HEADER TRANSFERASE 30-MAY-14 4UNS
TITLE MTB TMK IN COMPLEX WITH COMPOUND 40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-210;
COMPND 5 SYNONYM: DTMP KINASE;
COMPND 6 EC: 2.7.4.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, ATP TMP PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.READ,S.HUSSEIN,H.GINGELL,J.TUCKER
REVDAT 4 10-JAN-24 4UNS 1 REMARK LINK
REVDAT 3 04-APR-18 4UNS 1 REMARK
REVDAT 2 22-JUL-15 4UNS 1 JRNL
REVDAT 1 17-JUN-15 4UNS 0
JRNL AUTH M.NAIK,A.RAICHURKAR,B.S.BANDODKAR,B.V.VARUN,S.BHAT,
JRNL AUTH 2 R.KALKHAMBKAR,K.MURUGAN,R.MENON,J.BHAT,B.PAUL,H.IYER,
JRNL AUTH 3 S.HUSSEIN,J.A.TUCKER,M.VOGTHERR,K.J.EMBREY,H.MCMIKEN,
JRNL AUTH 4 S.PRASAD,A.GILL,B.G.UGARKAR,J.VENKATRAMAN,J.READ,M.PANDA
JRNL TITL STRUCTURE GUIDED LEAD GENERATION FOR M. TUBERCULOSIS
JRNL TITL 2 THYMIDYLATE KINASE (MTB TMK): DISCOVERY OF 3-CYANOPYRIDONE
JRNL TITL 3 AND 1,6-NAPHTHYRIDIN-2-ONE AS POTENT INHIBITORS.
JRNL REF J.MED.CHEM. V. 58 753 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25486447
JRNL DOI 10.1021/JM5012947
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 22586
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1217
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) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : 0.56000
REMARK 3 B33 (A**2) : -0.84000
REMARK 3 B12 (A**2) : 0.28000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.217
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.654
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2867 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1825 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3910 ; 1.281 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4408 ; 0.860 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 5.067 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;30.406 ;22.807
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 399 ;13.764 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;19.911 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 436 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3379 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 624 ; 0.001 ; 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): 1862 ; 0.621 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 786 ; 0.116 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2903 ; 1.156 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1005 ; 1.822 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1007 ; 3.087 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 1 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5893 24.1394 -13.4736
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: 0.0054
REMARK 3 T33: 0.0260 T12: -0.0103
REMARK 3 T13: 0.0218 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.1451 L22: 1.2466
REMARK 3 L33: 1.3080 L12: 0.3138
REMARK 3 L13: -0.3695 L23: -0.5749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: 0.0001 S13: -0.0336
REMARK 3 S21: 0.0153 S22: 0.0061 S23: 0.0088
REMARK 3 S31: -0.0467 S32: 0.0021 S33: 0.0291
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 1 B 209
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1556 12.7815 13.9088
REMARK 3 T TENSOR
REMARK 3 T11: 0.0284 T22: 0.0444
REMARK 3 T33: 0.0650 T12: 0.0079
REMARK 3 T13: 0.0198 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 1.8098 L22: 0.9128
REMARK 3 L33: 1.9156 L12: 0.7010
REMARK 3 L13: -1.3908 L23: -0.2341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0719 S12: 0.0716 S13: 0.0901
REMARK 3 S21: -0.0190 S22: 0.0245 S23: 0.0671
REMARK 3 S31: -0.0530 S32: -0.1639 S33: -0.0964
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4UNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1290060814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 72.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: PDB ENTRY 1G3U
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 47.87800
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 23.93900
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 LEU A 145
