PPIRE11138

Target Protein Information
Protein_Name Nibrin
Protein_Sequence MWKLLPAAGAAPGEPYRLLAGVEYVVGRKNCGILIENDQSISRNHAVLTVNFPVTSLSQTDEIPTLTIKDNSKYGTFVNEEKMQTGLSCTLKTGDRVTFGVFESKFRVEYEPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAVESKKQPPDIESFYPPIDEPAIGSKSVDLSGRHERKQIFKGKTFVFLNAKQHKKLSSAVAFGGGEARLMAEDDEEEQSFFSAPGTCVVDVGITNTQLIISHSQKKWIHLIMDTLQRNGLRPIPEAEIGLAVIFMTTENYCNPQGQPCTELKTTTPGPSLSQVLSANGKIIPSAPVNMTTYVADTESEPADTCMPLSERPEEVKIPGLEQSSRKLSQETFNIKEAPKPSSKANNVASDTLVRGKTPSYQLSPMKFPVANKNKDWTSQQQQNSIKNYFQPCTRKRERDEDNPELSSCKSSRMELSCSLLEQTQPAGPSLWKSKEHQSQNATLDREADTSSVGGMDIELNRKSPDRKPLPTETLRPRKRKDVDLATEEEVLEELLRSTKPELAVQVKVEKQEADDTIRKKPRMDAERNRPLNGGSEPESNSALQEDEREKKDELQTESWSTKHEIANSDGLQDSSEELPRKLLLTEFRSLVVSNHNSTSRNLCVNECGPLKNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVQKQQAKEESLADDLFRYNPNVKRR
Organism_Source Mus musculus
Functional_Classification telomeric proteins
Cellular_Localization Nucleus
Gene_Names Nbn
UniProt_ID Q9R207
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name mNBS1_TBM_S433A
Peptide_Sequence MRIPNYQLAPTKL
Peptide_Length 13
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)CCSC)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1544.88
Aliphatic_Index 97.69231
Aromaticity 0.07692
Average_Rotatable_Bonds 3.69231
Charge_at_pH_7 1.99684
Isoelectric_Point 10.45492
Number_of_Hydrogen_Bond_Acceptors 21
Number_of_Hydrogen_Bond_Donors 20
Topological_Polar_Surface_Area 609.50000
X_logP_energy -3.99813
Interaction Information
Affinity KD=21.7 mM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 5WQD
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title NBS1 Phosphorylation Status Dictates Repair Choice of Dysfunctional Telomeres.
Release_Year 2017
PMID 28216226
DOI 10.1016/j.molcel.2017.01.016