BMRB Entry 16991

Name: Solution NMR Structure of the N-terminal Domain of Putative ATP-dependent DNA Helicase RecG-related Protein from Nitrosomonas europaea, Northeast Structural Genomics Consortium Target NeR70A
Published: 2010-08-10

Click here to enlarge.

PDB ID: 2kyy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16991
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR Structure of the N-terminal Domain of Putative ATP-dependent DNA Helicase RecG-related Protein from Nitrosomonas europaea, Northeast Structural Genomics Consortium Target NeR70A

Deposition date:

2010-06-09

Original release date:

2010-08-10

Authors:

Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Maglaqui, Melissa; Ciccosanti, Colleen; Hamilton, Keith; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Maglaqui, Melissa; Ciccosanti, Colleen; Hamilton, Keith; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR Structure of the N-terminal Domain of Putative ATP-dependent DNA Helicase RecG-related Protein from Nitrosomonas europaea" To be published ., .-..

Assembly members:

Assembly members:
NeR70A, polymer, 153 residues, 16781.168 Da.

Natural source:

Natural source: Common Name: N. europaea Taxonomy ID: 915 Superkingdom: Bacteria Kingdom: not available Genus/species: Nitrosomonas europaea

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NeR70A: MRSATDLLDELNAVDESARI EAKRASDMGKSVMETVIAFA NEPGLDGGYLLLGVDWAIND KGDTVYRPVGLPDPDKVQRD LASQCASMLNVALRPEMQLE QVGGKTLLVVYVPEADVTHK PIYKKATGLPGGAYRRIGSS DQRCVLEHHHHHH

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- N
- Cali
- Caro

Data type	Count
13C chemical shifts	642
15N chemical shifts	153
1H chemical shifts	1032
residual dipolar couplings	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NeR70A	1

Entities:

Entity 1, NeR70A 153 residues - 16781.168 Da.

Residues 1-145 correspond to the native protein. Residues 146-153 represent a non-native affinity tag.

1

MET

ARG

SER

ALA

THR

ASP

LEU

ASP

GLU

2

LEU

ASN

ALA

VAL

ASP

GLU

SER

ALA

ARG

ILE

3

GLU

ALA

LYS

ARG

ALA

SER

ASP

MET

GLY

LYS

4

SER

VAL

MET

GLU

THR

VAL

ILE

ALA

PHE

ALA

5

ASN

GLU

PRO

GLY

LEU

ASP

GLY

TYR

LEU

6

LEU

GLY

VAL

ASP

TRP

ALA

ILE

ASN

ASP

7

LYS

GLY

ASP

THR

VAL

TYR

ARG

PRO

VAL

GLY

8

LEU

PRO

ASP

PRO

ASP

LYS

VAL

GLN

ARG

ASP

9

LEU

ALA

SER

GLN

CYS

ALA

SER

MET

LEU

ASN

10

VAL

ALA

LEU

ARG

PRO

GLU

MET

GLN

LEU

GLU

11

GLN

VAL

GLY

LYS

THR

LEU

VAL

12

TYR

VAL

PRO

GLU

ALA

ASP

VAL

THR

HIS

LYS

13

PRO

ILE

TYR

LYS

ALA

THR

GLY

LEU

PRO

14

GLY

ALA

TYR

ARG

ILE

GLY

SER

15

ASP

GLN

ARG

CYS

VAL

LEU

GLU

HIS

16

HIS

Samples:

NC: NeR70A, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5: NeR70A, [U-5% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5-phage: NeR70A, [U-5% 13C; U-100% 15N], 0.6 mM; MES 13 mM; sodium chloride 66 mM; calcium chloride 3.3 mM; DTT 6.6 mM; sodium azide 0.013%; Pf1 phage 13.5 mg/ml; H2O 88%; D2O 12%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D 1H-15N LR-HSQC (Histidine)	NC	isotropic	sample_conditions_1
2D 1H-15N J-modulated HSQC	NC5	isotropic	sample_conditions_1
2D 1H-15N J-modulated HSQC	NC5-phage	anisotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

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

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

AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY v1.3.13, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection

VNMRJ v2.1B, Varian - collection

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PROSA v6.4, Guntert - processing

NMR spectrometers:

Bruker Avance 900 MHz
Varian INOVA 600 MHz
Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2KYY
EMBL	CAD86437
GB	ABM43720 EPZ14923 ESQ97118
REF	WP_011112980 WP_011806704 WP_021250010 WP_023446977 WP_033977893