REMARK 465 ALA A 146
REMARK 465 GLY A 147
REMARK 465 GLU A 148
REMARK 465 ARG A 149
REMARK 465 SER A 150
REMARK 465 ARG A 151
REMARK 465 GLY A 152
REMARK 465 ARG A 153
REMARK 465 ALA A 154
REMARK 465 GLN A 155
REMARK 465 ARG A 156
REMARK 465 ASP A 157
REMARK 465 PRO A 158
REMARK 465 GLY A 159
REMARK 465 ARG A 160
REMARK 465 ALA A 161
REMARK 465 ARG A 162
REMARK 465 ASP A 163
REMARK 465 ASN A 164
REMARK 465 TYR A 165
REMARK 465 GLU A 166
REMARK 465 ARG A 167
REMARK 465 PRO A 210
REMARK 465 GLY B 147
REMARK 465 GLU B 148
REMARK 465 ARG B 149
REMARK 465 SER B 150
REMARK 465 ARG B 151
REMARK 465 GLY B 152
REMARK 465 ARG B 153
REMARK 465 ALA B 154
REMARK 465 GLN B 155
REMARK 465 ARG B 156
REMARK 465 ASP B 157
REMARK 465 PRO B 158
REMARK 465 GLY B 159
REMARK 465 ARG B 160
REMARK 465 ALA B 161
REMARK 465 ARG B 162
REMARK 465 ASP B 163
REMARK 465 ASN B 164
REMARK 465 TYR B 165
REMARK 465 GLU B 166
REMARK 465 ARG B 167
REMARK 465 PRO B 210
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 LYS A 19 CE NZ
REMARK 470 LYS A 115 CD CE NZ
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 GLU A 170 CG CD OE1 OE2
REMARK 470 ARG A 202 CZ NH1 NH2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 145 CG CD1 CD2
REMARK 470 ARG B 202 CG CD NE CZ NH1 NH2
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 OD1 ASP B 9 O HOH B 2005 2.11
REMARK 500 O HOH B 2005 O HOH B 2008 2.16
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 95 140.76 72.99
REMARK 500 TYR A 96 -151.28 -149.26
REMARK 500 ARG B 95 143.72 75.97
REMARK 500 TYR B 96 -147.35 -157.32
REMARK 500 ALA B 208 130.92 -26.32
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 A2001 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A2129 DISTANCE = 6.07 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 NA A1211 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 108 O
REMARK 620 2 HOH A2075 O 87.8
REMARK 620 3 HOH A2076 O 93.1 173.7
REMARK 620 4 HOH A2081 O 98.4 97.0 76.7
REMARK 620 5 HOH B2035 O 178.4 93.8 85.3 81.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B1211 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2076 O
REMARK 620 2 LEU B 108 O 171.4
REMARK 620 3 HOH B2035 O 92.5 93.5
REMARK 620 4 HOH B2036 O 92.5 81.1 173.9
REMARK 620 5 HOH B2040 O 87.6 99.2 82.6 100.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QZ3 A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QZ3 B 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1211
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UNN RELATED DB: PDB
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 8
REMARK 900 RELATED ID: 4UNP RELATED DB: PDB
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 34
REMARK 900 RELATED ID: 4UNQ RELATED DB: PDB
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 36
REMARK 900 RELATED ID: 4UNR RELATED DB: PDB
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 23
DBREF 4UNS A 1 210 UNP F2GKC3 F2GKC3_MYCTX 1 210
DBREF 4UNS B 1 210 UNP F2GKC3 F2GKC3_MYCTX 1 210
SEQRES 1 A 210 MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS
SEQRES 2 A 210 ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA
SEQRES 3 A 210 ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR
SEQRES 4 A 210 GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU
SEQRES 5 A 210 HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA
SEQRES 6 A 210 MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL
SEQRES 7 A 210 HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL
SEQRES 8 A 210 ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER
SEQRES 9 A 210 ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA
SEQRES 10 A 210 ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU
SEQRES 11 A 210 PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA
SEQRES 12 A 210 GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG
SEQRES 13 A 210 ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA
SEQRES 14 A 210 GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU
SEQRES 15 A 210 ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY
SEQRES 16 A 210 ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA
SEQRES 17 A 210 PRO PRO
SEQRES 1 B 210 MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS
SEQRES 2 B 210 ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA
SEQRES 3 B 210 ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR
SEQRES 4 B 210 GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU
SEQRES 5 B 210 HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA
SEQRES 6 B 210 MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL
SEQRES 7 B 210 HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL
SEQRES 8 B 210 ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER
SEQRES 9 B 210 ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA
SEQRES 10 B 210 ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU
SEQRES 11 B 210 PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA
SEQRES 12 B 210 GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG
SEQRES 13 B 210 ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA
SEQRES 14 B 210 GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU
SEQRES 15 B 210 ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY
SEQRES 16 B 210 ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA
SEQRES 17 B 210 PRO PRO
HET QZ3 A1210 27
HET NA A1211 1
HET QZ3 B1210 27
HET NA B1211 1
HETNAM QZ3 N-[4-(3-CYANO-7-ETHYL-5-METHYL-2-OXO-1H-1,6-
HETNAM 2 QZ3 NAPHTHYRIDIN-4-YL)PHENYL]METHANESULFONAMIDE
HETNAM NA SODIUM ION
FORMUL 3 QZ3 2(C19 H18 N4 O3 S)
FORMUL 4 NA 2(NA 1+)
FORMUL 7 HOH *211(H2 O)
HELIX 1 1 GLY A 12 ALA A 27 1 16
HELIX 2 2 SER A 42 HIS A 53 1 12
HELIX 3 3 ASP A 58 SER A 61 5 4
HELIX 4 4 SER A 62 ALA A 77 1 16
HELIX 5 5 ALA A 77 TYR A 88 1 12
HELIX 6 6 TYR A 96 LEU A 108 1 13
HELIX 7 7 GLY A 114 PHE A 125 1 12
HELIX 8 8 ASP A 168 GLY A 186 1 19
HELIX 9 9 ASP A 199 ALA A 208 1 10
HELIX 10 10 GLY B 12 ALA B 27 1 16
HELIX 11 11 SER B 42 HIS B 53 1 12
HELIX 12 12 ASP B 58 SER B 61 5 4
HELIX 13 13 SER B 62 GLY B 76 1 15
HELIX 14 14 ALA B 77 TYR B 88 1 12
HELIX 15 15 TYR B 96 LEU B 108 1 13
HELIX 16 16 GLY B 114 PHE B 125 1 12
HELIX 17 17 ASP B 168 GLY B 186 1 19
HELIX 18 18 ASP B 199 ALA B 208 1 10
SHEET 1 AA 5 VAL A 31 ALA A 35 0
SHEET 2 AA 5 VAL A 90 ASP A 94 1 O VAL A 90 N ALA A 32
SHEET 3 AA 5 LEU A 2 GLU A 6 1 O ILE A 3 N LEU A 93
SHEET 4 AA 5 TRP A 135 LEU A 139 1 O TRP A 135 N ALA A 4
SHEET 5 AA 5 ARG A 190 VAL A 194 1 O ARG A 190 N GLN A 136
SHEET 1 BA 5 VAL B 31 ALA B 35 0
SHEET 2 BA 5 VAL B 90 ASP B 94 1 O VAL B 90 N ALA B 32
SHEET 3 BA 5 LEU B 2 GLU B 6 1 O ILE B 3 N LEU B 93
SHEET 4 BA 5 TRP B 135 LEU B 139 1 O TRP B 135 N ALA B 4
SHEET 5 BA 5 ARG B 190 VAL B 194 1 O ARG B 190 N GLN B 136
LINK O LEU A 108 NA NA A1211 1555 1555 2.48
LINK NA NA A1211 O HOH A2075 1555 1555 2.31
LINK NA NA A1211 O HOH A2076 1555 1555 2.48
LINK NA NA A1211 O HOH A2081 1555 1555 2.84
LINK NA NA A1211 O HOH B2035 1555 2554 2.63
LINK O HOH A2076 NA NA B1211 3555 1555 2.47
LINK O LEU B 108 NA NA B1211 1555 1555 2.43
LINK NA NA B1211 O HOH B2035 1555 1555 2.32
LINK NA NA B1211 O HOH B2036 1555 1555 2.33
LINK NA NA B1211 O HOH B2040 1555 1555 2.58
CISPEP 1 PHE A 36 PRO A 37 0 -6.09
CISPEP 2 PHE B 36 PRO B 37 0 -2.50
SITE 1 AC1 14 ASP A 9 PRO A 37 TYR A 39 MET A 66
SITE 2 AC1 14 PHE A 70 ARG A 74 ARG A 95 ASN A 100
SITE 3 AC1 14 TYR A 103 ARG A 107 HOH A2014 HOH A2045
SITE 4 AC1 14 HOH A2127 HOH A2128
SITE 1 AC2 10 ASP B 9 PRO B 37 TYR B 39 MET B 66
SITE 2 AC2 10 PHE B 70 ARG B 74 ARG B 95 ASN B 100
SITE 3 AC2 10 TYR B 103 HOH B2005
SITE 1 AC3 6 LEU A 108 HOH A2075 HOH A2076 HOH A2081
SITE 2 AC3 6 NA B1211 HOH B2035
SITE 1 AC4 6 NA A1211 HOH A2076 LEU B 108 HOH B2035
SITE 2 AC4 6 HOH B2036 HOH B2040
CRYST1 75.513 75.513 71.817 90.00 90.00 120.00 P 32 6
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 0.013243 0.007646 0.000000 0.00000
SCALE2 0.000000 0.015291 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013924 0.00000
(ATOM LINES ARE NOT SHOWN.)
END