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- PDB-6yb5: Orthorhombic crystal structure of a native BcsRQ complex crystall... -

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Basic information

Entry
Database: PDB / ID: 6yb5
TitleOrthorhombic crystal structure of a native BcsRQ complex crystallized in the presence of ADP
Components
  • Bacterial cellulose secretion regulator BcsQ
  • Bacterial cellulose secretion regulator BcsR
KeywordsSIGNALING PROTEIN / Bacterial biofilms / Bacterial cellulose / Bacterial secretion system / ATP binding protein
Function / homology
Function and homology information


bacterial cellulose biosynthetic process / cell division / ATP binding / cytoplasm
Similarity search - Function
Cellulose synthase operon protein BcsQ / Protein YhjR / Cellulose biosynthesis protein BcsQ / Cellulose biosynthesis protein BcsR-like / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Cell division protein / Cellulose biosynthesis protein BcsR / Protein YhjR / Cellulose biosynthesis protein BcsQ
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.59 Å
AuthorsCaleechurn, M. / Abidi, W. / Zouhir, S. / Roche, S. / Krasteva, P.V.
Funding support5items
OrganizationGrant numberCountry
ATIP-Avenir
European Research Council (ERC)BioMatrix, ERC StG #757507
Centre National de la Recherche Scientifique (CNRS)
Institute for Integrative Biology of the Cell (I2BC)
European Institute of Chemistry and Biology (IECB)
CitationJournal: Sci Adv / Year: 2021
Title: Architecture and regulation of an enterobacterial cellulose secretion system.
Authors: Wiem Abidi / Samira Zouhir / Meryem Caleechurn / Stéphane Roche / Petya Violinova Krasteva /
Abstract: Many free-living and pathogenic enterobacteria secrete biofilm-promoting cellulose using a multicomponent, envelope-embedded Bcs secretion system under the control of intracellular second messenger c- ...Many free-living and pathogenic enterobacteria secrete biofilm-promoting cellulose using a multicomponent, envelope-embedded Bcs secretion system under the control of intracellular second messenger c-di-GMP. The molecular understanding of system assembly and cellulose secretion has been largely limited to the crystallographic studies of a distantly homologous BcsAB synthase tandem and a low-resolution reconstruction of an assembled macrocomplex that encompasses most of the inner membrane and cytosolic subunits and features an atypical layered architecture. Here, we present cryo-EM structures of the assembled Bcs macrocomplex, as well as multiple crystallographic snapshots of regulatory Bcs subcomplexes. The structural and functional data uncover the mechanism of asymmetric secretion system assembly and periplasmic crown polymerization and reveal unexpected subunit stoichiometry, multisite c-di-GMP recognition, and ATP-dependent regulation.
History
DepositionMar 15, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 24, 2021Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: 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: Bacterial cellulose secretion regulator BcsQ
B: Bacterial cellulose secretion regulator BcsQ
C: Bacterial cellulose secretion regulator BcsR
D: Bacterial cellulose secretion regulator BcsR
H: Bacterial cellulose secretion regulator BcsQ
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,8449
Polymers101,7815
Non-polymers1,0634
Water7,710428
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering, SEC-MALS measurements confirmed the existence of a stable and monodisperse BcsR2Q2 heterotetramer in solution.
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9460 Å2
ΔGint-67 kcal/mol
Surface area22470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.110, 73.160, 140.470
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

#1: Protein Bacterial cellulose secretion regulator BcsQ / Cellulose biosynthesis protein BcsQ / Cellulose synthase operon protein YhjQ / Cellulose synthase / putative


Mass: 29245.209 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: Bacterial cellulose synthesis subunit Q. The purified native BcsRQ complex was treated with EDTA and incubated with ADP prior to crystallisation.
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: bcsQ, yhjQ, A8C65_00290, ACU57_05335, BMT91_17060, BON75_10030, BvCmsHHP019_01723, BvCmsSINP011_05061, C2U48_15650, D3O91_11725, D9H68_14440, D9I18_15755, D9I97_13990, DAH34_22885, DAH37_19450, ...Gene: bcsQ, yhjQ, A8C65_00290, ACU57_05335, BMT91_17060, BON75_10030, BvCmsHHP019_01723, BvCmsSINP011_05061, C2U48_15650, D3O91_11725, D9H68_14440, D9I18_15755, D9I97_13990, DAH34_22885, DAH37_19450, E2127_16420, E2128_18010, E2129_18145, E2134_17810, EAI42_04085, EC1094V2_71, NCTC10429_00778, NCTC11022_03734, NCTC9058_01652
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0B1KWQ0, UniProt: P0DP92*PLUS
#2: Protein Bacterial cellulose secretion regulator BcsR / FIG004405: Putative cytoplasmic protein / Protein YhjR / Protein of uncharacterized function (DUF2629)


Mass: 7022.876 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Bacterial cellulose synthesis subunit R. / Source: (gene. exp.) Escherichia coli (E. coli)
Gene: yhjR, A6V01_14365, A8C65_00295, A9R57_18690, AC789_1c39040, ACN002_3620, ACN68_06780, ACN81_08775, ACU57_05330, ACU90_15155, AM270_16530, AM464_10395, AMK83_17075, AML07_15400, APZ14_14840, ...Gene: yhjR, A6V01_14365, A8C65_00295, A9R57_18690, AC789_1c39040, ACN002_3620, ACN68_06780, ACN81_08775, ACU57_05330, ACU90_15155, AM270_16530, AM464_10395, AMK83_17075, AML07_15400, APZ14_14840, AUQ13_21010, AUS26_05355, AW106_19925, BANRA_02188, BANRA_03431, BANRA_04333, BANRA_04566, BB545_03705, BHS81_21135, BHS87_19835, BJJ90_00965, BK292_24575, BMT91_17065, BN17_34711, BOH76_20305, BON63_23095, BON69_12460, BON71_17720, BON72_13310, BON76_21180, BON94_21140, BON95_21275, BTQ06_14355, BUE81_10045, BvCms12BK_03867, BvCms2454_00062, BvCms28BK_00015, BvCmsHHP001_04915, BvCmsHHP019_01722, BvCmsHHP056_04702, BvCmsKKP036_02918, BvCmsKKP061_02263, BvCmsKSNP073_03410, BvCmsKSNP081_04400, BvCmsKSP011_02716, BvCmsKSP024_02867, BvCmsKSP026_02341, BvCmsKSP045_00352, BvCmsKSP067_01939, BvCmsNSNP036_04602, BvCmsNSP006_05307, BvCmsNSP047_03956, BvCmsNSP072_04054, BvCmsOUP014_03413, BvCmsSINP011_05062, BvCmsSIP019_02407, BvCmsSIP044_03516, BVL39_08345, BW690_01625, BZL31_14290, C2U48_15645, C5N07_21610, C5P01_24180, C6669_10230, C7235_01450, C7B02_19840, C9098_17010, C9114_22000, C9141_22075, C9160_22970, C9162_26275, C9182_22470, C9201_19395, C9306_17625, C9E25_16190, C9Z03_00095, C9Z28_19620, C9Z37_15395, C9Z39_13945, C9Z69_16745, C9Z89_13935, CA593_08480, CI641_010930, COD30_23820, COD46_13475, CR538_01230, CRD98_22705, CRM83_21580, CWS33_18425, D0X26_22825, D2184_20785, D2185_17650, D3821_09240, D3Y67_04435, D6T60_22230, D9D20_19605, D9E35_13135, D9H68_14435, D9I18_15750, D9I97_13985, D9J11_18915, D9J44_18935, D9K48_10615, D9K54_10550, DAH18_11545, DAH30_06135, DAH32_17855, DAH34_22880, DAH37_19445, DBQ99_02170, DEN89_25155, DEN97_17470, DEO04_20390, DEO19_17140, DIV22_07035, DJ503_16110, DL545_01700, DL800_25095, DP277_20930, DQF57_09495, DQO13_19235, DS732_25515, DTL43_22125, DXT69_13975, DXT71_18500, DXT73_16115, E0I42_16815, E0J34_09730, E0K84_22700, E2119_10885, E2127_16425, E2128_18015, E2129_18150, E2134_17815, E2135_13675, E2855_04489, E2863_04566, E3B71_14240, E5P22_13630, E5P28_15170, E5P37_17785, E5S35_16770, E5S47_16125, EAI42_04080, EC1094V2_70, EC3234A_62c00180, EC3426_04694, EC95NR1_02922, ED600_16775, EEP23_03690, EHH55_25990, EJC75_16880, EKI52_16535, EL75_0168, EL79_0179, EL80_0171, ELT20_13340, ELV08_08625, EPT01_13645, EQ825_24275, ERS085365_03384, ERS085374_03939, ERS085379_03461, ERS085416_01810, ERS139211_03246, EXX13_15900, EXX71_20125, EXX78_22145, EYD11_00910, EYY78_10840, F0312_08835, F1E03_18480, F1E19_10145, F7F23_20655, F7F29_18335, FORC82_0211, FQ915_11140, FQR64_01380, FRV13_18835, FTV90_03830, FTV92_19380, FV293_20875, FWK02_16270, FY127_16255, HW43_22525, NCTC10090_03288, NCTC10418_00365, NCTC10429_00777, NCTC10865_00350, NCTC11022_03735, NCTC11126_00353, NCTC11181_02507, NCTC11341_02195, NCTC13148_03788, NCTC8009_01140, NCTC8179_05669, NCTC8500_00017, NCTC8960_02842, NCTC8985_04684, NCTC9045_00297, NCTC9055_02150, NCTC9058_01653, NCTC9062_02927, NCTC9111_00632, NCTC9703_04725, NCTC9706_02488, PGD_04560, PU06_03455, RG28_22775, RK56_020175, RX35_03299, SAMEA3472043_03895, SAMEA3472055_04880, SAMEA3472070_03765, SAMEA3472114_02155, SAMEA3484427_00198, SAMEA3484429_02974, SAMEA3752553_00829, SAMEA3752557_03916, SAMEA3752559_00583, SAMEA3753064_01978, SAMEA3753290_02280, SAMEA3753300_03978, SK85_03853, UN86_19365, WQ89_12680, WR15_14750
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: J7QAC9, UniProt: P0ADJ3*PLUS
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 428 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.14 Å3/Da / Density % sol: 42.6 %
Crystal growTemperature: 277.4 K / Method: vapor diffusion, hanging drop / Details: 100 mM MES pH 6.5 and 12% PEG 20 000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.980027019978 Å
DetectorType: DECTRIS EIGER2 X 9M / Detector: PIXEL / Date: Oct 1, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.980027019978 Å / Relative weight: 1
ReflectionResolution: 1.59→50 Å / Num. obs: 81659 / % possible obs: 99 % / Redundancy: 13.2 % / Biso Wilson estimate: 24.35 Å2 / CC1/2: 0.999 / Net I/σ(I): 17.2
Reflection shellResolution: 1.59→1.69 Å / Redundancy: 11.8 % / Num. unique obs: 12421 / CC1/2: 0.562 / % possible all: 94.3

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Processing

Software
NameVersionClassification
PHENIX1.17rc2_3619refinement
Cootmodel building
PHASERphasing
XDSdata scaling
XDSdata processing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6YAR

6yar


Resolution: 1.59→45.23 Å / SU ML: 0.1662 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 18.2678
RfactorNum. reflection% reflection
Rfree0.1842 4111 5.03 %
Rwork0.1603 --
obs0.1615 81657 99.03 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 29.71 Å2
Refinement stepCycle: LAST / Resolution: 1.59→45.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4401 0 64 428 4893
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00614769
X-RAY DIFFRACTIONf_angle_d0.77876533
X-RAY DIFFRACTIONf_chiral_restr0.0518730
X-RAY DIFFRACTIONf_plane_restr0.0042884
X-RAY DIFFRACTIONf_dihedral_angle_d16.09062870
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.59-1.610.32291080.31081953X-RAY DIFFRACTION74
1.61-1.630.30841380.27382680X-RAY DIFFRACTION99.82
1.63-1.650.29271470.27532676X-RAY DIFFRACTION99.86
1.65-1.670.2781470.25832630X-RAY DIFFRACTION99.86
1.67-1.690.2461350.22782674X-RAY DIFFRACTION99.82
1.69-1.720.23751610.21742623X-RAY DIFFRACTION99.89
1.72-1.740.25181050.21252738X-RAY DIFFRACTION99.82
1.74-1.770.2471630.21712609X-RAY DIFFRACTION99.71
1.77-1.80.24011490.20832684X-RAY DIFFRACTION99.65
1.8-1.830.24931410.19252668X-RAY DIFFRACTION99.82
1.83-1.870.19851390.17982652X-RAY DIFFRACTION99.79
1.87-1.90.21061410.1722689X-RAY DIFFRACTION99.86
1.9-1.940.20351400.16432635X-RAY DIFFRACTION99.75
1.94-1.980.181420.16112711X-RAY DIFFRACTION99.96
1.98-2.030.19621410.15822676X-RAY DIFFRACTION99.93
2.03-2.080.17791410.162676X-RAY DIFFRACTION100
2.08-2.140.20131430.16022725X-RAY DIFFRACTION100
2.14-2.20.18971410.15062662X-RAY DIFFRACTION100
2.2-2.270.2041420.14762701X-RAY DIFFRACTION99.96
2.27-2.350.18051430.15312719X-RAY DIFFRACTION100
2.35-2.440.18981410.15732691X-RAY DIFFRACTION100
2.44-2.560.19111430.16382704X-RAY DIFFRACTION100
2.56-2.690.18131420.15862707X-RAY DIFFRACTION99.96
2.69-2.860.15731430.15652713X-RAY DIFFRACTION100
2.86-3.080.19851440.1592729X-RAY DIFFRACTION100
3.08-3.390.15091440.14982741X-RAY DIFFRACTION99.97
3.39-3.880.16321450.13742757X-RAY DIFFRACTION99.93
3.88-4.890.13621470.13342795X-RAY DIFFRACTION100
4.89-45.230.19761550.1682928X-RAY DIFFRACTION99.84
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)
10.669376557491-0.1157236664320.1018723135910.6850880811040.01961960500040.4474945684680.0279433576666-0.0381030441617-0.02441828854530.105238303514-0.0225549205528-0.08802077728010.04616025884460.0622276114385-3.21298789174E-70.204314651345-0.000485873559892-0.01200984831280.1922034786490.01513581595960.204583556648.49713914002-40.22281556961.65494962572
20.07487806469710.07820367692590.06156202142610.07891779987930.0582004354540.1029451356920.04405840548480.1687918050640.0195170733159-0.311511815359-0.280790979704-0.130130806144-0.1801033478120.144757221347-3.22011958449E-50.2898194396570.03280432318680.01881746822220.2963326908380.03942473191180.28893581621320.4226093271-34.4621197831-10.2273302052
30.1205713231130.07540986141030.1034381811070.1227522213330.1174759595110.1740422750930.05597522266880.125077081408-0.2465848404010.04896985916610.002123102871240.00453785767544-0.0320259719308-0.0305985481631-4.91666475491E-50.2374814069680.0213911944535-0.04067797068950.2041988086890.02295230518590.28694156640410.3542161725-51.1838022781-2.00034140714
40.1342173937110.07458976864160.1625451408290.05162765921290.08067088476530.223553818440.03640571385180.173536026274-0.101225337331-0.0147810315982-0.1063250676420.07881782091120.03173102946210.149073705901-0.00010047488150.2192429603340.01707576624010.003222036277410.2397447340370.01823824361050.2079965665545.99282617924-44.1018434858-12.7266813991
50.3259160474530.175220960338-0.1434896915990.16262964193-0.08993308300110.60525245859-0.001108394335580.080336661279-0.0788263427865-0.0139724131514-0.03011216795360.09178030864720.110495179227-0.05925663996481.28686989052E-60.186535092717-0.001307103500350.006364479628360.190917109799-0.01056242459440.194813013657-10.5372978667-35.4255102036-16.4986028103
60.1052110989670.00626979997643-0.004397123852040.128206890398-0.1346037317050.1375845868840.04414263911970.040600689165-0.0325268426147-0.1415585355120.002000396043350.0131277667824-0.101731022459-0.0575959311315.64364508154E-60.228030927685-0.01708255580030.005915506941410.241824512051-0.02327630202040.218562198795-11.6713101799-39.2951486586-9.88849906954
70.4106399366440.0841369153958-0.1823960099260.294316074768-0.2810405773030.3491859606370.0181541629643-0.0780564446837-0.07601063789530.0633661911844-0.04411570126650.02892628102520.0764583706061-0.0859691549473-4.77592155716E-50.196213811248-0.009604188833170.01796788630190.2069668071970.005675295676780.236194116614-6.08134583803-39.94310535261.78017691281
80.5124438972060.0825945669983-0.09654615989150.51213719962-0.03141897484650.3100696880692.33145065836E-50.09022374417090.0291103036025-0.131397995577-0.0270786355193-0.0226649646891-0.01871193292270.0116297030728-2.13280828349E-50.2095375149880.003120583860540.003064260901310.1957122492940.01139108724340.1750324408742.70322557568-21.3029537349-30.6185943072
90.05362954030260.00737639204547-0.05769822200560.1089462072780.02127502417520.06522800011990.012367036867-0.152207158057-0.1152958088710.0526225857729-0.115703494164-0.2647200611320.07619662032380.116337781998-2.53931416692E-50.2426209329970.0162157368971-0.002729273440.2688210802260.01245538952720.2876270424111.0177263401-36.7128252035-28.5667799213
100.3644453626720.06554102256060.02686649239780.2968552134870.007994244848380.716754218466-0.00168458993526-0.004126630500980.0448561588633-0.0258551754678-0.0330678450625-0.0294578157515-0.06562193045940.0712109917709-3.7310833508E-60.193649894308-0.00210853630502-0.0001430669719460.1837901785930.009781543086920.1967224310754.60493637983-16.8280360953-16.7231996463
110.0367593605687-0.06597050382830.01839909201930.233570617023-0.00280151411510.1333309553940.238058509296-0.05635420476620.224686644238-0.0591039989766-0.187245069286-0.048493780093-0.3124604045750.01210821770620.0002533484413510.297418477326-0.02382706647030.02992015752940.2245904440150.005119333585730.2698837498473.57358254253-5.94433270683-20.3899549609
120.587527250859-0.361801373799-0.6268354137490.2302477438130.293194058162.34790118462-0.3723153445550.04538502121910.677665287380.31624422597-0.0588580865731-0.2276911516-0.259873567675-0.790313482611-0.4398743996750.2876433740480.0928573055123-0.1048830273390.537664843945-0.1070067526840.4575323664292.37156326767-8.7675449246410.3965508531
130.032461712402-0.00800635637881-0.02321003074960.0215445154640.03709503177260.0595118792520.152992732456-0.120512778906-0.158118428343-0.0759651498883-0.0921724572836-0.2687484945210.2762680054370.119037280455-8.74248984783E-60.250092468472-0.00974652318158-0.01451192882450.235439713449-0.02714850383660.2383669280699.48661821813-20.60253425657.5183878951
140.442514303148-0.279463548849-0.6336514485090.2655134995430.4847789691961.30229672465-0.1894520470590.0131160335815-0.2451052944110.1844885172830.006492440417350.3781864284570.4073567199-0.280051340707-0.1421342423040.254482254671-0.0255913218962-0.0566980604310.368211498252-0.05849434823920.35580648281-18.2967870627-39.9100041957-26.0097803629
150.0424197761059-0.0200319965086-0.01372079841750.02082647781160.01505625211440.0088369627338-0.0676986038930.0720535234677-0.144765997177-0.1996127128970.00877895068352-0.04977146042680.173251183382-0.1670360386924.90587474277E-50.349533612651-0.00562912515657-0.02451567821030.269532113903-0.02171448217430.264592775391-14.1882285036-33.5724927126-30.4199635852
160.0261214430231-0.008231145414620.02686766472720.00441060853663-0.0054055989940.0409011135715-0.001197792585060.3821276166410.180930354109-0.0602289388929-0.1136511701440.02176751177790.171700432741-0.352235859273-2.85355262665E-50.987956313030.15414668944-0.003834428505770.5682662694390.04671168557450.521225619073-15.5156260046-5.44498961096-15.2148431921
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 82 )
2X-RAY DIFFRACTION2chain 'A' and (resid 83 through 102 )
3X-RAY DIFFRACTION3chain 'A' and (resid 103 through 125 )
4X-RAY DIFFRACTION4chain 'A' and (resid 126 through 148 )
5X-RAY DIFFRACTION5chain 'A' and (resid 149 through 190 )
6X-RAY DIFFRACTION6chain 'A' and (resid 191 through 202 )
7X-RAY DIFFRACTION7chain 'A' and (resid 203 through 244 )
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 82 )
9X-RAY DIFFRACTION9chain 'B' and (resid 83 through 102 )
10X-RAY DIFFRACTION10chain 'B' and (resid 103 through 222 )
11X-RAY DIFFRACTION11chain 'B' and (resid 223 through 244 )
12X-RAY DIFFRACTION12chain 'C' and (resid 37 through 51 )
13X-RAY DIFFRACTION13chain 'C' and (resid 52 through 62 )
14X-RAY DIFFRACTION14chain 'D' and (resid 28 through 51 )
15X-RAY DIFFRACTION15chain 'D' and (resid 52 through 62 )
16X-RAY DIFFRACTION16chain 'H' and (resid 259 through 266 )

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