HEADER TRANSFERASE 22-AUG-14 4UXI
TITLE LEISHMANIA MAJOR THYMIDINE KINASE IN COMPLEX WITH THYMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDINE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-183;
COMPND 5 EC: 2.7.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 STRAIN: FRIEDLIN;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TRANSFERASE, AP5DT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.TIMM,C.BOSCH-NAVARRETE,E.RECIO,J.E.NETTLESHIP,H.RADA,
AUTHOR 2 D.GONZALEZ-PACANOWSKA,K.S.WILSON
REVDAT 2 02-MAR-16 4UXI 1 REMARK
REVDAT 1 27-MAY-15 4UXI 0
JRNL AUTH J.TIMM,C.BOSCH-NAVARRETE,E.RECIO,J.E.NETTLESHIP,H.RADA,
JRNL AUTH 2 D.GONZALEZ-PACANOWSKA,K.S.WILSON
JRNL TITL STRUCTURAL AND KINETIC CHARACTERIZATION OF THYMIDINE KINASE
JRNL TITL 2 FROM LEISHMANIA MAJOR.
JRNL REF PLOS NEGL TROP DIS V. 9 3781 2015
JRNL REFN ISSN 1935-2727
JRNL PMID 25978379
JRNL DOI 10.1371/JOURNAL.PNTD.0003781
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 104.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.01
REMARK 3 NUMBER OF REFLECTIONS : 12506
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) : 0.28353
REMARK 3 R VALUE (WORKING SET) : 0.28221
REMARK 3 FREE R VALUE : 0.31039
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 648
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) : 2.744
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.815
REMARK 3 REFLECTION IN BIN (WORKING SET) : 919
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.348
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.335
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2370
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.399
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58
REMARK 3 B22 (A**2) : 0.58
REMARK 3 B33 (A**2) : -1.89
REMARK 3 B12 (A**2) : 0.29
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.745
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.387
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.348
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.220
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2459 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2225 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3337 ; 1.292 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5062 ; 0.868 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 320 ; 5.666 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 95 ;27.480 ;23.368
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;13.452 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;10.797 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2799 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 553 ; 0.002 ; 0.020
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): 1292 ; 1.961 ; 4.306
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1291 ; 1.961 ; 4.304
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1608 ; 3.272 ; 6.445
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1167 ; 2.864 ; 4.464
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 180 B 3 180 8009 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 181
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8107 42.3481 4.0363
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: 0.4141
REMARK 3 T33: 0.1614 T12: -0.1277
REMARK 3 T13: -0.1423 T23: 0.0846
REMARK 3 L TENSOR
REMARK 3 L11: 1.6987 L22: 2.9641
REMARK 3 L33: 3.4368 L12: 0.1910
REMARK 3 L13: 1.1408 L23: -1.1806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: -0.0802 S13: 0.2628
REMARK 3 S21: 0.1936 S22: 0.0271 S23: -0.1987
REMARK 3 S31: 0.5291 S32: 0.1132 S33: -0.0358
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 180
REMARK 3 ORIGIN FOR THE GROUP (A): -39.1026 61.0724 3.2874
REMARK 3 T TENSOR
REMARK 3 T11: 0.7937 T22: 0.7405
REMARK 3 T33: 0.1772 T12: 0.3897
REMARK 3 T13: -0.0830 T23: 0.1629
REMARK 3 L TENSOR
REMARK 3 L11: 4.0539 L22: 1.0096
REMARK 3 L33: 3.5195 L12: 1.5068
REMARK 3 L13: 1.0957 L23: -0.5666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: 0.1575 S13: -0.0923
REMARK 3 S21: 0.5722 S22: 0.4301 S23: -0.0722
REMARK 3 S31: -1.2124 S32: -1.2257 S33: -0.3846
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 WITH TLS ADDED
REMARK 4
REMARK 4 4UXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-AUG-14.
