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 18496

Title: Solution NMR Structure of YdbC:dT19G1 complex. Northeast Structural Genomics Consortium (NESG) Target KR150

Authors: Rossi, Paolo; Barbieri, Christopher; Aramini, James; Bini, Elisabetta; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation: Rossi, Paolo; Barbieri, Christopher; Aramini, James; Bini, Elisabetta; Acton, Thomas; Xiao, Rong; Montelione, Gaetano. "Solution NMR Structure of YdbC:dT19G1 complex. Northeast Structural Genomics Consortium (NESG) Target KR150"  To be published ., .-..

Assembly members:
entity_1, polymer, 74 residues, 8659.957 Da.
DNA_(5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')_, polymer, 14 residues, 4213.782 Da.

Natural source:   Common Name: Lactococcus Lactis   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus Lactis

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

Entity Sequences (FASTA):
entity_1: MADKLKFEIIEELIVLSENA KGWRKELNRVSWNDAEPKYD IRTWSPDHEKMGKGITLSEE EFGVLLKELGNKLE
DNA_(5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')_: TTTTTTTTTTTTTT

Data typeCount
13C chemical shifts330
15N chemical shifts70
1H chemical shifts655

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KR150_11
2KR150_21
3DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3')2

Entities:

Entity 1, KR150_1 74 residues - 8659.957 Da.

1   METALAASPLYSLEULYSPHEGLUILEILE
2   GLUGLULEUILEVALLEUSERGLUASNALA
3   LYSGLYTRPARGLYSGLULEUASNARGVAL
4   SERTRPASNASPALAGLUPROLYSTYRASP
5   ILEARGTHRTRPSERPROASPHISGLULYS
6   METGLYLYSGLYILETHRLEUSERGLUGLU
7   GLUPHEGLYVALLEULEULYSGLULEUGLY
8   ASNLYSLEUGLU

Entity 2, DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3') 14 residues - 4213.782 Da.

1   DTDTDTDTDTDTDTDTDTDT
2   DTDTDTDT

Samples:

sample_1: KR150.020, [U-100% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; NaCL 100 mM; D2O 10%; DSS 50 uM; TRIS-HCl 10 mM; DNA chain 0.3 mM; H2O 90%

sample_conditions_1: pH: 7.5; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D-13C,15N X-filt-13C,15N-edited NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
1H-15N Hetnoesample_1isotropicsample_conditions_1
1D T1sample_1isotropicsample_conditions_1
1D T2(cpmg)sample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

HADDOCK, Bonvin A. M. J. J. - refinemen,structure solution,geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz

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