BMRB Entry 31080

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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/BMR31080
MolProbity Validation Chart

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Title:
BIVALENT INTERACTIONS OF PIN1 WITH THE C-TERMINAL TAIL OF PKC
Deposition date:
2023-04-11
Original release date:
2024-04-30
Authors:
Dixit, K.; Yang, Y.; Chen, X.; Igumenova, T.
Citation:

Citation: Dixit, K.; Yang, Y.; Chen, X.; Igumenova, T.. "Sequestration Without Isomerization: Non-Catalytic Role of Pin1 in PKC Regulation"  .

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 18271.309 Da.
entity_2, polymer, 25 residues, 2852.888 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 BL21(DE3)   Vector: PET SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MADEEKLPPGWEKRMSRSSG RVYYFNHITNASQWERPSGN SSSGGKNGQGEPARVRCSHL LVKHSQSRRPSSWRQEKITR TKEEALELINGYIQKIKSGE EDFESLASQFSDCSSAKARG DLGAFSRGQMQKPFEDASFA LRTGEMSGPVFTDSGIHIIL RTE
entity_2: XVLXPPDQEVIRNIDQSEFE GFXFX

Data typeCount
13C chemical shifts678
15N chemical shifts187
1H chemical shifts1095

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 163 residues - 18271.309 Da.

1   METALAASPGLUGLULYSLEUPROPROGLY
2   TRPGLULYSARGMETSERARGSERSERGLY
3   ARGVALTYRTYRPHEASNHISILETHRASN
4   ALASERGLNTRPGLUARGPROSERGLYASN
5   SERSERSERGLYGLYLYSASNGLYGLNGLY
6   GLUPROALAARGVALARGCYSSERHISLEU
7   LEUVALLYSHISSERGLNSERARGARGPRO
8   SERSERTRPARGGLNGLULYSILETHRARG
9   THRLYSGLUGLUALALEUGLULEUILEASN
10   GLYTYRILEGLNLYSILELYSSERGLYGLU
11   GLUASPPHEGLUSERLEUALASERGLNPHE
12   SERASPCYSSERSERALALYSALAARGGLY
13   ASPLEUGLYALAPHESERARGGLYGLNMET
14   GLNLYSPROPHEGLUASPALASERPHEALA
15   LEUARGTHRGLYGLUMETSERGLYPROVAL
16   PHETHRASPSERGLYILEHISILEILELEU
17   ARGTHRGLU

Entity 2, unit_2 25 residues - 2852.888 Da.

1   ACEVALLEUTPOPROPROASPGLNGLUVAL
2   ILEARGASNILEASPGLNSERGLUPHEGLU
3   GLYPHESEPPHENH2

Samples:

sample_1: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 1.05 mM; The C-terminal tail of PKC 0.9 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_2: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 1.05 mM; The C-terminal tail of PKC 0.9 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_3: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 1 mM; The C-terminal tail of PKC 1.3 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_4: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 0.8 mM; The C-terminal tail of PKC 5.5 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_5: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 0.5 mM; The C-terminal tail of PKC 1.8 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_6: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 0.5 mM; The C-terminal tail of PKC 2.5 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_7: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 1 mM; The C-terminal tail of PKC 1.5 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_8: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 1.3 mM; The C-terminal tail of PKC 1 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_9: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, [U-13C; U-15N], 0.8 mM; The C-terminal tail of PKC 1.3 mM; imidazole, [U-100% 2H], 10 mM; potassium chloride 100 mM; TCEP 1 mM; sodium azide 0.02 % w/v

sample_conditions_1: ionic strength: 0.1 M; pH: 6.66; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pH: 6.66; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D [15N,1H] HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 15N-EDITED NOESY- HSQCsample_1isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-15N-HSQCsample_1isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-13C-HSQCsample_2isotropicsample_conditions_2
3D 13C-EDITED NOESY- HSQCsample_2isotropicsample_conditions_2
3D 13Caro-EDITED NOESY- HSQCsample_2isotropicsample_conditions_2
2D CT [13C, 1H] HSQCsample_2isotropicsample_conditions_2
2D CT 1H-13C AROMATIC HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HCCH-COSYsample_2isotropicsample_conditions_2
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D [F1] 13C, 15N- FILTERED NOESYsample_3isotropicsample_conditions_1
2D [F2] 13C,15N- FILTERED NOESYsample_3isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED NOESYsample_3isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED TOCSYsample_3isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-15N-HSQCsample_4isotropicsample_conditions_1
3D [F1] 13C, 15N-FILTERED NOESY- 13Caro-HSQCsample_4isotropicsample_conditions_1
2D [F1] 13C,15N- FILTERED NOESYsample_5isotropicsample_conditions_1
2D [F2] 13C,15N- FILTERED NOESYsample_5isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED NOESYsample_5isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED TOCSYsample_5isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-15N-HSQCsample_6isotropicsample_conditions_1
3D [F1] 13C, 15N-FILTERED NOESY- 13Caro-HSQCsample_6isotropicsample_conditions_1
3D [F1] 13C, 15N-FILTERED NOESY- 13Cali-HSQCsample_6isotropicsample_conditions_1
2D [15N,1H] HSQCsample_6isotropicsample_conditions_1
2D CT [13C, 1H] HSQCsample_6isotropicsample_conditions_1
3D HNCACBsample_6isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-15N-HSQCsample_7isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-13C-HSQCsample_7isotropicsample_conditions_1
2D [15N,1H] HSQCsample_7isotropicsample_conditions_1
2D CT [13C, 1H] HSQCsample_7isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-15N-HSQCsample_8isotropicsample_conditions_1
3D [F1] 13C,15N-FILTERED NOESY-13C-HSQCsample_8isotropicsample_conditions_1
2D [F1] 13C, 15N- FILTERED NOESYsample_9isotropicsample_conditions_1
2D [F2] 13C, 15N- FILTERED NOESYsample_9isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED NOESYsample_9isotropicsample_conditions_1
2D [F1,F2] 13C,15N-FILTERED TOCSYsample_9isotropicsample_conditions_1

Software:

X-PLOR NIH, SCHWIETERS, KUSZEWSKI, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler, and Wuthrich - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 500 MHz

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