BMRB Entry 19906

Name: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide
Published: 2014-09-22

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PDB ID: 2mnu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19906
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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 and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide

Deposition date:

2014-04-10

Original release date:

2014-09-22

Authors:

Suh, Jeong-Yong; Yu, Tae-Kyung

Citation:

Citation: Yu, T.K.; Shin, S.A.; Kim, E.H.; Kim, S.; Ryu, K.S.; Cheong, H.; Ahn, H.C.; Jon, S.; Suh, Jeong-Yong. "An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding" Angew. Chem. Int. Ed. Engl. 53, 9784-9787 (2014).
PubMed: 24985319

Assembly members:

Assembly members:
EDB, polymer, 93 residues, Formula weight is not available
APT, polymer, 26 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EDB: GSEVPQLTDLSFVDITDSSI GLRWTPLNSSTIIGYRITVV AAGEGIPIFEDFVDSSVGYY TVTGLEPGIDYDISVITLIN GGESAPTTLTQQT
APT: SSSPIQGSWTWENGKWTWKG IIRLEQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	681
13C chemical shifts	328
15N chemical shifts	104

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EDB	1
2	APT	2

Entities:

Entity 1, EDB 93 residues - Formula weight is not available

1

GLY

SER

GLU

VAL

PRO

GLN

LEU

THR

ASP

LEU

2

SER

PHE

VAL

ASP

ILE

THR

ASP

SER

ILE

3

GLY

LEU

ARG

TRP

THR

PRO

LEU

ASN

SER

4

THR

ILE

GLY

TYR

ARG

ILE

THR

VAL

5

ALA

GLY

GLU

GLY

ILE

PRO

ILE

PHE

GLU

6

ASP

PHE

VAL

ASP

SER

VAL

GLY

TYR

7

THR

VAL

THR

GLY

LEU

GLU

PRO

GLY

ILE

ASP

8

TYR

ASP

ILE

SER

VAL

ILE

THR

LEU

ILE

ASN

9

GLY

GLU

SER

ALA

PRO

THR

LEU

THR

10

GLN

THR

Entity 2, APT 26 residues - Formula weight is not available

1

SER

PRO

ILE

GLN

GLY

SER

TRP

THR

2

TRP

GLU

ASN

GLY

LYS

TRP

THR

TRP

LYS

GLY

3

ILE

ARG

LEU

GLU

GLN

Samples:

sample_1: EDB, [U-100% 13C; U-100% 15N], 0.3 mM; APT, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 273 K; pH: 6; pressure: 1 atm; ionic strength: 20 mM

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR_NIH, Garrett, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, refinement

NMR spectrometers:

Bruker Avance 900 MHz

BMRB	4283
PDB	2FNB 2MNU 4GH7 2MNU
EMBL	CAB52437
GB	AAA52461 AAA67749