BMRB Entry 34560

Name: Solution structure of U1-A RRM2 (190-282)
Published: 2021-02-01

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PDB ID: 7aep
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34560
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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:

Solution structure of U1-A RRM2 (190-282)

Deposition date:

2020-09-18

Original release date:

2021-02-01

Authors:

Campagne, S.; Allain, F.

Citation:

Citation: Campagne, Sebastien; de Vries, Tebbe; Malard, Florian; Afanasyev, Pavel; Dorn, Georg; Dedic, Emil; Kohlbrecher, Joachim; Boehringer, Daniel; Clery, Antoine; Allain, Frederic H-T. "An in vitro reconstituted U1 snRNP allows the study of the disordered regions of the particle and the interactions with proteins and ligands" Nucleic Acids Res. 49, e63-e63 (2021).
PubMed: 33677607

Assembly members:

Assembly members:
entity_1, polymer, 126 residues, 13775.973 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPGQPPYMPPPGMIPPPGLA PGQIPPGAMPPQQLMPGQMP PAQPLSENPPNHILFLTNLP EETNELMLSMLFNQFPGFKE VRLVPGRHDIAFVEFDNEVQ AGAARDALQGFKITQNNAMK ISFAKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	492
15N chemical shifts	112
1H chemical shifts	718

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 126 residues - 13775.973 Da.

1

MET

PRO

GLY

GLN

PRO

TYR

MET

PRO

2

PRO

GLY

MET

ILE

PRO

GLY

LEU

ALA

3

PRO

GLY

GLN

ILE

PRO

GLY

ALA

MET

PRO

4

PRO

GLN

LEU

MET

PRO

GLY

GLN

MET

PRO

5

PRO

ALA

GLN

PRO

LEU

SER

GLU

ASN

PRO

6

ASN

HIS

ILE

LEU

PHE

LEU

THR

ASN

LEU

PRO

7

GLU

THR

ASN

GLU

LEU

MET

LEU

SER

MET

8

LEU

PHE

ASN

GLN

PHE

PRO

GLY

PHE

LYS

GLU

9

VAL

ARG

LEU

VAL

PRO

GLY

ARG

HIS

ASP

ILE

10

ALA

PHE

VAL

GLU

PHE

ASP

ASN

GLU

VAL

GLN

11

ALA

GLY

ALA

ARG

ASP

ALA

LEU

GLN

GLY

12

PHE

LYS

ILE

THR

GLN

ASN

ALA

MET

LYS

13

ILE

SER

PHE

ALA

LYS

Samples:

sample_1: entity_1 mM; NaPO4 10 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	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
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

Amber v20, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.94, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.9, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - peak picking

NMR spectrometers:

Bruker 600 AVIII 600 MHz
Bruker 900 AVII 900 MHz

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