BMRB Entry 17199

Name: Solution structure of Rap1-Taz1 fusion protein
Published: 2011-03-30

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PDB ID: 2l3n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17199
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Rap1-Taz1 fusion protein

Deposition date:

2010-09-19

Original release date:

2011-03-30

Authors:

Zhou, Zi-ren; Wang, Feng; Chen, Yong; Lei, Ming; Hu, Hong-yu

Citation:

Citation: Chen, Yong; Rai, Rekha; Zhou, Zi-Ren; Kanoh, Junko; Ribeyre, Cyril; Yang, Yuting; Zheng, Hong; Damay, Pascal; Wang, Feng; Tsujii, Hisayo; Hiraoka, Yasushi; Shore, David; Hu, Hong-Yu; Chang, Sandy; Lei, Ming. "A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms." Nat. Struct. Mol. Biol. 18, 213-221 (2011).
PubMed: 21217703

Assembly members:

Assembly members:
spRT6, polymer, 104 residues, 11117.421 Da.

Natural source:

Natural source: Common Name: fission Taxonomy ID: 4896 Superkingdom: not available Kingdom: Eukaryota Genus/species: Fungi Schizosaccharomyces

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
spRT6: SVSILRSSVNHREVDEAIDN ILRYTNSTEQQFLEAMESTG GRVRIAIAKLLSKQTSGGSG GSKLGGSGGSRKDLSVKGML YDSDSQQILNRLRERVSGST AQSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	380
15N chemical shifts	88
1H chemical shifts	535

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spRT6	1

Entities:

Entity 1, spRT6 104 residues - 11117.421 Da.

1

SER

VAL

SER

ILE

LEU

ARG

SER

VAL

ASN

2

HIS

ARG

GLU

VAL

ASP

GLU

ALA

ILE

ASP

ASN

3

ILE

LEU

ARG

TYR

THR

ASN

SER

THR

GLU

GLN

4

GLN

PHE

LEU

GLU

ALA

MET

GLU

SER

THR

GLY

5

GLY

ARG

VAL

ARG

ILE

ALA

ILE

ALA

LYS

LEU

6

LEU

SER

LYS

GLN

THR

SER

GLY

SER

GLY

7

GLY

SER

LYS

LEU

GLY

SER

GLY

SER

8

ARG

LYS

ASP

LEU

SER

VAL

LYS

GLY

MET

LEU

9

TYR

ASP

SER

ASP

SER

GLN

ILE

LEU

ASN

10

ARG

LEU

ARG

GLU

ARG

VAL

SER

GLY

SER

THR

11

ALA

GLN

SER

ALA

Samples:

sample_1: spRT6, [U-99% 13C; U-99% 15N], 1.1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: spRT6, [U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.07 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 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 HNCACO	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
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-15N IPAP HSQC	sample_2	isotropic	sample_conditions_1
3D CCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2L3N
DBJ	BAB70735
EMBL	CAC39280
GB	AAK57740
PIR	T39684
REF	NP_596285
SP	Q96TL7
AlphaFold	Q96TL7