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- PDB-5mps: Structure of a spliceosome remodeled for exon ligation -

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Basic information

Entry
Database: PDB / ID: 5mps
TitleStructure of a spliceosome remodeled for exon ligation
DescriptorUnknown
Small nuclear ribonucleoprotein-associated protein B
(Pre-mRNA-splicing factor ...) x 15
(Pre-mRNA-processing ...) x 2
(Small nuclear ribonucleoprotein ...) x 6
KeywordsSPLICING / pre-mRNA splicing / trans-esterification / lariat intermediate / complex C-star
Specimen sourceSaccharomyces cerevisiae / yeast / Baker's yeast / サッカロミセス・セレビシエ /
MethodElectron microscopy (3.85 Å resolution / Particle / Single particle)
AuthorsFica, S.M. / Oubridge, C. / Galej, W.P. / Wilkinson, M.E. / Newman, A.J. / Bai, X.-C. / Nagai, K.
CitationNature, 2017, 542, 377-380

primary. Nature, 2017, 542, 377-380 StrPapers
Structure of a spliceosome remodelled for exon ligation.
Sebastian M Fica / Chris Oubridge / Wojciech P Galej / Max E Wilkinson / Xiao-Chen Bai / Andrew J Newman / Kiyoshi Nagai

#1. Science, 2015, 349, 1191-1198 StrPapers
Structural basis of pre-mRNA splicing.
Hang, J. / Wan, R. / Yan, C. / Shi, Y.

#2. Nature, 2015, 523, 47-52 StrPapers
The architecture of the spliceosomal U4/U6.U5 tri-snRNP.
Nguyen, T.H. / Galej, W.P. / Bai, X.C. / Savva, C.G. / Newman, A.J. / Scheres, S.H. / Nagai, K.

#3. Nature, 2016, 530, 298-302 StrPapers
Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 A resolution.
Nguyen, T.H. / Galej, W.P. / Bai, X.C. / Oubridge, C. / Newman, A.J. / Scheres, S.H. / Nagai, K.

#4. Nature, 2016, 537, 197-201 StrPapers
Cryo-EM structure of the spliceosome immediately after branching.
Galej, W.P. / Wilkinson, M.E. / Fica, S.M. / Oubridge, C. / Newman, A.J. / Nagai, K.

Validation Report
SummaryFull reportAbout validation report
DateDeposition: Dec 18, 2016 / Release: Jan 18, 2017
RevisionDateData content typeGroupCategoryItemProviderType
1.0Jan 18, 2017Structure modelrepositoryInitial release
1.1Mar 1, 2017Structure modelDatabase references
1.2Jul 5, 2017Structure modelData collectionem_imaging_em_imaging.details
1.3Aug 30, 2017Structure modelAuthor supporting evidence / Data collectionem_image_scans / em_imaging_optics / em_software / pdbx_audit_support_em_imaging_optics.energyfilter_name / _em_software.name / _pdbx_audit_support.funding_organization

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Assembly

Deposited unit
I: Yeast UBC4 gene for ubiquitin-conjugating enzyme
E: UBC4 gene exon
2: U2 snRNA
6: Saccharomyces cerevisiae strain T.52_2H chromosome XII sequence
5: U5 snRNA
A: Pre-mRNA-splicing factor 8
C: Pre-mRNA-splicing factor SNU114
H: Pre-mRNA-splicing factor CWC22
J: Pre-mRNA-splicing factor PRP46
K: Pre-mRNA-processing protein 45
L: Pre-mRNA-splicing factor BUD31
M: Pre-mRNA-splicing factor CWC2
N: Pre-mRNA-splicing factor SLT11
O: Pre-mRNA-splicing factor CEF1
P: Pre-mRNA-splicing factor CWC15
R: Pre-mRNA-splicing factor CWC21
S: Pre-mRNA-splicing factor CLF1
T: Pre-mRNA-splicing factor SYF1
a: Pre-mRNA-splicing factor 18
c: Pre-mRNA-splicing factor SLU7
o: Pre-mRNA-processing factor 17
X: Unknown
y: Pre-mRNA-splicing factor SYF2
b: Small nuclear ribonucleoprotein-associated protein B
d: Small nuclear ribonucleoprotein Sm D3
e: Small nuclear ribonucleoprotein E
f: Small nuclear ribonucleoprotein F
g: Small nuclear ribonucleoprotein G
h: Small nuclear ribonucleoprotein Sm D1
j: Small nuclear ribonucleoprotein Sm D2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,696,09543
Polyers1,694,36830
Non-polymers1,72713
Water0
#1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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RNA chain , 5 types, 5 molecules IE265

