BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27037

Title: Alanine chemical shifts of the N-terminal domain (residues 1-215) of HtpG, the Hsp90 from Escherichia coli. Northeast Structural Genomics Consortium Target ER697A.   PubMed: 28653216

Authors: Ramelot, Theresa; Pederson, Kari; Wang, Huang; Maglaqui, Melissa; Mao, Lei; Xiao, Rong; Acton, Thomas; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael

Citation: Pederson, Kari; Chalmers, Gordon; Gao, Qi; Elnatan, Daniel; Ramelot, Theresa; Ma, Li-Chung; Montelione, Gaetano; Kennedy, Michael; Agard, David; Prestegard, James. "NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine"  J. Biomol. NMR 68, 225-236 (2017).

Assembly members:
NTD, polymer, 214 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NTD: KGQETRGFQSEVKQLLHLMI HSLYSNKEIFLRELISNASD AADKLRFRALSNPDLYEGDG ELRVRVSFDKDKRTLTISDN GVGMTRDEVIDHLGTIAKSG TKSFLESLGSDQAKDSQLIG QFGVGFYSAFIVADKVTVRT RAAGEKPENGVFWESAGEGE YTVADITKEDRGTEITLHLR EGEDEFLDDWRVRSIISKYS DHIALPVEIEKREE

Data sets:
Data typeCount
13C chemical shifts39
15N chemical shifts13
1H chemical shifts65

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NTD1

Entities:

Entity 1, NTD 214 residues - Formula weight is not available

10 N-terminal residues not included: MGHHHHHHSH

1   LYSGLYGLNGLUTHRARGGLYPHEGLNSER
2   GLUVALLYSGLNLEULEUHISLEUMETILE
3   HISSERLEUTYRSERASNLYSGLUILEPHE
4   LEUARGGLULEUILESERASNALASERASP
5   ALAALAASPLYSLEUARGPHEARGALALEU
6   SERASNPROASPLEUTYRGLUGLYASPGLY
7   GLULEUARGVALARGVALSERPHEASPLYS
8   ASPLYSARGTHRLEUTHRILESERASPASN
9   GLYVALGLYMETTHRARGASPGLUVALILE
10   ASPHISLEUGLYTHRILEALALYSSERGLY
11   THRLYSSERPHELEUGLUSERLEUGLYSER
12   ASPGLNALALYSASPSERGLNLEUILEGLY
13   GLNPHEGLYVALGLYPHETYRSERALAPHE
14   ILEVALALAASPLYSVALTHRVALARGTHR
15   ARGALAALAGLYGLULYSPROGLUASNGLY
16   VALPHETRPGLUSERALAGLYGLUGLYGLU
17   TYRTHRVALALAASPILETHRLYSGLUASP
18   ARGGLYTHRGLUILETHRLEUHISLEUARG
19   GLUGLYGLUASPGLUPHELEUASPASPTRP
20   ARGVALARGSERILEILESERLYSTYRSER
21   ASPHISILEALALEUPROVALGLUILEGLU
22   LYSARGGLUGLU

Samples:

sample_1: NTD, [U-100% 13C; U-100% 15N], 0.49 mM; TRIS 10 mM; sodium chloride 100 mM; sodium azide 0.02%; DTT 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D 1H-13C HSQC CT aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - peak picking

VNMR, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

Related Database Links: