BMRB Entry 30327

Name: NMR solution structure of Rtt103 (RTT) protein using two 4D-spectra
Published: 2018-01-29

Click here to enlarge.

PDB ID: 5woz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30327
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 Rtt103 (RTT) protein 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:
Regulator of Ty1 transposition protein 103, polymer, 138 residues, 16132.574 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Regulator of Ty1 transposition protein 103: SEQFTTKLNTLEDSQESISS ASKWLLLQYRDAPKVAEMWK EYMLRPSVNTRRKLLGLYLM NHVVQQAKGQKIIQFQDSFG KVAAEVLGRINQEFPRDLKK KLSRVVNILKERNIFSKQVV NDIERSLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	459
15N chemical shifts	144
1H chemical shifts	978

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_1 138 residues - 16132.574 Da.

1

SER

GLU

GLN

PHE

THR

LYS

LEU

ASN

THR

2

LEU

GLU

ASP

SER

GLN

GLU

SER

ILE

SER

3

ALA

SER

LYS

TRP

LEU

GLN

TYR

ARG

4

ASP

ALA

PRO

LYS

VAL

ALA

GLU

MET

TRP

LYS

5

GLU

TYR

MET

LEU

ARG

PRO

SER

VAL

ASN

THR

6

ARG

LYS

LEU

GLY

LEU

TYR

LEU

MET

7

ASN

HIS

VAL

GLN

ALA

LYS

GLY

GLN

8

LYS

ILE

GLN

PHE

GLN

ASP

SER

PHE

GLY

9

LYS

VAL

ALA

GLU

VAL

LEU

GLY

ARG

ILE

10

ASN

GLN

GLU

PHE

PRO

ARG

ASP

LEU

LYS

11

LYS

LEU

SER

ARG

VAL

ASN

ILE

LEU

LYS

12

GLU

ARG

ASN

ILE

PHE

SER

LYS

GLN

VAL

13

ASN

ASP

ILE

GLU

ARG

SER

LEU

ALA

14

LEU

GLU

HIS

Samples:

sample_1: Rtt103 (RTT) protein, [U-13C; U-15N], 0.8 mM; Potassium Phosphate 35 mM; KCl 100 mM

sample_conditions_1: ionic strength: 35 mM; pH: 6.8; 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:

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

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

SPARKY, Goddard - peak picking

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