BMRB Entry 10006

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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/BMR10006
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF FIBRONECTIN TYPE III DOMAIN OF MOUSE HYPOTHETICAL PROTEIN
Deposition date:
2005-10-14
Original release date:
2006-10-23
Authors:
Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of fibronectin type III domain of mouse hypothetical protein"  .

Assembly members:

Assembly members:
FN3 domain, polymer, 120 residues, 13500.288 Da.

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P031222-40

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FN3 domain: GSSGSSGMEPHKVVPLSKPH PPVVGKVTHHSIELYWDLEQ KEKRQGPQEQWLRFSIEEED PKMHSYGVIYTGYATRHVVE GLEPRTLYKFRLKVTSPSGE YEYSPVVSVATTRESGPSSG

Data sets:
Data typeCount
13C chemical shifts508
15N chemical shifts103
1H chemical shifts778

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 120 residues - 13500.288 Da.

1   GLYSERSERGLYSERSERGLYMETGLUPRO
2   HISLYSVALVALPROLEUSERLYSPROHIS
3   PROPROVALVALGLYLYSVALTHRHISHIS
4   SERILEGLULEUTYRTRPASPLEUGLUGLN
5   LYSGLULYSARGGLNGLYPROGLNGLUGLN
6   TRPLEUARGPHESERILEGLUGLUGLUASP
7   PROLYSMETHISSERTYRGLYVALILETYR
8   THRGLYTYRALATHRARGHISVALVALGLU
9   GLYLEUGLUPROARGTHRLEUTYRLYSPHE
10   ARGLEULYSVALTHRSERPROSERGLYGLU
11   TYRGLUTYRSERPROVALVALSERVALALA
12   THRTHRARGGLUSERGLYPROSERSERGLY

Samples:

sample_1: FN3 domain, [U-13C; U-15N], 1.1 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 0.12 M; pH: 7.5; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121 - processing

NMRView v5.0.4 - data analysis

Kujira v0.8994 - data analysis

CYANA v2.0.17 - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB24192 BAB30580
GB AAH46278 AAV68048 EDL17784
REF NP_080126 XP_006508183
SP Q9DAM9
AlphaFold Q9DAM9

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