BMRB Entry 17611

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PDB ID: 2n4b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17611
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of protein Rmet_5065 from Ralstonia metallidurans. Northeast Structural Genomics Consortium Target CrR115.

Deposition date:

2011-04-29

Original release date:

2011-06-01

Authors:

Ramelot, Theresa; Yang, Yunhuang; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rajesh, Nair; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Title: Solution NMR structure of protein Rmet_5065 from Ralstonia metallidurans. Northeast Structural Genomics Consortium Target CrR115." .

Assembly members:

Assembly members:
Rmet_5065, polymer, 142 residues, 16136.968 Da.

Natural source:

Natural source: Common Name: Ralstonia metallidurans Taxonomy ID: 119219 Superkingdom: Bacteria Kingdom: not available Genus/species: Ralstonia metallidurans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rmet_5065: MNITVETTVAAPVGKVWRAY TTPEDIKQWNAASDDWHTTA ATVDLREGGAFSSRMEAKDG SMGFDFAGTYTKVVENKRIE YAFGDRTAKVEFLEAPQGVT VRVSFVAETEYPVEQQQQGW QAILNNFKRHVESHLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	624
15N chemical shifts	159
1H chemical shifts	958

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein Rmet_5065	1

Entities:

Entity 1, protein Rmet_5065 142 residues - 16136.968 Da.

1

MET

ASN

ILE

THR

VAL

GLU

THR

VAL

ALA

2

ALA

PRO

VAL

GLY

LYS

VAL

TRP

ARG

ALA

TYR

3

THR

PRO

GLU

ASP

ILE

LYS

GLN

TRP

ASN

4

ALA

SER

ASP

TRP

HIS

THR

ALA

5

ALA

THR

VAL

ASP

LEU

ARG

GLU

GLY

ALA

6

PHE

SER

ARG

MET

GLU

ALA

LYS

ASP

GLY

7

SER

MET

GLY

PHE

ASP

PHE

ALA

GLY

THR

TYR

8

THR

LYS

VAL

GLU

ASN

LYS

ARG

ILE

GLU

9

TYR

ALA

PHE

GLY

ASP

ARG

THR

ALA

LYS

VAL

10

GLU

PHE

LEU

GLU

ALA

PRO

GLN

GLY

VAL

THR

11

VAL

ARG

VAL

SER

PHE

VAL

ALA

GLU

THR

GLU

12

TYR

PRO

VAL

GLU

GLN

GLY

TRP

13

GLN

ALA

ILE

LEU

ASN

PHE

LYS

ARG

HIS

14

VAL

GLU

SER

HIS

LEU

GLU

HIS

15

HIS

Samples:

NC_sample: protein, [U-100% 13C; U-100% 15N], 1.3 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; H2O 90%; D2O 10%

NC5_sample: protein, U-100% 15N and 5% 13C biosynthetically directed, 1.1 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC_sample_in_D2O: protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; DTT 10 ± 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY_aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY_arom	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC-NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC-aromatic	NC_sample	isotropic	sample_conditions_1
2D 1H-15N hetNOE	NC5_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC_His	NC5_sample	isotropic	sample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance III 850 MHz

PDB	2LCG 2N4A 2N4B
GB	ABF11927 EKZ95695
REF	WP_008651999 WP_011519477 WP_017515048 WP_029306526 WP_035883904