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LongText Report for: 2y2u-pdb

Name Class
2y2u-pdb
HEADER    HYDROLASE                               16-DEC-10   2Y2U              
TITLE     NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY VX-UPDATE     
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 VX                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F                                 
KEYWDS    HYDROLASE, CHOLINESTERASE, METHYLPHOSPHONATE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.AKFUR,E.ARTURSSON,F.EKSTROM                                         
REVDAT   1   30-NOV-11 2Y2U    0                                                
SPRSDE     30-NOV-11 2Y2U      2JGH                                             
JRNL        AUTH   C.AKFUR,E.ARTURSSON,F.EKSTROM                                
JRNL        TITL   METHYLPHOSPHONATE ADDUCTS OF ACETYLCHOLINESTERASE            
JRNL        TITL 2 INVESTIGATED BY TIME CORRELATED SINGLE PHOTON COUNTING AND   
JRNL        TITL 3 X-RAY CRYSTALLOGRAPHY                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.762                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.76                          
REMARK   3   NUMBER OF REFLECTIONS             : 61709                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1887                          
REMARK   3   R VALUE            (WORKING SET) : 0.1878                          
REMARK   3   FREE R VALUE                     : 0.2372                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1234                            
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 28.7638 -  5.3976    0.99     7022   138  0.1796 0.2293        
REMARK   3     2  5.3976 -  4.2888    1.00     6805   135  0.1514 0.1852        
REMARK   3     3  4.2888 -  3.7480    0.99     6707   127  0.1565 0.2108        
REMARK   3     4  3.7480 -  3.4059    1.00     6680   146  0.1954 0.2310        
REMARK   3     5  3.4059 -  3.1621    1.00     6659   112  0.2098 0.2735        
REMARK   3     6  3.1621 -  2.9759    1.00     6690   159  0.2216 0.2681        
REMARK   3     7  2.9759 -  2.8270    1.00     6627   132  0.2508 0.3105        
REMARK   3     8  2.8270 -  2.7040    1.00     6666   137  0.2719 0.3563        
REMARK   3     9  2.7040 -  2.6000    1.00     6619   148  0.2548 0.3064        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.346                                         
REMARK   3   B_SOL              : 63.076                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.73             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.16            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.0027                                               
REMARK   3    B22 (A**2) : 0.4209                                               
REMARK   3    B33 (A**2) : -3.4236                                              
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      :  0.008           8747                                  
REMARK   3   ANGLE     :  1.206          11936                                  
REMARK   3   CHIRALITY :  0.084           1282                                  
REMARK   3   PLANARITY :  0.006           1564                                  
REMARK   3   DIHEDRAL  : 16.502           3170                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Y2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-46647.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
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) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
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   : 61880                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.03                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.7                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.3                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.70                               
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   (%): 48.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% (V/V) PEG 750MME, 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       39.45700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.58900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.18400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.58900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.45700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.18400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   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   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 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     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA A 544    CA   C    O    CB                                   
REMARK 470     ARG B  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 496    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A     3     O    HOH A  2006              2.00            
REMARK 500   NH1  ARG A   177     O    HOH A  2088              2.02            
REMARK 500   O    ALA A   419     O    HOH A  2176              2.19            
REMARK 500   NH1  ARG B   177     O    HOH B  2066              2.06            
REMARK 500   OD2  ASP B   390     ND1A HIS B   393              2.17            
REMARK 500   O    HOH A  2076     O    HOH A  2193              2.14            
REMARK 500   O    HOH B  2042     O    HOH B  2086              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  37      -23.58     60.17                                   
REMARK 500    PHE A  47       -7.44     74.82                                   
REMARK 500    CYS A  96       -1.31   -145.83                                   
REMARK 500    PRO A 108      152.13    -46.84                                   
REMARK 500    ALA A 167       63.73   -155.05                                   
REMARK 500    ASN A 170       13.77     55.53                                   
REMARK 500    SVX A 203     -110.34     57.97                                   
REMARK 500    ASP A 306      -85.92   -127.04                                   
REMARK 500    HIS A 387       57.54   -151.65                                   
REMARK 500    VAL A 407      -69.56   -122.76                                   
REMARK 500    SER A 462        7.36    -65.97                                   
REMARK 500    ARG A 493      -73.91    -55.99                                   
REMARK 500    LYS A 496      108.71     66.39                                   
REMARK 500    PRO A 498     -158.62    -81.99                                   
REMARK 500    ARG A 525       55.50     28.05                                   
REMARK 500    PHE B  47       -2.35     74.24                                   
REMARK 500    ALA B  62       56.89   -115.42                                   
REMARK 500    SER B  93      146.71   -176.35                                   
REMARK 500    PRO B 108      132.12    -33.20                                   
REMARK 500    ALA B 167       72.92   -158.51                                   
REMARK 500    SVX B 203     -115.63     55.64                                   
REMARK 500    ASP B 306      -86.69   -116.81                                   
REMARK 500    GLU B 351       -8.87    -56.85                                   
REMARK 500    VAL B 407      -66.95   -122.72                                   
REMARK 500    ASN B 464       41.29     74.25                                   
REMARK 500    SER B 495      -43.34   -131.75                                   
REMARK 500    ALA B 506      -70.60    -64.22                                   
REMARK 500    ASN B 514     -163.57   -161.31                                   
REMARK 500    SER B 541       63.95    -68.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A  37        21.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 RESIDUE SVX REPRESENTS THE CATALYTIC SER 203 PHOSPHONYLATED BY SVX.  
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     PEG A 1547                                                       
REMARK 610     P33 B 1545                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P33 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 350 RESIDUES  601 TO  601                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 464 RESIDUES  701 TO  701                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 601 BOUND TO ASN B 350                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN (AGED) IN COMPLEX WITH HI-6                                  
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  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 SUCCINYLCHOLINE            
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED SARIN                                                   
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY            
REMARK 900   TABUN                                                              
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED VX AND SARIN                                                
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 WK)                                                               
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6ANTI COMPLEX                                                  
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE                      
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                           
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   MTH)                                                               
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6SYN COMPLEX                                                   
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED METHAMIDOPHOS                                           
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN           
REMARK 900   COMPLEX WITH AMTS13                                                
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 SYN INHIBITOR                                   
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (               
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH CHOLINE                                               
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                           
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 MTH)                                                              
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND HI-6                                           
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7             
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                       
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  PROPIDIUM COMPLEX                                                   
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED METHAMIDOPHOS                                               
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE              
REMARK 900  APOFORM                                                             
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND ORTHO-7                                                         
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY                
REMARK 900  TABUN                                                               
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX                  
REMARK 900  WITH SOAKED TZ2PA6 ANTI INHIBITOR                                   
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   WK)                                                                
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH           
REMARK 900   K027                                                               
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 ACETYLCHOLINESTERASE-                
REMARK 900  GALLAMINE COMPLEX                                                   
REMARK 900 RELATED ID: 2XUQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS                             
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: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN AND IN COMPLEX WITH HI-6                                     
REMARK 900 RELATED ID: 4A23   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC           
REMARK 900   C5685                                                              
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND HLO-7                                                           
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  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 ACETYLCHOLINE              
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  DECIDIUM COMPLEX                                                    
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  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 BUTYRYLTHIOCHOLINE         
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND ORTHO-7                                        
REMARK 900 RELATED ID: 2Y2V   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY             
REMARK 900  SARIN-UPDATE                                                        
REMARK 900 RELATED ID: 4A16   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH                
REMARK 900  HUPRINE DERIVATIVE                                                  
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
DBREF  2Y2U A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2Y2U B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 2Y2U ALA A  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U THR A  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U ALA B  544  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U THR B  545  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 2Y2U PRO B  548  UNP  P21836              EXPRESSION TAG                 
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 SVX 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 SVX 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 2Y2U SVX A  203  SER  MODIFIED SERINE                                    
MODRES 2Y2U SVX B  203  SER  MODIFIED SERINE                                    
HET    SVX  A 203      12                                                       
HET    SVX  B 203      12                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 701      14                                                       
HET    PEG  A1545       7                                                       
HET    PEG  A1546       7                                                       
HET    PEG  A1547       5                                                       
HET    NAG  B 601      14                                                       
HET    PEG  B1543       7                                                       
HET    PEG  B1544       7                                                       
HET    P33  B1545      20                                                       
HETNAM     SVX O-[(R)-ETHOXY(METHYL)PHOSPHORYL]-L-SERINE                        
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL                          
HETSYN     P33 HEPTAETHYLENE GLYCOL, PEG330                                     
FORMUL   1  SVX    2(C6 H14 N O5 P)                                             
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   3  PEG    5(C4 H10 O3)                                                 
FORMUL   4  P33    C14 H30 O8                                                   
FORMUL   5  HOH   *357(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SVX A  203  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  GLY A  256  1                                  17    
HELIX   12  12 ASN A  265  ARG A  274  1                                  10    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  THR A  318  1                                   8    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  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  GLU B  142  1                                   8    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 SVX B  203  LEU B  214  1                                  12    
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  274  1                                  10    
HELIX   40  40 PRO B  277  HIS B  284  1                                   8    
HELIX   41  41 GLU B  285  VAL B  288  5                                   4    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 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  GLY B  456  1                                   7    
HELIX   50  50 LEU B  457  ASN B  464  5                                   8    
HELIX   51  51 THR B  466  GLY B  487  1                                  22    
HELIX   52  52 ARG B  525  ARG B  534  1                                  10    
HELIX   53  53 ARG B  534  SER B  541  1                                   8    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  ILE A  35 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 LEU A  99  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
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  2.05  
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  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.08  
LINK         N   SVX A 203                 C   GLU A 202     1555   1555  1.34  
LINK         C   SVX A 203                 N   ALA A 204     1555   1555  1.33  
LINK         ND2 ASN A 350                 C1  NAG A 601     1555   1555  1.45  
LINK         ND2 ASN A 464                 C1  NAG A 701     1555   1555  1.45  
LINK         C   SVX B 203                 N   ALA B 204     1555   1555  1.33  
LINK         N   SVX B 203                 C   GLU B 202     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         3.36                     
CISPEP   2 SER A  497    PRO A  498          0        -2.96                     
CISPEP   3 TYR B  105    PRO B  106          0         8.53                     
SITE     1 AC1  2 ASP A 304  GLY A 305                                          
SITE     1 AC2  4 HIS A 381  TYR A 382  THR A 383  HOH A2169                    
SITE     1 AC3  2 TYR A 124  HOH A2207                                          
SITE     1 AC4  3 HIS B 381  HIS B 393  HOH B2148                               
SITE     1 AC5  1 SER B 309                                                     
SITE     1 AC6  9 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC6  9 LEU B 380  HIS B 381  GLN B 527  PHE B 535                    
SITE     3 AC6  9 HOH B2144                                                     
SITE     1 AC7  4 GLY A 345  SER A 347  ASN A 350  HOH A2205                    
SITE     1 AC8  1 ASN A 464                                                     
SITE     1 AC9  5 GLY B 345  ASN B 350  LEU B 353  HOH B2146                    
SITE     2 AC9  5 HOH B2147                                                     
CRYST1   78.914  110.368  227.178  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      0.012672  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009061  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004402        0.00000                         
TER    4212      ALA A 544                                                      
TER    8395      ALA B 542                                                      
MASTER      536    0   11   53   34    0   12    6 8845    2  138   86          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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