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LongText Report for: 2WU4-pdb

Name Class
2WU4-pdb
HEADER    HYDROLASE                               28-SEP-09   2WU4              
TITLE     CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX            
TITLE    2 WITH FENAMIPHOS AND ORTHO-7                                          
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: FENAMIPHOS COVALENTLY BOUND TO SER203                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: 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;                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1                                   
KEYWDS    GLYCOPROTEIN, SERINE ESTERASE, ACETYLCHOLINESTERASE,                  
KEYWDS   2 ALTERNATIVE SPLICING, NEUROTRANSMITTER DEGRADATION,                  
KEYWDS   3 SYNAPSE, MEMBRANE, HYDROLASE, FENAMIPHOS                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM                    
REVDAT   1   20-OCT-09 2WU4    0                                                
JRNL        AUTH   A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM           
JRNL        TITL   CRYSTAL STRUCTURES OF OXIME-BOUND FENAMIPHOS-                
JRNL        TITL 2 ACETYLCHOLINESTERASES: REACTIVATION INVOLVING                
JRNL        TITL 3 FLIPPING OF THE HIS447 RING TO FORM A REACTIVE               
JRNL        TITL 4 GLU334-HIS447-OXIME TRIAD.                                   
JRNL        REF    BIOCHEM.PHARM.                             2009              
JRNL        REFN                   ESSN 1873-2968                               
JRNL        PMID   19732756                                                     
JRNL        DOI    10.1016/J.BCP.2009.08.027                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.400                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.146                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.94                          
REMARK   3   NUMBER OF REFLECTIONS             : 80602                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1866                          
REMARK   3   R VALUE            (WORKING SET) : 0.1859                          
REMARK   3   FREE R VALUE                     : 0.2232                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  2.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1595                            
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 29.1477 -  5.3277    0.99     7486   149  0.1839 0.2191        
REMARK   3     2  5.3277 -  4.2329    1.00     7312   144  0.1388 0.1623        
REMARK   3     3  4.2329 -  3.6991    1.00     7218   141  0.1552 0.1785        
REMARK   3     4  3.6991 -  3.3614    1.00     7180   138  0.1744 0.2247        
REMARK   3     5  3.3614 -  3.1208    1.00     7169   145  0.1868 0.2147        
REMARK   3     6  3.1208 -  2.9370    1.00     7106   156  0.1859 0.2303        
REMARK   3     7  2.9370 -  2.7900    1.00     7132   143  0.1887 0.2372        
REMARK   3     8  2.7900 -  2.6686    1.00     7113   145  0.1896 0.2365        
REMARK   3     9  2.6686 -  2.5660    1.00     7078   163  0.2045 0.2107        
REMARK   3    10  2.5660 -  2.4775    1.00     7105   138  0.2269 0.3044        
REMARK   3    11  2.4775 -  2.4000    1.00     7108   133  0.2735 0.3393        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.364                                         
REMARK   3   B_SOL              : 66.695                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.23            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.4565                                              
REMARK   3    B22 (A**2) : -0.1888                                              
REMARK   3    B33 (A**2) : 0.6453                                               
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      :  0.012           8631                                  
REMARK   3   ANGLE     :  1.395          11775                                  
REMARK   3   CHIRALITY :  0.089           1258                                  
REMARK   3   PLANARITY :  0.007           1547                                  
REMARK   3   DIHEDRAL  : 18.649           3058                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1707  12.7397  16.6323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2266 T22:   0.1890                                     
REMARK   3      T33:   0.2614 T12:   0.0039                                     
REMARK   3      T13:   0.0112 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8141 L22:   0.6818                                     
REMARK   3      L33:   1.6728 L12:  -0.0913                                     
REMARK   3      L13:   0.1756 L23:  -0.2661                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0808 S12:   0.0047 S13:  -0.0022                       
REMARK   3      S21:  -0.0120 S22:   0.0271 S23:   0.0014                       
REMARK   3      S31:   0.1600 S32:  -0.0102 S33:   0.0506                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8848   4.2385 -40.4488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2775 T22:   0.2856                                     
REMARK   3      T33:   0.3021 T12:  -0.0199                                     
REMARK   3      T13:  -0.0262 T23:  -0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6684 L22:   0.9373                                     
REMARK   3      L33:   1.8831 L12:  -0.0243                                     
REMARK   3      L13:   0.2334 L23:   0.5108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1435 S12:   0.0767 S13:  -0.0462                       
REMARK   3      S21:   0.1425 S22:  -0.1347 S23:   0.1078                       
REMARK   3      S31:   0.1986 S32:   0.0107 S33:  -0.0029                       
