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***  BACTERIAL CELL DIVISION INHIBITOR 21-APR-03 1OFU  ***

elNémo ID: 23013017404219642

Job options:

ID        	=	 23013017404219642
JOBID     	=	 BACTERIAL CELL DIVISION INHIBITOR 21-APR-03 1OFU
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    BACTERIAL CELL DIVISION INHIBITOR       21-APR-03   1OFU              
TITLE     CRYSTAL STRUCTURE OF SULA:FTSZ FROM PSEUDOMONAS AERUGINOSA            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN PA3008;                               
COMPND   3 CHAIN: X, Y;                                                         
COMPND   4 FRAGMENT: RESIDUES 43-161;                                           
COMPND   5 SYNONYM: SULA;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: FIRST 42 RESIDUES REMOVED FROM N-TERMINUS;            
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CELL DIVISION PROTEIN FTSZ;                                
COMPND  10 CHAIN: A, B;                                                         
COMPND  11 FRAGMENT: RESIDUES 1-320;                                            
COMPND  12 SYNONYM: FTSZ;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: LAST 75 RESIDUES REMOVED FROM C-TERMINUS              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PHIS17;                                   
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   9 ORGANISM_TAXID: 287;                                                 
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PHIS17                                    
KEYWDS    BACTERIAL CELL DIVISION INHIBITOR, FTSZ, SULA PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.CORDELL,E.J.H.ROBINSON,J.LOWE                                     
REVDAT   3   24-FEB-09 1OFU    1       VERSN                                    
REVDAT   2   26-JUN-03 1OFU    1       JRNL                                     
REVDAT   1   19-JUN-03 1OFU    0                                                
JRNL        AUTH   S.C.CORDELL,E.J.H.ROBINSON,J.LOWE                            
JRNL        TITL   CRYSTAL STRUCTURE OF THE SOS CELL DIVISION                   
JRNL        TITL 2 INHIBITOR SULA AND IN COMPLEX WITH FTSZ                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100  7889 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12808143                                                     
JRNL        DOI    10.1073/PNAS.1330742100                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.1                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 60260                          
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 SET) : 0.2159                          
REMARK   3   FREE R VALUE                     : 0.2554                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3011                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 50                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.1                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.11                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1117                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3536                       
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5                            
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 47                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6244                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 441                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.820                                                
REMARK   3    B22 (A**2) : -19.056                                              
REMARK   3    B33 (A**2) : 12.236                                               
REMARK   3    B12 (A**2) : 0.0                                                  
REMARK   3    B13 (A**2) : 0.0                                                  
REMARK   3    B23 (A**2) : 0.0                                                  
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.261                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OFU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12614.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93930                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60044                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: MAD MODEL FROM C2 CRYSTAL FORM                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.79500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.52000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      120.52000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.79500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X, Y, B                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PHE B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     ALA B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     LEU B   320                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY X 161    CA   C    O                                         
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    PRO B 234   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
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 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    ASN A  33     -132.20    -92.50                                   
REMARK 500    ASN A  34       63.66   -115.05                                   
REMARK 500    ASP A 252       29.32    -78.99                                   
REMARK 500    PRO A 269       -5.01    -58.98                                   
REMARK 500    ASP A 305      -37.33     65.51                                   
REMARK 500    ASN B  33     -141.91   -114.58                                   
REMARK 500    ASN B  34     -124.53    -75.76                                   
REMARK 500    VAL B  35       74.41     60.41                                   
REMARK 500    ASN B  52       58.76    -94.43                                   
REMARK 500    GLU B 220       45.95     32.85                                   
REMARK 500    GLU B 251      -78.27    -41.52                                   
REMARK 500    PRO B 269       -6.82    -59.76                                   
REMARK 500    ASP B 305      -38.10     61.75                                   
REMARK 500    ALA X  45     -179.80   -176.44                                   
REMARK 500    ALA X  75       61.80    -69.58                                   
REMARK 500    ALA X  82       64.31     39.73                                   
REMARK 500    ALA Y  45     -169.14   -166.58                                   
REMARK 500    ALA Y  75       59.77    -63.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A1318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B1318                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OFT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SULA FROM PSEUDOMONAS                          
REMARK 900  AERUGINOSA                                                          
DBREF  1OFU A    1   320  UNP    P47204   FTSZ_PSEAE       1    320             
DBREF  1OFU B    1   320  UNP    P47204   FTSZ_PSEAE       1    320             
DBREF  1OFU X   43   161  UNP    Q9HZJ8   Q9HZJ8          43    161             
DBREF  1OFU Y   43   161  UNP    Q9HZJ8   Q9HZJ8          43    161             
SEQRES   1 A  320  MET PHE GLU LEU VAL ASP ASN ILE ALA GLN THR ALA VAL          
SEQRES   2 A  320  ILE LYS VAL ILE GLY VAL GLY GLY GLY GLY GLY ASN ALA          
SEQRES   3 A  320  VAL ASN HIS MET ALA LYS ASN ASN VAL GLU GLY VAL GLU          
SEQRES   4 A  320  PHE ILE CYS ALA ASN THR ASP ALA GLN ALA LEU LYS ASN          
SEQRES   5 A  320  ILE ALA ALA ARG THR VAL LEU GLN LEU GLY PRO GLY VAL          
SEQRES   6 A  320  THR LYS GLY LEU GLY ALA GLY ALA ASN PRO GLU VAL GLY          
SEQRES   7 A  320  ARG GLN ALA ALA LEU GLU ASP ARG GLU ARG ILE SER GLU          
SEQRES   8 A  320  VAL LEU GLU GLY ALA ASP MET VAL PHE ILE THR THR GLY          
SEQRES   9 A  320  MET GLY GLY GLY THR GLY THR GLY ALA ALA PRO ILE ILE          
SEQRES  10 A  320  ALA GLU VAL ALA LYS GLU MET GLY ILE LEU THR VAL ALA          
SEQRES  11 A  320  VAL VAL THR ARG PRO PHE PRO PHE GLU GLY ARG LYS ARG          
SEQRES  12 A  320  MET GLN ILE ALA ASP GLU GLY ILE ARG ALA LEU ALA GLU          
SEQRES  13 A  320  SER VAL ASP SER LEU ILE THR ILE PRO ASN GLU LYS LEU          
SEQRES  14 A  320  LEU THR ILE LEU GLY LYS ASP ALA SER LEU LEU ALA ALA          
SEQRES  15 A  320  PHE ALA LYS ALA ASP ASP VAL LEU ALA GLY ALA VAL ARG          
SEQRES  16 A  320  GLY ILE SER ASP ILE ILE LYS ARG PRO GLY MET ILE ASN          
SEQRES  17 A  320  VAL ASP PHE ALA ASP VAL LYS THR VAL MET SER GLU MET          
SEQRES  18 A  320  GLY MET ALA MET MET GLY THR GLY CYS ALA SER GLY PRO          
SEQRES  19 A  320  ASN ARG ALA ARG GLU ALA THR GLU ALA ALA ILE ARG ASN          
SEQRES  20 A  320  PRO LEU LEU GLU ASP VAL ASN LEU GLN GLY ALA ARG GLY          
SEQRES  21 A  320  ILE LEU VAL ASN ILE THR ALA GLY PRO ASP LEU SER LEU          
SEQRES  22 A  320  GLY GLU TYR SER ASP VAL GLY ASN ILE ILE GLU GLN PHE          
SEQRES  23 A  320  ALA SER GLU HIS ALA THR VAL LYS VAL GLY THR VAL ILE          
SEQRES  24 A  320  ASP ALA ASP MET ARG ASP GLU LEU HIS VAL THR VAL VAL          
SEQRES  25 A  320  ALA THR GLY LEU GLY ALA ARG LEU                              
SEQRES   1 B  320  MET PHE GLU LEU VAL ASP ASN ILE ALA GLN THR ALA VAL          
SEQRES   2 B  320  ILE LYS VAL ILE GLY VAL GLY GLY GLY GLY GLY ASN ALA          
SEQRES   3 B  320  VAL ASN HIS MET ALA LYS ASN ASN VAL GLU GLY VAL GLU          
SEQRES   4 B  320  PHE ILE CYS ALA ASN THR ASP ALA GLN ALA LEU LYS ASN          
SEQRES   5 B  320  ILE ALA ALA ARG THR VAL LEU GLN LEU GLY PRO GLY VAL          
SEQRES   6 B  320  THR LYS GLY LEU GLY ALA GLY ALA ASN PRO GLU VAL GLY          
SEQRES   7 B  320  ARG GLN ALA ALA LEU GLU ASP ARG GLU ARG ILE SER GLU          
SEQRES   8 B  320  VAL LEU GLU GLY ALA ASP MET VAL PHE ILE THR THR GLY          
SEQRES   9 B  320  MET GLY GLY GLY THR GLY THR GLY ALA ALA PRO ILE ILE          
SEQRES  10 B  320  ALA GLU VAL ALA LYS GLU MET GLY ILE LEU THR VAL ALA          
SEQRES  11 B  320  VAL VAL THR ARG PRO PHE PRO PHE GLU GLY ARG LYS ARG          
SEQRES  12 B  320  MET GLN ILE ALA ASP GLU GLY ILE ARG ALA LEU ALA GLU          
SEQRES  13 B  320  SER VAL ASP SER LEU ILE THR ILE PRO ASN GLU LYS LEU          
SEQRES  14 B  320  LEU THR ILE LEU GLY LYS ASP ALA SER LEU LEU ALA ALA          
SEQRES  15 B  320  PHE ALA LYS ALA ASP ASP VAL LEU ALA GLY ALA VAL ARG          
SEQRES  16 B  320  GLY ILE SER ASP ILE ILE LYS ARG PRO GLY MET ILE ASN          
SEQRES  17 B  320  VAL ASP PHE ALA ASP VAL LYS THR VAL MET SER GLU MET          
SEQRES  18 B  320  GLY MET ALA MET MET GLY THR GLY CYS ALA SER GLY PRO          
SEQRES  19 B  320  ASN ARG ALA ARG GLU ALA THR GLU ALA ALA ILE ARG ASN          
SEQRES  20 B  320  PRO LEU LEU GLU ASP VAL ASN LEU GLN GLY ALA ARG GLY          
SEQRES  21 B  320  ILE LEU VAL ASN ILE THR ALA GLY PRO ASP LEU SER LEU          
SEQRES  22 B  320  GLY GLU TYR SER ASP VAL GLY ASN ILE ILE GLU GLN PHE          
SEQRES  23 B  320  ALA SER GLU HIS ALA THR VAL LYS VAL GLY THR VAL ILE          
SEQRES  24 B  320  ASP ALA ASP MET ARG ASP GLU LEU HIS VAL THR VAL VAL          
SEQRES  25 B  320  ALA THR GLY LEU GLY ALA ARG LEU                              
SEQRES   1 X  119  PRO ALA ALA PHE SER GLU LEU SER LEU SER GLY LEU PRO          
SEQRES   2 X  119  GLY HIS CYS LEU THR LEU LEU ALA PRO ILE LEU ARG GLU          
SEQRES   3 X  119  LEU SER GLU GLU GLN ASP ALA ARG TRP LEU THR LEU ILE          
SEQRES   4 X  119  ALA PRO PRO ALA SER LEU THR HIS GLU TRP LEU ARG ARG          
SEQRES   5 X  119  ALA GLY LEU ASN ARG GLU ARG ILE LEU LEU LEU GLN ALA          
SEQRES   6 X  119  LYS ASP ASN ALA ALA ALA LEU ALA LEU SER CYS GLU ALA          
SEQRES   7 X  119  LEU ARG LEU GLY ARG SER HIS THR VAL VAL SER TRP LEU          
SEQRES   8 X  119  GLU PRO LEU SER ARG ALA ALA ARG LYS GLN LEU SER ARG          
SEQRES   9 X  119  ALA ALA GLN LEU GLY GLN ALA GLN SER LEU ASN ILE ARG          
SEQRES  10 X  119  LEU GLY                                                      
SEQRES   1 Y  119  PRO ALA ALA PHE SER GLU LEU SER LEU SER GLY LEU PRO          
SEQRES   2 Y  119  GLY HIS CYS LEU THR LEU LEU ALA PRO ILE LEU ARG GLU          
SEQRES   3 Y  119  LEU SER GLU GLU GLN ASP ALA ARG TRP LEU THR LEU ILE          
SEQRES   4 Y  119  ALA PRO PRO ALA SER LEU THR HIS GLU TRP LEU ARG ARG          
SEQRES   5 Y  119  ALA GLY LEU ASN ARG GLU ARG ILE LEU LEU LEU GLN ALA          
SEQRES   6 Y  119  LYS ASP ASN ALA ALA ALA LEU ALA LEU SER CYS GLU ALA          
SEQRES   7 Y  119  LEU ARG LEU GLY ARG SER HIS THR VAL VAL SER TRP LEU          
SEQRES   8 Y  119  GLU PRO LEU SER ARG ALA ALA ARG LYS GLN LEU SER ARG          
SEQRES   9 Y  119  ALA ALA GLN LEU GLY GLN ALA GLN SER LEU ASN ILE ARG          
SEQRES  10 Y  119  LEU GLY                                                      
HET    GDP  A1318      28                                                       
HET    GDP  B1318      28                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  HOH   *441(H2 O1)                                                   
HELIX    1   1 GLY A   20  ASN A   33  1                                  14
HELIX    2   2 ALA A   47  LYS A   51  1                                   5
HELIX    3   3 GLY A   62  LYS A   67  1                                   6
HELIX    4   4 ASN A   74  GLU A   94  1                                  21
HELIX    5   5 GLY A  108  MET A  124  1                                  17
HELIX    6   6 PHE A  136  GLU A  156  1                                  21
HELIX    7   7 ASN A  166  ARG A  203  1                                  38
HELIX    8   8 ASP A  210  SER A  219  1                                  10
HELIX    9   9 ASN A  235  GLU A  251  1                                  17
HELIX   10  10 ASN A  254  ALA A  258  1                                   5
HELIX   11  11 SER A  272  ALA A  287  1                                  16
SHEET    1   1 1 ILE A  14  VAL A  19  0
SHEET    2   2 1 VAL A  38  ASN A  44  0
SHEET    3   3 1 THR A  57  GLN A  60  0
SHEET    4   4 1 MET A  98  GLY A 104  0
SHEET    5   5 1 LEU A 127  ARG A 134  0
SHEET    6   6 1 SER A 160  PRO A 165  0
SHEET    7   7 1 GLY A 222  SER A 232  0
SHEET    8   8 1 GLY A 260  ALA A 267  0
SHEET    9   9 1 THR A 292  ILE A 299  0
SHEET   10  10 1 GLU A 306  THR A 314  0
CISPEP   1 GLU X  134    PRO X  135          0        -0.22                     
CISPEP   2 GLU Y  134    PRO Y  135          0         0.12                     
SITE     1 AC1 25 GLY A  20  GLY A  21  GLY A  22  ASN A  25                    
SITE     2 AC1 25 GLY A 104  GLY A 107  GLY A 108  THR A 109                    
SITE     3 AC1 25 GLY A 110  GLU A 139  ARG A 143  ASN A 166                    
SITE     4 AC1 25 PHE A 183  ALA A 186  ASP A 187  HOH A2006                    
SITE     5 AC1 25 HOH A2080  HOH A2081  HOH A2082  HOH A2118                    
SITE     6 AC1 25 HOH A2178  HOH A2179  HOH A2180  HOH A2181                    
SITE     7 AC1 25 HOH A2182                                                     
SITE     1 AC2 28 GLY B  20  GLY B  21  GLY B  22  ASN B  25                    
SITE     2 AC2 28 GLY B 104  GLY B 107  GLY B 108  THR B 109                    
SITE     3 AC2 28 GLY B 110  PRO B 135  GLU B 139  ARG B 143                    
SITE     4 AC2 28 ASN B 166  PHE B 183  ALA B 186  ASP B 187                    
SITE     5 AC2 28 LEU B 190  HOH B2050  HOH B2082  HOH B2150                    
SITE     6 AC2 28 HOH B2151  HOH B2152  HOH B2153  HOH B2154                    
SITE     7 AC2 28 HOH B2155  HOH B2156  HOH B2157  HOH B2158                    
CRYST1   55.590   75.410  241.040  90.00  90.00  90.00 P 21 21 21    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      0.017989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013261  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004149        0.00000                         
ATOM      1  N   THR A  11     -46.002  83.789 282.067  1.00 49.38           N
ATOM      2  CA  THR A  11     -47.118  84.680 282.503  1.00 50.77           C
ATOM      3  C   THR A  11     -48.001  83.981 283.539  1.00 49.37           C
ATOM      4  O   THR A  11     -49.042  84.507 283.939  1.00 50.30           O
ATOM      5  CB  THR A  11     -48.001  85.103 281.300  1.00 51.38           C
ATOM      6  OG1 THR A  11     -49.044  85.972 281.756  1.00 55.53           O
ATOM      7  CG2 THR A  11     -48.626  83.883 280.632  1.00 48.61           C
ATOM      8  N   ALA A  12     -47.572  82.801 283.977  1.00 44.24           N
ATOM      9  CA  ALA A  12     -48.326  82.030 284.958  1.00 42.85           C
ATOM     10  C   ALA A  12     -48.739  82.869 286.164  1.00 42.41           C
ATOM     11  O   ALA A  12     -47.954  83.673 286.678  1.00 41.41           O
ATOM     12  CB  ALA A  12     -47.511  80.828 285.418  1.00 36.92           C
ATOM     13  N   VAL A  13     -49.983  82.694 286.605  1.00 37.80           N
ATOM     14  CA  VAL A  13     -50.459  83.425 287.771  1.00 34.83           C
ATOM     15  C   VAL A  13     -50.206  82.527 288.981  1.00 31.79           C
ATOM     16  O   VAL A  13     -50.804  81.464 289.119  1.00 34.57           O
ATOM     17  CB  VAL A  13     -51.968  83.758 287.671  1.00 38.63           C
ATOM     18  CG1 VAL A  13     -52.394  84.567 288.884  1.00 37.60           C
ATOM     19  CG2 VAL A  13     -52.255  84.544 286.385  1.00 37.04           C
ATOM     20  N   ILE A  14     -49.290  82.954 289.839  1.00 31.98           N
ATOM     21  CA  ILE A  14     -48.936  82.200 291.032  1.00 32.51           C
ATOM     22  C   ILE A  14     -49.413  82.913 292.286  1.00 30.55           C
ATOM     23  O   ILE A  14     -49.113  84.088 292.497  1.00 32.76           O
ATOM     24  CB  ILE A  14     -47.410  82.031 291.155  1.00 32.68           C
ATOM     25  CG1 ILE A  14     -46.843  81.472 289.851  1.00 30.73           C
ATOM     26  CG2 ILE A  14     -47.086  81.151 292.363  1.00 30.67           C
ATOM     27  CD1 ILE A  14     -45.334  81.358 289.841  1.00 28.95           C
ATOM     28  N   LYS A  15     -50.145  82.200 293.129  1.00 29.47           N
ATOM     29  CA  LYS A  15     -50.628  82.798 294.362  1.00 28.96           C
ATOM     30  C   LYS A  15     -50.118  82.021 295.559  1.00 28.49           C
ATOM     31  O   LYS A  15     -50.033  80.789 295.526  1.00 30.79           O
ATOM     32  CB  LYS A  15     -52.157  82.844 294.362  1.00 31.62           C
ATOM     33  CG  LYS A  15     -52.720  83.678 293.229  1.00 35.02           C
ATOM     34  CD  LYS A  15     -54.226  83.857 293.335  1.00 34.35           C
ATOM     35  CE  LYS A  15     -54.725  84.724 292.183  1.00 39.00           C
ATOM     36  NZ  LYS A  15     -56.114  85.202 292.378  1.00 45.68           N
ATOM     37  N   VAL A  16     -49.765  82.751 296.609  1.00 28.72           N
ATOM     38  CA  VAL A  16     -49.255  82.150 297.834  1.00 29.36           C
ATOM     39  C   VAL A  16     -50.184  82.484 298.994  1.00 32.24           C
ATOM     40  O   VAL A  16     -50.346  83.658 299.367  1.00 27.94           O
ATOM     41  CB  VAL A  16     -47.840  82.675 298.180  1.00 28.38           C
ATOM     42  CG1 VAL A  16     -47.345  82.026 299.468  1.00 29.50           C
ATOM     43  CG2 VAL A  16     -46.878  82.373 297.038  1.00 33.85           C
ATOM     44  N   ILE A  17     -50.805  81.465 299.570  1.00 24.21           N
ATOM     45  CA  ILE A  17     -51.688  81.737 300.684  1.00 28.34           C
ATOM     46  C   ILE A  17     -51.158  81.204 302.005  1.00 25.28           C
ATOM     47  O   ILE A  17     -50.933  80.002 302.159  1.00 25.95           O
ATOM     48  CB  ILE A  17     -53.118  81.200 300.413  1.00 31.34           C
ATOM     49  CG1 ILE A  17     -54.024  81.519 301.605  1.00 33.86           C
ATOM     50  CG2 ILE A  17     -53.088  79.712 300.149  1.00 37.28           C
ATOM     51  CD1 ILE A  17     -55.506  81.324 301.304  1.00 42.53           C
ATOM     52  N   GLY A  18     -50.940  82.127 302.941  1.00 23.24           N
ATOM     53  CA  GLY A  18     -50.464  81.786 304.270  1.00 24.86           C
ATOM     54  C   GLY A  18     -51.679  81.612 305.162  1.00 30.54           C
ATOM     55  O   GLY A  18     -52.507  82.520 305.285  1.00 32.47           O
ATOM     56  N   VAL A  19     -51.785  80.447 305.790  1.00 28.26           N
ATOM     57  CA  VAL A  19     -52.931  80.123 306.631  1.00 23.50           C
ATOM     58  C   VAL A  19     -52.582  80.063 308.115  1.00 27.53           C
ATOM     59  O   VAL A  19     -51.711  79.295 308.525  1.00 28.19           O
ATOM     60  CB  VAL A  19     -53.535  78.753 306.206  1.00 25.15           C
ATOM     61  CG1 VAL A  19     -54.902  78.541 306.872  1.00 25.21           C
ATOM     62  CG2 VAL A  19     -53.675  78.694 304.686  1.00 23.98           C
ATOM     63  N   GLY A  20     -53.268  80.880 308.913  1.00 27.75           N
ATOM     64  CA  GLY A  20     -53.031  80.904 310.347  1.00 27.22           C
ATOM     65  C   GLY A  20     -51.911  81.842 310.766  1.00 30.38           C
ATOM     66  O   GLY A  20     -51.378  82.591 309.942  1.00 28.96           O
ATOM     67  N   GLY A  21     -51.555  81.794 312.051  1.00 28.05           N
ATOM     68  CA  GLY A  21     -50.504  82.645 312.584  1.00 25.47           C
ATOM     69  C   GLY A  21     -49.128  82.433 311.980  1.00 27.13           C
ATOM     70  O   GLY A  21     -48.533  83.361 311.442  1.00 30.52           O
ATOM     71  N   GLY A  22     -48.615  81.214 312.076  1.00 28.22           N
ATOM     72  CA  GLY A  22     -47.306  80.908 311.523  1.00 26.46           C
ATOM     73  C   GLY A  22     -47.303  81.075 310.017  1.00 29.83           C
ATOM     74  O   GLY A  22     -46.343  81.587 309.436  1.00 26.06           O
ATOM     75  N   GLY A  23     -48.392  80.648 309.383  1.00 25.99           N
ATOM     76  CA  GLY A  23     -48.502  80.773 307.943  1.00 24.29           C
ATOM     77  C   GLY A  23     -48.445  82.227 307.516  1.00 26.72           C
ATOM     78  O   GLY A  23     -47.804  82.564 306.517  1.00 25.04           O
ATOM     79  N   GLY A  24     -49.121  83.090 308.269  1.00 27.44           N
ATOM     80  CA  GLY A  24     -49.118  84.508 307.947  1.00 28.13           C
ATOM     81  C   GLY A  24     -47.730  85.109 308.087  1.00 30.36           C
ATOM     82  O   GLY A  24     -47.302  85.896 307.247  1.00 31.10           O
ATOM     83  N   ASN A  25     -47.027  84.753 309.157  1.00 28.66           N
ATOM     84  CA  ASN A  25     -45.678  85.263 309.379  1.00 31.60           C
ATOM     85  C   ASN A  25     -44.730  84.883 308.243  1.00 27.97           C
ATOM     86  O   ASN A  25     -43.880  85.672 307.848  1.00 34.30           O
ATOM     87  CB  ASN A  25     -45.126  84.741 310.711  1.00 29.42           C
ATOM     88  CG  ASN A  25     -45.845  85.337 311.907  1.00 35.71           C
ATOM     89  OD1 ASN A  25     -45.655  84.905 313.054  1.00 31.35           O
ATOM     90  ND2 ASN A  25     -46.679  86.336 311.646  1.00 32.09           N
ATOM     91  N   ALA A  26     -44.874  83.676 307.715  1.00 26.42           N
ATOM     92  CA  ALA A  26     -44.019  83.228 306.623  1.00 24.15           C
ATOM     93  C   ALA A  26     -44.321  84.014 305.347  1.00 28.46           C
ATOM     94  O   ALA A  26     -43.414  84.466 304.642  1.00 27.98           O
ATOM     95  CB  ALA A  26     -44.220  81.742 306.384  1.00 20.53           C
ATOM     96  N   VAL A  27     -45.605  84.185 305.059  1.00 30.51           N
ATOM     97  CA  VAL A  27     -46.015  84.912 303.873  1.00 29.47           C
ATOM     98  C   VAL A  27     -45.597  86.374 303.958  1.00 32.36           C
ATOM     99  O   VAL A  27     -45.146  86.949 302.974  1.00 31.05           O
ATOM    100  CB  VAL A  27     -47.540  84.817 303.667  1.00 27.52           C
ATOM    101  CG1 VAL A  27     -47.994  85.789 302.578  1.00 31.75           C
ATOM    102  CG2 VAL A  27     -47.895  83.414 303.262  1.00 33.91           C
ATOM    103  N   ASN A  28     -45.740  86.979 305.131  1.00 31.61           N
ATOM    104  CA  ASN A  28     -45.350  88.369 305.271  1.00 33.51           C
ATOM    105  C   ASN A  28     -43.834  88.498 305.170  1.00 33.09           C
ATOM    106  O   ASN A  28     -43.315  89.524 304.744  1.00 35.75           O
ATOM    107  CB  ASN A  28     -45.896  88.940 306.579  1.00 35.85           C
ATOM    108  CG  ASN A  28     -47.413  89.120 306.533  1.00 45.06           C
ATOM    109  OD1 ASN A  28     -47.950  89.665 305.566  1.00 43.90           O
ATOM    110  ND2 ASN A  28     -48.106  88.664 307.574  1.00 44.61           N
ATOM    111  N   HIS A  29     -43.119  87.445 305.541  1.00 32.89           N
ATOM    112  CA  HIS A  29     -41.670  87.461 305.424  1.00 32.92           C
ATOM    113  C   HIS A  29     -41.317  87.360 303.930  1.00 33.96           C
ATOM    114  O   HIS A  29     -40.380  87.998 303.469  1.00 31.38           O
ATOM    115  CB  HIS A  29     -41.054  86.298 306.205  1.00 31.97           C
ATOM    116  CG  HIS A  29     -39.576  86.160 306.016  1.00 30.98           C
ATOM    117  ND1 HIS A  29     -39.023  85.422 304.991  1.00 37.65           N
ATOM    118  CD2 HIS A  29     -38.535  86.683 306.705  1.00 33.92           C
ATOM    119  CE1 HIS A  29     -37.705  85.496 305.058  1.00 35.02           C
ATOM    120  NE2 HIS A  29     -37.383  86.255 306.089  1.00 30.44           N
ATOM    121  N   MET A  30     -42.080  86.567 303.181  1.00 33.70           N
ATOM    122  CA  MET A  30     -41.849  86.413 301.749  1.00 34.71           C
ATOM    123  C   MET A  30     -42.107  87.725 301.016  1.00 37.61           C
ATOM    124  O   MET A  30     -41.353  88.099 300.114  1.00 38.26           O
ATOM    125  CB  MET A  30     -42.776  85.352 301.154  1.00 31.15           C
ATOM    126  CG  MET A  30     -42.487  83.937 301.573  1.00 31.20           C
ATOM    127  SD  MET A  30     -43.772  82.863 300.950  1.00 32.85           S
ATOM    128  CE  MET A  30     -43.735  81.524 302.178  1.00 29.67           C
ATOM    129  N   ALA A  31     -43.190  88.404 301.391  1.00 35.99           N
ATOM    130  CA  ALA A  31     -43.559  89.672 300.765  1.00 38.23           C
ATOM    131  C   ALA A  31     -42.532  90.778 301.014  1.00 42.70           C
ATOM    132  O   ALA A  31     -42.487  91.766 300.278  1.00 47.48           O
ATOM    133  CB  ALA A  31     -44.924  90.115 301.260  1.00 32.26           C
ATOM    134  N   LYS A  32     -41.705  90.611 302.042  1.00 43.80           N
ATOM    135  CA  LYS A  32     -40.699  91.612 302.374  1.00 49.71           C
ATOM    136  C   LYS A  32     -39.325  91.283 301.818  1.00 50.81           C
ATOM    137  O   LYS A  32     -38.510  92.177 301.609  1.00 54.95           O
ATOM    138  CB  LYS A  32     -40.589  91.778 303.892  1.00 53.30           C
ATOM    139  CG  LYS A  32     -41.865  92.244 304.565  1.00 57.64           C
ATOM    140  CD  LYS A  32     -41.707  92.261 306.075  1.00 61.75           C
ATOM    141  CE  LYS A  32     -43.009  92.636 306.756  1.00 63.58           C
ATOM    142  NZ  LYS A  32     -42.879  92.625 308.239  1.00 67.85           N
ATOM    143  N   ASN A  33     -39.057  90.006 301.579  1.00 51.31           N
ATOM    144  CA  ASN A  33     -37.756  89.632 301.058  1.00 55.32           C
ATOM    145  C   ASN A  33     -37.692  89.555 299.533  1.00 57.18           C
ATOM    146  O   ASN A  33     -38.152  90.475 298.852  1.00 59.12           O
ATOM    147  CB  ASN A  33     -37.289  88.335 301.716  1.00 54.32           C
ATOM    148  CG  ASN A  33     -36.997  88.522 303.199  1.00 59.54           C
ATOM    149  OD1 ASN A  33     -37.910  88.713 304.005  1.00 56.74           O
ATOM    150  ND2 ASN A  33     -35.718  88.492 303.562  1.00 56.73           N
ATOM    151  N   ASN A  34     -37.134  88.481 298.984  1.00 54.81           N
ATOM    152  CA  ASN A  34     -37.011  88.399 297.528  1.00 56.01           C
ATOM    153  C   ASN A  34     -37.820  87.293 296.867  1.00 52.37           C
ATOM    154  O   ASN A  34     -37.263  86.374 296.271  1.00 51.51           O
ATOM    155  CB  ASN A  34     -35.534  88.259 297.136  1.00 57.73           C
ATOM    156  CG  ASN A  34     -35.325  88.246 295.627  1.00 63.75           C
ATOM    157  OD1 ASN A  34     -35.705  89.188 294.929  1.00 64.71           O
ATOM    158  ND2 ASN A  34     -34.715  87.176 295.119  1.00 61.22           N
ATOM    159  N   VAL A  35     -39.139  87.389 296.980  1.00 51.18           N
ATOM    160  CA  VAL A  35     -40.026  86.411 296.368  1.00 44.49           C
ATOM    161  C   VAL A  35     -40.916  87.181 295.408  1.00 43.57           C
ATOM    162  O   VAL A  35     -42.002  87.628 295.766  1.00 43.37           O
ATOM    163  CB  VAL A  35     -40.883  85.693 297.420  1.00 40.53           C
ATOM    164  CG1 VAL A  35     -41.733  84.633 296.759  1.00 40.60           C
ATOM    165  CG2 VAL A  35     -39.984  85.067 298.467  1.00 40.41           C
ATOM    166  N   GLU A  36     -40.424  87.344 294.187  1.00 39.63           N
ATOM    167  CA  GLU A  36     -41.130  88.077 293.153  1.00 40.04           C
ATOM    168  C   GLU A  36     -41.991  87.196 292.283  1.00 35.89           C
ATOM    169  O   GLU A  36     -41.921  85.969 292.355  1.00 37.20           O
ATOM    170  CB  GLU A  36     -40.134  88.817 292.256  1.00 46.66           C
ATOM    171  CG  GLU A  36     -39.894  90.272 292.629  1.00 58.84           C
ATOM    172  CD  GLU A  36     -39.261  90.429 293.987  1.00 63.43           C
ATOM    173  OE1 GLU A  36     -38.323  89.661 294.284  1.00 70.71           O
ATOM    174  OE2 GLU A  36     -39.687  91.323 294.749  1.00 65.37           O
ATOM    175  N   GLY A  37     -42.803  87.848 291.457  1.00 35.01           N
ATOM    176  CA  GLY A  37     -43.673  87.150 290.532  1.00 33.88           C
ATOM    177  C   GLY A  37     -44.885  86.451 291.111  1.00 34.74           C
ATOM    178  O   GLY A  37     -45.581  85.745 290.380  1.00 38.02           O
ATOM    179  N   VAL A  38     -45.161  86.639 292.401  1.00 35.29           N
ATOM    180  CA  VAL A  38     -46.310  85.974 293.010  1.00 35.57           C
ATOM    181  C   VAL A  38     -47.205  86.919 293.813  1.00 35.29           C
ATOM    182  O   VAL A  38     -46.777  87.992 294.228  1.00 34.36           O
ATOM    183  CB  VAL A  38     -45.853  84.813 293.941  1.00 35.50           C
ATOM    184  CG1 VAL A  38     -44.848  83.929 293.222  1.00 34.55           C
ATOM    185  CG2 VAL A  38     -45.250  85.362 295.213  1.00 37.23           C
ATOM    186  N   GLU A  39     -48.455  86.510 294.018  1.00 36.74           N
ATOM    187  CA  GLU A  39     -49.410  87.298 294.798  1.00 36.67           C
ATOM    188  C   GLU A  39     -49.480  86.677 296.192  1.00 36.55           C
ATOM    189  O   GLU A  39     -49.551  85.449 296.332  1.00 34.22           O
ATOM    190  CB  GLU A  39     -50.798  87.260 294.153  1.00 35.63           C
ATOM    191  CG  GLU A  39     -50.819  87.688 292.702  1.00 48.07           C
ATOM    192  CD  GLU A  39     -52.182  87.509 292.045  1.00 53.61           C
ATOM    193  OE1 GLU A  39     -52.301  87.816 290.839  1.00 58.55           O
ATOM    194  OE2 GLU A  39     -53.133  87.064 292.725  1.00 58.47           O
ATOM    195  N   PHE A  40     -49.457  87.517 297.219  1.00 32.85           N
ATOM    196  CA  PHE A  40     -49.508  87.022 298.590  1.00 36.05           C
ATOM    197  C   PHE A  40     -50.871  87.199 299.253  1.00 36.61           C
ATOM    198  O   PHE A  40     -51.487  88.265 299.176  1.00 34.18           O
ATOM    199  CB  PHE A  40     -48.444  87.711 299.441  1.00 30.92           C
ATOM    200  CG  PHE A  40     -47.041  87.507 298.942  1.00 33.24           C
ATOM    201  CD1 PHE A  40     -46.351  88.546 298.325  1.00 32.57           C
ATOM    202  CD2 PHE A  40     -46.400  86.280 299.105  1.00 35.77           C
ATOM    203  CE1 PHE A  40     -45.033  88.373 297.879  1.00 32.89           C
ATOM    204  CE2 PHE A  40     -45.082  86.094 298.661  1.00 33.18           C
ATOM    205  CZ  PHE A  40     -44.398  87.147 298.048  1.00 31.49           C
ATOM    206  N   ILE A  41     -51.338  86.142 299.908  1.00 30.87           N
ATOM    207  CA  ILE A  41     -52.619  86.189 300.601  1.00 28.32           C
ATOM    208  C   ILE A  41     -52.461  85.614 301.993  1.00 27.87           C
ATOM    209  O   ILE A  41     -51.804  84.588 302.178  1.00 32.00           O
ATOM    210  CB  ILE A  41     -53.690  85.342 299.889  1.00 30.13           C
ATOM    211  CG1 ILE A  41     -53.892  85.830 298.461  1.00 31.17           C
ATOM    212  CG2 ILE A  41     -55.007  85.398 300.668  1.00 29.72           C
ATOM    213  CD1 ILE A  41     -54.703  84.872 297.633  1.00 32.08           C
ATOM    214  N   CYS A  42     -53.048  86.279 302.976  1.00 27.54           N
ATOM    215  CA  CYS A  42     -53.013  85.774 304.334  1.00 31.22           C
ATOM    216  C   CYS A  42     -54.438  85.388 304.732  1.00 31.81           C
ATOM    217  O   CYS A  42     -55.354  86.208 304.661  1.00 33.25           O
ATOM    218  CB  CYS A  42     -52.446  86.829 305.285  1.00 38.70           C
ATOM    219  SG  CYS A  42     -50.637  86.910 305.250  1.00 39.36           S
ATOM    220  N   ALA A  43     -54.629  84.125 305.105  1.00 32.46           N
ATOM    221  CA  ALA A  43     -55.946  83.636 305.515  1.00 34.76           C
ATOM    222  C   ALA A  43     -55.865  83.283 306.995  1.00 35.62           C
ATOM    223  O   ALA A  43     -55.027  82.479 307.397  1.00 35.32           O
ATOM    224  CB  ALA A  43     -56.334  82.418 304.696  1.00 37.73           C
ATOM    225  N   ASN A  44     -56.744  83.869 307.804  1.00 34.00           N
ATOM    226  CA  ASN A  44     -56.689  83.637 309.243  1.00 35.52           C
ATOM    227  C   ASN A  44     -58.045  83.897 309.890  1.00 35.16           C
ATOM    228  O   ASN A  44     -58.822  84.720 309.405  1.00 37.03           O
ATOM    229  CB  ASN A  44     -55.620  84.574 309.834  1.00 30.76           C
ATOM    230  CG  ASN A  44     -55.093  84.119 311.193  1.00 32.54           C
ATOM    231  OD1 ASN A  44     -54.008  84.531 311.605  1.00 33.54           O
ATOM    232  ND2 ASN A  44     -55.855  83.288 311.896  1.00 27.31           N
ATOM    233  N   THR A  45     -58.333  83.181 310.972  1.00 34.23           N
ATOM    234  CA  THR A  45     -59.593  83.357 311.697  1.00 35.86           C
ATOM    235  C   THR A  45     -59.421  84.511 312.682  1.00 37.68           C
ATOM    236  O   THR A  45     -60.392  85.119 313.133  1.00 37.47           O
ATOM    237  CB  THR A  45     -59.961  82.093 312.491  1.00 35.32           C
ATOM    238  OG1 THR A  45     -58.808  81.637 313.219  1.00 34.25           O
ATOM    239  CG2 THR A  45     -60.442  80.999 311.557  1.00 33.35           C
ATOM    240  N   ASP A  46     -58.162  84.787 313.003  1.00 38.83           N
ATOM    241  CA  ASP A  46     -57.755  85.848 313.924  1.00 40.25           C
ATOM    242  C   ASP A  46     -57.779  87.162 313.135  1.00 41.13           C
ATOM    243  O   ASP A  46     -56.895  87.406 312.315  1.00 37.36           O
ATOM    244  CB  ASP A  46     -56.333  85.529 314.424  1.00 38.45           C
ATOM    245  CG  ASP A  46     -55.795  86.554 315.409  1.00 45.27           C
ATOM    246  OD1 ASP A  46     -56.352  87.670 315.507  1.00 46.83           O
ATOM    247  OD2 ASP A  46     -54.785  86.242 316.079  1.00 47.89           O
ATOM    248  N   ALA A  47     -58.785  88.004 313.376  1.00 41.06           N
ATOM    249  CA  ALA A  47     -58.907  89.270 312.645  1.00 43.00           C
ATOM    250  C   ALA A  47     -57.800  90.287 312.936  1.00 44.39           C
ATOM    251  O   ALA A  47     -57.393  91.037 312.049  1.00 45.79           O
ATOM    252  CB  ALA A  47     -60.263  89.902 312.915  1.00 41.56           C
ATOM    253  N   GLN A  48     -57.317  90.317 314.172  1.00 43.32           N
ATOM    254  CA  GLN A  48     -56.266  91.256 314.546  1.00 43.91           C
ATOM    255  C   GLN A  48     -54.947  90.971 313.821  1.00 44.48           C
ATOM    256  O   GLN A  48     -54.200  91.893 313.489  1.00 42.20           O
ATOM    257  CB  GLN A  48     -56.038  91.211 316.060  1.00 47.36           C
ATOM    258  CG  GLN A  48     -54.910  92.112 316.553  1.00 56.29           C
ATOM    259  CD  GLN A  48     -55.221  93.594 316.395  1.00 61.96           C
ATOM    260  OE1 GLN A  48     -54.334  94.440 316.522  1.00 65.45           O
ATOM    261  NE2 GLN A  48     -56.485  93.915 316.127  1.00 61.68           N
ATOM    262  N   ALA A  49     -54.667  89.696 313.573  1.00 41.70           N
ATOM    263  CA  ALA A  49     -53.427  89.311 312.900  1.00 42.97           C
ATOM    264  C   ALA A  49     -53.381  89.760 311.440  1.00 39.87           C
ATOM    265  O   ALA A  49     -52.309  89.860 310.845  1.00 39.74           O
ATOM    266  CB  ALA A  49     -53.236  87.802 312.984  1.00 38.78           C
ATOM    267  N   LEU A  50     -54.546  90.035 310.867  1.00 38.26           N
ATOM    268  CA  LEU A  50     -54.627  90.459 309.477  1.00 41.30           C
ATOM    269  C   LEU A  50     -54.549  91.974 309.302  1.00 44.27           C
ATOM    270  O   LEU A  50     -54.716  92.478 308.193  1.00 46.42           O
ATOM    271  CB  LEU A  50     -55.925  89.940 308.854  1.00 35.72           C
ATOM    272  CG  LEU A  50     -56.093  88.420 308.802  1.00 35.11           C
ATOM    273  CD1 LEU A  50     -57.487  88.088 308.272  1.00 33.87           C
ATOM    274  CD2 LEU A  50     -55.006  87.798 307.914  1.00 27.52           C
ATOM    275  N   LYS A  51     -54.290  92.693 310.390  1.00 47.60           N
ATOM    276  CA  LYS A  51     -54.201  94.152 310.343  1.00 49.48           C
ATOM    277  C   LYS A  51     -52.780  94.668 310.156  1.00 50.32           C
ATOM    278  O   LYS A  51     -51.849  94.214 310.821  1.00 50.17           O
ATOM    279  CB  LYS A  51     -54.773  94.766 311.625  1.00 51.86           C
ATOM    280  CG  LYS A  51     -56.274  94.607 311.802  1.00 57.45           C
ATOM    281  CD  LYS A  51     -56.722  95.210 313.130  1.00 60.72           C
ATOM    282  CE  LYS A  51     -58.214  95.012 313.357  1.00 65.37           C
ATOM    283  NZ  LYS A  51     -58.620  95.411 314.735  1.00 65.61           N
ATOM    284  N   ASN A  52     -52.631  95.634 309.254  1.00 51.09           N
ATOM    285  CA  ASN A  52     -51.342  96.255 308.971  1.00 52.26           C
ATOM    286  C   ASN A  52     -50.248  95.238 308.641  1.00 52.72           C
ATOM    287  O   ASN A  52     -49.207  95.199 309.301  1.00 53.05           O
ATOM    288  CB  ASN A  52     -50.907  97.106 310.169  1.00 55.22           C
ATOM    289  CG  ASN A  52     -52.060  97.893 310.777  1.00 59.29           C
ATOM    290  OD1 ASN A  52     -52.765  98.625 310.082  1.00 61.19           O
ATOM    291  ND2 ASN A  52     -52.252  97.744 312.084  1.00 59.59           N
ATOM    292  N   ILE A  53     -50.481  94.422 307.618  1.00 51.68           N
ATOM    293  CA  ILE A  53     -49.501  93.417 307.217  1.00 49.97           C
ATOM    294  C   ILE A  53     -49.027  93.636 305.785  1.00 49.78           C
ATOM    295  O   ILE A  53     -49.673  94.342 305.011  1.00 50.53           O
ATOM    296  CB  ILE A  53     -50.083  91.991 307.330  1.00 50.51           C
ATOM    297  CG1 ILE A  53     -51.292  91.843 306.404  1.00 46.14           C
ATOM    298  CG2 ILE A  53     -50.457  91.704 308.776  1.00 49.33           C
ATOM    299  CD1 ILE A  53     -51.913  90.471 306.424  1.00 46.77           C
ATOM    300  N   ALA A  54     -47.902  93.015 305.438  1.00 49.16           N
ATOM    301  CA  ALA A  54     -47.319  93.135 304.104  1.00 46.28           C
ATOM    302  C   ALA A  54     -48.215  92.610 302.987  1.00 46.91           C
ATOM    303  O   ALA A  54     -48.361  93.257 301.949  1.00 48.84           O
ATOM    304  CB  ALA A  54     -45.970  92.418 304.064  1.00 46.40           C
ATOM    305  N   ALA A  55     -48.806  91.437 303.192  1.00 46.92           N
ATOM    306  CA  ALA A  55     -49.672  90.830 302.184  1.00 49.55           C
ATOM    307  C   ALA A  55     -50.780  91.786 301.753  1.00 51.14           C
ATOM    308  O   ALA A  55     -51.482  92.358 302.585  1.00 53.20           O
ATOM    309  CB  ALA A  55     -50.273  89.535 302.719  1.00 47.44           C
ATOM    310  N   ARG A  56     -50.932  91.948 300.444  1.00 52.02           N
ATOM    311  CA  ARG A  56     -51.939  92.844 299.892  1.00 53.41           C
ATOM    312  C   ARG A  56     -53.363  92.309 300.007  1.00 50.46           C
ATOM    313  O   ARG A  56     -54.311  93.084 300.082  1.00 54.77           O
ATOM    314  CB  ARG A  56     -51.615  93.146 298.428  1.00 56.15           C
ATOM    315  CG  ARG A  56     -50.296  93.870 298.236  1.00 63.05           C
ATOM    316  CD  ARG A  56     -49.946  94.004 296.762  1.00 70.50           C
ATOM    317  NE  ARG A  56     -48.666  94.682 296.568  1.00 77.11           N
ATOM    318  CZ  ARG A  56     -48.078  94.847 295.387  1.00 80.71           C
ATOM    319  NH1 ARG A  56     -46.914  95.479 295.308  1.00 82.80           N
ATOM    320  NH2 ARG A  56     -48.649  94.377 294.284  1.00 81.31           N
ATOM    321  N   THR A  57     -53.519  90.989 300.012  1.00 47.80           N
ATOM    322  CA  THR A  57     -54.848  90.404 300.124  1.00 43.11           C
ATOM    323  C   THR A  57     -54.985  89.651 301.444  1.00 43.59           C
ATOM    324  O   THR A  57     -54.047  88.996 301.900  1.00 40.48           O
ATOM    325  CB  THR A  57     -55.139  89.418 298.974  1.00 41.87           C
ATOM    326  OG1 THR A  57     -54.851  90.042 297.718  1.00 44.97           O
ATOM    327  CG2 THR A  57     -56.608  89.002 298.989  1.00 39.50           C
ATOM    328  N   VAL A  58     -56.150  89.771 302.069  1.00 40.81           N
ATOM    329  CA  VAL A  58     -56.411  89.074 303.316  1.00 43.05           C
ATOM    330  C   VAL A  58     -57.740  88.354 303.205  1.00 45.45           C
ATOM    331  O   VAL A  58     -58.644  88.796 302.492  1.00 45.73           O
ATOM    332  CB  VAL A  58     -56.485  90.026 304.532  1.00 44.44           C
ATOM    333  CG1 VAL A  58     -55.145  90.724 304.744  1.00 40.57           C
ATOM    334  CG2 VAL A  58     -57.609  91.026 304.337  1.00 43.83           C
ATOM    335  N   LEU A  59     -57.842  87.229 303.898  1.00 42.51           N
ATOM    336  CA  LEU A  59     -59.062  86.449 303.907  1.00 42.43           C
ATOM    337  C   LEU A  59     -59.353  86.043 305.344  1.00 42.80           C
ATOM    338  O   LEU A  59     -58.721  85.128 305.878  1.00 40.67           O
ATOM    339  CB  LEU A  59     -58.917  85.207 303.027  1.00 43.45           C
ATOM    340  CG  LEU A  59     -60.135  84.279 303.013  1.00 45.27           C
ATOM    341  CD1 LEU A  59     -61.414  85.098 302.890  1.00 50.67           C
ATOM    342  CD2 LEU A  59     -60.012  83.288 301.868  1.00 43.15           C
ATOM    343  N   GLN A  60     -60.291  86.748 305.970  1.00 42.12           N
ATOM    344  CA  GLN A  60     -60.679  86.462 307.344  1.00 42.51           C
ATOM    345  C   GLN A  60     -61.645  85.287 307.323  1.00 42.33           C
ATOM    346  O   GLN A  60     -62.817  85.439 306.978  1.00 45.66           O
ATOM    347  CB  GLN A  60     -61.348  87.684 307.969  1.00 45.08           C
ATOM    348  CG  GLN A  60     -61.859  87.456 309.382  1.00 53.48           C
ATOM    349  CD  GLN A  60     -62.420  88.720 309.997  1.00 58.27           C
ATOM    350  OE1 GLN A  60     -63.020  89.548 309.310  1.00 63.52           O
ATOM    351  NE2 GLN A  60     -62.242  88.871 311.299  1.00 64.87           N
ATOM    352  N   LEU A  61     -61.138  84.117 307.694  1.00 39.01           N
ATOM    353  CA  LEU A  61     -61.920  82.893 307.697  1.00 38.48           C
ATOM    354  C   LEU A  61     -62.983  82.807 308.798  1.00 39.17           C
ATOM    355  O   LEU A  61     -62.752  83.208 309.944  1.00 39.47           O
ATOM    356  CB  LEU A  61     -60.970  81.689 307.797  1.00 38.80           C
ATOM    357  CG  LEU A  61     -59.985  81.487 306.636  1.00 36.03           C
ATOM    358  CD1 LEU A  61     -58.937  80.442 307.016  1.00 36.56           C
ATOM    359  CD2 LEU A  61     -60.750  81.053 305.389  1.00 32.71           C
ATOM    360  N   GLY A  62     -64.148  82.284 308.419  1.00 38.91           N
ATOM    361  CA  GLY A  62     -65.261  82.089 309.337  1.00 38.35           C
ATOM    362  C   GLY A  62     -65.585  83.190 310.327  1.00 35.89           C
ATOM    363  O   GLY A  62     -65.469  82.985 311.537  1.00 34.44           O
ATOM    364  N   PRO A  63     -65.999  84.370 309.853  1.00 38.55           N
ATOM    365  CA  PRO A  63     -66.328  85.464 310.775  1.00 42.99           C
ATOM    366  C   PRO A  63     -67.532  85.083 311.642  1.00 42.96           C
ATOM    367  O   PRO A  63     -67.724  85.625 312.727  1.00 45.54           O
ATOM    368  CB  PRO A  63     -66.657  86.627 309.838  1.00 42.56           C
ATOM    369  CG  PRO A  63     -65.937  86.279 308.564  1.00 42.92           C
ATOM    370  CD  PRO A  63     -66.158  84.796 308.455  1.00 40.10           C
ATOM    371  N   GLY A  64     -68.335  84.143 311.151  1.00 42.54           N
ATOM    372  CA  GLY A  64     -69.515  83.714 311.883  1.00 45.29           C
ATOM    373  C   GLY A  64     -69.243  82.637 312.914  1.00 45.98           C
ATOM    374  O   GLY A  64     -69.879  82.599 313.964  1.00 45.98           O
ATOM    375  N   VAL A  65     -68.296  81.756 312.619  1.00 44.51           N
ATOM    376  CA  VAL A  65     -67.949  80.683 313.538  1.00 42.45           C
ATOM    377  C   VAL A  65     -67.011  81.167 314.644  1.00 41.77           C
ATOM    378  O   VAL A  65     -67.136  80.775 315.804  1.00 40.81           O
ATOM    379  CB  VAL A  65     -67.230  79.526 312.801  1.00 46.32           C
ATOM    380  CG1 VAL A  65     -66.838  78.445 313.786  1.00 46.55           C
ATOM    381  CG2 VAL A  65     -68.124  78.948 311.728  1.00 48.65           C
ATOM    382  N   THR A  66     -66.086  82.045 314.282  1.00 37.54           N
ATOM    383  CA  THR A  66     -65.081  82.515 315.220  1.00 37.85           C
ATOM    384  C   THR A  66     -65.238  83.949 315.691  1.00 37.47           C
ATOM    385  O   THR A  66     -64.610  84.357 316.670  1.00 35.72           O
ATOM    386  CB  THR A  66     -63.692  82.391 314.581  1.00 38.46           C
ATOM    387  OG1 THR A  66     -63.592  83.332 313.506  1.00 39.74           O
ATOM    388  CG2 THR A  66     -63.485  80.990 314.017  1.00 31.77           C
ATOM    389  N   LYS A  67     -66.047  84.717 314.974  1.00 39.79           N
ATOM    390  CA  LYS A  67     -66.263  86.121 315.300  1.00 41.09           C
ATOM    391  C   LYS A  67     -64.954  86.908 315.310  1.00 39.35           C
ATOM    392  O   LYS A  67     -64.764  87.814 316.121  1.00 41.89           O
ATOM    393  CB  LYS A  67     -66.990  86.237 316.643  1.00 44.28           C
ATOM    394  CG  LYS A  67     -68.224  85.346 316.688  1.00 50.51           C
ATOM    395  CD  LYS A  67     -69.257  85.795 317.700  1.00 58.13           C
ATOM    396  CE  LYS A  67     -70.476  84.881 317.629  1.00 61.23           C
ATOM    397  NZ  LYS A  67     -70.920  84.665 316.215  1.00 60.09           N
ATOM    398  N   GLY A  68     -64.053  86.553 314.395  1.00 41.21           N
ATOM    399  CA  GLY A  68     -62.775  87.239 314.281  1.00 34.66           C
ATOM    400  C   GLY A  68     -61.818  87.068 315.446  1.00 36.24           C
ATOM    401  O   GLY A  68     -60.768  87.711 315.482  1.00 38.12           O
ATOM    402  N   LEU A  69     -62.162  86.199 316.391  1.00 36.90           N
ATOM    403  CA  LEU A  69     -61.323  85.980 317.572  1.00 40.38           C
ATOM    404  C   LEU A  69     -60.252  84.916 317.371  1.00 42.81           C
ATOM    405  O   LEU A  69     -59.473  84.633 318.283  1.00 44.09           O
ATOM    406  CB  LEU A  69     -62.186  85.566 318.767  1.00 43.10           C
ATOM    407  CG  LEU A  69     -63.272  86.527 319.235  1.00 43.39           C
ATOM    408  CD1 LEU A  69     -63.989  85.916 320.429  1.00 46.68           C
ATOM    409  CD2 LEU A  69     -62.651  87.864 319.605  1.00 45.14           C
ATOM    410  N   GLY A  70     -60.229  84.321 316.186  1.00 41.47           N
ATOM    411  CA  GLY A  70     -59.252  83.295 315.902  1.00 41.62           C
ATOM    412  C   GLY A  70     -59.756  81.957 316.391  1.00 43.89           C
ATOM    413  O   GLY A  70     -60.899  81.832 316.817  1.00 42.88           O
ATOM    414  N   ALA A  71     -58.909  80.943 316.298  1.00 40.99           N
ATOM    415  CA  ALA A  71     -59.272  79.624 316.763  1.00 41.52           C
ATOM    416  C   ALA A  71     -58.502  79.518 318.068  1.00 43.97           C
ATOM    417  O   ALA A  71     -57.736  80.414 318.412  1.00 49.97           O
ATOM    418  CB  ALA A  71     -58.819  78.567 315.758  1.00 37.30           C
ATOM    419  N   GLY A  72     -58.703  78.455 318.820  1.00 42.12           N
ATOM    420  CA  GLY A  72     -57.963  78.359 320.064  1.00 36.67           C
ATOM    421  C   GLY A  72     -57.041  77.177 319.954  1.00 38.08           C
ATOM    422  O   GLY A  72     -57.062  76.294 320.807  1.00 37.04           O
ATOM    423  N   ALA A  73     -56.239  77.156 318.892  1.00 32.90           N
ATOM    424  CA  ALA A  73     -55.324  76.048 318.654  1.00 35.17           C
ATOM    425  C   ALA A  73     -56.171  74.807 318.356  1.00 33.82           C
ATOM    426  O   ALA A  73     -55.656  73.702 318.226  1.00 40.32           O
ATOM    427  CB  ALA A  73     -54.427  75.818 319.890  1.00 28.86           C
ATOM    428  N   ASN A  74     -57.479  75.012 318.236  1.00 34.28           N
ATOM    429  CA  ASN A  74     -58.427  73.938 317.949  1.00 31.56           C
ATOM    430  C   ASN A  74     -58.619  73.784 316.436  1.00 33.90           C
ATOM    431  O   ASN A  74     -59.262  74.617 315.795  1.00 33.52           O
ATOM    432  CB  ASN A  74     -59.777  74.259 318.600  1.00 35.34           C
ATOM    433  CG  ASN A  74     -60.759  73.103 318.517  1.00 39.66           C
ATOM    434  OD1 ASN A  74     -60.708  72.293 317.589  1.00 39.37           O
ATOM    435  ND2 ASN A  74     -61.673  73.028 319.488  1.00 40.62           N
ATOM    436  N   PRO A  75     -58.073  72.708 315.849  1.00 33.04           N
ATOM    437  CA  PRO A  75     -58.182  72.446 314.410  1.00 33.53           C
ATOM    438  C   PRO A  75     -59.602  72.282 313.875  1.00 37.48           C
ATOM    439  O   PRO A  75     -59.839  72.474 312.680  1.00 36.08           O
ATOM    440  CB  PRO A  75     -57.331  71.192 314.215  1.00 30.46           C
ATOM    441  CG  PRO A  75     -57.403  70.512 315.541  1.00 33.08           C
ATOM    442  CD  PRO A  75     -57.291  71.653 316.519  1.00 36.67           C
ATOM    443  N   GLU A  76     -60.550  71.935 314.747  1.00 39.89           N
ATOM    444  CA  GLU A  76     -61.932  71.778 314.302  1.00 38.98           C
ATOM    445  C   GLU A  76     -62.512  73.149 314.001  1.00 36.03           C
ATOM    446  O   GLU A  76     -63.260  73.321 313.039  1.00 35.62           O
ATOM    447  CB  GLU A  76     -62.786  71.082 315.366  1.00 45.13           C
ATOM    448  CG  GLU A  76     -64.251  70.945 314.955  1.00 48.70           C
ATOM    449  CD  GLU A  76     -64.439  70.153 313.665  1.00 56.29           C
ATOM    450  OE1 GLU A  76     -65.558  70.179 313.111  1.00 57.58           O
ATOM    451  OE2 GLU A  76     -63.475  69.499 313.207  1.00 59.27           O
ATOM    452  N   VAL A  77     -62.173  74.127 314.836  1.00 36.22           N
ATOM    453  CA  VAL A  77     -62.643  75.492 314.622  1.00 36.00           C
ATOM    454  C   VAL A  77     -62.102  75.978 313.269  1.00 36.22           C
ATOM    455  O   VAL A  77     -62.828  76.569 312.472  1.00 38.04           O
ATOM    456  CB  VAL A  77     -62.151  76.435 315.749  1.00 37.38           C
ATOM    457  CG1 VAL A  77     -62.543  77.871 315.439  1.00 38.71           C
ATOM    458  CG2 VAL A  77     -62.755  76.006 317.091  1.00 37.94           C
ATOM    459  N   GLY A  78     -60.824  75.711 313.016  1.00 37.76           N
ATOM    460  CA  GLY A  78     -60.214  76.120 311.765  1.00 37.35           C
ATOM    461  C   GLY A  78     -60.922  75.481 310.588  1.00 32.48           C
ATOM    462  O   GLY A  78     -61.193  76.132 309.585  1.00 32.43           O
ATOM    463  N   ARG A  79     -61.234  74.198 310.713  1.00 35.88           N
ATOM    464  CA  ARG A  79     -61.927  73.498 309.642  1.00 34.08           C
ATOM    465  C   ARG A  79     -63.331  74.062 309.411  1.00 32.35           C
ATOM    466  O   ARG A  79     -63.734  74.267 308.274  1.00 28.45           O
ATOM    467  CB  ARG A  79     -62.022  72.000 309.952  1.00 39.55           C
ATOM    468  CG  ARG A  79     -62.489  71.158 308.766  1.00 39.56           C
ATOM    469  CD  ARG A  79     -62.493  69.679 309.105  1.00 43.73           C
ATOM    470  NE  ARG A  79     -63.625  69.320 309.955  1.00 53.70           N
ATOM    471  CZ  ARG A  79     -64.876  69.196 309.522  1.00 55.39           C
ATOM    472  NH1 ARG A  79     -65.161  69.400 308.243  1.00 59.23           N
ATOM    473  NH2 ARG A  79     -65.842  68.865 310.365  1.00 56.70           N
ATOM    474  N   GLN A  80     -64.073  74.317 310.484  1.00 34.39           N
ATOM    475  CA  GLN A  80     -65.430  74.847 310.345  1.00 35.33           C
ATOM    476  C   GLN A  80     -65.436  76.256 309.760  1.00 35.44           C
ATOM    477  O   GLN A  80     -66.323  76.609 308.981  1.00 34.21           O
ATOM    478  CB  GLN A  80     -66.147  74.848 311.699  1.00 37.59           C
ATOM    479  CG  GLN A  80     -66.483  73.454 312.204  1.00 45.00           C
ATOM    480  CD  GLN A  80     -67.366  72.680 311.235  1.00 51.70           C
ATOM    481  OE1 GLN A  80     -67.156  71.487 311.001  1.00 54.44           O
ATOM    482  NE2 GLN A  80     -68.367  73.355 310.672  1.00 51.61           N
ATOM    483  N   ALA A  81     -64.454  77.067 310.139  1.00 34.80           N
ATOM    484  CA  ALA A  81     -64.374  78.427 309.616  1.00 33.49           C
ATOM    485  C   ALA A  81     -64.099  78.358 308.113  1.00 35.12           C
ATOM    486  O   ALA A  81     -64.642  79.140 307.339  1.00 37.75           O
ATOM    487  CB  ALA A  81     -63.263  79.204 310.322  1.00 34.13           C
ATOM    488  N   ALA A  82     -63.262  77.413 307.698  1.00 37.34           N
ATOM    489  CA  ALA A  82     -62.949  77.276 306.280  1.00 39.66           C
ATOM    490  C   ALA A  82     -64.175  76.773 305.510  1.00 41.14           C
ATOM    491  O   ALA A  82     -64.453  77.237 304.404  1.00 39.23           O
ATOM    492  CB  ALA A  82     -61.776  76.333 306.088  1.00 34.42           C
ATOM    493  N   LEU A  83     -64.908  75.827 306.088  1.00 42.22           N
ATOM    494  CA  LEU A  83     -66.100  75.310 305.420  1.00 46.54           C
ATOM    495  C   LEU A  83     -67.105  76.436 305.189  1.00 44.83           C
ATOM    496  O   LEU A  83     -67.816  76.446 304.190  1.00 49.23           O
ATOM    497  CB  LEU A  83     -66.742  74.199 306.253  1.00 42.64           C
ATOM    498  CG  LEU A  83     -65.946  72.894 306.323  1.00 45.06           C
ATOM    499  CD1 LEU A  83     -66.637  71.927 307.259  1.00 43.65           C
ATOM    500  CD2 LEU A  83     -65.813  72.291 304.930  1.00 44.94           C
ATOM    501  N   GLU A  84     -67.139  77.391 306.114  1.00 44.12           N
ATOM    502  CA  GLU A  84     -68.040  78.536 306.033  1.00 43.08           C
ATOM    503  C   GLU A  84     -67.680  79.467 304.877  1.00 46.24           C
ATOM    504  O   GLU A  84     -68.561  80.088 304.275  1.00 41.21           O
ATOM    505  CB  GLU A  84     -67.996  79.327 307.347  1.00 41.57           C
ATOM    506  CG  GLU A  84     -68.872  80.582 307.374  1.00 44.09           C
ATOM    507  CD  GLU A  84     -68.615  81.470 308.594  1.00 48.90           C
ATOM    508  OE1 GLU A  84     -68.474  80.929 309.711  1.00 49.47           O
ATOM    509  OE2 GLU A  84     -68.566  82.713 308.440  1.00 47.11           O
ATOM    510  N   ASP A  85     -66.388  79.560 304.564  1.00 46.44           N
ATOM    511  CA  ASP A  85     -65.926  80.442 303.496  1.00 49.06           C
ATOM    512  C   ASP A  85     -65.422  79.773 302.218  1.00 46.60           C
ATOM    513  O   ASP A  85     -64.563  80.329 301.536  1.00 46.10           O
ATOM    514  CB  ASP A  85     -64.828  81.375 304.023  1.00 54.95           C
ATOM    515  CG  ASP A  85     -65.381  82.570 304.784  1.00 55.47           C
ATOM    516  OD1 ASP A  85     -66.219  83.299 304.219  1.00 57.16           O
ATOM    517  OD2 ASP A  85     -64.968  82.790 305.941  1.00 57.58           O
ATOM    518  N   ARG A  86     -65.942  78.596 301.883  1.00 44.16           N
ATOM    519  CA  ARG A  86     -65.501  77.921 300.667  1.00 44.21           C
ATOM    520  C   ARG A  86     -65.669  78.829 299.448  1.00 43.31           C
ATOM    521  O   ARG A  86     -64.844  78.822 298.532  1.00 40.47           O
ATOM    522  CB  ARG A  86     -66.277  76.617 300.462  1.00 46.03           C
ATOM    523  CG  ARG A  86     -65.669  75.427 301.177  1.00 48.69           C
ATOM    524  CD  ARG A  86     -66.536  74.190 301.050  1.00 55.88           C
ATOM    525  NE  ARG A  86     -65.769  73.025 300.611  1.00 61.30           N
ATOM    526  CZ  ARG A  86     -65.352  72.830 299.362  1.00 62.99           C
ATOM    527  NH1 ARG A  86     -65.631  73.721 298.419  1.00 64.78           N
ATOM    528  NH2 ARG A  86     -64.654  71.743 299.056  1.00 60.68           N
ATOM    529  N   GLU A  87     -66.736  79.621 299.447  1.00 41.26           N
ATOM    530  CA  GLU A  87     -66.992  80.526 298.340  1.00 41.39           C
ATOM    531  C   GLU A  87     -65.929  81.611 298.274  1.00 38.63           C
ATOM    532  O   GLU A  87     -65.365  81.870 297.214  1.00 34.59           O
ATOM    533  CB  GLU A  87     -68.369  81.174 298.483  1.00 44.49           C
ATOM    534  CG  GLU A  87     -68.869  81.847 297.210  1.00 52.71           C
ATOM    535  CD  GLU A  87     -70.275  82.413 297.361  1.00 54.39           C
ATOM    536  OE1 GLU A  87     -71.083  81.801 298.092  1.00 55.17           O
ATOM    537  OE2 GLU A  87     -70.576  83.457 296.740  1.00 56.74           O
ATOM    538  N   ARG A  88     -65.656  82.251 299.407  1.00 36.87           N
ATOM    539  CA  ARG A  88     -64.659  83.311 299.424  1.00 41.45           C
ATOM    540  C   ARG A  88     -63.260  82.759 299.175  1.00 37.58           C
ATOM    541  O   ARG A  88     -62.385  83.474 298.703  1.00 40.38           O
ATOM    542  CB  ARG A  88     -64.720  84.081 300.746  1.00 43.67           C
ATOM    543  CG  ARG A  88     -65.995  84.916 300.895  1.00 50.88           C
ATOM    544  CD  ARG A  88     -66.198  85.394 302.326  1.00 55.93           C
ATOM    545  NE  ARG A  88     -65.199  86.373 302.746  1.00 61.88           N
ATOM    546  CZ  ARG A  88     -64.773  86.514 303.997  1.00 62.43           C
ATOM    547  NH1 ARG A  88     -63.866  87.434 304.289  1.00 68.85           N
ATOM    548  NH2 ARG A  88     -65.236  85.723 304.956  1.00 63.16           N
ATOM    549  N   ILE A  89     -63.046  81.485 299.483  1.00 35.81           N
ATOM    550  CA  ILE A  89     -61.746  80.894 299.233  1.00 37.36           C
ATOM    551  C   ILE A  89     -61.632  80.728 297.719  1.00 40.40           C
ATOM    552  O   ILE A  89     -60.560  80.913 297.141  1.00 37.01           O
ATOM    553  CB  ILE A  89     -61.599  79.525 299.932  1.00 36.12           C
ATOM    554  CG1 ILE A  89     -61.507  79.721 301.453  1.00 34.97           C
ATOM    555  CG2 ILE A  89     -60.367  78.810 299.408  1.00 33.47           C
ATOM    556  CD1 ILE A  89     -61.625  78.426 302.260  1.00 30.93           C
ATOM    557  N   SER A  90     -62.752  80.391 297.079  1.00 41.21           N
ATOM    558  CA  SER A  90     -62.784  80.222 295.624  1.00 45.21           C
ATOM    559  C   SER A  90     -62.411  81.535 294.952  1.00 44.44           C
ATOM    560  O   SER A  90     -61.567  81.581 294.053  1.00 42.91           O
ATOM    561  CB  SER A  90     -64.188  79.830 295.140  1.00 45.80           C
ATOM    562  OG  SER A  90     -64.566  78.541 295.579  1.00 55.57           O
ATOM    563  N   GLU A  91     -63.061  82.602 295.397  1.00 42.44           N
ATOM    564  CA  GLU A  91     -62.838  83.916 294.828  1.00 45.50           C
ATOM    565  C   GLU A  91     -61.380  84.336 294.885  1.00 40.80           C
ATOM    566  O   GLU A  91     -60.803  84.695 293.872  1.00 41.99           O
ATOM    567  CB  GLU A  91     -63.718  84.948 295.540  1.00 48.87           C
ATOM    568  CG  GLU A  91     -65.187  84.540 295.608  1.00 60.66           C
ATOM    569  CD  GLU A  91     -66.081  85.624 296.191  1.00 67.14           C
ATOM    570  OE1 GLU A  91     -65.719  86.199 297.240  1.00 68.09           O
ATOM    571  OE2 GLU A  91     -67.152  85.894 295.601  1.00 68.04           O
ATOM    572  N   VAL A  92     -60.785  84.275 296.070  1.00 42.75           N
ATOM    573  CA  VAL A  92     -59.395  84.675 296.250  1.00 40.69           C
ATOM    574  C   VAL A  92     -58.428  83.848 295.385  1.00 40.25           C
ATOM    575  O   VAL A  92     -57.357  84.327 295.009  1.00 41.79           O
ATOM    576  CB  VAL A  92     -59.004  84.586 297.757  1.00 45.22           C
ATOM    577  CG1 VAL A  92     -58.465  83.199 298.094  1.00 44.48           C
ATOM    578  CG2 VAL A  92     -58.011  85.671 298.101  1.00 49.44           C
ATOM    579  N   LEU A  93     -58.810  82.616 295.061  1.00 39.19           N
ATOM    580  CA  LEU A  93     -57.980  81.738 294.232  1.00 41.33           C
ATOM    581  C   LEU A  93     -58.270  81.831 292.722  1.00 44.54           C
ATOM    582  O   LEU A  93     -57.452  81.396 291.899  1.00 39.83           O
ATOM    583  CB  LEU A  93     -58.155  80.282 294.666  1.00 42.85           C
ATOM    584  CG  LEU A  93     -57.705  79.880 296.073  1.00 47.96           C
ATOM    585  CD1 LEU A  93     -57.994  78.395 296.283  1.00 44.37           C
ATOM    586  CD2 LEU A  93     -56.220  80.177 296.250  1.00 43.15           C
ATOM    587  N   GLU A  94     -59.429  82.383 292.362  1.00 43.13           N
ATOM    588  CA  GLU A  94     -59.819  82.500 290.956  1.00 44.19           C
ATOM    589  C   GLU A  94     -58.706  83.064 290.071  1.00 41.34           C
ATOM    590  O   GLU A  94     -58.124  84.106 290.373  1.00 39.64           O
ATOM    591  CB  GLU A  94     -61.054  83.400 290.811  1.00 50.82           C
ATOM    592  CG  GLU A  94     -60.739  84.887 290.994  1.00 62.94           C
ATOM    593  CD  GLU A  94     -61.905  85.807 290.671  1.00 71.82           C
ATOM    594  OE1 GLU A  94     -62.955  85.706 291.349  1.00 74.53           O
ATOM    595  OE2 GLU A  94     -61.763  86.636 289.741  1.00 71.69           O
ATOM    596  N   GLY A  95     -58.411  82.370 288.978  1.00 44.36           N
ATOM    597  CA  GLY A  95     -57.395  82.855 288.061  1.00 44.08           C
ATOM    598  C   GLY A  95     -55.976  82.348 288.241  1.00 47.02           C
ATOM    599  O   GLY A  95     -55.126  82.577 287.372  1.00 46.60           O
ATOM    600  N   ALA A  96     -55.701  81.663 289.347  1.00 41.57           N
ATOM    601  CA  ALA A  96     -54.354  81.155 289.576  1.00 39.51           C
ATOM    602  C   ALA A  96     -54.052  79.942 288.708  1.00 39.11           C
ATOM    603  O   ALA A  96     -54.929  79.123 288.443  1.00 38.59           O
ATOM    604  CB  ALA A  96     -54.169  80.784 291.041  1.00 35.64           C
ATOM    605  N   ASP A  97     -52.805  79.848 288.258  1.00 36.84           N
ATOM    606  CA  ASP A  97     -52.348  78.711 287.470  1.00 36.11           C
ATOM    607  C   ASP A  97     -51.667  77.812 288.479  1.00 36.46           C
ATOM    608  O   ASP A  97     -51.484  76.613 288.267  1.00 36.34           O
ATOM    609  CB  ASP A  97     -51.331  79.155 286.422  1.00 40.32           C
ATOM    610  CG  ASP A  97     -51.959  79.984 285.329  1.00 41.37           C
ATOM    611  OD1 ASP A  97     -52.767  79.414 284.564  1.00 40.87           O
ATOM    612  OD2 ASP A  97     -51.657  81.198 285.244  1.00 43.64           O
ATOM    613  N   MET A  98     -51.300  78.417 289.600  1.00 33.17           N
ATOM    614  CA  MET A  98     -50.630  77.691 290.652  1.00 33.07           C
ATOM    615  C   MET A  98     -50.834  78.369 291.993  1.00 33.18           C
ATOM    616  O   MET A  98     -50.857  79.610 292.098  1.00 29.60           O
ATOM    617  CB  MET A  98     -49.133  77.596 290.341  1.00 26.92           C
ATOM    618  CG  MET A  98     -48.336  76.840 291.370  1.00 30.34           C
ATOM    619  SD  MET A  98     -46.597  76.699 290.879  1.00 36.63           S
ATOM    620  CE  MET A  98     -46.175  75.118 291.607  1.00 27.63           C
ATOM    621  N   VAL A  99     -50.997  77.550 293.022  1.00 29.88           N
ATOM    622  CA  VAL A  99     -51.159  78.080 294.360  1.00 30.49           C
ATOM    623  C   VAL A  99     -50.261  77.349 295.353  1.00 32.76           C
ATOM    624  O   VAL A  99     -50.149  76.111 295.334  1.00 32.18           O
ATOM    625  CB  VAL A  99     -52.633  77.984 294.831  1.00 33.44           C
ATOM    626  CG1 VAL A  99     -53.125  76.559 294.721  1.00 39.79           C
ATOM    627  CG2 VAL A  99     -52.753  78.460 296.273  1.00 34.05           C
ATOM    628  N   PHE A 100     -49.581  78.128 296.186  1.00 29.10           N
ATOM    629  CA  PHE A 100     -48.746  77.573 297.237  1.00 28.10           C
ATOM    630  C   PHE A 100     -49.551  77.810 298.501  1.00 28.87           C
ATOM    631  O   PHE A 100     -50.021  78.928 298.749  1.00 29.52           O
ATOM    632  CB  PHE A 100     -47.411  78.310 297.378  1.00 25.55           C
ATOM    633  CG  PHE A 100     -46.436  78.042 296.268  1.00 29.77           C
ATOM    634  CD1 PHE A 100     -46.465  78.796 295.100  1.00 30.59           C
ATOM    635  CD2 PHE A 100     -45.458  77.058 296.408  1.00 28.94           C
ATOM    636  CE1 PHE A 100     -45.531  78.580 294.084  1.00 33.17           C
ATOM    637  CE2 PHE A 100     -44.520  76.834 295.396  1.00 26.79           C
ATOM    638  CZ  PHE A 100     -44.556  77.595 294.235  1.00 28.61           C
ATOM    639  N   ILE A 101     -49.728  76.758 299.286  1.00 23.85           N
ATOM    640  CA  ILE A 101     -50.455  76.855 300.535  1.00 26.24           C
ATOM    641  C   ILE A 101     -49.420  76.656 301.618  1.00 30.60           C
ATOM    642  O   ILE A 101     -48.816  75.585 301.707  1.00 29.11           O
ATOM    643  CB  ILE A 101     -51.513  75.754 300.657  1.00 26.71           C
ATOM    644  CG1 ILE A 101     -52.651  76.019 299.673  1.00 29.19           C
ATOM    645  CG2 ILE A 101     -52.048  75.698 302.085  1.00 33.24           C
ATOM    646  CD1 ILE A 101     -53.660  74.888 299.599  1.00 31.06           C
ATOM    647  N   THR A 102     -49.189  77.678 302.435  1.00 27.06           N
ATOM    648  CA  THR A 102     -48.202  77.515 303.478  1.00 29.70           C
ATOM    649  C   THR A 102     -48.785  77.734 304.857  1.00 29.87           C
ATOM    650  O   THR A 102     -49.560  78.668 305.096  1.00 29.88           O
ATOM    651  CB  THR A 102     -46.979  78.434 303.266  1.00 32.30           C
ATOM    652  OG1 THR A 102     -45.969  78.080 304.218  1.00 35.78           O
ATOM    653  CG2 THR A 102     -47.348  79.904 303.461  1.00 28.97           C
ATOM    654  N   THR A 103     -48.405  76.859 305.776  1.00 29.81           N
ATOM    655  CA  THR A 103     -48.924  76.958 307.120  1.00 31.50           C
ATOM    656  C   THR A 103     -48.075  76.196 308.122  1.00 30.20           C
ATOM    657  O   THR A 103     -47.248  75.358 307.762  1.00 30.43           O
ATOM    658  CB  THR A 103     -50.379  76.402 307.171  1.00 30.41           C
ATOM    659  OG1 THR A 103     -51.051  76.935 308.310  1.00 41.57           O
ATOM    660  CG2 THR A 103     -50.372  74.877 307.277  1.00 32.25           C
ATOM    661  N   GLY A 104     -48.271  76.527 309.390  1.00 29.90           N
ATOM    662  CA  GLY A 104     -47.577  75.835 310.442  1.00 28.00           C
ATOM    663  C   GLY A 104     -48.602  74.830 310.940  1.00 32.30           C
ATOM    664  O   GLY A 104     -49.615  75.210 311.535  1.00 33.04           O
ATOM    665  N   MET A 105     -48.370  73.553 310.670  1.00 26.93           N
ATOM    666  CA  MET A 105     -49.291  72.522 311.120  1.00 32.00           C
ATOM    667  C   MET A 105     -49.111  72.321 312.617  1.00 29.64           C
ATOM    668  O   MET A 105     -47.993  72.338 313.127  1.00 33.59           O
ATOM    669  CB  MET A 105     -49.032  71.214 310.367  1.00 33.89           C
ATOM    670  CG  MET A 105     -49.345  71.287 308.879  1.00 35.80           C
ATOM    671  SD  MET A 105     -51.095  71.586 308.529  1.00 46.64           S
ATOM    672  CE  MET A 105     -51.738  70.070 308.964  1.00 40.36           C
ATOM    673  N   GLY A 106     -50.217  72.148 313.328  1.00 29.59           N
ATOM    674  CA  GLY A 106     -50.136  71.955 314.762  1.00 30.73           C
ATOM    675  C   GLY A 106     -51.070  72.872 315.525  1.00 31.57           C
ATOM    676  O   GLY A 106     -51.359  72.626 316.691  1.00 30.54           O
ATOM    677  N   GLY A 107     -51.535  73.932 314.871  1.00 30.51           N
ATOM    678  CA  GLY A 107     -52.437  74.866 315.519  1.00 29.86           C
ATOM    679  C   GLY A 107     -53.866  74.550 315.132  1.00 31.55           C
ATOM    680  O   GLY A 107     -54.170  73.413 314.788  1.00 30.30           O
ATOM    681  N   GLY A 108     -54.743  75.550 315.165  1.00 32.96           N
ATOM    682  CA  GLY A 108     -56.134  75.312 314.822  1.00 28.72           C
ATOM    683  C   GLY A 108     -56.506  75.766 313.424  1.00 34.18           C
ATOM    684  O   GLY A 108     -57.042  74.996 312.628  1.00 33.83           O
ATOM    685  N   THR A 109     -56.219  77.028 313.127  1.00 31.18           N
ATOM    686  CA  THR A 109     -56.532  77.616 311.832  1.00 33.12           C
ATOM    687  C   THR A 109     -55.781  76.922 310.703  1.00 29.59           C
ATOM    688  O   THR A 109     -56.385  76.409 309.763  1.00 31.51           O
ATOM    689  CB  THR A 109     -56.177  79.119 311.827  1.00 29.97           C
ATOM    690  OG1 THR A 109     -56.887  79.773 312.892  1.00 29.77           O
ATOM    691  CG2 THR A 109     -56.545  79.752 310.496  1.00 29.36           C
ATOM    692  N   GLY A 110     -54.459  76.907 310.803  1.00 26.26           N
ATOM    693  CA  GLY A 110     -53.660  76.273 309.775  1.00 26.37           C
ATOM    694  C   GLY A 110     -53.971  74.804 309.556  1.00 29.33           C
ATOM    695  O   GLY A 110     -54.298  74.403 308.444  1.00 32.61           O
ATOM    696  N   THR A 111     -53.891  73.986 310.602  1.00 29.82           N
ATOM    697  CA  THR A 111     -54.146  72.562 310.407  1.00 35.99           C
ATOM    698  C   THR A 111     -55.564  72.295 309.931  1.00 34.04           C
ATOM    699  O   THR A 111     -55.793  71.410 309.108  1.00 38.21           O
ATOM    700  CB  THR A 111     -53.900  71.743 311.688  1.00 33.61           C
ATOM    701  OG1 THR A 111     -55.106  71.672 312.448  1.00 48.08           O
ATOM    702  CG2 THR A 111     -52.840  72.394 312.533  1.00 27.86           C
ATOM    703  N   GLY A 112     -56.514  73.072 310.434  1.00 35.96           N
ATOM    704  CA  GLY A 112     -57.901  72.874 310.051  1.00 33.86           C
ATOM    705  C   GLY A 112     -58.335  73.408 308.696  1.00 35.26           C
ATOM    706  O   GLY A 112     -58.974  72.693 307.917  1.00 35.55           O
ATOM    707  N   ALA A 113     -57.994  74.659 308.407  1.00 31.89           N
ATOM    708  CA  ALA A 113     -58.394  75.294 307.151  1.00 30.89           C
ATOM    709  C   ALA A 113     -57.588  74.968 305.897  1.00 30.74           C
ATOM    710  O   ALA A 113     -58.139  74.988 304.795  1.00 29.46           O
ATOM    711  CB  ALA A 113     -58.429  76.805 307.338  1.00 32.16           C
ATOM    712  N   ALA A 114     -56.295  74.683 306.046  1.00 32.77           N
ATOM    713  CA  ALA A 114     -55.449  74.392 304.884  1.00 34.35           C
ATOM    714  C   ALA A 114     -55.992  73.258 304.017  1.00 34.74           C
ATOM    715  O   ALA A 114     -56.071  73.384 302.796  1.00 36.29           O
ATOM    716  CB  ALA A 114     -54.015  74.066 305.330  1.00 32.36           C
ATOM    717  N   PRO A 115     -56.370  72.131 304.635  1.00 33.28           N
ATOM    718  CA  PRO A 115     -56.896  71.014 303.841  1.00 35.20           C
ATOM    719  C   PRO A 115     -58.132  71.429 303.039  1.00 33.43           C
ATOM    720  O   PRO A 115     -58.312  71.029 301.894  1.00 38.62           O
ATOM    721  CB  PRO A 115     -57.208  69.958 304.898  1.00 35.14           C
ATOM    722  CG  PRO A 115     -56.185  70.243 305.970  1.00 37.34           C
ATOM    723  CD  PRO A 115     -56.245  71.756 306.054  1.00 34.14           C
ATOM    724  N   ILE A 116     -58.980  72.241 303.652  1.00 35.23           N
ATOM    725  CA  ILE A 116     -60.184  72.716 302.992  1.00 33.87           C
ATOM    726  C   ILE A 116     -59.832  73.672 301.867  1.00 36.25           C
ATOM    727  O   ILE A 116     -60.440  73.632 300.802  1.00 36.90           O
ATOM    728  CB  ILE A 116     -61.105  73.413 303.998  1.00 34.78           C
ATOM    729  CG1 ILE A 116     -61.666  72.362 304.963  1.00 35.63           C
ATOM    730  CG2 ILE A 116     -62.215  74.166 303.271  1.00 33.04           C
ATOM    731  CD1 ILE A 116     -62.615  72.922 305.986  1.00 49.21           C
ATOM    732  N   ILE A 117     -58.848  74.537 302.097  1.00 34.39           N
ATOM    733  CA  ILE A 117     -58.437  75.470 301.061  1.00 33.17           C
ATOM    734  C   ILE A 117     -57.892  74.650 299.896  1.00 33.71           C
ATOM    735  O   ILE A 117     -58.162  74.952 298.732  1.00 31.73           O
ATOM    736  CB  ILE A 117     -57.364  76.448 301.587  1.00 34.98           C
ATOM    737  CG1 ILE A 117     -58.016  77.439 302.558  1.00 34.55           C
ATOM    738  CG2 ILE A 117     -56.698  77.183 300.429  1.00 26.96           C
ATOM    739  CD1 ILE A 117     -57.028  78.371 303.265  1.00 34.19           C
ATOM    740  N   ALA A 118     -57.143  73.598 300.217  1.00 30.96           N
ATOM    741  CA  ALA A 118     -56.589  72.724 299.189  1.00 33.98           C
ATOM    742  C   ALA A 118     -57.717  72.039 298.402  1.00 38.60           C
ATOM    743  O   ALA A 118     -57.644  71.921 297.181  1.00 36.51           O
ATOM    744  CB  ALA A 118     -55.694  71.681 299.826  1.00 35.19           C
ATOM    745  N   GLU A 119     -58.757  71.575 299.096  1.00 41.07           N
ATOM    746  CA  GLU A 119     -59.870  70.922 298.409  1.00 38.94           C
ATOM    747  C   GLU A 119     -60.417  71.859 297.357  1.00 36.38           C
ATOM    748  O   GLU A 119     -60.629  71.463 296.215  1.00 37.76           O
ATOM    749  CB  GLU A 119     -60.997  70.559 299.377  1.00 43.15           C
ATOM    750  CG  GLU A 119     -60.719  69.348 300.250  1.00 52.51           C
ATOM    751  CD  GLU A 119     -61.917  68.975 301.112  1.00 60.48           C
ATOM    752  OE1 GLU A 119     -62.426  69.854 301.839  1.00 64.26           O
ATOM    753  OE2 GLU A 119     -62.349  67.803 301.065  1.00 66.56           O
ATOM    754  N   VAL A 120     -60.642  73.111 297.745  1.00 35.97           N
ATOM    755  CA  VAL A 120     -61.170  74.102 296.818  1.00 36.89           C
ATOM    756  C   VAL A 120     -60.262  74.292 295.600  1.00 39.38           C
ATOM    757  O   VAL A 120     -60.729  74.253 294.461  1.00 38.56           O
ATOM    758  CB  VAL A 120     -61.376  75.461 297.517  1.00 36.36           C
ATOM    759  CG1 VAL A 120     -61.890  76.478 296.524  1.00 34.63           C
ATOM    760  CG2 VAL A 120     -62.369  75.304 298.674  1.00 41.97           C
ATOM    761  N   ALA A 121     -58.968  74.496 295.841  1.00 38.16           N
ATOM    762  CA  ALA A 121     -58.013  74.690 294.752  1.00 38.56           C
ATOM    763  C   ALA A 121     -58.051  73.505 293.788  1.00 38.48           C
ATOM    764  O   ALA A 121     -58.050  73.681 292.572  1.00 36.66           O
ATOM    765  CB  ALA A 121     -56.596  74.858 295.322  1.00 37.59           C
ATOM    766  N   LYS A 122     -58.074  72.302 294.354  1.00 39.59           N
ATOM    767  CA  LYS A 122     -58.117  71.054 293.599  1.00 44.03           C
ATOM    768  C   LYS A 122     -59.403  70.992 292.780  1.00 49.04           C
ATOM    769  O   LYS A 122     -59.390  70.672 291.589  1.00 49.41           O
ATOM    770  CB  LYS A 122     -58.057  69.878 294.576  1.00 43.34           C
ATOM    771  CG  LYS A 122     -58.137  68.494 293.954  1.00 48.10           C
ATOM    772  CD  LYS A 122     -58.127  67.435 295.058  1.00 52.37           C
ATOM    773  CE  LYS A 122     -58.210  66.014 294.509  1.00 56.08           C
ATOM    774  NZ  LYS A 122     -57.019  65.654 293.696  1.00 58.93           N
ATOM    775  N   GLU A 123     -60.515  71.303 293.434  1.00 51.52           N
ATOM    776  CA  GLU A 123     -61.818  71.307 292.787  1.00 52.01           C
ATOM    777  C   GLU A 123     -61.783  72.256 291.589  1.00 51.57           C
ATOM    778  O   GLU A 123     -62.453  72.023 290.580  1.00 51.26           O
ATOM    779  CB  GLU A 123     -62.878  71.750 293.798  1.00 55.19           C
ATOM    780  CG  GLU A 123     -64.298  71.772 293.284  1.00 63.12           C
ATOM    781  CD  GLU A 123     -65.305  71.972 294.406  1.00 69.42           C
ATOM    782  OE1 GLU A 123     -65.166  72.955 295.168  1.00 69.15           O
ATOM    783  OE2 GLU A 123     -66.234  71.142 294.527  1.00 72.85           O
ATOM    784  N   MET A 124     -60.983  73.315 291.700  1.00 49.33           N
ATOM    785  CA  MET A 124     -60.853  74.307 290.633  1.00 46.54           C
ATOM    786  C   MET A 124     -59.787  73.940 289.597  1.00 45.76           C
ATOM    787  O   MET A 124     -59.541  74.697 288.661  1.00 44.09           O
ATOM    788  CB  MET A 124     -60.528  75.679 291.229  1.00 47.05           C
ATOM    789  CG  MET A 124     -61.612  76.228 292.135  1.00 47.48           C
ATOM    790  SD  MET A 124     -61.120  77.739 292.981  1.00 50.89           S
ATOM    791  CE  MET A 124     -61.420  78.952 291.726  1.00 49.12           C
ATOM    792  N   GLY A 125     -59.154  72.783 289.765  1.00 45.06           N
ATOM    793  CA  GLY A 125     -58.140  72.356 288.814  1.00 46.06           C
ATOM    794  C   GLY A 125     -56.863  73.183 288.808  1.00 48.74           C
ATOM    795  O   GLY A 125     -56.223  73.347 287.766  1.00 49.29           O
ATOM    796  N   ILE A 126     -56.482  73.705 289.969  1.00 44.65           N
ATOM    797  CA  ILE A 126     -55.269  74.508 290.068  1.00 43.99           C
ATOM    798  C   ILE A 126     -54.140  73.676 290.656  1.00 42.18           C
ATOM    799  O   ILE A 126     -54.339  72.987 291.662  1.00 42.15           O
ATOM    800  CB  ILE A 126     -55.485  75.739 290.977  1.00 46.96           C
ATOM    801  CG1 ILE A 126     -56.535  76.661 290.359  1.00 46.24           C
ATOM    802  CG2 ILE A 126     -54.164  76.470 291.194  1.00 45.37           C
ATOM    803  CD1 ILE A 126     -56.925  77.824 291.247  1.00 49.91           C
ATOM    804  N   LEU A 127     -52.964  73.725 290.026  1.00 37.00           N
ATOM    805  CA  LEU A 127     -51.809  72.990 290.539  1.00 36.15           C
ATOM    806  C   LEU A 127     -51.601  73.521 291.949  1.00 36.68           C
ATOM    807  O   LEU A 127     -51.495  74.731 292.146  1.00 37.02           O
ATOM    808  CB  LEU A 127     -50.558  73.269 289.706  1.00 33.12           C
ATOM    809  CG  LEU A 127     -49.281  72.680 290.310  1.00 33.71           C
ATOM    810  CD1 LEU A 127     -49.426  71.176 290.407  1.00 33.04           C
ATOM    811  CD2 LEU A 127     -48.067  73.055 289.465  1.00 35.38           C
ATOM    812  N   THR A 128     -51.542  72.627 292.927  1.00 36.03           N
ATOM    813  CA  THR A 128     -51.393  73.061 294.301  1.00 35.38           C
ATOM    814  C   THR A 128     -50.251  72.413 295.042  1.00 36.11           C
ATOM    815  O   THR A 128     -50.156  71.186 295.141  1.00 30.40           O
ATOM    816  CB  THR A 128     -52.695  72.819 295.091  1.00 43.00           C
ATOM    817  OG1 THR A 128     -53.760  73.561 294.484  1.00 48.51           O
ATOM    818  CG2 THR A 128     -52.538  73.275 296.536  1.00 40.27           C
ATOM    819  N   VAL A 129     -49.382  73.268 295.566  1.00 32.44           N
ATOM    820  CA  VAL A 129     -48.237  72.827 296.327  1.00 31.43           C
ATOM    821  C   VAL A 129     -48.322  73.372 297.748  1.00 32.10           C
ATOM    822  O   VAL A 129     -48.372  74.588 297.966  1.00 31.24           O
ATOM    823  CB  VAL A 129     -46.934  73.313 295.672  1.00 32.18           C
ATOM    824  CG1 VAL A 129     -45.740  72.799 296.447  1.00 35.84           C
ATOM    825  CG2 VAL A 129     -46.881  72.837 294.225  1.00 35.75           C
ATOM    826  N   ALA A 130     -48.374  72.471 298.719  1.00 30.91           N
ATOM    827  CA  ALA A 130     -48.406  72.897 300.106  1.00 29.63           C
ATOM    828  C   ALA A 130     -46.971  72.908 300.612  1.00 31.74           C
ATOM    829  O   ALA A 130     -46.186  72.013 300.284  1.00 30.76           O
ATOM    830  CB  ALA A 130     -49.234  71.947 300.939  1.00 26.74           C
ATOM    831  N   VAL A 131     -46.622  73.943 301.374  1.00 32.29           N
ATOM    832  CA  VAL A 131     -45.300  74.039 301.974  1.00 29.88           C
ATOM    833  C   VAL A 131     -45.590  74.289 303.446  1.00 28.65           C
ATOM    834  O   VAL A 131     -45.925  75.401 303.846  1.00 27.66           O
ATOM    835  CB  VAL A 131     -44.459  75.200 301.394  1.00 32.80           C
ATOM    836  CG1 VAL A 131     -43.010  75.056 301.871  1.00 32.74           C
ATOM    837  CG2 VAL A 131     -44.504  75.182 299.873  1.00 30.41           C
ATOM    838  N   VAL A 132     -45.475  73.242 304.252  1.00 25.41           N
ATOM    839  CA  VAL A 132     -45.791  73.363 305.660  1.00 32.40           C
ATOM    840  C   VAL A 132     -44.705  72.847 306.589  1.00 32.96           C
ATOM    841  O   VAL A 132     -43.819  72.085 306.189  1.00 31.70           O
ATOM    842  CB  VAL A 132     -47.098  72.608 305.980  1.00 29.01           C
ATOM    843  CG1 VAL A 132     -48.176  72.996 304.981  1.00 29.75           C
ATOM    844  CG2 VAL A 132     -46.851  71.099 305.937  1.00 30.50           C
ATOM    845  N   THR A 133     -44.788  73.273 307.843  1.00 33.39           N
ATOM    846  CA  THR A 133     -43.833  72.833 308.846  1.00 31.16           C
ATOM    847  C   THR A 133     -44.513  71.911 309.838  1.00 32.04           C
ATOM    848  O   THR A 133     -45.736  71.973 310.029  1.00 30.76           O
ATOM    849  CB  THR A 133     -43.236  74.017 309.648  1.00 33.29           C
ATOM    850  OG1 THR A 133     -44.293  74.750 310.289  1.00 30.26           O
ATOM    851  CG2 THR A 133     -42.435  74.936 308.738  1.00 31.36           C
ATOM    852  N   ARG A 134     -43.715  71.033 310.439  1.00 34.71           N
ATOM    853  CA  ARG A 134     -44.186  70.139 311.485  1.00 34.27           C
ATOM    854  C   ARG A 134     -43.639  70.855 312.715  1.00 35.15           C
ATOM    855  O   ARG A 134     -42.530  71.379 312.672  1.00 33.60           O
ATOM    856  CB  ARG A 134     -43.555  68.757 311.361  1.00 40.16           C
ATOM    857  CG  ARG A 134     -44.414  67.730 310.644  1.00 44.52           C
ATOM    858  CD  ARG A 134     -43.808  66.336 310.794  1.00 48.79           C
ATOM    859  NE  ARG A 134     -44.797  65.279 310.616  1.00 55.87           N
ATOM    860  CZ  ARG A 134     -45.348  64.952 309.453  1.00 61.34           C
ATOM    861  NH1 ARG A 134     -45.003  65.601 308.349  1.00 65.09           N
ATOM    862  NH2 ARG A 134     -46.247  63.977 309.394  1.00 58.48           N
ATOM    863  N   PRO A 135     -44.401  70.884 313.820  1.00 32.98           N
ATOM    864  CA  PRO A 135     -43.999  71.551 315.064  1.00 34.32           C
ATOM    865  C   PRO A 135     -42.633  71.149 315.602  1.00 34.13           C
ATOM    866  O   PRO A 135     -42.122  70.075 315.291  1.00 36.30           O
ATOM    867  CB  PRO A 135     -45.102  71.164 316.050  1.00 34.19           C
ATOM    868  CG  PRO A 135     -46.239  70.747 315.189  1.00 39.92           C
ATOM    869  CD  PRO A 135     -45.592  70.053 314.040  1.00 32.74           C
ATOM    870  N   PHE A 136     -42.048  72.026 316.409  1.00 33.35           N
ATOM    871  CA  PHE A 136     -40.772  71.733 317.038  1.00 35.64           C
ATOM    872  C   PHE A 136     -41.082  70.755 318.168  1.00 38.69           C
ATOM    873  O   PHE A 136     -42.175  70.782 318.740  1.00 36.40           O
ATOM    874  CB  PHE A 136     -40.148  72.983 317.662  1.00 33.32           C
ATOM    875  CG  PHE A 136     -39.530  73.924 316.675  1.00 35.40           C
ATOM    876  CD1 PHE A 136     -40.260  74.997 316.163  1.00 30.02           C
ATOM    877  CD2 PHE A 136     -38.202  73.759 316.280  1.00 32.32           C
ATOM    878  CE1 PHE A 136     -39.678  75.899 315.275  1.00 29.95           C
ATOM    879  CE2 PHE A 136     -37.606  74.652 315.392  1.00 32.48           C
ATOM    880  CZ  PHE A 136     -38.344  75.727 314.887  1.00 34.53           C
ATOM    881  N   PRO A 137     -40.122  69.888 318.516  1.00 41.87           N
ATOM    882  CA  PRO A 137     -40.377  68.936 319.600  1.00 41.44           C
ATOM    883  C   PRO A 137     -40.771  69.632 320.910  1.00 42.50           C
ATOM    884  O   PRO A 137     -41.562  69.097 321.691  1.00 42.22           O
ATOM    885  CB  PRO A 137     -39.060  68.166 319.703  1.00 43.88           C
ATOM    886  CG  PRO A 137     -38.032  69.166 319.221  1.00 50.11           C
ATOM    887  CD  PRO A 137     -38.736  69.784 318.028  1.00 45.21           C
ATOM    888  N   PHE A 138     -40.248  70.833 321.141  1.00 40.50           N
ATOM    889  CA  PHE A 138     -40.571  71.556 322.365  1.00 38.94           C
ATOM    890  C   PHE A 138     -42.023  72.025 322.455  1.00 44.20           C
ATOM    891  O   PHE A 138     -42.460  72.506 323.502  1.00 43.90           O
ATOM    892  CB  PHE A 138     -39.631  72.753 322.552  1.00 38.41           C
ATOM    893  CG  PHE A 138     -39.796  73.850 321.522  1.00 39.80           C
ATOM    894  CD1 PHE A 138     -40.923  74.664 321.514  1.00 37.06           C
ATOM    895  CD2 PHE A 138     -38.789  74.101 320.597  1.00 38.58           C
ATOM    896  CE1 PHE A 138     -41.040  75.712 320.599  1.00 39.00           C
ATOM    897  CE2 PHE A 138     -38.896  75.141 319.685  1.00 41.77           C
ATOM    898  CZ  PHE A 138     -40.024  75.951 319.685  1.00 38.88           C
ATOM    899  N   GLU A 139     -42.779  71.886 321.370  1.00 42.22           N
ATOM    900  CA  GLU A 139     -44.169  72.327 321.389  1.00 41.77           C
ATOM    901  C   GLU A 139     -45.118  71.290 321.976  1.00 40.89           C
ATOM    902  O   GLU A 139     -46.288  71.584 322.229  1.00 42.26           O
ATOM    903  CB  GLU A 139     -44.621  72.704 319.982  1.00 39.69           C
ATOM    904  CG  GLU A 139     -43.853  73.872 319.386  1.00 35.86           C
ATOM    905  CD  GLU A 139     -44.383  74.232 318.024  1.00 39.52           C
ATOM    906  OE1 GLU A 139     -45.581  74.584 317.948  1.00 39.61           O
ATOM    907  OE2 GLU A 139     -43.619  74.152 317.035  1.00 32.81           O
ATOM    908  N   GLY A 140     -44.621  70.074 322.181  1.00 41.11           N
ATOM    909  CA  GLY A 140     -45.455  69.041 322.769  1.00 42.93           C
ATOM    910  C   GLY A 140     -46.010  67.993 321.826  1.00 45.80           C
ATOM    911  O   GLY A 140     -46.130  68.204 320.613  1.00 42.82           O
ATOM    912  N   ARG A 141     -46.376  66.857 322.407  1.00 44.23           N
ATOM    913  CA  ARG A 141     -46.913  65.735 321.653  1.00 47.12           C
ATOM    914  C   ARG A 141     -48.280  66.073 321.061  1.00 43.68           C
ATOM    915  O   ARG A 141     -48.592  65.692 319.937  1.00 40.43           O
ATOM    916  CB  ARG A 141     -47.035  64.520 322.573  1.00 54.76           C
ATOM    917  CG  ARG A 141     -47.173  63.195 321.856  1.00 65.09           C
ATOM    918  CD  ARG A 141     -48.071  62.251 322.642  1.00 74.97           C
ATOM    919  NE  ARG A 141     -47.798  62.279 324.076  1.00 79.40           N
ATOM    920  CZ  ARG A 141     -48.473  61.570 324.975  1.00 82.46           C
ATOM    921  NH1 ARG A 141     -48.159  61.656 326.262  1.00 83.04           N
ATOM    922  NH2 ARG A 141     -49.462  60.773 324.588  1.00 83.23           N
ATOM    923  N   LYS A 142     -49.092  66.791 321.826  1.00 41.29           N
ATOM    924  CA  LYS A 142     -50.419  67.161 321.371  1.00 42.74           C
ATOM    925  C   LYS A 142     -50.374  67.841 319.999  1.00 42.60           C
ATOM    926  O   LYS A 142     -51.072  67.436 319.065  1.00 42.00           O
ATOM    927  CB  LYS A 142     -51.075  68.083 322.399  1.00 47.22           C
ATOM    928  CG  LYS A 142     -52.480  68.526 322.032  1.00 53.71           C
ATOM    929  CD  LYS A 142     -53.406  67.334 321.860  1.00 59.16           C
ATOM    930  CE  LYS A 142     -54.798  67.776 321.445  1.00 63.31           C
ATOM    931  NZ  LYS A 142     -55.679  66.610 321.178  1.00 67.73           N
ATOM    932  N   ARG A 143     -49.542  68.867 319.871  1.00 39.32           N
ATOM    933  CA  ARG A 143     -49.444  69.574 318.602  1.00 40.84           C
ATOM    934  C   ARG A 143     -48.857  68.714 317.494  1.00 35.00           C
ATOM    935  O   ARG A 143     -49.288  68.807 316.349  1.00 36.12           O
ATOM    936  CB  ARG A 143     -48.646  70.872 318.773  1.00 39.55           C
ATOM    937  CG  ARG A 143     -49.401  71.902 319.604  1.00 47.59           C
ATOM    938  CD  ARG A 143     -48.640  73.204 319.757  1.00 52.59           C
ATOM    939  NE  ARG A 143     -48.766  74.057 318.584  1.00 50.85           N
ATOM    940  CZ  ARG A 143     -49.559  75.123 318.510  1.00 47.98           C
ATOM    941  NH1 ARG A 143     -49.599  75.831 317.393  1.00 44.02           N
ATOM    942  NH2 ARG A 143     -50.301  75.490 319.545  1.00 41.37           N
ATOM    943  N   MET A 144     -47.893  67.862 317.826  1.00 38.04           N
ATOM    944  CA  MET A 144     -47.292  66.998 316.814  1.00 40.03           C
ATOM    945  C   MET A 144     -48.351  66.036 316.275  1.00 41.23           C
ATOM    946  O   MET A 144     -48.354  65.702 315.095  1.00 41.78           O
ATOM    947  CB  MET A 144     -46.117  66.217 317.410  1.00 41.25           C
ATOM    948  CG  MET A 144     -45.300  65.431 316.393  1.00 44.97           C
ATOM    949  SD  MET A 144     -44.563  66.441 315.057  1.00 56.45           S
ATOM    950  CE  MET A 144     -45.580  65.972 313.702  1.00 52.00           C
ATOM    951  N   GLN A 145     -49.261  65.610 317.148  1.00 42.96           N
ATOM    952  CA  GLN A 145     -50.334  64.695 316.764  1.00 42.30           C
ATOM    953  C   GLN A 145     -51.320  65.402 315.846  1.00 38.76           C
ATOM    954  O   GLN A 145     -51.768  64.857 314.833  1.00 36.83           O
ATOM    955  CB  GLN A 145     -51.085  64.211 318.007  1.00 49.08           C
ATOM    956  CG  GLN A 145     -50.237  63.428 318.993  1.00 60.12           C
ATOM    957  CD  GLN A 145     -50.991  63.084 320.271  1.00 65.43           C
ATOM    958  OE1 GLN A 145     -50.462  62.406 321.151  1.00 64.73           O
ATOM    959  NE2 GLN A 145     -52.233  63.556 320.377  1.00 67.20           N
ATOM    960  N   ILE A 146     -51.683  66.615 316.239  1.00 36.82           N
ATOM    961  CA  ILE A 146     -52.613  67.425 315.478  1.00 37.56           C
ATOM    962  C   ILE A 146     -52.014  67.697 314.105  1.00 39.80           C
ATOM    963  O   ILE A 146     -52.690  67.578 313.084  1.00 36.85           O
ATOM    964  CB  ILE A 146     -52.879  68.756 316.204  1.00 36.95           C
ATOM    965  CG1 ILE A 146     -53.677  68.483 317.484  1.00 37.69           C
ATOM    966  CG2 ILE A 146     -53.592  69.731 315.270  1.00 30.39           C
ATOM    967  CD1 ILE A 146     -53.889  69.706 318.366  1.00 40.59           C
ATOM    968  N   ALA A 147     -50.732  68.045 314.093  1.00 40.24           N
ATOM    969  CA  ALA A 147     -50.029  68.331 312.852  1.00 42.01           C
ATOM    970  C   ALA A 147     -50.063  67.116 311.942  1.00 43.64           C
ATOM    971  O   ALA A 147     -50.376  67.229 310.759  1.00 43.51           O
ATOM    972  CB  ALA A 147     -48.582  68.723 313.145  1.00 37.72           C
ATOM    973  N   ASP A 148     -49.743  65.949 312.495  1.00 46.57           N
ATOM    974  CA  ASP A 148     -49.734  64.729 311.697  1.00 48.73           C
ATOM    975  C   ASP A 148     -51.091  64.459 311.060  1.00 46.91           C
ATOM    976  O   ASP A 148     -51.162  64.056 309.899  1.00 46.72           O
ATOM    977  CB  ASP A 148     -49.311  63.529 312.548  1.00 52.88           C
ATOM    978  CG  ASP A 148     -47.851  63.592 312.967  1.00 59.23           C
ATOM    979  OD1 ASP A 148     -46.982  63.826 312.096  1.00 60.70           O
ATOM    980  OD2 ASP A 148     -47.570  63.394 314.167  1.00 63.66           O
ATOM    981  N   GLU A 149     -52.162  64.686 311.816  1.00 44.18           N
ATOM    982  CA  GLU A 149     -53.510  64.469 311.306  1.00 44.56           C
ATOM    983  C   GLU A 149     -53.822  65.464 310.201  1.00 42.13           C
ATOM    984  O   GLU A 149     -54.318  65.088 309.136  1.00 43.30           O
ATOM    985  CB  GLU A 149     -54.540  64.606 312.432  1.00 51.01           C
ATOM    986  CG  GLU A 149     -55.995  64.685 311.956  1.00 61.65           C
ATOM    987  CD  GLU A 149     -56.395  63.524 311.055  1.00 71.08           C
ATOM    988  OE1 GLU A 149     -56.216  62.357 311.468  1.00 78.58           O
ATOM    989  OE2 GLU A 149     -56.894  63.777 309.934  1.00 72.85           O
ATOM    990  N   GLY A 150     -53.534  66.737 310.453  1.00 39.18           N
ATOM    991  CA  GLY A 150     -53.784  67.748 309.444  1.00 34.54           C
ATOM    992  C   GLY A 150     -52.995  67.474 308.172  1.00 33.28           C
ATOM    993  O   GLY A 150     -53.477  67.698 307.064  1.00 32.60           O
ATOM    994  N   ILE A 151     -51.769  66.990 308.327  1.00 36.60           N
ATOM    995  CA  ILE A 151     -50.926  66.696 307.177  1.00 37.28           C
ATOM    996  C   ILE A 151     -51.515  65.553 306.361  1.00 39.62           C
ATOM    997  O   ILE A 151     -51.478  65.574 305.127  1.00 41.89           O
ATOM    998  CB  ILE A 151     -49.487  66.357 307.630  1.00 36.44           C
ATOM    999  CG1 ILE A 151     -48.778  67.655 308.031  1.00 37.75           C
ATOM   1000  CG2 ILE A 151     -48.724  65.645 306.516  1.00 33.38           C
ATOM   1001  CD1 ILE A 151     -47.401  67.467 308.619  1.00 42.51           C
ATOM   1002  N   ARG A 152     -52.077  64.568 307.052  1.00 41.01           N
ATOM   1003  CA  ARG A 152     -52.688  63.426 306.386  1.00 41.72           C
ATOM   1004  C   ARG A 152     -53.910  63.906 305.601  1.00 41.04           C
ATOM   1005  O   ARG A 152     -54.136  63.491 304.464  1.00 43.36           O
ATOM   1006  CB  ARG A 152     -53.092  62.376 307.424  1.00 49.87           C
ATOM   1007  CG  ARG A 152     -53.685  61.098 306.845  1.00 61.58           C
ATOM   1008  CD  ARG A 152     -55.166  60.957 307.191  1.00 71.54           C
ATOM   1009  NE  ARG A 152     -55.985  62.002 306.579  1.00 78.77           N
ATOM   1010  CZ  ARG A 152     -57.296  62.130 306.764  1.00 79.57           C
ATOM   1011  NH1 ARG A 152     -57.962  63.109 306.167  1.00 80.50           N
ATOM   1012  NH2 ARG A 152     -57.942  61.280 307.548  1.00 84.31           N
ATOM   1013  N   ALA A 153     -54.693  64.792 306.205  1.00 38.02           N
ATOM   1014  CA  ALA A 153     -55.873  65.329 305.534  1.00 38.96           C
ATOM   1015  C   ALA A 153     -55.467  66.208 304.351  1.00 39.97           C
ATOM   1016  O   ALA A 153     -56.168  66.265 303.339  1.00 40.41           O
ATOM   1017  CB  ALA A 153     -56.717  66.138 306.519  1.00 36.49           C
ATOM   1018  N   LEU A 154     -54.333  66.892 304.486  1.00 38.23           N
ATOM   1019  CA  LEU A 154     -53.832  67.778 303.433  1.00 37.59           C
ATOM   1020  C   LEU A 154     -53.362  67.008 302.201  1.00 33.55           C
ATOM   1021  O   LEU A 154     -53.646  67.388 301.067  1.00 35.03           O
ATOM   1022  CB  LEU A 154     -52.670  68.624 303.975  1.00 38.66           C
ATOM   1023  CG  LEU A 154     -52.113  69.745 303.093  1.00 38.11           C
ATOM   1024  CD1 LEU A 154     -53.246  70.689 302.658  1.00 39.25           C
ATOM   1025  CD2 LEU A 154     -51.051  70.510 303.882  1.00 33.54           C
ATOM   1026  N   ALA A 155     -52.642  65.920 302.431  1.00 35.01           N
ATOM   1027  CA  ALA A 155     -52.123  65.106 301.339  1.00 38.55           C
ATOM   1028  C   ALA A 155     -53.218  64.577 300.410  1.00 44.31           C
ATOM   1029  O   ALA A 155     -52.942  64.173 299.279  1.00 44.54           O
ATOM   1030  CB  ALA A 155     -51.308  63.944 301.905  1.00 33.84           C
ATOM   1031  N   GLU A 156     -54.463  64.588 300.875  1.00 47.15           N
ATOM   1032  CA  GLU A 156     -55.560  64.088 300.056  1.00 49.67           C
ATOM   1033  C   GLU A 156     -55.996  65.060 298.961  1.00 49.11           C
ATOM   1034  O   GLU A 156     -56.725  64.681 298.045  1.00 46.30           O
ATOM   1035  CB  GLU A 156     -56.757  63.740 300.947  1.00 55.15           C
ATOM   1036  CG  GLU A 156     -56.414  62.761 302.063  1.00 65.73           C
ATOM   1037  CD  GLU A 156     -57.600  62.447 302.958  1.00 75.79           C
ATOM   1038  OE1 GLU A 156     -58.255  63.398 303.435  1.00 82.20           O
ATOM   1039  OE2 GLU A 156     -57.874  61.250 303.193  1.00 80.67           O
ATOM   1040  N   SER A 157     -55.549  66.308 299.027  1.00 48.20           N
ATOM   1041  CA  SER A 157     -55.977  67.255 298.007  1.00 49.27           C
ATOM   1042  C   SER A 157     -54.928  68.188 297.403  1.00 47.58           C
ATOM   1043  O   SER A 157     -55.279  69.135 296.696  1.00 53.28           O
ATOM   1044  CB  SER A 157     -57.154  68.075 298.542  1.00 48.83           C
ATOM   1045  OG  SER A 157     -56.841  68.650 299.795  1.00 61.30           O
ATOM   1046  N   VAL A 158     -53.651  67.944 297.672  1.00 44.63           N
ATOM   1047  CA  VAL A 158     -52.604  68.785 297.093  1.00 40.28           C
ATOM   1048  C   VAL A 158     -51.804  67.940 296.118  1.00 39.27           C
ATOM   1049  O   VAL A 158     -51.715  66.725 296.281  1.00 38.36           O
ATOM   1050  CB  VAL A 158     -51.627  69.352 298.164  1.00 39.42           C
ATOM   1051  CG1 VAL A 158     -52.384  70.230 299.139  1.00 41.75           C
ATOM   1052  CG2 VAL A 158     -50.918  68.218 298.894  1.00 38.18           C
ATOM   1053  N   ASP A 159     -51.231  68.574 295.102  1.00 38.46           N
ATOM   1054  CA  ASP A 159     -50.434  67.838 294.136  1.00 39.39           C
ATOM   1055  C   ASP A 159     -49.128  67.418 294.779  1.00 40.05           C
ATOM   1056  O   ASP A 159     -48.723  66.259 294.682  1.00 37.08           O
ATOM   1057  CB  ASP A 159     -50.190  68.685 292.897  1.00 40.70           C
ATOM   1058  CG  ASP A 159     -51.441  68.842 292.063  1.00 42.10           C
ATOM   1059  OD1 ASP A 159     -52.132  69.873 292.200  1.00 42.26           O
ATOM   1060  OD2 ASP A 159     -51.742  67.914 291.280  1.00 45.13           O
ATOM   1061  N   SER A 160     -48.479  68.370 295.445  1.00 39.42           N
ATOM   1062  CA  SER A 160     -47.239  68.109 296.157  1.00 37.91           C
ATOM   1063  C   SER A 160     -47.317  68.762 297.528  1.00 36.91           C
ATOM   1064  O   SER A 160     -47.733  69.919 297.668  1.00 33.20           O
ATOM   1065  CB  SER A 160     -46.029  68.644 295.389  1.00 39.33           C
ATOM   1066  OG  SER A 160     -45.721  67.813 294.286  1.00 44.20           O
ATOM   1067  N   LEU A 161     -46.917  68.006 298.540  1.00 35.99           N
ATOM   1068  CA  LEU A 161     -46.944  68.484 299.911  1.00 37.42           C
ATOM   1069  C   LEU A 161     -45.533  68.493 300.469  1.00 36.21           C
ATOM   1070  O   LEU A 161     -45.025  67.463 300.921  1.00 31.23           O
ATOM   1071  CB  LEU A 161     -47.859  67.584 300.751  1.00 39.46           C
ATOM   1072  CG  LEU A 161     -47.938  67.680 302.283  1.00 45.52           C
ATOM   1073  CD1 LEU A 161     -47.954  69.117 302.755  1.00 44.62           C
ATOM   1074  CD2 LEU A 161     -49.206  66.946 302.742  1.00 44.75           C
ATOM   1075  N   ILE A 162     -44.895  69.661 300.418  1.00 34.85           N
ATOM   1076  CA  ILE A 162     -43.542  69.801 300.932  1.00 33.28           C
ATOM   1077  C   ILE A 162     -43.599  69.947 302.436  1.00 34.82           C
ATOM   1078  O   ILE A 162     -44.253  70.848 302.965  1.00 33.38           O
ATOM   1079  CB  ILE A 162     -42.825  71.036 300.351  1.00 34.58           C
ATOM   1080  CG1 ILE A 162     -42.722  70.905 298.830  1.00 33.04           C
ATOM   1081  CG2 ILE A 162     -41.424  71.174 300.980  1.00 31.97           C
ATOM   1082  CD1 ILE A 162     -42.111  72.108 298.151  1.00 35.26           C
ATOM   1083  N   THR A 163     -42.915  69.045 303.125  1.00 35.76           N
ATOM   1084  CA  THR A 163     -42.882  69.078 304.569  1.00 37.53           C
ATOM   1085  C   THR A 163     -41.546  69.556 305.102  1.00 37.28           C
ATOM   1086  O   THR A 163     -40.485  69.078 304.694  1.00 37.87           O
ATOM   1087  CB  THR A 163     -43.158  67.701 305.161  1.00 39.96           C
ATOM   1088  OG1 THR A 163     -44.538  67.364 304.958  1.00 47.10           O
ATOM   1089  CG2 THR A 163     -42.829  67.697 306.646  1.00 40.98           C
ATOM   1090  N   ILE A 164     -41.613  70.499 306.030  1.00 37.15           N
ATOM   1091  CA  ILE A 164     -40.423  71.039 306.663  1.00 39.61           C
ATOM   1092  C   ILE A 164     -40.485  70.780 308.161  1.00 38.63           C
ATOM   1093  O   ILE A 164     -41.141  71.509 308.901  1.00 37.14           O
ATOM   1094  CB  ILE A 164     -40.300  72.553 306.426  1.00 39.46           C
ATOM   1095  CG1 ILE A 164     -40.056  72.816 304.940  1.00 45.22           C
ATOM   1096  CG2 ILE A 164     -39.164  73.120 307.269  1.00 36.73           C
ATOM   1097  CD1 ILE A 164     -40.100  74.273 304.561  1.00 51.74           C
ATOM   1098  N   PRO A 165     -39.818  69.716 308.626  1.00 39.57           N
ATOM   1099  CA  PRO A 165     -39.835  69.417 310.060  1.00 39.67           C
ATOM   1100  C   PRO A 165     -38.974  70.422 310.813  1.00 36.55           C
ATOM   1101  O   PRO A 165     -37.753  70.441 310.659  1.00 37.53           O
ATOM   1102  CB  PRO A 165     -39.282  67.993 310.122  1.00 39.48           C
ATOM   1103  CG  PRO A 165     -38.376  67.932 308.932  1.00 43.75           C
ATOM   1104  CD  PRO A 165     -39.160  68.640 307.864  1.00 40.42           C
ATOM   1105  N   ASN A 166     -39.616  71.266 311.616  1.00 36.55           N
ATOM   1106  CA  ASN A 166     -38.902  72.285 312.369  1.00 35.52           C
ATOM   1107  C   ASN A 166     -37.765  71.720 313.198  1.00 38.81           C
ATOM   1108  O   ASN A 166     -36.800  72.424 313.492  1.00 36.52           O
ATOM   1109  CB  ASN A 166     -39.864  73.059 313.267  1.00 39.25           C
ATOM   1110  CG  ASN A 166     -40.785  73.966 312.478  1.00 43.35           C
ATOM   1111  OD1 ASN A 166     -40.424  74.449 311.405  1.00 40.78           O
ATOM   1112  ND2 ASN A 166     -41.973  74.216 313.011  1.00 44.81           N
ATOM   1113  N   GLU A 167     -37.884  70.451 313.577  1.00 38.66           N
ATOM   1114  CA  GLU A 167     -36.850  69.788 314.359  1.00 43.62           C
ATOM   1115  C   GLU A 167     -35.518  69.919 313.611  1.00 40.91           C
ATOM   1116  O   GLU A 167     -34.480  70.182 314.216  1.00 38.46           O
ATOM   1117  CB  GLU A 167     -37.221  68.313 314.558  1.00 47.12           C
ATOM   1118  CG  GLU A 167     -36.165  67.458 315.251  1.00 57.96           C
ATOM   1119  CD  GLU A 167     -35.790  67.965 316.634  1.00 70.00           C
ATOM   1120  OE1 GLU A 167     -35.105  69.009 316.730  1.00 73.83           O
ATOM   1121  OE2 GLU A 167     -36.182  67.317 317.628  1.00 76.26           O
ATOM   1122  N   LYS A 168     -35.561  69.759 312.290  1.00 39.74           N
ATOM   1123  CA  LYS A 168     -34.354  69.864 311.470  1.00 38.18           C
ATOM   1124  C   LYS A 168     -33.765  71.274 311.482  1.00 36.79           C
ATOM   1125  O   LYS A 168     -32.559  71.451 311.323  1.00 34.27           O
ATOM   1126  CB  LYS A 168     -34.657  69.468 310.026  1.00 42.28           C
ATOM   1127  CG  LYS A 168     -35.298  68.103 309.865  1.00 43.34           C
ATOM   1128  CD  LYS A 168     -34.367  66.983 310.261  1.00 46.20           C
ATOM   1129  CE  LYS A 168     -35.003  65.640 309.926  1.00 46.78           C
ATOM   1130  NZ  LYS A 168     -34.107  64.516 310.288  1.00 51.69           N
ATOM   1131  N   LEU A 169     -34.613  72.280 311.661  1.00 34.08           N
ATOM   1132  CA  LEU A 169     -34.124  73.653 311.687  1.00 34.14           C
ATOM   1133  C   LEU A 169     -33.169  73.869 312.852  1.00 34.71           C
ATOM   1134  O   LEU A 169     -32.257  74.691 312.768  1.00 36.87           O
ATOM   1135  CB  LEU A 169     -35.295  74.632 311.769  1.00 35.49           C
ATOM   1136  CG  LEU A 169     -36.230  74.541 310.560  1.00 33.72           C
ATOM   1137  CD1 LEU A 169     -37.423  75.471 310.749  1.00 31.83           C
ATOM   1138  CD2 LEU A 169     -35.461  74.898 309.305  1.00 32.74           C
ATOM   1139  N   LEU A 170     -33.382  73.130 313.939  1.00 37.83           N
ATOM   1140  CA  LEU A 170     -32.516  73.234 315.112  1.00 39.81           C
ATOM   1141  C   LEU A 170     -31.120  72.707 314.775  1.00 42.36           C
ATOM   1142  O   LEU A 170     -30.113  73.251 315.232  1.00 43.85           O
ATOM   1143  CB  LEU A 170     -33.116  72.451 316.282  1.00 37.75           C
ATOM   1144  CG  LEU A 170     -33.969  73.229 317.296  1.00 42.66           C
ATOM   1145  CD1 LEU A 170     -34.558  74.475 316.668  1.00 40.62           C
ATOM   1146  CD2 LEU A 170     -35.064  72.322 317.836  1.00 40.15           C
ATOM   1147  N   THR A 171     -31.057  71.651 313.969  1.00 42.61           N
ATOM   1148  CA  THR A 171     -29.765  71.105 313.572  1.00 45.04           C
ATOM   1149  C   THR A 171     -29.036  72.185 312.781  1.00 44.94           C
ATOM   1150  O   THR A 171     -27.883  72.524 313.068  1.00 45.08           O
ATOM   1151  CB  THR A 171     -29.922  69.876 312.668  1.00 47.17           C
ATOM   1152  OG1 THR A 171     -30.670  68.868 313.358  1.00 55.54           O
ATOM   1153  CG2 THR A 171     -28.552  69.322 312.286  1.00 48.84           C
ATOM   1154  N   ILE A 172     -29.723  72.730 311.785  1.00 41.87           N
ATOM   1155  CA  ILE A 172     -29.140  73.768 310.955  1.00 41.45           C
ATOM   1156  C   ILE A 172     -28.677  74.955 311.792  1.00 41.48           C
ATOM   1157  O   ILE A 172     -27.546  75.415 311.644  1.00 41.57           O
ATOM   1158  CB  ILE A 172     -30.147  74.261 309.883  1.00 40.85           C
ATOM   1159  CG1 ILE A 172     -30.505  73.105 308.948  1.00 38.66           C
ATOM   1160  CG2 ILE A 172     -29.551  75.417 309.086  1.00 40.70           C
ATOM   1161  CD1 ILE A 172     -31.547  73.442 307.906  1.00 36.75           C
ATOM   1162  N   LEU A 173     -29.537  75.442 312.681  1.00 40.08           N
ATOM   1163  CA  LEU A 173     -29.188  76.599 313.505  1.00 46.33           C
ATOM   1164  C   LEU A 173     -28.077  76.345 314.517  1.00 48.00           C
ATOM   1165  O   LEU A 173     -27.203  77.188 314.706  1.00 48.50           O
ATOM   1166  CB  LEU A 173     -30.430  77.131 314.227  1.00 43.51           C
ATOM   1167  CG  LEU A 173     -31.470  77.751 313.287  1.00 43.45           C
ATOM   1168  CD1 LEU A 173     -32.723  78.127 314.061  1.00 39.75           C
ATOM   1169  CD2 LEU A 173     -30.864  78.965 312.603  1.00 41.01           C
ATOM   1170  N   GLY A 174     -28.113  75.189 315.168  1.00 49.42           N
ATOM   1171  CA  GLY A 174     -27.093  74.876 316.148  1.00 53.91           C
ATOM   1172  C   GLY A 174     -27.082  75.824 317.335  1.00 56.11           C
ATOM   1173  O   GLY A 174     -28.124  76.100 317.930  1.00 54.67           O
ATOM   1174  N   LYS A 175     -25.898  76.327 317.672  1.00 59.00           N
ATOM   1175  CA  LYS A 175     -25.719  77.233 318.806  1.00 60.20           C
ATOM   1176  C   LYS A 175     -26.478  78.545 318.612  1.00 58.64           C
ATOM   1177  O   LYS A 175     -26.843  79.213 319.583  1.00 55.48           O
ATOM   1178  CB  LYS A 175     -24.221  77.509 319.008  1.00 65.16           C
ATOM   1179  CG  LYS A 175     -23.828  78.059 320.385  1.00 68.67           C
ATOM   1180  CD  LYS A 175     -24.274  79.500 320.598  1.00 71.39           C
ATOM   1181  CE  LYS A 175     -23.686  80.430 319.546  1.00 74.06           C
ATOM   1182  NZ  LYS A 175     -24.175  81.830 319.703  1.00 75.00           N
ATOM   1183  N   ASP A 176     -26.714  78.912 317.356  1.00 57.89           N
ATOM   1184  CA  ASP A 176     -27.432  80.143 317.048  1.00 53.32           C
ATOM   1185  C   ASP A 176     -28.935  80.004 317.240  1.00 49.55           C
ATOM   1186  O   ASP A 176     -29.702  80.891 316.861  1.00 45.66           O
ATOM   1187  CB  ASP A 176     -27.142  80.577 315.614  1.00 59.30           C
ATOM   1188  CG  ASP A 176     -25.714  81.024 315.428  1.00 68.24           C
ATOM   1189  OD1 ASP A 176     -25.350  81.398 314.293  1.00 74.02           O
ATOM   1190  OD2 ASP A 176     -24.956  81.003 316.424  1.00 73.26           O
ATOM   1191  N   ALA A 177     -29.361  78.892 317.827  1.00 44.94           N
ATOM   1192  CA  ALA A 177     -30.784  78.681 318.053  1.00 44.74           C
ATOM   1193  C   ALA A 177     -31.278  79.504 319.237  1.00 41.59           C
ATOM   1194  O   ALA A 177     -30.559  79.709 320.213  1.00 45.90           O
ATOM   1195  CB  ALA A 177     -31.071  77.197 318.289  1.00 39.47           C
ATOM   1196  N   SER A 178     -32.509  79.984 319.119  1.00 41.02           N
ATOM   1197  CA  SER A 178     -33.183  80.763 320.152  1.00 36.22           C
ATOM   1198  C   SER A 178     -34.645  80.672 319.732  1.00 35.36           C
ATOM   1199  O   SER A 178     -34.936  80.251 318.616  1.00 37.76           O
ATOM   1200  CB  SER A 178     -32.729  82.222 320.118  1.00 37.17           C
ATOM   1201  OG  SER A 178     -33.197  82.864 318.942  1.00 35.90           O
ATOM   1202  N   LEU A 179     -35.567  81.070 320.594  1.00 34.43           N
ATOM   1203  CA  LEU A 179     -36.972  80.987 320.228  1.00 35.41           C
ATOM   1204  C   LEU A 179     -37.276  81.841 318.989  1.00 34.68           C
ATOM   1205  O   LEU A 179     -37.885  81.361 318.033  1.00 34.05           O
ATOM   1206  CB  LEU A 179     -37.848  81.409 321.407  1.00 34.69           C
ATOM   1207  CG  LEU A 179     -39.346  81.096 321.298  1.00 39.68           C
ATOM   1208  CD1 LEU A 179     -40.001  82.061 320.333  1.00 50.46           C
ATOM   1209  CD2 LEU A 179     -39.543  79.650 320.834  1.00 34.71           C
ATOM   1210  N   LEU A 180     -36.847  83.099 319.003  1.00 34.56           N
ATOM   1211  CA  LEU A 180     -37.075  83.997 317.874  1.00 36.70           C
ATOM   1212  C   LEU A 180     -36.390  83.525 316.599  1.00 37.71           C
ATOM   1213  O   LEU A 180     -36.980  83.575 315.518  1.00 35.68           O
ATOM   1214  CB  LEU A 180     -36.589  85.412 318.204  1.00 43.89           C
ATOM   1215  CG  LEU A 180     -37.649  86.446 318.606  1.00 51.43           C
ATOM   1216  CD1 LEU A 180     -38.442  86.874 317.377  1.00 52.06           C
ATOM   1217  CD2 LEU A 180     -38.578  85.858 319.660  1.00 54.68           C
ATOM   1218  N   ALA A 181     -35.145  83.072 316.726  1.00 34.00           N
ATOM   1219  CA  ALA A 181     -34.381  82.606 315.576  1.00 32.04           C
ATOM   1220  C   ALA A 181     -34.967  81.337 314.956  1.00 30.31           C
ATOM   1221  O   ALA A 181     -34.923  81.159 313.737  1.00 31.20           O
ATOM   1222  CB  ALA A 181     -32.911  82.376 315.975  1.00 33.83           C
ATOM   1223  N   ALA A 182     -35.514  80.457 315.791  1.00 30.99           N
ATOM   1224  CA  ALA A 182     -36.112  79.205 315.313  1.00 29.88           C
ATOM   1225  C   ALA A 182     -37.276  79.430 314.348  1.00 29.27           C
ATOM   1226  O   ALA A 182     -37.342  78.818 313.282  1.00 29.15           O
ATOM   1227  CB  ALA A 182     -36.588  78.369 316.494  1.00 32.63           C
ATOM   1228  N   PHE A 183     -38.211  80.293 314.726  1.00 29.24           N
ATOM   1229  CA  PHE A 183     -39.351  80.556 313.856  1.00 31.60           C
ATOM   1230  C   PHE A 183     -38.956  81.459 312.701  1.00 29.60           C
ATOM   1231  O   PHE A 183     -39.573  81.415 311.641  1.00 32.28           O
ATOM   1232  CB  PHE A 183     -40.503  81.173 314.647  1.00 31.26           C
ATOM   1233  CG  PHE A 183     -41.188  80.203 315.561  1.00 35.03           C
ATOM   1234  CD1 PHE A 183     -41.216  80.420 316.936  1.00 35.58           C
ATOM   1235  CD2 PHE A 183     -41.788  79.056 315.050  1.00 30.91           C
ATOM   1236  CE1 PHE A 183     -41.829  79.505 317.792  1.00 40.25           C
ATOM   1237  CE2 PHE A 183     -42.402  78.136 315.895  1.00 32.14           C
ATOM   1238  CZ  PHE A 183     -42.422  78.358 317.268  1.00 33.16           C
ATOM   1239  N   ALA A 184     -37.927  82.276 312.911  1.00 28.25           N
ATOM   1240  CA  ALA A 184     -37.437  83.161 311.864  1.00 28.44           C
ATOM   1241  C   ALA A 184     -36.842  82.269 310.778  1.00 30.46           C
ATOM   1242  O   ALA A 184     -36.956  82.556 309.582  1.00 30.43           O
ATOM   1243  CB  ALA A 184     -36.359  84.088 312.417  1.00 27.48           C
ATOM   1244  N   LYS A 185     -36.210  81.180 311.212  1.00 29.91           N
ATOM   1245  CA  LYS A 185     -35.591  80.231 310.300  1.00 28.50           C
ATOM   1246  C   LYS A 185     -36.700  79.534 309.533  1.00 25.66           C
ATOM   1247  O   LYS A 185     -36.589  79.333 308.325  1.00 27.38           O
ATOM   1248  CB  LYS A 185     -34.766  79.197 311.071  1.00 30.79           C
ATOM   1249  CG  LYS A 185     -33.504  78.728 310.353  1.00 40.70           C
ATOM   1250  CD  LYS A 185     -33.781  78.196 308.964  1.00 48.17           C
ATOM   1251  CE  LYS A 185     -32.508  77.717 308.270  1.00 45.70           C
ATOM   1252  NZ  LYS A 185     -31.596  78.823 307.912  1.00 49.69           N
ATOM   1253  N   ALA A 186     -37.773  79.171 310.234  1.00 27.66           N
ATOM   1254  CA  ALA A 186     -38.898  78.506 309.582  1.00 25.75           C
ATOM   1255  C   ALA A 186     -39.436  79.408 308.470  1.00 28.08           C
ATOM   1256  O   ALA A 186     -39.662  78.952 307.351  1.00 26.73           O
ATOM   1257  CB  ALA A 186     -39.997  78.200 310.598  1.00 30.07           C
ATOM   1258  N   ASP A 187     -39.638  80.689 308.778  1.00 24.60           N
ATOM   1259  CA  ASP A 187     -40.128  81.632 307.776  1.00 30.13           C
ATOM   1260  C   ASP A 187     -39.220  81.637 306.541  1.00 29.17           C
ATOM   1261  O   ASP A 187     -39.679  81.503 305.409  1.00 29.64           O
ATOM   1262  CB  ASP A 187     -40.174  83.051 308.353  1.00 30.65           C
ATOM   1263  CG  ASP A 187     -41.219  83.217 309.450  1.00 34.66           C
ATOM   1264  OD1 ASP A 187     -41.174  84.259 310.130  1.00 37.45           O
ATOM   1265  OD2 ASP A 187     -42.087  82.331 309.626  1.00 32.40           O
ATOM   1266  N   ASP A 188     -37.922  81.797 306.776  1.00 31.57           N
ATOM   1267  CA  ASP A 188     -36.937  81.849 305.706  1.00 32.66           C
ATOM   1268  C   ASP A 188     -36.877  80.579 304.857  1.00 31.49           C
ATOM   1269  O   ASP A 188     -36.727  80.639 303.637  1.00 27.90           O
ATOM   1270  CB  ASP A 188     -35.562  82.148 306.299  1.00 39.42           C
ATOM   1271  CG  ASP A 188     -34.487  82.244 305.246  1.00 47.31           C
ATOM   1272  OD1 ASP A 188     -33.837  81.210 304.965  1.00 51.38           O
ATOM   1273  OD2 ASP A 188     -34.303  83.352 304.694  1.00 51.48           O
ATOM   1274  N   VAL A 189     -36.982  79.424 305.496  1.00 31.47           N
ATOM   1275  CA  VAL A 189     -36.951  78.178 304.746  1.00 28.58           C
ATOM   1276  C   VAL A 189     -38.188  78.084 303.853  1.00 29.26           C
ATOM   1277  O   VAL A 189     -38.088  77.719 302.682  1.00 30.28           O
ATOM   1278  CB  VAL A 189     -36.905  76.973 305.686  1.00 31.18           C
ATOM   1279  CG1 VAL A 189     -37.013  75.692 304.882  1.00 34.16           C
ATOM   1280  CG2 VAL A 189     -35.602  76.991 306.468  1.00 37.29           C
ATOM   1281  N   LEU A 190     -39.350  78.433 304.402  1.00 27.56           N
ATOM   1282  CA  LEU A 190     -40.588  78.383 303.636  1.00 28.49           C
ATOM   1283  C   LEU A 190     -40.491  79.304 302.431  1.00 26.82           C
ATOM   1284  O   LEU A 190     -40.976  78.971 301.360  1.00 27.23           O
ATOM   1285  CB  LEU A 190     -41.782  78.778 304.521  1.00 24.76           C
ATOM   1286  CG  LEU A 190     -42.142  77.690 305.540  1.00 30.02           C
ATOM   1287  CD1 LEU A 190     -43.000  78.240 306.668  1.00 26.79           C
ATOM   1288  CD2 LEU A 190     -42.859  76.566 304.802  1.00 33.14           C
ATOM   1289  N   ALA A 191     -39.861  80.463 302.622  1.00 30.01           N
ATOM   1290  CA  ALA A 191     -39.674  81.438 301.553  1.00 31.69           C
ATOM   1291  C   ALA A 191     -38.752  80.872 300.476  1.00 30.97           C
ATOM   1292  O   ALA A 191     -38.961  81.101 299.285  1.00 33.51           O
ATOM   1293  CB  ALA A 191     -39.076  82.734 302.113  1.00 26.69           C
ATOM   1294  N   GLY A 192     -37.737  80.129 300.901  1.00 29.68           N
ATOM   1295  CA  GLY A 192     -36.811  79.548 299.947  1.00 32.48           C
ATOM   1296  C   GLY A 192     -37.503  78.522 299.070  1.00 30.37           C
ATOM   1297  O   GLY A 192     -37.193  78.387 297.883  1.00 30.31           O
ATOM   1298  N   ALA A 193     -38.442  77.791 299.660  1.00 28.44           N
ATOM   1299  CA  ALA A 193     -39.191  76.777 298.925  1.00 34.95           C
ATOM   1300  C   ALA A 193     -40.038  77.447 297.846  1.00 32.33           C
ATOM   1301  O   ALA A 193     -39.955  77.094 296.669  1.00 33.70           O
ATOM   1302  CB  ALA A 193     -40.075  75.981 299.882  1.00 35.70           C
ATOM   1303  N   VAL A 194     -40.836  78.430 298.246  1.00 32.25           N
ATOM   1304  CA  VAL A 194     -41.682  79.147 297.298  1.00 32.44           C
ATOM   1305  C   VAL A 194     -40.837  79.865 296.240  1.00 35.49           C
ATOM   1306  O   VAL A 194     -41.158  79.833 295.047  1.00 36.62           O
ATOM   1307  CB  VAL A 194     -42.574  80.190 298.020  1.00 30.21           C
ATOM   1308  CG1 VAL A 194     -43.346  81.008 297.002  1.00 32.59           C
ATOM   1309  CG2 VAL A 194     -43.539  79.486 298.968  1.00 27.16           C
ATOM   1310  N   ARG A 195     -39.758  80.512 296.675  1.00 32.58           N
ATOM   1311  CA  ARG A 195     -38.883  81.228 295.747  1.00 35.28           C
ATOM   1312  C   ARG A 195     -38.211  80.275 294.752  1.00 36.30           C
ATOM   1313  O   ARG A 195     -38.166  80.552 293.559  1.00 35.26           O
ATOM   1314  CB  ARG A 195     -37.792  81.997 296.508  1.00 32.00           C
ATOM   1315  CG  ARG A 195     -36.934  82.899 295.608  1.00 36.16           C
ATOM   1316  CD  ARG A 195     -35.718  83.511 296.334  1.00 34.49           C
ATOM   1317  NE  ARG A 195     -36.076  84.235 297.552  1.00 36.04           N
ATOM   1318  CZ  ARG A 195     -35.937  83.749 298.785  1.00 37.75           C
ATOM   1319  NH1 ARG A 195     -36.297  84.480 299.831  1.00 36.41           N
ATOM   1320  NH2 ARG A 195     -35.420  82.541 298.978  1.00 38.29           N
ATOM   1321  N   GLY A 196     -37.696  79.156 295.254  1.00 36.29           N
ATOM   1322  CA  GLY A 196     -37.012  78.202 294.401  1.00 36.11           C
ATOM   1323  C   GLY A 196     -37.855  77.696 293.247  1.00 40.58           C
ATOM   1324  O   GLY A 196     -37.369  77.550 292.116  1.00 36.90           O
ATOM   1325  N   ILE A 197     -39.122  77.421 293.535  1.00 35.21           N
ATOM   1326  CA  ILE A 197     -40.045  76.920 292.530  1.00 33.32           C
ATOM   1327  C   ILE A 197     -40.601  78.046 291.666  1.00 33.34           C
ATOM   1328  O   ILE A 197     -40.527  77.988 290.438  1.00 37.66           O
ATOM   1329  CB  ILE A 197     -41.209  76.152 293.200  1.00 35.69           C
ATOM   1330  CG1 ILE A 197     -40.650  74.955 293.971  1.00 32.77           C
ATOM   1331  CG2 ILE A 197     -42.218  75.684 292.147  1.00 35.35           C
ATOM   1332  CD1 ILE A 197     -41.634  74.347 294.955  1.00 31.66           C
ATOM   1333  N   SER A 198     -41.143  79.077 292.301  1.00 31.29           N
ATOM   1334  CA  SER A 198     -41.711  80.196 291.563  1.00 33.54           C
ATOM   1335  C   SER A 198     -40.736  80.840 290.582  1.00 31.64           C
ATOM   1336  O   SER A 198     -41.131  81.209 289.476  1.00 33.67           O
ATOM   1337  CB  SER A 198     -42.238  81.255 292.531  1.00 34.95           C
ATOM   1338  OG  SER A 198     -43.366  80.762 293.231  1.00 46.61           O
ATOM   1339  N   ASP A 199     -39.473  80.977 290.981  1.00 31.89           N
ATOM   1340  CA  ASP A 199     -38.464  81.585 290.109  1.00 31.59           C
ATOM   1341  C   ASP A 199     -38.250  80.793 288.818  1.00 29.69           C
ATOM   1342  O   ASP A 199     -38.055  81.374 287.758  1.00 28.80           O
ATOM   1343  CB  ASP A 199     -37.126  81.725 290.844  1.00 33.82           C
ATOM   1344  CG  ASP A 199     -37.035  83.001 291.678  1.00 43.21           C
ATOM   1345  OD1 ASP A 199     -37.974  83.826 291.641  1.00 44.53           O
ATOM   1346  OD2 ASP A 199     -36.007  83.185 292.367  1.00 44.99           O
ATOM   1347  N   ILE A 200     -38.281  79.467 288.908  1.00 31.40           N
ATOM   1348  CA  ILE A 200     -38.084  78.630 287.729  1.00 31.58           C
ATOM   1349  C   ILE A 200     -39.187  78.923 286.726  1.00 35.07           C
ATOM   1350  O   ILE A 200     -38.965  78.911 285.517  1.00 32.29           O
ATOM   1351  CB  ILE A 200     -38.127  77.128 288.085  1.00 34.70           C
ATOM   1352  CG1 ILE A 200     -36.907  76.758 288.925  1.00 33.58           C
ATOM   1353  CG2 ILE A 200     -38.189  76.282 286.806  1.00 36.04           C
ATOM   1354  CD1 ILE A 200     -35.596  77.153 288.293  1.00 47.30           C
ATOM   1355  N   ILE A 201     -40.376  79.197 287.251  1.00 31.07           N
ATOM   1356  CA  ILE A 201     -41.542  79.496 286.438  1.00 33.49           C
ATOM   1357  C   ILE A 201     -41.577  80.946 285.969  1.00 31.50           C
ATOM   1358  O   ILE A 201     -41.899  81.218 284.817  1.00 33.90           O
ATOM   1359  CB  ILE A 201     -42.855  79.227 287.233  1.00 34.50           C
ATOM   1360  CG1 ILE A 201     -42.981  77.740 287.553  1.00 32.82           C
ATOM   1361  CG2 ILE A 201     -44.058  79.721 286.449  1.00 32.93           C
ATOM   1362  CD1 ILE A 201     -44.058  77.433 288.571  1.00 34.71           C
ATOM   1363  N   LYS A 202     -41.240  81.876 286.854  1.00 32.02           N
ATOM   1364  CA  LYS A 202     -41.315  83.292 286.508  1.00 32.56           C
ATOM   1365  C   LYS A 202     -40.082  83.991 285.947  1.00 35.49           C
ATOM   1366  O   LYS A 202     -40.218  84.936 285.172  1.00 36.76           O
ATOM   1367  CB  LYS A 202     -41.812  84.093 287.719  1.00 34.21           C
ATOM   1368  CG  LYS A 202     -43.115  83.577 288.330  1.00 35.87           C
ATOM   1369  CD  LYS A 202     -44.299  83.722 287.381  1.00 37.50           C
ATOM   1370  CE  LYS A 202     -44.719  85.173 287.232  1.00 31.44           C
ATOM   1371  NZ  LYS A 202     -45.919  85.322 286.360  1.00 37.84           N
ATOM   1372  N   ARG A 203     -38.887  83.559 286.334  1.00 34.14           N
ATOM   1373  CA  ARG A 203     -37.675  84.225 285.857  1.00 36.48           C
ATOM   1374  C   ARG A 203     -36.618  83.251 285.358  1.00 33.71           C
ATOM   1375  O   ARG A 203     -35.441  83.406 285.676  1.00 33.96           O
ATOM   1376  CB  ARG A 203     -37.054  85.049 286.989  1.00 41.68           C
ATOM   1377  CG  ARG A 203     -38.000  85.951 287.740  1.00 49.64           C
ATOM   1378  CD  ARG A 203     -37.432  86.247 289.115  1.00 56.39           C
ATOM   1379  NE  ARG A 203     -36.036  86.666 289.041  1.00 65.11           N
ATOM   1380  CZ  ARG A 203     -35.224  86.761 290.091  1.00 69.24           C
ATOM   1381  NH1 ARG A 203     -33.966  87.151 289.926  1.00 69.36           N
ATOM   1382  NH2 ARG A 203     -35.667  86.461 291.305  1.00 70.57           N
ATOM   1383  N   PRO A 204     -37.012  82.243 284.568  1.00 34.55           N
ATOM   1384  CA  PRO A 204     -36.012  81.289 284.077  1.00 32.54           C
ATOM   1385  C   PRO A 204     -34.954  81.959 283.204  1.00 33.46           C
ATOM   1386  O   PRO A 204     -35.272  82.852 282.428  1.00 34.43           O
ATOM   1387  CB  PRO A 204     -36.855  80.284 283.301  1.00 31.61           C
ATOM   1388  CG  PRO A 204     -37.931  81.149 282.722  1.00 36.16           C
ATOM   1389  CD  PRO A 204     -38.308  82.040 283.896  1.00 35.24           C
ATOM   1390  N   GLY A 205     -33.699  81.523 283.336  1.00 32.13           N
ATOM   1391  CA  GLY A 205     -32.618  82.086 282.540  1.00 27.86           C
ATOM   1392  C   GLY A 205     -32.353  81.238 281.307  1.00 31.74           C
ATOM   1393  O   GLY A 205     -31.789  81.703 280.320  1.00 32.86           O
ATOM   1394  N   MET A 206     -32.750  79.973 281.375  1.00 33.16           N
ATOM   1395  CA  MET A 206     -32.577  79.062 280.257  1.00 32.84           C
ATOM   1396  C   MET A 206     -33.957  78.738 279.691  1.00 35.31           C
ATOM   1397  O   MET A 206     -34.979  79.103 280.286  1.00 34.50           O
ATOM   1398  CB  MET A 206     -31.847  77.803 280.718  1.00 30.67           C
ATOM   1399  CG  MET A 206     -30.407  78.084 281.142  1.00 30.80           C
ATOM   1400  SD  MET A 206     -29.574  76.630 281.766  1.00 38.26           S
ATOM   1401  CE  MET A 206     -29.349  75.705 280.240  1.00 30.00           C
ATOM   1402  N   ILE A 207     -33.990  78.071 278.542  1.00 34.47           N
ATOM   1403  CA  ILE A 207     -35.255  77.745 277.894  1.00 33.88           C
ATOM   1404  C   ILE A 207     -35.596  76.266 277.948  1.00 36.52           C
ATOM   1405  O   ILE A 207     -36.505  75.817 277.246  1.00 36.45           O
ATOM   1406  CB  ILE A 207     -35.226  78.156 276.409  1.00 33.65           C
ATOM   1407  CG1 ILE A 207     -34.136  77.357 275.681  1.00 31.44           C
ATOM   1408  CG2 ILE A 207     -34.974  79.661 276.287  1.00 32.77           C
ATOM   1409  CD1 ILE A 207     -34.031  77.627 274.177  1.00 32.18           C
ATOM   1410  N   ASN A 208     -34.889  75.508 278.779  1.00 32.61           N
ATOM   1411  CA  ASN A 208     -35.138  74.074 278.842  1.00 35.66           C
ATOM   1412  C   ASN A 208     -36.260  73.629 279.789  1.00 33.02           C
ATOM   1413  O   ASN A 208     -36.722  72.494 279.698  1.00 35.05           O
ATOM   1414  CB  ASN A 208     -33.832  73.342 279.185  1.00 36.38           C
ATOM   1415  CG  ASN A 208     -33.343  73.647 280.583  1.00 38.05           C
ATOM   1416  OD1 ASN A 208     -33.442  74.779 281.050  1.00 44.51           O
ATOM   1417  ND2 ASN A 208     -32.800  72.637 281.258  1.00 46.91           N
ATOM   1418  N   VAL A 209     -36.690  74.506 280.694  1.00 35.15           N
ATOM   1419  CA  VAL A 209     -37.762  74.173 281.642  1.00 34.94           C
ATOM   1420  C   VAL A 209     -38.914  75.168 281.558  1.00 33.77           C
ATOM   1421  O   VAL A 209     -38.744  76.348 281.841  1.00 36.38           O
ATOM   1422  CB  VAL A 209     -37.265  74.174 283.120  1.00 40.11           C
ATOM   1423  CG1 VAL A 209     -38.416  73.775 284.055  1.00 40.08           C
ATOM   1424  CG2 VAL A 209     -36.089  73.229 283.296  1.00 35.57           C
ATOM   1425  N   ASP A 210     -40.087  74.694 281.168  1.00 35.35           N
ATOM   1426  CA  ASP A 210     -41.260  75.559 281.069  1.00 36.93           C
ATOM   1427  C   ASP A 210     -42.263  75.170 282.155  1.00 34.76           C
ATOM   1428  O   ASP A 210     -42.109  74.135 282.807  1.00 35.63           O
ATOM   1429  CB  ASP A 210     -41.927  75.408 279.695  1.00 40.40           C
ATOM   1430  CG  ASP A 210     -42.425  73.984 279.433  1.00 45.83           C
ATOM   1431  OD1 ASP A 210     -42.732  73.265 280.406  1.00 48.62           O
ATOM   1432  OD2 ASP A 210     -42.528  73.583 278.252  1.00 51.76           O
ATOM   1433  N   PHE A 211     -43.304  75.976 282.325  1.00 36.32           N
ATOM   1434  CA  PHE A 211     -44.313  75.682 283.338  1.00 36.57           C
ATOM   1435  C   PHE A 211     -44.796  74.238 283.259  1.00 36.41           C
ATOM   1436  O   PHE A 211     -44.987  73.584 284.285  1.00 35.65           O
ATOM   1437  CB  PHE A 211     -45.515  76.611 283.194  1.00 38.57           C
ATOM   1438  CG  PHE A 211     -46.512  76.474 284.308  1.00 45.47           C
ATOM   1439  CD1 PHE A 211     -47.870  76.637 284.069  1.00 48.06           C
ATOM   1440  CD2 PHE A 211     -46.090  76.197 285.608  1.00 46.80           C
ATOM   1441  CE1 PHE A 211     -48.795  76.527 285.107  1.00 50.54           C
ATOM   1442  CE2 PHE A 211     -47.006  76.087 286.650  1.00 46.65           C
ATOM   1443  CZ  PHE A 211     -48.361  76.252 286.398  1.00 47.68           C
ATOM   1444  N   ALA A 212     -44.999  73.741 282.043  1.00 35.01           N
ATOM   1445  CA  ALA A 212     -45.459  72.368 281.859  1.00 36.81           C
ATOM   1446  C   ALA A 212     -44.494  71.366 282.485  1.00 37.08           C
ATOM   1447  O   ALA A 212     -44.919  70.355 283.051  1.00 39.15           O
ATOM   1448  CB  ALA A 212     -45.639  72.066 280.368  1.00 38.96           C
ATOM   1449  N   ASP A 213     -43.195  71.640 282.383  1.00 38.36           N
ATOM   1450  CA  ASP A 213     -42.184  70.750 282.958  1.00 38.38           C
ATOM   1451  C   ASP A 213     -42.270  70.744 284.481  1.00 37.53           C
ATOM   1452  O   ASP A 213     -42.041  69.720 285.127  1.00 37.27           O
ATOM   1453  CB  ASP A 213     -40.778  71.186 282.536  1.00 43.54           C
ATOM   1454  CG  ASP A 213     -40.554  71.068 281.042  1.00 48.65           C
ATOM   1455  OD1 ASP A 213     -40.774  69.966 280.500  1.00 51.29           O
ATOM   1456  OD2 ASP A 213     -40.154  72.074 280.413  1.00 49.91           O
ATOM   1457  N   VAL A 214     -42.586  71.899 285.053  1.00 32.71           N
ATOM   1458  CA  VAL A 214     -42.705  72.011 286.497  1.00 35.91           C
ATOM   1459  C   VAL A 214     -43.959  71.265 286.946  1.00 35.05           C
ATOM   1460  O   VAL A 214     -43.949  70.561 287.949  1.00 32.49           O
ATOM   1461  CB  VAL A 214     -42.798  73.488 286.927  1.00 35.02           C
ATOM   1462  CG1 VAL A 214     -43.043  73.582 288.426  1.00 37.14           C
ATOM   1463  CG2 VAL A 214     -41.507  74.217 286.553  1.00 38.26           C
ATOM   1464  N   LYS A 215     -45.037  71.427 286.185  1.00 38.71           N
ATOM   1465  CA  LYS A 215     -46.296  70.769 286.479  1.00 40.62           C
ATOM   1466  C   LYS A 215     -46.069  69.257 286.465  1.00 41.74           C
ATOM   1467  O   LYS A 215     -46.610  68.524 287.293  1.00 44.03           O
ATOM   1468  CB  LYS A 215     -47.333  71.167 285.430  1.00 46.24           C
ATOM   1469  CG  LYS A 215     -48.751  70.731 285.745  1.00 54.77           C
ATOM   1470  CD  LYS A 215     -49.725  71.237 284.688  1.00 59.80           C
ATOM   1471  CE  LYS A 215     -49.653  72.753 284.545  1.00 61.96           C
ATOM   1472  NZ  LYS A 215     -50.653  73.275 283.571  1.00 65.32           N
ATOM   1473  N   THR A 216     -45.243  68.801 285.531  1.00 42.44           N
ATOM   1474  CA  THR A 216     -44.926  67.382 285.405  1.00 42.41           C
ATOM   1475  C   THR A 216     -44.233  66.782 286.637  1.00 43.03           C
ATOM   1476  O   THR A 216     -44.502  65.638 287.005  1.00 43.20           O
ATOM   1477  CB  THR A 216     -44.043  67.141 284.165  1.00 44.81           C
ATOM   1478  OG1 THR A 216     -44.806  67.412 282.984  1.00 49.67           O
ATOM   1479  CG2 THR A 216     -43.542  65.711 284.122  1.00 47.96           C
ATOM   1480  N   VAL A 217     -43.338  67.538 287.272  1.00 39.39           N
ATOM   1481  CA  VAL A 217     -42.640  67.026 288.447  1.00 39.69           C
ATOM   1482  C   VAL A 217     -43.406  67.280 289.742  1.00 38.25           C
ATOM   1483  O   VAL A 217     -43.118  66.675 290.770  1.00 41.17           O
ATOM   1484  CB  VAL A 217     -41.223  67.644 288.585  1.00 44.54           C
ATOM   1485  CG1 VAL A 217     -40.337  67.184 287.437  1.00 44.13           C
ATOM   1486  CG2 VAL A 217     -41.310  69.160 288.593  1.00 46.83           C
ATOM   1487  N   MET A 218     -44.404  68.154 289.673  1.00 41.89           N
ATOM   1488  CA  MET A 218     -45.210  68.532 290.835  1.00 43.73           C
ATOM   1489  C   MET A 218     -46.595  67.871 290.898  1.00 41.95           C
ATOM   1490  O   MET A 218     -47.051  67.471 291.967  1.00 43.96           O
ATOM   1491  CB  MET A 218     -45.399  70.055 290.830  1.00 44.43           C
ATOM   1492  CG  MET A 218     -44.781  70.820 291.983  1.00 54.55           C
ATOM   1493  SD  MET A 218     -42.996  70.670 292.180  1.00 60.85           S
ATOM   1494  CE  MET A 218     -42.929  70.317 293.929  1.00 54.80           C
ATOM   1495  N   SER A 219     -47.260  67.767 289.753  1.00 42.31           N
ATOM   1496  CA  SER A 219     -48.611  67.203 289.685  1.00 45.44           C
ATOM   1497  C   SER A 219     -48.788  65.774 290.200  1.00 48.55           C
ATOM   1498  O   SER A 219     -48.030  64.867 289.845  1.00 47.56           O
ATOM   1499  CB  SER A 219     -49.129  67.279 288.252  1.00 44.44           C
ATOM   1500  OG  SER A 219     -50.454  66.785 288.172  1.00 48.40           O
ATOM   1501  N   GLU A 220     -49.805  65.590 291.039  1.00 49.61           N
ATOM   1502  CA  GLU A 220     -50.136  64.284 291.612  1.00 51.58           C
ATOM   1503  C   GLU A 220     -48.908  63.511 292.079  1.00 50.03           C
ATOM   1504  O   GLU A 220     -48.760  62.335 291.753  1.00 51.11           O
ATOM   1505  CB  GLU A 220     -50.870  63.422 290.578  1.00 53.95           C
ATOM   1506  CG  GLU A 220     -51.642  64.182 289.511  1.00 63.84           C
ATOM   1507  CD  GLU A 220     -52.837  64.936 290.057  1.00 70.87           C
ATOM   1508  OE1 GLU A 220     -53.636  65.443 289.238  1.00 75.46           O
ATOM   1509  OE2 GLU A 220     -52.978  65.027 291.296  1.00 74.80           O
ATOM   1510  N   MET A 221     -48.034  64.148 292.848  1.00 48.17           N
ATOM   1511  CA  MET A 221     -46.834  63.460 293.298  1.00 47.05           C
ATOM   1512  C   MET A 221     -46.916  63.023 294.751  1.00 45.71           C
ATOM   1513  O   MET A 221     -46.371  61.986 295.124  1.00 48.05           O
ATOM   1514  CB  MET A 221     -45.607  64.352 293.093  1.00 51.57           C
ATOM   1515  CG  MET A 221     -44.399  63.624 292.502  1.00 58.37           C
ATOM   1516  SD  MET A 221     -44.510  63.338 290.718  1.00 62.28           S
ATOM   1517  CE  MET A 221     -45.660  61.995 290.648  1.00 65.58           C
ATOM   1518  N   GLY A 222     -47.602  63.809 295.571  1.00 43.09           N
ATOM   1519  CA  GLY A 222     -47.727  63.466 296.973  1.00 41.40           C
ATOM   1520  C   GLY A 222     -46.731  64.199 297.854  1.00 41.31           C
ATOM   1521  O   GLY A 222     -46.486  65.390 297.673  1.00 41.36           O
ATOM   1522  N   MET A 223     -46.150  63.480 298.806  1.00 37.86           N
ATOM   1523  CA  MET A 223     -45.193  64.061 299.737  1.00 42.22           C
ATOM   1524  C   MET A 223     -43.900  64.500 299.069  1.00 42.94           C
ATOM   1525  O   MET A 223     -43.444  63.886 298.101  1.00 40.07           O
ATOM   1526  CB  MET A 223     -44.866  63.065 300.852  1.00 46.52           C
ATOM   1527  CG  MET A 223     -45.437  63.441 302.207  1.00 56.59           C
ATOM   1528  SD  MET A 223     -47.199  63.781 302.135  1.00 56.70           S
ATOM   1529  CE  MET A 223     -47.849  62.104 302.046  1.00 62.42           C
ATOM   1530  N   ALA A 224     -43.311  65.568 299.602  1.00 39.09           N
ATOM   1531  CA  ALA A 224     -42.067  66.092 299.065  1.00 34.88           C
ATOM   1532  C   ALA A 224     -41.227  66.726 300.160  1.00 34.96           C
ATOM   1533  O   ALA A 224     -41.705  66.975 301.269  1.00 34.59           O
ATOM   1534  CB  ALA A 224     -42.364  67.115 297.972  1.00 34.72           C
ATOM   1535  N   MET A 225     -39.963  66.969 299.845  1.00 33.97           N
ATOM   1536  CA  MET A 225     -39.055  67.604 300.780  1.00 36.11           C
ATOM   1537  C   MET A 225     -37.974  68.314 299.979  1.00 38.56           C
ATOM   1538  O   MET A 225     -37.703  67.962 298.823  1.00 36.03           O
ATOM   1539  CB  MET A 225     -38.440  66.570 301.733  1.00 41.76           C
ATOM   1540  CG  MET A 225     -39.428  66.028 302.773  1.00 48.23           C
ATOM   1541  SD  MET A 225     -38.645  65.588 304.346  1.00 65.85           S
ATOM   1542  CE  MET A 225     -38.877  63.807 304.382  1.00 66.39           C
ATOM   1543  N   MET A 226     -37.368  69.328 300.582  1.00 33.93           N
ATOM   1544  CA  MET A 226     -36.332  70.068 299.893  1.00 36.41           C
ATOM   1545  C   MET A 226     -35.078  70.298 300.720  1.00 33.75           C
ATOM   1546  O   MET A 226     -35.071  70.138 301.938  1.00 32.64           O
ATOM   1547  CB  MET A 226     -36.865  71.416 299.427  1.00 39.37           C
ATOM   1548  CG  MET A 226     -37.217  72.372 300.546  1.00 52.96           C
ATOM   1549  SD  MET A 226     -36.869  74.074 300.032  1.00 63.74           S
ATOM   1550  CE  MET A 226     -37.642  74.095 298.435  1.00 64.46           C
ATOM   1551  N   GLY A 227     -34.017  70.673 300.019  1.00 31.77           N
ATOM   1552  CA  GLY A 227     -32.742  70.953 300.641  1.00 31.44           C
ATOM   1553  C   GLY A 227     -32.150  72.087 299.832  1.00 29.62           C
ATOM   1554  O   GLY A 227     -32.360  72.157 298.627  1.00 27.24           O
ATOM   1555  N   THR A 228     -31.440  72.994 300.487  1.00 30.10           N
ATOM   1556  CA  THR A 228     -30.834  74.117 299.785  1.00 32.45           C
ATOM   1557  C   THR A 228     -29.375  74.199 300.188  1.00 32.86           C
ATOM   1558  O   THR A 228     -28.996  73.756 301.270  1.00 34.33           O
ATOM   1559  CB  THR A 228     -31.510  75.454 300.168  1.00 33.26           C
ATOM   1560  OG1 THR A 228     -31.310  75.700 301.565  1.00 35.38           O
ATOM   1561  CG2 THR A 228     -33.013  75.408 299.887  1.00 30.63           C
ATOM   1562  N   GLY A 229     -28.564  74.777 299.313  1.00 35.83           N
ATOM   1563  CA  GLY A 229     -27.154  74.935 299.593  1.00 28.87           C
ATOM   1564  C   GLY A 229     -26.613  76.052 298.731  1.00 32.53           C
ATOM   1565  O   GLY A 229     -27.189  76.377 297.701  1.00 29.54           O
ATOM   1566  N   CYS A 230     -25.517  76.664 299.161  1.00 31.33           N
ATOM   1567  CA  CYS A 230     -24.905  77.733 298.399  1.00 33.33           C
ATOM   1568  C   CYS A 230     -23.420  77.673 298.667  1.00 31.22           C
ATOM   1569  O   CYS A 230     -22.990  77.198 299.714  1.00 35.25           O
ATOM   1570  CB  CYS A 230     -25.440  79.092 298.834  1.00 41.68           C
ATOM   1571  SG  CYS A 230     -25.045  79.485 300.540  1.00 63.75           S
ATOM   1572  N   ALA A 231     -22.637  78.150 297.715  1.00 28.52           N
ATOM   1573  CA  ALA A 231     -21.201  78.149 297.874  1.00 33.82           C
ATOM   1574  C   ALA A 231     -20.603  79.204 296.966  1.00 35.78           C
ATOM   1575  O   ALA A 231     -21.265  79.711 296.053  1.00 33.06           O
ATOM   1576  CB  ALA A 231     -20.628  76.770 297.554  1.00 26.42           C
ATOM   1577  N   SER A 232     -19.350  79.531 297.242  1.00 35.76           N
ATOM   1578  CA  SER A 232     -18.608  80.527 296.488  1.00 40.91           C
ATOM   1579  C   SER A 232     -17.246  79.917 296.151  1.00 38.48           C
ATOM   1580  O   SER A 232     -16.844  78.915 296.747  1.00 36.60           O
ATOM   1581  CB  SER A 232     -18.430  81.784 297.349  1.00 41.78           C
ATOM   1582  OG  SER A 232     -17.850  82.846 296.610  1.00 51.22           O
ATOM   1583  N   GLY A 233     -16.550  80.502 295.185  1.00 38.60           N
ATOM   1584  CA  GLY A 233     -15.242  79.987 294.824  1.00 39.13           C
ATOM   1585  C   GLY A 233     -15.202  78.986 293.684  1.00 41.33           C
ATOM   1586  O   GLY A 233     -16.230  78.679 293.083  1.00 41.33           O
ATOM   1587  N   PRO A 234     -14.007  78.449 293.376  1.00 43.20           N
ATOM   1588  CA  PRO A 234     -13.696  77.473 292.323  1.00 40.61           C
ATOM   1589  C   PRO A 234     -14.544  76.202 292.249  1.00 42.89           C
ATOM   1590  O   PRO A 234     -14.808  75.694 291.160  1.00 45.75           O
ATOM   1591  CB  PRO A 234     -12.223  77.147 292.579  1.00 41.66           C
ATOM   1592  CG  PRO A 234     -11.692  78.422 293.150  1.00 43.01           C
ATOM   1593  CD  PRO A 234     -12.782  78.813 294.119  1.00 41.62           C
ATOM   1594  N   ASN A 235     -14.954  75.669 293.391  1.00 41.83           N
ATOM   1595  CA  ASN A 235     -15.749  74.446 293.378  1.00 42.81           C
ATOM   1596  C   ASN A 235     -17.183  74.681 293.856  1.00 39.36           C
ATOM   1597  O   ASN A 235     -17.853  73.755 294.309  1.00 37.96           O
ATOM   1598  CB  ASN A 235     -15.080  73.386 294.256  1.00 46.18           C
ATOM   1599  CG  ASN A 235     -13.622  73.154 293.887  1.00 48.19           C
ATOM   1600  OD1 ASN A 235     -12.721  73.780 294.442  1.00 50.66           O
ATOM   1601  ND2 ASN A 235     -13.388  72.258 292.940  1.00 49.78           N
ATOM   1602  N   ARG A 236     -17.648  75.920 293.741  1.00 34.10           N
ATOM   1603  CA  ARG A 236     -18.989  76.282 294.197  1.00 36.38           C
ATOM   1604  C   ARG A 236     -20.137  75.433 293.651  1.00 32.25           C
ATOM   1605  O   ARG A 236     -21.083  75.144 294.377  1.00 33.29           O
ATOM   1606  CB  ARG A 236     -19.261  77.756 293.894  1.00 31.91           C
ATOM   1607  CG  ARG A 236     -19.329  78.084 292.405  1.00 28.33           C
ATOM   1608  CD  ARG A 236     -19.493  79.576 292.205  1.00 31.07           C
ATOM   1609  NE  ARG A 236     -19.671  79.925 290.802  1.00 31.65           N
ATOM   1610  CZ  ARG A 236     -20.114  81.102 290.378  1.00 34.37           C
ATOM   1611  NH1 ARG A 236     -20.424  82.053 291.251  1.00 31.18           N
ATOM   1612  NH2 ARG A 236     -20.269  81.316 289.079  1.00 36.66           N
ATOM   1613  N   ALA A 237     -20.066  75.032 292.385  1.00 35.36           N
ATOM   1614  CA  ALA A 237     -21.141  74.230 291.799  1.00 36.88           C
ATOM   1615  C   ALA A 237     -21.320  72.898 292.517  1.00 35.92           C
ATOM   1616  O   ALA A 237     -22.447  72.514 292.869  1.00 34.08           O
ATOM   1617  CB  ALA A 237     -20.889  73.998 290.310  1.00 35.16           C
ATOM   1618  N   ARG A 238     -20.218  72.192 292.744  1.00 33.62           N
ATOM   1619  CA  ARG A 238     -20.290  70.904 293.440  1.00 35.87           C
ATOM   1620  C   ARG A 238     -20.609  71.069 294.927  1.00 32.89           C
ATOM   1621  O   ARG A 238     -21.407  70.321 295.488  1.00 33.93           O
ATOM   1622  CB  ARG A 238     -18.971  70.144 293.307  1.00 37.61           C
ATOM   1623  CG  ARG A 238     -19.052  68.719 293.820  1.00 43.35           C
ATOM   1624  CD  ARG A 238     -17.777  67.940 293.529  1.00 53.49           C
ATOM   1625  NE  ARG A 238     -18.044  66.505 293.435  1.00 60.64           N
ATOM   1626  CZ  ARG A 238     -18.678  65.924 292.418  1.00 61.54           C
ATOM   1627  NH1 ARG A 238     -19.112  66.649 291.396  1.00 62.12           N
ATOM   1628  NH2 ARG A 238     -18.890  64.615 292.427  1.00 62.27           N
ATOM   1629  N   GLU A 239     -19.974  72.049 295.562  1.00 34.05           N
ATOM   1630  CA  GLU A 239     -20.184  72.303 296.982  1.00 32.57           C
ATOM   1631  C   GLU A 239     -21.620  72.731 297.302  1.00 31.51           C
ATOM   1632  O   GLU A 239     -22.181  72.309 298.306  1.00 32.56           O
ATOM   1633  CB  GLU A 239     -19.198  73.368 297.471  1.00 40.34           C
ATOM   1634  CG  GLU A 239     -17.736  73.021 297.200  1.00 45.56           C
ATOM   1635  CD  GLU A 239     -16.756  74.016 297.810  1.00 50.14           C
ATOM   1636  OE1 GLU A 239     -16.925  75.243 297.612  1.00 54.09           O
ATOM   1637  OE2 GLU A 239     -15.803  73.566 298.478  1.00 51.30           O
ATOM   1638  N   ALA A 240     -22.214  73.569 296.457  1.00 28.64           N
ATOM   1639  CA  ALA A 240     -23.586  74.012 296.698  1.00 27.98           C
ATOM   1640  C   ALA A 240     -24.544  72.846 296.501  1.00 28.29           C
ATOM   1641  O   ALA A 240     -25.476  72.656 297.284  1.00 29.97           O
ATOM   1642  CB  ALA A 240     -23.955  75.155 295.755  1.00 29.67           C
ATOM   1643  N   THR A 241     -24.316  72.061 295.453  1.00 31.57           N
ATOM   1644  CA  THR A 241     -25.184  70.915 295.181  1.00 33.62           C
ATOM   1645  C   THR A 241     -25.086  69.861 296.282  1.00 31.50           C
ATOM   1646  O   THR A 241     -26.100  69.419 296.813  1.00 31.67           O
ATOM   1647  CB  THR A 241     -24.850  70.273 293.817  1.00 28.98           C
ATOM   1648  OG1 THR A 241     -24.919  71.279 292.802  1.00 35.45           O
ATOM   1649  CG2 THR A 241     -25.849  69.177 293.476  1.00 25.45           C
ATOM   1650  N   GLU A 242     -23.869  69.456 296.630  1.00 33.87           N
ATOM   1651  CA  GLU A 242     -23.691  68.461 297.686  1.00 32.99           C
ATOM   1652  C   GLU A 242     -24.257  68.972 299.011  1.00 35.31           C
ATOM   1653  O   GLU A 242     -24.820  68.205 299.796  1.00 35.76           O
ATOM   1654  CB  GLU A 242     -22.206  68.116 297.842  1.00 37.43           C
ATOM   1655  CG  GLU A 242     -21.659  67.310 296.671  1.00 38.81           C
ATOM   1656  CD  GLU A 242     -20.167  67.026 296.772  1.00 48.25           C
ATOM   1657  OE1 GLU A 242     -19.689  66.128 296.039  1.00 52.28           O
ATOM   1658  OE2 GLU A 242     -19.473  67.700 297.569  1.00 47.36           O
ATOM   1659  N   ALA A 243     -24.116  70.272 299.253  1.00 32.17           N
ATOM   1660  CA  ALA A 243     -24.631  70.879 300.476  1.00 34.34           C
ATOM   1661  C   ALA A 243     -26.155  70.811 300.500  1.00 30.22           C
ATOM   1662  O   ALA A 243     -26.759  70.659 301.558  1.00 32.77           O
ATOM   1663  CB  ALA A 243     -24.173  72.338 300.578  1.00 32.52           C
ATOM   1664  N   ALA A 244     -26.778  70.938 299.331  1.00 29.75           N
ATOM   1665  CA  ALA A 244     -28.234  70.877 299.259  1.00 29.56           C
ATOM   1666  C   ALA A 244     -28.687  69.443 299.552  1.00 32.33           C
ATOM   1667  O   ALA A 244     -29.650  69.211 300.295  1.00 30.18           O
ATOM   1668  CB  ALA A 244     -28.708  71.313 297.875  1.00 26.72           C
ATOM   1669  N   ILE A 245     -27.972  68.488 298.967  1.00 34.92           N
ATOM   1670  CA  ILE A 245     -28.269  67.075 299.143  1.00 36.85           C
ATOM   1671  C   ILE A 245     -28.122  66.649 300.602  1.00 37.67           C
ATOM   1672  O   ILE A 245     -28.959  65.911 301.124  1.00 39.51           O
ATOM   1673  CB  ILE A 245     -27.348  66.218 298.247  1.00 36.51           C
ATOM   1674  CG1 ILE A 245     -27.651  66.529 296.782  1.00 37.23           C
ATOM   1675  CG2 ILE A 245     -27.554  64.734 298.532  1.00 39.66           C
ATOM   1676  CD1 ILE A 245     -26.769  65.805 295.798  1.00 46.50           C
ATOM   1677  N   ARG A 246     -27.078  67.121 301.275  1.00 40.00           N
ATOM   1678  CA  ARG A 246     -26.896  66.744 302.672  1.00 41.23           C
ATOM   1679  C   ARG A 246     -27.586  67.677 303.665  1.00 38.24           C
ATOM   1680  O   ARG A 246     -27.417  67.529 304.873  1.00 40.28           O
ATOM   1681  CB  ARG A 246     -25.405  66.617 303.011  1.00 41.96           C
ATOM   1682  CG  ARG A 246     -24.626  67.909 303.055  1.00 51.47           C
ATOM   1683  CD  ARG A 246     -23.134  67.599 303.088  1.00 59.13           C
ATOM   1684  NE  ARG A 246     -22.745  66.776 301.941  1.00 68.69           N
ATOM   1685  CZ  ARG A 246     -21.488  66.513 301.589  1.00 71.35           C
ATOM   1686  NH1 ARG A 246     -21.238  65.752 300.531  1.00 68.04           N
ATOM   1687  NH2 ARG A 246     -20.480  67.014 302.288  1.00 75.38           N
ATOM   1688  N   ASN A 247     -28.368  68.628 303.164  1.00 37.96           N
ATOM   1689  CA  ASN A 247     -29.094  69.544 304.040  1.00 38.55           C
ATOM   1690  C   ASN A 247     -29.948  68.666 304.951  1.00 38.04           C
ATOM   1691  O   ASN A 247     -30.579  67.718 304.487  1.00 36.12           O
ATOM   1692  CB  ASN A 247     -29.999  70.476 303.215  1.00 38.36           C
ATOM   1693  CG  ASN A 247     -30.773  71.479 304.080  1.00 39.57           C
ATOM   1694  OD1 ASN A 247     -31.541  71.098 304.963  1.00 35.80           O
ATOM   1695  ND2 ASN A 247     -30.574  72.766 303.815  1.00 35.34           N
ATOM   1696  N   PRO A 248     -29.956  68.949 306.263  1.00 37.14           N
ATOM   1697  CA  PRO A 248     -30.767  68.127 307.162  1.00 38.55           C
ATOM   1698  C   PRO A 248     -32.253  68.074 306.822  1.00 38.03           C
ATOM   1699  O   PRO A 248     -32.957  67.177 307.273  1.00 40.51           O
ATOM   1700  CB  PRO A 248     -30.480  68.715 308.552  1.00 41.30           C
ATOM   1701  CG  PRO A 248     -29.879  70.066 308.273  1.00 42.88           C
ATOM   1702  CD  PRO A 248     -29.083  69.856 307.023  1.00 37.51           C
ATOM   1703  N   LEU A 249     -32.730  69.016 306.014  1.00 38.85           N
ATOM   1704  CA  LEU A 249     -34.136  69.011 305.625  1.00 38.44           C
ATOM   1705  C   LEU A 249     -34.395  67.894 304.620  1.00 43.46           C
ATOM   1706  O   LEU A 249     -35.549  67.565 304.328  1.00 42.62           O
ATOM   1707  CB  LEU A 249     -34.529  70.362 305.027  1.00 42.01           C
ATOM   1708  CG  LEU A 249     -34.741  71.489 306.040  1.00 40.08           C
ATOM   1709  CD1 LEU A 249     -34.745  72.832 305.337  1.00 39.49           C
ATOM   1710  CD2 LEU A 249     -36.056  71.254 306.778  1.00 39.85           C
ATOM   1711  N   LEU A 250     -33.316  67.314 304.098  1.00 41.82           N
ATOM   1712  CA  LEU A 250     -33.403  66.212 303.138  1.00 48.55           C
ATOM   1713  C   LEU A 250     -32.729  64.945 303.667  1.00 51.13           C
ATOM   1714  O   LEU A 250     -32.499  64.006 302.909  1.00 52.79           O
ATOM   1715  CB  LEU A 250     -32.730  66.581 301.810  1.00 45.95           C
ATOM   1716  CG  LEU A 250     -33.494  67.204 300.638  1.00 45.74           C
ATOM   1717  CD1 LEU A 250     -32.539  67.297 299.446  1.00 40.17           C
ATOM   1718  CD2 LEU A 250     -34.707  66.355 300.260  1.00 37.61           C
ATOM   1719  N   GLU A 251     -32.408  64.915 304.958  1.00 55.76           N
ATOM   1720  CA  GLU A 251     -31.742  63.756 305.555  1.00 59.55           C
ATOM   1721  C   GLU A 251     -32.487  62.440 305.404  1.00 63.42           C
ATOM   1722  O   GLU A 251     -31.963  61.473 304.849  1.00 66.99           O
ATOM   1723  CB  GLU A 251     -31.501  63.972 307.052  1.00 62.36           C
ATOM   1724  CG  GLU A 251     -30.509  65.051 307.395  1.00 63.56           C
ATOM   1725  CD  GLU A 251     -30.250  65.140 308.888  1.00 63.97           C
ATOM   1726  OE1 GLU A 251     -31.222  65.052 309.670  1.00 63.10           O
ATOM   1727  OE2 GLU A 251     -29.075  65.309 309.279  1.00 62.79           O
ATOM   1728  N   ASP A 252     -33.713  62.408 305.911  1.00 64.80           N
ATOM   1729  CA  ASP A 252     -34.516  61.196 305.888  1.00 65.40           C
ATOM   1730  C   ASP A 252     -35.191  60.873 304.561  1.00 65.15           C
ATOM   1731  O   ASP A 252     -36.255  60.248 304.538  1.00 66.17           O
ATOM   1732  CB  ASP A 252     -35.561  61.271 307.000  1.00 67.32           C
ATOM   1733  CG  ASP A 252     -34.971  61.748 308.316  1.00 69.70           C
ATOM   1734  OD1 ASP A 252     -34.056  61.079 308.844  1.00 69.86           O
ATOM   1735  OD2 ASP A 252     -35.419  62.798 308.819  1.00 71.53           O
ATOM   1736  N   VAL A 253     -34.584  61.288 303.454  1.00 62.94           N
ATOM   1737  CA  VAL A 253     -35.165  60.986 302.152  1.00 62.28           C
ATOM   1738  C   VAL A 253     -34.207  60.228 301.252  1.00 59.13           C
ATOM   1739  O   VAL A 253     -33.016  60.535 301.180  1.00 56.94           O
ATOM   1740  CB  VAL A 253     -35.621  62.255 301.392  1.00 61.87           C
ATOM   1741  CG1 VAL A 253     -36.686  62.986 302.180  1.00 64.79           C
ATOM   1742  CG2 VAL A 253     -34.444  63.148 301.124  1.00 66.10           C
ATOM   1743  N   ASN A 254     -34.744  59.219 300.581  1.00 59.07           N
ATOM   1744  CA  ASN A 254     -33.971  58.418 299.649  1.00 57.70           C
ATOM   1745  C   ASN A 254     -34.172  59.103 298.304  1.00 54.65           C
ATOM   1746  O   ASN A 254     -35.161  58.848 297.619  1.00 54.70           O
ATOM   1747  CB  ASN A 254     -34.526  56.993 299.600  1.00 59.86           C
ATOM   1748  CG  ASN A 254     -33.788  56.105 298.614  1.00 62.63           C
ATOM   1749  OD1 ASN A 254     -34.250  55.010 298.291  1.00 63.87           O
ATOM   1750  ND2 ASN A 254     -32.634  56.566 298.136  1.00 63.56           N
ATOM   1751  N   LEU A 255     -33.252  59.991 297.943  1.00 53.03           N
ATOM   1752  CA  LEU A 255     -33.357  60.713 296.681  1.00 52.10           C
ATOM   1753  C   LEU A 255     -33.610  59.772 295.517  1.00 50.05           C
ATOM   1754  O   LEU A 255     -34.362  60.096 294.599  1.00 48.37           O
ATOM   1755  CB  LEU A 255     -32.088  61.525 296.413  1.00 50.11           C
ATOM   1756  CG  LEU A 255     -32.064  62.957 296.950  1.00 54.06           C
ATOM   1757  CD1 LEU A 255     -32.487  62.974 298.408  1.00 52.92           C
ATOM   1758  CD2 LEU A 255     -30.663  63.532 296.787  1.00 51.29           C
ATOM   1759  N   GLN A 256     -32.984  58.602 295.558  1.00 49.30           N
ATOM   1760  CA  GLN A 256     -33.160  57.638 294.488  1.00 51.74           C
ATOM   1761  C   GLN A 256     -34.569  57.053 294.493  1.00 48.68           C
ATOM   1762  O   GLN A 256     -34.990  56.437 293.520  1.00 51.33           O
ATOM   1763  CB  GLN A 256     -32.119  56.522 294.603  1.00 58.32           C
ATOM   1764  CG  GLN A 256     -32.080  55.603 293.387  1.00 67.22           C
ATOM   1765  CD  GLN A 256     -30.714  54.986 293.162  1.00 72.67           C
ATOM   1766  OE1 GLN A 256     -30.192  54.263 294.017  1.00 75.20           O
ATOM   1767  NE2 GLN A 256     -30.121  55.273 292.006  1.00 73.11           N
ATOM   1768  N   GLY A 257     -35.301  57.265 295.581  1.00 45.30           N
ATOM   1769  CA  GLY A 257     -36.651  56.744 295.673  1.00 43.74           C
ATOM   1770  C   GLY A 257     -37.729  57.767 295.360  1.00 45.95           C
ATOM   1771  O   GLY A 257     -38.913  57.504 295.553  1.00 45.04           O
ATOM   1772  N   ALA A 258     -37.325  58.936 294.871  1.00 46.57           N
ATOM   1773  CA  ALA A 258     -38.275  59.994 294.547  1.00 45.72           C
ATOM   1774  C   ALA A 258     -38.654  59.972 293.069  1.00 43.56           C
ATOM   1775  O   ALA A 258     -37.793  59.794 292.207  1.00 42.18           O
ATOM   1776  CB  ALA A 258     -37.681  61.349 294.913  1.00 44.51           C
ATOM   1777  N   ARG A 259     -39.942  60.161 292.791  1.00 41.46           N
ATOM   1778  CA  ARG A 259     -40.459  60.163 291.422  1.00 46.83           C
ATOM   1779  C   ARG A 259     -40.143  61.449 290.676  1.00 46.07           C
ATOM   1780  O   ARG A 259     -40.005  61.451 289.451  1.00 46.68           O
ATOM   1781  CB  ARG A 259     -41.977  59.966 291.421  1.00 49.37           C
ATOM   1782  CG  ARG A 259     -42.452  58.613 291.909  1.00 57.79           C
ATOM   1783  CD  ARG A 259     -43.961  58.512 291.747  1.00 68.67           C
ATOM   1784  NE  ARG A 259     -44.381  58.817 290.381  1.00 75.50           N
ATOM   1785  CZ  ARG A 259     -45.644  58.997 290.005  1.00 80.76           C
ATOM   1786  NH1 ARG A 259     -46.625  58.904 290.894  1.00 83.70           N
ATOM   1787  NH2 ARG A 259     -45.927  59.280 288.740  1.00 82.87           N
ATOM   1788  N   GLY A 260     -40.051  62.547 291.418  1.00 45.23           N
ATOM   1789  CA  GLY A 260     -39.753  63.827 290.805  1.00 39.93           C
ATOM   1790  C   GLY A 260     -38.598  64.532 291.490  1.00 39.84           C
ATOM   1791  O   GLY A 260     -38.376  64.377 292.699  1.00 35.95           O
ATOM   1792  N   ILE A 261     -37.853  65.303 290.710  1.00 39.17           N
ATOM   1793  CA  ILE A 261     -36.726  66.056 291.231  1.00 39.19           C
ATOM   1794  C   ILE A 261     -36.676  67.388 290.496  1.00 39.36           C
ATOM   1795  O   ILE A 261     -36.407  67.432 289.296  1.00 40.39           O
ATOM   1796  CB  ILE A 261     -35.378  65.333 290.999  1.00 43.36           C
ATOM   1797  CG1 ILE A 261     -35.384  63.947 291.657  1.00 44.18           C
ATOM   1798  CG2 ILE A 261     -34.235  66.188 291.555  1.00 39.39           C
ATOM   1799  CD1 ILE A 261     -35.286  63.961 293.168  1.00 43.57           C
ATOM   1800  N   LEU A 262     -36.962  68.469 291.213  1.00 37.10           N
ATOM   1801  CA  LEU A 262     -36.916  69.806 290.627  1.00 34.85           C
ATOM   1802  C   LEU A 262     -35.701  70.496 291.239  1.00 31.51           C
ATOM   1803  O   LEU A 262     -35.570  70.568 292.465  1.00 30.25           O
ATOM   1804  CB  LEU A 262     -38.192  70.585 290.960  1.00 33.25           C
ATOM   1805  CG  LEU A 262     -38.256  72.036 290.488  1.00 34.31           C
ATOM   1806  CD1 LEU A 262     -38.075  72.098 288.982  1.00 37.29           C
ATOM   1807  CD2 LEU A 262     -39.601  72.644 290.888  1.00 36.46           C
ATOM   1808  N   VAL A 263     -34.803  70.987 290.394  1.00 28.20           N
ATOM   1809  CA  VAL A 263     -33.603  71.648 290.887  1.00 29.12           C
ATOM   1810  C   VAL A 263     -33.570  73.092 290.438  1.00 30.64           C
ATOM   1811  O   VAL A 263     -33.794  73.387 289.265  1.00 33.51           O
ATOM   1812  CB  VAL A 263     -32.320  70.962 290.365  1.00 28.06           C
ATOM   1813  CG1 VAL A 263     -31.096  71.632 290.955  1.00 26.60           C
ATOM   1814  CG2 VAL A 263     -32.321  69.497 290.734  1.00 29.02           C
ATOM   1815  N   ASN A 264     -33.298  73.993 291.375  1.00 28.52           N
ATOM   1816  CA  ASN A 264     -33.205  75.408 291.046  1.00 26.82           C
ATOM   1817  C   ASN A 264     -31.761  75.878 291.210  1.00 28.30           C
ATOM   1818  O   ASN A 264     -31.203  75.804 292.306  1.00 30.55           O
ATOM   1819  CB  ASN A 264     -34.097  76.241 291.964  1.00 26.81           C
ATOM   1820  CG  ASN A 264     -33.912  77.740 291.754  1.00 28.50           C
ATOM   1821  OD1 ASN A 264     -32.791  78.253 291.772  1.00 31.15           O
ATOM   1822  ND2 ASN A 264     -35.011  78.446 291.564  1.00 33.64           N
ATOM   1823  N   ILE A 265     -31.145  76.330 290.122  1.00 24.83           N
ATOM   1824  CA  ILE A 265     -29.786  76.845 290.211  1.00 29.46           C
ATOM   1825  C   ILE A 265     -29.899  78.358 290.107  1.00 30.42           C
ATOM   1826  O   ILE A 265     -30.378  78.879 289.100  1.00 30.29           O
ATOM   1827  CB  ILE A 265     -28.875  76.389 289.050  1.00 32.01           C
ATOM   1828  CG1 ILE A 265     -28.652  74.880 289.091  1.00 26.71           C
ATOM   1829  CG2 ILE A 265     -27.516  77.102 289.155  1.00 28.86           C
ATOM   1830  CD1 ILE A 265     -27.854  74.378 287.912  1.00 31.11           C
ATOM   1831  N   THR A 266     -29.488  79.066 291.149  1.00 28.02           N
ATOM   1832  CA  THR A 266     -29.543  80.520 291.097  1.00 29.39           C
ATOM   1833  C   THR A 266     -28.123  81.063 291.186  1.00 27.14           C
ATOM   1834  O   THR A 266     -27.377  80.714 292.088  1.00 28.57           O
ATOM   1835  CB  THR A 266     -30.415  81.087 292.232  1.00 29.29           C
ATOM   1836  OG1 THR A 266     -31.782  80.720 291.996  1.00 30.65           O
ATOM   1837  CG2 THR A 266     -30.302  82.616 292.288  1.00 30.38           C
ATOM   1838  N   ALA A 267     -27.750  81.906 290.232  1.00 29.25           N
ATOM   1839  CA  ALA A 267     -26.407  82.474 290.205  1.00 31.13           C
ATOM   1840  C   ALA A 267     -26.399  83.761 289.403  1.00 30.26           C
ATOM   1841  O   ALA A 267     -27.389  84.108 288.760  1.00 28.34           O
ATOM   1842  CB  ALA A 267     -25.429  81.472 289.578  1.00 30.74           C
ATOM   1843  N   GLY A 268     -25.272  84.467 289.453  1.00 33.02           N
ATOM   1844  CA  GLY A 268     -25.130  85.696 288.696  1.00 30.08           C
ATOM   1845  C   GLY A 268     -24.600  85.361 287.311  1.00 32.62           C
ATOM   1846  O   GLY A 268     -24.391  84.189 287.001  1.00 31.99           O
ATOM   1847  N   PRO A 269     -24.370  86.363 286.450  1.00 34.67           N
ATOM   1848  CA  PRO A 269     -23.863  86.169 285.085  1.00 34.21           C
ATOM   1849  C   PRO A 269     -22.507  85.466 285.001  1.00 35.82           C
ATOM   1850  O   PRO A 269     -22.020  85.192 283.907  1.00 38.85           O
ATOM   1851  CB  PRO A 269     -23.782  87.592 284.538  1.00 35.34           C
ATOM   1852  CG  PRO A 269     -24.818  88.328 285.325  1.00 37.32           C
ATOM   1853  CD  PRO A 269     -24.626  87.789 286.711  1.00 33.79           C
ATOM   1854  N   ASP A 270     -21.880  85.196 286.141  1.00 35.83           N
ATOM   1855  CA  ASP A 270     -20.591  84.516 286.111  1.00 37.67           C
ATOM   1856  C   ASP A 270     -20.774  83.002 286.112  1.00 35.45           C
ATOM   1857  O   ASP A 270     -19.801  82.255 286.191  1.00 34.10           O
ATOM   1858  CB  ASP A 270     -19.697  84.942 287.286  1.00 37.74           C
ATOM   1859  CG  ASP A 270     -20.372  84.776 288.631  1.00 40.24           C
ATOM   1860  OD1 ASP A 270     -21.321  83.971 288.737  1.00 43.75           O
ATOM   1861  OD2 ASP A 270     -19.939  85.447 289.589  1.00 40.64           O
ATOM   1862  N   LEU A 271     -22.022  82.550 286.031  1.00 34.03           N
ATOM   1863  CA  LEU A 271     -22.293  81.115 285.976  1.00 33.82           C
ATOM   1864  C   LEU A 271     -21.686  80.594 284.675  1.00 36.71           C
ATOM   1865  O   LEU A 271     -21.991  81.107 283.591  1.00 35.51           O
ATOM   1866  CB  LEU A 271     -23.802  80.833 285.961  1.00 29.17           C
ATOM   1867  CG  LEU A 271     -24.185  79.351 285.799  1.00 30.00           C
ATOM   1868  CD1 LEU A 271     -23.834  78.577 287.070  1.00 24.66           C
ATOM   1869  CD2 LEU A 271     -25.678  79.235 285.528  1.00 26.53           C
ATOM   1870  N   SER A 272     -20.823  79.589 284.772  1.00 34.51           N
ATOM   1871  CA  SER A 272     -20.210  79.028 283.572  1.00 36.41           C
ATOM   1872  C   SER A 272     -20.974  77.780 283.139  1.00 34.19           C
ATOM   1873  O   SER A 272     -21.672  77.158 283.944  1.00 30.30           O
ATOM   1874  CB  SER A 272     -18.743  78.669 283.827  1.00 32.69           C
ATOM   1875  OG  SER A 272     -18.652  77.490 284.603  1.00 42.01           O
ATOM   1876  N   LEU A 273     -20.835  77.425 281.865  1.00 34.56           N
ATOM   1877  CA  LEU A 273     -21.502  76.259 281.296  1.00 34.68           C
ATOM   1878  C   LEU A 273     -21.073  75.005 282.050  1.00 34.07           C
ATOM   1879  O   LEU A 273     -21.888  74.127 282.327  1.00 35.04           O
ATOM   1880  CB  LEU A 273     -21.146  76.144 279.805  1.00 36.90           C
ATOM   1881  CG  LEU A 273     -21.763  75.060 278.913  1.00 37.50           C
ATOM   1882  CD1 LEU A 273     -21.207  73.702 279.287  1.00 45.88           C
ATOM   1883  CD2 LEU A 273     -23.283  75.083 279.039  1.00 30.56           C
ATOM   1884  N   GLY A 274     -19.788  74.935 282.386  1.00 37.06           N
ATOM   1885  CA  GLY A 274     -19.272  73.789 283.112  1.00 35.98           C
ATOM   1886  C   GLY A 274     -19.919  73.641 284.478  1.00 36.04           C
ATOM   1887  O   GLY A 274     -20.205  72.529 284.912  1.00 35.51           O
ATOM   1888  N   GLU A 275     -20.152  74.752 285.170  1.00 36.56           N
ATOM   1889  CA  GLU A 275     -20.779  74.677 286.490  1.00 37.62           C
ATOM   1890  C   GLU A 275     -22.187  74.116 286.352  1.00 37.63           C
ATOM   1891  O   GLU A 275     -22.638  73.324 287.181  1.00 37.86           O
ATOM   1892  CB  GLU A 275     -20.825  76.057 287.150  1.00 34.76           C
ATOM   1893  CG  GLU A 275     -19.456  76.610 287.463  1.00 40.50           C
ATOM   1894  CD  GLU A 275     -19.503  77.945 288.166  1.00 44.63           C
ATOM   1895  OE1 GLU A 275     -20.127  78.882 287.630  1.00 47.03           O
ATOM   1896  OE2 GLU A 275     -18.906  78.061 289.256  1.00 51.09           O
ATOM   1897  N   TYR A 276     -22.874  74.523 285.292  1.00 36.79           N
ATOM   1898  CA  TYR A 276     -24.230  74.054 285.047  1.00 37.39           C
ATOM   1899  C   TYR A 276     -24.234  72.547 284.830  1.00 38.68           C
ATOM   1900  O   TYR A 276     -25.065  71.834 285.393  1.00 36.16           O
ATOM   1901  CB  TYR A 276     -24.832  74.750 283.822  1.00 33.27           C
ATOM   1902  CG  TYR A 276     -26.187  74.206 283.441  1.00 39.47           C
ATOM   1903  CD1 TYR A 276     -26.324  73.250 282.429  1.00 42.05           C
ATOM   1904  CD2 TYR A 276     -27.326  74.597 284.134  1.00 37.60           C
ATOM   1905  CE1 TYR A 276     -27.569  72.698 282.125  1.00 44.59           C
ATOM   1906  CE2 TYR A 276     -28.568  74.053 283.843  1.00 46.52           C
ATOM   1907  CZ  TYR A 276     -28.686  73.106 282.844  1.00 46.59           C
ATOM   1908  OH  TYR A 276     -29.921  72.559 282.594  1.00 52.02           O
ATOM   1909  N   SER A 277     -23.301  72.059 284.017  1.00 38.47           N
ATOM   1910  CA  SER A 277     -23.237  70.628 283.755  1.00 40.04           C
ATOM   1911  C   SER A 277     -22.797  69.865 285.003  1.00 36.58           C
ATOM   1912  O   SER A 277     -23.187  68.720 285.190  1.00 40.68           O
ATOM   1913  CB  SER A 277     -22.296  70.327 282.576  1.00 41.24           C
ATOM   1914  OG  SER A 277     -20.943  70.562 282.917  1.00 51.74           O
ATOM   1915  N   ASP A 278     -21.993  70.493 285.859  1.00 36.22           N
ATOM   1916  CA  ASP A 278     -21.551  69.841 287.092  1.00 38.45           C
ATOM   1917  C   ASP A 278     -22.726  69.535 288.019  1.00 37.04           C
ATOM   1918  O   ASP A 278     -22.802  68.451 288.595  1.00 38.08           O
ATOM   1919  CB  ASP A 278     -20.548  70.708 287.856  1.00 39.08           C
ATOM   1920  CG  ASP A 278     -19.136  70.600 287.307  1.00 45.02           C
ATOM   1921  OD1 ASP A 278     -18.819  69.592 286.637  1.00 49.14           O
ATOM   1922  OD2 ASP A 278     -18.334  71.521 287.567  1.00 46.95           O
ATOM   1923  N   VAL A 279     -23.635  70.495 288.169  1.00 35.41           N
ATOM   1924  CA  VAL A 279     -24.796  70.299 289.027  1.00 35.16           C
ATOM   1925  C   VAL A 279     -25.672  69.208 288.427  1.00 36.56           C
ATOM   1926  O   VAL A 279     -26.141  68.321 289.136  1.00 37.94           O
ATOM   1927  CB  VAL A 279     -25.623  71.604 289.179  1.00 34.02           C
ATOM   1928  CG1 VAL A 279     -26.861  71.352 290.055  1.00 30.28           C
ATOM   1929  CG2 VAL A 279     -24.760  72.684 289.808  1.00 28.64           C
ATOM   1930  N   GLY A 280     -25.877  69.270 287.116  1.00 37.97           N
ATOM   1931  CA  GLY A 280     -26.693  68.265 286.457  1.00 38.55           C
ATOM   1932  C   GLY A 280     -26.135  66.868 286.647  1.00 39.14           C
ATOM   1933  O   GLY A 280     -26.871  65.930 286.948  1.00 39.21           O
ATOM   1934  N   ASN A 281     -24.826  66.723 286.479  1.00 38.48           N
ATOM   1935  CA  ASN A 281     -24.195  65.422 286.642  1.00 42.90           C
ATOM   1936  C   ASN A 281     -24.366  64.882 288.063  1.00 40.92           C
ATOM   1937  O   ASN A 281     -24.704  63.714 288.256  1.00 41.49           O
ATOM   1938  CB  ASN A 281     -22.711  65.516 286.266  1.00 43.03           C
ATOM   1939  CG  ASN A 281     -22.512  65.810 284.785  1.00 44.09           C
ATOM   1940  OD1 ASN A 281     -21.433  66.212 284.354  1.00 46.94           O
ATOM   1941  ND2 ASN A 281     -23.562  65.604 283.999  1.00 47.24           N
ATOM   1942  N   ILE A 282     -24.152  65.736 289.057  1.00 40.35           N
ATOM   1943  CA  ILE A 282     -24.288  65.324 290.447  1.00 39.22           C
ATOM   1944  C   ILE A 282     -25.707  64.862 290.755  1.00 39.66           C
ATOM   1945  O   ILE A 282     -25.908  63.894 291.485  1.00 40.08           O
ATOM   1946  CB  ILE A 282     -23.915  66.480 291.396  1.00 40.11           C
ATOM   1947  CG1 ILE A 282     -22.405  66.716 291.341  1.00 40.32           C
ATOM   1948  CG2 ILE A 282     -24.386  66.178 292.803  1.00 36.06           C
ATOM   1949  CD1 ILE A 282     -21.953  67.987 292.042  1.00 38.96           C
ATOM   1950  N   ILE A 283     -26.691  65.559 290.198  1.00 40.26           N
ATOM   1951  CA  ILE A 283     -28.090  65.209 290.426  1.00 42.83           C
ATOM   1952  C   ILE A 283     -28.429  63.865 289.788  1.00 45.67           C
ATOM   1953  O   ILE A 283     -29.071  63.026 290.415  1.00 44.25           O
ATOM   1954  CB  ILE A 283     -29.039  66.289 289.851  1.00 39.82           C
ATOM   1955  CG1 ILE A 283     -28.853  67.607 290.606  1.00 39.60           C
ATOM   1956  CG2 ILE A 283     -30.486  65.825 289.955  1.00 44.27           C
ATOM   1957  CD1 ILE A 283     -29.251  67.549 292.086  1.00 41.56           C
ATOM   1958  N   GLU A 284     -27.996  63.669 288.544  1.00 48.72           N
ATOM   1959  CA  GLU A 284     -28.261  62.426 287.822  1.00 53.74           C
ATOM   1960  C   GLU A 284     -27.693  61.216 288.556  1.00 53.20           C
ATOM   1961  O   GLU A 284     -28.212  60.108 288.440  1.00 54.16           O
ATOM   1962  CB  GLU A 284     -27.663  62.485 286.414  1.00 57.17           C
ATOM   1963  CG  GLU A 284     -28.238  63.573 285.524  1.00 68.23           C
ATOM   1964  CD  GLU A 284     -27.682  63.516 284.107  1.00 75.96           C
ATOM   1965  OE1 GLU A 284     -27.881  62.482 283.433  1.00 79.63           O
ATOM   1966  OE2 GLU A 284     -27.046  64.501 283.668  1.00 76.62           O
ATOM   1967  N   GLN A 285     -26.624  61.432 289.312  1.00 53.83           N
ATOM   1968  CA  GLN A 285     -25.999  60.352 290.058  1.00 55.83           C
ATOM   1969  C   GLN A 285     -26.833  59.925 291.267  1.00 56.96           C
ATOM   1970  O   GLN A 285     -26.712  58.796 291.742  1.00 58.35           O
ATOM   1971  CB  GLN A 285     -24.605  60.776 290.517  1.00 57.77           C
ATOM   1972  CG  GLN A 285     -23.891  59.741 291.359  1.00 63.70           C
ATOM   1973  CD  GLN A 285     -22.542  60.226 291.850  1.00 69.26           C
ATOM   1974  OE1 GLN A 285     -21.869  59.543 292.626  1.00 70.36           O
ATOM   1975  NE2 GLN A 285     -22.137  61.411 291.400  1.00 69.43           N
ATOM   1976  N   PHE A 286     -27.678  60.822 291.765  1.00 55.00           N
ATOM   1977  CA  PHE A 286     -28.514  60.501 292.916  1.00 54.23           C
ATOM   1978  C   PHE A 286     -29.955  60.198 292.526  1.00 52.00           C
ATOM   1979  O   PHE A 286     -30.663  59.505 293.248  1.00 53.32           O
ATOM   1980  CB  PHE A 286     -28.494  61.648 293.938  1.00 55.39           C
ATOM   1981  CG  PHE A 286     -27.219  61.734 294.733  1.00 60.47           C
ATOM   1982  CD1 PHE A 286     -26.014  62.071 294.116  1.00 61.02           C
ATOM   1983  CD2 PHE A 286     -27.218  61.453 296.098  1.00 60.61           C
ATOM   1984  CE1 PHE A 286     -24.825  62.124 294.846  1.00 61.38           C
ATOM   1985  CE2 PHE A 286     -26.033  61.504 296.839  1.00 60.85           C
ATOM   1986  CZ  PHE A 286     -24.835  61.840 296.210  1.00 59.74           C
ATOM   1987  N   ALA A 287     -30.391  60.708 291.382  1.00 49.90           N
ATOM   1988  CA  ALA A 287     -31.761  60.480 290.955  1.00 52.27           C
ATOM   1989  C   ALA A 287     -31.935  59.090 290.359  1.00 53.83           C
ATOM   1990  O   ALA A 287     -31.004  58.528 289.784  1.00 55.50           O
ATOM   1991  CB  ALA A 287     -32.175  61.541 289.944  1.00 50.65           C
ATOM   1992  N   SER A 288     -33.130  58.530 290.512  1.00 52.80           N
ATOM   1993  CA  SER A 288     -33.405  57.215 289.958  1.00 53.35           C
ATOM   1994  C   SER A 288     -33.649  57.404 288.466  1.00 54.55           C
ATOM   1995  O   SER A 288     -34.088  58.474 288.032  1.00 53.55           O
ATOM   1996  CB  SER A 288     -34.643  56.605 290.614  1.00 53.21           C
ATOM   1997  OG  SER A 288     -35.704  56.496 289.686  1.00 49.41           O
ATOM   1998  N   GLU A 289     -33.368  56.371 287.679  1.00 55.54           N
ATOM   1999  CA  GLU A 289     -33.560  56.461 286.243  1.00 56.24           C
ATOM   2000  C   GLU A 289     -35.037  56.558 285.878  1.00 54.55           C
ATOM   2001  O   GLU A 289     -35.379  56.980 284.777  1.00 56.14           O
ATOM   2002  CB  GLU A 289     -32.914  55.261 285.544  1.00 60.54           C
ATOM   2003  CG  GLU A 289     -33.607  53.928 285.771  1.00 65.14           C
ATOM   2004  CD  GLU A 289     -32.862  52.779 285.108  1.00 70.56           C
ATOM   2005  OE1 GLU A 289     -31.791  52.386 285.622  1.00 72.34           O
ATOM   2006  OE2 GLU A 289     -33.339  52.279 284.067  1.00 71.87           O
ATOM   2007  N   HIS A 290     -35.912  56.176 286.804  1.00 54.78           N
ATOM   2008  CA  HIS A 290     -37.351  56.243 286.558  1.00 56.15           C
ATOM   2009  C   HIS A 290     -37.958  57.546 287.061  1.00 57.30           C
ATOM   2010  O   HIS A 290     -39.182  57.685 287.126  1.00 56.74           O
ATOM   2011  CB  HIS A 290     -38.080  55.079 287.237  1.00 57.21           C
ATOM   2012  CG  HIS A 290     -37.958  53.779 286.507  1.00 61.97           C
ATOM   2013  ND1 HIS A 290     -36.854  52.961 286.618  1.00 65.15           N
ATOM   2014  CD2 HIS A 290     -38.795  53.166 285.637  1.00 61.50           C
ATOM   2015  CE1 HIS A 290     -37.017  51.899 285.849  1.00 65.50           C
ATOM   2016  NE2 HIS A 290     -38.187  52.000 285.243  1.00 65.75           N
ATOM   2017  N   ALA A 291     -37.106  58.504 287.408  1.00 54.56           N
ATOM   2018  CA  ALA A 291     -37.588  59.771 287.930  1.00 51.44           C
ATOM   2019  C   ALA A 291     -37.613  60.903 286.917  1.00 49.58           C
ATOM   2020  O   ALA A 291     -36.807  60.947 285.988  1.00 50.93           O
ATOM   2021  CB  ALA A 291     -36.747  60.178 289.138  1.00 51.51           C
ATOM   2022  N   THR A 292     -38.562  61.814 287.096  1.00 46.30           N
ATOM   2023  CA  THR A 292     -38.660  62.972 286.230  1.00 46.47           C
ATOM   2024  C   THR A 292     -37.735  64.004 286.874  1.00 45.70           C
ATOM   2025  O   THR A 292     -37.944  64.408 288.018  1.00 45.47           O
ATOM   2026  CB  THR A 292     -40.085  63.524 286.193  1.00 49.38           C
ATOM   2027  OG1 THR A 292     -40.996  62.465 285.879  1.00 51.47           O
ATOM   2028  CG2 THR A 292     -40.199  64.611 285.132  1.00 51.36           C
ATOM   2029  N   VAL A 293     -36.705  64.406 286.141  1.00 44.75           N
ATOM   2030  CA  VAL A 293     -35.725  65.359 286.638  1.00 41.48           C
ATOM   2031  C   VAL A 293     -35.746  66.627 285.799  1.00 40.94           C
ATOM   2032  O   VAL A 293     -35.627  66.572 284.583  1.00 43.45           O
ATOM   2033  CB  VAL A 293     -34.311  64.738 286.600  1.00 40.78           C
ATOM   2034  CG1 VAL A 293     -33.267  65.755 287.035  1.00 41.85           C
ATOM   2035  CG2 VAL A 293     -34.266  63.518 287.503  1.00 41.50           C
ATOM   2036  N   LYS A 294     -35.908  67.767 286.459  1.00 38.06           N
ATOM   2037  CA  LYS A 294     -35.945  69.061 285.785  1.00 34.54           C
ATOM   2038  C   LYS A 294     -34.997  70.010 286.517  1.00 36.16           C
ATOM   2039  O   LYS A 294     -35.137  70.238 287.720  1.00 33.90           O
ATOM   2040  CB  LYS A 294     -37.373  69.621 285.811  1.00 39.53           C
ATOM   2041  CG  LYS A 294     -38.133  69.542 284.487  1.00 43.43           C
ATOM   2042  CD  LYS A 294     -38.103  68.157 283.875  1.00 45.79           C
ATOM   2043  CE  LYS A 294     -38.801  68.146 282.520  1.00 50.27           C
ATOM   2044  NZ  LYS A 294     -38.318  67.035 281.639  1.00 49.13           N
ATOM   2045  N   VAL A 295     -34.026  70.550 285.793  1.00 34.78           N
ATOM   2046  CA  VAL A 295     -33.060  71.464 286.382  1.00 37.65           C
ATOM   2047  C   VAL A 295     -33.226  72.838 285.751  1.00 39.84           C
ATOM   2048  O   VAL A 295     -32.761  73.082 284.636  1.00 41.05           O
ATOM   2049  CB  VAL A 295     -31.608  70.972 286.156  1.00 36.97           C
ATOM   2050  CG1 VAL A 295     -30.617  71.948 286.788  1.00 34.79           C
ATOM   2051  CG2 VAL A 295     -31.427  69.579 286.760  1.00 35.80           C
ATOM   2052  N   GLY A 296     -33.906  73.725 286.469  1.00 40.71           N
ATOM   2053  CA  GLY A 296     -34.130  75.067 285.970  1.00 39.35           C
ATOM   2054  C   GLY A 296     -33.052  75.997 286.475  1.00 38.77           C
ATOM   2055  O   GLY A 296     -32.543  75.812 287.577  1.00 41.75           O
ATOM   2056  N   THR A 297     -32.711  77.000 285.673  1.00 35.12           N
ATOM   2057  CA  THR A 297     -31.682  77.959 286.037  1.00 33.00           C
ATOM   2058  C   THR A 297     -32.234  79.373 286.095  1.00 30.94           C
ATOM   2059  O   THR A 297     -33.011  79.784 285.240  1.00 33.92           O
ATOM   2060  CB  THR A 297     -30.506  77.922 285.029  1.00 34.58           C
ATOM   2061  OG1 THR A 297     -29.858  76.647 285.109  1.00 37.30           O
ATOM   2062  CG2 THR A 297     -29.483  79.016 285.340  1.00 33.74           C
ATOM   2063  N   VAL A 298     -31.828  80.111 287.120  1.00 30.02           N
ATOM   2064  CA  VAL A 298     -32.261  81.489 287.297  1.00 30.88           C
ATOM   2065  C   VAL A 298     -31.023  82.362 287.423  1.00 31.99           C
ATOM   2066  O   VAL A 298     -30.184  82.123 288.284  1.00 31.64           O
ATOM   2067  CB  VAL A 298     -33.119  81.648 288.574  1.00 30.04           C
ATOM   2068  CG1 VAL A 298     -33.467  83.117 288.797  1.00 26.87           C
ATOM   2069  CG2 VAL A 298     -34.397  80.824 288.449  1.00 28.99           C
ATOM   2070  N   ILE A 299     -30.902  83.363 286.557  1.00 30.61           N
ATOM   2071  CA  ILE A 299     -29.756  84.254 286.609  1.00 33.54           C
ATOM   2072  C   ILE A 299     -30.120  85.572 287.280  1.00 37.09           C
ATOM   2073  O   ILE A 299     -30.981  86.312 286.798  1.00 38.85           O
ATOM   2074  CB  ILE A 299     -29.199  84.569 285.195  1.00 32.30           C
ATOM   2075  CG1 ILE A 299     -28.738  83.281 284.508  1.00 33.05           C
ATOM   2076  CG2 ILE A 299     -28.008  85.521 285.303  1.00 32.90           C
ATOM   2077  CD1 ILE A 299     -27.578  82.595 285.211  1.00 38.17           C
ATOM   2078  N   ASP A 300     -29.481  85.857 288.407  1.00 37.61           N
ATOM   2079  CA  ASP A 300     -29.724  87.112 289.102  1.00 41.85           C
ATOM   2080  C   ASP A 300     -28.656  88.053 288.554  1.00 41.90           C
ATOM   2081  O   ASP A 300     -27.488  87.962 288.921  1.00 41.69           O
ATOM   2082  CB  ASP A 300     -29.580  86.920 290.611  1.00 48.12           C
ATOM   2083  CG  ASP A 300     -29.856  88.194 291.394  1.00 55.85           C
ATOM   2084  OD1 ASP A 300     -30.163  88.090 292.602  1.00 58.65           O
ATOM   2085  OD2 ASP A 300     -29.753  89.295 290.811  1.00 58.02           O
ATOM   2086  N   ALA A 301     -29.069  88.935 287.648  1.00 44.55           N
ATOM   2087  CA  ALA A 301     -28.167  89.876 286.992  1.00 50.65           C
ATOM   2088  C   ALA A 301     -27.186  90.614 287.897  1.00 51.15           C
ATOM   2089  O   ALA A 301     -26.112  91.002 287.450  1.00 51.98           O
ATOM   2090  CB  ALA A 301     -28.977  90.884 286.179  1.00 51.19           C
ATOM   2091  N   ASP A 302     -27.545  90.804 289.162  1.00 53.94           N
ATOM   2092  CA  ASP A 302     -26.669  91.513 290.088  1.00 53.85           C
ATOM   2093  C   ASP A 302     -25.935  90.606 291.071  1.00 53.64           C
ATOM   2094  O   ASP A 302     -25.255  91.084 291.983  1.00 55.39           O
ATOM   2095  CB  ASP A 302     -27.471  92.562 290.863  1.00 55.23           C
ATOM   2096  CG  ASP A 302     -28.160  93.558 289.949  1.00 61.43           C
ATOM   2097  OD1 ASP A 302     -29.303  93.286 289.524  1.00 65.21           O
ATOM   2098  OD2 ASP A 302     -27.551  94.606 289.643  1.00 62.09           O
ATOM   2099  N   MET A 303     -26.062  89.300 290.886  1.00 49.70           N
ATOM   2100  CA  MET A 303     -25.406  88.351 291.774  1.00 44.76           C
ATOM   2101  C   MET A 303     -24.006  87.999 291.265  1.00 43.20           C
ATOM   2102  O   MET A 303     -23.776  87.932 290.056  1.00 41.35           O
ATOM   2103  CB  MET A 303     -26.265  87.092 291.885  1.00 42.94           C
ATOM   2104  CG  MET A 303     -25.787  86.086 292.906  1.00 41.60           C
ATOM   2105  SD  MET A 303     -26.956  84.715 293.036  1.00 39.67           S
ATOM   2106  CE  MET A 303     -28.190  85.420 294.095  1.00 36.37           C
ATOM   2107  N   ARG A 304     -23.074  87.781 292.191  1.00 43.04           N
ATOM   2108  CA  ARG A 304     -21.700  87.434 291.828  1.00 44.91           C
ATOM   2109  C   ARG A 304     -21.074  86.491 292.842  1.00 43.09           C
ATOM   2110  O   ARG A 304     -21.405  86.530 294.023  1.00 43.55           O
ATOM   2111  CB  ARG A 304     -20.824  88.688 291.751  1.00 47.64           C
ATOM   2112  CG  ARG A 304     -21.353  89.790 290.865  1.00 51.68           C
ATOM   2113  CD  ARG A 304     -21.098  89.527 289.393  1.00 56.55           C
ATOM   2114  NE  ARG A 304     -21.813  90.508 288.582  1.00 62.17           N
ATOM   2115  CZ  ARG A 304     -21.623  90.692 287.283  1.00 63.46           C
ATOM   2116  NH1 ARG A 304     -22.325  91.612 286.635  1.00 61.94           N
ATOM   2117  NH2 ARG A 304     -20.726  89.963 286.636  1.00 68.23           N
ATOM   2118  N   ASP A 305     -20.163  85.650 292.362  1.00 44.77           N
ATOM   2119  CA  ASP A 305     -19.427  84.702 293.198  1.00 46.02           C
ATOM   2120  C   ASP A 305     -20.209  83.584 293.873  1.00 44.25           C
ATOM   2121  O   ASP A 305     -19.718  82.461 293.991  1.00 43.70           O
ATOM   2122  CB  ASP A 305     -18.635  85.474 294.249  1.00 48.32           C
ATOM   2123  CG  ASP A 305     -17.721  86.508 293.630  1.00 52.43           C
ATOM   2124  OD1 ASP A 305     -16.907  86.133 292.755  1.00 55.26           O
ATOM   2125  OD2 ASP A 305     -17.821  87.692 294.012  1.00 54.47           O
ATOM   2126  N   GLU A 306     -21.417  83.874 294.326  1.00 42.30           N
ATOM   2127  CA  GLU A 306     -22.206  82.843 294.980  1.00 42.10           C
ATOM   2128  C   GLU A 306     -23.037  82.047 293.981  1.00 37.98           C
ATOM   2129  O   GLU A 306     -23.378  82.528 292.900  1.00 40.48           O
ATOM   2130  CB  GLU A 306     -23.112  83.470 296.040  1.00 43.06           C
ATOM   2131  CG  GLU A 306     -23.975  84.593 295.512  1.00 55.94           C
ATOM   2132  CD  GLU A 306     -24.731  85.309 296.611  1.00 58.84           C
ATOM   2133  OE1 GLU A 306     -25.626  84.689 297.221  1.00 57.82           O
ATOM   2134  OE2 GLU A 306     -24.426  86.492 296.867  1.00 63.23           O
ATOM   2135  N   LEU A 307     -23.333  80.808 294.343  1.00 34.76           N
ATOM   2136  CA  LEU A 307     -24.144  79.941 293.510  1.00 32.55           C
ATOM   2137  C   LEU A 307     -25.053  79.166 294.462  1.00 34.11           C
ATOM   2138  O   LEU A 307     -24.591  78.548 295.421  1.00 32.38           O
ATOM   2139  CB  LEU A 307     -23.254  78.999 292.698  1.00 32.54           C
ATOM   2140  CG  LEU A 307     -23.964  78.112 291.670  1.00 32.20           C
ATOM   2141  CD1 LEU A 307     -23.024  77.807 290.515  1.00 34.42           C
ATOM   2142  CD2 LEU A 307     -24.447  76.841 292.333  1.00 29.75           C
ATOM   2143  N   HIS A 308     -26.352  79.231 294.209  1.00 32.05           N
ATOM   2144  CA  HIS A 308     -27.323  78.559 295.050  1.00 30.95           C
ATOM   2145  C   HIS A 308     -27.940  77.381 294.334  1.00 32.62           C
ATOM   2146  O   HIS A 308     -28.172  77.425 293.126  1.00 32.47           O
ATOM   2147  CB  HIS A 308     -28.440  79.525 295.444  1.00 30.61           C
ATOM   2148  CG  HIS A 308     -27.969  80.707 296.230  1.00 39.07           C
ATOM   2149  ND1 HIS A 308     -28.080  80.780 297.603  1.00 39.71           N
ATOM   2150  CD2 HIS A 308     -27.374  81.858 295.838  1.00 44.51           C
ATOM   2151  CE1 HIS A 308     -27.574  81.927 298.021  1.00 45.08           C
ATOM   2152  NE2 HIS A 308     -27.138  82.599 296.970  1.00 45.42           N
ATOM   2153  N   VAL A 309     -28.199  76.324 295.091  1.00 28.76           N
ATOM   2154  CA  VAL A 309     -28.839  75.147 294.536  1.00 28.99           C
ATOM   2155  C   VAL A 309     -30.002  74.740 295.428  1.00 27.40           C
ATOM   2156  O   VAL A 309     -29.831  74.516 296.625  1.00 30.26           O
ATOM   2157  CB  VAL A 309     -27.873  73.951 294.431  1.00 28.18           C
ATOM   2158  CG1 VAL A 309     -28.648  72.704 293.958  1.00 29.45           C
ATOM   2159  CG2 VAL A 309     -26.752  74.269 293.456  1.00 25.08           C
ATOM   2160  N   THR A 310     -31.193  74.671 294.852  1.00 25.33           N
ATOM   2161  CA  THR A 310     -32.347  74.235 295.618  1.00 27.27           C
ATOM   2162  C   THR A 310     -32.875  72.944 295.002  1.00 28.17           C
ATOM   2163  O   THR A 310     -33.125  72.866 293.800  1.00 27.46           O
ATOM   2164  CB  THR A 310     -33.472  75.290 295.639  1.00 31.11           C
ATOM   2165  OG1 THR A 310     -32.996  76.479 296.283  1.00 35.66           O
ATOM   2166  CG2 THR A 310     -34.686  74.765 296.419  1.00 28.77           C
ATOM   2167  N   VAL A 311     -33.030  71.924 295.833  1.00 30.91           N
ATOM   2168  CA  VAL A 311     -33.533  70.654 295.354  1.00 31.61           C
ATOM   2169  C   VAL A 311     -34.842  70.287 296.039  1.00 32.08           C
ATOM   2170  O   VAL A 311     -34.954  70.285 297.267  1.00 31.54           O
ATOM   2171  CB  VAL A 311     -32.498  69.542 295.572  1.00 36.93           C
ATOM   2172  CG1 VAL A 311     -32.000  69.583 296.996  1.00 45.48           C
ATOM   2173  CG2 VAL A 311     -33.112  68.182 295.261  1.00 41.31           C
ATOM   2174  N   VAL A 312     -35.846  70.008 295.224  1.00 31.61           N
ATOM   2175  CA  VAL A 312     -37.143  69.605 295.728  1.00 35.38           C
ATOM   2176  C   VAL A 312     -37.392  68.188 295.205  1.00 34.50           C
ATOM   2177  O   VAL A 312     -37.430  67.964 293.998  1.00 34.46           O
ATOM   2178  CB  VAL A 312     -38.253  70.560 295.233  1.00 37.29           C
ATOM   2179  CG1 VAL A 312     -39.627  70.024 295.628  1.00 37.43           C
ATOM   2180  CG2 VAL A 312     -38.043  71.941 295.837  1.00 38.42           C
ATOM   2181  N   ALA A 313     -37.517  67.233 296.123  1.00 35.89           N
ATOM   2182  CA  ALA A 313     -37.771  65.841 295.761  1.00 34.95           C
ATOM   2183  C   ALA A 313     -39.252  65.570 295.989  1.00 36.98           C
ATOM   2184  O   ALA A 313     -39.728  65.644 297.111  1.00 38.52           O
ATOM   2185  CB  ALA A 313     -36.938  64.918 296.624  1.00 32.69           C
ATOM   2186  N   THR A 314     -39.975  65.261 294.918  1.00 43.36           N
ATOM   2187  CA  THR A 314     -41.404  64.992 295.009  1.00 44.50           C
ATOM   2188  C   THR A 314     -41.705  63.505 294.814  1.00 46.40           C
ATOM   2189  O   THR A 314     -40.856  62.752 294.328  1.00 41.59           O
ATOM   2190  CB  THR A 314     -42.171  65.787 293.946  1.00 47.17           C
ATOM   2191  OG1 THR A 314     -41.817  65.309 292.645  1.00 45.70           O
ATOM   2192  CG2 THR A 314     -41.819  67.265 294.037  1.00 46.08           C
ATOM   2193  N   GLY A 315     -42.921  63.102 295.184  1.00 45.21           N
ATOM   2194  CA  GLY A 315     -43.336  61.714 295.059  1.00 43.99           C
ATOM   2195  C   GLY A 315     -42.403  60.768 295.784  1.00 45.88           C
ATOM   2196  O   GLY A 315     -41.917  59.790 295.212  1.00 50.39           O
ATOM   2197  N   LEU A 316     -42.153  61.057 297.054  1.00 46.90           N
ATOM   2198  CA  LEU A 316     -41.256  60.242 297.862  1.00 50.44           C
ATOM   2199  C   LEU A 316     -41.860  58.890 298.212  1.00 53.13           C
ATOM   2200  O   LEU A 316     -43.071  58.760 298.337  1.00 52.69           O
ATOM   2201  CB  LEU A 316     -40.897  60.983 299.151  1.00 49.20           C
ATOM   2202  CG  LEU A 316     -40.153  62.307 298.990  1.00 51.51           C
ATOM   2203  CD1 LEU A 316     -39.878  62.891 300.370  1.00 52.29           C
ATOM   2204  CD2 LEU A 316     -38.855  62.082 298.228  1.00 45.10           C
ATOM   2205  N   GLY A 317     -41.004  57.889 298.382  1.00 58.01           N
ATOM   2206  CA  GLY A 317     -41.478  56.562 298.722  1.00 60.84           C
ATOM   2207  C   GLY A 317     -41.161  55.568 297.624  1.00 61.29           C
ATOM   2208  O   GLY A 317     -41.231  55.901 296.441  1.00 65.75           O
END



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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: April 25th, 2023.