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 11090

Title: Solution structure of the N-terminal PapD-like domain of HYDIN protein from human

Deposition date: 2010-01-18 Original release date: 2011-01-19

Authors: Li, H.; Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the N-terminal PapD-like domain of HYDIN protein from human"  .

Assembly members:
PapD-like, UNP residues 182-296, polymer, 122 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: Cell free synthesis   Host organism: E. coli - cell free   Vector: P060327-16

Entity Sequences (FASTA):
PapD-like, UNP residues 182-296: GSSGSSGTEREKFIVPIKAR GARAILDFPDKLNFSTCPVK YSTQKILLVRNIGNKNAVFH IKTCRPFSIEPAIGTLNVGE SMQLEVEFEPQSVGDHSGRL IVCYDTGEKVFVSLYGAAID MN

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts119
1H chemical shifts842

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PapD-like, UNP residues 182-2961

Entities:

Entity 1, PapD-like, UNP residues 182-296 122 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRGLUARG
2   GLULYSPHEILEVALPROILELYSALAARG
3   GLYALAARGALAILELEUASPPHEPROASP
4   LYSLEUASNPHESERTHRCYSPROVALLYS
5   TYRSERTHRGLNLYSILELEULEUVALARG
6   ASNILEGLYASNLYSASNALAVALPHEHIS
7   ILELYSTHRCYSARGPROPHESERILEGLU
8   PROALAILEGLYTHRLEUASNVALGLYGLU
9   SERMETGLNLEUGLUVALGLUPHEGLUPRO
10   GLNSERVALGLYASPHISSERGLYARGLEU
11   ILEVALCYSTYRASPTHRGLYGLULYSVAL
12   PHEVALSERLEUTYRGLYALAALAILEASP
13   METASN

Samples:

sample_1: PapD-like, UNP residues 182-296, [U-13C; U-15N], 1.19 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

PDB
DBJ BAB14314 BAG61096 BAG61346
EMBL CAD38687
GB AAH28351 AIC60203
REF NP_001185471 NP_001185472 NP_001257903 NP_060028 XP_004057985
SP Q4G0P3
AlphaFold Q4G0P3

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