BMRB Entry 34638

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34638
MolProbity Validation Chart

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Title:
Structure of the human UFC1 protein in complex with the UBA5 C-terminal UFC1-binding motif.
Deposition date:
2021-06-14
Original release date:
2021-08-02
Authors:
Wesch, W.; Loehr, F.; Rogova, N.; Doetsch, V.; Rogov, V.
Citation:

Citation: Wesch, W.; Loehr, F.; Rogova, N.; Doetsch, V.; Rogov, V.. "A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1"  Int. J. Mol. Sci. 22, 7390-7390 (2021).
PubMed: 34299007

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 19486.395 Da.
entity_2, polymer, 27 residues, 3034.459 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: pET39_Ub19

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MADEATRRVVSEIPVLKTNA GPRDRELWVQRLKEEYQSLI RYVENNKNADNDWFRLESNK EGTRWFGKCWYIHDLLKYEF DIEFDIPITYPTTAPEIAVP ELDGKTAKMYRGGKICLTDH FKPLWARNVPKFGLAHLMAL GLGPWLAVEIPDLIQKGVIQ HKEKCNQ
entity_2: GMSVTELTVEDSGESLEDLM AKMKNMW

Data sets:
Data typeCount
13C chemical shifts676
15N chemical shifts196
1H chemical shifts1396

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 167 residues - 19486.395 Da.

1   METALAASPGLUALATHRARGARGVALVAL
2   SERGLUILEPROVALLEULYSTHRASNALA
3   GLYPROARGASPARGGLULEUTRPVALGLN
4   ARGLEULYSGLUGLUTYRGLNSERLEUILE
5   ARGTYRVALGLUASNASNLYSASNALAASP
6   ASNASPTRPPHEARGLEUGLUSERASNLYS
7   GLUGLYTHRARGTRPPHEGLYLYSCYSTRP
8   TYRILEHISASPLEULEULYSTYRGLUPHE
9   ASPILEGLUPHEASPILEPROILETHRTYR
10   PROTHRTHRALAPROGLUILEALAVALPRO
11   GLULEUASPGLYLYSTHRALALYSMETTYR
12   ARGGLYGLYLYSILECYSLEUTHRASPHIS
13   PHELYSPROLEUTRPALAARGASNVALPRO
14   LYSPHEGLYLEUALAHISLEUMETALALEU
15   GLYLEUGLYPROTRPLEUALAVALGLUILE
16   PROASPLEUILEGLNLYSGLYVALILEGLN
17   HISLYSGLULYSCYSASNGLN

Entity 2, unit_2 27 residues - 3034.459 Da.

1   GLYMETSERVALTHRGLULEUTHRVALGLU
2   ASPSERGLYGLUSERLEUGLUASPLEUMET
3   ALALYSMETLYSASNMETTRP

Samples:

sample_1: Ubiquitin-fold modifier-conjugating enzyme 1, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; Ubiquitin-like modifier-activating enzyme 5 1.0 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 100 ± 1 mM; TCEP 2 ± 0.1 mM; AEBSF protease inhibitor 5 ± 0.1 mM; DSS 0.15 ± 0.01 mM

sample_2: Ubiquitin-fold modifier-conjugating enzyme 1 1.2 ± 0.05 mM; Ubiquitin-like modifier-activating enzyme 5, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 100 ± 1 mM; TCEP 2 ± 0.1 mM; AEBSF protease inhibitor 5 ± 0.1 mM; DSS 0.15 ± 0.01 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D [15N,1H]-TROSY-(H)C(CC)(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D [15N,1H]-TROSY-H(C)(CC)(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCACBsample_1isotropicsample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-HSQCsample_1isotropicsample_conditions_1
3D F1-13C/15N-filtered NOESY-[15N,1H]-SOFAST-HMQCsample_1isotropicsample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-SOFAST-HMQC (aro)sample_1isotropicsample_conditions_1
3D NOESY-[13C,1H]-SOFAST-HMQC (aro)sample_1isotropicsample_conditions_1
3D NOESY-[13C,1H]-HSQC (aliphatic region)sample_1isotropicsample_conditions_1
3D NOESY-BEST-[15N,1H]-TROSYsample_1isotropicsample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCAsample_2isotropicsample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCACBsample_2isotropicsample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-HSQCsample_2isotropicsample_conditions_1
3D [15N,1H]-TROSY-(H)C(CC)(CO)NH-TOCSYsample_2isotropicsample_conditions_1
3D NOESY [13C,1H]-HSQCsample_2isotropicsample_conditions_1
3D [15N,1H]-TROSY-H(CC)(CO)NH-TOCSYsample_2isotropicsample_conditions_1
3D NOESY-[15N,1H]-SOFAST-HMQCsample_2isotropicsample_conditions_1

Software:

TopSpin v3.6.2, Bruker Biospin - collection

Sparky v3.114, Goddard - chemical shift assignment, peak picking

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp v1.4, Koradi, R., Billeter, M. and Guentert, P - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 700 MHz
  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE NEO 900 MHz
  • Bruker AVANCE III 950 MHz
  • Bruker AVANCE II 600 MHz

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