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 25397

Title: NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2

Deposition date: 2014-12-17 Original release date: 2015-08-17

Authors: Otikovs, Martins; Jaudzems, Kristaps; Chen, Gefei; Nordling, Kerstin; Rising, Anna; Johansson, Jan

Citation: Otikovs, Martins; Jaudzems, Kristaps; Chen, Gefei; Nordling, Kerstin; Rising, Anna; Johansson, Jan. "NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2"  To be Published ., .-..

Assembly members:
entity, polymer, 133 residues, 14067.897 Da.

Natural source:   Common Name: spiders   Taxonomy ID: 182803   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Araneus ventricosus

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

Entity Sequences (FASTA):
entity: GSGNSQPIWTNPNAAMTMTN NLVQCASRSGVLTADQMDDM GMMADSVNSQMQKMGPNPPQ HRLRAMNTAMAAEVAEVVAT SPPQSYSAVLNTIGACLRES MMQATGSVDNAFTNEVMQLV KMLSADSANEVST

Data sets:
Data typeCount
13C chemical shifts504
15N chemical shifts140
1H chemical shifts857

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 133 residues - 14067.897 Da.

Residues 1-4 are from a non-native affinity tag

1   GLYSERGLYASNSERGLNPROILETRPTHR
2   ASNPROASNALAALAMETTHRMETTHRASN
3   ASNLEUVALGLNCYSALASERARGSERGLY
4   VALLEUTHRALAASPGLNMETASPASPMET
5   GLYMETMETALAASPSERVALASNSERGLN
6   METGLNLYSMETGLYPROASNPROPROGLN
7   HISARGLEUARGALAMETASNTHRALAMET
8   ALAALAGLUVALALAGLUVALVALALATHR
9   SERPROPROGLNSERTYRSERALAVALLEU
10   ASNTHRILEGLYALACYSLEUARGGLUSER
11   METMETGLNALATHRGLYSERVALASPASN
12   ALAPHETHRASNGLUVALMETGLNLEUVAL
13   LYSMETLEUSERALAASPSERALAASNGLU
14   VALSERTHR

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.95 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.03%; protease inhibitor cocktail 0.01 tablet/100mL

sample_conditions_1: ionic strength: 0.085 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

VNMRJ v2.1b, Varian - collection

TOPSPIN v3.1, Bruker Biospin - processing

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

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

UNIO v2.0.2, T. Herrmann, F. Fiorito, J. Volk - data analysis, peak picking, structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 25398
PDB
GB AFV31615

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts