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HEADER SERINE HYDROLASE 26-JAN-99 1EEA
TITLE TETRAMERIC ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM
TITLE 2 ELECTROPHORUS ELECTRICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.7;
COMPND 5 BIOLOGICAL_UNIT: TETRAMER IN SOLUTION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ELECTROPHORUS ELECTRICUS;
SOURCE 3 ORGANISM_COMMON: ELECTRIC EEL;
SOURCE 4 VARIANT: A4 FORM;
SOURCE 5 ORGAN: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS SERINE HYDROLASE, ALPHA/BETA HYDROLASE, TETRAMER
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.RAVES,K.GILES,J.D.SCHRAG,M.F.SCHMID,G.N.PHILLIPS
AUTHOR 2 JUNIOR,W.CHIU,A.J.HOWARD,I.SILMAN,J.L.SUSSMAN
REVDAT 1 27-JAN-99 1EEA 0
JRNL AUTH M.L.RAVES,K.GILES,J.D.SCHRAG,M.F.SCHMID,
JRNL AUTH 2 G.N.PHILLIPS,C.WAH,A.J.HOWARD,I.SILMAN,J.L.SUSSMAN
JRNL TITL QUATERNARY STRUCTURE OF TETRAMERIC
JRNL TITL 2 ACETYLCHOLINESTERASE
JRNL EDIT B.P.DOCTOR,D.M.QUINN,R.L.ROTUNDO,P.TAYLOR,
JRNL REF STRUCTURE AND FUNCTION OF 1998
JRNL REF 2 CHOLINESTERASES AND RELATED
JRNL REF 3 PROTEINS
JRNL PUBL PLENUM PUBLISHING CORPORATION NEW YORK
JRNL REFN 9999
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.GILES
REMARK 1 TITL INTERACTIONS UNDERLYING SUBUNIT ASSOCIATION IN
REMARK 1 TITL 2 CHOLINESTERASES
REMARK 1 REF PROTEIN ENG. V. 10 677 1997
REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859
REMARK 1 REFERENCE 2
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 3
REMARK 1 AUTH J.D.SCHRAG,M.F.SCHMID,D.G.MORGAN,
REMARK 1 AUTH 2 W.G.N.P.JUNIORCHIU,L.TANG
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 ANALYSIS OF 11S ACETYLCHOLINESTERASE
REMARK 1 REF J.BIOL.CHEM. V. 263 9795 1988
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 2
REMARK 2 RESOLUTION. 4.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NONE
REMARK 3 AUTHORS : NONE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO REFINEMENT WAS CARRIED OUT ON
REMARK 3 THE MODEL. FINAL MODEL IS MOLECULAR REPLACEMENT SOLUTION
REMARK 3 FOR SEARCH MODEL 2ACE.
REMARK 4
REMARK 4 1EEA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 5
REMARK 5 WARNING
REMARK 5 1EEA: THIS IS LAYER 1 RELEASE.
REMARK 5
REMARK 5 PLEASE NOTE THAT THIS ENTRY WAS RELEASED AFTER DEPOSITOR
REMARK 5 CHECKING AND APPROVAL BUT WITHOUT PDB STAFF INTERVENTION.
REMARK 5 AN AUXILIARY FILE, AUX1EEA.RPT, IS AVAILABLE FROM THE
REMARK 5 PDB FTP SERVER AND IS ACCESSIBLE THROUGH THE 3DB BROWSER.
REMARK 5 THE FILE CONTAINS THE OUTPUT OF THE PROGRAM WHAT_CHECK AND
REMARK 5 OTHER DIAGNOSTICS.
REMARK 5
REMARK 5 NOMENCLATURE IN THIS ENTRY, INCLUDING HET RESIDUE NAMES
REMARK 5 AND HET ATOM NAMES, HAS NOT BEEN STANDARDIZED BY THE PDB
REMARK 5 PROCESSING STAFF. A LAYER 2 ENTRY WILL BE RELEASED SHORTLY
REMARK 5 AFTER THIS STANDARDIZATION IS COMPLETED AND APPROVED BY THE
REMARK 5 DEPOSITOR. THE LAYER 2 ENTRY WILL BE TREATED AS A
REMARK 5 CORRECTION TO THIS ONE, WITH THE APPROPRIATE REVDAT RECORD.
REMARK 5
REMARK 5 FURTHER INFORMATION INCLUDING VALIDATION CRITERIA USED IN
REMARK 5 CHECKING THIS ENTRY AND A LIST OF MANDATORY DATA FIELDS
REMARK 5 ARE AVAILABLE FROM THE PDB WEB SITE AT
REMARK 5 HTTP://WWW.PDB.BNL.GOV/.
REMARK 6
REMARK 6 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE IS AN A4
REMARK 6 TETRAMER IN SOLUTION. THE ASYMMETRIC UNIT CONTAINS A
REMARK 6 MONOMER, WITH THE CRYSTALLOGRAPHIC TWO-FOLD AXES RELATING
REMARK 6 THE FOUR MONOMERS.
REMARK 7
REMARK 7 ONLY ONE MONOMER WAS FOUND TO OCCUPY THE ASYMMETRIC UNIT.
REMARK 7 THE FULL PACKING OF THE UNIT CELL (16 MONOMERS, 4
REMARK 7 TETRAMERS) SHOWS LARGE VOIDS THAT COULD EASILY BE OCCUPIED
REMARK 7 BY FOUR MORE TETRAMERS BY SIMPLE TRANSLATION OF THE
REMARK 7 OBTAINED TETRAMERS BY HALF THE C AXIS. REFINEMENT DOES NOT
REMARK 7 AGREE WITH TWO MONOMERS IN THE ASYMMETRIC UNIT.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-1987
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.0
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 : ROTATING ANODE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE
REMARK 200 DETECTOR MANUFACTURER : XENTRONICS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : X-GEN
REMARK 200 DATA SCALING SOFTWARE : X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9717
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.5
REMARK 200 RESOLUTION RANGE LOW (A) : 34.3
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.097
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.5
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.7
REMARK 200 R MERGE FOR SHELL (I) : 0.272
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.0
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,1/2+Y,1/2+Z
REMARK 290 6555 -X,1/2-Y,1/2+Z
REMARK 290 7555 -X,1/2+Y,1/2-Z
REMARK 290 8555 X,1/2-Y,1/2-Z
REMARK 290 9555 1/2+X,Y,1/2+Z
REMARK 290 10555 1/2-X,-Y,1/2+Z
REMARK 290 11555 1/2-X,Y,1/2-Z
REMARK 290 12555 1/2+X,-Y,1/2-Z
REMARK 290 13555 1/2+X,1/2+Y,Z
REMARK 290 14555 1/2-X,1/2-Y,Z
REMARK 290 15555 1/2-X,1/2+Y,-Z
REMARK 290 16555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 100.72522
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 117.89672
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 100.72522
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 117.89672
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.72522
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 117.89672
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 100.72522
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 117.89672
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 117.89672
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 117.89672
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 117.89672
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 117.89672
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 100.72522
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 100.72522
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 100.72522
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 70.43246
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 100.72522
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO 485
REMARK 465 HIS 486
REMARK 465 SER 487
REMARK 465 GLN 488
REMARK 465 GLU 489
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 CG ND1 CE1 NE2 CD2
REMARK 470 ASN 42 CG OD1 ND2
REMARK 470 ARG 47 CD NE CZ NH1 NH2
REMARK 470 GLU 49 CD OE1 OE2
REMARK 470 ARG 88 CZ NH1 NH2
REMARK 470 GLU 89 CD OE1 OE2
REMARK 470 ASN 257 CG OD1 ND2
REMARK 470 GLU 260 CG CD OE1 OE2
REMARK 470 GLU 268 CD OE1 OE2
REMARK 470 LYS 270 CD CE NZ
REMARK 470 GLU 299 CD OE1 OE2
REMARK 470 LYS 325 NZ
REMARK 470 GLU 344 CD OE1 OE2
REMARK 470 GLU 350 CD OE1 OE2
REMARK 470 MET 353 SD CE
REMARK 470 ASP 365 CG OD1 OD2
REMARK 470 ASN 382 CG OD1 ND2
REMARK 470 GLU 434 CD OE1 OE2
REMARK 470 GLU 455 CD OE1 OE2
REMARK 470 GLU 461 CD OE1 OE2
REMARK 470 GLU 484 CD OE1 OE2
REMARK 470 LYS 498 NZ
REMARK 470 GLU 499 CD OE1 OE2
REMARK 470 GLU 508 CD OE1 OE2
REMARK 470 ARG 515 CZ NH1 NH2
REMARK 470 GLN 526 CD 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. 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 CG ARG 515 SD MET 379 2555 0.62
REMARK 500 CD ARG 515 SD MET 379 2555 1.08
REMARK 500 CE1 PHE 186 CE LYS 14 14555 1.17
REMARK 500 CD ARG 515 CG MET 379 2555 1.51
REMARK 500 CZ PHE 186 CE LYS 14 14555 1.53
REMARK 500 NZ LYS 530 OD2 ASP 369 2555 1.62
REMARK 500 CE1 PHE 186 NZ LYS 14 14555 1.63
REMARK 500 NE ARG 515 CB MET 379 2555 1.76
REMARK 500 CD ARG 515 CB MET 379 2555 1.87
REMARK 500 CB PHE 527 CD2 LEU 373 2555 1.91
REMARK 500 NE ARG 19 NE ARG 19 8555 1.94
REMARK 500 CB ARG 515 SD MET 379 2555 1.94
REMARK 500 NE2 GLN 500 CE MET 379 2555 2.00
REMARK 500 NE ARG 515 SD MET 379 2555 2.06
REMARK 500 CD1 PHE 186 NZ LYS 14 14555 2.11
REMARK 500 CD GLN 500 CE MET 379 2555 2.17
REMARK 500 CG ARG 515 CE MET 379 2555 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION
REMARK 500 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 0 LEU 97 CA - CB - CG ANGL. DEV. = 20.2 DEGREES
REMARK 500 0 ASN 167 C-1 - N - CA ANGL. DEV. = 25.5 DEGREES
REMARK 500 0 VAL 168 C - CA - CB ANGL. DEV. = 15.6 DEGREES
REMARK 500 0 ARG 216 CD - NE - CZ ANGL. DEV. = 17.4 DEGREES
REMARK 500 0 ARG 267 CD - NE - CZ ANGL. DEV. = 17.2 DEGREES
REMARK 500 0 GLU 278 CB - CG - CD ANGL. DEV. = 17.0 DEGREES
REMARK 500 0 ASP 285 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 0 ASP 285 C - CA - CB ANGL. DEV. = 19.3 DEGREES
REMARK 500 0 VAL 293 N - CA - CB ANGL. DEV. = 21.8 DEGREES
REMARK 500 0 VAL 293 C - CA - CB ANGL. DEV. = 17.1 DEGREES
REMARK 500 0 LEU 305 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 0 ILE 347 CB - CG1 - CD1 ANGL. DEV. = 15.9 DEGREES
REMARK 500 0 LEU 391 C - CA - CB ANGL. DEV. = 16.5 DEGREES
REMARK 500 0 GLU 434 CA - CB - CG ANGL. DEV. = 22.1 DEGREES
REMARK 500 0 LEU 494 CA - CB - CG ANGL. DEV. = 20.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE LISTED IN THE SEQRES RECORD
REMARK 999 IS OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE,
REMARK 999 (CORRESPONDING TO THE STRUCTURE)
REMARK 999 NOT OF ELECTROPHORUS ELECTRICUS. AT THE RESOLUTION
REMARK 999 OF THE EXPERIMENTAL DATA (4.5 A) NO SEQUENCE
REMARK 999 DISCREPANCIES CAN BE SEEN.
