HEADER TRANSFERASE 31-JUL-15 5CZI
TITLE EGFR L858R MUTANT IN COMPLEX WITH A SHC PEPTIDE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EGFR UNP RESIDUES 694-1022;
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;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: SHC PEPTIDE SUBSTRATE;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: SHC PEPTIDE UNP RESIDUES 345-353;
COMPND 14 SYNONYM: SHC-TRANSFORMING PROTEIN 3, SHC-TRANSFORMING PROTEIN A, SRC
COMPND 15 HOMOLOGY 2 DOMAIN-CONTAINING-TRANSFORMING PROTEIN C1, SH2 DOMAIN
COMPND 16 PROTEIN C1;
COMPND 17 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;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI H489;
SOURCE 11 ORGANISM_TAXID: 656404;
SOURCE 12 OTHER_DETAILS: THE OPTIMIZED PEPTIDE WAS GENERATED BY LIBRARY
SOURCE 13 SCREENING.
KEYWDS EGFR, L858R, KINASE, EGF, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.YUN,M.J.ECK
REVDAT 5 15-NOV-23 5CZI 1 REMARK
REVDAT 4 27-SEP-23 5CZI 1 REMARK
REVDAT 3 23-DEC-15 5CZI 1 JRNL
REVDAT 2 25-NOV-15 5CZI 1 JRNL
REVDAT 1 30-SEP-15 5CZI 0
JRNL AUTH M.J.BEGLEY,C.H.YUN,C.A.GEWINNER,J.M.ASARA,J.L.JOHNSON,
JRNL AUTH 2 A.J.COYLE,M.J.ECK,I.APOSTOLOU,L.C.CANTLEY
JRNL TITL EGF-RECEPTOR SPECIFICITY FOR PHOSPHOTYROSINE-PRIMED
JRNL TITL 2 SUBSTRATES PROVIDES SIGNAL INTEGRATION WITH SRC.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 983 2015
JRNL REFN ESSN 1545-9985
JRNL PMID 26551075
JRNL DOI 10.1038/NSMB.3117
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 15207
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 758
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 38.4615 - 4.4506 0.97 2903 144 0.1721 0.1969
REMARK 3 2 4.4506 - 3.5334 0.99 2925 149 0.1590 0.1974
REMARK 3 3 3.5334 - 3.0869 1.00 2869 142 0.1991 0.2635
REMARK 3 4 3.0869 - 2.8048 1.00 2883 160 0.2256 0.2812
REMARK 3 5 2.8048 - 2.6038 1.00 2869 163 0.2470 0.3089
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.30
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 : 0.010 2570
REMARK 3 ANGLE : 1.180 3481
REMARK 3 CHIRALITY : 0.083 388
REMARK 3 PLANARITY : 0.006 441
REMARK 3 DIHEDRAL : 17.034 960
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 5CZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925
REMARK 200 MONOCHROMATOR : SI(220)
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 : 15212
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.44700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2ITV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES 7.6, 0.15M NACL, 40%
REMARK 280 PEG400, 5MM TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K, PH 7.6
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 71.94500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 71.94500
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 71.94500
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 71.94500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 71.94500
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 71.94500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 71.94500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 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 692
REMARK 465 SER A 693
REMARK 465 PRO A 694
REMARK 465 SER A 695
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 GLU A 1005
REMARK 465 PRO A 1019
REMARK 465 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
REMARK 465 PRO B 101
REMARK 465 PHE B 109
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 GLU A 697 CD OE1 OE2
REMARK 470 ARG A 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 865 CG CD OE1 OE2
REMARK 470 LYS A 867 CG CD CE NZ
REMARK 470 ARG A 986 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 988 CG ND1 CD2 CE1 NE2
REMARK 470 MET A1007 CG SD CE
REMARK 470 ILE A1018 CG1 CG2 CD1
REMARK 470 ASP B 102 CG OD1 OD2
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 ARG A 836 -4.20 77.54
REMARK 500 ASP A 837 35.22 -143.63
REMARK 500 ASP A 855 74.37 60.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1221 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1222 DISTANCE = 6.39 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CZH RELATED DB: PDB
REMARK 900 EGFR L858R MUTANT IN COMPLEX WITH AN OPTIMAL PEPTIDE SUBSTRATE
DBREF 5CZI A 694 1022 UNP P00533 EGFR_HUMAN 694 1022
DBREF 5CZI B 101 109 PDB 5CZI 5CZI 101 109
SEQADV 5CZI GLY A 692 UNP P00533 EXPRESSION TAG
SEQADV 5CZI SER A 693 UNP P00533 EXPRESSION TAG
SEQADV 5CZI ARG A 858 UNP P00533 LEU 858 ENGINEERED MUTATION
SEQRES 1 A 331 GLY SER PRO SER GLY GLU ALA PRO ASN GLN ALA LEU LEU
SEQRES 2 A 331 ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL
SEQRES 3 A 331 LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU
SEQRES 4 A 331 TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA
SEQRES 5 A 331 ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN
SEQRES 6 A 331 LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL
SEQRES 7 A 331 ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU
SEQRES 8 A 331 THR SER THR VAL GLN LEU ILE THR GLN LEU MET PRO PHE
SEQRES 9 A 331 GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN
SEQRES 10 A 331 ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE
SEQRES 11 A 331 ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL
SEQRES 12 A 331 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR
SEQRES 13 A 331 PRO GLN HIS VAL LYS ILE THR ASP PHE GLY ARG ALA LYS
SEQRES 14 A 331 LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY
SEQRES 15 A 331 GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE
SEQRES 16 A 331 LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER
SEQRES 17 A 331 TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER
SEQRES 18 A 331 LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER
SEQRES 19 A 331 ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE
SEQRES 20 A 331 CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP
SEQRES 21 A 331 MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU
SEQRES 22 A 331 ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG
SEQRES 23 A 331 TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO
SEQRES 24 A 331 SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP
SEQRES 25 A 331 GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR
SEQRES 26 A 331 LEU ILE PRO GLN GLN GLY
SEQRES 1 B 9 PRO ASP HIS GLN TYR PTR ASN ASP PHE
MODRES 5CZI PTR B 106 TYR O-PHOSPHOTYROSINE
HET PTR B 106 16
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 3 HOH *129(H2 O)
HELIX 1 AA1 LYS A 708 THR A 710 5 3
HELIX 2 AA2 SER A 752 VAL A 769 1 18
HELIX 3 AA3 CYS A 797 HIS A 805 1 9
HELIX 4 AA4 LYS A 806 ILE A 809 5 4
HELIX 5 AA5 GLY A 810 ARG A 831 1 22
HELIX 6 AA6 ALA A 839 ARG A 841 5 3
HELIX 7 AA7 PRO A 877 MET A 881 5 5
HELIX 8 AA8 ALA A 882 ARG A 889 1 8
HELIX 9 AA9 THR A 892 THR A 909 1 18
HELIX 10 AB1 PRO A 919 SER A 921 5 3
HELIX 11 AB2 GLU A 922 GLY A 930 1 9
HELIX 12 AB3 THR A 940 TRP A 951 1 12
HELIX 13 AB4 ASP A 954 ARG A 958 5 5
HELIX 14 AB5 LYS A 960 ARG A 973 1 14
HELIX 15 AB6 ASP A 974 TYR A 978 5 5
HELIX 16 AB7 GLY A 983 MET A 987 5 5
HELIX 17 AB8 ASP A 1012 TYR A 1016 5 5
SHEET 1 AA1 5 PHE A 712 SER A 720 0
SHEET 2 AA1 5 GLY A 724 TRP A 731 -1 O LYS A 728 N ILE A 715
SHEET 3 AA1 5 ILE A 740 LEU A 747 -1 O ILE A 744 N TYR A 727
SHEET 4 AA1 5 VAL A 786 GLN A 791 -1 O THR A 790 N ALA A 743
SHEET 5 AA1 5 LEU A 777 LEU A 782 -1 N GLY A 779 O ILE A 789
SHEET 1 AA2 2 LEU A 833 VAL A 834 0
SHEET 2 AA2 2 LYS A 860 LEU A 861 -1 O LYS A 860 N VAL A 834
SHEET 1 AA3 2 VAL A 843 THR A 847 0
SHEET 2 AA3 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SHEET 1 AA4 2 TYR A 869 HIS A 870 0
SHEET 2 AA4 2 ILE A 890 TYR A 891 -1 O TYR A 891 N TYR A 869
SHEET 1 AA5 2 GLY A 874 VAL A 876 0
SHEET 2 AA5 2 PTR B 106 ASP B 108 -1 O PTR B 106 N VAL A 876
LINK C TYR B 105 N PTR B 106 1555 1555 1.33
LINK C PTR B 106 N ASN B 107 1555 1555 1.32
CRYST1 143.890 143.890 143.890 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 0.006950 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006950 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006950 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
