BMRB Entry 17822

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F
Published: 2012-08-29

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PDB ID: 2lgt
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/BMR17822
MolProbity Validation Chart

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F

Deposition date:

2011-08-02

Original release date:

2012-08-29

Authors:

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

Citation:

Citation: Wong, Leo; Li, Yan; Pillay, Shubhadra; Frolova, Ludmila; Pervushin, Konstantin. "Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1" Nucleic Acids Res. 40, 5751-5765 (2012).
PubMed: 22383581

Assembly members:

Assembly members:
entity, polymer, 144 residues, 16079.768 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADEFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NQFMYFCDNKFHTEALTALL SDLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	488
15N chemical shifts	150
1H chemical shifts	1026

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	QFMF	1

Entities:

Entity 1, QFMF 144 residues - 16079.768 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

GLN

PHE

MET

TYR

PHE

CYS

ASP

ASN

LYS

14

PHE

HIS

THR

GLU

ALA

LEU

THR

ALA

LEU

15

SER

ASP

LEU

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	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

BMRB	18092 19506
PDB	1DT9 2LGT 2LLX 3E1Y 3J5Y 4D5N 4D61
DBJ	BAA85489 BAC33839 BAE37589 BAE41096 BAE41644
EMBL	CAA37987 CAA57281 CAA57282 CAA78620 CAF90786
GB	AAB49726 AAD43966 AAH44515 AAH61387 AAH66583
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

BMRB Entry 17822

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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