BMRB Entry 11346

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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/BMR11346
MolProbity Validation Chart

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Title:
Solution structure of Fn14 CRD domain
Deposition date:
2010-09-07
Original release date:
2011-09-07
Authors:
He, F.; Dang, W.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation:

Citation: He, Fahu; Dang, Weirong; Saito, Kohei; Watanabe, Satoru; Kobayashi, Naohiro; Guntert, Peter; Kigawa, Takanori; Tanaka, Akiko; Muto, Yutaka; Yokoyama, Shigeyuki. "Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily."  Protein Sci. 18, 650-656 (2009).
PubMed: 19241374

Assembly members:

Assembly members:
CRD domain, UNP residues 28-70, polymer, 50 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: P060919-17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CRD domain, UNP residues 28-70: GSSGSSGEQAPGTAPCSRGS SWSADLDKCMDCASCRARPH SDFCLGCAAA

Data sets:
Data typeCount
13C chemical shifts161
15N chemical shifts40
1H chemical shifts242

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CRD domain, UNP residues 28-701

Entities:

Entity 1, CRD domain, UNP residues 28-70 50 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUGLNALA
2   PROGLYTHRALAPROCYSSERARGGLYSER
3   SERTRPSERALAASPLEUASPLYSCYSMET
4   ASPCYSALASERCYSARGALAARGPROHIS
5   SERASPPHECYSLEUGLYCYSALAALAALA

Samples:

sample_1: Fn14, [U-13C; U-15N], 1.1 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 1H-15N NOESYsample_1isotropiccondition_1
3D 1H-13C NOESYsample_1isotropiccondition_1

Software:

CYANA v2.1, P.GUNTERT, ET, AL. - refinement, structure solution

NMRPipe v20031121, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and, Bax - processing

NMRView v5.0.4, Johnson, One, Moon, Scientific - data analysis

xwinnmr v3.5, Bruker, Biospin - collection

Kujira v0.9839, Kobayashi N. - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17237
PDB
DBJ BAA94792 BAJ20302
GB AAF69108 AAH02718 ABM83894 ABM87215 EAW85429
REF NP_057723 XP_001089176 XP_001165479 XP_002826080 XP_003269240
SP Q9NP84
AlphaFold Q9NP84

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