BMRB Entry 16391

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16391

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Title:
13C and 15N Chemical Shift Assignments for human alphaB-crystallin
Deposition date:
2009-07-01
Original release date:
2009-08-06
Authors:
Jehle, Stefan; Rossum, Barth; Markovic, Stefan; Rajagopal, Ponni; Klevit, Rachel; Oschkinat, Hartmut
Citation:

Citation: Higman, Victoria; Flinders, Jeremy; Hiller, Matthias; Jehle, Stefan; Markovic, Stefan; Fiedler, Sebastian; Rossum, Barth; Oschkinat, Hartmut. "Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins"  J. Biomol. NMR 44, 245-260 (2009).
PubMed: 19609683

Assembly members:

Assembly members:
alphaB-crystallin, 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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alphaB-crystallin: MDIAIHHPWIRRPFFPFHSP SRLFDQFFGEHLLESDLFPT STSLSPFYLRPPSFLRAPSW FDTGLSEMRLEKDRFSVNLD VKHFSPEELKVKVLGDVIEV HGKHEERQDEHGFISREFHR KYRIPADVDPLTITSSLSSD GVLTVNGPRKQVSGPERTIP ITREEKPAVTAAPKK

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts128

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alphaB-crystallin1

Entities:

Entity 1, alphaB-crystallin 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: alphaB-crystallin, [U-100% 13C; U-100% 15N], 20 mg; H2O 100%

sample_2: alphaB-crystallin, [1,3-13C]-glycerol; U-100% 15N], 18 mg; H2O 100%

sample_3: alphaB-crystallin, [2-13C]-glycerol ; U-100% 15N, 17 mg; H2O 100%

sample_4: alphaB-crystallin, PFMW [U-100% 13C; U-100% 15N], 18 mg; H2O 100%

sample_conditions_1: pH: 7.6; temperature: 270 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C PDSDsample_1solidsample_conditions_1
2D 13C-13C PDSDsample_2solidsample_conditions_1
2D 13C-13C PDSDsample_3solidsample_conditions_1
2D 13C-13C PDSDsample_4solidsample_conditions_1
3D 15N-13C-13C NCOCXsample_1solidsample_conditions_1
3D 15N-13C-13C NCOCXsample_2solidsample_conditions_1
3D 15N-13C-13C NCOCXsample_3solidsample_conditions_1
3D 15N-13C-13C NCOCXsample_4solidsample_conditions_1
3D 15N-13C-13C NCACXsample_1solidsample_conditions_1
3D 15N-13C-13C NCACXsample_2solidsample_conditions_1
3D 15N-13C-13C NCACXsample_3solidsample_conditions_1
3D 15N-13C-13C NCACXsample_4solidsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 400 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 25527 26640
PDB
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