BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18726

Title: Repetitive domain (RP) of aciniform spidroin 1 from Nephila antipodiana   PubMed: 23129012

Authors: Wang, Shujing; Huang, Weidong; Yang, Daiwen

Citation: Wang, Shujing; Huang, Weidong; Yang, Daiwen. "NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana"  J. Biomol. NMR 54, 415-420 (2012).

Assembly members:
AcSp1-RP, polymer, 167 residues, 17079.383 Da.

Natural source:   Common Name: Spiders   Taxonomy ID: 171624   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Nephila antipodiana

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

Entity Sequences (FASTA):
AcSp1-RP: MHHHHHHSGSLGDQLTSTLA SALTKTNTLKAVSASKPSAN VAVAIVTSGLKKALGALRIN AGVSSQLTSAVSQAVANVRP GSSPAVYAKAIAAPSVQILV SSGSVNNNNAKQVASTLSEN LVREMANTARRYRVNVPEAS VQADVSLVTSMTSTFVISSQ TSVQMGG

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts165
1H chemical shifts1070

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AcSp1-RP1

Entities:

Entity 1, AcSp1-RP 167 residues - 17079.383 Da.

1   METHISHISHISHISHISHISSERGLYSER
2   LEUGLYASPGLNLEUTHRSERTHRLEUALA
3   SERALALEUTHRLYSTHRASNTHRLEULYS
4   ALAVALSERALASERLYSPROSERALAASN
5   VALALAVALALAILEVALTHRSERGLYLEU
6   LYSLYSALALEUGLYALALEUARGILEASN
7   ALAGLYVALSERSERGLNLEUTHRSERALA
8   VALSERGLNALAVALALAASNVALARGPRO
9   GLYSERSERPROALAVALTYRALALYSALA
10   ILEALAALAPROSERVALGLNILELEUVAL
11   SERSERGLYSERVALASNASNASNASNALA
12   LYSGLNVALALASERTHRLEUSERGLUASN
13   LEUVALARGGLUMETALAASNTHRALAARG
14   ARGTYRARGVALASNVALPROGLUALASER
15   VALGLNALAASPVALSERLEUVALTHRSER
16   METTHRSERTHRPHEVALILESERSERGLN
17   THRSERVALGLNMETGLYGLY

Samples:

sample_1: AcSp1-RP, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

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

NMRspy, Yu Zheng, Daiwen Yang - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

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