BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19065

Title: ADAPT-NMR automated assignments and manual assignments of RNaseA   PubMed: 24619609

Authors: Tonelli, Marco; Eller, Chelcie; Bahrami, Arash; Singarapu, Kiran; Westler, William; Raines, Ronald; Markley, John

Citation: Tonelli, Marco; Eller, Chelcie; Singarapu, Kiran; Lee, Woonghee; Bahrami, Arash; Westler, William; Raines, Ronald; Markley, John. "Assignments of RNase A by ADAPT-NMR and enhancer."  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
RnaseA, polymer, 124 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
RnaseA: KETAAAKFERQHMDSSTSAA SSSNYCNQMMKSRNLTKDRC KPVNTFVHESLADVQAVCSQ KNVACKNGQTNCYQSYSTMS ITDCRETGSSKYPNCAYKTT QANKHIIVACEGNPYVPVHF DASV

Data sets:
Data typeCount
15N chemical shifts116
1H chemical shifts116

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNaseA1

Entities:

Entity 1, RNaseA 124 residues - Formula weight is not available

1   LYSGLUTHRALAALAALALYSPHEGLUARG
2   GLNHISMETASPSERSERTHRSERALAALA
3   SERSERSERASNTYRCYSASNGLNMETMET
4   LYSSERARGASNLEUTHRLYSASPARGCYS
5   LYSPROVALASNTHRPHEVALHISGLUSER
6   LEUALAASPVALGLNALAVALCYSSERGLN
7   LYSASNVALALACYSLYSASNGLYGLNTHR
8   ASNCYSTYRGLNSERTYRSERTHRMETSER
9   ILETHRASPCYSARGGLUTHRGLYSERSER
10   LYSTYRPROASNCYSALATYRLYSTHRTHR
11   GLNALAASNLYSHISILEILEVALALACYS
12   GLUGLYASNPROTYRVALPROVALHISPHE
13   ASPALASERVAL

Samples:

sample_1: RnaseA, [U-100% 13C; U-100% 15N], 1.7 mM; potassium phosphate 100 mM; D2O 10%; H2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 4.7; temperature: 308 K

sample_conditions_2: ionic strength: 100 mM; pH: 4.7; temperature: 308 K

sample_conditions_3: ionic strength: 100 mM; pH: 4.7; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_3
2D 1H-15N HSQCsample_1isotropicsample_conditions_3
3D HN(CA)COsample_1isotropicsample_conditions_3
3D HN(CO)CAsample_1isotropicsample_conditions_3
3D HNCAsample_1isotropicsample_conditions_3
3D CBCA(CO)NHsample_1isotropicsample_conditions_3
3D HN(CA)CBsample_1isotropicsample_conditions_3

Software:

No software information available

NMR spectrometers:

  • Varian DirectDrive 600 MHz
  • Varian DirectDrive 900 MHz

Related Database Links:

BMRB 1072 16010 16011 16503 16742 17099 17172 2928 385 4031 4032 443
PDB
EMBL CAA30263 CAA33801 CAB37066
GB AAA72269 AAA72757 AAB35594 AAB36134 AAI49530
PIR JC5560 NRBOB
PRF 630436A
REF NP_001014408 XP_005211519 XP_005901936 XP_010837737
SP P61823 P61824
TPE CDG32088
TPG DAA25470