BMRB Entry 26558

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26558

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Title:
Chemical shift assignments of the fibronectin III like domains 7-8 of type VII collagen
Deposition date:
2015-04-14
Original release date:
2016-01-06
Authors:
Hermsdorf, Ulrike; Seeger, Karsten
Citation:

Citation: Hermsdorf, Ulrike; Seeger, Karsten. "Chemical shift assignments of the fibronectin III like domains 7-8 of type VII collagen"  Biomol. NMR Assignments 10, 53-55 (2016).
PubMed: 26364055

Assembly members:

Assembly members:
Col7_domains_FNIII7-8, polymer, 186 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTWIN1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Col7_domains_FNIII7-8: MTAPEPVGSVSKLQILNASS DVLRVTWVGVPGATSYKLAW GRSEGGPMKHRILPGNKESA EIRDLEGGVSYSVRVTALVG DREGAPVSIVITTPPATPAL LETLQVVQSGEHSLRLRWEP VPGAPGFRLHWQPEGGQEQS LTLGPESNSYNLVGLEPATK YQVWLTVLGQTGEGPPRKVT AYTEPS

Data sets:
Data typeCount
13C chemical shifts682
15N chemical shifts170
1H chemical shifts1066

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Col7 subdomains FNIII7-81

Entities:

Entity 1, Col7 subdomains FNIII7-8 186 residues - Formula weight is not available

The first residue of the protein (Met) originates from cloning into the vector.

1   METTHRALAPROGLUPROVALGLYSERVAL
2   SERLYSLEUGLNILELEUASNALASERSER
3   ASPVALLEUARGVALTHRTRPVALGLYVAL
4   PROGLYALATHRSERTYRLYSLEUALATRP
5   GLYARGSERGLUGLYGLYPROMETLYSHIS
6   ARGILELEUPROGLYASNLYSGLUSERALA
7   GLUILEARGASPLEUGLUGLYGLYVALSER
8   TYRSERVALARGVALTHRALALEUVALGLY
9   ASPARGGLUGLYALAPROVALSERILEVAL
10   ILETHRTHRPROPROALATHRPROALALEU
11   LEUGLUTHRLEUGLNVALVALGLNSERGLY
12   GLUHISSERLEUARGLEUARGTRPGLUPRO
13   VALPROGLYALAPROGLYPHEARGLEUHIS
14   TRPGLNPROGLUGLYGLYGLNGLUGLNSER
15   LEUTHRLEUGLYPROGLUSERASNSERTYR
16   ASNLEUVALGLYLEUGLUPROALATHRLYS
17   TYRGLNVALTRPLEUTHRVALLEUGLYGLN
18   THRGLYGLUGLYPROPROARGLYSVALTHR
19   ALATYRTHRGLUPROSER

Samples:

sample_1: Col7 domains FNIII7-8, [U-15N], 0.76 mM; sodium phosphate 10 mM; TSP 0.1 mM

sample_2: Col7 domains FNIII7-8, [U-13C; U-15N], 0.7 mM; sodium phosphate 10 mM; TSP 0.1 mM

sample_3: Col7 domains FNIII7-8, [U-13C; U-15N], 0.7 mM; sodium phosphate 10 mM; TSP 0.1 mM

sample_4: Col7 domains FNIII7-8, [U-13C; U-15N], 0.1-0.7 mM; sodium phosphate 10 mM; TSP 0.1 mM

sample_conditions_1: ionic strength: 24 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

UniProt Q63870
AlphaFold Q78EC6

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