#1: RNA chainYeast UBC4 gene for ubiquitin-conjugating enzyme


Mass: 30200.730 Da / Num. of mol.: 1
Details: Saccharomyces cerevisiae UBC4 pre-mRNA intron, in vitro transcribed.
Source: (gene. exp.) Saccharomyces cerevisiae / References: GenBank: 4718
#2: RNA chainUBC4 gene exon


Mass: 6518.976 Da / Num. of mol.: 1
Details: Saccharomyces cerevisiae UBC4 pre-mRNA exon, in vitro transcribed.
Source: (gene. exp.) Saccharomyces cerevisiae
#3: RNA chainU2 snRNA


Mass: 376267.406 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae U2 snRNA / Source: (gene. exp.) Saccharomyces cerevisiae / References: GenBank: 536627
#4: RNA chainSaccharomyces cerevisiae strain T.52_2H chromosome XII sequence


Mass: 35883.176 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae U6 snRNA / Source: (gene. exp.) Saccharomyces cerevisiae / References: GenBank: 1039022925
#5: RNA chainU5 snRNA


Mass: 57444.875 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae U5 snRNA / Source: (gene. exp.) Saccharomyces cerevisiae / References: GenBank: 1039023700

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Pre-mRNA-splicing factor ... , 15 types, 15 molecules ACHJLMNOPR...

#6: Polypeptide(L)Pre-mRNA-splicing factor 8


Mass: 279867.469 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Prp8 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P33334

Cellular component

Molecular function

Biological process

  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
  • mRNA 3'-splice site recognition (GO: 0000389)
  • spliceosomal tri-snRNP complex assembly (GO: 0000244)
#7: Polypeptide(L)Pre-mRNA-splicing factor SNU114 / 114 kDa U5 small nuclear ribonucleoprotein component / Growth inhibitory protein 10


Mass: 114174.008 Da / Num. of mol.: 1 / Details: c Snu114 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P36048

Cellular component

Molecular function

Biological process

  • generation of catalytic spliceosome for first transesterification step (GO: 0000349)
  • mRNA splicing, via spliceosome (GO: 0000398)
  • spliceosomal tri-snRNP complex assembly (GO: 0000244)
  • spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) (GO: 0000388)
#8: Polypeptide(L)Pre-mRNA-splicing factor CWC22 / Complexed with CEF1 protein 22


Mass: 67386.062 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Cwc22 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P53333

Cellular component

Molecular function

Biological process

#9: Polypeptide(L)Pre-mRNA-splicing factor PRP46 / Complexed with CEF1 protein 1 / PRP nineteen-associated complex protein 50 / PRP19-associated complex protein 50 / Pre-mRNA-processing protein 46


Mass: 50771.289 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Prp46 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q12417

Cellular component

Biological process

#11: Polypeptide(L)Pre-mRNA-splicing factor BUD31 / Bud site selection protein 31 / Complexed with CEF1 protein 14


Mass: 18484.502 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Bud31 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P25337

Cellular component

Biological process

#12: Polypeptide(L)Pre-mRNA-splicing factor CWC2 / Complexed with CEF1 protein 2 / PRP19-associated complex protein 40 / Synthetic lethal with CLF1 protein 3


Mass: 38486.562 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Cwc2 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q12046

Cellular component

Molecular function

Biological process

#13: Polypeptide(L)Pre-mRNA-splicing factor SLT11 / Extracellular mutant protein 2 / Synthetic lethality with U2 protein 11


Mass: 40988.590 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Ecm2 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P38241

Cellular component

Molecular function

Biological process

#14: Polypeptide(L)Pre-mRNA-splicing factor CEF1 / PRP nineteen-associated complex protein 85 / PRP19-associated complex protein 85


Mass: 67837.773 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Cef1 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q03654

Cellular component

Molecular function

  • RNA polymerase II transcription factor activity, sequence-specific DNA binding (GO: 0000981)
  • sequence-specific DNA binding (GO: 0043565)
  • transcription factor activity, RNA polymerase II transcription factor recruiting (GO: 0001135)
  • transcription regulatory region DNA binding (GO: 0044212)

Biological process

  • cell differentiation (GO: 0030154)
  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
  • mRNA splicing, via spliceosome (GO: 0000398)
  • regulation of transcription from RNA polymerase II promoter (GO: 0006357)
#15: Polypeptide(L)Pre-mRNA-splicing factor CWC15 / Complexed with CEF1 protein 15


Mass: 19975.195 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Cwc15 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q03772

Cellular component

Molecular function

Biological process

#16: Polypeptide(L)Pre-mRNA-splicing factor CWC21 / Complexed with CEF1 protein 21


Mass: 15793.596 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Cwc21 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q03375

Cellular component

Biological process

#17: Polypeptide(L)Pre-mRNA-splicing factor CLF1 / Crooked neck-like factor 1 / PRP19-associated complex protein 77 / Synthetic lethal with CDC40 protein 3


Mass: 82555.859 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Clf1 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q12309

Cellular component

Molecular function

Biological process

#18: Polypeptide(L)Pre-mRNA-splicing factor SYF1 / PRP19-associated complex protein 90 / Synthetic lethal with CDC40 protein 1


Mass: 101875.852 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Syf1 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q04048

Cellular component

Biological process

  • generation of catalytic spliceosome for first transesterification step (GO: 0000349)
#19: Polypeptide(L)Pre-mRNA-splicing factor 18


Mass: 28414.391 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Prp18 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P33411

Cellular component

Biological process

  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
  • mRNA splicing, via spliceosome (GO: 0000398)
  • nuclear retention of unspliced pre-mRNA at the site of transcription (GO: 0071048)
#20: Polypeptide(L)Pre-mRNA-splicing factor SLU7 / Synthetic lethal with U2 snRNA protein 17 / Synthetic lethal with U5 snRNA protein 7


Mass: 44722.875 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Slu7 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q02775

Cellular component

Molecular function

Biological process

  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
#23: Polypeptide(L)Pre-mRNA-splicing factor SYF2 / PRP19 complex protein 31 / Synthetic lethal with CDC40 protein 2


Mass: 24850.719 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Syf2 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P53277

Cellular component

Biological process

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Pre-mRNA-processing ... , 2 types, 2 molecules Ko

#10: Polypeptide(L)Pre-mRNA-processing protein 45


Mass: 42548.727 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Prp45 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P28004

Cellular component

Molecular function

Biological process

  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
  • regulation of transcription from RNA polymerase II promoter (GO: 0006357)
#21: Polypeptide(L)Pre-mRNA-processing factor 17 / Cell division control protein 40


Mass: 52128.762 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae Prp17 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P40968

Cellular component

Biological process

  • generation of catalytic spliceosome for second transesterification step (GO: 0000350)
  • mRNA 3'-splice site recognition (GO: 0000389)
  • mRNA branch site recognition (GO: 0000348)

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Polypeptide(L) , 2 types, 2 molecules Xb

#22: Polypeptide(L)Unknown


Mass: 5805.147 Da / Num. of mol.: 1 / Details: Unknown protein helices within C-star complex / Source: (natural) Saccharomyces cerevisiae
#24: Polypeptide(L)Small nuclear ribonucleoprotein-associated protein B / snRNP-B / Sm protein B / SmB


Mass: 22426.990 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmB protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P40018

Cellular component

Molecular function

Biological process

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Small nuclear ribonucleoprotein ... , 6 types, 6 molecules defghj

#25: Polypeptide(L)Small nuclear ribonucleoprotein Sm D3 / Sm-D3 / snRNP core protein D3


Mass: 11240.139 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmD3 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P43321

Cellular component

Molecular function

Biological process

#26: Polypeptide(L)Small nuclear ribonucleoprotein E / snRNP-E / Sm protein E / SmE


Mass: 10385.098 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmE protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q12330

Cellular component

Molecular function

Biological process

#27: Polypeptide(L)Small nuclear ribonucleoprotein F / snRNP-F / Sm protein F / SmF


Mass: 9669.945 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmF protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P54999

Cellular component

Molecular function

Biological process

#28: Polypeptide(L)Small nuclear ribonucleoprotein G / snRNP-G / Sm protein G / SmG


Mass: 8490.809 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmG protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: P40204

Cellular component

Molecular function

Biological process

#29: Polypeptide(L)Small nuclear ribonucleoprotein Sm D1 / Sm-D1 / snRNP core protein D1


Mass: 16296.798 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmD1 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q02260

Cellular component

Molecular function

Biological process

#30: Polypeptide(L)Small nuclear ribonucleoprotein Sm D2 / Sm-D2 / snRNP core protein D2


Mass: 12876.066 Da / Num. of mol.: 1 / Details: Saccharomyces cerevisiae SmD2 protein / Source: (natural) Saccharomyces cerevisiae / References: UniProt: Q06217

Cellular component

Molecular function

Biological process

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Non-polymers , 5 types, 13 molecules

#31: ChemicalChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Formula: Mg
#32: ChemicalChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Formula: K
#33: ChemicalChemComp-I6P / INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE / MYO-INOSITOL HEXAKISPHOSPHATE


Mass: 660.035 Da / Num. of mol.: 1 / Formula: C6H18O24P6
#34: ChemicalChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / GTP *YM


Mass: 523.180 Da / Num. of mol.: 1 / Formula: C10H16N5O14P3
#35: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE

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Sample preparation

ComponentName: Saccharomyces cerevisiae spliceosome. Complex C just after Prp16-mediated remodeling
Type: COMPLEX
Details: Splicing extract was prepared from Slu7-TAPS yeast strains. An in vitro transcribed yeast UBC4 pre-mRNA substrate (with 2 x MS2 bacteriophage coat protein-binding stem loops at the 5' end and with a 2'-deoxy substitution at the 3'-splice site sequence UAG sequence (UA-2'dG) was pre-bound to an MS2-maltose binding protein fusion protein. This substrate-protein complex was added to the splicing extract. The splicing reaction proceeded through the first step but the second step was blocked by the deoxy substitution. Substrate-bound spliceosomes from the splicing extract were purified on amylose resin and eluted with maltose. Subsequently the spliceosomes were captured on streptactin resin and eluted with desthiobiotin. Purified spliceosomes were concentrated in 20 mM HEPES KOH pH 7.9, 100 mM KCl, 0.25 mM EDTA.
Entity ID: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30
Source: MULTIPLE SOURCES
Buffer solutionDetails: NP-40 is also called IGEPAL CA-630 / pH: 7.9
Buffer component
IDConc.UnitsNameFormulaBuffer ID
120millimolarHepes.KOH pH 7.91
2100millimolarpotassium chlorideKCl1
3250micromolarEDTA1
41% v/vglycerol1
50.0025% v/vNonidet P-40 (NP-40)1
SpecimenConc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400 / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 kelvins
Details: 3.5 microlitres sample were applied to the grid, left for 25 seconds and then blotted for 3.0-3.5 seconds before plunging.

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS / Details: GIF Quantum energy filter, 20 eV slit width
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 / Nominal defocus max: 4500 nm / Nominal defocus min: 500 nm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 0.8 sec. / Electron dose: 2 e/Å2
Details: Total dose: 40 electrons/Angstrom^2 over 16 seconds. 20 movie frames collected at 1.25 frames per second.
Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Number of real images: 3596
EM imaging opticsEnergyfilter name: GIF Quantum

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Processing

SoftwareName: REFMAC / Version: 5.8.0124 / Classification: refinement
EM software
IDNameVersionCategoryImage processing IDDetailsFitting ID
1RELION1.4PARTICLE SELECTION1
4CTFFIND4CTF CORRECTION1
7Coot0.8.3MODEL FITTINGPaul Emsley's experimental version.1
9RELION1.4INITIAL EULER ASSIGNMENT1
10RELION1.4FINAL EULER ASSIGNMENT1
11RELION1.4CLASSIFICATION1
12RELION1.4RECONSTRUCTION1
13REFMAC5.8MODEL REFINEMENTUsed "SOURCE EM" command to get correct electron form factors for refinement of electron microscopy structure.1
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionDetails: Selected initial particles automatically using C complex 2D class averages, low-pass filtered to 20 Angstrom for automatic particle picking.
Number of particles selected: 350000
3D reconstructionResolution: 3.85 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 65824 / Number of class averages: 4 / Symmetry type: POINT
Atomic model buildingDetails: Used secondary structure restraints generated in ProSMART and LibG.
Overall b value: 330 / Ref protocol: FLEXIBLE FIT / Ref space: RECIPROCAL / Target criteria: Fourier Shell Correlation
Refine
Refine IDB iso meanAniso B11Aniso B12Aniso B13Aniso B22Aniso B23Aniso B33Correlation coeff Fo to FcDetailsR factor R workR factor obsHighest resolutionLowest resolutionNumber reflection obsPercent reflection obsOverall SU BOverall SU MLOverall ESU RStereochemistry target valuesSolvent model details
1170.6440.000.34-0.53-0.26-0.070.260.952HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS0.321770.321773.85257.40357071100.0037.7300.5260.868MAXIMUM LIKELIHOOD WITH PHASESPARAMETERS FOR MASK CACLULATION
ELECTRON MICROSCOPY
Number of atoms included #1Total: 59157
Refine LS restraints
Refine IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0080.01861218
ELECTRON MICROSCOPYr_bond_other_d0.0020.02053354
ELECTRON MICROSCOPYr_angle_refined_deg1.2871.85984337
ELECTRON MICROSCOPYr_angle_other_deg1.0123.000122254
ELECTRON MICROSCOPYr_dihedral_angle_1_deg9.7535.1836844
ELECTRON MICROSCOPYr_dihedral_angle_2_deg32.32023.4852126
ELECTRON MICROSCOPYr_dihedral_angle_3_deg14.39715.0008722
ELECTRON MICROSCOPYr_dihedral_angle_4_deg14.12915.000340
ELECTRON MICROSCOPYr_chiral_restr0.0830.2029725
ELECTRON MICROSCOPYr_gen_planes_refined0.0050.02063652
ELECTRON MICROSCOPYr_gen_planes_other0.0020.02013902
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it5.46717.89927134
ELECTRON MICROSCOPYr_mcbond_other5.46717.89827133
ELECTRON MICROSCOPYr_mcangle_it9.58026.79733767
ELECTRON MICROSCOPYr_mcangle_other9.58026.79833768
ELECTRON MICROSCOPYr_scbond_it5.40118.17334084
ELECTRON MICROSCOPYr_scbond_other5.40118.17334085
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other9.74927.20850571
ELECTRON MICROSCOPYr_long_range_B_refined19.018122798
ELECTRON MICROSCOPYr_long_range_B_other19.018122798
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
Refine LS shellHighest resolution: 3.85 Å / R factor R work: 0.599 / Lowest resolution: 3.95 Å / Number reflection R free: 0 / Number reflection R work: 26341 / Total number of bins used: 20 / Percent reflection obs: 1

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