SQLite format 3 @ D
-& t WkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_2MOLECULE_PROPERTY_DICTIONARY WkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_1MOLECULE_PROPERTY_DICTIONARYxGtableOBJECTSOBJECTSCREATE TABLE OBJECTS(OBJECTID INTEGER PRIMARY KEY, TYPE, FORMAT TEXT, DATA BLOB, SMILES TEXT)zStableMODELMODELCREATE TABLE MODEL(MODELID INTEGER PRIMARY KEY,CATCHALL BLOB,OFFLINEABLEHIERARCHY BLOB,FORMAT TEXT);++-tableINCOMPATIBILITYINCOMPATIBILITYCREATE TABLE INCOMPATIBILITY (TARGET_VERSION, SOURCE_VERSION, CONSTRAINT TARGET_SOURCE UNIQUE (TARGET_VERSION, SOURCE_VERSION) ON CONFLICT FAIL)=Q+ indexsqlite_autoindex_INCOMPATIBILITY_1INCOMPATIBILITY :ItableDOCUMENTDOCUMENTCREATE TABLE DO
4.0
3.04.0
3.03.6 DSX
3.0TEST
3.0TEST3.04.03.03.6 DSX
attached noitceleS deggaT segrahCetaluclaCotuA dekcoLytilibisiV dsx
vS4vaE*pS5 o M " 5 Hydrogen Bond EnergyC34! + Improper EnergyC33 ' CHARMm EnergyC32 5 Initial RMS GradientC31 ) ForcefieldFFMLC30 ) ForcefieldBaseC29 ! ForcefieldC28 ) ChiRotor E-vdwC27 - ChiRotor E-totalC26 + ChiRotor E-elecC25 ' ChiRotor RMSDC24$ = UseResidueTemplateChargeC23 3 PartialChargeMethodC22 SEQRESC21 REMARK99C20 ! ResolutionC19 LoopListC18 ' __PDBSeqres__C17 ) __PDBRemarks__C16 TaggedC15 / Calculate ChargesC14
1 Net Partial ChargeC13 / Net Formal ChargeC12 / Exact Mol. WeightC11
- Molecular WeightC10 - Molecular VolumeC9 / Molecular FormulaC8! 7 Molecular CompositionC7 + Number of AtomsC6 ColorC5 / Visibility LockedC4 VisibleC3 SelectC2 Na
" r\H3 {bN1tlV?+ y m TopHits2
Tagged7Solvation Free Energy%
Select
SEQRES!Resolution%RMS Gradient;REMARK99-Potential Energy93PartialChargeMethod#POSE_NUMBER5OBJECTID0+Number of Atoms1Net Partial Charge
/Net Formal Charge Name"IMolecule Solvent Accessibility1-Molecular Weight
-Molecular Volume /Molecular Formula7Molecular Composition7Minimization Criteria7LoopList5Initial RMS Gradient=Initial Potential Energy6+Improper Energy!5Hydrogen Bond Energy")ForcefieldFFML)ForcefieldBase!Forcefield/Exact Mol. Weight5Electrostatic Energy8+Dihedral Energy$ Color%Clean Energy<'ChiRotor RMSD)ChiRotor E-vdw-ChiRotor E-total+ChiRotor E-elec/Calculate Charges'CHARMm Energy #Bond Energy')AssignOBJECTID/%Angle Energy#C-CDOCKER_INTERACTION_ENERGY4+-CDOCKE 5Initial RMS Gradient
<* {skc[SLD<4,$~vnf^VNG?81* C9 C8C7C60<C6C59;C58:C579C568C557C546C535C524C513C502C5C491C480C47/C46.C45-C44,C43+C42*C41)C40(C4C39'C38&C37%C36$C35#C34"C33!C32 C31C30C3C29C28C27C26C25C24C23C22C21C20C2C19C18C17C16C15C14C13
C12C11C10
C1
t WkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_2MOLECULE_PROPERTY_DICTIONARY WkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_1MOLECULE_PROPERTY_DICTIONARYx:ItableDOCUMENTDOCUMENTCREATE TABLE DOCUMENT(VERSION);++-tableINCOMPATIBILITYINCOMPATIBILITYCREATE TABLE INCOMPATIBILITY (TARGET_VERSION, SOURCE_VERSION, CONSTRAINT TARGET_SOURCE UNIQUE (TARGET_VERSION, SOURCE_VERSION) ON CONFLICT FAIL)=Q+ indexsqlite_autoindex_INCOMPATIBILITY_1INCOMPATIBILITYzStableMODELMODELCREATE TABLE MODEL(MODELID INTEGER PRIMARY KEY,CATCHALL BLOB,OFFLINEABLEHIERARCHY BLOB,FORMAT TEXT)xGtableOBJECTSOBJECTSCREATE TABLE OBJECTS(OBJECTID INTEGER PRIMARY KEY, TYPE, FORMAT TEXT, DATA BLOB, SMILES TEXT)
c cfj _ EEtableMOLECULE_PROPERTY_DICTIONARYMOLECULE_PROPERTY_DICTIONARYCREATE TABLE MOLECULE_PROPERTY_DICTIONARY (ID INTEGER PRIMARY KEY AUTOINCREMENT,EXTERNAL_NAME TEXT UNIQUE,COLUMN_NAME TEXT UNIQUE NOT NULL,ORIGIN INTEGER DEFAULT 1 NOT NULL CHECK (ORIGIN IN (1, 2, 3)),EDITABLE INTEGER DEFAULT 1 NOT NULL CHECK (EDITABLE IN (0, 1)),HIDDEN INTEGER DEFAULT 0 NOT NULL CHECK (HIDDEN IN (0, 1)),INTRINSIC INTEGER DEFAULT 0 NOT NULL CHECK (INTRINSIC IN (0, 1)),USED INTEGER DEFAULT 1 NOT NULL CHECK (USED IN (0, 1)))WkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_1MOLECULE_PROPERTY_DICTIONARYWkE indexsqlite_autoindex_MOLECULE_PROPERTY_DICTIONARY_2MOLECULE_PROPERTY_DICTIONARY P ++Ytablesqlite_sequencesqlite_sequenceCREATE TABLE sqlite_sequence(name,seq)
;;=tableMOLECULE_PROPERTY_ORDERMOLECULE_PROPERTY_ORDERCREATE TABLE MOLECULE_PROPERTY_ORDER (OBJECTID INTEGER PRIMARY KEY, PROPERTY_ORDER BLOB)
" M vS4vaE*pS5 o M " 5 Hydrogen Bond EnergyC34! + Improper EnergyC33 ' CHARMm EnergyC32 5 Initial RMS GradientC31 ) ForcefieldFFMLC30 ) ForcefieldBaseC29 ! ForcefieldC28 ) ChiRotor E-vdwC27 - ChiRotor E-totalC26 + ChiRotor E-elecC25 ' ChiRotor RMSDC24$ = UseResidueTemplateChargeC23 3 PartialChargeMethodC22 SEQRESC21 REMARK99C20 ! ResolutionC19 LoopListC18 ' __PDBSeqres__C17 ) __PDBRemarks__C16 TaggedC15 / Calculate ChargesC14
1 Net Partial ChargeC13 / Net Formal ChargeC12 / Exact Mol. WeightC11
- Molecular WeightC10 - Molecular VolumeC9 / Molecular FormulaC8! 7 Molecular CompositionC7 + Number of AtomsC6 ColorC5 / Visibility LockedC4 VisibleC3 SelectC2 NameC1
l\D'fQ4iG- < % Clean EnergyC60; % RMS GradientC59 : 5 Van der Waals EnergyC589 - Potential EnergyC57 8 5 Electrostatic EnergyC56!7 7 Minimization CriteriaC55$6 = Initial Potential EnergyC545 # POSE_NUMBERC53'4 C -CDOCKER_INTERACTION_ENERGYC523 + -CDOCKER_ENERGYC512 TopHitsC50*1 I Molecule Solvent AccessibilityC490 OBJECTIDC48/ ) AssignOBJECTIDC47. ! VDW EnergyC46- ) deltaE FoldingC45, % Total ChargeC44+ pH listC43* + deltaE Deprot.C42) ! pH optimumC41( pIC40' # Bond EnergyC39& 3 Urey-Bradley EnergyC38!% 7 Solvation Free EnergyC37$ + Dihedral EnergyC36# % Angle EnergyC35
1 1EYy#4>RktlV?+ y m TopHits2
Tagged7Solvation Free Energy%
Select
SEQRES!Resolution%RMS Gradient;REMARK99-Potential Energy93PartialChargeMethod#POSE_NUMBER5OBJECTID0+Number of Atoms1Net Partial Charge
/Net Formal Charge Name"IMolecule Solvent Accessibility1-Molecular Weight
-Molecular Volume /Molecular Formula7Molecular Composition7Minimization Criteria7LoopList5Initial RMS Gradient+ deltaE Deprot.*+-CDOCKER_ENERGY3C-CDOCKER_INTERACTION_ENERGY4%Angle Energy#)AssignOBJECTID/#Bond Energy''CHARMm Energy /Calculate Charges+ChiRotor E-elec-ChiRotor E-total)ChiRotor E-vdw'ChiRotor RMSD%Clean Energy< Color+Dihedral Energy$5Electrostatic Energy8/Exact Mol. Weight!Forcefield)ForcefieldBase)ForcefieldFFML5Hydrogen Bond Energy"+Improper Energy!=Initial Potential Energy6
$k DQk1>Nf{, rk pI(!pH optimum)pH list+)deltaE Folding-'__PDBSeqres__)__PDBRemarks__Visible/Visibility Locked5Van der Waals Energy:!VDW Energy.=UseResidueTemplateCharge3Urey-Bradley Energy&LoopList7Minimization Criteria77Molecular Composition/Molecular Formula-Molecular Volume -Molecular Weight
"IMolecule Solvent Accessibility1 Name/Net Formal Charge1Net Partial Charge
+Number of AtomsOBJECTID0#POSE_NUMBER53PartialChargeMethod-Potential Energy9REMARK99%RMS Gradient;!Resolution