REMARK 100 THE PDBE ID CODE IS EBI-61573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13223
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.74
REMARK 200 RESOLUTION RANGE LOW (A) : 52.46
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 20.5
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 20.3
REMARK 200 R MERGE FOR SHELL (I) : 1.17
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M NA/K PO4 PH 5.4, 1 MM
REMARK 280 DTHD, 1 MM APPNHP, 3 MM MGCL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 77.48000
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 38.74000
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 58.11000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.37000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.85000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.48000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 38.74000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 19.37000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 58.11000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 96.85000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.9 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 0.500000 0.866025 0.000000 -60.57450
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 104.91811
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -19.37000
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 GLY A 0
REMARK 465 PRO A 1
REMARK 465 LYS A 42
REMARK 465 ASP A 43
REMARK 465 THR A 44
REMARK 465 ARG A 45
REMARK 465 TYR A 46
REMARK 465 ASP A 47
REMARK 465 GLU A 48
REMARK 465 HIS A 49
REMARK 465 ASN A 50
REMARK 465 VAL A 51
REMARK 465 ALA A 52
REMARK 465 SER A 53
REMARK 465 HIS A 54
REMARK 465 ASP A 55
REMARK 465 GLN A 56
REMARK 465 LEU A 57
REMARK 465 LEU A 182
REMARK 465 PRO A 183
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 PHE B 2
REMARK 465 LYS B 42
REMARK 465 ASP B 43
REMARK 465 THR B 44
REMARK 465 ARG B 45
REMARK 465 TYR B 46
REMARK 465 ASP B 47
REMARK 465 GLU B 48
REMARK 465 HIS B 49
REMARK 465 ASN B 50
REMARK 465 VAL B 51
REMARK 465 ALA B 52
REMARK 465 SER B 53
REMARK 465 HIS B 54
REMARK 465 ASP B 55
REMARK 465 GLN B 56
REMARK 465 LEU B 57
REMARK 465 MET B 58
REMARK 465 LEU B 59
REMARK 465 GLN B 181
REMARK 465 LEU B 182
REMARK 465 PRO B 183
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 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 ARG A 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 MET A 58 CG SD CE
REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 62 CG CD OE1 NE2
REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 MET A 107 CE
REMARK 470 LYS A 118 CG CD CE NZ
REMARK 470 THR A 137 CG2
REMARK 470 MET A 141 CG SD CE
REMARK 470 HIS A 144 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 158 CG CD OE1 OE2
REMARK 470 ASP A 167 CG OD1 OD2
REMARK 470 GLU A 175 CG CD OE1 OE2
REMARK 470 SER A 178 OG
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 GLN A 181 CG CD OE1 NE2
REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 26 CG CD CE NZ
REMARK 470 ARG B 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 33 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 60 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 62 CG CD OE1 NE2
REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 73 CG OD1 OD2
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 94 CG OD1 OD2
REMARK 470 THR B 98 OG1 CG2
REMARK 470 MET B 107 CE
REMARK 470 ARG B 116 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 118 CG CD CE NZ
REMARK 470 HIS B 144 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 145 CG CD OE1 OE2
REMARK 470 ARG B 152 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 156 CG OD1 ND2
REMARK 470 VAL B 157 CG1 CG2
REMARK 470 GLU B 158 CG CD OE1 OE2
REMARK 470 GLN B 159 CG CD OE1 NE2
REMARK 470 ILE B 163 CG1 CG2 CD1
REMARK 470 ILE B 170 CG1 CG2 CD1
REMARK 470 GLU B 175 CG CD OE1 OE2
REMARK 470 GLN B 180 CG CD OE1 NE2
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 ARG A 72 -121.14 48.10
REMARK 500 HIS A 144 19.79 53.64
REMARK 500 GLU A 145 38.05 -148.94
REMARK 500 ASN A 156 68.33 -105.66
REMARK 500 ARG B 72 -133.66 58.06
REMARK 500 MET B 142 -60.35 -94.48
REMARK 500 HIS B 144 19.82 52.83
REMARK 500 GLU B 145 36.14 -146.76
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 A1184 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 143 SG
REMARK 620 2 CYS A 176 SG 105.8
REMARK 620 3 CYS A 140 SG 104.4 94.3
REMARK 620 4 CYS A 173 SG 118.3 107.7 122.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1183 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 143 SG
REMARK 620 2 CYS B 140 SG 106.9
REMARK 620 3 CYS B 173 SG 119.1 119.3
REMARK 620 4 CYS B 176 SG 108.1 93.8 106.2
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 PO4 A1182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM A1183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM B1182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1184
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UXH RELATED DB: PDB
REMARK 900 LEISHMANIA MAJOR THYMIDINE KINASE IN COMPLEX WITH AP5DT
REMARK 900 RELATED ID: 4UXJ RELATED DB: PDB
REMARK 900 LEISHMANIA MAJOR THYMIDINE KINASE IN COMPLEX WITH DTTP
DBREF 4UXI A 2 183 UNP Q4QC75 Q4QC75_LEIMA 2 183
DBREF 4UXI B 2 183 UNP Q4QC75 Q4QC75_LEIMA 2 183
SEQADV 4UXI GLY A 0 UNP Q4QC75 EXPRESSION TAG
SEQADV 4UXI PRO A 1 UNP Q4QC75 EXPRESSION TAG
SEQADV 4UXI GLY B 0 UNP Q4QC75 EXPRESSION TAG
SEQADV 4UXI PRO B 1 UNP Q4QC75 EXPRESSION TAG
SEQRES 1 A 184 GLY PRO PHE ARG GLY ARG ILE GLU LEU ILE ILE GLY PRO
SEQRES 2 A 184 MET PHE ALA GLY LYS THR THR GLU LEU MET ARG ARG VAL
SEQRES 3 A 184 LYS ARG GLU ILE HIS ALA ARG ARG SER CYS PHE VAL ILE
SEQRES 4 A 184 LYS TYR SER LYS ASP THR ARG TYR ASP GLU HIS ASN VAL
SEQRES 5 A 184 ALA SER HIS ASP GLN LEU MET LEU ARG ALA GLN ALA ALA
SEQRES 6 A 184 VAL SER GLN LEU THR GLU VAL ARG ASP THR TRP LYS ARG
SEQRES 7 A 184 PHE ASP VAL LEU ALA ILE ASP GLU GLY GLN PHE PHE SER
SEQRES 8 A 184 ASP LEU VAL ASP PHE CYS ASN THR ALA ALA ASP ALA GLY
SEQRES 9 A 184 LYS VAL VAL MET VAL SER ALA LEU ASP GLY ASP TYR ARG
SEQRES 10 A 184 ARG LYS PRO PHE GLY GLN ILE CYS GLU LEU VAL PRO TYR
SEQRES 11 A 184 CYS GLU ALA VAL ASP LYS LEU THR ALA VAL CYS MET MET
SEQRES 12 A 184 CYS HIS GLU GLN PRO ALA CYS PHE THR ARG ARG THR VAL
SEQRES 13 A 184 ASN VAL GLU GLN GLN GLU LEU ILE GLY GLY ALA ASP MET
SEQRES 14 A 184 TYR ILE ALA THR CYS ARG GLU CYS TYR SER LYS GLN GLN
SEQRES 15 A 184 LEU PRO
SEQRES 1 B 184 GLY PRO PHE ARG GLY ARG ILE GLU LEU ILE ILE GLY PRO
SEQRES 2 B 184 MET PHE ALA GLY LYS THR THR GLU LEU MET ARG ARG VAL
SEQRES 3 B 184 LYS ARG GLU ILE HIS ALA ARG ARG SER CYS PHE VAL ILE
SEQRES 4 B 184 LYS TYR SER LYS ASP THR ARG TYR ASP GLU HIS ASN VAL
SEQRES 5 B 184 ALA SER HIS ASP GLN LEU MET LEU ARG ALA GLN ALA ALA
SEQRES 6 B 184 VAL SER GLN LEU THR GLU VAL ARG ASP THR TRP LYS ARG
SEQRES 7 B 184 PHE ASP VAL LEU ALA ILE ASP GLU GLY GLN PHE PHE SER
SEQRES 8 B 184 ASP LEU VAL ASP PHE CYS ASN THR ALA ALA ASP ALA GLY
SEQRES 9 B 184 LYS VAL VAL MET VAL SER ALA LEU ASP GLY ASP TYR ARG
SEQRES 10 B 184 ARG LYS PRO PHE GLY GLN ILE CYS GLU LEU VAL PRO TYR
SEQRES 11 B 184 CYS GLU ALA VAL ASP LYS LEU THR ALA VAL CYS MET MET
SEQRES 12 B 184 CYS HIS GLU GLN PRO ALA CYS PHE THR ARG ARG THR VAL
SEQRES 13 B 184 ASN VAL GLU GLN GLN GLU LEU ILE GLY GLY ALA ASP MET
SEQRES 14 B 184 TYR ILE ALA THR CYS ARG GLU CYS TYR SER LYS GLN GLN
SEQRES 15 B 184 LEU PRO
HET PO4 A1182 5
HET PO4 B1181 5
HET THM A1183 17
HET THM B1182 17
HET ZN B1183 1
HET ZN A1184 1
HETNAM THM THYMIDINE
HETNAM PO4 PHOSPHATE ION
HETNAM ZN ZINC ION
HETSYN THM DEOXYTHYMIDINE
FORMUL 3 THM 2(C10 H14 N2 O5)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 HOH *13(H2 O)
HELIX 1 1 GLY A 16 ALA A 31 1 16
HELIX 2 2 GLN A 67 ARG A 72 5 6
HELIX 3 3 ASP A 73 PHE A 78 5 6
HELIX 4 4 GLY A 86 PHE A 89 5 4
HELIX 5 5 ASP A 91 ALA A 102 1 12
HELIX 6 6 GLN A 122 VAL A 127 1 6
HELIX 7 7 PRO A 128 CYS A 130 5 3
HELIX 8 8 CYS A 173 LYS A 179 1 7
HELIX 9 9 GLY B 16 ALA B 31 1 16
HELIX 10 10 GLN B 67 ARG B 72 5 6
HELIX 11 11 ASP B 73 PHE B 78 5 6
HELIX 12 12 GLY B 86 PHE B 89 5 4
HELIX 13 13 ASP B 91 ALA B 102 1 12
HELIX 14 14 GLN B 122 VAL B 127 1 6
HELIX 15 15 PRO B 128 CYS B 130 5 3
HELIX 16 16 CYS B 173 LYS B 179 1 7
SHEET 1 AA 6 ARG A 60 VAL A 65 0
SHEET 2 AA 6 CYS A 35 TYR A 40 1 O CYS A 35 N ALA A 61
SHEET 3 AA 6 VAL A 80 ASP A 84 1 O VAL A 80 N PHE A 36
SHEET 4 AA 6 VAL A 105 SER A 109 1 O VAL A 105 N LEU A 81
SHEET 5 AA 6 ARG A 5 ILE A 10 1 O ARG A 5 N VAL A 106
SHEET 6 AA 6 ALA A 132 LYS A 135 1 O ALA A 132 N LEU A 8
SHEET 1 AB 2 ALA A 138 VAL A 139 0
SHEET 2 AB 2 PRO A 147 ALA A 148 -1 O ALA A 148 N ALA A 138
SHEET 1 AC 2 PHE A 150 ARG A 153 0
SHEET 2 AC 2 TYR A 169 THR A 172 -1 O ILE A 170 N ARG A 152
SHEET 1 BA 6 ALA B 61 VAL B 65 0
SHEET 2 BA 6 CYS B 35 TYR B 40 1 O CYS B 35 N ALA B 61
SHEET 3 BA 6 VAL B 80 ASP B 84 1 O VAL B 80 N PHE B 36
SHEET 4 BA 6 VAL B 105 SER B 109 1 O VAL B 105 N LEU B 81
SHEET 5 BA 6 ARG B 5 ILE B 10 1 O ARG B 5 N VAL B 106
SHEET 6 BA 6 ALA B 132 LYS B 135 1 O ALA B 132 N LEU B 8
SHEET 1 BB 2 ALA B 138 VAL B 139 0
SHEET 2 BB 2 PRO B 147 ALA B 148 -1 O ALA B 148 N ALA B 138
SHEET 1 BC 2 PHE B 150 ARG B 153 0
SHEET 2 BC 2 TYR B 169 THR B 172 -1 O ILE B 170 N ARG B 152
LINK ZN ZN A1184 SG CYS A 143 1555 1555 2.36
LINK ZN ZN A1184 SG CYS A 176 1555 1555 2.33
LINK ZN ZN A1184 SG CYS A 140 1555 1555 2.32
LINK ZN ZN A1184 SG CYS A 173 1555 1555 2.31
LINK ZN ZN B1183 SG CYS B 140 1555 1555 2.33
LINK ZN ZN B1183 SG CYS B 173 1555 1555 2.35
LINK ZN ZN B1183 SG CYS B 176 1555 1555 2.33
LINK ZN ZN B1183 SG CYS B 143 1555 1555 2.31
SITE 1 AC1 6 MET A 13 PHE A 14 ALA A 15 GLY A 16
SITE 2 AC1 6 LYS A 17 THR A 18
SITE 1 AC2 6 MET B 13 PHE B 14 ALA B 15 GLY B 16
SITE 2 AC2 6 LYS B 17 THR B 18
SITE 1 AC3 12 GLU A 85 LEU A 111 ASP A 114 TYR A 115
SITE 2 AC3 12 PHE A 120 THR A 151 GLN A 160 GLU A 161
SITE 3 AC3 12 LEU A 162 ILE A 163 GLY A 164 TYR A 169
SITE 1 AC4 12 GLU B 85 PHE B 88 LEU B 111 ASP B 114
SITE 2 AC4 12 TYR B 115 PHE B 120 THR B 151 GLN B 160
SITE 3 AC4 12 GLU B 161 LEU B 162 GLY B 164 TYR B 169
SITE 1 AC5 4 CYS B 140 CYS B 143 CYS B 173 CYS B 176
SITE 1 AC6 4 CYS A 140 CYS A 143 CYS A 173 CYS A 176
CRYST1 121.149 121.149 116.220 90.00 90.00 120.00 P 65 2 2 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 0.008254 0.004766 0.000000 0.00000
SCALE2 0.000000 0.009531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008604 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
