BMRB Entry 16253

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PDB ID: 2khr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16253
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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 chemical shift assignments for Rv2377c, a MbtH-like protein from Mycobacterium tuberculosis: A Structural Genomics Center for Infectious Disease (SSGCID) community request

Deposition date:

2009-04-11

Original release date:

2009-05-20

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Kim, Chang-Yub; Terwilliger, Thomas; Myler, Peter. "Solution structure of Rv2377c-founding member of the MbtH-like protein family." Tuberculosis (Edinb) 90, 245-251 (2010).
PubMed: 20434955

Assembly members:

Assembly members:
Rv2377c, polymer, 74 residues, Formula weight is not available

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 Vector: modifed pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv2377c: GSHMSTNPFDDDNGAFFVLV NDEDQHSLWPVFADIPAGWR VVHGEASRAACLDYVEKNWT DLRPKSLRDAMVED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	210
15N chemical shifts	52
1H chemical shifts	320

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv2377c	1

Entities:

Entity 1, Rv2377c 74 residues - Formula weight is not available

The first 3 N-terminal residues, GSH-, are non-native residues that remain after thrombin cleavage of an affinity tag.

1

GLY

SER

HIS

MET

SER

THR

ASN

PRO

PHE

ASP

2

ASP

ASN

GLY

ALA

PHE

VAL

LEU

VAL

3

ASN

ASP

GLU

ASP

GLN

HIS

SER

LEU

TRP

PRO

4

VAL

PHE

ALA

ASP

ILE

PRO

ALA

GLY

TRP

ARG

5

VAL

HIS

GLY

GLU

ALA

SER

ARG

ALA

6

CYS

LEU

ASP

TYR

VAL

GLU

LYS

ASN

TRP

THR

7

ASP

LEU

ARG

PRO

LYS

SER

LEU

ARG

ASP

ALA

8

MET

VAL

GLU

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HC(CO)NH	sample_1	isotropic	sample_conditions_1
deuterium X-change	sample_2	isotropic	sample_conditions_1

PDB	2KHR
DBJ	BAH26669 BAL66401 BAQ06468 GAA46054
EMBL	CAL72379 CCC27461 CCC44740 CCC64968 CCE37847
GB	AAK46740 ABQ74170 ABR06731 ACT24652 AEB03737
REF	NP_216893 NP_856047 WP_003412265 WP_003916994 WP_015290621
SP	P59965 P9WIP4 P9WIP5
AlphaFold	P59965 P9WIP4 P9WIP5

BMRB Entry 16253

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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