BMRB Entry 34473

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34473
MolProbity Validation Chart

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Title:
NMR structure of N-terminal domain from A. argentata tubuliform spidroin (TuSp) at pH 5.5
Deposition date:
2020-01-09
Original release date:
2021-02-04
Authors:
Fridmanis, J.; Jaudzems, K.
Citation:

Citation: Sede, Megija; Fridmanis, Jekabs; Otikovs, Martins; Johansson, Jan; Rising, Anna; Kronqvist, Nina; Jaudzems, Kristaps. "Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization"  Front. Mol. Biosci. 9, 936887-936887 (2022).
PubMed: 35775078

Assembly members:

Assembly members:
entity_1, polymer, 137 residues, 14055.446 Da.

Natural source:

Natural source:   Common Name: Argiope argentata   Taxonomy ID: 233271   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Argiope argentata

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAVTAVPSVFSSPNLASGFL QCLTFGIGNSPAFPTQEQQD LDAIAQVILNAVSTNTGATA SARAQALSTALASSLTDLLI AESAESNYNNQLSELTGILS NCFIQTTGSDNPAFVSRIQS LISVLSQNTDVNIISTA

Data sets:
Data typeCount
13C chemical shifts523
15N chemical shifts156
1H chemical shifts930

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 137 residues - 14055.446 Da.

1   GLYALAVALTHRALAVALPROSERVALPHE
2   SERSERPROASNLEUALASERGLYPHELEU
3   GLNCYSLEUTHRPHEGLYILEGLYASNSER
4   PROALAPHEPROTHRGLNGLUGLNGLNASP
5   LEUASPALAILEALAGLNVALILELEUASN
6   ALAVALSERTHRASNTHRGLYALATHRALA
7   SERALAARGALAGLNALALEUSERTHRALA
8   LEUALASERSERLEUTHRASPLEULEUILE
9   ALAGLUSERALAGLUSERASNTYRASNASN
10   GLNLEUSERGLULEUTHRGLYILELEUSER
11   ASNCYSPHEILEGLNTHRTHRGLYSERASP
12   ASNPROALAPHEVALSERARGILEGLNSER
13   LEUILESERVALLEUSERGLNASNTHRASP
14   VALASNILEILESERTHRALA

Samples:

sample_1: sodium chloride 20 mM; acetic acid, [U-99% 2H], 20 mM; Tubuliform protein N-terminal domain, [U-13C; U-15N], 2 mM; sodium azide 0.03%; EDTA 1 mM

sample_conditions_1: ionic strength: 0.0285 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CANDID v2.2, Herrmann, Guntert and Wuthrich - peak picking

TopSpin v4.0.6, Bruker Biospin - processing

CANDID, Herrmann, Guntert and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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