BMRB Entry 50957

Name: 1H, 15 N, and 13 C resonance assignments of the SH3-like tandem domain of human KIN17 protein
Published: 2021-06-04

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PDB ID: 9coj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50957
MolProbity Validation Chart

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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:

1H, 15 N, and 13 C resonance assignments of the SH3-like tandem domain of human KIN17 protein

Deposition date:

2021-06-01

Original release date:

2021-06-04

Authors:

Lourenco, Isabella; Seixas, Flavio; Almeida, Fabio; Fossey, Marcelo; Souza, Fatima; Caruso, Icaro

Citation:

Citation: Lourenco, Isabella; Seixas, Flavio; Fernandez, Maria Aparecida; Almeida, Fabio; Fossey, Marcelo; Souza, Fatima; Caruso, Icaro. "1H, 15N, and 13C resonance assignments of the SH3-like tandem domain of human KIN protein" Biomol. NMR Assignments 15, 449-453 (2021).
PubMed: 34417717

Assembly members:

Assembly members:
entity_1, polymer, 127 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: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEEEKKRTARTDYWLQPEII VKIITKKLGEKYHKKKAIVK EVIDKYTAVVKMIDSGDKLK LDQTHLETVIPAPGKRILVL NGGYRGNEGTLESINEKTFS ATIVIETGPLKGRRVEGIQY EDISKLA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	587
15N chemical shifts	127
1H chemical shifts	954

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3 tandem domain of KIN protein	1

Entities:

Entity 1, SH3 tandem domain of KIN protein 127 residues - Formula weight is not available

1

GLY

GLU

LYS

ARG

THR

ALA

ARG

2

THR

ASP

TYR

TRP

LEU

GLN

PRO

GLU

ILE

3

VAL

LYS

ILE

THR

LYS

LEU

GLY

GLU

4

LYS

TYR

HIS

LYS

ALA

ILE

VAL

LYS

5

GLU

VAL

ILE

ASP

LYS

TYR

THR

ALA

VAL

6

LYS

MET

ILE

ASP

SER

GLY

ASP

LYS

LEU

LYS

7

LEU

ASP

GLN

THR

HIS

LEU

GLU

THR

VAL

ILE

8

PRO

ALA

PRO

GLY

LYS

ARG

ILE

LEU

VAL

LEU

9

ASN

GLY

TYR

ARG

GLY

ASN

GLU

GLY

THR

10

LEU

GLU

SER

ILE

ASN

GLU

LYS

THR

PHE

SER

11

ALA

THR

ILE

VAL

ILE

GLU

THR

GLY

PRO

LEU

12

LYS

GLY

ARG

VAL

GLU

GLY

ILE

GLN

TYR

13

GLU

ASP

ILE

SER

LYS

LEU

ALA

Samples:

sample_1: SH3 tandem domain of KIN protein, [U-13C; U-15N], 0.35 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 0.5 mM; sodium azide 0.02%; EDTA 3 mM; DSS 0.33 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 0.1 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
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	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 CBCA(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
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRbox - data analysis

NMRDraw - processing

ANALYSIS - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks