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 17260

Title: Backbone and side-chain 1H, 13C and 15N assignments of the UCHL1 S18Y variant   PubMed: 21298373

Deposition date: 2010-10-20 Original release date: 2011-02-10

Authors: Tse, Ho Sum; Sze, Kong Hung

Citation: Tse, Ho-Sum; Hu, Hong-Yu; Sze, Kong-Hung. "Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1."  Biomol. NMR Assignments 5, 165-168 (2011).

Assembly members:
UCHL1_S18Y_variant, polymer, 231 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
UCHL1_S18Y_variant: MQLKPMEINPEMLNKVLYRL GVAGQWRFVDVLGLEEESLG SVPAPACALLLLFPLTAQHE NFRKKQIEELKGQEVSPKVY FMKQTIGNSCGTIGLIHAVA NNQDKLGFEDGSVLKQFLSE TEKMSPEDRAKCFEKNEAIQ AAHDAVAQEGQCRVDDKVNF HFILFNNVDGHLYELDGRMP FPVNHGASSEDTLLKDAAKV CREFTEREQGEVRFSAVALC KAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts842
15N chemical shifts236
1H chemical shifts1384

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UCHL1 S18Y variant1

Entities:

Entity 1, UCHL1 S18Y variant 231 residues - Formula weight is not available

Residues 226-231 represent a non-native affinity His tag

1   METGLNLEULYSPROMETGLUILEASNPRO
2   GLUMETLEUASNLYSVALLEUTYRARGLEU
3   GLYVALALAGLYGLNTRPARGPHEVALASP
4   VALLEUGLYLEUGLUGLUGLUSERLEUGLY
5   SERVALPROALAPROALACYSALALEULEU
6   LEULEUPHEPROLEUTHRALAGLNHISGLU
7   ASNPHEARGLYSLYSGLNILEGLUGLULEU
8   LYSGLYGLNGLUVALSERPROLYSVALTYR
9   PHEMETLYSGLNTHRILEGLYASNSERCYS
10   GLYTHRILEGLYLEUILEHISALAVALALA
11   ASNASNGLNASPLYSLEUGLYPHEGLUASP
12   GLYSERVALLEULYSGLNPHELEUSERGLU
13   THRGLULYSMETSERPROGLUASPARGALA
14   LYSCYSPHEGLULYSASNGLUALAILEGLN
15   ALAALAHISASPALAVALALAGLNGLUGLY
16   GLNCYSARGVALASPASPLYSVALASNPHE
17   HISPHEILELEUPHEASNASNVALASPGLY
18   HISLEUTYRGLULEUASPGLYARGMETPRO
19   PHEPROVALASNHISGLYALASERSERGLU
20   ASPTHRLEULEULYSASPALAALALYSVAL
21   CYSARGGLUPHETHRGLUARGGLUGLNGLY
22   GLUVALARGPHESERALAVALALALEUCYS
23   LYSALAALALEUGLUHISHISHISHISHIS
24   HIS

Samples:

sample_1: UCHL1 S18Y variant, [U-99% 13C; U-99% 15N], 0.7 – 0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16537
PDB
DBJ BAA28214 BAB33087 BAD51987 BAE87282 BAG37761
EMBL CAA28443
GB AAD09172 AAH00332 AAH05117 AAH06305 AAY40923
REF NP_004172 XP_002745940 XP_002814743 XP_003258669 XP_003800742
SP P09936 Q60HC8 Q9GM50

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