BMRB Entry 27499

Name: SFRS1-RRM1
Published: 2018-07-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27499

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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:

SFRS1-RRM1

Deposition date:

2018-05-31

Original release date:

2018-07-31

Authors:

Serrano, Pedro; Wuthrich, Kurt

Citation:

Citation: Wuthrich, Kurt; Serrano, Pedro. "NMR assignments of the the protein SFRS1-RRM1" .

Assembly members:

Assembly members:
SFRS1-RRM1, polymer, 111 residues, Formula weight is not available

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: pET28B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SFRS1-RRM1: GGSSGSSGMSGGGVIRGPAG NNDCRIYVGNLPPDIRTKDI EDVFYKYGAIRDIDLKNRRG GPPFAFVEFEDPRDAEDAVY GRDGYDYDGYRLRVEFPRSG RGTGSGSGPSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	110
15N chemical shifts	56
1H chemical shifts	59

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	sfrs1-RRM1	1

Entities:

Entity 1, sfrs1-RRM1 111 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

SER

2

GLY

VAL

ILE

ARG

GLY

PRO

ALA

GLY

3

ASN

ASP

CYS

ARG

ILE

TYR

VAL

GLY

ASN

4

LEU

PRO

ASP

ILE

ARG

THR

LYS

ASP

ILE

5

GLU

ASP

VAL

PHE

TYR

LYS

TYR

GLY

ALA

ILE

6

ARG

ASP

ILE

ASP

LEU

LYS

ASN

ARG

GLY

7

GLY

PRO

PHE

ALA

PHE

VAL

GLU

PHE

GLU

8

ASP

PRO

ARG

ASP

ALA

GLU

ASP

ALA

VAL

TYR

9

GLY

ARG

ASP

GLY

TYR

ASP

TYR

ASP

GLY

TYR

10

ARG

LEU

ARG

VAL

GLU

PHE

PRO

ARG

SER

GLY

11

ARG

GLY

THR

GLY

SER

GLY

SER

GLY

PRO

SER

12

SER

Samples:

sample_1: SFRS1-RRM1, [U-99% 13C; U-99% 15N], 0.5 mM; D2O, [U-99% 2H], 5%; sodium azide 0.1%; sodium chloride 150 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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
APSY CACBCoNH	sample_1	isotropic	sample_conditions_1
APSY HACANH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 600 MHz

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