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Biological Magnetic Resonance Data Bank


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BMRB Entry 18290

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18290
MolProbity Validation Chart

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Title: Solution NMR Structure of syc0711_d from Synechococcus sp., Northeast Structural Genomics Consortium (NESG) Target SnR212

Deposition date: 2012-02-23 Original release date: 2012-03-22

Authors: Mills, Jeffrey; Sathymoorthy, Bharathwaj; Pulavarti, Suryaven; Janjua, Haleema; Kohan, Eitan; Wang, Dongyan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Mills, Jeffrey; Sathymoorthy, Bharathwaj; Pulavarti, Suryaven; Janjua, Haleema; Kohan, Eitan; Wang, Dongyan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of syc0711_d from Synechococcus sp., Northeast Structural Genomics Consortium (NESG) Target SnR212"  To be published ., .-..

Assembly members:
SnR212, polymer, 130 residues, 14659.635 Da.

Natural source:   Common Name: Synechococcus sp.   Taxonomy ID: 1131   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechococcus sp.

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

Entity Sequences (FASTA):
SnR212: MGQGQNVLGQDLEVCCCAPM TGWYRNGFCQTDVQDRGSHT VCAEMTEEFLLFSRDRGNDL MTPRPEFNFPGLKAGDRWCL CASRWQEAFEAGMAPPVVLQ STEKSALRYVSLADLQAHAL PVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts115
1H chemical shifts719

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SnR2121

Entities:

Entity 1, SnR212 130 residues - 14659.635 Da.

1   METGLYGLNGLYGLNASNVALLEUGLYGLN
2   ASPLEUGLUVALCYSCYSCYSALAPROMET
3   THRGLYTRPTYRARGASNGLYPHECYSGLN
4   THRASPVALGLNASPARGGLYSERHISTHR
5   VALCYSALAGLUMETTHRGLUGLUPHELEU
6   LEUPHESERARGASPARGGLYASNASPLEU
7   METTHRPROARGPROGLUPHEASNPHEPRO
8   GLYLEULYSALAGLYASPARGTRPCYSLEU
9   CYSALASERARGTRPGLNGLUALAPHEGLU
10   ALAGLYMETALAPROPROVALVALLEUGLN
11   SERTHRGLULYSSERALALEUARGTYRVAL
12   SERLEUALAASPLEUGLNALAHISALALEU
13   PROVALLEUGLUHISHISHISHISHISHIS

Samples:

sampleNC: SnR212.015, [U-100% 13C; U-100% 15N], 0.89 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sampleNC5: SnR212.015, [U-100% 13C; U-100% 15N], 0.67 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleNCisotropicsample_conditions_1
2D 1H-13C HSQCsampleNCisotropicsample_conditions_1
3D HNCOsampleNCisotropicsample_conditions_1
3D CBCA(CO)NHsampleNCisotropicsample_conditions_1
3D HNCACBsampleNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsampleNCisotropicsample_conditions_1
2D 1H-13C HSQCsampleNC5isotropicsample_conditions_1
3D HBHA(CO)NHsampleNCisotropicsample_conditions_1
3D HCCH-COSYsampleNCisotropicsample_conditions_1
3D HNCAsampleNCisotropicsample_conditions_1
3D HN(CO)CAsampleNCisotropicsample_conditions_1
3D HN(CA)COsampleNCisotropicsample_conditions_1

Software:

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

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

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

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

PROSA, Guntert - processing

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

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

CARA, Keller et al. - data analysis

Molmol, Koradi, Billeter and Wuthrich - refinement

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAD78901
GB ABB56860 AJD58612
REF WP_011243023

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