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Biological Magnetic Resonance Data Bank


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BMRB Entry 16097

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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/BMR16097
MolProbity Validation Chart

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Title: NMR solution structure of an uncharacterized protein from Chlorobium tepidum. Northeast Structural Genomics target CtR107

Deposition date: 2008-12-29 Original release date: 2009-03-05

Authors: Mills, Jeffrey; Zhang, Qi; Sukumaran, Dinesh; Wang, Dongyan; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS

Citation: Mills, Jeffrey; Zhang, Qi; Sukumaran, Dinesh; Wang, Dongyan; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS. "Solution NMR structure of an uncharacterized protein from Chlorobium tepidum. Northeast Structural Genomics target CtR107"  Not known ., .-..

Assembly members:
CtR107, polymer, 166 residues, Formula weight is not available

Natural source:   Common Name: Chlorobium tepidum   Taxonomy ID: 1097   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Chlorobium tepidum

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

Entity Sequences (FASTA):
CtR107: MDFECQFVCELKELAPVPAL LIRTQTAMSELGSLFEAGYH DILQLLAGQGKSPSGPPFAR YFGMSAGTFEVEFGFPVEGG VEGSGRVVTGLTPSGKAASS LYIGPYGEIEAVYDALMKWV DDNGFDLSGEAYEIYLDNPA ETAPDQLRTRVSLMLHESLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts155
1H chemical shifts1034

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CtR1071

Entities:

Entity 1, CtR107 166 residues - Formula weight is not available

1   METASPPHEGLUCYSGLNPHEVALCYSGLU
2   LEULYSGLULEUALAPROVALPROALALEU
3   LEUILEARGTHRGLNTHRALAMETSERGLU
4   LEUGLYSERLEUPHEGLUALAGLYTYRHIS
5   ASPILELEUGLNLEULEUALAGLYGLNGLY
6   LYSSERPROSERGLYPROPROPHEALAARG
7   TYRPHEGLYMETSERALAGLYTHRPHEGLU
8   VALGLUPHEGLYPHEPROVALGLUGLYGLY
9   VALGLUGLYSERGLYARGVALVALTHRGLY
10   LEUTHRPROSERGLYLYSALAALASERSER
11   LEUTYRILEGLYPROTYRGLYGLUILEGLU
12   ALAVALTYRASPALALEUMETLYSTRPVAL
13   ASPASPASNGLYPHEASPLEUSERGLYGLU
14   ALATYRGLUILETYRLEUASPASNPROALA
15   GLUTHRALAPROASPGLNLEUARGTHRARG
16   VALSERLEUMETLEUHISGLUSERLEUGLU
17   HISHISHISHISHISHIS

Samples:

NC: CtR107, [U-99% 13C; U-99% 15N], 0.45 mM; D2O, [U-2H], 5%; H2O 95%; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM

NC5: CtR107, [U-5% 13C; U-99% 15N], 0.45 mM; D2O, [U-2H], 5%; H2O 95%; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM

sample_conditions_1: ionic strength: 235 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSYNCisotropicsample_conditions_1
3D simultaneous NCaliCaro HH NOESYNCisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

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

SPSCAN, Glaser - processing

XEASY, Bartels et al. - chemical shift assignment

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI, (CSI) Wishart and Sykes - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

Molmol, Koradi, Billeter and Wuthrich - data analysis

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAM71427
REF NP_661085 WP_010931873

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