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LongText Report for: 7jqz-pdb

Name Class
7jqz-pdb
HEADER    HYDROLASE                               11-AUG-20   7JQZ              
TITLE     CRYSTAL STRUCTURE OF CFL2 WILD-TYPE FROM BURKHOLDERIA CENOCEPACIA     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FOLD;                                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA (STRAIN MC0-3);        
SOURCE   3 ORGANISM_TAXID: 406425;                                              
SOURCE   4 STRAIN: MC0-3;                                                       
SOURCE   5 GENE: BCENMC03_3580;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DECAMER, ALPHA/BETA HYDROLASE FOLD, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.TAHER,D.R.MADDEN                                                  
REVDAT   1   17-MAR-21 7JQZ    0                                                
JRNL        AUTH   N.M.TAHER,K.L.HVORECNY,C.M.BURKE,M.S.A.GILMAN,G.E.HEUSSLER,  
JRNL        AUTH 2 J.ADOLF-BRYFOGLE,C.D.BAHL,G.A.O'TOOLE,D.R.MADDEN             
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TWO CIF-LIKE  
JRNL        TITL 2 EPOXIDE HYDROLASES FROM BURKHOLDERIA CENOCEPACIA             
JRNL        REF    CURR RES STRUCT BIOL                       2021              
JRNL        REFN                   ESSN 2665-928X                               
JRNL        DOI    10.1016/J.CRSTBI.2021.02.002                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 170263                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8500                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.33                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7JQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248678.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.18076                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 170389                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.450                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3KD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 784 MM SODIUM THIOCYANATE, 12% PEG       
REMARK 280  3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       91.36700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      105.23550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.36700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      105.23550            
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 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: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 101830 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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     TYR A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     MET B     1                                                      
REMARK 465     TYR B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     MET C     1                                                      
REMARK 465     TYR C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     LEU C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     ALA C    15                                                      
REMARK 465     MET D     1                                                      
REMARK 465     TYR D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     LEU D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     MET E     1                                                      
REMARK 465     TYR E     2                                                      
REMARK 465     GLN E     3                                                      
REMARK 465     HIS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     GLU E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     ALA E    10                                                      
REMARK 465     SER E    11                                                      
REMARK 465     HIS E    12                                                      
REMARK 465     LEU E    13                                                      
REMARK 465     GLU E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     MET F     1                                                      
REMARK 465     TYR F     2                                                      
REMARK 465     GLN F     3                                                      
REMARK 465     HIS F     4                                                      
REMARK 465     GLN F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     GLU F     8                                                      
REMARK 465     ALA F     9                                                      
REMARK 465     ALA F    10                                                      
REMARK 465     SER F    11                                                      
REMARK 465     HIS F    12                                                      
REMARK 465     LEU F    13                                                      
REMARK 465     GLU F    14                                                      
REMARK 465     ALA F    15                                                      
REMARK 465     MET G     1                                                      
REMARK 465     TYR G     2                                                      
REMARK 465     GLN G     3                                                      
REMARK 465     HIS G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     SER G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     GLU G     8                                                      
REMARK 465     ALA G     9                                                      
REMARK 465     ALA G    10                                                      
REMARK 465     SER G    11                                                      
REMARK 465     HIS G    12                                                      
REMARK 465     LEU G    13                                                      
REMARK 465     GLU G    14                                                      
REMARK 465     ALA G    15                                                      
REMARK 465     MET H     1                                                      
REMARK 465     TYR H     2                                                      
REMARK 465     GLN H     3                                                      
REMARK 465     HIS H     4                                                      
REMARK 465     GLN H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     GLU H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     ALA H    10                                                      
REMARK 465     SER H    11                                                      
REMARK 465     HIS H    12                                                      
REMARK 465     LEU H    13                                                      
REMARK 465     GLU H    14                                                      
REMARK 465     ALA H    15                                                      
REMARK 465     MET I     1                                                      
REMARK 465     TYR I     2                                                      
REMARK 465     GLN I     3                                                      
REMARK 465     HIS I     4                                                      
REMARK 465     GLN I     5                                                      
REMARK 465     SER I     6                                                      
REMARK 465     THR I     7                                                      
REMARK 465     GLU I     8                                                      
REMARK 465     ALA I     9                                                      
REMARK 465     ALA I    10                                                      
REMARK 465     SER I    11                                                      
REMARK 465     HIS I    12                                                      
REMARK 465     LEU I    13                                                      
REMARK 465     GLU I    14                                                      
REMARK 465     ALA I    15                                                      
REMARK 465     MET J     1                                                      
REMARK 465     TYR J     2                                                      
REMARK 465     GLN J     3                                                      
REMARK 465     HIS J     4                                                      
REMARK 465     GLN J     5                                                      
REMARK 465     SER J     6                                                      
REMARK 465     THR J     7                                                      
REMARK 465     GLU J     8                                                      
REMARK 465     ALA J     9                                                      
REMARK 465     ALA J    10                                                      
REMARK 465     SER J    11                                                      
REMARK 465     HIS J    12                                                      
REMARK 465     LEU J    13                                                      
REMARK 465     GLU J    14                                                      
REMARK 465     ALA J    15                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  60       58.52    -98.92                                   
REMARK 500    GLU A  61     -152.62   -121.11                                   
REMARK 500    ASP A 124     -132.68     59.16                                   
REMARK 500    ASP A 148       65.34     39.44                                   
REMARK 500    VAL A 154      -46.12   -136.35                                   
REMARK 500    ASP A 180      -37.59     68.36                                   
REMARK 500    ASP A 223      111.50    -37.85                                   
REMARK 500    PRO B  60       56.87    -99.63                                   
REMARK 500    GLU B  61     -152.10   -120.18                                   
REMARK 500    SER B  62     -175.06   -170.93                                   
REMARK 500    ASP B 124     -132.67     60.82                                   
REMARK 500    ASP B 180      -36.87     69.49                                   
REMARK 500    ASP B 223      109.04    -36.43                                   
REMARK 500    PRO C  60       57.07   -100.67                                   
REMARK 500    GLU C  61     -152.50   -118.60                                   
REMARK 500    ASP C 124     -133.07     63.08                                   
REMARK 500    ASP C 180      -39.78     67.86                                   
REMARK 500    PRO D  60       56.24    -99.83                                   
REMARK 500    GLU D  61     -151.73   -117.11                                   
REMARK 500    ASP D 124     -133.50     61.73                                   
REMARK 500    VAL D 154      -44.21   -130.08                                   
REMARK 500    ASP D 180      -36.85     69.73                                   
REMARK 500    PRO E  60       58.07   -100.64                                   
REMARK 500    GLU E  61     -151.82   -119.52                                   
REMARK 500    SER E  62     -176.83   -171.09                                   
REMARK 500    ASP E 124     -132.85     60.76                                   
REMARK 500    VAL E 154      -33.32   -133.05                                   
REMARK 500    ASP E 180      -39.24     68.82                                   
REMARK 500    ASP E 223      116.83    -35.65                                   
REMARK 500    PRO F  60       56.29   -100.09                                   
REMARK 500    GLU F  61     -151.06   -119.71                                   
REMARK 500    SER F  62     -175.21   -170.28                                   
REMARK 500    ASP F 124     -133.26     61.12                                   
REMARK 500    VAL F 154      -39.14   -132.73                                   
REMARK 500    ASP F 180      -36.37     68.66                                   
REMARK 500    ASP F 223      111.20    -38.82                                   
REMARK 500    PRO G  60       56.76    -99.90                                   
REMARK 500    GLU G  61     -152.31   -118.82                                   
REMARK 500    SER G  62     -175.14   -170.49                                   
REMARK 500    ASP G 124     -132.59     61.91                                   
REMARK 500    ASP G 180      -38.25     69.62                                   
