HEADER LIGASE 10-MAR-04 1VCM
TITLE CRYSTAL STRUCTURE OF T.TH. HB8 CTP SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CTP SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.4.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 GENE: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS TETRAMER, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 2 STRUCTURAL GENOMICS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GOTO,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 27-DEC-23 1VCM 1 REMARK
REVDAT 3 13-JUL-11 1VCM 1 VERSN
REVDAT 2 24-FEB-09 1VCM 1 VERSN
REVDAT 1 31-AUG-04 1VCM 0
JRNL AUTH M.GOTO,R.OMI,N.NAKAGAWA,I.MIYAHARA,K.HIROTSU
JRNL TITL CRYSTAL STRUCTURES OF CTP SYNTHETASE REVEAL ATP, UTP, AND
JRNL TITL 2 GLUTAMINE BINDING SITES
JRNL REF STRUCTURE V. 12 1413 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15296735
JRNL DOI 10.1016/J.STR.2004.05.013
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 31205
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) : 0.235
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3127
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 : 4015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 312
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) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.420
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1VCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000006466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31225
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 46.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
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) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 59.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA CITRATE, GLYCEROL, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 43.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.33500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.56500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.33500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.56500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.33500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.56500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.33500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 71.56500
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: CTPS IS IN AN EQUILIBRIUM STATE BETWEEN A MONOMER, A DIMER,
REMARK 300 AND A TETRAMER DEPENDING ON A PROTEIN CONCENTRATION.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 74760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 143.13000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 143.13000
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 1
REMARK 465 ASN A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 ASP A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 PRO A 9
REMARK 465 GLU A 192
REMARK 465 THR A 193
REMARK 465 LYS A 311
REMARK 465 MET A 312
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 GLY A 366
REMARK 465 VAL A 367
REMARK 465 ARG A 549
REMARK 465 ALA A 550
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 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 66 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 118 CG CD1 CD2
REMARK 470 GLU A 177 CG CD OE1 OE2
REMARK 470 GLU A 195 CG CD OE1 OE2
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 278 CG CD OE1 OE2
REMARK 470 GLU A 289 CG CD OE1 OE2
REMARK 470 ARG A 292 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 302 CG CD CE NZ
REMARK 470 ARG A 331 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 335 CG CD OE1 OE2
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 ASP A 348 CG OD1 OD2
REMARK 470 GLU A 351 CG CD OE1 OE2
REMARK 470 ARG A 354 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 365 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 368 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 375 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 430 CG CD OE1 OE2
REMARK 470 GLN A 431 CG CD OE1 NE2
REMARK 470 GLU A 435 CG CD OE1 OE2
REMARK 470 ARG A 449 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 451 CG CD CE NZ
REMARK 470 LYS A 462 CG CD CE NZ
REMARK 470 GLU A 464 CG CD OE1 OE2
REMARK 470 ASP A 481 CG OD1 OD2
REMARK 470 ARG A 498 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 511 CG CD CE NZ
REMARK 470 ASP A 512 CG OD1 OD2
REMARK 470 MET A 530 CG SD CE
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 O HOH A 563 O HOH A 563 3556 1.28
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 LEU A 261 CA - CB - CG ANGL. DEV. = 14.3 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 VAL A 21 -64.71 75.22
REMARK 500 PRO A 52 -3.57 -58.87
REMARK 500 TYR A 64 -54.51 -132.71
REMARK 500 GLU A 65 -79.62 -24.20
REMARK 500 HIS A 66 47.44 -93.30
REMARK 500 LYS A 144 59.67 33.40
REMARK 500 ASN A 240 13.81 85.41
REMARK 500 ALA A 341 -54.44 75.59
REMARK 500 ALA A 347 103.33 -49.25
REMARK 500 ASP A 348 24.59 -168.07
REMARK 500 ARG A 354 -70.58 -54.74
REMARK 500 ASP A 355 38.19 -84.75
REMARK 500 CYS A 391 -106.25 52.39
REMARK 500 ASN A 412 -175.57 -171.43
REMARK 500 ARG A 470 76.49 -167.85
REMARK 500 PRO A 495 2.34 -67.51
REMARK 500 MET A 497 114.00 -165.10
REMARK 500 PHE A 515 102.31 -163.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VCN RELATED DB: PDB
REMARK 900 T.TH. HB8 CTP SYNTHETASE COMPLEX WITH SULFATE ANION
REMARK 900 RELATED ID: 1VCO RELATED DB: PDB
REMARK 900 T.TH. HB8 CTP SYNTHETASE COMPLEX WITH GLUTAMINE
REMARK 900 RELATED ID: TTK003000122.1 RELATED DB: TARGETDB
DBREF 1VCM A 1 550 UNP Q5SIA8 PYRG_THET8 1 550
SEQRES 1 A 550 MET ASN GLY SER ALA ASP ALA GLY PRO ARG PRO ARG LYS
SEQRES 2 A 550 TYR VAL PHE ILE THR GLY GLY VAL VAL SER SER LEU GLY
SEQRES 3 A 550 LYS GLY ILE LEU THR SER SER LEU GLY ALA LEU LEU ARG
SEQRES 4 A 550 ALA ARG GLY TYR ARG VAL THR ALA ILE LYS ILE ASP PRO
SEQRES 5 A 550 TYR VAL ASN VAL ASP ALA GLY THR MET ARG PRO TYR GLU
SEQRES 6 A 550 HIS GLY GLU VAL PHE VAL THR ALA ASP GLY ALA GLU THR
SEQRES 7 A 550 ASP LEU ASP ILE GLY HIS TYR GLU ARG PHE LEU ASP MET
SEQRES 8 A 550 ASP LEU SER ARG GLY ASN ASN LEU THR THR GLY GLN VAL
SEQRES 9 A 550 TYR LEU SER VAL ILE GLN LYS GLU ARG ARG GLY GLU TYR
SEQRES 10 A 550 LEU SER GLN THR VAL GLN VAL ILE PRO HIS ILE THR ASP
SEQRES 11 A 550 GLU ILE LYS GLU ARG ILE ARG LYS VAL ALA GLU GLU GLN
SEQRES 12 A 550 LYS ALA GLU ILE VAL VAL VAL GLU VAL GLY GLY THR VAL
SEQRES 13 A 550 GLY ASP ILE GLU SER LEU PRO PHE LEU GLU ALA ILE ARG
SEQRES 14 A 550 GLN PHE ARG PHE ASP GLU GLY GLU GLY ASN THR LEU TYR
SEQRES 15 A 550 LEU HIS LEU THR LEU VAL PRO TYR LEU GLU THR SER GLU
SEQRES 16 A 550 GLU PHE LYS THR LYS PRO THR GLN HIS SER VAL ALA THR
SEQRES 17 A 550 LEU ARG GLY VAL GLY ILE GLN PRO ASP ILE LEU VAL LEU
SEQRES 18 A 550 ARG SER ALA ARG PRO VAL PRO GLU GLU VAL ARG ARG LYS
SEQRES 19 A 550 VAL ALA LEU PHE THR ASN VAL ARG PRO GLY HIS VAL PHE
SEQRES 20 A 550 SER SER PRO THR VAL GLU HIS LEU TYR GLU VAL PRO LEU
SEQRES 21 A 550 LEU LEU GLU GLU GLN GLY LEU GLY ARG ALA VAL GLU ARG
SEQRES 22 A 550 ALA LEU GLY LEU GLU ALA VAL ILE PRO ASN LEU SER PHE
SEQRES 23 A 550 TRP GLN GLU ALA VAL ARG VAL LEU LYS HIS PRO GLU ARG
SEQRES 24 A 550 THR VAL LYS ILE ALA ILE ALA GLY LYS TYR VAL LYS MET
SEQRES 25 A 550 PRO ASP ALA TYR LEU SER LEU LEU GLU ALA LEU ARG HIS
SEQRES 26 A 550 ALA GLY ILE LYS ASN ARG ALA ARG VAL GLU VAL LYS TRP
SEQRES 27 A 550 VAL ASP ALA GLU SER LEU GLU ALA ALA ASP LEU ASP GLU
SEQRES 28 A 550 ALA PHE ARG ASP VAL SER GLY ILE LEU VAL PRO GLY GLY
SEQRES 29 A 550 PHE GLY VAL ARG GLY ILE GLU GLY LYS VAL ARG ALA ALA
SEQRES 30 A 550 GLN TYR ALA ARG GLU ARG LYS ILE PRO TYR LEU GLY ILE
SEQRES 31 A 550 CYS LEU GLY LEU GLN ILE ALA VAL ILE GLU PHE ALA ARG
SEQRES 32 A 550 ASN VAL ALA GLY LEU LYS GLY ALA ASN SER THR GLU PHE
SEQRES 33 A 550 ASP PRO HIS THR PRO HIS PRO VAL ILE ASP LEU MET PRO
SEQRES 34 A 550 GLU GLN LEU GLU VAL GLU GLY LEU GLY GLY THR MET ARG
SEQRES 35 A 550 LEU GLY ASP TRP PRO MET ARG ILE LYS PRO GLY THR LEU
SEQRES 36 A 550 LEU HIS ARG LEU TYR GLY LYS GLU GLU VAL LEU GLU ARG
SEQRES 37 A 550 HIS ARG HIS ARG TYR GLU VAL ASN PRO LEU TYR VAL ASP
SEQRES 38 A 550 GLY LEU GLU ARG ALA GLY LEU VAL VAL SER ALA THR THR
SEQRES 39 A 550 PRO GLY MET ARG GLY ARG GLY ALA GLY LEU VAL GLU ALA
SEQRES 40 A 550 ILE GLU LEU LYS ASP HIS PRO PHE PHE LEU GLY LEU GLN
SEQRES 41 A 550 SER HIS PRO GLU PHE LYS SER ARG PRO MET ARG PRO SER
SEQRES 42 A 550 PRO PRO PHE VAL GLY PHE VAL GLU ALA ALA LEU ALA TYR
SEQRES 43 A 550 GLN GLU ARG ALA
FORMUL 2 HOH *312(H2 O)
HELIX 1 1 GLY A 26 ALA A 40 1 15
HELIX 2 2 ASP A 57 MET A 61 5 5
HELIX 3 3 LEU A 80 ASP A 90 1 11
HELIX 4 4 SER A 94 GLY A 96 5 3
HELIX 5 5 THR A 101 ARG A 114 1 14
HELIX 6 6 PRO A 126 GLN A 143 1 18
HELIX 7 7 SER A 161 GLN A 170 1 10
HELIX 8 8 GLN A 170 GLY A 176 1 7
HELIX 9 9 THR A 199 VAL A 212 1 14
HELIX 10 10 PRO A 228 ASN A 240 1 13
HELIX 11 11 ARG A 242 GLY A 244 5 3
HELIX 12 12 TYR A 256 GLY A 266 1 11
HELIX 13 13 GLY A 266 LEU A 275 1 10
HELIX 14 14 LEU A 284 HIS A 296 1 13
HELIX 15 15 TYR A 316 ASN A 330 1 15
HELIX 16 16 ASP A 348 PHE A 353 1 6
HELIX 17 17 GLY A 369 ARG A 383 1 15
HELIX 18 18 CYS A 391 VAL A 405 1 15
HELIX 19 19 PRO A 429 GLU A 433 5 5
HELIX 20 20 THR A 454 GLY A 461 1 8
HELIX 21 21 TYR A 479 ALA A 486 1 8
HELIX 22 22 HIS A 522 SER A 527 5 6
HELIX 23 23 SER A 533 GLU A 548 1 16
SHEET 1 A 7 ASN A 98 THR A 100 0
SHEET 2 A 7 VAL A 45 ASP A 51 1 N ASP A 51 O LEU A 99
SHEET 3 A 7 ILE A 147 VAL A 152 1 O GLU A 151 N ILE A 50
SHEET 4 A 7 LYS A 13 GLY A 19 1 N ILE A 17 O VAL A 152
SHEET 5 A 7 THR A 180 LEU A 187 1 O LEU A 185 N THR A 18
SHEET 6 A 7 ILE A 218 SER A 223 1 O ARG A 222 N THR A 186
SHEET 7 A 7 VAL A 246 PRO A 250 1 O PHE A 247 N LEU A 219
SHEET 1 B 2 PHE A 70 VAL A 71 0
SHEET 2 B 2 GLU A 77 THR A 78 -1 O THR A 78 N PHE A 70
SHEET 1 C 2 TYR A 190 LEU A 191 0
SHEET 2 C 2 GLU A 196 PHE A 197 -1 O GLU A 196 N LEU A 191
SHEET 1 D 9 ALA A 332 VAL A 339 0
SHEET 2 D 9 ARG A 299 ALA A 306 1 N ILE A 305 O LYS A 337
SHEET 3 D 9 ILE A 359 VAL A 361 1 O LEU A 360 N ALA A 304
SHEET 4 D 9 TYR A 387 ILE A 390 1 O ILE A 390 N VAL A 361
SHEET 5 D 9 PHE A 516 LEU A 519 1 O LEU A 519 N GLY A 389
SHEET 6 D 9 VAL A 505 GLU A 509 -1 N ILE A 508 O GLY A 518
SHEET 7 D 9 VAL A 489 THR A 493 -1 N ALA A 492 O GLU A 506
SHEET 8 D 9 ARG A 442 ILE A 450 -1 N ARG A 449 O THR A 493
SHEET 9 D 9 GLU A 464 HIS A 471 -1 O VAL A 465 N MET A 448
SHEET 1 E 3 ASN A 412 SER A 413 0
SHEET 2 E 3 PRO A 423 LEU A 427 1 O ILE A 425 N ASN A 412
SHEET 3 E 3 TYR A 473 VAL A 475 -1 O GLU A 474 N ASP A 426
CISPEP 1 ILE A 125 PRO A 126 0 0.62
CRYST1 86.000 120.670 143.130 90.00 90.00 90.00 I 2 2 2 8
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 0.011628 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008287 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
