BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16810

Title: Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A

Deposition date: 2010-03-31 Original release date: 2010-04-28

Authors: Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A"  To be published ., .-..

Assembly members:
PgR37A, polymer, 157 residues, 17546.934 Da.

Natural source:   Common Name: Porphyromonas gingivalis   Taxonomy ID: 837   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Porphyromonas gingivalis

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

Entity Sequences (FASTA):
PgR37A: MRVYKPEDVPNVQLADSTRL VTDEAGLLSNAQEEVMNGRL RAIRSSHAVEFAVVTLPSIG DAPLEDFTLKLARQWGVGNE KNNNGLLLVLVLDQRRVRFE TGYGLEGYLPDGLLSRIIHD RMIPHFRSGNYAEGLSEGVL AVQQVLDGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts667
15N chemical shifts169
1H chemical shifts1101

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PgR37A1

Entities:

Entity 1, PgR37A 157 residues - 17546.934 Da.

1   METARGVALTYRLYSPROGLUASPVALPRO
2   ASNVALGLNLEUALAASPSERTHRARGLEU
3   VALTHRASPGLUALAGLYLEULEUSERASN
4   ALAGLNGLUGLUVALMETASNGLYARGLEU
5   ARGALAILEARGSERSERHISALAVALGLU
6   PHEALAVALVALTHRLEUPROSERILEGLY
7   ASPALAPROLEUGLUASPPHETHRLEULYS
8   LEUALAARGGLNTRPGLYVALGLYASNGLU
9   LYSASNASNASNGLYLEULEULEUVALLEU
10   VALLEUASPGLNARGARGVALARGPHEGLU
11   THRGLYTYRGLYLEUGLUGLYTYRLEUPRO
12   ASPGLYLEULEUSERARGILEILEHISASP
13   ARGMETILEPROHISPHEARGSERGLYASN
14   TYRALAGLUGLYLEUSERGLUGLYVALLEU
15   ALAVALGLNGLNVALLEUASPGLYSERLEU
16   GLUHISHISHISHISHISHIS

Samples:

NC_sample: PgR37A, [U-100% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%

NC5_sample: PgR37A, [U-5% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; sodium azide 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNC_sampleisotropicsample_conditions_1
3D HCCH-COSY aliphaticNC_sampleisotropicsample_conditions_1
3D HCCH-COSY aromaticNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
2D long-range 1H-15N HSQC for histidineNC_sampleisotropicsample_conditions_1
3D HN(CA)CONC_sampleisotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation

AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

TOPSPIN v2.1, Bruker Biospin - collection, processing

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAG34119 BAK25626 GAP82223
GB AAQ65571 AIJ36374 AKV64744 ALA94086 ALJ26010
REF WP_005873820 WP_012458397 WP_013816169 WP_039417602 WP_043894154

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