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LongText Report for: 3DQZ-pdb

Name Class
3DQZ-pdb
HEADER    LYASE                                   10-JUL-08   3DQZ              
TITLE     STRUCTURE OF THE HYDROXYNITRILE LYASE FROM ARABIDOPSIS                
TITLE    2 THALIANA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-HYDROXYNITRILE LYASE-LIKE PROTEIN;                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ATHNL, AT5G10300/F18D22_70;                                 
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: F18D22_70, AT5G10300;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    A/B-HYDRLOASE FOLD, CYANOGENESIS, LYASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ANDEXER,N.STAUNIG,K.GRUBER                                          
REVDAT   1   14-JUL-09 3DQZ    0                                                
JRNL        AUTH   J.ANDEXER,N.STAUNIG,T.EGGERT,C.KRATKY,M.POHL,                
JRNL        AUTH 2 K.GRUBER                                                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE R-SELECTIVE                     
JRNL        TITL 2 HYDROXYNITRILE LYASE FROM ARABIDOPSIS THALIANA:              
JRNL        TITL 3 MECHANISTIC IMPLICATIONS AND EXPLANATIONS FOR THE            
JRNL        TITL 4 STEREOSELECTIVITY                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 33106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.720                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1561                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 24.79                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.17900                                             
REMARK   3    B22 (A**2) : 1.95800                                              
REMARK   3    B33 (A**2) : -0.77900                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -2.06200                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.4810                                                   
REMARK   3   OPERATOR: L,-K,H                                                   
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           NULL                                  
REMARK   3   ANGLE     :  0.899           NULL                                  
REMARK   3   CHIRALITY :  0.063           NULL                                  
REMARK   3   PLANARITY :  0.004           NULL                                  
REMARK   3   DIHEDRAL  : 16.596           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS IS A TWINNED STRUCTURE, THE          
REMARK   3  DETWIN FRACTION IS 0.481 AND OPERATOR IS 'L,-K,H'.                  
REMARK   4                                                                      
REMARK   4 3DQZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048379.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8081                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33151                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200   FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.21000                            
REMARK 200   FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1QJ4, 1DWP, 1XKL                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-18% PEG3350, 100MM BISTRIS,           
REMARK 280  PH6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K              
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      111.65650            
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: DIMERIC                           
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     MET B   258                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     MET D   258                                                      
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    TYR A  14       -2.33     73.86                                   
REMARK 500    HIS A  15     -166.58   -123.72                                   
REMARK 500    ALA A  41       16.46     58.83                                   
REMARK 500    ASN A  72       -1.94     74.85                                   
REMARK 500    SER A  81     -112.60     64.89                                   
REMARK 500    ASN A 105       39.35     38.39                                   
REMARK 500    ASP A 110     -163.99   -100.31                                   
REMARK 500    LEU A 129       44.07   -148.28                                   
REMARK 500    PHE A 223       95.49   -166.22                                   
REMARK 500    TYR A 257       63.12   -118.66                                   
REMARK 500    TYR B  14       -0.78     73.13                                   
REMARK 500    HIS B  15     -166.79   -126.36                                   
REMARK 500    ALA B  41       18.23     58.29                                   
REMARK 500    ASN B  72       -5.68     88.18                                   
REMARK 500    SER B  81     -111.87     62.40                                   
REMARK 500    ASN B 105       37.63     39.97                                   
REMARK 500    ASP B 110     -162.34   -100.03                                   
REMARK 500    PHE B 223       94.40   -164.94                                   
REMARK 500    TYR C  14       -2.34     73.48                                   
REMARK 500    HIS C  15     -165.90   -124.49                                   
REMARK 500    ALA C  41       16.82     57.96                                   
REMARK 500    ASN C  72       -2.00     76.11                                   
REMARK 500    SER C  81     -112.46     63.23                                   
REMARK 500    ASN C 105       38.13     38.99                                   
REMARK 500    ASP C 110     -163.81   -100.91                                   
REMARK 500    PHE C 223       95.71   -166.37                                   
REMARK 500    TYR D  14       -1.10     72.39                                   
REMARK 500    HIS D  15     -165.25   -125.72                                   
REMARK 500    ALA D  41       17.01     57.94                                   
REMARK 500    ASN D  72       -4.40     65.03                                   
REMARK 500    SER D  81     -111.86     64.52                                   
REMARK 500    ASN D 105       38.19     38.77                                   
REMARK 500    ASP D 110     -162.84   -101.09                                   
REMARK 500    PHE D 223       95.05   -165.04                                   
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 CL D 259                  
DBREF  3DQZ A    1   258  UNP    Q9LFT6   Q9LFT6_ARATH     1    258             
DBREF  3DQZ B    1   258  UNP    Q9LFT6   Q9LFT6_ARATH     1    258             
DBREF  3DQZ C    1   258  UNP    Q9LFT6   Q9LFT6_ARATH     1    258             
DBREF  3DQZ D    1   258  UNP    Q9LFT6   Q9LFT6_ARATH     1    258             
SEQRES   1 A  258  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 A  258  TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 A  258  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 A  258  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 A  258  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 A  258  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 A  258  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 A  258  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 A  258  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 A  258  VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY          
SEQRES  11 A  258  ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 A  258  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 A  258  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 A  258  ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU          
SEQRES  15 A  258  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 A  258  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 A  258  LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 A  258  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 A  258  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 A  258  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET                  
SEQRES   1 B  258  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 B  258  TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 B  258  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 B  258  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 B  258  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 B  258  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 B  258  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 B  258  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 B  258  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 B  258  VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY          
SEQRES  11 B  258  ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 B  258  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 B  258  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 B  258  ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU          
SEQRES  15 B  258  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 B  258  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 B  258  LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 B  258  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 B  258  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 B  258  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET                  
SEQRES   1 C  258  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 C  258  TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 C  258  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 C  258  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 C  258  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 C  258  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 C  258  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 C  258  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 C  258  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 C  258  VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY          
SEQRES  11 C  258  ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 C  258  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 C  258  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 C  258  ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU          
SEQRES  15 C  258  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 C  258  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 C  258  LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 C  258  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 C  258  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 C  258  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET                  
SEQRES   1 D  258  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 D  258  TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 D  258  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 D  258  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 D  258  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 D  258  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 D  258  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 D  258  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 D  258  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 D  258  VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY          
SEQRES  11 D  258  ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 D  258  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 D  258  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 D  258  ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU          
SEQRES  15 D  258  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 D  258  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 D  258  LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 D  258  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 D  258  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 D  258  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET                  
HET     CL  D 259       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *69(H2 O)                                                     
HELIX    1   1 GLY A   16  TYR A   21  5                                   6    
HELIX    2   2 LYS A   22  ALA A   30  1                                   9    
HELIX    3   3 PRO A   48  VAL A   52  5                                   5    
HELIX    4   4 THR A   54  SER A   68  1                                  15    
HELIX    5   5 PHE A   82  ASP A   92  1                                  11    
HELIX    6   6 PHE A   94  ALA A   96  5                                   3    
HELIX    7   7 SER A  116  GLU A  124  1                                   9    
HELIX    8   8 GLY A  150  LEU A  158  1                                   9    
HELIX    9   9 PRO A  163  HIS A  174  1                                  12    
HELIX   10  10 PHE A  180  LYS A  186  1                                   7    
HELIX   11  11 GLY A  194  VAL A  198  5                                   5    
HELIX   12  12 PRO A  212  PHE A  223  1                                  12    
HELIX   13  13 MET A  237  LYS A  242  1                                   6    
HELIX   14  14 LYS A  242  TYR A  257  1                                  16    
HELIX   15  15 GLY B   16  TYR B   21  5                                   6    
HELIX   16  16 LYS B   22  ALA B   30  1                                   9    
HELIX   17  17 PRO B   48  VAL B   52  5                                   5    
HELIX   18  18 THR B   54  SER B   68  1                                  15    
HELIX   19  19 PHE B   82  ASP B   92  1                                  11    
HELIX   20  20 ILE B   93  ALA B   96  5                                   4    
HELIX   21  21 SER B  116  GLU B  124  1                                   9    
HELIX   22  22 GLY B  150  LEU B  158  1                                   9    
HELIX   23  23 PRO B  163  MET B  172  1                                  10    
HELIX   24  24 PHE B  180  LYS B  186  1                                   7    
HELIX   25  25 GLY B  194  VAL B  198  5                                   5    
HELIX   26  26 PRO B  212  PHE B  223  1                                  12    
HELIX   27  27 MET B  237  LYS B  242  1                                   6    
HELIX   28  28 LYS B  242  TYR B  257  1                                  16    
HELIX   29  29 GLY C   16  TYR C   21  5                                   6    
HELIX   30  30 LYS C   22  ALA C   30  1                                   9    
HELIX   31  31 PRO C   48  VAL C   52  5                                   5    
HELIX   32  32 THR C   54  SER C   68  1                                  15    
HELIX   33  33 PHE C   82  ASP C   92  1                                  11    
HELIX   34  34 PHE C   94  ALA C   96  5                                   3    
HELIX   35  35 SER C  116  GLU C  124  1                                   9    
HELIX   36  36 GLY C  150  LEU C  158  1                                   9    
HELIX   37  37 PRO C  163  HIS C  174  1                                  12    
HELIX   38  38 PHE C  180  LYS C  186  1                                   7    
HELIX   39  39 GLY C  194  VAL C  198  5                                   5    
HELIX   40  40 PRO C  212  PHE C  223  1                                  12    
HELIX   41  41 MET C  237  LYS C  242  1                                   6    
HELIX   42  42 LYS C  242  TYR C  257  1                                  16    
HELIX   43  43 GLY D   16  TYR D   21  5                                   6    
HELIX   44  44 LYS D   22  ALA D   30  1                                   9    
HELIX   45  45 PRO D   48  VAL D   52  5                                   5    
HELIX   46  46 THR D   54  SER D   68  1                                  15    
HELIX   47  47 PHE D   82  ASP D   92  1                                  11    
HELIX   48  48 PHE D   94  ALA D   96  5                                   3    
HELIX   49  49 SER D  116  GLU D  124  1                                   9    
HELIX   50  50 GLY D  150  LEU D  158  1                                   9    
HELIX   51  51 PRO D  163  MET D  172  1                                  10    
HELIX   52  52 PHE D  180  LYS D  186  1                                   7    
HELIX   53  53 GLY D  194  VAL D  198  5                                   5    
HELIX   54  54 PRO D  212  PHE D  223  1                                  12    
HELIX   55  55 MET D  237  LYS D  242  1                                   6    
HELIX   56  56 LYS D  242  TYR D  257  1                                  16    
SHEET    1   A 6 ARG A  33  VAL A  37  0                                        
SHEET    2   A 6 HIS A   6  VAL A  10  1  N  LEU A   9   O  THR A  35           
SHEET    3   A 6 VAL A  75  PHE A  80  1  O  VAL A  78   N  VAL A   8           
SHEET    4   A 6 ILE A  98  LEU A 104  1  O  VAL A 102   N  LEU A  77           
SHEET    5   A 6 ARG A 200  SER A 205  1  O  VAL A 203   N  PHE A 103           
SHEET    6   A 6 VAL A 228  ILE A 231  1  O  TYR A 229   N  TYR A 202           
SHEET    1   B 3 GLU A 133  THR A 139  0                                        
SHEET    2   B 3 GLY A 142  LYS A 148 -1  O  LYS A 148   N  GLU A 133           
SHEET    3   B 3 GLY A 177  SER A 178 -1  O  GLY A 177   N  LEU A 147           
SHEET    1   C 6 ARG B  33  VAL B  37  0                                        
SHEET    2   C 6 HIS B   6  VAL B  10  1  N  PHE B   7   O  ARG B  33           
SHEET    3   C 6 VAL B  75  PHE B  80  1  O  VAL B  78   N  VAL B   8           
SHEET    4   C 6 ILE B  98  LEU B 104  1  O  VAL B 102   N  LEU B  77           
SHEET    5   C 6 GLN B 199  SER B 205  1  O  GLN B 199   N  LEU B 101           
SHEET    6   C 6 VAL B 228  ILE B 231  1  O  TYR B 229   N  TYR B 202           
SHEET    1   D 3 GLU B 133  THR B 139  0                                        
SHEET    2   D 3 GLY B 142  LYS B 148 -1  O  LYS B 148   N  GLU B 133           
SHEET    3   D 3 GLY B 177  SER B 178 -1  O  GLY B 177   N  LEU B 147           
SHEET    1   E 6 ARG C  33  VAL C  37  0                                        
SHEET    2   E 6 HIS C   6  VAL C  10  1  N  LEU C   9   O  THR C  35           
SHEET    3   E 6 VAL C  75  PHE C  80  1  O  VAL C  78   N  VAL C   8           
SHEET    4   E 6 ILE C  98  LEU C 104  1  O  VAL C 102   N  LEU C  77           
SHEET    5   E 6 ARG C 200  SER C 205  1  O  VAL C 203   N  PHE C 103           
SHEET    6   E 6 VAL C 228  ILE C 231  1  O  TYR C 229   N  TYR C 202           
SHEET    1   F 3 GLU C 133  THR C 139  0                                        
SHEET    2   F 3 GLY C 142  LYS C 148 -1  O  LYS C 148   N  GLU C 133           
SHEET    3   F 3 GLY C 177  SER C 178 -1  O  GLY C 177   N  LEU C 147           
SHEET    1   G 6 ARG D  33  VAL D  37  0                                        
SHEET    2   G 6 HIS D   6  VAL D  10  1  N  LEU D   9   O  THR D  35           
SHEET    3   G 6 VAL D  75  PHE D  80  1  O  VAL D  78   N  VAL D   8           
SHEET    4   G 6 ILE D  98  LEU D 104  1  O  VAL D 102   N  LEU D  77           
SHEET    5   G 6 ARG D 200  SER D 205  1  O  VAL D 203   N  PHE D 103           
SHEET    6   G 6 VAL D 228  ILE D 231  1  O  TYR D 229   N  TYR D 202           
SHEET    1   H 3 GLU D 133  THR D 139  0                                        
SHEET    2   H 3 GLY D 142  LYS D 148 -1  O  LYS D 148   N  GLU D 133           
SHEET    3   H 3 GLY D 177  SER D 178 -1  O  GLY D 177   N  LEU D 147           
SITE     1 AC1  2 ARG D 175  GLN D 176                                          
CRYST1   50.248  223.313   50.201  90.00 101.47  90.00 P 1 21 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      0.019901  0.000000  0.004038        0.00000                         
SCALE2      0.000000  0.004478  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020326        0.00000                         
MTRIX1   1 -0.892166 -0.224244 -0.392115      -12.09170                         
MTRIX2   1 -0.243977 -0.491335  0.836101        6.46592                         
MTRIX3   1 -0.380151  0.841608  0.383642       -7.37886                         
MTRIX1   2  0.194955 -0.002658 -0.980809      -16.27400                         
MTRIX2   2 -0.005533 -0.999983  0.001611      -56.47510                         
MTRIX3   2 -0.980797  0.005113 -0.194967      -27.60680                         
MTRIX1   3  0.203611  0.223737  0.953144       25.73530                         
MTRIX2   3 -0.869170  0.489421  0.070787       14.54750                         
MTRIX3   3 -0.450651 -0.842857  0.294117      -59.55490                         
TER    2038      MET A 258                                                      
TER    4067      TYR B 257                                                      
TER    6105      MET C 258                                                      
TER    8134      TYR D 257                                                      
MASTER      261    0    1   56   36    0    1   15 8200    4    0   80          
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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