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LongText Report for: 1F8U-pdb

Name Class
1F8U-pdb
HEADER    HYDROLASE/TOXIN                         05-JUL-00   1F8U              
TITLE     CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN                            
TITLE    2 ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM                
TITLE    3 PEPTIDE FASCICULIN-II                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.7;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FASCICULIN II;                                             
COMPND   8 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: ACHE;                                                          
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE   8 EXPRESSION_SYSTEM_TISSUE: KIDNEY;                                    
SOURCE   9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY CELLS;                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;                        
SOURCE  12 ORGANISM_COMMON: EASTERN GREEN MAMBA;                                
SOURCE  13 SECRETION: VENOM                                                     
KEYWDS    SERINE ESTERASE, HUMAN ACETYLCHOLINESTERASE, HYDROLASE,               
KEYWDS   2 SNAKE TOXIN, HYDROLASE/HYDROLASE INHIBITOR                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.KRYGER,M.HAREL,A.SHAFFERMAN,I.SILMAN,J.L.SUSSMAN                    
REVDAT   1   17-JAN-01 1F8U    0                                                
JRNL        AUTH   G.KRYGER,M.HAREL,M.HAREL,A.SHAFFERMAN,I.SILMAN,              
JRNL        AUTH 2 J.L.SUSSMAN                                                  
JRNL        TITL   STRUCTURES OF RECOMBINANT NATIVE AND E202Q MUTANT            
JRNL        TITL 2 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH THE                
JRNL        TITL 3 SNAKE-VENOM TOXIN FASCICULIN-II                              
JRNL        REF    ACTA CRYSTALLOGR., SECT.D     V.  56  1385 2000              
JRNL        REFN   ASTM ABCRE6  DK ISSN 0907-4449                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.90 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22803                          
REMARK   3                                                                      
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) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1134                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2578                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3180                       
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 134                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4594                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 16.29000                                             
REMARK   3    B22 (A**2) : 16.29000                                             
REMARK   3    B33 (A**2) : -32.58000                                            
REMARK   3    B12 (A**2) : 14.92000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.580                           
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) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.59                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95                            
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) : 6.42  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 9.86  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 9.65  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 13.31 ; 2.500                
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 59.89                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F8U COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-2000.                
REMARK 100 THE RCSB ID CODE IS RCSB011385.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.009                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   2/3+X,1/3+Y,1/3+Z                                       
REMARK 290       8555   2/3-Y,1/3+X-Y,1/3+Z                                     
REMARK 290       9555   2/3-X+Y,1/3-X,1/3+Z                                     
REMARK 290      10555   2/3+Y,1/3+X,1/3-Z                                       
REMARK 290      11555   2/3+X-Y,1/3-Y,1/3-Z                                     
REMARK 290      12555   2/3-X,1/3-X+Y,1/3-Z                                     
REMARK 290      13555   1/3+X,2/3+Y,2/3+Z                                       
REMARK 290      14555   1/3-Y,2/3+X-Y,2/3+Z                                     
REMARK 290      15555   1/3-X+Y,2/3-X,2/3+Z                                     
REMARK 290      16555   1/3+Y,2/3+X,2/3-Z                                       
REMARK 290      17555   1/3+X-Y,2/3-Y,2/3-Z                                     
REMARK 290      18555   1/3-X,2/3-X+Y,2/3-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 -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        0.00000            
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        0.00000            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       75.55500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.62170            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       82.34000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       75.55500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       43.62170            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       82.34000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       75.55500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       43.62170            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       82.34000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       75.55500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       43.62170            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       82.34000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       75.55500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       43.62170            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       82.34000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       75.55500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       43.62170            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       82.34000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       87.24340            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      164.68000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       87.24340            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      164.68000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       87.24340            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      164.68000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       87.24340            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      164.68000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       87.24340            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      164.68000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       87.24340            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      164.68000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B, X                               
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     GLU A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     ASP A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     ASP A   547                                                      
REMARK 465     GLU A   548                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     GLU A   550                                                      
REMARK 465     ARG A   551                                                      
REMARK 465     GLN A   552                                                      
REMARK 465     TRP A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     ALA A   555                                                      
REMARK 465     GLU A   556                                                      
REMARK 465     PHE A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     ARG A   559                                                      
REMARK 465     TRP A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     SER A   562                                                      
REMARK 465     TYR A   563                                                      
REMARK 465     MET A   564                                                      
REMARK 465     VAL A   565                                                      
REMARK 465     HIS A   566                                                      
REMARK 465     TRP A   567                                                      
REMARK 465     LYS A   568                                                      
REMARK 465     ASN A   569                                                      
REMARK 465     GLN A   570                                                      
REMARK 465     PHE A   571                                                      
REMARK 465     ASP A   572                                                      
REMARK 465     HIS A   573                                                      
REMARK 465     TYR A   574                                                      
REMARK 465     SER A   575                                                      
REMARK 465     LYS A   576                                                      
REMARK 465     GLN A   577                                                      
REMARK 465     ASP A   578                                                      
REMARK 465     ARG A   579                                                      
REMARK 465     CYS A   580                                                      
REMARK 465     SER A   581                                                      
REMARK 465     ASP A   582                                                      
REMARK 465     LEU A   583                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   O    HOH     601     O    HOH     602              2.09            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A 149   CE    MET A 149   SD     0.048                        
REMARK 500    MET A 241   CE    MET A 241   SD    -0.058                        
REMARK 500    MET A 443   CE    MET A 443   SD    -0.065                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A  39   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    PHE A 158   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
REMARK 500    LEU A 161   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    ASN A 186   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
REMARK 500    ARG A 219   N   -  CA  -  C   ANGL. DEV. =  9.2 DEGREES           
REMARK 500    GLN A 291   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES           
REMARK 500    GLY A 335   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES           
REMARK 500    ASP A 384   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    VAL A 407   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    GLY A 422   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    GLU A 491   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES           
REMARK 500    ARG B  27   N   -  CA  -  C   ANGL. DEV. = -8.5 DEGREES           
REMARK 500    SER B  55   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   6      -73.48     76.80                                   
REMARK 500    GLN A 291      168.26     62.90                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B41   RELATED DB: PDB                                   
REMARK 900 NATIVE HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN               
REMARK 900 MAMBA VENOM PEPTIDE FASCICULIN-II                                    
DBREF  1F8U A    1   583  SWS    P22303   ACES_HUMAN      32    614             
DBREF  1F8U B    1    61  SWS    P01403   TXF7_DENAN       1     61             
SEQADV 1F8U GLN A  202  SWS  P22303    GLU   233 ENGINEERED                     
SEQRES   1 A  583  GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG          
SEQRES   2 A  583  GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY          
SEQRES   3 A  583  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  583  PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO          
SEQRES   5 A  583  LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE          
SEQRES   6 A  583  GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  583  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  583  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  583  TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP          
SEQRES  10 A  583  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU          
SEQRES  11 A  583  ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG          
SEQRES  12 A  583  THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE          
SEQRES  13 A  583  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  583  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  583  VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR          
SEQRES  16 A  583  SER VAL THR LEU PHE GLY GLN SER ALA GLY ALA ALA SER          
SEQRES  17 A  583  VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU          
SEQRES  18 A  583  PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY          
SEQRES  19 A  583  PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  583  ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  583  GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU          
SEQRES  22 A  583  ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP          
SEQRES  23 A  583  HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE          
