HEADER TRANSFERASE 12-JAN-03 1NMX
TITLE CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE KINASE WITH FLTMP AND ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIMILAR TO THYMIDYLATE KINASE (DTMP KINASE);
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.4.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 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 THYMIDYLATE KINASE, P-LOOP, FLUOROTHYMIDINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,D.SEGURA-PENA,C.MEIER,T.VEIT,M.MONNERJAHN,M.KONRAD,
AUTHOR 2 A.LAVIE
REVDAT 6 14-FEB-24 1NMX 1 REMARK
REVDAT 5 27-OCT-21 1NMX 1 REMARK SEQADV LINK
REVDAT 4 11-OCT-17 1NMX 1 REMARK
REVDAT 3 13-JUL-11 1NMX 1 VERSN
REVDAT 2 24-FEB-09 1NMX 1 VERSN
REVDAT 1 18-MAR-03 1NMX 0
JRNL AUTH N.OSTERMANN,D.SEGURA-PENA,C.MEIER,T.VEIT,M.MONNERJAHN,
JRNL AUTH 2 M.KONRAD,A.LAVIE
JRNL TITL STRUCTURES OF HUMAN THYMIDYLATE KINASE IN COMPLEX WITH
JRNL TITL 2 PRODRUGS: IMPLICATIONS FOR THE STRUCTURE-BASED DESIGN OF
JRNL TITL 3 NOVEL COMPOUNDS
JRNL REF BIOCHEMISTRY V. 42 2568 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12614151
JRNL DOI 10.1021/BI027302T
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 28602
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2842
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1650
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 323
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) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; 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 1NMX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018018.
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 : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9076
REMARK 200 MONOCHROMATOR : NULL
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28602
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 32.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: ISOMORPHOUS WITH KNOWN STRUCTURE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 100 MM TRIS/HCL PH 8.0, 5%
REMARK 280 STERILE FILTERED DEAD SEA WATER, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 25.00600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.75750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.75750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.50900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.75750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.75750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.50300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.75750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.75750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.50900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.75750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.75750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 12.50300
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 25.00600
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: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 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 0.000000 -1.000000 0.000000 101.51500
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 101.51500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 25.00600
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG A 402 LIES ON A SPECIAL POSITION.
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
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 HIS A 148 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 205 CG CD CE NZ
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 OE1 GLN A 157 O HOH A 514 1.95
REMARK 500 NE2 GLN A 166 O HOH A 726 2.04
REMARK 500 O HOH A 655 O HOH A 813 2.06
REMARK 500 O HOH A 531 O HOH A 768 2.06
REMARK 500 O HOH A 510 O HOH A 512 2.07
REMARK 500 O HOH A 693 O HOH A 770 2.08
REMARK 500 O HOH A 682 O HOH A 684 2.11
REMARK 500 O HOH A 791 O HOH A 792 2.12
REMARK 500 O HOH A 794 O HOH A 795 2.15
REMARK 500 O HOH A 633 O HOH A 809 2.17
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 O HOH A 727 O HOH A 795 8665 1.94
REMARK 500 O HOH A 783 O HOH A 783 8665 2.04
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 4 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 15 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -3.6 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 97 148.98 74.72
REMARK 500 TYR A 98 -147.33 -149.26
REMARK 500 PHE A 146 -179.49 -56.18
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 20 OG
REMARK 620 2 ADP A 302 O2B 91.1
REMARK 620 3 HOH A 504 O 85.5 96.6
REMARK 620 4 HOH A 505 O 88.0 176.3 86.9
REMARK 620 5 HOH A 506 O 93.3 89.8 173.4 86.6
REMARK 620 6 HOH A 507 O 175.5 91.1 90.4 90.1 90.6
REMARK 620 N 1 2 3 4 5
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 A 501 O
REMARK 620 2 HOH A 501 O 176.2
REMARK 620 3 HOH A 502 O 90.2 86.1
REMARK 620 4 HOH A 502 O 91.4 87.6 86.4
REMARK 620 5 HOH A 503 O 97.5 83.4 90.9 170.7
REMARK 620 6 HOH A 503 O 88.9 94.7 179.0 94.1 88.7
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 FDM 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
DBREF 1NMX A 1 212 UNP P23919 DTYMK_HUMAN 1 212
SEQADV 1NMX GLY A -2 UNP P23919 CLONING ARTIFACT
SEQADV 1NMX SER A -1 UNP P23919 CLONING ARTIFACT
SEQADV 1NMX HIS A 0 UNP P23919 CLONING ARTIFACT
SEQADV 1NMX ALA A 200 UNP P23919 ARG 200 ENGINEERED MUTATION
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 PHE 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 GLY GLU LEU TRP LYS
HET MG A 401 1
HET MG A 402 1
HET FDM A 301 21
HET ADP A 302 27
HETNAM MG MAGNESIUM ION
HETNAM FDM 3'-FLUORO-3'-DEOXYTHYMIDINE MONOPHOSPHATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN FDM PHOSPHORIC ACID MONO-[3-FLUORO-5-(5-METHYL-2,4-DIOXO-3,
HETSYN 2 FDM 4-DIHYDRO-2H-PYRIMIDIN-1-YL)-TETRAHYRO-FURAN-2-
HETSYN 3 FDM YLMETHYL] ESTER
FORMUL 2 MG 2(MG 2+)
FORMUL 4 FDM C10 H14 F N2 O7 P
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 HOH *323(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 LYS A 142 1 7
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 VAL A 94 N LEU A 40
SHEET 3 A 5 LEU A 8 GLY A 13 1 N ILE A 9 O LEU A 93
SHEET 4 A 5 LEU A 129 GLN A 134 1 O LEU A 131 N VAL A 10
SHEET 5 A 5 TRP A 175 ASP A 179 1 O VAL A 178 N GLN A 134
LINK OG SER A 20 MG MG A 401 1555 1555 2.08
LINK O2B ADP A 302 MG MG A 401 1555 1555 2.05
LINK MG MG A 401 O HOH A 504 1555 1555 2.20
LINK MG MG A 401 O HOH A 505 1555 1555 2.06
LINK MG MG A 401 O HOH A 506 1555 1555 2.07
LINK MG MG A 401 O HOH A 507 1555 1555 2.13
LINK MG MG A 402 O HOH A 501 1555 1555 2.12
LINK MG MG A 402 O HOH A 501 1555 8665 2.27
LINK MG MG A 402 O HOH A 502 1555 1555 2.21
LINK MG MG A 402 O HOH A 502 1555 8665 2.16
LINK MG MG A 402 O HOH A 503 1555 1555 2.10
LINK MG MG A 402 O HOH A 503 1555 8665 2.04
CISPEP 1 PHE A 42 PRO A 43 0 -1.39
SITE 1 AC1 6 SER A 20 ADP A 302 HOH A 504 HOH A 505
SITE 2 AC1 6 HOH A 506 HOH A 507
SITE 1 AC2 3 HOH A 501 HOH A 502 HOH A 503
SITE 1 AC3 16 PHE A 42 PHE A 72 ARG A 76 ARG A 97
SITE 2 AC3 16 GLY A 102 PHE A 105 TYR A 151 HOH A 504
SITE 3 AC3 16 HOH A 505 HOH A 507 HOH A 509 HOH A 529
SITE 4 AC3 16 HOH A 555 HOH A 641 HOH A 684 HOH A 699
SITE 1 AC4 24 ARG A 16 ALA A 17 GLY A 18 LYS A 19
SITE 2 AC4 24 SER A 20 THR A 21 ARG A 143 LYS A 182
SITE 3 AC4 24 SER A 183 ILE A 184 ARG A 192 MG A 401
SITE 4 AC4 24 HOH A 506 HOH A 507 HOH A 508 HOH A 538
SITE 5 AC4 24 HOH A 574 HOH A 583 HOH A 592 HOH A 622
SITE 6 AC4 24 HOH A 649 HOH A 654 HOH A 681 HOH A 770
CRYST1 101.515 101.515 50.012 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 0.009851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019995 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
