HEADER TRANSFERASE 25-MAY-06 2ITO
TITLE CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH
TITLE 2 IRESSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 696-1022;
COMPND 5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;
COMPND 6 EC: 2.7.10.1;
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACG2T;
SOURCE 11 OTHER_DETAILS: EGFR 696-1022 G719S
KEYWDS RECEPTOR, CELL CYCLE, ATP-BINDING, TRANSFERASE, TRANSMEMBRANE,
KEYWDS 2 PHOSPHORYLATION, DISEASE MUTATION, GLYCOPROTEIN, ANTI-ONCOGENE,
KEYWDS 3 NUCLEOTIDE- BINDING, IRESSA, EGFR, G719S, ZD1839, TYROSINE-PROTEIN
KEYWDS 4 KINASE, EPIDERMAL GROWTH FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-H.YUN,T.J.BOGGON,Y.LI,S.WOO,H.GREULICH,M.MEYERSON,M.J.ECK
REVDAT 6 27-MAR-24 2ITO 1 REMARK
REVDAT 5 13-DEC-23 2ITO 1 REMARK
REVDAT 4 15-OCT-14 2ITO 1 SOURCE KEYWDS AUTHOR JRNL
REVDAT 4 2 1 REMARK VERSN HETNAM FORMUL
REVDAT 4 3 1 MASTER
REVDAT 3 24-FEB-09 2ITO 1 VERSN
REVDAT 2 29-JAN-08 2ITO 1 SOURCE
REVDAT 1 03-APR-07 2ITO 0
JRNL AUTH C.-H.YUN,T.J.BOGGON,Y.LI,S.WOO,H.GREULICH,M.MEYERSON,M.J.ECK
JRNL TITL STRUCTURES OF LUNG CANCER-DERIVED EGFR MUTANTS AND INHIBITOR
JRNL TITL 2 COMPLEXES: MECHANISM OF ACTIVATION AND INSIGHTS INTO
JRNL TITL 3 DIFFERENTIAL INHIBITOR SENSITIVITY
JRNL REF CANCER CELL V. 11 217 2007
JRNL REFN ISSN 1535-6108
JRNL PMID 17349580
JRNL DOI 10.1016/J.CCR.2006.12.017
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 6991
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 767
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 492
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2419
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 34
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.64
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.534
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2502 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3386 ; 1.686 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 300 ; 7.368 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;39.803 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 458 ;22.350 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;19.281 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 380 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1834 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1215 ; 0.255 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1704 ; 0.329 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 90 ; 0.190 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 43 ; 0.210 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.149 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1512 ; 0.904 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2455 ; 1.674 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 990 ; 1.580 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 931 ; 2.776 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2ITO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1290028807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8145
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
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: PDB ENTRY 1M17
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M KNA TARTRATE, 0.1M HEPES 7.5, PH
REMARK 280 7.5
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 71.46450
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 71.46450
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 71.46450
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 71.46450
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 71.46450
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 71.46450
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 71.46450
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 719 TO SER
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 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 PRO A 990
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 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 988 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A1004 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 699 C - N - CA ANGL. DEV. = 9.4 DEGREES
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 ILE A 715 -18.43 -150.11
REMARK 500 LYS A 716 143.98 170.05
REMARK 500 SER A 719 116.24 -166.12
REMARK 500 SER A 720 -165.71 -123.34
REMARK 500 ALA A 722 -108.45 31.76
REMARK 500 PRO A 733 85.98 -60.40
REMARK 500 GLU A 734 137.06 -37.80
REMARK 500 ARG A 748 127.07 -32.54
REMARK 500 ALA A 750 85.17 -54.05
REMARK 500 THR A 751 47.71 -92.44
REMARK 500 PRO A 772 -8.70 -48.85
REMARK 500 THR A 783 -77.20 -26.44
REMARK 500 SER A 784 -44.21 -160.03
REMARK 500 PHE A 795 0.18 -67.08
REMARK 500 LYS A 806 -29.15 -19.28
REMARK 500 ARG A 831 39.89 -81.59
REMARK 500 ARG A 832 46.42 32.66
REMARK 500 ASP A 837 38.46 -177.63
REMARK 500 ASP A 855 91.81 58.30
REMARK 500 HIS A 888 11.84 -150.62
REMARK 500 ARG A 889 23.00 40.66
REMARK 500 ILE A 918 107.83 -23.95
REMARK 500 SER A 921 -19.77 -46.18
REMARK 500 ILE A 941 -38.78 -38.87
REMARK 500 ASP A 984 -70.27 -54.44
REMARK 500 ASP A1003 -136.66 -176.41
REMARK 500 GLU A1004 -179.08 89.93
REMARK 500 GLU A1005 -144.51 50.96
REMARK 500 ASP A1006 -87.93 -72.22
REMARK 500 MET A1007 2.37 84.08
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 2020
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ITN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX
REMARK 900 WITH AMP-PNP
REMARK 900 RELATED ID: 2ITP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX
REMARK 900 WITH AEE788
REMARK 900 RELATED ID: 2ITQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX
REMARK 900 WITH AFN941
REMARK 900 RELATED ID: 2ITT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX
REMARK 900 WITH AEE788
REMARK 900 RELATED ID: 2ITU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX
REMARK 900 WITH AFN941
REMARK 900 RELATED ID: 2ITV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX
REMARK 900 WITH AMP-PNP
REMARK 900 RELATED ID: 2ITW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AFN941
REMARK 900 RELATED ID: 2ITX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AMP-PNP
REMARK 900 RELATED ID: 2ITY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH IRESSA
REMARK 900 RELATED ID: 2ITZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX
REMARK 900 WITH IRESSA
DBREF 2ITO A 696 1022 UNP P00533 EGFR_HUMAN 696 1022
SEQADV 2ITO SER A 719 UNP P00533 GLY 719 ENGINEERED MUTATION
SEQRES 1 A 327 GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE LEU LYS
SEQRES 2 A 327 GLU THR GLU PHE LYS LYS ILE LYS VAL LEU SER SER GLY
SEQRES 3 A 327 ALA PHE GLY THR VAL TYR LYS GLY LEU TRP ILE PRO GLU
SEQRES 4 A 327 GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE LYS GLU LEU
SEQRES 5 A 327 ARG GLU ALA THR SER PRO LYS ALA ASN LYS GLU ILE LEU
SEQRES 6 A 327 ASP GLU ALA TYR VAL MET ALA SER VAL ASP ASN PRO HIS
SEQRES 7 A 327 VAL CYS ARG LEU LEU GLY ILE CYS LEU THR SER THR VAL
SEQRES 8 A 327 GLN LEU ILE THR GLN LEU MET PRO PHE GLY CYS LEU LEU
SEQRES 9 A 327 ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 A 327 TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 A 327 ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 A 327 ALA ALA ARG ASN VAL LEU VAL LYS THR PRO GLN HIS VAL
SEQRES 13 A 327 LYS ILE THR ASP PHE GLY LEU ALA LYS LEU LEU GLY ALA
SEQRES 14 A 327 GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY LYS VAL PRO
SEQRES 15 A 327 ILE LYS TRP MET ALA LEU GLU SER ILE LEU HIS ARG ILE
SEQRES 16 A 327 TYR THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 A 327 VAL TRP GLU LEU MET THR PHE GLY SER LYS PRO TYR ASP
SEQRES 18 A 327 GLY ILE PRO ALA SER GLU ILE SER SER ILE LEU GLU LYS
SEQRES 19 A 327 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 A 327 VAL TYR MET ILE MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 A 327 ASP SER ARG PRO LYS PHE ARG GLU LEU ILE ILE GLU PHE
SEQRES 22 A 327 SER LYS MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 A 327 GLN GLY ASP GLU ARG MET HIS LEU PRO SER PRO THR ASP
SEQRES 24 A 327 SER ASN PHE TYR ARG ALA LEU MET ASP GLU GLU ASP MET
SEQRES 25 A 327 ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU ILE PRO GLN
SEQRES 26 A 327 GLN GLY
HET IRE A2020 31
HETNAM IRE GEFITINIB
FORMUL 2 IRE C22 H24 CL F N4 O3
FORMUL 3 HOH *34(H2 O)
HELIX 1 1 LYS A 708 PHE A 712 5 5
HELIX 2 2 SER A 752 VAL A 769 1 18
HELIX 3 3 CYS A 797 HIS A 805 1 9
HELIX 4 4 GLY A 810 ARG A 831 1 22
HELIX 5 5 ALA A 839 ARG A 841 5 3
HELIX 6 6 PRO A 877 MET A 881 5 5
HELIX 7 7 ALA A 882 ARG A 889 1 8
HELIX 8 8 THR A 892 THR A 909 1 18
HELIX 9 9 PRO A 919 SER A 921 5 3
HELIX 10 10 GLU A 922 LYS A 929 1 8
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 ALA A 972 1 13
HELIX 14 14 ARG A 973 TYR A 978 5 6
HELIX 15 15 GLY A 983 MET A 987 5 5
HELIX 16 16 ASP A 1012 TYR A 1016 5 5
SHEET 1 AA 5 LYS A 714 SER A 719 0
SHEET 2 AA 5 GLY A 724 TRP A 731 -1 O VAL A 726 N LEU A 718
SHEET 3 AA 5 ILE A 740 LEU A 747 -1 O ILE A 740 N TRP A 731
SHEET 4 AA 5 GLN A 787 GLN A 791 -1 O LEU A 788 N LYS A 745
SHEET 5 AA 5 LEU A 777 CYS A 781 -1 N LEU A 778 O ILE A 789
SHEET 1 AB 2 LEU A 833 VAL A 834 0
SHEET 2 AB 2 LYS A 860 LEU A 861 -1 O LYS A 860 N VAL A 834
SHEET 1 AC 2 VAL A 843 THR A 847 0
SHEET 2 AC 2 HIS A 850 ILE A 853 -1 O HIS A 850 N LYS A 846
SITE 1 AC1 12 SER A 719 ALA A 743 LYS A 745 GLU A 762
SITE 2 AC1 12 MET A 766 LEU A 788 THR A 790 GLN A 791
SITE 3 AC1 12 MET A 793 PRO A 794 GLY A 796 ASP A 800
CRYST1 142.929 142.929 142.929 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 0.006996 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006996 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006996 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
