HEADER TRANSFERASE 14-SEP-15 5AP1
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, UNP RESIDUES 519-808;
COMPND 5 SYNONYM: PHOSPHOTYROSINE PICKED THREONINE-PROTEIN KINASE, PYT,
COMPND 6 MONOPK, MONOPOLAR SPINDLE KINASE 1;
COMPND 7 EC: 2.7.12.1;
COMPND 8 ENGINEERED: 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, PROTEIN KINASE, MITOSIS, DRUG RESISTANCE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.GURDEN,I.M.WESTWOOD,A.FAISAL,S.NAUD,K.J.CHEUNG,C.MCANDREW,A.WOOD,
AUTHOR 2 J.SCHMITT,K.BOXALL,G.MAK,P.WORKMAN,R.BURKE,S.HOELDER,J.BLAGG,
AUTHOR 3 R.L.M.VAN MONTFORT,S.LINARDOPOULOS
REVDAT 2 10-JAN-24 5AP1 1 REMARK LINK
REVDAT 1 23-SEP-15 5AP1 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. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 28095
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1415
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 : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.48
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2936
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2363
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2788
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE : 0.2421
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.04
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 2109
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.84050
REMARK 3 B22 (A**2) : -5.58660
REMARK 3 B33 (A**2) : -0.25400
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) : 0.322
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.141
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.124
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.139
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.123
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 : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2207 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2997 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 740 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 53 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 332 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2207 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 297 ; 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 : 2552 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.78
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|515 - 561}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3762 -23.8079 -49.5036
REMARK 3 T TENSOR
REMARK 3 T11: -0.1839 T22: 0.1452
REMARK 3 T33: -0.1907 T12: 0.0626
REMARK 3 T13: 0.0217 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 7.6271
REMARK 3 L33: 6.7539 L12: 2.5654
REMARK 3 L13: 2.0080 L23: -1.3229
REMARK 3 S TENSOR
REMARK 3 S11: -0.1743 S12: 0.5442 S13: -0.1194
REMARK 3 S21: -0.3675 S22: 0.0038 S23: -0.5140
REMARK 3 S31: 0.1667 S32: 0.5442 S33: 0.1706
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|562 - 662}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5435 -22.9621 -38.2949
REMARK 3 T TENSOR
REMARK 3 T11: -0.1048 T22: -0.0400
REMARK 3 T33: -0.1244 T12: 0.0026
REMARK 3 T13: -0.0063 T23: 0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 5.7682 L22: 0.9309
REMARK 3 L33: 4.2131 L12: -0.6410
REMARK 3 L13: -2.1473 L23: 0.2893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: 0.3149 S13: 0.0130
REMARK 3 S21: -0.0662 S22: -0.0196 S23: 0.0771
REMARK 3 S31: 0.2393 S32: -0.0306 S33: -0.0191
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|663 - 691}
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3324 -9.8858 -41.4764
REMARK 3 T TENSOR
REMARK 3 T11: -0.1138 T22: -0.0492
REMARK 3 T33: 0.0378 T12: 0.0353
REMARK 3 T13: -0.0420 T23: 0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 1.9631 L22: 1.0736
REMARK 3 L33: 1.7357 L12: 1.1760
REMARK 3 L13: -2.9104 L23: -0.0168
REMARK 3 S TENSOR
REMARK 3 S11: 0.1571 S12: -0.0108 S13: 0.5441
REMARK 3 S21: 0.0853 S22: 0.0114 S23: 0.0627
REMARK 3 S31: -0.2068 S32: 0.3749 S33: -0.1684
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|692 - 748}
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0423 -5.5620 -29.7569
REMARK 3 T TENSOR
REMARK 3 T11: -0.1536 T22: -0.1088
REMARK 3 T33: 0.1344 T12: 0.0623
REMARK 3 T13: 0.0896 T23: -0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.6640 L22: 6.7277
REMARK 3 L33: 2.1048 L12: 2.8877
REMARK 3 L13: -1.3348 L23: -0.0512
REMARK 3 S TENSOR
REMARK 3 S11: 0.1609 S12: -0.3339 S13: 0.5442
REMARK 3 S21: 0.2736 S22: -0.0710 S23: 0.3427
REMARK 3 S31: -0.5305 S32: -0.1258 S33: -0.0899
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|749 - 761}
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9591 -2.9087 -30.7549
REMARK 3 T TENSOR
REMARK 3 T11: -0.2988 T22: 0.1017
REMARK 3 T33: 0.2948 T12: 0.1520
REMARK 3 T13: -0.0474 T23: 0.1499
REMARK 3 L TENSOR
REMARK 3 L11: 4.7678 L22: 4.5960
REMARK 3 L33: 1.3516 L12: -2.9104
REMARK 3 L13: -2.3938 L23: 0.7053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.0020 S13: 0.1540
REMARK 3 S21: 0.1057 S22: 0.1142 S23: 0.1131
REMARK 3 S31: -0.3017 S32: -0.1516 S33: -0.1683
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|762 - 781}
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9286 -11.3457 -25.3974
REMARK 3 T TENSOR
REMARK 3 T11: -0.2041 T22: 0.1052
REMARK 3 T33: 0.0951 T12: 0.0534
REMARK 3 T13: 0.1211 T23: -0.0748
REMARK 3 L TENSOR
REMARK 3 L11: 0.0568 L22: 3.0778
REMARK 3 L33: 2.0545 L12: -2.9104
REMARK 3 L13: -1.7879 L23: 1.9301
REMARK 3 S TENSOR
REMARK 3 S11: 0.0931 S12: -0.3286 S13: 0.5399
REMARK 3 S21: 0.3362 S22: 0.0530 S23: 0.3887
REMARK 3 S31: -0.4241 S32: -0.4807 S33: -0.1461
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|782 - 795}
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5210 -22.5556 -29.8680
REMARK 3 T TENSOR
REMARK 3 T11: -0.3019 T22: 0.2232
REMARK 3 T33: -0.2623 T12: -0.0480
REMARK 3 T13: 0.0244 T23: 0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 2.4138 L22: 0.9041
REMARK 3 L33: 0.0161 L12: -0.9268
REMARK 3 L13: -0.7263 L23: -2.3563
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.0521 S13: 0.2432
REMARK 3 S21: -0.1983 S22: 0.0625 S23: -0.0870
REMARK 3 S31: -0.0841 S32: -0.4334 S33: -0.0648
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AP1 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_1290065026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9173
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28097
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 41.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 1.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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 (%): 59.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 0.2M MGCL2, 10% (W/V)
REMARK 280 PEG4000, CO-CRYSTALLISED WITH 1MM INHIBITOR
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 35.34000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.19000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.76500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.34000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.19000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.76500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.34000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.19000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.76500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.34000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.19000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 57.76500
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 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 A1801 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 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 SER A 682
REMARK 465 GLN A 683
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 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 PHE A 515 CG CD1 CD2 CE1 CE2 CZ
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 GLU A 545 CG CD OE1 OE2
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 LYS A 547 CG CD CE NZ
REMARK 470 GLU A 559 CG CD OE1 OE2
REMARK 470 GLN A 563 CG CD OE1 NE2
REMARK 470 LYS A 614 CE NZ
REMARK 470 LYS A 615 CG CD CE NZ
REMARK 470 LYS A 617 CG CD CE NZ
REMARK 470 TRP A 622 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 622 CZ3 CH2
REMARK 470 ASP A 657 CG OD1 OD2
REMARK 470 ASN A 669 CG OD1 ND2
REMARK 470 GLN A 672 CD OE1 NE2
REMARK 470 VAL A 678 CG1 CG2
REMARK 470 LYS A 680 CG CD CE NZ
REMARK 470 ASP A 681 CG OD1 OD2
REMARK 470 VAL A 684 CG1 CG2
REMARK 470 LYS A 696 CG CD CE NZ
REMARK 470 SER A 699 OG
REMARK 470 SER A 700 OG
REMARK 470 LYS A 708 CG CD CE NZ
REMARK 470 SER A 709 OG
REMARK 470 LYS A 710 CG CD CE NZ
REMARK 470 ILE A 738 CG1 CG2 CD1
REMARK 470 SER A 742 OG
REMARK 470 HIS A 745 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 748 CG1 CG2 CD1
REMARK 470 ASN A 751 CG OD1 ND2
REMARK 470 GLU A 753 CD OE1 OE2
REMARK 470 LYS A 762 CG CD CE NZ
REMARK 470 LYS A 769 CE NZ
REMARK 470 LYS A 777 CG CD CE NZ
REMARK 470 THR A 795 OG1 CG2
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 -9.73 69.07
REMARK 500 LYS A 710 -56.25 74.19
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 A1801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO A 675 O3P
REMARK 620 2 TPO A 675 O3P 0.0
REMARK 620 3 SEP A 677 O3P 105.4 105.4
REMARK 620 4 SEP A 677 O3P 105.4 105.4 0.0
REMARK 620 5 HOH A2079 O 84.4 84.4 96.4 96.4
REMARK 620 6 HOH A2079 O 86.5 86.5 168.0 168.0 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO A 675 O2P
REMARK 620 2 TPO A 676 O2P 50.2
REMARK 620 3 HOH A2076 O 83.0 108.3
REMARK 620 4 HOH A2080 O 76.7 34.9 93.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO A 675 O3P
REMARK 620 2 SEP A 677 O3P 63.8
REMARK 620 3 SEP A 677 O2P 91.8 42.3
REMARK 620 4 HOH A2078 O 98.8 127.1 94.0
REMARK 620 5 HOH A2081 O 85.7 130.4 172.0 93.9
REMARK 620 6 HOH A2085 O 164.7 118.0 98.6 91.6 82.3
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 O38 A 1796
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1797
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1798
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1799
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1803
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: 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: 5AP6 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.
DBREF 5AP1 A 519 808 UNP P33981 TTK_HUMAN 519 808
SEQADV 5AP1 MET A 496 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 497 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 498 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 499 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 500 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 501 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 HIS A 502 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 SER A 503 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 SER A 504 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 GLY A 505 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 VAL A 506 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 ASP A 507 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 LEU A 508 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 GLY A 509 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 THR A 510 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 GLU A 511 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 ASN A 512 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 LEU A 513 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 TYR A 514 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 PHE A 515 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 GLN A 516 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 SER A 517 UNP P33981 EXPRESSION TAG
