[English] 日本語
Yorodumi
- PDB-4fdz: EutL from Clostridium perfringens, Crystallized Under Reducing Co... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4fdz
TitleEutL from Clostridium perfringens, Crystallized Under Reducing Conditions
ComponentsEthanolamine utilization protein
KeywordsTRANSPORT PROTEIN / bacterial microcompartment / Eut / BMC shell protein
Function / homology
Function and homology information


bacterial microcompartment / cobalamin binding / structural molecule activity / metal ion binding
Similarity search - Function
Bacterial microcompartment shell protein EutL / Bacterial microcompartment shell protein, EutL/PduB type / Bacterial microcompartment (BMC) circularly permuted domain / Bacterial microcompartment (BMC) circularly permuted domain profile. / BMC domain / Bacterial microcompartment domain / CcmK-like superfamily / BMC
Similarity search - Domain/homology
Bacterial microcompartment shell protein EutL
Similarity search - Component
Biological speciesClostridium perfringens (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.802 Å
AuthorsThompson, M.C. / Cascio, D. / Crowley, C.S. / Kopstein, J.S. / Yeates, T.O.
CitationJournal: Protein Sci. / Year: 2015
Title: An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein.
Authors: Thompson, M.C. / Cascio, D. / Leibly, D.J. / Yeates, T.O.
History
DepositionMay 29, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 29, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 10, 2016Group: Database references
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ethanolamine utilization protein
B: Ethanolamine utilization protein
C: Ethanolamine utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,2196
Polymers71,1503
Non-polymers693
Water11,151619
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9570 Å2
ΔGint-92 kcal/mol
Surface area24320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)87.970, 87.970, 252.460
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212

-
Components

#1: Protein Ethanolamine utilization protein


Mass: 23716.703 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium perfringens (bacteria) / Gene: CPE0900, eutL / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Rosetta / References: UniProt: Q8XLZ0
#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 619 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.43 Å3/Da / Density % sol: 64.16 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.1M HEPES buffer, 5% PEG 8000, 8% ethylene glycol, 5mM tris(2-carboxyethyl)phosphine, pH 7.0, vapor diffusion, hanging drop, temperature 298K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 23, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 1.8→19.824 Å / Num. obs: 91132 / % possible obs: 98.7 % / Observed criterion σ(I): -3 / Redundancy: 4.67 % / Biso Wilson estimate: 19.78 Å2 / Rmerge(I) obs: 0.055 / Net I/σ(I): 18.42
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
1.8-1.850.3933.8728100636495
1.85-1.90.3254.8129738647198.7
1.9-1.950.2576.129523632498.7
1.95-2.010.2067.5728802611299
2.01-2.080.1599.4328278596499
2.08-2.150.1311.3927641579499.1
2.15-2.240.10913.2926840558099.2
2.24-2.330.09714.7625879538799.3
2.33-2.430.08316.8324951519499.3
2.43-2.550.07119.223765496199.5
2.55-2.690.05922.622727475099.5
2.69-2.850.05225.2721476452299.6
2.85-3.050.04628.4419863422399.4
3.05-3.290.04131.3618301396499.6
3.29-3.60.03535.5516547364198.9
3.6-4.030.03238.0814823333198.8
4.03-4.650.02941.5313670295098.9
4.65-5.70.02842.111584253498.8
5.7-8.060.02941.398941199698.3
8.060.02842.144308107087.9

-
Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHENIX1.7.3_928refinement
PDB_EXTRACT3.11data extraction
ADSCQuantumdata collection
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EDI
Resolution: 1.802→19.824 Å / Occupancy max: 1 / Occupancy min: 0.05 / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 15.03 / Stereochemistry target values: ML
Details: REFINEMENT WAS CARRIED OUT WITH EXPLICIT HYDROGENS AS DEFINED BY THE RIDING MODEL
RfactorNum. reflection% reflectionSelection details
Rfree0.1773 4634 5.08 %RANDOM
Rwork0.16 ---
obs0.1609 91131 98.77 %-
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 34.198 Å2 / ksol: 0.355 e/Å3
Displacement parametersBiso max: 87.72 Å2 / Biso mean: 22.8876 Å2 / Biso min: 8.27 Å2
Baniso -1Baniso -2Baniso -3
1-4.3752 Å20 Å2-0 Å2
2--4.3752 Å2-0 Å2
3----1.091 Å2
Refinement stepCycle: LAST / Resolution: 1.802→19.824 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4864 0 3 619 5486
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0065137
X-RAY DIFFRACTIONf_angle_d1.037037
X-RAY DIFFRACTIONf_chiral_restr0.065826
X-RAY DIFFRACTIONf_plane_restr0.005929
X-RAY DIFFRACTIONf_dihedral_angle_d12.6941882
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.8022-1.82270.26261380.21522587272591
1.8227-1.84410.22611540.19332838299298
1.8441-1.86660.22271520.19112821297399
1.8666-1.89020.21421520.1842847299999
1.8902-1.91510.19021520.17552851300399
1.9151-1.94130.20711520.16722816296899
1.9413-1.9690.20631540.16992848300299
1.969-1.99840.18661520.16652879303199
1.9984-2.02960.1851390.15692821296099
2.0296-2.06280.17181520.1532861301399
2.0628-2.09830.17881550.15392886304199
2.0983-2.13640.16611520.15122853300599
2.1364-2.17750.17561560.14482841299799
2.1775-2.22190.16061580.1432876303499
2.2219-2.27010.16131450.14372880302599
2.2701-2.32280.16171560.14162864302099
2.3228-2.38080.15521520.14052898305099
2.3808-2.44510.17041470.14682902304999
2.4451-2.51690.17041460.154729083054100
2.5169-2.5980.17041880.15052854304299
2.598-2.69060.17721530.15082881303499
2.6906-2.79810.17581500.15429183068100
2.7981-2.9250.18061680.16362913308199
2.925-3.07870.17811400.158329363076100
3.0787-3.27080.2091600.166729593119100
3.2708-3.52210.16281340.16342949308399
3.5221-3.87410.19311870.16512893308099
3.8741-4.42920.14431520.15222977312999
4.4292-5.55990.15661640.14873009317399
5.5599-19.82530.18971740.19153131330598
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)
11.3025-1.27910.48224.0812-0.25251.01910.1087-0.1114-0.0953-0.0143-0.0762-0.0493-0.03730.04150.00320.0796-0.0488-0.03430.1610.02030.1281-37.85.4496-0.3136
21.14080.59990.32944.57480.24430.4951-0.0639-0.2360.15680.30860.00490.24580.06-0.09930.06140.1116-0.0358-0.0070.19280.0050.0956-44.12411.97942.782
30.73260.2109-0.16631.07450.35561.55220.1263-0.1607-0.01290.1229-0.1427-0.0193-0.04350.009-0.00030.1073-0.0748-0.00950.13150.01250.1154-40.72741.56221.4254
40.66850.61350.49332.57240.360.57350.1626-0.0951-0.11560.3519-0.1262-0.31260.06470.0619-0.0380.1366-0.0692-0.03210.19320.03080.1511-35.4867-1.8326.4382
55.4439-1.358-1.44974.9265-0.79770.68060.0765-0.33240.00550.2413-0.04170.36760.2753-0.5337-0.06530.2251-0.12320.02180.2614-0.02770.13-49.07150.005515.6165
60.3541-0.20050.03920.1632-0.20361.15270.1744-0.1957-0.09150.2968-0.12360.03340.1139-0.0703-0.05550.2185-0.1033-0.01450.16680.02950.1139-48.291-14.10887.6926
71.2416-0.8434-1.64191.90361.93514.4130.0318-0.4043-0.16520.44670.0906-0.20780.28540.49130.04630.2711-0.0756-0.11810.22060.09780.216-40.8066-21.038810.9671
80.67850.1562-0.1180.4723-0.48626.88160.0720.0267-0.1788-0.3063-0.0846-0.22380.42010.0775-0.04060.2920.0190.03450.07620.00580.1894-45.4783-27.7435-15.8588
94.478-1.98292.84764.8229-1.58954.77150.2869-0.6390.110.2712-0.3202-0.0730.1257-0.23980.03430.21-0.1626-0.00320.4304-0.00760.1676-57.509-20.620410.1319
100.96620.68780.2721.9098-0.10751.02590.0756-0.1709-0.06450.0007-0.09950.03310.1047-0.10540.02980.1004-0.0224-0.02540.08810.0210.0808-54.4275-22.896-6.1572
110.52730.0029-0.79620.32230.07151.23760.0126-0.2815-0.30470.0529-0.1294-0.07810.34120.07520.14230.1672-0.0418-0.02080.12460.06390.1437-55.4314-31.9587-4.1715
124.45331.8903-1.45326.49080.24971.54890.0293-0.2254-0.227-0.0427-0.3226-0.44480.38770.18370.23790.2531-0.00220.04480.0933-0.01010.1942-48.5607-26.6451-24.2304
132.30010.20951.14812.7870.380.9478-0.08370.2648-0.3973-0.38670.0326-0.43490.30740.00060.14460.2251-0.00210.01670.0439-0.00460.1261-49.6139-22.2198-26.7422
143.46060.4455-0.16854.7145-0.35960.8440.0849-0.0333-0.024-0.113-0.03160.27690.2181-0.3342-0.01490.2066-0.0863-0.04440.14550.04040.1244-68.9737-25.347-14.6944
150.94490.60750.27471.02960.63810.4118-0.050.05280.0381-0.35160.10750.18390.1623-0.0837-0.05090.2155-0.0417-0.04820.08460.01870.1164-59.2537-15.2048-28.1442
162.06821.77951.24461.92131.51831.2686-0.0581-0.12970.08-0.2157-0.04110.22540.1736-0.27530.04860.1653-0.0573-0.03940.0830.03340.1228-61.4154-15.1951-21.522
170.30670.1735-0.2580.8902-0.25270.6161-0.00560.0562-0.1193-0.29810.07470.06460.3112-0.08230.08130.3654-0.0522-0.03510.0229-0.03880.064-55.92-17.3759-34.9851
180.76090.06780.30781.4470.04541.3995-0.01680.13520.0966-0.3521-0.01210.1737-0.0542-0.0040.04190.18290.0003-0.02660.04980.00860.0969-54.6302-1.5265-30.1065
190.9743-0.17260.27961.133-0.37321.26450.02180.07210.053-0.2944-0.04090.0426-0.0578-0.01610.02060.16890.0047-0.01060.062-0.00610.093-52.06482.0775-29.4686
200.54740.0137-1.09173.0709-1.50682.8862-0.09880.1187-0.0769-0.47670.0634-0.11150.18670.34860.04070.1984-0.0770.03120.16450.02810.1238-36.9318.5544-26.899
211.14980.01480.3121.66240.10541.7771-0.05060.09040.1742-0.1551-0.14360.0359-0.30580.09410.12510.1731-0.0232-0.02350.07340.00360.1185-45.461414.364-18.4635
221.12950.7857-0.27194.0872-1.30240.5455-0.0524-0.16060.24510.0814-0.06420.3046-0.2914-0.07980.10460.21070.008-0.03990.1242-0.03720.133-48.662812.6409-13.7015
230.3695-0.0390.15330.9845-0.16410.4485-0.11540.06640.2237-0.0891-0.06180.0097-0.23040.1705-0.0570.272-0.1721-0.05530.11350.05960.2093-37.490319.4105-16.7427
240.69420.42480.59040.63170.48451.39580.03510.0469-0.04420.01240.0328-0.188-0.03920.14140.030.1301-0.186-0.05290.22250.04950.1968-25.386512.04184.2791
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:26)A1 - 26
2X-RAY DIFFRACTION2chain 'A' and (resseq 27:43)A27 - 43
3X-RAY DIFFRACTION3chain 'A' and (resseq 44:82)A44 - 82
4X-RAY DIFFRACTION4chain 'A' and (resseq 83:128)A83 - 128
5X-RAY DIFFRACTION5chain 'A' and (resseq 129:145)A129 - 145
6X-RAY DIFFRACTION6chain 'A' and (resseq 146:192)A146 - 192
7X-RAY DIFFRACTION7chain 'A' and (resseq 193:215)A193 - 215
8X-RAY DIFFRACTION8chain 'B' and (resseq 1:16)B1 - 16
9X-RAY DIFFRACTION9chain 'B' and (resseq 17:26)B17 - 26
10X-RAY DIFFRACTION10chain 'B' and (resseq 27:82)B27 - 82
11X-RAY DIFFRACTION11chain 'B' and (resseq 83:106)B83 - 106
12X-RAY DIFFRACTION12chain 'B' and (resseq 107:116)B107 - 116
13X-RAY DIFFRACTION13chain 'B' and (resseq 117:128)B117 - 128
14X-RAY DIFFRACTION14chain 'B' and (resseq 129:145)B129 - 145
15X-RAY DIFFRACTION15chain 'B' and (resseq 146:167)B146 - 167
16X-RAY DIFFRACTION16chain 'B' and (resseq 168:192)B168 - 192
17X-RAY DIFFRACTION17chain 'B' and (resseq 193:219)B193 - 219
18X-RAY DIFFRACTION18chain 'C' and (resseq 1:43)C1 - 43
19X-RAY DIFFRACTION19chain 'C' and (resseq 44:106)C44 - 106
20X-RAY DIFFRACTION20chain 'C' and (resseq 107:116)C107 - 116
21X-RAY DIFFRACTION21chain 'C' and (resseq 117:167)C117 - 167
22X-RAY DIFFRACTION22chain 'C' and (resseq 168:192)C168 - 192
23X-RAY DIFFRACTION23chain 'C' and (resseq 193:212)C193 - 212
24X-RAY DIFFRACTION24chain 'C' and (resseq 213:225)C213 - 225

+
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