BMRB Entry 16648

Title:
Solution NMR Structure of a Conserved Hypothetical Membrane Lipoprotein Obtained from Ureaplasma parvum: Northeast Structural Genomics Consortium Target UuR17A (139-239)
Deposition date:
2009-12-22
Original release date:
2010-07-26
Authors:
Mani, R.; Swapna, G.V.T; Janjua, H.; Ciccosanti, C.; Huang, Y. J.; Patel, D. J.; Xiao, R.; Acton, T.; Everett, J.; Montelione, G.T.
Citation:

Citation: Mani, Rajeswari; Vorobiev, Sergey; Swapna, G.; Neely, Helen; Janjua, Haleema; Ciccosanti, Colleen; Xiao, Rong; Acton, Thomas; Everett, John; Hunt, John; Montelione, Gaetano. "Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold."  J. Struct. Funct. Genomics 12, 27-32 (2011).
PubMed: 21153711

Assembly members:

Assembly members:
UuR17A,_Lipoprotein, polymer, 121 residues, 14356.324 Da.

Natural source:

Natural source:   Common Name: Ureaplasma parvum   Taxonomy ID: 134821   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Ureaplasma parvum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Data sets:
Data typeCount
13C chemical shifts508
15N chemical shifts120
1H chemical shifts775

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UuR17A1

Entities:

Entity 1, UuR17A 121 residues - 14356.324 Da.

Last 8 residues LEHHHHHH is a C-terminal tag

1   METLEUSERGLNALAASNGLUASPPHELYS
2   LYSILEVALASNASNILEARGLEULYSASP
3   THRPHEASPPHELYSLEUALAALAPHEPRO
4   ASNGLNASNTYRASPGLNLEULEUPROSER
5   GLNILETYRLYSASNTYRTYRGLNGLYILE
6   GLUILEGLNGLNHISLYSTYRGLNASNGLU
7   LEUASPILELYSILEILEASNPHELEUTYR
8   PROASPGLYASPPHEGLYSERALAASNLYS
9   ASNGLYTHRLEULYSLEUSERLEUMETLEU
10   THRASPLYSLYSASNASNGLNVALTYRTYR
11   LYSLEULEUGLUVALSERGLYPHELYSSER
12   ASNPROTYRLEUGLUHISHISHISHISHIS
13   HIS

Samples:

sample_1: UuR17A, Lipoprotein, [U-100% 13C; U-100% 15N], 0.91 ± 0.2 mM; NaN3 0.02%; DDT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_2: UuR17A, Lipoprotein, [U-100% 13C; U-100% 15N], 0.91 ± 0.2 mM; NaN3 0.02%; DDT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_3: UuR17A, Lipoprotein, [U-10% 13C; U-99% 15N], 0.7 ± 0.2 mM; NaN3 0.02%; DDT 100 mM; CaCl2 5 mM; NaCl 10 mM; MES 20 mM

sample_conditions_1: ionic strength: 15 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N/13C simultaneous NOESYsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
(4,3)D GFT-CBCACACONHNsample_2isotropicsample_conditions_1
(4,3)D GFT-HNNCABCAsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH TOCSYsample_2isotropicsample_conditions_1
3D CCCONH TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
Het NOE satsample_3isotropicsample_conditions_1
Het NOE no satsample_3isotropicsample_conditions_1

Software:

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

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

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAO73398
EMBL CPS23611
GB AAF30450 ACA32833 ACI60006 EDT48851 EDT49831
PIR B82940
REF WP_004026166 WP_004026422 WP_004026736 WP_004027175 WP_004027386
SP Q9PRA0
AlphaFold Q9PRA0

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks