BMRB Entry 6564

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6564
MolProbity Validation Chart

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Title:
Chemical Shift Assignment for OSCP-NT (1-120)
Deposition date:
2005-03-21
Original release date:
2005-09-22
Authors:
Carbajo, Rodrigo; Kellas, Fiona; Runswick, Michael; Walker, John; Neuhaus, David
Citation:

Citation: Carbajo, Rodrigo; Kellas, Fiona; Runswick, Michael; Montgomery, Martin; Walker, John; Neuhaus, David. "Structure of the F(1)-binding Domain of the Stator of Bovine F(1)F(o)-ATPase and How it Binds an alpha-Subunit."  J. Mol. Biol. 351, 824-838 (2005).

Assembly members:

Assembly members:
Nt OSCP, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nt OSCP: FAKLVRPPVQIYGIEGRYAT ALYSAASKQNKLEQVEKELL RVGQILKEPKMAASLLNPYV KRSVKVKSLSDMTAKEKFSP LTSNLINLLAENGRLTNTPA VISAFSTMMSVHRGEVPCTV

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts120
1H chemical shifts878

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1OSCP N-terminal domain1

Entities:

Entity 1, OSCP N-terminal domain 120 residues - Formula weight is not available

1   PHEALALYSLEUVALARGPROPROVALGLN
2   ILETYRGLYILEGLUGLYARGTYRALATHR
3   ALALEUTYRSERALAALASERLYSGLNASN
4   LYSLEUGLUGLNVALGLULYSGLULEULEU
5   ARGVALGLYGLNILELEULYSGLUPROLYS
6   METALAALASERLEULEUASNPROTYRVAL
7   LYSARGSERVALLYSVALLYSSERLEUSER
8   ASPMETTHRALALYSGLULYSPHESERPRO
9   LEUTHRSERASNLEUILEASNLEULEUALA
10   GLUASNGLYARGLEUTHRASNTHRPROALA
11   VALILESERALAPHESERTHRMETMETSER
12   VALHISARGGLYGLUVALPROCYSTHRVAL

Samples:

sample_1: OSCP N-terminal domain, [U-95% 13C; U-90% 15N], 0.5 mM; NaCl 0.5 M

conditions_1: pH: 6.5; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1isotropicconditions_1
1H13C_HSQCsample_1not availableconditions_1
1H1H_NOESYsample_1not availableconditions_1
1H1H_TOCSYsample_1not availableconditions_1
15N_NOESY_HSQCsample_1not availableconditions_1
13C_NOESY_HSQCsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
HCCH_COSYsample_1not availableconditions_1

Software:

xwinnmr, BRUKER - acquisition, processing

SPARKY - NMR analysis

CNS - NMR structure calculations

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz
  • Bruker DMX 500 MHz

Related Database Links:

BMRB 15072
PDB
GB AAA30676 AAI02205 ELR58089
PRF 1002210A
REF NP_776669 XP_005674722 XP_005893414 XP_005956973 XP_005956974
SP P13621
TPG DAA33707
AlphaFold P13621

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