BMRB Entry 15611

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PDB ID:
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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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:

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:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts141
1H chemical shifts858

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 130 residues - 14486.203 Da.

LEHHHHHH C-terminal His-tag

1   METSERGLNTRPTHRTHRVALCYSLYSLEU
2   ASPASPILELEUPROGLYTHRGLYVALCYS
3   ALALEUVALGLUGLNGLNGLNILEALAVAL
4   PHEARGPROARGASNASPGLUGLNVALTYR
5   ALAILESERASNILEASPPROPHEALAGLN
6   ALASERVALLEUSERARGGLYILEVALALA
7   GLUHISGLNASPASPLEUTRPVALALASER
8   PROLEULYSLYSGLNHISPHEARGLEUTYR
9   ASPGLYPHECYSLEUGLUASPGLYALATYR
10   SERVALALAALATYRASPTHRGLNVALTHR
11   ASNGLYASNVALGLNILESERILEALAASP
12   SERASPVALALAVALASPASNSERGLNPRO
13   LEUPROLEUGLUHISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_oneisotropicsample_conditions_1
3D HNCONC_oneisotropicsample_conditions_1
3D HNCACBNC_oneisotropicsample_conditions_1
3D HNCANC_oneisotropicsample_conditions_1
3D CBCA(CO)NHNC_oneisotropicsample_conditions_1
3D 1H-15N,13Cali,13Caro NOESYNC_twoisotropicsample_conditions_1
2D 1H-15N HSQCNC_twoisotropicsample_conditions_1
2D 1H-13C HSQC aliNC_twoisotropicsample_conditions_1
3D HCCH-COSY aliphaticNC_twoisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNC_twoisotropicsample_conditions_1
3D HBHA(CO)NHNC_twoisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_twoisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNC_twoisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNC_twoisotropicsample_conditions_1
3D HCCH-COSY aromaticNC_twoisotropicsample_conditions_1
2D 1Haro-15Naro LR-HSQCNC_twoisotropicsample_conditions_1
2D 1H-13C CT-HSQC 28msNC5isotropicsample_conditions_1
2D 1H-13C CT-HSQC 56msNC5isotropicsample_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

Related Database Links:

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

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