BMRB Entry 27038

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27038

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Title:
Alanine chemical shifts of the C-terminal dimerization domain (residues 511-624) of HtpG, the Hsp90 from Escherichia coli. Northeast Structural Genomics Consortium Target ER697C.
Deposition date:
2017-02-24
Original release date:
2017-06-30
Authors:
Ramelot, Theresa; Pederson, Kari; Wang, Huang; Maglaqui, Melissa; Mao, Lei; Xiao, Rong; Acton, Thomas; Everett, John; Prestegard, James; Montelione, Gaetano; Kennedy, Michael
Citation:

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).
PubMed: 28653216

Assembly members:

Assembly members:
CTD, polymer, 115 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CTD: MFIDRVKALLGERVKDVRLT HRLTDTPAIVSTDADEMSTQ MAKLFAAAGQKVPEVKYIFE LNPDHVLVKRAADTEDEAKF SEWVELLLDQALLAERGTLE DPNLFIRRMNQLLVS

Data sets:
Data typeCount
13C chemical shifts36
15N chemical shifts12
1H chemical shifts60

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTD1

Entities:

Entity 1, CTD 115 residues - Formula weight is not available

10 N-terminal residues not included: MGHHHHHHSH

1   METPHEILEASPARGVALLYSALALEULEU
2   GLYGLUARGVALLYSASPVALARGLEUTHR
3   HISARGLEUTHRASPTHRPROALAILEVAL
4   SERTHRASPALAASPGLUMETSERTHRGLN
5   METALALYSLEUPHEALAALAALAGLYGLN
6   LYSVALPROGLUVALLYSTYRILEPHEGLU
7   LEUASNPROASPHISVALLEUVALLYSARG
8   ALAALAASPTHRGLUASPGLUALALYSPHE
9   SERGLUTRPVALGLULEULEULEUASPGLN
10   ALALEULEUALAGLUARGGLYTHRLEUGLU
11   ASPPROASNLEUPHEILEARGARGMETASN
12   GLNLEULEUVALSER

Samples:

sample_1: CTD, [U-100% 13C; U-100% 15N], 0.56 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 HSQC CT aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC large SWsample_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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks