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- PDB-6ahy: Wnt signaling complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6ahy
TitleWnt signaling complex
Components
  • Frizzled-8
  • Proto-oncogene Wnt-3
KeywordsSIGNALING PROTEIN / Wnt signaling / Canonical Wnt pathway
Function / homology
Function and homology information


: / Spemann organizer formation at the anterior end of the primitive streak / : / : / positive regulation of collateral sprouting in absence of injury / Wnt-Frizzled-LRP5/6 complex / Regulation of FZD by ubiquitination / Asymmetric localization of PCP proteins / WNT ligand biogenesis and trafficking / canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation ...: / Spemann organizer formation at the anterior end of the primitive streak / : / : / positive regulation of collateral sprouting in absence of injury / Wnt-Frizzled-LRP5/6 complex / Regulation of FZD by ubiquitination / Asymmetric localization of PCP proteins / WNT ligand biogenesis and trafficking / canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation / negative regulation of axon extension involved in axon guidance / non-canonical Wnt signaling pathway / dorsal/ventral axis specification / limb bud formation / Wnt receptor activity / gamete generation / Wnt-protein binding / mammary gland epithelium development / head morphogenesis / frizzled binding / embryonic forelimb morphogenesis / Wnt signalosome / Class B/2 (Secretin family receptors) / embryonic hindlimb morphogenesis / anterior/posterior axis specification / neuronal dense core vesicle / mesoderm formation / regulation of neurogenesis / positive regulation of Wnt signaling pathway / canonical Wnt signaling pathway / cell fate commitment / cellular response to retinoic acid / extracellular matrix / stem cell proliferation / TCF dependent signaling in response to WNT / cytokine activity / PDZ domain binding / G protein-coupled receptor activity / axon guidance / cell morphogenesis / neuron differentiation / Wnt signaling pathway / Golgi lumen / endocytic vesicle membrane / T cell differentiation in thymus / angiogenesis / receptor ligand activity / positive regulation of protein phosphorylation / protein domain specific binding / endoplasmic reticulum lumen / signaling receptor binding / ubiquitin protein ligase binding / positive regulation of gene expression / Golgi apparatus / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Wnt-3 protein / Frizzled 8, cysteine-rich domain / Wnt protein, conserved site / Wnt-1 family signature. / Wnt / Wnt, C-terminal domain / wnt family / found in Wnt-1 / Frizzled cysteine-rich domain / Frizzled cysteine-rich domain ...Wnt-3 protein / Frizzled 8, cysteine-rich domain / Wnt protein, conserved site / Wnt-1 family signature. / Wnt / Wnt, C-terminal domain / wnt family / found in Wnt-1 / Frizzled cysteine-rich domain / Frizzled cysteine-rich domain / Frizzled/Smoothened, transmembrane domain / Frizzled/Smoothened family membrane region / Frizzled/Smoothened family membrane region / Frizzled/secreted frizzled-related protein / Frizzled / Frizzled domain / Frizzled cysteine-rich domain superfamily / Fz domain / Frizzled (fz) domain profile. / GPCR, family 2-like / G-protein coupled receptors family 2 profile 2. / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
PALMITOLEIC ACID / Proto-oncogene Wnt-3 / Frizzled-8
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHirai, H. / Arimori, T. / Matoba, K. / Mihara, E. / Takagi, J.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2019
Title: Crystal structure of a mammalian Wnt-frizzled complex.
Authors: Hirai, H. / Matoba, K. / Mihara, E. / Arimori, T. / Takagi, J.
History
DepositionAug 21, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 1, 2019Provider: repository / Type: Initial release
Revision 1.1May 15, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2May 22, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Frizzled-8
B: Proto-oncogene Wnt-3
C: Frizzled-8
D: Proto-oncogene Wnt-3
E: Frizzled-8
F: Proto-oncogene Wnt-3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,19917
Polymers157,4796
Non-polymers2,72011
Water00
1
A: Frizzled-8
B: Proto-oncogene Wnt-3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6507
Polymers52,4932
Non-polymers1,1575
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Frizzled-8
D: Proto-oncogene Wnt-3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6146
Polymers52,4932
Non-polymers1,1214
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Frizzled-8
F: Proto-oncogene Wnt-3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)52,9354
Polymers52,4932
Non-polymers4422
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)120.073, 141.611, 260.692
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Space group name H-MI212121

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Components

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein Frizzled-8 / mFz8


Mass: 16239.690 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Fzd8 / Production host: Homo sapiens (human) / References: UniProt: Q61091
#2: Protein Proto-oncogene Wnt-3 / Proto-oncogene Int-4 homolog


Mass: 36253.336 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: WNT3, INT4 / Production host: Homo sapiens (human) / References: UniProt: P56703

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Sugars , 2 types, 8 molecules

#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 3 molecules

#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-PAM / PALMITOLEIC ACID


Mass: 254.408 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H30O2

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.84 Å3/Da / Density % sol: 67.94 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.1 M HEPES-NaOH (pH 7.5), 0.1 M LiCl, 20%(v/v) Ethylene glycol, 7%(w/v) PEG 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Dec 19, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 55285 / % possible obs: 99.9 % / Redundancy: 7.5 % / Biso Wilson estimate: 72.94 Å2 / Rsym value: 0.092 / Net I/σ(I): 31.8
Reflection shellResolution: 2.8→2.85 Å / Redundancy: 7.5 % / Mean I/σ(I) obs: 2.1 / Num. unique obs: 2712 / Rsym value: 1.305 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4F0A

4f0a


Resolution: 2.8→44.157 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 26.76
RfactorNum. reflection% reflection
Rfree0.2442 2717 4.95 %
Rwork0.2054 --
obs0.2073 54944 99.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.8→44.157 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9781 0 166 0 9947
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00910252
X-RAY DIFFRACTIONf_angle_d1.19613920
X-RAY DIFFRACTIONf_dihedral_angle_d11.696023
X-RAY DIFFRACTIONf_chiral_restr0.0561458
X-RAY DIFFRACTIONf_plane_restr0.0061810
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.85090.37761270.3052754X-RAY DIFFRACTION100
2.8509-2.90570.31061540.28632695X-RAY DIFFRACTION100
2.9057-2.9650.32221410.27192726X-RAY DIFFRACTION100
2.965-3.02950.32531270.26842731X-RAY DIFFRACTION100
3.0295-3.09990.37871610.27962689X-RAY DIFFRACTION100
3.0999-3.17750.32831470.26292708X-RAY DIFFRACTION100
3.1775-3.26330.28881430.24462738X-RAY DIFFRACTION100
3.2633-3.35930.28041310.22652723X-RAY DIFFRACTION100
3.3593-3.46770.28541520.22942737X-RAY DIFFRACTION100
3.4677-3.59160.27821540.22072713X-RAY DIFFRACTION100
3.5916-3.73530.27051350.20932756X-RAY DIFFRACTION100
3.7353-3.90520.22861570.19662733X-RAY DIFFRACTION100
3.9052-4.1110.19251420.18442740X-RAY DIFFRACTION100
4.111-4.36830.21231280.17422752X-RAY DIFFRACTION100
4.3683-4.70530.22561330.16612794X-RAY DIFFRACTION100
4.7053-5.17810.23371480.17992763X-RAY DIFFRACTION100
5.1781-5.92590.22081520.19072785X-RAY DIFFRACTION100
5.9259-7.46020.24031470.21112809X-RAY DIFFRACTION100
7.4602-44.16210.20131380.1942881X-RAY DIFFRACTION98
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)
13.1773.2723-3.35265.3565-6.46078.08050.8771-2.07461.21552.1957-0.50260.899-1.99271.0895-0.621.5741-0.2640.21760.7558-0.17090.6594-12.25630.8846-52.8208
24.22134.69272.8775.95161.01528.98920.5308-2.21690.02850.5384-0.66270.8376-1.2963-1.04660.17671.0953-0.03660.23430.6612-0.1670.6893-13.880632.1358-58.9498
38.27723.7271-4.24326.0782-2.20132.86610.1678-0.8087-0.20360.6103-0.40050.0974-0.43730.14370.24140.85630.1226-0.03080.4087-0.05630.4403-10.239227.9074-63.9636
46.34527.0745-7.31917.8475-6.53528.14970.1530.39690.4974-0.06220.24650.4032-0.3446-0.3671-0.35071.03310.1958-0.04840.5296-0.1130.6044-8.740825.526-79.7376
58.71244.52730.7396.88284.23753.3274-0.32810.1164-2.3545-0.5621-0.69490.5621.42850.52160.62871.1210.20810.14670.5851-0.09871.2747-4.683120.0772-73.4751
67.9214-4.20261.44042.98431.89582.02530.93020.7092-0.8344-0.7776-0.1830.34441.2463-0.342-0.89351.0207-0.0847-0.05040.6687-0.10870.7249-22.064217.5164-68.3573
74.91282.02831.56546.98141.1925.07090.0618-0.3370.03890.40750.07570.48960.2068-0.4703-0.0870.5867-0.0169-0.16550.38210.02750.43861.4931.7563-33.2862
83.34060.0396-0.40417.4306-4.78577.60680.16340.07480.16360.3067-0.3062-0.41760.15630.42450.14340.6961-0.0489-0.22160.4195-0.04770.469413.32335.1356-41.4962
91.2068-0.8369-0.25953.9687-1.82933.0334-0.01080.0483-0.34670.23490.0834-0.17670.4595-0.1379-0.08950.9319-0.0952-0.32090.4691-0.010.59286.0969-7.0903-43.7661
101.7367-2.07960.70777.5841-4.86392.31430.1672-0.2708-0.5282-0.27690.44841.10640.258-0.6283-0.53210.8992-0.2803-0.11131.0222-0.05960.8513-26.7636-0.2504-47.9383
114.605-5.9039-0.18898.3872.19556.823-0.737-0.6716-0.3781.23210.6351-0.37661.1850.69180.130.54450.1004-0.02220.58440.0150.607427.259530.036713.8529
129.3672-6.49542.58937.6743-4.75293.3752-0.1972-0.8595-0.82860.27660.4410.93410.5922-0.5830.11530.411-0.1140.01010.54170.02560.932621.260429.59459.4249
132.32980.5518-2.57235.99070.09839.69960.0394-0.17590.51840.1548-0.14120.0627-0.36560.1352-0.00080.31970.0751-0.12150.455-0.02760.620127.489641.83928.1226
142.06756.3139-7.07973.5463-4.06174.4958-0.0387-0.5415-0.1104-0.1014-0.254-0.02851.0878-0.42160.32210.71330.0142-0.17010.70030.03710.772919.425430.676520.6445
153.55631.9206-0.70965.5413-1.75754.11580.30720.7131.57831.29360.3094-0.1206-2.0242-1.0142-0.68370.62260.18470.07870.62130.07741.365421.023153.255810.0072
166.77452.897-5.63122.1856-2.52114.6840.79090.29781.9484-0.54190.64110.74820.7638-0.216-1.09490.67450.2657-0.0831.21270.26381.375415.492146.26096.2984
173.6056-0.65-3.6972.390.40763.9435-0.2575-0.3960.57991.6149-0.18722.44520.0427-3.01740.58170.80610.08060.32831.4391-0.01231.144110.459340.663923.3362
184.87814.85511.43534.93780.72959.2835-0.4288-1.5180.80980.1517-1.11371.0412-0.5672-1.50781.38310.52810.01430.03860.84650.08940.966920.267642.032125.1545
196.6815-0.2031-5.23842.47750.67548.9719-0.183-0.8844-0.76930.0651-0.19830.3771.0821-0.06250.40520.6217-0.1524-0.10890.80570.01910.51943.41671.39780.3462
203.36321.2730.38966.45713.34752.6424-0.36310.2635-0.0753-0.73720.25010.27760.0779-0.25480.07730.5266-0.063-0.11330.91020.03410.53897.335212.9533-12.3047
216.1862.92681.55213.01590.80572.23910.0906-0.13370.2371-0.1368-0.23240.87270.4616-0.90590.09410.4961-0.1312-0.09671.0409-0.16250.7075-6.955210.9213-5.4805
225.62294.40620.27155.3244-0.26214.27050.1961-0.4544-0.17990.1513-0.2550.28770.5366-1.12280.01840.56350.04910.11940.96190.06670.6105-0.543112.240227.4018
238.740.16124.43416.26373.75866.70170.3353-1.1678-0.66821.35350.09850.6482.2557-0.8806-0.61271.6783-0.1127-0.0071.4531-0.04270.67558.5729-10.4975-59.2153
241.1945-0.2599-0.9325.7587-3.94264.1811-0.64340.84230.19311.64212.2013-1.3330.85151.2818-1.32960.85580.3042-0.22811.7291-0.62990.840968.6903-4.0339-63.3538
257.4848-2.29892.52847.77282.84517.4269-0.4245-1.9612-0.10210.66480.9741-1.25783.72410.7298-0.84021.87370.5951-0.45521.7256-0.24651.010171.9555-12.3738-58.9987
267.0686-1.05662.10630.7005-1.86565.38640.8919-2.0484-0.71840.83960.01970.05452.3481-0.5843-1.161.6837-0.1534-0.21491.56820.06051.181858.3805-18.5986-51.9645
275.8061-1.825-1.8115.98921.90652.2539-1.0187-1.96231.01821.82761.3785-1.40590.60643.3979-0.431.66690.6429-0.69812.5395-0.56391.758981.0935-8.6085-55.4528
287.6118-2.98292.35624.58562.04853.3121-0.6536-0.0571.20141.84071.8289-1.19551.1661.5655-1.04461.47560.8777-0.82452.933-1.4360.823976.0826-2.145-52.1146
294.9231-0.3554-3.74783.0655-0.10162.8075-0.2372-1.0948-0.964-1.5027-0.3087-0.26360.44381.40571.25772.24660.65-0.28872.00990.00391.189870.5556-17.5806-43.0837
303.2977-3.97431.52156.776-3.2746.41690.00410.51270.466-0.4959-0.1533-0.27570.58730.4661-0.08120.7902-0.0119-0.11760.5334-0.0620.474229.74162.502-39.3727
317.96660.4049-3.4148-0.0798-0.12729.7182-1.00570.0485-0.59710.33290.34590.22151.777-0.12270.80041.0375-0.0063-0.04980.64320.07550.668632.7465-5.9382-24.8573
325.52163.6435-5.89213.9315-2.64817.2823-0.41670.4186-0.1461-0.96170.0509-0.34320.46260.17120.38120.82260.2122-0.06760.7611-0.05420.433845.31797.8443-41.2327
332.50940.602-1.5521.7296-2.52543.2431-0.0582-0.37560.2368-0.27140.11840.28360.27650.0082-0.08160.63360.16-0.12460.8712-0.12680.495635.54459.7402-28.7452
343.2852-0.2627-3.1320.3221.84896.6593-0.0422-0.62290.1337-0.03380.4489-0.16650.46481.402-0.26870.67210.2587-0.08570.9826-0.16570.541749.04136.343-31.9583
352.9613-0.775-0.08981.82670.87243.28290.1861-0.4395-0.26370.0861-0.0244-0.23151.03340.5159-0.1960.85280.1587-0.07590.96790.02680.40136.63722.8524-13.0875
365.52517.0071-2.84598.7964-3.38372.2846-1.6887-0.8553-3.7239-0.06460.8082-1.66531.2169-0.20830.95621.72860.36980.16051.1325-0.17481.198442.8575-21.2676-16.4611
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 33 through 40 )
2X-RAY DIFFRACTION2chain 'A' and (resid 41 through 53 )
3X-RAY DIFFRACTION3chain 'A' and (resid 54 through 107 )
4X-RAY DIFFRACTION4chain 'A' and (resid 108 through 125 )
5X-RAY DIFFRACTION5chain 'A' and (resid 126 through 137 )
6X-RAY DIFFRACTION6chain 'A' and (resid 138 through 152 )
7X-RAY DIFFRACTION7chain 'B' and (resid 43 through 133 )
8X-RAY DIFFRACTION8chain 'B' and (resid 134 through 200 )
9X-RAY DIFFRACTION9chain 'B' and (resid 201 through 292 )
10X-RAY DIFFRACTION10chain 'B' and (resid 293 through 355 )
11X-RAY DIFFRACTION11chain 'C' and (resid 31 through 48 )
12X-RAY DIFFRACTION12chain 'C' and (resid 49 through 61 )
13X-RAY DIFFRACTION13chain 'C' and (resid 62 through 92 )
14X-RAY DIFFRACTION14chain 'C' and (resid 93 through 107 )
15X-RAY DIFFRACTION15chain 'C' and (resid 108 through 125 )
16X-RAY DIFFRACTION16chain 'C' and (resid 126 through 137 )
17X-RAY DIFFRACTION17chain 'C' and (resid 138 through 146 )
18X-RAY DIFFRACTION18chain 'C' and (resid 147 through 152 )
19X-RAY DIFFRACTION19chain 'D' and (resid 44 through 132 )
20X-RAY DIFFRACTION20chain 'D' and (resid 133 through 181 )
21X-RAY DIFFRACTION21chain 'D' and (resid 182 through 281 )
22X-RAY DIFFRACTION22chain 'D' and (resid 282 through 355 )
23X-RAY DIFFRACTION23chain 'E' and (resid 34 through 61 )
24X-RAY DIFFRACTION24chain 'E' and (resid 62 through 78 )
25X-RAY DIFFRACTION25chain 'E' and (resid 79 through 92 )
26X-RAY DIFFRACTION26chain 'E' and (resid 93 through 107 )
27X-RAY DIFFRACTION27chain 'E' and (resid 108 through 125 )
28X-RAY DIFFRACTION28chain 'E' and (resid 126 through 133 )
29X-RAY DIFFRACTION29chain 'E' and (resid 134 through 145 )
30X-RAY DIFFRACTION30chain 'F' and (resid 41 through 83 )
31X-RAY DIFFRACTION31chain 'F' and (resid 84 through 109 )
32X-RAY DIFFRACTION32chain 'F' and (resid 110 through 161 )
33X-RAY DIFFRACTION33chain 'F' and (resid 162 through 201 )
34X-RAY DIFFRACTION34chain 'F' and (resid 202 through 253 )
35X-RAY DIFFRACTION35chain 'F' and (resid 254 through 291 )
36X-RAY DIFFRACTION36chain 'F' and (resid 292 through 318 )

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