HEADER TRANSFERASE/TRANSFERASE INHIBITOR 11-JUL-14 4U0I
TITLE CRYSTAL STRUCTURE OF KIT IN COMPLEX WITH PONATINIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAST/STEM CELL GROWTH FACTOR RECEPTOR KIT,MAST/STEM CELL
COMPND 3 GROWTH FACTOR RECEPTOR KIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 563-693 AND 754-935 LINKED VIA LINKER (THR
COMPND 6 SER);
COMPND 7 SYNONYM: SCFR,PIEBALD TRAIT PROTEIN,PBT,PROTO-ONCOGENE C-KIT,
COMPND 8 TYROSINE-PROTEIN KINASE KIT,P145 C-KIT,V-KIT HARDY-ZUCKERMAN 4 FELINE
COMPND 9 SARCOMA VIRAL ONCOGENE HOMOLOG,SCFR,PIEBALD TRAIT PROTEIN,PBT,PROTO-
COMPND 10 ONCOGENE C-KIT,TYROSINE-PROTEIN KINASE KIT,P145 C-KIT,V-KIT HARDY-
COMPND 11 ZUCKERMAN 4 FELINE SARCOMA VIRAL ONCOGENE HOMOLOG;
COMPND 12 EC: 2.7.10.1;
COMPND 13 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: KIT, SCFR;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KIT, RECEPTOR TYROSINE KINASE, INHIBITOR, PONATINIB, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ZHOU,X.ZHU,D.C.DALGARNO
REVDAT 4 27-DEC-23 4U0I 1 COMPND REMARK HETNAM
REVDAT 3 22-NOV-17 4U0I 1 SOURCE REMARK
REVDAT 2 26-NOV-14 4U0I 1 JRNL
REVDAT 1 08-OCT-14 4U0I 0
JRNL AUTH A.P.GARNER,J.M.GOZGIT,R.ANJUM,S.VODALA,A.SCHROCK,T.ZHOU,
JRNL AUTH 2 C.SERRANO,G.EILERS,M.ZHU,J.KETZER,S.WARDWELL,Y.NING,Y.SONG,
JRNL AUTH 3 A.KOHLMANN,F.WANG,T.CLACKSON,M.C.HEINRICH,J.A.FLETCHER,
JRNL AUTH 4 S.BAUER,V.M.RIVERA
JRNL TITL PONATINIB INHIBITS POLYCLONAL DRUG-RESISTANT KIT
JRNL TITL 2 ONCOPROTEINS AND SHOWS THERAPEUTIC POTENTIAL IN HEAVILY
JRNL TITL 3 PRETREATED GASTROINTESTINAL STROMAL TUMOR (GIST) PATIENTS.
JRNL REF CLIN.CANCER RES. V. 20 5745 2014
JRNL REFN ISSN 1078-0432
JRNL PMID 25239608
JRNL DOI 10.1158/1078-0432.CCR-14-1397
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 3.14
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 24107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1164
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09600
REMARK 3 B22 (A**2) : -0.09600
REMARK 3 B33 (A**2) : 0.19300
REMARK 3 B12 (A**2) : 0.07800
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.135 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.753 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.854 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.605 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : AP24534_KIT.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4U0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.69400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.9-1.2M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 86.14133
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 43.07067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.07067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 86.14133
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: 330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 ILE A 563
REMARK 465 ASN A 564
REMARK 465 LYS A 613
REMARK 465 SER A 614
REMARK 465 ASP A 615
REMARK 465 LYS A 751
REMARK 465 THR A 752
REMARK 465 SER A 753
REMARK 465 PRO A 754
REMARK 465 ALA A 755
REMARK 465 ILE A 756
REMARK 465 MET A 757
REMARK 465 GLU A 758
REMARK 465 ASP A 759
REMARK 465 ASP A 760
REMARK 465 GLU A 761
REMARK 465 HIS A 934
REMARK 465 ILE A 935
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 N GLY A 565 O HOH A 1101 2.13
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 791 -20.01 79.28
REMARK 500 ASN A 828 50.49 -109.23
REMARK 500 ASP A 876 -167.70 -170.53
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 0LI A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1003
DBREF 4U0I A 563 751 UNP P10721 KIT_HUMAN 563 693
DBREF 4U0I A 754 935 UNP P10721 KIT_HUMAN 754 935
SEQADV 4U0I THR A 752 UNP P10721 LINKER
SEQADV 4U0I SER A 753 UNP P10721 LINKER
SEQRES 1 A 315 ILE ASN GLY ASN ASN TYR VAL TYR ILE ASP PRO THR GLN
SEQRES 2 A 315 LEU PRO TYR ASP HIS LYS TRP GLU PHE PRO ARG ASN ARG
SEQRES 3 A 315 LEU SER PHE GLY LYS THR LEU GLY ALA GLY ALA PHE GLY
SEQRES 4 A 315 LYS VAL VAL GLU ALA THR ALA TYR GLY LEU ILE LYS SER
SEQRES 5 A 315 ASP ALA ALA MET THR VAL ALA VAL LYS MET LEU LYS PRO
SEQRES 6 A 315 SER ALA HIS LEU THR GLU ARG GLU ALA LEU MET SER GLU
SEQRES 7 A 315 LEU LYS VAL LEU SER TYR LEU GLY ASN HIS MET ASN ILE
SEQRES 8 A 315 VAL ASN LEU LEU GLY ALA CYS THR ILE GLY GLY PRO THR
SEQRES 9 A 315 LEU VAL ILE THR GLU TYR CYS CYS TYR GLY ASP LEU LEU
SEQRES 10 A 315 ASN PHE LEU ARG ARG LYS ARG ASP SER PHE ILE CYS SER
SEQRES 11 A 315 LYS THR SER PRO ALA ILE MET GLU ASP ASP GLU LEU ALA
SEQRES 12 A 315 LEU ASP LEU GLU ASP LEU LEU SER PHE SER TYR GLN VAL
SEQRES 13 A 315 ALA LYS GLY MET ALA PHE LEU ALA SER LYS ASN CYS ILE
SEQRES 14 A 315 HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU LEU THR HIS
SEQRES 15 A 315 GLY ARG ILE THR LYS ILE CYS ASP PHE GLY LEU ALA ARG
SEQRES 16 A 315 ASP ILE LYS ASN ASP SER ASN TYR VAL VAL LYS GLY ASN
SEQRES 17 A 315 ALA ARG LEU PRO VAL LYS TRP MET ALA PRO GLU SER ILE
SEQRES 18 A 315 PHE ASN CYS VAL TYR THR PHE GLU SER ASP VAL TRP SER
SEQRES 19 A 315 TYR GLY ILE PHE LEU TRP GLU LEU PHE SER LEU GLY SER
SEQRES 20 A 315 SER PRO TYR PRO GLY MET PRO VAL ASP SER LYS PHE TYR
SEQRES 21 A 315 LYS MET ILE LYS GLU GLY PHE ARG MET LEU SER PRO GLU
SEQRES 22 A 315 HIS ALA PRO ALA GLU MET TYR ASP ILE MET LYS THR CYS
SEQRES 23 A 315 TRP ASP ALA ASP PRO LEU LYS ARG PRO THR PHE LYS GLN
SEQRES 24 A 315 ILE VAL GLN LEU ILE GLU LYS GLN ILE SER GLU SER THR
SEQRES 25 A 315 ASN HIS ILE
HET 0LI A1001 39
HET PO4 A1002 5
HET PO4 A1003 5
HETNAM 0LI 3-(IMIDAZO[1,2-B]PYRIDAZIN-3-YLETHYNYL)-4-METHYL-N-{4-
HETNAM 2 0LI [(4-METHYLPIPERAZIN-1-YL)METHYL]-3-(TRIFLUOROMETHYL)
HETNAM 3 0LI PHENYL}BENZAM IDE
HETNAM PO4 PHOSPHATE ION
HETSYN 0LI PONATINIB
FORMUL 2 0LI C29 H27 F3 N6 O
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *137(H2 O)
HELIX 1 AA1 ASP A 572 LEU A 576 5 5
HELIX 2 AA2 ASP A 579 GLU A 583 5 5
HELIX 3 AA3 PRO A 585 ASN A 587 5 3
HELIX 4 AA4 HIS A 630 GLY A 648 1 19
HELIX 5 AA5 ASP A 677 ARG A 686 1 10
HELIX 6 AA6 ASP A 687 PHE A 689 5 3
HELIX 7 AA7 ASP A 765 LYS A 786 1 22
HELIX 8 AA8 ALA A 794 ARG A 796 5 3
HELIX 9 AA9 PHE A 811 ARG A 815 5 5
HELIX 10 AB1 PRO A 832 MET A 836 5 5
HELIX 11 AB2 ALA A 837 CYS A 844 1 8
HELIX 12 AB3 THR A 847 SER A 864 1 18
HELIX 13 AB4 ASP A 876 GLY A 886 1 11
HELIX 14 AB5 PRO A 896 TRP A 907 1 12
HELIX 15 AB6 ASP A 910 ARG A 914 5 5
HELIX 16 AB7 THR A 916 SER A 931 1 16
SHEET 1 AA1 5 LEU A 589 ALA A 597 0
SHEET 2 AA1 5 GLY A 601 TYR A 609 -1 O VAL A 603 N LEU A 595
SHEET 3 AA1 5 ALA A 617 LEU A 625 -1 O MET A 618 N ALA A 608
SHEET 4 AA1 5 LEU A 667 GLU A 671 -1 O THR A 670 N ALA A 621
SHEET 5 AA1 5 LEU A 656 CYS A 660 -1 N LEU A 657 O ILE A 669
SHEET 1 AA2 2 ILE A 798 THR A 801 0
SHEET 2 AA2 2 ILE A 805 ILE A 808 -1 O LYS A 807 N LEU A 799
SHEET 1 AA3 2 VAL A 824 VAL A 825 0
SHEET 2 AA3 2 ARG A 830 LEU A 831 -1 O LEU A 831 N VAL A 824
SITE 1 AC1 22 LEU A 595 ALA A 621 VAL A 622 LYS A 623
SITE 2 AC1 22 GLU A 640 LEU A 647 ILE A 653 VAL A 654
SITE 3 AC1 22 THR A 670 GLU A 671 TYR A 672 CYS A 673
SITE 4 AC1 22 CYS A 788 ILE A 789 HIS A 790 ARG A 791
SITE 5 AC1 22 LEU A 799 ILE A 808 CYS A 809 ASP A 810
SITE 6 AC1 22 PHE A 811 HOH A1204
SITE 1 AC2 7 LYS A 642 TYR A 675 HIS A 802 GLY A 803
SITE 2 AC2 7 LYS A 913 HOH A1138 HOH A1188
SITE 1 AC3 7 THR A 619 TYR A 672 CYS A 674 HIS A 802
SITE 2 AC3 7 HOH A1105 HOH A1132 HOH A1193
CRYST1 70.032 70.032 129.212 90.00 90.00 120.00 P 32 2 1 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 0.014279 0.008244 0.000000 0.00000
SCALE2 0.000000 0.016488 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007739 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
