HEADER TRANSFERASE 14-AUG-92 1RAD
TITLE CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE
TITLE 2 AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE
TITLE 3 MECHANISM OF NEGATIVE COOPERATIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ASPARTATE TRANSCARBAMYLASE, ATCASE;
COMPND 5 EC: 2.1.3.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 9 CHAIN: B, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: PYRB, B4245, JW4204;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 83333;
SOURCE 9 STRAIN: K12;
SOURCE 10 GENE: PYRI, B4244, JW4203
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.P.KOSMAN,J.E.GOUAUX,W.N.LIPSCOMB
REVDAT 7 14-FEB-24 1RAD 1 REMARK LINK
REVDAT 6 29-NOV-17 1RAD 1 HELIX
REVDAT 5 02-JUL-14 1RAD 1 COMPND SOURCE DBREF REMARK
REVDAT 4 13-JUL-11 1RAD 1 VERSN
REVDAT 3 24-FEB-09 1RAD 1 VERSN
REVDAT 2 01-APR-03 1RAD 1 JRNL
REVDAT 1 31-JAN-94 1RAD 0
JRNL AUTH R.P.KOSMAN,J.E.GOUAUX,W.N.LIPSCOMB
JRNL TITL CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE
JRNL TITL 2 TRANSCARBAMOYLASE AT 2.5 A RESOLUTION: IMPLICATIONS FOR
JRNL TITL 3 ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY.
JRNL REF PROTEINS V. 15 147 1993
JRNL REFN ISSN 0887-3585
JRNL PMID 8441751
JRNL DOI 10.1002/PROT.340150206
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 2.6 ANGSTROMS
REMARK 1 TITL 4 RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 29 7691 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.H.KIM,Z.PAN,R.B.HONZATKO,H.-M.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 3
REMARK 1 AUTH H.K.SCHACHMAN,C.D.PAUZA,M.NAVRE,M.J.KARELS,L.WU,Y.R.YANG
REMARK 1 TITL LOCATION OF AMINO ACID ALTERATIONS IN MUTANTS OF ASPARTATE
REMARK 1 TITL 2 TRANSCARBAMOYLASE: STRUCTURAL ASPECTS OF INTERALLELIC
REMARK 1 TITL 3 COMPLEMENTATION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 81 115 1984
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.A.HOOVER,W.D.ROOF,K.F.FOLTERMANN,G.A.O'DONOVAN,
REMARK 1 AUTH 2 D.A.BENCINI,J.R.WILD
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF THE STRUCTURAL GENE (PYRB) THAT
REMARK 1 TITL 2 ENCODES THE CATALYTIC POLYPEPTIDE OF ASPARTATE
REMARK 1 TITL 3 TRANSCARBAMOYLASE OF ESCHERICHIA COLI
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 80 2462 1983
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 5
REMARK 1 AUTH W.H.KONIGSBERG,L.HENDERSON
REMARK 1 TITL AMINO ACID SEQUENCE OF THE CATALYTIC SUBUNIT OF ASPARTATE
REMARK 1 TITL 2 TRANSCARBAMOYLASE FROM ESCHERICHIA COLI
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 80 2467 1983
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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) : 0.189
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 : 7222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 93
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) : 3.726
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 1RAD 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_1000175966.
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 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: 35840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 105990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -0.500000 -0.866025 0.000000 122.13000
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 61.06500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 105.76768
REMARK 350 BIOMT3 3 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 GLN B 8 CB CG CD OE1 NE2
REMARK 470 GLN D 8 CB CG CD OE1 NE2
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 -0.068
REMARK 500 GLU A 60 CD GLU A 60 OE2 0.080
REMARK 500 HIS A 106 NE2 HIS A 106 CD2 -0.076
REMARK 500 GLU A 147 CD GLU A 147 OE2 0.077
REMARK 500 HIS A 156 NE2 HIS A 156 CD2 -0.067
REMARK 500 HIS A 212 NE2 HIS A 212 CD2 -0.069
REMARK 500 HIS B 20 NE2 HIS B 20 CD2 -0.068
REMARK 500 HIS B 147 NE2 HIS B 147 CD2 -0.076
REMARK 500 HIS C 8 NE2 HIS C 8 CD2 -0.066
REMARK 500 HIS C 64 NE2 HIS C 64 CD2 -0.071
REMARK 500 HIS C 106 NE2 HIS C 106 CD2 -0.066
REMARK 500 HIS C 134 NE2 HIS C 134 CD2 -0.073
REMARK 500 GLU C 147 CD GLU C 147 OE2 0.083
REMARK 500 HIS C 170 NE2 HIS C 170 CD2 -0.072
REMARK 500 HIS C 212 NE2 HIS C 212 CD2 -0.074
REMARK 500 HIS D 147 NE2 HIS D 147 CD2 -0.069
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 TYR A 5 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 VAL A 43 CG1 - CB - CG2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 SER A 80 N - CA - C ANGL. DEV. = 20.8 DEGREES
REMARK 500 LEU A 81 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 LYS A 83 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET A 159 CA - CB - CG ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP A 209 CD1 - CG - CD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 TRP A 209 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP A 209 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 MET A 227 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 234 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TRP A 284 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TRP A 284 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 VAL A 303 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 MET B 1 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ALA B 11 N - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 LEU B 30 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 GLU B 52 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 GLU B 52 CA - C - N ANGL. DEV. = -18.7 DEGREES
REMARK 500 MET B 53 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU B 66 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 GLN B 80 CA - CB - CG ANGL. DEV. = -15.0 DEGREES
REMARK 500 VAL B 106 N - CA - CB ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG B 128 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 133 N - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 PRO C 34 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG C 54 CA - CB - CG ANGL. DEV. = 17.8 DEGREES
REMARK 500 ARG C 56 CB - CG - CD ANGL. DEV. = -18.7 DEGREES
REMARK 500 ARG C 56 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG C 65 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 SER C 80 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 THR C 97 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 TYR C 98 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG C 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 GLN C 174 CA - CB - CG ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG C 183 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG C 183 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 TRP C 209 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP C 209 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 75 ANGLE DEVIATIONS.
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 THR A 79 106.19 -12.09
REMARK 500 SER A 80 -44.29 0.63
REMARK 500 LYS A 83 -71.70 45.94
REMARK 500 LYS A 84 123.77 150.05
REMARK 500 HIS A 134 63.67 -159.21
REMARK 500 GLN A 231 94.95 -66.98
REMARK 500 ARG A 234 40.13 -104.83
REMARK 500 VAL A 243 106.84 -54.88
REMARK 500 LYS A 244 -124.66 67.16
REMARK 500 GLN A 246 -178.85 63.96
REMARK 500 LEU A 267 153.59 64.97
REMARK 500 VAL A 270 -61.30 -11.79
REMARK 500 ASP A 271 -16.50 -153.11
REMARK 500 THR B 2 135.35 175.81
REMARK 500 HIS B 3 70.60 -4.48
REMARK 500 ASP B 4 -71.48 -48.19
REMARK 500 ASN B 5 -159.62 61.30
REMARK 500 LYS B 6 -0.27 -152.84
REMARK 500 ALA B 11 110.19 2.16
REMARK 500 ARG B 14 127.17 58.10
REMARK 500 GLN B 24 16.08 53.99
REMARK 500 LYS B 34 44.47 38.56
REMARK 500 GLU B 37 54.91 -92.96
REMARK 500 ASN B 47 75.34 40.91
REMARK 500 PRO B 49 60.62 -100.96
REMARK 500 SER B 50 -155.61 -161.38
REMARK 500 GLU B 52 91.54 -69.11
REMARK 500 MET B 53 -34.01 -137.81
REMARK 500 GLU B 68 -71.16 53.52
REMARK 500 ASN B 105 -21.97 60.38
REMARK 500 PRO B 120 41.08 -60.54
REMARK 500 LYS B 129 77.18 65.45
REMARK 500 ALA B 131 -17.47 41.84
REMARK 500 ASP B 133 83.18 120.45
REMARK 500 ILE B 134 121.17 -1.84
REMARK 500 SER C 52 87.88 -155.20
REMARK 500 ASP C 75 -138.04 -138.39
REMARK 500 ALA C 77 61.09 178.88
REMARK 500 ASN C 78 43.12 7.78
REMARK 500 SER C 80 -4.72 9.61
REMARK 500 LYS C 84 -100.88 70.31
REMARK 500 TYR C 98 5.31 -153.18
REMARK 500 ASN C 132 -90.26 -97.92
REMARK 500 HIS C 134 63.37 -159.84
REMARK 500 VAL C 243 -28.83 -19.98
REMARK 500 ALA C 245 16.74 -67.79
REMARK 500 GLN C 246 58.83 -99.19
REMARK 500 HIS C 255 -56.80 -14.90
REMARK 500 HIS C 265 117.24 -162.68
REMARK 500 LEU C 267 160.09 73.42
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU D 48 PRO D 49 145.16
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 PHE A 48 0.08 SIDE CHAIN
REMARK 500 TYR A 98 0.16 SIDE CHAIN
REMARK 500 PHE A 143 0.09 SIDE CHAIN
REMARK 500 TYR A 185 0.10 SIDE CHAIN
REMARK 500 TYR A 226 0.07 SIDE CHAIN
REMARK 500 TYR A 240 0.11 SIDE CHAIN
REMARK 500 ARG A 296 0.08 SIDE CHAIN
REMARK 500 TYR B 89 0.13 SIDE CHAIN
REMARK 500 TYR B 140 0.10 SIDE CHAIN
REMARK 500 TYR C 5 0.08 SIDE CHAIN
REMARK 500 TYR C 98 0.08 SIDE CHAIN
REMARK 500 PHE C 286 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 112.3
REMARK 620 3 CYS B 138 SG 113.9 107.0
REMARK 620 4 CYS B 141 SG 101.7 111.7 110.3
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 113.5
REMARK 620 3 CYS D 138 SG 117.6 105.0
REMARK 620 4 CYS D 141 SG 102.1 111.4 107.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE OF CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZND
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE OF CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP D 999
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AMINO ACID SEQUENCE OF ESCHERICHIA COLI ATCASE USED IN
REMARK 999 THIS ENTRY REPRESENTS A DEPARTURE FROM THE SEQUENCE USED IN
REMARK 999 PREVIOUS ATCASE STRUCTURES FROM THE SAME LABORATORY. THE
REMARK 999 NEW AMINO ACID ASSIGNMENTS FOR FIVE OF THE RESIDUES IN EACH
REMARK 999 CATALYTIC-REGULATORY SUBUNIT ARE NOW IN ACCORD WITH THE
REMARK 999 DNA-DETERMINED AMINO ACID SEQUENCE MOST RECENTLY DEFINED
REMARK 999 FOR THIS ENZYME. THE CHANGES ARE AS FOLLOWS:
REMARK 999
REMARK 999 PREVIOUS PRESENT
REMARK 999 GLN A 60 GLU A 60
REMARK 999 GLN A 147 GLU A 147
REMARK 999 GLU A 149 GLN A 149
REMARK 999 GLU A 196 GLN A 196
REMARK 999 GLY B 8 GLN B 8
REMARK 999 GLN C 60 GLU C 60
REMARK 999 GLN C 147 GLU C 147
REMARK 999 GLU C 149 GLN C 149
REMARK 999 GLU C 196 GLN C 196
REMARK 999 GLY D 8 GLN D 8
REMARK 999
REMARK 999 GLN 8 IS THE ONLY RESIDUE WHICH INVOLVED MORE THAN A SINGLE
REMARK 999 ATOM CHANGE AND, AS A RESULT, IT IS THE ONLY RESIDUE IN
REMARK 999 THIS LIST WHICH REQUIRED A REEXAMINATION OF THE
REMARK 999 CRYSTALLOGRAPHIC DATA IN ADDITION TO THE REEXAMINATION OF
REMARK 999 THE CHEMICAL ENVIRONMENT THAT WAS PERFORMED FOR ALL OF
REMARK 999 THESE RESIDUES. OMIT MAPS BASED ON THE CTP-LIGATED ENZYME
REMARK 999 DATA (SEE PAPER CITED ON *JRNL* RECORDS ABOVE) WERE
REMARK 999 CREATED, AND IN BOTH RESIDUES WITHIN THE ASYMMETRIC UNIT
REMARK 999 (GLN B 8 AND GLN D 8) ELECTRON DENSITY CONSISTENT WITH THE
REMARK 999 GLUTAMINE SIDE CHAINS WAS IDENTIFIED, ALTHOUGH IT WAS NOT
REMARK 999 POSSIBLE TO POSITION THE SIDE CHAINS WITH CERTAINTY IN THIS
REMARK 999 ELECTRON DENSITY. CONSEQUENTLY, GLN 8 IS IDENTIFIED
REMARK 999 PROPERLY AS A GLUTAMINE BUT IT LACKS THE SIDE CHAIN ATOMS.
REMARK 999 THERE IS STILL AN UNRESOLVED CONFLICT IN THE LITERATURE
REMARK 999 REGARDING THE IDENTITY OF RESIDUE 220 OF THE CATALYTIC
REMARK 999 CHAIN (SEE THE PAPERS CITED AS REFERENCES 3 - 5 ABOVE).
REMARK 999 SINCE THERE WAS NO UNEQUIVOCAL CRYSTALLOGRAPHIC EVIDENCE
REMARK 999 FOR A VALINE AT THIS POSITION (REFERENCES 4 AND 5), ALA
REMARK 999 (REFERENCE 3) WAS LEFT IN THIS SITE.
DBREF 1RAD A 1 310 UNP P0A786 PYRB_ECOLI 2 311
DBREF 1RAD B 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
DBREF 1RAD C 1 310 UNP P0A786 PYRB_ECOLI 2 311
DBREF 1RAD D 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
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 GLU 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 GLU THR GLN 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 GLN 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 GLN 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 GLU 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 GLU THR GLN 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 GLN 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 GLN 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 ZN B 154 1
HET CTP B 999 29
HET ZN D 154 1
HET CTP D 999 29
HETNAM ZN ZINC ION
HETNAM CTP CYTIDINE-5'-TRIPHOSPHATE
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CTP 2(C9 H16 N3 O14 P3)
FORMUL 9 HOH *93(H2 O)
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 GLN A 149 1 15
HELIX 6 H6A ARG A 167 PHE A 179 1 13
HELIX 7 H7A GLN A 196 LYS A 205 1 10
HELIX 8 H8A ILE A 215 ALA A 220 1 6
HELIX 9 H9A ALA A 251 ASN A 256 1 6
HELIX 10 H0A THR A 275 LYS A 279 1 5
HELIX 11 HEA 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 GLN C 149 1 15
HELIX 20 H6C ARG C 167 PHE C 179 1 13
HELIX 21 H7C GLN C 196 LYS C 205 1 10
HELIX 22 H8C ILE C 215 ALA C 220 1 6
HELIX 23 H9C ALA C 251 ASN C 256 1 6
HELIX 24 H0C THR C 275 LYS C 279 1 5
HELIX 25 HEC 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 SG CYS B 109 ZN ZN B 154 1555 1555 2.35
LINK SG CYS B 114 ZN ZN B 154 1555 1555 2.30
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 2.33
LINK SG CYS D 114 ZN ZN D 154 1555 1555 2.27
LINK SG CYS D 138 ZN ZN D 154 1555 1555 2.30
LINK SG CYS D 141 ZN ZN D 154 1555 1555 2.33
CISPEP 1 LEU A 267 PRO A 268 0 3.83
CISPEP 2 LEU C 267 PRO C 268 0 -2.96
SITE 1 ZNB 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 ZND 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
SITE 1 AC1 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 AC2 4 CYS D 109 CYS D 114 CYS D 138 CYS D 141
SITE 1 AC3 7 VAL B 9 ALA B 11 ILE B 12 LYS B 60
SITE 2 AC3 7 TYR B 89 VAL B 91 LYS B 94
SITE 1 AC4 10 GLU D 10 ALA D 11 ILE D 12 ASP D 19
SITE 2 AC4 10 THR D 82 ASN D 84 TYR D 89 GLU D 90
SITE 3 AC4 10 VAL D 91 LYS D 94
CRYST1 122.130 122.130 142.510 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 0.008188 0.004727 0.000000 0.00000
SCALE2 0.000000 0.009455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007017 0.00000
(ATOM LINES ARE NOT SHOWN.)
END