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- PDB-9spu: Echovirus 18 particle missing one pentamer in situ, symmetrized r... -

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Basic information

Entry
Database: PDB / ID: 9spu
TitleEchovirus 18 particle missing one pentamer in situ, symmetrized reconstruction (C5)
Components
  • Echovirus 18 viral protein 1
  • Echovirus 18 viral protein 2
  • Echovirus 18 viral protein 3
KeywordsVIRUS / in situ structure
Function / homology
Function and homology information


symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / DNA replication / RNA helicase activity / endocytosis involved in viral entry into host cell / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / virion attachment to host cell / host cell nucleus / structural molecule activity / DNA-templated transcription / proteolysis / RNA binding / zinc ion binding / ATP binding
Similarity search - Function
Picornavirus coat protein VP4 superfamily / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) ...Picornavirus coat protein VP4 superfamily / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesEchovirus E18
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.5 Å
AuthorsMukhamedova, L. / Plevka, P.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
European Research Council (ERC)European Union
CitationJournal: Proc Natl Acad Sci U S A / Year: 2026
Title: Particles of echovirus 18 open to release their genomes in vivo.
Authors: Liya Mukhamedova / David Buchta / Zuzana Trebichalská / Yevgen Levdansky / Jana Moravcová / David Potěšil / Zbyněk Zdráhal / Dominik Hrebík / Lucie Nepovímová / Torleif Tollefsrud ...Authors: Liya Mukhamedova / David Buchta / Zuzana Trebichalská / Yevgen Levdansky / Jana Moravcová / David Potěšil / Zbyněk Zdráhal / Dominik Hrebík / Lucie Nepovímová / Torleif Tollefsrud Gjølberg / Jan Terje Andersen / Jiří Nováček / Tibor Füzik / Pavel Plevka /
Abstract: Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. ...Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. Enterovirus cell entry involves receptor-mediated endocytosis followed by destabilizing rearrangements of the virus capsid that enable genome release. However, the mechanism of enterovirus genome release has not been visualized in infected cells. Here, we used cryoelectron tomography and microscopy to image echovirus 18 (E18) entry into host cells and its interaction with the neonatal Fc receptor (FcRn). 30 min postinfection, endosomes and cytoplasm contained empty capsids missing one or several pentamers of capsid proteins, providing evidence that in vivo E18 releases its genome through capsid opening. In vitro, FcRn binding induced the expulsion of pocket factors from hydrophobic pockets in VP1, priming the virus for uncoating. The cryoelectron microscopy reconstruction of genome-containing particles of E18 inside infected cells did not reveal pocket factors, indicating that receptor binding triggers the same priming process during infection. We did not detect activated particles in infected cells, suggesting that these intermediates are short-lived and rapidly release their genomes in vivo. Our results identify capsid opening as the in vivo mechanism of echovirus 18 genome release, providing structural evidence for a process previously only inferred from in vitro experiments.
History
DepositionSep 18, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 17, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Echovirus 18 viral protein 1
g: Echovirus 18 viral protein 3
f: Echovirus 18 viral protein 2
e: Echovirus 18 viral protein 1
b: Echovirus 18 viral protein 1
c: Echovirus 18 viral protein 2
d: Echovirus 18 viral protein 3
Y: Echovirus 18 viral protein 1
Z: Echovirus 18 viral protein 2
a: Echovirus 18 viral protein 3
V: Echovirus 18 viral protein 1
W: Echovirus 18 viral protein 2
X: Echovirus 18 viral protein 3
S: Echovirus 18 viral protein 1
T: Echovirus 18 viral protein 2
U: Echovirus 18 viral protein 3
P: Echovirus 18 viral protein 1
Q: Echovirus 18 viral protein 2
R: Echovirus 18 viral protein 3
M: Echovirus 18 viral protein 1
N: Echovirus 18 viral protein 2
O: Echovirus 18 viral protein 3
J: Echovirus 18 viral protein 1
K: Echovirus 18 viral protein 2
L: Echovirus 18 viral protein 3
G: Echovirus 18 viral protein 1
H: Echovirus 18 viral protein 2
I: Echovirus 18 viral protein 3
D: Echovirus 18 viral protein 1
E: Echovirus 18 viral protein 2
F: Echovirus 18 viral protein 3
C: Echovirus 18 viral protein 3
B: Echovirus 18 viral protein 2


Theoretical massNumber of molelcules
Total (without water)962,61633
Polymers962,61633
Non-polymers00
Water00
1
A: Echovirus 18 viral protein 1
g: Echovirus 18 viral protein 3
f: Echovirus 18 viral protein 2
e: Echovirus 18 viral protein 1
b: Echovirus 18 viral protein 1
c: Echovirus 18 viral protein 2
d: Echovirus 18 viral protein 3
Y: Echovirus 18 viral protein 1
Z: Echovirus 18 viral protein 2
a: Echovirus 18 viral protein 3
V: Echovirus 18 viral protein 1
W: Echovirus 18 viral protein 2
X: Echovirus 18 viral protein 3
S: Echovirus 18 viral protein 1
T: Echovirus 18 viral protein 2
U: Echovirus 18 viral protein 3
P: Echovirus 18 viral protein 1
Q: Echovirus 18 viral protein 2
R: Echovirus 18 viral protein 3
M: Echovirus 18 viral protein 1
N: Echovirus 18 viral protein 2
O: Echovirus 18 viral protein 3
J: Echovirus 18 viral protein 1
K: Echovirus 18 viral protein 2
L: Echovirus 18 viral protein 3
G: Echovirus 18 viral protein 1
H: Echovirus 18 viral protein 2
I: Echovirus 18 viral protein 3
D: Echovirus 18 viral protein 1
E: Echovirus 18 viral protein 2
F: Echovirus 18 viral protein 3
C: Echovirus 18 viral protein 3
B: Echovirus 18 viral protein 2
x 5


Theoretical massNumber of molelcules
Total (without water)4,813,081165
Polymers4,813,081165
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
MethodUCSF CHIMERA
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
d_1ens_1chain "e"
d_2ens_1chain "D"
d_3ens_1chain "G"
d_4ens_1chain "J"
d_5ens_1chain "M"
d_6ens_1chain "P"
d_7ens_1chain "S"
d_8ens_1chain "V"
d_9ens_1chain "Y"
d_10ens_1chain "b"
d_11ens_1chain "A"
d_1ens_2chain "c"
d_2ens_2chain "E"
d_3ens_2chain "H"
d_4ens_2chain "K"
d_5ens_2chain "N"
d_6ens_2chain "Q"
d_7ens_2chain "T"
d_8ens_2chain "W"
d_9ens_2chain "Z"
d_10ens_2chain "B"
d_11ens_2chain "f"
d_1ens_3chain "F"
d_2ens_3chain "C"
d_3ens_3chain "I"
d_4ens_3chain "L"
d_5ens_3chain "O"
d_6ens_3chain "R"
d_7ens_3chain "U"
d_8ens_3chain "X"
d_9ens_3chain "a"
d_10ens_3chain "d"
d_11ens_3chain "g"

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_1ens_1GLNGLNASPASPeD1043 - 127543 - 275
d_2ens_1GLNGLNASPASPDCA1043 - 127543 - 275
d_3ens_1GLNGLNASPASPGZ1043 - 127543 - 275
d_4ens_1GLNGLNASPASPJW1043 - 127543 - 275
d_5ens_1GLNGLNASPASPMT1043 - 127543 - 275
d_6ens_1GLNGLNASPASPPQ1043 - 127543 - 275
d_7ens_1GLNGLNASPASPSN1043 - 127543 - 275
d_8ens_1GLNGLNASPASPVK1043 - 127543 - 275
d_9ens_1GLNGLNASPASPYH1043 - 127543 - 275
d_10ens_1GLNGLNASPASPbE1043 - 127543 - 275
d_11ens_1GLNGLNASPASPAA1043 - 127543 - 275
d_1ens_2VALVALALAALAcF2013 - 225713 - 257
d_2ens_2VALVALALAALAEDA2013 - 225713 - 257
d_3ens_2VALVALALAALAHAA2013 - 225713 - 257
d_4ens_2VALVALALAALAKX2013 - 225713 - 257
d_5ens_2VALVALALAALANU2013 - 225713 - 257
d_6ens_2VALVALALAALAQR2013 - 225713 - 257
d_7ens_2VALVALALAALATO2013 - 225713 - 257
d_8ens_2VALVALALAALAWL2013 - 225713 - 257
d_9ens_2VALVALALAALAZI2013 - 225713 - 257
d_10ens_2VALVALALAALABGA2013 - 225713 - 257
d_11ens_2VALVALALAALAfC2013 - 225713 - 257
d_1ens_3GLYGLYALAALAFEA3001 - 32331 - 233
d_2ens_3GLYGLYALAALACFA3001 - 32331 - 233
d_3ens_3GLYGLYALAALAIBA3001 - 32331 - 233
d_4ens_3GLYGLYALAALALY3001 - 32331 - 233
d_5ens_3GLYGLYALAALAOV3001 - 32331 - 233
d_6ens_3GLYGLYALAALARS3001 - 32331 - 233
d_7ens_3GLYGLYALAALAUP3001 - 32331 - 233
d_8ens_3GLYGLYALAALAXM3001 - 32331 - 233
d_9ens_3GLYGLYALAALAaJ3001 - 32331 - 233
d_10ens_3GLYGLYALAALAdG3001 - 32331 - 233
d_11ens_3GLYGLYALAALAgB3001 - 32331 - 233

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(0.376136821278, -0.626297007227, -0.682841965917), (0.273677993109, 0.779176326626, -0.56390123968), (0.885223953453, 0.0252252009653, 0.464480614741)-2.03958024219, -4.4263650599, 0.205449659253
2given(0.199726719758, -0.93086529158, -0.305939612254), (-0.415197574365, -0.363214307119, 0.834078138633), (-0.887536034004, -0.0395623057411, -0.459036613255)-0.320126913594, 1.12518955838, -0.359845338218
3given(0.199624667289, -0.424868421901, -0.882970450401), (-0.939013289308, -0.340446563114, -0.0484786568195), (-0.280007204751, 0.838798522731, -0.466918626263)-1.23435732508, 2.97185779889, -3.09542884342
4given(0.701470445616, -0.672159811763, 0.236939657673), (0.167425505016, 0.478565195689, 0.861942024585), (-0.692753862636, -0.564957114236, 0.448236037012)-0.48744705969, 0.195699578162, -1.18324448155
5given(0.85099735144, -0.524937188301, 0.0156350945497), (-0.525010819509, -0.851095247164, 0.000720869129412), (0.0129285436463, -0.0088220515225, -0.99987750458)-0.572948988167, 1.40873914077, -1.99541729712
6given(0.947181705298, -0.0948583885242, -0.306347357219), (0.221913406593, -0.495755428692, 0.839631463737), (-0.231519453011, -0.863266147286, -0.448520124218)-0.228766338943, 0.418424264995, -0.90610735805
7given(0.701890759483, 0.141858735041, -0.698015373072), (-0.664620522376, 0.482890914397, -0.570171839035), (0.256181425925, 0.864113687014, 0.43321889724)-2.82816270514, -1.24845440765, -1.44419287601
8given(0.490245356511, -0.84398848815, -0.217584287784), (-0.495249861846, -0.0643211088447, -0.866366186608), (0.717207825362, 0.532490588488, -0.449518307093)0.519522890876, -0.988145885954, -3.70492904442
9given(0.651822064425, -0.163679924358, -0.740497723623), (0.693995587561, 0.522436628893, 0.495409016104), (0.30577462415, -0.836820680405, 0.454128867253)-1.36295503204, -0.0771798081819, 0.804907960721
10given(0.62610525482, 0.331367444928, 0.705824217726), (-0.218060277041, -0.794677432506, 0.566513454246), (0.748626692994, -0.508609275089, -0.425293639536)1.16348277465, 2.57113856754, -1.28139173808
11given(0.844665543941, -0.409145481483, 0.345166762393), (0.482602125634, 0.303080759059, -0.821728204348), (0.231592977468, 0.860663713927, 0.453456353266)-2.12964253301, -4.23772967469, 0.550462148938
12given(0.469654573161, -0.50399870635, 0.724851630271), (-0.853136231002, -0.047873916441, 0.519486919447), (-0.227119248987, -0.862376595301, -0.452463760557)0.397640722219, 5.77627993003, -0.204707670993
13given(0.853046807584, -0.520992804408, 0.0296250202595), (-0.520621092707, -0.853559912849, -0.0197269613927), (0.0355643346493, 0.00140461102039, -0.999366401861)-2.30404025905, 1.92556280684, -2.86139332328
14given(0.368648369703, 0.238027158291, 0.898577459895), (-0.604808543053, 0.795491891281, 0.037406913209), (-0.705907221783, -0.557257321909, 0.437217647646)-0.115168389604, -0.238807627951, 1.97905605919
15given(0.620735358837, 0.318688287402, 0.716327711151), (-0.218386998931, -0.807217218952, 0.548368015228), (0.752990526493, -0.496828075796, -0.431470891386)-0.649060650235, 2.44731470853, -2.11916854421
