HEADER TRANSFERASE 24-OCT-12 2YOG
TITLE PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH A
TITLE 2 (THIO)UREA-ALPHA-DEOXYTHYMIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.4.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28
KEYWDS TRANSFERASE, MALARIA, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HUAQING,J.CARRERO-LERIDA,A.P.G.SILVA,J.L.WHITTINGHAM,J.A.BRANNIGAN,
AUTHOR 2 L.M.RUIZ-PEREZ,K.D.READ,K.S.WILSON,D.GONZALEZ-PACANOWSKA,
AUTHOR 3 I.H.GILBERT
REVDAT 1 24-JUL-13 2YOG 0
JRNL AUTH H.CUI,J.CARRERO-LERIDA,A.P.G.SILVA,J.L.WHITTINGHAM,
JRNL AUTH 2 J.A.BRANNIGAN,L.M.RUIZ-PEREZ,K.D.READ,K.S.WILSON,
JRNL AUTH 3 D.GONZALEZ-PACANOWSKA,I.H.GILBERT
JRNL TITL SYNTHESIS AND EVALUATION OF ALPHA-THYMIDINE ANALOGUES AS
JRNL TITL 2 NOVEL ANTIMALARIALS.
JRNL REF J.MED.CHEM. V. 55 10948 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 23240776
JRNL DOI 10.1021/JM301328H
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.90
REMARK 3 NUMBER OF REFLECTIONS : 61653
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 + TEST SET) : 0.18480
REMARK 3 R VALUE (WORKING SET) : 0.18233
REMARK 3 FREE R VALUE : 0.23262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3308
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.539
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4489
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.336
REMARK 3 BIN FREE R VALUE SET COUNT : 267
REMARK 3 BIN FREE R VALUE : 0.388
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 434
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.236
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.92
REMARK 3 B22 (A**2) : 0.06
REMARK 3 B33 (A**2) : -1.12
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.71
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3650 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4993 ; 1.443 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 456 ; 5.142 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;35.772 ;25.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 686 ;13.588 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;21.592 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 536 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2779 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2069 ; 1.343 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3408 ; 2.124 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1581 ; 3.024 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1551 ; 4.313 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3650 ; 1.838 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 434 ; 5.871 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3529 ; 4.664 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 2YOG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-12.
REMARK 100 THE PDBE ID CODE IS EBI-54565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-09
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 : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 23.40
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.5
REMARK 200 R MERGE FOR SHELL (I) : 0.80
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 0.2 M LICL,
REMARK 280 20% PEG6000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 29.39500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 THR A 2
REMARK 465 ASP A 3
REMARK 465 ALA A 142
REMARK 465 GLN A 143
REMARK 465 ASN A 144
REMARK 465 ARG A 145
REMARK 465 SER A 146
REMARK 465 ASP A 147
REMARK 465 TYR A 148
REMARK 465 GLY A 149
REMARK 465 GLU A 150
REMARK 465 GLU A 151
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ARG B 18
REMARK 465 SER B 19
REMARK 465 GLY B 20
REMARK 465 GLN B 143
REMARK 465 ASN B 144
REMARK 465 ARG B 145
REMARK 465 SER B 146
REMARK 465 ASP B 147
REMARK 465 TYR B 148
REMARK 465 GLY B 149
REMARK 465 GLU B 150
REMARK 465 GLU B 151
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 30 CA CB CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1B ASN A 83 O HOH A 2113 2.16
REMARK 500 CD2B HIS B 41 CE1B TYR B 43 2.12
REMARK 500 NE2B HIS B 41 CZ B TYR B 43 2.08
REMARK 500 NE2B HIS B 41 CE1B TYR B 43 1.98
REMARK 500
REMARK 500 REMARK: NULL
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 OD2B ASP A 173 O HOH A 2042 2545 2.19
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 19 -7.08 -58.88
REMARK 500 ARG A 99 150.45 79.99
REMARK 500 TYR A 100 -149.26 -156.62
REMARK 500 TYR A 153 -1.67 65.22
REMARK 500 TRP A 209 45.90 -105.65
REMARK 500 ARG B 99 145.23 75.84
REMARK 500 TYR B 100 -150.74 -155.36
REMARK 500 TYR B 153 -14.99 74.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B 154 24.7 L L OUTSIDE RANGE
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 74X A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 74X B 211
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WWF RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 TMP AND ADP
REMARK 900 RELATED ID: 2WWG RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 DGMP AND ADP
REMARK 900 RELATED ID: 2WWH RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 AP5DT
REMARK 900 RELATED ID: 2WWI RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 AZTMP AND ADP
REMARK 900 RELATED ID: 2YOF RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 A (THIO)UREA-BETA-DEOXYTHYMIDINE INHIBITOR
REMARK 900 RELATED ID: 2YOH RELATED DB: PDB
REMARK 900 PLASMODIUM FALCIPARUM THYMIDYLATE KINASE IN COMPLEX WITH
REMARK 900 A UREA-ALPHA-DEOXYTHYMIDINE INHIBITOR
DBREF 2YOG A 1 210 UNP Q8I4S1 Q8I4S1_PLAF7 1 210
DBREF 2YOG B 1 210 UNP Q8I4S1 Q8I4S1_PLAF7 1 210
SEQRES 1 A 210 MET THR ASP ASP LYS LYS LYS GLY LYS PHE ILE VAL PHE
SEQRES 2 A 210 GLU GLY LEU ASP ARG SER GLY LYS SER THR GLN SER LYS
SEQRES 3 A 210 LEU LEU VAL GLU TYR LEU LYS ASN ASN ASN VAL GLU VAL
SEQRES 4 A 210 LYS HIS LEU TYR PHE PRO ASN ARG GLU THR GLY ILE GLY
SEQRES 5 A 210 GLN ILE ILE SER LYS TYR LEU LYS MET GLU ASN SER MET
SEQRES 6 A 210 SER ASN GLU THR ILE HIS LEU LEU PHE SER ALA ASN ARG
SEQRES 7 A 210 TRP GLU HIS MET ASN GLU ILE LYS SER LEU LEU LEU LYS
SEQRES 8 A 210 GLY ILE TRP VAL VAL CYS ASP ARG TYR ALA TYR SER GLY
SEQRES 9 A 210 VAL ALA TYR SER SER GLY ALA LEU ASN LEU ASN LYS THR
SEQRES 10 A 210 TRP CYS MET ASN PRO ASP GLN GLY LEU ILE LYS PRO ASP
SEQRES 11 A 210 VAL VAL PHE TYR LEU ASN VAL PRO PRO ASN TYR ALA GLN
SEQRES 12 A 210 ASN ARG SER ASP TYR GLY GLU GLU ILE TYR GLU LYS VAL
SEQRES 13 A 210 GLU THR GLN LYS LYS ILE TYR GLU THR TYR LYS HIS PHE
SEQRES 14 A 210 ALA HIS GLU ASP TYR TRP ILE ASN ILE ASP ALA THR ARG
SEQRES 15 A 210 LYS ILE GLU ASP ILE HIS ASN ASP ILE VAL LYS GLU VAL
SEQRES 16 A 210 THR LYS ILE LYS VAL GLU PRO GLU GLU PHE ASN PHE LEU
SEQRES 17 A 210 TRP SER
SEQRES 1 B 210 MET THR ASP ASP LYS LYS LYS GLY LYS PHE ILE VAL PHE
SEQRES 2 B 210 GLU GLY LEU ASP ARG SER GLY LYS SER THR GLN SER LYS
SEQRES 3 B 210 LEU LEU VAL GLU TYR LEU LYS ASN ASN ASN VAL GLU VAL
SEQRES 4 B 210 LYS HIS LEU TYR PHE PRO ASN ARG GLU THR GLY ILE GLY
SEQRES 5 B 210 GLN ILE ILE SER LYS TYR LEU LYS MET GLU ASN SER MET
SEQRES 6 B 210 SER ASN GLU THR ILE HIS LEU LEU PHE SER ALA ASN ARG
SEQRES 7 B 210 TRP GLU HIS MET ASN GLU ILE LYS SER LEU LEU LEU LYS
SEQRES 8 B 210 GLY ILE TRP VAL VAL CYS ASP ARG TYR ALA TYR SER GLY
SEQRES 9 B 210 VAL ALA TYR SER SER GLY ALA LEU ASN LEU ASN LYS THR
SEQRES 10 B 210 TRP CYS MET ASN PRO ASP GLN GLY LEU ILE LYS PRO ASP
SEQRES 11 B 210 VAL VAL PHE TYR LEU ASN VAL PRO PRO ASN TYR ALA GLN
SEQRES 12 B 210 ASN ARG SER ASP TYR GLY GLU GLU ILE TYR GLU LYS VAL
SEQRES 13 B 210 GLU THR GLN LYS LYS ILE TYR GLU THR TYR LYS HIS PHE
SEQRES 14 B 210 ALA HIS GLU ASP TYR TRP ILE ASN ILE ASP ALA THR ARG
SEQRES 15 B 210 LYS ILE GLU ASP ILE HIS ASN ASP ILE VAL LYS GLU VAL
SEQRES 16 B 210 THR LYS ILE LYS VAL GLU PRO GLU GLU PHE ASN PHE LEU
SEQRES 17 B 210 TRP SER
HET 74X A 211 31
HET 74X B 211 31
HETNAM 74X 1-[4-CHLORANYL-3-(TRIFLUOROMETHYL)PHENYL]-3-
HETNAM 2 74X [[(2R,3S)-5-[5-METHYL-2,4-BIS(OXIDANYLIDENE)
HETNAM 3 74X PYRIMIDIN-1-YL]-3-OXIDANYL-OXOLAN-2-YL]METHYL]
HETNAM 4 74X THIOUREA
HETSYN 74X (THIO)UREA-ALPHA-DEOXYTHYMIDINE DERIVATIVE
FORMUL 3 74X 2(C18 H18 CL F3 N4 O4 S)
FORMUL 4 HOH *434(H2 O)
HELIX 1 1 GLY A 20 ASN A 35 1 16
HELIX 2 2 THR A 49 LYS A 60 1 12
HELIX 3 3 SER A 66 GLU A 80 1 15
HELIX 4 4 HIS A 81 GLY A 92 1 12
HELIX 5 5 TYR A 100 LEU A 112 1 13
HELIX 6 6 ASN A 115 ASN A 121 1 7
HELIX 7 7 PRO A 122 GLN A 124 5 3
HELIX 8 8 LYS A 155 LYS A 167 1 13
HELIX 9 9 HIS A 168 ALA A 170 5 3
HELIX 10 10 LYS A 183 LYS A 197 1 15
HELIX 11 11 LYS B 21 ASN B 35 1 15
HELIX 12 12 THR B 49 LYS B 60 1 12
HELIX 13 13 SER B 66 GLU B 80 1 15
HELIX 14 14 HIS B 81 LYS B 91 1 11
HELIX 15 15 TYR B 100 ASN B 113 1 14
HELIX 16 16 ASN B 115 ASN B 121 1 7
HELIX 17 17 PRO B 122 GLN B 124 5 3
HELIX 18 18 LYS B 155 LYS B 167 1 13
HELIX 19 19 HIS B 168 ALA B 170 5 3
HELIX 20 20 LYS B 183 LYS B 197 1 15
SHEET 1 AA 5 VAL A 39 TYR A 43 0
SHEET 2 AA 5 TRP A 94 ASP A 98 1 O TRP A 94 N LYS A 40
SHEET 3 AA 5 PHE A 10 GLY A 15 1 O ILE A 11 N CYS A 97
SHEET 4 AA 5 VAL A 131 ASN A 136 1 O VAL A 131 N VAL A 12
SHEET 5 AA 5 TRP A 175 ASP A 179 1 O ILE A 176 N TYR A 134
SHEET 1 BA 5 VAL B 39 TYR B 43 0
SHEET 2 BA 5 TRP B 94 ASP B 98 1 O TRP B 94 N LYS B 40
SHEET 3 BA 5 PHE B 10 GLY B 15 1 O ILE B 11 N CYS B 97
SHEET 4 BA 5 VAL B 131 ASN B 136 1 O VAL B 131 N VAL B 12
SHEET 5 BA 5 TRP B 175 ASP B 179 1 O ILE B 176 N TYR B 134
CISPEP 1 PHE A 44 PRO A 45 0 -7.82
CISPEP 2 LEU A 208 TRP A 209 0 -1.42
CISPEP 3 PHE B 44 PRO B 45 0 -3.50
CISPEP 4 LEU B 208 TRP B 209 0 3.31
SITE 1 AC1 15 ASP A 17 PHE A 44 PRO A 45 LEU A 59
SITE 2 AC1 15 LYS A 60 PHE A 74 ARG A 78 ARG A 99
SITE 3 AC1 15 SER A 103 GLY A 104 TYR A 107 HOH A2011
SITE 4 AC1 15 HOH A2102 HOH A2167 HOH A2220
SITE 1 AC2 16 PHE B 44 PRO B 45 ARG B 47 LEU B 59
SITE 2 AC2 16 LYS B 60 PHE B 74 ARG B 78 ARG B 99
SITE 3 AC2 16 SER B 103 GLY B 104 TYR B 107 HOH B2085
SITE 4 AC2 16 HOH B2112 HOH B2157 HOH B2213 HOH B2214
CRYST1 49.060 58.790 71.710 90.00 95.78 90.00 P 1 21 1 4
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 0.020383 0.000000 0.002063 0.00000
SCALE2 0.000000 0.017010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014016 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
