HEADER TRANSFERASE 12-MAY-00 1EZZ
TITLE CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT
TITLE 2 IN THE T-STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ASPARTATE TRANSCARBAMOYLASE CATALYTIC CHAIN;
COMPND 5 EC: 2.1.3.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: ASPARTATE TRANSCARBAMOYLASE REGULATORY CHAIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PEK412, A PLASMID WITH THE PYRBI GENES
SOURCE 7 INSERTED INTO PUC119;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PEK412, A PLASMID WITH THE PYRBI GENES
SOURCE 14 INSERTED INTO PUC119
KEYWDS ASPARTATE TRANSCARBAMOYLASE, ASPARTATE CARBAMOYLTRANSFERASE, CIS-
KEYWDS 2 PROLINE, CIS-AMINO ACID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JIN,B.STEC,E.R.KANTROWITZ
REVDAT 4 07-FEB-24 1EZZ 1 REMARK
REVDAT 3 03-NOV-21 1EZZ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1EZZ 1 VERSN
REVDAT 1 22-NOV-00 1EZZ 0
JRNL AUTH L.JIN,B.STEC,E.R.KANTROWITZ
JRNL TITL A CIS-PROLINE TO ALANINE MUTANT OF E. COLI ASPARTATE
JRNL TITL 2 TRANSCARBAMOYLASE: KINETIC STUDIES AND THREE-DIMENSIONAL
JRNL TITL 3 CRYSTAL STRUCTURES.
JRNL REF BIOCHEMISTRY V. 39 8058 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10891088
JRNL DOI 10.1021/BI000418+
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-A
REMARK 1 TITL 4 RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 29 7691 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 29421
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2900
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 : 7228
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.10
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.860
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.570
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 1EZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 295.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : UCSD MARK III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34422
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.2960
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.17
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME: 24 MG/ML; 1:1 ENZYME TO-BUFFER
REMARK 280 RATIO, BUFFER: 20 MM HEPES, 14% (W/V) PEG 1450, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+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 1.000000 0.000000 0.000000 64.93500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.49024
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.11333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 64.93500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 37.49024
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 66.11333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 64.93500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 37.49024
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.11333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.98048
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 132.22667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 74.98048
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 132.22667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 74.98048
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 132.22667
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 BIOLOGICAL ASSEMBLY IS A DODECAMER. THE ENTIRE MOLECULE
REMARK 300 REQUIRES TWO SYMMETRY PARTNERS GENERATED BY ROTATIONS AROUND THE
REMARK 300 THREE-FOLD
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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 338 LIES ON A SPECIAL POSITION.
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 GLU A 60 CD GLU A 60 OE2 0.069
REMARK 500 GLU A 147 CD GLU A 147 OE2 0.079
REMARK 500 GLU C 147 CD GLU C 147 OE2 0.072
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 PRO A 3 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO A 34 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP B 4 N - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 PRO B 79 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 LEU C 225 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 PRO C 281 C - N - CA ANGL. DEV. = 9.1 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 ILE A 10 -67.11 -127.99
REMARK 500 ALA A 32 -71.45 -79.56
REMARK 500 LEU A 39 51.00 -109.95
REMARK 500 HIS A 41 -7.59 76.59
REMARK 500 SER A 52 54.73 -164.18
REMARK 500 THR A 53 -68.24 -16.66
REMARK 500 ARG A 56 -72.83 -82.66
REMARK 500 LEU A 57 -55.15 -28.32
REMARK 500 LEU A 66 25.02 -64.70
REMARK 500 ASP A 75 -178.96 65.58
REMARK 500 SER A 76 108.70 -176.32
REMARK 500 ALA A 77 84.50 -162.13
REMARK 500 THR A 79 -90.18 -155.26
REMARK 500 SER A 80 -144.85 -115.10
REMARK 500 ASN A 132 -88.25 -68.73
REMARK 500 HIS A 134 78.14 -173.88
REMARK 500 MET A 194 125.99 -30.86
REMARK 500 GLN A 196 -69.45 -14.45
REMARK 500 TYR A 197 -38.49 -39.14
REMARK 500 ILE A 215 -49.22 -18.96
REMARK 500 GLU A 216 -43.89 -29.50
REMARK 500 LYS A 232 -18.65 -44.53
REMARK 500 LYS A 244 81.22 -62.35
REMARK 500 ALA A 245 -30.39 -151.02
REMARK 500 PHE A 247 39.33 -83.57
REMARK 500 VAL A 248 -152.59 -120.93
REMARK 500 LEU A 249 89.41 -173.19
REMARK 500 HIS A 255 -72.47 -2.04
REMARK 500 ALA A 257 131.85 -29.30
REMARK 500 LEU A 267 165.17 72.92
REMARK 500 THR B 2 51.05 22.38
REMARK 500 HIS B 3 -111.92 -106.56
REMARK 500 LYS B 6 -149.55 -147.55
REMARK 500 LEU B 7 82.56 174.23
REMARK 500 GLN B 8 -80.70 -131.22
REMARK 500 VAL B 9 113.55 -10.75
REMARK 500 LYS B 13 -157.30 179.06
REMARK 500 HIS B 20 90.12 95.85
REMARK 500 LEU B 30 -28.39 -38.36
REMARK 500 PHE B 33 70.30 -100.03
REMARK 500 LYS B 34 90.82 -14.11
REMARK 500 ASP B 39 49.93 -144.37
REMARK 500 ARG B 41 115.86 -18.86
REMARK 500 ASN B 47 39.27 79.80
REMARK 500 GLU B 52 29.12 -157.40
REMARK 500 MET B 53 -12.67 75.53
REMARK 500 LYS B 56 -144.35 -143.51
REMARK 500 ASN B 63 55.76 74.49
REMARK 500 ALA B 75 -94.94 -24.05
REMARK 500 LEU B 76 -55.13 -22.15
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
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 226 0.06 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 313 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 109 SG
REMARK 620 2 CYS B 114 SG 116.6
REMARK 620 3 CYS B 138 SG 120.8 109.6
REMARK 620 4 CYS B 141 SG 105.6 109.8 90.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 314 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 109 SG
REMARK 620 2 CYS D 114 SG 127.8
REMARK 620 3 CYS D 138 SG 118.5 107.7
REMARK 620 4 CYS D 141 SG 97.8 104.4 91.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 314
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6AT1 RELATED DB: PDB
REMARK 900 6AT1 IS WILD-TYPE STRUCTURE OF ASPARTATE TRANSCARBAMOYLASE T STATE
REMARK 900 WITH NO MUTATION AT POSITION 268
REMARK 900 RELATED ID: 1D09 RELATED DB: PDB
REMARK 900 1D09 IS WILD-TYPE STRUCTURE OF ASPARTATE TRANSCARBAMOYLASE R STATE
REMARK 900 WITH NO MUTATION AT POSITION 268 IN THE PRESENCE OF N-
REMARK 900 PHOSPHONACETYL-L-ASPARTATE
REMARK 900 RELATED ID: 1F1B RELATED DB: PDB
REMARK 900 1F1B IS ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE R-STATE IN
REMARK 900 THE PRESENCE OF N-PHOSPHONACETYL-L-ASPARTATE
DBREF 1EZZ A 1 310 UNP P0A786 PYRB_ECOLI 1 310
DBREF 1EZZ C 1 310 UNP P0A786 PYRB_ECOLI 1 310
DBREF 1EZZ B 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
DBREF 1EZZ D 1 153 UNP P0A7F3 PYRI_ECOLI 1 153
SEQADV 1EZZ ALA A 268 UNP P0A786 PRO 268 ENGINEERED MUTATION
SEQADV 1EZZ ALA C 268 UNP P0A786 PRO 268 ENGINEERED MUTATION
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 ALA 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 ALA 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 313 1
HET ZN D 314 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *247(H2 O)
HELIX 1 1 SER A 16 ASN A 33 1 18
HELIX 2 2 SER A 52 LEU A 66 1 15
HELIX 3 3 THR A 87 VAL A 99 1 13
HELIX 4 4 GLY A 110 GLU A 117 1 8
HELIX 5 5 HIS A 134 GLY A 150 1 17
HELIX 6 6 GLY A 166 ALA A 177 1 12
HELIX 7 7 GLN A 196 GLU A 204 1 9
HELIX 8 8 SER A 214 VAL A 218 5 5
HELIX 9 9 SER A 238 LYS A 244 1 7
HELIX 10 10 ARG A 250 HIS A 255 1 6
HELIX 11 11 ALA A 274 LYS A 279 1 6
HELIX 12 12 TRP A 284 ASN A 305 1 22
HELIX 13 13 ILE B 25 PHE B 33 1 9
HELIX 14 14 SER B 67 GLN B 73 1 7
HELIX 15 15 ILE B 115 GLU B 119 5 5
HELIX 16 16 HIS B 147 LEU B 151 1 5
HELIX 17 17 SER C 16 LYS C 31 1 16
HELIX 18 18 SER C 52 LEU C 66 1 15
HELIX 19 19 THR C 79 LYS C 83 5 5
HELIX 20 20 THR C 87 VAL C 99 1 13
HELIX 21 21 GLY C 110 GLU C 117 1 8
HELIX 22 22 HIS C 134 GLY C 150 1 17
HELIX 23 23 GLY C 166 ALA C 177 1 12
HELIX 24 24 PRO C 195 LYS C 205 1 11
HELIX 25 25 SER C 214 MET C 219 1 6
HELIX 26 26 GLN C 231 LEU C 235 5 5
HELIX 27 27 ASP C 236 VAL C 243 1 8
HELIX 28 28 ARG C 250 ALA C 257 5 8
HELIX 29 29 ALA C 274 LYS C 279 5 6
HELIX 30 30 TRP C 284 ASN C 305 1 22
HELIX 31 31 ILE D 25 PHE D 33 1 9
HELIX 32 32 SER D 67 LEU D 74 1 8
HELIX 33 33 HIS D 147 LEU D 151 1 5
SHEET 1 A 4 SER A 69 SER A 74 0
SHEET 2 A 4 VAL A 43 PHE A 48 1 N ILE A 44 O SER A 69
SHEET 3 A 4 ALA A 101 HIS A 106 1 O ALA A 101 N ALA A 45
SHEET 4 A 4 VAL A 124 ASP A 129 1 N LEU A 125 O ILE A 102
SHEET 1 B 5 ALA A 208 HIS A 212 0
SHEET 2 B 5 ASN A 182 ILE A 187 1 O ASN A 182 N ALA A 208
SHEET 3 B 5 LEU A 155 VAL A 160 1 O LEU A 155 N ARG A 183
SHEET 4 B 5 ILE A 224 MET A 227 1 N ILE A 224 O HIS A 156
SHEET 5 B 5 VAL A 263 LEU A 264 1 O LEU A 264 N MET A 227
SHEET 1 C10 GLU D 90 VAL D 92 0
SHEET 2 C10 VAL D 83 ASP D 87 -1 O ARG D 85 N VAL D 92
SHEET 3 C10 GLY D 15 ILE D 18 -1 O GLY D 15 N ILE D 86
SHEET 4 C10 MET D 53 ILE D 61 -1 O ILE D 59 N ILE D 18
SHEET 5 C10 ILE D 42 SER D 50 -1 N THR D 43 O LYS D 60
SHEET 6 C10 ILE B 42 LEU B 46 -1 O ILE B 42 N LEU D 46
SHEET 7 C10 ARG B 55 ILE B 61 -1 O LEU B 58 N GLY B 45
SHEET 8 C10 VAL B 17 ILE B 21 -1 N ILE B 18 O ILE B 59
SHEET 9 C10 VAL B 83 ASP B 87 -1 N ASN B 84 O VAL B 17
SHEET 10 C10 GLU B 90 SER B 95 -1 O GLU B 90 N ASP B 87
SHEET 1 D 8 GLU D 90 VAL D 92 0
SHEET 2 D 8 VAL D 83 ASP D 87 -1 O ARG D 85 N VAL D 92
SHEET 3 D 8 GLY D 15 ILE D 18 -1 O GLY D 15 N ILE D 86
SHEET 4 D 8 MET D 53 ILE D 61 -1 O ILE D 59 N ILE D 18
SHEET 5 D 8 ILE D 42 SER D 50 -1 N THR D 43 O LYS D 60
SHEET 6 D 8 ILE B 42 LEU B 46 -1 O ILE B 42 N LEU D 46
SHEET 7 D 8 ARG B 55 ILE B 61 -1 O LEU B 58 N GLY B 45
SHEET 8 D 8 LEU B 48 PRO B 49 -1 O LEU B 48 N LYS B 56
SHEET 1 E 3 ARG B 128 ARG B 130 0
SHEET 2 E 3 ASP B 133 LYS B 137 -1 O ASP B 133 N ARG B 130
SHEET 3 E 3 GLU B 144 SER B 146 -1 N PHE B 145 O LEU B 136
SHEET 1 F 2 LYS C 42 ILE C 44 0
SHEET 2 F 2 ALA C 68 VAL C 70 1 O SER C 69 N ILE C 44
SHEET 1 G 3 CYS C 47 PHE C 48 0
SHEET 2 G 3 ILE C 102 HIS C 106 1 O VAL C 103 N CYS C 47
SHEET 3 G 3 VAL C 124 ASP C 129 1 N LEU C 125 O ILE C 102
SHEET 1 H 5 TRP C 209 HIS C 212 0
SHEET 2 H 5 ARG C 183 ILE C 187 1 O PHE C 184 N SER C 210
SHEET 3 H 5 HIS C 156 VAL C 160 1 N VAL C 157 O ARG C 183
SHEET 4 H 5 ILE C 224 MET C 227 1 O ILE C 224 N ALA C 158
SHEET 5 H 5 LYS C 262 LEU C 264 1 O LYS C 262 N LEU C 225
SHEET 1 I 2 ALA D 135 LYS D 137 0
SHEET 2 I 2 GLU D 144 SER D 146 -1 O PHE D 145 N LEU D 136
LINK SG CYS B 109 ZN ZN B 313 1555 1555 2.33
LINK SG CYS B 114 ZN ZN B 313 1555 1555 2.31
LINK SG CYS B 138 ZN ZN B 313 1555 1555 2.36
LINK SG CYS B 141 ZN ZN B 313 1555 1555 2.36
LINK SG CYS D 109 ZN ZN D 314 1555 1555 2.35
LINK SG CYS D 114 ZN ZN D 314 1555 1555 2.29
LINK SG CYS D 138 ZN ZN D 314 1555 1555 2.35
LINK SG CYS D 141 ZN ZN D 314 1555 1555 2.26
CISPEP 1 LEU A 267 ALA A 268 0 -1.43
CISPEP 2 LEU C 267 ALA C 268 0 -0.28
SITE 1 AC1 4 CYS B 109 CYS B 114 CYS B 138 CYS B 141
SITE 1 AC2 5 CYS D 109 CYS D 114 SER D 116 CYS D 138
SITE 2 AC2 5 CYS D 141
CRYST1 129.870 129.870 198.340 90.00 90.00 120.00 H 3 18
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 0.007700 0.004445 0.000000 0.00000
SCALE2 0.000000 0.008891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END