[English] 日本語
Yorodumi
- PDB-6gvc: Structure of ArhGAP12 bound to G-Actin -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6gvc
TitleStructure of ArhGAP12 bound to G-Actin
Components
  • Actin, alpha skeletal muscle
  • Rho GTPase-activating protein 12
KeywordsHYDROLASE / GAP / RAC / Actin
Function / homology
Function and homology information


RHOV GTPase cycle / RHOF GTPase cycle / negative regulation of small GTPase mediated signal transduction / RHOD GTPase cycle / RAC1 GTPase cycle / cytoskeletal motor activator activity / phagocytosis, engulfment / tropomyosin binding / myosin heavy chain binding / mesenchyme migration ...RHOV GTPase cycle / RHOF GTPase cycle / negative regulation of small GTPase mediated signal transduction / RHOD GTPase cycle / RAC1 GTPase cycle / cytoskeletal motor activator activity / phagocytosis, engulfment / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / phagocytic cup / skeletal muscle myofibril / actin monomer binding / stress fiber / skeletal muscle fiber development / titin binding / actin filament polymerization / GTPase activator activity / filopodium / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / cell body / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / signal transduction / ATP binding / identical protein binding / cytoplasm
Similarity search - Function
ARHGAP12, SH3 domain / Linker region between SH3 and WW domains on ARHGAP12 / : / Phosphatidylinositol 3-kinase; Chain A / Rho GTPase activation protein / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / ATPase, substrate binding domain, subdomain 4 ...ARHGAP12, SH3 domain / Linker region between SH3 and WW domains on ARHGAP12 / : / Phosphatidylinositol 3-kinase; Chain A / Rho GTPase activation protein / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / ATPase, substrate binding domain, subdomain 4 / Rho GTPase activation protein / Actin; Chain A, domain 4 / WW domain / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / ATPase, nucleotide binding domain / PH domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / ATPase, nucleotide binding domain / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Nucleotidyltransferase; domain 5 / PH-like domain superfamily / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / LATRUNCULIN B / Actin, alpha skeletal muscle / Rho GTPase-activating protein 12
Similarity search - Component
Biological speciesMus musculus (house mouse)
Oryctolagus cuniculus (rabbit)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsMouilleron, S. / Treisman, R. / Diring, J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
European Research Council268690 United Kingdom
CitationJournal: Nat.Cell Biol. / Year: 2019
Title: RPEL-family rhoGAPs link Rac/Cdc42 GTP loading to G-actin availability.
Authors: Diring, J. / Mouilleron, S. / McDonald, N.Q. / Treisman, R.
History
DepositionJun 20, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 27, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 23, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 17, 2024Group: 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
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Actin, alpha skeletal muscle
A: Actin, alpha skeletal muscle
C: Actin, alpha skeletal muscle
D: Actin, alpha skeletal muscle
R: Rho GTPase-activating protein 12
Q: Rho GTPase-activating protein 12
S: Rho GTPase-activating protein 12
T: Rho GTPase-activating protein 12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)279,27228
Polymers275,0678
Non-polymers4,20520
Water3,279182
1
B: Actin, alpha skeletal muscle
R: Rho GTPase-activating protein 12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,8187
Polymers68,7672
Non-polymers1,0515
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5720 Å2
ΔGint-30 kcal/mol
Surface area23710 Å2
MethodPISA
2
A: Actin, alpha skeletal muscle
S: Rho GTPase-activating protein 12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,8808
Polymers68,7672
Non-polymers1,1136
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5730 Å2
ΔGint-31 kcal/mol
Surface area23980 Å2
MethodPISA
3
C: Actin, alpha skeletal muscle
T: Rho GTPase-activating protein 12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,7566
Polymers68,7672
Non-polymers9894
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5730 Å2
ΔGint-38 kcal/mol
Surface area24040 Å2
MethodPISA
4
D: Actin, alpha skeletal muscle
Q: Rho GTPase-activating protein 12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,8187
Polymers68,7672
Non-polymers1,0515
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6050 Å2
ΔGint-34 kcal/mol
Surface area24210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)101.650, 130.240, 109.300
Angle α, β, γ (deg.)90.00, 111.17, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

-
Protein , 2 types, 8 molecules BACDRQST

#1: Protein
Actin, alpha skeletal muscle / Alpha-actin-1


Mass: 42096.953 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / References: UniProt: P68135
#2: Protein
Rho GTPase-activating protein 12 / Rho-type GTPase-activating protein 12


Mass: 26669.887 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Arhgap12 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8C0D4

-
Non-polymers , 5 types, 202 molecules

#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-LAB / LATRUNCULIN B


Mass: 395.513 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: C20H29NO5S / Comment: toxin*YM
#5: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 182 / 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: 2.45 Å3/Da / Density % sol: 49.85 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 20% PEG 3350, 0.2M Sodium Thiocyanate 0.1 M Bis Tris Propane pH6.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.97 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: May 7, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2.6→54.132 Å / Num. obs: 81113 / % possible obs: 99.43 % / Redundancy: 6.2 % / Biso Wilson estimate: 47.76 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.17 / Rpim(I) all: 0.06 / Rrim(I) all: 0.18 / Net I/av σ(I): 10.8 / Net I/σ(I): 10.8
Reflection shellResolution: 2.6→2.69 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.77 / Mean I/σ(I) obs: 1.66 / Num. unique obs: 7746 / CC1/2: 0.62 / Rpim(I) all: 0.48 / Rrim(I) all: 0.91 / % possible all: 95.83

-
Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2v52
Resolution: 2.6→54.132 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.34
RfactorNum. reflection% reflection
Rfree0.2508 4063 5.01 %
Rwork0.2067 --
