HEADER TRANSFERASE 08-DEC-09 3KZK
TITLE CRYSTAL STRUCTURE OF ACETYLORNITHINE TRANSCARBAMYLASE COMPLEXED WITH
TITLE 2 ACETYLCITRULLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLORNITHINE CARBAMOYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AOTCASE;
COMPND 5 EC: 2.1.3.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS;
SOURCE 3 ORGANISM_TAXID: 190485;
SOURCE 4 STRAIN: ATCC 33913;
SOURCE 5 GENE: ARGF, ARGF', XCC2249;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TRANSCARBAMYLASE, AMINO-ACID BIOSYNTHESIS, ARGININE BIOSYNTHESIS,
KEYWDS 2 CYTOPLASM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SHI,X.YU,N.M.ALLEWELL,M.TUCHMAN
REVDAT 4 22-NOV-23 3KZK 1 REMARK
REVDAT 3 06-SEP-23 3KZK 1 REMARK SEQADV LINK
REVDAT 2 01-NOV-17 3KZK 1 REMARK
REVDAT 1 31-MAR-10 3KZK 0
SPRSDE 31-MAR-10 3KZK 1YH1
JRNL AUTH D.SHI,H.MORIZONO,X.YU,L.ROTH,L.CALDOVIC,N.M.ALLEWELL,
JRNL AUTH 2 M.H.MALAMY,M.TUCHMAN
JRNL TITL CRYSTAL STRUCTURE OF N-ACETYLORNITHINE TRANSCARBAMYLASE FROM
JRNL TITL 2 XANTHOMONAS CAMPESTRIS: A NOVEL ENZYME IN A NEW ARGININE
JRNL TITL 3 BIOSYNTHETIC PATHWAY FOUND IN SEVERAL EUBACTERIA.
JRNL REF J.BIOL.CHEM. V. 280 14366 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15731101
JRNL DOI 10.1074/JBC.C500005200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.94
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) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 28390
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) : 0.219
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2818
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4172
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 475
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2632
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.000
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) : 1.230 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.820 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.490 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 58.44
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KZK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9186
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28390
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1AKM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, BIS-TRIS, PEG3350, PH
REMARK 280 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 64.72300
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 64.72300
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 64.72300
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 64.72300
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 64.72300
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 0.000000 -1.000000 194.16900
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 129.44600
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 64.72300
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 129.44600
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 -64.72300
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 194.16900
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 S SO4 A 350 LIES ON A SPECIAL POSITION.
REMARK 375 O2 SO4 A 350 LIES ON A SPECIAL POSITION.
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 A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 337
REMARK 465 ARG A 338
REMARK 465 PRO A 339
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 125 OE2 GLU A 125 15656 1.98
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 SER A 49 141.40 -170.01
REMARK 500 MET A 50 -60.85 -123.17
REMARK 500 LYS A 74 -69.33 -105.43
REMARK 500 GLU A 144 114.89 111.20
REMARK 500 THR A 145 -91.74 -131.30
REMARK 500 PRO A 181 -8.86 -54.17
REMARK 500 LEU A 295 152.41 69.04
REMARK 500 VAL A 301 -56.98 -130.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLN A 345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 349
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FG7 RELATED DB: PDB
REMARK 900 THE HOMOLOG PROTEIN FROM B. FRAGILIS COMPLEXED WITH CARBAMYL
REMARK 900 PHOSPHATE AND N-SUCCINYL-L-NORVALINE
REMARK 900 RELATED ID: 3KZC RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH SULFATE
REMARK 900 RELATED ID: 3KZM RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL PHOSPHATE
REMARK 900 RELATED ID: 3KZN RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL PHOSPHATE
REMARK 900 RELATED ID: 3KZO RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL PHOSPHATE AND
REMARK 900 N-ACETYL-L-NORVALINE
REMARK 900 RELATED ID: 3L02 RELATED DB: PDB
REMARK 900 THE E92A MUTANT OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL
REMARK 900 PHOSPHATE AND N-SUCCINYL-L-NORVALINE
REMARK 900 RELATED ID: 3L04 RELATED DB: PDB
REMARK 900 THE E92P MUTANT OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL
REMARK 900 PHOSPHATE AND N-SUCCINYL-L-NORVALINE
REMARK 900 RELATED ID: 3L05 RELATED DB: PDB
REMARK 900 THE E92SSSRCANT OF THE SAME PROTEIN COMPLEXED WITH CARBAMYL
REMARK 900 PHOSPHATE AND N-SUCCINYL-L-NORVALINE
REMARK 900 RELATED ID: 3L06 RELATED DB: PDB
REMARK 900 THE E92V MUTANT COMPLEXED WITH CARBAMYL PHOSPHATE AND N-SUCCINYL-L-
REMARK 900 NORVALINE
DBREF 3KZK A 1 339 UNP Q8P8J2 AOTC_XANCP 1 339
SEQADV 3KZK MET A -19 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK GLY A -18 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK SER A -17 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK SER A -16 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -15 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -14 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -13 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -12 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -11 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A -10 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK SER A -9 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK SER A -8 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK GLY A -7 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK LEU A -6 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK VAL A -5 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK PRO A -4 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK ARG A -3 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK GLY A -2 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK SER A -1 UNP Q8P8J2 EXPRESSION TAG
SEQADV 3KZK HIS A 0 UNP Q8P8J2 EXPRESSION TAG
SEQRES 1 A 359 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 359 LEU VAL PRO ARG GLY SER HIS MET SER LEU LYS HIS PHE
SEQRES 3 A 359 LEU ASN THR GLN ASP TRP SER ARG ALA GLU LEU ASP ALA
SEQRES 4 A 359 LEU LEU THR GLN ALA ALA LEU PHE LYS ARG ASN LYS LEU
SEQRES 5 A 359 GLY SER GLU LEU LYS GLY LYS SER ILE ALA LEU VAL PHE
SEQRES 6 A 359 PHE ASN PRO SER MET ARG THR ARG THR SER PHE GLU LEU
SEQRES 7 A 359 GLY ALA PHE GLN LEU GLY GLY HIS ALA VAL VAL LEU GLN
SEQRES 8 A 359 PRO GLY LYS ASP ALA TRP PRO ILE GLU PHE ASN LEU GLY
SEQRES 9 A 359 THR VAL MET ASP GLY ASP THR GLU GLU HIS ILE ALA GLU
