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 16691

Title: Solution NMR Structure of Probable 30S Ribosomal Protein PSRP-3 (Ycf65-like protein) from Synechocystis sp. (strain PCC 6803), Northeast Structural Genomics Consortium Target Target SgR46

Authors: Liu, G.; Janjua, J.; Xiao, R.; Buchwald, W.; Ciccosanti, C.; Belote, R.; Everett, J.; Nair, R.; Acton, T; Rost, B.; Montelione, G.

Citation: Liu, G.; Janjua, J.; Xiao, R.; Buchwald, W.; Ciccosanti, C.; Belote, R.; Everett, J.; Nair, R.; Acton, T; Rost, B.; Montelione, G.. "Solution NMR Structure of Probable 30S ribosomal protein PSRP-3 (Ycf65-like protein) from Synechocystis sp. (PCC 6803), Northeast Structural Genomics Consortium Target Target SgR46"  To be published ., .-..

Assembly members:
SgR46, polymer, 116 residues, 13318.086 Da.

Natural source:   Common Name: Synechocystis sp. PCC 6803   Taxonomy ID: 1148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis Synechocystis sp. PCC 6803

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

Entity Sequences (FASTA):
SgR46: MAASTVHTSFILKVLWLDQN VAIAVDQIVGKGTSPLTSYF FWPRADAWQQLKDELEAKHW IAEADRINVLNQATEVINFW QDLKNQNKQISMAEAQGKFP EVVFSGSNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts117
1H chemical shifts783

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SgR461

Entities:

Entity 1, SgR46 116 residues - 13318.086 Da.

1   METALAALASERTHRVALHISTHRSERPHE
2   ILELEULYSVALLEUTRPLEUASPGLNASN
3   VALALAILEALAVALASPGLNILEVALGLY
4   LYSGLYTHRSERPROLEUTHRSERTYRPHE
5   PHETRPPROARGALAASPALATRPGLNGLN
6   LEULYSASPGLULEUGLUALALYSHISTRP
7   ILEALAGLUALAASPARGILEASNVALLEU
8   ASNGLNALATHRGLUVALILEASNPHETRP
9   GLNASPLEULYSASNGLNASNLYSGLNILE
10   SERMETALAGLUALAGLNGLYLYSPHEPRO
11   GLUVALVALPHESERGLYSERASNLEUGLU
12   HISHISHISHISHISHIS

Samples:

sample: SgR46, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%

sample_1: SgR46, [U-10% 13C; U-100% 15N], 0.8 mM; H2O 95%; D2O 5%

sample_2: SgR46, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7.5; pressure: 1.0 atm; temperature: 293 K

sample_conditions_2: pH: 4.5; pressure: 1.0 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic 927sampleisotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_2
3D CBCA(CO)NH 816sample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D 1H-13C arom NOESYsampleisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsampleisotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSY 829sampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D CBCA(CO)NH 819sample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D HNCOCAsample_2isotropicsample_conditions_2
3D 1H-15N NOESY 939sample_1isotropicsample_conditions_1
3D 1H-15N NOESY 940sample_1isotropicsample_conditions_1
1D T1sample_1isotropicsample_conditions_1
1D T2sample_1isotropicsample_conditions_1
3D 1H-13C arom TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C arom HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSY 830sample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic 928sample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA10474 BAK51259 BAL30257 BAL33426 BAL36595
GB AGF52766 AIE74500 ALJ68680
REF WP_010873701 WP_038531511
SP Q55385