BMRB Entry 34463

Name: Structural and DNA Binding Properties of Mycobacterial Integration Host Factor mIHF
Published: 2019-12-20

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PDB ID: 6tob
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34463
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:

Structural and DNA Binding Properties of Mycobacterial Integration Host Factor mIHF

Deposition date:

2019-12-11

Original release date:

2019-12-20

Authors:

Herrmann, T.

Citation:

Citation: Odermatt, N.; Lelli, M.; Herrmann, T.; Abriata, L.; Japaridze, A.; Voilquin, H.; Singh, R.; Piton, J.; Emsley, L.; Dietler, G.; Cole, S.. "Structural and DNA binding properties of mycobacterial integration host factor mIHF" J. Struct. Biol. 209, 107434-107434 (2019).
PubMed: 31846718

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 11909.892 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMVALPQLTDEQRAAALE KAAAARRARAELKDRLKRGG TNLTQVLKDAESDEVLGKMK VSALLEALPKVGKVKAQEIM TELEIAPTRRLRGLGDRQRK ALLEKFGSA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	324
15N chemical shifts	111
1H chemical shifts	674

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_1 109 residues - 11909.892 Da.

1

GLY

SER

HIS

MET

VAL

ALA

LEU

PRO

GLN

LEU

2

THR

ASP

GLU

GLN

ARG

ALA

LEU

GLU

3

LYS

ALA

ARG

ALA

ARG

ALA

4

GLU

LEU

LYS

ASP

ARG

LEU

LYS

ARG

GLY

5

THR

ASN

LEU

THR

GLN

VAL

LEU

LYS

ASP

ALA

6

GLU

SER

ASP

GLU

VAL

LEU

GLY

LYS

MET

LYS

7

VAL

SER

ALA

LEU

GLU

ALA

LEU

PRO

LYS

8

VAL

GLY

LYS

VAL

LYS

ALA

GLN

GLU

ILE

MET

9

THR

GLU

LEU

GLU

ILE

ALA

PRO

THR

ARG

10

LEU

ARG

GLY

LEU

GLY

ASP

ARG

GLN

ARG

LYS

11

ALA

LEU

GLU

LYS

PHE

GLY

SER

ALA

Samples:

sample_1: Mycobacterial integration host factor (mIHF), [U-13C; U-15N], 1.34 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCACONH	sample_1	isotropic	sample_conditions_1
HACACONH	sample_1	isotropic	sample_conditions_1
HACANH	sample_1	isotropic	sample_conditions_1
1H-13C 3D HSQC NOESY	sample_1	isotropic	sample_conditions_1
1H-15N 3D HSQC NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

UNIO v2.9, Herrmann, T. et al., UNIO-ATNOS module, UNIO-ATNOS/CANDID for automated NOE assignment - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 1000 MHz
Bruker AVANCE III 600 MHz

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