16given(0.866334634348, 0.431304041261, 0.251875217758), (-0.409030026773, 0.32325141938, 0.853348086695), (0.286633456747, -0.842309529722, 0.456460203756)-1.55748810121, 0.635748155562, 1.66015914977
17given(0.95481302704, 0.210615415701, -0.209697949592), (-0.0852186691524, -0.481925475238, -0.872058263389), (-0.284727697672, 0.85052277041, -0.442200356391)-3.13343819947, -0.544128481743, -2.18716079077
18given(0.62375284178, -0.198942609463, 0.755879772524), (0.329902802623, -0.80969538283, -0.485342691143), (0.708587703247, 0.552100738239, -0.439418071593)-0.28157218186, -1.01370771119, -0.692281062448
19given(-0.126912819537, 0.964196092115, 0.232849806072), (-0.441455379884, -0.26512242845, 0.857220651585), (0.888262508388, 0.00599949026207, 0.459296987044)-2.493505207, 1.6550250681, -0.0842089598886
20given(0.648258539812, 0.686495695366, 0.329369892073), (-0.12434335544, 0.522212500566, -0.843701863345), (-0.751198772309, 0.505981980407, 0.423889891345)-1.49209369149, -1.82039806025, 3.10508154511
21given(-0.441708422528, 0.0328543478788, 0.89655689239), (0.0174571122814, -0.99882529689, 0.0452026052623), (0.896988806339, 0.0356176658017, 0.440616004231)-1.47777539725, -0.324987532654, 0.676160133414
22given(0.859867405304, -0.510498368988, 0.00441141216887), (-0.510506599339, -0.859873346254, 0.000916750819313), (0.00332525594533, -0.00304033917293, -0.999989849454)0.0674030509822, -1.19058927239, -0.0820602892949
23given(0.940821513835, 0.23881910413, -0.240458550706), (-0.0913351053254, -0.504593536317, -0.858512237328), (-0.326362953842, 0.829669089824, -0.452919886679)1.81951326533, -1.10184575182, 2.20489240433
24given(0.526075422011, -0.470517420113, 0.708419372777), (-0.820976875678, -0.0636202560315, 0.56740587997), (-0.221904528927, -0.880094211089, -0.419752974557)-1.85602712323, -2.16981199481, -4.05017910857
25given(0.633206684369, -0.198929253662, 0.747981581931), (0.328467711755, -0.805994904701, -0.492423776772), (0.700826838245, 0.557493825646, -0.445019524473)0.0954177043473, -0.272626475001, 0.448823065634
26given(0.617055683676, 0.362598799728, 0.69840131277), (-0.179042217465, -0.799544744682, 0.573299298461), (0.766280736811, -0.478800910282, -0.428443135906)2.20827551736, -3.66801932414, -2.9484584061
27given(0.646332433243, 0.699527130008, 0.304821554554), (-0.171857037285, 0.522660108502, -0.835039861154), (-0.743451104293, 0.487327616049, 0.458030839751)1.18124308933, 1.05453226977, -0.490084727978
28given(0.856093935356, -0.414081489981, 0.309256678993), (0.452387932971, 0.311063291675, -0.835813846903), (0.249896642533, 0.855439155187, 0.453624866849)0.927620008976, 0.311826723795, -1.5665626728
29given(0.855656419874, 0.463445908095, 0.230369228412), (-0.401166672615, 0.312695645406, 0.860980100889), (0.326982250148, -0.829119607544, 0.453479089346)1.16230394482, 0.00321530158125, -1.48704983887
30given(0.360402746128, 0.272445641761, 0.892122879916), (-0.625951217227, 0.779722635991, 0.0147541375399), (-0.691588703085, -0.563742834285, 0.451551860318)1.97968837513, 3.34019110167, -1.26382345985

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Components

#1: Protein
Echovirus 18 viral protein 1 / VP1


Mass: 32564.445 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Echovirus E18
References: UniProt: Q8V635, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase
#2: Protein
Echovirus 18 viral protein 3 / VP3


Mass: 26143.783 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Echovirus E18
References: UniProt: Q8V635, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase
#3: Protein
Echovirus 18 viral protein 2 / VP2


Mass: 28802.328 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Echovirus E18
References: UniProt: Q8V635, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: CELL / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Echovirus E18 / Type: VIRUS / Entity ID: all / Source: NATURAL
Molecular weightValue: 7.9 MDa / Experimental value: NO
Source (natural)Organism: Echovirus E18
Details of virusEmpty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION
Natural hostOrganism: Homo sapiens
Virus shellDiameter: 330 nm
Buffer solutionpH: 7.4
SpecimenConc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 42000 X / Nominal defocus max: 4500 nm / Nominal defocus min: 2500 nm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 8 sec. / Electron dose: 34 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 1290
EM imaging opticsPhase plate: OTHER

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.21_5207model refinement
5CTFFIND4CTF correction
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
12cryoSPARCclassification
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 3896 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL
Atomic model buildingPDB-ID: 6hbk

6hbk


Accession code: 6hbk / Source name: PDB / Type: experimental model
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 17.72 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.001558751
ELECTRON MICROSCOPYf_angle_d0.416780256
ELECTRON MICROSCOPYf_chiral_restr0.0419108
ELECTRON MICROSCOPYf_plane_restr0.003410153
ELECTRON MICROSCOPYf_dihedral_angle_d2.83177975
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2DeELECTRON MICROSCOPYNCS constraints2.24188452307E-13
ens_1d_3DeELECTRON MICROSCOPYNCS constraints1.01174901049E-13
ens_1d_4DeELECTRON MICROSCOPYNCS constraints2.59785005888E-11
ens_1d_5DeELECTRON MICROSCOPYNCS constraints5.32926124747E-11
ens_1d_6DeELECTRON MICROSCOPYNCS constraints9.17857115361E-14
ens_1d_7DeELECTRON MICROSCOPYNCS constraints1.42684358579E-13
ens_1d_8DeELECTRON MICROSCOPYNCS constraints5.20586002064E-11
ens_1d_9DeELECTRON MICROSCOPYNCS constraints3.91722453401E-10
ens_1d_10DeELECTRON MICROSCOPYNCS constraints2.33364446384E-13
ens_1d_11DeELECTRON MICROSCOPYNCS constraints1.43114062568E-13
ens_2d_2FcELECTRON MICROSCOPYNCS constraints3.61138329142E-13
ens_2d_3FcELECTRON MICROSCOPYNCS constraints2.05927157469E-13
ens_2d_4FcELECTRON MICROSCOPYNCS constraints9.21154142942E-14
ens_2d_5FcELECTRON MICROSCOPYNCS constraints1.89577533931E-11
ens_2d_6FcELECTRON MICROSCOPYNCS constraints4.08744428152E-11
ens_2d_7FcELECTRON MICROSCOPYNCS constraints1.64769599866E-13
ens_2d_8FcELECTRON MICROSCOPYNCS constraints2.08200205055E-13
ens_2d_9FcELECTRON MICROSCOPYNCS constraints3.29551765695E-13
ens_2d_10FcELECTRON MICROSCOPYNCS constraints4.01003416709E-13
ens_2d_11FcELECTRON MICROSCOPYNCS constraints2.96147835555E-13
ens_3d_2EAFELECTRON MICROSCOPYNCS constraints2.60877995817E-13
ens_3d_3EAFELECTRON MICROSCOPYNCS constraints2.32464002501E-13
ens_3d_4EAFELECTRON MICROSCOPYNCS constraints4.19896871116E-13
ens_3d_5EAFELECTRON MICROSCOPYNCS constraints4.80847916705E-11
ens_3d_6EAFELECTRON MICROSCOPYNCS constraints7.08004030011E-13
ens_3d_7EAFELECTRON MICROSCOPYNCS constraints1.98992138862E-13
ens_3d_8EAFELECTRON MICROSCOPYNCS constraints3.45021517532E-13
ens_3d_9EAFELECTRON MICROSCOPYNCS constraints1.87055764488E-11
ens_3d_10EAFELECTRON MICROSCOPYNCS constraints2.03616712602E-13
ens_3d_11EAFELECTRON MICROSCOPYNCS constraints1.82828427803E-13

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