BMRB Entry 27062

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27062

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Title:
1H, 13C and 15N NMR Assignments of a Bacterial Immunoglobulin- like Domain (group 2) of a Protein from a Bacterium Paenarthrobacter aurescens TC1
Deposition date:
2017-04-02
Original release date:
2017-06-29
Authors:
Verma, Deepshikha; Pawar, Asmita; Sharma, Yogendra; Chary, Kandala
Citation:

Citation: Pawar, Asmita; Verma, Deepshikha; Raman, Rajeev; Sharma, Yogendra; Chary, Kandala. "(1)H, (13)C and (15)N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1"  Biomol. NMR Assign. 11, 203-206 (2017).
PubMed: 28593559

Assembly members:

Assembly members:
Arig2, polymer, 133 residues, 13692.36 Da.

Natural source:

Natural source:   Common Name: Paenarthrobacter aurescens   Taxonomy ID: 43663   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Paenarthrobacter aurescens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Arig2: TAMHSDVKGMLNLTVTDGPG LLTGLRIKPDQTTVSLGGTT QLIAEGTFSDNSIGNRNEPA IWESRNPGIATVDGLGMVTG MNPGVATISATEGTIQATAA ITVTDPGTPNPTVVPNGCVV DPATLRVHHHHHH

Data sets:
Data typeCount
13C chemical shifts349
15N chemical shifts113
1H chemical shifts684

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Arig21

Entities:

Entity 1, Arig2 133 residues - 13692.36 Da.

Residues 128-133 represent a non-native affinity tag

1   THRALAMETHISSERASPVALLYSGLYMET
2   LEUASNLEUTHRVALTHRASPGLYPROGLY
3   LEULEUTHRGLYLEUARGILELYSPROASP
4   GLNTHRTHRVALSERLEUGLYGLYTHRTHR
5   GLNLEUILEALAGLUGLYTHRPHESERASP
6   ASNSERILEGLYASNARGASNGLUPROALA
7   ILETRPGLUSERARGASNPROGLYILEALA
8   THRVALASPGLYLEUGLYMETVALTHRGLY
9   METASNPROGLYVALALATHRILESERALA
10   THRGLUGLYTHRILEGLNALATHRALAALA
11   ILETHRVALTHRASPPROGLYTHRPROASN
12   PROTHRVALVALPROASNGLYCYSVALVAL
13   ASPPROALATHRLEUARGVALHISHISHIS
14   HISHISHIS

Samples:

sample_1: Arig2, [U-100% 15N], 0.8 mM; HEPES 50 mM; potassium chloride 50 mM; Calcium chloride 8 mM

sample_2: Arig2, [U-100% 13C; U-100% 15N], 0.8 mM; HEPES 50 mM; potassium chloride 50 mM; Calcium chloride 8 mM

sample_3: Arig2, [U-100% 13C; U-100% 15N], 0.8 mM; HEPES 50 mM; potassium chloride 50 mM; Calcium chloride 8 mM

sample_conditions_1: ionic strength: 0.062 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.1, BRUKER - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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