HEADER TRANSFERASE (CARBAMOYL-P,ASPARTATE) 24-MAR-82 2ATC
TITLE CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED ASPARTATE
TITLE 2 CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN;
COMPND 3 CHAIN: A;
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;
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 R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER,B.F.P.EDWARDS,
AUTHOR 2 D.R.EVANS,S.G.WARREN,D.C.WILEY,R.C.LADNER,W.N.LIPSCOMB
REVDAT 10 05-JUN-24 2ATC 1 REMARK SEQADV SSBOND LINK
REVDAT 9 13-JUL-11 2ATC 1 VERSN
REVDAT 8 24-FEB-09 2ATC 1 VERSN
REVDAT 7 01-APR-03 2ATC 1 JRNL
REVDAT 6 15-JUL-92 2ATC 1 SHEET
REVDAT 5 19-APR-89 2ATC 1 REMARK
REVDAT 4 22-OCT-84 2ATC 1 SEQRES
REVDAT 3 30-SEP-83 2ATC 1 REVDAT
REVDAT 2 07-MAR-83 2ATC 1 REMARK
REVDAT 1 07-DEC-82 2ATC 0
JRNL AUTH R.B.HONZATKO,J.L.CRAWFORD,H.L.MONACO,J.E.LADNER,B.F.EWARDS,
JRNL AUTH 2 D.R.EVANS,S.G.WARREN,D.C.WILEY,R.C.LADNER,W.N.LIPSCOMB
JRNL TITL CRYSTAL AND MOLECULAR STRUCTURES OF NATIVE AND CTP-LIGANDED
JRNL TITL 2 ASPARTATE CARBAMOYLTRANSFERASE FROM ESCHERICHIA COLI.
JRNL REF J.MOL.BIOL. V. 160 219 1982
JRNL REFN ISSN 0022-2836
JRNL PMID 6757446
JRNL DOI 10.1016/0022-2836(82)90175-9
REMARK 1
REMARK 1 REFERENCE 1
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 2
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 3
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 4
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 5
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 6
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 TRIPOSPHATE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 75 5276 1978
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 7
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 8
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. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.270
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
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3510
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ATC 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_1000177782.
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 (%): 62.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 SMTRY1 7 1.000000 0.000000 0.000000 65.85000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 38.01852
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.40000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 65.85000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 38.01852
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.40000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 65.85000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 38.01852
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.40000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 65.85000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 38.01852
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 66.40000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 65.85000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 38.01852
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 66.40000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 65.85000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 38.01852
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 66.40000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 76.03703
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 132.80000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 76.03703
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 132.80000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 76.03703
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 132.80000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 76.03703
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 132.80000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 76.03703
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 132.80000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 76.03703
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 132.80000
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 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: 30140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 122010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 0.00000
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 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
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 PRO B 49 CB CG CD
REMARK 470 SER B 50 CB OG
REMARK 470 GLU B 52 CB CG CD OE1 OE2
REMARK 470 MET B 53 CB CG SD CE
REMARK 470 ARG B 55 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 56 CB CG CD CE NZ
REMARK 470 ASP B 57 CB CG OD1 OD2
REMARK 470 LEU B 58 CB CG CD1 CD2
REMARK 470 ILE B 59 CB CG1 CG2 CD1
REMARK 470 LYS B 60 CB CG CD CE NZ
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 153 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 109 SG
REMARK 620 2 CYS B 114 SG 116.9
REMARK 620 3 CYS B 137 SG 95.0 103.2
REMARK 620 4 CYS B 140 SG 109.3 117.6 112.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES BELIEVED TO BE INVOLVED IN THE BINDING
REMARK 800 OF SUBSTRATES
REMARK 800
REMARK 800 SITE_IDENTIFIER: RGB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES WHICH BIND EFFECTOR MOLECULES
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 153
DBREF 2ATC A 1 305 UNP P0A786 PYRB_ECOLI 1 310
DBREF 2ATC B 2 152 UNP P0A7F3 PYRI_ECOLI 1 152
SEQADV 2ATC SER A 7 UNP P0A786 LYS 7 CONFLICT
SEQADV 2ATC GLN A 60 UNP P0A786 GLU 60 CONFLICT
SEQADV 2ATC GLN A 86 UNP P0A786 GLU 86 CONFLICT
SEQADV 2ATC ASN A 90 UNP P0A786 ASP 90 CONFLICT
SEQADV 2ATC GLN A 147 UNP P0A786 GLU 147 CONFLICT
SEQADV 2ATC GLU A 149 UNP P0A786 GLN 149 CONFLICT
SEQADV 2ATC ASN A 153 UNP P0A786 ASP 153 CONFLICT
SEQADV 2ATC GLU A 196 UNP P0A786 GLN 196 CONFLICT
SEQADV 2ATC A UNP P0A786 MET 219 DELETION
SEQADV 2ATC A UNP P0A786 ALA 220 DELETION
SEQADV 2ATC A UNP P0A786 GLU 221 DELETION
SEQADV 2ATC A UNP P0A786 VAL 222 DELETION
SEQADV 2ATC A UNP P0A786 ASP 223 DELETION
SEQADV 2ATC A UNP P0A786 ILE 224 DELETION
SEQADV 2ATC A UNP P0A786 LEU 225 DELETION
SEQADV 2ATC A UNP P0A786 TYR 226 DELETION
SEQADV 2ATC ASX A 234 UNP P0A786 ASN 242 CONFLICT
SEQADV 2ATC LEU A 240 UNP P0A786 VAL 248 CONFLICT
SEQADV 2ATC VAL A 241 UNP P0A786 LEU 249 CONFLICT
SEQADV 2ATC ASN A 244 UNP P0A786 INSERTION
SEQADV 2ATC LEU A 246 UNP P0A786 INSERTION
SEQADV 2ATC GLY A 247 UNP P0A786 INSERTION
SEQADV 2ATC GLY A 248 UNP P0A786 ASP 253 CONFLICT
SEQADV 2ATC MET A 254 UNP P0A786 ALA 259 CONFLICT
SEQADV 2ATC ALA A 256 UNP P0A786 MET 261 CONFLICT
SEQADV 2ATC ASN B 4 UNP P0A7F3 ASP 3 CONFLICT
SEQADV 2ATC ASP B 5 UNP P0A7F3 ASN 4 CONFLICT
SEQADV 2ATC ALA B 10 UNP P0A7F3 GLU 9 CONFLICT
SEQADV 2ATC GLU B 11 UNP P0A7F3 ALA 10 CONFLICT
SEQADV 2ATC ASN B 19 UNP P0A7F3 ASP 18 CONFLICT
SEQADV 2ATC GLU B 24 UNP P0A7F3 GLN 23 CONFLICT
SEQADV 2ATC GLN B 39 UNP P0A7F3 ASP 38 CONFLICT
SEQADV 2ATC ASP B 40 UNP P0A7F3 GLN 39 CONFLICT
SEQADV 2ATC GLU B 70 UNP P0A7F3 GLN 69 CONFLICT
SEQADV 2ATC GLU B 73 UNP P0A7F3 GLN 72 CONFLICT
SEQADV 2ATC ASN B 87 UNP P0A7F3 ASP 86 CONFLICT
SEQADV 2ATC ASP B 88 UNP P0A7F3 ASN 87 CONFLICT
SEQADV 2ATC ASN B 103 UNP P0A7F3 INSERTION
SEQADV 2ATC B UNP P0A7F3 ASN 104 DELETION
SEQADV 2ATC ASP B 111 UNP P0A7F3 ASN 110 CONFLICT
SEQADV 2ATC B UNP P0A7F3 LYS 128 DELETION
SEQADV 2ATC ASP B 131 UNP P0A7F3 ASN 131 CONFLICT
SEQRES 1 A 305 ALA ASN PRO LEU TYR GLN SER HIS ILE ILE SER ILE ASN
SEQRES 2 A 305 ASP LEU SER ARG ASP ASP LEU ASN LEU VAL LEU ALA THR
SEQRES 3 A 305 ALA ALA LYS LEU LYS ALA ASN PRO GLN PRO GLU LEU LEU
SEQRES 4 A 305 LYS HIS LYS VAL ILE ALA SER CYS PHE PHE GLU ALA SER
SEQRES 5 A 305 THR ARG THR ARG LEU SER PHE GLN THR SER MET HIS ARG
SEQRES 6 A 305 LEU GLY ALA SER VAL VAL GLY PHE SER ASP SER ALA ASN
SEQRES 7 A 305 THR SER LEU GLY LYS LYS GLY GLN THR LEU ALA ASN THR
SEQRES 8 A 305 ILE SER VAL ILE SER THR TYR VAL ASP ALA ILE VAL MET
SEQRES 9 A 305 ARG HIS PRO GLN GLU GLY ALA ALA ARG LEU ALA THR GLU
SEQRES 10 A 305 PHE SER GLY ASN VAL PRO VAL LEU ASN ALA GLY ASP GLY
SEQRES 11 A 305 SER ASN GLN HIS PRO THR GLN THR LEU LEU ASP LEU PHE
SEQRES 12 A 305 THR ILE GLN GLN THR GLU GLY ARG LEU ASN ASN LEU HIS
SEQRES 13 A 305 VAL ALA MET VAL GLY ASP LEU LYS TYR GLY ARG THR VAL
SEQRES 14 A 305 HIS SER LEU THR GLN ALA LEU ALA LYS PHE ASP GLY ASN
SEQRES 15 A 305 ARG PHE TYR PHE ILE ALA PRO ASP ALA LEU ALA MET PRO
SEQRES 16 A 305 GLU TYR ILE LEU ASP MET LEU ASP GLU LYS GLY ILE ALA
SEQRES 17 A 305 TRP SER LEU HIS SER SER ILE GLU GLU VAL MET THR ARG
SEQRES 18 A 305 VAL GLN LYS GLU ARG LEU ASP PRO SER GLU TYR ALA ASX
SEQRES 19 A 305 VAL LYS ALA GLN PHE LEU VAL ARG ALA ASN SER LEU GLY
SEQRES 20 A 305 GLY LEU HIS ASN ALA LYS MET ASN ALA LYS VAL LEU HIS
SEQRES 21 A 305 PRO LEU PRO ARG VAL ASP GLU ILE ALA THR ASP VAL ASP
SEQRES 22 A 305 LYS THR PRO HIS ALA TRP TYR PHE GLN GLN ALA GLY ASN
SEQRES 23 A 305 GLY ILE PHE ALA ARG GLN ALA LEU LEU ALA LEU VAL LEU
SEQRES 24 A 305 ASN ARG ASP LEU VAL LEU
SEQRES 1 B 152 MET THR HIS ASN ASP LYS LEU GLN VAL ALA GLU ILE LYS
SEQRES 2 B 152 ARG GLY THR VAL ILE ASN HIS ILE PRO ALA GLU ILE GLY
SEQRES 3 B 152 PHE LYS LEU LEU SER LEU PHE LYS LEU THR GLU THR GLN
SEQRES 4 B 152 ASP ARG ILE THR ILE GLY LEU ASN LEU PRO SER GLY GLU
SEQRES 5 B 152 MET GLY ARG LYS ASP LEU ILE LYS ILE GLU ASN THR PHE
SEQRES 6 B 152 LEU SER GLU ASP GLU VAL ASP GLU LEU ALA LEU TYR ALA
SEQRES 7 B 152 PRO GLN ALA THR VAL ASN ARG ILE ASN ASP TYR GLU VAL
SEQRES 8 B 152 VAL GLY LYS SER ARG PRO SER LEU PRO GLU ARG ASN ILE
SEQRES 9 B 152 ASP VAL LEU VAL CYS PRO ASP SER ASN CYS ILE SER HIS
SEQRES 10 B 152 ALA GLU PRO VAL SER SER SER PHE ALA VAL ARG ARG ALA
SEQRES 11 B 152 ASP ASP ILE ALA LEU LYS CYS LYS TYR CYS GLU LYS GLU
SEQRES 12 B 152 PHE SER HIS ASN VAL VAL LEU ALA ASN
HET ZN B 153 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
HELIX 1 H1A SER A 16 PRO A 34 1CATALYTIC CHAIN 19
HELIX 2 H2A SER A 52 ARG A 65 1CATALYTIC CHAIN 14
HELIX 3 H3A THR A 87 TYR A 98 1CATALYTIC CHAIN 12
HELIX 4 H4A GLY A 110 SER A 119 1CATALYTIC CHAIN 10
HELIX 5 H5A THR A 136 GLU A 149 1CATALYTIC CHAIN 14
HELIX 6 H6A GLY A 166 PHE A 179 1CATALYTIC CHAIN 14
HELIX 7 H7A PRO A 195 GLU A 204 1CATALYTIC CHAIN 10
HELIX 8 H8A ASP A 271 THR A 275 1CATALYTIC CHAIN 5
HELIX 9 H9A TYR A 280 ASN A 300 1CATALYTIC CHAIN 21
HELIX 10 H1B ILE B 25 LYS B 34 1REGULATORY CHAIN 10
HELIX 11 H2B GLU B 68 PRO B 79 1REGULATORY CHAIN 12
HELIX 12 H3B HIS B 146 ALA B 151 1REGULATORY CHAIN 6
SHEET 1 S1A 5 HIS A 8 SER A 11 0
SHEET 2 S1A 5 PRO A 123 GLY A 128 1
SHEET 3 S1A 5 ASP A 100 PRO A 107 1
SHEET 4 S1A 5 HIS A 41 GLU A 50 1
SHEET 5 S1A 5 LEU A 66 SER A 74 1
SHEET 1 S2A 6 GLY A 206 SER A 213 0
SHEET 2 S2A 6 ASP A 180 PRO A 189 1
SHEET 3 S2A 6 ASN A 154 ASP A 162 1
SHEET 4 S2A 6 GLN A 223 PRO A 229 1
SHEET 5 S2A 6 ASN A 255 PRO A 261 1
SHEET 6 S2A 6 HIS A 277 TRP A 279 1
SHEET 1 S3B 5 ASP B 40 ASN B 47 0
SHEET 2 S3B 5 LYS B 13 HIS B 20 1
SHEET 3 S3B 5 LYS B 60 THR B 64 -1
SHEET 4 S3B 5 THR B 82 ASN B 87 1
SHEET 5 S3B 5 VAL B 91 PRO B 97 -1
SHEET 1 S4B 4 GLU B 101 ASP B 105 0
SHEET 2 S4B 4 VAL B 121 ARG B 129 -1
SHEET 3 S4B 4 ILE B 133 CYS B 137 -1
SHEET 4 S4B 4 CYS B 140 PHE B 144 -1
SSBOND 1 CYS B 109 CYS B 114 1555 1555 3.00
SSBOND 2 CYS B 109 CYS B 137 1555 1555 2.90
SSBOND 3 CYS B 109 CYS B 140 1555 1555 2.96
LINK SG CYS B 109 ZN ZN B 153 1555 1555 1.79
LINK SG CYS B 114 ZN ZN B 153 1555 1555 1.73
LINK SG CYS B 137 ZN ZN B 153 1555 1555 2.13
LINK SG CYS B 140 ZN ZN B 153 1555 1555 1.84
CISPEP 1 LEU A 262 PRO A 263 0 7.58
SITE 1 CTA 13 SER A 52 ARG A 54 THR A 55 LYS A 83
SITE 2 CTA 13 LYS A 84 ARG A 105 GLY A 128 HIS A 134
SITE 3 CTA 13 GLN A 137 TYR A 165 ARG A 167 LYS A 224
SITE 4 CTA 13 TYR A 232
SITE 1 RGB 2 LYS B 6 LEU B 7
SITE 1 AC1 4 CYS B 109 CYS B 114 CYS B 137 CYS B 140
CRYST1 131.700 131.700 199.200 90.00 90.00 120.00 H 3 2 18
ORIGX1 1.000000 0.577351 0.000000 0.00000
ORIGX2 0.000000 1.154701 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007593 0.004384 0.000000 0.00000
SCALE2 0.000000 0.008768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005020 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
