HEADER TRANSFERASE 16-MAY-03 1UEI
TITLE CRYSTAL STRUCTURE OF HUMAN URIDINE-CYTIDINE KINASE 2 COMPLEXED WITH A
TITLE 2 FEEDBACK-INHIBITOR, UTP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URIDINE-CYTIDINE KINASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-250;
COMPND 5 SYNONYM: URIDINE-CYTIDINE KINASE;
COMPND 6 EC: 2.7.1.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P
KEYWDS ALPHA/BETA MONONUCLEOTIDE-BINDING HOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.N.SUZUKI,K.KOIZUMI,M.FUKUSHIMA,A.MATSUDA,F.INAGAKI
REVDAT 4 25-OCT-23 1UEI 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1UEI 1 VERSN
REVDAT 2 18-MAY-04 1UEI 1 JRNL REMARK
REVDAT 1 04-MAY-04 1UEI 0
JRNL AUTH N.N.SUZUKI,K.KOIZUMI,M.FUKUSHIMA,A.MATSUDA,F.INAGAKI
JRNL TITL STRUCTURAL BASIS FOR THE SPECIFICITY, CATALYSIS, AND
JRNL TITL 2 REGULATION OF HUMAN URIDINE-CYTIDINE KINASE
JRNL REF STRUCTURE V. 12 751 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15130468
JRNL DOI 10.1016/J.STR.2004.02.038
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.N.SUZUKI,K.KOIZUMI,M.FUKUSHIMA,A.MATSUDA,F.INAGAKI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF HUMAN
REMARK 1 TITL 2 URIDINE-CYTIDINE KINASE 2
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 59 1477 2003
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 12876357
REMARK 1 DOI 10.1107/S0907444903011533
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 350363.520
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.9
REMARK 3 NUMBER OF REFLECTIONS : 19277
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1898
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2888
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 316
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3228
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 90
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.07000
REMARK 3 B22 (A**2) : -12.26000
REMARK 3 B33 (A**2) : 0.18000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.31
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.270 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 42.85
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : UTP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : UTP.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9000
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED MONOCHROMATOR
REMARK 200 AND VERTICAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19587
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1UDW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM TARTRATE, HEPES, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 123.87400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.83650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 123.87400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.83650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 123.87400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.83650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 123.87400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 45.83650
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 45.83650
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 45.83650
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 45.83650
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 45.83650
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 123.87400
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 123.87400
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 123.87400
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 65.76450
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 123.87400
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 -1.000000 0.000000 0.000000 65.76450
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 45.83650
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 65.76450
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 45.83650
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 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 GLN A 7
REMARK 465 THR A 8
REMARK 465 LEU A 9
REMARK 465 GLN A 10
REMARK 465 ASN A 11
REMARK 465 HIS A 12
REMARK 465 GLN A 13
REMARK 465 GLN A 14
REMARK 465 PRO A 15
REMARK 465 ASN A 16
REMARK 465 GLY A 17
REMARK 465 GLY A 18
REMARK 465 GLY A 45
REMARK 465 GLN A 46
REMARK 465 ASN A 47
REMARK 465 GLU A 48
REMARK 465 VAL A 49
REMARK 465 ASP A 50
REMARK 465 TYR A 51
REMARK 465 ARG A 52
REMARK 465 GLY A 231
REMARK 465 GLY A 232
REMARK 465 PRO A 233
REMARK 465 SER A 234
REMARK 465 LYS A 235
REMARK 465 ARG A 236
REMARK 465 GLN A 237
REMARK 465 THR A 238
REMARK 465 ASN A 239
REMARK 465 GLY A 240
REMARK 465 CYS A 241
REMARK 465 LEU A 242
REMARK 465 ASN A 243
REMARK 465 GLY A 244
REMARK 465 TYR A 245
REMARK 465 THR A 246
REMARK 465 PRO A 247
REMARK 465 SER A 248
REMARK 465 ARG A 249
REMARK 465 LYS A 250
REMARK 465 PRO B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 ASP B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 GLN B 7
REMARK 465 THR B 8
REMARK 465 LEU B 9
REMARK 465 GLN B 10
REMARK 465 ASN B 11
REMARK 465 HIS B 12
REMARK 465 GLN B 13
REMARK 465 GLN B 14
REMARK 465 PRO B 15
REMARK 465 ASN B 16
REMARK 465 GLY B 17
REMARK 465 GLY B 18
REMARK 465 ASN B 47
REMARK 465 GLU B 48
REMARK 465 VAL B 49
REMARK 465 ASP B 50
REMARK 465 GLY B 232
REMARK 465 PRO B 233
REMARK 465 SER B 234
REMARK 465 LYS B 235
REMARK 465 ARG B 236
REMARK 465 GLN B 237
REMARK 465 THR B 238
REMARK 465 ASN B 239
REMARK 465 GLY B 240
REMARK 465 CYS B 241
REMARK 465 LEU B 242
REMARK 465 ASN B 243
REMARK 465 GLY B 244
REMARK 465 TYR B 245
REMARK 465 THR B 246
REMARK 465 PRO B 247
REMARK 465 SER B 248
REMARK 465 ARG B 249
REMARK 465 LYS B 250
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 GLU A 19 CG CD OE1 OE2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 GLN A 53 CG CD OE1 NE2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 TYR B 51 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 52 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 53 CG CD OE1 NE2
REMARK 470 SER B 70 OG
REMARK 470 GLU B 71 CG CD OE1 OE2
REMARK 470 GLU B 92 CG CD OE1 OE2
REMARK 470 GLU B 121 CG CD OE1 OE2
REMARK 470 GLU B 179 CG CD OE1 OE2
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 PRO A 128 161.67 -44.08
REMARK 500 PHE A 188 -56.57 -121.10
REMARK 500 CYS A 197 -72.87 -74.28
REMARK 500 PHE B 188 -52.13 -125.36
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 UTP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP B 1301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UDW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CTP.
REMARK 900 RELATED ID: 1UEJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A SUBSTRATE, CYTIDINE.
DBREF 1UEI A 1 250 UNP Q9BZX2 UCK2_HUMAN 1 250
DBREF 1UEI B 1 250 UNP Q9BZX2 UCK2_HUMAN 1 250
SEQADV 1UEI PRO A -1 UNP Q9BZX2 CLONING ARTIFACT
SEQADV 1UEI GLY A 0 UNP Q9BZX2 CLONING ARTIFACT
SEQADV 1UEI PRO B -1 UNP Q9BZX2 CLONING ARTIFACT
SEQADV 1UEI GLY B 0 UNP Q9BZX2 CLONING ARTIFACT
SEQRES 1 A 252 PRO GLY MET ALA GLY ASP SER GLU GLN THR LEU GLN ASN
SEQRES 2 A 252 HIS GLN GLN PRO ASN GLY GLY GLU PRO PHE LEU ILE GLY
SEQRES 3 A 252 VAL SER GLY GLY THR ALA SER GLY LYS SER SER VAL CYS
SEQRES 4 A 252 ALA LYS ILE VAL GLN LEU LEU GLY GLN ASN GLU VAL ASP
SEQRES 5 A 252 TYR ARG GLN LYS GLN VAL VAL ILE LEU SER GLN ASP SER
SEQRES 6 A 252 PHE TYR ARG VAL LEU THR SER GLU GLN LYS ALA LYS ALA
SEQRES 7 A 252 LEU LYS GLY GLN PHE ASN PHE ASP HIS PRO ASP ALA PHE
SEQRES 8 A 252 ASP ASN GLU LEU ILE LEU LYS THR LEU LYS GLU ILE THR
SEQRES 9 A 252 GLU GLY LYS THR VAL GLN ILE PRO VAL TYR ASP PHE VAL
SEQRES 10 A 252 SER HIS SER ARG LYS GLU GLU THR VAL THR VAL TYR PRO
SEQRES 11 A 252 ALA ASP VAL VAL LEU PHE GLU GLY ILE LEU ALA PHE TYR
SEQRES 12 A 252 SER GLN GLU VAL ARG ASP LEU PHE GLN MET LYS LEU PHE
SEQRES 13 A 252 VAL ASP THR ASP ALA ASP THR ARG LEU SER ARG ARG VAL
SEQRES 14 A 252 LEU ARG ASP ILE SER GLU ARG GLY ARG ASP LEU GLU GLN
SEQRES 15 A 252 ILE LEU SER GLN TYR ILE THR PHE VAL LYS PRO ALA PHE
SEQRES 16 A 252 GLU GLU PHE CYS LEU PRO THR LYS LYS TYR ALA ASP VAL
SEQRES 17 A 252 ILE ILE PRO ARG GLY ALA ASP ASN LEU VAL ALA ILE ASN
SEQRES 18 A 252 LEU ILE VAL GLN HIS ILE GLN ASP ILE LEU ASN GLY GLY
SEQRES 19 A 252 PRO SER LYS ARG GLN THR ASN GLY CYS LEU ASN GLY TYR
SEQRES 20 A 252 THR PRO SER ARG LYS
SEQRES 1 B 252 PRO GLY MET ALA GLY ASP SER GLU GLN THR LEU GLN ASN
SEQRES 2 B 252 HIS GLN GLN PRO ASN GLY GLY GLU PRO PHE LEU ILE GLY
SEQRES 3 B 252 VAL SER GLY GLY THR ALA SER GLY LYS SER SER VAL CYS
SEQRES 4 B 252 ALA LYS ILE VAL GLN LEU LEU GLY GLN ASN GLU VAL ASP
SEQRES 5 B 252 TYR ARG GLN LYS GLN VAL VAL ILE LEU SER GLN ASP SER
SEQRES 6 B 252 PHE TYR ARG VAL LEU THR SER GLU GLN LYS ALA LYS ALA
SEQRES 7 B 252 LEU LYS GLY GLN PHE ASN PHE ASP HIS PRO ASP ALA PHE
SEQRES 8 B 252 ASP ASN GLU LEU ILE LEU LYS THR LEU LYS GLU ILE THR
SEQRES 9 B 252 GLU GLY LYS THR VAL GLN ILE PRO VAL TYR ASP PHE VAL
SEQRES 10 B 252 SER HIS SER ARG LYS GLU GLU THR VAL THR VAL TYR PRO
SEQRES 11 B 252 ALA ASP VAL VAL LEU PHE GLU GLY ILE LEU ALA PHE TYR
SEQRES 12 B 252 SER GLN GLU VAL ARG ASP LEU PHE GLN MET LYS LEU PHE
SEQRES 13 B 252 VAL ASP THR ASP ALA ASP THR ARG LEU SER ARG ARG VAL
SEQRES 14 B 252 LEU ARG ASP ILE SER GLU ARG GLY ARG ASP LEU GLU GLN
SEQRES 15 B 252 ILE LEU SER GLN TYR ILE THR PHE VAL LYS PRO ALA PHE
SEQRES 16 B 252 GLU GLU PHE CYS LEU PRO THR LYS LYS TYR ALA ASP VAL
SEQRES 17 B 252 ILE ILE PRO ARG GLY ALA ASP ASN LEU VAL ALA ILE ASN
SEQRES 18 B 252 LEU ILE VAL GLN HIS ILE GLN ASP ILE LEU ASN GLY GLY
SEQRES 19 B 252 PRO SER LYS ARG GLN THR ASN GLY CYS LEU ASN GLY TYR
SEQRES 20 B 252 THR PRO SER ARG LYS
HET UTP A 301 29
HET UTP B1301 29
HETNAM UTP URIDINE 5'-TRIPHOSPHATE
FORMUL 3 UTP 2(C9 H15 N2 O15 P3)
FORMUL 5 HOH *90(H2 O)
HELIX 1 1 GLY A 32 LEU A 44 1 13
HELIX 2 2 ASP A 62 TYR A 65 5 4
HELIX 3 3 THR A 69 LYS A 78 1 10
HELIX 4 4 HIS A 85 PHE A 89 5 5
HELIX 5 5 ASP A 90 GLU A 103 1 14
HELIX 6 6 SER A 142 ASP A 147 1 6
HELIX 7 7 ASP A 158 ARG A 174 1 17
HELIX 8 8 ASP A 177 PHE A 188 1 12
HELIX 9 9 PHE A 188 PHE A 196 1 9
HELIX 10 10 CYS A 197 ALA A 204 5 8
HELIX 11 11 GLY A 211 ASP A 213 5 3
HELIX 12 12 ASN A 214 LEU A 229 1 16
HELIX 13 13 GLY B 32 GLY B 45 1 14
HELIX 14 14 ASP B 62 TYR B 65 5 4
HELIX 15 15 THR B 69 LYS B 78 1 10
HELIX 16 16 HIS B 85 PHE B 89 5 5
HELIX 17 17 ASP B 90 GLU B 103 1 14
HELIX 18 18 SER B 142 PHE B 149 1 8
HELIX 19 19 ASP B 158 ARG B 174 1 17
HELIX 20 20 ASP B 177 PHE B 188 1 12
HELIX 21 21 PHE B 188 PHE B 196 1 9
HELIX 22 22 CYS B 197 ALA B 204 5 8
HELIX 23 23 GLY B 211 ASP B 213 5 3
HELIX 24 24 ASN B 214 GLY B 231 1 18
SHEET 1 A 5 VAL A 56 SER A 60 0
SHEET 2 A 5 VAL A 131 GLU A 135 1 O LEU A 133 N LEU A 59
SHEET 3 A 5 PHE A 21 GLY A 27 1 N VAL A 25 O PHE A 134
SHEET 4 A 5 MET A 151 ASP A 156 1 O LEU A 153 N SER A 26
SHEET 5 A 5 VAL A 206 PRO A 209 1 O ILE A 208 N PHE A 154
SHEET 1 B 2 VAL A 107 ASP A 113 0
SHEET 2 B 2 SER A 118 VAL A 126 -1 O VAL A 126 N VAL A 107
SHEET 1 C 5 VAL B 56 SER B 60 0
SHEET 2 C 5 VAL B 131 GLU B 135 1 O LEU B 133 N LEU B 59
SHEET 3 C 5 PHE B 21 GLY B 27 1 N ILE B 23 O VAL B 132
SHEET 4 C 5 MET B 151 ASP B 156 1 O VAL B 155 N SER B 26
SHEET 5 C 5 VAL B 206 PRO B 209 1 O ILE B 208 N PHE B 154
SHEET 1 D 2 VAL B 107 ASP B 113 0
SHEET 2 D 2 SER B 118 VAL B 126 -1 O SER B 118 N ASP B 113
SITE 1 AC1 24 THR A 29 ALA A 30 SER A 31 GLY A 32
SITE 2 AC1 24 LYS A 33 SER A 34 ASP A 62 TYR A 65
SITE 3 AC1 24 PHE A 83 ASP A 84 TYR A 112 PHE A 114
SITE 4 AC1 24 HIS A 117 GLU A 135 ILE A 137 ARG A 166
SITE 5 AC1 24 ARG A 169 ARG A 174 ARG A 176 GLN A 184
SITE 6 AC1 24 HOH A 302 HOH A 308 HOH A 310 HOH A 316
SITE 1 AC2 24 THR B 29 ALA B 30 SER B 31 GLY B 32
SITE 2 AC2 24 LYS B 33 SER B 34 ASP B 62 TYR B 65
SITE 3 AC2 24 PHE B 83 ASP B 84 TYR B 112 PHE B 114
SITE 4 AC2 24 HIS B 117 GLU B 135 ILE B 137 ARG B 166
SITE 5 AC2 24 ARG B 169 ARG B 174 ARG B 176 GLN B 184
SITE 6 AC2 24 HOH B1303 HOH B1304 HOH B1349 HOH B1353
CRYST1 131.529 247.748 91.673 90.00 90.00 90.00 F 2 2 2 32
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 0.007603 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004036 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010908 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
