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HEADER SERINE HYDROLASE 23-JUN-96 2ACE
TITLE NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO
TITLE 2 CALIFORNICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.7;
COMPND 5 BIOLOGICAL_UNIT: DIMER IN SOLUTION, ACTIVE AS MONOMER
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.L.RAVES,I.SILMAN,J.L.SUSSMAN
REVDAT 1 08-NOV-96 2ACE 0
SPRSDE 08-NOV-96 2ACE 1ACE
JRNL AUTH M.L.RAVES,M.HAREL,Y.-P.PANG,I.SILMAN,
JRNL AUTH 2 A.P.KOZIKOWSKI,J.L.SUSSMAN
JRNL TITL 3D STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
JRNL TITL 2 THE NOOTROPIC ALKALOID, (-)-HUPERZINE A
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS
JRNL REFN 0353
REMARK 1
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 0113
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 0795
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 0040
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 0038
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 0070
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
REMARK 1 TITL 3 SEQUENCE
REMARK 1 REF NATURE V. 319 407 1986
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 30035
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) : 0.199
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.2
REMARK 3 FREE R VALUE TEST SET COUNT : 1555
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3181
REMARK 3 BIN R VALUE (WORKING SET) : 0.308
REMARK 3 BIN FREE R VALUE : 0.390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.2
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 167
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4143
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 204
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED 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) : NULL
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) : 24.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.60
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) : 1.41 ; 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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM11.WAT
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.WAT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ACE COMPLIES WITH FORMAT V. 2.1, 25-OCT-1996
REMARK 6
REMARK 6 TORPEDO CALIFONICA ACETYLCHOLINESTERASE IS A G2 DIMER IN
REMARK 6 SOLUTION (SEE SUSSMAN 1988). THE ASYMMETRIC UNIT CONTAINS
REMARK 6 A MONOMER, WITH THE CRYSTALLOGRAPHIC TWO-FOLD AXIS RELATING
REMARK 6 THE TWO MONOMERS IN A DIMER.
REMARK 7
REMARK 7 THE ORIGINAL ACETYLCHOLINESTERASE STRUCTURE, 1ACE, WAS
REMARK 7 SHOWN TO CONTAIN AN INHIBITOR, DECAMETHONIUM, INSIDE THE
REMARK 7 ACTIVE-SITE GORGE (SEE AXELSEN 1994), AND HAS, THEREFORE,
REMARK 7 BEEN REPLACED WITH THE CURRENT NATIVE STRUCTURE.
REMARK 8
REMARK 8 SEVERAL RESIDUES ARE NOT SEEN IN THE CRYSTAL STRUCTURE,
REMARK 8 DUE TO DISORDER. THESE INCLUDE THREE N-TERMINAL RESIDUES
REMARK 8 (ASP 1, ASP 2, HIS 3), THE LOOP FROM PRO 485 TO GLU 489
REMARK 8 AND THE C-TERMINAL RESIDUES AFTER THR 535.
REMARK 9
REMARK 9 THERE IS RECENT EVIDENCE (SEE BUCHT 1996) THAT THE GPI
REMARK 9 ANCHOR IS ATTACHED TO EITHER SER 543 OR SER 544, NOT TO
REMARK 9 CYS 537.
REMARK 10
REMARK 10 THE NATURAL SUBSTRATE ACETYLCHOLINE, IN AN ALL-TRANS
REMARK 10 CONFORMATION, HAS BEEN MANUALLY DOCKED INTO THE ACTIVE
REMARK 10 SITE, COVALENTLY BOUND TO SER 200 IN A TETRAHEDRAL
REMARK 10 INTERMEDIATE CONFORMATION. THE ACETYLCHOLINE IS A MODEL,
REMARK 10 NOT DERIVED FROM THE EXPERIMENTAL DATA.
REMARK 11
REMARK 11 THR 535 IS THE LAST RESIDUE OBSERVED AT THE C-TERMINUS.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-1993
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DESY
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46243
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.25
REMARK 200 RESOLUTION RANGE LOW (A) : 25.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 1.9
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.095
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.8
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.713
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.9
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1ACE
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 -0.866007 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866044 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.56847
REMARK 290 SMTRY1 3 -0.500000 0.866007 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866044 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.13693
REMARK 290 SMTRY1 4 -0.500000 0.866007 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866044 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 91.13693
REMARK 290 SMTRY1 6 -0.500000 -0.866007 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866044 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.56847
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THE ENZYME IS A GPI-ANCHORED DIMER, THE TWO MONOMERS IN
REMARK 300 THE DIMER ARE RELATED BY CRYSTALLOGRAPHIC TWO-FOLD
REMARK 300 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 APPLY THE FOLLOWING TO CHAINS: NULL
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 56.20500
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 97.35000
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 91.13300
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH 732 LIES ON A SPECIAL POSITION.
