HEADER TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 7AT1
TITLE CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH
TITLE 2 PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS
TITLE 3 RESOLUTION AND NEUTRAL P*H
CAVEAT 7AT1 GLC E 2 HAS WRONG CHIRALITY AT ATOM C1 GLC E 2 HAS WRONG
CAVEAT 2 7AT1 CHIRALITY AT ATOM C3 GLC F 2 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 7AT1 GLC F 2 HAS WRONG CHIRALITY AT ATOM C3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE (R STATE), CATALYTIC CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 EC: 2.1.3.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 8 CHAIN: B, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 562
KEYWDS TRANSFERASE (CARBAMOYL-P, ASPARTATE)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB
REVDAT 7 06-MAR-24 7AT1 1 HETSYN
REVDAT 6 29-JUL-20 7AT1 1 CAVEAT COMPND REMARK SEQADV
REVDAT 6 2 1 HET HETNAM FORMUL LINK
REVDAT 6 3 1 SITE ATOM
REVDAT 5 29-NOV-17 7AT1 1 REMARK HELIX
REVDAT 4 13-JUL-11 7AT1 1 VERSN
REVDAT 3 24-FEB-09 7AT1 1 VERSN
REVDAT 2 01-APR-03 7AT1 1 JRNL
REVDAT 1 15-OCT-90 7AT1 0
JRNL AUTH J.E.GOUAUX,R.C.STEVENS,W.N.LIPSCOMB
JRNL TITL CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED
JRNL TITL 2 WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-A
JRNL TITL 3 RESOLUTION AND NEUTRAL PH.
JRNL REF BIOCHEMISTRY V. 29 7702 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2271529
JRNL DOI 10.1021/BI00485A020
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.C.STEVENS,J.E.GOUAUX,W.N.LIPSCOMB
REMARK 1 TITL STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE
REMARK 1 TITL 2 OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE
REMARK 1 TITL 3 UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT
REMARK 1 TITL 4 2.6-ANGSTROMS RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 29 7691 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB
REMARK 1 TITL CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND
REMARK 1 TITL 2 PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF
REMARK 1 TITL 3 ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION
REMARK 1 TITL 4 AND NEUTRAL PH
REMARK 1 REF BIOCHEMISTRY V. 29 389 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB,S.A.MIDDLETON,E.R.KANTROWITZ
REMARK 1 TITL STRUCTURE OF A SINGLE AMINO ACID MUTANT OF ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE AT 2.5-ANGSTROMS RESOLUTION.
REMARK 1 TITL 3 IMPLICATIONS FOR THE COOPERATIVE MECHANISM
REMARK 1 REF BIOCHEMISTRY V. 28 1798 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB
REMARK 1 TITL STRUCTURAL TRANSITIONS IN CRYSTALS OF NATIVE ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 86 845 1989
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 5
REMARK 1 AUTH H.KE,W.N.LIPSCOMB,Y.CHO,R.B.HONZATKO
REMARK 1 TITL COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF
REMARK 1 TITL 3 CONFORMATIONAL CHANGES AND CATALYTIC AND ALLOSTERIC
REMARK 1 TITL 4 MECHANISMS
REMARK 1 REF J.MOL.BIOL. V. 204 725 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH E.R.KANTROWITZ,W.N.LIPSCOMB
REMARK 1 TITL ESCHERICHIA COLI ASPARTATE TRANSCARBAMYLASE. THE RELATION
REMARK 1 TITL 2 BETWEEN STRUCTURE AND FUNCTION
REMARK 1 REF SCIENCE V. 241 669 1988
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 7
REMARK 1 AUTH J.E.GOUAUX,W.N.LIPSCOMB
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF CARBAMOYL PHOSPHATE AND
REMARK 1 TITL 2 SUCCINATE BOUND TO ASPARTATE CARBAMOYLTRANSFERASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 85 4205 1988
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 8
REMARK 1 AUTH K.H.KIM,Z.PAN,R.B.HONZATKO,H.KE,W.N.LIPSCOMB
REMARK 1 TITL STRUCTURAL ASYMMETRY IN THE CTP-LIGANDED FORM OF ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 196 853 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 9
REMARK 1 AUTH K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB
REMARK 1 TITL 2.5 ANGSTROMS STRUCTURE OF ASPARTATE CARBAMOYLTRANSFERASE
REMARK 1 TITL 2 COMPLEXED WITH THE BISUBSTRATE ANALOG
REMARK 1 TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE
REMARK 1 REF J.MOL.BIOL. V. 193 527 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 10
REMARK 1 AUTH J.E.GOUAUX,K.L.KRAUSE,W.N.LIPSCOMB
REMARK 1 TITL THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE. A MOLECULAR MODELLING STUDY
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 142 893 1987
REMARK 1 REFN ISSN 0006-291X
REMARK 1 REFERENCE 11
REMARK 1 AUTH K.L.KRAUSE,K.W.VOLZ,W.N.LIPSCOMB
REMARK 1 TITL STRUCTURE AT 2.9-ANGSTROMS RESOLUTION OF ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE COMPLEXED WITH THE BISUBSTRATE ANALOGUE
REMARK 1 TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 82 1643 1985
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 12
REMARK 1 AUTH H.KE,R.B.HONZATKO,W.N.LIPSCOMB
REMARK 1 TITL STRUCTURE OF UNLIGATED ASPARTATE CARBAMOYLTRANSFERASE OF
REMARK 1 TITL 2 ESCHERICHIA COLI AT 2.6-ANGSTROMS RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 81 4037 1984
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 13
REMARK 1 AUTH R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER,
REMARK 1 AUTH 2 B.F.P.EDWARDS,D.R.EVANS,S.G.WARREN,D.C.WILEY,R.C.LADNER,
REMARK 1 AUTH 3 W.N.LIPSCOMB
REMARK 1 TITL CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED
REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 160 219 1982
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 14
REMARK 1 AUTH R.B.HONZATKO,W.N.LIPSCOMB
REMARK 1 TITL INTERACTIONS OF PHOSPHATE LIGANDS WITH ESCHERICHIA COLI
REMARK 1 TITL 2 ASPARTATE CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE
REMARK 1 REF J.MOL.BIOL. V. 160 265 1982
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 15
REMARK 1 AUTH R.B.HONZATKO,W.N.LIPSCOMB
REMARK 1 TITL INTERACTIONS OF METAL-NUCLEOTIDE COMPLEXES WITH ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE IN THE CRYSTALLINE STATE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 79 7171 1982
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 16
REMARK 1 AUTH J.E.LADNER,J.P.KITCHELL,R.B.HONZATKO,H.M.KE,K.W.VOLZ,
REMARK 1 AUTH 2 A.J.KALB(GILBOA),R.C.LADNER,W.N.LIPSCOMB
REMARK 1 TITL GROSS QUATERNARY CHANGES IN ASPARTATE CARBAMOYLTRANSFERASE
REMARK 1 TITL 2 ARE INDUCED BY THE BINDING OF
REMARK 1 TITL 3 N-(PHOSPHONACETYL)-L-ASPARTATE. A 3.5-ANGSTROMS RESOLUTION
REMARK 1 TITL 4 STUDY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 79 3125 1982
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 17
REMARK 1 AUTH R.B.HONZATKO,H.L.MONACO,W.N.LIPSCOMB
REMARK 1 TITL A 3.0-ANGSTROMS RESOLUTION STUDY OF NUCLEOTIDE COMPLEXES
REMARK 1 TITL 2 WITH ASPARTATE CARBAMOYLTRANSFERASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 76 5105 1979
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 18
REMARK 1 AUTH H.L.MONACO,J.L.CRAWFORD,W.N.LIPSCOMB
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF ASPARTATE
REMARK 1 TITL 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI AND OF ITS
REMARK 1 TITL 3 COMPLEX WITH CYTIDINE TRIPHOSPHATE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 75 5276 1978
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 19
REMARK 1 AUTH W.N.LIPSCOMB,B.F.P.EDWARDS,D.R.EVANS,S.C.PASTRA-LANDIS
REMARK 1 TITL BINDING SITE AT 5.5 ANGSTROMS RESOLUTION OF CYTIDINE
REMARK 1 TITL 2 TRIPHOSPHATE, THE ALLOSTERIC INHIBITOR OF ASPARTATE
REMARK 1 TITL 3 TRANSCARBAMYLASE FROM ESCHERICHIA COLI. RELATION TO
REMARK 1 TITL 4 MECHANISMS OF CONTROL
REMARK 1 EDIT M.SUNDARALINGAM, S.T.RAO
REMARK 1 REF STRUCTURE AND CONFORMATION 333 1975
REMARK 1 REF 2 OF NUCLEIC ACIDS AND
REMARK 1 REF 3 PROTEIN-NUCLEIC ACID
REMARK 1 REF 4 INTERACTIONS : PROCEEDINGS
REMARK 1 REF 5 OF THE FOURTH ANNUAL HARRY
REMARK 1 REF 6 STEENBOCK SYMPOSIUM, JUNE
REMARK 1 REF 7 16-19, 1974, MADISON,
REMARK 1 REF 8 WISCONSIN
REMARK 1 PUBL UNIVERSITY PARK PRESS,BALTIMORE
REMARK 1 REFN
REMARK 1 REFERENCE 20
REMARK 1 AUTH S.G.WARREN,B.F.P.EDWARDS,D.R.EVANS,D.C.WILEY,W.N.LIPSCOMB
REMARK 1 TITL ASPARTATE TRANSCARBAMOYLASE FROM ESCHERICHIA COLI. ELECTRON
REMARK 1 TITL 2 DENSITY AT 5.5 ANGSTROMS RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 70 1117 1973
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 3.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7AT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTALS WERE GROWN IN A SOLUTION
REMARK 280 OF PHOSPHONACETAMIDE (PAM) AND MALONATE (MAL) AT PH 5.8. THEY
REMARK 280 WERE THEN SOAKED IN A SOLUTION CONTAINING PAM, MAL, AND ATP AT
REMARK 280 PH 7.0.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+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 -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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS, WHICH IS SPECIFIED
REMARK 300 ON THE *MTRIX* RECORDS BELOW, RELATES THE *A* AND *B*
REMARK 300 CHAINS TO THE *C* AND *D* CHAINS.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 33650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 101400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 2 -0.500000 -0.866025 0.000000 122.50000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 61.25000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 106.08811
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 3
REMARK 465 ASP B 4
REMARK 465 ASN B 5
REMARK 465 LYS B 6
REMARK 465 LEU B 7
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 HIS D 3
REMARK 465 ASP D 4
REMARK 465 ASN D 5
REMARK 465 LYS D 6
REMARK 465 LEU D 7
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 O4 GLC E 1 O5 GLC E 2 2.15
REMARK 500 O4 GLC F 1 O5 GLC F 2 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 41 NE2 HIS A 41 CD2 -0.067
REMARK 500 HIS A 64 NE2 HIS A 64 CD2 -0.071
REMARK 500 HIS A 106 NE2 HIS A 106 CD2 -0.074
REMARK 500 HIS A 134 NE2 HIS A 134 CD2 -0.067
REMARK 500 HIS A 212 NE2 HIS A 212 CD2 -0.067
REMARK 500 HIS A 265 NE2 HIS A 265 CD2 -0.076
REMARK 500 HIS A 282 NE2 HIS A 282 CD2 -0.076
REMARK 500 HIS B 117 NE2 HIS B 117 CD2 -0.073
REMARK 500 HIS B 147 NE2 HIS B 147 CD2 -0.076
REMARK 500 HIS C 8 NE2 HIS C 8 CD2 -0.068
REMARK 500 HIS C 64 NE2 HIS C 64 CD2 -0.083
REMARK 500 HIS C 156 NE2 HIS C 156 CD2 -0.079
REMARK 500 HIS C 170 NE2 HIS C 170 CD2 -0.068
REMARK 500 HIS C 212 NE2 HIS C 212 CD2 -0.070
REMARK 500 HIS C 255 NE2 HIS C 255 CD2 -0.070
REMARK 500 HIS C 265 NE2 HIS C 265 CD2 -0.070
REMARK 500 HIS C 282 NE2 HIS C 282 CD2 -0.072
REMARK 500 HIS D 20 NE2 HIS D 20 CD2 -0.074
REMARK 500 HIS D 117 NE2 HIS D 117 CD2 -0.070
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 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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 54 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 54 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 98 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 MET A 104 CG - SD - CE ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TYR A 165 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TRP A 209 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 269 CB - CG - CD ANGL. DEV. = -16.7 DEGREES
REMARK 500 TRP A 284 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP A 284 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 306 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 VAL A 309 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 VAL A 309 O - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG B 55 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ALA B 152 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 TYR C 98 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG C 105 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG C 151 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG C 183 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TRP C 209 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP C 209 CB - CG - CD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 TRP C 209 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG C 234 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 MET C 261 CG - SD - CE ANGL. DEV. = -10.5 DEGREES
REMARK 500 TRP C 284 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP C 284 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG D 14 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 85 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG D 102 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASN D 105 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 6 9.44 50.01
REMARK 500 THR A 53 -74.03 -126.84
REMARK 500 ARG A 54 -82.53 -46.05
REMARK 500 ASN A 132 -79.47 -94.32
REMARK 500 HIS A 134 75.46 -150.92
REMARK 500 PRO A 237 -36.00 -36.54
REMARK 500 ALA A 259 0.71 -63.72
REMARK 500 LEU A 267 157.74 66.17
REMARK 500 VAL A 270 -94.24 -116.67
REMARK 500 VAL B 9 -138.55 51.09
REMARK 500 LYS B 13 -75.34 -66.27
REMARK 500 GLN B 24 -55.73 96.87
REMARK 500 LYS B 34 49.28 -65.49
REMARK 500 ASN B 47 67.11 60.38
REMARK 500 ASN B 88 71.44 31.05
REMARK 500 ASN B 105 -43.47 70.47
REMARK 500 ARG B 130 -81.04 -100.39
REMARK 500 ALA B 131 25.69 -159.16
REMARK 500 ASN B 132 -62.05 -178.81
REMARK 500 ASP B 133 -169.51 -120.13
REMARK 500 TYR B 140 -70.54 -81.76
REMARK 500 ALA B 152 173.85 60.41
REMARK 500 GLN C 35 72.14 -116.16
REMARK 500 THR C 53 -70.74 -102.56
REMARK 500 ALA C 77 -29.46 -39.28
REMARK 500 ASN C 132 -77.49 -80.25
REMARK 500 HIS C 134 73.05 -153.68
REMARK 500 LEU C 267 155.47 70.60
REMARK 500 VAL C 270 -128.38 -115.01
REMARK 500 GLU D 10 179.99 86.54
REMARK 500 GLN D 24 -26.98 73.22
REMARK 500 SER D 50 83.02 -158.22
REMARK 500 GLU D 68 -59.67 -27.31
REMARK 500 TYR D 89 -10.95 60.17
REMARK 500 ASN D 105 16.87 34.88
REMARK 500 PRO D 120 67.41 -59.99
REMARK 500 ASP D 133 -167.65 -173.69
REMARK 500 TYR D 140 -67.98 -92.81
REMARK 500 ALA D 152 96.39 -61.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 5 0.09 SIDE CHAIN
REMARK 500 TYR A 240 0.09 SIDE CHAIN
REMARK 500 TYR B 89 0.07 SIDE CHAIN
REMARK 500 TYR C 165 0.08 SIDE CHAIN
REMARK 500 TYR C 226 0.08 SIDE CHAIN
REMARK 500 PHE D 27 0.09 SIDE CHAIN
REMARK 500 TYR D 77 0.10 SIDE CHAIN
REMARK 500 TYR D 89 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THERE ARE NO ATP COORDINATES FOR THE D CHAIN BECAUSE THERE
REMARK 600 WAS NOT SUFFICIENT DENSITY TO BUILD THE MOLECULE INTO THE
REMARK 600 ELECTRON DENSITY MAPS.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GLC E 2
REMARK 610 GLC F 2
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 109 SG
REMARK 620 2 CYS B 114 SG 121.2
REMARK 620 3 CYS B 138 SG 115.7 105.8
REMARK 620 4 CYS B 141 SG 103.0 107.5 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 109 SG
REMARK 620 2 CYS D 114 SG 121.9
REMARK 620 3 CYS D 138 SG 110.2 105.9
REMARK 620 4 CYS D 141 SG 105.3 110.9 100.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PMA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITES OF COMBINED *PCT* AND *MAL*
REMARK 800 MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF
REMARK 800 SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE
REMARK 800 IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: zn binding site
REMARK 800
REMARK 800 SITE_IDENTIFIER: ATB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ALLOSTERIC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: PMC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITES OF COMBINED *PCT* AND *MAL*
REMARK 800 MOLECULES. SITE ACTUALLY CONTAIN AN ADDITIONAL TWO RESIDUES OF
REMARK 800 SYMMETRY RELATED. THE OTHER RESIDUES, SER A 80, AND LYS A 84 ARE
REMARK 800 IN AN ADJACENT (THREE-FOLD RELATED) CATALYTIC CHAIN.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZND
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: zn binding site
DBREF 7AT1 A 1 310 UNP P0A786 PYRB_ECOLI 1 310
DBREF 7AT1 B 2 153 UNP P0A7F3 PYRI_ECOLI 1 152
DBREF 7AT1 C 1 310 UNP P0A786 PYRB_ECOLI 1 310
DBREF 7AT1 D 2 153 UNP P0A7F3 PYRI_ECOLI 1 152
SEQADV 7AT1 GLN A 60 UNP P0A786 GLU 60 CONFLICT
SEQADV 7AT1 GLN A 147 UNP P0A786 GLU 147 CONFLICT
SEQADV 7AT1 GLU A 149 UNP P0A786 GLN 149 CONFLICT
SEQADV 7AT1 GLU A 196 UNP P0A786 GLN 196 CONFLICT
SEQADV 7AT1 GLY B 8 UNP P0A7F3 GLN 7 CONFLICT
SEQADV 7AT1 GLN C 60 UNP P0A786 GLU 60 CONFLICT
SEQADV 7AT1 GLN C 147 UNP P0A786 GLU 147 CONFLICT
SEQADV 7AT1 GLU C 149 UNP P0A786 GLN 149 CONFLICT
SEQADV 7AT1 GLU C 196 UNP P0A786 GLN 196 CONFLICT
SEQADV 7AT1 GLY D 8 UNP P0A7F3 GLN 7 CONFLICT
SEQRES 1 A 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 A 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 A 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 A 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 A 310 THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG
SEQRES 6 A 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 A 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 A 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 A 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 A 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 A 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 A 310 THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 A 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 A 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 A 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 A 310 GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 A 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 A 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 A 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 A 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 A 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 A 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 A 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 A 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 B 153 MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS
SEQRES 2 B 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 B 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 B 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 B 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 B 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 B 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 B 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 B 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 B 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 B 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 B 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
SEQRES 1 C 310 ALA ASN PRO LEU TYR GLN LYS HIS ILE ILE SER ILE ASN
SEQRES 2 C 310 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 C 310 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 C 310 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 C 310 THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG
SEQRES 6 C 310 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 C 310 THR SER LEU GLY LYS LYS GLY GLU THR LEU ALA ASP THR
SEQRES 8 C 310 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 C 310 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 C 310 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 C 310 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 C 310 THR ILE GLN GLN THR GLU GLY ARG LEU ASP ASN LEU HIS
SEQRES 13 C 310 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 C 310 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 C 310 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 C 310 GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 C 310 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET ALA GLU
SEQRES 18 C 310 VAL ASP ILE LEU TYR MET THR ARG VAL GLN LYS GLU ARG
SEQRES 19 C 310 LEU ASP PRO SER GLU TYR ALA ASN VAL LYS ALA GLN PHE
SEQRES 20 C 310 VAL LEU ARG ALA SER ASP LEU HIS ASN ALA LYS ALA ASN
SEQRES 21 C 310 MET LYS VAL LEU HIS PRO LEU PRO ARG VAL ASP GLU ILE
SEQRES 22 C 310 ALA THR ASP VAL ASP LYS THR PRO HIS ALA TRP TYR PHE
SEQRES 23 C 310 GLN GLN ALA GLY ASN GLY ILE PHE ALA ARG GLN ALA LEU
SEQRES 24 C 310 LEU ALA LEU VAL LEU ASN ARG ASP LEU VAL LEU
SEQRES 1 D 153 MET THR HIS ASP ASN LYS LEU GLY VAL GLU ALA ILE LYS
SEQRES 2 D 153 ARG GLY THR VAL ILE ASP HIS ILE PRO ALA GLN ILE GLY
SEQRES 3 D 153 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR ASP
SEQRES 4 D 153 GLN ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 D 153 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 D 153 LEU SER GLU ASP GLN VAL ASP GLN LEU ALA LEU TYR ALA
SEQRES 7 D 153 PRO GLN ALA THR VAL ASN ARG ILE ASP ASN TYR GLU VAL
SEQRES 8 D 153 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ILE ASP
SEQRES 9 D 153 ASN VAL LEU VAL CYS PRO ASN SER ASN CYS ILE SER HIS
SEQRES 10 D 153 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG LYS ARG
SEQRES 11 D 153 ALA ASN ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS
SEQRES 12 D 153 GLU PHE SER HIS ASN VAL VAL LEU ALA ASN
HET GLC E 1 1
HET GLC E 2 6
HET GLC F 1 1
HET GLC F 2 6
HET PCT A 311 8
HET ZN B 154 1
HET ATP B 155 31
HET PCT C 311 8
HET ZN D 154 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM PCT PHOSPHONOACETAMIDE
HETNAM ZN ZINC ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 5 GLC 4(C6 H12 O6)
FORMUL 7 PCT 2(C2 H6 N O4 P)
FORMUL 8 ZN 2(ZN 2+)
FORMUL 9 ATP C10 H16 N5 O13 P3
HELIX 1 H1A ARG A 17 ALA A 32 1 16
HELIX 2 H2A THR A 53 LEU A 66 1 14
HELIX 3 H3A ALA A 89 VAL A 99 1 11
HELIX 4 H4A ALA A 111 SER A 119 1 9
HELIX 5 H5A PRO A 135 GLU A 149 1 15
HELIX 6 H6A ARG A 167 PHE A 179 1 13
HELIX 7 H7A GLU A 196 LYS A 205 1 10
HELIX 8 H8A ILE A 215 ALA A 220 1 6
HELIX 9 H0A ALA A 251 ASN A 256 1 6
HELIX 10 HEA THR A 275 LYS A 279 1 5
HELIX 11 HTA TYR A 285 LEU A 304 1 20
HELIX 12 H1B ILE B 25 PHE B 33 1 9
HELIX 13 H2B ASP B 69 TYR B 77 5ENDS TYPE 1 9
HELIX 14 H3B HIS B 147 VAL B 150 1 4
HELIX 15 H1C ARG C 17 ALA C 32 1 16
HELIX 16 H2C THR C 53 LEU C 66 1 14
HELIX 17 H3C ALA C 89 VAL C 99 1 11
HELIX 18 H4C ALA C 111 SER C 119 1 9
HELIX 19 H5C PRO C 135 GLU C 149 1 15
HELIX 20 H6C ARG C 167 PHE C 179 1 13
HELIX 21 H7C GLU C 196 LYS C 205 1 10
HELIX 22 H8C ILE C 215 ALA C 220 1 6
HELIX 23 H0C ALA C 251 ASN C 256 1 6
HELIX 24 HEC THR C 275 LYS C 279 1 5
HELIX 25 HTC TYR C 285 LEU C 304 1 20
HELIX 26 H1D ILE D 25 PHE D 33 1 9
HELIX 27 H2D ASP D 69 TYR D 77 5ENDS TYPE 1 9
HELIX 28 H3D HIS D 147 VAL D 150 1 4
SHEET 1 C1A 5 LYS A 7 ILE A 9 0
SHEET 2 C1A 5 PRO A 123 ALA A 127 1
SHEET 3 C1A 5 ALA A 101 HIS A 106 1
SHEET 4 C1A 5 LYS A 42 PHE A 48 1
SHEET 5 C1A 5 ALA A 68 SER A 74 1
SHEET 1 C2A 6 ALA A 208 HIS A 212 0
SHEET 2 C2A 6 ASN A 182 ALA A 188 1
SHEET 3 C2A 6 LEU A 155 VAL A 160 1
SHEET 4 C2A 6 ILE A 224 VAL A 230 1
SHEET 5 C2A 6 LYS A 262 HIS A 265 1
SHEET 6 C2A 6 PRO A 281 ALA A 283 1
SHEET 1 R1B 5 ARG B 41 LEU B 46 0
SHEET 2 R1B 5 ARG B 55 GLU B 62 -1
SHEET 3 R1B 5 ARG B 14 ASP B 19 -1
SHEET 4 R1B 5 THR B 82 ASP B 87 -1
SHEET 5 R1B 5 GLY B 93 PRO B 97 -1
SHEET 1 R2B 4 GLU B 101 ASP B 104 0
SHEET 2 R2B 4 SER B 123 LYS B 129 -1
SHEET 3 R2B 4 ILE B 134 CYS B 138 -1
SHEET 4 R2B 4 LYS B 143 SER B 146 -1
SHEET 1 C1C 5 LYS C 7 ILE C 9 0
SHEET 2 C1C 5 PRO C 123 ALA C 127 1
SHEET 3 C1C 5 ALA C 101 HIS C 106 1
SHEET 4 C1C 5 LYS C 42 PHE C 48 1
SHEET 5 C1C 5 ALA C 68 SER C 74 1
SHEET 1 C2C 6 ALA C 208 HIS C 212 0
SHEET 2 C2C 6 ASN C 182 ALA C 188 1
SHEET 3 C2C 6 LEU C 155 VAL C 160 1
SHEET 4 C2C 6 ILE C 224 VAL C 230 1
SHEET 5 C2C 6 LYS C 262 HIS C 265 1
SHEET 6 C2C 6 PRO C 281 ALA C 283 1
SHEET 1 R1D 5 ARG D 41 LEU D 46 0
SHEET 2 R1D 5 ARG D 55 GLU D 62 -1
SHEET 3 R1D 5 ARG D 14 ASP D 19 -1
SHEET 4 R1D 5 THR D 82 ASP D 87 -1
SHEET 5 R1D 5 GLY D 93 PRO D 97 -1
SHEET 1 R2D 4 GLU D 101 ASP D 104 0
SHEET 2 R2D 4 SER D 123 LYS D 129 -1
SHEET 3 R2D 4 ILE D 134 CYS D 138 -1
SHEET 4 R2D 4 LYS D 143 SER D 146 -1
LINK O4 GLC E 1 C1 GLC E 2 1555 1555 1.24
LINK O4 GLC F 1 C1 GLC F 2 1555 1555 1.22
LINK SG CYS B 109 ZN ZN B 154 1555 1555 2.33
LINK SG CYS B 114 ZN ZN B 154 1555 1555 2.35
LINK SG CYS B 138 ZN ZN B 154 1555 1555 2.34
LINK SG CYS B 141 ZN ZN B 154 1555 1555 2.31
LINK SG CYS D 109 ZN ZN D 154 1555 1555 2.36
LINK SG CYS D 114 ZN ZN D 154 1555 1555 2.32
LINK SG CYS D 138 ZN ZN D 154 1555 1555 2.38
LINK SG CYS D 141 ZN ZN D 154 1555 1555 2.32
CISPEP 1 LEU A 267 PRO A 268 0 -4.81
CISPEP 2 LEU C 267 PRO C 268 0 -5.34
SITE 1 PMA 10 ARG A 54 THR A 55 ARG A 105 HIS A 134
SITE 2 PMA 10 GLN A 137 ARG A 167 ARG A 229 GLN A 231
SITE 3 PMA 10 PRO A 266 LEU A 267
SITE 1 ZNB 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 ATB 12 GLY B 8 VAL B 9 GLU B 10 ALA B 11
SITE 2 ATB 12 ILE B 12 ASP B 19 HIS B 20 LYS B 56
SITE 3 ATB 12 LYS B 60 ASN B 84 TYR B 89 LYS B 94
SITE 1 PMC 10 ARG C 54 THR C 55 ARG C 105 HIS C 134
SITE 2 PMC 10 GLN C 137 ARG C 167 ARG C 229 GLN C 231
SITE 3 PMC 10 PRO C 266 LEU C 267
SITE 1 ZND 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
CRYST1 122.500 122.500 156.500 90.00 90.00 120.00 P 3 2 1 12
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 0.008163 0.004713 0.000000 0.00000
SCALE2 0.000000 0.009426 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006390 0.00000
MTRIX1 1 -0.109515 -0.993509 0.030771 102.21250 1
MTRIX2 1 -0.993693 0.108679 -0.027637 92.59020 1
MTRIX3 1 0.024113 -0.033603 -0.999144 80.22470 1
(ATOM LINES ARE NOT SHOWN.)
END