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Biological Magnetic Resonance Data Bank


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BMRB Entry 25398

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25398
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Title: NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 5.5

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 5.5"  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 shifts469
15N chemical shifts145
1H chemical shifts878

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 133 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], 0.5 mM; sodium chloride 20 mM; sodium azide 0.03%; sodium acetate, [U-99% 2H], 20 mM; protease inhibitor cocktail 0.01 tablet/100mL

sample_2: entity, [U-99% 13C; U-99% 15N], 11.3 mg/mL; entity 11.3 mg/mL; sodium chloride 20 mM; sodium azide 0.03%; sodium acetate, [U-2H], 20 mM; protease inhibitor cocktail 0.01 tablet/100mL

sample_conditions_1: ionic strength: 0.04 M; pH: 5.5; pressure: 1 atm; temperature: 295 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-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 13C,15N filtered 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

VNMRJ v2.1b, Varian - collection

TOPSPIN v3.1, Bruker Biospin - collection, 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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 25397
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