SEQADV 5AP1 MET A 518 UNP P33981 EXPRESSION TAG
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 TPO TPO SEP
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 PRO VAL ASN GLN MET ALA LYS GLY THR THR GLU
SEQRES 25 A 313 GLU
MODRES 5AP1 TPO A 675 THR PHOSPHOTHREONINE
MODRES 5AP1 TPO A 676 THR PHOSPHOTHREONINE
MODRES 5AP1 SEP A 677 SER PHOSPHOSERINE
MODRES 5AP1 TPO A 686 THR PHOSPHOTHREONINE
HET TPO A 675 11
HET TPO A 676 11
HET SEP A 677 10
HET TPO A 686 11
HET O38 A1796 32
HET GOL A1797 6
HET GOL A1798 6
HET GOL A1799 6
HET GOL A1800 6
HET MG A1801 1
HET MG A1802 1
HET MG A1803 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM O38 6-{[3-(CYANOMETHOXY)-4-(1-METHYL-1H-PYRAZOL-4-YL)
HETNAM 2 O38 PHENYL]AMINO}-2-(CYCLOHEXYLAMINO)PYRIDINE-3-
HETNAM 3 O38 CARBONITRILE
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 TPO 3(C4 H10 N O6 P)
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 O38 C24 H25 N7 O
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 MG 3(MG 2+)
FORMUL 10 HOH *128(H2 O)
HELIX 1 1 ASP A 561 LEU A 578 1 18
HELIX 2 2 GLN A 579 HIS A 581 5 3
HELIX 3 3 LEU A 609 LYS A 616 1 8
HELIX 4 4 ASP A 620 HIS A 641 1 22
HELIX 5 5 LYS A 649 ALA A 651 5 3
HELIX 6 6 PRO A 691 MET A 698 1 8
HELIX 7 7 SER A 712 GLY A 730 1 19
HELIX 8 8 ASN A 739 ASP A 749 1 11
HELIX 9 9 GLU A 761 LEU A 772 1 12
HELIX 10 10 SER A 781 LEU A 786 1 6
HELIX 11 11 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
LINK C ASP A 674 N TPO A 675 1555 1555 1.33
LINK C TPO A 675 N TPO A 676 1555 1555 1.34
LINK C TPO A 676 N SEP A 677 1555 1555 1.35
LINK C SEP A 677 N VAL A 678 1555 1555 1.35
LINK C GLY A 685 N TPO A 686 1555 1555 1.34
LINK C TPO A 686 N VAL A 687 1555 1555 1.34
LINK O3P TPO A 675 MG MG A1801 1555 1555 2.01
LINK O3P TPO A 675 MG MG A1801 1555 3554 2.01
LINK O2P TPO A 675 MG MG A1802 1555 1555 2.55
LINK O3P TPO A 675 MG MG A1803 1555 1555 2.26
LINK O2P TPO A 676 MG MG A1802 1555 3554 2.37
LINK O3P SEP A 677 MG MG A1801 1555 1555 2.12
LINK O3P SEP A 677 MG MG A1801 1555 3554 2.12
LINK O3P SEP A 677 MG MG A1803 1555 3554 2.03
LINK O2P SEP A 677 MG MG A1803 1555 1555 1.95
LINK MG MG A1801 O HOH A2079 1555 3554 2.06
LINK MG MG A1801 O HOH A2079 1555 1555 2.06
LINK MG MG A1802 O HOH A2076 1555 1555 2.06
LINK MG MG A1802 O HOH A2080 1555 1555 2.48
LINK MG MG A1803 O HOH A2078 1555 1555 2.24
LINK MG MG A1803 O HOH A2081 1555 1555 2.09
LINK MG MG A1803 O HOH A2085 1555 1555 2.24
SITE 1 AC1 16 ILE A 531 GLN A 541 ALA A 551 MET A 602
SITE 2 AC1 16 CYS A 604 GLY A 605 ASN A 606 ILE A 607
SITE 3 AC1 16 ASP A 608 SER A 611 LEU A 654 ILE A 663
SITE 4 AC1 16 MET A 671 GLN A 672 PRO A 673 HOH A2012
SITE 1 AC2 1 LYS A 538
SITE 1 AC3 3 TYR A 525 ASN A 544 TYR A 550
SITE 1 AC4 6 LYS A 714 LYS A 777 ARG A 779 ILE A 780
SITE 2 AC4 6 GLU A 784 HOH A2123
SITE 1 AC5 5 ASN A 576 ASP A 766 HIS A 788 PRO A 789
SITE 2 AC5 5 HOH A2127
SITE 1 AC6 4 TPO A 675 SEP A 677 MG A1803 HOH A2079
SITE 1 AC7 4 TPO A 675 TPO A 676 HOH A2076 HOH A2080
SITE 1 AC8 6 TPO A 675 SEP A 677 MG A1801 HOH A2078
SITE 2 AC8 6 HOH A2081 HOH A2085
CRYST1 70.680 108.380 115.530 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 0.014148 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
