BMRB Entry 25921

Name: NMR assignment of the 65-residue-long inactivating factor of glutanmine synthetase I from cyanobacterirum Synechocystis sp. PCC 6803
Published: 2016-06-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25921

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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:

NMR assignment of the 65-residue-long inactivating factor of glutanmine synthetase I from cyanobacterirum Synechocystis sp. PCC 6803

Deposition date:

2015-12-15

Original release date:

2016-06-13

Authors:

Pantoja-Uceda, David; Neira, Jose; Santoro, Jorge

Citation:

Citation: Pantoja-Uceda, David; Neira, Jose; Saelices, Lorena; Robles-Rengel, Rocio; Florencio, Francsico; Muro-Pastor, M. Isabel; Santoro, Jorge. "Dissecting the Binding between Glutamine Synthetase and Its Two Natively Unfolded Protein Inhibitors" Biochemistry 55, 3370-3382 (2016).
PubMed: 27232663

Assembly members:

Assembly members:
IF7, polymer, 85 residues, Formula weight is not available

Natural source:

Natural source: Common Name: cyanobacteria Taxonomy ID: 1148 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis sp. PPC 6803

Experimental source:

Experimental source: Production method: recombinant technology Host organism: E.coli (BL21) Vector: pet24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IF7: MGSSHHHHHHSSGLVPRGSH MSTQQQARALMMRHHQFIKN RQQSMLSRAAAEIGVEAEKD FWTTVQGKPQSSFRTTYDRS NASLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	226
15N chemical shifts	74
1H chemical shifts	272

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IF7	1

Entities:

Entity 1, IF7 85 residues - Formula weight is not available

Residues 1-20 are not presente in native IF7 renumbering -20 numbers

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

SER

THR

GLN

ALA

ARG

ALA

LEU

4

MET

ARG

HIS

GLN

PHE

ILE

LYS

ASN

5

ARG

GLN

SER

MET

LEU

SER

ARG

ALA

6

ALA

GLU

ILE

GLY

VAL

GLU

ALA

GLU

LYS

ASP

7

PHE

TRP

THR

VAL

GLN

GLY

LYS

PRO

GLN

8

SER

PHE

ARG

THR

TYR

ASP

ARG

SER

9

ASN

ALA

SER

LEU

SER

Samples:

sample_1: IF7, [U-99% 13C; U-99% 15N], 1.7 mM; ammonium acetate 10 mM; H2O 90%; D2O, [U-2H], 10%; DSS 50 uM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v216, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 500 MHz

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