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 17482

Title: Structural Characterization of small heat shock protein (Hsp12)   PubMed: 21998307

Deposition date: 2011-02-22 Original release date: 2011-10-26

Authors: Singarapu, Kiran; Tonelli, Marco; Westler, William; Markley, John

Citation: Singarapu, Kiran; Tonelli, Marco; Chow, Darius; Frederick, Ronnie; Westler, William; Markley, John. "Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical."  J. Biol. Chem. 286, 43447-43453 (2011).

Assembly members:
entity, polymer, 109 residues, 11712.830 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
entity: MSDAGRKGFGEKASEALKPD SQKSYAEQGKEYITDKADKV AGKVQPEDNKGVFQGVHDSA EKGKDNAEGQGESLADQARD YMGAAKSKLNDAVEYVSGRV HGEEDPTKK

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts102
1H chemical shifts610

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hsp121

Entities:

Entity 1, Hsp12 109 residues - 11712.830 Da.

1   METSERASPALAGLYARGLYSGLYPHEGLY
2   GLULYSALASERGLUALALEULYSPROASP
3   SERGLNLYSSERTYRALAGLUGLNGLYLYS
4   GLUTYRILETHRASPLYSALAASPLYSVAL
5   ALAGLYLYSVALGLNPROGLUASPASNLYS
6   GLYVALPHEGLNGLYVALHISASPSERALA
7   GLULYSGLYLYSASPASNALAGLUGLYGLN
8   GLYGLUSERLEUALAASPGLNALAARGASP
9   TYRMETGLYALAALALYSSERLYSLEUASN
10   ASPALAVALGLUTYRVALSERGLYARGVAL
11   HISGLYGLUGLUASPPROTHRLYSLYS

Samples:

sample_1: Hsp12, [U-100% 15N], 0.2 mM; Hsp12, [U-100% 13C; U-100% 15N], 1.0 mM; MOPS 10 mM; NaCl 100 mM; SDS 100 mM; DTT 5 mM; NaN3 3 mM; H2O 95 mM; D2O 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - structure solution

VNMRJ, Varian - collection

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

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

TALOS, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 17483 17948 18523
PDB
DBJ BAA09224 BAA14033 GAA23069
EMBL CAA39306 CAA86349 CAY79436
GB AAA34647 AAL06077 AAS56790 AHY75775 AJP38487
REF NP_116640
SP P22943
TPG DAA12425

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