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LongText Report for: 6szo-pdb

Name Class
6szo-pdb
HEADER    HYDROLASE                               02-OCT-19   6SZO              
TITLE     THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS TERRAE IN
TITLE    2 COMPLEX WITH D-GALACTURONATE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE PB90-1;                         
SOURCE   3 ORGANISM_TAXID: 452637;                                              
SOURCE   4 GENE: OTER_0116;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ESTERASE, COMPLEX, BIOMASS, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO             
REVDAT   1   27-NOV-19 6SZO    0                                                
JRNL        AUTH   S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO    
JRNL        TITL   THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS 
JRNL        TITL 2 TERRAE IN COMPLEX WITH D-GALACTURONATE                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.15.2_3472                                   
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16672                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1249                            
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 44.7400 -  4.5700    0.97     1721   136  0.1726 0.2381        
REMARK   3     2  4.5700 -  3.6300    0.98     1731   145  0.1306 0.1779        
REMARK   3     3  3.6300 -  3.1700    0.98     1722   146  0.1331 0.1837        
REMARK   3     4  3.1700 -  2.8800    0.98     1736   139  0.1349 0.1967        
REMARK   3     5  2.8800 -  2.6700    0.97     1715   135  0.1532 0.2360        
REMARK   3     6  2.6700 -  2.5200    0.97     1711   132  0.1716 0.2532        
REMARK   3     7  2.5200 -  2.3900    0.97     1711   132  0.1784 0.2745        
REMARK   3     8  2.3900 -  2.2900    0.96     1710   143  0.1874 0.3295        
REMARK   3     9  2.2900 -  2.2000    0.95     1666   141  0.1955 0.2782        
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)     : 0.242            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.546           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.10                          
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      :  0.012           3020                                  
REMARK   3   ANGLE     :  1.262           4036                                  
REMARK   3   CHIRALITY :  0.063            414                                  
REMARK   3   PLANARITY :  0.009            520                                  
REMARK   3   DIHEDRAL  : 24.172           1088                                  
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 6SZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292104623.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, DESY                    
REMARK 200  BEAMLINE                       : P11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9891                             
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   : 16711                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.198                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.08127                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.6600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47980                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472                                    
REMARK 200 STARTING MODEL: 6GS0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR        
REMARK 280  SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION E8: 0.12 M ETHYLENE    
REMARK 280  GLYCOLS (0.3M DIETHYLENE GLYCOL; 0.3M TRIETHYLENE GLYCOL; 0.3M      
REMARK 280  TETRAETHYLENE GLYCOL; 0.3M PENTAETHYLENE GLYCOL), 0.1 M BUFFER      
REMARK 280  SYSTEM 2 PH 7.5 (SODIUM HEPES; MOPS), AND 50 % V/V PRECIPITANT      
REMARK 280  MIX 4 (25% V/V MPD; 25% PEG 1000; 25% W/V PEG 3350), VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 92.0 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     MET A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     HIS A    18                                                      
REMARK 465     HIS A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     ASN A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     GLN A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     HIS A   148                                                      
REMARK 465     THR A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     ALA A   152                                                      
REMARK 465     ILE A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     LEU A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     TRP A   159                                                      
REMARK 465     ILE A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     ALA A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     ALA A   164                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     ASN A   169                                                      
REMARK 465     HIS A   170                                                      
REMARK 465     ARG A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     THR A   173                                                      
REMARK 465     GLU A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     ALA A   176                                                      
REMARK 465     ARG A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     LEU A   220                                                      
REMARK 465     ASP A   221                                                      
REMARK 465     ALA A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     SER A   428                                                      
REMARK 465     ALA A   429                                                      
REMARK 465     LEU A   430                                                      
REMARK 465     PRO A   431                                                      
REMARK 465     ALA A   432                                                      
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   OD2  ASP A   207    HH11  ARG A   268              1.51            
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    TYR A  34       69.37   -164.86                                   
REMARK 500    VAL A  70      -67.72   -122.55                                   
REMARK 500    ALA A  92       39.58   -140.97                                   
REMARK 500    HIS A 145       38.79    -96.74                                   
REMARK 500    GLN A 182      -31.80    113.66                                   
REMARK 500    LYS A 183      124.25    -26.30                                   
REMARK 500    GLN A 227     -160.94   -176.38                                   
REMARK 500    ALA A 267     -125.46     53.98                                   
REMARK 500    HIS A 328       43.57   -146.43                                   
REMARK 500    ASP A 360       79.30     65.18                                   
REMARK 500    HIS A 408      127.56    -39.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 506  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 303   O                                                      
REMARK 620 2 GLU A 305   O    95.6                                              
REMARK 620 3 HOH A 641   O    93.2  95.9                                        
REMARK 620 4 HOH A 689   O   163.9  83.0 102.9                                  
REMARK 620 5 HOH A 637   O    91.3 153.9 108.8  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GTR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 537                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 538                 
DBREF  6SZO A   33   432  UNP    B1ZMF4   B1ZMF4_OPITP    33    432             
SEQADV 6SZO MET A   12  UNP  B1ZMF4              INITIATING METHIONINE          
SEQADV 6SZO GLY A   13  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO SER A   14  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO SER A   15  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   16  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   17  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   18  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   19  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   20  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   21  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO SER A   22  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO SER A   23  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO GLU A   24  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO ASN A   25  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO LEU A   26  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO TYR A   27  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO PHE A   28  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO GLN A   29  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO GLY A   30  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO HIS A   31  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO SER A   32  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6SZO ALA A  267  UNP  B1ZMF4    SER   267 ENGINEERED MUTATION            
SEQRES   1 A  421  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU          
SEQRES   2 A  421  ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO          
SEQRES   3 A  421  ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP          
SEQRES   4 A  421  ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU          
SEQRES   5 A  421  GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU          
SEQRES   6 A  421  GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET          
SEQRES   7 A  421  GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU          
SEQRES   8 A  421  VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER          
SEQRES   9 A  421  MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA          
SEQRES  10 A  421  ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE          
SEQRES  11 A  421  TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA          
SEQRES  12 A  421  LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY          
SEQRES  13 A  421  ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP          
SEQRES  14 A  421  ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY          
SEQRES  15 A  421  TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO          
SEQRES  16 A  421  ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP          
SEQRES  17 A  421  LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA          
SEQRES  18 A  421  TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG          
SEQRES  19 A  421  ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA          
SEQRES  20 A  421  SER ARG VAL ALA VAL HIS GLY HIS ALA ARG LEU GLY LYS          
SEQRES  21 A  421  ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA          
SEQRES  22 A  421  LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA          
SEQRES  23 A  421  LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE          
SEQRES  24 A  421  ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG          
SEQRES  25 A  421  ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN          
SEQRES  26 A  421  HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR          
SEQRES  27 A  421  VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG          
SEQRES  28 A  421  GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE          
SEQRES  29 A  421  ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL          
SEQRES  30 A  421  PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR          
SEQRES  31 A  421  HIS ILE ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP          
SEQRES  32 A  421  TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS          
SEQRES  33 A  421  SER ALA LEU PRO ALA                                          
HET    GTR  A 501      22                                                       
HET    DMS  A 502      10                                                       
HET    DMS  A 503      10                                                       
HET    DMS  A 504      10                                                       
HET    DMS  A 505      10                                                       
HET     MG  A 506       1                                                       
HET    EDO  A 507      10                                                       
HET    EDO  A 508      10                                                       
HET    EDO  A 509      10                                                       
HET    EDO  A 510      10                                                       
HET    EDO  A 511      10                                                       
HET    EDO  A 512      10                                                       
HET    EDO  A 513      10                                                       
HET    EDO  A 514      10                                                       
HET    EDO  A 515      10                                                       
HET    EDO  A 516      10                                                       
HET    EDO  A 517      10                                                       
HET    EDO  A 518      10                                                       
HET    EDO  A 519      10                                                       
HET    EDO  A 520      10                                                       
HET    EDO  A 521      10                                                       
HET    EDO  A 522      10                                                       
HET    EDO  A 523      10                                                       
HET    EDO  A 524      10                                                       
HET    EDO  A 525      10                                                       
HET    EDO  A 526      10                                                       
HET    EDO  A 527      10                                                       
HET    EDO  A 528      10                                                       
HET    EDO  A 529      10                                                       
HET    EDO  A 530      10                                                       
HET    PEG  A 531      17                                                       
HET    PEG  A 532      17                                                       
HET    PEG  A 533      17                                                       
HET    PEG  A 534      17                                                       
HET    PGE  A 535      24                                                       
HET    PGE  A 536      24                                                       
HET    PGE  A 537      24                                                       
HET    PGE  A 538      24                                                       
HETNAM     GTR BETA-D-GALACTOPYRANURONIC ACID                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     GTR GALACTURONIC ACID                                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  GTR    C6 H10 O7                                                    
FORMUL   3  DMS    4(C2 H6 O S)                                                 
FORMUL   7   MG    MG 2+                                                        
FORMUL   8  EDO    24(C2 H6 O2)                                                 
FORMUL  32  PEG    4(C4 H10 O3)                                                 
FORMUL  36  PGE    4(C6 H14 O4)                                                 
FORMUL  40  HOH   *122(H2 O)                                                    
HELIX    1 AA1 ASP A   50  ARG A   57  1                                   8    
HELIX    2 AA2 ARG A   57  VAL A   70  1                                  14    
HELIX    3 AA3 LEU A   94  GLY A   96  5                                   3    
HELIX    4 AA4 ASN A  124  ALA A  128  1                                   5    
HELIX    5 AA5 GLY A  143  HIS A  145  5                                   3    
HELIX    6 AA6 THR A  146  VAL A  147  1                                   2    
HELIX    7 AA7 GLN A  182  TRP A  184  1                                   3    
HELIX    8 AA8 PRO A  185  ARG A  192  1                                   8    
HELIX    9 AA9 GLY A  202  LEU A  204  5                                   3    
HELIX   10 AB1 ASP A  210  TRP A  219  5                                  10    
HELIX   11 AB2 GLY A  234  ASP A  253  1                                  20    
HELIX   12 AB3 ALA A  267  ASP A  280  1                                  14    
HELIX   13 AB4 LEU A  298  ILE A  302  5                                   5    
HELIX   14 AB5 THR A  306  PHE A  314  1                                   9    
HELIX   15 AB6 ALA A  319  ASP A  326  5                                   8    
HELIX   16 AB7 HIS A  328  LEU A  332  5                                   5    
HELIX   17 AB8 ASP A  335  LEU A  342  1                                   8    
HELIX   18 AB9 ASP A  356  ALA A  359  5                                   4    
HELIX   19 AC1 ASP A  360  PHE A  378  1                                  19    
HELIX   20 AC2 THR A  411  LYS A  427  1                                  17    
SHEET    1 AA110 VAL A  83  ALA A  93  0                                        
SHEET    2 AA110 ALA A  98  ARG A 106 -1  O  ARG A 106   N  VAL A  83           
SHEET    3 AA110 SER A 115  PRO A 123 -1  O  MET A 116   N  VAL A 105           
SHEET    4 AA110 ALA A 195  TYR A 200 -1  O  VAL A 196   N  TYR A 121           
SHEET    5 AA110 ALA A 133  ASN A 140  1  N  PRO A 134   O  ALA A 195           
SHEET    6 AA110 VAL A 256  HIS A 266  1  O  ALA A 262   N  VAL A 135           
SHEET    7 AA110 LEU A 285  ASN A 289  1  O  LEU A 285   N  VAL A 263           
SHEET    8 AA110 LEU A 348  ALA A 353  1  O  TYR A 349   N  SER A 288           
SHEET    9 AA110 LEU A 399  ARG A 404  1  O  ARG A 400   N  VAL A 350           
SHEET   10 AA110 SER A 395  GLY A 396 -1  N  SER A 395   O  TYR A 401           
LINK         O   HIS A 303                MG    MG A 506     1555   1555  2.34  
LINK         O   GLU A 305                MG    MG A 506     1555   1555  2.29  
LINK        MG    MG A 506                 O   HOH A 641     1555   1555  2.47  
LINK        MG    MG A 506                 O   HOH A 689     1555   1555  2.44  
LINK        MG    MG A 506                 O   HOH A 637     1555   1555  2.39  
CISPEP   1 ALA A  344    PRO A  345          0        -2.14                     
SITE     1 AC1 14 ALA A 267  ARG A 268  LYS A 271  SER A 291                    
SITE     2 AC1 14 GLU A 305  ILE A 310  PHE A 314  TRP A 358                    
SITE     3 AC1 14 HIS A 408  DMS A 502  HOH A 642  HOH A 645                    
SITE     4 AC1 14 HOH A 673  HOH A 687                                          
SITE     1 AC2  5 HIS A 266  ALA A 267  ARG A 268  GTR A 501                    
SITE     2 AC2  5 DMS A 505                                                     
SITE     1 AC3  4 ALA A  43  PEG A 532  PGE A 536  HOH A 665                    
SITE     1 AC4  6 ARG A 129  GLU A 131  ASN A 311  THR A 312                    
SITE     2 AC4  6 ARG A 323  ASP A 326                                          
SITE     1 AC5  4 TYR A 142  GLN A 182  DMS A 502  EDO A 527                    
SITE     1 AC6  5 HIS A 303  GLU A 305  HOH A 637  HOH A 641                    
SITE     2 AC6  5 HOH A 689                                                     
SITE     1 AC7  2 TYR A  34  LEU A  36                                          
SITE     1 AC8  3 ARG A  51  ASN A 112  LEU A 377                               
SITE     1 AC9  5 GLU A 131  ARG A 132  GLN A 227  PRO A 254                    
SITE     2 AC9  5 HOH A 626                                                     
SITE     1 AD1  5 ALA A  97  PRO A 123  ASN A 124  ALA A 125                    
SITE     2 AD1  5 ALA A 191                                                     
SITE     1 AD2  5 TRP A 241  SER A 244  ARG A 245  GLN A 279                    
SITE     2 AD2  5 HOH A 605                                                     
SITE     1 AD3  3 PRO A 394  SER A 395  GLY A 396                               
SITE     1 AD4  3 ARG A 208  PRO A 209  ASP A 210                               
SITE     1 AD5  3 ASP A 207  ARG A 268  HOH A 693                               
SITE     1 AD6  3 ALA A  43  GLN A 413  PEG A 532                               
SITE     1 AD7  5 ASP A  44  PRO A 394  PHE A 417  PGE A 536                    
SITE     2 AD7  5 HOH A 644                                                     
SITE     1 AD8  4 ALA A  67  THR A  74  GLN A 279  HOH A 627                    
SITE     1 AD9  5 GLU A 251  THR A 252  ASP A 253  PRO A 254                    
SITE     2 AD9  5 HOH A 608                                                     
SITE     1 AE1  3 SER A 259  ASP A 281  HOH A 601                               
SITE     1 AE2  4 GLN A 380  THR A 381  GLY A 397  ALA A 398                    
SITE     1 AE3  5 LYS A 101  TYR A 249  THR A 252  ASP A 253                    
SITE     2 AE3  5 PRO A 254                                                     
SITE     1 AE4  3 ASP A  50  ARG A  51  ALA A  52                               
SITE     1 AE5  2 PRO A 345  GLN A 380                                          
SITE     1 AE6  4 ARG A 129  GLU A 131  ARG A 260  LYS A 427                    
SITE     1 AE7  5 GLN A 182  TRP A 184  HIS A 266  MET A 410                    
SITE     2 AE7  5 DMS A 505                                                     
SITE     1 AE8  2 HIS A  56  ARG A  57                                          
SITE     1 AE9  3 ASN A 124  HOH A 616  HOH A 676                               
SITE     1 AF1  2 ARG A 228  TRP A 233                                          
SITE     1 AF2  6 ALA A  43  LEU A  65  ARG A  68  GLN A 188                    
SITE     2 AF2  6 ALA A 412  ALA A 416                                          
SITE     1 AF3  5 ASP A  38  VAL A  41  ARG A  58  DMS A 503                    
SITE     2 AF3  5 EDO A 517                                                     
SITE     1 AF4  5 LYS A  85  THR A 104  ARG A 106  ASP A 355                    
SITE     2 AF4  5 HOH A 674                                                     
SITE     1 AF5  7 ASP A 110  ASP A 355  ASP A 356  ASP A 357                    
SITE     2 AF5  7 TRP A 358  PRO A 407  HIS A 408                               
SITE     1 AF6  9 ALA A 128  ARG A 129  ALA A 130  PRO A 209                    
SITE     2 AF6  9 GLN A 227  ARG A 228  PRO A 315  ARG A 320                    
SITE     3 AF6  9 ARG A 323                                                     
SITE     1 AF7  7 GLY A  45  ASN A 392  GLU A 393  PRO A 394                    
SITE     2 AF7  7 DMS A 503  EDO A 518  HOH A 665                               
SITE     1 AF8  5 PHE A 141  TYR A 200  GLY A 202  PRO A 206                    
SITE     2 AF8  5 ASP A 207                                                     
SITE     1 AF9  5 TYR A  34  GLU A  80  ARG A 301  HIS A 303                    
SITE     2 AF9  5 ARG A 362                                                     
CRYST1   44.626   46.138   50.195  63.65  86.79  71.17 P 1           1          
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      0.022408 -0.007643  0.002451        0.00000                         
SCALE2      0.000000  0.022900 -0.011557        0.00000                         
SCALE3      0.000000  0.000000  0.022351        0.00000                         
TER    5433      LYS A 427                                                      
MASTER      462    0   38   20   10    0   58    6 3098    1  473   33          
END                                                                             

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