BMRB Entry 17008

Name: Solution NMR Structure of Peptide methionine sulfoxide reductase msrB from Bacillus subtilis, Northeast Structural Genomics Consortium Target SR10
Published: 2010-07-07

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PDB ID: 2kzn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17008
MolProbity Validation Chart

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

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Title:

Solution NMR Structure of Peptide methionine sulfoxide reductase msrB from Bacillus subtilis, Northeast Structural Genomics Consortium Target SR10

Deposition date:

2010-06-18

Original release date:

2010-07-07

Authors:

Ertekin, Asli; Cooper, Bonnie; Ciccosanti, Colleen; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Rossi, Paolo; Maglaqui, Melissa; Janjua, Haleema; Prestegard, James; Lee, Hsiau-Wei; Aramini, James

Citation:

Citation: Ertekin, Asli; Xiao, R.; Montelione, G.. "Northeast Structural Genomics Consortium Target SR10" To be published ., .-..

Assembly members:

Assembly members:
SR10, polymer, 151 residues, 17145.258 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SR10: MAYNKEEKIKSLNRMQYEVT QNNGTEPPFQNEYWDHKEEG LYVDIVSGKPLFTSKDKFDS QCGWPSFTKPIEEEVEEKLD TSHGMIRTEVRSRTADSHLG HVFNDGPGPNGLRYCINSAA LRFVPKHKLKEEGYESYLHL FNKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	456
15N chemical shifts	140
1H chemical shifts	276

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SR10	1

Entities:

Entity 1, SR10 151 residues - 17145.258 Da.

The construct studied has LEHHHHHH purification tag on C-terminus.

1

MET

ALA

TYR

ASN

LYS

GLU

LYS

ILE

LYS

2

SER

LEU

ASN

ARG

MET

GLN

TYR

GLU

VAL

THR

3

GLN

ASN

GLY

THR

GLU

PRO

PHE

GLN

4

ASN

GLU

TYR

TRP

ASP

HIS

LYS

GLU

GLY

5

LEU

TYR

VAL

ASP

ILE

VAL

SER

GLY

LYS

PRO

6

LEU

PHE

THR

SER

LYS

ASP

LYS

PHE

ASP

SER

7

GLN

CYS

GLY

TRP

PRO

SER

PHE

THR

LYS

PRO

8

ILE

GLU

VAL

GLU

LYS

LEU

ASP

9

THR

SER

HIS

GLY

MET

ILE

ARG

THR

GLU

VAL

10

ARG

SER

ARG

THR

ALA

ASP

SER

HIS

LEU

GLY

11

HIS

VAL

PHE

ASN

ASP

GLY

PRO

GLY

PRO

ASN

12

GLY

LEU

ARG

TYR

CYS

ILE

ASN

SER

ALA

13

LEU

ARG

PHE

VAL

PRO

LYS

HIS

LYS

LEU

LYS

14

GLU

GLY

TYR

GLU

SER

TYR

LEU

HIS

LEU

15

PHE

ASN

LYS

LEU

GLU

HIS

16

HIS

Samples:

SR10.026: SR10, [U-100% 13C; U-100% 15N; U-100% 2H], 0.8 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

SR10.022: SR10, [U-5% 13C; U-100% 15N], 1.2 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

SR10.022_2: SR10, [U-5% 13C; U-100% 15N], 1.2 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 200 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	SR10.026	isotropic	sample_conditions_1
2D 1H-13C HSQC	SR10.026	isotropic	sample_conditions_1
3D HNCO	SR10.026	isotropic	sample_conditions_1
3D HNCA	SR10.026	isotropic	sample_conditions_1
3D TRHNCACB 2H dec	SR10.026	isotropic	sample_conditions_1
3D HN(CA)CO	SR10.026	isotropic	sample_conditions_1
2D 1H-15N HSQC - T1	SR10.026	isotropic	sample_conditions_1
2D 1H-15N HSQC - T2	SR10.026	isotropic	sample_conditions_1
3D 1H-15N NOESY	SR10.026	isotropic	sample_conditions_1
3D 1H-13C NOESY	SR10.026	isotropic	sample_conditions_1
3D (N15)HSQC-NOESY-(N15)HSQC	SR10.026	isotropic	sample_conditions_1
3D (C13)HSQC-NOESY-(C13)HSQC	SR10.026	isotropic	sample_conditions_1
3D (N15)HSQC-NOESY-(C13)HSQC	SR10.026	isotropic	sample_conditions_1
3D (C13)HSQC-NOESY-(N15)HSQC	SR10.026	isotropic	sample_conditions_1
2D 1H-13C HSQC	SR10.022	isotropic	sample_conditions_1
2D 1H-15N TROSY	SR10.022_2	anisotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis, peak picking

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

PDB	2KZN 3E0O
DBJ	BAI85662 BAM52650 BAM58225 GAK79338
EMBL	CAB14086 CCU58667 CEI57380 CEJ77805 CJS85990
GB	AAA96648 ADV92894 AEP91184 AFQ58114 AGA23472
REF	NP_390051 WP_003230813 WP_014477116 WP_014480061 WP_021481498
SP	P54155
AlphaFold	P54155