BMRB Entry 25085

Name: Solution structure of the rhodanese domain of YgaP from E. coli
Published: 2014-09-19

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PDB ID: 2mrm
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/BMR25085
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:

Solution structure of the rhodanese domain of YgaP from E. coli

Deposition date:

2014-07-12

Original release date:

2014-09-19

Authors:

Wang, Wei; Zhou, Peng; Tian, Changlin; Wu, Fangming

Citation:

Citation: Wang, Wei; Zhou, Peng; He, Yao; Yu, Lu; Xiong, Ying; Tian, Changlin; Wu, Fangming. "Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP." Biochem. Biophys. Res. Commun. ., .-. (2014).
PubMed: 25204500

Assembly members:

Assembly members:
YgaP, polymer, 114 residues, 11660.426 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YgaP: MHHHHHHMALTTISPHDAQE LIARGAKLIDIRDADEYLRE HIPEADLAPLSVLEQSGLPA KLRHEQIIFHCQAGKRTSNN ADKLAAIAAPAEIFLLEDGI DGWKRAGLPVAVNK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	724
13C chemical shifts	415
15N chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	rhodanese domain of YgaP	1

Entities:

Entity 1, rhodanese domain of YgaP 114 residues - 11660.426 Da.

1

MET

HIS

MET

ALA

LEU

2

THR

ILE

SER

PRO

HIS

ASP

ALA

GLN

GLU

3

LEU

ILE

ALA

ARG

GLY

ALA

LYS

LEU

ILE

ASP

4

ILE

ARG

ASP

ALA

ASP

GLU

TYR

LEU

ARG

GLU

5

HIS

ILE

PRO

GLU

ALA

ASP

LEU

ALA

PRO

LEU

6

SER

VAL

LEU

GLU

GLN

SER

GLY

LEU

PRO

ALA

7

LYS

LEU

ARG

HIS

GLU

GLN

ILE

PHE

HIS

8

CYS

GLN

ALA

GLY

LYS

ARG

THR

SER

ASN

9

ALA

ASP

LYS

LEU

ALA

ILE

ALA

PRO

10

ALA

GLU

ILE

PHE

LEU

GLU

ASP

GLY

ILE

11

ASP

GLY

TRP

LYS

ARG

ALA

GLY

LEU

PRO

VAL

12

ALA

VAL

ASN

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

BMRB	17137 19943 19946
PDB	2MOI 2MOL 2MRM
DBJ	BAB36952 BAE76780 BAG78445 BAI26930 BAI31960
EMBL	CAQ33005 CAQ87965 CAQ99590 CAR04179 CAR09287
GB	AAC75715 AAG57776 AAN44189 AAN81669 AAP18017
REF	NP_311556 NP_417154 NP_708482 WP_001229433 WP_001229437
SP	P55734
AlphaFold	P55734

BMRB Entry 25085

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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