BMRB Entry 25016

Name: Solution structure of Y125F mutant of eRF1 N-domain
Published: 2015-06-15

Click here to enlarge.

PDB ID: 2mq6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25016
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:

Solution structure of Y125F mutant of eRF1 N-domain

Deposition date:

2014-06-12

Original release date:

2015-06-15

Authors:

Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin

Citation:

Citation: Pillay, Shubhadra; Li, Yan; Wong, Leo E; Pervushin, Konstantin. "Structural insights of eRF1 mutants and their correlation with stop codon recognition" ACS chemical biology ., .-..

Assembly members:

Assembly members:
entity, polymer, 142 residues, 15682.319 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET23(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADEFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NTSLFLCDNKFHTEALTALL SD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	441
15N chemical shifts	146
1H chemical shifts	975

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Y125F mutant of eRF1 N-domain	1

Entities:

Entity 1, Y125F mutant of eRF1 N-domain 142 residues - 15682.319 Da.

1

MET

ALA

ASP

PRO

SER

ALA

ASP

ARG

2

ASN

VAL

GLU

ILE

TRP

LYS

ILE

LYS

LEU

3

ILE

LYS

SER

LEU

GLU

ALA

ARG

GLY

ASN

4

GLY

THR

SER

MET

ILE

SER

LEU

ILE

PRO

5

PRO

LYS

ASP

GLN

ILE

SER

ARG

VAL

ALA

LYS

6

MET

LEU

ALA

ASP

GLU

PHE

GLY

THR

ALA

SER

7

ASN

ILE

LYS

SER

ARG

VAL

ASN

ARG

LEU

SER

8

VAL

LEU

GLY

ALA

ILE

THR

SER

VAL

GLN

9

ARG

LEU

LYS

LEU

TYR

ASN

LYS

VAL

PRO

10

ASN

GLY

LEU

VAL

TYR

CYS

GLY

THR

ILE

11

VAL

THR

GLU

GLY

LYS

GLU

LYS

VAL

12

ASN

ILE

ASP

PHE

GLU

PRO

PHE

LYS

PRO

ILE

13

ASN

THR

SER

LEU

PHE

LEU

CYS

ASP

ASN

LYS

14

PHE

HIS

THR

GLU

ALA

LEU

THR

ALA

LEU

15

SER

ASP

Samples:

sample_1: Y125F mutant of eRF1 N-domain, [U-99% 15N], 1 mM; MES 20 mM; potassium chloride 100 mM; DTT 2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz

BMRB	18092 19506 25020
PDB	1DT9 2LLX 2MQ6 2MQ9 3E1Y 3J5Y 4D5N 4D61
DBJ	BAA85489 BAC33839 BAE31210 BAE31619 BAE37589
EMBL	CAA37987 CAA57281 CAA57282 CAA78620 CAF90786
GB	AAA36665 AAB49726 AAD43966 AAH13717 AAH14269
REF	NP_001008345 NP_001069722 NP_001076236 NP_001084363 NP_001126989
SP	P35615 P62495 P62496 P62497 P62498
TPG	DAA27419
AlphaFold	P35615 P62495 P62496 P62497 P62498