HEADER TRANSFERASE 21-FEB-16 5I9X
TITLE CRYSTAL STRUCTURE OF EPHRIN A2 (EPHA2) RECEPTOR PROTEIN KINASE WITH
TITLE 2 BOSUTINIB (SKI-606)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 596-900;
COMPND 5 SYNONYM: EPITHELIAL CELL KINASE,TYROSINE-PROTEIN KINASE RECEPTOR ECK;
COMPND 6 EC: 2.7.10.1;
COMPND 7 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: EPHA2, ECK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS TRANSFERASE, TYROSINE-PROTEIN KINASE, RECEPTOR, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KUDLINZKI,V.L.LINHARD,S.L.GANDE,S.SREERAMULU,K.SAXENA,S.HEINZLMEIR,
AUTHOR 2 G.MEDARD,B.KUESTER,H.SCHWALBE
REVDAT 5 10-JAN-24 5I9X 1 REMARK
REVDAT 4 12-JUN-19 5I9X 1 AUTHOR
REVDAT 3 07-MAR-18 5I9X 1 SOURCE REMARK
REVDAT 2 28-DEC-16 5I9X 1 JRNL
REVDAT 1 09-NOV-16 5I9X 0
JRNL AUTH S.HEINZLMEIR,D.KUDLINZKI,S.SREERAMULU,S.KLAEGER,S.L.GANDE,
JRNL AUTH 2 V.LINHARD,M.WILHELM,H.QIAO,D.HELM,B.RUPRECHT,K.SAXENA,
JRNL AUTH 3 G.MEDARD,H.SCHWALBE,B.KUSTER
JRNL TITL CHEMICAL PROTEOMICS AND STRUCTURAL BIOLOGY DEFINE EPHA2
JRNL TITL 2 INHIBITION BY CLINICAL KINASE DRUGS.
JRNL REF ACS CHEM. BIOL. V. 11 3400 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27768280
JRNL DOI 10.1021/ACSCHEMBIO.6B00709
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 94776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4745
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 38.4161 - 4.4319 0.98 3054 164 0.1730 0.1847
REMARK 3 2 4.4319 - 3.5185 0.99 3059 162 0.1409 0.1460
REMARK 3 3 3.5185 - 3.0739 0.99 3059 157 0.1480 0.1690
REMARK 3 4 3.0739 - 2.7930 0.98 3067 163 0.1521 0.1799
REMARK 3 5 2.7930 - 2.5928 0.98 3032 161 0.1594 0.1749
REMARK 3 6 2.5928 - 2.4400 0.99 3065 163 0.1544 0.1717
REMARK 3 7 2.4400 - 2.3178 0.99 3038 159 0.1549 0.1949
REMARK 3 8 2.3178 - 2.2169 0.98 3053 159 0.1538 0.1951
REMARK 3 9 2.2169 - 2.1316 0.99 3017 159 0.1500 0.1615
REMARK 3 10 2.1316 - 2.0580 0.98 3044 160 0.1496 0.1973
REMARK 3 11 2.0580 - 1.9937 0.97 3088 162 0.1521 0.1622
REMARK 3 12 1.9937 - 1.9367 0.98 2958 155 0.1532 0.1740
REMARK 3 13 1.9367 - 1.8857 0.98 3113 163 0.1527 0.1716
REMARK 3 14 1.8857 - 1.8397 0.98 2962 157 0.1566 0.1556
REMARK 3 15 1.8397 - 1.7979 0.98 3063 161 0.1588 0.1590
REMARK 3 16 1.7979 - 1.7596 0.97 3004 158 0.1586 0.1731
REMARK 3 17 1.7596 - 1.7244 0.97 2960 156 0.1726 0.2095
REMARK 3 18 1.7244 - 1.6919 0.97 3049 164 0.1806 0.2118
REMARK 3 19 1.6919 - 1.6617 0.97 2962 155 0.1863 0.1813
REMARK 3 20 1.6617 - 1.6335 0.95 2932 156 0.1905 0.1690
REMARK 3 21 1.6335 - 1.6072 0.97 3030 161 0.1974 0.1816
REMARK 3 22 1.6072 - 1.5824 0.97 2976 156 0.1972 0.1921
REMARK 3 23 1.5824 - 1.5592 0.97 2966 155 0.2007 0.2327
REMARK 3 24 1.5592 - 1.5372 0.96 2978 155 0.2200 0.2054
REMARK 3 25 1.5372 - 1.5164 0.96 2992 158 0.2174 0.2750
REMARK 3 26 1.5164 - 1.4967 0.96 2955 156 0.2269 0.2210
REMARK 3 27 1.4967 - 1.4780 0.96 2987 156 0.2361 0.2474
REMARK 3 28 1.4780 - 1.4602 0.96 3026 160 0.2292 0.2673
