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LongText Report for: 7jqx-pdb

Name Class
7jqx-pdb
HEADER    HYDROLASE                               11-AUG-20   7JQX              
TITLE     CRYSTAL STRUCTURE OF CFL1 WILD-TYPE FROM BURKHOLDERIA CENOCEPACIA     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CIF-LIKE 1 WILD-TYPE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA (STRAIN ATCC BAA-245 / 
SOURCE   3 DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610);                
SOURCE   4 ORGANISM_TAXID: 216591;                                              
SOURCE   5 STRAIN: ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /  
SOURCE   6 CF5610;                                                              
SOURCE   7 GENE: BCAM1529;                                                      
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OCTAMER, ALPHA/BETA HYDROLASE FOLD, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.M.TAHER,D.R.MADDEN                                                  
REVDAT   1   17-MAR-21 7JQX    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) : 48.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 76601                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3819                            
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) : 21.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.27                          
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 : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 5672                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 5672                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 5672                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7JQX 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_1000249036.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS-II                            
REMARK 200  BEAMLINE                       : 17-ID-1                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76696                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 13.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.7100                            
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         : NULL                               
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   (%): 56.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 750 MM POTASSIUM SODIUM TARTRATE, 100    
REMARK 280  MM HEPES PH 8.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       66.07500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      170.85000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       66.07500            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      170.85000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       66.07500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      170.85000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       66.07500            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      170.85000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       66.07500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      170.85000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       66.07500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      170.85000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       66.07500            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      170.85000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       66.07500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       66.07500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      170.85000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18110 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 78300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -132.15000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -132.15000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000     -132.15000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000     -132.15000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17670 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 79090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 463  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     MET A    10                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     MET B    10                                                      
REMARK 465     ALA B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     SER B   307                                                      
REMARK 465     GLY B   308                                                      
REMARK 465     ARG B   309                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     GLN C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     MET C    10                                                      
REMARK 465     ALA C   305                                                      
REMARK 465     ALA C   306                                                      
REMARK 465     SER C   307                                                      
REMARK 465     GLY C   308                                                      
REMARK 465     ARG C   309                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     GLN D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     MET D    10                                                      
REMARK 465     ALA D   305                                                      
REMARK 465     ALA D   306                                                      
REMARK 465     SER D   307                                                      
REMARK 465     GLY D   308                                                      
REMARK 465     ARG D   309                                                      
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    THR A 115      -54.77   -139.27                                   
REMARK 500    ASP A 123     -125.01     52.22                                   
REMARK 500    ASP A 147      -39.32     71.60                                   
REMARK 500    ASP A 177      -36.50     75.91                                   
REMARK 500    SER A 258     -116.61   -130.00                                   
REMARK 500    TRP A 285       76.08   -112.45                                   
