BMRB Entry 17805

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17805
MolProbity Validation Chart

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Title:
THE HIGH RESOLUTION STRUCTURE OF UBIQUITIN LIKE DOMAIN OF UBLCP1
Deposition date:
2011-07-25
Original release date:
2012-08-31
Authors:
Lee, Weontae; Ko, Sunggeon
Citation:

Citation: Lee, N.; Ko, S.. "The High Resolution Structure of Ubiquitin Like Dom Ublcp1"  To be Published ., .-..

Assembly members:

Assembly members:
UBIQUITIN-LIKE_DOMAIN-CONTAINING_CTD_PHOSPHATASE_1, 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):
UBIQUITIN-LIKE_DOMAIN-CONTAINING_CTD_PHOSPHATASE_1: MALPIIVKWGGQEYSVTTLS EDDTVLDLKQFLKTLTGVLP ERQKLLGLKVKGKPAENDVK LGALKLKPNTKIMMMGTREE S

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts77
1H chemical shifts463

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 11

Entities:

Entity 1, UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1 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: UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1, [U-99% 15N], 1.5 mM; H2O 90%; D2O 10%

sample_2: UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1, [U-95% 13C], 1.5 mM; D2O 100%

sample_3: UBIQUITIN-LIKE DOMAIN-CONTAINING CTD PHOSPHATASE 1, [U-95% 13C; U-95% 15N], 1.5 mM; H2O 90%; D2O 10%

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_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1 15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

MOLMOL_NMRDRAW, Koradi, Billeter and Wuthrich - data analysis

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

ProcheckNMR, Laskowski and MacArthur - refinement

SPARKY, Goddard - chemical shift assignment, peak picking

xwinnmr, Bruker Biospin - processing

TALOS, Cornilescu, Delaglio and Bax - structure solution

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

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

NMR spectrometers:

  • BRUKER DRX 900 MHz

Related Database Links:

BMRB 16899 16908 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