Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6t0i-pdb

Name Class
6t0i-pdb
HEADER    HYDROLASE                               03-OCT-19   6T0I              
TITLE     THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS TERRAE IN    
TITLE    2 COMPLEX WITH THE ALDOTETRAURONIC ACID XUX                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE;                                
SOURCE   3 ORGANISM_TAXID: 107709;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 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 6T0I    0                                                
JRNL        AUTH   S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO    
JRNL        TITL   THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS     
JRNL        TITL 2 TERRAE IN COMPLEX WITH THE ALDOTETRAURONIC ACID XUX          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 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) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42107                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4168                            
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 32.4900 -  4.7600    0.98     1403   160  0.1642 0.1977        
REMARK   3     2  4.7600 -  3.7800    0.99     1421   154  0.1138 0.1363        
REMARK   3     3  3.7800 -  3.3100    0.98     1406   158  0.1236 0.1532        
REMARK   3     4  3.3100 -  3.0000    0.98     1392   158  0.1292 0.1472        
REMARK   3     5  3.0000 -  2.7900    0.98     1396   156  0.1356 0.1673        
REMARK   3     6  2.7900 -  2.6200    0.98     1401   154  0.1284 0.1640        
REMARK   3     7  2.6200 -  2.4900    0.86     1242   140  0.1418 0.2074        
REMARK   3     8  2.4900 -  2.3800    0.69      968   110  0.1446 0.1867        
REMARK   3     9  2.3800 -  2.2900    0.81     1167   121  0.1368 0.1583        
REMARK   3    10  2.2900 -  2.2100    0.85     1210   140  0.1487 0.2064        
REMARK   3    11  2.2100 -  2.1400    0.88     1269   130  0.1511 0.1975        
REMARK   3    12  2.1400 -  2.0800    0.88     1263   143  0.1540 0.2291        
REMARK   3    13  2.0800 -  2.0300    0.89     1263   145  0.1673 0.2235        
REMARK   3    14  2.0300 -  1.9800    0.90     1291   140  0.1629 0.2019        
REMARK   3    15  1.9800 -  1.9300    0.91     1291   142  0.1680 0.2248        
REMARK   3    16  1.9300 -  1.8900    0.90     1280   144  0.2021 0.2324        
REMARK   3    17  1.8900 -  1.8500    0.90     1312   145  0.1870 0.2193        
REMARK   3    18  1.8500 -  1.8200    0.92     1294   141  0.2002 0.2580        
REMARK   3    19  1.8200 -  1.7900    0.91     1317   147  0.2137 0.2523        
REMARK   3    20  1.7900 -  1.7600    0.92     1306   140  0.2434 0.2756        
REMARK   3    21  1.7600 -  1.7300    0.91     1313   140  0.2554 0.2853        
REMARK   3    22  1.7300 -  1.7000    0.93     1310   144  0.2776 0.3233        
REMARK   3    23  1.7000 -  1.6800    0.91     1304   153  0.2931 0.3325        
REMARK   3    24  1.6800 -  1.6500    0.92     1350   133  0.3358 0.3974        
REMARK   3    25  1.6500 -  1.6300    0.92     1300   145  0.3731 0.3883        
REMARK   3    26  1.6300 -  1.6100    0.91     1290   147  0.3854 0.4110        
REMARK   3    27  1.6100 -  1.5900    0.93     1335   138  0.3380 0.3615        
REMARK   3    28  1.5900 -  1.5700    0.91     1308   148  0.3393 0.3408        
REMARK   3    29  1.5700 -  1.5500    0.92     1317   137  0.3875 0.3904        
REMARK   3    30  1.5500 -  1.5300    0.15      220    15  0.8076 0.8522        
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)     : 0.266            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.871           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.33                          
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      :  0.010           3299                                  
REMARK   3   ANGLE     :  1.159           4474                                  
REMARK   3   CHIRALITY :  0.063            473                                  
REMARK   3   PLANARITY :  0.008            590                                  
REMARK   3   DIHEDRAL  : 21.291           1196                                  
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 6T0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292104614.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-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               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.04434                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.33000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.720                              
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   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
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 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     ALA A    33                                                      
REMARK 465     TYR A    34                                                      
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   OE1  GLN A    64    HH22  ARG A    73              1.54            
REMARK 500   O4B  XYP A   502     C2B  XYP A   503              2.17            
