BMRB Entry 11546

Name: 1H, 15N and 13C resonance assignments of the conserved domain in the middle of Schizosaccharomyces pombe SAPK-interacting protein 1
Published: 2015-07-27

Click here to enlarge.

PDB ID: 2rvk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11546
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: 1H, 15N and 13C resonance assignments of the conserved domain in the middle of Schizosaccharomyces pombe SAPK-interacting protein 1 PubMed: 25428765

Deposition date: 2013-11-27 Original release date: 2015-07-27

Authors: Kataoka, Saori; Furuita, Kyoko; Hattori, Yoshikazu; Kobayashi, Naohiro; Ikegami, Takahisa; Shiozaki, Kazuhiro; Fujiwara, Toshimichi; Kojima, Chojiro

Citation: Furuita, Kyoko; Kataoka, Saori; Hattori, Yoshikazu; Kobayashi, Naohiro; Ikegami, Takahisa; Shiozaki, Kazuhiro; Fujiwara, Toshimichi; Kojima, Chojiro. "Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints" Biomol. NMR Assignments 61, 55-64 (2015).

Assembly members:
sin1, polymer, 160 residues, 17037.0 Da.

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

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

Entity Sequences (FASTA):
sin1: GPGHMGSVSNAKAPTSALRA LLEHKENSSQNGPLAENFAT FSGHAESNALRLNIYFPSSE SPSKPLFVELRKNVLVSEAI GYILLQYVNQQLVPPIEDEA QNPNYWNLRIVEDDGELDED FPALDRVGPLSKFGFDAFAL VKATPAQIKENQAAYPFKSK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	559
15N chemical shifts	144
1H chemical shifts	890

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

1	GLY	PRO	GLY	HIS	MET	GLY	SER	VAL	SER	ASN
2	ALA	LYS	ALA	PRO	THR	SER	ALA	LEU	ARG	ALA
3	LEU	LEU	GLU	HIS	LYS	GLU	ASN	SER	SER	GLN
4	ASN	GLY	PRO	LEU	ALA	GLU	ASN	PHE	ALA	THR
5	PHE	SER	GLY	HIS	ALA	GLU	SER	ASN	ALA	LEU
6	ARG	LEU	ASN	ILE	TYR	PHE	PRO	SER	SER	GLU
7	SER	PRO	SER	LYS	PRO	LEU	PHE	VAL	GLU	LEU
8	ARG	LYS	ASN	VAL	LEU	VAL	SER	GLU	ALA	ILE
9	GLY	TYR	ILE	LEU	LEU	GLN	TYR	VAL	ASN	GLN
10	GLN	LEU	VAL	PRO	PRO	ILE	GLU	ASP	GLU	ALA
11	GLN	ASN	PRO	ASN	TYR	TRP	ASN	LEU	ARG	ILE
12	VAL	GLU	ASP	ASP	GLY	GLU	LEU	ASP	GLU	ASP
13	PHE	PRO	ALA	LEU	ASP	ARG	VAL	GLY	PRO	LEU
14	SER	LYS	PHE	GLY	PHE	ASP	ALA	PHE	ALA	LEU
15	VAL	LYS	ALA	THR	PRO	ALA	GLN	ILE	LYS	GLU
16	ASN	GLN	ALA	ALA	TYR	PRO	PHE	LYS	SER	LYS

Name	Sample	Sample state	Sample conditions
3D HNCO	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(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

EMBL	CAB66311
GB	AAD37449
PIR	T51293
REF	NP_594703
SP	Q9P7Y9

Biological Magnetic Resonance Data Bank

BMRB Entry 11546

Title: 1H, 15N and 13C resonance assignments of the conserved domain in the middle of Schizosaccharomyces pombe SAPK-interacting protein 1 PubMed: 25428765

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	PRO	GLY	HIS	MET	GLY	SER	VAL	SER	ASN
2	ALA	LYS	ALA	PRO	THR	SER	ALA	LEU	ARG	ALA
3	LEU	LEU	GLU	HIS	LYS	GLU	ASN	SER	SER	GLN
4	ASN	GLY	PRO	LEU	ALA	GLU	ASN	PHE	ALA	THR
5	PHE	SER	GLY	HIS	ALA	GLU	SER	ASN	ALA	LEU
6	ARG	LEU	ASN	ILE	TYR	PHE	PRO	SER	SER	GLU
7	SER	PRO	SER	LYS	PRO	LEU	PHE	VAL	GLU	LEU
8	ARG	LYS	ASN	VAL	LEU	VAL	SER	GLU	ALA	ILE
9	GLY	TYR	ILE	LEU	LEU	GLN	TYR	VAL	ASN	GLN
10	GLN	LEU	VAL	PRO	PRO	ILE	GLU	ASP	GLU	ALA
11	GLN	ASN	PRO	ASN	TYR	TRP	ASN	LEU	ARG	ILE
12	VAL	GLU	ASP	ASP	GLY	GLU	LEU	ASP	GLU	ASP
13	PHE	PRO	ALA	LEU	ASP	ARG	VAL	GLY	PRO	LEU
14	SER	LYS	PHE	GLY	PHE	ASP	ALA	PHE	ALA	LEU
15	VAL	LYS	ALA	THR	PRO	ALA	GLN	ILE	LYS	GLU
16	ASN	GLN	ALA	ALA	TYR	PRO	PHE	LYS	SER	LYS

1	GLY	PRO	GLY	HIS	MET	GLY	SER	VAL	SER	ASN
2	ALA	LYS	ALA	PRO	THR	SER	ALA	LEU	ARG	ALA
3	LEU	LEU	GLU	HIS	LYS	GLU	ASN	SER	SER	GLN
4	ASN	GLY	PRO	LEU	ALA	GLU	ASN	PHE	ALA	THR
5	PHE	SER	GLY	HIS	ALA	GLU	SER	ASN	ALA	LEU
6	ARG	LEU	ASN	ILE	TYR	PHE	PRO	SER	SER	GLU
7	SER	PRO	SER	LYS	PRO	LEU	PHE	VAL	GLU	LEU
8	ARG	LYS	ASN	VAL	LEU	VAL	SER	GLU	ALA	ILE
9	GLY	TYR	ILE	LEU	LEU	GLN	TYR	VAL	ASN	GLN
10	GLN	LEU	VAL	PRO	PRO	ILE	GLU	ASP	GLU	ALA
11	GLN	ASN	PRO	ASN	TYR	TRP	ASN	LEU	ARG	ILE
12	VAL	GLU	ASP	ASP	GLY	GLU	LEU	ASP	GLU	ASP
13	PHE	PRO	ALA	LEU	ASP	ARG	VAL	GLY	PRO	LEU
14	SER	LYS	PHE	GLY	PHE	ASP	ALA	PHE	ALA	LEU
15	VAL	LYS	ALA	THR	PRO	ALA	GLN	ILE	LYS	GLU
16	ASN	GLN	ALA	ALA	TYR	PRO	PHE	LYS	SER	LYS

1	GLY	PRO	GLY	HIS	MET	GLY	SER	VAL	SER	ASN
2	ALA	LYS	ALA	PRO	THR	SER	ALA	LEU	ARG	ALA
3	LEU	LEU	GLU	HIS	LYS	GLU	ASN	SER	SER	GLN
4	ASN	GLY	PRO	LEU	ALA	GLU	ASN	PHE	ALA	THR
5	PHE	SER	GLY	HIS	ALA	GLU	SER	ASN	ALA	LEU
6	ARG	LEU	ASN	ILE	TYR	PHE	PRO	SER	SER	GLU
7	SER	PRO	SER	LYS	PRO	LEU	PHE	VAL	GLU	LEU
8	ARG	LYS	ASN	VAL	LEU	VAL	SER	GLU	ALA	ILE
9	GLY	TYR	ILE	LEU	LEU	GLN	TYR	VAL	ASN	GLN
10	GLN	LEU	VAL	PRO	PRO	ILE	GLU	ASP	GLU	ALA
11	GLN	ASN	PRO	ASN	TYR	TRP	ASN	LEU	ARG	ILE
12	VAL	GLU	ASP	ASP	GLY	GLU	LEU	ASP	GLU	ASP
13	PHE	PRO	ALA	LEU	ASP	ARG	VAL	GLY	PRO	LEU
14	SER	LYS	PHE	GLY	PHE	ASP	ALA	PHE	ALA	LEU
15	VAL	LYS	ALA	THR	PRO	ALA	GLN	ILE	LYS	GLU
16	ASN	GLN	ALA	ALA	TYR	PRO	PHE	LYS	SER	LYS