BMRB Entry 30325

Name: NMR solution structure of KanY protein (ms6282) using two 4D-spectra
Published: 2018-01-29

Click here to enlarge.

PDB ID: 5wox
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30325
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:

NMR solution structure of KanY protein (ms6282) using two 4D-spectra

Deposition date:

2017-08-03

Original release date:

2018-01-29

Authors:

Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.

Citation:

Citation: Evangelidis, T.; Nerli, S.; Novacek, J.; Brereton, A.; Karplus, P.; Dotas, R.; Venditti, V.; Sgourakis, N.; Tripsianes, K.. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra" Nat. Commun. 9, 384-384 (2018).
PubMed: 29374165

Assembly members:

Assembly members:
Uncharacterized protein, polymer, 145 residues, 15285.261 Da.

Natural source:

Natural source: Common Name: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) Taxonomy ID: 246196 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium smegmatis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Uncharacterized protein: MGQVSAVSTVLINAEPAAVL AAISDYQTVRPKILSSHYSG YQVLEGGQGAGTVATWKLQA TKSRVRDVKATVDVAGHTVI EKDANSSLVSNWTVAPAGTG SSVNLKTTWTGAGGVKGFFE KTFAPLGLRRIQDEVLENLK KHVEG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	445
15N chemical shifts	152
1H chemical shifts	959

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 145 residues - 15285.261 Da.

1

MET

GLY

GLN

VAL

SER

ALA

VAL

SER

THR

VAL

2

LEU

ILE

ASN

ALA

GLU

PRO

ALA

VAL

LEU

3

ALA

ILE

SER

ASP

TYR

GLN

THR

VAL

ARG

4

PRO

LYS

ILE

LEU

SER

HIS

TYR

SER

GLY

5

TYR

GLN

VAL

LEU

GLU

GLY

GLN

GLY

ALA

6

GLY

THR

VAL

ALA

THR

TRP

LYS

LEU

GLN

ALA

7

THR

LYS

SER

ARG

VAL

ARG

ASP

VAL

LYS

ALA

8

THR

VAL

ASP

VAL

ALA

GLY

HIS

THR

VAL

ILE

9

GLU

LYS

ASP

ALA

ASN

SER

LEU

VAL

SER

10

ASN

TRP

THR

VAL

ALA

PRO

ALA

GLY

THR

GLY

11

SER

VAL

ASN

LEU

LYS

THR

TRP

THR

12

GLY

ALA

GLY

VAL

LYS

GLY

PHE

GLU

13

LYS

THR

PHE

ALA

PRO

LEU

GLY

LEU

ARG

14

ILE

GLN

ASP

GLU

VAL

LEU

GLU

ASN

LEU

LYS

15

LYS

HIS

VAL

GLU

GLY

Samples:

sample_1: KanY protein ms6282, [U-13C; U-15N], 1.2 mM; sodium phosphate 50 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
4D HC(CC TOCSY(CO))NH	sample_1	isotropic	sample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation

SPARKY, Goddard - peak picking

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

NMR spectrometers:

Bruker AvanceIII 850 MHz

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