BMRB Entry 16908

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16908

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Title:
The high resolution structure of Ubiquitin like domain of UBLCP1
Deposition date:
2010-04-29
Original release date:
2011-05-02
Authors:
Lee, Weontae; Ko, Sunggeon
Citation:

Citation: Lee, Weontae; Ko, Sunggeon. "Null"  To be Published ., .-..

Assembly members:

Assembly members:
UBLCP1, polymer, 81 residues, 8997.747 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: pGEX 4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBLCP1: MALPIIVKWGGQEYSVTTLS EDDTVLDLKQFLKTLTGVLP ERQKLLGLKVKGKPAENDVK LGALKLKPNTKIMMMGTREE S

Data sets:
Data typeCount
13C chemical shifts258
15N chemical shifts77
1H chemical shifts565

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBLCP11

Entities:

Entity 1, UBLCP1 81 residues - 8997.747 Da.

1   METALALEUPROILEILEVALLYSTRPGLY
2   GLYGLNGLUTYRSERVALTHRTHRLEUSER
3   GLUASPASPTHRVALLEUASPLEULYSGLN
4   PHELEULYSTHRLEUTHRGLYVALLEUPRO
5   GLUARGGLNLYSLEULEUGLYLEULYSVAL
6   LYSGLYLYSPROALAGLUASNASPVALLYS
7   LEUGLYALALEULYSLEULYSPROASNTHR
8   LYSILEMETMETMETGLYTHRARGGLUGLU
9   SER

Samples:

sample_1: UBLdomain of UBLCP1, [U-99% 15N], 1.5 mM; H2O 90%; D2O 10%; HEPES 10 mM; NaCl 100 mM

sample_2: UBLdomain of UBLCP1, [U-99% 13C; U-99% 15N], 1.5 mM; H2O 90%; D2O 10%; HEPES 10 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.2.5, P.GUNTERT ET AL. - structure solution

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

ProcheckNMR, Laskowski and MacArthur - geometry optimization

SPARKY, Goddard - chemical shift assignment

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 900 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 16899 17805 18844
PDB
DBJ BAB71628 BAC31711 BAC34039 BAE28110 BAI46037
EMBL CAH93392
GB AAH13425 AAH85111 AAH89210 AAI05395 AAI06094
REF NP_001014139 NP_001039459 NP_001126990 NP_001253320 NP_077795
SP Q2KJD7 Q5FWT7 Q5R4C4 Q8BGR9 Q8WVY7
TPG DAA27217
AlphaFold Q2KJD7 Q5FWT7 Q5R4C4 Q8BGR9 Q8WVY7

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