SEQRES
Select7Solvation Free Energy%
TaggedTopHits2%Total Charge,
/> ( $ ;;/tableCONFORMATION_PROPERTIESCONFORMATION_PROPERTIESCREATE TABLE CONFORMATION_PROPERTIES (OBJECTID INTEGER PRIMARY KEY,C1 TEXT,C2,C3)v''+tableCONFORMATIONSCONFORMATIONSCREATE TABLE CONFORMATIONS(OBJECTID INTEGER PRIMARY KEY, DATA BLOB,FORMAT TEXT)MMtableCONFORMATION_PROPERTY_DICTIONARYCONFORMATION_PROPERTY_DICTIONARYCREATE TABLE CONFORMATION_PROPERTY_DICTIONARY (ID INTEGER PRIMARY KEY AUTOINCREMENT,EXTERNAL_NAME TEXT UNIQUE,COLUMN_NAME TEXT UNIQUE NOT NULL,ORIGIN INTEGER DEFAULT 1 NOT NULL CHECK (ORIGIN IN (1, 2, 3)),EDITABLE INTEGER DEFAULT 1 NOT NULL CHECK (EDITABLE IN (0, 1)),HIDDEN INTEGER DEFAULT 0 NOT NULL CHECK (HIDDEN IN (0, 1)),INTRINSIC INTEGER DEFAULT 0 NOT NULL CHECK (INTRINSIC IN (0, 1)),USED INTEGER DEFAULT 1 NOT NULL CHECK (USED IN (0, 1)))_
sM indexsqlite_autoindex_CONFORMATION_PROPERTY_DICTIONARY_1CONFORMATION_PROPERTY_DICTIONARY_sM indexsqlite_autoindex_CONFORMATION_PROPERTY_DICTIONARY_2CONFORMATION_PROPERTY_DICTIONARY
VisibleC3 SelectC2 NameC1
Visible
Select Name
C3C2 C1
h _q h f!3indexNAME_INDEXDOCUMENT_PROPERTIESDCREATE UNIQUE INDEX NAME_INDEX ON DOCUMENT_PROPERTIES (NAME);;/tableCONFORMATION_PROPERTIESCONFORMATION_PROPERTIESCREATE TABLE CONFORMATION_PROPERTIES (OBJECTID INTEGER PRIMARY KEY,C1 TEXT,C2,C3)CCEtableCONFORMATION_PROPERTY_ORDERCONFORMATION_PROPERTY_ORDERCREATE TABLE CONFORMATION_PROPERTY_ORDER (OBJECTID INTEGER PRIMARY KEY, PROPERTY_ORDER BLOB)n33tableDOCUMENT_PROPERTIESDOCUMENT_PROPERTIESCREATE TABLE DOCUMENT_PROPERTIES(NAME STRING, VALUE STRING)33?tableMOLECULE_PROPERTIESMOLECULE_PROPERTIESCREATE TABLE "MOLECULE_PROPERTIES"(OBJECTID INTEGER PRIMARY KEY,C1 TEXT,C2,C3,C4,C5,C6,C7,C8,C9,C10,C11,C12,C13,C14,C15, C16, C17, C18, C19, C20, C21, C22, C23, C24, C25, C26, C27, C28, C29, C30, C31, C32, C33, C34, C35, C36, C37, C38, C39, C40, C41, C42, C43, C44, C45, C46, C47, C48, C49, C50, C51, C52, C53, C54, C55, C56, C57, C58, C59, C60)
L udL )Scenes Visiblefalse%
BSML NA Name%
BSML NA File
BSML Name
BSML File#%Active ViewGraphicsView'Show Graphicstrue!Show Tablefalse)Show Hierarchyfalse C r@ ! W 'T5369186MomanyRoneTrue
@H]ce@AV$/@'X_F?Z@jUp
@/=K@?2W@TӥS CONJUG> Minimization exiting with gradient tolerance ( 0.0100000) satisfied.@"iB@AV$/@$#9?+@: B RGANISM_TAXID: 7787;
SOURCE 5 VARIANT: G2 FORM;
SOURCE 6 ORGAN: ELECTRIC ORGAN;
SOURCE 7 TISSUE: ELECTROPLAQUE
KEYWDS SERINE ESTERASE, SERINE HYDROLASE, ALZHEIMER'S DISEASE,
KEYWDS 2 NERVE, MUSCLE, SYNAPSE, MEMBRANE, HYDROLASE, GPI-ANCHOR,
KEYWDS 3 LIPOPROTEIN, GLYCOPROTEIN, CHOLINESTERASE, ALTERNATIVE
KEYWDS 4 SPLICING, NEUROTRANSMITTER DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BRUMSHTEIN,E.H.RYDBERG,H.M.GREENBLATT,D.M.WONG,D.SHAYA,
AUTHOR 2 L.D.WILLIAMS,P.R.CARLIER,Y.P.PANG,I.SILMAN,J.L.SUSSMAN
REVDAT 2 24-FEB-09 2CKM 1 VERSN
REVDAT 1 04-SEP-06 2CKM 0
JRNL AUTH E.H.RYDBERG,B.BRUMSHTEIN,H.M.GREENBLATT,D.M.WONG,
JRNL AUTH 2 D.SHAYA,L.D.WILLIAMS,P.R.CARLIER,Y.P.PANG,I.SILMAN,
JRNL AUTH 3 J.L.SUSSMAN
JRNL TITL COMPLEXES OF ALKYLENE-LINKED TACRINE DIMERS WITH
JRNL TITL 2 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE: BINDING
JRNL TITL 3 OF BIS(5)-TACRINE PRODUCES A DRAMATIC
JRNL TITL 4 REARRANGEMENT IN THE ACTIVE-S ITE GORGE
JRNL REF J.MED.CHEM. V. 49 5491 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 16942022
JRNL DOI 10.1021/JM060164B
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2192213.75
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92
REMARK 3 NUMBER OF REFLECTIONS : 50424
REMARK 3
REMARK 3 FIT TO DATA USED I N REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2517
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 716
REMARK 3 BIN R VALUE (WORKING SET) : 0.42
REMARK 3 BIN FREE R VALUE : 0.38
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMA RK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.34
REMARK 3 B22 (A**2) : 8.34
REMARK 3 B33 (A**2) : -16.69
REMARK 3 B12 (A**2) : 6.53
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.53
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS D !EVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 1.9
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.12 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.81 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.55 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.10 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.338604
REMARK 3 BSOL : 40.9311
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR " (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE BIOLOGICALLY ACTIVE FORM OF THIS
REMARK 3 MOLECULE IS A DIMER, FORMED BY ROTATING THE ASYMMETRIC UNIT
REMARK 3 ABOUT THE CRYSTALLOGRAPHIC TWO-FOLD AXIS
REMARK 4
REMARK 4 2CKM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-06.
REMARK 100 THE PDBE ID CODE IS EBI-28490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL # : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE (RAXIS4++)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80692
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SH $ELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-33% V/V PEG 200, 0.5M MES
REMARK 280 PH5.8, 4DEG CELCIUS, SEEDING
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPE %RATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.80433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 & 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.60867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.60867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.80433
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 PROVID 'E INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 -55.94200
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 96.89439
REMARK 350 BIOMT3 2 0.000000 0.00 (0000 1.000000 -45.79975
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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 486
REMARK 465 SER A 487
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
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 LEU A 7 CD1 CD2
REMARK 470 ARG A 19 NE CZ NH1 ) NH2
REMARK 470 ASN A 42 CG OD1 ND2
REMARK 470 LYS A 52 CD CE NZ
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 ARG A 250 NH1 NH2
REMARK 470 GLU A 260 CD OE1 OE2
REMARK 470 HIS A 264 ND1 CD2 CE1 NE2
REMARK 470 GLU A 268 OE1 OE2
REMARK 470 LYS A 270 CD CE NZ
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 LYS A 346 CE NZ
REMARK 470 GLU A 350 CG CD OE1 OE2
REMARK 470 ASP A 365 OD1 OD2
