BMRB Entry 31281

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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/BMR31281
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
Solution NMR Structure of the PACS1 Furin binding region (FBR)
Deposition date:
2025-11-05
Original release date:
2026-03-31
Authors:
Byeon, I.; Krzysiak, T.; Gronenborn, A.
Citation:

Citation: Krzysiak, T.; Byeon, I.; Ponticelli, R.; Lucas, M.; Thompson, L.; DeHaven, C.; Thomas, G.; Gronenborn, A.. "The R203W Substitution Drives PACS-1 Syndrome by Disrupting Intramolecular Regulation"  .

Assembly members:

Assembly members:
entity_1, polymer, 173 residues, 19572.920 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNLYATWEVDRSSSSCVPRL FSLTLKKLVMLKEMDKDLNS VVIAVKLQGSKRILRSNEIV LPASGLVETELQLTFSLQYP HFLKRDANKLQIMLQRRKRY KNRTILGYKTLAVGLINMAE VMQHPNEGALVLGLHSNVKD VSVKVAEIWIASLSSQPIDH EGIKSKLSDRSPD

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts181
1H chemical shifts1221

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 173 residues - 19572.920 Da.

1   METASNLEUTYRALATHRTRPGLUVALASP
2   ARGSERSERSERSERCYSVALPROARGLEU
3   PHESERLEUTHRLEULYSLYSLEUVALMET
4   LEULYSGLUMETASPLYSASPLEUASNSER
5   VALVALILEALAVALLYSLEUGLNGLYSER
6   LYSARGILELEUARGSERASNGLUILEVAL
7   LEUPROALASERGLYLEUVALGLUTHRGLU
8   LEUGLNLEUTHRPHESERLEUGLNTYRPRO
9   HISPHELEULYSARGASPALAASNLYSLEU
10   GLNILEMETLEUGLNARGARGLYSARGTYR
11   LYSASNARGTHRILELEUGLYTYRLYSTHR
12   LEUALAVALGLYLEUILEASNMETALAGLU
13   VALMETGLNHISPROASNGLUGLYALALEU
14   VALLEUGLYLEUHISSERASNVALLYSASP
15   VALSERVALLYSVALALAGLUILETRPILE
16   ALASERLEUSERSERGLNPROILEASPHIS
17   GLUGLYILELYSSERLYSLEUSERASPARG
18   SERPROASP

Samples:

sample_1: PCAS1, [U-100% 13C; U-100% 15N], 0.6 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_2: PACS1, [U-100% 13C; U-100% 15N; U-100% 2H], 0.2 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_3: PACS1, [U-100% 13C; U-100% 15N; U-100% 2H], 0.1 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_4: PACS1, [U-100% 13C; U-100% 15N; U-100% 2H], 0.05 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_5: PACS1, [U-100% 13C; U-100% 15N; U-100% 2H], 0.3 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_6: PACS1, [U-100% 13C; U-100% 15N], 0.6 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_7: PACS1, [U-100% 13C; U-100% 15N], 0.6 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_8: PACS1, [U-100% 13C; U-100% 15N], 0.3 ± 0.015 mM; citrate buffer 20 mM; NaCl 70 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D simultaneous 13C/15N-edited NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D TROSY-HNCACBsample_5isotropicsample_conditions_1
3D simultaneous 13C/15N-edited NOESYsample_6isotropicsample_conditions_1
3D TROSY-HNCOCACBsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D simultaneous 13C/15N-edited NOESYsample_7isotropicsample_conditions_1
3D HCCH-TOCSYsample_7isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(COCA)CBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HN(COCA)CBsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D simultaneous 13C/15N-edited NOESYsample_8isotropicsample_conditions_1
3D HCCH-TOCSYsample_8isotropicsample_conditions_1

Software:

X-PLOR NIH v3.6, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

CcpNmr Analysis v2.4, CCPN - chemical shift assignment

TopSpin v3.0, Bruker Biospin - collection

CcpNmr Analysis, CCPN - data analysis, peak picking

TopSpin, Bruker Biospin - processing

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 700 MHz
  • Bruker AVANCE 600 MHz

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