BMRB Entry 15611

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PDB ID: 2jza
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15611
MolProbity Validation Chart

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

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Title: Solution NMR structure of Nitrite reductase [NAD(P)H] small subunit from Erwinia carotovora, Northeast Structural Genomics Consortium target EwR120.

Deposition date: 2007-12-31 Original release date: 2008-03-07

Authors: Sathyamoorthy, Bharathwaj; Eletsky, Alexander; Wang, Dongyang; Stokes, Kate; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS

Citation: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; SZYPERSKI, THOMAS. "Solution NMR structure of Nitrite reductase [NAD(P)H] small subunit from Erwinia carotovora" J. Biomol. NMR ., .-..

Assembly members:
ewr120_protein, polymer, 130 residues, 14486.203 Da.

Natural source: Common Name: Erwinia carotovora Taxonomy ID: 554 Superkingdom: Bacteria Kingdom: not available Genus/species: Erwinia carotovora

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

Entity Sequences (FASTA):
ewr120_protein: MSQWTTVCKLDDILPGTGVC ALVEQQQIAVFRPRNDEQVY AISNIDPFAQASVLSRGIVA EHQDDLWVASPLKKQHFRLY DGFCLEDGAYSVAAYDTQVT NGNVQISIADSDVAVDNSQP LPLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	506
15N chemical shifts	141
1H chemical shifts	858

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 130 residues - 14486.203 Da.

LEHHHHHH C-terminal His-tag

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

Samples:

NC5: ewr120 protein, [U-5% 13C; U-100% 15N], 0.24 mM; calcium chloride 5 mM; ammonium acetate 20 mM; sodium chloride 100 mM; DTT 10 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%

NC_two: ewr120 protein, [U-100% 13C; U-100% 15N], 0.7 mM; calcium chloride 5 mM; ammonium acetate 20 mM; sodium chloride 100 mM; DTT 10 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%

NC_one: ewr120 protein, [U-100% 13C; U-100% 15N], 0.32 mM; calcium chloride 5 mM; ammonium acetate 20 mM; sodium chloride 100 mM; DTT 10 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 138 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_one	isotropic	sample_conditions_1
3D HNCO	NC_one	isotropic	sample_conditions_1
3D HNCACB	NC_one	isotropic	sample_conditions_1
3D HNCA	NC_one	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_one	isotropic	sample_conditions_1
3D 1H-15N,13Cali,13Caro NOESY	NC_two	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC_two	isotropic	sample_conditions_1
2D 1H-13C HSQC ali	NC_two	isotropic	sample_conditions_1
3D HCCH-COSY aliphatic	NC_two	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC_two	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_two	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_two	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC_two	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC_two	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	NC_two	isotropic	sample_conditions_1
2D 1Haro-15Naro LR-HSQC	NC_two	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC 28ms	NC5	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC 56ms	NC5	isotropic	sample_conditions_1

Software:

AutoStruct v2.0.0, Huang, Tejero, Powers and Montelione - structure solution

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking, refinement

CSI v2.0, Wishart and Sykes - data analysis

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization

PROSA v6.0.2, Guntert - processing

TALOS v98.040.21.02, Cornilescu, Delaglio and Bax - data analysis

VNMRJ v2.1B, Varian - collection

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TOPSPIN v1.4, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 750 MHz

PDB	2JZA
EMBL	CAG76977
GB	AFR05266 AIU89979 KFF61641 KFF64753 KFF69607
REF	WP_010277621 WP_011095554 WP_039492133

Biological Magnetic Resonance Data Bank