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- EMDB-53923: Structure of the Human Peptide-Loading Complex Arrested by HCMV US6 -

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Basic information

Entry
Database: EMDB / ID: EMD-53923
TitleStructure of the Human Peptide-Loading Complex Arrested by HCMV US6
Map data
Sample
  • Complex: Human peptide-loading complex arrested by HCMV US6
    • Protein or peptide: x 6 types
  • Ligand: x 5 types
Keywordsantigen processing / adaptive immunity / cryo-EM / ER chaperones / MHC class I / transporter associated with antigen processing / IMMUNE SYSTEM
Function / homology
Function and homology information


MHC class Ib protein complex assembly / peptide antigen stabilization / MHC class I protein complex binding / antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / MHC class Ib protein binding ...MHC class Ib protein complex assembly / peptide antigen stabilization / MHC class I protein complex binding / antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / MHC class Ib protein binding / peptide antigen transport / cytosol to endoplasmic reticulum transport / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / regulation of protein complex stability / TAP2 binding / TAP1 binding / peptide transport / peptide transmembrane transporter activity / TAP complex binding / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / MHC class I protein binding / molecular sequestering activity / antigen processing and presentation of peptide antigen via MHC class I / endoplasmic reticulum-Golgi intermediate compartment membrane / protein folding chaperone / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / T cell mediated cytotoxicity / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / lumenal side of endoplasmic reticulum membrane / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / regulation of iron ion transport / cellular response to iron(III) ion / negative regulation of iron ion transport / negative regulation of forebrain neuron differentiation / response to molecule of bacterial origin / regulation of erythrocyte differentiation / peptide antigen assembly with MHC class I protein complex / ER to Golgi transport vesicle membrane / defense response / HFE-transferrin receptor complex / MHC class I peptide loading complex / transferrin transport / negative regulation of receptor-mediated endocytosis / cellular response to iron ion / positive regulation of T cell cytokine production / multicellular organismal-level iron ion homeostasis / antigen processing and presentation of endogenous peptide antigen via MHC class I / MHC class I protein complex / ADP binding / peptide antigen assembly with MHC class II protein complex / positive regulation of T cell mediated cytotoxicity / negative regulation of epithelial cell proliferation / cellular response to nicotine / MHC class II protein complex / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / specific granule lumen / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / peptide antigen binding / recycling endosome membrane / phagocytic vesicle membrane / positive regulation of T cell activation / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / transmembrane transport / T cell differentiation in thymus / sensory perception of smell / Modulation by Mtb of host immune system / : / tertiary granule lumen / positive regulation of cellular senescence / MHC class II protein complex binding / DAP12 signaling / negative regulation of neuron projection development / late endosome membrane / protein transport / regulation of gene expression / protein refolding / ER-Phagosome pathway / protein-containing complex assembly / early endosome membrane / amyloid fibril formation / molecular adaptor activity / protein homotetramerization / adaptive immune response / intracellular iron ion homeostasis / learning or memory / immune response / host cell endoplasmic reticulum membrane / endoplasmic reticulum lumen / Amyloid fiber formation / external side of plasma membrane / Golgi membrane / lysosomal membrane / focal adhesion / Neutrophil degranulation
Similarity search - Function
Viral unique short region 6 / Viral unique short region 6 / Tapasin / Antigen peptide transporter 2 / ABC transporter Tap-like / Type 1 protein exporter / : / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / ABC transporter transmembrane region ...Viral unique short region 6 / Viral unique short region 6 / Tapasin / Antigen peptide transporter 2 / ABC transporter Tap-like / Type 1 protein exporter / : / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / MHC classes I/II-like antigen recognition protein / : / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Immunoglobulin-like fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
MHC class I antigen / Tapasin / Unique short US6 glycoprotein / Beta-2-microglobulin / Antigen peptide transporter 1 / Antigen peptide transporter 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.7 Å
AuthorsStolz M / Susac L / Trowitzsch S / Tampe R
Funding supportEuropean Union, Germany, United States, 5 items
OrganizationGrant numberCountry
European Research Council (ERC)789121European Union
European Research Council (ERC)101141396European Union
German Research Foundation (DFG)TA157/12-1 Germany
German Research Foundation (DFG)CRC1507/P18 Germany
Other privateUR013222 United States
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionMay 29, 2025-
Header (metadata) releaseDec 3, 2025-
Map releaseDec 3, 2025-
UpdateApr 15, 2026-
Current statusApr 15, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_53923.png

Downloads & links

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Map

FileDownload / File: emd_53923.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.11
Minimum - Maximum-0.042457413 - 0.92385787
Average (Standard dev.)0.008457146 (±0.017306233)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 424.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Human peptide-loading complex arrested by HCMV US6

EntireName: Human peptide-loading complex arrested by HCMV US6
Components
  • Complex: Human peptide-loading complex arrested by HCMV US6
    • Protein or peptide: Antigen peptide transporter 1
    • Protein or peptide: Tapasin
    • Protein or peptide: MHC class I antigen
    • Protein or peptide: Beta-2-microglobulin
    • Protein or peptide: Antigen peptide transporter 2
    • Protein or peptide: Unique short US6 glycoprotein
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: water

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Supramolecule #1: Human peptide-loading complex arrested by HCMV US6

SupramoleculeName: Human peptide-loading complex arrested by HCMV US6 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Antigen peptide transporter 1

MacromoleculeName: Antigen peptide transporter 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: ABC-type antigen peptide transporter
Source (natural)Organism: Homo sapiens (human) / Tissue: Burkitt lymphoma
Molecular weightTheoretical: 81.080383 KDa
SequenceString: MASSRCPAPR GCRCLPGASL AWLGTVLLLL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV GLSRWAVLWL GACGVLRATV GSKSENAGA QGWLAALKPL AAALGLALPG LALFRELISW GAPGSADSTR LLHWGSHPTA FVVSYAAALP AAALWHKLGS L WVPGGQGG ...String:
MASSRCPAPR GCRCLPGASL AWLGTVLLLL ADWVLLRTAL PRIFSLLVPT ALPLLRVWAV GLSRWAVLWL GACGVLRATV GSKSENAGA QGWLAALKPL AAALGLALPG LALFRELISW GAPGSADSTR LLHWGSHPTA FVVSYAAALP AAALWHKLGS L WVPGGQGG SGNPVRRLLG CLGSETRRLS LFLVLVVLSS LGEMAIPFFT GRLTDWILQD GSADTFTRNL TLMSILTIAS AV LEFVGDG IYNNTMGHVH SHLQGEVFGA VLRQETEFFQ QNQTGNIMSR VTEDTSTLSD SLSENLSLFL WYLVRGLCLL GIM LWGSVS LTMVTLITLP LLFLLPKKVG KWYQLLEVQV RESLAKSSQV AIEALSAMPT VRSFANEEGE AQKFREKLQE IKTL NQKEA VAYAVNSWTT SISCMLLKVG ILYIGGQLVT SGAVSSGNLV TFVLYQMQFT QAVEVLLSIY PRVQKAVGSS EKIFE YLDR TPRCPPSGLL TPLHLEGLVQ FQDVSFAYPN RPDVLVLQGL TFTLRPGEVT ALVGPNGSGK STVAALLQNL YQPTGG QLL LDGKPLPQYE HRYLHRQVAA VGQEPQVFGR SLQENIAYGL TQKPTMEEIT AAAVKSGAHS FISGLPQGYD TEVDEAG SQ LSGGQRQAVA LARALIRKPC VLILDDATSA LDANSQLQVE QLLYESPERY SRSVLLITQH LSLVEQADHI LFLEGGAI R EGGTHQQLME KKGCYWAMVQ APADAPE

UniProtKB: Antigen peptide transporter 1

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Macromolecule #2: Tapasin

MacromoleculeName: Tapasin / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Burkitt lymphoma
Molecular weightTheoretical: 47.673539 KDa
SequenceString: MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL DPELYLSVHD PAGALQAAFR RYPRGAPAP HCEMSRFVPL PASAKWASGL TPAQNCPRAL DGAWLMVSIS SPVLSLSSLL RPQPEPQQEP VLITMATVVL T VLTHTPAP ...String:
MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL DPELYLSVHD PAGALQAAFR RYPRGAPAP HCEMSRFVPL PASAKWASGL TPAQNCPRAL DGAWLMVSIS SPVLSLSSLL RPQPEPQQEP VLITMATVVL T VLTHTPAP RVRLGQDALL DLSFAYMPPT SEAASSLAPG PPPFGLEWRR QHLGKGHLLL AATPGLNGQM PAAQEGAVAF AA WDDDEPW GPWTGNGTFW LPRVQPFQEG TYLATIHLPY LQGQVTLELA VYKPPKVSLM PATLARAAPG EAPPELLCLV SHF YPSGGL EVEWELRGGP GGRSQKAEGQ RWLSALRHHS DGSVSLSGHL QPPPVTTEQH GARYACRIHH PSLPASGRSA EVTL EVAGL SGPSLEDSVG LFLSAFLLLG LFKALGWAAV YLSTCKDSKK KAE

UniProtKB: Tapasin

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Macromolecule #3: MHC class I antigen

MacromoleculeName: MHC class I antigen / type: protein_or_peptide / ID: 3 / Details: HLA-B*15:10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Burkitt lymphoma
Molecular weightTheoretical: 40.480973 KDa
SequenceString: MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQ IYKAQAQTDR ESLRNLRGYY NQSEAGSHTL QSMYGCDVGP DGRLLRGHDQ YAYDGKDYIA LNEDLRSWTA A DTAAQITQ ...String:
MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQ IYKAQAQTDR ESLRNLRGYY NQSEAGSHTL QSMYGCDVGP DGRLLRGHDQ YAYDGKDYIA LNEDLRSWTA A DTAAQITQ RKWEAAREAE QRRAYLEGEC VEWLRRYLEN GKDKLERADP PKTHVTHHPI SDHEATLRCW ALGFYPAEIT LT WQRDGED QTQDTELVET RPAGDRTFQK WAAVVVPSGE EQRYTCHVQH EGLPKPLTLR WEPSSQSTVP IVGIVAGLAV LAV VVIGAV VAAVMCRKKS SGGKGGSYSQ AACSDSAQGS DVSLTA

UniProtKB: MHC class I antigen

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Macromolecule #4: Beta-2-microglobulin

MacromoleculeName: Beta-2-microglobulin / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Burkitt lymphoma
Molecular weightTheoretical: 13.732547 KDa
SequenceString:
MSRSVALAVL ALLSLSGLEA IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL KNGERIEKVE HSDLSFSKDW SFYLLYYTE FTPTEKDEYA CRVNHVTLSQ PKIVKWDRDM

UniProtKB: Beta-2-microglobulin

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Macromolecule #5: Antigen peptide transporter 2

MacromoleculeName: Antigen peptide transporter 2 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: ABC-type antigen peptide transporter
Source (natural)Organism: Homo sapiens (human) / Tissue: Burkitt lymphoma
Molecular weightTheoretical: 74.697242 KDa
SequenceString: RPWTSLLLVD AALLWLLQGP LGTLLPQGLP GLWLEGTLRL GGLWGLLKLR GLLGFVGTLL LPLCLATPLT VSLRALVAGA SRAPPARVA SAPWSWLLVG YGAAGLSWSL WAVLSPPGAQ EKEQDQVNNK VLMWRLLKLS RPDLPLLVAA FFFLVLAVLG E TLIPHYSG ...String:
RPWTSLLLVD AALLWLLQGP LGTLLPQGLP GLWLEGTLRL GGLWGLLKLR GLLGFVGTLL LPLCLATPLT VSLRALVAGA SRAPPARVA SAPWSWLLVG YGAAGLSWSL WAVLSPPGAQ EKEQDQVNNK VLMWRLLKLS RPDLPLLVAA FFFLVLAVLG E TLIPHYSG RVIDILGGDF DPHAFASAIF FMCLFSFGSS LSAGCRGGCF TYTMSRINLR IREQLFSSLL RQDLGFFQET KT GELNSRL SSDTTLMSNW LPLNANVLLR SLVKVVGLYG FMLSISPRLT LLSLLHMPFT IAAEKVYNTR HQEVLREIQD AVA RAGQVV REAVGGLQTV RSFGAEEHEV CRYKEALEQC RQLYWRRDLE RALYLLVRRV LHLGVQMLML SCGLQQMQDG ELTQ GSLLS FMIYQESVGS YVQTLVYIYG DMLSNVGAAE KVFSYMDRQP NLPSPGTLAP TTLQGVVKFQ DVSFAYPNRP DRPVL KGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RNNIAY GLQ SCEDDKVMAA AQAAHADDFI QEMEHGIYTD VGEKGSQLAA GQKQRLAIAR ALVRDPRVLI LDEATSALDV QCEQALQ DW NSRGDRTVLV IAHRLQTVQR AHQILVLQEG KLQKL

UniProtKB: Antigen peptide transporter 2

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Macromolecule #6: Unique short US6 glycoprotein

MacromoleculeName: Unique short US6 glycoprotein / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.671127 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MDLLIRLGFL LMCALPTPGE RSSRDPKTLL SLSPRQQACV PRTKSHRPVC YNDTGDCTDA DDSWKQLGED FAHQCLQAAK KRPKTHKSR PNDRNLEGRL TCQRVRRLLP CDLDIHPSHR LLTLMNNCVC DGAVWNAFRL IERHGFFAVT LYLCCGITLL V VILALLCS ITYESTGRGI RRCGS

UniProtKB: Unique short US6 glycoprotein

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Macromolecule #8: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #9: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 9 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #10: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 10 / Number of copies: 2 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #12: water

MacromoleculeName: water / type: ligand / ID: 12 / Number of copies: 4 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration3.5 mg/mL
BufferpH: 6.5
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4S-NaOHHEPES-sodium hydroxide
150.0 mMNaClsodium chloride
10.0 mMMgCl2magnesium chloride
0.05 %C56H92O25glycodiosgenin
2.5 mMC10H16N2O3Sbiotin

Details: 20 mM HEPES-NaOH pH 6.5, 150 mM NaCl, 10 mM MgCl2, 2.5 mM biotin, 0.05% (w/v) glycodiosgenin
GridModel: UltrAuFoil / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: Blot force 5, Blot time 5 s.

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 3 / Number real images: 25454 / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 60241 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 726723
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.7 Å / Resolution method: OTHER
Details: Composite map generated from 4 focus maps ranging 2.59 - 2.88 A
Number images used: 269213
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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