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 GLU A 434 CD OE1 OE2
REMARK 470 LYS A 454 CG CD CE NZ
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 GLU A 508 OE1 OE2
REMARK 470 LYS A 511 CD CE NZ
REMARK 470 ARG A 515 NH1 NH2
REMARK 470 GLN A 526 OE1 NE2
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 468 - O HOH A 2184 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 O HOH A 2149 + O HOH A 2149 4556 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 344 CD GLU A 344 OE1 0.075
REMARK 500 GLU A 344 CD GLU A 344 OE2 0.091
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOC ,HEMICAL 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 LYS A 14 CD - CE - NZ ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 46 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REM -ARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 45 -10.66 80.53
REMARK 500 SER A 108 73.37 -158.70
REMARK 500 LEU A 158 76.85 -118.06
REMARK 500 ASN A 167 15.01 55.03
REMARK 500 SER A 200 -125.66 58.57
REMARK 500 GLU A 299 -73.77 -113.17
REMARK 500 THR A 317 -157.92 -161.20
REMARK 500 ASP A 380 50.00 -152.09
REMARK 500 VAL A 400 -62.72 -127.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK . 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 442 0.07 SIDE CHAIN
REMARK 500 TRP A 473 0.06 SIDE CHAIN
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 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 LYS A 491 24.9 L L OUTSIDE RANGE
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 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDEN 0CE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AA7 A1536
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE
REMARK 900 COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 LAUE DATA
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-
REMARK 900 ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)
REMARK 900 RELATED I 1D: 1DX6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-GALANTHAMINE AT 2.3A RESOLUTION
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH BW284C51
REMARK 900 RELATED ID: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-HUPRINE X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7
REMARK 900 ) FROM TORPEDO CALIFORNICA AT 1.8A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-
REMARK 900 ALZHEIMER DRUG, E2020 (ARICEPT), COMPLEXED
REMARK 900 WITH ITS TARGET ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900 II
REMARK 900 RELATED ID: 2 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH
REMARK 900 (+)-HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 HUPERZINE B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH RIVASTIGMINE
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH NAP
REMARK 900 RELATED ID: 1H22 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1HBJ 3 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN
REMARK 900 TORPEDO CALIFORNICA ACHE AND A REVERSIBLE
REMARK 900 INHIBITOR, 4-AMINO-5-FLUORO-2-METHYL-3-(
REMARK 900 3-TRIFLUOROACETYLBENZYLTHIOMETHYL)QUINOLINE
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-
REMARK 900 HEPTYLENE-BIS-N,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-
REMARK 900 PROPYLENE-BIS-N,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1JJB RELATED DB: PDB
REMARK 900 A NEUTRAL MOLECULE IN CATION-BINDING SITE:
REMARK 900 SPECIFIC BINDINGOF PEG-SH TO
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH MF268
REMARK 900 RELATED ID: 1ODC RELATED DB: PDB
REMARK 4900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH N-4'-QUINOLYL-N'-9
REMARK 900 "-(1",2",3",4"-TETRAHYDROACRIDINYL)-1,8-
REMARK 900 DIAMINOOCTANE AT 2.2A RESOLUTION
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT A) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT B) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT C) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL A 5ND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT D) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT E) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT F) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT G) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMA 6RK 900 NINE TIME POINTS (POINT H) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT I) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1SOM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NERVE AGENT GD (SOMAN).
REMARK 900 RELATED ID: 1U65 RELATED DB: PDB
REMARK 900 ACHE W. CPT-11
REMARK 900 RELATED ID: 1UT6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH N-9-(1',2',3',4
REMARK 900 '-TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT
REMARK 900 2.4 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COM 7PLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERA 8SE (ACHE) COMPLEXED WITH BIS-
REMARK 900 ACTING GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (R)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 1ZGC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (RS)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 MONOCHROMATIC DATA
REMARK 900 RELATED ID: 2C4H RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2C58 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM AC 9ETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2C5F RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-TRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM THIOCHOLINE
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL
REMARK 900 SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 REVEALED BY THE COMPLEX STRUCTURE WITH A
REMARK 900 BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF AGED DI-ISOPROPYL-
REMARK 900 PHOSPHORO-FLUORIDATE (DFP) BOUND TO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 THEORETICAL MO :DEL OF (S)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
DBREF 2CKM A 1 543 UNP P04058 ACES_TORCA 22 564
HET NAG A1537 14
HET NAG A1538 14
HET AA7 A1536 37
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM AA7 N,N'-DI-1,2,3,4-TETRAHYDROACRIDIN-9-
HETNAM 2 AA7 YLHEPTANE-1,7-DIAMINE
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 4 AA7 C33 H40 N4
FORMUL 5 HOH *206(H2 O1)
CRYST1 111.884 111.884 137.413 90.00 90.00 120.00 P 31 2 1 6
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 0.008938 0.005160 0.000000 0.00000
SCALE2 0.000000 0.010321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007277 0.00000SEQRES 1 A 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES ; 3 A 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 543 HIS ILE LEU SE