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LongText Report for: 6g17-pdb

Name Class
6g17-pdb
HEADER    HYDROLASE                               20-MAR-18   6G17              
TITLE     NON-AGED FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED BY
TITLE    2 NERVE AGENT TABUN                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;                         
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    ACETYLCHOLINESTERASE, TABUN, NERVE AGENT, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SANTONI,E.DE LA MORA,J.DE SOUZA,I.SILMAN,J.SUSSMAN,R.BAATI,M.WEIK,  
AUTHOR   2 F.NACHON                                                             
REVDAT   1   29-AUG-18 6G17    0                                                
JRNL        AUTH   G.SANTONI,J.DE SOUSA,E.DE LA MORA,J.DIAS,L.JEAN,J.L.SUSSMAN, 
JRNL        AUTH 2 I.SILMAN,P.Y.RENARD,R.C.D.BROWN,M.WEIK,R.BAATI,F.NACHON      
JRNL        TITL   STRUCTURE-BASED OPTIMIZATION OF NON-QUATERNARY REACTIVATORS  
JRNL        TITL 2 OF ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHORUS NERVE  
JRNL        TITL 3 AGENTS.                                                      
JRNL        REF    J. MED. CHEM.                              2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   30125110                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00592                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 45.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 50208                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1507                            
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 45.7482 -  4.8911    0.95     4490   139  0.1685 0.2012        
REMARK   3     2  4.8911 -  3.8828    0.98     4456   138  0.1227 0.1512        
REMARK   3     3  3.8828 -  3.3922    0.99     4433   137  0.1306 0.1792        
REMARK   3     4  3.3922 -  3.0821    1.00     4465   138  0.1535 0.2034        
REMARK   3     5  3.0821 -  2.8612    1.00     4433   138  0.1756 0.2110        
REMARK   3     6  2.8612 -  2.6926    1.00     4445   137  0.1935 0.2750        
REMARK   3     7  2.6926 -  2.5577    1.00     4449   138  0.2222 0.2896        
REMARK   3     8  2.5577 -  2.4464    1.00     4387   135  0.2452 0.3023        
REMARK   3     9  2.4464 -  2.3522    0.99     4413   137  0.2672 0.3341        
REMARK   3    10  2.3522 -  2.2711    0.99     4394   136  0.2887 0.2817        
REMARK   3    11  2.2711 -  2.2000    0.98     4336   134  0.3262 0.3409        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.008           4532                                  
REMARK   3   ANGLE     :  0.910           6147                                  
REMARK   3   CHIRALITY :  0.054            641                                  
REMARK   3   PLANARITY :  0.005            796                                  
REMARK   3   DIHEDRAL  : 16.189           2681                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -51.1153  31.9887 -33.4365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2654 T22:   0.2137                                     
REMARK   3      T33:   0.2626 T12:  -0.0002                                     
REMARK   3      T13:   0.0147 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3035 L22:   1.0112                                     
REMARK   3      L33:   1.9671 L12:   0.1789                                     
REMARK   3      L13:  -0.4569 L23:  -0.0585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0221 S12:   0.0112 S13:  -0.1053                       
REMARK   3      S21:   0.0194 S22:  -0.0547 S23:  -0.0134                       
REMARK   3      S31:   0.1519 S32:  -0.0224 S33:   0.0366                       
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 6G17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008999.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 274775                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6700                            
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1EA5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150MM MES PH 5.6 36% PEG200, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.73833            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.47667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.47667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.73833            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 50.0 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -91.47667            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 705  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1053  LIES ON A SPECIAL POSITION.                          
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     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     CYS A   537                                                      
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    SER A  25     -160.81   -122.82                                   
REMARK 500    PHE A  45       -4.82     78.12                                   
REMARK 500    ALA A  60       40.39   -106.83                                   
REMARK 500    SER A 108       80.79   -165.77                                   
REMARK 500    PHE A 155       14.31   -143.22                                   
REMARK 500    SER A 200     -121.69     65.56                                   
REMARK 500    GLU A 299      -72.10   -114.50                                   
REMARK 500    ASP A 326       67.39   -119.81                                   
REMARK 500    ASP A 380       53.38   -166.32                                   
REMARK 500    VAL A 400      -60.85   -129.43                                   
REMARK 500    HIS A 440      126.03    -27.40                                   
REMARK 500    GLN A 488     -125.50    -79.43                                   
REMARK 500    GLU A 489      118.22     57.39                                   
REMARK 500    ARG A 515       67.28     61.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NTJ A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to ASN A 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 416                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EA5   RELATED DB: PDB                                   
DBREF  6G17 A    1   537  UNP    P04058   ACES_TETCF      22    558             
SEQRES   1 A  537  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 A  537  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 A  537  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 A  537  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 A  537  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 A  537  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 A  537  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 A  537  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 A  537  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 A  537  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 A  537  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 A  537  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 A  537  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  537  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 A  537  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 A  537  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 A  537  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 A  537  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 A  537  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 A  537  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 A  537  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 A  537  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 A  537  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 A  537  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 A  537  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 A  537  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 A  537  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 A  537  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 A  537  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 A  537  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 A  537  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 A  537  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 A  537  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 A  537  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 A  537  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 A  537  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 A  537  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 A  537  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 A  537  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 A  537  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 A  537  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 A  537  ALA THR ALA CYS                                              
HET    NTJ  A 601       8                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    EDO  A 604       4                                                       
HET    PGE  A 605      10                                                       
HET    EDO  A 606       4                                                       
HET    EDO  A 607       4                                                       
HET    PEG  A 608       7                                                       
HET    PEG  A 609       7                                                       
HET    PEG  A 610       7                                                       
HET    PEG  A 611       7                                                       
HET    PEG  A 612       7                                                       
HETNAM     NTJ R-ETHYL N,N-DIMETHYLPHOSPHONAMIDATE                              
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NTJ    C4 H12 N O2 P                                                
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   6  PGE    C6 H14 O4                                                    
FORMUL   9  PEG    5(C4 H10 O3)                                                 
FORMUL  14  HOH   *446(H2 O)                                                    
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5    
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6    
HELIX    3 AA3 LEU A  127  ASN A  131  5                                   5    
HELIX    4 AA4 GLY A  132  GLU A  140  1                                   9    
HELIX    5 AA5 VAL A  150  LEU A  156  1                                   7    
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18    
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3    
HELIX    8 AA8 SER A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  212  ASP A  217  1                                   6    
HELIX   10 AB1 SER A  237  LEU A  252  1                                  16    
HELIX   11 AB2 SER A  258  LYS A  269  1                                  12    
HELIX   12 AB3 LYS A  270  GLU A  278  1                                   9    
HELIX   13 AB4 TRP A  279  LEU A  282  5                                   4    
HELIX   14 AB5 SER A  304  GLY A  312  1                                   9    
HELIX   15 AB6 GLY A  328  ALA A  336  1                                   9    
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13    
HELIX   17 AB8 ASN A  364  THR A  376  1                                  13    
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18    
HELIX   19 AC1 VAL A  400  LYS A  413  1                                  14    
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5    
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6    
HELIX   22 AC4 GLY A  449  ASN A  457  5                                   9    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  THR A  535  1                                  10    
SHEET    1 AA1 3 LEU A   7  THR A  10  0                                        
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1 AA211 THR A  18  VAL A  22  0                                        
SHEET    2 AA211 SER A  25  PRO A  34 -1  O  ALA A  29   N  THR A  18           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  LEU A  97   N  ILE A  33           
SHEET    4 AA211 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100           
SHEET    5 AA211 THR A 109  ILE A 115  1  N  MET A 112   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  THR A 195   N  VAL A 113           
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8 AA211 GLN A 318  ASN A 324  1  O  LEU A 320   N  LEU A 224           
SHEET    9 AA211 GLY A 417  PHE A 423  1  O  PHE A 423   N  VAL A 323           
SHEET   10 AA211 LYS A 501  LEU A 505  1  O  LEU A 505   N  PHE A 422           
SHEET   11 AA211 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.06  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.04  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.07  
LINK         ND2 ASN A  59                 C1  NAG A 603     1555   1555  1.45  
LINK         OG  SER A 200                 P1  NTJ A 601     1555   1555  1.60  
LINK         ND2 ASN A 416                 C1  NAG A 602     1555   1555  1.46  
CISPEP   1 SER A  103    PRO A  104          0         5.07                     
SITE     1 AC1 11 GLY A 118  GLY A 119  SER A 200  ALA A 201                    
SITE     2 AC1 11 TRP A 233  PHE A 288  PHE A 290  PHE A 331                    
SITE     3 AC1 11 HIS A 440  PEG A 610  HOH A 737                               
SITE     1 AC2  6 PRO A  76  ARG A 220  ARG A 221  THR A 317                    
SITE     2 AC2  6 GLN A 318  HOH A 848                                          
SITE     1 AC3  7 TYR A 121  GLN A 185  LYS A 192  TRP A 279                    
SITE     2 AC3  7 HOH A 728  HOH A 948  HOH A 949                               
SITE     1 AC4  6 PHE A 330  PHE A 331  TYR A 334  PEG A 610                    
SITE     2 AC4  6 HOH A 728  HOH A 737                                          
SITE     1 AC5  3 ARG A 267  GLU A 268  LYS A 269                               
SITE     1 AC6  5 THR A  10  LYS A  11  TRP A  54  PEG A 611                    
SITE     2 AC6  5 HOH A 725                                                     
SITE     1 AC7  7 ARG A 105  PRO A 106  LYS A 107  GLN A 185                    
SITE     2 AC7  7 PHE A 186  ASN A 251  HOH A 723                               
SITE     1 AC8  9 TRP A  84  GLY A 117  GLY A 118  GLU A 199                    
SITE     2 AC8  9 SER A 200  PHE A 330  HIS A 440  NTJ A 601                    
SITE     3 AC8  9 EDO A 606                                                     
SITE     1 AC9  5 ASN A   9  PHE A 186  ASP A 285  PEG A 608                    
SITE     2 AC9  5 HOH A1001                                                     
SITE     1 AD1  3 PHE A 422  HIS A 513  HOH A 718                               
SITE     1 AD2  3 ASN A  59  SER A  61  HOH A 710                               
SITE     1 AD3  4 ASN A 416  HOH A 720  HOH A 798  HOH A 904                    
CRYST1  111.767  111.767  137.215  90.00  90.00 120.00 P 31 2 1      6          
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      0.008947  0.005166  0.000000        0.00000                         
SCALE2      0.000000  0.010331  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007288        0.00000                         
TER    4309      THR A 535                                                      
MASTER      334    0   12   25   14    0   22    6 4783    1  102   42          
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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