BMRB Entry 18215

Name: Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50.
Published: 2012-02-03

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PDB ID: 2lok
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18215
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50.

Deposition date:

2012-01-24

Original release date:

2012-02-03

Authors:

Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50." To be published ., .-..

Assembly members:

Assembly members:
HsR50, polymer, 191 residues, 20753.697 Da.

Natural source:

Natural source: Common Name: Halobacterium salinarium Taxonomy ID: 2242 Superkingdom: Archaea Kingdom: not available Genus/species: Halobacterium salinarium

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HsR50: MSPIPLPVTDTDDAWRARIA AHRADKDEFLATHDQSPIPP ADRGAFDGLRYFDIDASFRV AARYQPARDPEAVELETTRG PPAEYTRAAVLGFDLGDSHH TLTAFRVEGESSLFVPFTDE TTDDGRTYEHGRYLDVDPAG ADGGDEVALDFNLAYNPFCA YGGSFSCALPPADNHVPAAI TAGERVDADLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	704
15N chemical shifts	169
1H chemical shifts	1023

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HsR50	1

Entities:

Entity 1, HsR50 191 residues - 20753.697 Da.

1

MET

SER

PRO

ILE

PRO

LEU

PRO

VAL

THR

ASP

2

THR

ASP

ALA

TRP

ARG

ALA

ARG

ILE

ALA

3

ALA

HIS

ARG

ALA

ASP

LYS

ASP

GLU

PHE

LEU

4

ALA

THR

HIS

ASP

GLN

SER

PRO

ILE

PRO

5

ALA

ASP

ARG

GLY

ALA

PHE

ASP

GLY

LEU

ARG

6

TYR

PHE

ASP

ILE

ASP

ALA

SER

PHE

ARG

VAL

7

ALA

ARG

TYR

GLN

PRO

ALA

ARG

ASP

PRO

8

GLU

ALA

VAL

GLU

LEU

GLU

THR

ARG

GLY

9

PRO

ALA

GLU

TYR

THR

ARG

ALA

VAL

10

LEU

GLY

PHE

ASP

LEU

GLY

ASP

SER

HIS

11

THR

LEU

THR

ALA

PHE

ARG

VAL

GLU

GLY

GLU

12

SER

LEU

PHE

VAL

PRO

PHE

THR

ASP

GLU

13

THR

ASP

GLY

ARG

THR

TYR

GLU

HIS

14

GLY

ARG

TYR

LEU

ASP

VAL

ASP

PRO

ALA

GLY

15

ALA

ASP

GLY

ASP

GLU

VAL

ALA

LEU

ASP

16

PHE

ASN

LEU

ALA

TYR

ASN

PRO

PHE

CYS

ALA

17

TYR

GLY

SER

PHE

SER

CYS

ALA

LEU

PRO

18

PRO

ALA

ASP

ASN

HIS

VAL

PRO

ALA

ILE

19

THR

ALA

GLY

GLU

ARG

VAL

ASP

ALA

ASP

LEU

20

GLU

Samples:

sample_1: hsr50.005, [U-100% 13C; U-100% 15N], 0.726 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_2: hsr50.009, [U-100% 13C; U-100% 15N; U-2H], 0.800 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_3: hsr50.007, [U-100% 13C; U-100% 15N], 0.674 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM

sample_conditions_1: pH: 6.5; 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 HNCO	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 1H-13C arom NOESY	sample_1	isotropic	sample_conditions_1
cCH_NOESY	sample_2	isotropic	sample_conditions_1
nNH_NOESY	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	anisotropic	sample_conditions_1
3D HA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

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

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

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

PDBStat v5.5-exp, Tejero; Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 900 MHz
Varian INOVA 600 MHz

PDB	2LOK 4DLH 4FJ4
EMBL	CAP13480
GB	AAG19211
REF	WP_010902507