BMRB Entry 16208

Name: NmerAHg
Published: 2010-09-10

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PDB ID: 2kt3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16208
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NmerAHg

Deposition date:

2009-03-10

Original release date:

2010-09-10

Authors:

Doetsch, Volker

Citation:

Citation: Ledwidge, Richard; Hong, Baoyu; Dotsch, Volker; Miller, Susan. "NmerA of Tn501 Mercuric Ion Reductase: Structural Modulation of the pK(a) Values of the Metal Binding Cysteine Thiols" Biochemistry 49, 8988-8998 (2010).
PubMed: 20828160

Assembly members:

Assembly members:
NmerA, polymer, 69 residues, 200.590 Da.
HG, non-polymer, 200.590 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NmerA: MTHLKITGMTCDSCAAHVKE ALEKVPGVQSALVSYPKGTA QLAIVPGTSPDALTAAVAGL GYKATLADA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	176
15N chemical shifts	60
1H chemical shifts	449

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NmerA	1
2	Hg	2

Entities:

Entity 1, NmerA 69 residues - 200.590 Da.

1

MET

THR

HIS

LEU

LYS

ILE

THR

GLY

MET

THR

2

CYS

ASP

SER

CYS

ALA

HIS

VAL

LYS

GLU

3

ALA

LEU

GLU

LYS

VAL

PRO

GLY

VAL

GLN

SER

4

ALA

LEU

VAL

SER

TYR

PRO

LYS

GLY

THR

ALA

5

GLN

LEU

ALA

ILE

VAL

PRO

GLY

THR

SER

PRO

6

ASP

ALA

LEU

THR

ALA

VAL

ALA

GLY

LEU

7

GLY

TYR

LYS

ALA

THR

LEU

ALA

ASP

ALA

Entity 2, Hg - Hg - 200.590 Da.

1

HG

Samples:

sample_1: NmerA, [U-100% 13C; U-100% 15N], 1 mM; Hg 1 mM; phosphate buffer 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz

BMRB	16207
PDB	2KT2 2KT3
DBJ	BAQ41837 GAA19190 GAP34039
EMBL	CAA77323 CAD10787 CAD97551 CAI11285 CAI30249
GB	AAC38220 AAK18580 AAR31066 AAZ65793 ABF13033
REF	NP_085424 WP_003156770 WP_003158917 WP_005413388 WP_011514825
SP	P00392
AlphaFold	P00392