BMRB Entry 27885

Name: Backbone 1H, 13C, and 15N chemical shift assignments for the N-terminal domain of Sfr1
Published: 2020-03-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27885

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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 the N-terminal domain of Sfr1

Deposition date:

2019-04-27

Original release date:

2020-03-18

Authors:

Sakakura, Masayoshi; Kurihara, Misato; Ito, Kentaro; Maki, Takahisa; Argunhan, Bilge; Iwasaki, Hiroshi; Takahashi, Hideo

Citation:

Citation: Argunhan, Bilge; Sakakura, Masayoshi; Afshar, Negar; Kurihara, Misato; Ito, Kentaro; Maki, Takahisa; Kanamaru, Shuji; Murayama, Yasuto; Tsubouchi, Hideo; Takahashi, Masayuki; Takahashi, Hideo; Iwasaki, Hiroshi. "Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex" Elife 9, e52566-e52566 (2020).
PubMed: 32204793

Assembly members:

Assembly members:
Sfr1N, polymer, 176 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBKN220

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sfr1N: MSQTINSELNENATSQCKED LKVSLSESDLRDSQGQLGIE NPPKCNNSGNHSDNLGFIEQ SETVHPENEKALTPDLRDTK IHTSLPITTPFSKKRAREAK NILLKPFKSPLRQTASPQVA DTNLKPSLAVTNLNSDETNT SSEPVTSPLRTTPNSIKRQK RLFKSPISNCLNPKSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	515
15N chemical shifts	157
1H chemical shifts	157

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sfr1N	1

Entities:

Entity 1, Sfr1N 176 residues - Formula weight is not available

1

MET

SER

GLN

THR

ILE

ASN

SER

GLU

LEU

ASN

2

GLU

ASN

ALA

THR

SER

GLN

CYS

LYS

GLU

ASP

3

LEU

LYS

VAL

SER

LEU

SER

GLU

SER

ASP

LEU

4

ARG

ASP

SER

GLN

GLY

GLN

LEU

GLY

ILE

GLU

5

ASN

PRO

LYS

CYS

ASN

SER

GLY

ASN

6

HIS

SER

ASP

ASN

LEU

GLY

PHE

ILE

GLU

GLN

7

SER

GLU

THR

VAL

HIS

PRO

GLU

ASN

GLU

LYS

8

ALA

LEU

THR

PRO

ASP

LEU

ARG

ASP

THR

LYS

9

ILE

HIS

THR

SER

LEU

PRO

ILE

THR

PRO

10

PHE

SER

LYS

ARG

ALA

ARG

GLU

ALA

LYS

11

ASN

ILE

LEU

LYS

PRO

PHE

LYS

SER

PRO

12

LEU

ARG

GLN

THR

ALA

SER

PRO

GLN

VAL

ALA

13

ASP

THR

ASN

LEU

LYS

PRO

SER

LEU

ALA

VAL

14

THR

ASN

LEU

ASN

SER

ASP

GLU

THR

ASN

THR

15

SER

GLU

PRO

VAL

THR

SER

PRO

LEU

ARG

16

THR

PRO

ASN

SER

ILE

LYS

ARG

GLN

LYS

17

ARG

LEU

PHE

LYS

SER

PRO

ILE

SER

ASN

CYS

18

LEU

ASN

PRO

LYS

SER

ASP

Samples:

sample_1: Sfr1N, [U-13C; U-15N], 0.175 mM; sodium phosphate 20 mM; sodium chloride 25 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.05 M; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

NMRPipe v2012.090.12.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.134, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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