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BMRB Entry 17688

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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/BMR17688
MolProbity Validation Chart

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Title: Solution NMR Structure of Tfu_2981 from Thermobifida fusca, Northeast Structural Genomics Consortium Target TfR85A

Deposition date: 2011-06-03 Original release date: 2011-07-06

Authors: Pulavarti, S. V. S. R. K; Eletsky, A; Mills, J.; Sukumaran, D.; Wang, D; Ciccosanti, C.; Hamilton, K.; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Lee, H; Prestegard, J.; Montelione, G.; Szyperski, Thomas

Citation: Pulavarti, S. V. S. R. K; Eletsky, A; Mills, J.; Sukumaran, D.; Wang, D.; Ciccosanti, C.; Hamilton, K.; Rost, B.; Acton, T; Xiao, R.; Everett, J.; Lee, H; Prestegard, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR Structure of Tfu_2981 from Thermobifida fusca, Northeast Structural Genomics Consortium Target TfR85A"  To be published ., .-..

Assembly members:
TfR85A, polymer, 151 residues, 16854.9 Da.

Natural source:   Common Name: Thermobifida fusca   Taxonomy ID: 2021   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermobifida fusca

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

Entity Sequences (FASTA):
TfR85A: MATLRRSVEVAAPAADVWTL VGDFSAIHRWHPQVSAPTLR GASPHTPGAERVFGAGTEEE LVERLVERDESARRLVYTMP DPPFPITNHRAVLEVVPRDD RHCTVVWTAMFDCSPETARE LESVIGDGVFAVGLNALAER YGRLEHHHHHH

Data typeCount
13C chemical shifts631
15N chemical shifts149
1H chemical shifts990

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TfR85A1

Entities:

Entity 1, TfR85A 151 residues - 16854.9 Da.

Residues1-143 in the sequence correspond to residues 1-143 of native protein. Residues from 144-151 represent non native affinity tag.

1   METALATHRLEUARGARGSERVALGLUVAL
2   ALAALAPROALAALAASPVALTRPTHRLEU
3   VALGLYASPPHESERALAILEHISARGTRP
4   HISPROGLNVALSERALAPROTHRLEUARG
5   GLYALASERPROHISTHRPROGLYALAGLU
6   ARGVALPHEGLYALAGLYTHRGLUGLUGLU
7   LEUVALGLUARGLEUVALGLUARGASPGLU
8   SERALAARGARGLEUVALTYRTHRMETPRO
9   ASPPROPROPHEPROILETHRASNHISARG
10   ALAVALLEUGLUVALVALPROARGASPASP
11   ARGHISCYSTHRVALVALTRPTHRALAMET
12   PHEASPCYSSERPROGLUTHRALAARGGLU
13   LEUGLUSERVALILEGLYASPGLYVALPHE
14   ALAVALGLYLEUASNALALEUALAGLUARG
15   TYRGLYARGLEUGLUHISHISHISHISHIS
16   HIS

Samples:

NC5: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC: TfR85A, [U-100% 13C; U-100% 15N], 1.07 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_Pf1_phage: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; Pf1 phage 12.5 mg/mL; H2O 90%; D2O 10%

NC5_PEG: TfR85A, [U-5% 13C; U-100% 15N], 1.338 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; DSS 50 uM; calcium chloride 5 mM; sodium azide 0.02%; PEG 4%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQCNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY-aliphaticNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY-aromaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_Pf1_phageanisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCNC5_PEGanisotropicsample_conditions_1
2D 1H-15N LR-HSQC for HistidineNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
2D (HB)CB(CGCDCE)HDHENCisotropicsample_conditions_1

Software:

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

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PROSA v6.4, Guntert - processing

TOPSPIN v2.1, Bruker Biospin - collection, processing

PSVS, Bhattacharya and Montelione - structure analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

CARA v1.8.4, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
GB AAZ57014 EOR69926
REF WP_011293398

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