PRO A 317      20.982  17.529  59.635  1.00 29.26           C  
HETATM 2421  N   MSE A 318      24.000  20.720  59.893  1.00 33.83           N  
HETATM 2422  CA  MSE A 318      24.981  21.522  59.182  1.00 35.96           C  
HETATM 2423  C   MSE A 318      25.527  22.564  60.115  1.00 35.12           C  
HETATM 2424  O   MSE A 318      24.863  22.971  61.072  1.00 35.01           O  
HETATM 2425  CB  MSE A 318      24.391  22.266  57.972  1.00 35.99           C  
HETATM 2426  CG  MSE A 318      23.306  21.556  57.144  1.00 38.49           C  
HETATM 2427 SE   MSE A 318      22.102  22.949  56.420  0.40 40.47          SE  
HETATM 2428  CE  MSE A 318      21.902  24.064  58.012  1.00 39.71           C  
ATOM   2429  N   GLY A 319      26.740  23.004  59.810  1.00 34.80           N  
ATOM   2430  CA  GLY A 319      27.339  24.133  60.481  1.00 34.04           C  
ATOM   2431  C   GLY A 319      27.500  23.961  61.970  1.00 33.26           C  
ATOM   2432  O   GLY A 319      28.291  23.136  62.436  1.00 33.29           O  
ATOM   2433  N   ALA A 320      26.734  24.749  62.709  1.00 32.58           N  
ATOM   2434  CA  ALA A 320      26.888  24.873  64.166  1.00 31.59           C  
ATOM   2435  C   ALA A 320      25.750  24.203  64.943  1.00 30.90           C  
ATOM   2436  O   ALA A 320      25.625  24.374  66.162  1.00 30.74           O  
ATOM   2437  CB  ALA A 320      26.974  26.351  64.534  1.00 31.63           C  
ATOM   2438  N   ASN A 321      24.896  23.494  64.210  1.00 29.77           N  
ATOM   2439  CA  ASN A 321      23.802  22.710  64.780  1.00 28.63           C  
ATOM   2440  C   ASN A 321      24.326  21.382  65.319  1.00 27.54           C  
ATOM   2441  O   ASN A 321      25.429  20.930  64.987  1.00 27.23           O  
ATOM   2442  CB  ASN A 321      22.699  22.442  63.721  1.00 28.95           C  
ATOM   2443  CG  ASN A 321      22.209  23.716  63.033  1.00 29.78           C  
ATOM   2444  OD1 ASN A 321      22.446  24.827  63.497  1.00 31.53           O  
ATOM   2445  ND2 ASN A 321      21.529  23.549  61.922  1.00 32.04           N  
ATOM   2446  N   GLY A 322      23.519  20.758  66.156  1.00 26.79           N  
ATOM   2447  CA  GLY A 322      23.848  19.463  66.684  1.00 24.90           C  
ATOM   2448  C   GLY A 322      24.602  19.555  67.996  1.00 24.04           C  
ATOM   2449  O   GLY A 322      24.071  20.082  68.987  1.00 23.14           O  
ATOM   2450  N   ALA A 323      25.817  18.996  67.998  1.00 22.29           N  
ATOM   2451  CA  ALA A 323      26.586  18.845  69.204  1.00 21.60           C  
ATOM   2452  C   ALA A 323      26.887  20.211  69.886  1.00 21.63           C  
ATOM   2453  O   ALA A 323      26.756  20.346  71.116  1.00 21.34           O  
ATOM   2454  CB  ALA A 323      27.847  18.072  68.903  1.00 21.32           C  
ATOM   2455  N   SER A 324      27.254  21.212  69.081  1.00 20.68           N  
ATOM   2456  CA  SER A 324      27.511  22.556  69.596  1.00 20.09           C  
ATOM   2457  C   SER A 324      26.347  23.077  70.418  1.00 20.46           C  
ATOM   2458  O   SER A 324      26.548  23.633  71.509  1.00 21.01           O  
ATOM   2459  CB  SER A 324      27.812  23.522  68.474  1.00 19.42           C  
ATOM   2460  OG  SER A 324      29.040  23.192  67.872  1.00 18.70           O  
ATOM   2461  N   GLN A 325      25.130  22.902  69.915  1.00 19.81           N  
ATOM   2462  CA  GLN A 325      23.967  23.384  70.651  1.00 19.42           C  
ATOM   2463  C   GLN A 325      23.675  22.518  71.900  1.00 18.85           C  
ATOM   2464  O   GLN A 325      23.279  23.042  72.934  1.00 19.34           O  
ATOM   2465  CB  GLN A 325      22.734  23.526  69.733  1.00 18.82           C  
ATOM   2466  CG  GLN A 325      23.014  24.245  68.420  1.00 20.40           C  
ATOM   2467  CD  GLN A 325      23.480  25.679  68.613  1.00 24.21           C  
ATOM   2468  OE1 GLN A 325      23.110  26.355  69.579  1.00 27.00           O  
ATOM   2469  NE2 GLN A 325      24.289  26.154  67.691  1.00 27.87           N  
ATOM   2470  N   ALA A 326      23.873  21.217  71.805  1.00 17.86           N  
ATOM   2471  CA  ALA A 326      23.644  20.322  72.924  1.00 18.71           C  
ATOM   2472  C   ALA A 326      24.619  20.564  74.102  1.00 19.15           C  
ATOM   2473  O   ALA A 326      24.222  20.602  75.284  1.00 18.41           O  
ATOM   2474  CB  ALA A 326      23.710  18.879  72.459  1.00 18.12           C  
ATOM   2475  N   ILE A 327      25.898  20.716  73.776  1.00 20.14           N  
ATOM   2476  CA  ILE A 327      26.893  21.131  74.765  1.00 20.13           C  
ATOM   2477  C   ILE A 327      26.517  22.464  75.419  1.00 21.38           C  
ATOM   2478  O   ILE A 327      26.632  22.596  76.630  1.00 22.30           O  
ATOM   2479  CB  ILE A 327      28.270  21.252  74.120  1.00 20.84           C  
ATOM   2480  CG1 ILE A 327      28.765  19.849  73.635  1.00 19.81           C  
ATOM   2481  CG2 ILE A 327      29.259  21.960  75.099  1.00 18.69           C  
ATOM   2482  CD1 ILE A 327      29.998  19.910  72.707  1.00 18.93           C  
ATOM   2483  N   LEU A 328      26.055  23.440  74.641  1.00 21.63           N  
ATOM   2484  CA  LEU A 328      25.718  24.762  75.197  1.00 23.47           C  
ATOM   2485  C   LEU A 328      24.436  24.806  76.034  1.00 24.19           C  
ATOM   2486  O   LEU A 328      24.305  25.676  76.917  1.00 23.84           O  
ATOM   2487  CB  LEU A 328      25.706  25.855  74.112  1.00 23.31           C  
ATOM   2488  CG  LEU A 328      27.124  26.089  73.529  1.00 24.72           C  
ATOM   2489  CD1 LEU A 328      27.040  26.879  72.224  1.00 25.91           C  
ATOM   2490  CD2 LEU A 328      28.118  26.771  74.523  1.00 23.82           C  
ATOM   2491  N   ASP A 329      23.505  23.885  75.726  1.00 24.42           N  
ATOM   2492  CA  ASP A 329      22.321  23.615  76.516  1.00 24.58           C  
ATOM   2493  C   ASP A 329      22.749  23.182  77.923  1.00 25.77           C  
ATOM   2494  O   ASP A 329      22.189  23.646  78.920  1.00 25.70           O  
ATOM   2495  CB  ASP A 329      21.533  22.466  75.885  1.00 24.65           C  
ATOM   2496  CG  ASP A 329      20.762  22.872  74.650  1.00 26.36           C  
ATOM   2497  OD1 ASP A 329      20.664  24.088  74.382  1.00 30.54           O  
ATOM   2498  OD2 ASP A 329      20.229  21.978  73.949  1.00 25.89           O  
ATOM   2499  N   GLY A 330      23.744  22.284  77.992  1.00 26.23           N  
ATOM   2500  CA  GLY A 330      24.122  21.626  79.241  1.00 26.70           C  
ATOM   2501  C   GLY A 330      24.713  22.634  80.174  1.00 27.08           C  
ATOM   2502  O   GLY A 330      24.375  22.684  81.346  1.00 26.98           O  
ATOM   2503  N   ILE A 331      25.586  23.462  79.627  1.00 28.06           N  
ATOM   2504  CA  ILE A 331      26.163  24.576  80.357  1.00 28.88           C  
ATOM   2505  C   ILE A 331      25.058  25.415  81.020  1.00 29.49           C  
ATOM   2506  O   ILE A 331      25.133  25.708  82.227  1.00 29.16           O  
ATOM   2507  CB  ILE A 331      27.030  25.457  79.401  1.00 28.85           C  
ATOM   2508  CG1 ILE A 331      28.132  24.612  78.759  1.00 28.13           C  
ATOM   2509  CG2 ILE A 331      27.616  26.687  80.133  1.00 29.31           C  
ATOM   2510  CD1 ILE A 331      29.026  23.820  79.781  1.00 28.40           C  
ATOM   2511  N   GLU A 332      24.025  25.757  80.243  1.00 29.95           N  
ATOM   2512  CA  GLU A 332      22.951  26.617  80.740  1.00 31.22           C  
ATOM   2513  C   GLU A 332      22.103  25.951  81.793  1.00 30.89           C  
ATOM   2514  O   GLU A 332      21.659  26.618  82.719  1.00 31.68           O  
ATOM   2515  CB  GLU A 332      22.071  27.158  79.612  1.00 31.71           C  
ATOM   2516  CG  GLU A 332      20.999  28.168  80.073  1.00 36.36           C  
ATOM   2517  CD  GLU A 332      21.539  29.315  81.004  1.00 44.01           C  
ATOM   2518  OE1 GLU A 332      21.570  29.164  82.277  1.00 44.30           O  
ATOM   2519  OE2 GLU A 332      21.899  30.386  80.448  1.00 44.23           O  
ATOM   2520  N   LEU A 333      21.907  24.638  81.666  1.00 31.08           N  
ATOM   2521  CA  LEU A 333      21.084  23.852  82.588  1.00 30.70           C  
ATOM   2522  C   LEU A 333      21.755  23.707  83.966  1.00 30.95           C  
ATOM   2523  O   LEU A 333      21.131  23.982  84.998  1.00 30.04           O  
ATOM   2524  CB  LEU A 333      20.791  22.481  81.984  1.00 30.27           C  
ATOM   2525  CG  LEU A 333      20.115  21.457  82.908  1.00 30.16           C  
ATOM   2526  CD1 LEU A 333      18.773  21.939  83.422  1.00 30.60           C  
ATOM   2527  CD2 LEU A 333      19.917  20.154  82.151  1.00 31.86           C  
ATOM   2528  N   ALA A 334      23.018  23.269  83.964  1.00 30.79           N  
ATOM   2529  CA  ALA A 334      23.859  23.318  85.135  1.00 31.67           C  
ATOM   2530  C   ALA A 334      23.842  24.715  85.775  1.00 32.70           C  
ATOM   2531  O   ALA A 334      23.598  24.854  86.970  1.00 32.73           O  
ATOM   2532  CB  ALA A 334      25.258  22.920  84.780  1.00 31.27           C  
ATOM   2533  N   ALA A 335      24.078  25.756  84.988  1.00 33.60           N  
ATOM   2534  CA  ALA A 335      24.083  27.089  85.575  1.00 35.04           C  
ATOM   2535  C   ALA A 335      22.716  27.437  86.155  1.00 36.05           C  
ATOM   2536  O   ALA A 335      22.658  27.942  87.284  1.00 36.99           O  
ATOM   2537  CB  ALA A 335      24.554  28.159  84.583  1.00 34.72           C  
ATOM   2538  N   ALA A 336      21.633  27.166  85.415  1.00 36.26           N  
ATOM   2539  CA  ALA A 336      20.276  27.422  85.926  1.00 36.98           C  
ATOM   2540  C   ALA A 336      20.022  26.694  87.248  1.00 37.97           C  
ATOM   2541  O   ALA A 336      19.642  27.322  88.236  1.00 38.39           O  
ATOM   2542  CB  ALA A 336      19.212  27.072  84.900  1.00 35.91           C  
ATOM   2543  N   LEU A 337      20.257  25.382  87.261  1.00 39.23           N  
ATOM   2544  CA  LEU A 337      20.124  24.544  88.468  1.00 40.37           C  
ATOM   2545  C   LEU A 337      20.980  25.006  89.667  1.00 41.59           C  
ATOM   2546  O   LEU A 337      20.592  24.789  90.817  1.00 41.51           O  
ATOM   2547  CB  LEU A 337      20.458  23.078  88.140  1.00 39.76           C  
ATOM   2548  CG  LEU A 337      19.433  21.930  88.025  1.00 38.80           C  
ATOM   2549  CD1 LEU A 337      17.980  22.308  88.124  1.00 36.55           C  
ATOM   2550  CD2 LEU A 337      19.674  21.126  86.767  1.00 35.94           C  
ATOM   2551  N   ALA A 338      22.133  25.624  89.393  1.00 42.93           N  
ATOM   2552  CA  ALA A 338      23.057  26.067  90.442  1.00 44.42           C  
ATOM   2553  C   ALA A 338      22.563  27.360  91.096  1.00 45.71           C  
ATOM   2554  O   ALA A 338      22.779  27.597  92.287  1.00 45.83           O  
ATOM   2555  CB  ALA A 338      24.454  26.261  89.876  1.00 43.84           C  
ATOM   2556  N   ARG A 339      21.868  28.158  90.293  1.00 46.96           N  
ATOM   2557  CA  ARG A 339      21.456  29.511  90.614  1.00 48.01           C  
ATOM   2558  C   ARG A 339      20.152  29.553  91.428  1.00 48.65           C  
ATOM   2559  O   ARG A 339      20.028  30.338  92.371  1.00 48.55           O  
ATOM   2560  CB  ARG A 339      21.247  30.242  89.291  1.00 48.20           C  
ATOM   2561  CG  ARG A 339      21.689  31.682  89.260  1.00 49.19           C  
ATOM   2562  CD  ARG A 339      21.707  32.209  87.819  1.00 49.99           C  
ATOM   2563  NE  ARG A 339      20.485  31.870  87.093  1.00 48.93           N  
ATOM   2564  CZ  ARG A 339      20.446  31.272  85.902  1.00 49.27           C  
ATOM   2565  NH1 ARG A 339      21.567  30.941  85.269  1.00 47.48           N  
ATOM   2566  NH2 ARG A 339      19.272  31.023  85.336  1.00 48.91           N  
ATOM   2567  N   ASN A 340      19.187  28.712  91.044  1.00 49.40           N  
ATOM   2568  CA  ASN A 340      17.863  28.682  91.659  1.00 49.71           C  
ATOM   2569  C   ASN A 340      17.582  27.407  92.429  1.00 49.99           C  
ATOM   2570  O   ASN A 340      17.556  26.317  91.843  1.00 50.51           O  
ATOM   2571  CB  ASN A 340      16.784  28.863  90.606  1.00 49.87           C  
ATOM   2572  CG  ASN A 340      15.455  29.313  91.205  1.00 51.19           C  
ATOM   2573  OD1 ASN A 340      14.930  28.706  92.149  1.00 51.35           O  
ATOM   2574  ND2 ASN A 340      14.902  30.382  90.649  1.00 51.28           N  
ATOM   2575  N   ALA A 341      17.338  27.556  93.734  1.00 49.79           N  
ATOM   2576  CA  ALA A 341      17.022  26.432  94.621  1.00 49.43           C  
ATOM   2577  C   ALA A 341      15.696  25.734  94.274  1.00 49.27           C  
ATOM   2578  O   ALA A 341      15.540  24.527  94.508  1.00 49.17           O  
ATOM   2579  CB  ALA A 341      17.013  26.893  96.058  1.00 49.62           C  
ATOM   2580  N   ASP A 342      14.751  26.488  93.710  1.00 48.69           N  
ATOM   2581  CA  ASP A 342      13.455  25.931  93.269  1.00 48.25           C  
ATOM   2582  C   ASP A 342      13.538  25.273  91.862  1.00 47.31           C  
ATOM   2583  O   ASP A 342      13.386  25.950  90.838  1.00 46.90           O  
ATOM   2584  CB  ASP A 342      12.381  27.030  93.355  1.00 48.42           C  
ATOM   2585  CG  ASP A 342      11.119  26.710  92.568  1.00 49.89           C  
ATOM   2586  OD1 ASP A 342      10.829  25.518  92.302  1.00 51.70           O  
ATOM   2587  OD2 ASP A 342      10.413  27.681  92.214  1.00 50.03           O  
ATOM   2588  N   VAL A 343      13.765  23.952  91.844  1.00 46.08           N  
ATOM   2589  CA  VAL A 343      14.019  23.167  90.605  1.00 44.86           C  
ATOM   2590  C   VAL A 343      13.144  23.459  89.380  1.00 43.73           C  
ATOM   2591  O   VAL A 343      13.679  23.602  88.288  1.00 43.76           O  
ATOM   2592  CB  VAL A 343      14.090  21.631  90.856  1.00 45.04           C  
ATOM   2593  CG1 VAL A 343      12.836  21.123  91.499  1.00 45.37           C  
ATOM   2594  CG2 VAL A 343      14.341  20.885  89.556  1.00 45.29           C  
ATOM   2595  N   ALA A 344      11.825  23.536  89.544  1.00 42.54           N  
ATOM   2596  CA  ALA A 344      10.941  23.771  88.397  1.00 41.59           C  
ATOM   2597  C   ALA A 344      11.158  25.169  87.805  1.00 41.16           C  
ATOM   2598  O   ALA A 344      11.134  25.355  86.574  1.00 40.89           O  
ATOM   2599  CB  ALA A 344       9.482  23.539  88.753  1.00 41.21           C  
ATOM   2600  N   ALA A 345      11.402  26.151  88.665  1.00 40.12           N  
ATOM   2601  CA  ALA A 345      11.717  27.484  88.155  1.00 39.61           C  
ATOM   2602  C   ALA A 345      13.096  27.534  87.483  1.00 38.84           C  
ATOM   2603  O   ALA A 345      13.269  28.283  86.536  1.00 39.39           O  
ATOM   2604  CB  ALA A 345      11.607  28.532  89.249  1.00 39.91           C  
ATOM   2605  N   ALA A 346      14.060  26.750  87.972  1.00 37.59           N  
ATOM   2606  CA  ALA A 346      15.385  26.646  87.356  1.00 37.10           C  
ATOM   2607  C   ALA A 346      15.293  26.063  85.938  1.00 37.04           C  
ATOM   2608  O   ALA A 346      15.737  26.680  84.957  1.00 36.55           O  
ATOM   2609  CB  ALA A 346      16.284  25.803  88.207  1.00 36.93           C  
ATOM   2610  N   LEU A 347      14.685  24.878  85.853  1.00 37.22           N  
ATOM   2611  CA  LEU A 347      14.329  24.219  84.592  1.00 37.06           C  
ATOM   2612  C   LEU A 347      13.648  25.120  83.565  1.00 37.45           C  
ATOM   2613  O   LEU A 347      14.016  25.072  82.392  1.00 37.87           O  
ATOM   2614  CB  LEU A 347      13.480  22.978  84.866  1.00 36.88           C  
ATOM   2615  CG  LEU A 347      14.187  21.630  84.983  1.00 35.09           C  
ATOM   2616  CD1 LEU A 347      15.662  21.735  85.345  1.00 31.34           C  
ATOM   2617  CD2 LEU A 347      13.463  20.833  85.992  1.00 34.11           C  
ATOM   2618  N   ARG A 348      12.681  25.927  84.002  1.00 37.78           N  
ATOM   2619  CA  ARG A 348      12.053  26.960  83.169  1.00 39.00           C  
ATOM   2620  C   ARG A 348      13.021  28.060  82.740  1.00 38.46           C  
ATOM   2621  O   ARG A 348      12.996  28.511  81.596  1.00 38.38           O  
ATOM   2622  CB  ARG A 348      10.902  27.638  83.918  1.00 39.16           C  
ATOM   2623  CG  ARG A 348       9.591  26.868  83.941  1.00 40.84           C  
ATOM   2624  CD  ARG A 348       8.384  27.799  84.266  1.00 42.29           C  
ATOM   2625  NE  ARG A 348       8.548  28.665  85.456  1.00 47.56           N  
ATOM   2626  CZ  ARG A 348       8.344  28.294  86.729  1.00 48.15           C  
ATOM   2627  NH1 ARG A 348       7.991  27.047  87.047  1.00 47.06           N  
ATOM   2628  NH2 ARG A 348       8.518  29.183  87.697  1.00 48.13           N  
ATOM   2629  N   GLU A 349      13.853  28.501  83.677  1.00 37.89           N  
ATOM   2630  CA  GLU A 349      14.826  29.544  83.446  1.00 37.97           C  
ATOM   2631  C   GLU A 349      15.924  29.084  82.467  1.00 36.73           C  
ATOM   2632  O   GLU A 349      16.491  29.883  81.723  1.00 36.29           O  
ATOM   2633  CB  GLU A 349      15.450  29.881  84.784  1.00 38.99           C  
ATOM   2634  CG  GLU A 349      15.543  31.322  85.165  1.00 42.52           C  
ATOM   2635  CD  GLU A 349      15.785  31.454  86.684  1.00 48.73           C  
ATOM   2636  OE1 GLU A 349      14.915  32.049  87.380  1.00 50.08           O  
ATOM   2637  OE2 GLU A 349      16.826  30.926  87.184  1.00 50.36           O  
ATOM   2638  N   TYR A 350      16.236  27.793  82.493  1.00 35.50           N  
ATOM   2639  CA  TYR A 350      17.146  27.191  81.509  1.00 34.41           C  
ATOM   2640  C   TYR A 350      16.608  27.280  80.060  1.00 34.32           C  
ATOM   2641  O   TYR A 350      17.346  27.691  79.160  1.00 33.82           O  
ATOM   2642  CB  TYR A 350      17.511  25.742  81.914  1.00 33.63           C  
ATOM   2643  CG  TYR A 350      17.651  24.768  80.763  1.00 32.91           C  
ATOM   2644  CD1 TYR A 350      18.713  24.880  79.851  1.00 32.34           C  
ATOM   2645  CD2 TYR A 350      16.723  23.727  80.581  1.00 32.53           C  
ATOM   2646  CE1 TYR A 350      18.841  24.008  78.780  1.00 31.18           C  
ATOM   2647  CE2 TYR A 350      16.857  22.832  79.511  1.00 31.57           C  
ATOM   2648  CZ  TYR A 350      17.924  22.986  78.620  1.00 31.07           C  
ATOM   2649  OH  TYR A 350      18.089  22.127  77.568  1.00 30.09           O  
ATOM   2650  N   GLU A 351      15.340  26.922  79.841  1.00 34.57           N  
ATOM   2651  CA  GLU A 351      14.780  26.835  78.464  1.00 35.62           C  
ATOM   2652  C   GLU A 351      14.328  28.165  77.894  1.00 34.92           C  
ATOM   2653  O   GLU A 351      14.263  28.357  76.665  1.00 34.68           O  
ATOM   2654  CB  GLU A 351      13.633  25.827  78.363  1.00 35.50           C  
ATOM   2655  CG  GLU A 351      13.023  25.417  79.686  1.00 37.86           C  
ATOM   2656  CD  GLU A 351      11.675  24.725  79.530  1.00 38.18           C  
ATOM   2657  OE1 GLU A 351      11.491  23.639  80.182  1.00 36.23           O  
ATOM   2658  OE2 GLU A 351      10.846  25.290  78.743  1.00 39.21           O  
ATOM   2659  N   GLU A 352      14.024  29.089  78.787  1.00 34.25           N  
ATOM   2660  CA  GLU A 352      13.731  30.426  78.363  1.00 34.32           C  
ATOM   2661  C   GLU A 352      15.028  31.099  77.935  1.00 33.23           C  
ATOM   2662  O   GLU A 352      15.040  31.992  77.094  1.00 32.63           O  
ATOM   2663  CB  GLU A 352      13.002  31.162  79.471  1.00 35.59           C  
ATOM   2664  CG  GLU A 352      11.588  30.610  79.696  1.00 39.25           C  
ATOM   2665  CD  GLU A 352      10.779  30.541  78.393  1.00 46.56           C  
ATOM   2666  OE1 GLU A 352      10.166  31.579  78.024  1.00 47.74           O  
ATOM   2667  OE2 GLU A 352      10.757  29.449  77.739  1.00 48.56           O  
ATOM   2668  N   ALA A 353      16.138  30.609  78.452  1.00 32.26           N  
ATOM   2669  CA  ALA A 353      17.407  31.032  77.912  1.00 32.20           C  
ATOM   2670  C   ALA A 353      17.669  30.381  76.539  1.00 31.95           C  
ATOM   2671  O   ALA A 353      18.098  31.070  75.604  1.00 32.43           O  
ATOM   2672  CB  ALA A 353      18.539  30.749  78.900  1.00 31.70           C  
ATOM   2673  N   ARG A 354      17.373  29.082  76.404  1.00 31.10           N  
ATOM   2674  CA  ARG A 354      17.810  28.306  75.223  1.00 30.43           C  
ATOM   2675  C   ARG A 354      16.774  28.070  74.099  1.00 30.10           C  
ATOM   2676  O   ARG A 354      17.142  27.945  72.930  1.00 29.20           O  
ATOM   2677  CB  ARG A 354      18.477  26.994  75.656  1.00 30.69           C  
ATOM   2678  CG  ARG A 354      19.706  27.167  76.553  1.00 30.09           C  
ATOM   2679  CD  ARG A 354      20.967  27.636  75.796  1.00 28.99           C  
ATOM   2680  NE  ARG A 354      21.340  26.730  74.708  1.00 30.41           N  
ATOM   2681  CZ  ARG A 354      22.004  27.092  73.603  1.00 31.81           C  
ATOM   2682  NH1 ARG A 354      22.397  28.364  73.429  1.00 30.67           N  
ATOM   2683  NH2 ARG A 354      22.260  26.179  72.657  1.00 28.95           N  
ATOM   2684  N   ARG A 355      15.492  28.030  74.445  1.00 30.21           N  
ATOM   2685  CA  ARG A 355      14.448  27.770  73.456  1.00 30.92           C  
ATOM   2686  C   ARG A 355      14.280  28.807  72.318  1.00 30.86           C  
ATOM   2687  O   ARG A 355      14.150  28.408  71.137  1.00 30.73           O  
ATOM   2688  CB  ARG A 355      13.113  27.487  74.149  1.00 31.07           C  
ATOM   2689  CG  ARG A 355      11.992  26.978  73.248  1.00 31.16           C  
ATOM   2690  CD  ARG A 355      10.669  26.976  74.018  1.00 32.85           C  
ATOM   2691  NE  ARG A 355      10.510  28.148  74.896  1.00 38.11           N  
ATOM   2692  CZ  ARG A 355       9.970  29.315  74.528  1.00 39.71           C  
ATOM   2693  NH1 ARG A 355       9.510  29.505  73.289  1.00 39.62           N  
ATOM   2694  NH2 ARG A 355       9.877  30.302  75.409  1.00 40.08           N  
ATOM   2695  N   PRO A 356      14.255  30.122  72.649  1.00 30.67           N  
ATOM   2696  CA  PRO A 356      14.032  31.109  71.588  1.00 30.38           C  
ATOM   2697  C   PRO A 356      15.168  31.148  70.572  1.00 30.13           C  
ATOM   2698  O   PRO A 356      14.913  31.273  69.369  1.00 30.58           O  
ATOM   2699  CB  PRO A 356      13.901  32.438  72.361  1.00 30.58           C  
ATOM   2700  CG  PRO A 356      13.526  32.031  73.770  1.00 30.63           C  
ATOM   2701  CD  PRO A 356      14.355  30.783  73.964  1.00 30.98           C  
ATOM   2702  N   THR A 357      16.404  31.018  71.038  1.00 29.55           N  
ATOM   2703  CA  THR A 357      17.554  30.896  70.149  1.00 29.62           C  
ATOM   2704  C   THR A 357      17.392  29.688  69.215  1.00 29.30           C  
ATOM   2705  O   THR A 357      17.531  29.832  67.981  1.00 29.80           O  
ATOM   2706  CB  THR A 357      18.852  30.747  70.952  1.00 29.75           C  
ATOM   2707  OG1 THR A 357      18.895  31.755  71.960  1.00 32.37           O  
ATOM   2708  CG2 THR A 357      20.078  30.912  70.069  1.00 31.83           C  
ATOM   2709  N   ALA A 358      17.081  28.521  69.807  1.00 28.38           N  
ATOM   2710  CA  ALA A 358      16.914  27.247  69.082  1.00 27.46           C  
ATOM   2711  C   ALA A 358      15.821  27.356  68.023  1.00 27.20           C  
ATOM   2712  O   ALA A 358      16.007  26.912  66.881  1.00 27.22           O  
ATOM   2713  CB  ALA A 358      16.619  26.070  70.055  1.00 26.61           C  
ATOM   2714  N   ASN A 359      14.701  27.966  68.402  1.00 26.31           N  
ATOM   2715  CA  ASN A 359      13.636  28.224  67.464  1.00 26.35           C  
ATOM   2716  C   ASN A 359      14.003  29.258  66.375  1.00 27.12           C  
ATOM   2717  O   ASN A 359      13.553  29.135  65.229  1.00 26.94           O  
ATOM   2718  CB  ASN A 359      12.342  28.575  68.213  1.00 26.35           C  
ATOM   2719  CG  ASN A 359      11.763  27.368  69.009  1.00 26.41           C  
ATOM   2720  OD1 ASN A 359      12.259  26.233  68.927  1.00 24.68           O  
ATOM   2721  ND2 ASN A 359      10.703  27.624  69.771  1.00 26.38           N  
ATOM   2722  N   LYS A 360      14.855  30.241  66.708  1.00 27.91           N  
ATOM   2723  CA  LYS A 360      15.371  31.181  65.698  1.00 28.56           C  
ATOM   2724  C   LYS A 360      16.127  30.413  64.620  1.00 26.84           C  
ATOM   2725  O   LYS A 360      15.967  30.671  63.423  1.00 26.52           O  
ATOM   2726  CB  LYS A 360      16.282  32.287  66.318  1.00 29.21           C  
ATOM   2727  CG  LYS A 360      15.553  33.561  66.871  1.00 31.38           C  
ATOM   2728  CD  LYS A 360      16.506  34.513  67.696  1.00 31.08           C  
ATOM   2729  CE  LYS A 360      16.101  34.651  69.204  1.00 37.70           C  
ATOM   2730  NZ  LYS A 360      17.222  34.936  70.243  1.00 34.90           N  
ATOM   2731  N   ILE A 361      16.924  29.436  65.047  1.00 26.36           N  
ATOM   2732  CA  ILE A 361      17.793  28.722  64.111  1.00 25.19           C  
ATOM   2733  C   ILE A 361      16.970  27.770  63.251  1.00 25.22           C  
ATOM   2734  O   ILE A 361      17.193  27.690  62.048  1.00 25.25           O  
ATOM   2735  CB  ILE A 361      18.942  27.934  64.791  1.00 25.15           C  
ATOM   2736  CG1 ILE A 361      19.674  28.755  65.861  1.00 25.51           C  
ATOM   2737  CG2 ILE A 361      19.915  27.451  63.761  1.00 23.41           C  
ATOM   2738  CD1 ILE A 361      20.573  27.875  66.804  1.00 24.55           C  
ATOM   2739  N   ILE A 362      16.043  27.042  63.869  1.00 24.35           N  
ATOM   2740  CA  ILE A 362      15.153  26.204  63.117  1.00 24.70           C  
ATOM   2741  C   ILE A 362      14.442  26.998  62.015  1.00 24.85           C  
ATOM   2742  O   ILE A 362      14.526  26.617  60.842  1.00 25.36           O  
ATOM   2743  CB  ILE A 362      14.147  25.439  64.030  1.00 25.62           C  
ATOM   2744  CG1 ILE A 362      14.896  24.416  64.913  1.00 25.83           C  
ATOM   2745  CG2 ILE A 362      13.045  24.739  63.194  1.00 23.91           C  
ATOM   2746  CD1 ILE A 362      14.214  24.130  66.239  1.00 26.99           C  
ATOM   2747  N   LEU A 363      13.810  28.123  62.348  1.00 24.70           N  
ATOM   2748  CA  LEU A 363      13.068  28.854  61.315  1.00 24.91           C  
ATOM   2749  C   LEU A 363      13.965  29.441  60.202  1.00 25.15           C  
ATOM   2750  O   LEU A 363      13.556  29.467  59.036  1.00 24.90           O  
ATOM   2751  CB  LEU A 363      12.079  29.878  61.914  1.00 24.88           C  
ATOM   2752  CG  LEU A 363      10.952  29.352  62.848  1.00 26.60           C  
ATOM   2753  CD1 LEU A 363      10.092  30.485  63.415  1.00 29.14           C  
ATOM   2754  CD2 LEU A 363      10.036  28.259  62.237  1.00 23.97           C  
ATOM   2755  N   ALA A 364      15.187  29.881  60.558  1.00 25.23           N  
ATOM   2756  CA  ALA A 364      16.097  30.501  59.575  1.00 25.07           C  
ATOM   2757  C   ALA A 364      16.664  29.482  58.600  1.00 25.63           C  
ATOM   2758  O   ALA A 364      16.723  29.744  57.387  1.00 25.81           O  
ATOM   2759  CB  ALA A 364      17.212  31.262  60.247  1.00 23.95           C  
ATOM   2760  N   ASN A 365      17.086  28.333  59.137  1.00 25.67           N  
ATOM   2761  CA  ASN A 365      17.514  27.191  58.351  1.00 25.91           C  
ATOM   2762  C   ASN A 365      16.468  26.766  57.306  1.00 25.91           C  
ATOM   2763  O   ASN A 365      16.795  26.499  56.176  1.00 25.57           O  
ATOM   2764  CB  ASN A 365      17.682  25.997  59.288  1.00 27.16           C  
ATOM   2765  CG  ASN A 365      19.055  25.902  59.935  1.00 27.08           C  
ATOM   2766  OD1 ASN A 365      19.529  24.792  60.215  1.00 29.77           O  
ATOM   2767  ND2 ASN A 365      19.679  27.034  60.204  1.00 26.84           N  
ATOM   2768  N   ARG A 366      15.208  26.661  57.716  1.00 26.56           N  
ATOM   2769  CA  ARG A 366      14.131  26.276  56.796  1.00 26.91           C  
ATOM   2770  C   ARG A 366      14.036  27.292  55.666  1.00 27.55           C  
ATOM   2771  O   ARG A 366      14.033  26.928  54.477  1.00 26.58           O  
ATOM   2772  CB  ARG A 366      12.798  26.157  57.528  1.00 26.03           C  
ATOM   2773  CG  ARG A 366      12.752  24.945  58.465  1.00 26.03           C  
ATOM   2774  CD  ARG A 366      11.447  24.885  59.238  1.00 22.01           C  
ATOM   2775  NE  ARG A 366      11.277  23.592  59.875  1.00 22.74           N  
ATOM   2776  CZ  ARG A 366      10.146  23.170  60.424  1.00 24.34           C  
ATOM   2777  NH1 ARG A 366       9.067  23.932  60.402  1.00 24.29           N  
ATOM   2778  NH2 ARG A 366      10.083  21.976  60.982  1.00 22.61           N  
ATOM   2779  N   GLU A 367      14.031  28.562  56.061  1.00 28.07           N  
ATOM   2780  CA  GLU A 367      13.896  29.655  55.128  1.00 30.23           C  
ATOM   2781  C   GLU A 367      15.066  29.785  54.128  1.00 30.05           C  
ATOM   2782  O   GLU A 367      14.824  29.930  52.935  1.00 29.27           O  
ATOM   2783  CB  GLU A 367      13.623  30.953  55.889  1.00 30.56           C  
ATOM   2784  CG  GLU A 367      13.213  32.110  54.993  1.00 36.19           C  
ATOM   2785  CD  GLU A 367      11.927  31.843  54.200  1.00 42.10           C  
ATOM   2786  OE1 GLU A 367      11.054  31.058  54.674  1.00 43.15           O  
ATOM   2787  OE2 GLU A 367      11.794  32.438  53.098  1.00 44.00           O  
ATOM   2788  N   ARG A 368      16.313  29.714  54.614  1.00 30.85           N  
ATOM   2789  CA  ARG A 368      17.497  29.632  53.739  1.00 32.48           C  
ATOM   2790  C   ARG A 368      17.394  28.459  52.796  1.00 32.18           C  
ATOM   2791  O   ARG A 368      17.649  28.610  51.619  1.00 32.31           O  
ATOM   2792  CB  ARG A 368      18.801  29.482  54.521  1.00 31.79           C  
ATOM   2793  CG  ARG A 368      19.314  30.767  55.182  1.00 35.42           C  
ATOM   2794  CD  ARG A 368      20.758  30.588  55.721  1.00 36.23           C  
ATOM   2795  NE  ARG A 368      21.698  30.218  54.648  1.00 42.47           N  
ATOM   2796  CZ  ARG A 368      22.430  31.089  53.952  1.00 44.06           C  
ATOM   2797  NH1 ARG A 368      22.368  32.395  54.222  1.00 46.82           N  
ATOM   2798  NH2 ARG A 368      23.238  30.655  53.000  1.00 43.43           N  
ATOM   2799  N   GLU A 369      17.027  27.286  53.320  1.00 32.45           N  
ATOM   2800  CA  GLU A 369      16.888  26.109  52.483  1.00 33.39           C  
ATOM   2801  C   GLU A 369      15.836  26.309  51.394  1.00 33.25           C  
ATOM   2802  O   GLU A 369      16.091  26.030  50.233  1.00 33.39           O  
ATOM   2803  CB  GLU A 369      16.578  24.874  53.324  1.00 33.44           C  
ATOM   2804  CG  GLU A 369      17.317  23.620  52.899  1.00 34.52           C  
ATOM   2805  CD  GLU A 369      18.849  23.721  52.992  1.00 35.80           C  
ATOM   2806  OE1 GLU A 369      19.391  24.140  54.022  1.00 37.00           O  
ATOM   2807  OE2 GLU A 369      19.529  23.348  52.027  1.00 36.89           O  
ATOM   2808  N   LYS A 370      14.679  26.813  51.788  1.00 33.73           N  
ATOM   2809  CA  LYS A 370      13.554  27.083  50.893  1.00 35.44           C  
ATOM   2810  C   LYS A 370      13.945  27.981  49.711  1.00 35.16           C  
ATOM   2811  O   LYS A 370      13.672  27.645  48.548  1.00 34.85           O  
ATOM   2812  CB  LYS A 370      12.404  27.727  51.694  1.00 35.74           C  
ATOM   2813  CG  LYS A 370      11.055  27.840  50.948  1.00 36.83           C  
ATOM   2814  CD  LYS A 370      10.055  28.693  51.772  1.00 37.07           C  
ATOM   2815  CE  LYS A 370       8.712  28.883  51.071  1.00 38.85           C  
ATOM   2816  NZ  LYS A 370       8.851  29.717  49.835  1.00 42.27           N  
ATOM   2817  N   GLU A 371      14.593  29.096  50.043  1.00 35.25           N  
ATOM   2818  CA  GLU A 371      15.056  30.121  49.112  1.00 36.50           C  
ATOM   2819  C   GLU A 371      16.091  29.597  48.119  1.00 36.05           C  
ATOM   2820  O   GLU A 371      16.008  29.880  46.908  1.00 36.23           O  
ATOM   2821  CB  GLU A 371      15.543  31.346  49.927  1.00 36.85           C  
ATOM   2822  CG  GLU A 371      16.856  32.070  49.482  1.00 39.36           C  
ATOM   2823  CD  GLU A 371      17.563  32.837  50.650  1.00 39.87           C  
ATOM   2824  OE1 GLU A 371      16.857  33.261  51.620  1.00 44.38           O  
ATOM   2825  OE2 GLU A 371      18.817  33.005  50.590  1.00 40.03           O  
ATOM   2826  N   GLU A 372      17.041  28.799  48.606  1.00 35.24           N  
ATOM   2827  CA  GLU A 372      18.042  28.213  47.719  1.00 34.99           C  
ATOM   2828  C   GLU A 372      17.439  27.153  46.772  1.00 33.67           C  
ATOM   2829  O   GLU A 372      17.880  27.015  45.632  1.00 32.91           O  
ATOM   2830  CB  GLU A 372      19.207  27.634  48.519  1.00 34.53           C  
ATOM   2831  CG  GLU A 372      19.876  28.622  49.470  1.00 35.29           C  
ATOM   2832  CD  GLU A 372      20.721  27.913  50.563  1.00 37.55           C  
ATOM   2833  OE1 GLU A 372      20.447  26.719  50.901  1.00 39.73           O  
ATOM   2834  OE2 GLU A 372      21.665  28.552  51.097  1.00 40.20           O  
ATOM   2835  N   TRP A 373      16.447  26.409  47.252  1.00 32.46           N  
ATOM   2836  CA  TRP A 373      15.774  25.431  46.423  1.00 32.11           C  
ATOM   2837  C   TRP A 373      14.980  26.143  45.307  1.00 32.62           C  
ATOM   2838  O   TRP A 373      15.091  25.773  44.135  1.00 32.69           O  
ATOM   2839  CB  TRP A 373      14.880  24.519  47.277  1.00 31.85           C  
ATOM   2840  CG  TRP A 373      13.710  23.906  46.519  1.00 31.34           C  
ATOM   2841  CD1 TRP A 373      12.402  24.336  46.521  1.00 31.28           C  
ATOM   2842  CD2 TRP A 373      13.752  22.768  45.648  1.00 30.97           C  
ATOM   2843  NE1 TRP A 373      11.635  23.536  45.698  1.00 30.79           N  
ATOM   2844  CE2 TRP A 373      12.443  22.572  45.147  1.00 30.86           C  
ATOM   2845  CE3 TRP A 373      14.774  21.908  45.223  1.00 31.61           C  
ATOM   2846  CZ2 TRP A 373      12.131  21.540  44.265  1.00 30.77           C  
ATOM   2847  CZ3 TRP A 373      14.457  20.881  44.341  1.00 31.58           C  
ATOM   2848  CH2 TRP A 373      13.146  20.708  43.874  1.00 31.29           C  
ATOM   2849  N   ALA A 374      14.199  27.164  45.678  1.00 32.44           N  
ATOM   2850  CA  ALA A 374      13.442  27.967  44.729  1.00 32.57           C  
ATOM   2851  C   ALA A 374      14.345  28.536  43.627  1.00 33.13           C  
ATOM   2852  O   ALA A 374      13.986  28.466  42.445  1.00 33.78           O  
ATOM   2853  CB  ALA A 374      12.740  29.079  45.444  1.00 33.10           C  
ATOM   2854  N   ALA A 375      15.510  29.071  44.014  1.00 32.96           N  
ATOM   2855  CA  ALA A 375      16.519  29.598  43.088  1.00 32.81           C  
ATOM   2856  C   ALA A 375      17.111  28.538  42.151  1.00 33.43           C  
ATOM   2857  O   ALA A 375      17.333  28.799  40.974  1.00 32.77           O  
ATOM   2858  CB  ALA A 375      17.614  30.282  43.853  1.00 32.36           C  
ATOM   2859  N   ALA A 376      17.354  27.344  42.686  1.00 34.65           N  
ATOM   2860  CA  ALA A 376      17.877  26.212  41.914  1.00 36.19           C  
ATOM   2861  C   ALA A 376      16.896  25.726  40.873  1.00 37.45           C  
ATOM   2862  O   ALA A 376      17.293  25.112  39.895  1.00 37.40           O  
ATOM   2863  CB  ALA A 376      18.216  25.043  42.852  1.00 35.62           C  
ATOM   2864  N   SER A 377      15.613  25.967  41.125  1.00 39.81           N  
ATOM   2865  CA  SER A 377      14.533  25.402  40.325  1.00 42.22           C  
ATOM   2866  C   SER A 377      14.175  26.225  39.089  1.00 44.20           C  
ATOM   2867  O   SER A 377      13.666  25.672  38.123  1.00 45.49           O  
ATOM   2868  CB  SER A 377      13.297  25.114  41.184  1.00 41.75           C  
ATOM   2869  OG  SER A 377      13.601  24.110  42.126  1.00 39.43           O  
ATOM   2870  N   ARG A 378      14.458  27.521  39.104  1.00 46.17           N  
ATOM   2871  CA  ARG A 378      14.283  28.350  37.915  1.00 48.57           C  
ATOM   2872  C   ARG A 378      15.220  27.932  36.764  1.00 49.53           C  
ATOM   2873  O   ARG A 378      16.367  27.526  37.018  1.00 49.61           O  
ATOM   2874  CB  ARG A 378      14.496  29.817  38.274  1.00 49.02           C  
ATOM   2875  CG  ARG A 378      13.608  30.277  39.418  1.00 51.31           C  
ATOM   2876  CD  ARG A 378      13.758  31.757  39.650  1.00 55.09           C  
ATOM   2877  NE  ARG A 378      13.052  32.513  38.618  1.00 58.53           N  
ATOM   2878  CZ  ARG A 378      13.421  33.714  38.171  1.00 61.50           C  
ATOM   2879  NH1 ARG A 378      14.504  34.327  38.650  1.00 61.07           N  
ATOM   2880  NH2 ARG A 378      12.699  34.304  37.231  1.00 63.21           N  
ATOM   2881  N   PRO A 379      14.737  28.030  35.494  1.00 50.60           N  
ATOM   2882  CA  PRO A 379      15.529  27.641  34.291  1.00 51.15           C  
ATOM   2883  C   PRO A 379      16.518  28.714  33.787  1.00 51.40           C  
ATOM   2884  O   PRO A 379      17.412  28.417  32.966  1.00 51.61           O  
ATOM   2885  CB  PRO A 379      14.448  27.378  33.234  1.00 51.39           C  
ATOM   2886  CG  PRO A 379      13.325  28.373  33.605  1.00 51.38           C  
ATOM   2887  CD  PRO A 379      13.385  28.520  35.133  1.00 50.83           C  
TER    2888      PRO A 379                                                      
HETATM 2889  PA  FAD A 403      22.355  11.828  70.400  1.00 19.88           P  
HETATM 2890  O1A FAD A 403      21.664  11.213  69.233  1.00 20.81           O  
HETATM 2891  O2A FAD A 403      23.847  11.889  70.216  1.00 20.76           O  
HETATM 2892  O5B FAD A 403      22.088  11.021  71.755  1.00 24.60           O  
HETATM 2893  C5B FAD A 403      20.857  10.425  72.073  1.00 25.82           C  
HETATM 2894  C4B FAD A 403      21.214   9.237  72.963  1.00 25.50           C  
HETATM 2895  O4B FAD A 403      20.110   8.807  73.741  1.00 26.96           O  
HETATM 2896  C3B FAD A 403      21.623   8.057  72.100  1.00 25.67           C  
HETATM 2897  O3B FAD A 403      22.778   7.466  72.669  1.00 23.35           O  
HETATM 2898  C2B FAD A 403      20.418   7.136  72.127  1.00 24.46           C  
HETATM 2899  O2B FAD A 403      20.847   5.811  72.000  1.00 26.55           O  
HETATM 2900  C1B FAD A 403      19.872   7.426  73.512  1.00 23.72           C  
HETATM 2901  N9A FAD A 403      18.443   7.147  73.687  1.00 22.84           N  
HETATM 2902  C8A FAD A 403      17.450   7.218  72.741  1.00 23.15           C  
HETATM 2903  N7A FAD A 403      16.274   6.917  73.330  1.00 21.80           N  
HETATM 2904  C5A FAD A 403      16.510   6.625  74.637  1.00 21.16           C  
HETATM 2905  C6A FAD A 403      15.680   6.234  75.699  1.00 22.49           C  
HETATM 2906  N6A FAD A 403      14.470   5.703  75.479  1.00 19.79           N  
HETATM 2907  N1A FAD A 403      16.247   6.044  76.943  1.00 22.10           N  
HETATM 2908  C2A FAD A 403      17.597   6.206  77.168  1.00 21.78           C  
HETATM 2909  N3A FAD A 403      18.388   6.579  76.108  1.00 24.54           N  
HETATM 2910  C4A FAD A 403      17.863   6.789  74.868  1.00 21.65           C  
HETATM 2911  N1  FAD A 403      25.233  13.614  64.094  1.00 22.39           N  
HETATM 2912  C2  FAD A 403      25.909  14.145  63.046  1.00 21.94           C  
HETATM 2913  O2  FAD A 403      25.771  15.340  62.835  1.00 21.96           O  
HETATM 2914  N3  FAD A 403      26.671  13.314  62.257  1.00 21.36           N  
HETATM 2915  C4  FAD A 403      26.769  11.990  62.556  1.00 21.31           C  
HETATM 2916  O4  FAD A 403      27.463  11.271  61.868  1.00 22.48           O  
HETATM 2917  C4X FAD A 403      26.072  11.449  63.624  1.00 22.73           C  
HETATM 2918  N5  FAD A 403      26.126  10.086  63.933  1.00 23.01           N  
HETATM 2919  C5X FAD A 403      25.422   9.605  65.027  1.00 21.89           C  
HETATM 2920  C6  FAD A 403      25.491   8.243  65.337  1.00 22.05           C  
HETATM 2921  C7  FAD A 403      24.749   7.774  66.441  1.00 22.39           C  
HETATM 2922  C7M FAD A 403      24.804   6.328  66.804  1.00 21.90           C  
HETATM 2923  C8  FAD A 403      23.977   8.656  67.229  1.00 21.90           C  
HETATM 2924  C8M FAD A 403      23.169   8.170  68.395  1.00 21.97           C  
HETATM 2925  C9  FAD A 403      23.928  10.008  66.899  1.00 22.13           C  
HETATM 2926  C9A FAD A 403      24.643  10.494  65.794  1.00 22.02           C  
HETATM 2927  N10 FAD A 403      24.579  11.854  65.453  1.00 21.59           N  
HETATM 2928  C10 FAD A 403      25.300  12.295  64.394  1.00 21.27           C  
HETATM 2929  C1' FAD A 403      23.674  12.864  66.113  1.00 18.97           C  
HETATM 2930  C2' FAD A 403      24.463  13.802  67.039  1.00 20.07           C  
HETATM 2931  O2' FAD A 403      25.113  13.078  68.074  1.00 20.66           O  
HETATM 2932  C3' FAD A 403      23.535  14.806  67.690  1.00 21.29           C  
HETATM 2933  O3' FAD A 403      22.714  15.359  66.717  1.00 21.82           O  
HETATM 2934  C4' FAD A 403      24.190  15.982  68.423  1.00 22.57           C  
HETATM 2935  O4' FAD A 403      25.591  15.823  68.623  1.00 22.46           O  
HETATM 2936  C5' FAD A 403      23.462  16.194  69.764  1.00 21.04           C  
HETATM 2937  O5' FAD A 403      23.390  14.949  70.420  1.00 20.82           O  
HETATM 2938  P   FAD A 403      22.264  14.496  71.467  1.00 19.20           P  
HETATM 2939  O1P FAD A 403      22.931  13.997  72.692  1.00 17.52           O  
HETATM 2940  O2P FAD A 403      21.164  15.501  71.677  1.00 18.80           O  
HETATM 2941  O3P FAD A 403      21.616  13.219  70.735  1.00 21.55           O  
HETATM 2942  O   HOH A 404      25.705  28.236  77.317  1.00 27.89           O  
HETATM 2943  O   HOH A 405      27.862  21.197  66.165  1.00 16.76           O  
HETATM 2944  O   HOH A 406      20.390  21.496  67.256  1.00 25.81           O  
HETATM 2945  O   HOH A 407      18.914  15.037  72.982  1.00 12.64           O  
HETATM 2946  O   HOH A 408      22.577  12.445  74.807  1.00 15.27           O  
HETATM 2947  O   HOH A 409      19.666  12.562  67.708  1.00 22.41           O  
HETATM 2948  O   HOH A 410      44.305  26.994  67.127  1.00 26.74           O  
HETATM 2949  O   HOH A 411      42.032  27.345  65.543  1.00 14.97           O  
HETATM 2950  O   HOH A 412      26.831  23.237  51.100  1.00 46.44           O  
HETATM 2951  O   HOH A 413      20.848  17.295  42.270  1.00 17.78           O  
HETATM 2952  O   HOH A 414      32.881  19.961  38.019  1.00 26.34           O  
HETATM 2953  O   HOH A 415      24.281  10.800  55.703  1.00 30.40           O  
HETATM 2954  O   HOH A 416      35.643  30.901  71.223  1.00 45.42           O  
HETATM 2955  O   HOH A 417      44.155  16.244  58.640  1.00 19.84           O  
HETATM 2956  O   HOH A 418      42.947  13.976  59.537  1.00 26.93           O  
HETATM 2957  O   HOH A 419      15.421  23.741  60.521  1.00 28.20           O  
HETATM 2958  O   HOH A 420      21.947   5.248  49.593  1.00 22.47           O  
HETATM 2959  O   HOH A 421      10.569  20.430  52.461  1.00 35.89           O  
HETATM 2960  O   HOH A 422      11.948  20.354  57.830  1.00 24.15           O  
HETATM 2961  O   HOH A 423      25.307   7.749  71.569  1.00 18.05           O  
HETATM 2962  O   HOH A 424       9.026  -0.278  82.631  1.00 37.79           O  
HETATM 2963  O   HOH A 425       6.324  16.751  84.750  1.00 21.38           O  
HETATM 2964  O   HOH A 426      17.742  23.359  61.446  1.00 25.25           O  
HETATM 2965  O   HOH A 427       9.288  22.985  84.755  1.00 33.31           O  
HETATM 2966  O   HOH A 428      20.187  18.813  65.978  1.00 25.87           O  
HETATM 2967  O   HOH A 429       9.574  24.078  82.551  1.00 35.67           O  
HETATM 2968  O   HOH A 430      40.070  25.903  64.413  1.00 27.64           O  
HETATM 2969  O   HOH A 431      42.163  20.274  54.756  1.00 20.18           O  
HETATM 2970  O   HOH A 432      53.091  20.803  53.399  1.00 27.98           O  
HETATM 2971  O   HOH A 433      39.356   5.443  52.584  1.00 23.03           O  
HETATM 2972  O   HOH A 434      27.257  25.992  84.251  1.00 36.65           O  
HETATM 2973  O   HOH A 435      41.560  16.638  78.366  1.00 30.90           O  
HETATM 2974  O   HOH A 436       7.945  18.240  63.543  1.00 41.33           O  
HETATM 2975  O   HOH A 437      19.764   9.065  68.933  1.00 28.27           O  
HETATM 2976  O   HOH A 438      22.484   7.604  58.828  1.00 20.26           O  
HETATM 2977  O   HOH A 439      44.944  25.883  62.872  1.00 34.38           O  
HETATM 2978  O   HOH A 440      14.073  22.326  49.897  1.00 32.15           O  
HETATM 2979  O   HOH A 441       2.114  15.203  80.167  1.00 36.28           O  
HETATM 2980  O   HOH A 442      40.703  22.164  78.969  1.00 25.83           O  
HETATM 2981  O   HOH A 443      13.441  20.787  66.227  1.00 24.92           O  
HETATM 2982  O   HOH A 444       9.770  12.693  70.184  1.00 32.39           O  
HETATM 2983  O   HOH A 445       7.872  19.505  67.647  1.00 32.29           O  
HETATM 2984  O   HOH A 446      24.421  19.522  77.499  1.00 41.88           O  
HETATM 2985  O   HOH A 447      38.158  12.775  65.469  1.00 30.77           O  
HETATM 2986  O   HOH A 448      18.319  16.094  61.551  1.00 31.04           O  
HETATM 2987  O   HOH A 449      35.511  29.104  63.666  1.00 39.41           O  
HETATM 2988  O   HOH A 450      47.564  30.589  58.610  1.00 37.93           O  
HETATM 2989  O   HOH A 451      31.525  29.945  68.314  1.00 34.24           O  
HETATM 2990  O   HOH A 452      46.950  16.525  55.003  1.00 36.93           O  
HETATM 2991  O   HOH A 453      39.286  20.438  59.175  1.00 38.96           O  
HETATM 2992  O   HOH A 454       7.761  16.458  56.751  1.00 37.25           O  
HETATM 2993  O   HOH A 455      11.930  21.742  68.330  1.00 32.86           O  
HETATM 2994  O   HOH A 456      13.817  14.666  52.670  1.00 44.70           O  
HETATM 2995  O   HOH A 457      21.295  19.375  69.676  1.00 25.14           O  
CONECT  770  777                                                                
CONECT  777  770  778                                                           
CONECT  778  777  779  781                                                      
CONECT  779  778  780  785                                                      
CONECT  780  779                                                                
CONECT  781  778  782                                                           
CONECT  782  781  783                                                           
CONECT  783  782  784                                                           
CONECT  784  783                                                                
CONECT  785  779                                                                
CONECT 1351 1356                                                                
CONECT 1356 1351 1357                                                           
CONECT 1357 1356 1358 1360                                                      
CONECT 1358 1357 1359 1364                                                      
CONECT 1359 1358                                                                
CONECT 1360 1357 1361                                                           
CONECT 1361 1360 1362                                                           
CONECT 1362 1361 1363                                                           
CONECT 1363 1362                                                                
CONECT 1364 1358                                                                
CONECT 1488 1493                                                                
CONECT 1493 1488 1494                                                           
CONECT 1494 1493 1495 1497                                                      
CONECT 1495 1494 1496 1501                                                      
CONECT 1496 1495                                                                
CONECT 1497 1494 1498                                                           
CONECT 1498 1497 1499                                                           
CONECT 1499 1498 1500                                                           
CONECT 1500 1499                                                                
CONECT 1501 1495                                                                
CONECT 1750 1754                                                                
CONECT 1754 1750 1755                                                           
CONECT 1755 1754 1756 1758                                                      
CONECT 1756 1755 1757 1762                                                      
CONECT 1757 1756                                                                
CONECT 1758 1755 1759                                                           
CONECT 1759 1758 1760                                                           
CONECT 1760 1759 1761                                                           
CONECT 1761 1760                                                                