REMARK 3 29 1.4602 - 1.4432 0.95 2893 151 0.2474 0.2561
REMARK 3 30 1.4432 - 1.4270 0.86 2649 143 0.2738 0.2871
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 2410
REMARK 3 ANGLE : 0.877 3250
REMARK 3 CHIRALITY : 0.082 346
REMARK 3 PLANARITY : 0.005 410
REMARK 3 DIHEDRAL : 21.065 923
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5I9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000217940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94778
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.427
REMARK 200 RESOLUTION RANGE LOW (A) : 38.402
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 1MQB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37.5 % MPD_P1K_P3350, 0.1 M
REMARK 280 AMINOACIDSMIX, 0.1 M MES PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 53.84750
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 TOTAL BURIED SURFACE AREA: 730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 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 GLY A 595
REMARK 465 ASP A 596
REMARK 465 PRO A 597
REMARK 465 ASN A 598
REMARK 465 GLN A 599
REMARK 465 ALA A 600
REMARK 465 VAL A 601
REMARK 465 LEU A 602
REMARK 465 LYS A 603
REMARK 465 SER A 635
REMARK 465 SER A 636
REMARK 465 GLY A 637
REMARK 465 LYS A 638
REMARK 465 LYS A 639
REMARK 465 THR A 773
REMARK 465 THR A 774
REMARK 465 SER A 775
REMARK 465 GLY A 776
REMARK 465 SER A 897
REMARK 465 THR A 898
REMARK 465 SER A 899
REMARK 465 GLY A 900
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 O HOH A 1108 O HOH A 1216 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1226 O HOH A 1307 1455 2.17
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 THR A 605 165.14 65.37
REMARK 500 ARG A 738 -16.23 76.15
REMARK 500 ASP A 757 79.94 76.64
REMARK 500 LEU A 760 -110.33 -96.70
REMARK 500 TRP A 819 -130.62 54.97
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 DB8 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1005
DBREF 5I9X A 596 900 UNP P29317 EPHA2_HUMAN 596 900
SEQADV 5I9X GLY A 595 UNP P29317 EXPRESSION TAG
SEQRES 1 A 306 GLY ASP PRO ASN GLN ALA VAL LEU LYS PHE THR THR GLU
SEQRES 2 A 306 ILE HIS PRO SER CYS VAL THR ARG GLN LYS VAL ILE GLY
SEQRES 3 A 306 ALA GLY GLU PHE GLY GLU VAL TYR LYS GLY MET LEU LYS
SEQRES 4 A 306 THR SER SER GLY LYS LYS GLU VAL PRO VAL ALA ILE LYS
SEQRES 5 A 306 THR LEU LYS ALA GLY TYR THR GLU LYS GLN ARG VAL ASP
SEQRES 6 A 306 PHE LEU GLY GLU ALA GLY ILE MET GLY GLN PHE SER HIS
SEQRES 7 A 306 HIS ASN ILE ILE ARG LEU GLU GLY VAL ILE SER LYS TYR
SEQRES 8 A 306 LYS PRO MET MET ILE ILE THR GLU TYR MET GLU ASN GLY
SEQRES 9 A 306 ALA LEU ASP LYS PHE LEU ARG GLU LYS ASP GLY GLU PHE
SEQRES 10 A 306 SER VAL LEU GLN LEU VAL GLY MET LEU ARG GLY ILE ALA
SEQRES 11 A 306 ALA GLY MET LYS TYR LEU ALA ASN MET ASN TYR VAL HIS
SEQRES 12 A 306 ARG ASP LEU ALA ALA ARG ASN ILE LEU VAL ASN SER ASN
SEQRES 13 A 306 LEU VAL CYS LYS VAL SER ASP PHE GLY LEU SER ARG VAL
SEQRES 14 A 306 LEU GLU ASP ASP PRO GLU ALA THR TYR THR THR SER GLY
SEQRES 15 A 306 GLY LYS ILE PRO ILE ARG TRP THR ALA PRO GLU ALA ILE
SEQRES 16 A 306 SER TYR ARG LYS PHE THR SER ALA SER ASP VAL TRP SER
SEQRES 17 A 306 PHE GLY ILE VAL MET TRP GLU VAL MET THR TYR GLY GLU
SEQRES 18 A 306 ARG PRO TYR TRP GLU LEU SER ASN HIS GLU VAL MET LYS
SEQRES 19 A 306 ALA ILE ASN ASP GLY PHE ARG LEU PRO THR PRO MET ASP
SEQRES 20 A 306 CYS PRO SER ALA ILE TYR GLN LEU MET MET GLN CYS TRP
SEQRES 21 A 306 GLN GLN GLU ARG ALA ARG ARG PRO LYS PHE ALA ASP ILE
SEQRES 22 A 306 VAL SER ILE LEU ASP LYS LEU ILE ARG ALA PRO ASP SER
SEQRES 23 A 306 LEU LYS THR LEU ALA ASP PHE ASP PRO ARG VAL SER ILE
SEQRES 24 A 306 ARG LEU PRO SER THR SER GLY
HET DB8 A1001 36
HET EDO A1002 4
HET EDO A1003 4
HET EDO A1004 4
HET EDO A1005 4
HETNAM DB8 4-[(2,4-DICHLORO-5-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-
HETNAM 2 DB8 (4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-
HETNAM 3 DB8 CARBONITRILE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN DB8 BOSUTINIB
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 DB8 C26 H29 CL2 N5 O3
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 7 HOH *235(H2 O)
HELIX 1 AA1 HIS A 609 SER A 611 5 3
HELIX 2 AA2 THR A 653 GLY A 668 1 16
HELIX 3 AA3 LEU A 700 LYS A 707 1 8
HELIX 4 AA4 SER A 712 MET A 733 1 22
HELIX 5 AA5 ALA A 741 ARG A 743 5 3
HELIX 6 AA6 SER A 761 ASP A 767 1 7
HELIX 7 AA7 PRO A 780 THR A 784 5 5
HELIX 8 AA8 ALA A 785 ARG A 792 1 8
HELIX 9 AA9 THR A 795 THR A 812 1 18
HELIX 10 AB1 SER A 822 ASP A 832 1 11
HELIX 11 AB2 PRO A 843 TRP A 854 1 12
HELIX 12 AB3 GLU A 857 ARG A 861 5 5
HELIX 13 AB4 LYS A 863 ALA A 877 1 15
HELIX 14 AB5 PRO A 878 LYS A 882 5 5
SHEET 1 AA1 5 VAL A 613 ALA A 621 0
SHEET 2 AA1 5 GLU A 626 LEU A 632 -1 O VAL A 627 N GLY A 620
SHEET 3 AA1 5 VAL A 641 LEU A 648 -1 O ILE A 645 N TYR A 628
SHEET 4 AA1 5 MET A 688 GLU A 693 -1 O ILE A 690 N LYS A 646
SHEET 5 AA1 5 LEU A 678 ILE A 682 -1 N GLY A 680 O ILE A 691
SHEET 1 AA2 3 GLY A 698 ALA A 699 0
SHEET 2 AA2 3 ILE A 745 VAL A 747 -1 O VAL A 747 N GLY A 698
SHEET 3 AA2 3 CYS A 753 VAL A 755 -1 O LYS A 754 N LEU A 746
CISPEP 1 LYS A 686 PRO A 687 0 1.95
SITE 1 AC1 17 ILE A 619 ALA A 644 ILE A 645 LYS A 646
SITE 2 AC1 17 GLU A 663 SER A 671 ILE A 676 ILE A 690
SITE 3 AC1 17 THR A 692 GLU A 693 TYR A 694 MET A 695
SITE 4 AC1 17 GLU A 696 LEU A 746 HOH A1130 HOH A1175
SITE 5 AC1 17 HOH A1251
SITE 1 AC2 6 ASN A 732 GLU A 815 LYS A 863 PHE A 864
SITE 2 AC2 6 ALA A 865 HOH A1140
SITE 1 AC3 7 ILE A 781 THR A 784 ILE A 789 MET A 827
SITE 2 AC3 7 ILE A 830 EDO A1004 HOH A1116
SITE 1 AC4 4 GLU A 710 PRO A 786 ASN A 831 EDO A1003
SITE 1 AC5 6 HIS A 673 ASN A 748 ASN A 750 VAL A 752
SITE 2 AC5 6 LYS A 754 HOH A1135
CRYST1 32.803 107.695 40.604 90.00 108.95 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 0.030485 0.000000 0.010467 0.00000
SCALE2 0.000000 0.009285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
