BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17031

Title: Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C

Authors: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Yang, Yunhuang; Cort, John; Hamilton, Keith; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C"  Not known ., .-..

Assembly members:
SLR0335, polymer, 155 residues, 17840 Da.

Natural source:   Common Name: Synechocystis sp.   Taxonomy ID: 1143   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis not available

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

Entity Sequences (FASTA):
SLR0335: PQSYFNAAAKRQKYAMKPGL SALEKNAVIKAAYRQIFERD ITKAYSQSISYLESQVRNGD ISMKEFVRRLAKSPLYRKQF FEPFINSRALELAFRHILGR GPSSREEVQKYFSIVSSGGL PALVDALVDSQEYADYFGEE TVPYLRGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts652
15N chemical shifts156
1H chemical shifts1025

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SLR03351

Entities:

Entity 1, SLR0335 155 residues - 17840 Da.

1   PROGLNSERTYRPHEASNALAALAALALYS
2   ARGGLNLYSTYRALAMETLYSPROGLYLEU
3   SERALALEUGLULYSASNALAVALILELYS
4   ALAALATYRARGGLNILEPHEGLUARGASP
5   ILETHRLYSALATYRSERGLNSERILESER
6   TYRLEUGLUSERGLNVALARGASNGLYASP
7   ILESERMETLYSGLUPHEVALARGARGLEU
8   ALALYSSERPROLEUTYRARGLYSGLNPHE
9   PHEGLUPROPHEILEASNSERARGALALEU
10   GLULEUALAPHEARGHISILELEUGLYARG
11   GLYPROSERSERARGGLUGLUVALGLNLYS
12   TYRPHESERILEVALSERSERGLYGLYLEU
13   PROALALEUVALASPALALEUVALASPSER
14   GLNGLUTYRALAASPTYRPHEGLYGLUGLU
15   THRVALPROTYRLEUARGGLYLEUGLUHIS
16   HISHISHISHISHIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 1.4 ± .05 mM; H2O 95%; D2O 5%

NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 100 ± 1 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1.2 ± .05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphNC_sampleisotropicsample_conditions_1
4D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HCCH-COSYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
3D H(CC)(CO)NH-TOCSYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aromNC_sampleisotropicsample_conditions_1
(H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

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

X-PLOR NIH v2.25, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - structure validation

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

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz
  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

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