BMRB Entry 30310

Name: Solution Structure of XPH2, a Hybrid Sequence of Xfaso 1 and Pfl 6, Two Cro Proteins With Different Folds
Published: 2018-07-03

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PDB ID: 5w8z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30310
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:

Solution Structure of XPH2, a Hybrid Sequence of Xfaso 1 and Pfl 6, Two Cro Proteins With Different Folds

Deposition date:

2017-06-22

Original release date:

2018-07-03

Authors:

Kumirov, V.; Dykstra, E.; Cordes, M.

Citation:

Citation: Kumirov, V.; Dykstra, E.; Hall, B.; Anderson, W.; Szyszka, T.; Cordes, M.. "Multistep mutational transformation of a protein fold through structural intermediates" Protein Sci. 27, 1767-1779 (2018).
PubMed: 30051937

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7887.996 Da.

Natural source:

Natural source: Common Name: Pseudomonas fluorescens PF5 Taxonomy ID: 1218948 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas fluorescens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKKIPLSKYLEEHGTQSALA AALGVNQSAISQMVRAGRCI DIELYTDGRVECRELRPDVF GALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	227
15N chemical shifts	64
1H chemical shifts	416

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 70 residues - 7887.996 Da.

1	MET	LYS	LYS	ILE	PRO	LEU	SER	LYS	TYR	LEU
2	GLU	GLU	HIS	GLY	THR	GLN	SER	ALA	LEU	ALA
3	ALA	ALA	LEU	GLY	VAL	ASN	GLN	SER	ALA	ILE
4	SER	GLN	MET	VAL	ARG	ALA	GLY	ARG	CYS	ILE
5	ASP	ILE	GLU	LEU	TYR	THR	ASP	GLY	ARG	VAL
6	GLU	CYS	ARG	GLU	LEU	ARG	PRO	ASP	VAL	PHE
7	GLY	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_3	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1

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

BMRB Entry 30310

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	LYS	LYS	ILE	PRO	LEU	SER	LYS	TYR	LEU
2	GLU	GLU	HIS	GLY	THR	GLN	SER	ALA	LEU	ALA
3	ALA	ALA	LEU	GLY	VAL	ASN	GLN	SER	ALA	ILE
4	SER	GLN	MET	VAL	ARG	ALA	GLY	ARG	CYS	ILE
5	ASP	ILE	GLU	LEU	TYR	THR	ASP	GLY	ARG	VAL
6	GLU	CYS	ARG	GLU	LEU	ARG	PRO	ASP	VAL	PHE
7	GLY	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	LYS	LYS	ILE	PRO	LEU	SER	LYS	TYR	LEU
2	GLU	GLU	HIS	GLY	THR	GLN	SER	ALA	LEU	ALA
3	ALA	ALA	LEU	GLY	VAL	ASN	GLN	SER	ALA	ILE
4	SER	GLN	MET	VAL	ARG	ALA	GLY	ARG	CYS	ILE
5	ASP	ILE	GLU	LEU	TYR	THR	ASP	GLY	ARG	VAL
6	GLU	CYS	ARG	GLU	LEU	ARG	PRO	ASP	VAL	PHE
7	GLY	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	LYS	LYS	ILE	PRO	LEU	SER	LYS	TYR	LEU
2	GLU	GLU	HIS	GLY	THR	GLN	SER	ALA	LEU	ALA
3	ALA	ALA	LEU	GLY	VAL	ASN	GLN	SER	ALA	ILE
4	SER	GLN	MET	VAL	ARG	ALA	GLY	ARG	CYS	ILE
5	ASP	ILE	GLU	LEU	TYR	THR	ASP	GLY	ARG	VAL
6	GLU	CYS	ARG	GLU	LEU	ARG	PRO	ASP	VAL	PHE
7	GLY	ALA	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS