BMRB Entry 16899

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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/BMR16899
MolProbity Validation Chart

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Title:
The solution structure of the mutant of UBL domain of UBLCP1, I5M.
Deposition date:
2010-04-23
Original release date:
2015-06-19
Authors:
Lee, Weontae; Ko, Sunggeon
Citation:

Citation: Lee, Weontae; Ko, Sunggeon. "The solution structure of the mutant of UBL domain of UBLCP1, I5M."  To be Published ., .-..

Assembly members:

Assembly members:
UBLCP1, polymer, 81 residues, 9015.780 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: MALPMIVKWGGQEYSVTTLS EDDTVLDLKQFLKTLTGVLP ERQKLLGLKVKGKPAENDVK LGALKLKPNTKIMMMGTREE S

Data sets:
Data typeCount
13C chemical shifts340
15N chemical shifts76
1H chemical shifts562

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBLCP11

Entities:

Entity 1, UBLCP1 81 residues - 9015.780 Da.

this protein is the mutant of UBL domain of UBLCP1. The mutation site is M5. Original sequence is "MALPIIVK" nad mutant sequence is "MALPMIVK".

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

Samples:

sample_1: UBLI5M, [U-99% 15N], 1.5 mM; H2O 90%; D2O 10%; HEPES 10 mM; NaCl 100 mM; DTT 5 mM

sample_2: UBLI5M, [U-99% 13C; U-99% 15N], 1.5 mM; H2O 90%; D2O 10%; HEPES 10 mM; NaCl 100 mM; DTT 5 mM

sample_3: UBLI5M, [U-100% 13C], 1.5 mM; D2O 100%; HEPES 10 mM; NaCl 100 mM; DTT 5 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_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.2.5, P.GUNTERT ET AL. - refinement, 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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - processing

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 900 MHz

Related Database Links:

BMRB 16908 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