BMRB Entry 27830

Name: Backbone 1H, 13C and 15N Chemical Shift Assignment of complex of MarH with L-Trp
Published: 2019-04-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27830

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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:

Backbone 1H, 13C and 15N Chemical Shift Assignment of complex of MarH with L-Trp

Deposition date:

2019-03-07

Original release date:

2019-04-11

Authors:

Liu, Bin; Ma, Xiaofang; Hu, Kaifeng

Citation:

Citation: Liu, Bin; Hou, Yan; Wang, Xiaozheng; Ma, Xiaofang; Fang, Shiqi; Huang, Tao; Chen, Yanli; Bai, Zhiqiang; Lin, Shuangjun; Zhang, Rundong; Hu, Kaifeng. "Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH" Org. Biomol. Chem. 17, 9605-9614 (2019).
PubMed: 31681917

Assembly members:

Assembly members:
MarH, polymer, 126 residues, Formula weight is not available
entity_TRP, non-polymer, 204.225 Da.

Natural source:

Natural source: Common Name: Streptomyces Taxonomy ID: 1883 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MarH: GSRPADPEIVEGLPIPLAVA GHHQPAPFYLTADMFGGLPV QLAGGELSTLVGKPVAAPHT HPVDELYLLVSPNKGGARIE VQLDGRRHELLSPAVMRIPA GSEHCFLTLEAEVGSYCFGI LLGDRL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	391
15N chemical shifts	103
1H chemical shifts	484

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MarH	1
2	L-Tryptophan	2

Entities:

Entity 1, MarH 126 residues - Formula weight is not available

1

GLY

SER

ARG

PRO

ALA

ASP

PRO

GLU

ILE

VAL

2

GLU

GLY

LEU

PRO

ILE

PRO

LEU

ALA

VAL

ALA

3

GLY

HIS

GLN

PRO

ALA

PRO

PHE

TYR

LEU

4

THR

ALA

ASP

MET

PHE

GLY

LEU

PRO

VAL

5

GLN

LEU

ALA

GLY

GLU

LEU

SER

THR

LEU

6

VAL

GLY

LYS

PRO

VAL

ALA

PRO

HIS

THR

7

HIS

PRO

VAL

ASP

GLU

LEU

TYR

LEU

VAL

8

SER

PRO

ASN

LYS

GLY

ALA

ARG

ILE

GLU

9

VAL

GLN

LEU

ASP

GLY

ARG

HIS

GLU

LEU

10

LEU

SER

PRO

ALA

VAL

MET

ARG

ILE

PRO

ALA

11

GLY

SER

GLU

HIS

CYS

PHE

LEU

THR

LEU

GLU

12

ALA

GLU

VAL

GLY

SER

TYR

CYS

PHE

GLY

ILE

13

LEU

GLY

ASP

ARG

LEU

Entity 2, L-Tryptophan - C11 H12 N2 O2 - 204.225 Da.

1

TRP

Samples:

sample_1: MarH, [U-100% 13C; U-100% 15N], 0.65 mM; L-Tryptophan 2 mM; sodium phosphate 50 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	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

Software:

SPARKY, Goddard - chemical shift assignment

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

AutoAssign, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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