HEADER TRANSFERASE 10-OCT-00 1E9C
TITLE MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND APPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DTMP KINASE;
COMPND 5 EC: 2.7.4.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE, THYMIDYLATE KINASE, P-LOOP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,A.LAVIE,S.PADIYAR,R.BRUNDIERS,T.VEIT,J.REINTEIN,
AUTHOR 2 R.S.GOODY,M.KONRAD,I.SCHLICHTING
REVDAT 6 06-MAR-19 1E9C 1 REMARK
REVDAT 5 19-FEB-14 1E9C 1 HEADER KEYWDS REMARK VERSN
REVDAT 5 2 1 FORMUL LINK SITE
REVDAT 4 24-FEB-09 1E9C 1 VERSN
REVDAT 3 18-JUL-03 1E9C 1 REMARK
REVDAT 2 24-JUN-03 1E9C 1 HETATM
REVDAT 1 11-OCT-01 1E9C 0
JRNL AUTH N.OSTERMANN,A.LAVIE,S.PADIYAR,R.BRUNDIERS,T.VEIT,J.REINTEIN,
JRNL AUTH 2 R.S.GOODY,M.KONRAD,I.SCHLICHTING
JRNL TITL POTENTIATING AZT ACTIVATION: STRUCTURES OF WILDTYPE AND
JRNL TITL 2 MUTANT HUMAN THYMIDYLATE KINASE SUGGEST REASONS FOR THE
JRNL TITL 3 MUTANTS' IMPROVED KINETICS WITH THE HIV PRODRUG METABOLITE
JRNL TITL 4 AZTMP
JRNL REF J.MOL.BIOL. V. 304 43 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11071809
JRNL DOI 10.1006/JMBI.2000.4175
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.OSTERMANN,I.SCHLICHTING,R.BRUNDIERS,M.KONRAD,J.REINSTEIN,
REMARK 1 AUTH 2 T.VEIT,R.S.GOODY,A.LAVIE
REMARK 1 TITL INSIGHTS INTO THE PHOSPHORYLTRANSFER MECHANISM OF HUMAN
REMARK 1 TITL 2 THYMIDYLATE KINASE GAINED FROM CRYSTAL STRUCTURES OF ENZYME
REMARK 1 TITL 3 COMPLEXES ALONG THE REACTION COORDINATE.
REMARK 1 REF STRUCTURE V. 8 629 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10873853
REMARK 1 DOI 10.1016/S0969-2126(00)00149-0
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 30118
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1660
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 262
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.800 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1290005441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
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 : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : YES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28322
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 70.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION AT 293 K MIXING 2
REMARK 280 MICROLITERS OF A SOLUTION CONTAINING THE ENZYME, NUCLEOTIDES,
REMARK 280 AND 50 MM MGCL2 WITH 2 MICROLITERS OF A SOLUTION CONTAINING 21%
REMARK 280 PEG 3350, 100 MM TRIS HCL PH 8.0 AND 50 MICROLITERS OF DEAD SEA
REMARK 280 WATER., PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 24.60000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.65000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.90000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.65000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.30000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.65000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.65000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.90000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.65000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.65000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 12.30000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 24.60000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.7 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 -1.000000 0.000000 101.30000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 101.30000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 24.60000
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 -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
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 O1G ANP A 303 O HOH A 2261 1.99
REMARK 500 OD2 ASP A 15 O HOH A 2015 2.02
REMARK 500 O HOH A 2052 O HOH A 2055 2.02
REMARK 500 NH1 ARG A 41 O HOH A 2052 2.04
REMARK 500 O HOH A 2152 O HOH A 2243 2.08
REMARK 500 O HOH A 2179 O HOH A 2247 2.11
