BMRB Entry 17207

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17207

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Title:
Solution NMR Structure of the PBS linker domain of phycobilisome rod linker polypeptide from Synechococcus elongatus, Northeast Structural Genomics Consortium Target SnR168A
Deposition date:
2010-09-24
Original release date:
2010-10-06
Authors:
Eletsky, Alexander; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the PBS linker domain of phycobilisome rod linker polypeptide from Synechococcus elongatus, Northeast Structural Genomics Consortium Target SnR168A"  To be published ., .-..

Assembly members:

Assembly members:
SnR168A, polymer, 143 residues, 16426.244 Da.

Natural source:

Natural source:   Common Name: Synechococcus elongatus   Taxonomy ID: 32046   Superkingdom: not available   Kingdom: not available   Genus/species: Synechococcus elongatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SnR168A: MPLEWRAGASSDEINAIIRA VYRQVLGNDYVMSTERLTSA ESLLRGGEISVRDFVRAVAL SELYREKFFHNNAHNRFIEL NFKHLLGRAPYDQAEVAAHA ATYHSHGYDADINSYIDSAE YTESFGDNVVPYFRGLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts605
15N chemical shifts157
1H chemical shifts953

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SnR168A1

Entities:

Entity 1, SnR168A 143 residues - 16426.244 Da.

Residues 2-135 correspond to residues 20-153 of the native protein. Residues 136-143 represent a non-native affinity tag. The first residue is the initiating methionine

1   METPROLEUGLUTRPARGALAGLYALASER
2   SERASPGLUILEASNALAILEILEARGALA
3   VALTYRARGGLNVALLEUGLYASNASPTYR
4   VALMETSERTHRGLUARGLEUTHRSERALA
5   GLUSERLEULEUARGGLYGLYGLUILESER
6   VALARGASPPHEVALARGALAVALALALEU
7   SERGLULEUTYRARGGLULYSPHEPHEHIS
8   ASNASNALAHISASNARGPHEILEGLULEU
9   ASNPHELYSHISLEULEUGLYARGALAPRO
10   TYRASPGLNALAGLUVALALAALAHISALA
11   ALATHRTYRHISSERHISGLYTYRASPALA
12   ASPILEASNSERTYRILEASPSERALAGLU
13   TYRTHRGLUSERPHEGLYASPASNVALVAL
14   PROTYRPHEARGGLYLEUGLUHISHISHIS
15   HISHISHIS

Samples:

NC5-PEG: SnR168A, [5% 13C; U-100% 15N], 0.46 mM; MES 18 mM; sodium chloride 90 mM; calcium chloride 4.5 mM; DTT 9 mM; sodium azide 0.02%; C12E5 PEG 4%; hexanol 4%; H2O 85%; D2O 15%

NC: SnR168A, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: SnR168A, [5% 13C; U-100% 15N], 0.7 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5-phage: SnR168A, [5% 13C; U-100% 15N], 0.45 mM; MES 13 mM; sodium chloride 160 mM; calcium chloride 3.2 mM; DTT 6.4 mM; sodium azide 0.025%; potassium phosphate 2.4 mM; magnesium chloride 0.5 mM; Pf1 phage 13.2 g/l; H2O 85%; D2O 15%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_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 CBCA(CO)NHNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticNCisotropicsample_conditions_1
3D (H)CCH-COSY aromaticNCisotropicsample_conditions_1
3D (H)CCH-TOCSYNCisotropicsample_conditions_1
2D 1H-15N LR-HSQC (Histidine)NCisotropicsample_conditions_1
1D 1H-15N HSQC T1NCisotropicsample_conditions_1
1D 1H-15N HSQC T2NCisotropicsample_conditions_1
2D 1H-13C CT-HSQC (methyl)NC5isotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5isotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5-phageanisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5-PEGanisotropicsample_conditions_1

Software:

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

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

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

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

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

XEASY, Bartels et al. - data analysis

TOPSPIN, Bruker Biospin - collection, processing

VNMRJ, Varian - collection

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

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

PROSA v6.4, Guntert - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 750 MHz
  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAD78689
GB AAA64528 ABB57079 AJD58404
PRF 1912291C
REF WP_011242811 WP_011377844

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