BMRB Entry 27978

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27978

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Title:
Complete 1H, 13C, 15N resonance assignments of the Vpr binding region of hHR23A (residues 223-363)
Deposition date:
2019-07-17
Original release date:
2019-11-08
Authors:
Byeon, In-Ja; Jung, Jinwon; Byeon, Chang; Gronenborn, Angela
Citation:

Citation: Byeon, In-Ja; Jung, Jinwon; Byeon, Chang; DeLucia, Maria; Ahn, Jinwoo; Gronenborn, Angela. "Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363)"  Biomol. NMR Assign. 14, 13-17 (2020).
PubMed: 31463759

Assembly members:

Assembly members:
hHR23A, polymer, 149 residues, Formula weight is not available

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: pET21 vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hHR23A: ATEAAGENPLEFLRDQPQFQ NMRQVIQQNPALLPALLQQL GQENPQLLQQISRHQEQFIQ MLNEPPGELADISDVEGEVG AIGEEAPQMNYIQVTPQEKE AIERLKALGFPESLVIQAYF ACEKNENLAANFLLSQNFDD ELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts628
15N chemical shifts165
1H chemical shifts1017

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hHR23A(223-363) monomoer1

Entities:

Entity 1, hHR23A(223-363) monomoer 149 residues - Formula weight is not available

1   ALATHRGLUALAALAGLYGLUASNPROLEU
2   GLUPHELEUARGASPGLNPROGLNPHEGLN
3   ASNMETARGGLNVALILEGLNGLNASNPRO
4   ALALEULEUPROALALEULEUGLNGLNLEU
5   GLYGLNGLUASNPROGLNLEULEUGLNGLN
6   ILESERARGHISGLNGLUGLNPHEILEGLN
7   METLEUASNGLUPROPROGLYGLULEUALA
8   ASPILESERASPVALGLUGLYGLUVALGLY
9   ALAILEGLYGLUGLUALAPROGLNMETASN
10   TYRILEGLNVALTHRPROGLNGLULYSGLU
11   ALAILEGLUARGLEULYSALALEUGLYPHE
12   PROGLUSERLEUVALILEGLNALATYRPHE
13   ALACYSGLULYSASNGLUASNLEUALAALA
14   ASNPHELEULEUSERGLNASNPHEASPASP
15   GLULEUGLUHISHISHISHISHISHIS

Samples:

sample_1: hHR23A(223-363), [U-99% 13C; U-99% 15N], 0.6 ± 0.03 mM; DSS, [U-100% 13C], 0.1 ± 0.01 mM; sodium phosphate 25 ± 1 mM; sodium chloride 50 ± 1 mM; sodium azide 0.02 ± 0.001 %; zinc sulphate 1 ± 0.05 mM; EDTA 1 ± 0.05 mM; TCEP 1 ± 0.05 mM

sample_2: hHR23A(223-363), [U-99% 13C; U-99% 15N], 1.2 ± 0.06 mM; DSS, [U-100% 13C], 0.1 ± 0.01 mM; sodium phosphate 25 ± 1 mM; sodium chloride 50 ± 1 mM; sodium azide 0.02 ± 0.001 %; zinc sulphate 1 ± 0.05 mM; EDTA 1 ± 0.05 mM; TCEP 1 ± 0.05 mM

sample_3: hHR23A(223-363), [U-99% 13C; U-99% 15N], 2.7 ± 0.1 mM; DSS, [U-100% 13C], 0.1 ± 0.01 mM; HEPES 10 ± 0.5 mM; sodium chloride 50 ± 1 mM; sodium azide 0.02 ± 0.001 %; zinc sulphate 1 ± 0.05 mM; EDTA 1 ± 0.05 mM; TCEP 1 ± 0.05 mM

sample_4: hHR23A(223-363), [U-99% 13C; U-99% 15N], 0.084 ± 0.05 mM; MES 10 ± 0.5 mM; sodium chloride 50 ± 1 mM; sodium azide 0.02 ± 0.001 %; DTT 2 ± 0.1 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.050 M; pH: 6.5; pressure: 1 atm; temperature: 291 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_2
3D HNCACBsample_4isotropicsample_conditions_2
3D HNCOsample_4isotropicsample_conditions_2
3D HN(CA)COsample_4isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP P54725
AlphaFold Q5M7Z1

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