BMRB Entry 16039

Name: NMR structure of the unphosphorylated form of OdhI, OdhI.
Published: 2009-04-29

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PDB ID: 2kb4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16039
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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 structure of the unphosphorylated form of OdhI, OdhI.

Deposition date:

2008-11-20

Original release date:

2009-04-29

Authors:

Barthe, Philippe; Roumestand, Christian; Canova, Marc; Hurard, Corinne; Molle, Virginie; Cohen-Gonsaud, Martin

Citation:

Citation: Barthe, Philippe; Roumestand, Christian; Canova, Marc; Kremer, Laurent; Hurard, Corinne; Molle, Virginie; Cohen-Gonsaud, Martin. "Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism" Structure 17, 568-578 (2009).
PubMed: 19368890

Assembly members:

Assembly members:
OdhI, polymer, 143 residues, 15700.225 Da.

Natural source:

Natural source: Common Name: Corynebacterium glutamicum Taxonomy ID: 1718 Superkingdom: Bacteria Kingdom: not available Genus/species: Corynebacterium glutamicum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OdhI: MSDNNGTPEPQVETTSVFRA DLLKEMESSTGTAPASTGAE NLPAGSALLVVKRGPNAGAR FLLDQPTTTAGRHPESDIFL DDVTVSRRHAEFRINEGEFE VVDVGSLNGTYVNREPRNAQ VMQTGDEIQIGKFRLVFLAG PAE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	145
1H chemical shifts	970

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OdhI	1

Entities:

Entity 1, OdhI 143 residues - 15700.225 Da.

1

MET

SER

ASP

ASN

GLY

THR

PRO

GLU

PRO

2

GLN

VAL

GLU

THR

SER

VAL

PHE

ARG

ALA

3

ASP

LEU

LYS

GLU

MET

GLU

SER

THR

4

GLY

THR

ALA

PRO

ALA

SER

THR

GLY

ALA

GLU

5

ASN

LEU

PRO

ALA

GLY

SER

ALA

LEU

VAL

6

VAL

LYS

ARG

GLY

PRO

ASN

ALA

GLY

ALA

ARG

7

PHE

LEU

ASP

GLN

PRO

THR

ALA

8

GLY

ARG

HIS

PRO

GLU

SER

ASP

ILE

PHE

LEU

9

ASP

VAL

THR

VAL

SER

ARG

HIS

ALA

10

GLU

PHE

ARG

ILE

ASN

GLU

GLY

GLU

PHE

GLU

11

VAL

ASP

VAL

GLY

SER

LEU

ASN

GLY

THR

12

TYR

VAL

ASN

ARG

GLU

PRO

ARG

ASN

ALA

GLN

13

VAL

MET

GLN

THR

GLY

ASP

GLU

ILE

GLN

ILE

14

GLY

LYS

PHE

ARG

LEU

VAL

PHE

LEU

ALA

GLY

15

PRO

ALA

GLU

Samples:

sample_1: OdhI, [U-100% 15N], 0.3 mM; H2O 95%; D2O 5%; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

BMRB	16038
PDB	2KB3 2KB4 4QCJ
DBJ	BAB98834 BAF54493
EMBL	CAF21450 CCH24605
GB	AGG66772 AGN19176 AGN22201 AGT05407 AIK85116
REF	NP_600658 WP_003856253 WP_015651203
SP	Q8NQJ3
AlphaFold	Q8NQJ3