Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3DL7-pdb

Name Class
3DL7-pdb
HEADER    HYDROLASE                               26-JUN-08   3DL7              
TITLE     AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN-           
TITLE    2 UPDATE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-576;                                       
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HEK293F;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    HYDROLASE, TABUN, ORGANOPHOSPHATE, AGING, ALTERNATIVE                 
KEYWDS   2 SPLICING, CELL JUNCTION, GLYCOPROTEIN, GPI-ANCHOR,                   
KEYWDS   3 LIPOPROTEIN, MEMBRANE, NEUROTRANSMITTER DEGRADATION,                 
KEYWDS   4 SECRETED, SERINE ESTERASE, SYNAPSE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CARLETTI,H.LI,B.LI,F.EKSTROM,Y.NICOLET,M.LOIODICE,                  
AUTHOR   2 E.GILLON,M.T.FROMENT,O.LOCKRIDGE,L.M.SCHOPFER,P.MASSON,              
AUTHOR   3 F.NACHON                                                             
REVDAT   1   02-DEC-08 3DL7    0                                                
JRNL        AUTH   E.CARLETTI,H.LI,B.LI,F.EKSTROM,Y.NICOLET,                    
JRNL        AUTH 2 M.LOIODICE,E.GILLON,M.T.FROMENT,O.LOCKRIDGE,                 
JRNL        AUTH 3 L.M.SCHOPFER,P.MASSON,F.NACHON                               
JRNL        TITL   AGING OF CHOLINESTERASES PHOSPHYLATED BY TABUN               
JRNL        TITL 2 PROCEEDS THROUGH O-DEALKYLATION.                             
JRNL        REF    J.AM.CHEM.SOC.                V. 130 16011 2008              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   18975951                                                     
JRNL        DOI    10.1021/JA804941Z                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 69037                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1381                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4887                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 8926                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.249         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.208         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.892         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8735 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11943 ; 1.461 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1078 ; 6.473 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   402 ;33.485 ;22.761       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1268 ;17.585 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    75 ;20.097 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1281 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6867 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4609 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6024 ; 0.315 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   591 ; 0.147 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.204 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5461 ; 0.776 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8661 ; 1.355 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3713 ; 1.792 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3277 ; 2.901 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DL7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048176.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9694                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69074                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 7.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (V/V) PEG750MME, 0.1M            
REMARK 280  HEPES, 100 MM HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 277K                                                    
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       39.51000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.19000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.44000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.19000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.51000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.44000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   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     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     LYS B   496                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     SER B 497    OG                                                  
REMARK 470     ALA B 544    CA   C    O    CB                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. = -15.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -9.01     75.37                                   
REMARK 500    PRO A 104      163.07    -49.27                                   
REMARK 500    ALA A 127      140.37   -172.51                                   
REMARK 500    PHE A 158       -5.05   -140.89                                   
REMARK 500    ASN A 170       17.62     55.83                                   
REMARK 500    ASP A 306      -88.94   -130.91                                   
REMARK 500    SER A 371     -174.77    -60.83                                   
REMARK 500    VAL A 407      -65.73   -129.74                                   
REMARK 500    ASN A 464       10.98     82.23                                   
REMARK 500    ASP A 494      120.54    169.69                                   
REMARK 500    SER A 541      -86.14    -60.80                                   
REMARK 500    ALA A 542       51.58    -69.10                                   
REMARK 500    PHE B  47       -2.59     71.19                                   
REMARK 500    ALA B  62       58.34   -115.87                                   
REMARK 500    PRO B 111      117.56    -37.81                                   
REMARK 500    ALA B 167       68.45   -150.51                                   
REMARK 500    ASP B 306      -78.60   -123.24                                   
REMARK 500    ASP B 323       53.54   -103.45                                   
REMARK 500    TYR B 341       34.29    -95.21                                   
REMARK 500    ASN B 350     -129.38   -104.35                                   
REMARK 500    LEU B 353       92.62    -67.19                                   
REMARK 500    VAL B 407      -62.46   -123.02                                   
REMARK 500    GLN B 421       32.17    -99.97                                   
REMARK 500    PRO B 492       57.61   -114.71                                   
REMARK 500    ASP B 494     -155.95    -78.27                                   
REMARK 500    ASN B 514     -169.11   -161.52                                   
REMARK 500    SER B 541       24.07    -69.10                                   
REMARK 500    THR B 543       86.45     35.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 704        DISTANCE =  5.62 ANGSTROMS                       
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 549                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 550                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 551                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 549                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN           
REMARK 900 - SAME DATASET WITH OLDER REFINEMENT.                                
