BMRB Entry 52531

Name: HvfA-DSR2- 3 unmodified peptide
Published: 2024-08-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52531

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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:

HvfA-DSR2- 3 unmodified peptide

Deposition date:

2024-06-27

Original release date:

2024-08-15

Authors:

Manley, Olivia; Shriver, Tucker; Robson, Scott; Ziarek, Joshua; Rosenzweig, Amy

Citation:

Citation: Manley, Olivia; Shriver, Tucker; Xu, Tian; Melendrez, Isaac; Palacios, Philip; Robson, Scott; Guo, Yisong; Kelleher, Neil; Ziarek, Joshua; Rosenzweig, Amy. "A multi-iron enzyme installs copper-binding oxazolone/thioamide pairs on a nontypeable Haemophilus inlfuenzae virulence factor" Proc. Natl. Acad. Sci. U. S. A. 121, e2408092121-e2408092121 (2024).
PubMed: 38968106

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Haemophilus influenzae Taxonomy ID: 727 Superkingdom: Bacteria Kingdom: not available Genus/species: Haemophilus influenzae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MESKSSSTDNTATPCVGDKC VKTKAAEGKCGEGKCGADKA KSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	81
15N chemical shifts	43
1H chemical shifts	43

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HvfAunmod	1

Entities:

Entity 1, HvfAunmod 50 residues - Formula weight is not available

1	MET	GLU	SER	LYS	SER	SER	SER	THR	ASP	ASN
2	THR	ALA	THR	PRO	CYS	VAL	GLY	ASP	LYS	CYS
3	VAL	LYS	THR	LYS	ALA	ALA	GLU	GLY	LYS	CYS
4	GLY	GLU	GLY	LYS	CYS	GLY	ALA	ASP	LYS	ALA
5	LYS	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: HvfA peptide, unmodified, [U-13C; U-15N], 5 mM; PBS 100 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

NMRbox vv3 - chemical shift assignment, peak picking

NMRPipe - processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

1	MET	GLU	SER	LYS	SER	SER	SER	THR	ASP	ASN
2	THR	ALA	THR	PRO	CYS	VAL	GLY	ASP	LYS	CYS
3	VAL	LYS	THR	LYS	ALA	ALA	GLU	GLY	LYS	CYS
4	GLY	GLU	GLY	LYS	CYS	GLY	ALA	ASP	LYS	ALA
5	LYS	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	GLU	SER	LYS	SER	SER	SER	THR	ASP	ASN
2	THR	ALA	THR	PRO	CYS	VAL	GLY	ASP	LYS	CYS
3	VAL	LYS	THR	LYS	ALA	ALA	GLU	GLY	LYS	CYS
4	GLY	GLU	GLY	LYS	CYS	GLY	ALA	ASP	LYS	ALA
5	LYS	SER	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS