BMRB Entry 30309

Name: Solution Structure of XPH1, 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: 5w8y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30309
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of XPH1, a Hybrid Sequence of Xfaso 1 and Pfl 6, Two Cro Proteins With Different Folds PubMed: 30051937

Deposition date: 2017-06-22 Original release date: 2018-07-03

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

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).

Assembly members:
entity_1, polymer, 73 residues, 8036.125 Da.

Natural source: Common Name: Xylella fastidiosa subsp. sandyi Ann-1 Taxonomy ID: 155920 Superkingdom: Bacteria Kingdom: not available Genus/species: Xylella fastidiosa

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

Entity Sequences (FASTA):
entity_1: MNAIDIAINKLGSVSALAAA LGVNQSAISQWRARGRVPAG RCIDIELYTDGRVECRELRP DVFGALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	255
15N chemical shifts	77
1H chemical shifts	473

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 73 residues - 8036.125 Da.

1

MET

ASN

ALA

ILE

ASP

ILE

ALA

ILE

ASN

LYS

2

LEU

GLY

SER

VAL

SER

ALA

LEU

ALA

3

LEU

GLY

VAL

ASN

GLN

SER

ALA

ILE

SER

GLN

4

TRP

ARG

ALA

ARG

GLY

ARG

VAL

PRO

ALA

GLY

5

ARG

CYS

ILE

ASP

ILE

GLU

LEU

TYR

THR

ASP

6

GLY

ARG

VAL

GLU

CYS

ARG

GLU

LEU

ARG

PRO

7

ASP

VAL

PHE

GLY

ALA

LEU

GLU

HIS

8

HIS

Samples:

sample_1: DSS 0.1 mM; XPH1, [U-13C; U-15N], 0.4 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_2: DSS 0.1 mM; XPH1, [U-13C; U-15N], 0.4 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_3: DSS 0.1 mM; XPH1, [U-13C; U-15N], 0.6 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_4: DSS 0.1 mM; XPH1, [U-10% 13C], 1.8 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts