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LongText Report for: 2V98-pdb

Name Class
2V98-pdb
HEADER    HYDROLASE                               22-AUG-07   2V98              
TITLE     STRUCTURE OF THE COMPLEX OF TCACHE WITH 1-(2-NITROPHENYL)-2,          
TITLE    2 2,2-TRIFLUOROETHYL-ARSENOCHOLINE AFTER A 9 SECONDS                   
TITLE    3 ANNEALING TO ROOM TEMPERATURE, DURING THE FIRST 5 SECONDS            
TITLE    4 OF WHICH LASER IRRADIATION AT 266NM TOOK PLACE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 SYNONYM: ACHE;                                                       
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;                            
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 VARIANT: G2 FORM;                                                    
SOURCE   5 ORGAN: ELECTRIC ORGAN;                                               
SOURCE   6 TISSUE: ELECTROPLAQUE                                                
KEYWDS    PARTIAL Q-WEIGHTED DIFFERENCE REFINEMENT,                             
KEYWDS   2 NEUROTRANSMITTER DEGRADATION,                                        
KEYWDS   3 ALTERNATIVE SPLICING, KINETIC CRYSTALLOGRAPHY,                       
KEYWDS   4 SERINE ESTERASE, CAGED COMPOUNDS, ACETYLCHOLINESTERASE,              
KEYWDS   5 SYNAPSE, MEMBRANE, BACKDOOR, HYDROLASE, GPI-ANCHOR,                  
KEYWDS   6 LIPOPROTEIN, GLYCOPROTEIN, CELL JUNCTION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J-.P.COLLETIER,B.SANSON,A.ROYANT,A.SPECHT,F.NACHON,                   
AUTHOR   2 P.MASSON,G.ZACCAI,J.L.SUSSMAN,M.GOELDNER,                            
AUTHOR   3 I.SILMAN,D.BOURGEOIS,M.WEIK                                          
REVDAT   1   20-NOV-07 2V98    0                                                
JRNL        AUTH   J-.P.COLLETIER,A.ROYANT,A.SPECHT,B.SANSON,                   
JRNL        AUTH 2 F.NACHON,P.MASSON,G.ZACCAI,J.L.SUSSMAN,                      
JRNL        AUTH 3 M.GOELDNER,I.SILMAN,D.BOURGEOIS,M.WEIK                       
JRNL        TITL   USE OF A 'CAGED' ANALOG TO STUDY TRAFFIC OF                  
JRNL        TITL 2 CHOLINE WITHIN ACETYLCHOLINESTERASE BY KINETIC               
JRNL        TITL 3 CRYSTALLOGRAPHY                                              
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63  1115 2007              
JRNL        REFN   ASTM ABCRE6  DK ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 3.0  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,                     
REMARK   3                 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,             
REMARK   3                 PANNU,READ,RICE,SIMONSON,WARREN                      
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3                              
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.0                            
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 3426122.57                     
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 50200                          
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) : 0.2016                          
REMARK   3   FREE R VALUE                     : 0.2490                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2510                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3                            
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.05                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.5                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1906                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.282                        
REMARK   3   BIN FREE R VALUE                    : 0.266                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5                            
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16760                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 282                                     
REMARK   3   SOLVENT ATOMS            :   1942                                  
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.54                                                
REMARK   3    B22 (A**2) : 6.86                                                 
REMARK   3    B33 (A**2) : -2.32                                                
REMARK   3    B12 (A**2) : 0.000                                                
REMARK   3    B13 (A**2) : 0.000                                                
REMARK   3    B23 (A**2) : 0.000                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008702                        
REMARK   3   BOND ANGLES            (DEGREES) : 1.41236                         
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.3                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.935 ;   1.5                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.123 ;   2.0                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.583 ;   2.0                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.717 ;   2.5                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.04135534                                           
REMARK   3   BSOL        : 300                                                  
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   GROUP  2  POSITIONAL            (A) :  NULL ;  NULL                
REMARK   3   GROUP  2  B-FACTOR           (A**2) :  NULL ;  NULL                
REMARK   3   GROUP  3  POSITIONAL            (A) :  NULL ;  NULL                
REMARK   3   GROUP  3  B-FACTOR           (A**2) :  NULL ;  NULL                
REMARK   3   GROUP  4  POSITIONAL            (A) :  NULL ;  NULL                
REMARK   3   GROUP  4  B-FACTOR           (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  TOPOLOGY FILE   1  : PROTEIN.TOP                                    
REMARK   3  PARAMETER FILE  2  : CFN.PARAM                                      
REMARK   3  TOPOLOGY FILE   2  : CFN.TOP                                        
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE   3  : WATER.TOP                                      
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  TOPOLOGY FILE   4  : ION.TOP                                        
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  TOPOLOGY FILE   5  : CARBOHYDRATE.TOP                               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2V98 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 22-AUG-2007.                
REMARK 100 THE EBI ID CODE IS EBI-33554.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF BEAMLINE ID14-4               
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) : 0.932240                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53938                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.5                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.3                                
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.84                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.02                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1W75                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG200, 150MM MES, PH6, 4            
REMARK 280  DEG. C.  THE CRYSTAL WAS SOAKED IN A  MOTHER  LIQUOR                
REMARK 280  SOLUTION CONTAINING 0.5MM CAGED ARSENOCHOLINE DURING 12             
REMARK 280  HOURS, IN THE DARK AND AT 4 DEG. C.                                 
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.81000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.23500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.81000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.23500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM                   
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK ALSO PROVIDES INFORMATION ON                 
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     HIS A   486                                                      
REMARK 465     SER A   487                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     GLU A   489                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  46    CZ   NH1  NH2                                       
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     GLU A  89    CD   OE1  OE2                                       
REMARK 470     ARG A 250    CZ   NH1  NH2                                       
REMARK 470     GLU A 268    OE1  OE2                                            
REMARK 470     GLU A 344    OE1  OE2                                            
REMARK 470     GLU A 350    OE1  OE2                                            
REMARK 470     LYS A 413    CD   CE   NZ                                        
REMARK 470     LYS A 498    CD   CE   NZ                                        
REMARK 470     LYS A 511    CD   CE   NZ                                        
REMARK 470     ARG A 515    CZ   NH1  NH2                                       
REMARK 470     ARG B  19    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B  46    CZ   NH1  NH2                                       
REMARK 470     GLU B  89    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 250    CZ   NH1  NH2                                       
REMARK 470     GLU B 268    OE1  OE2                                            
REMARK 470     ASP B 285    OD1  OD2                                            
REMARK 470     GLU B 350    OE1  OE2                                            
REMARK 470     LYS B 413    CD   CE   NZ                                        
REMARK 470     LYS B 454    CG   CD   CE   NZ                                   
REMARK 470     HIS B 486    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     GLN B 488    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 489    CD   OE1  OE2                                       
REMARK 470     ARG B 515    CZ   NH1  NH2                                       
REMARK 470     GLN B 526    OE1  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 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     -167.61   -165.63                                   
REMARK 500    PRO A  39       47.42    -79.38                                   
REMARK 500    PRO A  53      152.10    -46.91                                   
REMARK 500    ALA A  60       58.11   -110.18                                   
REMARK 500    CYS A  94       10.85   -140.53                                   
REMARK 500    SER A 108       60.97     39.47                                   
REMARK 500    PHE A 120       -9.07     68.64                                   
REMARK 500    LEU A 158       72.07   -109.17                                   
REMARK 500    ALA A 164       69.26   -154.48                                   
REMARK 500    SER A 200     -132.35     62.20                                   
REMARK 500    GLU A 299      -72.41   -101.99                                   
REMARK 500    THR A 317     -158.57   -158.72                                   
REMARK 500    ASP A 380       51.81   -153.92                                   
REMARK 500    VAL A 400      -60.89   -123.01                                   
REMARK 500    ARG A 515       72.53     45.47                                   
REMARK 500    ARG A 517       48.63     39.05                                   
REMARK 500    PHE B  45       -3.08     74.73                                   
REMARK 500    PRO B  53      146.05    -39.41                                   
REMARK 500    ALA B  60       52.45   -114.24                                   
REMARK 500    SER B 108       69.81   -154.34                                   
REMARK 500    ASN B 167       14.80     59.47                                   
REMARK 500    SER B 200     -125.90     56.01                                   
REMARK 500    GLU B 299      -70.04   -127.75                                   
REMARK 500    THR B 317     -154.76   -158.95                                   
REMARK 500    VAL B 360       66.45   -117.90                                   
REMARK 500    ASP B 380       51.83   -144.88                                   
REMARK 500    VAL B 400      -70.57   -121.23                                   
REMARK 500    LYS B 454      -33.55    -38.60                                   
REMARK 500    ARG B 515       72.20     54.29                                   
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 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A 1539                                                       
REMARK 610     NAG A 1540                                                       
REMARK 610     NAG B 1538                                                       
REMARK 610     NAG B 1539                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ A1537  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ A1537A  C3                                                     
REMARK 620 2 CFQ A1537A  C2  110.2                                              
REMARK 620 3 CFQ A1537A  C1  106.8 108.5                                        
REMARK 620 4 CFQ A1537A  C4  110.0 110.2 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ A1537  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ A1537B  C1                                                     
REMARK 620 2 CFQ A1537B  C3  108.4                                              
REMARK 620 3 CFQ A1537B  C2  109.1 108.9                                        
REMARK 620 4 CFQ A1537B  C4  109.9 109.8 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ A1538  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ A1538A  C3                                                     
REMARK 620 2 CFQ A1538A  C1  109.8                                              
REMARK 620 3 CFQ A1538A  C2  108.9 106.7                                        
REMARK 620 4 CFQ A1538A  C4  110.8 112.0 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ A1538  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ A1538B  C2                                                     
REMARK 620 2 CFQ A1538B  C3  108.3                                              
REMARK 620 3 CFQ A1538B  C1  108.5 109.4                                        
REMARK 620 4 CFQ A1538B  C4  109.9 110.3 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ B1536  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ B1536A  C3                                                     
REMARK 620 2 CFQ B1536A  C1  108.2                                              
REMARK 620 3 CFQ B1536A  C2  108.8 108.1                                        
REMARK 620 4 CFQ B1536A  C4  110.1 109.2 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ B1536  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ B1536B  C3                                                     
REMARK 620 2 CFQ B1536B  C2  108.4                                              
REMARK 620 3 CFQ B1536B  C1  108.8 108.4                                        
REMARK 620 4 CFQ B1536B  C4  110.1 110.5 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ B1537  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ B1537A  C1                                                     
REMARK 620 2 CFQ B1537A  C3  105.9                                              
REMARK 620 3 CFQ B1537A  C4  110.0 110.3                                        
REMARK 620 4 CFQ B1537A  C2  108.3 110.0 112.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CFQ B1537  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CFQ B1537B  C3                                                     
REMARK 620 2 CFQ B1537B  C4  110.3                                              
REMARK 620 3 CFQ B1537B  C1  107.5 110.8                                        
REMARK 620 4 CFQ B1537B  C2  109.3 111.0 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: CFQ BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: CFQ BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: CFQ BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: CFQ BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DX6   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH                    
REMARK 900   (-)-GALANTHAMINE AT 2.3A RESOLUTION                                
REMARK 900 RELATED ID: 1E66   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH                    
REMARK 900   (-)-HUPRINE X AT 2.1A RESOLUTION                                   
REMARK 900 RELATED ID: 1EA5   RELATED DB: PDB                                   
REMARK 900  NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7                           
REMARK 900  ) FROM TORPEDO CALIFORNICA AT 1.8A                                  
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1GPK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH                     
REMARK 900   (+)-HUPERZINE A AT 2.1A RESOLUTION                                 
REMARK 900 RELATED ID: 1GPN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH                    
REMARK 900   HUPERZINE B AT 2.35A RESOLUTION                                    
REMARK 900 RELATED ID: 1H22   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1                         
REMARK 900  .1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-                             
REMARK 900  HUPERZINE A-LIKE INHIBITOR AT 2.15A                                 
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1H23   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1                         
REMARK 900  .1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-                             
REMARK 900  HUPERZINE A-LIKE INHIBITOR AT 2.15A                                 
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1JGA   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-                     
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-                            
REMARK 900  HEPTYLENE-BIS-N,N'-SYN-2-PYRIDINIUMALDOXIME                         
REMARK 900 RELATED ID: 1JGB   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-                     
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-                            
REMARK 900  PROPYLENE-BIS-N,N'-SYN-4-PYRIDINIUMALDOXIME                         
REMARK 900 RELATED ID: 1JJB   RELATED DB: PDB                                   
REMARK 900  A NEUTRAL MOLECULE IN CATION-BINDING SITE:                          
REMARK 900  SPECIFIC BINDINGOF PEG-SH TO                                        
REMARK 900  ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA                       
REMARK 900 RELATED ID: 1QID   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT A) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIG   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT D) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIH   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT E) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QII   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT F) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1ACJ   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE                         
REMARK 900 RELATED ID: 1ACL   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM                   
REMARK 900 RELATED ID: 1AMN   RELATED DB: PDB                                   
REMARK 900  TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE                       
REMARK 900  COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)                           
REMARK 900  TRIFLUOROACETOPHENONE                                               
REMARK 900 RELATED ID: 1AX9   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,                    
REMARK 900  LAUE DATA                                                           
REMARK 900 RELATED ID: 1CFJ   RELATED DB: PDB                                   
REMARK 900  METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)                    
REMARK 900  OBTAINED BY REACTION WITH O-                                        
REMARK 900  ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)                      
REMARK 900 RELATED ID: 1E3Q   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED                  
REMARK 900   WITH BW284C51                                                      
REMARK 900 RELATED ID: 1EEA   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 1EVE   RELATED DB: PDB                                   
REMARK 900  THREE DIMENSIONAL STRUCTURE OF THE ANTI-                            
REMARK 900  ALZHEIMER DRUG, E2020 (ARICEPT), COMPLEXED                          
REMARK 900  WITH ITS TARGET ACETYLCHOLINESTERASE                                
REMARK 900 RELATED ID: 1FSS   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-                     
REMARK 900  II                                                                  
REMARK 900 RELATED ID: 1GQR   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE (E.C. 3.1.1.7)                                 
REMARK 900  COMPLEXED WITH RIVASTIGMINE                                         
REMARK 900 RELATED ID: 1GQS   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE (E.C. 3.1.1.7)                                 
REMARK 900  COMPLEXED WITH NAP                                                  
REMARK 900 RELATED ID: 1HBJ   RELATED DB: PDB                                   
REMARK 900  X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN                          
REMARK 900  TORPEDO CALIFORNICA ACHE AND A REVERSIBLE                           
REMARK 900  INHIBITOR, 4-AMINO-5-FLUORO-2-METHYL-3-(                            
REMARK 900  3-TRIFLUOROACETYLBENZYLTHIOMETHYL)QUINOLINE                         
REMARK 900 RELATED ID: 1OCE   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH MF268                           
REMARK 900 RELATED ID: 1ODC   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1                         
REMARK 900  .1.7) COMPLEXED WITH N-4'-QUINOLYL-N'-9                             
REMARK 900  "-(1",2",3",4"-TETRAHYDROACRIDINYL)-1,8-                            
REMARK 900  DIAMINOOCTANE AT 2.2A RESOLUTION                                    
REMARK 900 RELATED ID: 1QIE   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT B) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIF   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT C) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIJ   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT G) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIK   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT H) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QIM   RELATED DB: PDB                                   
REMARK 900  SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT                          
REMARK 900  NINE TIME POINTS (POINT I) CAUSED BY                                
REMARK 900  INTENSE SYNCHROTRON RADIATION TO TORPEDO                            
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE                                    
REMARK 900 RELATED ID: 1QTI   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 1U65   RELATED DB: PDB                                   
REMARK 900  ACHE W. CPT-11                                                      
REMARK 900 RELATED ID: 1UT6   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1                         
REMARK 900  .1.7) COMPLEXED WITH N-9-(1',2',3',4                                
REMARK 900  '-TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT                        
REMARK 900  2.4 ANGSTROMS RESOLUTION.                                           
REMARK 900 RELATED ID: 1VOT   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A                     
REMARK 900 RELATED ID: 1W6R   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE                      
REMARK 900 RELATED ID: 1W75   RELATED DB: PDB                                   
REMARK 900  NATIVE ORTHORHOMBIC FORM OF TORPEDO                                 
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE (ACHE)                             
REMARK 900 RELATED ID: 1ZGC   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TORPEDO                                        
REMARK 900  CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH                     
REMARK 900  AN (RS)-TACRINE(10)-HUPYRIDONE INHIBITOR.                           
