BMRB Entry 34248

Name: NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)
Published: 2018-09-14

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PDB ID: 6g04
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34248
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119) PubMed: 30201955

Deposition date: 2018-03-16 Original release date: 2018-09-14

Authors: Michel, E.; Schuetz, S.; Damberger, F.; Allain, F.; Panse, V.

Citation: Schutz, S.; Michel, E.; Damberger, F.; Oplova, M.; Pena, C.; Leitner, A.; Aebersold, R.; Allain, F.; Panse, V.. "Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2." Nat. Commun. 9, 3669-3669 (2018).

Assembly members:
entity_1, polymer, 156 residues, 17938.062 Da.
entity_2, polymer, 26 residues, 2903.303 Da.

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: SGSHMSTQYIDETAFVQAEQ GKTNLMFSDEKQQARFELGV SMVIYKWDALDVAVENSWGG PDSAEKRDWITGIVVDLFKN EKVVDAALIEETLLYAMIDE FETNVEDDSALPIAVEVINI YNDCFNLNYNKVEKLYLEWQ EKQRTKKSKRVVHIEG
entity_2: SGSQHMRPRFNRENKVSPAD AAKKAL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	638
15N chemical shifts	202
1H chemical shifts	1294

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_1 156 residues - 17938.062 Da.

1

SER

GLY

SER

HIS

MET

SER

THR

GLN

TYR

ILE

2

ASP

GLU

THR

ALA

PHE

VAL

GLN

ALA

GLU

GLN

3

GLY

LYS

THR

ASN

LEU

MET

PHE

SER

ASP

GLU

4

LYS

GLN

ALA

ARG

PHE

GLU

LEU

GLY

VAL

5

SER

MET

VAL

ILE

TYR

LYS

TRP

ASP

ALA

LEU

6

ASP

VAL

ALA

VAL

GLU

ASN

SER

TRP

GLY

7

PRO

ASP

SER

ALA

GLU

LYS

ARG

ASP

TRP

ILE

8

THR

GLY

ILE

VAL

ASP

LEU

PHE

LYS

ASN

9

GLU

LYS

VAL

ASP

ALA

LEU

ILE

GLU

10

GLU

THR

LEU

TYR

ALA

MET

ILE

ASP

GLU

11

PHE

GLU

THR

ASN

VAL

GLU

ASP

SER

ALA

12

LEU

PRO

ILE

ALA

VAL

GLU

VAL

ILE

ASN

ILE

13

TYR

ASN

ASP

CYS

PHE

ASN

LEU

ASN

TYR

ASN

14

LYS

VAL

GLU

LYS

LEU

TYR

LEU

GLU

TRP

GLN

15

GLU

LYS

GLN

ARG

THR

LYS

SER

LYS

ARG

16

VAL

HIS

ILE

GLU

GLY

Entity 2, entity_2 26 residues - 2903.303 Da.

1

SER

GLY

SER

GLN

HIS

MET

ARG

PRO

ARG

PHE

2

ASN

ARG

GLU

ASN

LYS

VAL

SER

PRO

ALA

ASP

3

ALA

LYS

ALA

LEU

Samples:

sample_1: Tsr2(1-152), [U-13C; U-15N], 0.5 mM; S26A(100-119) 0.5 mM; sodium phosphate 20 mM; DTT, [U-2H], 1 mM; EDTA 10 uM

sample_2: Tsr2(1-152) 0.5 mM; S26A(100-119), [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; DTT, [U-2H], 1 mM; EDTA 10 uM

sample_conditions_1: ionic strength: 41 mM; pH: 7; pressure: 1 atm; temperature: 293.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)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 aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 750 MHz
Bruker Avance 900 MHz
Bruker Avance 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts