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LongText Report for: 2WHQ-pdb

Name Class
2WHQ-pdb
HEADER    HYDROLASE                               06-MAY-09   2WHQ              
TITLE     CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED             
TITLE    2 BY SARIN (AGED) IN COMPLEX WITH HI-6                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: CATALYTIC SER203 PHOSPHONYLATED BY SARIN.             
COMPND   9  THE COMPLEX WAS SUBSEQUENTLY AGED                                   
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: HUMAN EMBRYONIC KIDNEY (HEK)            
SOURCE   8  293 CELLS;                                                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    HI-6, SYNAPSE, MEMBRANE, SECRETED, HYDROLASE,                         
KEYWDS   2 NEUROTRANSMITTER DEGRADATION, CHOLINESTERASE, SERINE                 
KEYWDS   3 ESTERASE, ALTERNATIVE SPLICING, CELL JUNCTION, CELL                  
KEYWDS   4 MEMBRANE, DISULFIDE BOND, AGED SARIN, GPI-ANCHOR,                    
KEYWDS   5 LIPOPROTEIN, GLYCOPROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,                     
AUTHOR   2 G.SCHNEIDER,Y.P.PANG                                                 
REVDAT   1   30-JUN-09 2WHQ    0                                                
JRNL        AUTH   F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,            
JRNL        AUTH 2 G.SCHNEIDER,Y.P.PANG                                         
JRNL        TITL   STRUCTURE OF HI-6*SARIN-ACETYLCHOLINESTERASE                 
JRNL        TITL 2 DETERMINED BY X-RAY CRYSTALLOGRAPHY AND MOLECULAR            
JRNL        TITL 3 DYNAMICS SIMULATION: REACTIVATOR MECHANISM AND               
JRNL        TITL 4 DESIGN.                                                      
JRNL        REF    PLOS ONE                      V.   4 E5957 2009              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   19536291                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0005957                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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) : 2.150                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.089                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.59                          
REMARK   3   NUMBER OF REFLECTIONS             : 110749                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1860                          
REMARK   3   R VALUE            (WORKING SET) : 0.1855                          
REMARK   3   FREE R VALUE                     : 0.2119                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  2.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2191                            
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 29.0921 -  5.4068    0.95     6856   137  0.1812 0.1964        
REMARK   3     2  5.4068 -  4.2960    1.00     6938   137  0.1349 0.1531        
REMARK   3     3  4.2960 -  3.7542    1.00     6880   134  0.1402 0.1739        
REMARK   3     4  3.7542 -  3.4115    1.00     6839   146  0.1580 0.1663        
REMARK   3     5  3.4115 -  3.1673    1.00     6831   125  0.1736 0.2072        
REMARK   3     6  3.1673 -  2.9808    1.00     6785   148  0.1769 0.1891        
REMARK   3     7  2.9808 -  2.8316    1.00     6796   137  0.1710 0.2064        
REMARK   3     8  2.8316 -  2.7085    1.00     6784   133  0.1742 0.2079        
REMARK   3     9  2.7085 -  2.6043    1.00     6741   151  0.1698 0.2257        
REMARK   3    10  2.6043 -  2.5145    1.00     6766   147  0.1778 0.2102        
REMARK   3    11  2.5145 -  2.4359    1.00     6754   115  0.1830 0.2132        
REMARK   3    12  2.4359 -  2.3663    1.00     6776   131  0.2075 0.2350        
REMARK   3    13  2.3663 -  2.3040    1.00     6720   147  0.2123 0.2668        
REMARK   3    14  2.3040 -  2.2478    1.00     6691   139  0.2268 0.2711        
REMARK   3    15  2.2478 -  2.1967    1.00     6743   141  0.2686 0.2762        
REMARK   3    16  2.1967 -  2.1500    0.99     6658   123  0.3523 0.3714        
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              : 0.361                                         
REMARK   3   B_SOL              : 70.001                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.38            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8334                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 152                                     
REMARK   3   SOLVENT ATOMS            : 650                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.8764                                              
REMARK   3    B22 (A**2) : 0.7953                                               
REMARK   3    B33 (A**2) : 0.0811                                               
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      :  0.010           8737                                  
REMARK   3   ANGLE     :  1.235          11909                                  
REMARK   3   CHIRALITY :  0.085           1280                                  
REMARK   3   PLANARITY :  0.006           1562                                  
REMARK   3   DIHEDRAL  : 18.237           3130                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0729  12.3020  16.6363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2717 T22:   0.2513                                     
REMARK   3      T33:   0.2752 T12:  -0.0071                                     
REMARK   3      T13:   0.0032 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6099 L22:   0.5173                                     
REMARK   3      L33:   1.4607 L12:  -0.1201                                     
REMARK   3      L13:   0.0894 L23:  -0.2302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0379 S12:   0.0316 S13:  -0.0027                       
REMARK   3      S21:   0.0209 S22:   0.0189 S23:   0.0022                       
REMARK   3      S31:   0.1179 S32:  -0.0715 S33:   0.0183                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5217   4.9684 -40.2912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2751 T22:   0.2859                                     
REMARK   3      T33:   0.2815 T12:  -0.0115                                     
REMARK   3      T13:  -0.0325 T23:  -0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5673 L22:   0.7957                                     
REMARK   3      L33:   1.9925 L12:  -0.0111                                     
REMARK   3      L13:   0.3331 L23:   0.4133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1026 S12:   0.0610 S13:  -0.0450                       
REMARK   3      S21:   0.0504 S22:  -0.0700 S23:   0.0669                       
REMARK   3      S31:   0.1943 S32:   0.0211 S33:  -0.0265                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN W                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.3865   9.2199  -8.1312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2948 T22:   0.2910                                     
REMARK   3      T33:   0.2849 T12:  -0.0163                                     
REMARK   3      T13:   0.0017 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1510 L22:   0.0325                                     
REMARK   3      L33:   0.3622 L12:  -0.0721                                     
REMARK   3      L13:   0.1424 L23:  -0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0135 S12:   0.0206 S13:  -0.0581                       
REMARK   3      S21:  -0.0086 S22:  -0.0096 S23:  -0.0072                       
REMARK   3      S31:   0.0979 S32:   0.0485 S33:  -0.0045                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 258-264 ARE DISORDERED           
REMARK   4                                                                      
REMARK   4 2WHQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-MAY-09.                 
REMARK 100 THE PDBE ID CODE IS EBI-39644.                                       
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) : 1.041                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110895                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.7                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.44                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.50                               
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): 4.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30 % (V/V) PEG750MME 0.1 M            
REMARK 280  HEPES 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   -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       39.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.53000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.16000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.53000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.16000            
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     ARG A 165    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 286    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3              
REMARK 470     TRP A 286    CH2                                                 
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     GLU B 268    CG   CD   OE1  OE2                                  
REMARK 470     TRP B 286    CH2                                                 
REMARK 470     TRP B 286    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3              
REMARK 470     ASP B 323    CG   OD1  OD2                                       
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: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -6.43     75.85                                   
REMARK 500    ASP A 306      -89.05   -126.27                                   
REMARK 500    VAL A 407      -59.02   -131.54                                   
REMARK 500    ARG A 493       43.21    -83.56                                   
REMARK 500    ASP A 494       73.62   -175.19                                   
REMARK 500    ARG A 525       50.50     37.28                                   
REMARK 500    PHE B  47       -5.54     69.25                                   
REMARK 500    ALA B  62       55.84   -119.62                                   
REMARK 500    ASN B 170       19.67     57.47                                   
REMARK 500    ASP B 306      -87.44   -128.67                                   
REMARK 500    VAL B 407      -59.31   -124.27                                   
REMARK 500    ASP B 494       98.54    111.10                                   
REMARK 500    SER B 495      -95.94    -69.87                                   
REMARK 500    LYS B 496      105.21     -8.48                                   
REMARK 500    SER B 497     -158.98    -55.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     HI6 B 1545                                                       
REMARK 610     HI6 A 1543                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1549                 
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: 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: 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: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-GALLAMINE COMPLEX                              
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH SUCCINYLCHOLINE                                      
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: 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: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN                        
REMARK 900  COMPLEX WITH K027                                                   
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                                                               
DBREF  2WHQ A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2WHQ A  544   548  PDB    2WHQ     2WHQ           544    548             
DBREF  2WHQ B    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2WHQ B  544   548  PDB    2WHQ     2WHQ           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 SBG 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 SBG 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 2WHQ SBG A  203  SER  O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE         
MODRES 2WHQ SBG B  203  SER  O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE         
HET    SBG  A 203      10                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 701      14                                                       
HET    SBG  B 203      10                                                       
HET    NAG  B 601      14                                                       
HET    HI6  A1543      12                                                       
HET    HI6  B1545      12                                                       
HET    P6G  A1544      19                                                       
HET    PEG  B1546       7                                                       
HET    PGE  B1547      10                                                       
HET    PGE  A1545      10                                                       
HET    PGE  B1548      10                                                       
HET    PGE  B1549      10                                                       
HETNAM     SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE                       
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]                          
HETNAM   3 HI6  PYRIDINIUM                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  SBG    2(C4 H10 N O5 P)                                             
FORMUL   4  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL   5  P6G    C12 H26 O7                                                   
FORMUL   6  PGE    4(C6 H14 O4)                                                 
FORMUL   7  NAG    3(C8 H15 N O6)                                               
FORMUL   8  PEG    C4 H10 O3                                                    
FORMUL   9  HOH   *650(H2 O1)                                                   
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 ALA A  204  SER A  215  1                                  12    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  VAL A  255  1                                  16    
HELIX   12  12 ASN A  265  ARG A  276  1                                  12    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  GLY A  342  5                                   8    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  ALA A  542  1                                   9    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 ALA B  204  LEU B  214  1                                  11    
HELIX   37  37 SER B  215  SER B  220  1                                   6    
HELIX   38  38 ALA B  241  VAL B  255  1                                  15    
HELIX   39  39 ASN B  265  ARG B  276  1                                  12    
HELIX   40  40 PRO B  277  TRP B  286  1                                  10    
HELIX   41  41 HIS B  287  LEU B  289  5                                   3    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 GLY B  335  VAL B  340  1                                   6    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  PHE B  455  1                                   6    
HELIX   50  50 GLY B  456  ASP B  460  5                                   5    
HELIX   51  51 ASP B  460  ASN B  464  5                                   5    
HELIX   52  52 THR B  466  GLY B  487  1                                  22    
HELIX   53  53 ARG B  525  ARG B  534  1                                  10    
HELIX   54  54 ARG B  534  ALA B  542  1                                   9    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  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  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  2.02  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.10  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05  
LINK         C   GLU A 202                 N   SBG A 203     1555   1555  1.33  
LINK         C   SBG A 203                 N   ALA A 204     1555   1555  1.33  
LINK         ND2 ASN A 350                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A 464                 C1  NAG A 701     1555   1555  1.44  
LINK         C   GLU B 202                 N   SBG B 203     1555   1555  1.33  
LINK         C   SBG B 203                 N   ALA B 204     1555   1555  1.34  
LINK         ND2 ASN B 350                 C1  NAG B 601     1555   1555  1.45  
CISPEP   1 TYR A  105    PRO A  106          0        -0.74                     
CISPEP   2 TYR B  105    PRO B  106          0         3.13                     
CISPEP   3 SER B  497    PRO B  498          0        -7.15                     
SITE     1 AC1  4 SER A 347  ASN A 350  HOH A2361  HOH A2362                    
SITE     1 AC2  1 ASN A 464                                                     
SITE     1 AC3  5 GLY B 345  SER B 347  ASN B 350  LEU B 353                    
SITE     2 AC3  5 HOH B2286                                                     
SITE     1 AC4  6 TRP A  86  GLY A 121  TYR A 337  HIS A 447                    
SITE     2 AC4  6 TYR A 449  HOH A2123                                          
SITE     1 AC5  8 TRP B  86  GLY B 121  TYR B 124  TYR B 337                    
SITE     2 AC5  8 TYR B 341  HIS B 447  TYR B 449  HOH B2084                    
SITE     1 AC6  9 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC6  9 HOH A2363  LEU B 380  HIS B 381  GLN B 527                    
SITE     3 AC6  9 PHE B 535                                                     
SITE     1 AC7  3 LYS B 332  ASP B 396  HOH B2190                               
SITE     1 AC8  3 HIS B 381  TYR B 382  ASP B 384                               
SITE     1 AC9  5 HIS A 381  TYR A 382  HIS A 393  THR A 528                    
SITE     2 AC9  5 HOH A2364                                                     
SITE     1 BC1  3 ASP B 304  GLY B 305  SER B 309                               
SITE     1 BC2  1 GLN B 291                                                     
CRYST1   79.550  112.320  227.060  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      0.012571  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008903  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004404        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:
ESTHER Home Page and ACEDB Home Page
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