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- PDB-5w8m: Crystal structure of Chaetomium thermophilum Vps29 -

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Basic information

Entry
Database: PDB / ID: 5w8m
TitleCrystal structure of Chaetomium thermophilum Vps29
ComponentsVacuolar protein sorting-associated protein 29Vacuole
KeywordsENDOCYTOSIS / endosome / retromer / vps29
Function / homology
Function and homology information


retromer complex / retrograde transport, endosome to Golgi / protein transport / cytosol
Similarity search - Function
Vacuolar protein sorting-associated protein 29 / Phosphodiesterase MJ0936/Vps29 / Calcineurin-like phosphoesterase domain, lpxH-type / Calcineurin-like phosphoesterase superfamily domain / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Metallo-dependent phosphatase-like / 4-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
TRIETHYLENE GLYCOL / Vacuolar protein sorting-associated protein 29
Similarity search - Component
Biological speciesChaetomium thermophilum (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.52 Å
AuthorsCollins, B.M. / Leneva, N.
Funding support Australia, 3items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP1061574 Australia
National Health and Medical Research Council (NHMRC, Australia)APP1058734 Australia
Australian Research Council (ARC)DP160101743 Australia
CitationJournal: Nature / Year: 2018
Title: Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.
Authors: Oleksiy Kovtun / Natalya Leneva / Yury S Bykov / Nicholas Ariotti / Rohan D Teasdale / Miroslava Schaffer / Benjamin D Engel / David J Owen / John A G Briggs / Brett M Collins /
Abstract: Eukaryotic cells traffic proteins and lipids between different compartments using protein-coated vesicles and tubules. The retromer complex is required to generate cargo-selective tubulovesicular ...Eukaryotic cells traffic proteins and lipids between different compartments using protein-coated vesicles and tubules. The retromer complex is required to generate cargo-selective tubulovesicular carriers from endosomal membranes. Conserved in eukaryotes, retromer controls the cellular localization and homeostasis of hundreds of transmembrane proteins, and its disruption is associated with major neurodegenerative disorders. How retromer is assembled and how it is recruited to form coated tubules is not known. Here we describe the structure of the retromer complex (Vps26-Vps29-Vps35) assembled on membrane tubules with the bin/amphiphysin/rvs-domain-containing sorting nexin protein Vps5, using cryo-electron tomography and subtomogram averaging. This reveals a membrane-associated Vps5 array, from which arches of retromer extend away from the membrane surface. Vps35 forms the 'legs' of these arches, and Vps29 resides at the apex where it is free to interact with regulatory factors. The bases of the arches connect to each other and to Vps5 through Vps26, and the presence of the same arches on coated tubules within cells confirms their functional importance. Vps5 binds to Vps26 at a position analogous to the previously described cargo- and Snx3-binding site, which suggests the existence of distinct retromer-sorting nexin assemblies. The structure provides insight into the architecture of the coat and its mechanism of assembly, and suggests that retromer promotes tubule formation by directing the distribution of sorting nexin proteins on the membrane surface while providing a scaffold for regulatory-protein interactions.
History
DepositionJun 21, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 13, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 10, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Feb 20, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Oct 4, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _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: Vacuolar protein sorting-associated protein 29
B: Vacuolar protein sorting-associated protein 29
C: Vacuolar protein sorting-associated protein 29
D: Vacuolar protein sorting-associated protein 29
E: Vacuolar protein sorting-associated protein 29
F: Vacuolar protein sorting-associated protein 29
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,6609
Polymers134,3266
Non-polymers3343
Water26,3381462
1
A: Vacuolar protein sorting-associated protein 29


Theoretical massNumber of molelcules
Total (without water)22,3881
Polymers22,3881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Vacuolar protein sorting-associated protein 29
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,5382
Polymers22,3881
Non-polymers1501
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Vacuolar protein sorting-associated protein 29
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,5723
Polymers22,3881
Non-polymers1842
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Vacuolar protein sorting-associated protein 29


Theoretical massNumber of molelcules
Total (without water)22,3881
Polymers22,3881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: Vacuolar protein sorting-associated protein 29


Theoretical massNumber of molelcules
Total (without water)22,3881
Polymers22,3881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: Vacuolar protein sorting-associated protein 29


Theoretical massNumber of molelcules
Total (without water)22,3881
Polymers22,3881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)65.460, 106.740, 88.118
Angle α, β, γ (deg.)90.00, 95.45, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Vacuolar protein sorting-associated protein 29 / Vacuole


Mass: 22387.654 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chaetomium thermophilum (fungus) / Production host: Escherichia coli (E. coli) / References: UniProt: G0RZB5
#2: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1462 / Source method: isolated from a natural source / Formula: H2O

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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: 2.28 Å3/Da / Density % sol: 46.09 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 8
Details: 8% PEG20000, 8% PEG550MME, 0.2 M calcium acetate and 0.1 M Tris (pH 8.0)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Jun 1, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.52→48.8 Å / Num. obs: 184667 / % possible obs: 99.8 % / Redundancy: 7.5 % / CC1/2: 0.997 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.057 / Net I/σ(I): 9.9
Reflection shellResolution: 1.52→1.55 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.707 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 8919 / CC1/2: 0.681 / Rpim(I) all: 0.431 / % possible all: 97.7

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1W24

1w24


Resolution: 1.52→45.594 Å / SU ML: 0.14 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 17.18
RfactorNum. reflection% reflection
Rfree0.1766 2000 1.08 %
Rwork0.1551 --
obs0.1553 184620 99.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.52→45.594 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8895 0 22 1462 10379
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.019119
X-RAY DIFFRACTIONf_angle_d1.29612378
X-RAY DIFFRACTIONf_dihedral_angle_d13.4433355
X-RAY DIFFRACTIONf_chiral_restr0.0521448
X-RAY DIFFRACTIONf_plane_restr0.0071571
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5194-1.55740.2461400.228712809X-RAY DIFFRACTION99
1.5574-1.59950.22941430.205812993X-RAY DIFFRACTION100
1.5995-1.64660.24421420.197313032X-RAY DIFFRACTION100
1.6466-1.69970.20741420.186312980X-RAY DIFFRACTION100
1.6997-1.76050.2161430.179713093X-RAY DIFFRACTION100
1.7605-1.8310.1831430.173212999X-RAY DIFFRACTION100
1.831-1.91430.16781430.157513041X-RAY DIFFRACTION100
1.9143-2.01520.16961430.145513047X-RAY DIFFRACTION100
2.0152-2.14150.17231430.144413066X-RAY DIFFRACTION100
2.1415-2.30680.191430.141613060X-RAY DIFFRACTION100
2.3068-2.53890.18191430.144113067X-RAY DIFFRACTION100
2.5389-2.90630.15771440.146813088X-RAY DIFFRACTION100
2.9063-3.66140.16431430.148613133X-RAY DIFFRACTION100
3.6614-45.61480.15821450.147413212X-RAY DIFFRACTION100
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)
13.1025-0.79840.12787.23211.17062.7828-0.0287-0.05530.00330.1478-0.05970.20890.1138-0.32110.11770.0852-0.02570.00770.1362-0.00130.039848.311450.040957.9016
23.0241-1.80390.38154.4546-1.30130.54340.043-0.1424-0.24770.1910.05720.48470.1983-0.3218-0.05530.1402-0.05870.02560.1754-0.00070.143947.017745.53960.4031
31.5851-0.19041.87753.3351-3.55176.0789-0.2078-0.35470.20110.8850.25670.1576-0.7149-0.3916-0.11570.27820.02630.01540.1713-0.03970.148755.384153.696971.6203
42.4214-0.28510.05551.0879-0.06861.2121-0.0133-0.00420.23850.0278-0.0889-0.1055-0.18440.08420.08670.1161-0.0342-0.00810.08650.00460.089462.692952.897855.7453
57.3022-4.04882.48534.7743-1.0473.7638-0.05290.57560.2985-0.1359-0.2317-0.033-0.19480.02790.26440.0993-0.0297-0.00860.12750.01840.08855.072349.919944.642
61.91680.148-0.60032.2936-0.89683.0431-0.00930.06650.0389-0.05720.06550.3795-0.0872-0.2359-0.04530.07070.0081-0.01760.08350.00030.160625.778642.994532.953
75.47813.1188-3.6683.1276-3.02473.1906-0.11560.5053-0.0275-0.41890.290.40090.2121-0.3338-0.16830.1922-0.0325-0.0790.1497-0.01270.182324.316738.112625.773
83.68772.0702-1.82615.03-2.67114.2216-0.12840.1734-0.2017-0.39520.12860.14090.3514-0.0640.0310.10940.0204-0.02680.0629-0.02190.094737.046335.203727.7747
93.45530.9225-0.32692.3051-0.84370.52770.0072-0.1543-0.10990.08770.00060.01430.03960.0827-0.01460.09090.0083-0.00520.0801-0.0030.062144.313838.17636.1951
104.1310.4608-1.32371.2711-0.21261.5164-0.0378-0.1128-0.05850.06880.01640.0404-0.02470.09770.01620.09040.0059-0.00410.0497-0.00930.066938.089645.682837.5386
117.63761.116-6.1392.6207-1.84385.6438-0.0259-0.83390.2180.59120.22990.3786-0.18020.6001-0.21790.24140.04340.04840.1803-0.00570.172129.198352.656343.3187
126.7510.4457-5.91742.99460.00845.4793-0.0626-0.47180.43850.06360.1309-0.00930.08050.3343-0.13580.07830.0176-0.03060.10560.01660.085136.829854.604437.1089
131.6489-0.44340.47661.9383-0.24362.38290.02080.08880.0778-0.12430.0214-0.3070.00880.4844-0.0420.0883-0.01320.02090.1514-0.01770.134253.331914.220748.4229
146.2301-2.45683.82121.4878-2.2325.8320.05480.31920.5516-0.081-0.127-0.2971-0.330.66710.07890.1292-0.06240.01790.1530.01350.210654.528922.725947.5692
151.65630.21121.35730.96440.39623.3747-0.0002-0.11960.14310.0135-0.05670.0874-0.1099-0.02770.06170.07980.00340.01850.0511-0.01660.107537.183519.35652.9787
166.37890.2712.7640.3691.12895.4979-0.0622-0.18740.00090.14690.0356-0.01020.10320.0423-0.0760.0572-0.00810.02140.0396-0.00930.057838.251111.52550.9056
172.90763.18770.66064.64362.33293.74850.09190.1586-0.23450.01950.03790.25930.1642-0.0438-0.11960.0709-0.01150.00060.05450.01310.098332.22198.476446.2328
182.3451-0.3319-0.08761.07961.09321.082-0.0026-0.2298-0.18350.17050.03450.01270.40940.187-0.09210.12440.0037-0.00130.07960.00770.119445.8276.239352.8948
192.6119-3.81712.55635.9813-3.80913.13880.0142-0.0624-0.36210.15240.1270.05130.05120.2476-0.18190.15140.0294-0.020.1698-0.01620.150248.57083.010443.468
202.54960.41222.63966.1322-0.68934.36840.12390.2822-1.2258-0.22940.06850.73990.11060.0466-0.17850.0596-0.01840.02280.0739-0.00240.04140.21064.834639.0979
214.59993.41234.08646.38454.3636.4521-0.18550.0791-0.0005-0.14530.1154-0.4172-0.38910.38450.02590.1429-0.0448-0.02570.18060.04940.161381.277238.297381.3221
225.4377-3.87354.56932.7363-3.26283.8784-0.05940.6720.0402-0.0428-0.2573-0.47850.35391.43190.31340.21330.02660.06910.34190.08270.345286.049629.253877.8313
233.47441.73622.48995.30094.71764.7305-0.0690.24170.0024-0.14320.2164-0.6121-0.36370.6497-0.14380.1852-0.0585-0.00510.25170.0530.184281.257141.040673.5828
241.4898-0.35620.50344.02610.58687.1714-0.0688-0.0520.33690.12930.00970.0165-0.88060.22870.04590.3017-0.0487-0.03630.17870.00170.175974.01950.537676.7635
252.47270.09980.04621.79350.04412.0615-0.0523-0.0740.11010.17690.06290.0417-0.1295-0.0758-0.00330.12660.0009-0.00170.10840.03980.094662.629939.080678.3025
264.90120.41362.12652.61060.76932.4973-0.0685-0.24740.03220.25960.0619-0.1421-0.125-0.1253-0.02610.1265-0.00830.00470.13620.02160.09966.775936.600982.3272
272.87010.16270.34911.7202-0.04191.6375-0.054-0.17630.03190.24740.0179-0.0744-0.07790.0034-0.01060.1485-0.0017-0.0120.13850.02830.109169.612833.418483.8651
287.67323.74552.53844.93284.36674.04610.0961-0.532-0.17990.1527-0.009-0.08330.2318-0.3492-0.03580.0984-0.00110.00410.13140.0410.129875.297425.55683.596
298.04890.87446.96960.28141.01875.8999-0.1386-0.4892-0.1710.06220.10940.0067-0.054-0.35550.01460.1295-0.01740.00230.19940.0340.132767.525124.052781.9019
304.71571.3891-3.74453.0615-0.97093.28420.0679-0.2013-0.01850.1595-0.0035-0.0930.04930.46730.02680.12020.0107-0.03610.1326-0.02130.090438.855814.63679.3443
316.99561.3186-1.40094.5087-5.36387.10620.1364-0.677-0.60430.461-0.373-0.58620.15771.11210.24420.25970.039-0.07540.3752-0.05010.256143.852317.623288.3761
324.58521.3938-1.17962.3949-2.39882.6863-0.0579-0.2336-0.32950.2097-0.0017-0.28590.34070.28180.09410.23550.051-0.04770.1577-0.01750.163939.64546.658381.7816
333.52921.7415-0.52019.1056-2.03536.95430.06750.2216-0.2609-0.08720.161-0.12580.1845-0.0248-0.19660.1725-0.0005-0.04640.1995-0.03620.141532.2683.89270.9073
343.81731.5106-0.71864.0792-1.85082.51490.018-0.4403-0.20370.09620.07860.22210.66530.31860.1370.25050.0220.00940.16730.05690.184424.26283.923188.5222
355.9166-0.3406-2.6931.05880.92886.25010.05810.3306-0.1473-0.094-0.09480.23920.1303-0.425-0.01360.1392-0.0317-0.04020.1304-0.00760.172918.154710.31275.4322
365.16271.8314-2.96472.25681.19156.1782-0.07590.04630.046-0.09620.08160.15360.171-0.1413-0.13840.07370.0112-0.03110.09240.0210.104924.180314.379680.0753
372.264-1.2998-0.13857.36865.15114.13010.0481-0.27730.06590.04330.02140.3334-0.0218-0.0622-0.10650.1088-0.0127-0.00470.15440.05850.114217.858316.475284.9245
384.1612-2.7924-2.47676.7612-0.69872.86820.30920.22030.2116-0.2618-0.01240.1444-0.3689-0.0757-0.22740.1446-0.01350.00220.136-0.00020.108434.346922.33273.4555
396.10625.9563-6.2466.4118-5.51968.22160.1903-0.4308-0.2430.4386-0.0230.14720.03950.1218-0.13290.22570.03010.02770.18140.04070.165729.043613.822792.3676
404.38654.9322-4.9976.4102-6.35027.51460.0670.15650.47770.27040.18480.4017-0.5201-0.0586-0.17820.25180.00680.01310.20260.01630.203134.743626.803886.7057
414.34533.2986-5.03813.0118-45.826-0.19970.00840.0175-0.14920.20240.11970.1152-0.1901-0.0750.12810.0104-0.00450.1479-0.0160.128227.245821.352891.2042
421.3865-0.4846-0.25093.0189-0.53072.0751-0.0216-0.1183-0.06870.025-0.1457-0.38270.09050.50320.11620.13880.04030.01180.22730.05660.167258.652828.0489103.3283
433.1712-5.34711.84639.1614-3.1721.0946-0.0954-0.31850.26420.6724-0.22-0.7069-0.13580.35250.24950.2396-0.0364-0.06450.30920.04060.176159.6332.6811110.5331
443.8322-2.71641.90687.1941-2.95534.3761-0.4077-0.8042-0.18590.97450.1475-0.09180.03840.37750.20230.28310.07070.03570.31420.10130.170449.097324.7821116.1774
453.7886-0.29730.64642.2958-0.62192.81280.0646-0.0336-0.1811-0.1864-0.0830.08680.1787-0.070.02150.11830.02670.01640.0942-0.01830.050238.858530.3214105.6402
463.9634-1.46480.04471.1523-0.39691.84450.02390.1098-0.3716-0.141-0.09110.11640.23610.07090.03350.17450.0210.01040.0987-0.00580.112843.876525.49699.0692
471.96331.8405-0.26881.8356-0.2863.89040.0102-0.11380.2746-0.1695-0.0943-0.0904-0.21540.12370.12910.1534-0.00110.00720.12170.00550.110550.26435.771695.6526
484.2334-4.7094-2.00046.29081.83132.7988-0.28250.1143-0.27820.10360.0239-0.01950.23260.18920.19330.19380.00990.03880.13850.01670.153953.421228.206489.6065
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 0 through 21 )
2X-RAY DIFFRACTION2chain 'A' and (resid 22 through 60 )
3X-RAY DIFFRACTION3chain 'A' and (resid 61 through 75 )
4X-RAY DIFFRACTION4chain 'A' and (resid 76 through 165 )
5X-RAY DIFFRACTION5chain 'A' and (resid 166 through 195 )
6X-RAY DIFFRACTION6chain 'B' and (resid -1 through 44 )
7X-RAY DIFFRACTION7chain 'B' and (resid 45 through 60 )
8X-RAY DIFFRACTION8chain 'B' and (resid 61 through 87 )
9X-RAY DIFFRACTION9chain 'B' and (resid 88 through 122 )
10X-RAY DIFFRACTION10chain 'B' and (resid 123 through 165 )
11X-RAY DIFFRACTION11chain 'B' and (resid 166 through 181 )
12X-RAY DIFFRACTION12chain 'B' and (resid 182 through 194 )
13X-RAY DIFFRACTION13chain 'C' and (resid 2 through 44 )
14X-RAY DIFFRACTION14chain 'C' and (resid 45 through 60 )
15X-RAY DIFFRACTION15chain 'C' and (resid 61 through 108 )
16X-RAY DIFFRACTION16chain 'C' and (resid 109 through 122 )
17X-RAY DIFFRACTION17chain 'C' and (resid 123 through 134 )
18X-RAY DIFFRACTION18chain 'C' and (resid 135 through 165 )
19X-RAY DIFFRACTION19chain 'C' and (resid 166 through 182 )
20X-RAY DIFFRACTION20chain 'C' and (resid 183 through 194 )
21X-RAY DIFFRACTION21chain 'D' and (resid 2 through 21 )
22X-RAY DIFFRACTION22chain 'D' and (resid 22 through 34 )
23X-RAY DIFFRACTION23chain 'D' and (resid 35 through 60 )
24X-RAY DIFFRACTION24chain 'D' and (resid 61 through 75 )
25X-RAY DIFFRACTION25chain 'D' and (resid 76 through 108 )
26X-RAY DIFFRACTION26chain 'D' and (resid 109 through 122 )
27X-RAY DIFFRACTION27chain 'D' and (resid 123 through 165 )
28X-RAY DIFFRACTION28chain 'D' and (resid 166 through 176 )
29X-RAY DIFFRACTION29chain 'D' and (resid 177 through 201 )
30X-RAY DIFFRACTION30chain 'E' and (resid 2 through 21 )
31X-RAY DIFFRACTION31chain 'E' and (resid 22 through 32 )
32X-RAY DIFFRACTION32chain 'E' and (resid 33 through 60 )
33X-RAY DIFFRACTION33chain 'E' and (resid 61 through 75 )
34X-RAY DIFFRACTION34chain 'E' and (resid 76 through 87 )
35X-RAY DIFFRACTION35chain 'E' and (resid 88 through 108 )
36X-RAY DIFFRACTION36chain 'E' and (resid 109 through 122 )
37X-RAY DIFFRACTION37chain 'E' and (resid 123 through 134 )
38X-RAY DIFFRACTION38chain 'E' and (resid 135 through 155 )
39X-RAY DIFFRACTION39chain 'E' and (resid 156 through 165 )
40X-RAY DIFFRACTION40chain 'E' and (resid 166 through 181 )
41X-RAY DIFFRACTION41chain 'E' and (resid 182 through 194 )
42X-RAY DIFFRACTION42chain 'F' and (resid 2 through 44 )
43X-RAY DIFFRACTION43chain 'F' and (resid 45 through 60 )
44X-RAY DIFFRACTION44chain 'F' and (resid 61 through 75 )
45X-RAY DIFFRACTION45chain 'F' and (resid 76 through 107 )
46X-RAY DIFFRACTION46chain 'F' and (resid 108 through 154 )
47X-RAY DIFFRACTION47chain 'F' and (resid 155 through 165 )
48X-RAY DIFFRACTION48chain 'F' and (resid 166 through 194 )

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