Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 2JEZ-pdb

Name Class
2JEZ-pdb
HEADER    HYDROLASE                               25-JAN-07   2JEZ              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND           
TITLE    2 HLO-7                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 SYNONYM: ACHE;                                                       
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   6 EC: 3.1.1.7, 3.1.1.1;                                                
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   3 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1;                                 
SOURCE   4 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   6 ORGANISM_COMMON: MOUSE                                               
KEYWDS    ACETYLCHOLINESTERASE, ALTERNATIVE SPLICING,                           
KEYWDS   2 NEUROTRANSMITTER DEGRADATION,                                        
KEYWDS   3 HYDROLASE, MUS MUSCULUS, GLYCOPROTEIN, SERINE ESTERASE,              
KEYWDS   4 OXIME, MOUSE, HLO-7, TABUN, SYNAPSE, MEMBRANE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.EKSTROM,C.ASTOT,Y.P.PANG                                            
REVDAT   1   03-JUL-07 2JEZ    0                                                
JRNL        AUTH   F.EKSTROM,C,ASTOT,Y.P.PANG                                   
JRNL        TITL   NOVEL NERVE-AGENT ANTIDOTE DESIGN BASED ON                   
JRNL        TITL 2 CRYSTALLOGRAPHIC AND MASS SPECTROMETRIC ANALYSES             
JRNL        TITL 3 OF TABUN-CONJUGATED ACETYLCHOLINESTERASE IN                  
JRNL        TITL 4 COMPLEX WITH ANTIDOTES.                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.6  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) :   2.60                         
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) :  29.14                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) :  99.99                         
REMARK   3   NUMBER OF REFLECTIONS             :   56619                        
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 + TEST SET) : 0.19346                         
REMARK   3   R VALUE            (WORKING SET) :  0.19249                        
REMARK   3   FREE R VALUE                     :  0.24315                        
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  2.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      :  1144                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           :      20                      
REMARK   3   BIN RESOLUTION RANGE HIGH           :    2.600                     
REMARK   3   BIN RESOLUTION RANGE LOW            :    2.667                     
REMARK   3   REFLECTION IN BIN     (WORKING SET) :     4113                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) :    99.98                     
REMARK   3   BIN R VALUE           (WORKING SET) :    0.267                     
REMARK   3   BIN FREE R VALUE SET COUNT          :       85                     
REMARK   3   BIN FREE R VALUE                    :    0.364                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8324                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 95                                      
REMARK   3   SOLVENT ATOMS            : 294                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  40.148                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) :    -0.01                                             
REMARK   3    B22 (A**2) :     0.02                                             
REMARK   3    B33 (A**2) :    -0.01                                             
REMARK   3    B12 (A**2) :     0.00                                             
REMARK   3    B13 (A**2) :     0.00                                             
REMARK   3    B23 (A**2) :     0.00                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A):   0.319       
REMARK   3   ESU BASED ON FREE R VALUE                       (A):   0.250       
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A):   0.165       
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):   7.622       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      :   0.937                       
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE :   0.894                       
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  8672 ; 0.013 ; 0.022          
REMARK   3   BOND ANGLES REFINED      (DEGREES): 11833 ; 1.458 ; 1.966          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):  1060 ; 6.678 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):   395 ;35.087 ;22.861          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):  1253 ;17.850 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):    72 ;19.683 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):  1264 ; 0.091 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  6836 ; 0.005 ; 0.020          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  6364 ; 0.237 ; 0.200          
REMARK   3   NON-BONDED TORSION REFINED     (A):  6154 ; 0.327 ; 0.200          
REMARK   3   H-BOND (X...Y) REFINED         (A):   785 ; 0.163 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):    68 ; 0.251 ; 0.200          
REMARK   3   SYMMETRY H-BOND REFINED        (A):    14 ; 0.235 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT   RMS    WEIGHT          
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  5387 ; 0.685 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  8576 ; 1.216 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  3715 ; 1.564 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  3257 ; 2.615 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED :  MASK                                                
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   :   1.20                                        
REMARK   3   ION PROBE RADIUS   :   0.80                                        
REMARK   3   SHRINKAGE RADIUS   :   0.80                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN                       
REMARK   3   ADDED IN THE RIDING POSITIONS                                      
REMARK   3   TABUN REACTION PRODUCT COVALENTELY ATTACHED TO SER203.             
REMARK   4                                                                      
REMARK   4 2JEZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 25-JAN-2007.                
REMARK 100 THE EBI ID CODE IS EBI-31210.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II BEAMLINE I711               
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08191                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESERACH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57837                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.14                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.10                              
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) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.42                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 70                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-30 % PEG750MME, 0.1 M HEPES           
REMARK 280  PH 7.0                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.46000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      110.16000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      110.16000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.46000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.47000            
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 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 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC                       
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                                     
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 BIOMOLECULE:  2                                                      
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     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
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 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
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 470     ALA B 544    CA   C    O    CB                                   
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    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    LEU A 251   CA  -  CB  -  CG  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    LEU B 161   CA  -  CB  -  CG  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    LEU B 216   CA  -  CB  -  CG  ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG B 274   CG  -  CD  -  NE  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LEU B 360   CA  -  CB  -  CG  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ILE B 429   N   -  CA  -  C   ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    PRO B 498   C   -  N   -  CA  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    GLU B 519   N   -  CA  -  C   ANGL. DEV. =  -8.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH Y    53     O    HOH Y   117               1.67           
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A    13     O    SER B    57     2555      2.10           
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO                 
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY            
REMARK 525 ASSOCIATED WITH:                                                     
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN                                       
REMARK 525     A              Z                                                 
REMARK 525     B              Y                                                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: HLO BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: HLO BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: P6G BINDING SITE FOR CHAIN B                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN THE APOFORM                                                     
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-DECIDIUM COMPLEX                               
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-GALLAMINE COMPLEX                              
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-PROPIDIUM COMPLEX                              
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX                              
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6ANTI COMPLEX                             
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE                             
REMARK 900  INHIBITED BY TABUN                                                  
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN                                                  
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)                           
REMARK 900  TRIFLUOROACETOPHENONE                                               
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                          
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH SUCCINYLCHOLINE                                      
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH CHOLINE                                              
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  ACETYLCHOLINE                                                       
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE                
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  SUCCINYLCHOLINE                                                     
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  BUTYRYLTHIOCHOLINE                                                  
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH TABUN AND ORTHO-7                                              
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH HLO-7                                                          
DBREF  2JEZ A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2JEZ A  544   548  PDB    2JEZ     2JEZ           544    548             
DBREF  2JEZ B    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2JEZ B  544   548  PDB    2JEZ     2JEZ           544    548             
SEQRES   1 A  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  548  SER VAL THR LEU PHE GLY GLU SUN ALA GLY ALA ALA SER          
SEQRES  17 A  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 A  548  ALA PRO                                                      
SEQRES   1 B  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  548  SER VAL THR LEU PHE GLY GLU SUN ALA GLY ALA ALA SER          
SEQRES  17 B  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 B  548  ALA PRO                                                      