SEQRES 10 A 359 VAL ALA ARG VAL LEU GLY ARG TYR VAL ASP LEU ILE GLY
SEQRES 11 A 359 VAL ARG ALA PHE PRO LYS PHE VAL ASP TRP SER LYS ASP
SEQRES 12 A 359 ARG GLU ASP GLN VAL LEU LYS SER PHE ALA LYS TYR SER
SEQRES 13 A 359 PRO VAL PRO VAL ILE ASN MET GLU THR ILE THR HIS PRO
SEQRES 14 A 359 CYS GLN GLU LEU ALA HIS ALA LEU ALA LEU GLN GLU HIS
SEQRES 15 A 359 PHE GLY THR PRO ASP LEU ARG GLY LYS LYS TYR VAL LEU
SEQRES 16 A 359 THR TRP THR TYR HIS PRO LYS PRO LEU ASN THR ALA VAL
SEQRES 17 A 359 ALA ASN SER ALA LEU THR ILE ALA THR ARG MET GLY MET
SEQRES 18 A 359 ASP VAL THR LEU LEU CYS PRO THR PRO ASP TYR ILE LEU
SEQRES 19 A 359 ASP GLU ARG TYR MET ASP TRP ALA ALA GLN ASN VAL ALA
SEQRES 20 A 359 GLU SER GLY GLY SER LEU GLN VAL SER HIS ASP ILE ASP
SEQRES 21 A 359 SER ALA TYR ALA GLY ALA ASP VAL VAL TYR ALA LYS SER
SEQRES 22 A 359 TRP GLY ALA LEU PRO PHE PHE GLY ASN TRP GLU PRO GLU
SEQRES 23 A 359 LYS PRO ILE ARG ASP GLN TYR GLN HIS PHE ILE VAL ASP
SEQRES 24 A 359 GLU ARG LYS MET ALA LEU THR ASN ASN GLY VAL PHE SER
SEQRES 25 A 359 HIS CYS LEU PRO LEU ARG ARG ASN VAL KCX ALA THR ASP
SEQRES 26 A 359 ALA VAL MET ASP SER PRO ASN CYS ILE ALA ILE ASP GLU
SEQRES 27 A 359 ALA GLU ASN ARG LEU HIS VAL GLN LYS ALA ILE MET ALA
SEQRES 28 A 359 ALA LEU VAL GLY GLN SER ARG PRO
MODRES 3KZK KCX A 302 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 302 12
HET OLN A 345 15
HET SO4 A 349 5
HET SO4 A 350 5
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM OLN (S)-2-ACETAMIDO-5-UREIDOPENTANOIC ACID
HETNAM SO4 SULFATE ION
HETSYN OLN N-ACETYL-L-CITRULLINE
FORMUL 1 KCX C7 H14 N2 O4
FORMUL 2 OLN C8 H15 N3 O4
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *145(H2 O)
HELIX 1 1 ASN A 8 TRP A 12 5 5
HELIX 2 2 SER A 13 ASN A 30 1 18
HELIX 3 3 MET A 50 LEU A 63 1 14
HELIX 4 4 ILE A 95 VAL A 106 1 12
HELIX 5 5 ASP A 119 ARG A 124 1 6
HELIX 6 6 ASP A 126 SER A 136 1 11
HELIX 7 7 HIS A 148 GLY A 164 1 17
HELIX 8 8 THR A 186 MET A 199 1 14
HELIX 9 9 THR A 209 ILE A 213 5 5
HELIX 10 10 ASP A 215 GLY A 230 1 16
HELIX 11 11 ASP A 238 ALA A 244 1 7
HELIX 12 12 ALA A 256 PHE A 260 5 5
HELIX 13 13 GLU A 266 GLN A 272 1 7
HELIX 14 14 ASP A 279 ALA A 284 1 6
HELIX 15 15 THR A 304 ASP A 309 1 6
HELIX 16 16 ILE A 314 VAL A 334 1 21
SHEET 1 A 4 HIS A 66 LEU A 70 0
SHEET 2 A 4 SER A 40 PHE A 45 1 N PHE A 45 O LEU A 70
SHEET 3 A 4 LEU A 108 ARG A 112 1 O GLY A 110 N ALA A 42
SHEET 4 A 4 VAL A 140 ASN A 142 1 O ILE A 141 N VAL A 111
SHEET 1 B 2 ILE A 79 GLU A 80 0
SHEET 2 B 2 GLU A 93 HIS A 94 1 O GLU A 93 N GLU A 80
SHEET 1 C 5 SER A 232 SER A 236 0
SHEET 2 C 5 ASP A 202 LEU A 206 1 N LEU A 205 O GLN A 234
SHEET 3 C 5 LYS A 172 TRP A 177 1 N TYR A 173 O THR A 204
SHEET 4 C 5 VAL A 248 LYS A 252 1 O VAL A 248 N VAL A 174
SHEET 5 C 5 VAL A 290 SER A 292 1 O VAL A 290 N VAL A 249
LINK C KCX A 302 N ALA A 303 1555 1555 1.33
CISPEP 1 LEU A 295 PRO A 296 0 0.01
SITE 1 AC1 17 THR A 52 TRP A 77 GLU A 92 ARG A 112
SITE 2 AC1 17 GLU A 144 HIS A 148 GLN A 151 LYS A 252
SITE 3 AC1 17 CYS A 294 LEU A 295 PRO A 296 ARG A 322
SITE 4 AC1 17 HOH A 346 SO4 A 349 HOH A 370 HOH A 399
SITE 5 AC1 17 HOH A 443
SITE 1 AC2 7 SER A 49 MET A 50 ARG A 51 THR A 52
SITE 2 AC2 7 TRP A 77 ARG A 112 OLN A 345
SITE 1 AC3 3 PHE A 61 HIS A 66 HOH A 342
CRYST1 129.446 129.446 129.446 90.00 90.00 90.00 I 21 3 24
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 0.007725 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007725 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007725 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
