BMRB Entry 7170

Title:
1H, 13C, and 15N Chemical Shift Assignments for Bacillus subtilis Hypothetical Protein yvyC: Northeast Structural Genomics Consortium target SR482
Deposition date:
2006-06-15
Original release date:
2015-04-23
Authors:
Eletsky, Alexandre; Liu, Gaohua; Atreya, Hanudatta; Sukumaran, Dinesh; Wang, Dongyan; Cunningham, Kellie; Janjua, Haleema; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexandre; Liu, Gaohua; Atreya, Hanudatta; Sukumaran, Dinesh; Wang, Dongyan; Cunningham, Kellie; Janjua, Haleema; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Bacillus subtilis Protein yvyC"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
sr482, polymer, 117 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: B. subtilis   Taxonomy ID: 1423   Superkingdom: Eubacteria   Kingdom: Not applicable   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pET21

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts125
1H chemical shifts854

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sr482 monomer1

Entities:

Entity 1, sr482 monomer 117 residues - Formula weight is not available

Contains C-terminal His-tag LEHHHHHH

1   LEUASNILEGLUARGLEUTHRTHRLEUGLN
2   PROVALTRPASPARGTYRASPTHRGLNILE
3   HISASNGLNLYSASPASNASPASNGLUVAL
4   PROVALHISGLNVALSERTYRTHRASNLEU
5   ALAGLUMETVALGLYGLUMETASNLYSLEU
6   LEUGLUPROSERGLNVALHISLEULYSPHE
7   GLULEUHISASPLYSLEUASNGLUTYRTYR
8   VALLYSVALILEGLUASPSERTHRASNGLU
9   VALILEARGGLUILEPROPROLYSARGTRP
10   LEUASPPHETYRALAALAMETTHRGLUPHE
11   LEUGLYLEUPHEVALASPGLULYSLYSLEU
12   GLUHISHISHISHISHISHIS

Samples:

NC: sr482, [U-100% 13C; U-100% 15N], 1.1 mM; Tris 10 mM; NaCl 100 mM; NaN3 0.02 % w/w

NC5: sr482, [U-5% 13C; U-100% 15N], 1.1 mM; Tris 10 mM; NaCl 100 mM; NaN3 0.02 % w/w

conditions_1: pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H15N_HSQCnot availablenot availableconditions_1
2D 1H13C_HSQC (ali)not availablenot availableconditions_1
2D 1H13C_HSQC (aro)not availablenot availableconditions_1
2D CT-1H13C_HSQC (ali)not availablenot availableconditions_1
2D CT-1H13C_HSQC (aro)not availablenot availableconditions_1
3D HNCOnot availablenot availableconditions_1
(4,3)D GFT CABCA(CO)NHNnot availablenot availableconditions_1
(4,3)D GFT HNNCABCAnot availablenot availableconditions_1
(4,3)D GFT HABCAB(CO)NHNnot availablenot availableconditions_1
(4,3)D GFT HCCH-COSY (ali)not availablenot availableconditions_1
(4,3)D GFT HCCH-COSY (aro)not availablenot availableconditions_1
3D 15N-, 13Cali-, 13Caro-resolved NOESYnot availablenot availableconditions_1
2D CT-1H13C_HSQC (methyl)not availablenot availableconditions_1

Software:

VNMR v6.1C, Varian, Inc. - NMR data acqusition

XEASY v1.3.13, xeasy - Spectral analysis

CARA v1.5.3, CARA - Spectral analysis

PROSA v6.0, PROSA - NMR data processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

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