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LongText Report for: 3MVE-pdb

Name Class
3MVE-pdb
HEADER    LYASE                                   04-MAY-10   3MVE              
TITLE     CRYSTAL STRUCTURE OF A NOVEL PYRUVATE DECARBOXYLASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UPF0255 PROTEIN VV1_0328;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FRSA;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;                              
SOURCE   3 ORGANISM_TAXID: 672;                                                 
SOURCE   4 STRAIN: M06-24/0;                                                    
SOURCE   5 GENE: FRSA, VV1_0328;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    FRSA,FERMENTATION/RESPIRATION SWITCH PROTEIN, HYDROLASE ACTIVATOR,    
KEYWDS   2 LYASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.CHA,C.S.JEONG,Y.J.AN                                              
REVDAT   2   08-JUN-11 3MVE    1       JRNL                                     
REVDAT   1   18-MAY-11 3MVE    0                                                
JRNL        AUTH   K.J.LEE,C.S.JEONG,Y.J.AN,H.J.LEE,S.J.PARK,Y.J.SEOK,P.KIM,    
JRNL        AUTH 2 J.H.LEE,K.H.LEE,S.S.CHA                                      
JRNL        TITL   FRSA FUNCTIONS AS A COFACTOR-INDEPENDENT DECARBOXYLASE TO    
JRNL        TITL 2 CONTROL METABOLIC FLUX.                                      
JRNL        REF    NAT.CHEM.BIOL.                             2011              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   21623357                                                     
JRNL        DOI    10.1038/NCHEMBIO.589                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.100                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 80851.970                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 39288                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1962                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5805                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 303                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6136                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 304                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.56000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -2.56000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.72000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 41.07                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : EDO.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : EDO.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MVE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059041.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ELECTRON MICROSCOPE                
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : PHOTON FACTORY BEAMLINE BL-17A     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41404                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.4                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AM-SULFATE, 0.1M TRIS-HCL (PH       
REMARK 280  8.5), 0.2M NA-ACETATE, MICRO BATH, TEMPERATURE 295K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       44.10050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     THR B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     PHE B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     LYS A  43    CG   CD   CE   NZ                                   
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A  57    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  57    CZ3  CH2                                            
REMARK 470     ARG A 104    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 141    CG   CD   CE   NZ                                   
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     GLU A 242    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 355    CG   CD   CE   NZ                                   
REMARK 470     LYS A 385    CG   CD   CE   NZ                                   
REMARK 470     ILE A 394    CG1  CG2  CD1                                       
REMARK 470     GLU A 399    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 400    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 403    CG   OD1  OD2                                       
REMARK 470     LYS A 407    CG   CD   CE   NZ                                   
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     GLU B  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     ARG B 104    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     ARG B 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 115    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 179    CG   CD   CE   NZ                                   
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     SER B 351    OG                                                  
REMARK 470     ARG B 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 363    CG   CD1  CD2                                       
REMARK 470     GLU B 364    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 385    CG   CD   CE   NZ                                   
REMARK 470     LYS B 387    CG   CD   CE   NZ                                   
REMARK 470     LYS B 388    CG   CD   CE   NZ                                   
REMARK 470     LYS B 392    CG   CD   CE   NZ                                   
REMARK 470     LEU B 402    CG   CD1  CD2                                       
REMARK 470     LEU B 404    CG   CD1  CD2                                       
REMARK 470     LYS B 407    CG   CD   CE   NZ                                   
REMARK 470     GLU B 410    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 415    CG   CD   NE   CZ   NH1  NH2                        
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    ASN A 118     -133.62     50.83                                   
REMARK 500    HIS A 216      -63.13   -124.94                                   
REMARK 500    SER A 231        0.88     81.74                                   
REMARK 500    THR A 241     -160.80    -67.97                                   
REMARK 500    ARG A 272     -131.08     51.54                                   
REMARK 500    HIS A 300      -51.50   -152.13                                   
REMARK 500    LEU A 349       73.60   -104.02                                   
REMARK 500    SER A 350      -51.72   -158.50                                   
REMARK 500    SER A 351     -107.44    -88.06                                   
REMARK 500    SER A 390       -5.78    -53.26                                   
REMARK 500    LYS B 191      157.58    178.55                                   
REMARK 500    HIS B 216      -80.83   -131.49                                   
REMARK 500    SER B 231       -0.10     85.71                                   
REMARK 500    THR B 241      175.81     63.32                                   
REMARK 500    ASP B 243       65.25   -103.91                                   
REMARK 500    ARG B 272     -127.42     54.35                                   
REMARK 500    HIS B 300      -57.52   -154.69                                   
REMARK 500    SER B 327      -76.62    -69.84                                   
REMARK 500    SER B 350      -57.11   -148.91                                   
REMARK 500    SER B 351     -111.28    -87.24                                   
REMARK 500    TYR B 383       17.09     86.97                                   
REMARK 500    LYS B 392      -27.64     73.49                                   
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 A 432        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 434        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B 574        DISTANCE =  5.72 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 421                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 422                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 423                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 424                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 421                 
DBREF  3MVE A    1   415  UNP    Q8DF91   Y328_VIBVU       1    415             
DBREF  3MVE B    1   415  UNP    Q8DF91   Y328_VIBVU       1    415             
SEQRES   1 A  415  MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU          
SEQRES   2 A  415  PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU          
SEQRES   3 A  415  THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU          
SEQRES   4 A  415  ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU          
SEQRES   5 A  415  ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE          
SEQRES   6 A  415  GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS          
SEQRES   7 A  415  HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET          
SEQRES   8 A  415  GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG          
SEQRES   9 A  415  LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR          
SEQRES  10 A  415  ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU          
SEQRES  11 A  415  CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP          
SEQRES  12 A  415  ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA          
SEQRES  13 A  415  TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS          
SEQRES  14 A  415  GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA          
SEQRES  15 A  415  HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL          
SEQRES  16 A  415  VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP          
SEQRES  17 A  415  MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP          
SEQRES  18 A  415  ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR          
SEQRES  19 A  415  SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU          
SEQRES  20 A  415  HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR          
SEQRES  21 A  415  VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE          
SEQRES  22 A  415  GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN          
SEQRES  23 A  415  GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE          
SEQRES  24 A  415  HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET          
SEQRES  25 A  415  PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY          
SEQRES  26 A  415  LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET          
SEQRES  27 A  415  ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER          
SEQRES  28 A  415  ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU          
SEQRES  29 A  415  GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL          
SEQRES  30 A  415  ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER          
SEQRES  31 A  415  SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP          
SEQRES  32 A  415  LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG              
SEQRES   1 B  415  MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU          
SEQRES   2 B  415  PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU          
SEQRES   3 B  415  THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU          
SEQRES   4 B  415  ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU          
SEQRES   5 B  415  ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE          
SEQRES   6 B  415  GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS          
SEQRES   7 B  415  HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET          
SEQRES   8 B  415  GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG          
SEQRES   9 B  415  LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR          
SEQRES  10 B  415  ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU          
SEQRES  11 B  415  CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP          
SEQRES  12 B  415  ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA          
SEQRES  13 B  415  TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS          
SEQRES  14 B  415  GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA          
SEQRES  15 B  415  HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL          
SEQRES  16 B  415  VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP          
SEQRES  17 B  415  MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP          
SEQRES  18 B  415  ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR          
SEQRES  19 B  415  SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU          
SEQRES  20 B  415  HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR          
SEQRES  21 B  415  VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE          
SEQRES  22 B  415  GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN          
SEQRES  23 B  415  GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE          
SEQRES  24 B  415  HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET          
SEQRES  25 B  415  PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY          
SEQRES  26 B  415  LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET          
SEQRES  27 B  415  ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER          
SEQRES  28 B  415  ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU          
SEQRES  29 B  415  GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL          
SEQRES  30 B  415  ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER          
SEQRES  31 B  415  SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP          
SEQRES  32 B  415  LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG              
HET    SO4  A 416       5                                                       
HET    EDO  A 417       4                                                       
HET    EDO  A 418       4                                                       
HET    EDO  A 419       4                                                       
HET    EDO  A 420       4                                                       
HET    EDO  A 421       4                                                       
HET    EDO  A 422       4                                                       
HET    EDO  A 423       4                                                       
HET    EDO  A 424       4                                                       
HET    SO4  B 416       5                                                       
HET    SO4  B 417       5                                                       
HET    SO4  B 418       5                                                       
HET    SO4  B 419       5                                                       
HET    EDO  B 420       4                                                       
HET    EDO  B 421       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   4  EDO    10(C2 H6 O2)                                                 
FORMUL  18  HOH   *304(H2 O)                                                    
HELIX    1   1 GLU A   22  LEU A   26  5                                   5    
HELIX    2   2 MET A   30  GLY A   45  1                                  16    
HELIX    3   3 ASN A   51  GLN A   56  1                                   6    
HELIX    4   4 TRP A   57  GLY A   61  5                                   5    
HELIX    5   5 ASP A   63  SER A   77  1                                  15    
HELIX    6   6 ASN A   97  GLY A  114  1                                  18    
HELIX    7   7 THR A  117  TYR A  137  1                                  21    
HELIX    8   8 ASP A  143  SER A  164  1                                  22    
HELIX    9   9 LEU A  205  ASP A  208  5                                   4    
HELIX   10  10 MET A  209  HIS A  216  1                                   8    
HELIX   11  11 LEU A  217  ASP A  221  5                                   5    
HELIX   12  12 VAL A  232  SER A  236  5                                   5    
HELIX   13  13 SER A  245  LEU A  255  1                                  11    
HELIX   14  14 PHE A  256  ILE A  258  5                                   3    
HELIX   15  15 ARG A  272  GLU A  285  1                                  14    
HELIX   16  16 HIS A  300  SER A  305  1                                   6    
HELIX   17  17 SER A  305  GLN A  310  1                                   6    
HELIX   18  18 PRO A  313  LEU A  324  1                                  12    
HELIX   19  19 ASP A  330  MET A  338  1                                   9    
HELIX   20  20 ALA A  339  SER A  342  5                                   4    
HELIX   21  21 PRO A  370  PHE A  380  1                                  11    
HELIX   22  22 THR A  393  LEU A  414  1                                  22    
HELIX   23  23 GLU B   22  LEU B   26  5                                   5    
HELIX   24  24 MET B   30  GLY B   45  1                                  16    
HELIX   25  25 ARG B   53  GLN B   60  1                                   8    
HELIX   26  26 ASP B   63  SER B   77  1                                  15    
HELIX   27  27 ASN B   97  ALA B  113  1                                  17    
HELIX   28  28 GLY B  114  MET B  116  5                                   3    
HELIX   29  29 THR B  117  TYR B  137  1                                  21    
HELIX   30  30 ASP B  143  SER B  164  1                                  22    
HELIX   31  31 LEU B  205  ASP B  208  5                                   4    
HELIX   32  32 MET B  209  ASP B  215  1                                   7    
HELIX   33  33 HIS B  216  ASP B  221  5                                   6    
HELIX   34  34 VAL B  232  SER B  236  5                                   5    
HELIX   35  35 SER B  245  LEU B  255  1                                  11    
HELIX   36  36 PHE B  256  ILE B  258  5                                   3    
HELIX   37  37 ARG B  272  GLU B  285  1                                  14    
HELIX   38  38 GLN B  286  ILE B  289  5                                   4    
HELIX   39  39 HIS B  300  SER B  305  1                                   6    
HELIX   40  40 SER B  305  GLN B  310  1                                   6    
HELIX   41  41 PRO B  313  LEU B  324  1                                  12    
HELIX   42  42 ASP B  330  MET B  338  1                                   9    
HELIX   43  43 ALA B  339  SER B  342  5                                   4    
HELIX   44  44 PRO B  370  PHE B  380  1                                  11    
HELIX   45  45 GLY B  397  ARG B  415  1                                  19    
SHEET    1   A 8 ILE A 167  PRO A 174  0                                        
SHEET    2   A 8 LYS A 179  LEU A 186 -1  O  ALA A 182   N  LEU A 171           
SHEET    3   A 8 ALA A 223  VAL A 227 -1  O  MET A 224   N  HIS A 185           
SHEET    4   A 8 HIS A 193  SER A 199  1  N  PRO A 194   O  ALA A 223           
SHEET    5   A 8 VAL A 261  PHE A 271  1  O  PHE A 271   N  SER A 199           
SHEET    6   A 8 ALA A 291  LEU A 295  1  O  VAL A 293   N  LEU A 268           
SHEET    7   A 8 ILE A 358  LEU A 363  1  O  LEU A 359   N  ILE A 294           
SHEET    8   A 8 LYS A 385  ILE A 389  1  O  LYS A 385   N  ALA A 360           
SHEET    1   B 2 GLN B  28  TYR B  29  0                                        
SHEET    2   B 2 VAL B 328  VAL B 329  1  O  VAL B 329   N  GLN B  28           
SHEET    1   C 8 ILE B 167  PHE B 175  0                                        
SHEET    2   C 8 GLY B 178  LEU B 186 -1  O  ALA B 182   N  LEU B 171           
SHEET    3   C 8 ALA B 223  VAL B 227 -1  O  MET B 224   N  HIS B 185           
SHEET    4   C 8 HIS B 193  SER B 199  1  N  VAL B 196   O  LEU B 225           
SHEET    5   C 8 VAL B 261  PHE B 271  1  O  GLY B 267   N  VAL B 195           
SHEET    6   C 8 ALA B 291  LEU B 295  1  O  VAL B 293   N  LEU B 268           
SHEET    7   C 8 ILE B 358  LEU B 363  1  O  LEU B 359   N  CYS B 292           
SHEET    8   C 8 LYS B 385  ILE B 389  1  O  LYS B 385   N  ALA B 360           
CISPEP   1 TYR A  137    PRO A  138          0         0.20                     
CISPEP   2 TYR B  137    PRO B  138          0         0.60                     
SITE     1 AC1  5 HIS A  79  SER A  80  HIS A  94  HOH A 521                    
SITE     2 AC1  5 HOH A 551                                                     
SITE     1 AC2  5 GLY A 201  LEU A 202  ARG A 272  PHE A 273                    
SITE     2 AC2  5 TYR A 316                                                     
SITE     1 AC3  8 TYR A  93  THR A 103  MET A 107  EDO A 419                    
SITE     2 AC3  8 HOH A 543  GLN B 110  SER B 155  HOH B 504                    
SITE     1 AC4  6 TYR A  93  THR A 103  LEU A 145  LEU A 152                    
SITE     2 AC4  6 EDO A 418  SER B 155                                          
SITE     1 AC5  7 LEU A 125  GLU A 159  LYS A 162  LYS A 163                    
SITE     2 AC5  7 HOH A 554  GLY B  92  TYR B  93                               
SITE     1 AC6  4 PHE A  46  SER A  47  TRP A  48  HOH A 562                    
SITE     1 AC7  4 PHE A 283  GLY A 347  PHE A 348  ARG A 352                    
SITE     1 AC8  7 SER A  77  LYS A  78  HIS A  79  SER A  95                    
SITE     2 AC8  7 GLY A  96  HOH A 508  HOH A 571                               
SITE     1 AC9 10 LYS A  21  GLU A  22  THR A  23  ARG A  50                    
SITE     2 AC9 10 ASN A  97  TRP A  98  ALA A  99  LEU A 145                    
SITE     3 AC9 10 HOH A 505  HOH A 545                                          
SITE     1 BC1  4 HIS B  79  SER B  80  HOH B 452  HOH B 453                    
SITE     1 BC2  6 GLY B 201  LEU B 202  ASP B 203  ARG B 272                    
SITE     2 BC2  6 PHE B 273  HOH B 522                                          
SITE     1 BC3  3 LYS B 179  LYS B 237  HOH B 549                               
SITE     1 BC4  6 HIS B 216  HIS B 220  ILE B 222  ILE B 406                    
SITE     2 BC4  6 LYS B 407  GLU B 410                                          
SITE     1 BC5 10 GLU B  22  THR B  23  ARG B  50  ASN B  97                    
SITE     2 BC5 10 ALA B  99  LEU B 145  HOH B 438  HOH B 456                    
SITE     3 BC5 10 HOH B 463  HOH B 565                                          
SITE     1 BC6  7 VAL B  58  GLY B  61  VAL B  62  ASP B  63                    
SITE     2 BC6  7 ARG B 211  HOH B 449  HOH B 557                               
CRYST1   60.834   88.201   79.629  90.00 106.62  90.00 P 1 21 1      4          
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      0.016438  0.000000  0.004906        0.00000                         
SCALE2      0.000000  0.011338  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013106        0.00000                         
TER    3080      ARG A 415                                                      
TER    6138      ARG B 415                                                      
MASTER      421    0   15   45   18    0   28    6 6505    2   65   64          
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:
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