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 17762

Title: Solution structure of the monomeric derivative of BS-RNase   PubMed: 22253705

Deposition date: 2011-07-06 Original release date: 2012-01-23

Authors: Spadaccini, Roberta; Picone, Delia

Citation: Spadaccini, Roberta; Ercole, Carmine; Gentile, Maria; Sanfelice, Domenico; Boelens, Rolf; Wechselberger, Rainer; Batta, Gyula; Bernini, Andrea; Niccolai, Neri; Picone, Delia. "NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping."  PLoS ONE 7, .-. (2012).

Assembly members:
mBS, polymer, 124 residues, 13633.684 Da.

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b(+)

Entity Sequences (FASTA):
mBS: KESAAAKFERQHMDSGNSPS SSSNYCNLMMCCRKMTQGKC KPVNTFVHESLADVKAVCSQ KKVTCKDGQTNCYQSKSTMR ITDCRETGSSKYPNCAYKTT QVEKHIIVACGGKPSVPVHF DASV

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts132
1H chemical shifts634

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mBS1

Entities:

Entity 1, mBS 124 residues - 13633.684 Da.

1   LYSGLUSERALAALAALALYSPHEGLUARG
2   GLNHISMETASPSERGLYASNSERPROSER
3   SERSERSERASNTYRCYSASNLEUMETMET
4   CYSCYSARGLYSMETTHRGLNGLYLYSCYS
5   LYSPROVALASNTHRPHEVALHISGLUSER
6   LEUALAASPVALLYSALAVALCYSSERGLN
7   LYSLYSVALTHRCYSLYSASPGLYGLNTHR
8   ASNCYSTYRGLNSERLYSSERTHRMETARG
9   ILETHRASPCYSARGGLUTHRGLYSERSER
10   LYSTYRPROASNCYSALATYRLYSTHRTHR
11   GLNVALGLULYSHISILEILEVALALACYS
12   GLYGLYLYSPROSERVALPROVALHISPHE
13   ASPALASERVAL

Samples:

sample_1: mBS, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: mBS, [U-100% 15N], 1 mM; H2O 90%; D2O 10%

comditions_1: pH: 5.8; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropiccomditions_1
3D HNCAsample_1isotropiccomditions_1
3D HNCACBsample_1isotropiccomditions_1
3D CBCA(CO)NHsample_1isotropiccomditions_1
3D HCCH-TOCSYsample_1isotropiccomditions_1
2D 1H-15N HSQCsample_2isotropiccomditions_1
3D 1H-15N NOESYsample_2isotropiccomditions_1
3D 1H-13C NOESY aliphaticsample_1isotropiccomditions_1
2D 1H-13C HSQC aromaticsample_1isotropiccomditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Related Database Links:

PDB
EMBL CAA04155 CAA26832 CAA35716
GB AAB27820 AAB36140 ELR52955
REF NP_861526 XP_005211518 XP_005900636 XP_010837733
SP P00669
TPE CDG32087
TPG DAA25468

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