CONECT 1762 1756                                                                
CONECT 2193 2198                                                                
CONECT 2198 2193 2199                                                           
CONECT 2199 2198 2200 2202                                                      
CONECT 2200 2199 2201 2206                                                      
CONECT 2201 2200                                                                
CONECT 2202 2199 2203                                                           
CONECT 2203 2202 2204                                                           
CONECT 2204 2203 2205                                                           
CONECT 2205 2204                                                                
CONECT 2206 2200                                                                
CONECT 2388 2394                                                                
CONECT 2394 2388 2395                                                           
CONECT 2395 2394 2396 2398                                                      
CONECT 2396 2395 2397 2402                                                      
CONECT 2397 2396                                                                
CONECT 2398 2395 2399                                                           
CONECT 2399 2398 2400                                                           
CONECT 2400 2399 2401                                                           
CONECT 2401 2400                                                                
CONECT 2402 2396                                                                
CONECT 2416 2421                                                                
CONECT 2421 2416 2422                                                           
CONECT 2422 2421 2423 2425                                                      
CONECT 2423 2422 2424 2429                                                      
CONECT 2424 2423                                                                
CONECT 2425 2422 2426                                                           
CONECT 2426 2425 2427                                                           
CONECT 2427 2426 2428                                                           
CONECT 2428 2427                                                                
CONECT 2429 2423                                                                
CONECT 2889 2890 2891 2892 2941                                                 
CONECT 2890 2889                                                                
CONECT 2891 2889                                                                
CONECT 2892 2889 2893                                                           
CONECT 2893 2892 2894                                                           
CONECT 2894 2893 2895 2896                                                      
CONECT 2895 2894 2900                                                           
CONECT 2896 2894 2897 2898                                                      
CONECT 2897 2896                                                                
CONECT 2898 2896 2899 2900                                                      
CONECT 2899 2898                                                                
CONECT 2900 2895 2898 2901                                                      
CONECT 2901 2900 2902 2910                                                      
CONECT 2902 2901 2903                                                           
CONECT 2903 2902 2904                                                           
CONECT 2904 2903 2905 2910                                                      
CONECT 2905 2904 2906 2907                                                      
CONECT 2906 2905                                                                
CONECT 2907 2905 2908                                                           
CONECT 2908 2907 2909                                                           
CONECT 2909 2908 2910                                                           
CONECT 2910 2901 2904 2909                                                      
CONECT 2911 2912 2928                                                           
CONECT 2912 2911 2913 2914                                                      
CONECT 2913 2912                                                                
CONECT 2914 2912 2915                                                           
CONECT 2915 2914 2916 2917                                                      
CONECT 2916 2915                                                                
CONECT 2917 2915 2918 2928                                                      
CONECT 2918 2917 2919                                                           
CONECT 2919 2918 2920 2926                                                      
CONECT 2920 2919 2921                                                           
CONECT 2921 2920 2922 2923                                                      
CONECT 2922 2921                                                                
CONECT 2923 2921 2924 2925                                                      
CONECT 2924 2923                                                                
CONECT 2925 2923 2926                                                           
CONECT 2926 2919 2925 2927                                                      
CONECT 2927 2926 2928 2929                                                      
CONECT 2928 2911 2917 2927                                                      
CONECT 2929 2927 2930                                                           
CONECT 2930 2929 2931 2932                                                      
CONECT 2931 2930                                                                
CONECT 2932 2930 2933 2934                                                      
CONECT 2933 2932                                                                
CONECT 2934 2932 2935 2936                                                      
CONECT 2935 2934                                                                
CONECT 2936 2934 2937                                                           
CONECT 2937 2936 2938                                                           
CONECT 2938 2937 2939 2940 2941                                                 
CONECT 2939 2938                                                                
CONECT 2940 2938                                                                
CONECT 2941 2889 2938                                                           
MASTER      352    0    8   15   17    0    7    6 2976    1  123   31          
END                                                                             



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

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.