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LongText Report for: 4MEA-pdb

Name Class
4MEA-pdb
HEADER    HYDROLASE                               25-AUG-13   4MEA              
TITLE     CRYSTAL STRUCTURE OF THE CIF EPOXIDE HYDROLASE FROM ACINETOBACTER     
TITLE    2 NOSOCOMIALIS                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PREDICTED PROTEIN;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 25-349;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACINETOBACTER SP. RUH2624;                      
SOURCE   3 ORGANISM_TAXID: 575564;                                              
SOURCE   4 GENE: ACIF, HMPREF0014_00517;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PMQ70                                     
KEYWDS    ALPHA/BETA HYDROLASE FOLD, EPOXIDE HYDROLASE, SECRETED, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.BAHL,D.R.MADDEN                                                   
REVDAT   1   05-FEB-14 4MEA    0                                                
JRNL        AUTH   C.D.BAHL,K.L.HVORECNY,A.A.BRIDGES,A.E.BALLOK,J.M.BOMBERGER,  
JRNL        AUTH 2 K.C.CADY,G.A.O'TOOLE JR.,D.R.MADDEN                          
JRNL        TITL   SIGNATURE MOTIFS IDENTIFY AN ACINETOBACTER CIF VIRULENCE     
JRNL        TITL 2 FACTOR WITH EPOXIDE HYDROLASE ACTIVITY.                      
JRNL        REF    J.BIOL.CHEM.                               2014              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        DOI    10.1074/JBC.M113.518092                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
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) : 42.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 45523                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2296                            
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 42.4266 -  4.9112    0.99     2863   107  0.1850 0.2264        
REMARK   3     2  4.9112 -  3.8991    1.00     2644   229  0.1187 0.1423        
REMARK   3     3  3.8991 -  3.4064    1.00     2780   113  0.1307 0.1592        
REMARK   3     4  3.4064 -  3.0951    1.00     2726   113  0.1462 0.1786        
REMARK   3     5  3.0951 -  2.8733    1.00     2744   115  0.1404 0.1829        
REMARK   3     6  2.8733 -  2.7039    1.00     2614   233  0.1464 0.1811        
REMARK   3     7  2.7039 -  2.5685    1.00     2728   115  0.1472 0.1809        
REMARK   3     8  2.5685 -  2.4567    1.00     2703   117  0.1486 0.2060        
REMARK   3     9  2.4567 -  2.3622    1.00     2709   114  0.1429 0.1918        
REMARK   3    10  2.3622 -  2.2807    1.00     2643   185  0.1422 0.1956        
REMARK   3    11  2.2807 -  2.2094    1.00     2686   162  0.1407 0.2031        
REMARK   3    12  2.2094 -  2.1462    1.00     2698   115  0.1495 0.2153        
REMARK   3    13  2.1462 -  2.0897    1.00     2712   116  0.1482 0.1944        
REMARK   3    14  2.0897 -  2.0387    1.00     2657   153  0.1459 0.2433        
REMARK   3    15  2.0387 -  1.9924    1.00     2653   174  0.1586 0.2107        
REMARK   3    16  1.9924 -  1.9500    1.00     2667   135  0.1744 0.2552        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 40.29                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.510           
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) : 0.77910                                              
REMARK   3    B22 (A**2) : -0.45620                                             
REMARK   3    B33 (A**2) : -0.32280                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -3.17770                                             
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.007           5245                                  
REMARK   3   ANGLE     :  1.028           7112                                  
REMARK   3   CHIRALITY :  0.075            747                                  
REMARK   3   PLANARITY :  0.005            916                                  
REMARK   3   DIHEDRAL  : 11.685           1924                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 25:348)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7248   5.6928 -18.9426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0238 T22:   0.0303                                     
REMARK   3      T33:   0.0259 T12:  -0.0130                                     
REMARK   3      T13:  -0.0112 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0064 L22:   0.0041                                     
REMARK   3      L33:   0.0039 L12:   0.0016                                     
REMARK   3      L13:   0.0033 L23:   0.0004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:   0.0033 S13:   0.0078                       
REMARK   3      S21:   0.0051 S22:  -0.0058 S23:  -0.0111                       
REMARK   3      S31:  -0.0066 S32:   0.0070 S33:  -0.0216                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 26:348)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -44.2920  16.4001 -22.7176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0154 T22:   0.0065                                     
REMARK   3      T33:   0.0078 T12:  -0.0036                                     
REMARK   3      T13:   0.0044 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0137 L22:   0.0113                                     
REMARK   3      L33:   0.0056 L12:  -0.0064                                     
REMARK   3      L13:   0.0068 L23:  -0.0075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:  -0.0049 S13:  -0.0023                       
REMARK   3      S21:   0.0014 S22:   0.0014 S23:   0.0052                       
REMARK   3      S31:  -0.0017 S32:  -0.0029 S33:   0.0006                       
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 4MEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081801.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL CUT MONOCHROMATOR  
REMARK 200  OPTICS                         : TOROIDAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS-PACKAGE                        
REMARK 200  DATA SCALING SOFTWARE          : XDS-PACKAGE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45537                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3KD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MONOPOTASSIUM PHOSPHATE, 100 MM   
REMARK 280  SODIUM CITRATE, 20% PEG 4000, PH 4.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 291K                                              
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       21.29200            
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: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     LYS A   349                                                      
REMARK 465     HIS A   350                                                      
REMARK 465     HIS A   351                                                      
REMARK 465     HIS A   352                                                      
REMARK 465     HIS A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     LYS B   349                                                      
REMARK 465     HIS B   350                                                      
REMARK 465     HIS B   351                                                      
REMARK 465     HIS B   352                                                      
REMARK 465     HIS B   353                                                      
REMARK 465     HIS B   354                                                      
REMARK 465     HIS B   355                                                      
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    SER A  80      -64.61   -156.21                                   
REMARK 500    TYR A 130       31.69    -99.24                                   
REMARK 500    ASP A 158     -130.36     54.54                                   
