BMRB Entry 34865

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

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PDB ID: 8qnt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34865
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:

2023-09-27

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, 49 residues, 5860.950 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: GSMKNYQPNKDLLEILESQK IKIKNLKEEVKILQRKIDQQ IAKERVIKQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	96
15N chemical shifts	45
1H chemical shifts	262

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 49 residues - 5860.950 Da.

1

GLY

SER

MET

LYS

ASN

TYR

GLN

PRO

ASN

LYS

2

ASP

LEU

GLU

ILE

LEU

GLU

SER

GLN

LYS

3

ILE

LYS

ILE

LYS

ASN

LEU

LYS

GLU

VAL

4

LYS

ILE

LEU

GLN

ARG

LYS

ILE

ASP

GLN

5

ILE

ALA

LYS

GLU

ARG

VAL

ILE

LYS

GLN

Samples:

sample_1: Orphan7, [U-99% 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-15N 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:

TopSpin, Bruker Biospin - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CcpNmr Analysis, CCPN - peak picking

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