BMRB Entry 36395

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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/BMR36395
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
NMR structure of TuSp2-RP
Deposition date:
2020-11-07
Original release date:
2025-10-13
Authors:
Lin, Z.; Fan, T.; Fan, J.
Citation:

Citation: Fan, Carl; Zhang, Sean; Fan, Xinsong; Yuan, Robert; Lin, Carl. "(1)H, (15)N and (13)C resonance assignments of a repetitive domain of tubuliform spidroin 2."  Biomol. NMR Assign. 15, 475-477 (2021).
PubMed: 34436735

Assembly members:

Assembly members:
B6 protein, polymer, 284 residues, 15340.556 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 2730554   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Trichonephila antipodiana

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
B6 protein: NLSIGDTTSIIQLFKNFTGP PSVATFISNFHSIVQSSKTL LNLFDVAEENPLEFAKCMYE LVLKSANSLGVLNPHLIANN IYQSVVSNLDILHSSAMVNL YANAMAGSLFLEGILNSDNA ATLAKKCANDMEAFAKKMVE IG

Data sets:
Data typeCount
13C chemical shifts916
15N chemical shifts298
1H chemical shifts1924

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21

Entities:

Entity 1, entity_1_1 284 residues - 15340.556 Da.

1   ASNLEUSERILEGLYASPTHRTHRSERILE
2   ILEGLNLEUPHELYSASNPHETHRGLYPRO
3   PROSERVALALATHRPHEILESERASNPHE
4   HISSERILEVALGLNSERSERLYSTHRLEU
5   LEUASNLEUPHEASPVALALAGLUGLUASN
6   PROLEUGLUPHEALALYSCYSMETTYRGLU
7   LEUVALLEULYSSERALAASNSERLEUGLY
8   VALLEUASNPROHISLEUILEALAASNASN
9   ILETYRGLNSERVALVALSERASNLEUASP
10   ILELEUHISSERSERALAMETVALASNLEU
11   TYRALAASNALAMETALAGLYSERLEUPHE
12   LEUGLUGLYILELEUASNSERASPASNALA
13   ALATHRLEUALALYSLYSCYSALAASNASP
14   METGLUALAPHEALALYSLYSMETVALGLU
15   ILEGLY

Samples:

sample_1: TuSp2-RP, [U-99% 13C; U-99% 15N], 0.6 ± 0.05 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0 mM; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CCH TOCSYsample_1isotropicsample_conditions_1
4D 13C,15N-edited NOESYsample_1isotropicsample_conditions_1
3D 13C, 15N-filtered NOESYsample_1isotropicsample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Bruker Avance 800 MHz

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