REMARK 500    ASP G 223      112.81    -32.15                                   
REMARK 500    PRO H  60       57.08   -103.40                                   
REMARK 500    GLU H  61     -150.41   -118.38                                   
REMARK 500    ASP H 124     -134.66     61.72                                   
REMARK 500    VAL H 154      -59.52   -126.59                                   
REMARK 500    ASP H 180      -39.22     68.99                                   
REMARK 500    ASP H 223      114.05    -36.40                                   
REMARK 500    PHE H 291       59.97    -93.74                                   
REMARK 500    PRO I  60       55.84   -101.30                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH I 487        DISTANCE =  6.04 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7JQX   RELATED DB: PDB                                   
REMARK 900 7JQX IS FOR THE SAME CITATION                                        
REMARK 900 RELATED ID: 7JQY   RELATED DB: PDB                                   
REMARK 900 7JQY IS FOR THE SAME CITATION                                        
DBREF  7JQZ A    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ B    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ C    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ D    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ E    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ F    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ G    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ H    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ I    1   309  UNP    B1K378   B1K378_BURCC     1    309             
DBREF  7JQZ J    1   309  UNP    B1K378   B1K378_BURCC     1    309             
SEQRES   1 A  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 A  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 A  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 A  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 A  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 A  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 A  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 A  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 A  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 A  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 A  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 A  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 A  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 A  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 A  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 A  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 A  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 A  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 A  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 A  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 A  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 A  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 A  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 A  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 B  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 B  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 B  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 B  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 B  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 B  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 B  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 B  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 B  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 B  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 B  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 B  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 B  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 B  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 B  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 B  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 B  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 B  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 B  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 B  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 B  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 B  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 B  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 B  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 C  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 C  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 C  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 C  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 C  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 C  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 C  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 C  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 C  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 C  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 C  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 C  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 C  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 C  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 C  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 C  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 C  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 C  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 C  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 C  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 C  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 C  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 C  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 C  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 D  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 D  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 D  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 D  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 D  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 D  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 D  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 D  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 D  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 D  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 D  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 D  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 D  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 D  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 D  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 D  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 D  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 D  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 D  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 D  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 D  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 D  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 D  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 D  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 E  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 E  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 E  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 E  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 E  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 E  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 E  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 E  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 E  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 E  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 E  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 E  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 E  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 E  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 E  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 E  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 E  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 E  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 E  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 E  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 E  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 E  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 E  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 E  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 F  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 F  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 F  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 F  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 F  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 F  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 F  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 F  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 F  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 F  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 F  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 F  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 F  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 F  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 F  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 F  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 F  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 F  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 F  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 F  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 F  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 F  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 F  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 F  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 G  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 G  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 G  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 G  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 G  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 G  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 G  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 G  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 G  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 G  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 G  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 G  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 G  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 G  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 G  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 G  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 G  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 G  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 G  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 G  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 G  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 G  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 G  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 G  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 H  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 H  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 H  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 H  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 H  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 H  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 H  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 H  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 H  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 H  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 H  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 H  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 H  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 H  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 H  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 H  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 H  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 H  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 H  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 H  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 H  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 H  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 H  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 H  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 I  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 I  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 I  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 I  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 I  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 I  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 I  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 I  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 I  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 I  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 I  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 I  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 I  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 I  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 I  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 I  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 I  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 I  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 I  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 I  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 I  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 I  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 I  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 I  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
SEQRES   1 J  309  MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU          
SEQRES   2 J  309  GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR          
SEQRES   3 J  309  GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG          
SEQRES   4 J  309  LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR          
SEQRES   5 J  309  ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA          
SEQRES   6 J  309  TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG          
SEQRES   7 J  309  ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP          
SEQRES   8 J  309  ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA          
SEQRES   9 J  309  THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG          
SEQRES  10 J  309  PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA          
SEQRES  11 J  309  TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG          
SEQRES  12 J  309  LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU          
SEQRES  13 J  309  PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG          
SEQRES  14 J  309  THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO          
SEQRES  15 J  309  GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP          
SEQRES  16 J  309  TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE          
SEQRES  17 J  309  SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR          
SEQRES  18 J  309  ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG          
SEQRES  19 J  309  ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN          
SEQRES  20 J  309  ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER          
SEQRES  21 J  309  ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU          
SEQRES  22 J  309  GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA          
SEQRES  23 J  309  TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA          
SEQRES  24 J  309  LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG                      
FORMUL  11  HOH   *1141(H2 O)                                                   
HELIX    1 AA1 SER A   62  ARG A   67  5                                   6    
HELIX    2 AA2 VAL A   69  ALA A   74  1                                   6    
HELIX    3 AA3 ASP A   98  GLN A  113  1                                  16    
HELIX    4 AA4 ASP A  124  TYR A  137  1                                  14    
HELIX    5 AA5 ASN A  166  THR A  170  5                                   5    
HELIX    6 AA6 TRP A  171  VAL A  178  1                                   8    
HELIX    7 AA7 ASP A  180  ALA A  187  1                                   8    
HELIX    8 AA8 LYS A  189  ALA A  202  1                                  14    
HELIX    9 AA9 ASN A  204  PHE A  208  5                                   5    
HELIX   10 AB1 SER A  209  ARG A  222  1                                  14    
HELIX   11 AB2 GLY A  224  ALA A  235  1                                  12    
HELIX   12 AB3 ALA A  235  ALA A  248  1                                  14    
HELIX   13 AB4 MET A  269  HIS A  275  1                                   7    
HELIX   14 AB5 PHE A  291  GLN A  296  1                                   6    
HELIX   15 AB6 GLN A  296  PHE A  308  1                                  13    
HELIX   16 AB7 SER B   62  ARG B   67  5                                   6    
HELIX   17 AB8 VAL B   69  ALA B   74  1                                   6    
HELIX   18 AB9 ASP B   98  GLN B  113  1                                  16    
HELIX   19 AC1 ASP B  124  TYR B  137  1                                  14    
HELIX   20 AC2 ASN B  166  TRP B  171  1                                   6    
HELIX   21 AC3 TRP B  171  VAL B  178  1                                   8    
HELIX   22 AC4 ASP B  180  ALA B  187  1                                   8    
HELIX   23 AC5 LYS B  189  ALA B  202  1                                  14    
HELIX   24 AC6 ASN B  204  PHE B  208  5                                   5    
HELIX   25 AC7 SER B  209  ARG B  222  1                                  14    
HELIX   26 AC8 GLY B  224  ALA B  235  1                                  12    
HELIX   27 AC9 ALA B  235  LEU B  249  1                                  15    
HELIX   28 AD1 MET B  269  GLU B  274  1                                   6    
HELIX   29 AD2 PHE B  291  GLN B  296  1                                   6    
HELIX   30 AD3 GLN B  296  PHE B  308  1                                  13    
HELIX   31 AD4 SER C   62  ARG C   67  5                                   6    
HELIX   32 AD5 VAL C   69  ALA C   74  1                                   6    
HELIX   33 AD6 ASP C   98  GLN C  113  1                                  16    
HELIX   34 AD7 ASP C  124  TYR C  137  1                                  14    
HELIX   35 AD8 ASN C  166  THR C  170  5                                   5    
HELIX   36 AD9 TRP C  171  VAL C  178  1                                   8    
HELIX   37 AE1 ASP C  180  ALA C  187  1                                   8    
HELIX   38 AE2 LYS C  189  ALA C  202  1                                  14    
