HEADER TRANSFERASE 24-DEC-09 2KS1
TITLE HETERODIMERIC ASSOCIATION OF TRANSMEMBRANE DOMAINS OF ERBB1 AND ERBB2
TITLE 2 RECEPTORS ENABLING KINASE ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ERBB2TM DOMAIN, UNP RESIDUES 641-684;
COMPND 5 SYNONYM: P185ERBB2, C-ERBB-2, NEU PROTO-ONCOGENE, TYROSINE KINASE-
COMPND 6 TYPE CELL SURFACE RECEPTOR HER2, MLN 19;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: ERBB1TM DOMAIN, UNP RESIDUES 634-677;
COMPND 13 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;
COMPND 14 EC: 2.7.10.1;
COMPND 15 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: ERBB2, HER2, NEU, NGL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: EGFR, ERBB1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ERBB1, ERBB2, TRANSMEMBRANE, HETERODIMER, COMPLEX, TYROSINE KINASE
KEYWDS 2 RECEPTOR, BICELLES, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR K.S.MINEEV,E.V.BOCHAROV,Y.E.PUSTOVALOVA,O.V.BOCHAROVA,V.V.CHUPIN,
AUTHOR 2 A.S.ARSENIEV
REVDAT 1 09-JUN-10 2KS1 0
JRNL AUTH K.S.MINEEV,E.V.BOCHAROV,Y.E.PUSTOVALOVA,O.V.BOCHAROVA,
JRNL AUTH 2 V.V.CHUPIN,A.S.ARSENIEV
JRNL TITL SPATIAL STRUCTURE OF THE TRANSMEMBRANE DOMAIN HETERODIMER
JRNL TITL 2 OF ERBB1 AND ERBB2 RECEPTOR TYROSINE KINASES
JRNL REF J.MOL.BIOL. 2010
JRNL REFN ESSN 1089-8638
JRNL PMID 20471394
JRNL DOI 10.1016/J.JMB.2010.05.016
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KS1 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB101502.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 15N] ERBB1TM-1, 1
REMARK 210 MM [U-100% 15N] ERBB2TM-2, 12 MM
REMARK 210 DMPC-3, 48 MM DHPC-4, 95% H2O/5%
REMARK 210 D2O; 1 MM [U-100% 13C; U-100%
REMARK 210 15N] ERBB1TM-5, 1 MM ERBB2TM-6,
REMARK 210 12 MM [U-2H] DMPC-7, 48 MM [U-2H]
REMARK 210 DHPC-8, 100% D2O; 1 MM ERBB1TM-9,
REMARK 210 1 MM [U-100% 13C; U-100% 15N]
REMARK 210 ERBB2TM-10, 12 MM [U-2H] DMPC-11,
REMARK 210 48 MM [U-2H] DHPC-12, 95% H2O/5%
REMARK 210 D2O; 1 MM [U-100% 13C; U-100%
REMARK 210 15N] ERBB1TM-13, 1 MM ERBB2TM-14,
REMARK 210 12 MM [U-2H] DMPC-15, 48 MM [U-
REMARK 210 2H] DHPC-16, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCA; 3D HN(CO)CA; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-15N TOCSY; 3D HCCH-
REMARK 210 TOCSY; 3D 1H-13C NOESY; 3D-
REMARK 210 13CFILT NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN 2.1, CARA 1.8.4, CYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 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 1 ALA A 44 170.17 -55.38
REMARK 500 1 ARG A 47 38.90 -174.03
REMARK 500 1 SER A 49 72.58 62.33
REMARK 500 1 CYS B 136 72.02 55.65
REMARK 500 1 ASN B 139 -177.91 61.80
REMARK 500 1 PRO B 141 82.04 -69.72
REMARK 500 1 SER B 145 -75.89 -177.33
REMARK 500 2 ALA A 44 -169.74 -68.89
REMARK 500 2 GLU A 45 139.35 -174.11
