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LongText Report for: 3I6M-pdb

Name Class
3I6M-pdb
HEADER    HYDROLASE                               07-JUL-09   3I6M              
TITLE     3D STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE              
TITLE    2 COMPLEXED WITH N-PIPERIDINOPROPYL-GALANTHAMINE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-556;                                       
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;                            
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    SERINE HYDROLASE, CHOLINESTERASE, NEUROTRANSMITTER                    
KEYWDS   2 DEGRADATION, ALZHEIMER'S DISEASE, BIS-FUNCTIONAL                     
KEYWDS   3 GALANTHAMINE DERIVATIVE, ALTERNATIVE SPLICING, CELL                  
KEYWDS   4 JUNCTION, CELL MEMBRANE, DISULFIDE BOND, GLYCOPROTEIN, GPI-          
KEYWDS   5 ANCHOR, HYDROLASE, LIPOPROTEIN, MEMBRANE, SERINE ESTERASE,           
KEYWDS   6 SYNAPSE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.LAMBA,C.BARTOLUCCI                                                  
REVDAT   1   12-JAN-10 3I6M    0                                                
JRNL        AUTH   C.BARTOLUCCI,L.A.HALLER,U.JORDIS,G.FELS,D.LAMBA              
JRNL        TITL   PROBING TORPEDO CALIFORNICA ACETYLCHOLINESTERASE             
JRNL        TITL 2 CATALYTIC GORGE WITH TWO NOVEL BIS-FUNCTIONAL                
JRNL        TITL 3 GALANTHAMINE DERIVATIVES.                                    
JRNL        REF    J.MED.CHEM.                                2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20025280                                                     
JRNL        DOI    10.1021/JM901296P                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.M.GREENBLATT,C.GUILLOU,D.GUENARD,A.ARGAMAN,                
REMARK   1  AUTH 2 S.BOTTI,B.BADET,C.THAL,I.SILMAN,J.L.SUSSMAN                  
REMARK   1  TITL   THE COMPLEX OF A BIVALENT DERIVATIVE OF                      
REMARK   1  TITL 2 GALANTHAMINE WITH TORPEDO ACETYLCHOLINESTERASE               
REMARK   1  TITL 3 DISPLAYS DRASTIC DEFORMATION OF THE ACTIVE-SITE              
REMARK   1  TITL 4 GORGE: IMPLICATIONS FOR STRUCTURE-BASED DRUG DESIGN          
REMARK   1  REF    J.AM.CHEM.SOC.                V. 126 15405 2004              
REMARK   1  REFN                   ISSN 0002-7863                               
REMARK   1  PMID   15563167                                                     
REMARK   1  DOI    10.1021/JA0466154                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.M.GREENBLATT,G.KRYGER,T.LEWIS,I.SILMAN,                    
REMARK   1  AUTH 2 J.L.SUSSMAN                                                  
REMARK   1  TITL   STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH             
REMARK   1  TITL 2 (-)-GALANTHAMINE AT 2.3A RESOLUTION                          
REMARK   1  REF    FEBS LETT.                    V. 463   321 1999              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1  PMID   10606746                                                     
REMARK   1  DOI    10.1016/S0014-5793(99)01637-3                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.BARTOLUCCI,E.PEROLA,C.PILGER,G.FELS,D.LAMBA                
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A COMPLEX OF                  
REMARK   1  TITL 2 GALANTHAMINE (NIVALIN) WITH ACETYLCHOLINESTERASE             
REMARK   1  TITL 3 FROM TORPEDO CALIFORNICA: IMPLICATIONS FOR THE               
REMARK   1  TITL 4 DESIGN OF NEW ANTI-ALZHEIMER DRUGS                           
REMARK   1  REF    PROTEINS                      V.  42   182 2001              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  PMID   11119642                                                     
REMARK   1  DOI    10.1002/1097-0134                                            
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   C.PILGER,C.BARTOLUCCI,D.LAMBA,A.TROPSHA,G.FELS               
REMARK   1  TITL   ACCURATE PREDICTION OF THE BOUND CONFORMATION OF             
REMARK   1  TITL 2 GALANTHAMINE IN THE ACTIVE SITE OF TORPEDO                   
REMARK   1  TITL 3 CALIFORNICA ACETYLCHOLINESTERASE USING MOLECULAR             
REMARK   1  TITL 4 DOCKING                                                      
REMARK   1  REF    J.MOL.GRAPH.MODEL.            V.  19   288 2001              
REMARK   1  REFN                   ISSN 1093-3263                               
REMARK   1  PMID   11449566                                                     
REMARK   1  DOI    10.1016/S1093-3263(00)00056-5                                
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   E.LUTTMANN,E.LINNEMANN,G.FELS                                
REMARK   1  TITL   GALANTHAMINE AS BIS-FUNCTIONAL LIGAND FOR THE                
REMARK   1  TITL 2 ACETYLCHOLINESTERASE.                                        
REMARK   1  REF    J.MOL.MODEL.                  V.   8   208 2002              
REMARK   1  REFN                   ESSN 0948-5023                               
REMARK   1  PMID   12140604                                                     
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   L.ALISARAIE,G.FELS                                           
REMARK   1  TITL   A QXP-BASED MULTISTEP DOCKING PROCEDURE FOR                  
REMARK   1  TITL 2 ACCURATE PREDICTION OF PROTEIN-LIGAND COMPLEXES              
REMARK   1  REF    J.CHEM.INF.MODEL.             V.  46  1174 2006              
REMARK   1  REFN                   ISSN 1549-9596                               
REMARK   1  PMID   16711737                                                     
REMARK   1  DOI    10.1021/CI050343M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1997132.140                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 46822                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4701                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3572                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE                    : 0.2710                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 397                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4263                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 398                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.30000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 8.30000                                              
REMARK   3    B13 (A**2) : -16.60000                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED INDIVIDUAL ISOTROPIC           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.733 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.525 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.789 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.908 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 62.80                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3I6M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054029.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : THREE-SEGMENT PT-COATED            
REMARK 200                                   TOROIDAL MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46878                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41800                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1EA5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 42% PEG200, 100MM MES PH 6.0, 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       45.73133            
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       91.46267            
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       91.46267            
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       45.73133            
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: 2900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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      137.19400            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP A    2   CG    OD1   OD2                                     
REMARK 480     HIS A    3   CG    ND1   CD2   CE1   NE2                         
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    HIS A   3      -40.49   -155.13                                   
REMARK 500    LEU A  23       53.07     38.67                                   
REMARK 500    PHE A  45      -11.84     81.24                                   
REMARK 500    ALA A  60       50.25   -108.56                                   
REMARK 500    SER A 108       74.63   -162.24                                   
REMARK 500    ASN A 131      109.48    -58.37                                   
REMARK 500    LEU A 158       78.93   -119.72                                   
REMARK 500    SER A 200     -119.95     57.64                                   
REMARK 500    GLU A 299      -71.63   -120.21                                   
REMARK 500    THR A 317     -158.87   -158.31                                   
REMARK 500    ASP A 326       66.36   -119.74                                   
REMARK 500    TRP A 378        1.22    -69.96                                   
REMARK 500    ASP A 380       51.66   -155.35                                   
REMARK 500    VAL A 400      -60.86   -125.99                                   
REMARK 500    HIS A 486       -0.30     73.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 442         0.07    SIDE CHAIN                              
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 NAG A 536                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 537                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 538                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G3X A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W4L   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING GALANTHAMINE DERIVATIVE            
REMARK 900 RELATED ID: 1W6R   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE                       
REMARK 900 RELATED ID: 1QTI   RELATED DB: PDB                                   
REMARK 900 ACETYLCHOLINESTERASE (E.C.3.1.1.7) COMPLEXED WITH                    
REMARK 900 GALANTHAMINE                                                         
REMARK 900 RELATED ID: 1W76   RELATED DB: PDB                                   
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA                             
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-ACTING                
REMARK 900 GALANTHAMINE DERIVATIVE                                              
REMARK 900 RELATED ID: 1DX6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE WITH (-)-GALANTHAMINE AT           
REMARK 900 2.3A RESOLUTION                                                      
REMARK 900 RELATED ID: 3I6Z   RELATED DB: PDB                                   
REMARK 900 3D STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE             
REMARK 900 COMPLEXED WITH N-SACCHARINOHEXYL-GALANTHAMINE                        
DBREF  3I6M A    2   535  UNP    P04058   ACES_TORCA      23    556             
SEQRES   1 A  534  ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS          
SEQRES   2 A  534  VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE          
SEQRES   3 A  534  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 A  534  GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO          
SEQRES   5 A  534  TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN          
SEQRES   6 A  534  CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER          
SEQRES   7 A  534  GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU          
SEQRES   8 A  534  ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG          
SEQRES   9 A  534  PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY          
SEQRES  10 A  534  GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN          
SEQRES  11 A  534  GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL          
SEQRES  12 A  534  SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA          
SEQRES  13 A  534  LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU          
SEQRES  14 A  534  LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN          
SEQRES  15 A  534  ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE          
SEQRES  16 A  534  PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS          
SEQRES  17 A  534  ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA          
SEQRES  18 A  534  ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER          
SEQRES  19 A  534  VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU          
SEQRES  20 A  534  GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU          
SEQRES  21 A  534  LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU          
SEQRES  22 A  534  ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE          
SEQRES  23 A  534  PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE          
SEQRES  24 A  534  PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN          
SEQRES  25 A  534  PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP          
SEQRES  26 A  534  GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE          
SEQRES  27 A  534  SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE          
SEQRES  28 A  534  MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP          
SEQRES  29 A  534  LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP          
SEQRES  30 A  534  MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU          
SEQRES  31 A  534  ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU          
SEQRES  32 A  534  MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY          
SEQRES  33 A  534  THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU          
SEQRES  34 A  534  VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU          
SEQRES  35 A  534  ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU          
SEQRES  36 A  534  ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE          
SEQRES  37 A  534  MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO          
SEQRES  38 A  534  ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE          
SEQRES  39 A  534  THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU          
SEQRES  40 A  534  PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS          
SEQRES  41 A  534  VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA          
SEQRES  42 A  534  THR                                                          
MODRES 3I6M ASN A   59  ASN  GLYCOSYLATION SITE                                 
MODRES 3I6M ASN A  416  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 536      14                                                       
HET    NAG  A 537      14                                                       
HET    NAG  A 538      14                                                       
HET    G3X  A   1      29                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     G3X (4AS,6R,8AS)-3-METHOXY-11-(3-PIPERIDIN-1-YLPROPYL)-5,6,          
HETNAM   2 G3X  9,10,11,12-HEXAHYDRO-4AH-[1]BENZOFURO[3A,3,2-                   
HETNAM   3 G3X  EF][2]BENZAZEPIN-6-OL                                           
HETSYN     NAG NAG                                                              
HETSYN     G3X (4AS,6R,8AS)-4A,5,9,10,11,12-HEXAHYDRO-3-METHOXY-11-[3-          
HETSYN   2 G3X  (1-PIPERIDINYL)PROPYL]-6H-BENZOFURO[3A,3,2-                     
HETSYN   3 G3X  EF][2]BENZAZEPIN-6-OL                                           
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   4  G3X    C24 H34 N2 O3                                                
FORMUL   5  HOH   *398(H2 O)                                                    
HELIX    1   1 VAL A   40  ARG A   44  5                                   5    
HELIX    2   2 PHE A   78  MET A   83  1                                   6    
HELIX    3   3 LEU A  127  ASN A  131  5                                   5    
HELIX    4   4 GLY A  132  GLU A  140  1                                   9    
HELIX    5   5 VAL A  150  LEU A  156  1                                   7    
HELIX    6   6 ASN A  167  ILE A  184  1                                  18    
HELIX    7   7 GLN A  185  PHE A  187  5                                   3    
HELIX    8   8 SER A  200  SER A  212  1                                  13    
HELIX    9   9 SER A  215  PHE A  219  5                                   5    
HELIX   10  10 SER A  237  LEU A  252  1                                  16    
HELIX   11  11 SER A  258  LYS A  269  1                                  12    
HELIX   12  12 LYS A  270  GLU A  278  1                                   9    
HELIX   13  13 TRP A  279  LEU A  282  5                                   4    
HELIX   14  14 SER A  304  GLY A  312  1                                   9    
HELIX   15  15 GLY A  328  ALA A  336  1                                   9    
HELIX   16  16 SER A  348  VAL A  360  1                                  13    
HELIX   17  17 ASN A  364  THR A  376  1                                  13    
HELIX   18  18 ASN A  383  VAL A  400  1                                  18    
HELIX   19  19 VAL A  400  GLY A  415  1                                  16    
HELIX   20  20 PRO A  433  GLY A  437  5                                   5    
HELIX   21  21 GLU A  443  PHE A  448  1                                   6    
HELIX   22  22 GLY A  449  ASN A  457  5                                   9    
HELIX   23  23 THR A  459  GLY A  480  1                                  22    
HELIX   24  24 ARG A  517  GLN A  526  1                                  10    
HELIX   25  25 GLN A  526  THR A  535  1                                  10    
SHEET    1   A 3 LEU A   7  THR A  10  0                                        
SHEET    2   A 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3   A 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1   B11 THR A  18  VAL A  22  0                                        
SHEET    2   B11 SER A  25  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3   B11 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
SHEET    4   B11 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100           
SHEET    5   B11 THR A 109  ILE A 115  1  N  TRP A 114   O  VAL A 144           
SHEET    6   B11 GLY A 189  GLU A 199  1  O  THR A 195   N  VAL A 113           
SHEET    7   B11 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8   B11 GLN A 318  ASN A 324  1  O  LEU A 320   N  LEU A 224           
SHEET    9   B11 GLY A 417  PHE A 423  1  O  PHE A 423   N  VAL A 323           
SHEET   10   B11 LYS A 501  LEU A 505  1  O  LEU A 505   N  PHE A 422           
SHEET   11   B11 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  2.05  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.04  
LINK         ND2 ASN A  59                 C1  NAG A 536     1555   1555  1.46  
LINK         ND2 ASN A 416                 C1  NAG A 537     1555   1555  1.45  
LINK         O4  NAG A 537                 C1  NAG A 538     1555   1555  1.40  
CISPEP   1 SER A  103    PRO A  104          0         0.31                     
SITE     1 AC1  3 ASN A  59  SER A  61  HOH A 906                               
SITE     1 AC2  5 ASN A 416  NAG A 538  HOH A 732  HOH A 894                    
SITE     2 AC2  5 HOH A 918                                                     
SITE     1 AC3  2 NAG A 537  HOH A 918                                          
SITE     1 AC4 13 TRP A  84  GLY A 117  GLY A 118  GLY A 119                    
SITE     2 AC4 13 TYR A 121  GLU A 199  SER A 200  PHE A 290                    
SITE     3 AC4 13 PHE A 330  PHE A 331  TYR A 334  HIS A 440                    
SITE     4 AC4 13 HOH A 547                                                     
CRYST1  112.194  112.194  137.194  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      0.008913  0.005146  0.000000        0.00000                         
SCALE2      0.000000  0.010292  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007289        0.00000                         
TER    4264      THR A 535                                                      
MASTER      371    0    4   25   14    0    8    6 4732    1   79   42          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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