REMARK 500    THR B 115      -40.81   -134.56                                   
REMARK 500    ASP B 123     -127.88     51.33                                   
REMARK 500    ASP B 147      -39.31     71.82                                   
REMARK 500    ASP B 177      -36.89     76.28                                   
REMARK 500    SER B 258     -115.73   -127.35                                   
REMARK 500    TRP B 285       77.58   -109.04                                   
REMARK 500    LYS C  91       77.17   -119.98                                   
REMARK 500    THR C 115      -56.44   -132.44                                   
REMARK 500    ASP C 123     -128.03     52.28                                   
REMARK 500    ASP C 147      -39.26     70.77                                   
REMARK 500    ASP C 177      -37.89     75.07                                   
REMARK 500    SER C 258     -116.01   -127.70                                   
REMARK 500    TRP C 285       77.34   -112.46                                   
REMARK 500    ASP D  34     -119.80     56.16                                   
REMARK 500    THR D 115      -51.40   -139.37                                   
REMARK 500    ASP D 123     -124.39     52.67                                   
REMARK 500    ASP D 147      -39.98     71.08                                   
REMARK 500    ASP D 177      -36.63     76.75                                   
REMARK 500    SER D 258     -114.95   -127.84                                   
REMARK 500    TRP D 285       77.12   -110.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7JQX A    1   309  UNP    B4EJL9   B4EJL9_BURCJ     1    309             
DBREF  7JQX B    1   309  UNP    B4EJL9   B4EJL9_BURCJ     1    309             
DBREF  7JQX C    1   309  UNP    B4EJL9   B4EJL9_BURCJ     1    309             
DBREF  7JQX D    1   309  UNP    B4EJL9   B4EJL9_BURCJ     1    309             
SEQRES   1 A  309  MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET          
SEQRES   2 A  309  PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE          
SEQRES   3 A  309  SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS          
SEQRES   4 A  309  TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL          
SEQRES   5 A  309  LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG          
SEQRES   6 A  309  HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL          
SEQRES   7 A  309  VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS          
SEQRES   8 A  309  PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP          
SEQRES   9 A  309  ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE          
SEQRES  10 A  309  HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR          
SEQRES  11 A  309  ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU          
SEQRES  12 A  309  ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP          
SEQRES  13 A  309  ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS          
SEQRES  14 A  309  PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU          
SEQRES  15 A  309  ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR          
SEQRES  16 A  309  LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE          
SEQRES  17 A  309  ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU          
SEQRES  18 A  309  ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP          
SEQRES  19 A  309  GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO          
SEQRES  20 A  309  MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY          
SEQRES  21 A  309  ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP          
SEQRES  22 A  309  VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU          
SEQRES  23 A  309  PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU          
SEQRES  24 A  309  ASP PHE PHE ARG GLU ALA ALA SER GLY ARG                      
SEQRES   1 B  309  MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET          
SEQRES   2 B  309  PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE          
SEQRES   3 B  309  SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS          
SEQRES   4 B  309  TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL          
SEQRES   5 B  309  LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG          
SEQRES   6 B  309  HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL          
SEQRES   7 B  309  VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS          
SEQRES   8 B  309  PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP          
SEQRES   9 B  309  ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE          
SEQRES  10 B  309  HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR          
SEQRES  11 B  309  ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU          
SEQRES  12 B  309  ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP          
SEQRES  13 B  309  ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS          
SEQRES  14 B  309  PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU          
SEQRES  15 B  309  ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR          
SEQRES  16 B  309  LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE          
SEQRES  17 B  309  ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU          
SEQRES  18 B  309  ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP          
SEQRES  19 B  309  GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO          
SEQRES  20 B  309  MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY          
SEQRES  21 B  309  ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP          
SEQRES  22 B  309  VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU          
SEQRES  23 B  309  PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU          
SEQRES  24 B  309  ASP PHE PHE ARG GLU ALA ALA SER GLY ARG                      
SEQRES   1 C  309  MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET          
SEQRES   2 C  309  PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE          
SEQRES   3 C  309  SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS          
SEQRES   4 C  309  TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL          
