BMRB Entry 36768

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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/BMR36768
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Phosphorylation dependent recognition of RIPK1 by phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
Deposition date:
2025-06-20
Original release date:
2026-03-31
Authors:
Liu, J.; Liu, Z.; Xue, H.; Xie, X.; Sun, W.; Chou, J.
Citation:

Citation: Xie, Xingxing; Liu, Jianping; Liang, Wei; Zhang, Yici; Gong, Xueqi; Yuan, Shenghao; Qi, Chunting; Huang, Maoqing; Shi, Linyu; Hou, Meiling; Zhang, Mengmeng; Liu, Wei; Sun, Weimin; Wu, Yaqi; Li, Cui; Cao, Ze; Jing, Hongyang; Qian, Lihui; Liu, Jingli; Yuan, Shufen; Wang, Qiong; Shen, Yong; Liu, Zhijun; Li, Yunxia; Pan, Heling; Zhu, Bing; Shan, Bing; He, Kaiwen; Wang, Wenyuan; Zou, Chengyu; Li, Ying; Chou, James; Yuan, Junying. "Repression of RIPK1 kinase by INPP5D inhibits expression of diverse proinflammatory mediators and late-onset Alzheimer's disease risk factors."  Immunity 59, 419-437 (2026).
PubMed: 41633359

Assembly members:

Assembly members:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1, polymer, 106 residues, 12026.712 Da.
Receptor-interacting serine/threonine-protein kinase 1, polymer, 16 residues, 1936.962 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1: GPGSPGWNHGNITRSKAEEL LSRAGKDGSFLVRASESIPR AYALCVLFRNCVYTYRILPN EDDKFTVQASEGVPMRFFTK LDQLIDFYKKENMGLVTHLQ YPVPLE
Receptor-interacting serine/threonine-protein kinase 1: QEEASXHAFGIFAEKQ

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts108
1H chemical shifts802

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 106 residues - 12026.712 Da.

1   GLYPROGLYSERPROGLYTRPASNHISGLY
2   ASNILETHRARGSERLYSALAGLUGLULEU
3   LEUSERARGALAGLYLYSASPGLYSERPHE
4   LEUVALARGALASERGLUSERILEPROARG
5   ALATYRALALEUCYSVALLEUPHEARGASN
6   CYSVALTYRTHRTYRARGILELEUPROASN
7   GLUASPASPLYSPHETHRVALGLNALASER
8   GLUGLYVALPROMETARGPHEPHETHRLYS
9   LEUASPGLNLEUILEASPPHETYRLYSLYS
10   GLUASNMETGLYLEUVALTHRHISLEUGLN
11   TYRPROVALPROLEUGLU

Entity 2, entity_2 16 residues - 1936.962 Da.

1   GLNGLUGLUALASERPTRHISALAPHEGLY
2   ILEPHEALAGLULYSGLN

Samples:

sample_1: Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1, [U-13C; U-15N], 0.60 mM; Receptor-interacting serine/threonine-protein kinase 1 3.00 mM; DTT 1 mM; EDTA 1 mM; sodium chloride 50 mM; Na2HPO4-NaH2PO4 20 mM; H2O 100%

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

Sparky, Goddard - peak picking

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

NMR spectrometers:

  • Agilent Direct Drive 600 MHz

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