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 15324

Title: A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris

Authors: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl

Citation: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Bansal, Sonal; Semest, Anthony; Guido, Valerie; Kennedy, Michael; Prestegard, James; Arrowsmith, Cheryl. "A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris"  Not known ., .-..

Assembly members:
unknown_function_protein_RPA2121, polymer, 67 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
unknown_function_protein_RPA2121: MMTASDRLGADPTQAASSPG GARAVSIVGNQIDSRELFTV DREIVIAHGDDRYRLRLTSQ NKLILTK

Data sets:
Data typeCount
13C chemical shifts267
15N chemical shifts64
1H chemical shifts446

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21

Entities:

Entity 1, subunit 1 67 residues - Formula weight is not available

1   METMETTHRALASERASPARGLEUGLYALA
2   ASPPROTHRGLNALAALASERSERPROGLY
3   GLYALAARGALAVALSERILEVALGLYASN
4   GLNILEASPSERARGGLULEUPHETHRVAL
5   ASPARGGLUILEVALILEALAHISGLYASP
6   ASPARGTYRARGLEUARGLEUTHRSERGLN
7   ASNLYSLEUILELEUTHRLYS

Samples:

sample_1: unknown function protein RPA2121, [U-99% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM

sample_2: unknown function protein RPA2121, [U-7% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 1 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D IPAP 15N-HSQCsample_2isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.95, Goddard - data analysis, peak picking

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

CNS v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.1.0, Huang, Tejero, Powers and Montelione - Validation

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAE27562
REF WP_011157676