[English] 日本語
Yorodumi
- PDB-3s7p: Crystal Structure of the Infrared Fluorescent D207H variant of De... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3s7p
TitleCrystal Structure of the Infrared Fluorescent D207H variant of Deinococcus Bacteriophytochrome chromophore binding domain at 1.72 angstrom resolution
ComponentsBacteriophytochrome
KeywordsFLUORESCENT PROTEIN / BILIVERDIN / PAS / GAF / Phytochrome / bacteriophytochrome / Photoreceptor
Function / homology
Function and homology information


osmosensory signaling via phosphorelay pathway / detection of visible light / phosphorelay response regulator activity / histidine kinase / phosphorelay sensor kinase activity / protein kinase activator activity / photoreceptor activity / regulation of DNA-templated transcription / ATP binding / identical protein binding
Similarity search - Function
: / Phytochrome, PHY domain superfamily / PAS fold-2 / PAS fold / Phytochrome, central region / Phytochrome region / GAF domain / Phytochrome chromophore attachment domain / Phytochrome chromophore attachment site domain profile. / Signal transduction histidine kinase-related protein, C-terminal ...: / Phytochrome, PHY domain superfamily / PAS fold-2 / PAS fold / Phytochrome, central region / Phytochrome region / GAF domain / Phytochrome chromophore attachment domain / Phytochrome chromophore attachment site domain profile. / Signal transduction histidine kinase-related protein, C-terminal / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / PAS domain / Histidine kinase domain / Histidine kinase domain profile. / GAF domain / Domain present in phytochromes and cGMP-specific phosphodiesterases. / GAF domain / GAF-like domain superfamily / Beta-Lactamase / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / PAS domain superfamily / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-LBV / Bacteriophytochrome
Similarity search - Component
Biological speciesDeinococcus radiodurans (radioresistant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.722 Å
AuthorsForest, K.T. / Auldridge, M.E. / Satyshur, K.A.
CitationJournal: J.Biol.Chem. / Year: 2012
Title: Structure-guided engineering enhances a phytochrome-based infrared fluorescent protein.
Authors: Auldridge, M.E. / Satyshur, K.A. / Anstrom, D.M. / Forest, K.T.
History
DepositionMay 26, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 21, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 28, 2012Group: Database references
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif / struct_site
Item: _chem_comp.name / _database_2.pdbx_DOI ..._chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Bacteriophytochrome
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,7622
Polymers37,1761
Non-polymers5861
Water5,368298
1
A: Bacteriophytochrome
hetero molecules

A: Bacteriophytochrome
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,5244
Polymers74,3532
Non-polymers1,1712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area5030 Å2
ΔGint-55 kcal/mol
Surface area25770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)87.072, 51.666, 80.228
Angle α, β, γ (deg.)90.00, 115.33, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein Bacteriophytochrome / Phytochrome-like protein


Mass: 37176.418 Da / Num. of mol.: 1 / Fragment: chromophore binidng domain (UNP Residues 1-321) / Mutation: D207H Y307S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Deinococcus radiodurans (radioresistant)
Gene: bphP, DR_A0050 / Plasmid: pET21a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: Q9RZA4, histidine kinase
#2: Chemical ChemComp-LBV / 3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium -2-ylidene]methyl]-5-[(Z)-[(3E)-3-ethylidene-4-methyl-5-oxidanylidene-pyrrolidin-2-ylidene]methyl]-4-methyl-1H-pyrrol-3- yl]propanoic acid / 2(R),3(E)- PHYTOCHROMOBILIN


Mass: 585.670 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C33H37N4O6
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 298 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.19 Å3/Da / Density % sol: 43.93 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 14% v/v PEG 4000, 20% v/v isopropanol, 0.1M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.9785 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 8, 2010 / Details: mirrors
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9785 Å / Relative weight: 1
ReflectionResolution: 1.72→50 Å / Num. all: 34268 / Num. obs: 33621 / % possible obs: 98.5 % / Observed criterion σ(F): -3 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Biso Wilson estimate: 18.8 Å2 / Rmerge(I) obs: 0.039 / Net I/σ(I): 31.12
Reflection shellResolution: 1.72→1.75 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.215 / Mean I/σ(I) obs: 5.53 / Num. unique all: 1642 / % possible all: 97.3

-
Processing

Software
NameVersionClassification
MAR345dtbdata collection
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2O9C

2o9c


Resolution: 1.722→43.19 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.954 / SU B: 4.267 / SU ML: 0.065 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.109 / ESU R Free: 0.103 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19623 1701 5.1 %RANDOM
Rwork0.16753 ---
all0.16901 33564 --
obs0.16901 31863 97.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 21.053 Å2
Baniso -1Baniso -2Baniso -3
1--0.71 Å20 Å2-0.08 Å2
2--0.48 Å20 Å2
3---0.16 Å2
Refinement stepCycle: LAST / Resolution: 1.722→43.19 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2395 0 43 298 2736
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0222548
X-RAY DIFFRACTIONr_bond_other_d0.0010.021696
X-RAY DIFFRACTIONr_angle_refined_deg1.47923496
X-RAY DIFFRACTIONr_angle_other_deg0.9593.0024119
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3835321
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.79522.941102
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.69315383
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.0311520
X-RAY DIFFRACTIONr_chiral_restr0.0780.2397
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0212839
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02487
X-RAY DIFFRACTIONr_mcbond_it0.7421.51600
X-RAY DIFFRACTIONr_mcbond_other0.1541.5633
X-RAY DIFFRACTIONr_mcangle_it1.34322586
X-RAY DIFFRACTIONr_scbond_it2.0133948
X-RAY DIFFRACTIONr_scangle_it3.2434.5909
LS refinement shellResolution: 1.722→1.767 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.235 111 -
Rwork0.181 2167 -
obs--90.43 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.8748-0.2525-0.91290.1780.6065.73650.0069-0.2749-0.27790.2152-0.1495-0.10860.3695-0.00950.14260.2218-0.1232-0.07450.17950.10720.143117.137-31.18632.35
21.3462-0.16140.06320.46920.30631.06120.09-0.26880.13860.0396-0.1282-0.01540.0365-0.14460.03810.1088-0.03880.01420.1677-0.04680.08838.164-18.09725.772
39.2181-4.9924-3.76865.45253.81492.03080.7908-0.36450.9942-0.7201-0.5447-0.1306-0.5716-0.3619-0.24610.21190.0809-0.00720.2605-0.17170.2005-2.816-5.01125.208
42.14931.2183-1.01153.60011.23415.71110.11460.18010.1479-0.9844-0.51130.19130.1827-0.77630.39680.40090.1230.01170.1909-0.03570.0898-4.789-15.62216.575
50.88880.41170.61450.42780.97162.1572-0.0085-0.00420.3397-0.0987-0.0850.1218-0.1748-0.15020.09360.12190.0370.00530.09730.00940.2172.317-13.86311.596
60.89420.4196-0.11861.69180.73771.1739-0.02580.12080.0089-0.0943-0.0140.1479-0.0904-0.00590.03980.10180.0143-0.01570.10510.00020.116212.6-29.273-4.452
70.40730.31110.2320.85530.61690.96480.0524-0.0354-0.04440.07330.0069-0.0650.06160.0808-0.05940.09710.0069-0.0080.09270.00730.105419.039-29.14911.199
82.9208-0.4962-1.60120.53290.4462.121-0.0048-0.1555-0.05640.1322-0.0469-0.03170.10710.00110.05180.1252-0.0284-0.00280.1155-0.00990.084513.722-21.37424.719
90.62330.67240.11392.0465-0.23760.54210.01660.01250.0020.03210.02660.05640.02890.0134-0.04310.10460.00040.00420.09410.00010.10515.158-26.4738.976
102.25352.68581.886213.6853.60031.5961-0.12550.17-0.18380.04690.23630.2219-0.07560.149-0.11080.0868-0.00410.00150.12330.00350.13645.577-29.4342.876
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A5 - 23
2X-RAY DIFFRACTION2A24 - 60
3X-RAY DIFFRACTION2A330
4X-RAY DIFFRACTION3A61 - 84
5X-RAY DIFFRACTION4A85 - 105
6X-RAY DIFFRACTION5A106 - 143
7X-RAY DIFFRACTION6A144 - 170
8X-RAY DIFFRACTION7A171 - 234
9X-RAY DIFFRACTION8A235 - 267
10X-RAY DIFFRACTION9A268 - 296
11X-RAY DIFFRACTION10A297 - 323

+
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