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BMRB: 17209


17209
7KZI
Backbone 1H, 13C, and 15N chemical shift assignments for the nucleotide-binding domain of E.coli DnaK in the nucleotide-free state
Authors
Zhuravleva, A., Gierasch, L.M.
Assembly
NBD(1-388)
Entity
1. NBD(1-388) (polymer, Thiol state: all free), 388 monomers, 42009.22 Da Detail

MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGAF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIELL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKD


Formula weight
42009.22 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 95.6 %, Completeness: 42.0 %, Completeness (bb): 67.3 % Detail
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Polymer type: polypeptide(L)

Total1H13C15N
All42.0 % (1835 of 4374)27.7 % (627 of 2267)51.1 % (870 of 1701)83.3 % (338 of 406)
Backbone67.3 % (1545 of 2296)52.2 % (414 of 793)70.2 % (794 of 1131)90.6 % (337 of 372)
Sidechain15.4 % (374 of 2433)14.1 % (208 of 1474)17.8 % (165 of 925) 2.9 % (1 of 34)
Aromatic14.8 % (26 of 176)14.8 % (13 of 88)14.9 % (13 of 87) 0.0 % (0 of 1)
Methyl16.5 % (82 of 496)16.1 % (40 of 248)16.9 % (42 of 248)

1. the nucleotide-binding domain of DnaK

MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGAF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIELL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKD

Show sample condition
Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 299 (±0.2) K, pH 7.0 (±0.1)


#NameIsotope labelingTypeConcentration
1potassium phosphatenatural abundance10 mM
2magnesium chloridenatural abundance10 mM
3AEBSF protease inhibitornatural abundance1 uM
4DTTnatural abundance5 mM
5DSSnatural abundance0.5 mM
6potassium chloridenatural abundance10 mM
7the nucleotide-binding domain of DnaK[U-97% 2H; U-95% 13C; U-95% 15N]0.5 mM
8H2Onatural abundance95 %
9D2Onatural abundance5 %

Release date
2011-05-04
Citation 1
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 ,
Show more 3 citaions
Citation 2
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
Zhuravleva, A., Gierasch, L.M.
Proc. Natl. Acad. Sci. U. S. A. (2011), 108, 6987-6992, PubMed 21482798 , DOI 10.1073/pnas.1014448108 ,
Citation 3
Automated analysis of protein NMR assignments using methods from artificial intelligence
Zimmerman, D., Kulikowski, C., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., Montelione, G.
J. Mol. Biol. (1997), 269, 592-610, PubMed 9217263 , DOI 10.1006/jmbi.1997.1052 ,
Citation 4
Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment
Keller, R.
Related entities 1. NBD(1-388), : 1 : 18 : 283 entities Detail
More details for 302 related entities
Interaction partners 1. NBD(1-388), : 322 interactors Detail
More details for 322 interactors identified by 9 citations
Experiments performed 3 experiments Detail
Chemical shift validation 3 contents Detail
Keywords allostery, conformational ensemble, DnaK, Hsp70 molecular chaperone, interdomain linker, nucleotide-binding domain, subdomain motions