SEQRES   5 C  309  LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG          
SEQRES   6 C  309  HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL          
SEQRES   7 C  309  VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS          
SEQRES   8 C  309  PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP          
SEQRES   9 C  309  ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE          
SEQRES  10 C  309  HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR          
SEQRES  11 C  309  ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU          
SEQRES  12 C  309  ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP          
SEQRES  13 C  309  ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS          
SEQRES  14 C  309  PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU          
SEQRES  15 C  309  ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR          
SEQRES  16 C  309  LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE          
SEQRES  17 C  309  ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU          
SEQRES  18 C  309  ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP          
SEQRES  19 C  309  GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO          
SEQRES  20 C  309  MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY          
SEQRES  21 C  309  ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP          
SEQRES  22 C  309  VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU          
SEQRES  23 C  309  PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU          
SEQRES  24 C  309  ASP PHE PHE ARG GLU ALA ALA SER GLY ARG                      
SEQRES   1 D  309  MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET          
SEQRES   2 D  309  PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE          
SEQRES   3 D  309  SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS          
SEQRES   4 D  309  TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL          
SEQRES   5 D  309  LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG          
SEQRES   6 D  309  HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL          
SEQRES   7 D  309  VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS          
SEQRES   8 D  309  PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP          
SEQRES   9 D  309  ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE          
SEQRES  10 D  309  HIS LEU VAL GLY ARG ASP ILE GLY VAL MET VAL ALA TYR          
SEQRES  11 D  309  ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU          
SEQRES  12 D  309  ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP          
SEQRES  13 D  309  ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS          
SEQRES  14 D  309  PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU          
SEQRES  15 D  309  ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR          
SEQRES  16 D  309  LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE          
SEQRES  17 D  309  ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU          
SEQRES  18 D  309  ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP          
SEQRES  19 D  309  GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO          
SEQRES  20 D  309  MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY          
SEQRES  21 D  309  ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP          
SEQRES  22 D  309  VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU          
SEQRES  23 D  309  PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU          
SEQRES  24 D  309  ASP PHE PHE ARG GLU ALA ALA SER GLY ARG                      
FORMUL   5  HOH   *604(H2 O)                                                    
HELIX    1 AA1 GLY A   21  ARG A   25  1                                   5    
HELIX    2 AA2 THR A   60  ARG A   65  5                                   6    
HELIX    3 AA3 VAL A   67  ASP A   74  1                                   8    
HELIX    4 AA4 ASP A   97  LEU A  112  1                                  16    
HELIX    5 AA5 ASP A  123  TRP A  136  1                                  14    
HELIX    6 AA6 THR A  153  ALA A  163  1                                  11    
HELIX    7 AA7 ASP A  164  ILE A  167  5                                   4    
HELIX    8 AA8 TRP A  168  GLN A  174  1                                   7    
HELIX    9 AA9 ASP A  177  ALA A  184  1                                   8    
HELIX   10 AB1 LYS A  186  THR A  199  1                                  14    
HELIX   11 AB2 SER A  204  ALA A  216  1                                  13    
HELIX   12 AB3 GLY A  219  ALA A  230  1                                  12    
HELIX   13 AB4 ALA A  230  MET A  242  1                                  13    
HELIX   14 AB5 ALA A  261  GLU A  269  1                                   9    
HELIX   15 AB6 TRP A  285  ASN A  290  1                                   6    
HELIX   16 AB7 ASN A  290  GLU A  304  1                                  15    
HELIX   17 AB8 GLY B   21  ARG B   25  1                                   5    
HELIX   18 AB9 THR B   60  ARG B   65  5                                   6    
HELIX   19 AC1 VAL B   67  ASP B   74  1                                   8    
HELIX   20 AC2 ASP B   97  LEU B  112  1                                  16    
HELIX   21 AC3 ASP B  123  TRP B  136  1                                  14    
HELIX   22 AC4 THR B  153  SER B  162  1                                  10    
HELIX   23 AC5 ASP B  164  ILE B  167  5                                   4    
HELIX   24 AC6 TRP B  168  GLN B  174  1                                   7    
HELIX   25 AC7 ASP B  177  ALA B  184  1                                   8    
HELIX   26 AC8 LYS B  186  THR B  199  1                                  14    
HELIX   27 AC9 SER B  204  ALA B  216  1                                  13    
HELIX   28 AD1 GLY B  219  ALA B  230  1                                  12    
HELIX   29 AD2 ALA B  230  MET B  242  1                                  13    
HELIX   30 AD3 ALA B  261  GLU B  269  1                                   9    
HELIX   31 AD4 TRP B  285  ASN B  290  1                                   6    
HELIX   32 AD5 ASN B  290  GLU B  304  1                                  15    
HELIX   33 AD6 GLY C   21  ARG C   25  1                                   5    
HELIX   34 AD7 THR C   60  ARG C   65  5                                   6    
HELIX   35 AD8 VAL C   67  ASP C   74  1                                   8    
HELIX   36 AD9 ASP C   97  LEU C  112  1                                  16    
HELIX   37 AE1 ASP C  123  TRP C  136  1                                  14    
HELIX   38 AE2 THR C  153  SER C  162  1                                  10    
HELIX   39 AE3 ASP C  164  ILE C  167  5                                   4    
HELIX   40 AE4 TRP C  168  GLN C  174  1                                   7    
HELIX   41 AE5 ASP C  177  ALA C  184  1                                   8    
HELIX   42 AE6 LYS C  186  THR C  199  1                                  14    
HELIX   43 AE7 SER C  204  ALA C  216  1                                  13    
HELIX   44 AE8 GLY C  219  ALA C  230  1                                  12    
HELIX   45 AE9 ALA C  230  MET C  242  1                                  13    
HELIX   46 AF1 ALA C  261  GLU C  269  1                                   9    
HELIX   47 AF2 TRP C  285  ASN C  290  1                                   6    
HELIX   48 AF3 ASN C  290  GLU C  304  1                                  15    
HELIX   49 AF4 GLY D   21  PHE D   26  1                                   6    
HELIX   50 AF5 THR D   60  ARG D   65  5                                   6    
HELIX   51 AF6 VAL D   67  ASP D   74  1                                   8    
HELIX   52 AF7 ASP D   97  LEU D  112  1                                  16    
HELIX   53 AF8 ASP D  123  TRP D  136  1                                  14    
HELIX   54 AF9 THR D  153  SER D  162  1                                  10    
HELIX   55 AG1 ASP D  164  ILE D  167  5                                   4    
HELIX   56 AG2 TRP D  168  GLN D  174  1                                   7    
HELIX   57 AG3 ASP D  177  ALA D  184  1                                   8    
HELIX   58 AG4 LYS D  186  THR D  199  1                                  14    
HELIX   59 AG5 SER D  204  ALA D  216  1                                  13    
HELIX   60 AG6 GLY D  219  ALA D  230  1                                  12    
HELIX   61 AG7 ALA D  230  MET D  242  1                                  13    
HELIX   62 AG8 ALA D  261  GLU D  269  1                                   9    
HELIX   63 AG9 TRP D  285  ASN D  290  1                                   6    
HELIX   64 AH1 ASN D  290  GLU D  304  1                                  15    
SHEET    1 AA1 8 PHE A  26  GLN A  32  0                                        
SHEET    2 AA1 8 ARG A  37  GLY A  43 -1  O  LEU A  38   N  ALA A  31           
SHEET    3 AA1 8 ARG A  77  ASP A  82 -1  O  ASP A  82   N  HIS A  39           
SHEET    4 AA1 8 MET A  50  LEU A  54  1  N  VAL A  51   O  ARG A  77           
SHEET    5 AA1 8 ILE A 117  ARG A 122  1  O  VAL A 120   N  VAL A  52           
SHEET    6 AA1 8 ILE A 140  LEU A 146  1  O  ALA A 144   N  LEU A 119           
SHEET    7 AA1 8 VAL A 250  GLY A 255  1  O  LEU A 251   N  MET A 145           
SHEET    8 AA1 8 VAL A 274  ALA A 279  1  O  ALA A 279   N  ALA A 254           
SHEET    1 AA2 8 PHE B  26  GLN B  32  0                                        
SHEET    2 AA2 8 ARG B  37  GLY B  43 -1  O  LEU B  38   N  ALA B  31           
SHEET    3 AA2 8 ARG B  77  ASP B  82 -1  O  ALA B  80   N  VAL B  41           
SHEET    4 AA2 8 MET B  50  LEU B  54  1  N  VAL B  51   O  ARG B  77           
SHEET    5 AA2 8 ILE B 117  ARG B 122  1  O  HIS B 118   N  VAL B  52           
SHEET    6 AA2 8 ILE B 140  LEU B 146  1  O  ALA B 144   N  LEU B 119           
SHEET    7 AA2 8 VAL B 250  GLY B 255  1  O  LEU B 251   N  MET B 145           
SHEET    8 AA2 8 VAL B 274  ALA B 279  1  O  ALA B 279   N  ALA B 254           
SHEET    1 AA3 8 PHE C  26  GLN C  32  0                                        
SHEET    2 AA3 8 ARG C  37  GLY C  43 -1  O  TYR C  40   N  ARG C  29           
SHEET    3 AA3 8 ARG C  77  ASP C  82 -1  O  ALA C  80   N  VAL C  41           
SHEET    4 AA3 8 MET C  50  LEU C  54  1  N  VAL C  51   O  VAL C  79           
SHEET    5 AA3 8 ILE C 117  ARG C 122  1  O  HIS C 118   N  VAL C  52           
SHEET    6 AA3 8 ILE C 140  LEU C 146  1  O  VAL C 141   N  ILE C 117           
SHEET    7 AA3 8 VAL C 250  GLY C 255  1  O  LEU C 251   N  MET C 145           
SHEET    8 AA3 8 VAL C 274  ALA C 279  1  O  ARG C 275   N  VAL C 250           
SHEET    1 AA4 8 SER D  27  LEU D  33  0                                        
SHEET    2 AA4 8 VAL D  36  GLY D  43 -1  O  TYR D  40   N  ARG D  29           
SHEET    3 AA4 8 ARG D  77  ASP D  82 -1  O  ALA D  80   N  VAL D  41           
SHEET    4 AA4 8 MET D  50  LEU D  54  1  N  VAL D  51   O  ARG D  77           
SHEET    5 AA4 8 ILE D 117  ARG D 122  1  O  HIS D 118   N  MET D  50           
SHEET    6 AA4 8 ILE D 140  LEU D 146  1  O  ALA D 144   N  LEU D 119           
SHEET    7 AA4 8 VAL D 250  GLY D 255  1  O  LEU D 251   N  MET D 145           
SHEET    8 AA4 8 VAL D 274  ALA D 279  1  O  ALA D 279   N  ALA D 254           
CISPEP   1 TRP A   57    PRO A   58          0        -4.92                     
CISPEP   2 TRP B   57    PRO B   58          0        -3.46                     
CISPEP   3 TRP C   57    PRO C   58          0        -4.44                     
CISPEP   4 TRP D   57    PRO D   58          0        -3.19                     
CRYST1  132.150  132.150  341.700  90.00  90.00  90.00 I 4 2 2      64          
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      0.007567  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007567  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002927        0.00000                         
TER    2320      GLU A 304                                                      
TER    4640      GLU B 304                                                      
TER    6960      GLU C 304                                                      
TER    9280      GLU D 304                                                      
MASTER      403    0    0   64   32    0    0    6 9880    4    0   96          
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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