[English] 日本語
Yorodumi
- PDB-8r9h: Multicopy-refined carboxymyoglobin photolysis time series at 23 m... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8r9h
TitleMulticopy-refined carboxymyoglobin photolysis time series at 23 mJ/cm2 laser fluence, 661 fs time delay
ComponentsMyoglobin
KeywordsOXYGEN STORAGE / Free-electron laser / time-resolved crystallography / serial crystallography
Function / homology
Function and homology information


Oxidoreductases; Acting on other nitrogenous compounds as donors / nitrite reductase activity / oxygen transport / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / removal of superoxide radicals / oxygen carrier activity / peroxidase activity / oxygen binding / heme binding / metal ion binding
Similarity search - Function
Myoglobin / Globin domain profile. / Globin / Globin / Globin-like superfamily
Similarity search - Domain/homology
CARBON MONOXIDE / PROTOPORPHYRIN IX CONTAINING FE / Myoglobin
Similarity search - Component
Biological speciesEquus caballus (horse)
MethodX-RAY DIFFRACTION / FREE ELECTRON LASER / FOURIER SYNTHESIS / Resolution: 1.4 Å
AuthorsBarends, T. / Schlichting, I.
Funding support Germany, 1items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Nature / Year: 2024
Title: Influence of pump laser fluence on ultrafast myoglobin structural dynamics.
Authors: Barends, T.R.M. / Gorel, A. / Bhattacharyya, S. / Schiro, G. / Bacellar, C. / Cirelli, C. / Colletier, J.P. / Foucar, L. / Grunbein, M.L. / Hartmann, E. / Hilpert, M. / Holton, J.M. / ...Authors: Barends, T.R.M. / Gorel, A. / Bhattacharyya, S. / Schiro, G. / Bacellar, C. / Cirelli, C. / Colletier, J.P. / Foucar, L. / Grunbein, M.L. / Hartmann, E. / Hilpert, M. / Holton, J.M. / Johnson, P.J.M. / Kloos, M. / Knopp, G. / Marekha, B. / Nass, K. / Nass Kovacs, G. / Ozerov, D. / Stricker, M. / Weik, M. / Doak, R.B. / Shoeman, R.L. / Milne, C.J. / Huix-Rotllant, M. / Cammarata, M. / Schlichting, I.
History
DepositionNov 30, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 31, 2024Provider: repository / Type: Initial release
Revision 1.1Feb 21, 2024Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Feb 28, 2024Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3Mar 6, 2024Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Myoglobin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,7635
Polymers16,9261
Non-polymers8374
Water2,018112
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1500 Å2
ΔGint-36 kcal/mol
Surface area7970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)64.100, 28.800, 35.800
Angle α, β, γ (deg.)90.000, 106.900, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

-
Components

#1: Protein Myoglobin


Mass: 16926.463 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Equus caballus (horse) / References: UniProt: P68082
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-CMO / CARBON MONOXIDE


Mass: 28.010 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: CO / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 112 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 1.87 Å3/Da / Density % sol: 34.15 %
Crystal growTemperature: 293 K / Method: batch mode / Details: 3.1 M ammonium sulfate

-
Data collection

DiffractionMean temperature: 293 K / Serial crystal experiment: N
Diffraction sourceSource: FREE ELECTRON LASER / Site: SwissFEL ARAMIS / Beamline: ESB / Wavelength: 1.03 Å
DetectorType: PSI JUNGFRAU 16M / Detector: PIXEL / Date: Mar 1, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 1.32→10 Å / Num. obs: 25100 / % possible obs: 99.8 % / Redundancy: 80.5 % / Biso Wilson estimate: 14.4 Å2 / CC star: 0.977 / R split: 0.25 / Net I/σ(I): 3.5
Reflection shellResolution: 1.32→1.35 Å / Num. unique obs: 1925 / R split: 0.723

-
Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
REFMACphasing
CrystFEL0.8.0data reduction
CrystFEL0.8.0data scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 1.4→9.96 Å / SU ML: 0.1282 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 21.5945
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2216 1801 7.18 %
Rwork0.1849 23299 -
obs0.1875 25100 99.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 18.02 Å2
Refinement stepCycle: LAST / Resolution: 1.4→9.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1194 0 55 112 1361
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00932560
X-RAY DIFFRACTIONf_angle_d1.10643468
X-RAY DIFFRACTIONf_chiral_restr0.0805356
X-RAY DIFFRACTIONf_plane_restr0.0111428
X-RAY DIFFRACTIONf_dihedral_angle_d15.064942
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.4-1.430.31491380.27811729X-RAY DIFFRACTION95.94
1.43-1.480.23061350.24341762X-RAY DIFFRACTION100
1.48-1.520.24621370.22151779X-RAY DIFFRACTION100
1.52-1.580.24091370.20661777X-RAY DIFFRACTION100
1.58-1.640.26941370.19761801X-RAY DIFFRACTION99.95
1.64-1.710.2441430.20111779X-RAY DIFFRACTION100
1.71-1.80.24861380.19911785X-RAY DIFFRACTION99.95
1.8-1.920.17941340.18591797X-RAY DIFFRACTION99.95
1.92-2.060.22271420.18081791X-RAY DIFFRACTION100
2.06-2.270.2151370.17861801X-RAY DIFFRACTION100
2.27-2.590.21971390.18431807X-RAY DIFFRACTION99.95
2.59-3.250.20051420.18711821X-RAY DIFFRACTION100
3.25-9.960.2171420.16031870X-RAY DIFFRACTION100

+
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