BMRB Entry 17371

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17371
MolProbity Validation Chart

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Title:
Solution NMR structure of N-terminal Ubiquitin-like domain of FUBI, a ribosomal protein S30 precursor from Homo sapiens. NorthEast Structural Genomics consortium (NESG) target HR6166
Deposition date:
2010-12-20
Original release date:
2011-01-24
Authors:
Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Semesi, Antony; Doherty, Ryan; Dhe-Paganon, Sirano; Arrowsmith, Cheryl
Citation:

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Doherty, Ryan; Semesi, Antony; Dhe-Paganon, Sirano; Arrowsmith, Cheryl. "Solution NMR structure of human Ubiquitin-like protein hs00113."  .

Assembly members:

Assembly members:
hs00113, polymer, 93 residues, 7764.862 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p15Tv lic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hs00113: MGSSHHHHHHSSGLVPRGSM QLFVRAQELHTFEVTGQETV AQIKAHVASLEGIAPEDQVV LLAGAPLEDEATLGQCGVEA LTTLEVAGRMLGG

Data sets:
Data typeCount
13C chemical shifts305
15N chemical shifts72
1H chemical shifts514

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hs001131

Entities:

Entity 1, hs00113 93 residues - 7764.862 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERMET
3   GLNLEUPHEVALARGALAGLNGLULEUHIS
4   THRPHEGLUVALTHRGLYGLNGLUTHRVAL
5   ALAGLNILELYSALAHISVALALASERLEU
6   GLUGLYILEALAPROGLUASPGLNVALVAL
7   LEULEUALAGLYALAPROLEUGLUASPGLU
8   ALATHRLEUGLYGLNCYSGLYVALGLUALA
9   LEUTHRTHRLEUGLUVALALAGLYARGMET
10   LEUGLYGLY

Samples:

sample_1: hs00113, [U-13C; U-15N], 0.5 mM; mops 10 mM; sodium chloride 450 mM; ZnSO4 10 mM; DTT 10 mM; NaN3 0.01%; benzamidine 10 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

Software:

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

SPARKY, Goddard - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - structure validation

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB15515
EMBL CAA44544 CAA44545 CAA46714 CAA46716 CAG46772
GB AAB52915 AAH33877 AAH91402 AAQ87877 AAX36613
REF NP_001012757 NP_001125384 NP_001153703 NP_001153704 NP_001181567
SP P0C2F1 P35544 P55812 Q05474
AlphaFold P0C2F1 P35544 P55812 Q05474

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