BMRB Entry 11183

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11183
MolProbity Validation Chart

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Title:
Solution structure of the FNIII domain of human RIM-binding protein 2
Deposition date:
2010-07-21
Original release date:
2011-07-20
Authors:
Inoue, K.; Hayashi, F.; Yokoyama, S.
Citation:

Citation: Inoue, K.; Hayashi, F.; Yokoyama, S.. "Solution structure of the FNIII domain of human RIM-binding protein 2"  .

Assembly members:

Assembly members:
fn3 domain, polymer, 130 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P040705-13

Entity Sequences (FASTA):

Entity Sequences (FASTA):
fn3 domain: GSSGSSGVEFSTLPAGPPAP PQDVTVQAGVTPATIRVSWR PPVLTPTGLSNGANVTGYGV YAKGQRVAEVIFPTADSTAV ELVRLRSLEAKGVTVRTLSA QGESVDSAVAAVPPELLVPP TPHPSGPSSG

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts110
1H chemical shifts817

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1fn3 domain1

Entities:

Entity 1, fn3 domain 130 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALGLUPHE
2   SERTHRLEUPROALAGLYPROPROALAPRO
3   PROGLNASPVALTHRVALGLNALAGLYVAL
4   THRPROALATHRILEARGVALSERTRPARG
5   PROPROVALLEUTHRPROTHRGLYLEUSER
6   ASNGLYALAASNVALTHRGLYTYRGLYVAL
7   TYRALALYSGLYGLNARGVALALAGLUVAL
8   ILEPHEPROTHRALAASPSERTHRALAVAL
9   GLULEUVALARGLEUARGSERLEUGLUALA
10   LYSGLYVALTHRVALARGTHRLEUSERALA
11   GLNGLYGLUSERVALASPSERALAVALALA
12   ALAVALPROPROGLULEULEUVALPROPRO
13   THRPROHISPROSERGLYPROSERSERGLY

Samples:

sample_1: fn3 domain, [U-13C; U-15N], 1.09 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAA20776 BAG72745
GB AAH07632 ADZ15327 AIC62116 EAW98512 EHH21329
REF NP_056162 XP_005572673 XP_005572674 XP_005572675 XP_005572676
SP O15034
AlphaFold O15034

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