BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16934

Title: Solution NMR structure of the PBS linker domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E

Deposition date: 2010-05-14 Original release date: 2010-07-08

Authors: He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the PBS linker domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E"  Not known ., .-..

Assembly members:
PBS, polymer, 149 residues, 17254.771 Da.

Natural source:   Common Name: Anabaena sp.   Taxonomy ID: 1167   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Anabaena Anabaena sp.

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

Entity Sequences (FASTA):
PBS: MKVFKRVAGIKDKAAIKTLI SAAYRQIFERDIAPYIAQNE FSGWESKLGNGEITVKEFIE GLGYSNLYLKEFYTPYPNTK VIELGTKHFLGRAPIDQAEI RKYNQILATQGIRAFINALV NSQEYNEVFGEDTVPYRRFP TLEHHHHHH

Data typeCount
13C chemical shifts671
15N chemical shifts156
1H chemical shifts1078

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PBS1

Entities:

Entity 1, PBS 149 residues - 17254.771 Da.

1   METLYSVALPHELYSARGVALALAGLYILE
2   LYSASPLYSALAALAILELYSTHRLEUILE
3   SERALAALATYRARGGLNILEPHEGLUARG
4   ASPILEALAPROTYRILEALAGLNASNGLU
5   PHESERGLYTRPGLUSERLYSLEUGLYASN
6   GLYGLUILETHRVALLYSGLUPHEILEGLU
7   GLYLEUGLYTYRSERASNLEUTYRLEULYS
8   GLUPHETYRTHRPROTYRPROASNTHRLYS
9   VALILEGLULEUGLYTHRLYSHISPHELEU
10   GLYARGALAPROILEASPGLNALAGLUILE
11   ARGLYSTYRASNGLNILELEUALATHRGLN
12   GLYILEARGALAPHEILEASNALALEUVAL
13   ASNSERGLNGLUTYRASNGLUVALPHEGLY
14   GLUASPTHRVALPROTYRARGARGPHEPRO
15   THRLEUGLUHISHISHISHISHISHIS

Samples:

sample_4: entity, [U-5% 13C; U-100% 15N], 0.851 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; poly acrylamide gel 7%; H2O 83%; D2O 17%

sample_1: entity, [U-100% 13C; U-100% 15N], 0.95 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_2: entity, [U-5% 13C; U-100% 15N], 0.975 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_3: entity, [U-5% 13C; U-100% 15N], 0.664 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02%; DSS 50 uM; poly ethylene glycol 4%; H2O 82%; D2O 18%

sample_conditions_1: ionic strength: 117.5 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC alisample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC arosample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC (methyl)sample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSY alisample_1isotropicsample_conditions_1
3D HCCH-COSY arosample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
13C/15N-NOESYsample_1isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_4anisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

NMRPipe v2007.030.16.06, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PROSA v6.4, Guntert - processing

XEASY, Bartels et al. - data analysis

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

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

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

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis

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

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - validation

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

Molmol, Koradi, Billeter and Wuthrich - refinement

TOPSPIN v2.1, Bruker Biospin - data analysis

NMR spectrometers:

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

Related Database Links:

PDB

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