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- PDB-3ifp: X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) ... -

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Open data


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Basic information

Entry
Database: PDB / ID: 3ifp
TitleX-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex
Components
  • 12B4 FAB antibody heavy chain
  • 12B4 FAB antibody light chain
  • Amyloid beta A4 protein
KeywordsIMMUNE SYSTEM / antibody / amyloid beta peptide
Function / homology
Function and homology information


regulation of epidermal growth factor-activated receptor activity / cytosolic mRNA polyadenylation / collateral sprouting in absence of injury / microglia development / regulation of synapse structure or activity / regulation of Wnt signaling pathway / Formyl peptide receptors bind formyl peptides and many other ligands / axo-dendritic transport / synaptic assembly at neuromuscular junction / signaling receptor activator activity ...regulation of epidermal growth factor-activated receptor activity / cytosolic mRNA polyadenylation / collateral sprouting in absence of injury / microglia development / regulation of synapse structure or activity / regulation of Wnt signaling pathway / Formyl peptide receptors bind formyl peptides and many other ligands / axo-dendritic transport / synaptic assembly at neuromuscular junction / signaling receptor activator activity / smooth endoplasmic reticulum calcium ion homeostasis / axon midline choice point recognition / astrocyte activation involved in immune response / regulation of spontaneous synaptic transmission / mating behavior / NMDA selective glutamate receptor signaling pathway / ciliary rootlet / Lysosome Vesicle Biogenesis / PTB domain binding / Golgi-associated vesicle / positive regulation of amyloid fibril formation / neuron remodeling / : / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / suckling behavior / nuclear envelope lumen / dendrite development / COPII-coated ER to Golgi transport vesicle / presynaptic active zone / modulation of excitatory postsynaptic potential / TRAF6 mediated NF-kB activation / Advanced glycosylation endproduct receptor signaling / neuromuscular process controlling balance / The NLRP3 inflammasome / regulation of presynapse assembly / transition metal ion binding / negative regulation of long-term synaptic potentiation / regulation of multicellular organism growth / intracellular copper ion homeostasis / negative regulation of neuron differentiation / ECM proteoglycans / smooth endoplasmic reticulum / positive regulation of T cell migration / spindle midzone / Purinergic signaling in leishmaniasis infection / positive regulation of calcium-mediated signaling / protein serine/threonine kinase binding / positive regulation of chemokine production / clathrin-coated pit / regulation of peptidyl-tyrosine phosphorylation / forebrain development / Notch signaling pathway / Mitochondrial protein degradation / neuron projection maintenance / positive regulation of G2/M transition of mitotic cell cycle / positive regulation of protein metabolic process / ionotropic glutamate receptor signaling pathway / positive regulation of glycolytic process / cholesterol metabolic process / positive regulation of mitotic cell cycle / response to interleukin-1 / adult locomotory behavior / extracellular matrix organization / axonogenesis / platelet alpha granule lumen / trans-Golgi network membrane / positive regulation of peptidyl-threonine phosphorylation / dendritic shaft / learning / positive regulation of interleukin-1 beta production / positive regulation of long-term synaptic potentiation / locomotory behavior / central nervous system development / endosome lumen / astrocyte activation / positive regulation of JNK cascade / Post-translational protein phosphorylation / synapse organization / regulation of long-term neuronal synaptic plasticity / microglial cell activation / TAK1-dependent IKK and NF-kappa-B activation / visual learning / serine-type endopeptidase inhibitor activity / neuromuscular junction / recycling endosome / cognition / neuron cellular homeostasis / Golgi lumen / positive regulation of inflammatory response / positive regulation of non-canonical NF-kappaB signal transduction / endocytosis / cellular response to amyloid-beta / G2/M transition of mitotic cell cycle / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / neuron projection development / cell-cell junction / synaptic vesicle
Similarity search - Function
Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. / Amyloidogenic glycoprotein, amyloid-beta peptide superfamily / Beta-amyloid peptide (beta-APP) / Amyloidogenic glycoprotein, amyloid-beta peptide / Beta-amyloid precursor protein C-terminal / Amyloidogenic glycoprotein, intracellular domain, conserved site ...Amyloidogenic glycoprotein, copper-binding / Amyloidogenic glycoprotein, copper-binding domain conserved site / Amyloidogenic glycoprotein, copper-binding domain superfamily / Copper-binding of amyloid precursor, CuBD / Amyloid precursor protein (APP) copper-binding (CuBD) domain signature. / Amyloidogenic glycoprotein, amyloid-beta peptide superfamily / Beta-amyloid peptide (beta-APP) / Amyloidogenic glycoprotein, amyloid-beta peptide / Beta-amyloid precursor protein C-terminal / Amyloidogenic glycoprotein, intracellular domain, conserved site / Beta-amyloid precursor protein C-terminus / Amyloid precursor protein (APP) intracellular domain signature. / Amyloid precursor protein (APP) E1 domain profile. / Amyloid precursor protein (APP) E2 domain profile. / Amyloidogenic glycoprotein, extracellular / Amyloidogenic glycoprotein, heparin-binding / Amyloidogenic glycoprotein, E2 domain / E2 domain superfamily / Amyloidogenic glycoprotein, heparin-binding domain superfamily / Amyloid A4 N-terminal heparin-binding / E2 domain of amyloid precursor protein / amyloid A4 / Amyloidogenic glycoprotein / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / PH-like domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Amyloid-beta precursor protein
Similarity search - Component
Biological speciesMus musculus (house mouse)
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å
AuthorsWeis, W.I. / Feinberg, H. / Basi, G.S. / Schenk, D.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Structural correlates of antibodies associated with acute reversal of amyloid beta-related behavioral deficits in a mouse model of Alzheimer disease.
Authors: Basi, G.S. / Feinberg, H. / Oshidari, F. / Anderson, J. / Barbour, R. / Baker, J. / Comery, T.A. / Diep, L. / Gill, D. / Johnson-Wood, K. / Goel, A. / Grantcharova, K. / Lee, M. / Li, J. / ...Authors: Basi, G.S. / Feinberg, H. / Oshidari, F. / Anderson, J. / Barbour, R. / Baker, J. / Comery, T.A. / Diep, L. / Gill, D. / Johnson-Wood, K. / Goel, A. / Grantcharova, K. / Lee, M. / Li, J. / Partridge, A. / Griswold-Prenner, I. / Piot, N. / Walker, D. / Widom, A. / Pangalos, M.N. / Seubert, P. / Jacobsen, J.S. / Schenk, D. / Weis, W.I.
History
DepositionJul 24, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 17, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jun 19, 2013Group: Database references
Revision 1.3Sep 25, 2013Group: Derived calculations

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
H: 12B4 FAB antibody heavy chain
L: 12B4 FAB antibody light chain
P: Amyloid beta A4 protein
A: 12B4 FAB antibody heavy chain
B: 12B4 FAB antibody light chain
Q: Amyloid beta A4 protein
C: 12B4 FAB antibody heavy chain
D: 12B4 FAB antibody light chain
R: Amyloid beta A4 protein
E: 12B4 FAB antibody heavy chain
F: 12B4 FAB antibody light chain
S: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)198,62112
Polymers198,62112
Non-polymers00
Water00
1
H: 12B4 FAB antibody heavy chain
L: 12B4 FAB antibody light chain
P: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)49,6553
Polymers49,6553
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-26 kcal/mol
Surface area19940 Å2
MethodPISA
2
A: 12B4 FAB antibody heavy chain
B: 12B4 FAB antibody light chain
Q: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)49,6553
Polymers49,6553
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4650 Å2
ΔGint-27 kcal/mol
Surface area19530 Å2
MethodPISA
3
C: 12B4 FAB antibody heavy chain
D: 12B4 FAB antibody light chain
R: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)49,6553
Polymers49,6553
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4640 Å2
ΔGint-24 kcal/mol
Surface area19640 Å2
MethodPISA
4
E: 12B4 FAB antibody heavy chain
F: 12B4 FAB antibody light chain
S: Amyloid beta A4 protein


Theoretical massNumber of molelcules
Total (without water)49,6553
Polymers49,6553
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4570 Å2
ΔGint-24 kcal/mol
Surface area19590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.86, 79.24, 94.10
Angle α, β, γ (deg.)68.66, 65.28, 78.47
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11H
21L
31P
41A
51B
61Q
71C
81D
91R
101E
111F
121S
12H
22L
32A
42B
52C
62D
72E
82F

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain H and resid 1-123) or (chain L and resid 1-112) or (chain P and resid 1-7)H1 - 123
211(chain H and resid 1-123) or (chain L and resid 1-112) or (chain P and resid 1-7)L1 - 123
311(chain H and resid 1-123) or (chain L and resid 1-112) or (chain P and resid 1-7)P1 - 123
411(chain A and resid 1-123) or (chain B and resid 1-112) or (chain Q and resid 1-7)A1 - 123
511(chain A and resid 1-123) or (chain B and resid 1-112) or (chain Q and resid 1-7)B1 - 123
611(chain A and resid 1-123) or (chain B and resid 1-112) or (chain Q and resid 1-7)Q1 - 123
711(chain C and resid 1-123) or (chain D and resid 1-112) or (chain R and resid 1-7)C1 - 123
811(chain C and resid 1-123) or (chain D and resid 1-112) or (chain R and resid 1-7)D1 - 123
911(chain C and resid 1-123) or (chain D and resid 1-112) or (chain R and resid 1-7)R1 - 123
1011(chain E and resid 1-123) or (chain F and resid 1-112) or (chain S and resid 1-7)E1 - 123
1111(chain E and resid 1-123) or (chain F and resid 1-112) or (chain S and resid 1-7)F1 - 123
1211(chain E and resid 1-123) or (chain F and resid 1-112) or (chain S and resid 1-7)S1 - 123
112(chain H and resid 124-225) or (chain L and resid 113-219)H124 - 225
212(chain H and resid 124-225) or (chain L and resid 113-219)L124 - 225
312(chain A and resid 124-225) or (chain B and resid 113-219)A124 - 225
412(chain A and resid 124-225) or (chain B and resid 113-219)B124 - 225
512(chain C and resid 124-225) or (chain D and resid 113-219)C124 - 225
612(chain C and resid 124-225) or (chain D and resid 113-219)D124 - 225
712(chain E and resid 124-225) or (chain F and resid 113-219)E124 - 225
812(chain E and resid 124-225) or (chain F and resid 113-219)F124 - 225

NCS ensembles :
ID
1
2

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Components

#1: Antibody
12B4 FAB antibody heavy chain


Mass: 24590.529 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: CET1018 / Cell line (production host): CHO CELLS / Production host: Cricetulus griseus (Chinese hamster) / Tissue (production host): OVARY
#2: Antibody
12B4 FAB antibody light chain


Mass: 24173.838 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: CET1018 / Cell line (production host): CHO CELLS / Production host: Cricetulus griseus (Chinese hamster) / Tissue (production host): OVARY
#3: Protein/peptide
Amyloid beta A4 protein


Mass: 890.897 Da / Num. of mol.: 4 / Fragment: residues 672-678 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P05067

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.5 Å3/Da / Density % sol: 50.82 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7
Details: Protein: 4.1 mg/ml, 10 mM Hepes pH 7.5, 75 mM NaCl. Protein:peptide molar ratio: 1:1.8. Reservoir: 30%PEG8K, 0.1M Hepes pH 7.0, 0.2M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.9794 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: May 7, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 2.95→81.13 Å / Num. obs: 38904 / Rmerge(I) obs: 0.129

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Processing

SoftwareName: PHENIX / Version: (phenix.refine) / Classification: refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.95→81.13 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.47 / σ(F): 2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2691 1945 5 %
Rwork0.2348 --
obs0.2365 38903 95.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 0.783 Å2 / ksol: 0.332 e/Å3
Displacement parametersBiso max: 115.3 Å2 / Biso mean: 27.474 Å2 / Biso min: 13.3 Å2
Baniso -1Baniso -2Baniso -3
1--5.951 Å21.164 Å21.254 Å2
2---3.236 Å2-7.574 Å2
3---9.187 Å2
Refinement stepCycle: LAST / Resolution: 2.95→81.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13667 0 0 0 13667
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00914016
X-RAY DIFFRACTIONf_angle_d1.15719069
X-RAY DIFFRACTIONf_chiral_restr0.0712162
X-RAY DIFFRACTIONf_plane_restr0.0052426
X-RAY DIFFRACTIONf_dihedral_angle_d17.6814954
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11H1886X-RAY DIFFRACTIONPOSITIONAL0.035
12L1886X-RAY DIFFRACTIONPOSITIONAL0.035
13P1886X-RAY DIFFRACTIONPOSITIONAL0.035
14A1886X-RAY DIFFRACTIONPOSITIONAL0.035
15B1886X-RAY DIFFRACTIONPOSITIONAL0.035
16Q1886X-RAY DIFFRACTIONPOSITIONAL0.035
17C1886X-RAY DIFFRACTIONPOSITIONAL0.04
18D1886X-RAY DIFFRACTIONPOSITIONAL0.04
19R1886X-RAY DIFFRACTIONPOSITIONAL0.04
110E1877X-RAY DIFFRACTIONPOSITIONAL0.04
111F1877X-RAY DIFFRACTIONPOSITIONAL0.04
112S1877X-RAY DIFFRACTIONPOSITIONAL0.04
21H1523X-RAY DIFFRACTIONPOSITIONAL0.036
22L1523X-RAY DIFFRACTIONPOSITIONAL0.036
23A1523X-RAY DIFFRACTIONPOSITIONAL0.036
24B1523X-RAY DIFFRACTIONPOSITIONAL0.036
25C1523X-RAY DIFFRACTIONPOSITIONAL0.037
26D1523X-RAY DIFFRACTIONPOSITIONAL0.037
27E1523X-RAY DIFFRACTIONPOSITIONAL0.038
28F1523X-RAY DIFFRACTIONPOSITIONAL0.038
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.95-3.02380.40611190.34472633X-RAY DIFFRACTION95
3.0238-3.10550.35211630.32462633X-RAY DIFFRACTION96
3.1055-3.19690.39181360.30122611X-RAY DIFFRACTION96
3.1969-3.30010.3131420.28782671X-RAY DIFFRACTION95
3.3001-3.41810.3431380.27862607X-RAY DIFFRACTION96
3.4181-3.55490.29131450.25842608X-RAY DIFFRACTION96
3.5549-3.71670.28021500.23382654X-RAY DIFFRACTION96
3.7167-3.91270.24321530.21682622X-RAY DIFFRACTION96
3.9127-4.15780.22431200.20852664X-RAY DIFFRACTION96
4.1578-4.47880.23641260.17952674X-RAY DIFFRACTION96
4.4788-4.92950.18221340.16432640X-RAY DIFFRACTION96
4.9295-5.64260.19371330.17032644X-RAY DIFFRACTION96
5.6426-7.10850.21571230.20982662X-RAY DIFFRACTION96
7.1085-81.16060.21291630.20182635X-RAY DIFFRACTION96
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.5359-0.5338-0.16290.54080.03990.36350.0308-0.0569-0.1664-0.0097-0.02880.13110.02530.14140.02270.04820.03130.01330.1876-0.01960.234280.5562-0.18941.0577
20.9878-0.18380.75450.26950.03841.1184-0.1447-0.1468-0.1355-0.0293-0.10270.0295-0.159-0.14720.21140.08320.0258-0.00550.3422-0.12930.240378.908636.082434.2936
3-0.3589-1.0509-0.8995-0.26570.10350.62840.14360.03580.2879-0.02990.27350.3384-0.039-0.1515-0.31310.0282-0.07640.09120.0480.14130.530674.5102-14.299245.291
40.66780.431-0.07470.30750.20141.21750.0874-0.0356-0.0232-0.0299-0.0610.0846-0.18190.2013-0.0360.1193-0.0298-0.02680.1508-0.02560.191120.264262.639774.2736
51.28270.43950.14980.20520.12950.78850.0070.13850.22460.0421-0.04790.08190.1618-0.05760.04920.09420.0176-0.06260.2388-0.07410.1911118.125127.072481.0168
61.20042.57271.6158-4.4509-2.82222.6521-0.04930.04260.02630.73250.3417-1.2401-0.6947-0.0146-0.2690.22180.0452-0.1362-0.0015-0.15030.6293114.394776.830870.1052
71.04050.59010.40760.91270.23570.3660.1883-0.31120.09980.0999-0.36790.12190.1873-0.44630.19970.1158-0.08440.05330.4766-0.18230.221477.422919.323181.9202
80.62550.730.30140.49170.23420.7892-0.18060.2203-0.04260.00670.0892-0.0625-0.13830.10370.07870.11210.0084-0.01390.4883-0.14750.226979.332555.467776.1029
90.90940.74040.69980.26280.04480.0379-0.07030.2571-0.1703-0.040.23790.41370.03940.0112-0.16230.2197-0.22240.09610.3383-0.13160.695883.5714.66182.696
100.5933-0.79360.11390.813-0.26380.46070.034-0.0190.0379-0.0309-0.1040.067-0.0246-0.08330.07650.05520.0137-0.02570.2368-0.08910.1416116.705743.122433.504
11-0.40020.12840.13370.54220.01770.7465-0.14340.1439-0.01770.01780.0641-0.08550.16920.07290.06450.0880.00650.0250.4389-0.13880.2375118.65287.073739.3511
12-0.8034-1.4472-2.6718-0.7523-0.42711.02420.0681-0.7210.6298-0.0107-0.00670.2179-0.09530.4419-0.0628-0.0498-0.1044-0.02550.5949-0.22970.5479123.430356.881632.9131
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain H and resid 1-123) or (chain L and resid 1-112)H1 - 123
2X-RAY DIFFRACTION1(chain H and resid 1-123) or (chain L and resid 1-112)L1 - 112
3X-RAY DIFFRACTION2(chain H and resid 124-225) or (chain L and resid 113-219)H124 - 225
4X-RAY DIFFRACTION2(chain H and resid 124-225) or (chain L and resid 113-219)L113 - 219
5X-RAY DIFFRACTION3chain P and resid 1-7P1 - 7
6X-RAY DIFFRACTION4(chain A and resid 1-123) or (chain B and resid 1-112)A1 - 123
7X-RAY DIFFRACTION4(chain A and resid 1-123) or (chain B and resid 1-112)B1 - 112
8X-RAY DIFFRACTION5(chain A and resid 124-225) or (chain B and resid 113-219)A124 - 225
9X-RAY DIFFRACTION5(chain A and resid 124-225) or (chain B and resid 113-219)B113 - 219
10X-RAY DIFFRACTION6chain Q and resid 1-7Q1 - 7
11X-RAY DIFFRACTION7(chain C and resid 1-123) or (chain D and resid 1-112)C1 - 123
12X-RAY DIFFRACTION7(chain C and resid 1-123) or (chain D and resid 1-112)D1 - 112
13X-RAY DIFFRACTION8(chain C and resid 124-225) or (chain D and resid 113-219)C124 - 225
14X-RAY DIFFRACTION8(chain C and resid 124-225) or (chain D and resid 113-219)D113 - 219
15X-RAY DIFFRACTION9chain R and resid 1-7R1 - 7
16X-RAY DIFFRACTION10(chain E and resid 1-123) or (chain F and resid 1-112)E1 - 123
17X-RAY DIFFRACTION10(chain E and resid 1-123) or (chain F and resid 1-112)F1 - 112
18X-RAY DIFFRACTION11(chain E and resid 124-225) or (chain F and resid 113-219)E124 - 225
19X-RAY DIFFRACTION11(chain E and resid 124-225) or (chain F and resid 113-219)F113 - 219
20X-RAY DIFFRACTION12chain S and resid 1-7S1 - 7

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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

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