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HEADER SERINE HYDROLASE 20-JUN-00 1E3Q
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
TITLE 2 BW284C51
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 ORGAN: ELECTRIC ORGAN;
SOURCE 5 TISSUE: ELECTROPLAQUE
KEYWDS SERINE HYDROLASE, BW284C51, ACETYLCHOLINESTERASE,
KEYWDS 2 HYDROLASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.FELDER,M.HAREL,I.SILMAN,J.L.SUSSMAN
REVDAT 1 03-JUL-00 1E3Q 0
JRNL AUTH C.E.FELDER,M.HAREL,I.SILMAN,J.L.SUSSMAN
JRNL TITL CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED
JRNL TITL 2 WITH BW284C51: COMPARISON WITH THE DECAMETHONIUM
JRNL TITL 3 AND E2020 COMPLEXES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.KRYGER,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 1 TITL 2 E2020 (ARICEPT): IMPLICATIONS FOR THE DESIGN OF NEW
REMARK 1 TITL 3 ANTI-ALZHEIMER DRUGS
REMARK 1 REF STRUCTURE (LONDON) V. 7 297 1999
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.HAREL,I.SCHALK,L.EHRET-SABATTIER,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 2
REMARK 2 RESOLUTION. 2.85 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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 8544140.69
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 22783
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) : 0.190
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 1110
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.5
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2117
REMARK 3 BIN R VALUE (WORKING SET) : 0.386
REMARK 3 BIN FREE R VALUE : 0.393
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 114
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.21
REMARK 3 B22 (A**2) : 4.21
REMARK 3 B33 (A**2) : -8.41
REMARK 3 B12 (A**2) : 11.37
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.90
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) : 1.02
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.7
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.8
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.06
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) : 1.40 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.47 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.01 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.26 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.329151
REMARK 3 BSOL : 48.655
REMARK 3
REMARK 3 NCS MODEL : NONE
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 PARAMETER FILE 3 : BW.PAR
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : BW.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEVERAL RESIDUES ARE NOT SEEN IN THE
REMARK 3 CRYSTAL STRUCTURE, DUE TO DISORDER. THESE INCLUDE ASP 1, ASP 2
REMARK 6 AND THE C-TERMINAL RESIDUES AFTER THR 535.
REMARK 4
REMARK 4 1E3Q COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-JUN-2000.
REMARK 100 THE EBI ID CODE IS EBI-5071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-1991
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : XENTRONICS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48244
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.83
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.104
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.286
REMARK 200 FOR SHELL : 2.8
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.9
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 46.06667
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 92.13333
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 92.13333
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 46.06667
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 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 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 350 BIOMT1 1 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 1 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 138.20000
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 ALA A 536
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 GLU A 89 OE1 OE2
REMARK 470 GLN A 162 CD OE1 NE2
REMARK 470 GLU A 299 CD OE1 OE2
REMARK 470 LYS A 413 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 MET A 43 N - CA - C ANGL. DEV. = -11.2 DEGREES
REMARK 500 SER A 108 N - CA - C ANGL. DEV. = -11.1 DEGREES
REMARK 500 ALA A 157 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 HIS A 159 N - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 PRO A 165 N - CA - C ANGL. DEV. = -11.0 DEGREES
REMARK 500 ALA A 234 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. = -11.1 DEGREES
REMARK 500 LYS A 511 N - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 O HOH Z 1 O HOH Z 73 1564 2.17
REMARK 525
REMARK 525 SOLVENT
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
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 HET GROUP BW (BW284C51), 30 ATOMS
REMARK 600
REMARK 600 C25 C9---C8 O1
REMARK 600 | / \ ||
REMARK 600 C28==C27--C24--N2--C10 O C7--C6--C2--C1-...
