BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 26974

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26974

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hsp31   PubMed: 28258548

Deposition date: 2016-12-16 Original release date: 2017-03-31

Authors: Kim, Jihong; Choi, Dongwook; Park, Chankyu; Ryu, Kyoung-Seok

Citation: Kim, Jihong; Choi, Dongwook; Park, Chankyu; Ryu, Kyoung-Seok. "Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31"  Biomol. NMR Assign. 11, 159-163 (2017).

Assembly members:
Hsp31, polymer, 283 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   Vector: pET21b

Entity Sequences (FASTA):
Hsp31: MTVQTSKNPQVDIAEDNAFF PSEYSLSQYTSPVSDLDGVD YPKPYRGKHKILVIAADERY LPTDNGKLFSTGNHPIETLL PLYHLHAAGFEFEVATISGL MTKFEYWAMPHKDEKVMPFF EQHKSLFRNPKKLADVVASL NADSEYAAIFVPGGHGALIG LPESQDVAAALQWAIKNDRF VISLCHGPAAFLALRHGDNP LNGYSICAFPDAADKQTPEI GYMPGHLTWYFGEELKKMGM NIINDDITGRVHKDRKLLTG DSPFAANALGKLAAQEMLAA YAG

Data sets:
Data typeCount
13C chemical shifts763
15N chemical shifts240
1H chemical shifts240

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hsp31, subunit 11
2Hsp31, subunit 21

Entities:

Entity 1, Hsp31, subunit 1 283 residues - Formula weight is not available

1   METTHRVALGLNTHRSERLYSASNPROGLN
2   VALASPILEALAGLUASPASNALAPHEPHE
3   PROSERGLUTYRSERLEUSERGLNTYRTHR
4   SERPROVALSERASPLEUASPGLYVALASP
5   TYRPROLYSPROTYRARGGLYLYSHISLYS
6   ILELEUVALILEALAALAASPGLUARGTYR
7   LEUPROTHRASPASNGLYLYSLEUPHESER
8   THRGLYASNHISPROILEGLUTHRLEULEU
9   PROLEUTYRHISLEUHISALAALAGLYPHE
10   GLUPHEGLUVALALATHRILESERGLYLEU
11   METTHRLYSPHEGLUTYRTRPALAMETPRO
12   HISLYSASPGLULYSVALMETPROPHEPHE
13   GLUGLNHISLYSSERLEUPHEARGASNPRO
14   LYSLYSLEUALAASPVALVALALASERLEU
15   ASNALAASPSERGLUTYRALAALAILEPHE
16   VALPROGLYGLYHISGLYALALEUILEGLY
17   LEUPROGLUSERGLNASPVALALAALAALA
18   LEUGLNTRPALAILELYSASNASPARGPHE
19   VALILESERLEUCYSHISGLYPROALAALA
20   PHELEUALALEUARGHISGLYASPASNPRO
21   LEUASNGLYTYRSERILECYSALAPHEPRO
22   ASPALAALAASPLYSGLNTHRPROGLUILE
23   GLYTYRMETPROGLYHISLEUTHRTRPTYR
24   PHEGLYGLUGLULEULYSLYSMETGLYMET
25   ASNILEILEASNASPASPILETHRGLYARG
26   VALHISLYSASPARGLYSLEULEUTHRGLY
27   ASPSERPROPHEALAALAASNALALEUGLY
28   LYSLEUALAALAGLNGLUMETLEUALAALA
29   TYRALAGLY

Samples:

sample_1: Hsp31, [U-13C; U-15N; U-2H], 0.8 mM; HEPES 50 mM; sodium chloride 50 mM; DTT 10 mM; D2O, [U-2H], 5%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 313.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

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