BMRB Entry 31161

Name: Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26
Published: 2024-05-31

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PDB ID: 9bb5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31161
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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 Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26

Deposition date:

2024-04-05

Original release date:

2024-05-31

Authors:

Lin, Y.; Horne, W.

Citation:

Citation: Lin, Y.; Horne, W.. "Backbone Modification in a Protein Hydrophobic Core" Chemistry ., .-. (2024).
PubMed: 38753977

Assembly members:

Assembly members:
entity_1, polymer, 48 residues, 5126.900 Da.

Natural source:

Natural source: Common Name: Finegoldia magna Taxonomy ID: 1260 Superkingdom: Bacteria Kingdom: not available Genus/species: Finegoldia magna

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LKNAKEDAIAELKKAGITSD FXFNAXNKAKTVEEVNALKN EILKAHAX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	346

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 48 residues - 5126.900 Da.

1

LEU

LYS

ASN

ALA

LYS

GLU

ASP

ALA

ILE

ALA

2

GLU

LEU

LYS

ALA

GLY

ILE

THR

SER

ASP

3

PHE

XCP

PHE

ASN

ALA

XCP

ASN

LYS

ALA

LYS

4

THR

VAL

GLU

VAL

ASN

ALA

LEU

LYS

ASN

5

GLU

ILE

LEU

LYS

ALA

HIS

ALA

NH2

Samples:

sample_1: GA Module of Protein PAB: ACPC residues at positions 22 and 26 1 mM; DSS 0.2 mM

sample_conditions_1: ionic strength: 1 mM; pH: 5.9 pH*; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - data analysis

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE 700 MHz