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 7206

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Human RNase 7   PubMed: 17150966

Deposition date: 2006-07-04 Original release date: 2006-08-14

Authors: Huang, Yu-Chie

Citation: Huang, Yu-Chie; Lin, Yu-Min; Chang, Tin-Wei; Wu, Shi-Jung; Lee, Yan-Shin; Yu, Hui-Ming; Chang, Dah-Tsyr; Chen, Chinpan; Wu, Shih-Hsiung; Liao, You-Di. "The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity"  J. Biol. Chem. 282, 4626-4633 (2007).

Assembly members:
human RNase 7, polymer, 129 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
human RNase 7: MKPKGMTSSQWFKIQHMQPS PQACNSAMKNINKHTKRCKD LNTFLHEPFSSVAATCQTPK IACKNGDKNCHQSHGPVSLT MCKLTSGKYPNCRYKEKRQN KSYVVACKPPQKKDSQQFHL VPVHLDRVL

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts118
1H chemical shifts849

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human RNase 71

Entities:

Entity 1, human RNase 7 129 residues - Formula weight is not available

1   METLYSPROLYSGLYMETTHRSERSERGLN
2   TRPPHELYSILEGLNHISMETGLNPROSER
3   PROGLNALACYSASNSERALAMETLYSASN
4   ILEASNLYSHISTHRLYSARGCYSLYSASP
5   LEUASNTHRPHELEUHISGLUPROPHESER
6   SERVALALAALATHRCYSGLNTHRPROLYS
7   ILEALACYSLYSASNGLYASPLYSASNCYS
8   HISGLNSERHISGLYPROVALSERLEUTHR
9   METCYSLYSLEUTHRSERGLYLYSTYRPRO
10   ASNCYSARGTYRLYSGLULYSARGGLNASN
11   LYSSERTYRVALVALALACYSLYSPROPRO
12   GLNLYSLYSASPSERGLNGLNPHEHISLEU
13   VALPROVALHISLEUASPARGVALLEU

Samples:

sample_1: human RNase 7, [U-95% 13C; U-90% 15N], 0.6 mM

conditions_1: pH: 3.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D TOCSYsample_1not availableconditions_1
2D NOESYsample_1not availableconditions_1
2D 1H-13C HSQCsample_1not availableconditions_1
2D 1H-15N HSQCsample_1not availableconditions_1
3D HNCACBsample_1not availableconditions_1
3D CBCA(CO)NHsample_1not availableconditions_1
3D HNCOsample_1not availableconditions_1
3D HN(CA)COsample_1not availableconditions_1
3D 15N NOESY-HSQCsample_1not availableconditions_1
3D 15N TOCSY-HSQCsample_1not availableconditions_1
3D C(CO)NHsample_1not availableconditions_1
3D HC(CO)NHsample_1not availableconditions_1
3D HCCH-TOCSYsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • BRUKER DRX 600 MHz
  • BRUKER AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAF85386
EMBL CAC20410 CAC84457 CAC84458 CAC84462
GB AAH74960 AAI12335 AAO12510 AAQ89455 AIC57364
REF NP_115961 XP_003314288 XP_003804787 XP_004054925
SP Q9H1E1
TPE CDG31915 CDG31930 CDG31937

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