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 HIS 26 ND1 CE1 NE2 CD2
REMARK 470 ASN 42 CG OD1 ND2
REMARK 470 ARG 46 CZ NH1 NH2
REMARK 470 GLU 89 CD OE1 OE2
REMARK 470 GLN 162 OE1 NE2
REMARK 470 ARG 250 CZ NH1 NH2
REMARK 470 ASN 257 CG OD1 ND2
REMARK 470 GLU 260 OE1 OE2
REMARK 470 GLU 268 OE1 OE2
REMARK 470 LYS 270 CE NZ
REMARK 470 GLU 344 OE1 OE2
REMARK 470 GLU 350 OE1 OE2
REMARK 470 LYS 357 NZ
REMARK 470 ASP 365 OD1 OD2
REMARK 470 LYS 413 CD CE NZ
REMARK 470 LYS 491 CD CE NZ
REMARK 470 LYS 498 CG CD CE NZ
REMARK 470 GLU 499 OE1 OE2
REMARK 470 GLU 508 CD OE1 OE2
REMARK 470 LYS 511 CD CE NZ
REMARK 470 ARG 515 CZ NH1 NH2
REMARK 470 GLN 526 OE1 NE2
REMARK 470 ASN 533 CG OD1 ND2
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. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 732 O HOH 732 4556 0.01
REMARK 500 NE2 GLN 374 O HOH 732 4556 2.04
REMARK 500 O HOH 732 NE2 GLN 374 4556 2.04
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ACH 998, ACETYLCHOLINE WAS MANUALLY MODELED IN THE ACTIVE
REMARK 600 SITE, AND IS COVALENTLY ATTACHED TO SER 200 IN THE
REMARK 600 TETRAHEDRAL INTERMEDIATE STATE.
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD:
REMARK 650 AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 700 STRAND: B 1; THERE IS A CENTRAL ELEVEN-STRANDED SHEET AND
REMARK 700 A SMALL THREE-STRANDED SHEET AT THE N-TERMINUS.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 2ACE SWS P04058 1 - 24 NOT IN ATOMS LIST
REMARK 999 2ACE SWS P04058 557 - 586 NOT IN ATOMS LIST
DBREF 2ACE 4 484 SWS P04058 ACES_TORCA 25 505
DBREF 2ACE 490 535 SWS P04058 ACES_TORCA 511 556
SEQADV 2ACE SWS P04058 PRO 506 GAP IN PDB ENTRY
SEQADV 2ACE SWS P04058 HIS 507 GAP IN PDB ENTRY
SEQADV 2ACE SWS P04058 SER 508 GAP IN PDB ENTRY
SEQADV 2ACE SWS P04058 GLN 509 GAP IN PDB ENTRY
SEQADV 2ACE SWS P04058 GLU 510 GAP IN PDB ENTRY
SEQRES 1 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 537 ALA THR ALA CYS
HET ACH 998 10
HETNAM ACH ACETYLCHOLINE
FORMUL 2 ACH C7 H16 N1 O2 1+
FORMUL 3 HOH *204(H2 O1)
HELIX 1 1A SER 79 ASN 85 1 7
HELIX 2 2A GLY 132 GLU 139 1 8
HELIX 3 3A VAL 168 ASN 183 1 16
HELIX 4 4A SER 200 LEU 211 1 12
HELIX 5 5A VAL 238 LEU 252 1 15
HELIX 6 6A ASP 259 GLU 268 1 10
HELIX 7 7A PRO 271 GLU 278 1 8
HELIX 8 8A LEU 305 SER 311 1 7
HELIX 9 9A SER 329 GLY 335 1 7
HELIX 10 10A ARG 349 VAL 360 1 12
HELIX 11 11A ASP 365 THR 376 1 12
HELIX 12 12A GLY 384 VAL 400 1 17
HELIX 13 13A VAL 400 TYR 411 1 12
HELIX 14 14A GLU 443 PHE 448 1 6
HELIX 15 15A ALA 460 THR 479 1 20
HELIX 16 16A VAL 518 THR 535 1 18
SHEET 1 A 3 LEU 6 THR 10 0
SHEET 2 A 3 GLY 13 MET 16 -1 N VAL 15 O VAL 8
SHEET 3 A 3 VAL 57 ALA 60 1 N TRP 58 O LYS 14
SHEET 1 B11 MET 16 PRO 21 0
SHEET 2 B11 HIS 26 PRO 34 -1 O ALA 29 N THR 18
SHEET 3 B11 TYR 96 PRO 102 -1 N ILE 99 O PHE 30
SHEET 4 B11 VAL 142 SER 147 -1 N LEU 143 O TRP 100
SHEET 5 B11 THR 109 TYR 116 1 N MET 112 O VAL 142
SHEET 6 B11 THR 193 GLU 199 1 O THR 195 N VAL 113
SHEET 7 B11 ARG 220 SER 226 1 N ILE 223 O ILE 196
SHEET 8 B11 GLN 318 ASN 324 1 N GLY 322 O LEU 224
SHEET 9 B11 GLY 417 PHE 423 1 N TYR 421 O LEU 321
SHEET 10 B11 PHE 502 LEU 505 1 N ILE 503 O LEU 420
SHEET 11 B11 MET 510 GLN 514 -1 N HIS 513 O PHE 502
SSBOND 1 CYS 67 CYS 94
SSBOND 2 CYS 254 CYS 265
SSBOND 3 CYS 402 CYS 521
LINK C5 ACH 998 OG SER 200
CISPEP 1 SER 103 PRO 104 0 0.18
SITE 1 CAT 3 SER 200 GLU 327 HIS 440
CRYST1 112.410 112.410 136.700 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 0.008896 0.005136 0.000000 0.00000
SCALE2 0.000000 0.010272 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007315 0.00000 |