BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11111

Title: The solution structure of the sixth fibronectin type III domain of human Neogenin

Deposition date: 2010-02-18 Original release date: 2011-02-18

Authors: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the sixth fibronectin type III domain of human Neogenin"  .

Assembly members:
fn3 domain, polymer, 124 residues, Formula weight is not available

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P041213-07

Entity Sequences (FASTA):
fn3 domain: GSSGSSGTAHGTTFELVPTS PPKDVTVVSKEGKPKTIIVN WQPPSEANGKITGYIIYYST DVNAEIHDWVIEPVVGNRLT HQIQELTLDTPYYFKIQARN SKGMGPMSEAVQFRTPKASG PSSG

Data sets:
Data typeCount
13C chemical shifts514
15N chemical shifts112
1H chemical shifts798

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1fn3 domain1

Entities:

Entity 1, fn3 domain 124 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRALAHIS
2   GLYTHRTHRPHEGLULEUVALPROTHRSER
3   PROPROLYSASPVALTHRVALVALSERLYS
4   GLUGLYLYSPROLYSTHRILEILEVALASN
5   TRPGLNPROPROSERGLUALAASNGLYLYS
6   ILETHRGLYTYRILEILETYRTYRSERTHR
7   ASPVALASNALAGLUILEHISASPTRPVAL
8   ILEGLUPROVALVALGLYASNARGLEUTHR
9   HISGLNILEGLNGLULEUTHRLEUASPTHR
10   PROTYRTYRPHELYSILEGLNALAARGASN
11   SERLYSGLYMETGLYPROMETSERGLUALA
12   VALGLNPHEARGTHRPROLYSALASERGLY
13   PROSERSERGLY

Samples:

sample_1: FN3 domain, [U-13C; U-15N], 1.3 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:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
REF XP_004056579 XP_009917344 XP_010190209

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