SEQRES  24 A  583  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  583  GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN          
SEQRES  26 A  583  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  583  LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  583  SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  583  VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  583  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  583  PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY          
SEQRES  32 A  583  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  583  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL          
SEQRES  34 A  583  PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP          
SEQRES  35 A  583  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  583  GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU          
SEQRES  37 A  583  GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA          
SEQRES  38 A  583  ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP          
SEQRES  39 A  583  PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA          
SEQRES  40 A  583  GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL          
SEQRES  41 A  583  ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN          
SEQRES  42 A  583  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU          
SEQRES  43 A  583  ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU PHE HIS ARG          
SEQRES  44 A  583  TRP SER SER TYR MET VAL HIS TRP LYS ASN GLN PHE ASP          
SEQRES  45 A  583  HIS TYR SER LYS GLN ASP ARG CYS SER ASP LEU                  
SEQRES   1 B   61  THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE          
SEQRES   2 B   61  LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER          
SEQRES   3 B   61  ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS          
SEQRES   4 B   61  GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS          
SEQRES   5 B   61  CYS THR SER PRO ASP LYS CYS ASN TYR                          
MODRES 1F8U ASN A  350  ASN  GLYCOSYLATION SITE                                 
HET    NAG  X3002      14                                                       
HET    NAG  X3003      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     NAG NAG                                                              
FORMUL   3  NAG    2(C8 H15 N1 O6)                                              
FORMUL   4  HOH   *117(H2 O1)                                                   
HELIX    1   1 MET A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  ARG A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  VAL A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 SER A  203  SER A  215  1                                  13    
HELIX    9   9 PRO A  216  PHE A  222  5                                   7    
HELIX   10  10 MET A  241  VAL A  255  1                                  15    
HELIX   11  11 ASN A  265  ARG A  274  1                                  10    
HELIX   12  12 PRO A  277  HIS A  284  1                                   8    
HELIX   13  13 GLU A  285  LEU A  289  5                                   5    
HELIX   14  14 THR A  311  GLY A  319  1                                   9    
HELIX   15  15 GLY A  335  VAL A  340  1                                   6    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  GLN A  421  1                                  15    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 THR A  466  GLY A  487  1                                  22    
HELIX   24  24 ARG A  525  ARG A  534  1                                  10    
HELIX   25  25 ARG A  534  ALA A  542  1                                   9    
SHEET    1   A 3 LEU A   9  THR A  11  0                                        
SHEET    2   A 3 ARG A  16  ARG A  18 -1  N  LEU A  17   O  VAL A  10           
SHEET    3   A 3 VAL A  59  ASP A  61  1  N  VAL A  60   O  ARG A  16           
SHEET    1   B11 ILE A  20  LEU A  22  0                                        
SHEET    2   B11 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3   B11 TYR A  98  PRO A 104 -1  N  LEU A  99   O  ILE A  35           
SHEET    4   B11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5   B11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6   B11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    7   B11 LEU A 324  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    8   B11 ALA A 423  PHE A 430  1  N  ARG A 424   O  LEU A 324           
SHEET    9   B11 GLN A 509  LEU A 513  1  O  VAL A 511   N  VAL A 429           
SHEET   10   B11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1   C 2 ALA A  38  GLU A  39  0                                        
SHEET    2   C 2 GLU A  51  PRO A  52 -1  O  GLU A  51   N  GLU A  39           
SHEET    1   D 2 VAL A  68  CYS A  69  0                                        
SHEET    2   D 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1   E 2 VAL A 239  GLY A 240  0                                        
SHEET    2   E 2 VAL A 302  VAL A 303  1  N  VAL A 303   O  VAL A 239           
SHEET    1   F 2 MET B   2  SER B   5  0                                        
SHEET    2   F 2 ILE B  13  ASN B  16 -1  N  ILE B  13   O  SER B   5           
SHEET    1   G 3 VAL B  34  CYS B  39  0                                        
SHEET    2   G 3 CYS B  22  ARG B  27 -1  N  TYR B  23   O  GLY B  38           
SHEET    3   G 3 LEU B  48  CYS B  53 -1  N  GLU B  49   O  SER B  26           
SSBOND   1 CYS A   69    CYS A   96                                             
SSBOND   2 CYS A  257    CYS A  272                                             
SSBOND   3 CYS A  409    CYS A  529                                             
SSBOND   4 CYS B    3    CYS B   22                                             
SSBOND   5 CYS B   17    CYS B   39                                             
SSBOND   6 CYS B   41    CYS B   52                                             
SSBOND   7 CYS B   53    CYS B   59                                             
LINK         O4  NAG X3002                 C1  NAG X3003                        
LINK         C1  NAG X3002                 ND2 ASN A 350                        
CISPEP   1 TYR A  105    PRO A  106          0         0.48                     
CISPEP   2 CYS A  257    PRO A  258          0         0.57                     
CISPEP   3 PRO B   30    PRO B   31          0         0.13                     
CRYST1  151.110  151.110  247.020  90.00  90.00 120.00 H 3 2        18          
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      0.006618  0.003821  0.000000        0.00000                         
SCALE2      0.000000  0.007641  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004048        0.00000                                  
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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