DBREF 1EEA 4 484 SWS P04058 ACES_TORCA 25 505
DBREF 1EEA 490 535 SWS P04058 ACES_TORCA 511 556
SEQADV 1EEA SWS P04058 PRO 506 GAP IN PDB ENTRY
SEQADV 1EEA SWS P04058 HIS 507 GAP IN PDB ENTRY
SEQADV 1EEA SWS P04058 SER 508 GAP IN PDB ENTRY
SEQADV 1EEA SWS P04058 GLN 509 GAP IN PDB ENTRY
SEQADV 1EEA SWS P04058 GLU 510 GAP IN PDB ENTRY
SEQRES 1 534 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 534 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 534 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 534 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 534 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 534 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 534 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 534 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 534 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 534 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 534 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 534 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 534 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 534 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 534 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 534 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 534 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 534 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 534 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 534 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 534 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 534 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 534 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 534 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 534 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 534 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 534 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 534 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 534 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 534 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 534 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 534 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 534 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 534 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 534 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 534 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 534 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 534 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 534 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 534 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 534 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 534 ALA
HELIX 1 1 GLY 41 MET 43 5 3
HELIX 2 2 SER 79 TRP 84 1 6
HELIX 3 3 ASP 128 TYR 130 5 3
HELIX 4 4 LYS 133 GLU 139 1 7
HELIX 5 5 GLY 151 PHE 155 1 5
HELIX 6 6 VAL 168 PHE 186 1 19
HELIX 7 7 ALA 201 LEU 211 1 11
HELIX 8 8 ARG 216 LEU 218 5 3
HELIX 9 9 VAL 238 ASN 251 1 14
HELIX 10 10 ASP 259 GLU 268 1 10
HELIX 11 11 PRO 271 ASN 280 1 10
HELIX 12 12 LEU 305 SER 311 1 7
HELIX 13 13 SER 329 GLY 335 1 7
HELIX 14 14 ARG 349 SER 359 1 11
HELIX 15 15 ASP 365 TYR 375 1 11
HELIX 16 16 GLY 384 ASN 399 1 16
HELIX 17 17 ILE 401 LYS 413 1 13
HELIX 18 18 GLU 434 MET 436 5 3
HELIX 19 19 ILE 444 VAL 447 1 4
HELIX 20 20 LEU 450 LEU 452 5 3
HELIX 21 21 LYS 454 LEU 456 5 3
HELIX 22 22 ALA 460 THR 479 1 20
HELIX 23 23 VAL 518 ASN 525 1 8
HELIX 24 24 PHE 527 LEU 532 1 6
SHEET 1 A 3 LEU 7 THR 10 0
SHEET 2 A 3 GLY 13 MET 16 -1 N VAL 15 O VAL 8
SHEET 3 A 3 VAL 57 ASN 59 1 N TRP 58 O LYS 14
SHEET 1 B11 THR 18 PRO 21 0
SHEET 2 B11 HIS 26 PHE 30 -1 N ALA 29 O THR 18
SHEET 3 B11 LEU 97 VAL 101 -1 N VAL 101 O SER 28
SHEET 4 B11 VAL 142 LEU 146 -1 N SER 145 O ASN 98
SHEET 5 B11 VAL 111 ILE 115 1 N MET 112 O VAL 142
SHEET 6 B11 VAL 194 GLU 199 1 N THR 195 O VAL 111
SHEET 7 B11 ARG 221 GLN 225 1 N ARG 221 O ILE 196
SHEET 8 B11 ILE 319 ASN 324 1 N LEU 320 O ALA 222
SHEET 9 B11 THR 418 PHE 423 1 N TYR 419 O ILE 319
SHEET 10 B11 LYS 501 LEU 505 1 N ILE 503 O PHE 422
SHEET 11 B11 VAL 512 GLN 514 -1 N HIS 513 O PHE 502
SHEET 1 C 2 SER 235 SER 237 0
SHEET 2 C 2 PRO 294 ILE 296 1 N PRO 294 O VAL 236
CISPEP 1 SER 103 PRO 104 0 2.22
CRYST1 140.860 201.460 235.770 90.00 90.00 90.00 F 2 2 2 16
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 0.007099 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004241 0.00000 |