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY             
REMARK 900 TABUN - OLDER REFINEMENT                                             
REMARK 900 RELATED ID: 3DKK   RELATED DB: PDB                                   
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN.         
REMARK 900 RELATED ID: 3DJY   RELATED DB: PDB                                   
REMARK 900 NON-AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900 TABUN.                                                               
REMARK 900 RELATED ID: 3DL4   RELATED DB: PDB                                   
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY             
REMARK 900 TABUN.                                                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE C-TERMINAL PART WAS ENGINEERED TO GET MONOMERIC ENZYME.          
DBREF  3DL7 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  3DL7 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 3DL7 SEN A  203  UNP  P21836    SER   234 MICROHETEROGENEITY             
SEQADV 3DL7 SUN A  203  UNP  P21836    SER   234 MICROHETEROGENEITY             
SEQADV 3DL7 ALA A  544  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 THR A  545  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 GLU A  546  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 ALA A  547  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 PRO A  548  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 SEN B  203  UNP  P21836    SER   234 MICROHETEROGENEITY             
SEQADV 3DL7 SUN B  203  UNP  P21836    SER   234 MICROHETEROGENEITY             
SEQADV 3DL7 ALA B  544  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 THR B  545  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 GLU B  546  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 ALA B  547  UNP  P21836              SEE REMARK 999                 
SEQADV 3DL7 PRO B  548  UNP  P21836              SEE REMARK 999                 
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 SEN 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 SEN 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 3DL7 ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 3DL7 SEN A  203  SER                                                     
MODRES 3DL7 SUN A  203  SER                                                     
MODRES 3DL7 SEN B  203  SER                                                     
MODRES 3DL7 SUN B  203  SER                                                     
HET    SEN  A 203      12                                                       
HET    SUN  A 203      14                                                       
HET    SEN  B 203      12                                                       
HET    SUN  B 203      14                                                       
HET    NAG  A 549      14                                                       
HET     CL  A 550       1                                                       
HET    P6G  A 551      19                                                       
HET    PG4  B 549      13                                                       
HETNAM     SEN O-[N,N-DIMETHYLPHOSPHORAMIDATE]-L-SERINE                         
HETNAM     SUN O-[(R)-(DIMETHYLAMINO)(ETHOXY)PHOSPHORYL]-L-SERINE               
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CL CHLORIDE ION                                                     
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     SUN TABUN CONJUGATED SERINE                                          
HETSYN     NAG NAG                                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   1  SEN    2(C5 H13 N2 O5 P)                                            
FORMUL   1  SUN    2(C7 H17 N2 O5 P)                                            
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  P6G    C12 H26 O7                                                   
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL   7  HOH   *439(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 SEN A  203  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 ALA A  241  VAL A  255  1                                  15    
HELIX   12  12 ASN A  265  THR A  275  1                                  11    
HELIX   13  13 PRO A  277  TRP A  286  1                                  10    
HELIX   14  14 HIS A  287  LEU A  289  5                                   3    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  343  1                                   9    
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  ASN A  464  5                                   9    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 ARG A  534  ALA A  542  1                                   9    
HELIX   27  27 VAL B   42  ARG B   46  5                                   5    
HELIX   28  28 PHE B   80  MET B   85  1                                   6    
HELIX   29  29 LEU B  130  ASP B  134  5                                   5    
HELIX   30  30 GLY B  135  GLY B  143  1                                   9    
HELIX   31  31 VAL B  153  LEU B  159  1                                   7    
HELIX   32  32 ASN B  170  ILE B  187  1                                  18    
HELIX   33  33 ALA B  188  PHE B  190  5                                   3    
HELIX   34  34 SEN B  203  LEU B  214  1                                  12    
HELIX   35  35 SER B  215  SER B  220  1                                   6    
HELIX   36  36 ALA B  241  VAL B  255  1                                  15    
HELIX   37  37 ASN B  265  THR B  275  1                                  11    
HELIX   38  38 PRO B  277  GLU B  285  1                                   9    
HELIX   39  39 TRP B  286  VAL B  288  5                                   3    
HELIX   40  40 THR B  311  GLY B  319  1                                   9    
HELIX   41  41 GLY B  335  VAL B  340  1                                   6    
HELIX   42  42 SER B  355  VAL B  367  1                                  13    
HELIX   43  43 SER B  371  THR B  383  1                                  13    
HELIX   44  44 ASP B  390  VAL B  407  1                                  18    
HELIX   45  45 VAL B  407  GLN B  421  1                                  15    
HELIX   46  46 PRO B  440  GLY B  444  5                                   5    
HELIX   47  47 GLU B  450  GLY B  456  1                                   7    
HELIX   48  48 LEU B  457  ASN B  464  5                                   8    
HELIX   49  49 THR B  466  GLY B  487  1                                  22    
HELIX   50  50 ARG B  525  ARG B  534  1                                  10    
HELIX   51  51 ARG B  534  SER B  541  1                                   8    
SHEET    1   A 3 LEU A   9  VAL A  12  0                                        
SHEET    2   A 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3   A 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  GLN A  16           
SHEET    1   B11 ILE A  20  ALA A  24  0                                        
SHEET    2   B11 GLY A  27  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3   B11 TYR A  98  PRO A 104 -1  O  VAL A 101   N  PHE A  32           
SHEET    4   B11 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5   B11 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 145           
SHEET    6   B11 GLY A 192  GLU A 202  1  O  SER A 196   N  VAL A 114           
SHEET    7   B11 ARG A 224  GLN A 228  1  O  VAL A 226   N  LEU A 199           
SHEET    8   B11 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9   B11 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10   B11 GLN A 509  LEU A 513  1  O  LEU A 513   N  ILE A 429           
SHEET   11   B11 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1   C 2 VAL A  68  CYS A  69  0                                        
SHEET    2   C 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1   D 2 VAL A 239  SER A 240  0                                        
SHEET    2   D 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1   E 3 LEU B   9  VAL B  12  0                                        
SHEET    2   E 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3   E 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  GLN B  16           
SHEET    1   F11 ILE B  20  ALA B  24  0                                        
SHEET    2   F11 GLY B  27  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3   F11 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4   F11 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5   F11 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6   F11 GLY B 192  GLU B 202  1  O  SER B 196   N  VAL B 114           
SHEET    7   F11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8   F11 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9   F11 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10   F11 GLN B 509  LEU B 513  1  O  LEU B 513   N  ILE B 429           
SHEET   11   F11 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1   G 2 VAL B  68  CYS B  69  0                                        
SHEET    2   G 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1   H 2 VAL B 239  SER B 240  0                                        
SHEET    2   H 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  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  2.12  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.07  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.11  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.11  
LINK         C   GLU A 202                 N  ASEN A 203     1555   1555  1.33  
LINK         C   GLU A 202                 N  BSUN A 203     1555   1555  1.33  
LINK         C  ASEN A 203                 N   ALA A 204     1555   1555  1.34  
LINK         C  BSUN A 203                 N   ALA A 204     1555   1555  1.34  
LINK         C   GLU B 202                 N  ASEN B 203     1555   1555  1.34  
LINK         C   GLU B 202                 N  BSUN B 203     1555   1555  1.34  
LINK         C  ASEN B 203                 N   ALA B 204     1555   1555  1.34  
LINK         C  BSUN B 203                 N   ALA B 204     1555   1555  1.34  
LINK         ND2 ASN A 464                 C1  NAG A 549     1555   1555  1.46  
LINK         C   GLU A 202                 N  BSEN A 203     1555   1555  1.33  
LINK         C  BSEN A 203                 N   ALA A 204     1555   1555  1.34  
LINK         C   GLU B 202                 N  BSEN B 203     1555   1555  1.34  
LINK         C  BSEN B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0        -0.85                     
CISPEP   2 TYR B  105    PRO B  106          0         3.97                     
CISPEP   3 PRO B  492    ARG B  493          0        26.78                     
CISPEP   4 ARG B  493    ASP B  494          0        18.61                     
SITE     1 AC1  2 SER A 462  ASN A 464                                          
SITE     1 AC2  2 ILE A 429  ARG A 525                                          
SITE     1 AC3  8 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC3  8 LEU B 380  HIS B 381  GLN B 527  PHE B 535                    
SITE     1 AC4  3 HIS B 381  TYR B 382  HIS B 393                               
CRYST1   79.020  110.880  226.380  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      0.012655  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009019  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004417        0.00000                         
TER    4230      THR A 543                                                      
TER    8442      ALA B 544                                                      
MASTER      378    0    8   51   36    0    5    6 8926    2  111   86          
END                                                                             

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

Acknowledgements and disclaimer