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 17272

Title: Solution structures of human PIWI-like 1 PAZ domain   PubMed: 21465557

Deposition date: 2010-11-01 Original release date: 2011-04-08

Authors: Zeng, Lei; Zhang, Qiang; Yan, Kelley; Zhou, Ming-Ming

Citation: Zeng, Lei; Zhang, Qiang; Yan, Kelley; Zhou, Ming-Ming. "Structural insights into piRNA recognition by the human PIWI-like 1 PAZ domain."  Proteins 79, 2004-2009 (2011).

Assembly members:
Human PIWI-like 1 PAZ domain, polymer, 134 residues, 15673.891 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX 4T-1

Entity Sequences (FASTA):
Human PIWI-like 1 PAZ domain: CTDVSHKVLRSETVLDFMFN FYHQTEEHKFQEQVSKELIG LVVLTKYNNKTYRVDDIDWD QNPKSTFKKADGSEVSFLEY YRKQYNQEITDLKQPVLVSQ PKRRRGPGGTLPGPAMLIPE LCYLTGLTDKMRND

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts138
1H chemical shifts878

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human PIWI-like 1 PAZ domain1

Entities:

Entity 1, Human PIWI-like 1 PAZ domain 134 residues - 15673.891 Da.

1   CYSTHRASPVALSERHISLYSVALLEUARG
2   SERGLUTHRVALLEUASPPHEMETPHEASN
3   PHETYRHISGLNTHRGLUGLUHISLYSPHE
4   GLNGLUGLNVALSERLYSGLULEUILEGLY
5   LEUVALVALLEUTHRLYSTYRASNASNLYS
6   THRTYRARGVALASPASPILEASPTRPASP
7   GLNASNPROLYSSERTHRPHELYSLYSALA
8   ASPGLYSERGLUVALSERPHELEUGLUTYR
9   TYRARGLYSGLNTYRASNGLNGLUILETHR
10   ASPLEULYSGLNPROVALLEUVALSERGLN
11   PROLYSARGARGARGGLYPROGLYGLYTHR
12   LEUPROGLYPROALAMETLEUILEPROGLU
13   LEUCYSTYRLEUTHRGLYLEUTHRASPLYS
14   METARGASNASP

Samples:

sample_1: sodium phosphate 100 mM; sodium chloride 150 mM; DTT, [U-100% 2H], 5 mM; D2O 100%

sample_2: sodium phosphate 100 mM; sodium chloride 150 mM; DTT, [U-100% 2H], 5 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 13C-Edited-13C/15N-filtered NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, processing

NMRView v5.04, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 17273
PDB
DBJ BAA93705 BAC04068 BAF49084
GB AAC97371 AAH28581 AAH66846 AAI29858 AAI29859
REF NP_001102323 NP_001177900 NP_001181902 NP_001182640 NP_001302505
SP Q96J94 Q9JMB7
AlphaFold Q96J94 Q9JMB7

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