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LongText Report for: 6xyc-pdb

Name Class
6xyc-pdb
HEADER    HYDROLASE                               30-JAN-20   6XYC              
TITLE     TRUNCATED FORM OF CARBOHYDRATE ESTERASE FROM GUT MICROBIOTA           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL XYLAN ESTERASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METAGENOME;                                     
SOURCE   3 ORGANISM_TAXID: 256318;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ACETYL XYLAN ESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.PENTTINEN,N.HAKULINEN,E.MASTER                                      
REVDAT   1   27-JAN-21 6XYC    0                                                
JRNL        AUTH   L.PENTTINEN,L.HAMELEERS,N.HAKULINEN,E.MASTER,E.JURAK         
JRNL        TITL   CRYSTAL STRUCTURE AND CHARACTERIZATION OF AN ACETYL XYLAN    
JRNL        TITL 2 ESTERASE FROM BEAVER GUT METAGENOMICS                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22925                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1147                            
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 29.8300 -  3.6900    1.00     2908   153  0.1588 0.1784        
REMARK   3     2  3.6900 -  2.9300    1.00     2760   146  0.1701 0.1925        
REMARK   3     3  2.9300 -  2.5600    1.00     2724   143  0.1726 0.1927        
REMARK   3     4  2.5600 -  2.3300    1.00     2701   142  0.1705 0.2128        
REMARK   3     5  2.3300 -  2.1600    1.00     2711   143  0.1806 0.2092        
REMARK   3     6  2.1600 -  2.0300    1.00     2670   141  0.1970 0.2484        
REMARK   3     7  2.0300 -  1.9300    1.00     2664   140  0.2236 0.2735        
REMARK   3     8  1.9300 -  1.8500    0.99     2640   139  0.2696 0.3161        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.507           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.03                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           2236                                  
REMARK   3   ANGLE     :  0.701           3047                                  
REMARK   3   CHIRALITY :  0.047            336                                  
REMARK   3   PLANARITY :  0.004            397                                  
REMARK   3   DIHEDRAL  :  2.546           1784                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 6XYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292106528.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-18                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9159                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.984                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.2600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
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: PHASER                                                
REMARK 200 STARTING MODEL: 6TKX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 30 % PEG MME     
REMARK 280  5000, 0.1 M MES PH 6.0, PROTEIN CONCENTRATION 12 MG/ML, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       22.18900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       53.78000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       53.78000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.28350            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       53.78000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       53.78000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       11.09450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       53.78000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.78000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       33.28350            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       53.78000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.78000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       11.09450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       22.18900            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 410 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 465     HIS A   300                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   192     OG   SER A   194              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  41      100.06    -54.33                                   
REMARK 500    SER A  55       20.35   -168.16                                   
REMARK 500    ASN A  61       20.35   -147.86                                   
REMARK 500    SER A 128     -121.51     48.59                                   
REMARK 500    PHE A 176       55.34     36.06                                   
REMARK 500    VAL A 239      -56.14   -120.68                                   
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 AES A 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6TKX   RELATED DB: PDB                                   
DBREF  6XYC A    8   300  PDB    6XYC     6XYC             8    300             
SEQRES   1 A  293  LYS GLY PRO ALA GLU ASP THR TYR SER THR SER TRP THR          
SEQRES   2 A  293  ASN VAL ASN TYR ALA SER ASP SER LEU GLU SER HIS ASN          
SEQRES   3 A  293  LEU ASP ILE TYR LEU PRO LYS GLU GLN LYS THR ALA TYR          
SEQRES   4 A  293  LYS ALA ILE ILE ILE ILE TYR GLY SER ALA TRP PHE ALA          
SEQRES   5 A  293  ASN ASN ALA LYS ALA MET ALA SER ALA SER ILE GLY ALA          
SEQRES   6 A  293  PRO LEU LEU LYS ALA GLY PHE ALA VAL ILE SER ILE ASN          
SEQRES   7 A  293  HIS ARG SER SER MET GLU ALA ILE TRP PRO ALA GLN ILE          
SEQRES   8 A  293  GLN ASP VAL LYS ALA ALA ILE ARG TYR VAL ARG SER ASN          
SEQRES   9 A  293  ALA ALA LYS TYR ASN ILE ASP PRO SER PHE ILE GLY ILE          
SEQRES  10 A  293  THR GLY PHE SER SER GLY GLY HIS LEU SER ALA PHE ALA          
SEQRES  11 A  293  GLY VAL THR ASN GLY VAL LYS THR LEU THR SER GLY ASP          
SEQRES  12 A  293  LEU THR VAL ASP ILE GLU GLY SER LEU GLY ASN TYR LEU          
SEQRES  13 A  293  SER THR GLY SER HIS VAL ASP ALA VAL VAL ASP TRP PHE          
SEQRES  14 A  293  GLY PRO VAL ASP MET ALA HIS MET SER ASN CYS VAL ALA          
SEQRES  15 A  293  PRO ASN ASP ALA SER THR PRO GLU ALA VAL LEU ILE GLY          
SEQRES  16 A  293  LYS LYS ASP PRO ARG GLU GLU PRO ASP TRP VAL LYS LEU          
SEQRES  17 A  293  ILE SER PRO ILE ASN PHE VAL ASP LYS ASP ASP PRO ASP          
SEQRES  18 A  293  ILE LEU ILE ILE HIS GLY ASP ALA ASP ASN VAL VAL PRO          
SEQRES  19 A  293  HIS CYS GLN SER VAL ASN LEU LYS ASN VAL TYR ASP ASN          
SEQRES  20 A  293  ALA GLY ALA LYS ALA THR PHE ILE SER VAL PRO GLY GLY          
SEQRES  21 A  293  GLY HIS GLY PRO GLY CYS PHE ASP THR GLN TYR PHE LYS          
SEQRES  22 A  293  ASP MET THR ASP PHE PHE THR GLU GLN SER THR LYS LEU          
SEQRES  23 A  293  GLU HIS HIS HIS HIS HIS HIS                                  
HET    AES  A 701      22                                                       
HETNAM     AES 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE                         
HETSYN     AES AEBSF                                                            
FORMUL   2  AES    C8 H10 F N O2 S                                              
FORMUL   3  HOH   *189(H2 O)                                                    
HELIX    1 AA1 ALA A   11  ASP A   13  5                                   3    
HELIX    2 AA2 LEU A   29  SER A   31  5                                   3    
HELIX    3 AA3 ALA A   62  ALA A   77  1                                  16    
HELIX    4 AA4 PRO A   95  ASN A  111  1                                  17    
HELIX    5 AA5 ALA A  112  TYR A  115  5                                   4    
HELIX    6 AA6 SER A  128  VAL A  139  1                                  12    
HELIX    7 AA7 ASP A  180  VAL A  188  5                                   9    
HELIX    8 AA8 THR A  195  ILE A  201  1                                   7    
HELIX    9 AA9 ASP A  205  GLU A  208  5                                   4    
HELIX   10 AB1 GLU A  209  ILE A  216  1                                   8    
HELIX   11 AB2 SER A  217  VAL A  222  5                                   6    
HELIX   12 AB3 HIS A  242  GLY A  256  1                                  15    
HELIX   13 AB4 ASP A  275  LYS A  292  1                                  18    
SHEET    1 AA1 8 TYR A  15  ASN A  23  0                                        
SHEET    2 AA1 8 ASN A  33  PRO A  39 -1  O  ILE A  36   N  TRP A  19           
SHEET    3 AA1 8 ALA A  80  ILE A  84 -1  O  VAL A  81   N  TYR A  37           
SHEET    4 AA1 8 TYR A  46  ILE A  52  1  N  LYS A  47   O  ALA A  80           
SHEET    5 AA1 8 ILE A 117  PHE A 127  1  O  ASP A 118   N  TYR A  46           
SHEET    6 AA1 8 ALA A 171  TRP A 175  1  O  TRP A 175   N  GLY A 126           
SHEET    7 AA1 8 ILE A 229  GLY A 234  1  O  LEU A 230   N  ASP A 174           
SHEET    8 AA1 8 ALA A 259  VAL A 264  1  O  THR A 260   N  ILE A 231           
SHEET    1 AA2 2 THR A 145  SER A 148  0                                        
SHEET    2 AA2 2 LEU A 151  ASP A 154 -1  O  LEU A 151   N  SER A 148           
SSBOND   1 CYS A  187    CYS A  243                          1555   1555  2.03  
LINK         OG  SER A 128                 S   AES A 701     1555   1555  1.47  
CISPEP   1 TRP A   94    PRO A   95          0         7.84                     
SITE     1 AC1 14 SER A  55  ALA A  56  SER A 128  SER A 129                    
SITE     2 AC1 14 PRO A 178  MET A 184  VAL A 188  ASN A 191                    
SITE     3 AC1 14 PRO A 196  GLU A 197  VAL A 239  HIS A 269                    
SITE     4 AC1 14 HOH A 811  HOH A 876                                          
CRYST1  107.560  107.560   44.378  90.00  90.00  90.00 P 43 21 2     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      0.009297  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009297  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022534        0.00000                         
TER    4253      LYS A 292                                                      
MASTER      271    0    1   13   10    0    4    6 2356    1   25   23          
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.
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