[English] 日本語
Yorodumi
- PDB-4muc: The 4th and 5th C-terminal domains of Factor H related protein 1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4muc
TitleThe 4th and 5th C-terminal domains of Factor H related protein 1
ComponentsComplement factor H-related protein 1
KeywordsIMMUNE SYSTEM / Sushi domains / Complement Alternative Pathway / Factor H related proteins
Function / homology
Function and homology information


complement component C3b binding / complement activation / cytolysis by host of symbiont cells / negative regulation of protein binding / Regulation of Complement cascade / blood microparticle / protein-containing complex / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Complement Module, domain 1 / Complement Module; domain 1 / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Ribbon / Mainly Beta
Similarity search - Domain/homology
Complement factor H-related protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.897 Å
AuthorsBhattacharjee, A. / Goldman, A. / Kolodziejczyk, R. / Jokiranta, T.S.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: The Major Autoantibody Epitope on Factor H in Atypical Hemolytic Uremic Syndrome Is Structurally Different from Its Homologous Site in Factor H-related Protein 1, Supporting a Novel Model for ...Title: The Major Autoantibody Epitope on Factor H in Atypical Hemolytic Uremic Syndrome Is Structurally Different from Its Homologous Site in Factor H-related Protein 1, Supporting a Novel Model for Induction of Autoimmunity in This Disease.
Authors: Bhattacharjee, A. / Reuter, S. / Trojnar, E. / Kolodziejczyk, R. / Seeberger, H. / Hyvarinen, S. / Uzonyi, B. / Szilagyi, A. / Prohaszka, Z. / Goldman, A. / Jozsi, M. / Jokiranta, T.S.
History
DepositionSep 21, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 18, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 25, 2015Group: Database references
Revision 1.2May 6, 2015Group: Database references

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Complement factor H-related protein 1
B: Complement factor H-related protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,1519
Polymers28,4782
Non-polymers6727
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-111 kcal/mol
Surface area14120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)143.406, 143.406, 77.784
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number177
Space group name H-MP622

-
Components

#1: Protein Complement factor H-related protein 1 / FHR-1 / H factor-like protein 1 / H-factor-like 1 / H36


Mass: 14239.248 Da / Num. of mol.: 2 / Fragment: Sushi domains 4 and 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFHR1, CFHL, CFHL1, CFHL1P, CFHR1P, FHR1, HFL1, HFL2 / Production host: Pichia pastoris (fungus) / References: UniProt: Q03591
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 4.05 Å3/Da / Density % sol: 69.66 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6
Details: 2 M ammonium sulphate and 0.1 M sodium acetate , pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.97952 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 14, 2012
RadiationMonochromator: ESRF monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97952 Å / Relative weight: 1
ReflectionResolution: 2.89→50 Å / Num. obs: 10935 / % possible obs: 12.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shellResolution: 2.897→3.07 Å / % possible all: 99.2

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8.2_1309)refinement
DNAdata collection
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.897→48.529 Å / SU ML: 0.41 / σ(F): 2 / Phase error: 28.59 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2686 1092 10 %RANDOM
Rwork0.207 ---
obs0.2132 10921 99.65 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.897→48.529 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1904 0 35 0 1939
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0091989
X-RAY DIFFRACTIONf_angle_d1.1622703
X-RAY DIFFRACTIONf_dihedral_angle_d15.733714
X-RAY DIFFRACTIONf_chiral_restr0.067290
X-RAY DIFFRACTIONf_plane_restr0.005345
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8972-3.0290.37081320.30311184X-RAY DIFFRACTION98
3.029-3.18870.33351330.29091198X-RAY DIFFRACTION100
3.1887-3.38840.31251320.26681198X-RAY DIFFRACTION100
3.3884-3.650.3241340.22631206X-RAY DIFFRACTION100
3.65-4.01710.22991350.17331217X-RAY DIFFRACTION100
4.0171-4.5980.22551370.16491231X-RAY DIFFRACTION100
4.598-5.79150.23691390.17571248X-RAY DIFFRACTION100
5.7915-48.53580.2751500.21611347X-RAY DIFFRACTION100
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
17.70290.4952-0.40873.64193.64363.9323-0.4024-0.7338-0.42521.0820.37060.0999-0.2799-0.1047-0.01950.83730.0933-0.15070.4440.05030.691481.614210.544452.1251
25.68310.54221.90736.297-4.44734.07530.1629-0.1216-0.7711-0.33120.0579-0.35670.98990.4266-0.34060.89120.1566-0.00020.4641-0.07470.706381.97167.735939.9746
36.6891-1.6692.24763.25370.21812.0651-0.28982.0460.2392-0.29420.2740.002-0.4876-0.2103-0.0560.8858-0.1459-0.02671.00310.03550.619776.080513.265613.2848
40.8621.27340.57532.21271.83213.4907-0.24331.9680.0201-0.54080.279-0.3038-0.63140.9341-0.21261.23720.16060.15651.6590.05920.483584.41019.14453.3876
59.10682.6303-2.21145.2153-2.34251.61160.27070.60440.3685-0.2451-0.3801-0.54391.729-0.43860.53240.91870.0994-0.2060.8147-0.02850.578283.68529.460816.8973
64.3672-1.1079-1.87752.96531.21891.0065-0.01221.02620.91240.4414-0.0936-0.4709-2.51870.72280.37841.1478-0.35560.04070.72480.1240.646377.85624.923721.9548
75.00160.5410.84542.09371.17830.7219-0.40940.76480.6226-0.15460.4355-0.4914-1.21230.122-0.04951.2014-0.1474-0.33630.49910.18590.967170.749626.496522.3493
84.0135-1.58260.94374.6721-4.76874.99280.0399-0.16671.0647-0.30030.39110.2942-2.6460.4205-0.63881.4458-0.1078-0.25140.76060.1030.788975.747726.786835.5879
94.00580.5581.47882.33311.18112.6063-0.53990.5571.7955-0.0531-0.14250.0042-1.23760.4754-0.64011.9407-0.9077-0.39880.58190.22461.158780.172232.238325.6433
106.8691.4324-0.40737.271-2.47148.90810.1368-0.9409-0.7586-0.15070.1033-0.79460.98241.2965-0.44231.0736-0.1409-0.23550.8593-0.01870.799489.128219.165550.5879
115.432-1.45861.97673.5102-1.70982.4985-0.2797-0.6982-0.59031.10181.3152-0.7148-0.09591.4496-0.12141.19970.2679-0.39781.9235-0.22490.437489.828822.502262.9306
124.3152-4.07120.22559.34-6.20276.5507-1.1069-0.98540.8553-1.10291.42410.3529-0.6577-0.4363-0.23910.9538-0.2816-0.11930.7607-0.10270.616182.766525.387751.7747
135.6459-1.33653.41969.4135-6.1545.8296-0.6711-0.9796-0.06331.3746-0.5527-2.2024-1.39671.83950.96331.3519-0.2588-0.45321.4152-0.03991.20697.563525.360763.0501
145.2981-2.8807-2.23867.4376-3.45617.9824-2.2488-0.3062.1927-0.38670.2471-1.2724-1.17591.43651.42651.128-0.4126-0.20571.1784-0.09971.079494.538825.689253.1561
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 205 through 231 )
2X-RAY DIFFRACTION2chain 'A' and (resid 232 through 269 )
3X-RAY DIFFRACTION3chain 'A' and (resid 270 through 300 )
4X-RAY DIFFRACTION4chain 'A' and (resid 301 through 313 )
5X-RAY DIFFRACTION5chain 'A' and (resid 314 through 327 )
6X-RAY DIFFRACTION6chain 'B' and (resid 205 through 216 )
7X-RAY DIFFRACTION7chain 'B' and (resid 217 through 231 )
8X-RAY DIFFRACTION8chain 'B' and (resid 232 through 241 )
9X-RAY DIFFRACTION9chain 'B' and (resid 242 through 260 )
10X-RAY DIFFRACTION10chain 'B' and (resid 261 through 275 )
11X-RAY DIFFRACTION11chain 'B' and (resid 276 through 285 )
12X-RAY DIFFRACTION12chain 'B' and (resid 286 through 294 )
13X-RAY DIFFRACTION13chain 'B' and (resid 295 through 313 )
14X-RAY DIFFRACTION14chain 'B' and (resid 314 through 329 )

+
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://pdbjlvh1.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