obs0.209 81098 99.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.6→54.132 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17871 0 268 182 18321
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00418551
X-RAY DIFFRACTIONf_angle_d0.61525194
X-RAY DIFFRACTIONf_dihedral_angle_d11.79312828
X-RAY DIFFRACTIONf_chiral_restr0.0432878
X-RAY DIFFRACTIONf_plane_restr0.0043213
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6002-2.63080.39081370.32832297X-RAY DIFFRACTION89
2.6308-2.66290.34651270.31552704X-RAY DIFFRACTION100
2.6629-2.69660.33751370.3012620X-RAY DIFFRACTION99
2.6966-2.7320.33751500.29022634X-RAY DIFFRACTION100
2.732-2.76950.34861390.28582687X-RAY DIFFRACTION100
2.7695-2.8090.34511340.28682662X-RAY DIFFRACTION100
2.809-2.8510.3461300.27672652X-RAY DIFFRACTION100
2.851-2.89550.30891350.27692683X-RAY DIFFRACTION100
2.8955-2.9430.3031230.26752639X-RAY DIFFRACTION100
2.943-2.99370.32091160.25862706X-RAY DIFFRACTION100
2.9937-3.04810.31531330.25432636X-RAY DIFFRACTION100
3.0481-3.10680.2881560.25082666X-RAY DIFFRACTION100
3.1068-3.17020.32241330.25172661X-RAY DIFFRACTION100
3.1702-3.23910.3071560.25482640X-RAY DIFFRACTION100
3.2391-3.31440.2711480.24052662X-RAY DIFFRACTION100
3.3144-3.39730.26691620.2232649X-RAY DIFFRACTION100
3.3973-3.48920.26111350.21082648X-RAY DIFFRACTION100
3.4892-3.59180.27431520.20362658X-RAY DIFFRACTION100
3.5918-3.70770.2121470.18692657X-RAY DIFFRACTION100
3.7077-3.84020.24891240.18692700X-RAY DIFFRACTION100
3.8402-3.99390.22971530.17642644X-RAY DIFFRACTION100
3.9939-4.17560.21631460.17232680X-RAY DIFFRACTION100
4.1756-4.39570.18541540.15982663X-RAY DIFFRACTION100
4.3957-4.67090.17691330.14612684X-RAY DIFFRACTION100
4.6709-5.03130.20451300.16532699X-RAY DIFFRACTION100
5.0313-5.53720.25261580.18662667X-RAY DIFFRACTION100
5.5372-6.33740.23861370.19792690X-RAY DIFFRACTION100
6.3374-7.98030.24121220.19882723X-RAY DIFFRACTION100
7.9803-54.14340.20751560.18012724X-RAY DIFFRACTION99
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)
10.5113-0.2337-0.07110.14860.02910.0141-0.1131-0.03560.2781-0.1824-0.1821-0.15180.0782-0.3916-0.03040.3676-0.0643-0.00610.63020.1030.2837-12.4181-21.561943.4373
20.3880.173-0.62980.1209-0.23911.0715-0.2890.06060.5189-0.3903-0.28230.19460.1824-0.1407-0.20530.50840.1962-0.09810.70620.13990.5479-12.0351-4.103340.5477
30.6078-0.4735-0.52050.40240.53640.98710.2558-0.09840.16590.09720.16940.0566-0.5677-0.65330.60030.28420.2097-0.03250.47620.20630.3214-11.0496-7.676947.0228
4-0.0003-0.017-0.050.00390.10130.54920.05510.16480.0496-0.03010.08010.0343-0.0177-0.42890.21620.2750.0128-0.0350.46470.08520.3105-5.0715-21.831752.3813
50.02340.03280.02650.42420.35030.28290.0250.08310.05560.18030.0539-0.2629-0.2955-0.10220.00010.34-0.00420.00980.29430.03770.30569.76-15.508841.1971
60.3080.5079-0.03750.8726-0.09930.44680.02540.25360.0264-0.81660.336-0.1639-0.1458-0.13940.24880.4594-0.05180.07270.43990.10490.33128.3591-10.940123.3625
70.38970.1221-0.10670.29180.24150.3193-0.1977-0.05120.2775-0.21880.0833-0.55610.1969-0.00820.01510.2550.0050.00760.21510.01750.320115.9197-16.683834.9081
80.08420.06460.08650.04190.05510.0815-0.18240.10240.00610.07480.184-0.58820.1586-0.2666-0.00170.3915-0.0144-0.05190.3373-0.01760.34911.0267-30.66943.2714
90.11210.1139-0.08130.1127-0.07990.0562-0.34970.16230.2345-0.46390.2371-0.35620.4642-0.105-0.00550.43710.00380.0740.4184-0.04650.411814.6505-31.6936.4133
100.21140.1576-0.290.2285-0.250.386-0.07480.19620.04130.1279-0.0967-0.0142-0.0621-0.4669-0.13760.2323-0.0628-0.05980.44840.10460.3182-10.674-26.64455.6823
110.3236-0.0659-0.24850.5442-0.04660.4273-0.2552-0.0454-0.137-0.05060.3412-0.07240.57070.62860.25030.12710.5819-0.08480.39150.02710.2459-20.245814.258724.4424
120.27880.20430.00530.2213-0.00970.0471-0.2297-0.0544-0.0711-0.13370.24970.30860.02440.14120.00060.34180.0613-0.0010.3625-0.00520.3791-28.707313.76816.8538
130.1863-0.1194-0.17431.16410.43480.2389-0.23710.05790.0951-0.46690.3853-0.22810.02760.20330.13710.28210.00930.01920.3153-0.05960.1833-18.95219.8072-5.0046
140.3594-0.037-0.47951.27390.19580.6076-0.04170.030.0842-0.12770.253-0.0172-0.08670.27360.16050.16190.10840.00020.30880.00920.2377-28.285727.08415.3998
150.1339-0.1111-0.04430.08990.02330.0743-0.13810.1890.2341-0.21920.162-0.45290.0580.27540.03020.2984-0.12860.01040.4385-0.07140.6680.9885-10.7682-28.0728
160.2045-0.1391-0.07760.28180.08380.21260.07220.15530.1002-0.1583-0.1109-0.3518-0.0598-0.11780.00040.3462-0.06460.11090.4174-0.05230.6003-1.5691-16.2367-32.1627
170.0573-0.12850.07470.3519-0.32680.26880.0350.0282-0.0272-0.13830.082-0.2369-0.09540.010100.24460.00740.02840.3403-0.07340.3735-12.8087-18.4783-25.0854
180.6992-0.01320.20770.23370.08290.1101-0.17720.2592-0.2015-0.26320.0861-0.1736-0.246-0.1505-0.02780.5703-0.10860.03350.37090.02360.2815-19.1977-3.2104-32.4291
190.2780.08880.24380.02990.07770.2121-0.17920.31790.5774-0.44340.14790.255-0.26460.1063-0.04460.6419-0.21290.10980.53320.12620.4915-5.58128.9231-36.0638
200.99980.1751-0.14881.20710.61791.02110.10750.10380.0305-0.04280.01370.0303-0.5053-0.2130.12060.41760.03950.06490.2901-0.0110.2867-21.81553.2288-24.6562
210.05820.0607-0.02160.0788-0.0480.0471-0.17290.04130.03950.10080.2726-0.23210.04120.0070.00010.32260.01780.02830.3474-0.05840.5308-9.4894-31.4439-21.1046
220.1625-0.15030.06210.20010.03130.14290.07110.23460.0949-0.55950.30130.312-0.16640.14640.15080.395-0.148-0.11180.41550.02530.437910.80529.9729-1.13
230.0226-0.01910.00360.0162-0.0023-0.0013-0.38050.2007-0.389-0.35260.3656-0.0863-0.01740.3119-0.00160.668-0.1472-0.10530.501-0.04150.504320.22658.1603-11.6963
240.3874-0.2568-0.23460.18510.03020.5067-0.06210.06930.0057-0.197-0.010.06130.23330.1023-0.03510.3392-0.0742-0.06390.27110.04940.297916.687617.24042.3016
250.64950.14080.51470.09390.06030.4455-0.4811-0.0302-0.1093-0.27560.1840.3440.05240.5356-0.4160.5013-0.03810.20660.2828-0.05310.346729.37821.19775.6572
260.2211-0.1463-0.20050.3534-0.19840.629-0.28250.0797-0.2696-0.3067-0.04220.04910.9316-0.5276-0.04780.7822-0.03950.20810.3762-0.04470.564923.545-15.58421.0377
270.18020.20480.23960.836-0.15050.5916-0.17630.052-0.0820.13280.0503-0.00180.3620.1543-0.00490.3957-0.01390.06080.3001-0.00160.336226.5427-0.700715.3487
280.0458-0.01870.01410.27340.24610.22860.1592-0.1120.1190.06310.04540.303-0.10710.2463-0.00010.3382-0.0122-0.09120.35030.02540.403614.175629.4968.0852
290.09720.106-0.03280.1687-0.08160.0571-0.1042-0.10420.05830.2468-0.00910.04420.0144-0.066500.3926-0.0546-0.0230.44120.04010.33542.6565-34.327658.0845
300.3132-0.142-0.18410.11190.23450.53940.07230.17870.1272-0.12750.0286-0.3226-0.24940.08320.03690.24360.0126-0.03910.1686-0.01020.244314.0077-7.978965.1187
310.14730.00180.12150.52090.26470.22910.0311-0.1030.0646-0.09270.1510.32870.1886-0.227900.4060.0259-0.00390.3620.00590.41968.0111-10.103670.5209
320.0025-0.0002-0.0260.10350.02090.05940.0021-0.34860.28730.33230.1785-0.0806-0.07650.395900.54030.04040.05340.4702-0.0830.424111.2252-6.566983.8212
330.1148-0.05470.24720.0443-0.18880.89230.04220.01970.2241-0.04190.2519-0.1641-0.6226-0.43070.25430.3960.12130.06560.3473-0.09570.48872.9159-1.470674.9591
340.64410.2533-0.09320.9699-0.52520.29030.27730.25850.1820.31210.24530.2097-0.33720.33920.3810.37130.02050.1580.4632-0.16410.43894.8796-2.878384.315
350.06420.1416-0.12190.3346-0.22520.20570.0410.1483-0.09490.00110.12810.275-0.4607-0.13330.01250.33620.0519-0.01520.36110.05480.48377.411112.973921.3586
360.0643-0.0739-0.05210.07560.0490.02850.05490.1152-0.1107-0.0756-0.132-0.0256-0.23910.2490.00010.3465-0.0511-0.06030.4744-0.03450.575130.969924.111219.026
370.11070.12980.0290.35-0.18830.2301-0.0519-0.0394-0.1528-0.1236-0.0741-0.07970.3075-0.073300.31350.01870.05640.33830.05150.340846.990723.018-0.3895
380.04490.0314-0.03090.02-0.0140.0237-0.1011-0.3907-0.1662-0.024-0.2170.46230.12640.11590.00060.36670.02390.06610.32760.03550.409736.487514.88192.9032
390.03940.03270.02490.04710.02710.0175-0.0911-0.14790.1916-0.54660.0708-0.40790.0444-0.14960.00080.53410.04110.09980.30110.03720.460545.156710.55640.8813
400.0796-0.1403-0.26570.65590.4120.8508-0.00730.26860.31480.0423-0.27110.5625-0.0542-0.3759-0.17210.26660.0566-0.08580.34950.03440.51239.406335.38540.3708
410.1195-0.09650.03230.1254-0.08440.0799-0.1868-0.05330.12920.0373-0.0278-0.0959-0.62220.1448-0.02510.5107-0.1226-0.15380.39230.20180.595848.761547.46281.1236
420.0775-0.00120.04210.03260.04340.078-0.05540.03050.2882-0.0945-0.3171-0.2374-0.14220.2383-0.09180.428-0.0546-0.0310.41350.19310.431750.886532.818-1.9934
430.07190.1416-0.10170.3964-0.18740.1089-0.0984-0.0955-0.1154-0.2606-0.05960.22-0.10720.18390.00160.38520.0134-0.09980.61310.07960.489840.775333.7732-9.1521
440.1222-0.0066-0.01070.0790.14060.24320.03640.0530.2527-0.7283-0.2262-0.3663-0.3383-0.3454-0.03780.45610.0685-0.11370.40650.13920.657146.059641.7799-6.8056
450.034-0.0107-0.07760.2139-0.00590.1829-0.018-0.31760.23740.3194-0.07350.32180.10.1432-0.0060.35290.11570.0210.4207-0.04480.4711-34.262932.775923.9753
460.42910.2283-0.38150.1173-0.20090.32430.11720.2087-0.0417-0.1285-0.1919-0.20850.4388-0.1676-0.00110.65150.0143-0.00710.33850.05210.4963-50.66314.577723.0054
470.1525-0.0859-0.07930.08460.07480.06890.25690.36420.0844-0.1381-0.15220.14860.51520.66930.00010.50170.10290.06130.31360.04650.423-42.14977.421714.4459
480.42750.3858-0.15630.4804-0.4340.76170.0383-0.1958-0.0520.138-0.0363-0.04630.3351-0.231-0.06150.58780.0063-0.00230.29340.08590.32-51.99015.00737.7828
490.1845-0.2626-0.08150.4422-0.01750.1998-0.11060.0438-0.0440.01740.2238-0.0354-0.0135-0.07140.00030.4532-0.0525-0.06390.4618-0.04090.4945-21.0073-19.7914-14.6201
500.3306-0.0371-0.00110.31450.32130.31360.118-0.1524-0.0007-0.285-0.1282-0.0523-0.00860.2282-00.4270.05320.02880.3811-0.00980.3896-28.2848-24.7051-48.8382
510.25180.21070.22720.17660.19270.19740.0541-0.10560.1054-0.0514-0.1268-0.2475-0.0781-0.1701-0.00010.3196-0.02690.00230.3269-0.05850.3072-23.9443-18.0757-43.99
520.51020.10360.04140.4568-0.01510.4933-0.04660.2214-0.6052-0.2041-0.0965-0.17540.28270.3023-0.02290.44750.08650.01630.4074-0.09210.5441-24.5881-40.9228-49.6638
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 5 through 28 )
2X-RAY DIFFRACTION2chain 'B' and (resid 29 through 60 )
3X-RAY DIFFRACTION3chain 'B' and (resid 61 through 97 )
4X-RAY DIFFRACTION4chain 'B' and (resid 98 through 165 )
5X-RAY DIFFRACTION5chain 'B' and (resid 166 through 196 )
6X-RAY DIFFRACTION6chain 'B' and (resid 197 through 246 )
7X-RAY DIFFRACTION7chain 'B' and (resid 247 through 283 )
8X-RAY DIFFRACTION8chain 'B' and (resid 284 through 308 )
9X-RAY DIFFRACTION9chain 'B' and (resid 309 through 334 )
10X-RAY DIFFRACTION10chain 'B' and (resid 335 through 375 )
11X-RAY DIFFRACTION11chain 'A' and (resid 5 through 165 )
12X-RAY DIFFRACTION12chain 'A' and (resid 166 through 196 )
13X-RAY DIFFRACTION13chain 'A' and (resid 197 through 273 )
14X-RAY DIFFRACTION14chain 'A' and (resid 274 through 375 )
15X-RAY DIFFRACTION15chain 'C' and (resid 5 through 60 )
16X-RAY DIFFRACTION16chain 'C' and (resid 61 through 112 )
17X-RAY DIFFRACTION17chain 'C' and (resid 113 through 165 )
18X-RAY DIFFRACTION18chain 'C' and (resid 166 through 196 )
19X-RAY DIFFRACTION19chain 'C' and (resid 197 through 216 )
20X-RAY DIFFRACTION20chain 'C' and (resid 217 through 348 )
21X-RAY DIFFRACTION21chain 'C' and (resid 349 through 375 )
22X-RAY DIFFRACTION22chain 'D' and (resid 6 through 38 )
23X-RAY DIFFRACTION23chain 'D' and (resid 39 through 78 )
24X-RAY DIFFRACTION24chain 'D' and (resid 79 through 165 )
25X-RAY DIFFRACTION25chain 'D' and (resid 166 through 196 )
26X-RAY DIFFRACTION26chain 'D' and (resid 197 through 246 )
27X-RAY DIFFRACTION27chain 'D' and (resid 247 through 347 )
28X-RAY DIFFRACTION28chain 'D' and (resid 348 through 375 )
29X-RAY DIFFRACTION29chain 'R' and (resid 568 through 602 )
30X-RAY DIFFRACTION30chain 'R' and (resid 603 through 653 )
31X-RAY DIFFRACTION31chain 'R' and (resid 654 through 702 )
32X-RAY DIFFRACTION32chain 'R' and (resid 703 through 737 )
33X-RAY DIFFRACTION33chain 'R' and (resid 738 through 770 )
34X-RAY DIFFRACTION34chain 'R' and (resid 771 through 790 )
35X-RAY DIFFRACTION35chain 'Q' and (resid 561 through 581 )
36X-RAY DIFFRACTION36chain 'Q' and (resid 582 through 602 )
37X-RAY DIFFRACTION37chain 'Q' and (resid 603 through 641 )
38X-RAY DIFFRACTION38chain 'Q' and (resid 642 through 653 )
39X-RAY DIFFRACTION39chain 'Q' and (resid 654 through 667 )
40X-RAY DIFFRACTION40chain 'Q' and (resid 668 through 702 )
41X-RAY DIFFRACTION41chain 'Q' and (resid 703 through 718 )
42X-RAY DIFFRACTION42chain 'Q' and (resid 719 through 737 )
43X-RAY DIFFRACTION43chain 'Q' and (resid 738 through 770 )
44X-RAY DIFFRACTION44chain 'Q' and (resid 771 through 790 )
45X-RAY DIFFRACTION45chain 'S' and (resid 567 through 602 )
46X-RAY DIFFRACTION46chain 'S' and (resid 603 through 641 )
47X-RAY DIFFRACTION47chain 'S' and (resid 642 through 667 )
48X-RAY DIFFRACTION48chain 'S' and (resid 668 through 790 )
49X-RAY DIFFRACTION49chain 'T' and (resid 561 through 602 )
50X-RAY DIFFRACTION50chain 'T' and (resid 603 through 641 )
51X-RAY DIFFRACTION51chain 'T' and (resid 642 through 681 )
52X-RAY DIFFRACTION52chain 'T' and (resid 682 through 790 )

+
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