BMRB Entry 18734

Name: NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799
Published: 2012-10-25

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PDB ID: 2lz0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18734
MolProbity Validation Chart

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

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Title: NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799

Deposition date: 2012-09-21 Original release date: 2012-10-25

Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; Dutta, Samit

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799" Not known ., .-..

Assembly members:
ZP_02034617.1, polymer, 100 residues, 11087.459 Da.

Natural source: Common Name: firmicutes Taxonomy ID: 411467 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudoflavonifractor Pseudoflavonifractor capillosus

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

Entity Sequences (FASTA):
ZP_02034617.1: GSHEGEPVVGMDKSLFAGNT VIREITVQPNIGLLYDGMFS GCTALEKLILTGEDPSAYSA GDGLRDGADFLICVPEEALD RYRRDYFWQTYAAWIQPMEQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	315
15N chemical shifts	100
1H chemical shifts	673

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ZP_02034617.1	1

Entities:

Entity 1, ZP_02034617.1 100 residues - 11087.459 Da.

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

Samples:

sample_1: ZP_02034617.1, [U-99% 13C; U-99% 15N], 1.2 mM; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

XEASY, Bartels et al. - processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

UNIO, Herrmann and Wuthrich - chemical shift assignment, peak picking, structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LZ0
GB	EDN01860
REF	WP_006570766

Biological Magnetic Resonance Data Bank