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 18560

Title: NMR solution structure of the N-terminal domain of human USP28. Northeast structural genomics consortium target HT8470A

Deposition date: 2012-06-29 Original release date: 2012-07-31

Authors: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Dhe-Paganon, Sirano; Arrowsmith, Cheryl

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "NMR solution structure of the N-terminal domain of human USP28"  Not known ., .-..

Assembly members:
hs356_22_132, polymer, 129 residues, 12045.456 Da.

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

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

Entity Sequences (FASTA):
hs356_22_132: MHHHHHHSSGRENLYFQGQM LLNQLREITGIQDPSFLHEA LKASNGDITQAVSLLTDERV KEPSQDTVATEPSEVEGSAA NKEVLAKVIDLTHDNKDDLQ AAIALSLLESPKIQADGRDL NRMHEATSA

Data sets:
Data typeCount
13C chemical shifts424
15N chemical shifts117
1H chemical shifts706

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hs356_22_1321

Entities:

Entity 1, hs356_22_132 129 residues - 12045.456 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   ARGGLUASNLEUTYRPHEGLNGLYGLNMET
3   LEULEUASNGLNLEUARGGLUILETHRGLY
4   ILEGLNASPPROSERPHELEUHISGLUALA
5   LEULYSALASERASNGLYASPILETHRGLN
6   ALAVALSERLEULEUTHRASPGLUARGVAL
7   LYSGLUPROSERGLNASPTHRVALALATHR
8   GLUPROSERGLUVALGLUGLYSERALAALA
9   ASNLYSGLUVALLEUALALYSVALILEASP
10   LEUTHRHISASPASNLYSASPASPLEUGLN
11   ALAALAILEALALEUSERLEULEUGLUSER
12   PROLYSILEGLNALAASPGLYARGASPLEU
13   ASNARGMETHISGLUALATHRSERALA

Samples:

sample_1: hs356_22_132, [U-13C; U-15N], 0.5 mM; mops 10 mM; sodium chloride 450 mM; ZnSO4 10 uM; DTT 1 mM; NaN3 0.01%; benzamidine 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19077
PDB
DBJ BAG65214
GB AAH65928 AAK58565 ACA06098 ACA06099 AIC60511
REF NP_065937 XP_001085291 XP_002799842 XP_003253212 XP_004052203
SP Q96RU2

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