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LongText Report for: 3ZLU-pdb

Name Class
3ZLU-pdb
HEADER    HYDROLASE                               04-FEB-13   3ZLU              
TITLE     CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX            
TITLE    2 WITH CYCLOSARIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: CATALYTIC SER203 PHOSPHONYLATED BY CYCLOSARIN         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F                                 
KEYWDS    HYDROLASE, RUSSIAN VX, CYCLOSARIN, GF, TABUN, GA, HI-6, OXIME         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ARTURSSON,P.O.ANDERSSON,C.AKFUR,A.LINUSSON,S.BORJEGREN,F.EKSTROM    
REVDAT   1   27-MAR-13 3ZLU    0                                                
JRNL        AUTH   E.ARTURSSON,P.O.ANDERSSON,C.AKFUR,A.LINUSSON,S.BORJEGREN,    
JRNL        AUTH 2 F.EKSTROM                                                    
JRNL        TITL   CATALYTIC-SITE CONFORMATIONAL EQUILIBRIUM IN NERVE-AGENT     
JRNL        TITL 2 ADDUCTS OF ACETYLCHOLINESTERASE; POSSIBLE IMPLICATIONS FOR   
JRNL        TITL 3 THE HI-6 ANTIDOTE SUBSTRATE SPECIFICITY.                     
JRNL        REF    BIOCHEM.PHARMACOL.                         2013              
JRNL        REFN                   ESSN 1873-2968                               
JRNL        PMID   23376121                                                     
JRNL        DOI    10.1016/J.BCP.2013.01.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.600                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.333                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 64481                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1763                          
REMARK   3   R VALUE            (WORKING SET) : 0.1755                          
REMARK   3   FREE R VALUE                     : 0.2171                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1283                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.3348 -  5.3982    0.99     7316   147  0.1589 0.1845        
REMARK   3     2  5.3982 -  4.2890    1.00     7111   140  0.1330 0.1647        
REMARK   3     3  4.2890 -  3.7481    1.00     7035   137  0.1530 0.2008        
REMARK   3     4  3.7481 -  3.4060    1.00     7018   140  0.1798 0.2215        
REMARK   3     5  3.4060 -  3.1622    1.00     6958   135  0.1984 0.2129        
REMARK   3     6  3.1622 -  2.9759    1.00     6941   158  0.2165 0.2811        
REMARK   3     7  2.9759 -  2.8270    1.00     6951   135  0.2419 0.3352        
REMARK   3     8  2.8270 -  2.7040    1.00     6937   141  0.2620 0.3354        
REMARK   3     9  2.7040 -  2.6000    1.00     6931   150  0.2510 0.2879        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.308                                         
REMARK   3   B_SOL              : 46.426                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.65             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.60            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.0009                                               
REMARK   3    B22 (A**2) : 0.1511                                               
REMARK   3    B33 (A**2) : -2.1520                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           8773                                  
REMARK   3   ANGLE     :  1.139          11957                                  
REMARK   3   CHIRALITY :  0.082           1280                                  
REMARK   3   PLANARITY :  0.006           1563                                  
REMARK   3   DIHEDRAL  : 17.463           3206                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-55714.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : CCDCHESS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64575                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.02                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.7                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.99350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.75400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.75950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.75400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.99350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.75950            
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/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: PISA                                                  
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     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
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     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
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           DISTANCE          
REMARK 500   CD1A PHE A   338     O    HOH A  2182              1.25            
REMARK 500   CE1A PHE A   338     O    HOH A  2182              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -9.85     77.39                                   
REMARK 500    ALA A  62       55.60   -119.81                                   
REMARK 500    ALA A 127      144.42   -173.10                                   
REMARK 500    ALA A 167       68.64   -151.55                                   
REMARK 500    ASP A 306      -92.25   -129.53                                   
REMARK 500    VAL A 407      -66.20   -129.84                                   
REMARK 500    HIS A 447      133.90    -34.23                                   
REMARK 500    ARG A 493      -85.25    -61.06                                   
REMARK 500    SER B  93      144.97   -174.62                                   
REMARK 500    CYS B  96       -2.38   -146.19                                   
REMARK 500    PRO B 108      136.50    -39.21                                   
REMARK 500    ASP B 306      -88.53   -106.62                                   
REMARK 500    ASP B 323       47.57   -100.77                                   
REMARK 500    TYR B 341       36.91    -98.25                                   
REMARK 500    ASN B 350     -135.13   -104.75                                   
REMARK 500    VAL B 407      -66.05   -120.16                                   
REMARK 500    ASN B 514     -167.02   -166.09                                   
REMARK 500    ALA B 542       57.40   -103.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  496     SER B  497                 -136.53                    
REMARK 500 ALA B  542     THR B  543                  149.13                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER B 497        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2249        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A2250        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH B2091        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH B2195        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH B2198        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH B2199        DISTANCE =  7.82 ANGSTROMS                       
REMARK 525    HOH B2200        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH B2202        DISTANCE =  5.65 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P15 A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA A1546                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZLT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH           
REMARK 900   RVX                                                                
REMARK 900 RELATED ID: 3ZLV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH TABUN AND HI-6                                                
DBREF  3ZLU A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  3ZLU B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQRES   1 A  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  543  SER VAL THR LEU PHE GLY GLU GFT ALA GLY ALA ALA SER          
SEQRES  17 A  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 B  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  543  SER VAL THR LEU PHE GLY GLU GFT ALA GLY ALA ALA SER          
SEQRES  17 B  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
MODRES 3ZLU GFT A  203  SER  CYCLOSARIN BOUND SERINE                            
MODRES 3ZLU GFT B  203  SER  CYCLOSARIN BOUND SERINE                            
HET    GFT  A 203      16                                                       
HET    GFT  B 203      16                                                       
HET    1KA  B1544       7                                                       
HET    1KA  A1543       7                                                       
HET    1KA  B1545       7                                                       
HET    P15  A1544      20                                                       
HET    1KA  A1545       7                                                       
HET    1KA  A1546       7                                                       
HETNAM     1KA (2-HYDROXYETHOXY)ACETALDEHYDE                                    
HETNAM     P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL                            
HETNAM     GFT (2S)-2-AZANYL-3-[CYCLOHEXYLOXY(METHYL)                           
HETNAM   2 GFT  PHOSPHORYL]OXY-PROPANOIC ACID                                   
HETSYN     GFT CYCLOSARIN BOUND SERINE                                          
FORMUL   3  1KA    5(C4 H8 O3)                                                  
FORMUL   4  P15    C13 H28 O7                                                   
FORMUL   5  GFT    2(C10 H20 N O5 P)                                            
FORMUL   7  HOH   *454(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 GFT A  203  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  GLY A  256  1                                  17    
HELIX   12  12 ASN A  265  ARG A  276  1                                  12    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  THR A  318  1                                   8    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  ALA A  420  1                                  14    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  SER A  541  1                                   8    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLU B  142  1                                   8    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 GFT B  203  LEU B  214  1                                  12    
HELIX   37  37 SER B  215  SER B  220  1                                   6    
HELIX   38  38 SER B  240  GLY B  256  1                                  17    
HELIX   39  39 ASN B  265  THR B  275  1                                  11    
HELIX   40  40 PRO B  277  HIS B  284  1                                   8    
HELIX   41  41 GLU B  285  VAL B  288  5                                   4    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 SER B  336  GLY B  342  5                                   7    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  GLY B  456  1                                   7    
HELIX   50  50 LEU B  457  ASN B  464  5                                   8    
HELIX   51  51 THR B  466  GLY B  487  1                                  22    
HELIX   52  52 ARG B  525  ARG B  534  1                                  10    
HELIX   53  53 ARG B  534  ALA B  542  1                                   9    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.07  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         N   GFT A 203                 C   GLU A 202     1555   1555  1.31  
LINK         C   GFT A 203                 N   ALA A 204     1555   1555  1.32  
LINK         C   GFT B 203                 N   ALA B 204     1555   1555  1.33  
LINK         N   GFT B 203                 C   GLU B 202     1555   1555  1.32  
CISPEP   1 TYR A  105    PRO A  106          0         1.07                     
CISPEP   2 TYR B  105    PRO B  106          0         5.63                     
CISPEP   3 SER B  497    PRO B  498          0       -11.39                     
SITE     1 AC1  3 TYR B 382  ASP B 384  HOH B2196                               
SITE     1 AC2  3 VAL A 303  ASP A 304  GLY A 305                               
SITE     1 AC3  2 SER B 309  HOH B2197                                          
SITE     1 AC4  9 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC4  9 HOH A2198  LEU B 380  HIS B 381  GLN B 527                    
SITE     3 AC4  9 PHE B 535                                                     
SITE     1 AC5  3 HIS A 381  TYR A 382  HOH A2252                               
SITE     1 AC6  2 TYR A  72  TYR A 124                                          
CRYST1   79.987  113.519  227.508  90.00  90.00  90.00 P 21 21 21    4          
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      0.012502  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004395        0.00000                         
TER    4228      ALA A 542                                                      
TER    8417      THR B 543                                                      
MASTER      368    0    8   53   32    0    8    6 8924    2  103   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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