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Assignment of 1H and 15N chemical shifts for the Ig1 module of FGFR1
Authors
Vladislav, K.V., Vladimir, B., Elisabeth, B., Flemming, P.M.
Assembly
Ig1 module
Entity
1. Ig1 module (polymer, Thiol state: all disulfide bound), 107 monomers, 11677.76 Da Detail

EARPAPTLPE QAQPWGVPVE VESLLVHPGD LLQLRCRLRD DVQSINWLRD GVQLVESNRT RITGEEVEVR DSIPADSGLY ACVTSSPSGS DTTYFSVNVS DALPSSE


Formula weight
11677.76 Da
Entity Connection
disulfide 1 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:CYS36:SG1:CYS82:SG

Source organism
Rattus norvegicus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 99.1 %, Completeness: 83.9 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

Total1H15N
All83.9 % (601 of 716)81.6 % (496 of 608)97.2 % (105 of 108)
Backbone97.1 % (300 of 309)96.7 % (204 of 211)98.0 % (96 of 98)
Sidechain74.0 % (301 of 407)73.6 % (292 of 397)90.0 % (9 of 10)
Aromatic75.9 % (22 of 29)74.1 % (20 of 27)100.0 % (2 of 2)
Methyl79.7 % (51 of 64)79.7 % (51 of 64)

1. Ig1 module of FGFR1

EARPAPTLPE QAQPWGVPVE VESLLVHPGD LLQLRCRLRD DVQSINWLRD GVQLVESNRT RITGEEVEVR DSIPADSGLY ACVTSSPSGS DTTYFSVNVS DALPSSE

Sample

Temperature 298 (±0.1) K, pH 7.4 (±0.01)


#NameIsotope labelingTypeConcentration
1Ig1 module of FGFR12 mM
2H2O
3D2O
4sodium phosphate10 mM
5NaCl150 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2CKN, Strand ID: A Detail


Release date
2006-11-05
Citation
1H and 15N resonance assignment of the first module of FGFR1
Kiselyov, V.V., Berezin, V., Bock, E., Poulsen, F.M.
J. Biomol. NMR (2006), 36 Suppl 1, 28-28, PubMed 16609835 , DOI 10.1007/s10858-006-0012-z ,
Related entities 1. Ig1 module, : 1 : 2 : 106 entities Detail
Interaction partners 1. Ig1 module, : 6 interactors Detail
Experiments performed 4 experiments Detail
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