[English] 日本語
Yorodumi
- PDB-2moc: Membrane induced structure of novel human tachykinin Hemokinin-1 ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2moc
TitleMembrane induced structure of novel human tachykinin Hemokinin-1 (hHK1)
ComponentsTachykinin-4
KeywordsNEUROPEPTIDE / Tachykinin
Function / homology
Function and homology information


substance K receptor binding / substance P receptor binding / positive regulation of flagellated sperm motility / tachykinin receptor signaling pathway / negative regulation of sensory perception of pain / regulation of sensory perception of pain / negative regulation of systemic arterial blood pressure / detection of temperature stimulus involved in sensory perception of pain / regulation of blood pressure / positive regulation of cytosolic calcium ion concentration ...substance K receptor binding / substance P receptor binding / positive regulation of flagellated sperm motility / tachykinin receptor signaling pathway / negative regulation of sensory perception of pain / regulation of sensory perception of pain / negative regulation of systemic arterial blood pressure / detection of temperature stimulus involved in sensory perception of pain / regulation of blood pressure / positive regulation of cytosolic calcium ion concentration / receptor ligand activity / inflammatory response / extracellular space
Similarity search - Function
Tachykinin/Neurokinin-like, conserved site / Tachykinin family signature.
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
Model detailsclosest to the average, model1
AuthorsGanjiwale, A. / Cowsik, S.
CitationJournal: To be Published
Title: Membrane induced structure of novel human tachykinin Hemokinin-1
Authors: Ganjiwale, A. / Cowsik, S.
History
DepositionApr 24, 2014Deposition site: BMRB / Processing site: PDBJ
Revision 1.0May 27, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tachykinin-4


Theoretical massNumber of molelcules
Total (without water)1,1871
Polymers1,1871
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50target function
RepresentativeModel #1closest to the average

-
Components

#1: Protein/peptide Tachykinin-4 / Endokinin-A/B


Mass: 1187.388 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Custom synthesized peptide with >99% purity / Source: (synth.) Homo sapiens (human) / References: UniProt: Q86UU9

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
Details: NMR solution structure of Hemokinin-1 in SDS Micelles
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H TOCSY
1212D 1H-1H NOESY

-
Sample preparation

DetailsContents: 4.5 mM Hemokinin-1, 90 % H2O-2, 10 % [U-2H] D2O-3, 300 mM [U-99% 2H] SDS-4, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
4.5 mMHemokinin-11
90 %H2O-21
10 %D2O-3[U-2H]1
300 mMSDS-4[U-99% 2H]1
Sample conditionspH: 3.5 / Pressure: ambient / Temperature: 305 K

-
NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

-
Processing

NMR software
NameVersionDeveloperClassification
CYANA2.1Guntert, Mumenthaler and Wuthrichdata analysis
CYANA2.1Guntert, Mumenthaler and Wuthrichstructure solution
CYANA2.1Guntert, Mumenthaler and Wuthrichrefinement
TopSpinBruker Biospinchemical shift calculation
TopSpinBruker Biospinprocessing
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20 / Representative conformer: 1

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more