HEADER TRANSFERASE 19-MAR-09 3GOP
TITLE CRYSTAL STRUCTURE OF THE EGF RECEPTOR JUXTAMEMBRANE AND KINASE DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 669-1018;
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 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: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC
KEYWDS KINASE, JUXTAMEMBRANE, EGFR, ANTI-ONCOGENE, ATP-BINDING, CELL CYCLE,
KEYWDS 2 CELL MEMBRANE, DISEASE MUTATION, DISULFIDE BOND, GLYCOPROTEIN,
KEYWDS 3 ISOPEPTIDE BOND, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 4 RECEPTOR, SECRETED, TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN
KEYWDS 5 KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.CHOI,D.ALVARADO,K.MORAVCEVIC,M.A.LEMMON
REVDAT 6 06-SEP-23 3GOP 1 REMARK
REVDAT 5 20-OCT-21 3GOP 1 SEQADV
REVDAT 4 01-NOV-17 3GOP 1 REMARK
REVDAT 3 21-MAR-12 3GOP 1 JRNL
REVDAT 2 13-JUL-11 3GOP 1 VERSN
REVDAT 1 07-JUL-09 3GOP 0
JRNL AUTH M.RED BREWER,S.H.CHOI,D.ALVARADO,K.MORAVCEVIC,A.POZZI,
JRNL AUTH 2 M.A.LEMMON,G.CARPENTER
JRNL TITL THE JUXTAMEMBRANE REGION OF THE EGF RECEPTOR FUNCTIONS AS AN
JRNL TITL 2 ACTIVATION DOMAIN.
JRNL REF MOL.CELL V. 34 641 2009
JRNL REFN ISSN 1097-2765
JRNL PMID 19560417
JRNL DOI 10.1016/J.MOLCEL.2009.04.034
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 9024
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 902
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 565
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57000
REMARK 3 B22 (A**2) : 0.57000
REMARK 3 B33 (A**2) : -1.14000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.410
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.278
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.834
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2444 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3313 ; 1.522 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 297 ; 5.728 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;41.177 ;23.429
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 435 ;18.900 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;18.935 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 381 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1800 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1500 ; 0.726 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2427 ; 1.400 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 944 ; 2.023 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 884 ; 3.344 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 652 A 994
REMARK 3 RESIDUE RANGE : A 1 A 6
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9357 -22.1793 -36.5158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1478 T22: 0.0388
REMARK 3 T33: 0.0808 T12: -0.0259
REMARK 3 T13: -0.0057 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 0.2729 L22: 0.7453
REMARK 3 L33: 1.4145 L12: -0.0736
REMARK 3 L13: -0.0482 L23: 0.9577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0543 S12: 0.0918 S13: 0.0322
REMARK 3 S21: -0.0910 S22: 0.0019 S23: 0.0637
REMARK 3 S31: -0.2389 S32: 0.0465 S33: 0.0523
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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, U VALUES :RESIDUAL ONLY
REMARK 4
REMARK 4 3GOP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : HORIZONTAL BENT SI(111),
REMARK 200 ASYMMETRICALLY CUT WITH WATER
REMARK 200 COOLED CU BLOCK
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : 0.30600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 2GS7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 0.1M KCL, 0.1M TRIS
REMARK 280 PH8.5, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+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 88.57900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.03650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.03650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 132.86850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.03650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.03650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.28950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.03650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.03650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 132.86850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.03650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.03650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.28950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 88.57900
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: DIMERIC
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 0.000000 -1.000000 0.000000 -31.03650
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -31.03650
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -44.28950
REMARK 350
REMARK 350 BIOMOLECULE: 2
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 MET A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
REMARK 465 HIS A 642
REMARK 465 HIS A 643
REMARK 465 HIS A 644
REMARK 465 ARG A 645
REMARK 465 ARG A 646
REMARK 465 ARG A 647
REMARK 465 HIS A 648
REMARK 465 ILE A 649
REMARK 465 VAL A 650
REMARK 465 ARG A 651
REMARK 465 SER A 696
REMARK 465 GLY A 697
REMARK 465 ALA A 698
REMARK 465 PHE A 699
REMARK 465 LYS A 713
REMARK 465 ARG A 724
REMARK 465 GLU A 725
REMARK 465 ALA A 726
REMARK 465 THR A 727
REMARK 465 SER A 728
REMARK 465 PRO A 729
REMARK 465 LEU A 834
REMARK 465 ALA A 835
REMARK 465 LYS A 836
REMARK 465 LEU A 837
REMARK 465 LEU A 838
REMARK 465 GLY A 839
REMARK 465 ALA A 840
REMARK 465 GLU A 841
REMARK 465 GLU A 842
REMARK 465 LYS A 843
REMARK 465 GLU A 844
REMARK 465 TYR A 845
REMARK 465 HIS A 846
REMARK 465 ALA A 847
REMARK 465 GLU A 848
REMARK 465 GLY A 849
REMARK 465 GLY A 850
REMARK 465 LYS A 851
REMARK 465 ARG A 962
REMARK 465 MET A 963
REMARK 465 HIS A 964
REMARK 465 LEU A 965
REMARK 465 PRO A 966
REMARK 465 SER A 967
REMARK 465 PRO A 968
REMARK 465 THR A 969
REMARK 465 ASP A 979
REMARK 465 GLU A 980
REMARK 465 GLU A 981
REMARK 465 ASP A 982
REMARK 465 MET A 983
REMARK 465 ASP A 984
REMARK 465 PRO A 995
REMARK 465 GLN A 996
REMARK 465 GLN A 997
REMARK 465 GLY A 998
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 LYS A 652 CG CD CE NZ
REMARK 470 ARG A 657 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 715 CG CD CE NZ
REMARK 470 MET A 721 CG SD CE
REMARK 470 LYS A 730 CG CD CE NZ
REMARK 470 LYS A 733 CG CD CE NZ
REMARK 470 GLU A 734 CG CD OE1 OE2
REMARK 470 GLU A 738 CG CD OE1 OE2
REMARK 470 GLU A 898 CG CD OE1 OE2
REMARK 470 ASP A 985 CG OD1 OD2
REMARK 470 VAL A 986 CG1 CG2
REMARK 470 ILE A 994 CG1 CG2 CD1
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 812 -7.53 80.15
REMARK 500 ASP A 813 47.24 -151.25
REMARK 500 ARG A 865 18.25 53.37
REMARK 500 ARG A 865 15.17 56.31
REMARK 500 ALA A 976 -72.05 -53.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3GOP A 645 998 UNP P00533 EGFR_HUMAN 669 1022
SEQADV 3GOP MET A 638 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 639 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 640 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 641 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 642 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 643 UNP P00533 EXPRESSION TAG
SEQADV 3GOP HIS A 644 UNP P00533 EXPRESSION TAG
SEQADV 3GOP MET A 721 UNP P00533 LYS 745 ENGINEERED MUTATION
SEQRES 1 A 361 MET HIS HIS HIS HIS HIS HIS ARG ARG ARG HIS ILE VAL
SEQRES 2 A 361 ARG LYS ARG THR LEU ARG ARG LEU LEU GLN GLU ARG GLU
SEQRES 3 A 361 LEU VAL GLU PRO LEU THR PRO SER GLY GLU ALA PRO ASN
SEQRES 4 A 361 GLN ALA LEU LEU ARG ILE LEU LYS GLU THR GLU PHE LYS
SEQRES 5 A 361 LYS ILE LYS VAL LEU GLY SER GLY ALA PHE GLY THR VAL
SEQRES 6 A 361 TYR LYS GLY LEU TRP ILE PRO GLU GLY GLU LYS VAL LYS
SEQRES 7 A 361 ILE PRO VAL ALA ILE MET GLU LEU ARG GLU ALA THR SER
SEQRES 8 A 361 PRO LYS ALA ASN LYS GLU ILE LEU ASP GLU ALA TYR VAL
SEQRES 9 A 361 MET ALA SER VAL ASP ASN PRO HIS VAL CYS ARG LEU LEU
SEQRES 10 A 361 GLY ILE CYS LEU THR SER THR VAL GLN LEU ILE THR GLN
SEQRES 11 A 361 LEU MET PRO PHE GLY CYS LEU LEU ASP TYR VAL ARG GLU
SEQRES 12 A 361 HIS LYS ASP ASN ILE GLY SER GLN TYR LEU LEU ASN TRP
SEQRES 13 A 361 CYS VAL GLN ILE ALA LYS GLY MET ASN TYR LEU GLU ASP
SEQRES 14 A 361 ARG ARG LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL
SEQRES 15 A 361 LEU VAL LYS THR PRO GLN HIS VAL LYS ILE THR ASP PHE
SEQRES 16 A 361 GLY LEU ALA LYS LEU LEU GLY ALA GLU GLU LYS GLU TYR
SEQRES 17 A 361 HIS ALA GLU GLY GLY LYS VAL PRO ILE LYS TRP MET ALA
SEQRES 18 A 361 LEU GLU SER ILE LEU HIS ARG ILE TYR THR HIS GLN SER
SEQRES 19 A 361 ASP VAL TRP SER TYR GLY VAL THR VAL TRP GLU LEU MET
SEQRES 20 A 361 THR PHE GLY SER LYS PRO TYR ASP GLY ILE PRO ALA SER
SEQRES 21 A 361 GLU ILE SER SER ILE LEU GLU LYS GLY GLU ARG LEU PRO
SEQRES 22 A 361 GLN PRO PRO ILE CYS THR ILE ASP VAL TYR MET ILE MET
SEQRES 23 A 361 VAL LYS CYS TRP MET ILE ASP ALA ASP SER ARG PRO LYS
SEQRES 24 A 361 PHE ARG GLU LEU ILE ILE GLU PHE SER LYS MET ALA ARG
SEQRES 25 A 361 ASP PRO GLN ARG TYR LEU VAL ILE GLN GLY ASP GLU ARG
SEQRES 26 A 361 MET HIS LEU PRO SER PRO THR ASP SER ASN PHE TYR ARG
SEQRES 27 A 361 ALA LEU MET ASP GLU GLU ASP MET ASP ASP VAL VAL ASP
SEQRES 28 A 361 ALA ASP GLU TYR LEU ILE PRO GLN GLN GLY
FORMUL 2 HOH *5(H2 O)
HELIX 1 1 THR A 654 GLU A 661 1 8
HELIX 2 2 ARG A 662 LEU A 664 5 3
HELIX 3 3 LYS A 684 THR A 686 5 3
HELIX 4 4 ALA A 731 VAL A 745 1 15
HELIX 5 5 CYS A 773 HIS A 781 1 9
HELIX 6 6 LYS A 782 ILE A 785 5 4
HELIX 7 7 GLY A 786 ARG A 807 1 22
HELIX 8 8 ALA A 815 ARG A 817 5 3
HELIX 9 9 PRO A 853 MET A 857 5 5
HELIX 10 10 ALA A 858 ARG A 865 1 8
HELIX 11 11 THR A 868 THR A 885 1 18
HELIX 12 12 PRO A 895 LYS A 905 1 11
HELIX 13 13 THR A 916 CYS A 926 1 11
HELIX 14 14 ASP A 930 ARG A 934 5 5
HELIX 15 15 LYS A 936 ASP A 950 1 15
HELIX 16 16 ASP A 950 LEU A 955 1 6
HELIX 17 17 SER A 971 LEU A 977 1 7
HELIX 18 18 ASP A 988 LEU A 993 1 6
SHEET 1 A 5 PHE A 688 VAL A 693 0
SHEET 2 A 5 THR A 701 TRP A 707 -1 O LYS A 704 N ILE A 691
SHEET 3 A 5 ILE A 716 GLU A 722 -1 O ILE A 716 N TRP A 707
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 VAL A 819 THR A 823 0
SHEET 2 B 2 HIS A 826 ILE A 829 -1 O LYS A 828 N LEU A 820
CRYST1 62.073 62.073 177.158 90.00 90.00 90.00 P 43 21 2 8
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 0.016110 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016110 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005645 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