REMARK 600 | \ /
REMARK 600 C26 C11--C10
REMARK 600
REMARK 600 C19--C18 C21
REMARK 600 / \ |
REMARK 600 ...-C5--C13--C14 O C17--N1--C22--C23==C29
REMARK 600 \ / |
REMARK 600 C15--C16 C20
REMARK 600
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: IHB
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SITE.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 RELATED ID: 1SOM RELATED DB: PDB
REMARK 900 RELATED ID: 2DX6 RELATED DB: PDB
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
DBREF 1E3Q 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 EBW A 550 30 SEE REMARK 600
HET NAG A 900 15
HET NAG A 901 15
HET NAG A 902 15
HET SO4 A 593 5
HETNAM EBW 4-(5-{4-[DIMETHYL(PROP-2-ENYL)AMMONIO]PHENYL}-3-OXOPENTYL)
HETNAM 2 EBW -N,N-DIMETHYL-N-PROP-2-ENYLBENZENAMINIUM
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETSYN EBW BW284C51
FORMUL 2 EBW C27 H38 N2 O1 2+
FORMUL 3 NAG 3(C8 H15 N1 O6)
FORMUL 4 SO4 O4 S1 2-
FORMUL 5 HOH *132(H2 O1)
HELIX 1 1 PHE A 78 MET A 83 1 6
HELIX 2 2 LEU A 127 ASN A 131 5 5
HELIX 3 3 GLY A 132 GLU A 140 1 9
HELIX 4 4 GLY A 151 LEU A 156 1 6
HELIX 5 5 ASN A 167 ILE A 184 1 18
HELIX 6 6 GLN A 185 PHE A 187 5 3
HELIX 7 7 SER A 200 SER A 212 1 13
HELIX 8 8 SER A 212 ASP A 217 1 6
HELIX 9 9 VAL A 238 LEU A 252 1 15
HELIX 10 10 SER A 258 LYS A 269 1 12
HELIX 11 11 LYS A 270 GLU A 278 1 9
HELIX 12 12 TRP A 279 LEU A 282 5 4
HELIX 13 13 SER A 304 GLY A 312 1 9
HELIX 14 14 GLY A 328 ALA A 336 1 9
HELIX 15 15 GLU A 350 VAL A 360 1 11
HELIX 16 16 ASN A 364 THR A 376 1 13
HELIX 17 17 ASN A 383 VAL A 400 1 18
HELIX 18 18 VAL A 400 LYS A 413 1 14
HELIX 19 19 PRO A 433 GLY A 437 5 5
HELIX 20 20 GLU A 443 PHE A 448 1 6
HELIX 21 21 GLY A 449 VAL A 453 5 5
HELIX 22 22 VAL A 453 ASN A 457 5 5
HELIX 23 23 THR A 459 LYS A 478 1 20
HELIX 24 24 ARG A 517 GLN A 526 1 10
HELIX 25 25 GLN A 526 THR A 535 1 10
SHEET 1 A1 1 LEU A 6 THR A 10 0
SHEET 1 A2 1 GLY A 13 MET A 16 -1 N VAL A 15 O VAL A 8
SHEET 1 A3 1 VAL A 57 ALA A 60 1 N TRP A 58 O LYS A 14
SHEET 1 B1 1 MET A 16 PRO A 21 0
SHEET 1 B2 1 HIS A 26 PRO A 34 -1 O ALA A 29 N THR A 18
SHEET 1 B3 1 TYR A 96 VAL A 101 -1 N ILE A 99 O PHE A 30
SHEET 1 B4 1 VAL A 142 SER A 147 -1 N LEU A 143 O TRP A 100
SHEET 1 B5 1 THR A 109 TYR A 116 1 N MET A 112 O VAL A 142
SHEET 1 B6 1 THR A 193 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 1 B7 1 ARG A 221 SER A 226 1 N ILE A 223 O ILE A 196
SHEET 1 B8 1 GLN A 318 ASN A 324 1 N GLY A 322 O LEU A 224
SHEET 1 B9 1 GLY A 417 PHE A 423 1 N TYR A 421 O LEU A 321
SHEET 1 B10 1 LYS A 501 LEU A 505 1 N ILE A 503 O LEU A 420
SHEET 1 B11 1 MET A 510 GLN A 514 -1 N HIS A 513 O PHE A 502
SSBOND 1 CYS A 67 CYS A 94
SSBOND 2 CYS A 254 CYS A 265
SSBOND 3 CYS A 402 CYS A 521
LINK C1 NAG A 900 ND2 ASN A 59
LINK C1 NAG A 901 ND2 ASN A 416
LINK C1 NAG A 902 ND2 ASN A 457
CISPEP 1 SER A 103 PRO A 104 0 0.49
SITE 1 CAT 3 SER A 200 GLU A 327 HIS A 440
SITE 1 IHB 5 TYR A 70 TRP A 84 TRP A 279 PHE A 330
SITE 2 IHB 5 EBW A 550
CRYST1 114.000 114.000 138.200 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 0.008772 0.005064 0.000000 0.00000
SCALE2 0.000000 0.010129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007236 0.00000 |