REMARK 500 2 ARG A 47 82.91 -164.91
REMARK 500 2 SER A 49 70.55 -155.01
REMARK 500 2 GLN A 79 -74.92 -67.88
REMARK 500 2 GLN A 80 -74.84 -160.42
REMARK 500 2 LYS A 81 65.49 -165.02
REMARK 500 2 ILE A 82 68.25 64.57
REMARK 500 2 LYS B 142 38.52 -148.77
REMARK 500 2 ILE B 143 135.40 65.02
REMARK 500 2 SER B 145 -33.27 177.46
REMARK 500 2 ARG B 171 25.74 -144.86
REMARK 500 2 ILE B 173 98.29 63.15
REMARK 500 2 LYS B 176 -64.63 -169.60
REMARK 500 3 CYS A 42 160.53 63.09
REMARK 500 3 PRO A 43 82.57 -69.76
REMARK 500 3 ALA A 44 50.65 -174.93
REMARK 500 3 GLU A 45 -44.43 -156.57
REMARK 500 3 GLN A 46 102.40 61.97
REMARK 500 3 ARG A 47 -169.86 -64.98
REMARK 500 3 SER A 49 142.57 66.85
REMARK 500 3 GLN A 80 95.59 -65.96
REMARK 500 3 ILE A 82 -48.21 -136.90
REMARK 500 3 ARG A 83 -174.48 58.40
REMARK 500 3 PRO B 137 -173.03 -69.75
REMARK 500 3 PRO B 141 -170.76 -69.74
REMARK 500 3 LYS B 142 108.31 64.06
REMARK 500 3 ILE B 143 87.93 49.07
REMARK 500 3 SER B 145 -77.18 179.28
REMARK 500 3 HIS B 172 71.95 -154.85
REMARK 500 3 LYS B 176 125.49 -170.34
REMARK 500 4 CYS A 42 153.65 64.37
REMARK 500 4 PRO A 43 86.58 -69.72
REMARK 500 4 ALA A 44 -36.24 -175.09
REMARK 500 4 GLU A 45 158.11 63.96
REMARK 500 4 GLN A 46 164.96 62.11
REMARK 500 4 ARG A 47 -76.04 -165.04
REMARK 500 4 ALA A 48 -169.06 -175.27
REMARK 500 4 SER A 49 68.30 63.95
REMARK 500 4 GLN A 80 70.41 -155.77
REMARK 500 4 ILE A 82 -66.45 -93.02
REMARK 500 4 ARG A 83 -177.32 57.39
REMARK 500 4 PRO B 137 -174.70 -69.71
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JWA RELATED DB: PDB
REMARK 900 RELATED ID: 16658 RELATED DB: BMRB
DBREF 2KS1 A 41 84 UNP P04626 ERBB2_HUMAN 641 684
DBREF 2KS1 B 134 177 UNP P00533 EGFR_HUMAN 634 677
SEQRES 1 A 44 GLY CYS PRO ALA GLU GLN ARG ALA SER PRO LEU THR SER
SEQRES 2 A 44 ILE ILE SER ALA VAL VAL GLY ILE LEU LEU VAL VAL VAL
SEQRES 3 A 44 LEU GLY VAL VAL PHE GLY ILE LEU ILE LYS ARG ARG GLN
SEQRES 4 A 44 GLN LYS ILE ARG LYS
SEQRES 1 B 44 GLU GLY CYS PRO THR ASN GLY PRO LYS ILE PRO SER ILE
SEQRES 2 B 44 ALA THR GLY MET VAL GLY ALA LEU LEU LEU LEU LEU VAL
SEQRES 3 B 44 VAL ALA LEU GLY ILE GLY LEU PHE MET ARG ARG ARG HIS
SEQRES 4 B 44 ILE VAL ARG LYS ARG
HELIX 1 1 PRO A 50 GLN A 80 1 31
HELIX 2 2 ALA B 147 ARG B 170 1 24
CISPEP 1 ILE B 143 PRO B 144 1 -0.07
CISPEP 2 ILE B 143 PRO B 144 2 -0.08
CISPEP 3 ILE B 143 PRO B 144 3 -0.13
CISPEP 4 ILE B 143 PRO B 144 4 -0.17
CISPEP 5 ILE B 143 PRO B 144 5 -0.12
CISPEP 6 ILE B 143 PRO B 144 6 -0.07
CISPEP 7 ILE B 143 PRO B 144 7 -0.14
CISPEP 8 ILE B 143 PRO B 144 8 -0.15
CISPEP 9 ILE B 143 PRO B 144 9 -0.15
CISPEP 10 ILE B 143 PRO B 144 10 -0.18
CISPEP 11 ILE B 143 PRO B 144 11 -0.13
CISPEP 12 ILE B 143 PRO B 144 12 -0.13
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END