HEADER TRANSFERASE 25-APR-06 2GS6
TITLE CRYSTAL STRUCTURE OF THE ACTIVE EGFR KINASE DOMAIN IN COMPLEX WITH AN
TITLE 2 ATP ANALOG-PEPTIDE CONJUGATE
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 MOL_ID: 2;
COMPND 9 MOLECULE: PEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 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, ERBB1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULORVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HT;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES
KEYWDS EGFR, KINASE, ACTIVE, ATP-ANALOG PEPTIDE CONJUGATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.ZHANG,J.GUREASKO,K.SHEN,P.A.COLE,J.KURIYAN
REVDAT 5 30-AUG-23 2GS6 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2GS6 1 REMARK
REVDAT 3 24-FEB-09 2GS6 1 VERSN
REVDAT 2 27-JUN-06 2GS6 1 JRNL
REVDAT 1 20-JUN-06 2GS6 0
JRNL AUTH X.ZHANG,J.GUREASKO,K.SHEN,P.A.COLE,J.KURIYAN
JRNL TITL AN ALLOSTERIC MECHANISM FOR ACTIVATION OF THE KINASE DOMAIN
JRNL TITL 2 OF EPIDERMAL GROWTH FACTOR RECEPTOR
JRNL REF CELL(CAMBRIDGE,MASS.) V. 125 1137 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16777603
JRNL DOI 10.1016/J.CELL.2006.05.013
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
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) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 14724
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 SET) : 0.206
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1486
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 : 2502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.09
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) : 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) : 1.436 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.513 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.044 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.135 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 41.33
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 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : ATP_LINKER_PAR.TXT
REMARK 3 PARAMETER FILE 5 : 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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GS6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-04
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 : ALS
REMARK 200 BEAMLINE : 8.2.2
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 : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BOS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15419
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
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 1M14
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2 M LICITRATE, 4%
REMARK 280 POLYPROPROPYLENE GLYCOL, 100 MM HEPES, PH 7.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 72.09100
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 72.09100
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 72.09100
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 72.09100
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 72.09100
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 72.09100
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 72.09100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN ASYMMETRIC DIMER THAT IS
REMARK 300 GENERATED BY A 3(2) FOLD OPERATION OF THE MONOMER IN THE ASYMMETRIC
REMARK 300 UNIT: -Z+3/2,X-1/2,-Y+1/2
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 0.000000 0.000000 -1.000000 216.27300
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -72.09100
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 72.09100
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 ARG A 724
REMARK 465 GLU A 725
REMARK 465 ALA A 726
REMARK 465 PRO A 968
REMARK 465 THR A 969
REMARK 465 ASP A 970
REMARK 465 SER A 971
REMARK 465 ASN A 972
REMARK 465 PHE A 973
REMARK 465 TYR A 974
REMARK 465 ARG A 975
REMARK 465 ALA A 976
REMARK 465 LEU A 977
REMARK 465 MET A 978
REMARK 465 ASP A 979
REMARK 465 GLU A 980
REMARK 465 GLN A 996
REMARK 465 GLN A 997
REMARK 465 GLY A 998
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 PHE B 9
REMARK 465 GLU B 10
REMARK 465 ALA B 11
REMARK 465 LYS B 12
REMARK 465 LYS B 13
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 PHE A 699 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 962 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 4 CG CD OE1 OE2
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 GLN A 677 32.23 -93.86
REMARK 500 LYS A 689 56.76 -143.59
REMARK 500 LYS A 690 84.66 -30.06
REMARK 500 ALA A 698 62.03 -104.20
REMARK 500 PHE A 699 -4.80 179.21
REMARK 500 GLU A 712 135.57 -32.34
REMARK 500 GLU A 722 30.03 -99.80
REMARK 500 SER A 760 -57.02 -7.83
REMARK 500 ASP A 783 15.98 -69.15
REMARK 500 ASP A 813 36.31 -149.95
REMARK 500 ASP A 831 83.42 53.49
REMARK 500 PRO A 853 93.43 -66.85
REMARK 500 ASP A 950 60.91 -154.41
REMARK 500 GLN A 952 -9.34 -59.48
REMARK 500 PRO A 966 -161.55 -52.74
REMARK 500 MET A 983 105.29 -50.20
REMARK 500 ASP A 984 -68.62 -160.13
REMARK 500 ILE B 5 115.09 56.11
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 CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 112 B 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GS2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ACTIVE EGFR KINASE DOMAIN
REMARK 900 RELATED ID: 2GS7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INACTIVE EGFR KINASE DOMAIN IN COMPLEX
REMARK 900 WITH AMP-PNP
DBREF 2GS6 A 672 998 UNP Q9H2C9 EGFR_HUMAN 696 1022
DBREF 2GS6 B 1 13 PDB 2GS6 2GS6 1 13
SEQADV 2GS6 GLY A 669 UNP Q9H2C9 CLONING ARTIFACT
SEQADV 2GS6 ALA A 670 UNP Q9H2C9 CLONING ARTIFACT
SEQADV 2GS6 MET A 671 UNP Q9H2C9 CLONING ARTIFACT
SEQRES 1 A 330 GLY ALA MET GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG
SEQRES 2 A 330 ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU
SEQRES 3 A 330 GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP
SEQRES 4 A 330 ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE
SEQRES 5 A 330 LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS
SEQRES 6 A 330 GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP
SEQRES 7 A 330 ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR
SEQRES 8 A 330 SER THR VAL GLN LEU ILE THR GLN LEU MET PRO PHE GLY
SEQRES 9 A 330 CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE
SEQRES 10 A 330 GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA
SEQRES 11 A 330 LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS
SEQRES 12 A 330 ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO
SEQRES 13 A 330 GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS LEU
SEQRES 14 A 330 LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY
SEQRES 15 A 330 LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU
SEQRES 16 A 330 HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR
SEQRES 17 A 330 GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS
SEQRES 18 A 330 PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE
SEQRES 19 A 330 LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS
SEQRES 20 A 330 THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP MET
SEQRES 21 A 330 ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE
SEQRES 22 A 330 ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR
SEQRES 23 A 330 LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER
SEQRES 24 A 330 PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU
SEQRES 25 A 330 GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU
SEQRES 26 A 330 ILE PRO GLN GLN GLY
SEQRES 1 B 13 ALA GLU GLU GLU ILE TYR GLY GLU PHE GLU ALA LYS LYS
HET CL A 201 1
HET 112 B 101 35
HETNAM CL CHLORIDE ION
HETNAM 112 THIOPHOSPHORIC ACID O-((ADENOSYL-PHOSPHO)PHOSPHO)-S-
HETNAM 2 112 ACETAMIDYL-DIESTER
FORMUL 3 CL CL 1-
FORMUL 4 112 C12 H19 N6 O13 P3 S
FORMUL 5 HOH *74(H2 O)
HELIX 1 1 LYS A 684 PHE A 688 5 5
HELIX 2 2 SER A 728 SER A 744 1 17
HELIX 3 3 CYS A 773 HIS A 781 1 9
HELIX 4 4 LYS A 782 ILE A 785 5 4
HELIX 5 5 GLY A 786 ARG A 807 1 22
HELIX 6 6 ALA A 815 ARG A 817 5 3
HELIX 7 7 PRO A 853 MET A 857 5 5
HELIX 8 8 ALA A 858 ARG A 865 1 8
HELIX 9 9 THR A 868 THR A 885 1 18
HELIX 10 10 PRO A 895 LYS A 905 1 11
HELIX 11 11 THR A 916 TRP A 927 1 12
HELIX 12 12 ASP A 930 ARG A 934 5 5
HELIX 13 13 LYS A 936 ARG A 949 1 14
HELIX 14 14 ASP A 950 TYR A 954 5 5
HELIX 15 15 GLY A 959 MET A 963 5 5
HELIX 16 16 ASP A 988 TYR A 992 5 5
SHEET 1 A 5 LYS A 692 SER A 696 0
SHEET 2 A 5 THR A 701 TRP A 707 -1 O VAL A 702 N LEU A 694
SHEET 3 A 5 ILE A 716 LYS A 721 -1 O VAL A 718 N GLY A 705
SHEET 4 A 5 GLN A 763 GLN A 767 -1 O THR A 766 N ALA A 719
SHEET 5 A 5 LEU A 753 CYS A 757 -1 N LEU A 754 O ILE A 765
SHEET 1 B 2 LEU A 809 VAL A 810 0
SHEET 2 B 2 LYS A 836 LEU A 837 -1 O LYS A 836 N VAL A 810
SHEET 1 C 2 VAL A 819 THR A 823 0
SHEET 2 C 2 HIS A 826 ILE A 829 -1 O LYS A 828 N LEU A 820
SHEET 1 D 2 TYR A 845 HIS A 846 0
SHEET 2 D 2 ILE A 866 TYR A 867 -1 O TYR A 867 N TYR A 845
LINK CZ TYR B 6 NS 112 B 101 1555 1555 1.45
SITE 1 AC1 1 ARG A 812
SITE 1 AC2 13 LEU A 694 ALA A 698 PHE A 699 ALA A 719
SITE 2 AC2 13 LYS A 721 THR A 766 GLN A 767 MET A 769
SITE 3 AC2 13 CYS A 773 ARG A 817 LEU A 820 ASP A 831
SITE 4 AC2 13 TYR B 6
CRYST1 144.182 144.182 144.182 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 0.006936 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006936 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
