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HEADER HYDROLASE 15-FEB-03 1ODC
TITLE STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED
TITLE 2 WITH N-4'-QUINOLYL-N'-9"-(1",2",3",4"
TITLE 3 -TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE AT 2.2A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 SYNONYM: ACHE;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.1.1.7;
COMPND 6 OTHER_DETAILS: INTER-MONOMER DISULFIDE BRIDGE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 VARIANT: G2 FORM;
SOURCE 5 ORGAN: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE;
SOURCE 7 OTHER_DETAILS: SYNTHETIC HETEROBIVALENT TACRINE-BASED
SOURCE 8 DIMER, A8B (N-4'-QUINOLYL-N'-9"-(1",2",3",4"
SOURCE 10 -TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE) DIHYDROCHLORIDE
SOURCE 11 WITH THE TACRINE MOIETY BOUND TO THE 'ANIONIC' SUBSITE,
SOURCE 12 NEAR THE BOTTOM OF THE ACTIVE SITE GORGE, AND THE
SOURCE 13 4-AMINOQUINOLINE MOIETY BOUND TO THE 'PERIPHERAL' ANIONIC
SOURCE 14 SITE (PAS) AT THE TOP OF THE GORGE OF TCACHE, BOTH IN A
SOURCE 15 DOUBLE-STACKING SANDWICH. THE LIGAND, A8B, THUS BINDS BY
SOURCE 16 SPANNING THE ACTIVE-SITE GORGE.
KEYWDS SERINE HYDROLASE, ACETYLCHOLINESTERASE, NEUROTRANSMITTER
KEYWDS 2 CLEAVAGE, ALZHEIMER'S DISEASE, BIVALENT LIGAND, DUAL-SITE
KEYWDS 3 BINDING, INHIBITOR, TACRINE, QUINOLINE, HETERODIMER,
KEYWDS 4 HYDROLASE, SERINE ESTERASE SYNAPSE, MEMBRANE, NERVE,
KEYWDS 5 MUSCLE, SIGNAL, GPI-ANCHOR NEUROTRANSMITTER DEGRADATION,
KEYWDS 6 GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.WONG,H.M.GREENBLATT,P.R.CARLIER,Y.-F.HAN,
AUTHOR 2 Y.-P.PANG,I.SILMAN,J.L.SUSSMAN
REVDAT 1 23-MAR-05 1ODC 0
JRNL AUTH D.M.WONG,B.BRUMSTEIN,H.M.GREENBLATT,P.R.CARLIER,
JRNL AUTH 2 Y.-F.HAN,Y.-P.PANG,I.SILMAN,J.L.SUSSMAN
JRNL TITL ACETYLCHOLINESTERASE COMPLEXED WITH A TACRINE-BASED
JRNL TITL 2 BIVALENT LIGAND: X-RAY EVIDENCE FOR A
JRNL TITL 3 DOUBLE-STACKING SANDWICH WITH TRYPTOPHAN AT THE
JRNL TITL 4 PERIPHERAL ANIONIC SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.M.WONG,H.M.GREENBLATT,H.DVIR,P.R.CARLIER,Y.-F.HAN,
REMARK 1 AUTH 2 Y.-P.PANG,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL ACETYLCHOLINESTERASE COMPLEXED WITH BIVALENT
REMARK 1 TITL 2 LIGANDS RELATED TO HUPERZINE A: EXPERIMENTAL
REMARK 1 TITL 3 EVIDENCE FOR SPECIES-DEPENDENT PROTEIN-LIGAND
REMARK 1 TITL 4 COMPLEMENTARITY
REMARK 1 REF J.AM.CHEM.SOC. V. 125 363 2003
REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.R.CARLIER,E.S.-H.CHOW,Y.-F.HAN,J.LIU,J.EL YAZAL,
REMARK 1 AUTH 2 Y.-P.PANG
REMARK 1 TITL HETERODIMERIC TACRINE-BASED ACETYLCHOLINESTERASE
REMARK 1 TITL 2 INHIBITORS: INVESTIGATING LIGAND-PERIPHERAL SITE
REMARK 1 TITL 3 INTERACTIONS
REMARK 1 REF J.MED.CHEM. V. 42 4225 1999
REMARK 1 REFN ASTM JMCMAR US ISSN 0022-2623
REMARK 1 REFERENCE 3
REMARK 1 AUTH Y.-P.PANG,A.P.KOZIKOWSKI
REMARK 1 TITL PREDICTION OF THE BINDING SITES OF HUPERZINE A IN
REMARK 1 TITL 2 ACETYLCHOLINESTERASE BY DOCKING STUDIES
REMARK 1 REF J.COMPUT.-AIDED MOL.DES. V. 8 669 1994
REMARK 1 REFN ASTM JCADEQ NE ISSN 0920-654X
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.HAREL,I.SCHALK,L.EHRET-SABATIER,F.BOUET,
REMARK 1 AUTH 2 M.GOELDNER,C.HIRTH,P.H.AXELSEN,I.SILMAN,
REMARK 1 AUTH 3 J.L.SUSSMAN
REMARK 1 TITL QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN
REMARK 1 TITL 2 THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE
REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 90 9031 1993
REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,
REMARK 1 AUTH 2 L.TOKER,I.SILMAN
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN
REMARK 1 REF SCIENCE V. 253 872 1991
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0; CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 2034289.24
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 49443
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 SET) : 0.1991
REMARK 3 FREE R VALUE : 0.2401
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2428
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.1
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4544
REMARK 3 BIN R VALUE (WORKING SET) : 0.234
REMARK 3 BIN FREE R VALUE : 0.226
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 225
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.03
REMARK 3 B22 (A**2) : 7.03
REMARK 3 B33 (A**2) : -14.04
REMARK 3 B12 (A**2) : 3.07
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.9
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.0
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.27
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) : 1.233 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.811 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.153 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.994 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 51.6
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : A8B_1.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : A8B.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEVERAL RESIDUES ARE NOT SEEN IN
REMARK 3 THE CRYSTAL STRUCTURE, DUE TO DISORDER. THESE INCLUDE
REMARK 3 ASP 1, ASP 2, HIS 3 AND THE C-TERMINAL RESIDUES AFTER
REMARK 3 ALA 536. SEVERAL RESIDUES MISSING IN CHAIN BREAK, FROM
REMARK 3 HIS 486 - GLU 489 (INCLUSIVE). TWO WATER MOLECULES WERE
REMARK 3 FITTED WITH 0.75 OCCUPANCIES EACH
REMARK 3 (HOH Z 152 AND HOH Z 153).
REMARK 4
REMARK 4 1ODC COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-FEB-2003.
REMARK 100 THE EBI ID CODE IS EBI-12137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2000
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NONE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU-H3R
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 CONFOCAL
REMARK 200 MIRRORS
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU R-AXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50284
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 0.35
REMARK 200 R MERGE (I) : 0.049
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.1
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.81
REMARK 200 R MERGE FOR SHELL (I) : 0.287
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED FROM
REMARK 280 28-33% V/V PEG 200 0.5M MES PH 5.8 AT 4 DEG. CELSIUS; THEN
REMARK 280 SOAKED IN MOTHER LIQUOR (40% V/V PEG 200 IN 0.1 M MES
REMARK 280 BUFFER, PH 5.8) CONTAINING 1MM N-4'-QUINOLYL-N'-9"-(1",2",
REMARK 280 3",4"-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE DIHYRDOCHLORIDE
REMARK 280 FOR ONE DAY.
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 OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 Y-X,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,Y-X,1/3-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 -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 45.58133
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 91.16267
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 91.16267
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 45.58133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 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 400
REMARK 400 COMPOUND
REMARK 400 COMPOUND HYDROLYZES CHOLINE RELEASED INTO THE SYNAPSE.