REMARK 500    ASP A 182      -62.84     59.80                                   
REMARK 500    ASP A 223       78.68   -156.65                                   
REMARK 500    ASN A 283       30.52    -89.32                                   
REMARK 500    LYS A 285       40.84    -61.71                                   
REMARK 500    ASN A 301     -113.94     70.84                                   
REMARK 500    ASN A 335       58.71   -161.22                                   
REMARK 500    SER B  80      -66.74   -153.65                                   
REMARK 500    ASP B 158     -130.27     59.16                                   
REMARK 500    ASP B 182      -60.01     59.74                                   
REMARK 500    ASP B 223       78.96   -156.13                                   
REMARK 500    ASN B 301     -113.45     68.77                                   
REMARK 500    ASN B 335       58.68   -157.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2   RELATED DB: PDB                                   
REMARK 900 HOMOLOGUE FROM PSEUDOMONAS AERUGINOSA PA14                           
REMARK 900 RELATED ID: 4MEB   RELATED DB: PDB                                   
DBREF  4MEA A   25   349  UNP    D0BWK6   D0BWK6_9GAMM    25    349             
DBREF  4MEA B   25   349  UNP    D0BWK6   D0BWK6_9GAMM    25    349             
SEQADV 4MEA HIS A  350  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS A  351  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS A  352  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS A  353  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS A  354  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS A  355  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  350  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  351  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  352  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  353  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  354  UNP  D0BWK6              EXPRESSION TAG                 
SEQADV 4MEA HIS B  355  UNP  D0BWK6              EXPRESSION TAG                 
SEQRES   1 A  331  GLU TYR ASP PRO ASN LEU LYS SER ILE ASP THR PRO PRO          
SEQRES   2 A  331  ALA VAL SER GLN GLN MET PHE ASN LYS VAL LYS SER ASN          
SEQRES   3 A  331  GLY LEU GLY GLN TYR ALA TYR ALA LYS GLY LEU SER SER          
SEQRES   4 A  331  LYS PHE ILE GLU SER GLU GLY VAL LYS LEU HIS TYR VAL          
SEQRES   5 A  331  GLU GLY GLY SER LYS GLY THR PRO ILE VAL PHE ILE HIS          
SEQRES   6 A  331  GLY PHE GLY SER THR TRP LYS MET TRP GLU PRO VAL MET          
SEQRES   7 A  331  LEU SER TYR MET LYS ASP HIS LYS VAL ILE ALA ILE ASP          
SEQRES   8 A  331  LEU PRO GLY LEU GLY GLN SER GLY PRO ILE LEU ASN ASP          
SEQRES   9 A  331  ASP TYR SER ALA GLU ASN THR SER LYS ILE LEU ILE GLY          
SEQRES  10 A  331  ALA ILE LYS LYS ILE ALA GLY LYS GLY PRO ILE TYR TYR          
SEQRES  11 A  331  VAL SER HIS ASP LEU GLY ASN THR ALA SER TYR PRO LEU          
SEQRES  12 A  331  VAL ALA ASN ASN GLN GLY TYR ILE LYS LYS ALA VAL PHE          
SEQRES  13 A  331  MET ASP SER PRO ILE PRO ASP ARG ALA MET PHE GLU TYR          
SEQRES  14 A  331  PRO GLY TYR THR ALA ASP GLY PRO GLY LEU GLY TRP HIS          
SEQRES  15 A  331  PHE GLY TYR PHE SER PHE GLY ASP ILE ALA GLU LYS GLN          
SEQRES  16 A  331  ILE ALA ASN ASP PRO ASN LEU PHE PHE SER TYR PHE ILE          
SEQRES  17 A  331  LYS THR TYR ALA GLY LYS LYS GLU ILE PHE THR PRO GLU          
SEQRES  18 A  331  LEU LEU ALA GLU LEU ILE GLU PRO TYR SER THR ARG ASP          
SEQRES  19 A  331  LYS LEU LYS ALA ALA PHE GLY TYR TYR ARG SER HIS ALA          
SEQRES  20 A  331  ASP SER ILE ARG GLN ASN GLU ALA LEU LEU ALA ASN GLY          
SEQRES  21 A  331  LYS LYS LEU THR ILE PRO SER MET ALA LEU THR GLY GLN          
SEQRES  22 A  331  LYS GLY VAL ASN ASP VAL LEU VAL LYS GLU MET ARG ALA          
SEQRES  23 A  331  ARG PHE VAL ALA ASP PRO ALA GLN TYR THR ALA ILE ILE          
