BMRB Entry 16312

Name: Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C.
Published: 2009-06-11

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PDB ID: 2kj5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16312
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 a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C.

Deposition date:

2009-05-21

Original release date:

2009-06-11

Authors:

Mills, Jeffrey; Eletsky, Alexander; Ghosh, Arindam; Wang, Dongyang; Lee, Hsiau-Wei; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G. V. T.; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Mills, Jeffrey. "Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C." .

Assembly members:

Assembly members:
NmR46C, polymer, 116 residues, 13400.581 Da.

Natural source:

Natural source: Common Name: Nitrosospira multiformis Taxonomy ID: 1231 Superkingdom: Bacteria Kingdom: not available Genus/species: Nitrosospira multiformis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NmR46C: MAEKNAYTVAQLADEYFERM IAGRWKHPNIVRSRIEKDIK PAIGSLKVEDVKPRHIDDVL KAVMKRGAPSIANDTLRWLK RMFNYAIKRHIIEYNPAAAF DPGDAGGKLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
spectral_peak_list
- NNOESY
- CNOESY

Data type	Count
13C chemical shifts	392
15N chemical shifts	124
1H chemical shifts	830
residual dipolar couplings	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NmR46C	1

Entities:

Entity 1, NmR46C 116 residues - 13400.581 Da.

L46 is a sequence variation; Please add a "remark 999"

1

MET

ALA

GLU

LYS

ASN

ALA

TYR

THR

VAL

ALA

2

GLN

LEU

ALA

ASP

GLU

TYR

PHE

GLU

ARG

MET

3

ILE

ALA

GLY

ARG

TRP

LYS

HIS

PRO

ASN

ILE

4

VAL

ARG

SER

ARG

ILE

GLU

LYS

ASP

ILE

LYS

5

PRO

ALA

ILE

GLY

SER

LEU

LYS

VAL

GLU

ASP

6

VAL

LYS

PRO

ARG

HIS

ILE

ASP

VAL

LEU

7

LYS

ALA

VAL

MET

LYS

ARG

GLY

ALA

PRO

SER

8

ILE

ALA

ASN

ASP

THR

LEU

ARG

TRP

LEU

LYS

9

ARG

MET

PHE

ASN

TYR

ALA

ILE

LYS

ARG

HIS

10

ILE

GLU

TYR

ASN

PRO

ALA

PHE

11

ASP

PRO

GLY

ASP

ALA

GLY

LYS

LEU

GLU

12

HIS

Samples:

NC: NmR46C, [U-98% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

NC5: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

NC5ani: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

sample_conditions_1: ionic strength: 430 mM; 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 HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5	isotropic	sample_conditions_1
3D sim 15N,13C NOESY	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
(4,3)D HNCABCA	NC	isotropic	sample_conditions_1
GFT (4,3)D CABCA(CO)NH	NC	isotropic	sample_conditions_1
GFT (4,3)D HABCAB(CO)NH	NC	isotropic	sample_conditions_1
GFT (4,3)D arom. HCCH	NC	isotropic	sample_conditions_1
GFT (4,3)D aliph. HCCH	NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5ani	anisotropic	sample_conditions_1
2D 1H-15N TROSY	NC5ani	anisotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

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

SPSCAN, Glaser - processing

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

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment, refinement, structure solution

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2KJ5
GB	ABB73373
REF	WP_011379428