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Biological Magnetic Resonance Data Bank


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BMRB Entry 34048

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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/BMR34048
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Title: Solution structure of isolated 15th Fibronectin III domain from human fibronectin

Deposition date: 2016-10-04 Original release date: 2017-11-21

Authors: Waltho, J.; Cliff, M.; Blumson, E.; Humphries, M.

Citation: Waltho, J.; Cliff, M.; Blumson, E.; Humphries, M.. "Solution structure of isolated 15th Fibronectin III domain from human fibronectin"  . ., .-..

Assembly members:
Fibronectin, polymer, 86 residues, 9344.231 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Fibronectin: NASTGQEALSQTTISWAPFQ DTSEYIISCHPVGTDEEPLQ FRVPGTSTSATLTGLTRGAT YNIIVEALKDQQRHKVREEV VTVGNS

Data sets:
Data typeCount
13C chemical shifts280
15N chemical shifts90
1H chemical shifts583

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 86 residues - 9344.231 Da.

1   ASNALASERTHRGLYGLNGLUALALEUSER
2   GLNTHRTHRILESERTRPALAPROPHEGLN
3   ASPTHRSERGLUTYRILEILESERCYSHIS
4   PROVALGLYTHRASPGLUGLUPROLEUGLN
5   PHEARGVALPROGLYTHRSERTHRSERALA
6   THRLEUTHRGLYLEUTHRARGGLYALATHR
7   TYRASNILEILEVALGLUALALEULYSASP
8   GLNGLNARGHISLYSVALARGGLUGLUVAL
9   VALTHRVALGLYASNSER

Samples:

sample_1: 15th Fibronectin III domain from human fibronectin, [U-13C; U-15N], 0.35 ± 0.02 mM; EDTA 0.5 ± 0.02 mM; TRIS 10 ± 0.2 mM; TSP 0.00002 ± 0.0000002 mg/mL; sodium azide 1 ± 0.02 mM; sodium chloride 150 ± 0.2 mM; H2O 90%; D2O 10%

sample_2: 15th Fibronectin III domain from human fibronectin, [U-13C; U-15N], 0.35 ± 0.2 mM; EDTA 0.5 ± 0.2 mM; TRIS, [U-2H], 10 ± 0.2 mM; TSP 0.00002 ± 0.0000002 mg/mL; sodium azide 1 ± 0.2 mM; sodium chloride 150 ± 0.2 mM; D2O 100 mM

sample_conditions_2: ionic strength: 161 mM; pH: 6.5 pH*; pressure: 1 bar; temperature: 298 K

sample_conditions_1: ionic strength: 161 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3d hncocacbsample_1isotropicsample_conditions_1
3d HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C trosy aromaticsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

Analysis v2.4.0, CCPN - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 950 MHz

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