HEADER TRANSFERASE 21-NOV-12 4I22
TITLE STRUCTURE OF THE MONOMERIC (V948R)GEFITINIB/ERLOTINIB RESISTANT DOUBLE
TITLE 2 MUTANT (L858R+T790M) EGFR KINASE DOMAIN CO-CRYSTALLIZED WITH
TITLE 3 GEFITINIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 695-1022, EGFR KINASE DOMAIN;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-ERBB-1, RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 6 ERBB-1;
COMPND 7 EC: 2.7.10.1;
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 GENE: EGFR, ERBB, ERBB1, HER1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE DOMAIN, PHOSPHOTRASFER, ATP BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,J.FENG,R.FERRE,K.RYAN,O.BRODSKY,A.STEWART
REVDAT 6 27-MAR-24 4I22 1 REMARK
REVDAT 5 28-FEB-24 4I22 1 REMARK SEQADV
REVDAT 4 15-NOV-17 4I22 1 REMARK
REVDAT 3 15-OCT-14 4I22 1 HETNAM
REVDAT 2 27-FEB-13 4I22 1 JRNL
REVDAT 1 16-JAN-13 4I22 0
JRNL AUTH K.S.GAJIWALA,J.FENG,R.FERRE,K.RYAN,O.BRODSKY,S.WEINRICH,
JRNL AUTH 2 J.C.KATH,A.STEWART
JRNL TITL INSIGHTS INTO THE ABERRANT ACTIVITY OF MUTANT EGFR KINASE
JRNL TITL 2 DOMAIN AND DRUG RECOGNITION.
JRNL REF STRUCTURE V. 21 209 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 23273428
JRNL DOI 10.1016/J.STR.2012.11.014
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 927519.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 39296
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1980
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1980
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1970
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1980
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0050
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 39296
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5109
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 250
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2400
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 134
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66000
REMARK 3 B22 (A**2) : 3.37000
REMARK 3 B33 (A**2) : -1.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.81000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.620
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.430 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.300 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.320 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 42.31
REMARK 3
REMARK 3 NCS MODEL : NONE
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.PARA
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARA
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : LIG.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : LIG.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4I22 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : 1.0
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39302
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 42.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.02800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.0% PEG 3350, 0.2 M LI SULFATE, 0.1
REMARK 280 M BIS-TRIS PH 5.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 GLU A 697
REMARK 465 ALA A 698
REMARK 465 PRO A 699
REMARK 465 GLU A 749
REMARK 465 ALA A 750
REMARK 465 THR A 751
REMARK 465 SER A 752
REMARK 465 PRO A 753
REMARK 465 GLY A 863
REMARK 465 ALA A 864
REMARK 465 GLU A 865
REMARK 465 GLU A 866
REMARK 465 LYS A 867
REMARK 465 GLU A 868
REMARK 465 TYR A 869
REMARK 465 HIS A 870
REMARK 465 ALA A 871
REMARK 465 GLU A 872
REMARK 465 GLY A 873
REMARK 465 GLY A 874
REMARK 465 LYS A 875
REMARK 465 GLU A 1015
REMARK 465 TYR A 1016
REMARK 465 LEU A 1017
REMARK 465 ILE A 1018
REMARK 465 PRO A 1019
REMARK 465 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
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 783 -127.98 -127.48
REMARK 500 ARG A 836 -10.75 82.39
REMARK 500 ASP A 837 45.66 -146.26
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 IRE A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 9003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I1Z RELATED DB: PDB
REMARK 900 RELATED ID: 4I20 RELATED DB: PDB
REMARK 900 RELATED ID: 4I21 RELATED DB: PDB
REMARK 900 RELATED ID: 4I23 RELATED DB: PDB
REMARK 900 RELATED ID: 4I24 RELATED DB: PDB
DBREF 4I22 A 695 1022 UNP P00533 EGFR_HUMAN 695 1022
SEQADV 4I22 GLY A 694 UNP P00533 EXPRESSION TAG
SEQADV 4I22 MET A 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 4I22 ARG A 858 UNP P00533 LEU 858 ENGINEERED MUTATION
SEQADV 4I22 ARG A 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQRES 1 A 329 GLY SER GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE
SEQRES 2 A 329 LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU GLY
SEQRES 3 A 329 SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP ILE
SEQRES 4 A 329 PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE LYS
SEQRES 5 A 329 GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS GLU
SEQRES 6 A 329 ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP ASN
SEQRES 7 A 329 PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR SER
SEQRES 8 A 329 THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE GLY CYS
SEQRES 9 A 329 LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE GLY
SEQRES 10 A 329 SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS
SEQRES 11 A 329 GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS ARG
SEQRES 12 A 329 ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO GLN
SEQRES 13 A 329 HIS VAL LYS ILE THR ASP PHE GLY ARG ALA LYS LEU LEU
SEQRES 14 A 329 GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY LYS
SEQRES 15 A 329 VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU HIS
SEQRES 16 A 329 ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR GLY
SEQRES 17 A 329 VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS PRO
SEQRES 18 A 329 TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE LEU
SEQRES 19 A 329 GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR
SEQRES 20 A 329 ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP MET ILE
SEQRES 21 A 329 ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE ILE
SEQRES 22 A 329 GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR LEU
SEQRES 23 A 329 VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER PRO
SEQRES 24 A 329 THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU GLU
SEQRES 25 A 329 ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU ILE
SEQRES 26 A 329 PRO GLN GLN GLY
HET IRE A9001 31
HET SO4 A9002 5
HET SO4 A9003 5
HETNAM IRE GEFITINIB
HETNAM SO4 SULFATE ION
FORMUL 2 IRE C22 H24 CL F N4 O3
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *134(H2 O)
HELIX 1 1 ASN A 700 LEU A 704 5 5
HELIX 2 2 LYS A 708 THR A 710 5 3
HELIX 3 3 ALA A 755 ALA A 767 1 13
HELIX 4 4 CYS A 797 HIS A 805 1 9
HELIX 5 5 GLY A 810 ARG A 831 1 22
HELIX 6 6 ALA A 839 ARG A 841 5 3
HELIX 7 7 GLY A 857 LEU A 862 1 6
HELIX 8 8 PRO A 877 MET A 881 5 5
HELIX 9 9 ALA A 882 ARG A 889 1 8
HELIX 10 10 THR A 892 THR A 909 1 18
HELIX 11 11 PRO A 919 SER A 921 5 3
HELIX 12 12 GLU A 922 LYS A 929 1 8
HELIX 13 13 THR A 940 TRP A 951 1 12
HELIX 14 14 ASP A 954 ARG A 958 5 5
HELIX 15 15 LYS A 960 ARG A 973 1 14
HELIX 16 16 ASP A 974 LEU A 979 1 6
HELIX 17 17 GLY A 983 MET A 987 5 5
HELIX 18 18 SER A 991 ASP A 1003 1 13
SHEET 1 A 6 ARG A 705 ILE A 706 0
SHEET 2 A 6 GLY A 779 LEU A 782 1 O ILE A 780 N ARG A 705
SHEET 3 A 6 VAL A 786 MET A 790 -1 O ILE A 789 N GLY A 779
SHEET 4 A 6 ILE A 740 LEU A 747 -1 N ALA A 743 O MET A 790
SHEET 5 A 6 GLY A 724 TRP A 731 -1 N TYR A 727 O ILE A 744
SHEET 6 A 6 PHE A 712 SER A 720 -1 N LEU A 718 O VAL A 726
SHEET 1 B 2 VAL A 843 THR A 847 0
SHEET 2 B 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SITE 1 AC1 18 LEU A 718 ALA A 743 LYS A 745 LEU A 788
SITE 2 AC1 18 MET A 790 GLN A 791 LEU A 792 MET A 793
SITE 3 AC1 18 PRO A 794 GLY A 796 ASP A 800 LEU A 844
SITE 4 AC1 18 THR A 854 ASP A 855 HOH A9101 HOH A9102
SITE 5 AC1 18 HOH A9183 HOH A9224
SITE 1 AC2 3 ARG A 748 ARG A 832 HIS A 893
SITE 1 AC3 6 ARG A 803 LYS A 913 ARG A 962 HOH A9208
SITE 2 AC3 6 HOH A9210 HOH A9217
CRYST1 76.519 35.486 77.781 90.00 112.89 90.00 P 1 2 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 0.013069 0.000000 0.005517 0.00000
SCALE2 0.000000 0.028180 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013955 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