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 2WU4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-09                   
REMARK 100 THE PDBE ID CODE IS EBI-41274                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-07                          
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) : 1.04123                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80714                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.22                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
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: 28% PEG750MME, 0.1M HEPES PH7.0          
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   -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       39.87000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.34500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.34500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.87000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.35000            
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 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 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     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     SER A   497                                                      
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     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     SER B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     SER B   497                                                      
REMARK 465     LEU B   540                                                      
REMARK 465     SER B   541                                                      
REMARK 465     ALA B   542                                                      
REMARK 465     THR B   543                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
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, 1999                                
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 458   C   -  N   -  CA  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    PRO B 108   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 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       -8.07     72.69                                   
REMARK 500    PRO A  49      150.05    -45.37                                   
REMARK 500    ALA A  62       51.78   -119.30                                   
REMARK 500    ASN A  67      150.43    -46.68                                   
REMARK 500    PHE A 158       -7.11   -141.83                                   
REMARK 500    ALA A 167       69.19   -153.20                                   
REMARK 500    PRO A 290      124.24    -39.52                                   
REMARK 500    ILE A 294       31.35    -77.09                                   
REMARK 500    ASP A 306      -90.13   -129.99                                   
REMARK 500    TYR A 341       53.43    -98.12                                   
REMARK 500    SER A 371     -178.90    -66.18                                   
REMARK 500    VAL A 407      -60.62   -129.09                                   
REMARK 500    PHE B  47       -3.54     73.62                                   
REMARK 500    ALA B  62       55.85   -119.25                                   
REMARK 500    SER B  93      142.34   -176.02                                   
REMARK 500    CYS B  96       10.75   -144.12                                   
REMARK 500    PRO B 108      140.07    -21.78                                   
REMARK 500    ALA B 127      144.85   -174.55                                   
REMARK 500    ALA B 167       66.36   -150.25                                   
REMARK 500    SER B 293     -143.37   -124.91                                   
REMARK 500    ASP B 306      -82.00   -115.80                                   
REMARK 500    TYR B 341       57.90   -101.32                                   
REMARK 500    VAL B 407      -64.31   -123.16                                   
REMARK 500    ASN B 514     -167.58   -166.08                                   
REMARK 500    LEU B 518      127.68    -39.09                                   
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 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO] PHOSPHORYL}-L-SERINE             
REMARK 600  (SXE): MODIFIED SER203                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HBP A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HBP B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED VX                                           
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,                          
REMARK 900  PHOSPHONYLATED BY SARIN (AGED) IN COMPLEX                           
REMARK 900  WITH HI-6                                                           
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
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: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
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: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED SARIN                                        
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED VX AND SARIN                                     
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6ANTI COMPLEX                             
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED DIISOPROPYL FLUOROPHOSPHATE                      
REMARK 900   (DFP)                                                              
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED METHAMIDOPHOS                                
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX                              
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS                                   
REMARK 900  ACETYLCHOLINESTERASE IN COMPLEX WITH AMTS13                         
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH CHOLINE                                              
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                          
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH HLO-7                                                          
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED DIISOPROPYL                                  
REMARK 900  FLUOROPHOSPHATE (DFP)                                               
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-PROPIDIUM COMPLEX                              
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED METHAMIDOPHOS                                    
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN THE APOFORM                                                     
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: 2C0P   RELATED DB: PDB                                   
REMARK 900  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: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN                        
REMARK 900  COMPLEX WITH K027                                                   
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-GALLAMINE COMPLEX                              
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: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH SUCCINYLCHOLINE                                      
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,                          
REMARK 900  PHOSPHONYLATED BY SARIN AND IN COMPLEX WITH                         
REMARK 900   HI-6                                                               
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH TABUN AND HLO-7                                                
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED FENAMIPHOS                                       
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
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: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-DECIDIUM COMPLEX                               
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED FENAMIPHOS                                   
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: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN COMPLEX WITH FENAMIPHOS AND HI-6                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 STRUCTURE STARTS AT RESIDUE 32 AND ENDS AT RESIDUE 574               
DBREF  2WU4 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2WU4 A  544   548  PDB    2WU4     2WU4           544    548             
DBREF  2WU4 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2WU4 B  544   548  PDB    2WU4     2WU4           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 SXE 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 SXE 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 2WU4 SXE A  203  SER  MODIFIED SERINE                                    
MODRES 2WU4 SXE B  203  SER  MODIFIED SERINE                                    
HET    SXE  A 203      30                                                       
HET    SXE  B 203      20                                                       
HET    HBP  A1544      25                                                       
HET    HBP  B1545      25                                                       
HET    P6G  A1545      19                                                       
HET    NAG  A1543      14                                                       
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     HBP 1,7-HEPTYLENE-BIS-N,N'-SYN-2-                                    
HETNAM   2 HBP  PYRIDINIUMALDOXIME                                              
HETNAM     SXE O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO]                              
HETNAM   2 SXE  PHOSPHORYL}-L-SERINE                                            
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     NAG NAG                                                              
FORMUL   3  P6G    C12 H26 O7                                                   
FORMUL   4  HBP    2(C19 H26 N4 O2 2+)                                          
FORMUL   5  SXE    2(C8 H19 N2 O5 P)                                            
FORMUL   6  NAG    C8 H15 N O6                                                  
FORMUL   7  HOH   *325(H2 O)                                                    
HELIX    1   1 ASP A    5  LEU A    9  5                                   5    
HELIX    2   2 THR A   83  ASN A   87  5                                   5    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 ARG A  136  GLU A  142  1                                   7    
HELIX    5   5 LEU A  173  ILE A  187  1                                  15    
HELIX    6   6 ALA A  188  PHE A  190  5                                   3    
HELIX    7   7 SER A  215  SER A  220  1                                   6    
HELIX    8   8 GLU A  243  VAL A  255  1                                  13    
HELIX    9   9 ASN A  265  THR A  275  1                                  11    
HELIX   10  10 PRO A  277  TRP A  286  1                                  10    
HELIX   11  11 HIS A  287  LEU A  289  5                                   3    
HELIX   12  12 THR A  311  THR A  318  1                                   8    
HELIX   13  13 SER A  336  TYR A  341  5                                   6    
HELIX   14  14 SER A  355  ALA A  361  1                                   7    
HELIX   15  15 SER A  371  THR A  383  1                                  13    
HELIX   16  16 ASP A  390  VAL A  402  1                                  13    
HELIX   17  17 VAL A  407  ALA A  415  1                                   9    
HELIX   18  18 GLU A  450  PHE A  455  1                                   6    
HELIX   19  19 ASP A  460  ASN A  464  5                                   5    
HELIX   20  20 THR A  466  THR A  486  1                                  21    
HELIX   21  21 ARG A  525  ARG A  534  1                                  10    
HELIX   22  22 ARG A  534  ALA A  542  1                                   9    
HELIX   23  23 ASP B    5  LEU B    9  5                                   5    
HELIX   24  24 THR B   83  ASN B   87  5                                   5    
HELIX   25  25 LEU B  130  ASP B  134  5                                   5    
HELIX   26  26 ARG B  136  GLU B  142  1                                   7    
HELIX   27  27 LEU B  173  ILE B  187  1                                  15    
HELIX   28  28 ALA B  188  PHE B  190  5                                   3    
HELIX   29  29 SER B  215  SER B  220  1                                   6    
HELIX   30  30 GLU B  243  VAL B  255  1                                  13    
HELIX   31  31 ASN B  265  THR B  275  1                                  11    
HELIX   32  32 PRO B  277  TRP B  286  1                                  10    
HELIX   33  33 HIS B  287  LEU B  289  5                                   3    
HELIX   34  34 THR B  311  THR B  318  1                                   8    
HELIX   35  35 SER B  355  ALA B  361  1                                   7    
HELIX   36  36 SER B  371  THR B  383  1                                  13    
HELIX   37  37 ASP B  390  VAL B  402  1                                  13    
HELIX   38  38 VAL B  407  ALA B  415  1                                   9    
HELIX   39  39 GLU B  450  PHE B  455  1                                   6    
HELIX   40  40 ASP B  460  ASN B  464  5                                   5    
HELIX   41  41 THR B  466  THR B  486  1                                  21    
HELIX   42  42 ARG B  525  ARG B  534  1                                  10    
HELIX   43  43 ARG B  534  LEU B  539  1                                   6    
SHEET    1  AA 2 LEU A  17  ARG A  18  0                                        
SHEET    2  AA 2 LEU A  60  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ARG A  21  LEU A  22  0                                        
SHEET    2  AB11 VAL A  29  PHE A  32 -1  O  VAL A  29   N  LEU A  22           
SHEET    3  AB11 LEU A  99  PRO A 104 -1  O  VAL A 101   N  PHE A  32           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 VAL A 114  TRP A 117  1  O  LEU A 115   N  VAL A 147           
SHEET    6  AB11 VAL A 197  PHE A 200  1  O  THR A 198   N  ILE A 116           
SHEET    7  AB11 ARG A 224  VAL A 226  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 TYR A 510  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 521 -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 2 LEU B  17  ARG B  18  0                                        
SHEET    2  BA 2 LEU B  60  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ARG B  21  LEU B  22  0                                        
SHEET    2  BB11 VAL B  29  PHE B  32 -1  O  VAL B  29   N  LEU B  22           
SHEET    3  BB11 LEU B  99  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 VAL B 114  TRP B 117  1  O  LEU B 115   N  VAL B 147           
SHEET    6  BB11 VAL B 197  PHE B 200  1  O  THR B 198   N  ILE B 116           
SHEET    7  BB11 ARG B 224  VAL B 226  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 TYR B 510  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 521 -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  2.08  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.08  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.06  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.11  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05  
LINK         C   GLU A 202                 N  ASXE A 203     1555   1555  1.34  
LINK         C   GLU A 202                 N  BSXE A 203     1555   1555  1.34  
LINK         C  ASXE A 203                 N   ALA A 204     1555   1555  1.34  
LINK         C  BSXE A 203                 N   ALA A 204     1555   1555  1.34  
LINK         ND2 ASN A 350                 C1  NAG A1543     1555   1555  1.48  
LINK         C   GLU B 202                 N  BSXE B 203     1555   1555  1.34  
LINK         C   GLU B 202                 N  ASXE B 203     1555   1555  1.34  
LINK         C  BSXE B 203                 N   ALA B 204     1555   1555  1.34  
LINK         C  ASXE B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0        -6.62                     
CISPEP   2 TYR B  105    PRO B  106          0         2.90                     
SITE     1 AC1 13 TYR A  72  TRP A  86  TYR A 124  SXE A 203                    
SITE     2 AC1 13 GLU A 285  TRP A 286  ILE A 294  PHE A 297                    
SITE     3 AC1 13 TYR A 337  PHE A 338  TYR A 341  HIS A 447                    
SITE     4 AC1 13 HOH A2140                                                     
SITE     1 AC2 10 TYR B  72  TRP B  86  TYR B 124  GLU B 285                    
SITE     2 AC2 10 TRP B 286  ILE B 294  TYR B 337  PHE B 338                    
SITE     3 AC2 10 TYR B 341  HIS B 447                                          
SITE     1 AC3  7 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC3  7 ALA B 377  LEU B 380  HIS B 381                               
SITE     1 AC4  4 SER A 347  ASN A 350  LEU A 353  HOH A2192                    
CRYST1   79.740  112.700  226.690  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      0.012541  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004411        0.00000                         
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:
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