BMRB Entry 25767

Name: NMR structure of the Vta1NTD-Did2(176-204) complex
Published: 2016-09-29

Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25767

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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:

NMR structure of the Vta1NTD-Did2(176-204) complex

Deposition date:

2015-08-25

Original release date:

2016-09-29

Authors:

Shen, Jie; Yang, Zhongzheng; Wang, Jiaolong; Vild, Cody

Citation:

Citation: Shen, Jie; Yang, Zhongzheng; Wang, Jiaolong; Zhao, Bin; Lan, Wenxian; Wang, Chunxi; Zhang, Xu; Wild, Cody; Liu, Maili; Xu, Zhaohui; Cao, Chunyang. "NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway" Sci. Rep. 6, 38710-38710 (2016).
PubMed: 27924850

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 19062.176 Da.
entity_2, polymer, 29 residues, 3341.826 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASNAARVVATAKDFDKVGL GIIGYYLQLYAVELILSEED RSQEMTALATELLDTIEAFK KEIGGESEAEDSDKSLHVMN TLIHDQEKAKIYMLNFTMSL YNEKLKQLKDGPWDVMLKRS LWCCIDLFSCILHLWKENIS ETSTNSLQKRIKYCKIYLSK LAKGEIG
entity_2: NVPEIKAKEVNVDDEKEDKL AQRLRALRG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	688
15N chemical shifts	185
1H chemical shifts	1304

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_1 167 residues - 19062.176 Da.

1

MET

ALA

SER

ASN

ALA

ARG

VAL

ALA

2

THR

ALA

LYS

ASP

PHE

ASP

LYS

VAL

GLY

LEU

3

GLY

ILE

GLY

TYR

LEU

GLN

LEU

TYR

4

ALA

VAL

GLU

LEU

ILE

LEU

SER

GLU

ASP

5

ARG

SER

GLN

GLU

MET

THR

ALA

LEU

ALA

THR

6

GLU

LEU

ASP

THR

ILE

GLU

ALA

PHE

LYS

7

LYS

GLU

ILE

GLY

GLU

SER

GLU

ALA

GLU

8

ASP

SER

ASP

LYS

SER

LEU

HIS

VAL

MET

ASN

9

THR

LEU

ILE

HIS

ASP

GLN

GLU

LYS

ALA

LYS

10

ILE

TYR

MET

LEU

ASN

PHE

THR

MET

SER

LEU

11

TYR

ASN

GLU

LYS

LEU

LYS

GLN

LEU

LYS

ASP

12

GLY

PRO

TRP

ASP

VAL

MET

LEU

LYS

ARG

SER

13

LEU

TRP

CYS

ILE

ASP

LEU

PHE

SER

CYS

14

ILE

LEU

HIS

LEU

TRP

LYS

GLU

ASN

ILE

SER

15

GLU

THR

SER

THR

ASN

SER

LEU

GLN

LYS

ARG

16

ILE

LYS

TYR

CYS

LYS

ILE

TYR

LEU

SER

LYS

17

LEU

ALA

LYS

GLY

GLU

ILE

GLY

Entity 2, entity_2 29 residues - 3341.826 Da.

1

ASN

VAL

PRO

GLU

ILE

LYS

ALA

LYS

GLU

VAL

2

ASN

VAL

ASP

GLU

LYS

GLU

ASP

LYS

LEU

3

ALA

GLN

ARG

LEU

ARG

ALA

LEU

ARG

GLY

Samples:

sample_1: entity_1, [U-13C; U-15N], 1.5 mM; entity_1, [U-13C; U-15N; U-70% 2H], 1.5 mM; entity_2 1.8 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 5 mM; D2O, [U-100% 2H], 10%; sodium azide 0.02%

sample_2: entity_1 1.8 mM; entity_2, [U-13C; U-15N], 1.5 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 5 mM; D2O, [U-100% 2H], 10%; sodium azide 0.02%

sample_conditions_1: ionic strength: 175 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 13C-F1 edited NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-F1 edited NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

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