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 16377

Title: RpR325/RPA3574 from Rhodopseudomonas palustris

Authors: Kennedy, Michael; Ramelot, Theresa; Wang, Huang; Ciccosanti, Colleen; Jang, Mei; Nair, R; Rost, Burkhardt; Swapna, G.V.T.; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Kennedy, Michael; Ramelot, Theresa; Wang, Huang; Ciccosanti, Colleen; Jang, Mei; Nair, R; Rost, Burkhardt; Swapna, G.V.T.; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "RpR325/RPA3574 from Rhodopseudomonas palustris"  Not known ., .-..

Assembly members:
RPA3574, polymer, 73 residues, 13648.825 Da.

Natural source:   Common Name: Rhodopseudomonas palustris   Taxonomy ID: 1076   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustrisa

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

Entity Sequences (FASTA):
RPA3574: MLVTINGEQREVQSASVAAL MTELDCTDGHYAVALNYDVV PRGKWDETPVTAGDEIEILT PRQGGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts287
15N chemical shifts72
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RPA35741

Entities:

Entity 1, RPA3574 73 residues - 13648.825 Da.

65 + 8 residues for his tag = 73 residues

1   METLEUVALTHRILEASNGLYGLUGLNARG
2   GLUVALGLNSERALASERVALALAALALEU
3   METTHRGLULEUASPCYSTHRASPGLYHIS
4   TYRALAVALALALEUASNTYRASPVALVAL
5   PROARGGLYLYSTRPASPGLUTHRPROVAL
6   THRALAGLYASPGLUILEGLUILELEUTHR
7   PROARGGLNGLYGLYLEUGLUHISHISHIS
8   HISHISHIS

Samples:

NC_sample: RPA3574, [U-100% 13C; U-100% 15N], 0.92 mM; MES 20 mM; potassium chloride 200 mM

NC5_sample: RPA3574, [U-5% 13C; U-99% 15N], 0.85 mM; MES 20 mM; potassium chloride 200 mM

sample_conditions_1: ionic strength: .2 M; pH: 6.5; pressure: 1.0 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1

Software:

AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.3, Bruker Biospin - collection

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

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

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS, Bhattacharya and Montelione - structure solution

PDBStat v5.1, Roberto Tejero and Gaetano T. Montelione - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 850 MHz
  • Varian INOVA 500 MHz

Related Database Links:

SWS Q6N3W8_RHOPA
PDB
EMBL CAE29015
REF WP_011159114