REMARK 400 CATALYTIC ACTIVITY: ACETYLCHOLINE + H(2)O = CHOLINE
REMARK 400 ACETATE. INHIBITORS OF THE ENZYME ACETYLCHOLINESTERASE
REMARK 400 (ACHE) IMPROVE THE COGNITIVE ABILITIES OF INDIVIDUALS WITH
REMARK 400 EARLY STAGE ALZHEIMER'S DISEASE. 9-AMINO-1,2,3,4-TETRA-
REMARK 400 HYDROACRIDINE (TACRINE, ALSO KNOWN AS THA OR COGNEX), A
REMARK 400 SYNTHETIC COMPOUND, IS AMONG THE POTENT ACHE INHIBITORS
REMARK 400 USED IN THIS TREATMENT. THE LIGAND, A8B
REMARK 400 (N-4'-QUINOLYL-N'- 9"-(1",2",3",4"
REMARK 400 -TETRA-HYDROACRIDINYL)-1,8-DIAMINOOCTANE) DIHYDROCHLORIDE,
REMARK 400 A C8-ALKYLENE LINKED HETERODIMER OF TACRINE AND
REMARK 400 4-AMINOQUINOLINE, WAS DESIGNED TO PROBE THE PROTEIN-LIGAND
REMARK 400 INTERACTIONS AT THE 'PERIPHEAL' ANIONIC
REMARK 400 SITE (PAS) OF THE ACTIVE-SITE GORGE OF ACHE. IT HAS BEEN
REMARK 400 SHOWN TO EXHIBIT POTENT INHIBITION OF ACHE. THE TACRINE
REMARK 400 MOIETY BINDS TO THE 'ANIONIC' SUBSITE, NEAR THE BOTTOM OF
REMARK 400 THE ACTIVE-SITE GORGE OF TCACHE, BETWEEN THE AROMATIC RINGS
REMARK 400 OF TRP84 AND PHE330, AS SEEN FOR THE TCACHE/TACRINE
REMARK 400 COMPLEX, AND THE 4-AMINOQUINOLINE MOIETY BINDS TO THE PAS
REMARK 400 AT THE TOP OF THE GORGE, BETWEEN THE AROMATIC RINGS OF
REMARK 400 TRP279 AND TYR70. THE LIGAND, A8B, THUS BINDS BY SPANNING
REMARK 400 THE ACTIVE SITE GORGE, WITH BOTH BINDING MOIETIES OF A8B
REMARK 400 BINDING IN A DOUBLE-STACKING SANDWICH.
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 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 LYS A 52 CD CE NZ
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 GLU A 260 CD OE1 OE2
REMARK 470 GLU A 268 OE1 OE2
REMARK 470 LYS A 270 CE NZ
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 GLU A 350 OE1
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 GLU A 434 OE2
REMARK 470 LYS A 454 CG CD CE NZ
REMARK 470 LYS A 498 CD CE NZ
REMARK 470 GLU A 508 OE2
REMARK 470 LYS A 511 CD CE NZ
REMARK 470 ALA A 536 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 97 CA - CB - CG ANGL. DEV. = 12.6 DEGREES
REMARK 500 LEU A 143 CA - CB - CG ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 LYS A 491 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 VAL A 518 CB - CA - C ANGL. DEV. = -11.9 DEGREES
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 43 SD MET A 43 CE 0.161
REMARK 500 MET A 175 SD MET A 175 CE -0.378
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 ND2 ASN A 59 C1 NAG G 59 1.46
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A X
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 NAG A1536 IS COVALENTLY ATTACHED TO THE ND2 ATOM OF ASN A 59
REMARK 600 BY ITS C1 ATOM;
REMARK 600 NAG A1537 IS COVALENTLY ATTACHED TO THE ND2 ATOM OF ASN A 416
REMARK 600 BY ITS C1 ATOM.
REMARK 600
REMARK 600 ATOM N1 A8B A1538 IS PROTONATED,
REMARK 600 ATOM N32 A8B A1538 IS PROTONATED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION: ACTIVE-SITE CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: IHB
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: A8B
REMARK 800 SITE_DESCRIPTION: A8B BINDING SITE FOR CHAIN A
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 ID: 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: 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 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: 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 AND 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
REMARK 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: 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 COMPLEXED 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 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-
REMARK 900 ACTING GALANTHAMINE DERIVATIVE
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: 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 MODEL OF (S)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
DBREF 1ODC A 1 543 SWS P04058 ACES_TORCA 22 564
SEQRES 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 SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
HET NAG A1536 14 SEE REMARK 600
HET NAG A1537 14 SEE REMARK 600
HET A8B A1538 34 SEE REMARK 600
HETNAM A8B N-4'-QUINOLYL-N'-9"-(1",2",3",4"-TETRAHYDRO-
HETNAM 2 A8B ACRIDINYL)-1,8-DIAMINOOCTANE DIHYDROCHLORIDE
HETSYN A8B TACRINE(8)-4-AMINOQUINOLINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 3 A8B C30 H38 N4
FORMUL 4 HOH *153(H2 O1)
HELIX 1 1 VAL A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASN A 131 5 5
HELIX 4 4 GLY A 132 GLU A 140 1 9
HELIX 5 5 VAL A 150 LEU A 156 1 7
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 GLN A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 SER A 215 PHE A 219 5 5
HELIX 10 10 VAL A 238 LEU A 252 1 15
HELIX 11 11 SER A 258 LYS A 269 1 12
HELIX 12 12 LYS A 270 GLU A 278 1 9
HELIX 13 13 TRP A 279 LEU A 282 5 4
HELIX 14 14 SER A 304 GLY A 312 1 9
HELIX 15 15 GLY A 328 ALA A 336 1 9
HELIX 16 16 SER A 348 VAL A 360 1 13
HELIX 17 17 ASN A 364 THR A 376 1 13
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 GLY A 415 1 16
HELIX 20 20 PRO A 433 GLY A 437 5 5
HELIX 21 21 GLU A 443 PHE A 448 1 6
HELIX 22 22 GLY A 449 VAL A 453 5 5
HELIX 23 23 VAL A 453 ASN A 457 5 5
HELIX 24 24 THR A 459 GLY A 480 1 22
HELIX 25 25 ARG A 517 GLN A 526 1 10
HELIX 26 26 GLN A 526 THR A 535 1 10
SHEET 1 AA 3 LEU A 7 THR A 10 0
SHEET 2 AA 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AB11 THR A 18 VAL A 22 0
SHEET 2 AB11 SER A 25 PRO A 34 -1 O SER A 25 N VAL A 22
SHEET 3 AB11 TYR A 96 VAL A 101 -1 O LEU A 97 N ILE A 33
SHEET 4 AB11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AB11 THR A 109 ILE A 115 1 O THR A 110 N VAL A 142
SHEET 6 AB11 GLY A 189 GLU A 199 1 N ASP A 190 O THR A 109
SHEET 7 AB11 ARG A 221 GLN A 225 1 O ARG A 221 N ILE A 196
SHEET 8 AB11 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AB11 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AB11 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AB11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AC 2 VAL A 236 SER A 237 0
SHEET 2 AC 2 VAL A 295 ILE A 296 1 N ILE A 296 O VAL A 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555
SSBOND 2 CYS A 254 CYS A 265 1555 1555
SSBOND 3 CYS A 402 CYS A 521 1555 1555
LINK C1 NAG A1536 ND2 ASN A 59 1555 1555
LINK C1 NAG A1537 ND2 ASN A 416 1555 1555
CISPEP 1 SER A 103 PRO A 104 0 1.29
SITE 1 ACT 3 SER A 200 HIS A 440 GLU A 327
SITE 1 IHB 14 TRP A 84 TYR A 70 TYR A 121 GLU A 199
SITE 2 IHB 14 ILE A 275 GLU A 278 TRP A 279 PHE A 330
SITE 3 IHB 14 HIS A 440 HOH X 29 HOH X 33 HOH X 78
SITE 4 IHB 14 HOH X 85 A8B A1538
SITE 1 A8B 12 TYR A 70 TRP A 84 GLY A 118 TYR A 121
SITE 2 A8B 12 GLU A 199 TRP A 279 PHE A 330 TRP A 432
SITE 3 A8B 12 HIS A 440 HOH X 29 HOH X 78 HOH X 85
CRYST1 111.487 111.487 136.744 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 0.008970 0.005179 0.000000 0.00000
SCALE2 0.000000 0.010357 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007313 0.00000
TER 4179 ALA A 536
MASTER 594 0 3 26 16 0 8 6 4393 1 70 42
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