HEADER TRANSFERASE 27-FEB-17 5N9S
TITLE TTK KINASE DOMAIN IN COMPLEX WITH BAY 1161909
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN KINASE TTK;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOTYROSINE PICKED THREONINE-PROTEIN KINASE,PYT;
COMPND 5 EC: 2.7.12.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TTK, MPS1, MPS1L1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, INHIBITOR, MITOSIS, MPS1, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.UITDEHAAG,N.WILLEMSEN-SEEGERS,J.DE MAN,R.C.BUIJSMAN,G.J.R.ZAMAN
REVDAT 5 17-JAN-24 5N9S 1 REMARK
REVDAT 4 23-AUG-17 5N9S 1 REMARK
REVDAT 3 05-JUL-17 5N9S 1 JRNL
REVDAT 2 07-JUN-17 5N9S 1 JRNL REMARK
REVDAT 1 31-MAY-17 5N9S 0
JRNL AUTH J.C.M.UITDEHAAG,J.DE MAN,N.WILLEMSEN-SEEGERS,M.B.W.PRINSEN,
JRNL AUTH 2 M.A.A.LIBOUBAN,J.G.STERRENBURG,J.J.P.DE WIT,J.R.F.DE VETTER,
JRNL AUTH 3 J.A.D.M.DE ROOS,R.C.BUIJSMAN,G.J.R.ZAMAN
JRNL TITL TARGET RESIDENCE TIME-GUIDED OPTIMIZATION ON TTK KINASE
JRNL TITL 2 RESULTS IN INHIBITORS WITH POTENT ANTI-PROLIFERATIVE
JRNL TITL 3 ACTIVITY.
JRNL REF J. MOL. BIOL. V. 429 2211 2017
JRNL REFN ESSN 1089-8638
JRNL PMID 28539250
JRNL DOI 10.1016/J.JMB.2017.05.014
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19653
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1062
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1414
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
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): 0.204
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.613
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2217 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2133 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3000 ; 1.796 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4926 ; 0.838 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.573 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;41.382 ;25.644
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 413 ;18.137 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;28.976 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2445 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 490 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5N9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.966
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20720
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 60.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07700
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) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.57500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: 5N7V
REMARK 200
REMARK 200 REMARK: PRISM SHAPE, TRANSPARENT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32 - 37% PEG400 (ACROS, GEEL,
REMARK 280 BELGIUM), 0.1 M NA/K PHOSPHATE PH 6.3 AND 250 MM NACL.PH 6.3,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.79000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.92500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.79000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.92500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.79000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.09000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.92500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.79000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.09000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.92500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 SER A 503
REMARK 465 SER A 504
REMARK 465 GLY A 505
REMARK 465 VAL A 506
REMARK 465 ASP A 507
REMARK 465 LEU A 508
REMARK 465 GLY A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 ASN A 512
REMARK 465 LEU A 513
REMARK 465 TYR A 514
REMARK 465 PHE A 515
REMARK 465 ASP A 674
REMARK 465 THR A 675
REMARK 465 THR A 676
REMARK 465 SER A 677
REMARK 465 VAL A 678
REMARK 465 VAL A 679
REMARK 465 LYS A 680
REMARK 465 MET A 698
REMARK 465 SER A 699
REMARK 465 SER A 700
REMARK 465 SER A 701
REMARK 465 ARG A 702
REMARK 465 GLU A 703
REMARK 465 ASN A 704
REMARK 465 GLY A 705
REMARK 465 LYS A 706
REMARK 465 SER A 707
REMARK 465 LYS A 708
REMARK 465 SER A 709
REMARK 465 THR A 795
REMARK 465 HIS A 796
REMARK 465 LEU A 797
REMARK 465 VAL A 798
REMARK 465 ASN A 799
REMARK 465 GLN A 800
REMARK 465 MET A 801
REMARK 465 ALA A 802
REMARK 465 LYS A 803
REMARK 465 GLY A 804
REMARK 465 THR A 805
REMARK 465 THR A 806
REMARK 465 GLU A 807
REMARK 465 GLU A 808
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 ASP A 647 45.74 -140.82
REMARK 500 SER A 682 124.26 -171.11
REMARK 500 VAL A 684 127.56 176.56
REMARK 500 PRO A 757 140.84 -36.79
REMARK 500 LEU A 772 40.77 -101.59
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 A1066 DISTANCE = 7.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8QW A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5N7V RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINED UNDER RELATED EXPERIMENTAL CONDITIONS
DBREF 5N9S A 519 808 UNP P33981 TTK_HUMAN 519 808
SEQADV 5N9S MET A 496 UNP P33981 INITIATING METHIONINE
SEQADV 5N9S HIS A 497 UNP P33981 EXPRESSION TAG
SEQADV 5N9S HIS A 498 UNP P33981 EXPRESSION TAG
SEQADV 5N9S HIS A 499 UNP P33981 EXPRESSION TAG
SEQADV 5N9S HIS A 500 UNP P33981 EXPRESSION TAG
SEQADV 5N9S HIS A 501 UNP P33981 EXPRESSION TAG
SEQADV 5N9S HIS A 502 UNP P33981 EXPRESSION TAG
SEQADV 5N9S SER A 503 UNP P33981 EXPRESSION TAG
SEQADV 5N9S SER A 504 UNP P33981 EXPRESSION TAG
SEQADV 5N9S GLY A 505 UNP P33981 EXPRESSION TAG
SEQADV 5N9S VAL A 506 UNP P33981 EXPRESSION TAG
SEQADV 5N9S ASP A 507 UNP P33981 EXPRESSION TAG
SEQADV 5N9S LEU A 508 UNP P33981 EXPRESSION TAG
SEQADV 5N9S GLY A 509 UNP P33981 EXPRESSION TAG
SEQADV 5N9S THR A 510 UNP P33981 EXPRESSION TAG
SEQADV 5N9S GLU A 511 UNP P33981 EXPRESSION TAG
SEQADV 5N9S ASN A 512 UNP P33981 EXPRESSION TAG
SEQADV 5N9S LEU A 513 UNP P33981 EXPRESSION TAG
SEQADV 5N9S TYR A 514 UNP P33981 EXPRESSION TAG
SEQADV 5N9S PHE A 515 UNP P33981 EXPRESSION TAG
SEQADV 5N9S GLN A 516 UNP P33981 EXPRESSION TAG
SEQADV 5N9S SER A 517 UNP P33981 EXPRESSION TAG
SEQADV 5N9S MET A 518 UNP P33981 EXPRESSION TAG
SEQADV 5N9S LEU A 797 UNP P33981 PRO 797 CONFLICT
SEQRES 1 A 313 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 313 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER VAL LYS
SEQRES 3 A 313 GLY ARG ILE TYR SER ILE LEU LYS GLN ILE GLY SER GLY
SEQRES 4 A 313 GLY SER SER LYS VAL PHE GLN VAL LEU ASN GLU LYS LYS
SEQRES 5 A 313 GLN ILE TYR ALA ILE LYS TYR VAL ASN LEU GLU GLU ALA
SEQRES 6 A 313 ASP ASN GLN THR LEU ASP SER TYR ARG ASN GLU ILE ALA
SEQRES 7 A 313 TYR LEU ASN LYS LEU GLN GLN HIS SER ASP LYS ILE ILE
SEQRES 8 A 313 ARG LEU TYR ASP TYR GLU ILE THR ASP GLN TYR ILE TYR
SEQRES 9 A 313 MET VAL MET GLU CYS GLY ASN ILE ASP LEU ASN SER TRP
SEQRES 10 A 313 LEU LYS LYS LYS LYS SER ILE ASP PRO TRP GLU ARG LYS
SEQRES 11 A 313 SER TYR TRP LYS ASN MET LEU GLU ALA VAL HIS THR ILE
SEQRES 12 A 313 HIS GLN HIS GLY ILE VAL HIS SER ASP LEU LYS PRO ALA
SEQRES 13 A 313 ASN PHE LEU ILE VAL ASP GLY MET LEU LYS LEU ILE ASP
SEQRES 14 A 313 PHE GLY ILE ALA ASN GLN MET GLN PRO ASP THR THR SER
SEQRES 15 A 313 VAL VAL LYS ASP SER GLN VAL GLY TPO VAL ASN TYR MET
SEQRES 16 A 313 PRO PRO GLU ALA ILE LYS ASP MET SER SER SER ARG GLU
SEQRES 17 A 313 ASN GLY LYS SER LYS SER LYS ILE SER PRO LYS SER ASP
SEQRES 18 A 313 VAL TRP SER LEU GLY CYS ILE LEU TYR TYR MET THR TYR
SEQRES 19 A 313 GLY LYS THR PRO PHE GLN GLN ILE ILE ASN GLN ILE SER
SEQRES 20 A 313 LYS LEU HIS ALA ILE ILE ASP PRO ASN HIS GLU ILE GLU
SEQRES 21 A 313 PHE PRO ASP ILE PRO GLU LYS ASP LEU GLN ASP VAL LEU
SEQRES 22 A 313 LYS CYS CYS LEU LYS ARG ASP PRO LYS GLN ARG ILE SER
SEQRES 23 A 313 ILE PRO GLU LEU LEU ALA HIS PRO TYR VAL GLN ILE GLN
SEQRES 24 A 313 THR HIS LEU VAL ASN GLN MET ALA LYS GLY THR THR GLU
SEQRES 25 A 313 GLU
MODRES 5N9S TPO A 686 THR MODIFIED RESIDUE
HET TPO A 686 11
HET 8QW A 901 40
HETNAM TPO PHOSPHOTHREONINE
HETNAM 8QW (2~{R})-2-(4-FLUOROPHENYL)-~{N}-[4-[2-[(2-METHOXY-4-
HETNAM 2 8QW METHYLSULFONYL-PHENYL)AMINO]-[1,2,4]TRIAZOLO[1,5-
HETNAM 3 8QW A]PYRIDIN-6-YL]PHENYL]PROPANAMIDE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 8QW C29 H26 F N5 O4 S
FORMUL 3 HOH *66(H2 O)
HELIX 1 AA1 ASP A 561 GLN A 579 1 19
HELIX 2 AA2 LEU A 609 LYS A 615 1 7
HELIX 3 AA3 ASP A 620 HIS A 641 1 22
HELIX 4 AA4 LYS A 649 ALA A 651 5 3
HELIX 5 AA5 PRO A 691 ASP A 697 1 7
HELIX 6 AA6 SER A 712 GLY A 730 1 19
HELIX 7 AA7 ASN A 739 ASP A 749 1 11
HELIX 8 AA8 GLU A 761 LEU A 772 1 12
HELIX 9 AA9 SER A 781 LEU A 786 1 6
HELIX 10 AB1 HIS A 788 ILE A 793 1 6
SHEET 1 AA1 6 SER A 517 VAL A 520 0
SHEET 2 AA1 6 ARG A 523 GLY A 532 -1 O TYR A 525 N MET A 518
SHEET 3 AA1 6 SER A 537 ASN A 544 -1 O VAL A 539 N ILE A 531
SHEET 4 AA1 6 ILE A 549 ASN A 556 -1 O TYR A 554 N LYS A 538
SHEET 5 AA1 6 TYR A 597 MET A 602 -1 O MET A 602 N ALA A 551
SHEET 6 AA1 6 LEU A 588 ILE A 593 -1 N TYR A 589 O VAL A 601
SHEET 1 AA2 3 ILE A 607 ASP A 608 0
SHEET 2 AA2 3 PHE A 653 VAL A 656 -1 O ILE A 655 N ILE A 607
SHEET 3 AA2 3 MET A 659 LEU A 662 -1 O MET A 659 N VAL A 656
LINK C GLY A 685 N TPO A 686 1555 1555 1.34
LINK C TPO A 686 N VAL A 687 1555 1555 1.32
SITE 1 AC1 19 ILE A 531 GLN A 541 ALA A 551 LYS A 553
SITE 2 AC1 19 TYR A 568 GLU A 571 ILE A 598 MET A 600
SITE 3 AC1 19 MET A 602 GLU A 603 GLY A 605 ASN A 606
SITE 4 AC1 19 ASP A 608 SER A 611 LEU A 654 ILE A 663
SITE 5 AC1 19 ALA A 668 ASP A 681 HOH A1017
CRYST1 71.580 112.180 113.850 90.00 90.00 90.00 I 2 2 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 0.013970 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008914 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008783 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
