BMRB Entry 18180

Name: Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11.
Published: 2012-01-12

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PDB ID: 2lnu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18180
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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 rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11.

Deposition date:

2012-01-05

Original release date:

2012-01-12

Authors:

Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11." To be published ., .-..

Assembly members:

Assembly members:
HmR11, polymer, 185 residues, 21399.959 Da.

Natural source:

Natural source: Common Name: Haloarcula marismortui Taxonomy ID: 2238 Superkingdom: Archaea Kingdom: not available Genus/species: Haloarcula marismortui

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HmR11: MDEDTEDWETQLQANRDEKD RFFSEHRQSPIPPEERDDFD GLSYFDPDPDYRVEATVTVH ETPESVDLETSDDRTVRYLH VATLSFDLDGESRDLHAFRQ AADESRTLFVPFRDKTTGQQ SYDGGRYMELEPDRDLSDGD EITLDFNLAYSPFCAYSDTF SCPLPPESNWLETAVTAGER TDLEH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	803
15N chemical shifts	197
1H chemical shifts	1209

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HmR11	1

Entities:

Entity 1, HmR11 185 residues - 21399.959 Da.

1

MET

ASP

GLU

ASP

THR

GLU

ASP

TRP

GLU

THR

2

GLN

LEU

GLN

ALA

ASN

ARG

ASP

GLU

LYS

ASP

3

ARG

PHE

SER

GLU

HIS

ARG

GLN

SER

PRO

4

ILE

PRO

GLU

ARG

ASP

PHE

ASP

5

GLY

LEU

SER

TYR

PHE

ASP

PRO

ASP

PRO

ASP

6

TYR

ARG

VAL

GLU

ALA

THR

VAL

THR

VAL

HIS

7

GLU

THR

PRO

GLU

SER

VAL

ASP

LEU

GLU

THR

8

SER

ASP

ARG

THR

VAL

ARG

TYR

LEU

HIS

9

VAL

ALA

THR

LEU

SER

PHE

ASP

LEU

ASP

GLY

10

GLU

SER

ARG

ASP

LEU

HIS

ALA

PHE

ARG

GLN

11

ALA

ASP

GLU

SER

ARG

THR

LEU

PHE

VAL

12

PRO

PHE

ARG

ASP

LYS

THR

GLY

GLN

13

SER

TYR

ASP

GLY

ARG

TYR

MET

GLU

LEU

14

GLU

PRO

ASP

ARG

ASP

LEU

SER

ASP

GLY

ASP

15

GLU

ILE

THR

LEU

ASP

PHE

ASN

LEU

ALA

TYR

16

SER

PRO

PHE

CYS

ALA

TYR

SER

ASP

THR

PHE

17

SER

CYS

PRO

LEU

PRO

GLU

SER

ASN

TRP

18

LEU

GLU

THR

ALA

VAL

THR

ALA

GLY

GLU

ARG

19

THR

ASP

LEU

GLU

HIS

Samples:

sample_1: HmR11-1, [U-100% 13C; U-100% 15N], 0.7 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM

sample_2: HmR11-1, [U-5% 13C; U-100% 15N], 1.2 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM

sample_3: HmR11, [U-5% 13C; U-100% 15N], 0.75 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 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
3D 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D hetnoe	sample_2	isotropic	sample_conditions_1
1D T1 inv.rec	sample_2	isotropic	sample_conditions_1
1D T2 CPMG	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC highres	sample_2	isotropic	sample_conditions_1
Jmod 15N TROSY	sample_3	anisotropic	sample_conditions_1
jmod 15N TROSY	sample_3	anisotropic	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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - 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

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

PDB	2LNU
GB	AAV45400 EMA13016 EMA22096
REF	WP_004962568 WP_007188424 WP_011222974