BMRB Entry 26640

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26640

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Title:
1H, 15N and 13C chemical shift assignment of the alpha-crystallin domain and the C-terminal domain in human alpha-B crystallin oligomers.
Deposition date:
2015-08-26
Original release date:
2015-09-28
Authors:
Mainz, Andi; Reif, Bernd
Citation:

Citation: Mainz, Andi; Peschek, Jirka; Stavropoulou, Maria; Back, Katrin; Asami, Sam; Bardiaux, Benjamin; Prade, Elke; Peters, Carsten; Weinkauf, Sevil; Buchner, Johannes; Reif, Bernd. "The chaperone AlphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client"  Nat. Struct. Mol. Biol. 22, 898-905 (2015).
PubMed: 26458046

Assembly members:

Assembly members:
aB, polymer, 175 residues, 20159 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: pET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
aB: MDIAIHHPWIRRPFFPFHSP SRLFDQFFGEHLLESDLFPT STSLSPFYLRPPSFLRAPSW FDTGLSEMRLEKDRFSVNLD VKHFSPEELKVKVLGDVIEV HGKHEERQDEHGFISREFHR KYRIPADVDPLTITSSLSSD GVLTVNGPRKQVSGPERTIP ITREEKPAVTAAPKK

Data sets:
Data typeCount
13C chemical shifts240
15N chemical shifts100
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha B crystallin, 11
2alpha B crystallin, 21
3alpha B crystallin, 31
4alpha B crystallin, 41
5alpha B crystallin, 51
6alpha B crystallin, 61
7alpha B crystallin, 71
8alpha B crystallin, 81
9alpha B crystallin, 91
10alpha B crystallin, 101
11alpha B crystallin, 111
12alpha B crystallin, 121
13alpha B crystallin, 131
14alpha B crystallin, 141
15alpha B crystallin, 151
16alpha B crystallin, 161
17alpha B crystallin, 171
18alpha B crystallin, 181
19alpha B crystallin, 191
20alpha B crystallin, 201
21alpha B crystallin, 211
22alpha B crystallin, 221
23alpha B crystallin, 231
24alpha B crystallin, 241
25alpha B crystallin, 251
26alpha B crystallin, 261
27alpha B crystallin, 271
28alpha B crystallin, 281

Entities:

Entity 1, alpha B crystallin, 1 175 residues - 20159 Da.

1   METASPILEALAILEHISHISPROTRPILE
2   ARGARGPROPHEPHEPROPHEHISSERPRO
3   SERARGLEUPHEASPGLNPHEPHEGLYGLU
4   HISLEULEUGLUSERASPLEUPHEPROTHR
5   SERTHRSERLEUSERPROPHETYRLEUARG
6   PROPROSERPHELEUARGALAPROSERTRP
7   PHEASPTHRGLYLEUSERGLUMETARGLEU
8   GLULYSASPARGPHESERVALASNLEUASP
9   VALLYSHISPHESERPROGLUGLULEULYS
10   VALLYSVALLEUGLYASPVALILEGLUVAL
11   HISGLYLYSHISGLUGLUARGGLNASPGLU
12   HISGLYPHEILESERARGGLUPHEHISARG
13   LYSTYRARGILEPROALAASPVALASPPRO
14   LEUTHRILETHRSERSERLEUSERSERASP
15   GLYVALLEUTHRVALASNGLYPROARGLYS
16   GLNVALSERGLYPROGLUARGTHRILEPRO
17   ILETHRARGGLUGLULYSPROALAVALTHR
18   ALAALAPROLYSLYS

Samples:

sample_1: aB, [U-13C; U-15N; U-2H], 2 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: aB, [U-13C; U-15N; U-2H], 25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; Cu(II)-EDTA 60 mM

sample_3: aB, [U-13C; U-15N; U-2H], 25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; Cu(II)-EDTA 60 mM

sample_conditions_1: pH: 7.5; temperature: 295 K

sample_conditions_2: pH: 7.5; temperature: 277 K

sample_conditions_3: pH: 7.5; temperature: 289 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N CPsample_2anisotropicsample_conditions_2
3D hCAhNHsample_2anisotropicsample_conditions_2
3D hCOhNHsample_2anisotropicsample_conditions_2
2D 1H-15N CPsample_3anisotropicsample_conditions_3
3D RFDR-HSQC HHNsample_3anisotropicsample_conditions_3

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
BMRB 16391 25527
DBJ BAD51947 BAE27257 BAE40798 BAE87237 BAG36739
EMBL CAA42910 CAA42911 CAA64669 CAC33095 CAF02108
GB AAA03655 AAA37472 AAA40977 AAA52104 AAA67045
PIR I53319
PRF 2015215A
REF NP_001012475 NP_001075876 NP_001125917 NP_001247830 NP_001271991
SP P02510 P02511 P23927 P23928 P41316
TPG DAA22360
AlphaFold P02510 P02511 P23927 P23928 P41316

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