BMRB Entry 27109

Title:
Solution-state NMR assignment of the flexible C-terminal domain of the human eye lens molecular chaperone alphaA-crystallin
Deposition date:
2017-05-18
Original release date:
2019-10-04
Authors:
Stavropoulou, Maria; Asami, Sam; Kaiser, Christoph; Haslbeck, Martin; Buchner, Johannes; Weinkauf, Sevil; Reif, Bernd
Citation:

Citation: Kaiser, Christoph; Peters, Carsten; Schmid, Philipp; Stavropoulou, Maria; Zou, Juan; Dahiya, Vinay; Mymrikov, Evgeny; Rockel, Beate; Asami, Sam; Haslbeck, Martin; Rappsilber, Juri; Reif, Bernd; Zacharias, Martin; Buchner, Johannes; Weinkauf, Sevil. "The structure and oxidation of the eye lens chaperone alphaA-crystallin"  Nat. Struct. Mol. Biol. 26, 1141-1150 (2019).
PubMed: 31792453

Assembly members:

Assembly members:
alphaA-crystallin_or_HspB1, polymer, 173 residues, Formula weight is not available

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: pET28b+

Data sets:
Data typeCount
13C chemical shifts81
15N chemical shifts22
1H chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alphaA-crystallin (or HSPB1)1

Entities:

Entity 1, alphaA-crystallin (or HSPB1) 173 residues - Formula weight is not available

1   METASPVALTHRILEGLNHISPROTRPPHE
2   LYSARGTHRLEUGLYPROPHETYRPROSER
3   ARGLEUPHEASPGLNPHEPHEGLYGLUGLY
4   LEUPHEGLUTYRASPLEULEUPROPHELEU
5   SERSERTHRILESERPROTYRTYRARGGLN
6   SERLEUPHEARGTHRVALLEUASPSERGLY
7   ILESERGLUVALARGSERASPARGASPLYS
8   PHEVALILEPHELEUASPVALLYSHISPHE
9   SERPROGLUASPLEUTHRVALLYSVALGLN
10   ASPASPPHEVALGLUILEHISGLYLYSHIS
11   ASNGLUARGGLNASPASPHISGLYTYRILE
12   SERARGGLUPHEHISARGARGTYRARGLEU
13   PROSERASNVALASPGLNSERALALEUSER
14   CYSSERLEUSERALAASPGLYMETLEUTHR
15   PHECYSGLYPROLYSILEGLNTHRGLYLEU
16   ASPALATHRHISALAGLUARGALAILEPRO
17   VALSERARGGLUGLULYSPROTHRSERALA
18   PROSERSER

Samples:

sample_1: alphaA-crystallin (or HspB1), [U-100% 13C; U-100% 15N], 3 mM; HEPES 10 mM; EDTA 1 mM; DTT 2 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR-STAR, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 950 MHz

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