HEADER TRANSFERASE 21-NOV-12 4I23
TITLE CRYSTAL STRUCTURE OF THE WILD-TYPE EGFR KINASE DOMAIN IN COMPLEX WITH
TITLE 2 DACOMITINIB (SOAKED)
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
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, PHOSPHOTRANSFER, ATP BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,J.FENG,R.FERRE,K.RYAN,O.BRODSKY,A.STEWART
REVDAT 3 28-FEB-24 4I23 1 REMARK SEQADV
REVDAT 2 27-FEB-13 4I23 1 JRNL
REVDAT 1 16-JAN-13 4I23 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2762218.050
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 12873
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 658
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.4760
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 664
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0120
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 13013
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2008
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2429
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.41
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) : 0.54
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 1.790 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.090 ; 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 : 0.32
REMARK 3 BSOL : 33.13
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 4I23 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_1000076206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 6.9 - 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.910
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 0.57900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
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 (%): 64.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.4 M NA-K TARTRATE 0.1 M MES, PH
REMARK 280 6.9-7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 73.17100
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 73.17100
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 73.17100
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 73.17100
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 73.17100
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 73.17100
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 694
REMARK 465 GLY A 721
REMARK 465 ALA A 722
REMARK 465 PHE A 723
REMARK 465 ARG A 748
REMARK 465 GLU A 749
REMARK 465 SER A 991
REMARK 465 PRO A 992
REMARK 465 THR A 993
REMARK 465 ASP A 994
REMARK 465 SER A 995
REMARK 465 ASN A 996
REMARK 465 PHE A 997
REMARK 465 TYR A 998
REMARK 465 ARG A 999
REMARK 465 ALA A 1000
REMARK 465 LEU A 1001
REMARK 465 MET A 1002
REMARK 465 ASP A 1003
REMARK 465 GLU A 1004
REMARK 465 GLU A 1005
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 LYS A 713 48.58 -145.52
REMARK 500 LYS A 714 128.11 -32.83
REMARK 500 LYS A 716 149.45 177.60
REMARK 500 GLU A 746 -146.99 -116.92
REMARK 500 LEU A 782 48.49 -95.25
REMARK 500 SER A 784 -60.15 -12.36
REMARK 500 LYS A 806 -50.21 -21.89
REMARK 500 ASP A 837 43.96 -150.79
REMARK 500 ASP A 855 72.46 62.68
REMARK 500 LEU A 858 -1.34 -155.25
REMARK 500 GLU A 865 -9.64 -150.06
REMARK 500 LYS A 867 50.53 -114.30
REMARK 500 GLU A 868 173.71 174.55
REMARK 500 GLU A 872 -127.24 -142.72
REMARK 500 ARG A 889 47.61 39.51
REMARK 500 ARG A 986 60.73 -104.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1C9 A 9001
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1C9 A 9001
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: 4I22 RELATED DB: PDB
REMARK 900 RELATED ID: 4I24 RELATED DB: PDB
DBREF 4I23 A 695 1022 UNP P00533 EGFR_HUMAN 695 1022
SEQADV 4I23 GLY A 694 UNP P00533 EXPRESSION TAG
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 THR 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 LEU 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 VAL 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 1C9 A9001 22
HETNAM 1C9 (2E)-N-{4-[(3-CHLORO-4-FLUOROPHENYL)AMINO]-7-
HETNAM 2 1C9 METHOXYQUINAZOLIN-6-YL}-4-(PIPERIDIN-1-YL)BUT-2-
HETNAM 3 1C9 ENAMIDE
HETSYN 1C9 DACOMITINIB
FORMUL 2 1C9 C24 H25 CL F N5 O2
HELIX 1 1 LYS A 708 PHE A 712 5 5
HELIX 2 2 LYS A 754 ALA A 767 1 14
HELIX 3 3 CYS A 797 LYS A 806 1 10
HELIX 4 4 ASP A 807 ILE A 809 5 3
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 PRO A 877 MET A 881 5 5
HELIX 8 8 LEU A 883 HIS A 888 1 6
HELIX 9 9 THR A 892 THR A 909 1 18
HELIX 10 10 PRO A 919 LEU A 927 1 9
HELIX 11 11 THR A 940 CYS A 950 1 11
HELIX 12 12 ASP A 954 ARG A 958 5 5
HELIX 13 13 LYS A 960 ASP A 974 1 15
HELIX 14 14 PRO A 975 TYR A 978 5 4
HELIX 15 15 ASP A 1012 TYR A 1016 5 5
SHEET 1 A 5 LYS A 716 GLY A 719 0
SHEET 2 A 5 THR A 725 TRP A 731 -1 O VAL A 726 N LEU A 718
SHEET 3 A 5 ILE A 740 GLU A 746 -1 O ILE A 740 N TRP A 731
SHEET 4 A 5 VAL A 786 GLN A 791 -1 O LEU A 788 N LYS A 745
SHEET 5 A 5 LEU A 777 LEU A 782 -1 N LEU A 778 O ILE A 789
SHEET 1 B 2 LEU A 833 VAL A 834 0
SHEET 2 B 2 LYS A 860 LEU A 861 -1 O LYS A 860 N VAL A 834
SHEET 1 C 2 VAL A 843 THR A 847 0
SHEET 2 C 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SITE 1 AC1 11 LEU A 718 ALA A 743 LYS A 745 GLU A 762
SITE 2 AC1 11 MET A 766 LEU A 788 THR A 790 GLN A 791
SITE 3 AC1 11 MET A 793 PRO A 794 GLY A 796
CRYST1 146.342 146.342 146.342 90.00 90.00 90.00 I 2 3 24
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 0.006833 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006833 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