HELIX   39 AE3 ASN C  204  PHE C  208  5                                   5    
HELIX   40 AE4 SER C  209  THR C  221  1                                  13    
HELIX   41 AE5 GLY C  224  ALA C  235  1                                  12    
HELIX   42 AE6 ALA C  235  LEU C  249  1                                  15    
HELIX   43 AE7 MET C  269  GLU C  274  1                                   6    
HELIX   44 AE8 PHE C  291  GLN C  296  1                                   6    
HELIX   45 AE9 GLN C  296  PHE C  308  1                                  13    
HELIX   46 AF1 SER D   62  ARG D   67  5                                   6    
HELIX   47 AF2 VAL D   69  ALA D   74  1                                   6    
HELIX   48 AF3 ASP D   98  GLN D  113  1                                  16    
HELIX   49 AF4 ASP D  124  TYR D  137  1                                  14    
HELIX   50 AF5 ASN D  166  THR D  170  5                                   5    
HELIX   51 AF6 TRP D  171  VAL D  178  1                                   8    
HELIX   52 AF7 ASP D  180  ALA D  187  1                                   8    
HELIX   53 AF8 LYS D  189  ALA D  202  1                                  14    
HELIX   54 AF9 ASN D  204  PHE D  208  5                                   5    
HELIX   55 AG1 SER D  209  ARG D  222  1                                  14    
HELIX   56 AG2 GLY D  224  ALA D  235  1                                  12    
HELIX   57 AG3 ALA D  235  LEU D  249  1                                  15    
HELIX   58 AG4 MET D  269  GLU D  274  1                                   6    
HELIX   59 AG5 PHE D  291  GLN D  296  1                                   6    
HELIX   60 AG6 GLN D  296  PHE D  308  1                                  13    
HELIX   61 AG7 SER E   62  ARG E   67  5                                   6    
HELIX   62 AG8 VAL E   69  ASP E   75  1                                   7    
HELIX   63 AG9 ASP E   98  GLN E  113  1                                  16    
HELIX   64 AH1 ASP E  124  TYR E  137  1                                  14    
HELIX   65 AH2 GLU E  163  TRP E  168  1                                   6    
HELIX   66 AH3 TRP E  171  VAL E  178  1                                   8    
HELIX   67 AH4 ASP E  180  ALA E  187  1                                   8    
HELIX   68 AH5 LYS E  189  ALA E  202  1                                  14    
HELIX   69 AH6 ASN E  204  PHE E  208  5                                   5    
HELIX   70 AH7 SER E  209  ARG E  222  1                                  14    
HELIX   71 AH8 GLY E  224  ALA E  235  1                                  12    
HELIX   72 AH9 ALA E  235  ALA E  248  1                                  14    
HELIX   73 AI1 MET E  269  GLU E  274  1                                   6    
HELIX   74 AI2 PHE E  291  GLN E  296  1                                   6    
HELIX   75 AI3 GLN E  296  PHE E  308  1                                  13    
HELIX   76 AI4 SER F   62  ARG F   67  5                                   6    
HELIX   77 AI5 VAL F   69  ALA F   74  1                                   6    
HELIX   78 AI6 ASP F   98  GLN F  113  1                                  16    
HELIX   79 AI7 ASP F  124  TYR F  137  1                                  14    
HELIX   80 AI8 GLU F  163  TRP F  168  1                                   6    
HELIX   81 AI9 TRP F  171  VAL F  178  1                                   8    
HELIX   82 AJ1 ASP F  180  ALA F  187  1                                   8    
HELIX   83 AJ2 LYS F  189  ALA F  202  1                                  14    
HELIX   84 AJ3 ASN F  204  PHE F  208  5                                   5    
HELIX   85 AJ4 SER F  209  ARG F  222  1                                  14    
HELIX   86 AJ5 GLY F  224  ALA F  235  1                                  12    
HELIX   87 AJ6 ALA F  235  ALA F  248  1                                  14    
HELIX   88 AJ7 MET F  269  GLU F  274  1                                   6    
HELIX   89 AJ8 PHE F  291  GLN F  296  1                                   6    
HELIX   90 AJ9 GLN F  296  PHE F  308  1                                  13    
HELIX   91 AK1 SER G   62  ARG G   67  5                                   6    
HELIX   92 AK2 VAL G   69  ASP G   75  1                                   7    
HELIX   93 AK3 ASP G   98  GLN G  113  1                                  16    
HELIX   94 AK4 ASP G  124  TYR G  137  1                                  14    
HELIX   95 AK5 ASN G  166  TRP G  171  1                                   6    
HELIX   96 AK6 TRP G  171  VAL G  178  1                                   8    
HELIX   97 AK7 ASP G  180  ALA G  187  1                                   8    
HELIX   98 AK8 LYS G  189  ALA G  202  1                                  14    
HELIX   99 AK9 ASN G  204  PHE G  208  5                                   5    
HELIX  100 AL1 SER G  209  ARG G  222  1                                  14    
HELIX  101 AL2 GLY G  224  ALA G  235  1                                  12    
HELIX  102 AL3 ALA G  235  ALA G  248  1                                  14    
HELIX  103 AL4 MET G  269  GLU G  274  1                                   6    
HELIX  104 AL5 PHE G  291  GLN G  296  1                                   6    
HELIX  105 AL6 GLN G  296  PHE G  308  1                                  13    
HELIX  106 AL7 SER H   62  ARG H   67  5                                   6    
HELIX  107 AL8 VAL H   69  ALA H   74  1                                   6    
HELIX  108 AL9 ASP H   98  GLN H  113  1                                  16    
HELIX  109 AM1 ASP H  124  TYR H  137  1                                  14    
HELIX  110 AM2 ASN H  166  TRP H  171  1                                   6    
HELIX  111 AM3 TRP H  171  VAL H  178  1                                   8    
HELIX  112 AM4 ASP H  180  ALA H  187  1                                   8    
HELIX  113 AM5 LYS H  189  LYS H  201  1                                  13    
HELIX  114 AM6 ASN H  204  PHE H  208  5                                   5    
HELIX  115 AM7 SER H  209  THR H  221  1                                  13    
HELIX  116 AM8 GLY H  224  ALA H  235  1                                  12    
HELIX  117 AM9 ALA H  235  ALA H  248  1                                  14    