REMARK 900 RELATED ID: 2ACE   RELATED DB: PDB                                   
REMARK 900  NATIVE ACETYLCHOLINESTERASE FROM TORPEDO                            
REMARK 900  CALIFORNICA                                                         
REMARK 900 RELATED ID: 2ACK   RELATED DB: PDB                                   
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,                    
REMARK 900  MONOCHROMATIC DATA                                                  
REMARK 900 RELATED ID: 2C58   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN                         
REMARK 900  COMPLEX WITH 20MM ACETYLTHIOCHOLINE                                 
REMARK 900 RELATED ID: 2C5F   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN                         
REMARK 900  COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE                           
REMARK 900  ANALOGUE, 4-OXO-N,N,N-TRIMETHYLAMMONIUM                             
REMARK 900 RELATED ID: 2C5G   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN                         
REMARK 900  COMPLEX WITH 20MM THIOCHOLINE                                       
REMARK 900 RELATED ID: 2CEK   RELATED DB: PDB                                   
REMARK 900  CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL                        
REMARK 900  SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE                    
REMARK 900   REVEALED BY THE COMPLEX STRUCTURE WITH A                           
REMARK 900  BIFUNCTIONAL INHIBITOR                                              
REMARK 900 RELATED ID: 2J3D   RELATED DB: PDB                                   
REMARK 900  NATIVE MONOCLINIC FORM OF TORPEDO                                   
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 4ACE   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF (S)-E2020 BOUND                                
REMARK 900  ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES                          
REMARK 900 RELATED ID: 1SOM   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED                  
REMARK 900   BY NERVE AGENT GD (SOMAN).                                         
REMARK 900 RELATED ID: 1VXO   RELATED DB: PDB                                   
REMARK 900  METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)                    
REMARK 900  OBTAINED BY REACTION WITH O-ETHYL-S-[2-[                            
REMARK 900  BIS(1-METHYLETHYL) AMINO]ETHYL]                                     
REMARK 900  METHYLPHOSPHONOTHIOATE (VX)                                         
REMARK 900 RELATED ID: 1VXR   RELATED DB: PDB                                   
REMARK 900  O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE                    
REMARK 900  OBTAINED BY REACTION WITH O-ETHYL-S-[2-[                            
REMARK 900  BIS(1-METHYLETHYL) AMINO]ETHYL]                                     
REMARK 900  METHYLPHOSPHONOTHIOATE (VX)                                         
REMARK 900 RELATED ID: 1W4L   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF TCACHE WITH BIS-ACTING                                   
REMARK 900  GALANTHAMINE DERIVATIVE                                             
REMARK 900 RELATED ID: 1W76   RELATED DB: PDB                                   
REMARK 900  ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA                            
REMARK 900  ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-                     
REMARK 900  ACTING GALANTHAMINE DERIVATIVE                                      
REMARK 900 RELATED ID: 1ZGB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TORPEDO                                        
REMARK 900  CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH                     
REMARK 900  AN (R)-TACRINE(10)-HUPYRIDONE INHIBITOR.                            
REMARK 900 RELATED ID: 2C4H   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN                         
REMARK 900  COMPLEX WITH 500MM ACETYLTHIOCHOLINE                                
REMARK 900 RELATED ID: 2CKM   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED                  
REMARK 900   WITH ALKYLENE-LINKED BIS-TACRINE DIMER (7                          
REMARK 900   CARBON LINKER)                                                     
REMARK 900 RELATED ID: 2CMF   RELATED DB: PDB                                   
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED                  
REMARK 900   WITH ALKYLENE-LINKED BIS-TACRINE DIMER (5                          
REMARK 900   CARBON LINKER)                                                     
REMARK 900 RELATED ID: 2DFP   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF AGED DI-ISOPROPYL-                               
REMARK 900  PHOSPHORO-FLUORIDATE (DFP) BOUND TO                                 
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 2J3Q   RELATED DB: PDB                                   
REMARK 900  TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH                         
REMARK 900  FLUOROPHORE THIOFLAVIN T                                            
REMARK 900 RELATED ID: 2J4F   RELATED DB: PDB                                   
REMARK 900  TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM                        
REMARK 900  DERIVATIVE                                                          
REMARK 900 RELATED ID: 3ACE   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF (R)-E2020 BOUND                                
REMARK 900  ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES                          
REMARK 900 RELATED ID: 2V96   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF                            
REMARK 900  TCACHE WITH 1-(2-NITROPHENYL)-2,2,2-                                
REMARK 900  TRIFLUOROETHYL-ARSENOCHOLINE AT 100K                                
REMARK 900 RELATED ID: 2V97   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF                            
REMARK 900  TCACHE WITH 1-(2-NITROPHENYL)-2,2,2-                                
REMARK 900  TRIFLUOROETHYL-ARSENOCHOLINE AFTER A 9 SECONDS                      
REMARK 900   ANNEALING TO ROOM TEMPERATURE                                      
DBREF  2V98 A    1   537  UNP    P04058   ACES_TORCA      22    558             
DBREF  2V98 B    1   537  UNP    P04058   ACES_TORCA      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     CL  A1536       2                                                       
HET    CFQ  A1537      42                                                       
HET    CFQ  A1538      42                                                       
HET    NAG  A1539      28                                                       
HET    NAG  A1540      28                                                       
HET    CFQ  B1536      42                                                       
HET    CFQ  B1537      42                                                       
HET    NAG  B1538      28                                                       
HET    NAG  B1539      28                                                       
HETNAM     CFQ 1-(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL]-                         
HETNAM   2 CFQ  ARSENOCHOLINE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  CFQ    4(C13 H19 N1 O3 AS1 F3)                                      
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  NAG    4(C8 H15 N O6)                                               
FORMUL   6  HOH   *1942(H2 O1)                                                  
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  212  ASP A  217  1                                   6    
HELIX   10  10 VAL A  238  LEU A  252  1                                  15    
HELIX   11  11 SER A  258  LYS A  269  1                                  12    
HELIX   12  12 LYS A  270  ASP A  276  1                                   7    
HELIX   13  13 VAL A  277  LEU A  282  5                                   6    
HELIX   14  14 SER A  304  SER A  311  1                                   8    
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  THR A  412  1                                  13    
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  VAL A  453  5                                   5    
HELIX   23  23 VAL A  453  ASN A  457  5                                   5    
HELIX   24  24 THR A  459  GLY A  480  1                                  22    
HELIX   25  25 ARG A  517  GLN A  526  1                                  10    
HELIX   26  26 GLN A  526  THR A  535  1                                  10    
HELIX   27  27 VAL B   40  ARG B   44  5                                   5    
HELIX   28  28 PHE B   78  MET B   83  1                                   6    
HELIX   29  29 LEU B  127  ASN B  131  5                                   5    
HELIX   30  30 GLY B  132  GLU B  140  1                                   9    
HELIX   31  31 VAL B  150  LEU B  156  1                                   7    
HELIX   32  32 ASN B  167  ILE B  184  1                                  18    
HELIX   33  33 GLN B  185  PHE B  187  5                                   3    
HELIX   34  34 SER B  200  SER B  212  1                                  13    
HELIX   35  35 SER B  215  PHE B  219  5                                   5    
HELIX   36  36 SER B  237  LEU B  252  1                                  16    
HELIX   37  37 SER B  258  ARG B  267  1                                  10    
HELIX   38  38 LYS B  270  ASP B  276  1                                   7    
HELIX   39  39 VAL B  277  LEU B  282  5                                   6    
HELIX   40  40 SER B  304  SER B  311  1                                   8    
HELIX   41  41 GLY B  328  ALA B  336  1                                   9    
HELIX   42  42 SER B  348  VAL B  360  1                                  13    
HELIX   43  43 ASN B  364  TYR B  375  1                                  12    
HELIX   44  44 ASN B  383  VAL B  400  1                                  18    
HELIX   45  45 VAL B  400  THR B  412  1                                  13    
HELIX   46  46 PRO B  433  GLY B  437  5                                   5    
HELIX   47  47 GLU B  443  PHE B  448  1                                   6    
HELIX   48  48 GLY B  449  VAL B  453  5                                   5    
HELIX   49  49 VAL B  453  ASN B  457  5                                   5    
HELIX   50  50 THR B  459  GLY B  480  1                                  22    
HELIX   51  51 ARG B  517  GLN B  526  1                                  10    
HELIX   52  52 GLN B  526  THR B  535  1                                  10    
SHEET    1  AA 3 LEU A   7  ASN A   9  0                                        
SHEET    2  AA 3 LYS A  14  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3  AA 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1  AB11 THR A  18  PRO A  21  0                                        
SHEET    2  AB11 HIS A  26  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3  AB11 TYR A  96  VAL A 101 -1  O  LEU A  97   N  ILE A  33           
SHEET    4  AB11 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100           
SHEET    5  AB11 THR A 109  ILE A 115  1  O  THR A 110   N  VAL A 142           
SHEET    6  AB11 GLY A 189  GLU A 199  1  N  ASP A 190   O  THR A 109           
SHEET    7  AB11 ARG A 221  GLN A 225  1  O  ARG A 221   N  ILE A 196           
SHEET    8  AB11 ILE A 319  ASN A 324  1  O  LEU A 320   N  LEU A 224           
SHEET    9  AB11 THR A 418  PHE A 423  1  O  TYR A 419   N  LEU A 321           
SHEET   10  AB11 LYS A 501  ASP A 504  1  O  ILE A 503   N  PHE A 422           
SHEET   11  AB11 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502           
SHEET    1  AC 2 VAL A 236  SER A 237  0                                        
SHEET    2  AC 2 VAL A 295  ILE A 296  1  N  ILE A 296   O  VAL A 236           
SHEET    1  BA 3 LEU B   7  ASN B   9  0                                        
SHEET    2  BA 3 LYS B  14  MET B  16 -1  O  VAL B  15   N  VAL B   8           
SHEET    3  BA 3 VAL B  57  ASN B  59  1  O  TRP B  58   N  MET B  16           
SHEET    1  BB11 THR B  18  VAL B  22  0                                        
SHEET    2  BB11 SER B  25  PRO B  34 -1  O  SER B  25   N  VAL B  22           
SHEET    3  BB11 TYR B  96  PRO B 102 -1  O  LEU B  97   N  ILE B  33           
SHEET    4  BB11 VAL B 142  SER B 145 -1  O  LEU B 143   N  TRP B 100           
SHEET    5  BB11 THR B 109  ILE B 115  1  O  THR B 110   N  VAL B 142           
SHEET    6  BB11 GLY B 189  GLU B 199  1  N  ASP B 190   O  THR B 109           
SHEET    7  BB11 ARG B 221  GLN B 225  1  O  ARG B 221   N  ILE B 196           
SHEET    8  BB11 ILE B 319  ASN B 324  1  O  LEU B 320   N  LEU B 224           
SHEET    9  BB11 THR B 418  PHE B 423  1  O  TYR B 419   N  LEU B 321           
SHEET   10  BB11 LYS B 501  LEU B 505  1  O  ILE B 503   N  PHE B 422           
SHEET   11  BB11 VAL B 512  GLN B 514 -1  O  HIS B 513   N  PHE B 502           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.01  
SSBOND   3 CYS A  254    CYS A  265                          1555   1555  2.02  
SSBOND   5 CYS A  402    CYS A  521                          1555   1555  2.04  
SSBOND   7 CYS B   67    CYS B   94                          1555   1555  2.03  
SSBOND   9 CYS B  254    CYS B  265                          1555   1555  2.03  
SSBOND  11 CYS B  402    CYS B  521                          1555   1555  2.04  
CISPEP   1 SER A  103    PRO A  104          0        -0.74                     
CISPEP   2 SER B  103    PRO B  104          0         1.73                     
SITE     1 AC1  4 SER A 161  GLU A 163  GLU A 260  LYS B 511                    
SITE     1 AC2 26 TYR A  70  TYR A 121  TRP A 279  SER A 286                    
SITE     2 AC2 26 ILE A 287  PHE A 288  ARG A 289  PHE A 290                    
SITE     3 AC2 26 PHE A 331  TYR A 334  GLY A 335  HOH A2166                    
SITE     4 AC2 26 HOH A2175  HOH A2506  HOH A2507  HOH A2509                    
SITE     5 AC2 26 HOH A2510  HOH A2524  SER B 108  GLN B 185                    
SITE     6 AC2 26 HOH B2325  HOH B2416  HOH B2421  HOH B2422                    
SITE     7 AC2 26 HOH B2423  HOH B2427                                          
SITE     1 AC3 19 ASP A  72  TRP A  84  GLY A 118  GLY A 119                    
SITE     2 AC3 19 TYR A 121  GLU A 199  SER A 200  PHE A 290                    
SITE     3 AC3 19 PHE A 330  PHE A 331  TYR A 334  HIS A 440                    
SITE     4 AC3 19 GLY A 441  ILE A 444  HOH A2201  HOH A2202                    
SITE     5 AC3 19 HOH A2207  HOH A2278  HOH A2279                               
SITE     1 AC4  2 ASN A  59  SER A  61                                          
SITE     1 AC5 18 GLY A 415  ASN A 416  LEU A 494  HOH A2702                    
SITE     2 AC5 18 HOH A2703  HOH A2704  HOH A2705  HOH A2910                    
SITE     3 AC5 18 HOH A2912  HOH A2913  HOH A2915  HOH A2916                    
SITE     4 AC5 18 HOH A2918  HOH A2919  HOH A2920  HOH A2921                    
SITE     5 AC5 18 HOH A2923  HOH A2925                                          
SITE     1 AC6 14 SER A 108  GLN A 185  TYR B  70  ASP B  72                    
SITE     2 AC6 14 TYR B 121  TRP B 279  ILE B 287  PHE B 288                    
SITE     3 AC6 14 PHE B 290  PHE B 331  TYR B 334  GLY B 335                    
SITE     4 AC6 14 HOH B2570  HOH B2991                                          
SITE     1 AC7 19 TRP B  84  GLY B 118  GLY B 119  TYR B 121                    
SITE     2 AC7 19 GLU B 199  SER B 200  PHE B 290  PHE B 330                    
SITE     3 AC7 19 PHE B 331  TYR B 334  HIS B 440  GLY B 441                    
SITE     4 AC7 19 ILE B 444  HOH B2225  HOH B2235  HOH B2236                    
SITE     5 AC7 19 HOH B2332  HOH B2333  HOH B2992                               
SITE     1 AC8 10 ASN B  59  SER B  61  THR B  62  HOH B2173                    
SITE     2 AC8 10 HOH B2993  HOH B2994  HOH B2995  HOH B2999                    
SITE     3 AC8 10 HOH B3000  HOH B3001                                          
SITE     1 AC9 15 ASN B 416  HOH B2744  HOH B2745  HOH B2750                    
SITE     2 AC9 15 HOH B2751  HOH B3002  HOH B3003  HOH B3004                    
SITE     3 AC9 15 HOH B3005  HOH B3006  HOH B3007  HOH B3008                    
SITE     4 AC9 15 HOH B3009  HOH B3016  HOH B3017                               
CRYST1   91.620  104.470  148.800  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      0.010915  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009572  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006720        0.00000                         
TER    8363      THR A 535                                                      
TER   16762      THR B 535                                                      
MASTER      689    0    9   52   30    0   35    618984    2  272   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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