BMRB Entry 15642

Name: Solution structure of the aminoterminal domain of E. coli NusG
Published: 2009-06-10

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PDB ID: 2k06
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/BMR15642
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the aminoterminal domain of E. coli NusG

Deposition date:

2008-01-25

Original release date:

2009-06-10

Authors:

Schweimer, Kristian; Scheckenhofer, Ulrich; Roesch, Paul

Citation:

Citation: Mooney, Rachel Anne; Schweimer, Kristian; Roesch, Paul; Gottesman, Max; Landick, Robert. "Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators." J. Mol. Biol. 391, 341-358 (2009).
PubMed: 19500594

Assembly members:

Assembly members:
NusG, polymer, 123 residues, 14096.366 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NusG: MSEAPKKRWYVVQAFSGFEG RVATSLREHIKLHNMEDLFG EVMVPTEEVVEIRGGQRRKS ERKFFPGYVLVQMVMNDASW HLVRSVPRVMGFIGGTSDRP APISDKEVDAIMNRLQQVGD KPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	498
15N chemical shifts	122
1H chemical shifts	790

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NusG	1

Entities:

Entity 1, NusG 123 residues - 14096.366 Da.

1

MET

SER

GLU

ALA

PRO

LYS

ARG

TRP

TYR

2

VAL

GLN

ALA

PHE

SER

GLY

PHE

GLU

GLY

3

ARG

VAL

ALA

THR

SER

LEU

ARG

GLU

HIS

ILE

4

LYS

LEU

HIS

ASN

MET

GLU

ASP

LEU

PHE

GLY

5

GLU

VAL

MET

VAL

PRO

THR

GLU

VAL

6

GLU

ILE

ARG

GLY

GLN

ARG

LYS

SER

7

GLU

ARG

LYS

PHE

PRO

GLY

TYR

VAL

LEU

8

VAL

GLN

MET

VAL

MET

ASN

ASP

ALA

SER

TRP

9

HIS

LEU

VAL

ARG

SER

VAL

PRO

ARG

VAL

MET

10

GLY

PHE

ILE

GLY

THR

SER

ASP

ARG

PRO

11

ALA

PRO

ILE

SER

ASP

LYS

GLU

VAL

ASP

ALA

12

ILE

MET

ASN

ARG

LEU

GLN

VAL

GLY

ASP

13

LYS

PRO

ARG

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.4 mM; potassium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6.4; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 700 MHz

BMRB	15490
PDB	2JVV 2K06
DBJ	BAB38328 BAE73404 BAE77338 BAG79793 BAH61119
EMBL	CAD09492 CAG73137 CAH19518 CAL10413 CAL22339
GB	AAA24622 AAC43080 AAC76956 AAF33495 AAG59178
PIR	AB0934
REF	NP_312932 NP_418409 NP_457922 NP_463017 NP_709777
SP	P0AA01 P0AA02 P0AA03 P0AFG0 P0AFG1
AlphaFold	P0AA01 P0AA02 P0AA03 P0AFG0 P0AFG1