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LongText Report for: 6ezg-pdb

Name Class
6ezg-pdb
HEADER    HYDROLASE                               15-NOV-17   6EZG              
TITLE     TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH MR33112      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
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, MULTI-TARGET INHIBITOR, ALZHEIMER DESEASE,      
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SANTONI,J.LALUT,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,I.SILLMAN,     
AUTHOR   2 J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS                    
REVDAT   1   21-NOV-18 6EZG    0                                                
JRNL        AUTH   J.LALUT,G.SANTONI,D.KARILA,C.LECOUTEY,A.DAVIS,F.NACHON,      
JRNL        AUTH 2 I.SILLMAN,J.SUSSMAN,M.WEIK,T.MAURICE,P.DALLEMAGNE,C.ROCHAIS  
JRNL        TITL   NOVEL MULTITARGET-DIRECTED LIGANDS TARGETING                 
JRNL        TITL 2 ACETYLCHOLINESTERASE AND SIGMA1 RECEPTORS AS LEAD COMPOUNDS  
JRNL        TITL 3 FOR TREATMENT OF ALZHEIMER'S DISEASE: SYNTHESIS, EVALUATION, 
JRNL        TITL 4 AND STRUCTURAL CHARACTERIZATION OF THEIR COMPLEXES WITH      
JRNL        TITL 5 ACETYLCHOLINESTERASE                                         
JRNL        REF    EUR.J.MED.CHEM.                            2018              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        DOI    10.1016/J.EJMECH.2018.10.064                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 45.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 73468                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3671                            
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 45.4300 -  6.5113    0.97     2895   153  0.1857 0.2101        
REMARK   3     2  6.5113 -  5.1706    0.98     2811   123  0.1574 0.2098        
REMARK   3     3  5.1706 -  4.5177    0.98     2762   148  0.1360 0.1538        
REMARK   3     4  4.5177 -  4.1049    0.99     2765   141  0.1321 0.1850        
REMARK   3     5  4.1049 -  3.8108    0.99     2738   155  0.1448 0.1840        
REMARK   3     6  3.8108 -  3.5863    0.97     2670   169  0.1671 0.2132        
REMARK   3     7  3.5863 -  3.4067    0.97     2721   144  0.1741 0.2149        
REMARK   3     8  3.4067 -  3.2585    0.97     2667   154  0.1972 0.2173        
REMARK   3     9  3.2585 -  3.1331    0.98     2700   132  0.2025 0.2521        
REMARK   3    10  3.1331 -  3.0250    0.98     2701   166  0.2148 0.2924        
REMARK   3    11  3.0250 -  2.9304    0.98     2668   144  0.2074 0.2611        
REMARK   3    12  2.9304 -  2.8467    0.98     2715   152  0.2101 0.3312        
REMARK   3    13  2.8467 -  2.7717    0.95     2625   116  0.2011 0.2322        
REMARK   3    14  2.7717 -  2.7041    0.97     2683   116  0.2138 0.2722        
REMARK   3    15  2.7041 -  2.6426    0.96     2630   148  0.2212 0.2991        
REMARK   3    16  2.6426 -  2.5864    0.97     2676   146  0.2277 0.2809        
REMARK   3    17  2.5864 -  2.5347    0.98     2671   150  0.2411 0.3160        
REMARK   3    18  2.5347 -  2.4868    0.97     2677   134  0.2309 0.3102        
REMARK   3    19  2.4868 -  2.4424    0.97     2663   134  0.2281 0.2974        
REMARK   3    20  2.4424 -  2.4010    0.98     2670   125  0.2407 0.3075        
REMARK   3    21  2.4010 -  2.3623    0.97     2660   139  0.2463 0.3013        
REMARK   3    22  2.3623 -  2.3260    0.96     2633   127  0.2491 0.2913        
REMARK   3    23  2.3260 -  2.2918    0.95     2561   143  0.2668 0.2908        
REMARK   3    24  2.2918 -  2.2595    0.95     2607   134  0.2781 0.3638        
REMARK   3    25  2.2595 -  2.2289    0.97     2611   149  0.2980 0.3542        
REMARK   3    26  2.2289 -  2.2000    0.95     2617   129  0.3172 0.3695        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.470           
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      :  0.007           8876                                  
REMARK   3   ANGLE     :  0.998          12044                                  
REMARK   3   CHIRALITY :  0.042           1262                                  
REMARK   3   PLANARITY :  0.005           1562                                  
REMARK   3   DIHEDRAL  : 14.316           3218                                  
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 6EZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007514.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03                               
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73468                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.510                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.8000                            
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) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG 200 150MM MES PH 5.8, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.85550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.24700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.49800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.24700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.85550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.49800            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 465     ASP B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ALA B   536                                                      
REMARK 465     CYS B   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    PHE A  45       -5.92     82.05                                   
REMARK 500    ASN A 131      108.09    -56.15                                   
REMARK 500    SER A 200     -122.15     56.65                                   
REMARK 500    GLU A 299      -57.91   -134.90                                   
REMARK 500    ASN A 313       77.87    -69.28                                   
REMARK 500    THR A 317     -167.35   -163.85                                   
REMARK 500    ASP A 380       50.71   -163.65                                   
REMARK 500    VAL A 400      -59.97   -121.13                                   
REMARK 500    HIS A 486     -118.10    -68.32                                   
REMARK 500    SER A 487      116.71     69.59                                   
REMARK 500    ARG A 517       44.07     33.35                                   
REMARK 500    PHE B  45      -10.05     79.68                                   
REMARK 500    ALA B  60       48.88   -105.21                                   
REMARK 500    SER B 108       78.99   -155.97                                   
REMARK 500    PHE B 155       17.38   -145.67                                   
REMARK 500    SER B 200     -120.14     58.47                                   
REMARK 500    GLU B 299      -70.44   -121.40                                   
REMARK 500    ASP B 380       51.30   -161.40                                   
REMARK 500    VAL B 400      -64.04   -121.62                                   
REMARK 500    HIS B 486       -8.15     75.37                                   
REMARK 500    ASN B 506     -166.43   -164.77                                   
REMARK 500    ARG B 515       74.59     52.59                                   
REMARK 500    ARG B 517       48.27     35.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 984        DISTANCE =  7.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C6K A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C6K B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound   
REMARK 800  to ASN B 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound   
REMARK 800  to ASN B 416                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EA5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2W75   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1EVE   RELATED DB: PDB                                   
DBREF  6EZG A    1   537  UNP    P04058   ACES_TETCF      22    558             
DBREF  6EZG B    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                                              
SEQRES   1 B  537  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 B  537  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 B  537  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 B  537  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 B  537  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 B  537  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 B  537  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 B  537  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 B  537  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 B  537  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 B  537  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 B  537  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 B  537  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 B  537  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 B  537  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 B  537  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 B  537  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 B  537  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 B  537  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 B  537  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 B  537  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 B  537  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 B  537  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 B  537  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 B  537  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 B  537  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 B  537  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 B  537  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 B  537  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 B  537  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 B  537  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 B  537  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 B  537  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 B  537  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 B  537  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 B  537  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 B  537  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 B  537  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 B  537  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 B  537  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 B  537  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 B  537  ALA THR ALA CYS                                              
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    C6K  A 603      29                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    C6K  B 603      29                                                       
HET    PEG  B 604      17                                                       
HET    PEG  B 605      17                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     C6K 1-(7-CHLORANYL-4-METHOXY-1~{H}-INDOL-5-YL)-3-[1-                 
HETNAM   2 C6K  (PHENYLMETHYL)PIPERIDIN-4-YL]PROPAN-1-ONE                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  C6K    2(C24 H27 CL N2 O2)                                          
FORMUL   9  PEG    2(C4 H10 O3)                                                 
FORMUL  11  HOH   *564(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 VAL A  238  LEU A  252  1                                  15    
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  TYR A  375  1                                  12    
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    
HELIX   26 AC8 VAL B   40  ARG B   44  5                                   5    
HELIX   27 AC9 PHE B   78  MET B   83  1                                   6    
HELIX   28 AD1 LEU B  127  ASN B  131  5                                   5    
HELIX   29 AD2 GLY B  132  GLU B  140  1                                   9    
HELIX   30 AD3 VAL B  150  LEU B  156  1                                   7    
HELIX   31 AD4 ASN B  167  ILE B  184  1                                  18    
HELIX   32 AD5 GLN B  185  PHE B  187  5                                   3    
HELIX   33 AD6 SER B  200  SER B  212  1                                  13    
HELIX   34 AD7 SER B  215  PHE B  219  5                                   5    
HELIX   35 AD8 VAL B  238  ASN B  251  1                                  14    
HELIX   36 AD9 SER B  258  GLU B  268  1                                  11    
HELIX   37 AE1 LYS B  270  GLU B  278  1                                   9    
HELIX   38 AE2 TRP B  279  LEU B  282  5                                   4    
HELIX   39 AE3 SER B  304  GLY B  312  1                                   9    
HELIX   40 AE4 GLY B  328  ALA B  336  1                                   9    
HELIX   41 AE5 SER B  348  VAL B  360  1                                  13    
HELIX   42 AE6 ASN B  364  TYR B  375  1                                  12    
HELIX   43 AE7 ASN B  383  VAL B  400  1                                  18    
HELIX   44 AE8 VAL B  400  LYS B  413  1                                  14    
HELIX   45 AE9 PRO B  433  GLY B  437  5                                   5    
HELIX   46 AF1 GLU B  443  PHE B  448  1                                   6    
HELIX   47 AF2 GLY B  449  ASN B  457  5                                   9    
HELIX   48 AF3 THR B  459  GLY B  480  1                                  22    
HELIX   49 AF4 ARG B  517  GLN B  526  1                                  10    
HELIX   50 AF5 GLN B  526  ALA B  534  1                                   9    
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  LYS A  14           
SHEET    1 AA211 THR A  18  PRO A  21  0                                        
SHEET    2 AA211 HIS A  26  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
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  TRP A 114   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 ILE A 319  ASN A 324  1  O  LEU A 320   N  ALA A 222           
SHEET    9 AA211 THR A 418  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           
SHEET    1 AA3 2 VAL A 236  SER A 237  0                                        
SHEET    2 AA3 2 VAL A 295  ILE A 296  1  O  ILE A 296   N  VAL A 236           
SHEET    1 AA4 3 LEU B   7  ASN B   9  0                                        
SHEET    2 AA4 3 LYS B  14  MET B  16 -1  O  VAL B  15   N  VAL B   8           
SHEET    3 AA4 3 VAL B  57  ASN B  59  1  O  TRP B  58   N  MET B  16           
SHEET    1 AA511 THR B  18  VAL B  22  0                                        
SHEET    2 AA511 SER B  25  PRO B  34 -1  O  SER B  25   N  VAL B  22           
SHEET    3 AA511 TYR B  96  VAL B 101 -1  O  ILE B  99   N  PHE B  30           
SHEET    4 AA511 VAL B 142  SER B 145 -1  O  SER B 145   N  ASN B  98           
SHEET    5 AA511 THR B 109  ILE B 115  1  N  TRP B 114   O  VAL B 144           
SHEET    6 AA511 GLY B 189  GLU B 199  1  O  THR B 195   N  VAL B 111           
SHEET    7 AA511 ARG B 221  GLN B 225  1  O  GLN B 225   N  GLY B 198           
SHEET    8 AA511 ILE B 319  ASN B 324  1  O  LEU B 320   N  ALA B 222           
SHEET    9 AA511 THR B 418  PHE B 423  1  O  PHE B 423   N  VAL B 323           
SHEET   10 AA511 LYS B 501  LEU B 505  1  O  ILE B 503   N  PHE B 422           
SHEET   11 AA511 VAL B 512  GLN B 514 -1  O  HIS B 513   N  PHE B 502           
SHEET    1 AA6 2 VAL B 236  SER B 237  0                                        
SHEET    2 AA6 2 VAL B 295  ILE B 296  1  O  ILE B 296   N  VAL B 236           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.06  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.05  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.05  
SSBOND   4 CYS B   67    CYS B   94                          1555   1555  2.06  
SSBOND   5 CYS B  254    CYS B  265                          1555   1555  2.04  
SSBOND   6 CYS B  402    CYS B  521                          1555   1555  2.03  
LINK         ND2 ASN A  59                 C1  NAG A 601     1555   1555  1.45  
LINK         ND2 ASN A 416                 C1  NAG A 602     1555   1555  1.45  
LINK         ND2 ASN B  59                 C1  NAG B 601     1555   1555  1.46  
LINK         ND2 ASN B 416                 C1  NAG B 602     1555   1555  1.41  
CISPEP   1 SER A  103    PRO A  104          0         2.07                     
CISPEP   2 SER B  103    PRO B  104          0         6.90                     
SITE     1 AC1 10 TYR A  70  TRP A  84  GLY A 118  GLU A 199                    
SITE     2 AC1 10 ILE A 287  PHE A 288  PHE A 290  PHE A 330                    
SITE     3 AC1 10 PHE A 331  HOH A 716                                          
SITE     1 AC2  6 TYR B  70  GLU B 199  SER B 286  PHE B 330                    
SITE     2 AC2  6 PHE B 331  HIS B 440                                          
SITE     1 AC3  3 ASN B 409  GLN B 500  ASN B 525                               
SITE     1 AC4  2 SER B  55  VAL B  57                                          
SITE     1 AC5  2 ASN A  59  SER A  61                                          
SITE     1 AC6  4 ASN A 416  LEU A 494  HOH A 853  HOH A 908                    
SITE     1 AC7  6 ASN B  59  SER B  61  HOH B 703  HOH B 706                    
SITE     2 AC7  6 HOH B 826  HOH B 832                                          
SITE     1 AC8  1 ASN B 416                                                     
CRYST1   91.711  106.996  150.494  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010904  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009346  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006645        0.00000                         
TER    4245      THR A 535                                                      
TER    8490      THR B 535                                                      
MASTER      329    0    8   50   32    0   12    6 9180    2  164   84          
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
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