Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 1GXS-pdb

Name Class
1GXS-pdb
HEADER    LYASE                                   11-APR-02   1GXS              
TITLE     CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM SORGHUM                
TITLE    2 BICOLOR IN COMPLEX WITH INHIBITOR BENZOIC ACID: A NOVEL              
TITLE    3 CYANOGENIC ENZYME                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROXYNITRILE LYASE;                                      
COMPND   3 SYNONYM: HNL;                                                        
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 EC: 4.1.2.11;                                                        
COMPND   6 OTHER_DETAILS: ISOENZYME II;                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HYDROXYNITRILE LYASE;                                      
COMPND   9 SYNONYM: HNL;                                                        
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 EC: 4.1.2.11;                                                        
COMPND  12 OTHER_DETAILS: ISOENZYME II                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SORGHUM BICOLOR;                                
SOURCE   3 ORGANISM_COMMON: SORGHUM;                                            
SOURCE   4 TISSUE: PRIMARY LEAVES OF SEEDLINGS;                                 
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SORGHUM BICOLOR;                                
SOURCE   7 ORGANISM_COMMON: SORGHUM;                                            
SOURCE   8 TISSUE: PRIMARY LEAVES OF SEEDLINGS                                  
KEYWDS    HYDROXYNITRILE LYASE, INHIBITOR COMPLEX, CYANOGENESIS                 
KEYWDS   2 MECHANISM                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LAUBLE,B.MIEHLICH,S.FOERSTER,H.WAJANT,F.EFFENBERGER                 
REVDAT   1   01-OCT-02 1GXS    0                                                
JRNL        AUTH   H.LAUBLE,B.MIEHLICH,S.FOERSTER,H.WAJANT,                     
JRNL        AUTH 2 F.EFFENBERGER                                                
JRNL        TITL   CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM               
JRNL        TITL 2 SORGHUM BICOLOR IN COMPLEX WITH THE INHIBITOR                
JRNL        TITL 3 BENZOIC ACID: A NOVEL CYANOGENIC ENZYME                      
JRNL        REF    BIOCHEMISTRY                  V.  41 12043 2002              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.3  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.00                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.001000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 50480                          
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) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.1                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5122                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.5                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5693                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.216                        
REMARK   3   BIN FREE R VALUE                    : 0.264                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.3                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 655                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6748                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 146                                     
REMARK   3   SOLVENT ATOMS            : 331                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.9                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.1                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.1                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
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) : 2.61  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.91  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.42  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.32  ; 2.50                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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  : PARAM19XHOH.PRO                                
REMARK   3  PARAMETER FILE  2  : PARBEZ.PRO                                     
REMARK   3  PARAMETER FILE  3  : PARDKA.PRO                                     
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : TOPBEZ.PRO                                     
REMARK   3  TOPOLOGY FILE  3   : TOPDKA.PRO                                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ASYMMETRIC UNIT CONTAINS 2                
REMARK   3   ALPHA/BETA-DIMERS                                                  
REMARK   4                                                                      
REMARK   4 1GXS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 12-APR-2002.                
REMARK 100 THE EBI ID CODE IS EBI-9691.                                         
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 291                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR571                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100992                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.3                                
REMARK 200  RESOLUTION RANGE LOW       (A) : 17                                 
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2                                  
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 2.0                                
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.5                                
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.0                                
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.7                                
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3SC2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 61                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NA-CITRATE PH 5.4 USING            
REMARK 280  1.6 M AMMONIUM SULFATE                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP:  C 1 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   1/2+X,1/2+Y,Z                                           
REMARK 290       4555   1/2-X,1/2+Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       75.35000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       75.35000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   4 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC                      
REMARK 300                                                                      
REMARK 300 THE BIOLOGICALLY ACTIVE SUBUNIT IS A HETEROTETRAMER FORMED           
REMARK 300 BY TWO AB-HETERODIMERS                                               
REMARK 300                                                                      
REMARK 300 THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 APPEARS                  
REMARK 300 TO BE A CASE OF STRONG CRYSTAL PACKING WITH                          
REMARK 300 THE MEAN DIFFERENCE IN ACCESSIBLE SURFACE AREA PER                   
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR                        
REMARK 300 THE CHAIN IN THE COMPLEX IS  5506.4 ANGSTROM**2                      
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLN A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO                 
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY            
REMARK 525 ASSOCIATED WITH:                                                     
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN                                       
REMARK 525     A              U                                                 
REMARK 525     B              V                                                 
REMARK 525     C              W                                                 
REMARK 525     D              X                                                 
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES FOR DIMER AB                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES FOR DIMER CD                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BZ1                                                 
REMARK 800 SITE_DESCRIPTION: BEZ BINDING SITE FOR DIMER AB                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DK1                                                 
REMARK 800 SITE_DESCRIPTION: DKA BINDING SITE FOR DIMER AB                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BZ2                                                 
REMARK 800 SITE_DESCRIPTION: BEZ BINDING SITE FOR DIMER CD                      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DK2                                                 
REMARK 800 SITE_DESCRIPTION: DKA BINDING SITE FOR DIMER CD                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 VARIANTS LISTED IN SEQADV RECORDS WERE SUPPLIED BY THE               
REMARK 999 AUTHORS OF THE PDB ENTRY, AND WERE NOT OBTAINED FROM THE             
REMARK 999 SWISS-PROT ENTRY                                                     
DBREF  1GXS A    1   270  SWS    Q8W4X3   Q8W4X3          56    325             
DBREF  1GXS B  283   440  SWS    Q8W4X3   Q8W4X3         338    495             
DBREF  1GXS C    1   270  SWS    Q8W4X3   Q8W4X3          56    325             
DBREF  1GXS D  283   440  SWS    Q8W4X3   Q8W4X3         338    495             
SEQADV 1GXS LEU A   11  SWS  Q8W4X3    PRO    66 VARIANT                        
SEQADV 1GXS ALA A   79  SWS  Q8W4X3    PRO   134 VARIANT                        
SEQADV 1GXS GLY A  112  SWS  Q8W4X3    VAL   167 VARIANT                        
SEQADV 1GXS SER A  203  SWS  Q8W4X3    LEU   258 VARIANT                        
SEQADV 1GXS LEU C   11  SWS  Q8W4X3    PRO    66 VARIANT                        
SEQADV 1GXS ALA C   79  SWS  Q8W4X3    PRO   134 VARIANT                        
SEQADV 1GXS GLY C  112  SWS  Q8W4X3    VAL   167 VARIANT                        
SEQADV 1GXS SER C  203  SWS  Q8W4X3    LEU   258 VARIANT                        
SEQADV 1GXS THR B  408  SWS  Q8W4X3    SER   463 VARIANT                        
SEQADV 1GXS VAL B  409  SWS  Q8W4X3    PRO   464 VARIANT                        
SEQADV 1GXS ARG B  410  SWS  Q8W4X3    SER   465 VARIANT                        
SEQADV 1GXS THR D  408  SWS  Q8W4X3    SER   463 VARIANT                        
SEQADV 1GXS VAL D  409  SWS  Q8W4X3    PRO   464 VARIANT                        
SEQADV 1GXS ARG D  410  SWS  Q8W4X3    SER   465 VARIANT                        
SEQRES   1 A  270  GLN LEU GLN GLN GLN GLU ASP ASP ARG ILE LEU GLY LEU          
SEQRES   2 A  270  PRO GLY GLN PRO ASN GLY VAL ALA PHE GLY MET TYR GLY          
SEQRES   3 A  270  GLY TYR VAL THR ILE ASP ASP ASN ASN GLY ARG ALA LEU          
SEQRES   4 A  270  TYR TYR TRP PHE GLN GLU ALA ASP THR ALA ASP PRO ALA          
SEQRES   5 A  270  ALA ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY          
SEQRES   6 A  270  CYS SER SER ILE GLY LEU GLY ALA MET GLN GLU LEU GLY          
SEQRES   7 A  270  ALA PHE ARG VAL HIS THR ASN GLY GLU SER LEU LEU LEU          
SEQRES   8 A  270  ASN GLU TYR ALA TRP ASN LYS ALA ALA ASN ILE LEU PHE          
SEQRES   9 A  270  ALA GLU SER PRO ALA GLY VAL GLY PHE SER TYR SER ASN          
SEQRES  10 A  270  THR SER SER ASP LEU SER MET GLY ASP ASP LYS MET ALA          
SEQRES  11 A  270  GLN ASP THR TYR THR PHE LEU VAL LYS TRP PHE GLU ARG          
SEQRES  12 A  270  PHE PRO HIS TYR ASN TYR ARG GLU PHE TYR ILE ALA GLY          
SEQRES  13 A  270  GLU SER GLY HIS PHE ILE PRO GLN LEU SER GLN VAL VAL          
SEQRES  14 A  270  TYR ARG ASN ARG ASN ASN SER PRO PHE ILE ASN PHE GLN          
SEQRES  15 A  270  GLY LEU LEU VAL SER SER GLY LEU THR ASN ASP HIS GLU          
SEQRES  16 A  270  ASP MET ILE GLY MET PHE GLU SER TRP TRP HIS HIS GLY          
SEQRES  17 A  270  LEU ILE SER ASP GLU THR ARG ASP SER GLY LEU LYS VAL          
SEQRES  18 A  270  CYS PRO GLY THR SER PHE MET HIS PRO THR PRO GLU CYS          
SEQRES  19 A  270  THR GLU VAL TRP ASN LYS ALA LEU ALA GLU GLN GLY ASN          
SEQRES  20 A  270  ILE ASN PRO TYR THR ILE TYR THR PRO THR CYS ASP ARG          
SEQRES  21 A  270  GLU PRO SER PRO TYR GLN ARG ARG PHE TRP                      
SEQRES   1 B  158  LEU PRO PRO TYR ASP PRO CYS ALA VAL PHE ASN SER ILE          
SEQRES   2 B  158  ASN TYR LEU ASN LEU PRO GLU VAL GLN THR ALA LEU HIS          
SEQRES   3 B  158  ALA ASN VAL SER GLY ILE VAL GLU TYR PRO TRP THR VAL          
SEQRES   4 B  158  CYS SER ASN THR ILE PHE ASP GLN TRP GLY GLN ALA ALA          
SEQRES   5 B  158  ASP ASP LEU LEU PRO VAL TYR ARG GLU LEU ILE GLN ALA          
SEQRES   6 B  158  GLY LEU ARG VAL TRP VAL TYR SER GLY ASP THR ASP SER          
SEQRES   7 B  158  VAL VAL PRO VAL SER SER THR ARG ARG SER LEU ALA ALA          
SEQRES   8 B  158  LEU GLU LEU PRO VAL LYS THR SER TRP TYR PRO TRP TYR          
SEQRES   9 B  158  MET ALA PRO THR GLU ARG GLU VAL GLY GLY TRP SER VAL          
SEQRES  10 B  158  GLN TYR GLU GLY LEU THR TYR VAL THR VAL ARG GLY ALA          
SEQRES  11 B  158  GLY HIS LEU VAL PRO VAL HIS ARG PRO ALA GLN ALA PHE          
SEQRES  12 B  158  LEU LEU PHE LYS GLN PHE LEU LYS GLY GLU PRO MET PRO          
SEQRES  13 B  158  ALA GLU                                                      
SEQRES   1 C  270  GLN LEU GLN GLN GLN GLU ASP ASP ARG ILE LEU GLY LEU          
SEQRES   2 C  270  PRO GLY GLN PRO ASN GLY VAL ALA PHE GLY MET TYR GLY          
SEQRES   3 C  270  GLY TYR VAL THR ILE ASP ASP ASN ASN GLY ARG ALA LEU          
SEQRES   4 C  270  TYR TYR TRP PHE GLN GLU ALA ASP THR ALA ASP PRO ALA          
SEQRES   5 C  270  ALA ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY          
SEQRES   6 C  270  CYS SER SER ILE GLY LEU GLY ALA MET GLN GLU LEU GLY          
SEQRES   7 C  270  ALA PHE ARG VAL HIS THR ASN GLY GLU SER LEU LEU LEU          
SEQRES   8 C  270  ASN GLU TYR ALA TRP ASN LYS ALA ALA ASN ILE LEU PHE          
SEQRES   9 C  270  ALA GLU SER PRO ALA GLY VAL GLY PHE SER TYR SER ASN          
SEQRES  10 C  270  THR SER SER ASP LEU SER MET GLY ASP ASP LYS MET ALA          
SEQRES  11 C  270  GLN ASP THR TYR THR PHE LEU VAL LYS TRP PHE GLU ARG          
SEQRES  12 C  270  PHE PRO HIS TYR ASN TYR ARG GLU PHE TYR ILE ALA GLY          
SEQRES  13 C  270  GLU SER GLY HIS PHE ILE PRO GLN LEU SER GLN VAL VAL          
SEQRES  14 C  270  TYR ARG ASN ARG ASN ASN SER PRO PHE ILE ASN PHE GLN          
SEQRES  15 C  270  GLY LEU LEU VAL SER SER GLY LEU THR ASN ASP HIS GLU          
SEQRES  16 C  270  ASP MET ILE GLY MET PHE GLU SER TRP TRP HIS HIS GLY          
SEQRES  17 C  270  LEU ILE SER ASP GLU THR ARG ASP SER GLY LEU LYS VAL          
SEQRES  18 C  270  CYS PRO GLY THR SER PHE MET HIS PRO THR PRO GLU CYS          
SEQRES  19 C  270  THR GLU VAL TRP ASN LYS ALA LEU ALA GLU GLN GLY ASN          
SEQRES  20 C  270  ILE ASN PRO TYR THR ILE TYR THR PRO THR CYS ASP ARG          
SEQRES  21 C  270  GLU PRO SER PRO TYR GLN ARG ARG PHE TRP                      
SEQRES   1 D  158  LEU PRO PRO TYR ASP PRO CYS ALA VAL PHE ASN SER ILE          
SEQRES   2 D  158  ASN TYR LEU ASN LEU PRO GLU VAL GLN THR ALA LEU HIS          
SEQRES   3 D  158  ALA ASN VAL SER GLY ILE VAL GLU TYR PRO TRP THR VAL          
SEQRES   4 D  158  CYS SER ASN THR ILE PHE ASP GLN TRP GLY GLN ALA ALA          
SEQRES   5 D  158  ASP ASP LEU LEU PRO VAL TYR ARG GLU LEU ILE GLN ALA          
SEQRES   6 D  158  GLY LEU ARG VAL TRP VAL TYR SER GLY ASP THR ASP SER          
SEQRES   7 D  158  VAL VAL PRO VAL SER SER THR ARG ARG SER LEU ALA ALA          
SEQRES   8 D  158  LEU GLU LEU PRO VAL LYS THR SER TRP TYR PRO TRP TYR          
SEQRES   9 D  158  MET ALA PRO THR GLU ARG GLU VAL GLY GLY TRP SER VAL          
SEQRES  10 D  158  GLN TYR GLU GLY LEU THR TYR VAL THR VAL ARG GLY ALA          
SEQRES  11 D  158  GLY HIS LEU VAL PRO VAL HIS ARG PRO ALA GLN ALA PHE          
SEQRES  12 D  158  LEU LEU PHE LYS GLN PHE LEU LYS GLY GLU PRO MET PRO          
SEQRES  13 D  158  ALA GLU                                                      
MODRES 1GXS ASN A  117  ASN  GLYCOSYLATION SITE                                 
MODRES 1GXS ASN B  310  ASN  GLYCOSYLATION SITE                                 
MODRES 1GXS ASN C  117  ASN  GLYCOSYLATION SITE                                 
MODRES 1GXS ASN D  310  ASN  GLYCOSYLATION SITE                                 
HET    BEZ  A 601       9                                                       
HET    DKA  A 701      12                                                       
HET    NAG  A1117      14                                                       
HET    NAG  A1118      14                                                       
HET    FUC  A1119      10                                                       
HET    NAG  B1310      14                                                       
HET    BEZ  C 602       9                                                       
HET    DKA  C 702      12                                                       
HET    NAG  C1117      14                                                       
HET    NAG  C1118      14                                                       
HET    FUC  C1119      10                                                       
HET    NAG  D1310      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     NAG NAG                                                              
HETNAM     FUC FUCOSE                                                           
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM     DKA DECANOIC ACID                                                    
FORMUL   5  NAG    6(C8 H15 N1 O6)                                              
FORMUL   6  FUC    2(C6 H12 O5)                                                 
FORMUL   7  BEZ    2(C7 H6 O2)                                                  
FORMUL   8  DKA    2(C10 H20 O2)                                                
FORMUL   9  HOH   *331(H2 O1)                                                   
HELIX    1   1 GLN A    4  ARG A    9  1                                   6    
HELIX    2   2 ASP A   50  ALA A   54  5                                   5    
HELIX    3   3 SER A   68  GLY A   78  5                                  11    
HELIX    4   4 ALA A   95  ALA A   99  5                                   5    
HELIX    5   5 THR A  118  SER A  123  5                                   6    
HELIX    6   6 GLY A  125  PHE A  144  1                                  20    
HELIX    7   7 PRO A  145  ASN A  148  5                                   4    
HELIX    8   8 HIS A  160  ASN A  172  1                                  13    
HELIX    9   9 ASN A  192  HIS A  207  1                                  16    
HELIX   10  10 SER A  211  CYS A  222  1                                  12    
HELIX   11  11 THR A  231  GLN A  245  1                                  15    
HELIX   12  12 ALA B  290  ASN B  299  1                                  10    
HELIX   13  13 LEU B  300  HIS B  308  1                                   9    
HELIX   14  14 ASN B  310  ILE B  314  5                                   5    
HELIX   15  15 SER B  323  GLN B  329  1                                   7    
HELIX   16  16 LEU B  337  ALA B  347  1                                  11    
HELIX   17  17 PRO B  363  ALA B  373  1                                  11    
HELIX   18  18 LEU B  415  ARG B  420  1                                   6    
HELIX   19  19 ARG B  420  GLY B  434  1                                  15    
HELIX   20  20 GLN C    4  ASP C    8  5                                   5    
HELIX   21  21 ASP C   50  ALA C   54  5                                   5    
HELIX   22  22 SER C   68  LEU C   77  3                                  10    
HELIX   23  23 ALA C   95  ALA C   99  5                                   5    
HELIX   24  24 THR C  118  SER C  123  5                                   6    
HELIX   25  25 GLY C  125  PHE C  144  1                                  20    
HELIX   26  26 PRO C  145  ASN C  148  5                                   4    
HELIX   27  27 HIS C  160  ASN C  172  1                                  13    
HELIX   28  28 ASN C  192  HIS C  207  1                                  16    
HELIX   29  29 SER C  211  CYS C  222  1                                  12    
HELIX   30  30 THR C  231  GLN C  245  1                                  15    
HELIX   31  31 ALA D  290  ASN D  299  1                                  10    
HELIX   32  32 LEU D  300  HIS D  308  1                                   9    
HELIX   33  33 ASN D  310  ILE D  314  5                                   5    
HELIX   34  34 SER D  323  GLN D  329  1                                   7    
HELIX   35  35 LEU D  337  ALA D  347  1                                  11    
HELIX   36  36 PRO D  363  ALA D  373  1                                  11    
HELIX   37  37 LEU D  415  ARG D  420  1                                   6    
HELIX   38  38 ARG D  420  GLY D  434  1                                  15    
SHEET    1  AA 3 MET A  24  ASP A  32  0                                        
SHEET    2  AA 3 ARG A  37  GLN A  44 -1  O  ARG A  37   N  ILE A  31           
SHEET    3  AA 3 TYR A 115  SER A 116 -1  O  TYR A 115   N  ALA A  38           
SHEET    1  AB10 MET A  24  ASP A  32  0                                        
SHEET    2  AB10 ARG A  37  GLN A  44 -1  O  ARG A  37   N  ILE A  31           
SHEET    3  AB10 ASN A 101  ALA A 105 -1  O  ILE A 102   N  GLN A  44           
SHEET    4  AB10 LEU A  56  ASN A  61  1  O  VAL A  57   N  LEU A 103           
SHEET    5  AB10 GLU A 151  GLU A 157  1  O  GLU A 151   N  LEU A  56           
SHEET    6  AB10 ASN A 180  SER A 187  1  O  ASN A 180   N  PHE A 152           
SHEET    7  AB10 ARG B 350  GLY B 356  1  O  ARG B 350   N  LEU A 184           
SHEET    8  AB10 LEU B 404  VAL B 409  1  O  THR B 405   N  VAL B 353           
SHEET    9  AB10 VAL B 394  TYR B 401 -1  O  TRP B 397   N  THR B 408           
SHEET   10  AB10 VAL B 378  TYR B 386 -1  N  LYS B 379   O  GLN B 400           
SHEET    1  AC 2 PHE A  80  VAL A  82  0                                        
SHEET    2  AC 2 LEU A  89  LEU A  91 -1  O  LEU A  90   N  ARG A  81           
SHEET    1  CA 3 MET C  24  ASP C  32  0                                        
SHEET    2  CA 3 ARG C  37  GLN C  44 -1  O  ARG C  37   N  ILE C  31           
SHEET    3  CA 3 TYR C 115  SER C 116 -1  O  TYR C 115   N  ALA C  38           
SHEET    1  CB10 MET C  24  ASP C  32  0                                        
SHEET    2  CB10 ARG C  37  GLN C  44 -1  O  ARG C  37   N  ILE C  31           
SHEET    3  CB10 ASN C 101  ALA C 105 -1  O  ILE C 102   N  GLN C  44           
SHEET    4  CB10 LEU C  56  LEU C  60  1  O  VAL C  57   N  LEU C 103           
SHEET    5  CB10 GLU C 151  GLY C 156  1  O  GLU C 151   N  LEU C  56           
SHEET    6  CB10 ASN C 180  SER C 187  1  O  ASN C 180   N  PHE C 152           
SHEET    7  CB10 ARG D 350  GLY D 356  1  O  ARG D 350   N  LEU C 184           
SHEET    8  CB10 THR D 405  VAL D 409  1  O  THR D 405   N  VAL D 353           
SHEET    9  CB10 GLY D 396  TYR D 401 -1  O  TRP D 397   N  THR D 408           
SHEET   10  CB10 VAL D 378  TRP D 385 -1  N  LYS D 379   O  GLN D 400           
SHEET    1  CC 2 PHE C  80  VAL C  82  0                                        
SHEET    2  CC 2 LEU C  89  LEU C  91 -1  O  LEU C  90   N  ARG C  81           
SSBOND   1 CYS A   66    CYS B  322                          1555   1555        
SSBOND   2 CYS A  222    CYS A  234                          1555   1555        
SSBOND   3 CYS A  258    CYS B  289                          1555   1555        
SSBOND   4 CYS C   66    CYS D  322                          1555   1555        
SSBOND   5 CYS C  222    CYS C  234                          1555   1555        
SSBOND   6 CYS C  258    CYS D  289                          1555   1555        
LINK         ND2 ASN A 117                 C1  NAG A1117     1555   1555        
LINK         O3  NAG A1117                 C1  FUC A1119     1555   1555        
LINK         O4  NAG A1117                 C1  NAG A1118     1555   1555        
LINK         ND2 ASN B 310                 C1  NAG B1310     1555   1555        
LINK         ND2 ASN C 117                 C1  NAG C1117     1555   1555        
LINK         O4  NAG C1117                 C1  NAG C1118     1555   1555        
LINK         O3  NAG C1117                 C1  FUC C1119     1555   1555        
LINK         ND2 ASN D 310                 C1  NAG D1310     1555   1555        
CISPEP   1 GLY A   63    PRO A   64          0       -16.06                     
CISPEP   2 SER A  107    PRO A  108          0        -1.81                     
CISPEP   3 GLY C   63    PRO C   64          0        -6.70                     
CISPEP   4 SER C  107    PRO C  108          0         1.71                     
SITE     1 CA1  2 SER A 158  TRP A 270                                          
SITE     1 CA2  2 SER C 158  TRP C 270                                          
SITE     1 BZ1  8 GLY A  62  GLY A  63  PRO A  64  ASP A 126                    
SITE     2 BZ1  8 SER A 158  HIS A 160  PHE A 161  HOH U  40                    
SITE     1 DK1  8 ASN A  61  GLY A  62  GLU A 157  ASN A 249                    
SITE     2 DK1  8 TYR A 251  TRP A 270  HIS B 414  LEU B 415                    
SITE     1 BZ2  8 GLY C  62  GLY C  63  PRO C  64  ASP C 126                    
SITE     2 BZ2  8 SER C 158  HIS C 160  PHE C 161  HOH W  47                    
SITE     1 DK2  8 ASN C  61  GLY C  62  GLU C 157  ASN C 249                    
SITE     2 DK2  8 TYR C 251  TRP C 270  HIS D 414  LEU D 415                    
CRYST1  150.700  103.700   90.600  90.00 101.30  90.00 C 1 2 1       8          
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      0.006636  0.000000  0.001326        0.00000                         
SCALE2      0.000000  0.009643  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011256        0.00000                         
END                                                                             

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

Acknowledgements and disclaimer