BMRB Entry 36129

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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/BMR36129
MolProbity Validation Chart

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Title:
Solution NMR Structure and Backbone Dynamics of the Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, A Putative mRNA Transporter
Deposition date:
2017-11-04
Original release date:
2018-05-10
Authors:
Bhuyan, A.; Sashi, P.
Citation:

Citation: Sashi, P.; Singarapu, K.; Bhuyan, A.. "Solution NMR Structure and Backbone Dynamics of Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, a Putative mRNA Transporter."  Biochemistry 57, 912-924 (2018).
PubMed: 29320165

Assembly members:

Assembly members:
entity_1, polymer, 162 residues, 18154.422 Da.

Natural source:

Natural source:   Common Name: Mouse-ear cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAVGILEVSLISGKGLKRSD FLGKIDPYVEIQYKGQTRKS SVAKEDGGRNPTWNDKLKWR AEFPGSGADYKLIVKVMDHD TFSSDDFIGEATVHVKELLE MGVEKGTAELRPTKYNIVDS DLSFVGELLIGVSYSLLQDR GMDGEQFGGWKHSNVDHHHH HH

Data sets:
Data typeCount
13C chemical shifts464
15N chemical shifts155
1H chemical shifts1039

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 162 residues - 18154.422 Da.

1   METALAVALGLYILELEUGLUVALSERLEU
2   ILESERGLYLYSGLYLEULYSARGSERASP
3   PHELEUGLYLYSILEASPPROTYRVALGLU
4   ILEGLNTYRLYSGLYGLNTHRARGLYSSER
5   SERVALALALYSGLUASPGLYGLYARGASN
6   PROTHRTRPASNASPLYSLEULYSTRPARG
7   ALAGLUPHEPROGLYSERGLYALAASPTYR
8   LYSLEUILEVALLYSVALMETASPHISASP
9   THRPHESERSERASPASPPHEILEGLYGLU
10   ALATHRVALHISVALLYSGLULEULEUGLU
11   METGLYVALGLULYSGLYTHRALAGLULEU
12   ARGPROTHRLYSTYRASNILEVALASPSER
13   ASPLEUSERPHEVALGLYGLULEULEUILE
14   GLYVALSERTYRSERLEULEUGLNASPARG
15   GLYMETASPGLYGLUGLNPHEGLYGLYTRP
16   LYSHISSERASNVALASPHISHISHISHIS
17   HISHIS

Samples:

sample_1: Arabidopsis thaliana phloem protein 16-1, [U-99% 13C; U-99% 15N], 100 uM; Sodium Acetate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 20 mM; pH: 4.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

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

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

XEASY, Bartels et al. - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 700 MHz

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