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HEADER HYDROLASE 20-MAY-04 1VZJ
TITLE STRUCTURE OF THE TETRAMERIZATION DOMAIN OF
TITLE 2 ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF
TITLE 3 WITH A LEFT-HANDED POLYPROLINE HELIX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 SYNONYM: ACETYLCHOLINESTERASE COLLAGENIC TAIL PEPTIDE
COMPND 4 (WAT);
COMPND 5 CHAIN: A, B, C, D, E, F, G, H;
COMPND 6 EC: 3.1.1.7;
COMPND 7 FRAGMENT: C TERMINAL TETRAMERIZATION DOMAIN,
COMPND 8 RESIDUES 575-614;
COMPND 9 OTHER_DETAILS: WAT CHAINS A-D INTERACT WITH PRAD CHAIN I
COMPND 10 WHILE WAT CHAINS E-H INTERACT WITH PRAD CHAIN J;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: ACETYLCHOLINESTERASE COLLAGENIC TAIL PEPTIDE;
COMPND 13 SYNONYM: COLQ, ACETYLCHOLINESTERASE-ASSOCIATED COLLAGEN,
COMPND 14 ACHE Q SUBUNIT;
COMPND 15 CHAIN: I, J;
COMPND 16 FRAGMENT: PRAD PEPTIDE, RESIDUES 53-67;
COMPND 17 OTHER_DETAILS: PROLINE RICH ATTACHMENT DOMAIN (PRAD)
COMPND 18 OF THE ACHE-ASSOCIATED COLLAGEN PROTEIN (COLQ)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 OTHER_DETAILS: THE HUMAN ACHE SEQUENCE OF WAT WAS MODIFIED
SOURCE 6 AT TWO POSITIONS, 21 AND 37, TO REPLACE MET AND CYS BY
SOURCE 7 MSE AND SER, RESPECTIVELY;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 SYNTHETIC: YES
KEYWDS HYDROLASE, ACETYLCHOLINESTERASE, SIGNAL, SYNAPSE,
KEYWDS 2 NEUROTRANSMITTER DEGRADATION, ALTERNATIVE SPLICING,
KEYWDS 3 DISEASE MUTATION.
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DVIR,M.HAREL,S.BON,W.-Q.LIU,M.VIDAL,C.GARBAY,J.L.SUSSMAN,
AUTHOR 2 J.MASSOULIE,I.SILMAN
REVDAT 1 10-JAN-05 1VZJ 0
JRNL AUTH H.DVIR,M.HAREL,S.BON,W.-Q.LIU,M.VIDAL,C.GARBAY,
JRNL AUTH 2 J.L.SUSSMAN,J.MASSOULIE,I.SILMAN
JRNL TITL THE SYNAPTIC ACETYLCHOLINESTERASE TETRAMER
JRNL TITL 2 ASSEMBLES AROUND A POLYPROLINE-II HELIX
JRNL REF EMBO J. V. 23 4394 2004
JRNL REFN ASTM EMJODG UK ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : 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 : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 10000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 12889
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) : 0.247
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 662
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.43
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 59.2
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 800
REMARK 3 BIN R VALUE (WORKING SET) : 0.5169
REMARK 3 BIN FREE R VALUE : 0.4251
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.4
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 36
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.627
REMARK 3 B22 (A**2) : 6.272
REMARK 3 B33 (A**2) : -2.644
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : 1.757
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM SIGMAA (A) : 0.61
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009308
REMARK 3 BOND ANGLES (DEGREES) : 1.20223
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.73127
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88574
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 38.99
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 : WATER_REP.PARAM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VZJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-MAY-2004.
REMARK 100 THE EBI ID CODE IS EBI-14881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-2001
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS BEAMLINE X4A
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU-H3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96672,0.97927,0.97895;
REMARK 200 1.5415
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12935
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.3
REMARK 200 RESOLUTION RANGE LOW (A) : 29
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : 2.7
REMARK 200 R MERGE (I) : 0.054
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.75
REMARK 200 R MERGE FOR SHELL (I) : 0.035
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.47
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% ISOPROPANOL, 10% PEG, 4K
REMARK 280 0.05 M TRISODIUM CITRATE, PH 5.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 29.39500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 E 3 .. 31 A 3 .. 31 0.42
REMARK 295 M 1 F 3 .. 31 B 3 .. 31 0.42
REMARK 295 M 1 G 3 .. 31 C 3 .. 31 0.42
REMARK 295 M 1 H 3 .. 31 D 3 .. 31 0.42
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 10 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: PENTAMERIC
REMARK 300
REMARK 300 HOMOTETRAMER COMPOSED OF DISULFIDE-LINKED HOMODIMERS.
REMARK 300 INTERACTS WITH PRIMA1 TO ANCHOR IT TO THE BASAL LAMINA
REMARK 300 OF CELLS AND ORGANIZE INTO TETRAMERS
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, I, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J, F, G, H
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 CATALYTIC ACTIVITY: ACETYLCHOLINE + H(2)O = CHOLINE + ACETATE.
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 THR A 2
REMARK 465 ASP A 29
REMARK 465 HIS A 30
REMARK 465 TYR A 31
REMARK 465 SER A 32
REMARK 465 LYS A 33
REMARK 465 GLN A 34
REMARK 465 ASP A 35
REMARK 465 ARG A 36
REMARK 465 CYS A 37
REMARK 465 SER A 38
REMARK 465 ASP A 39
REMARK 465 LEU A 40
REMARK 465 SER B 32
REMARK 465 LYS B 33
REMARK 465 GLN B 34
REMARK 465 ASP B 35
REMARK 465 ARG B 36
REMARK 465 CYS B 37
REMARK 465 SER B 38
REMARK 465 ASP B 39
REMARK 465 LEU B 40
REMARK 465 LYS C 33
REMARK 465 GLN C 34
REMARK 465 ASP C 35
REMARK 465 ARG C 36
REMARK 465 CYS C 37
REMARK 465 SER C 38
REMARK 465 ASP C 39
REMARK 465 LEU C 40
REMARK 465 LYS D 33
REMARK 465 GLN D 34
REMARK 465 ASP D 35
REMARK 465 ARG D 36
REMARK 465 CYS D 37
REMARK 465 SER D 38
REMARK 465 ASP D 39
REMARK 465 LEU D 40
REMARK 465 ASP E 1
REMARK 465 ASP E 29
REMARK 465 HIS E 30
REMARK 465 TYR E 31
REMARK 465 SER E 32
REMARK 465 LYS E 33
REMARK 465 GLN E 34
REMARK 465 ASP E 35
REMARK 465 ARG E 36
REMARK 465 CYS E 37
REMARK 465 SER E 38
REMARK 465 ASP E 39
REMARK 465 LEU E 40
REMARK 465 ASP F 35
REMARK 465 ARG F 36
REMARK 465 CYS F 37
REMARK 465 SER F 38
REMARK 465 ASP F 39
REMARK 465 LEU F 40
REMARK 465 ASP G 35
REMARK 465 ARG G 36
REMARK 465 CYS G 37
REMARK 465 SER G 38
REMARK 465 ASP G 39
REMARK 465 LEU G 40
REMARK 465 LYS H 33
REMARK 465 GLN H 34
REMARK 465 ASP H 35
REMARK 465 ARG H 36
REMARK 465 CYS H 37
REMARK 465 SER H 38
REMARK 465 ASP H 39
REMARK 465 LEU H 40
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 ARG C 8 CD NE CZ NH1 NH2
REMARK 470 SER C 32 OG
REMARK 470 GLN F 27 CD OE1 NE2
REMARK 470 GLN F 34 CG CD OE1 NE2
REMARK 470 GLU G 5 CD OE1 OE2
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 TYR D 20 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 SER G 32 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP H 4 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU I 2 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU J 2 CA - CB - CG ANGL. DEV. = 8.9 DEGREES
REMARK 500 PRO J 4 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 525 B Y
REMARK 525 C X
REMARK 525 D W
REMARK 525 E V
REMARK 525 F U
REMARK 525 G T
REMARK 525 H S
REMARK 525 I R
REMARK 525 J Q
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 FASCICULIN-II,GLYCOSYLATED PROTEIN
REMARK 900 RELATED ID: 1F8U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT E202Q OF
REMARK 900 HUMANACETYLCHOLINESTERASE COMPLEXED WITH GREEN
REMARK 900 MAMBA VENOMPEPTIDE FASCICULIN-II
REMARK 900 RELATED ID: 2CLJ RELATED DB: PDB
REMARK 900 HOMOLOGY-BUILT MODEL OF HUMAN
REMARK 900 ACETYLCHOLINESTERASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 37 IN CHAINS A-H HAS BEEN MUTATED TO A CYS FROM A SER
REMARK 999 BUT WAS NOT VISIBLE IN THE ELECTRON DENSITY MAP FOR THIS ENTRY
DBREF 1VZJ A 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ B 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ C 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ D 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ E 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ F 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ G 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ H 1 40 UNP P22303 ACES_HUMAN 575 614
DBREF 1VZJ I 1 15 UNP Q9Y215 COLQ_HUMAN 53 67
DBREF 1VZJ J 1 15 UNP Q9Y215 COLQ_HUMAN 53 67
SEQRES 1 A 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 A 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 A 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 A 40 LEU
SEQRES 1 B 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 B 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 B 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 B 40 LEU
SEQRES 1 C 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 C 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 C 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 C 40 LEU
SEQRES 1 D 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 D 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 D 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 D 40 LEU
SEQRES 1 E 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 E 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 E 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 E 40 LEU
SEQRES 1 F 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 F 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 F 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 F 40 LEU
SEQRES 1 G 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 G 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 G 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 G 40 LEU
SEQRES 1 H 40 ASP THR LEU ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU
SEQRES 2 H 40 PHE HIS ARG TRP SER SER TYR MSE VAL HIS TRP LYS ASN
SEQRES 3 H 40 GLN PHE ASP HIS TYR SER LYS GLN ASP ARG CYS SER ASP
SEQRES 4 H 40 LEU
SEQRES 1 I 15 LEU LEU THR PRO PRO PRO PRO PRO LEU PHE PRO PRO PRO
SEQRES 2 I 15 PHE PHE
SEQRES 1 J 15 LEU LEU THR PRO PRO PRO PRO PRO LEU PHE PRO PRO PRO
SEQRES 2 J 15 PHE PHE
MODRES 1VZJ MSE A 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE B 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE C 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE D 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE E 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE F 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE G 21 MET SELENOMETHIONINE
MODRES 1VZJ MSE H 21 MET SELENOMETHIONINE
HET MSE A 21 8
HET MSE B 21 8
HET MSE C 21 8
HET MSE D 21 8
HET MSE E 21 8
HET MSE F 21 8
HET MSE G 21 8
HET MSE H 21 8
HETNAM MSE SELENOMETHIONINE
FORMUL 11 MSE 8(C5 H11 N1 O2 SE1)
FORMUL 12 HOH *39(H2 O1)
HELIX 1 1 GLU A 5 PHE A 28 1 24
HELIX 2 2 ASP B 1 GLU B 13 1 13
HELIX 3 3 GLU B 13 TYR B 31 1 19
HELIX 4 4 ASP C 1 SER C 32 1 32
HELIX 5 5 ASP D 1 SER D 32 1 32
HELIX 6 6 GLU E 7 PHE E 28 1 22
HELIX 7 7 ASP F 1 GLU F 13 1 13
HELIX 8 8 GLU F 13 GLN F 34 1 22
HELIX 9 9 ASP G 1 HIS G 30 1 30
HELIX 10 10 ASP H 1 TYR H 31 1 31
LINK C TYR A 20 N MSE A 21 1555 1555
LINK C MSE A 21 N VAL A 22 1555 1555
LINK C TYR B 20 N MSE B 21 1555 1555
LINK C MSE B 21 N VAL B 22 1555 1555
LINK C TYR C 20 N MSE C 21 1555 1555
LINK C MSE C 21 N VAL C 22 1555 1555
LINK C TYR D 20 N MSE D 21 1555 1555
LINK C MSE D 21 N VAL D 22 1555 1555
LINK C TYR E 20 N MSE E 21 1555 1555
LINK C MSE E 21 N VAL E 22 1555 1555
LINK C TYR F 20 N MSE F 21 1555 1555
LINK C MSE F 21 N VAL F 22 1555 1555
LINK C TYR G 20 N MSE G 21 1555 1555
LINK C MSE G 21 N VAL G 22 1555 1555
LINK C TYR H 20 N MSE H 21 1555 1555
LINK C MSE H 21 N VAL H 22 1555 1555
CRYST1 53.730 58.790 58.800 90.00 111.38 90.00 P 1 21 1 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 0.018611 0.000000 0.007286 0.00000
SCALE2 0.000000 0.017010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018264 0.00000
MTRIX1 1 -0.988733 0.015964 0.148832 56.38270 1
MTRIX2 1 0.020030 0.999465 0.025859 22.76779 1
MTRIX3 1 -0.148340 0.028549 -0.988524 76.72089 1
TER 243 PHE A 28
TER 540 TYR B 31
TER 837 SER C 32
TER 1131 SER D 32
TER 1381 PHE E 28
TER 1708 GLN F 34
TER 2017 GLN G 34
TER 2332 SER H 32
TER 2453 PHE I 15
TER 2574 PHE J 15
MASTER 378 0 8 10 0 0 0 9 2603 10 80 36
END |