HELIX  118 AN1 MET H  269  GLU H  274  1                                   6    
HELIX  119 AN2 PHE H  291  GLN H  296  1                                   6    
HELIX  120 AN3 GLN H  296  PHE H  308  1                                  13    
HELIX  121 AN4 SER I   62  ARG I   67  5                                   6    
HELIX  122 AN5 VAL I   69  ALA I   74  1                                   6    
HELIX  123 AN6 ASP I   98  GLN I  113  1                                  16    
HELIX  124 AN7 ASP I  124  TYR I  137  1                                  14    
HELIX  125 AN8 ASN I  166  THR I  170  5                                   5    
HELIX  126 AN9 TRP I  171  VAL I  178  1                                   8    
HELIX  127 AO1 ASP I  180  ALA I  187  1                                   8    
HELIX  128 AO2 LYS I  189  ALA I  202  1                                  14    
HELIX  129 AO3 ASN I  204  PHE I  208  5                                   5    
HELIX  130 AO4 SER I  209  ARG I  222  1                                  14    
HELIX  131 AO5 GLY I  224  ALA I  235  1                                  12    
HELIX  132 AO6 ALA I  235  ALA I  248  1                                  14    
HELIX  133 AO7 MET I  269  GLU I  274  1                                   6    
HELIX  134 AO8 PHE I  291  GLN I  296  1                                   6    
HELIX  135 AO9 GLN I  296  PHE I  308  1                                  13    
HELIX  136 AP1 SER J   62  ARG J   67  5                                   6    
HELIX  137 AP2 VAL J   69  ALA J   74  1                                   6    
HELIX  138 AP3 ASP J   98  GLN J  113  1                                  16    
HELIX  139 AP4 ASP J  124  TYR J  137  1                                  14    
HELIX  140 AP5 ASN J  166  THR J  170  5                                   5    
HELIX  141 AP6 TRP J  171  VAL J  178  1                                   8    
HELIX  142 AP7 ASP J  180  ALA J  187  1                                   8    
HELIX  143 AP8 LYS J  189  ALA J  202  1                                  14    
HELIX  144 AP9 ASN J  204  PHE J  208  5                                   5    
HELIX  145 AQ1 SER J  209  ARG J  222  1                                  14    
HELIX  146 AQ2 GLY J  224  ALA J  235  1                                  12    
HELIX  147 AQ3 ALA J  235  ALA J  248  1                                  14    
HELIX  148 AQ4 MET J  269  GLU J  274  1                                   6    
HELIX  149 AQ5 PHE J  291  GLN J  296  1                                   6    
HELIX  150 AQ6 GLN J  296  PHE J  308  1                                  13    
SHEET    1 AA1 9 ARG A  20  GLU A  21  0                                        
SHEET    2 AA1 9 ARG A  29  VAL A  35 -1  O  HIS A  30   N  ARG A  20           
SHEET    3 AA1 9 VAL A  38  GLY A  46 -1  O  VAL A  38   N  VAL A  35           
SHEET    4 AA1 9 ARG A  78  PRO A  82 -1  O  ALA A  81   N  VAL A  43           
SHEET    5 AA1 9 THR A  52  LEU A  56  1  N  ILE A  53   O  ARG A  78           
SHEET    6 AA1 9 PHE A 118  HIS A 123  1  O  TYR A 119   N  THR A  52           
SHEET    7 AA1 9 VAL A 141  LEU A 147  1  O  ALA A 145   N  ALA A 122           
SHEET    8 AA1 9 VAL A 256  ALA A 261  1  O  LEU A 257   N  LEU A 144           
SHEET    9 AA1 9 VAL A 280  ILE A 285  1  O  ILE A 285   N  SER A 260           
SHEET    1 AA2 2 ALA A 159  PRO A 161  0                                        
SHEET    2 AA2 2 ALA B 159  PRO B 161 -1  O  LEU B 160   N  LEU A 160           
SHEET    1 AA3 9 ARG B  20  GLU B  21  0                                        
SHEET    2 AA3 9 ARG B  29  VAL B  35 -1  O  HIS B  30   N  ARG B  20           
SHEET    3 AA3 9 VAL B  38  GLY B  46 -1  O  VAL B  38   N  VAL B  35           
SHEET    4 AA3 9 ARG B  78  PRO B  82 -1  O  ILE B  79   N  GLY B  45           
SHEET    5 AA3 9 THR B  52  LEU B  56  1  N  ILE B  53   O  ARG B  78           
SHEET    6 AA3 9 PHE B 118  HIS B 123  1  O  TYR B 119   N  THR B  52           
SHEET    7 AA3 9 VAL B 141  LEU B 147  1  O  ALA B 145   N  LEU B 120           
SHEET    8 AA3 9 VAL B 256  ALA B 261  1  O  VAL B 259   N  LEU B 146           
SHEET    9 AA3 9 VAL B 280  ILE B 285  1  O  THR B 281   N  ALA B 258           
SHEET    1 AA4 9 ARG C  20  GLU C  21  0                                        
SHEET    2 AA4 9 ARG C  29  VAL C  35 -1  O  HIS C  30   N  ARG C  20           
SHEET    3 AA4 9 VAL C  38  GLY C  46 -1  O  LEU C  40   N  ASP C  33           
SHEET    4 AA4 9 ARG C  78  PRO C  82 -1  O  ALA C  81   N  VAL C  43           
SHEET    5 AA4 9 THR C  52  LEU C  56  1  N  ILE C  53   O  ARG C  78           
SHEET    6 AA4 9 PHE C 118  HIS C 123  1  O  TYR C 119   N  THR C  52           
SHEET    7 AA4 9 VAL C 141  LEU C 147  1  O  LYS C 142   N  PHE C 118           
SHEET    8 AA4 9 VAL C 256  ALA C 261  1  O  LEU C 257   N  LEU C 144           
SHEET    9 AA4 9 VAL C 280  ILE C 285  1  O  THR C 281   N  ALA C 258           
SHEET    1 AA5 2 ALA C 159  PRO C 161  0                                        
SHEET    2 AA5 2 ALA D 159  PRO D 161 -1  O  LEU D 160   N  LEU C 160           
SHEET    1 AA6 9 ARG D  20  GLU D  21  0                                        
SHEET    2 AA6 9 ARG D  29  VAL D  35 -1  O  HIS D  30   N  ARG D  20           
SHEET    3 AA6 9 VAL D  38  GLY D  46 -1  O  GLU D  44   N  ARG D  29           
SHEET    4 AA6 9 ARG D  78  PRO D  82 -1  O  ALA D  81   N  VAL D  43           
SHEET    5 AA6 9 THR D  52  LEU D  56  1  N  ILE D  53   O  ARG D  78           
SHEET    6 AA6 9 PHE D 118  HIS D 123  1  O  TYR D 119   N  THR D  52           
SHEET    7 AA6 9 VAL D 141  LEU D 147  1  O  ALA D 145   N  LEU D 120           
SHEET    8 AA6 9 VAL D 256  ALA D 261  1  O  LEU D 257   N  LEU D 144           
SHEET    9 AA6 9 VAL D 280  ILE D 285  1  O  THR D 281   N  ALA D 258           
SHEET    1 AA7 9 ARG E  20  GLU E  21  0                                        
SHEET    2 AA7 9 ARG E  29  VAL E  35 -1  O  HIS E  30   N  ARG E  20           
SHEET    3 AA7 9 VAL E  38  GLY E  46 -1  O  VAL E  38   N  VAL E  35           
SHEET    4 AA7 9 ARG E  78  PRO E  82 -1  O  ALA E  81   N  VAL E  43           
SHEET    5 AA7 9 THR E  52  LEU E  56  1  N  ILE E  53   O  ARG E  78           
SHEET    6 AA7 9 PHE E 118  HIS E 123  1  O  TYR E 119   N  VAL E  54           
SHEET    7 AA7 9 VAL E 141  LEU E 147  1  O  ALA E 145   N  LEU E 120           