SEQRES  24 A  331  LEU PRO ASP THR GLY HIS TRP MET VAL GLU GLU ASN ALA          
SEQRES  25 A  331  GLU GLY VAL GLU LYS SER LEU SER ASN PHE LEU PHE LYS          
SEQRES  26 A  331  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  331  GLU TYR ASP PRO ASN LEU LYS SER ILE ASP THR PRO PRO          
SEQRES   2 B  331  ALA VAL SER GLN GLN MET PHE ASN LYS VAL LYS SER ASN          
SEQRES   3 B  331  GLY LEU GLY GLN TYR ALA TYR ALA LYS GLY LEU SER SER          
SEQRES   4 B  331  LYS PHE ILE GLU SER GLU GLY VAL LYS LEU HIS TYR VAL          
SEQRES   5 B  331  GLU GLY GLY SER LYS GLY THR PRO ILE VAL PHE ILE HIS          
SEQRES   6 B  331  GLY PHE GLY SER THR TRP LYS MET TRP GLU PRO VAL MET          
SEQRES   7 B  331  LEU SER TYR MET LYS ASP HIS LYS VAL ILE ALA ILE ASP          
SEQRES   8 B  331  LEU PRO GLY LEU GLY GLN SER GLY PRO ILE LEU ASN ASP          
SEQRES   9 B  331  ASP TYR SER ALA GLU ASN THR SER LYS ILE LEU ILE GLY          
SEQRES  10 B  331  ALA ILE LYS LYS ILE ALA GLY LYS GLY PRO ILE TYR TYR          
SEQRES  11 B  331  VAL SER HIS ASP LEU GLY ASN THR ALA SER TYR PRO LEU          
SEQRES  12 B  331  VAL ALA ASN ASN GLN GLY TYR ILE LYS LYS ALA VAL PHE          
SEQRES  13 B  331  MET ASP SER PRO ILE PRO ASP ARG ALA MET PHE GLU TYR          
SEQRES  14 B  331  PRO GLY TYR THR ALA ASP GLY PRO GLY LEU GLY TRP HIS          
SEQRES  15 B  331  PHE GLY TYR PHE SER PHE GLY ASP ILE ALA GLU LYS GLN          
SEQRES  16 B  331  ILE ALA ASN ASP PRO ASN LEU PHE PHE SER TYR PHE ILE          
SEQRES  17 B  331  LYS THR TYR ALA GLY LYS LYS GLU ILE PHE THR PRO GLU          
SEQRES  18 B  331  LEU LEU ALA GLU LEU ILE GLU PRO TYR SER THR ARG ASP          
SEQRES  19 B  331  LYS LEU LYS ALA ALA PHE GLY TYR TYR ARG SER HIS ALA          
SEQRES  20 B  331  ASP SER ILE ARG GLN ASN GLU ALA LEU LEU ALA ASN GLY          
SEQRES  21 B  331  LYS LYS LEU THR ILE PRO SER MET ALA LEU THR GLY GLN          
SEQRES  22 B  331  LYS GLY VAL ASN ASP VAL LEU VAL LYS GLU MET ARG ALA          
SEQRES  23 B  331  ARG PHE VAL ALA ASP PRO ALA GLN TYR THR ALA ILE ILE          
SEQRES  24 B  331  LEU PRO ASP THR GLY HIS TRP MET VAL GLU GLU ASN ALA          
SEQRES  25 B  331  GLU GLY VAL GLU LYS SER LEU SER ASN PHE LEU PHE LYS          
SEQRES  26 B  331  HIS HIS HIS HIS HIS HIS                                      
FORMUL   3  HOH   *608(H2 O)                                                    
HELIX    1   1 PRO A   36  ASN A   50  1                                  15    
HELIX    2   2 LEU A   52  ALA A   56  5                                   5    
HELIX    3   3 THR A   94  MET A   97  5                                   4    
HELIX    4   4 TRP A   98  MET A  106  1                                   9    
HELIX    5   5 SER A  131  GLY A  148  1                                  18    
HELIX    6   6 LEU A  159  ASN A  171  1                                  13    
HELIX    7   7 ASP A  187  GLU A  192  5                                   6    
HELIX    8   8 GLY A  204  PHE A  210  1                                   7    
HELIX    9   9 ASP A  214  ASP A  223  1                                  10    
HELIX   10  10 ASP A  223  ALA A  236  1                                  14    
HELIX   11  11 LYS A  238  PHE A  242  5                                   5    
HELIX   12  12 THR A  243  GLU A  252  1                                  10    
HELIX   13  13 PRO A  253  SER A  255  5                                   3    
HELIX   14  14 THR A  256  SER A  269  1                                  14    
HELIX   15  15 SER A  269  ASN A  283  1                                  15    
HELIX   16  16 ASP A  302  PHE A  312  1                                  11    
HELIX   17  17 ASP A  315  ALA A  317  5                                   3    
HELIX   18  18 TRP A  330  PHE A  348  1                                  19    
HELIX   19  19 PRO B   36  ASN B   50  1                                  15    
HELIX   20  20 LEU B   52  ALA B   56  5                                   5    
HELIX   21  21 THR B   94  MET B   97  5                                   4    
HELIX   22  22 TRP B   98  MET B  106  1                                   9    
HELIX   23  23 SER B  131  GLY B  148  1                                  18    
HELIX   24  24 ASP B  158  ASN B  171  1                                  14    
HELIX   25  25 ASP B  187  GLU B  192  5                                   6    
HELIX   26  26 GLY B  204  PHE B  210  1                                   7    
HELIX   27  27 ASP B  214  ASP B  223  1                                  10    
HELIX   28  28 ASP B  223  ALA B  236  1                                  14    
HELIX   29  29 LYS B  238  PHE B  242  5                                   5    
HELIX   30  30 THR B  243  GLU B  252  1                                  10    
HELIX   31  31 PRO B  253  SER B  255  5                                   3    
HELIX   32  32 THR B  256  SER B  269  1                                  14    
HELIX   33  33 SER B  269  ASN B  283  1                                  15    
HELIX   34  34 ASP B  302  PHE B  312  1                                  11    
HELIX   35  35 ASP B  315  ALA B  317  5                                   3    
HELIX   36  36 TRP B  330  PHE B  348  1                                  19    
SHEET    1   A 8 LEU A  61  SER A  68  0                                        
SHEET    2   A 8 VAL A  71  GLY A  78 -1  O  LEU A  73   N  ILE A  66           
SHEET    3   A 8 VAL A 111  ILE A 114 -1  O  ALA A 113   N  VAL A  76           
SHEET    4   A 8 ILE A  85  ILE A  88  1  N  PHE A  87   O  ILE A 112           
SHEET    5   A 8 ILE A 152  HIS A 157  1  O  VAL A 155   N  VAL A  86           
SHEET    6   A 8 ILE A 175  MET A 181  1  O  VAL A 179   N  TYR A 154           
SHEET    7   A 8 SER A 291  GLY A 296  1  O  MET A 292   N  PHE A 180           
SHEET    8   A 8 TYR A 319  LEU A 324  1  O  LEU A 324   N  THR A 295           
SHEET    1   B 2 TYR A 196  THR A 197  0                                        
SHEET    2   B 2 GLY A 200  PRO A 201 -1  O  GLY A 200   N  THR A 197           
SHEET    1   C 8 SER B  62  SER B  68  0                                        
SHEET    2   C 8 VAL B  71  GLY B  78 -1  O  LEU B  73   N  ILE B  66           
SHEET    3   C 8 VAL B 111  ILE B 114 -1  O  ALA B 113   N  VAL B  76           
SHEET    4   C 8 ILE B  85  ILE B  88  1  N  PHE B  87   O  ILE B 112           
SHEET    5   C 8 ILE B 152  HIS B 157  1  O  VAL B 155   N  VAL B  86           
SHEET    6   C 8 ILE B 175  MET B 181  1  O  LYS B 176   N  ILE B 152           
SHEET    7   C 8 SER B 291  GLY B 296  1  O  MET B 292   N  PHE B 180           
SHEET    8   C 8 TYR B 319  LEU B 324  1  O  LEU B 324   N  THR B 295           
SHEET    1   D 2 TYR B 196  THR B 197  0                                        
SHEET    2   D 2 GLY B 200  PRO B 201 -1  O  GLY B 200   N  THR B 197           
CISPEP   1 GLY A  150    PRO A  151          0         1.42                     
CISPEP   2 GLY B  150    PRO B  151          0         1.09                     
CRYST1   85.688   42.584   86.470  90.00  98.10  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      0.011670  0.000000  0.001661        0.00000                         
SCALE2      0.000000  0.023483  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011681        0.00000                         
TER    2559      PHE A 348                                                      
TER    5100      PHE B 348                                                      
MASTER      290    0    0   36   20    0    0    6 5667    2    0   52          
END                                                                             

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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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