BMRB Entry 36129

Name: Solution NMR Structure and Backbone Dynamics of the Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, A Putative mRNA Transporter
Published: 2018-05-10

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PDB ID: 5yq3
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	464
15N chemical shifts	155
1H chemical shifts	1039

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 162 residues - 18154.422 Da.

1

MET

ALA

VAL

GLY

ILE

LEU

GLU

VAL

SER

LEU

2

ILE

SER

GLY

LYS

GLY

LEU

LYS

ARG

SER

ASP

3

PHE

LEU

GLY

LYS

ILE

ASP

PRO

TYR

VAL

GLU

4

ILE

GLN

TYR

LYS

GLY

GLN

THR

ARG

LYS

SER

5

SER

VAL

ALA

LYS

GLU

ASP

GLY

ARG

ASN

6

PRO

THR

TRP

ASN

ASP

LYS

LEU

LYS

TRP

ARG

7

ALA

GLU

PHE

PRO

GLY

SER

GLY

ALA

ASP

TYR

8

LYS

LEU

ILE

VAL

LYS

VAL

MET

ASP

HIS

ASP

9

THR

PHE

SER

ASP

PHE

ILE

GLY

GLU

10

ALA

THR

VAL

HIS

VAL

LYS

GLU

LEU

GLU

11

MET

GLY

VAL

GLU

LYS

GLY

THR

ALA

GLU

LEU

12

ARG

PRO

THR

LYS

TYR

ASN

ILE

VAL

ASP

SER

13

ASP

LEU

SER

PHE

VAL

GLY

GLU

LEU

ILE

14

GLY

VAL

SER

TYR

SER

LEU

GLN

ASP

ARG

15

GLY

MET

ASP

GLY

GLU

GLN

PHE

GLY

TRP

16

LYS

HIS

SER

ASN

VAL

ASP

HIS

17

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 36129

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: