BMRB Entry 27247

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27247

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Title:
Backbone assignments of domain swapped dimer of engineered hairpin loop3 mutant of single chain Monellin
Deposition date:
2017-09-08
Original release date:
2019-02-08
Authors:
Surana, Parag; Nandwani, Neha; Udgaonkar, Jayant; Gosavi, Shachi; Das, Ranabir
Citation:

Citation: Nandwani, Neha; Surana, Parag; Negi, Hitendra; Mascarenhas, Nahren; Udgaonkar, Jayant; Das, Ranabir; Gosavi, Shachi. "A five-residue motif for the design of domain swapping in proteins."  Nat. Commun. 10, 452-452 (2019).
PubMed: 30692525

Assembly members:

Assembly members:
single_chain_monellin, polymer, 100 residues, 11479 Da.

Natural source:

Natural source:   Common Name: serendipity berry   Taxonomy ID: 3457   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Dioscoreophyllum cumminsi

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
single_chain_monellin: MGEWEIIDIGPFTQNLGKFA VDEENKIGQYGRLTFNKVIR PCMKKTIYENEGFREIKGYE YQLYVYASDKLFRADISEQV VAGGRKLLRFNGPVPPPSTP

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts90
1H chemical shifts90

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1single chain monellin, 11
2single chain monellin, 21

Entities:

Entity 1, single chain monellin, 1 100 residues - 11479 Da.

1   METGLYGLUTRPGLUILEILEASPILEGLY
2   PROPHETHRGLNASNLEUGLYLYSPHEALA
3   VALASPGLUGLUASNLYSILEGLYGLNTYR
4   GLYARGLEUTHRPHEASNLYSVALILEARG
5   PROCYSMETLYSLYSTHRILETYRGLUASN
6   GLUGLYPHEARGGLUILELYSGLYTYRGLU
7   TYRGLNLEUTYRVALTYRALASERASPLYS
8   LEUPHEARGALAASPILESERGLUGLNVAL
9   VALALAGLYGLYARGLYSLEULEUARGPHE
10   ASNGLYPROVALPROPROPROSERTHRPRO

Samples:

sample_1: single chain monellin, [U-13C; U-15N], 350 uM

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N 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

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

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