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LongText Report for: 4I4C-pdb

Name Class
4I4C-pdb
HEADER    UNKNOWN FUNCTION                        27-NOV-12   4I4C              
TITLE     CRYSTAL STRUCTURE OF THE PROTEIN FRSA COMPLEXED WITH UNKNOWN LIGAND   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UPF0255 PROTEIN FRSA;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;                              
SOURCE   3 ORGANISM_TAXID: 672;                                                 
SOURCE   4 GENE: FRSA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TWO-DOMAIN PROTEIN FRSA, UNKNOWN FUNCTION, UNKNOWN LIGAND             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.FEDOROV,E.V.FEDOROV,B.DESAI,J.A.GERLT,N.RICHARDS,S.C.ALMO         
REVDAT   1   09-OCT-13 4I4C    0                                                
JRNL        AUTH   W.F.KELLETT,E.BRUNK,B.J.DESAI,A.A.FEDOROV,S.C.ALMO,          
JRNL        AUTH 2 J.A.GERLT,U.ROTHLISBERGER,N.G.RICHARDS                       
JRNL        TITL   COMPUTATIONAL, STRUCTURAL, AND KINETIC EVIDENCE THAT VIBRIO  
JRNL        TITL 2 VULNIFICUS FRSA IS NOT A COFACTOR-INDEPENDENT PYRUVATE       
JRNL        TITL 3 DECARBOXYLASE.                                               
JRNL        REF    BIOCHEMISTRY                  V.  52  1842 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23452154                                                     
JRNL        DOI    10.1021/BI400093Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 51363                          
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) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2608                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.2916 -  5.1993    1.00     2672   142  0.1465 0.1586        
REMARK   3     2  5.1993 -  4.1284    1.00     2634   153  0.1342 0.1827        
REMARK   3     3  4.1284 -  3.6070    1.00     2611   143  0.1487 0.1790        
REMARK   3     4  3.6070 -  3.2774    0.98     2606   117  0.1751 0.2431        
REMARK   3     5  3.2774 -  3.0426    0.96     2522   146  0.1922 0.2279        
REMARK   3     6  3.0426 -  2.8633    0.96     2526   128  0.1890 0.2432        
REMARK   3     7  2.8633 -  2.7199    0.96     2529   158  0.2015 0.2258        
REMARK   3     8  2.7199 -  2.6015    0.97     2549   130  0.1965 0.2602        
REMARK   3     9  2.6015 -  2.5014    0.97     2511   140  0.2060 0.3009        
REMARK   3    10  2.5014 -  2.4151    0.98     2574   143  0.2110 0.2397        
REMARK   3    11  2.4151 -  2.3396    0.98     2550   135  0.2067 0.3044        
REMARK   3    12  2.3396 -  2.2727    0.97     2556   139  0.2049 0.2838        
REMARK   3    13  2.2727 -  2.2129    0.98     2567   115  0.2050 0.2633        
REMARK   3    14  2.2129 -  2.1589    0.98     2550   152  0.2044 0.2806        
REMARK   3    15  2.1589 -  2.1098    0.98     2553   129  0.2125 0.2783        
REMARK   3    16  2.1098 -  2.0649    0.98     2567   153  0.2193 0.3182        
REMARK   3    17  2.0649 -  2.0236    0.98     2567   130  0.2290 0.3061        
REMARK   3    18  2.0236 -  1.9855    0.98     2571   131  0.2346 0.3002        
REMARK   3    19  1.9855 -  1.9500    0.98     2540   124  0.2465 0.2882        
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) : 25.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.008           6609                                  
REMARK   3   ANGLE     :  1.053           8925                                  
REMARK   3   CHIRALITY :  0.072            972                                  
REMARK   3   PLANARITY :  0.004           1125                                  
REMARK   3   DIHEDRAL  : 15.081           2469                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3107  17.1156  81.7416              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1446 T22:   0.1183                                     
REMARK   3      T33:   0.1497 T12:  -0.0025                                     
REMARK   3      T13:  -0.0206 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9237 L22:   1.4985                                     
REMARK   3      L33:   1.2091 L12:  -0.2360                                     
REMARK   3      L13:  -0.1698 L23:   0.5780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0616 S12:   0.0112 S13:  -0.0899                       
REMARK   3      S21:  -0.2386 S22:   0.0031 S23:  -0.0397                       
REMARK   3      S31:   0.0035 S32:  -0.0474 S33:  -0.0544                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5066  36.7994  41.7463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1432 T22:   0.1457                                     
REMARK   3      T33:   0.1266 T12:  -0.0159                                     
REMARK   3      T13:   0.0154 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7679 L22:   1.6510                                     
REMARK   3      L33:   0.6416 L12:   0.0877                                     
REMARK   3      L13:   0.2143 L23:   0.1930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0387 S12:  -0.0708 S13:   0.0329                       
REMARK   3      S21:   0.2413 S22:  -0.0406 S23:  -0.0278                       
REMARK   3      S31:   0.0369 S32:  -0.0682 S33:   0.0043                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4I4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076287.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51363                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.284                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: BALBES                                                
REMARK 200 STARTING MODEL: 3MVE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MONOMETHYL ETHER 2000, 0.1M      
REMARK 280  TRIS, 0.2M TRIMETHYLAMINE N-OXIDE, PH 8.5, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 293.0K                                    
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       52.27100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     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 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     -118.76     54.73                                   
REMARK 500    PHE A 175      118.63   -170.71                                   
REMARK 500    LYS A 177       -7.64     70.92                                   
REMARK 500    HIS A 216      -67.95   -134.51                                   
REMARK 500    SER A 231      -10.21     89.26                                   
REMARK 500    ARG A 272     -137.44     48.79                                   
REMARK 500    HIS A 300      -53.78   -153.57                                   
REMARK 500    SER A 351      -48.82   -142.60                                   
REMARK 500    LEU A 414       42.21    -89.53                                   
REMARK 500    GLN B  19       35.15    -96.82                                   
REMARK 500    PHE B 175      121.98   -173.84                                   
REMARK 500    HIS B 216      -65.23   -131.35                                   
REMARK 500    LYS B 219      -19.80    -49.41                                   
REMARK 500    SER B 231       -5.40     82.56                                   
REMARK 500    THR B 241     -164.11   -109.07                                   
REMARK 500    ASP B 243       63.81   -100.58                                   
REMARK 500    ARG B 272     -130.52     47.79                                   
REMARK 500    HIS B 300      -56.54   -151.39                                   
REMARK 500    SER B 350      -52.81   -124.56                                   
REMARK 500    SER B 351      -53.59   -143.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PG B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NA B 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MVE   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER LIGANDS                      
REMARK 900 RELATED ID: 3OUR   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER PROTEIN                      
DBREF  4I4C A    1   415  UNP    D9IR22   D9IR22_VIBVL     1    415             
DBREF  4I4C B    1   415  UNP    D9IR22   D9IR22_VIBVL     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    1PG  A 501      17                                                       
HET    6NA  A 502       8                                                       
HET    1PG  B 501      17                                                       
HET    GOL  B 502       6                                                       
HET    6NA  B 503       8                                                       
HETNAM     1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-           
HETNAM   2 1PG  ETHANOL                                                         
HETNAM     6NA HEXANOIC ACID                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  1PG    2(C11 H24 O6)                                                
FORMUL   4  6NA    2(C6 H12 O2)                                                 
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *274(H2 O)                                                    
HELIX    1   1 PHE A   14  LYS A   18  5                                   5    
HELIX    2   2 GLU A   22  LEU A   26  5                                   5    
HELIX    3   3 MET A   30  GLY A   45  1                                  16    
HELIX    4   4 ARG A   53  GLY A   61  1                                   9    
HELIX    5   5 ASP A   63  SER A   76  1                                  14    
HELIX    6   6 ASN A   97  GLU A  115  1                                  19    
HELIX    7   7 ALA A  120  TYR A  137  1                                  18    
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 SER A  305  GLN A  310  1                                   6    
HELIX   17  17 PRO A  313  LEU A  324  1                                  12    
HELIX   18  18 ASP A  330  MET A  338  1                                   9    
HELIX   19  19 ALA A  339  SER A  342  5                                   4    
HELIX   20  20 PRO A  370  PHE A  380  1                                  11    
HELIX   21  21 THR A  393  LEU A  414  1                                  22    
HELIX   22  22 GLU B   22  LEU B   26  5                                   5    
HELIX   23  23 MET B   30  GLY B   45  1                                  16    
HELIX   24  24 ARG B   53  GLY B   61  1                                   9    
HELIX   25  25 ASP B   63  SER B   76  1                                  14    
HELIX   26  26 ASN B   97  GLY B  114  1                                  18    
HELIX   27  27 THR B  117  TYR B  137  1                                  21    
HELIX   28  28 ASP B  143  SER B  164  1                                  22    
HELIX   29  29 LEU B  205  ASP B  208  5                                   4    
HELIX   30  30 MET B  209  HIS B  216  1                                   8    
HELIX   31  31 LEU B  217  ASP B  221  5                                   5    
HELIX   32  32 VAL B  232  SER B  236  5                                   5    
HELIX   33  33 SER B  245  ASN B  253  1                                   9    
HELIX   34  34 ARG B  272  GLU B  285  1                                  14    
HELIX   35  35 SER B  305  GLN B  310  1                                   6    
HELIX   36  36 PRO B  313  LEU B  324  1                                  12    
HELIX   37  37 ASP B  330  MET B  338  1                                   9    
HELIX   38  38 ALA B  339  SER B  342  5                                   4    
HELIX   39  39 PRO B  370  PHE B  380  1                                  11    
HELIX   40  40 THR B  393  LEU B  414  1                                  22    
SHEET    1   A 2 GLN A  28  TYR A  29  0                                        
SHEET    2   A 2 VAL A 328  VAL A 329  1  O  VAL A 329   N  GLN A  28           
SHEET    1   B 8 ILE A 167  PHE A 175  0                                        
SHEET    2   B 8 GLY A 178  LEU A 186 -1  O  LEU A 186   N  ILE A 167           
SHEET    3   B 8 ALA A 223  THR A 226 -1  O  MET A 224   N  HIS A 185           
SHEET    4   B 8 HIS A 193  SER A 199  1  N  PRO A 194   O  ALA A 223           
SHEET    5   B 8 VAL A 261  PHE A 271  1  O  GLY A 267   N  VAL A 195           
SHEET    6   B 8 ALA A 291  LEU A 295  1  O  VAL A 293   N  LEU A 268           
SHEET    7   B 8 ILE A 358  LEU A 363  1  O  LEU A 359   N  CYS A 292           
SHEET    8   B 8 LYS A 385  ILE A 389  1  O  LYS A 385   N  ALA A 360           
SHEET    1   C 8 ILE B 167  PHE B 175  0                                        
SHEET    2   C 8 GLY B 178  LEU B 186 -1  O  ILE B 180   N  ILE B 173           
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 ILE B 289  LEU B 295  1  O  LYS B 290   N  VAL B 266           
SHEET    7   C 8 ILE B 358  LEU B 363  1  O  LEU B 359   N  ILE B 294           
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         5.52                     
CISPEP   2 TYR B  137    PRO B  138          0         6.55                     
SITE     1 AC1  7 GLN A  56  TRP A  59  GLN A  60  MET A 209                    
SITE     2 AC1  7 LEU A 295  TYR A 398  LEU A 402                               
SITE     1 AC2  6 GLY A 201  LEU A 202  ARG A 272  PHE A 273                    
SITE     2 AC2  6 HOH A 652  HOH A 703                                          
SITE     1 AC3  8 TRP B  59  GLN B  60  LEU B 212  ARG B 272                    
SITE     2 AC3  8 LEU B 295  TYR B 398  LEU B 402  HOH B 626                    
SITE     1 AC4  2 LYS B 308  MET B 312                                          
SITE     1 AC5  6 GLY B 201  LEU B 202  ARG B 272  PHE B 273                    
SITE     2 AC5  6 LEU B 320  HOH B 664                                          
CRYST1   42.659  104.542   82.302  90.00  91.18  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      0.023442  0.000000  0.000483        0.00000                         
SCALE2      0.000000  0.009566  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012153        0.00000                         
TER    3212      ARG A 415                                                      
TER    6407      ARG B 415                                                      
MASTER      341    0    5   40   18    0    9    6 6715    2   56   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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