BMRB Entry 19627

Name: NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492
Published: 2013-12-20

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PDB ID: 2mhd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19627
MolProbity Validation Chart

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

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Title: NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492

Deposition date: 2013-11-21 Original release date: 2013-12-20

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

Citation: Shnitkind, Sergey; Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492" Not known ., .-..

Assembly members:
entity, polymer, 110 residues, 12814.421 Da.

Natural source: Common Name: CFB group bacteria Taxonomy ID: 820 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides uniformis

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

Entity Sequences (FASTA):
entity: GDEDDKVEIPQLVGKWIVKE PVLQDDFVTCYTFNADKTYE VYTGSPLSNGVPFRGTYIIS LDEKLIKLYDKEEHCTEQYH ILKLTSKEMKWENASPKDGN SDKRLEKYND

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	380
15N chemical shifts	113
1H chemical shifts	773

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 110 residues - 12814.421 Da.

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

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-99% 13C; U-99% 15N], 1.2 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 HACANH APSY	sample_1	isotropic	sample_conditions_1
5D HACACONH APSY	sample_1	isotropic	sample_conditions_1
5D CBCACONH APSY	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
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bartels et al., Bruker Biospin - collection, data analysis, processing

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

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

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MHD
EMBL	CUN47051 CUP01591 CUQ01617
GB	EDO53099 EFA19032 EFV25840
REF	WP_005829739

Biological Magnetic Resonance Data Bank