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- EMDB-76179: Structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation -

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Basic information

Entry
Database: EMDB / ID: EMD-76179
TitleStructure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation
Map dataThe map of AlphaIIbbeta3-R21C11 Fab complex in nearly-bent conformation
Sample
  • Complex: The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation
    • Complex: Integrin AlphaIIbbeta3
      • Protein or peptide: Integrin alpha-IIb
      • Protein or peptide: Integrin beta-3
    • Complex: R21C11 Fab
      • Protein or peptide: R21C11 Fab heavy chain
      • Protein or peptide: R21C11 Fab light chain
  • Ligand: CALCIUM ION
  • Ligand: MAGNESIUM ION
KeywordsMonoclonal antibody / integrin receptor / platelets / inhibiter of PDI binding to AlphaIIbbeta3 integrin / BLOOD CLOTTING
Function / homology
Function and homology information


regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / tube development / alpha9-beta1 integrin-ADAM8 complex / response to platelet-derived growth factor / integrin alphaIIb-beta3 complex / regulation of postsynaptic neurotransmitter receptor diffusion trapping / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-vitronectin complex / platelet alpha granule membrane ...regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / tube development / alpha9-beta1 integrin-ADAM8 complex / response to platelet-derived growth factor / integrin alphaIIb-beta3 complex / regulation of postsynaptic neurotransmitter receptor diffusion trapping / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-vitronectin complex / platelet alpha granule membrane / integrin alphav-beta3 complex / negative regulation of lipoprotein metabolic process / positive regulation of glomerular mesangial cell proliferation / smooth muscle cell migration / alphav-beta3 integrin-PKCalpha complex / fibrinogen binding / positive regulation of leukocyte migration / alphav-beta3 integrin-HMGB1 complex / negative regulation of lipid transport / vascular endothelial growth factor receptor 2 binding / angiogenesis involved in wound healing / positive regulation of vascular endothelial growth factor signaling pathway / regulation of release of sequestered calcium ion into cytosol / Elastic fibre formation / mesodermal cell differentiation / positive regulation of bone resorption / alphav-beta3 integrin-IGF-1-IGF1R complex / platelet-derived growth factor receptor binding / cell-cell adhesion mediated by integrin / filopodium membrane / glycinergic synapse / extracellular matrix binding / positive regulation of fibroblast migration / positive regulation of cell adhesion mediated by integrin / positive regulation of vascular endothelial growth factor receptor signaling pathway / apolipoprotein A-I-mediated signaling pathway / regulation of bone resorption / negative regulation of low-density lipoprotein particle clearance / apoptotic cell clearance / wound healing, spreading of epidermal cells / positive regulation of smooth muscle cell migration / integrin complex / Molecules associated with elastic fibres / heterotypic cell-cell adhesion / cell adhesion mediated by integrin / negative chemotaxis / positive regulation of osteoblast proliferation / Mechanical load activates signaling by PIEZO1 and integrins in osteocytes / cellular response to insulin-like growth factor stimulus / Syndecan interactions / p130Cas linkage to MAPK signaling for integrins / regulation of postsynaptic neurotransmitter receptor internalization / cell-substrate adhesion / protein disulfide isomerase activity / microvillus membrane / PECAM1 interactions / GRB2:SOS provides linkage to MAPK signaling for Integrins / negative regulation of endothelial cell apoptotic process / TGF-beta receptor signaling activates SMADs / fibronectin binding / lamellipodium membrane / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / Integrin cell surface interactions / ECM proteoglycans / substrate adhesion-dependent cell spreading / positive regulation of T cell migration / cell-matrix adhesion / embryo implantation / coreceptor activity / Integrin signaling / positive regulation of endothelial cell proliferation / positive regulation of smooth muscle cell proliferation / positive regulation of endothelial cell migration / cell adhesion molecule binding / integrin-mediated signaling pathway / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / response to activity / protein kinase C binding / wound healing / Signal transduction by L1 / cellular response to xenobiotic stimulus / regulation of actin cytoskeleton organization / cell-cell adhesion / cellular response to mechanical stimulus / platelet activation / Signaling by high-kinase activity BRAF mutants / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / MAP2K and MAPK activation / platelet aggregation / VEGFA-VEGFR2 Pathway / integrin binding / ruffle membrane / blood coagulation / positive regulation of angiogenesis / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / cell-cell junction
Similarity search - Function
Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / : / Integrin beta tail domain / Integrin beta cytoplasmic domain / Integrin alpha Ig-like domain 3 / Integrin_b_cyt / : / Integrin EGF domain ...Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / Integrin beta subunit, cytoplasmic domain / : / Integrin beta tail domain / Integrin beta cytoplasmic domain / Integrin alpha Ig-like domain 3 / Integrin_b_cyt / : / Integrin EGF domain / EGF-like domain, extracellular / EGF-like domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin alpha cytoplasmic region / : / Integrins beta chain EGF (I-EGF) domain profile. / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain EGF (I-EGF) domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / Integrins alpha chain signature. / Integrin alpha chain / Integrin alpha beta-propellor / : / Integrin alpha Ig-like domain 2 / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin domain superfamily / Integrin alpha, N-terminal / PSI domain / domain found in Plexins, Semaphorins and Integrins / EGF-like domain signature 1. / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2.
Similarity search - Domain/homology
Integrin beta-3 / Integrin alpha-IIb
Similarity search - Component
Biological speciesHomo sapiens (human) / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsWang JL / Coller B / Wang L / Li JH
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)5R01HL019278-48 United States
CitationJournal: Blood Adv / Year: 2026
Title: A monoclonal antibody to platelet αIIbβ3 that inhibits protein disulfide isomerase binding and platelet aggregation.
Authors: Lu Wang / Jialing Wang / Jihong Li / Barry S Coller /
Abstract: Platelet integrin αIIbβ3 plays a pivotal role in hemostasis and thrombosis. Protein disulfide isomerase (PDI) binds to αIIbβ3 and mediates its activation. The binding region(s) on αIIbβ3 for ...Platelet integrin αIIbβ3 plays a pivotal role in hemostasis and thrombosis. Protein disulfide isomerase (PDI) binds to αIIbβ3 and mediates its activation. The binding region(s) on αIIbβ3 for PDI remains to be established. We identified a new anti-αIIbβ3 murine monoclonal antibody, R21C11, that inhibits PDI binding to platelets, ligand binding to αIIbβ3, and platelet aggregation. R21C11 inhibited recombinant PDI binding to platelets activated with the PAR1 thrombin receptor activating peptide SFLLRN (T6). Reciprocally, PDI partially reduced R21C11 binding to platelets. PDI was translocated to the platelet surface after activation and activated platelets showed higher PDI reductase activity. R211C11 decreased both the amount of PDI and the reductase activity. R21C11 partially inhibited both fibrinogen and PAC-1 binding to αIIbβ3 and platelet aggregation induced by ADP and T6. R21C11 bound slowly to unactivated platelets and more rapidly after T6 activation; eptifibatide, which induces the αIIbβ3 extended-open conformation, also increased the speed of R21C11 binding. Activation also increased total R21C11 binding. Cryogenic electron microscopy single-particle analysis of the R21C11 Fab-αIIbβ3 complex revealed that R21C11 binds to the β3 β-tail domain in both nearly bent and semiextended-closed conformations of αIIbβ3. R21C11 Fab clashed with the β3 β-I domain in the fully bent conformation, accounting for the slow binding rate of R21C11. These data are consistent with R21C11 inhibiting PDI binding by steric hindrance and the activation dependence of PDI binding. Taken together, these data suggest that the β-tail domain and/or neighboring area is the binding site for PDI on integrin αIIbβ3.
History
DepositionMar 17, 2026-
Header (metadata) releaseSep 9, 2026-
Map releaseSep 9, 2026-
UpdateSep 9, 2026-
Current statusSep 9, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_76179.png

Downloads & links

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Map

FileDownload / File: emd_76179.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe map of AlphaIIbbeta3-R21C11 Fab complex in nearly-bent conformation
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 400 pix.
= 344. Å		0.86 Å/pix.
x 400 pix.
= 344. Å		0.86 Å/pix.
x 400 pix.
= 344. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.25
Minimum - Maximum-1.9211195 - 3.081627
Average (Standard dev.)0.0003942717 (±0.04838097)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 344.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half A map of AlphaIIbbeta3-R21C11 Fab complex in...

Fileemd_76179_half_map_1.map
AnnotationHalf A map of AlphaIIbbeta3-R21C11 Fab complex in nearly-bent conformation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half B map of AlphaIIbbeta3-R21C11 Fab complex in...

Fileemd_76179_half_map_2.map
AnnotationHalf B map of AlphaIIbbeta3-R21C11 Fab complex in nearly-bent conformation
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent confor...

EntireName: The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation
Components
  • Complex: The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation
    • Complex: Integrin AlphaIIbbeta3
      • Protein or peptide: Integrin alpha-IIb
      • Protein or peptide: Integrin beta-3
    • Complex: R21C11 Fab
      • Protein or peptide: R21C11 Fab heavy chain
      • Protein or peptide: R21C11 Fab light chain
  • Ligand: CALCIUM ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent confor...

SupramoleculeName: The structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50 KDa

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Supramolecule #2: Integrin AlphaIIbbeta3

SupramoleculeName: Integrin AlphaIIbbeta3 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: R21C11 Fab

SupramoleculeName: R21C11 Fab / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3-#4
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Integrin alpha-IIb

MacromoleculeName: Integrin alpha-IIb / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 113.477523 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPW RAEGGQCPSL LFDLRDETRN VGSQTLQTFK ARQGLGASVV SWSDVIVACA PWQHWNVLEK TEEAEKTPVG S CFLAQPES ...String:
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPW RAEGGQCPSL LFDLRDETRN VGSQTLQTFK ARQGLGASVV SWSDVIVACA PWQHWNVLEK TEEAEKTPVG S CFLAQPES GRRAEYSPCR GNTLSRIYVE NDFSWDKRYC EAGFSSVVTQ AGELVLGAPG GYYFLGLLAQ APVADIFSSY RP GILLWHV SSQSLSFDSS NPEYFDGYWG YSVAVGEFDG DLNTTEYVVG APTWSWTLGA VEILDSYYQR LHRLRGEQMA SYF GHSVAV TDVNGDGRHD LLVGAPLYME SRADRKLAEV GRVYLFLQPR GPHALGAPSL LLTGTQLYGR FGSAIAPLGD LDRD GYNDI AVAAPYGGPS GRGQVLVFLG QSEGLRSRPS QVLDSPFPTG SAFGFSLRGA VDIDDNGYPD LIVGAYGANQ VAVYR AQPV VKASVQLLVQ DSLNPAVKSC VLPQTKTPVS CFNIQMCVGA TGHNIPQKLS LNAELQLDRQ KPRQGRRVLL LGSQQA GTT LNLDLGGKHS PICHTTMAFL RDEADFRDKL SPIVLSLNVS LPPTEAGMAP AVVLHGDTHV QEQTRIVLDC GEDDVCV PQ LQLTASVTGS PLLVGADNVL ELQMDAANEG EGAYEAELAV HLPQGAHYMR ALSNVEGFER LICNQKKENE TRVVLCEL G NPMKKNAQIG IAMLVSVGNL EEAGESVSFQ LQIRSKNSQN PNSKIVLLDV PVRAEAQVEL RGNSFPASLV VAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDR RQIFLPEPEQ PSRLQDPVLV SCDSAPCTVV QCDLQEMARG QRAMVTVLAF LWLPSLYQRP LDQFVLQSHA W FNVSSLPY AVPPLSLPRG EAQVWTQLLR ALEERAIPIW WVLVGVLGGL LLLTILVLAM WKVGFFKRNR PPLEEDDEEG E

UniProtKB: Integrin alpha-IIb

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Macromolecule #2: Integrin beta-3

MacromoleculeName: Integrin beta-3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 87.150773 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG SPRCDLKENL LKDNCAPESI EFPVSEARV LEDRPLSDKG SGDSSQVTQV SPQRIALRLR PDDSKNFSIQ VRQVEDYPVD IYYLMDLSYS MKDDLWSIQN L GTKLATQM ...String:
MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG SPRCDLKENL LKDNCAPESI EFPVSEARV LEDRPLSDKG SGDSSQVTQV SPQRIALRLR PDDSKNFSIQ VRQVEDYPVD IYYLMDLSYS MKDDLWSIQN L GTKLATQM RKLTSNLRIG FGAFVDKPVS PYMYISPPEA LENPCYDMKT TCLPMFGYKH VLTLTDQVTR FNEEVKKQSV SR NRDAPEG GFDAIMQATV CDEKIGWRND ASHLLVFTTD AKTHIALDGR LAGIVQPNDG QCHVGSDNHY SASTTMDYPS LGL MTEKLS QKNINLIFAV TENVVNLYQN YSELIPGTTV GVLSMDSSNV LQLIVDAYGK IRSKVELEVR DLPEELSLSF NATC LNNEV IPGLKSCMGL KIGDTVSFSI EAKVRGCPQE KEKSFTIKPV GFKDSLIVQV TFDCDCACQA QAEPNSHRCN NGNGT FECG VCRCGPGWLG SQCECSEEDY RPSQQDECSP REGQPVCSQR GECLCGQCVC HSSDFGKITG KYCECDDFSC VRYKGE MCS GHGQCSCGDC LCDSDWTGYY CNCTTRTDTC MSSNGLLCSG RGKCECGSCV CIQPGSYGDT CEKCPTCPDA CTFKKEC VE CKKFDRGALH DENTCNRYCR DEIESVKELK DTGKDAVNCT YKNEDDCVVR FQYYEDSSGK SILYVVEEPE CPKGPDIL V VLLSVMGAIL LIGLAALLIW KLLITIHDRK EFAKFEEERA RAKWDTANNP LYKEATSTFT NITYRGT

UniProtKB: Integrin beta-3

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Macromolecule #3: R21C11 Fab heavy chain

MacromoleculeName: R21C11 Fab heavy chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 23.931814 KDa
Recombinant expressionOrganism: Mus musculus (house mouse)
SequenceString: EVQLQESGAE LAKPGASVKM SCKASGYTFI SYWMHWVKQR PGQGLEWIGY INPTTGYSEY NQKFKDKTTL TADKSSSTAY MQLISLTSE DSAVYYCSRS YGSSSWFVYW GQGTLVTVSA AKTTPPSVYP LAPGSAAQTN SMVTLGCLVK GYFPEPVTVT W NSGSLSSG ...String:
EVQLQESGAE LAKPGASVKM SCKASGYTFI SYWMHWVKQR PGQGLEWIGY INPTTGYSEY NQKFKDKTTL TADKSSSTAY MQLISLTSE DSAVYYCSRS YGSSSWFVYW GQGTLVTVSA AKTTPPSVYP LAPGSAAQTN SMVTLGCLVK GYFPEPVTVT W NSGSLSSG VHTFPAVLQS DLYTLSSSVT VPSSTWPSET VTCNVAHPAS STKVDKKIVP RDC

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Macromolecule #4: R21C11 Fab light chain

MacromoleculeName: R21C11 Fab light chain / type: protein_or_peptide / ID: 4
Details: LLTQSPATLSVTPGETVSLSCRASQSIYKNLHWYQQKSHRSPSLLIKSASESISGIPSRFTGSGSGTDYILSINSVEPEDEGIYYCLQGYSIPFTFGAGSKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDLNVKWKLDGSERQNGVLDSWTDQDSKDSTYMSSTLTLTKDEYERHNSYTCEATHKTSTSPLVKSFNRNEC
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 23.218652 KDa
Recombinant expressionOrganism: Mus musculus (house mouse)
SequenceString: LLTQSPATLS VTPGETVSLS CRASQSIYKN LHWYQQKSHR SPSLLIKSAS ESISGIPSRF TGSGSGTDYI LSINSVEPED EGIYYCLQG YSIPFTFGAG SKLELKRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP KDLNVKWKLD GSERQNGVLD S WTDQDSKD ...String:
LLTQSPATLS VTPGETVSLS CRASQSIYKN LHWYQQKSHR SPSLLIKSAS ESISGIPSRF TGSGSGTDYI LSINSVEPED EGIYYCLQG YSIPFTFGAG SKLELKRADA APTVSIFPPS SEQLTSGGAS VVCFLNNFYP KDLNVKWKLD GSERQNGVLD S WTDQDSKD STYMSSTLTL TKDEYERHNS YTCEATHKTS TSPLVKSFNR NEC

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Macromolecule #5: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 5 / Number of copies: 7 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #6: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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

Concentration0.05 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK I

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 54.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 81000
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: 1332000
CTF correctionSoftware - Name: cryoSPARC (ver. v4.4.0) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Details: generate initial model based on selected averages of particles after 2D-classification in CryoSPARC.
Final reconstructionNumber classes used: 1 / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v4.4.0) / Number images used: 49648
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. v4.4.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. v4.4.0)
Final 3D classificationNumber classes: 4 / Avg.num./class: 183000 / Software - Name: cryoSPARC (ver. v4.4.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

8t2v

chain_id: A, source_name: PDB, initial_model_type: experimental model

8t2v

chain_id: B, source_name: PDB, initial_model_type: experimental model

7la4

chain_id: H, source_name: PDB, initial_model_type: experimental model

7la4

chain_id: L, source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-11yb:
Structure of AlphaIIbBeta3-R21C11 Fab in the near-bent conformation

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