BMRB Entry 34317

Name: Structure of human SRSF1 RRM1 bound to AACAAA RNA
Published: 2020-11-12

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PDB ID: 6hpj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34317
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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:

Structure of human SRSF1 RRM1 bound to AACAAA RNA

Deposition date:

2018-09-21

Original release date:

2020-11-12

Authors:

Allain, F.; Clery, A.

Citation:

Citation: Clery, Antoine; Krepl, Miroslav; Nguyen, Cristina; Moursy, Ahmed; Jorjani, Hadi; Katsantoni, Maria; Okoniewski, Michal; Mittal, Nitish; Zavolan, Mihaela; Sponer, Jiri; Allain, Frederic H-T. "Structure of SRSF1 RRM1 bound to RNA reveals an unexpected bimodal mode of interaction and explains its involvement in SMN1 exon7 splicing" Nat. Commun. 12, 428-428 (2021).
PubMed: 33462199

Assembly members:

Assembly members:
entity_1, polymer, 161 residues, 17956.693 Da.
entity_2, polymer, 6 residues, 1906.253 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTEGSHH HHHHMSGGGVIRGPAGNNDC RIYVGNLPPDIRTKDIEDVF SKYGAIRDIDLKNRRGGPPF AFVEFEDPRDAEDAVSGRDG YDYDGYRLRVEFPRSGRGTG R
entity_2: AACAAA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	213
15N chemical shifts	74
1H chemical shifts	557

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 161 residues - 17956.693 Da.

1

MET

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

GLY

SER

HIS

7

HIS

MET

SER

GLY

VAL

8

ILE

ARG

GLY

PRO

ALA

GLY

ASN

ASP

CYS

9

ARG

ILE

TYR

VAL

GLY

ASN

LEU

PRO

ASP

10

ILE

ARG

THR

LYS

ASP

ILE

GLU

ASP

VAL

PHE

11

SER

LYS

TYR

GLY

ALA

ILE

ARG

ASP

ILE

ASP

12

LEU

LYS

ASN

ARG

GLY

PRO

PHE

13

ALA

PHE

VAL

GLU

PHE

GLU

ASP

PRO

ARG

ASP

14

ALA

GLU

ASP

ALA

VAL

SER

GLY

ARG

ASP

GLY

15

TYR

ASP

TYR

ASP

GLY

TYR

ARG

LEU

ARG

VAL

16

GLU

PHE

PRO

ARG

SER

GLY

ARG

GLY

THR

GLY

17

ARG

Entity 2, entity_2 6 residues - 1906.253 Da.

1

A

C

A

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1

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BMRB Entry 34317

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: