BMRB Entry 26518

Name: NMR solution structure of the putative transfer protein TraH from Gram-positive conjugative plasmid pIP501
Published: 2016-07-13

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PDB ID: 5aiw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26518
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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:

NMR solution structure of the putative transfer protein TraH from Gram-positive conjugative plasmid pIP501

Deposition date:

2015-02-23

Original release date:

2016-07-13

Authors:

Meyer, Niels Helge; Fercher, C.; Zangger, K.; Keller, W.

Citation:

Citation: Fercher, Christian; Probst, Ines; Kohler, Verena; Goessweiner-Mohr, Nikolaus; Arends, Karsten; Grohmann, Elisabeth; Zangger, Klaus; Meyer, N. Helge; Keller, Walter. "VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis" Sci. Rep. 6, 24643-24643 (2016).
PubMed: 27103580

Assembly members:

Assembly members:
TRAH, polymer, 128 residues, 14896.3656 Da.

Natural source:

Natural source: Common Name: Enterococcus faecalis Taxonomy ID: 1351 Superkingdom: Bacteria Kingdom: not available Genus/species: Enterococcus faecalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI BL21 Vector: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRAH: SNTNQSESEKIIKEFYKTVY NYEKSQKEISMTTVKELATD NVYQELQNEINVNNSYSPQQ NTIQKSSVNENEIKILAYES KDNSQQYLVTAPIHQVFNGT KNDFEINQLIQIKNQKITQR TTIQLGEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	563
15N chemical shifts	147
1H chemical shifts	925

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRAH	1

Entities:

Entity 1, TRAH 128 residues - 14896.3656 Da.

1

SER

ASN

THR

ASN

GLN

SER

GLU

SER

GLU

LYS

2

ILE

LYS

GLU

PHE

TYR

LYS

THR

VAL

TYR

3

ASN

TYR

GLU

LYS

SER

GLN

LYS

GLU

ILE

SER

4

MET

THR

VAL

LYS

GLU

LEU

ALA

THR

ASP

5

ASN

VAL

TYR

GLN

GLU

LEU

GLN

ASN

GLU

ILE

6

ASN

VAL

ASN

SER

TYR

SER

PRO

GLN

7

ASN

THR

ILE

GLN

LYS

SER

VAL

ASN

GLU

8

ASN

GLU

ILE

LYS

ILE

LEU

ALA

TYR

GLU

SER

9

LYS

ASP

ASN

SER

GLN

TYR

LEU

VAL

THR

10

ALA

PRO

ILE

HIS

GLN

VAL

PHE

ASN

GLY

THR

11

LYS

ASN

ASP

PHE

GLU

ILE

ASN

GLN

LEU

ILE

12

GLN

ILE

LYS

ASN

GLN

LYS

ILE

THR

GLN

ARG

13

THR

ILE

GLN

LEU

GLY

GLU

Samples:

sample_1: TRAH, [U-13C; U-15N], 0.5 mM; PO4 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 200.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
NOESY	sample_1	solution	sample_conditions_1

Software:

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

CYANA vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

RECOORD_CNS vany, A.J. NEDERVEEN, J.F. DORELEIJERS, W.F. - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks