BMRB Entry 16249

Title:
The carboxy-terminal non-repetitive domain of a spider dragline silk protein regulates nucleation of silk assembly
Deposition date:
2009-04-09
Original release date:
2010-05-07
Authors:
Hagn, Franz; Eisoldt, Lukas; Hardy, John; Vendrely, Charlotte; Coles, Murray; Scheibel, Thomas; Kessler, Horst
Citation:

Citation: Hagn, Franz; Eisoldt, Lukas; Hardy, John; Vendrely, Charlotte; Coles, Murray; Scheibel, Thomas; Kessler, Horst. "A conserved spider silk domain acts as a molecular switch that controls fibre assembly."  Nature 465, 239-242 (2010).
PubMed: 20463741

Assembly members:

Assembly members:
NR3, polymer, 140 residues, 13329.825 Da.

Natural source:

Natural source:   Common Name: spiders   Taxonomy ID: 45920   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Araneus Diadematus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts148
1H chemical shifts860

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NR3,chain_11
2NR3,chain_21

Entities:

Entity 1, NR3,chain_1 140 residues - 13329.825 Da.

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGGLYSERMETGLYALAALASERALA
3   ALAVALSERVALGLYGLYTYRGLYPROGLN
4   SERSERSERALAPROVALALASERALAALA
5   ALASERARGLEUSERSERPROALAALASER
6   SERARGVALSERSERALAVALSERSERLEU
7   VALSERSERGLYPROTHRASNGLNALAALA
8   LEUSERASNTHRILESERSERVALVALSER
9   GLNVALSERALASERASNPROGLYLEUSER
10   GLYCYSASPVALLEUVALGLNALALEULEU
11   GLUVALVALSERALALEUVALSERILELEU
12   GLYSERSERSERILEGLYGLNILEASNTYR
13   GLYALASERALAGLNTYRTHRGLNMETVAL
14   GLYGLNSERVALALAGLNALALEUALAGLY

Samples:

sample_1: NR3, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; trifluoroethanol 1%; H2O 95%; D2O 5%

sample_2: NR30.6 – 1 mM; H2O 95%; D2O 5%

sample_3: NR3, [U-99% 13C; U-99% 15N], 1 mM; NR3 1 mM; H2O 95%; D2O 5%

sample_4: NR3, [U-99% 15N], 0.2 – 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.02 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_4isotropicsample_conditions_1
3D HNHBsample_4isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CNH NOESYsample_1isotropicsample_conditions_1
3D NNH NOESYsample_4isotropicsample_conditions_1
3D CCH NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
filtered NOESYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - processing

SPARKY v3.11, Goddard - peak picking

PASTA v0.1, Kessler and Gemmecker - chemical shift assignment

TALOS v9.4, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB

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