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HEADER CHOLINESTERASE 06-NOV-00 1EA5
TITLE NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO
TITLE 2 CALIFORNICA AT 1.8A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7
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
KEYWDS SERINE HYDROLASE, NEUROTRANSMITTER CLEAVAGE, CATALYTIC
KEYWDS 2 TRIAD, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,M.WEIK,I.SILMAN,J.L.SUSSMAN
REVDAT 1 08-NOV-00 1EA5 0
JRNL AUTH M.HAREL,M.WEIK,I.SILMAN,J.L.SUSSMAN
JRNL TITL NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM
JRNL TITL 2 TORPEDO CALIFORNICA AT 1.8A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.BUCHT,K.HJALMARSSON
REMARK 1 TITL RESIDUES IN TORPEDO CALIFORNICA
REMARK 1 TITL 2 ACETYLCHOLINESTERASE NECESSARY FOR PROCESSING TO A
REMARK 1 TITL 3 GLYCOSYL PHOSPHATIDYLINOSITOL-ANCHORED FORM
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1292 223 1996
REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.H.AXELSEN,M.HAREL,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL STRUCTURE AND DYNAMICS OF THE ACTIVE SITE GORGE OF
REMARK 1 TITL 2 ACETYLCHOLINESTERASE: SYNERGISTIC USE OF MOLECULAR
REMARK 1 TITL 3 DYNAMICS SIMULATION AND X-RAY CRYSTALLOGRAPHY
REMARK 1 REF PROTEIN SCI. V. 3 188 1994
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1 REFERENCE 3
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 4
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 1 REFERENCE 5
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,L.VARON,L.TOKER,
REMARK 1 AUTH 2 A.H.FUTERMAN,I.SILMAN
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF A DIMERIC FORM
REMARK 1 TITL 2 OF ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 1 TITL 3 SUBSEQUENT TO SOLUBILIZATION WITH
REMARK 1 TITL 4 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
REMARK 1 REF J.MOL.BIOL. V. 203 821 1988
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.SCHUMACHER,S.CAMP,Y.MAULET,M.NEWTON,
REMARK 1 AUTH 2 K.MACPHEE-QUIGLEY,S.S.TAYLOR,T.FRIEDMANN,P.TAYLOR
REMARK 1 TITL PRIMARY STRUCTURE OF TORPEDO CALIFORNICA
REMARK 1 TITL 2 ACETYLCHOLINESTERASE DEDUCED FROM ITS CDNA SEQUENCE
REMARK 1 REF NATURE V. 319 407 1986
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 1.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 1738173.08
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 86179
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) : 0.185
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4317
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.8
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.9
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11185
REMARK 3 BIN R VALUE (WORKING SET) : 0.289
REMARK 3 BIN FREE R VALUE : 0.292
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 597
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4390
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 741
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.58
REMARK 3 B22 (A**2) : 6.58
REMARK 3 B33 (A**2) : -13.17
REMARK 3 B12 (A**2) : 2.62
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.9
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.9
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.41 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.26 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.09 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.12 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.367212
REMARK 3 BSOL : 82.8547
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEVERAL RESIDUES ARE NOT
REMARK 3 SEEN IN THE CRYSTAL STRUCTURE, DUE TO DISORDER. THESE
REMARK 3 INCLUDE THREE N-TERMINAL RESIDUES (ASP 1, ASP 2, HIS 3),
REMARK 3 AND THE C-TERMINAL RESIDUES AFTER THR 535.
REMARK 3 THERE ARE 2 ALTERNATE CONFORMATIONS OBSERVED FOR RESIDUES:
REMARK 3 9, 16, 19, 24, 46, 49, 55, 65, 221, 228, 260, 344, 353,
REMARK 3 408, 430, 455, 468, 478, 508, 526.
REMARK 4
REMARK 4 1EA5 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 6-NOV-2000.
REMARK 100 THE EBI ID CODE IS EBI-5523.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-1999
REMARK 200 TEMPERATURE (KELVIN) : 155
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14
REMARK 200 BEAMLINE : ID14-EH4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9312
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC 2X2 QUANTUM4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86444
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.8
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 1.9
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.067
REMARK 200 FOR THE DATA SET : 16.4
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.9
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.251
REMARK 200 FOR SHELL : 2.2
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 (%): 68.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 35% PEG 200, 100 MM MES, PH 5.8, AT 4 DEG.
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 45.86233
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 91.72467
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 91.72467
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 45.86233
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 BIOLOGICAL UNIT: DIMER IN SOLUTION, ACTIVE AS MONOMER
REMARK 300
REMARK 300 THE ENZYME IS A GPI-ANCHORED DIMER, THE TWO
REMARK 300 MONOMERS IN THE DIMER ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 300 TWO-FOLD SYMMETRY.
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 HYDROLYZES CHOLINE RELEASED INTO THE SYNAPSE.
REMARK 400 CATALYTIC ACTIVITY: ACETYLCHOLINE + H(2)O = CHOLINE + ACETATE.
REMARK 400 INHIBITORS OF THE ENZYME ACETYLCHOLINESTERASE (ACHE) SLOW AND
REMARK 400 SOMETIMES REVERSE THE COGNITIVE DECLINE EXPERIENCED BY INDIVIDUALS
REMARK 400 WITH ALZHEIMER'S DISEASE.
REMARK 400 TORPEDO CALIFONICA ACETYLCHOLINESTERASE IS A G2 DIMER IN
REMARK 400 SOLUTION (SEE SUSSMAN 1988). THE ASYMMETRIC UNIT CONTAINS A
REMARK 400 MONOMER, WITH THE CRYSTALLOGRAPHIC TWO-FOLD AXIS RELATING
REMARK 400 THE TWO MONOMERS IN A DIMER.
REMARK 400 THIS IS THE HIGHEST RESOLUTION ACETYLCHLINESTERASE
REMARK 400 DETERMINED SO FAR.
REMARK 400 THERE IS RECENT EVIDENCE (SEE BUCHT 1996) THAT THE GPI
REMARK 400 ANCHOR IS ATTACHED TO EITHER SER 543 OR SER 544, NOT TO CYS
REMARK 400 537.
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 ALA A 536
REMARK 465 CYS A 537
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 14 CE NZ
REMARK 470 ASN A 42 CG OD1 ND2
REMARK 470 GLU A 89 CD OE1 OE2
REMARK 470 LYS A 270 CE NZ
REMARK 470 GLU A 299 CD OE1 OE2
REMARK 470 GLU A 434 OE1 OE2
REMARK 470 LYS A 454 CD CE NZ
REMARK 470 GLU A 489 CD OE1 OE2
REMARK 470 SER A 490 OG
REMARK 470 LYS A 491 CE NZ
REMARK 470 LYS A 530 CE NZ
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 ASP A 93 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 VAL A 142 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASN A 183 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 ALA A 234 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 PRO A 283 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 SER A 291 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 297 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLY A 328 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 LYS A 346 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP A 377 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ILE A 439 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 THR A 479 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 8.2 DEGREES
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 O HOH Z 1338 O HOH Z 1339 2.15
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER A 200 54.52 -115.74
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 Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 NAG 598, IS BOUND TO ASN 416; NAG 599, IS BOUND TO ASN 59
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE
REMARK 900 DATA
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH
REMARK 900 O-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 WITH
REMARK 900 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: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG,
REMARK 900 E2020 (ARICEPT), COMPLEXED WITH ITS TARGET
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II
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 NINE TIME
REMARK 900 POINTS (POINT A) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT B) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT C) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT D) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT E) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT G) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT H) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT I) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO 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 BY
REMARK 900 NERVE AGENT GD (SOMAN).
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
REMARK 900 O-ETHYL-S-[2-[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
REMARK 900 O-ETHYL-S-[2-[BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO 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
REMARK 900 DI-ISOPROPYL-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
DBREF 1EA5 A 1 537 SWS P04058 ACES_TORCA 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
HET NAG A 598 14
HET NAG A 599 14 SEE REMARK 600
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 3 HOH *732(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 212 ASP A 217 1 6
HELIX 10 10 SER A 237 LEU A 252 1 16
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 TYR A 375 1 12
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 LYS A 413 1 14
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
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.04
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.03
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
LINK ND2 ASN A 59 C1 NAG A 599 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 598 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 2.02
SITE 1 CAT 3 SER A 200 GLU A 327 HIS A 440
CRYST1 111.573 111.573 137.587 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 0.008963 0.005175 0.000000 0.00000
SCALE2 0.000000 0.010349 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007268 0.00000
END |