SHEET    8 AA7 9 VAL E 256  ALA E 261  1  O  LEU E 257   N  LEU E 144           
SHEET    9 AA7 9 VAL E 280  ILE E 285  1  O  THR E 281   N  ALA E 258           
SHEET    1 AA8 2 ALA E 159  PRO E 161  0                                        
SHEET    2 AA8 2 ALA F 159  PRO F 161 -1  O  LEU F 160   N  LEU E 160           
SHEET    1 AA9 9 ARG F  20  GLU F  21  0                                        
SHEET    2 AA9 9 ARG F  29  VAL F  35 -1  O  HIS F  30   N  ARG F  20           
SHEET    3 AA9 9 VAL F  38  GLY F  46 -1  O  LEU F  40   N  ASP F  33           
SHEET    4 AA9 9 ARG F  78  PRO F  82 -1  O  ALA F  81   N  VAL F  43           
SHEET    5 AA9 9 THR F  52  LEU F  56  1  N  ILE F  53   O  ARG F  78           
SHEET    6 AA9 9 PHE F 118  HIS F 123  1  O  TYR F 119   N  VAL F  54           
SHEET    7 AA9 9 VAL F 141  LEU F 147  1  O  LYS F 142   N  PHE F 118           
SHEET    8 AA9 9 VAL F 256  ALA F 261  1  O  LEU F 257   N  LEU F 144           
SHEET    9 AA9 9 VAL F 280  ILE F 285  1  O  THR F 281   N  ALA F 258           
SHEET    1 AB1 9 ARG G  20  GLU G  21  0                                        
SHEET    2 AB1 9 PHE G  28  VAL G  35 -1  O  HIS G  30   N  ARG G  20           
SHEET    3 AB1 9 VAL G  38  GLY G  46 -1  O  LEU G  40   N  ASP G  33           
SHEET    4 AB1 9 PHE G  77  PRO G  82 -1  O  ALA G  81   N  VAL G  43           
SHEET    5 AB1 9 GLU G  51  LEU G  56  1  N  GLU G  51   O  ARG G  78           
SHEET    6 AB1 9 PHE G 118  HIS G 123  1  O  TYR G 119   N  VAL G  54           
SHEET    7 AB1 9 VAL G 141  LEU G 147  1  O  ALA G 145   N  LEU G 120           
SHEET    8 AB1 9 VAL G 256  ALA G 261  1  O  LEU G 257   N  LEU G 144           
SHEET    9 AB1 9 VAL G 280  ILE G 285  1  O  THR G 281   N  VAL G 256           
SHEET    1 AB2 2 ALA G 159  PRO G 161  0                                        
SHEET    2 AB2 2 ALA H 159  PRO H 161 -1  O  LEU H 160   N  LEU G 160           
SHEET    1 AB3 9 ARG H  20  GLU H  21  0                                        
SHEET    2 AB3 9 ARG H  29  VAL H  35 -1  O  HIS H  30   N  ARG H  20           
SHEET    3 AB3 9 VAL H  38  GLY H  46 -1  O  LEU H  40   N  ASP H  33           
SHEET    4 AB3 9 ARG H  78  PRO H  82 -1  O  ALA H  81   N  VAL H  43           
SHEET    5 AB3 9 THR H  52  LEU H  56  1  N  ILE H  53   O  ARG H  78           
SHEET    6 AB3 9 PHE H 118  HIS H 123  1  O  TYR H 119   N  THR H  52           
SHEET    7 AB3 9 VAL H 141  LEU H 147  1  O  ALA H 145   N  LEU H 120           
SHEET    8 AB3 9 VAL H 256  ALA H 261  1  O  LEU H 257   N  LEU H 144           
SHEET    9 AB3 9 VAL H 280  ILE H 285  1  O  ALA H 283   N  SER H 260           
SHEET    1 AB4 9 ARG I  20  GLU I  21  0                                        
SHEET    2 AB4 9 ARG I  29  VAL I  35 -1  O  HIS I  30   N  ARG I  20           
SHEET    3 AB4 9 VAL I  38  GLY I  46 -1  O  VAL I  38   N  VAL I  35           
SHEET    4 AB4 9 PHE I  77  PRO I  82 -1  O  ALA I  81   N  VAL I  43           
SHEET    5 AB4 9 GLU I  51  LEU I  56  1  N  ILE I  53   O  ARG I  78           
SHEET    6 AB4 9 PHE I 118  HIS I 123  1  O  TYR I 119   N  THR I  52           
SHEET    7 AB4 9 VAL I 141  LEU I 147  1  O  LYS I 142   N  PHE I 118           
SHEET    8 AB4 9 VAL I 256  ALA I 261  1  O  LEU I 257   N  LEU I 144           
SHEET    9 AB4 9 VAL I 280  ILE I 285  1  O  ALA I 283   N  SER I 260           
SHEET    1 AB5 2 ALA I 159  PRO I 161  0                                        
SHEET    2 AB5 2 ALA J 159  PRO J 161 -1  O  LEU J 160   N  LEU I 160           
SHEET    1 AB6 9 ARG J  20  GLU J  21  0                                        
SHEET    2 AB6 9 ARG J  29  VAL J  35 -1  O  HIS J  30   N  ARG J  20           
SHEET    3 AB6 9 VAL J  38  GLY J  46 -1  O  VAL J  38   N  VAL J  35           
SHEET    4 AB6 9 ARG J  78  PRO J  82 -1  O  ALA J  81   N  VAL J  43           
SHEET    5 AB6 9 THR J  52  LEU J  56  1  N  ILE J  53   O  ARG J  78           
SHEET    6 AB6 9 PHE J 118  HIS J 123  1  O  TYR J 119   N  THR J  52           
SHEET    7 AB6 9 VAL J 141  LEU J 147  1  O  ALA J 145   N  LEU J 120           
SHEET    8 AB6 9 VAL J 256  ALA J 261  1  O  LEU J 257   N  LEU J 144           
SHEET    9 AB6 9 VAL J 280  ILE J 285  1  O  ALA J 283   N  SER J 260           
CISPEP   1 PHE A   59    PRO A   60          0        -4.81                     
CISPEP   2 PHE B   59    PRO B   60          0        -3.14                     
CISPEP   3 PHE C   59    PRO C   60          0        -3.14                     
CISPEP   4 PHE D   59    PRO D   60          0        -3.82                     
CISPEP   5 PHE E   59    PRO E   60          0        -3.27                     
CISPEP   6 PHE F   59    PRO F   60          0        -3.77                     
CISPEP   7 PHE G   59    PRO G   60          0        -3.73                     
CISPEP   8 PHE H   59    PRO H   60          0        -2.92                     
CISPEP   9 PHE I   59    PRO I   60          0        -3.37                     
CISPEP  10 PHE J   59    PRO J   60          0        -3.50                     
CRYST1  182.734  210.471   86.956  90.00  90.00  90.00 P 21 21 2    40          
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      0.005472  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004751  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011500        0.00000                         
TER    2349      ARG A 309                                                      
TER    4687      ARG B 309                                                      
TER    7014      ARG C 309                                                      
TER    9341      ARG D 309                                                      
TER   11668      ARG E 309                                                      
TER   14006      ARG F 309                                                      
TER   16344      ARG G 309                                                      
TER   18682      ARG H 309                                                      
TER   21009      ARG I 309                                                      
TER   23347      ARG J 309                                                      
MASTER      436    0    0  150  100    0    0    624401   10    0  240          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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