BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
11443 Chemical Shifts: 1 set
Crystal structure of the UBA domain of p62 and its interaction with ubiquitin Crystal structure of the UBA domain of p62 and its interaction with ubiquitin Download bibtex for citation iamge Daichi Morimoto, Hidehito Tochio, Keiji Tanaka, Kyouhei Arita, Masaaki Komatsu, Masahiro Shirakawa, Satoru Unzai, Shin Isogai, Takeshi Tenno, Yu-shin Sou
11420 Chemical Shifts: 1 set
NMR structure of vasoactive intestinal peptide in DPC Micelle Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments. Download bibtex for citation iamge Hidekazu Hiroaki, Masahiro Shirakawa, Natsuko Goda, Takahisa Ikegami, Takeshi Tenno, Yoshitaka Umetsu
11419 Chemical Shifts: 1 set
NMR structure of vasoactive intestinal peptide in Methanol Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments. Download bibtex for citation iamge Hidekazu Hiroaki, Masahiro Shirakawa, Natsuko Goda, Takahisa Ikegami, Takeshi Tenno, Yoshitaka Umetsu
11250 Chemical Shifts: 1 set
Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal. Structure and Function of the N-terminal Nucleolin Binding Domain of Nuclear Valosin-containing Protein-like 2 (NVL2) Harboring a Nucleolar Localization Signal. Download bibtex for citation iamge Hidekazu Hiroaki, Ken-Ichiro Fujiwara, Masahiro Shirakawa, Naoko Iwaya, Natsuko Goda, Takeshi Tenno, Yoshie Fujiwara
11149 Chemical Shifts: 1 set
Structural study of the UBA domain of p62 and its interaction with ubiquitin Structural study of the UBA domain of p62 and its interaction with ubiquitin Download bibtex for citation iamge Daichi Morimoto, Hidehito Tochio, Shin Isogai, Takeshi Tenno
11075 Chemical Shifts: 1 set
1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain of kp60 A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization. Download bibtex for citation iamge Hidehito Tochio, Hidekazu Hiroaki, Kohei Akiyama, Masahiro Shirakawa, Naoko Iwaya, Natsuko Goda, Shogo Mase, Takahisa Ikegami, Takeshi Tenno, Yohta Kuwahara, Yoshie Fujiwara