BMRB Entry 34864

Name: Folded alpha helical de novo proteins from Apilactobacillus kunkeei
Published: 2024-02-14

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PDB ID: 8qnj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34864
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:

Folded alpha helical de novo proteins from Apilactobacillus kunkeei

Deposition date:

2023-09-26

Original release date:

2024-02-14

Authors:

Celestine, C.

Citation:

Citation: Ye, Weihua; Krishna Behra, Phani Rama; Dyrhage, Karl; Seeger, Christian; Joiner, Joe; Karlsson, Elin; Andersson, Eva; Chi, Celestine; Andersson, Siv; Jemth, Per. "Folded Alpha Helical Putative New Proteins from Apilactobacillus kunkeei" J. Mol. Biol. 436, 168490-168490 (2024).
PubMed: 38355092

Assembly members:

Assembly members:
entity_1, polymer, 65 residues, 7437.335 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMKKEELIDKIKANNRLLN AVVQEMYLDNSLDIKTRDYY ASNITSVRQNGDQIIQILDE EGIAE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	143
15N chemical shifts	73
1H chemical shifts	438

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 65 residues - 7437.335 Da.

1

GLY

SER

MET

LYS

GLU

LEU

ILE

ASP

2

LYS

ILE

LYS

ALA

ASN

ARG

LEU

ASN

3

ALA

VAL

GLN

GLU

MET

TYR

LEU

ASP

ASN

4

SER

LEU

ASP

ILE

LYS

THR

ARG

ASP

TYR

5

ALA

SER

ASN

ILE

THR

SER

VAL

ARG

GLN

ASN

6

GLY

ASP

GLN

ILE

GLN

ILE

LEU

ASP

GLU

7

GLU

GLY

ILE

ALA

GLU

Samples:

sample_1: Orphan 5, [U-10% 13C; U-99% 15N], 500 uM

sample_conditions_1: ionic strength: 150 mM; 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	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	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
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - chemical shift assignment

CcpNmr Analysis, CCPN - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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