BMRB Entry 27681

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27681

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Title:
Chemical shift assignments for HSPB1 containing residues 1-176
Deposition date:
2018-11-05
Original release date:
2019-10-10
Authors:
Clouser, Amanda; Klevit, Rachel
Citation:

Citation: Clouser, Amanda; Baughman, Hannah Er; Basanta, Benjamin; Guttman, Miklos; Nath, Abhinav; Klevit, Rachel. "Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states"  Elife 8, e50259-e50259 (2019).
PubMed: 31573509

Assembly members:

Assembly members:
HSPB1, polymer, 176 residues, 19853 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET151d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSPB1: MTERRVPFSLLRGPDWDPFR DWYPHSRLFDQAFGLPRLPE EWSQWLGGSSWPGYVRPLPP AAIESPAVAAPAYSRALDRQ LDSGVSEIRHTADRWRVSLD VNHFAPDELTVKTKDGVVEI TGKHEERQDEHGYISRCFTR KYTLPPGVDPTQVSSSLSPE GTLTVEAPMPKLATQS

Data typeCount
13C chemical shifts294
15N chemical shifts100
1H chemical shifts100

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HSPB1, Subunit 11
2HSPB1, Subunit 21

Entities:

Entity 1, HSPB1, Subunit 1 176 residues - 19853 Da.

Phosphomimetic form of HSPB1 (Ser15Asp, Ser78Asp, Ser82Asp) truncated after residue 176

1   METTHRGLUARGARGVALPROPHESERLEU
2   LEUARGGLYPROASPTRPASPPROPHEARG
3   ASPTRPTYRPROHISSERARGLEUPHEASP
4   GLNALAPHEGLYLEUPROARGLEUPROGLU
5   GLUTRPSERGLNTRPLEUGLYGLYSERSER
6   TRPPROGLYTYRVALARGPROLEUPROPRO
7   ALAALAILEGLUSERPROALAVALALAALA
8   PROALATYRSERARGALALEUASPARGGLN
9   LEUASPSERGLYVALSERGLUILEARGHIS
10   THRALAASPARGTRPARGVALSERLEUASP
11   VALASNHISPHEALAPROASPGLULEUTHR
12   VALLYSTHRLYSASPGLYVALVALGLUILE
13   THRGLYLYSHISGLUGLUARGGLNASPGLU
14   HISGLYTYRILESERARGCYSPHETHRARG
15   LYSTYRTHRLEUPROPROGLYVALASPPRO
16   THRGLNVALSERSERSERLEUSERPROGLU
17   GLYTHRLEUTHRVALGLUALAPROMETPRO
18   LYSLEUALATHRGLNSER

Samples:

sample_1: HSPB1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 0.5 mM

sample_2: HSPB1, [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOCANNHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCBsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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