HEADER TRANSFERASE 14-SEP-15 5AP6
TITLE NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
TITLE 2 KINASE INHIBITOR DRUG RESISTANCE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY PROTEIN KINASE TTK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 519-808;
COMPND 5 SYNONYM: PHOSPHOTYROSINE PICKED THREONINE-PROTEIN KINASE, PYT,
COMPND 6 MONOPOLAR SPINDLE KINASE 1;
COMPND 7 EC: 2.7.12.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: AI
KEYWDS TRANSFERASE, MPS1, MITOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.GURDEN,I.M.WESTWOOD,A.FAISAL,S.NAUD,K.M.CHEUNG,C.MCANDREW,A.WOOD,
AUTHOR 2 J.SCHMITT,K.BOXALL,G.MAK,P.WORKMAN,R.BURKE,S.HOELDER,J.BLAGG,R.VAN
AUTHOR 3 MONTFORT,S.LINARDOPOULOS
REVDAT 2 10-JAN-24 5AP6 1 REMARK
REVDAT 1 23-SEP-15 5AP6 0
JRNL AUTH M.D.GURDEN,I.M.WESTWOOD,A.FAISAL,S.NAUD,K.J.CHEUNG,
JRNL AUTH 2 C.MCANDREW,A.WOOD,J.SCHMITT,K.BOXALL,G.MAK,P.WORKMAN,
JRNL AUTH 3 R.BURKE,S.HOELDER,J.BLAGG,R.L.M.VAN MONTFORT,S.LINARDOPOULOS
JRNL TITL NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE
JRNL TITL 2 CELLS TO KINASE INHIBITOR DRUG RESISTANCE.
JRNL REF CANCER RES. V. 75 3340 2015
JRNL REFN ISSN 0008-5472
JRNL PMID 26202014
JRNL DOI 10.1158/0008-5472.CAN-14-3272
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 24151
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1233
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.49
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2804
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2597
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2646
REMARK 3 BIN R VALUE (WORKING SET) : 0.2603
REMARK 3 BIN FREE R VALUE : 0.2493
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.63
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2077
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 79
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.26510
REMARK 3 B22 (A**2) : -6.26370
REMARK 3 B33 (A**2) : 0.99850
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.292
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.145
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.132
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.146
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.133
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2205 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2977 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 748 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 341 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2205 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 287 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2465 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.12
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.08
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|516 - 662}
REMARK 3 ORIGIN FOR THE GROUP (A): -36.4039 -20.3739 -16.2342
REMARK 3 T TENSOR
REMARK 3 T11: -0.1226 T22: 0.0713
REMARK 3 T33: -0.1917 T12: -0.0132
REMARK 3 T13: -0.0299 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 3.3056 L22: 1.5136
REMARK 3 L33: 2.7681 L12: 1.3151
REMARK 3 L13: -1.0843 L23: 0.5218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: -0.0730 S13: -0.0466
REMARK 3 S21: 0.1377 S22: -0.0420 S23: 0.0159
REMARK 3 S31: 0.0690 S32: 0.0300 S33: -0.0285
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|663 - 794}
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1396 -8.0669 -29.6437
REMARK 3 T TENSOR
REMARK 3 T11: -0.1246 T22: 0.1194
REMARK 3 T33: -0.1542 T12: 0.0017
REMARK 3 T13: 0.0454 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.8883 L22: 2.6234
REMARK 3 L33: 2.2476 L12: -1.2996
REMARK 3 L13: 0.2683 L23: 0.9316
REMARK 3 S TENSOR
REMARK 3 S11: 0.0837 S12: 0.1284 S13: 0.3059
REMARK 3 S21: -0.3224 S22: -0.0136 S23: -0.3476
REMARK 3 S31: -0.3742 S32: 0.0059 S33: -0.0701
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1290065030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600
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: PDB ENTRY 4C4J
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 38% (V/V) PEG300, PH 7.5
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 34.86000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.18500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.09500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.18500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.09500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.18500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.09500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.18500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.09500
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 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 604 TO TRP
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 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 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 PRO 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 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 GLN A 516 CG CD OE1 NE2
REMARK 470 ARG A 523 CZ NH1 NH2
REMARK 470 LYS A 529 CE NZ
REMARK 470 LYS A 538 CE NZ
REMARK 470 GLU A 545 CD OE1 OE2
REMARK 470 LYS A 546 CE NZ
REMARK 470 LYS A 547 CE NZ
REMARK 470 GLU A 559 CG CD OE1 OE2
REMARK 470 GLN A 563 CD OE1 NE2
REMARK 470 LYS A 615 CE NZ
REMARK 470 LYS A 617 CG CD CE NZ
REMARK 470 LYS A 629 CE NZ
REMARK 470 ASP A 657 CG OD1 OD2
REMARK 470 GLN A 670 CG CD OE1 NE2
REMARK 470 SER A 682 OG
REMARK 470 LYS A 696 CE NZ
REMARK 470 LYS A 710 CG CD CE NZ
REMARK 470 ILE A 738 CG1 CG2 CD1
REMARK 470 GLU A 753 CG CD OE1 OE2
REMARK 470 GLU A 755 CG CD OE1 OE2
REMARK 470 LYS A 762 CD CE NZ
REMARK 470 LYS A 769 CE NZ
REMARK 470 LYS A 777 CD CE NZ
REMARK 470 GLN A 794 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 SER A 646 -11.90 72.48
REMARK 500 LEU A 772 41.52 -100.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PWU A 1795
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1796
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1798
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1799
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1806
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AP0 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP1 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP2 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP3 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP4 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP5 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 900 RELATED ID: 5AP7 RELATED DB: PDB
REMARK 900 NATURALLY OCCURRING MUTATIONS IN THE MPS1 GENE PREDISPOSE CELLS TO
REMARK 900 KINASE INHIBITOR DRUG RESISTANCE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE INCLUDING HEXAHISTIDINE TAG IS AS DESCRIBED
REMARK 999 IN NAT. CHEM. BIOL. 2010, 6, 259-368 WITH AN ADDITIONAL
REMARK 999 MUTATION C604W
DBREF 5AP6 A 519 808 UNP P33981 TTK_HUMAN 519 808
SEQADV 5AP6 MET A 496 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 497 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 498 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 499 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 500 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 501 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 HIS A 502 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 SER A 503 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 SER A 504 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 GLY A 505 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 VAL A 506 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 ASP A 507 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 LEU A 508 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 GLY A 509 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 THR A 510 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 GLU A 511 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 ASN A 512 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 LEU A 513 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 TYR A 514 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 PHE A 515 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 GLN A 516 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 SER A 517 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 MET A 518 UNP P33981 EXPRESSION TAG
SEQADV 5AP6 TRP A 604 UNP P33981 CYS 604 ENGINEERED MUTATION
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 TRP 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 THR 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 PRO VAL ASN GLN MET ALA LYS GLY THR THR GLU
SEQRES 25 A 313 GLU
HET PWU A1795 35
HET EDO A1796 4
HET EDO A1797 4
HET EDO A1798 4
HET EDO A1799 4
HET EDO A1800 4
HET EDO A1801 4
HET EDO A1802 4
HET EDO A1803 4
HET EDO A1804 4
HET EDO A1805 4
HET DMS A1806 4
HETNAM PWU ISOPROPYL 6-((4-(1,2-DIMETHYL-1H-IMIDAZOL-5-YL)PHENYL)
HETNAM 2 PWU AMINO)-2-(1-METHYL-1H-PYRAZOL-4-YL)-1H-PYRROLO[3,2-
HETNAM 3 PWU C]PYRIDINE-1-CARBOXYLATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 PWU C26 H27 N7 O2
FORMUL 3 EDO 10(C2 H6 O2)
FORMUL 13 DMS C2 H6 O S
FORMUL 14 HOH *63(H2 O)
HELIX 1 1 ASP A 561 GLN A 579 1 19
HELIX 2 2 LEU A 609 LYS A 616 1 8
HELIX 3 3 ASP A 620 HIS A 641 1 22
HELIX 4 4 LYS A 649 ALA A 651 5 3
HELIX 5 5 PRO A 691 ASP A 697 1 7
HELIX 6 6 SER A 712 GLY A 730 1 19
HELIX 7 7 ASN A 739 ASP A 749 1 11
HELIX 8 8 GLU A 761 LEU A 772 1 12
HELIX 9 9 SER A 781 LEU A 786 1 6
HELIX 10 10 HIS A 788 ILE A 793 1 6
SHEET 1 AA 2 SER A 517 VAL A 520 0
SHEET 2 AA 2 ARG A 523 GLY A 534 -1 O ARG A 523 N VAL A 520
SHEET 1 AB 6 LEU A 588 ILE A 593 0
SHEET 2 AB 6 TYR A 597 MET A 602 -1 O TYR A 599 N GLU A 592
SHEET 3 AB 6 ILE A 549 ASN A 556 -1 O ALA A 551 N MET A 602
SHEET 4 AB 6 SER A 537 LEU A 543 -1 O LYS A 538 N TYR A 554
SHEET 5 AB 6 ARG A 523 GLY A 534 -1 O SER A 526 N LEU A 543
SHEET 6 AB 6 GLN A 672 PRO A 673 1 O GLN A 672 N SER A 533
SHEET 1 AC 6 LEU A 588 ILE A 593 0
SHEET 2 AC 6 TYR A 597 MET A 602 -1 O TYR A 599 N GLU A 592
SHEET 3 AC 6 ILE A 549 ASN A 556 -1 O ALA A 551 N MET A 602
SHEET 4 AC 6 SER A 537 LEU A 543 -1 O LYS A 538 N TYR A 554
SHEET 5 AC 6 ARG A 523 GLY A 534 -1 O SER A 526 N LEU A 543
SHEET 6 AC 6 SER A 517 VAL A 520 -1 O MET A 518 N TYR A 525
SHEET 1 AD 2 GLN A 672 PRO A 673 0
SHEET 2 AD 2 ARG A 523 GLY A 534 1 O SER A 533 N GLN A 672
SHEET 1 AE 3 ILE A 607 ASP A 608 0
SHEET 2 AE 3 PHE A 653 VAL A 656 -1 N ILE A 655 O ILE A 607
SHEET 3 AE 3 MET A 659 LEU A 662 -1 O MET A 659 N VAL A 656
SITE 1 AC1 15 ILE A 531 ALA A 551 LYS A 553 ILE A 586
SITE 2 AC1 15 MET A 602 GLU A 603 GLY A 605 ASN A 606
SITE 3 AC1 15 ILE A 607 ASP A 608 SER A 611 LEU A 654
SITE 4 AC1 15 ILE A 663 MET A 671 PRO A 673
SITE 1 AC2 3 TYR A 550 TYR A 589 HOH A2008
SITE 1 AC3 3 THR A 594 ASP A 595 GLN A 596
SITE 1 AC4 4 TYR A 525 TYR A 550 TYR A 589 ASP A 590
SITE 1 AC5 2 PHE A 540 TYR A 599
SITE 1 AC6 5 SER A 519 GLU A 592 TYR A 597 TYR A 599
SITE 2 AC6 5 EDO A1801
SITE 1 AC7 5 SER A 519 LYS A 521 GLY A 522 GLU A 592
SITE 2 AC7 5 EDO A1800
SITE 1 AC8 5 PRO A 760 GLU A 761 LYS A 762 ASP A 763
SITE 2 AC8 5 HOH A2062
SITE 1 AC9 4 GLY A 522 ILE A 524 GLU A 545 HOH A2004
SITE 1 BC1 4 SER A 526 TRP A 604 ASN A 606 ASP A 657
SITE 1 BC2 3 SER A 682 GLN A 683 TYR A 726
SITE 1 BC3 2 ILE A 619 THR A 728
CRYST1 69.720 104.370 112.190 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 0.014343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008913 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