REMARK 500 OE2 GLU A 185 O HOH A 2205 2.12
REMARK 500 OD1 ASP A 170 N THR A 172 2.13
REMARK 500 OD2 ASP A 170 OG1 THR A 172 2.13
REMARK 500 O HOH A 2179 O HOH A 2261 2.18
REMARK 500 OE1 GLU A 85 O HOH A 2122 2.19
REMARK 500 O HOH A 2139 O HOH A 2140 2.19
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 ARG A 5 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 PHE A 42 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 PHE A 42 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 45 CD - NE - CZ ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH1 ANGL. DEV. = 4.0 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 ARG A 97 147.15 78.15
REMARK 500 TYR A 98 -143.56 -150.62
REMARK 500 TYR A 151 -7.95 79.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2008 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A2025 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A2103 DISTANCE = 6.68 ANGSTROMS
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 20 OG
REMARK 620 2 HOH A2024 O 87.3
REMARK 620 3 ANP A 303 O3G 174.3 89.0
REMARK 620 4 HOH A2248 O 86.3 87.9 89.2
REMARK 620 5 ANP A 303 O2B 89.6 176.3 94.3 93.8
REMARK 620 6 HOH A2255 O 173.0 86.6 2.6 90.2 96.7
REMARK 620 7 HOH A2249 O 90.7 87.6 93.5 174.7 90.6 92.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2057 O
REMARK 620 2 HOH A2142 O 87.7
REMARK 620 3 HOH A2057 O 97.1 96.2
REMARK 620 4 HOH A2146 O 77.6 96.3 166.1
REMARK 620 5 HOH A2142 O 80.4 167.5 89.2 77.3
REMARK 620 6 HOH A2146 O 167.7 92.5 95.1 90.2 98.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E2D RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,
REMARK 900 ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION
REMARK 900 RELATED ID: 1E2E RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,
REMARK 900 ADENOSINE DIPHOSPHATE,A MAGNESIUM-ION AND ALF3
REMARK 900 RELATED ID: 1E2F RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE,
REMARK 900 ADENOSINE DIPHOSPHATE AND A MAGNESIUM-ION
REMARK 900 RELATED ID: 1E2G RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH ADP, TDP AND A MAGNESIUM-ION
REMARK 900 RELATED ID: 1E2Q RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH TP5A AND A MAGNESIUM-ION
REMARK 900 RELATED ID: 1E98 RELATED DB: PDB
REMARK 900 WILD TYPE HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND ADP
REMARK 900 RELATED ID: 1E99 RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND ADP
REMARK 900 RELATED ID: 1E9A RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH THE BISUBSTRATE INHIBITOR
REMARK 900 AZTP5A
REMARK 900 RELATED ID: 1E9B RELATED DB: PDB
REMARK 900 HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND APPNP
REMARK 900 RELATED ID: 1E9D RELATED DB: PDB
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE (F105Y) COMPLEXED WITH AZTMP AND ADP
REMARK 900 RELATED ID: 1E9E RELATED DB: PDB
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE (F105Y) COMPLEXED WITH DTMP AND ADP
REMARK 900 RELATED ID: 1E9F RELATED DB: PDB
REMARK 900 MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND ADP
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SAMPLE COMTAINS SER183, ILE184, ASP190, AND A ILE191
REMARK 999 (CONFIRMED BY THE DNA SEQUENCE AND ELECTRON DENSITY OF
REMARK 999 SIDE-CHAINS). POSSIBLE ERROR IN SWISSPROT ENTRY.
DBREF 1E9C A -3 -1 PDB 1E9C 1E9C -3 -1
DBREF 1E9C A 1 212 UNP P23919 KTHY_HUMAN 1 212
SEQADV 1E9C ALA A 200 UNP P23919 ARG 200 ENGINEERED MUTATION
SEQADV 1E9C SER A 183 UNP P23919 ARG 183 CONFLICT
SEQADV 1E9C ASP A 190 UNP P23919 GLU 190 CONFLICT
SEQADV 1E9C ILE A 184 UNP P23919 LEU 184 CONFLICT
SEQADV 1E9C ILE A 191 UNP P23919 LEU 191 CONFLICT
SEQADV 1E9C TYR A 105 UNP P23919 PHE 105 CONFLICT
SEQADV 1E9C LYS A 208 UNP P23919 GLY 208 CONFLICT
SEQRES 1 A 215 GLY SER HIS MET ALA ALA ARG ARG GLY ALA LEU ILE VAL
SEQRES 2 A 215 LEU GLU GLY VAL ASP ARG ALA GLY LYS SER THR GLN SER
SEQRES 3 A 215 ARG LYS LEU VAL GLU ALA LEU CYS ALA ALA GLY HIS ARG
SEQRES 4 A 215 ALA GLU LEU LEU ARG PHE PRO GLU ARG SER THR GLU ILE
SEQRES 5 A 215 GLY LYS LEU LEU SER SER TYR LEU GLN LYS LYS SER ASP
SEQRES 6 A 215 VAL GLU ASP HIS SER VAL HIS LEU LEU PHE SER ALA ASN
SEQRES 7 A 215 ARG TRP GLU GLN VAL PRO LEU ILE LYS GLU LYS LEU SER
SEQRES 8 A 215 GLN GLY VAL THR LEU VAL VAL ASP ARG TYR ALA PHE SER
SEQRES 9 A 215 GLY VAL ALA TYR THR GLY ALA LYS GLU ASN PHE SER LEU
SEQRES 10 A 215 ASP TRP CYS LYS GLN PRO ASP VAL GLY LEU PRO LYS PRO
SEQRES 11 A 215 ASP LEU VAL LEU PHE LEU GLN LEU GLN LEU ALA ASP ALA
SEQRES 12 A 215 ALA LYS ARG GLY ALA PHE GLY HIS GLU ARG TYR GLU ASN
SEQRES 13 A 215 GLY ALA PHE GLN GLU ARG ALA LEU ARG CYS PHE HIS GLN
SEQRES 14 A 215 LEU MET LYS ASP THR THR LEU ASN TRP LYS MET VAL ASP
SEQRES 15 A 215 ALA SER LYS SER ILE GLU ALA VAL HIS GLU ASP ILE ARG
SEQRES 16 A 215 VAL LEU SER GLU ASP ALA ILE ALA THR ALA THR GLU LYS
SEQRES 17 A 215 PRO LEU LYS GLU LEU TRP LYS
HET TMP A 301 27
HET ADP A 302 27
HET ANP A 303 31
HET MG A 401 1
HET MG A 402 1
HETNAM TMP THYMIDINE-5'-PHOSPHATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 2 TMP C10 H15 N2 O8 P
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 ANP C10 H17 N6 O12 P3
FORMUL 5 MG 2(MG 2+)
FORMUL 7 HOH *262(H2 O)
HELIX 1 1 GLY A 18 ALA A 33 1 16
HELIX 2 2 THR A 47 GLN A 58 1 12
HELIX 3 3 GLU A 64 GLU A 78 1 15
HELIX 4 4 GLN A 79 GLN A 89 1 11
HELIX 5 5 TYR A 98 ALA A 108 1 11
HELIX 6 6 SER A 113 GLN A 119 1 7
HELIX 7 7 PRO A 120 VAL A 122 5 3
HELIX 8 8 GLN A 136 ALA A 141 1 6
HELIX 9 9 ASN A 153 MET A 168 1 16
HELIX 10 10 SER A 183 THR A 203 1 21
SHEET 1 A 5 ALA A 37 ARG A 41 0
SHEET 2 A 5 THR A 92 ASP A 96 1 O THR A 92 N GLU A 38
SHEET 3 A 5 LEU A 8 GLU A 12 1 O ILE A 9 N VAL A 95
SHEET 4 A 5 LEU A 129 GLN A 134 1 O LEU A 129 N VAL A 10
SHEET 5 A 5 TRP A 175 ASP A 179 1 O LYS A 176 N PHE A 132
LINK MG MG A 401 OG SER A 20 1555 1555 2.13
LINK MG MG A 401 O HOH A2024 1555 1555 2.13
LINK MG MG A 401 O3G ANP A 303 1555 1555 2.07
LINK MG MG A 401 O HOH A2248 1555 1555 2.19
LINK MG MG A 401 O2B ANP A 303 1555 1555 2.14
LINK MG MG A 401 O HOH A2255 1555 1555 2.12
LINK MG MG A 401 O HOH A2249 1555 1555 2.08
LINK MG MG A 402 O HOH A2057 1555 8665 2.50
LINK MG MG A 402 O HOH A2142 1555 8665 2.23
LINK MG MG A 402 O HOH A2057 1555 1555 2.13
LINK MG MG A 402 O HOH A2146 1555 1555 2.45
LINK MG MG A 402 O HOH A2142 1555 1555 2.53
LINK MG MG A 402 O HOH A2146 1555 8665 2.07
CISPEP 1 PHE A 42 PRO A 43 0 -2.53
SITE 1 AC1 7 SER A 20 ADP A 302 ANP A 303 HOH A2024
SITE 2 AC1 7 HOH A2248 HOH A2249 HOH A2255
SITE 1 AC2 3 HOH A2057 HOH A2142 HOH A2146
SITE 1 AC3 18 PHE A 42 PHE A 72 ARG A 76 ARG A 97
SITE 2 AC3 18 GLY A 102 TYR A 105 TYR A 151 ANP A 303
SITE 3 AC3 18 HOH A2015 HOH A2024 HOH A2176 HOH A2244
SITE 4 AC3 18 HOH A2245 HOH A2246 HOH A2247 HOH A2248
SITE 5 AC3 18 HOH A2255 HOH A2256
SITE 1 AC4 25 ARG A 16 ALA A 17 GLY A 18 LYS A 19
SITE 2 AC4 25 SER A 20 THR A 21 ARG A 143 LYS A 182
SITE 3 AC4 25 ILE A 184 ARG A 192 ANP A 303 MG A 401
SITE 4 AC4 25 HOH A2248 HOH A2249 HOH A2250 HOH A2251
SITE 5 AC4 25 HOH A2252 HOH A2253 HOH A2254 HOH A2255
SITE 6 AC4 25 HOH A2256 HOH A2257 HOH A2258 HOH A2259
SITE 7 AC4 25 HOH A2260
SITE 1 AC5 33 ASP A 15 ARG A 16 ALA A 17 GLY A 18
SITE 2 AC5 33 LYS A 19 SER A 20 THR A 21 ARG A 97
SITE 3 AC5 33 ARG A 143 LYS A 182 SER A 183 ILE A 184
SITE 4 AC5 33 ARG A 192 TMP A 301 ADP A 302 MG A 401
SITE 5 AC5 33 HOH A2015 HOH A2024 HOH A2030 HOH A2248
SITE 6 AC5 33 HOH A2249 HOH A2250 HOH A2252 HOH A2253
SITE 7 AC5 33 HOH A2254 HOH A2255 HOH A2256 HOH A2257
SITE 8 AC5 33 HOH A2258 HOH A2259 HOH A2260 HOH A2261
SITE 9 AC5 33 HOH A2262
CRYST1 101.300 101.300 49.200 90.00 90.00 90.00 P 43 21 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 0.009872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020325 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