REMARK 500   C4B  XYP A   502     C1B  XYP A   503              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    VAL A  70      -72.19   -125.09                                   
REMARK 500    ASP A 150      105.30    -28.05                                   
REMARK 500    SER A 267     -124.16     58.13                                   
REMARK 500    SER A 267     -119.73     42.47                                   
REMARK 500    HIS A 328       35.59   -144.97                                   
REMARK 500    ASP A 356       57.73    -90.38                                   
REMARK 500    ASP A 360       71.40     59.78                                   
REMARK 500    LYS A 427      -39.34   -159.33                                   
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                               K A 506   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 250   O                                                      
REMARK 620 2 GLU A 251   O    75.2                                              
REMARK 620 3 ASP A 253   O    82.7 109.1                                        
REMARK 620 4 VAL A 256   O   104.0 171.0  79.5                                  
REMARK 620 5 HOH A 790   O   108.4  88.9 161.0  82.9                            
REMARK 620 6 HOH A 838   O   148.6  79.1  89.0 104.2  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 303   O                                                      
REMARK 620 2 GLU A 305   O    93.2                                              
REMARK 620 3 HOH A 771   O   101.9  95.3                                        
REMARK 620 4 HOH A 622   O    84.1  81.9 173.5                                  
REMARK 620 5 HOH A 815   O   159.3  87.4  98.6  75.5                            
REMARK 620 6 HOH A 682   O    86.0 154.9 109.4  73.1  84.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 506                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues XYP A    
REMARK 800  501 through GCV A 504                                               
DBREF  6T0I A   33   432  UNP    B1ZMF4   B1ZMF4_OPITP    33    432             
SEQADV 6T0I MET A   12  UNP  B1ZMF4              INITIATING METHIONINE          
SEQADV 6T0I GLY A   13  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I SER A   14  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I SER A   15  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   16  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   17  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   18  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   19  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   20  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   21  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I SER A   22  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I SER A   23  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I GLU A   24  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I ASN A   25  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I LEU A   26  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I TYR A   27  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I PHE A   28  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I GLN A   29  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I GLY A   30  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I HIS A   31  UNP  B1ZMF4              EXPRESSION TAG                 
SEQADV 6T0I SER A   32  UNP  B1ZMF4              EXPRESSION TAG                 
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 SER 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    XYP  A 501      19                                                       
HET    XYP  A 502      15                                                       
HET    XYP  A 503      18                                                       
HET    GCV  A 504      24                                                       
HET     MG  A 505       1                                                       
HET      K  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    PEG  A 523      17                                                       
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID                               
HETNAM      MG MAGNESIUM ION                                                    
HETNAM       K POTASSIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  XYP    3(C5 H10 O5)                                                 
FORMUL   2  GCV    C7 H12 O7                                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4    K    K 1+                                                         
FORMUL   5  EDO    16(C2 H6 O2)                                                 
FORMUL  21  PEG    C4 H10 O3                                                    
FORMUL  22  HOH   *258(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  VAL A  147  5                                   5    
HELIX    6 AA6 THR A  173  ARG A  177  5                                   5    
HELIX    7 AA7 ASP A  180  TRP A  184  5                                   5    
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  ALA A  214  5                                   5    
HELIX   11 AB2 SER A  215  ASP A  221  1                                   7    
HELIX   12 AB3 GLY A  234  ASP A  253  1                                  20    
HELIX   13 AB4 SER A  267  ASP A  280  1                                  14    
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  LEU A  426  1                                  16    
SHEET    1 AA1 9 VAL A  83  ALA A  93  0                                        
SHEET    2 AA1 9 ALA A  98  ARG A 106 -1  O  ARG A 106   N  VAL A  83           
SHEET    3 AA1 9 SER A 115  PRO A 123 -1  O  LEU A 118   N  VAL A 103           
SHEET    4 AA1 9 ALA A 195  TYR A 200 -1  O  THR A 198   N  LEU A 119           
SHEET    5 AA1 9 ALA A 133  ASN A 140  1  N  PRO A 134   O  ALA A 195           
SHEET    6 AA1 9 VAL A 256  HIS A 266  1  O  ALA A 262   N  LEU A 137           
SHEET    7 AA1 9 LEU A 285  ASN A 289  1  O  LEU A 285   N  VAL A 263           
SHEET    8 AA1 9 LEU A 348  ALA A 353  1  O  TYR A 349   N  SER A 288           
SHEET    9 AA1 9 LEU A 399  ARG A 404  1  O  ARG A 400   N  VAL A 350           
LINK         O   LEU A 250                 K     K A 506     1555   1555  2.75  
LINK         O   GLU A 251                 K     K A 506     1555   1555  2.85  
LINK         O   ASP A 253                 K     K A 506     1555   1555  2.65  
LINK         O   VAL A 256                 K     K A 506     1555   1555  2.77  
LINK         O   HIS A 303                MG    MG A 505     1555   1555  2.22  
LINK         O   GLU A 305                MG    MG A 505     1555   1555  2.27  
LINK         O4B XYP A 501                 C1B XYP A 502     1555   1555  1.37  
LINK         C2B XYP A 502                 O1  GCV A 504     1555   1555  1.38  
LINK         O4B XYP A 502                 C1B XYP A 503     1555   1555  1.38  
LINK        MG    MG A 505                 O   HOH A 771     1555   1555  2.31  
LINK        MG    MG A 505                 O   HOH A 622     1555   1555  2.62  
LINK        MG    MG A 505                 O   HOH A 815     1555   1555  2.50  
LINK        MG    MG A 505                 O   HOH A 682     1555   1555  2.27  
LINK         K     K A 506                 O   HOH A 790     1555   1555  2.69  
LINK         K     K A 506                 O   HOH A 838     1555   1555  3.03  
CISPEP   1 ALA A  344    PRO A  345          0         4.47                     
SITE     1 AC1  6 HIS A 303  GLU A 305  HOH A 622  HOH A 682                    
SITE     2 AC1  6 HOH A 771  HOH A 815                                          
SITE     1 AC2  6 LEU A 250  GLU A 251  ASP A 253  VAL A 256                    
SITE     2 AC2  6 HOH A 790  HOH A 838                                          
SITE     1 AC3  4 GLU A  69  ALA A 412  HOH A 805  HOH A 814                    
SITE     1 AC4  6 ALA A  67  ARG A  73  THR A  74  GLN A 279                    
SITE     2 AC4  6 HOH A 658  HOH A 684                                          
SITE     1 AC5  6 GLY A  81  ARG A 109  ARG A 362  VAL A 388                    
SITE     2 AC5  6 HOH A 629  HOH A 656                                          
SITE     1 AC6  2 ASN A 392  PRO A 394                                          
SITE     1 AC7  3 ALA A  43  GLN A 413  EDO A 519                               
SITE     1 AC8  2 SER A 395  GLY A 396                                          
SITE     1 AC9  3 VAL A  86  THR A  87  GLU A 330                               
SITE     1 AD1  1 GLU A 131                                                     
SITE     1 AD2  6 ARG A 268  PHE A 314  XYP A 501  HOH A 699                    
SITE     2 AD2  6 HOH A 717  HOH A 786                                          
SITE     1 AD3  5 HIS A 408  XYP A 502  XYP A 503  GCV A 504                    
SITE     2 AD3  5 HOH A 699                                                     
SITE     1 AD4  3 PRO A  79  GLU A  80  HOH A 604                               
SITE     1 AD5  3 LYS A  85  THR A 104  ARG A 106                               
SITE     1 AD6  8 ASP A  38  VAL A  41  GLY A  42  ALA A  43                    
SITE     2 AD6  8 ARG A  58  EDO A 511  HOH A 639  HOH A 774                    
SITE     1 AD7  3 THR A  74  GLY A  95  HOH A 636                               
SITE     1 AD8  3 HIS A  56  ARG A  57  ALA A 191                               
SITE     1 AD9  2 HOH A 767  HOH A 796                                          
SITE     1 AE1  6 ALA A 152  ILE A 153  ALA A 154  LEU A 155                    
SITE     2 AE1  6 ARG A 177  HOH A 611                                          
SITE     1 AE2 20 ALA A  52  GLN A  55  HIS A  56  SER A 267                    
SITE     2 AE2 20 ARG A 268  LYS A 271  SER A 291  GLU A 305                    
SITE     3 AE2 20 ILE A 310  VAL A 313  PHE A 314  TRP A 317                    
SITE     4 AE2 20 TRP A 358  PRO A 407  HIS A 408  EDO A 515                    
SITE     5 AE2 20 EDO A 516  HOH A 711  HOH A 744  HOH A 747                    
CRYST1   43.406   44.173   50.237  75.80  65.49  70.98 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      0.023038 -0.007940 -0.009567        0.00000                         
SCALE2      0.000000  0.023945 -0.003091        0.00000                         
SCALE3      0.000000  0.000000  0.022059        0.00000                         
TER    6084      PRO A 431                                                      
MASTER      385    0   23   20    9    0   32    6 3440    1  269   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:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer