BMRB Entry 15844

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15844
MolProbity Validation Chart

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Title:
NMR Solution Structure of a Thiamine Biosynthesis Protein from Geobacter Metallireducens: Northeast Structural Genomics Consortium Target GmR137
Deposition date:
2008-06-30
Original release date:
2008-08-25
Authors:
Mani, Rajeswari; Wang, Huang; Jiang, Mei; Magliaqui, Melissa; Xiao, Rong; Nair, Rajesh; Baran, Michael; G., Swapna; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation:

Citation: Mani, Rajeswari; Wang, Huang; Jiang, Mei; Magliaqui, Melissa; Xiao, Rong; Nair, Rajesh; Baran, Michael; G., Swapna; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of a Thiamine Biosynthesis Protein from Geobacter Metallireducens: Northeast Structural Genomics Consortium Target GmR137"  .

Assembly members:

Assembly members:
GmR137, polymer, 78 residues, 8530.543 Da.

Natural source:

Natural source:   Common Name: Geobacter metallireducens   Taxonomy ID: 28232   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacter metallireducens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GmR137: MNLTVNGKPSTVDGAESLNV TELLSALKVAQAEYVTVELN GEVLEREAFDATTVKDGDAV EFLYFMGGGKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts311
15N chemical shifts77
1H chemical shifts498

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GmR1371

Entities:

Entity 1, GmR137 78 residues - 8530.543 Da.

Last 8 residues LEHHHHHH is a C-terminal tag

1   METASNLEUTHRVALASNGLYLYSPROSER
2   THRVALASPGLYALAGLUSERLEUASNVAL
3   THRGLULEULEUSERALALEULYSVALALA
4   GLNALAGLUTYRVALTHRVALGLULEUASN
5   GLYGLUVALLEUGLUARGGLUALAPHEASP
6   ALATHRTHRVALLYSASPGLYASPALAVAL
7   GLUPHELEUTYRPHEMETGLYGLYGLYLYS
8   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: GmR137, THiS protein, [U-100% 13C; U-100% 15N], 1.06 ± 0.2 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: GmR137, THiS protein, [U-10% 13C; U-99% 15N], 1.26 ± 0.2 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
(4,3)D GFT-HNNCABCAsample_1isotropicsample_conditions_1
(4,3)D GFT-CABCA(CO)NHNsample_1isotropicsample_conditions_1
(4,3)D GFT-HABCAB(CO)NHNsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D-CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aliph NOESYsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC (NH2 only)sample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC (Large SW)sample_1isotropicsample_conditions_1

Software:

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

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

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
GB ABB31799 AJE02784 EHP89319
REF WP_004511498 WP_039740961

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