HEADER TRANSFERASE/TRANSFERASE INHIBITOR 30-MAR-17 5VC4
TITLE CRYSTAL STRUCTURE OF HUMAN WEE1 KINASE DOMAIN IN COMPLEX WITH
TITLE 2 BOSUTINIB-ISOMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WEE1-LIKE PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 291-575;
COMPND 5 SYNONYM: WEE1HU,WEE1A KINASE;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: WEE1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS KINASE DOMAIN, CELL CYCLE, WEE1, TRANSFERASE, INHIBITOR, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZHU,E.SCHONBRUNN
REVDAT 4 04-OCT-23 5VC4 1 REMARK
REVDAT 3 11-DEC-19 5VC4 1 REMARK
REVDAT 2 11-OCT-17 5VC4 1 JRNL
REVDAT 1 23-AUG-17 5VC4 0
JRNL AUTH J.Y.ZHU,R.A.CUELLAR,N.BERNDT,H.E.LEE,S.H.OLESEN,M.P.MARTIN,
JRNL AUTH 2 J.T.JENSEN,G.I.GEORG,E.SCHONBRUNN
JRNL TITL STRUCTURAL BASIS OF WEE KINASES FUNCTIONALITY AND
JRNL TITL 2 INACTIVATION BY DIVERSE SMALL MOLECULE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 7863 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28792760
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00996
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 16098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 805
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.0269 - 3.8142 0.94 2550 135 0.1694 0.2060
REMARK 3 2 3.8142 - 3.0281 0.96 2523 133 0.1913 0.2368
REMARK 3 3 3.0281 - 2.6455 0.97 2554 134 0.2223 0.2792
REMARK 3 4 2.6455 - 2.4037 0.98 2547 134 0.2097 0.2754
REMARK 3 5 2.4037 - 2.2314 0.98 2565 135 0.2208 0.2481
REMARK 3 6 2.2314 - 2.0999 0.98 2554 134 0.2489 0.3353
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 2165
REMARK 3 ANGLE : 0.642 2924
REMARK 3 CHIRALITY : 0.026 314
REMARK 3 PLANARITY : 0.003 373
REMARK 3 DIHEDRAL : 13.384 812
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 352 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5033 -5.1278 9.6296
REMARK 3 T TENSOR
REMARK 3 T11: 0.2934 T22: 0.2927
REMARK 3 T33: 0.4546 T12: -0.0291
REMARK 3 T13: 0.0198 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 3.4106 L22: 1.9762
REMARK 3 L33: 1.3502 L12: -1.8098
REMARK 3 L13: 1.0559 L23: 0.2035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: 0.4558 S13: -0.4776
REMARK 3 S21: -0.2087 S22: 0.1134 S23: -0.0513
REMARK 3 S31: 0.1005 S32: 0.1225 S33: -0.1572
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 353 THROUGH 461 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7826 6.6932 18.5897
REMARK 3 T TENSOR
REMARK 3 T11: 0.1818 T22: 0.1734
REMARK 3 T33: 0.1735 T12: 0.0333
REMARK 3 T13: 0.0121 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 3.2896 L22: 2.3433
REMARK 3 L33: 2.2988 L12: -0.2906
REMARK 3 L13: 0.9375 L23: -0.3044
REMARK 3 S TENSOR
REMARK 3 S11: -0.1420 S12: -0.3077 S13: 0.3551
REMARK 3 S21: 0.1418 S22: -0.0036 S23: 0.0808
REMARK 3 S31: -0.2422 S32: -0.0040 S33: 0.0315
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 462 THROUGH 484 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4279 -0.8499 13.7331
REMARK 3 T TENSOR
REMARK 3 T11: 0.3163 T22: 0.4244
REMARK 3 T33: 0.4096 T12: 0.1152
REMARK 3 T13: 0.0603 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 4.0745 L22: 1.1502
REMARK 3 L33: 1.7253 L12: -0.0416
REMARK 3 L13: 0.8286 L23: 0.4138
REMARK 3 S TENSOR
REMARK 3 S11: 0.1424 S12: 0.7283 S13: -0.5083
REMARK 3 S21: -0.5510 S22: -0.4554 S23: -0.4559
REMARK 3 S31: 0.3773 S32: 0.6507 S33: 0.0159
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 485 THROUGH 571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2918 13.8558 18.8918
REMARK 3 T TENSOR
REMARK 3 T11: 0.3182 T22: 0.3559
REMARK 3 T33: 0.5422 T12: -0.0257
REMARK 3 T13: -0.1076 T23: 0.0739
REMARK 3 L TENSOR
REMARK 3 L11: 3.5730 L22: 3.1005
REMARK 3 L33: 1.5761 L12: -0.5356
REMARK 3 L13: 0.3975 L23: -0.7522
REMARK 3 S TENSOR
REMARK 3 S11: -0.1078 S12: -0.1151 S13: 1.0813
REMARK 3 S21: 0.3123 S22: -0.2749 S23: -1.0445
REMARK 3 S31: -0.3744 S32: 0.3068 S33: 0.0971
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16101
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 33.023
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.999
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3700
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) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.96
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.240
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: 5V5Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.0 MG/ML WEE1, 25 MM NA/K PHOSPHATE,
REMARK 280 1 MM DTT, 0.05 M AMMONIUM SULFATE, 0.05 M BIS-TRIS (PH 5.5), 7.5
REMARK 280 % PEG 3350, 1 MM BOSUTINIB-ISOMER, PH 6.9, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 22.12500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 287
REMARK 465 ALA A 288
REMARK 465 GLY A 289
REMARK 465 SER A 290
REMARK 465 MET A 291
REMARK 465 LYS A 292
REMARK 465 SER A 438
REMARK 465 ILE A 439
REMARK 465 PRO A 440
REMARK 465 ASN A 441
REMARK 465 ALA A 442
REMARK 465 ALA A 443
REMARK 465 SER A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLY A 447
REMARK 465 ASP A 448
REMARK 465 GLU A 449
REMARK 465 ASP A 450
REMARK 465 ASP A 451
REMARK 465 TRP A 452
REMARK 465 ALA A 453
REMARK 465 SER A 454
REMARK 465 ASN A 455
REMARK 465 ALA A 572
REMARK 465 SER A 573
REMARK 465 ARG A 574
REMARK 465 LYS A 575
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 426 42.84 -157.96
REMARK 500 ASP A 463 85.77 53.99
REMARK 500 ASN A 519 -177.29 -170.19
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 XZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VC3 RELATED DB: PDB
REMARK 900 RELATED ID: 5VC5 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD2 RELATED DB: PDB
REMARK 900 RELATED ID: 5VC6 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD9 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD8 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD7 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD5 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD4 RELATED DB: PDB
REMARK 900 RELATED ID: 5VDA RELATED DB: PDB
DBREF 5VC4 A 291 575 UNP P30291 WEE1_HUMAN 291 575
SEQADV 5VC4 GLY A 287 UNP P30291 EXPRESSION TAG
SEQADV 5VC4 ALA A 288 UNP P30291 EXPRESSION TAG
SEQADV 5VC4 GLY A 289 UNP P30291 EXPRESSION TAG
SEQADV 5VC4 SER A 290 UNP P30291 EXPRESSION TAG
SEQRES 1 A 289 GLY ALA GLY SER MET LYS SER ARG TYR THR THR GLU PHE
SEQRES 2 A 289 HIS GLU LEU GLU LYS ILE GLY SER GLY GLU PHE GLY SER
SEQRES 3 A 289 VAL PHE LYS CYS VAL LYS ARG LEU ASP GLY CYS ILE TYR
SEQRES 4 A 289 ALA ILE LYS ARG SER LYS LYS PRO LEU ALA GLY SER VAL
SEQRES 5 A 289 ASP GLU GLN ASN ALA LEU ARG GLU VAL TYR ALA HIS ALA
SEQRES 6 A 289 VAL LEU GLY GLN HIS SER HIS VAL VAL ARG TYR PHE SER
SEQRES 7 A 289 ALA TRP ALA GLU ASP ASP HIS MET LEU ILE GLN ASN GLU
SEQRES 8 A 289 TYR CYS ASN GLY GLY SER LEU ALA ASP ALA ILE SER GLU
SEQRES 9 A 289 ASN TYR ARG ILE MET SER TYR PHE LYS GLU ALA GLU LEU
SEQRES 10 A 289 LYS ASP LEU LEU LEU GLN VAL GLY ARG GLY LEU ARG TYR
SEQRES 11 A 289 ILE HIS SER MET SER LEU VAL HIS MET ASP ILE LYS PRO
SEQRES 12 A 289 SER ASN ILE PHE ILE SER ARG THR SER ILE PRO ASN ALA
SEQRES 13 A 289 ALA SER GLU GLU GLY ASP GLU ASP ASP TRP ALA SER ASN
SEQRES 14 A 289 LYS VAL MET PHE LYS ILE GLY ASP LEU GLY HIS VAL THR
SEQRES 15 A 289 ARG ILE SER SER PRO GLN VAL GLU GLU GLY ASP SER ARG
SEQRES 16 A 289 PHE LEU ALA ASN GLU VAL LEU GLN GLU ASN TYR THR HIS
SEQRES 17 A 289 LEU PRO LYS ALA ASP ILE PHE ALA LEU ALA LEU THR VAL
SEQRES 18 A 289 VAL CYS ALA ALA GLY ALA GLU PRO LEU PRO ARG ASN GLY
SEQRES 19 A 289 ASP GLN TRP HIS GLU ILE ARG GLN GLY ARG LEU PRO ARG
SEQRES 20 A 289 ILE PRO GLN VAL LEU SER GLN GLU PHE THR GLU LEU LEU
SEQRES 21 A 289 LYS VAL MET ILE HIS PRO ASP PRO GLU ARG ARG PRO SER
SEQRES 22 A 289 ALA MET ALA LEU VAL LYS HIS SER VAL LEU LEU SER ALA
SEQRES 23 A 289 SER ARG LYS
HET XZN A 601 36
HET PO4 A 602 5
HETNAM XZN 4-[(3,5-DICHLORO-4-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-
HETNAM 2 XZN (4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-
HETNAM 3 XZN CARBONITRILE
HETNAM PO4 PHOSPHATE ION
HETSYN XZN BOSUTINIB ISOFORM 1
FORMUL 2 XZN C26 H29 CL2 N5 O3
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *67(H2 O)
HELIX 1 AA1 SER A 293 GLU A 298 1 6
HELIX 2 AA2 SER A 337 LEU A 353 1 17
HELIX 3 AA3 LEU A 384 MET A 395 1 12
HELIX 4 AA4 LYS A 399 MET A 420 1 22
HELIX 5 AA5 LYS A 428 SER A 430 5 3
HELIX 6 AA6 ALA A 484 GLN A 489 1 6
HELIX 7 AA7 LEU A 495 ALA A 511 1 17
HELIX 8 AA8 GLY A 520 GLN A 528 1 9
HELIX 9 AA9 SER A 539 ILE A 550 1 12
HELIX 10 AB1 SER A 559 VAL A 564 1 6
SHEET 1 AA1 5 PHE A 299 GLY A 308 0
SHEET 2 AA1 5 GLY A 311 LYS A 318 -1 O LYS A 315 N GLU A 303
SHEET 3 AA1 5 ILE A 324 LYS A 331 -1 O ARG A 329 N SER A 312
SHEET 4 AA1 5 HIS A 371 GLU A 377 -1 O MET A 372 N SER A 330
SHEET 5 AA1 5 TYR A 362 GLU A 368 -1 N SER A 364 O GLN A 375
SHEET 1 AA2 3 GLY A 382 SER A 383 0
SHEET 2 AA2 3 ILE A 432 SER A 435 -1 O ILE A 434 N GLY A 382
SHEET 3 AA2 3 MET A 458 ILE A 461 -1 O LYS A 460 N PHE A 433
SHEET 1 AA3 2 LEU A 422 VAL A 423 0
SHEET 2 AA3 2 THR A 468 ARG A 469 -1 O THR A 468 N VAL A 423
CISPEP 1 LEU A 570 SER A 571 0 -2.23
SITE 1 AC1 14 GLU A 303 ILE A 305 ALA A 326 LYS A 328
SITE 2 AC1 14 VAL A 360 ILE A 374 ASN A 376 GLU A 377
SITE 3 AC1 14 TYR A 378 CYS A 379 GLY A 382 PHE A 433
SITE 4 AC1 14 ASP A 463 HOH A 744
SITE 1 AC2 5 HIS A 494 PRO A 496 LYS A 497 HOH A 702
SITE 2 AC2 5 HOH A 723
CRYST1 50.670 44.250 64.800 90.00 101.73 90.00 P 1 21 1 2
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 0.019736 0.000000 0.004099 0.00000
SCALE2 0.000000 0.022599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015761 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