MODRES 2JEZ SUN A  203  SER  TABUN CONJUGATED SERINE                            
MODRES 2JEZ SUN B  203  SER  TABUN CONJUGATED SERINE                            
HET    SUN  A 203      14                                                       
HET    HLO  A1543      24                                                       
HET    SUN  B 203      14                                                       
HET    HLO  B1545      24                                                       
HET    P6G  B1546      19                                                       
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     SUN O-[(R)-(DIMETHYLAMINO)(ETHOXY)PHOSPHORYL]-L-                     
HETNAM   2 SUN  SERINE                                                          
HETSYN     SUN TABUN CONJUGATED SERINE                                          
HETNAM     HLO 1-[({2,4-BIS[(E)-(HYDROXYIMINO)METHYL]                           
HETNAM   2 HLO  PYRIDINIUM-1-YL}METHOXY)METHYL]-4-                              
HETNAM   3 HLO  CARBAMOYLPYRIDINIUM                                             
FORMUL   3  P6G    C12 H26 O7                                                   
FORMUL   4  SUN    2(C7 H17 N2 O5 P1)                                           
FORMUL   5  HLO    2(C15 H17 N5 O4)                                             
FORMUL   6  HOH   *294(H2 O1)                                                   
HELIX    1   1 VAL 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  GLY A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  ILE A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 ALA A  204  SER A  215  1                                  12    
HELIX    9   9 SER A  215  SER A  220  1                                   6    
HELIX   10  10 ALA A  241  VAL A  255  1                                  15    
HELIX   11  11 ASN A  265  ARG A  276  1                                  12    
HELIX   12  12 PRO A  277  TRP A  286  1                                  10    
HELIX   13  13 HIS A  287  LEU A  289  5                                   3    
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  ALA A  420  1                                  14    
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 ASP A  460  ASN A  464  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 ARG A  534  SER A  541  1                                   8    
HELIX   27  27 ASP B    5  GLN B    7  5                                   3    
HELIX   28  28 VAL B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  GLY B  143  1                                   9    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  ILE B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 ALA B  204  LEU B  214  1                                  11    
HELIX   36  36 SER B  215  SER B  220  1                                   6    
HELIX   37  37 ALA B  241  VAL B  255  1                                  15    
HELIX   38  38 ASN B  265  THR B  275  1                                  11    
HELIX   39  39 PRO B  277  TRP B  286  1                                  10    
HELIX   40  40 HIS B  287  LEU B  289  5                                   3    
HELIX   41  41 THR B  311  GLY B  319  1                                   9    
HELIX   42  42 GLY B  335  VAL B  340  1                                   6    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  PHE B  455  1                                   6    
HELIX   49  49 GLY B  456  ASP B  460  5                                   5    
HELIX   50  50 ASP B  460  ASN B  464  5                                   5    
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  SER B  541  1                                   8    
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  GLY A 201  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  AD 2 VAL A 239  SER A 240  0                                        
SHEET    2  AD 2 VAL A 302  VAL A 303  1  N  VAL A 303   O  VAL A 239           
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  GLY B 201  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           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555        
SSBOND   2 CYS A  257    CYS A  272                          1555   1555        
SSBOND   3 CYS A  409    CYS A  529                          1555   1555        
SSBOND   4 CYS B   69    CYS B   96                          1555   1555        
SSBOND   5 CYS B  257    CYS B  272                          1555   1555        
SSBOND   6 CYS B  409    CYS B  529                          1555   1555        
LINK         C   GLU A 202                 N   SUN A 203     1555   1555        
LINK         C   SUN A 203                 N   ALA A 204     1555   1555        
LINK         C   GLU B 202                 N   SUN B 203     1555   1555        
LINK         C   SUN B 203                 N   ALA B 204     1555   1555        
CISPEP   1 TYR A  105    PRO A  106          0        -1.36                     
CISPEP   2 TYR B  105    PRO B  106          0         7.42                     
CISPEP   3 SER B  497    PRO B  498          0       -26.56                     
SITE     1 AC1 14 TYR A  72  ASP A  74  TRP A  86  TYR A 124                    
SITE     2 AC1 14 GLU A 285  TRP A 286  ILE A 294  PHE A 295                    
SITE     3 AC1 14 PHE A 297  SER A 298  TYR A 337  PHE A 338                    
SITE     4 AC1 14 TYR A 341  HOH Z  92                                          
SITE     1 AC2 12 TYR B  72  TYR B 124  GLU B 285  TRP B 286                    
SITE     2 AC2 12 ILE B 294  PHE B 295  TYR B 337  PHE B 338                    
SITE     3 AC2 12 TYR B 341  HIS B 447  HOH Y 134  HOH Y 135                    
SITE     1 AC3 10 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC3 10 ALA B 377  LEU B 380  HIS B 381  GLN B 527                    
SITE     3 AC3 10 PHE B 531  PHE B 535                                          
CRYST1   76.920  108.940  220.320  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013001  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009179  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004539        0.00000                         
TER    4186      ALA A 542                                                      
TER    8354      ALA B 544                                                      
MASTER      401    0    5   53   36    0   10    6 8713    2  111   86          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer