BMRB Entry 34551

Title:
NMR structure of flagelliform spidroin (FlagSp) N-terminal domain from Trichonephila clavipes at pH 5.5
Deposition date:
2020-08-10
Original release date:
2021-08-17
Authors:
Sarr, M.; Kitoka, K.; Walsh-White, K.; Kaldmae, M.; Landreh, M.; Rising, A.; Johansson, J.; Jaudzems, K.; Kronqvist, N.
Citation:

Citation: Sarr, Medoune; Kitoka, Kristine; Walsh-White, Kellie-Ann; Kaldmae, Margit; Metlans, Rimants; Tars, Kaspar; Mantese, Alessandro; Shah, Dipen; Landreh, Michael; Rising, Anna; Johansson, Jan; Jaudzems, Kristaps; Kronqvist, Nina. "The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence"  J. Biol. Chem. 298, 101913-101913 (2022).
PubMed: 35398358

Assembly members:

Assembly members:
entity_1, polymer, 135 residues, 14256.615 Da.

Natural source:

Natural source:   Common Name: Golden silk orbweaver   Taxonomy ID: 2585209   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Nephila clavipes

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts155
1H chemical shifts901

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21

Entities:

Entity 1, unit_1 135 residues - 14256.615 Da.

1   GLYSERGLYASNSERALASERGLNSERPRO
2   PHESERASNPROASNTHRALAGLUALAPHE
3   ALAARGSERPHEVALSERASNILEVALSER
4   SERGLYGLUPHEGLYALAGLNGLYALAGLU
5   ASPPHEASPASPILEILEGLNSERLEUILE
6   GLNALAGLNSERMETGLYLYSGLYARGHIS
7   ASPTHRLYSALALYSALALYSALAMETGLN
8   VALALALEUALASERSERILEALAGLULEU
9   VALILEALAGLUSERSERGLYGLYASPVAL
10   GLNARGLYSTHRASNVALILESERASNALA
11   LEUARGASNALALEUMETSERTHRTHRGLY
12   SERPROASNGLUGLUPHEVALHISGLUVAL
13   GLNASPLEUILEGLNMETLEUSERGLNGLU
14   GLNILEASNGLUVAL

Samples:

sample_1: Flagelliform spidroin N-terminal domain, [U-13C; U-15N], 1.2 mM; sodium acetate, [U-100% 2H], 20 mM; sodium chloride 20 mM; sodium azide 0.03%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.04 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 HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA, Keller and Wuthrich - chemical shift assignment

TopSpin v4.0, Bruker Biospin - collection

CANDID, Herrmann, Guntert and Wuthrich - peak picking

TopSpin, Bruker Biospin - processing

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