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 17952

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for E.coli Ribonuclease P protein   PubMed: 22423363

Deposition date: 2011-09-21 Original release date: 2011-12-09

Authors: Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyongseok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok

Citation: Shin, Jae-Sun; Kim, Kwang-Sun; Ryu, Kyoung-Seok; Han, Kook; Lee, Younghoon; Choi, Byong-Seok. "Structural analysis of Escherichia coli C5 protein."  Proteins 80, 963-967 (2012).

Assembly members:
E.coli_Ribonuclease_P_protein, polymer, 119 residues, 13818.382 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
E.coli_Ribonuclease_P_protein: MVKLAFPRELRLLTPSQFTF VFQQPQRAGTPQITILGRLN SLGHPRIGLTVAKKNVRRAH ERNRIKRLTRESFRLRQHEL PAMDFVVVAKKGVADLDNRA LSEALEKLWRRHCRLARGS

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts116
1H chemical shifts560

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C5 protein monomer1

Entities:

Entity 1, C5 protein monomer 119 residues - 13818.382 Da.

1   METVALLYSLEUALAPHEPROARGGLULEU
2   ARGLEULEUTHRPROSERGLNPHETHRPHE
3   VALPHEGLNGLNPROGLNARGALAGLYTHR
4   PROGLNILETHRILELEUGLYARGLEUASN
5   SERLEUGLYHISPROARGILEGLYLEUTHR
6   VALALALYSLYSASNVALARGARGALAHIS
7   GLUARGASNARGILELYSARGLEUTHRARG
8   GLUSERPHEARGLEUARGGLNHISGLULEU
9   PROALAMETASPPHEVALVALVALALALYS
10   LYSGLYVALALAASPLEUASPASNARGALA
11   LEUSERGLUALALEUGLULYSLEUTRPARG
12   ARGHISCYSARGLEUALAARGGLYSER

Samples:

E.coli_Ribonuclease_P_protein_sample: E.coli Ribonuclease P protein, [U-95% 13C; U-95% 15N], 0.8 ± 0.2 mM; H2O 90%; D2O 10%; Sodium Phosphate 25 mM; Sodium Chloride 200 mM

E.coli_Ribonuclease_P_protein_conditions: ionic strength: 0.2 M; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
2D 1H-13C HSQCE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D CBCA(CO)NHE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D C(CO)NHE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D HNCOE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D HNCACBE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D HBHA(CO)NHE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D HCCH-TOCSYE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D HCCH-COSYE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D 1H-13C NOESY aliphaticE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions
3D 1H-15N NOESYE.coli_Ribonuclease_P_protein_sampleisotropicE.coli_Ribonuclease_P_protein_conditions

Software:

SPARKY, Goddard - data analysis

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB38062 BAE77590 BAG79514 BAI28036 BAI33155
EMBL CAA25983 CAD03155 CAP78163 CAQ34048 CAQ91434
GB AAA24567 AAA62055 AAC76727 AAG58901 AAL22699
PIR AG0957
PRF 1112173A
REF NP_312666 NP_418159 NP_458102 NP_462740 NP_709496
SP A1AHN8 A7ZTR0 A8A6G5 A8ACL6 A9MJT8

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts