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- PDB-6rj4: Molybdenum storage protein - P6422, ADP -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6rj4
TitleMolybdenum storage protein - P6422, ADP
Components(Molybdenum storage protein subunit ...) x 2
KeywordsMETAL BINDING PROTEIN / Mo storage / ATP hydrolysis / polyoxomolybdate clusters / amino acid kinase
Function / homology
Function and homology information


nutrient reservoir activity / molybdenum ion binding / cytoplasm
Similarity search - Function
Molybdenum storage protein subunit alpha/beta / Carbamate kinase / Acetylglutamate kinase-like / Aspartate/glutamate/uridylate kinase / Acetylglutamate kinase-like superfamily / Amino acid kinase family / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / PHOSPHATE ION / Molybdenum storage protein subunit beta / Molybdenum storage protein subunit alpha
Similarity search - Component
Biological speciesAzotobacter vinelandii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsErmler, U. / Bruenle, S.
CitationJournal: Proc Natl Acad Sci U S A / Year: 2019
Title: Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism.
Authors: Steffen Brünle / Martin L Eisinger / Juliane Poppe / Deryck J Mills / Julian D Langer / Janet Vonck / Ulrich Ermler /
Abstract: The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (αβ) cage-like protein complex under ATP consumption. Here, we suggest ...The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (αβ) cage-like protein complex under ATP consumption. Here, we suggest a unique mechanism for the ATP-powered molybdate pumping process based on X-ray crystallography, cryoelectron microscopy, hydrogen-deuterium exchange mass spectrometry, and mutational studies of MoSto from . First, we show that molybdate, ATP, and Mg consecutively bind into the open ATP-binding groove of the β-subunit, which thereafter becomes tightly locked by fixing the previously disordered N-terminal arm of the α-subunit over the β-ATP. Next, we propose a nucleophilic attack of molybdate onto the γ-phosphate of β-ATP, analogous to the similar reaction of the structurally related UMP kinase. The formed instable phosphoric-molybdic anhydride becomes immediately hydrolyzed and, according to the current data, the released and accelerated molybdate is pressed through the cage wall, presumably by turning aside the Metβ149 side chain. A structural comparison between MoSto and UMP kinase provides valuable insight into how an enzyme is converted into a molecular machine during evolution. The postulated direct conversion of chemical energy into kinetic energy via an activating molybdate kinase and an exothermic pyrophosphatase reaction to overcome a proteinous barrier represents a novelty in ATP-fueled biochemistry, because normally, ATP hydrolysis initiates large-scale conformational changes to drive a distant process.
History
DepositionApr 26, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 18, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / refine / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _refine.pdbx_diffrn_id / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Molybdenum storage protein subunit beta
A: Molybdenum storage protein subunit alpha
D: Molybdenum storage protein subunit beta
C: Molybdenum storage protein subunit alpha
F: Molybdenum storage protein subunit beta
E: Molybdenum storage protein subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)175,97323
Polymers172,4796
Non-polymers3,49317
Water14,376798
1
B: Molybdenum storage protein subunit beta
A: Molybdenum storage protein subunit alpha
D: Molybdenum storage protein subunit beta
C: Molybdenum storage protein subunit alpha
F: Molybdenum storage protein subunit beta
E: Molybdenum storage protein subunit alpha
hetero molecules

B: Molybdenum storage protein subunit beta
A: Molybdenum storage protein subunit alpha
D: Molybdenum storage protein subunit beta
C: Molybdenum storage protein subunit alpha
F: Molybdenum storage protein subunit beta
E: Molybdenum storage protein subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)351,94546
Polymers344,95912
Non-polymers6,98634
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation11_655-x+y+1,y,-z1
Buried area68160 Å2
ΔGint-620 kcal/mol
Surface area94830 Å2
MethodPISA
Unit cell
Length a, b, c (Å)188.680, 188.680, 188.630
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number181
Space group name H-MP6422
Components on special symmetry positions
IDModelComponents
11D-523-

HOH

21C-488-

HOH

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Components

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Molybdenum storage protein subunit ... , 2 types, 6 molecules BDFACE

#1: Protein Molybdenum storage protein subunit beta / MoSto subunit beta


Mass: 28247.582 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (bacteria)
Strain: DJ / ATCC BAA-1303 / Gene: mosB, Avin_43210 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P84253
#2: Protein Molybdenum storage protein subunit alpha / Mo storage protein subunit alpha / MoSto subunit alpha


Mass: 29245.582 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (bacteria)
Strain: DJ / ATCC BAA-1303 / Gene: mosA, Avin_43200 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P84308

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Non-polymers , 6 types, 815 molecules

#3: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#6: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 798 / 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: 2.81 Å3/Da / Density % sol: 56.22 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 8.5 / Details: 1.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 14, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 154099 / % possible obs: 99.8 % / Redundancy: 6.6 % / Rsym value: 0.07 / Net I/σ(I): 16.4
Reflection shellResolution: 1.9→2 Å / Num. unique obs: 21666 / Rsym value: 1.032

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4ndo

4ndo


Resolution: 1.9→47.167 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 21.27 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2003 7787 5.05 %
Rwork0.1716 --
obs0.1731 154075 99.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.9→47.167 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11507 0 209 798 12514
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00712112
X-RAY DIFFRACTIONf_angle_d0.94316566
X-RAY DIFFRACTIONf_dihedral_angle_d15.1557304
X-RAY DIFFRACTIONf_chiral_restr0.0541933
X-RAY DIFFRACTIONf_plane_restr0.0052154
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.92160.30912670.3024783X-RAY DIFFRACTION100
1.9216-1.94420.28852710.25564806X-RAY DIFFRACTION100
1.9442-1.9680.29132320.25484818X-RAY DIFFRACTION100
1.968-1.99290.29192370.24394824X-RAY DIFFRACTION100
1.9929-2.01910.252500.23324822X-RAY DIFFRACTION100
2.0191-2.04670.29292600.22164836X-RAY DIFFRACTION100
2.0467-2.0760.26762360.23164815X-RAY DIFFRACTION100
2.076-2.1070.24412650.2084839X-RAY DIFFRACTION100
2.107-2.13990.21812590.20374778X-RAY DIFFRACTION100
2.1399-2.1750.23882520.19774855X-RAY DIFFRACTION100
2.175-2.21250.22962500.18694800X-RAY DIFFRACTION99
2.2125-2.25270.2492550.19914824X-RAY DIFFRACTION100
2.2527-2.2960.23462760.19354825X-RAY DIFFRACTION100
2.296-2.34290.22852600.18214876X-RAY DIFFRACTION100
2.3429-2.39390.19962660.17344816X-RAY DIFFRACTION100
2.3939-2.44950.23062610.18044871X-RAY DIFFRACTION100
2.4495-2.51080.23942770.18014814X-RAY DIFFRACTION100
2.5108-2.57870.20982570.17354866X-RAY DIFFRACTION100
2.5787-2.65450.22932520.1754883X-RAY DIFFRACTION100
2.6545-2.74020.21472530.18684885X-RAY DIFFRACTION100
2.7402-2.83810.22722390.17754892X-RAY DIFFRACTION100
2.8381-2.95180.21772790.18294852X-RAY DIFFRACTION100
2.9518-3.08610.20962600.18144891X-RAY DIFFRACTION100
3.0861-3.24870.21942640.18544902X-RAY DIFFRACTION100
3.2487-3.45220.20062640.16844890X-RAY DIFFRACTION100
3.4522-3.71870.16762620.15344944X-RAY DIFFRACTION100
3.7187-4.09270.17772690.14864975X-RAY DIFFRACTION100
4.0927-4.68450.14932610.12534967X-RAY DIFFRACTION100
4.6845-5.90010.15462810.14455044X-RAY DIFFRACTION100
5.9001-47.18140.17192720.15965295X-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)
18.52536.70831.06579.27073.24894.1374-0.05960.3395-0.7013-0.51560.4634-1.2137-0.09111.0917-0.43390.31270.04440.04780.5159-0.00670.299180.5185-12.7699-42.1466
25.15421.1953-0.35692.78351.61734.7234-0.0620.0791-0.1042-0.2584-0.00870.11390.2373-0.18560.07350.26690.0035-0.03860.24470.010.145742.5966-22.8528-47.7106
30.68570.3816-0.0462.62570.8010.60220.00050.036-0.06470.06190.0712-0.1920.10240.138-0.07480.26090.0323-0.02540.2984-0.01720.200849.3409-14.3959-36.9095
41.90930.4888-0.11821.4358-0.81322.28960.01720.13180.0573-0.16990.0480.0906-0.16820.007-0.05360.33920.0057-0.00760.3041-0.05210.214652.3277-11.0624-54.811
58.7317-3.05040.23925.5872.34482.6528-0.01070.01980.7765-0.3185-0.24750.0964-0.3034-0.12340.25640.2665-0.0149-0.00020.2713-0.00590.232159.93635.2145-21.1369
68.7405-4.5172-0.74997.21375.02586.91510.1257-0.17670.31170.15660.3259-0.7697-0.02180.7211-0.4980.1942-0.075-0.00920.308-0.02070.285679.5026-2.2955-13.629
70.5653-0.4933-0.57130.88680.83821.3660.05780.0636-0.0244-0.06950.0132-0.1486-0.00090.0579-0.07250.21350.00250.00420.3593-0.04760.277272.9175-10.4819-23.8615
88.8488-3.0130.88474.9439-1.3335.260.20950.4601-0.3682-0.4144-0.19330.38110.2429-0.3064-0.00610.1886-0.0244-0.00230.2034-0.02410.232558.88-7.6995-15.9576
90.876-0.1942-0.81611.78512.49524.5012-0.0215-0.0392-0.0042-0.04950.0526-0.00670.21760.2029-0.02430.16940.0229-0.01190.2448-0.01480.177966.4169-7.8501-29.9917
100.5574-0.41040.94481.8130.1441.73150.04030.29530.1112-0.19510.0522-0.32570.00390.4575-0.08610.21-0.02580.03760.3465-0.04720.227674.28933.9365-28.0878
113.6954-2.46072.99696.8361-0.73845.8151-0.16590.77660.6979-0.7375-0.017-0.8545-0.13380.87960.1380.3943-0.05840.12090.4750.00410.358480.063912.1528-35.3263
123.2388-0.02592.27061.96630.77553.45320.03640.22880.2069-0.2687-0.0065-0.2269-0.1830.4425-0.03640.2055-0.04820.05660.2675-0.00310.223371.97877.2124-27.9481
135.35366.11795.48979.74664.612.1268-0.4055-0.02570.8703-0.84080.0650.3341-0.8388-0.78160.23130.33740.04010.04750.4993-0.02370.268469.062815.2566-27.3849
146.11892.5933-3.20995.37873.83432.03450.12660.98260.1206-0.9390.09450.648-0.4986-0.6589-0.21170.36140.0628-0.12020.40850.00310.381821.3623-15.0207-33.7259
151.7919-2.64542.93715.9975-4.75995.54590.09860.1241-0.1341-0.26490.041-0.0170.28940.0796-0.1560.1537-0.0167-0.0140.2058-0.04630.222843.1907-46.035-23.1196
161.4054-1.3978-2.97043.55414.88638.32320.033-0.1364-0.0358-0.05330.0375-0.0310.09170.088-0.05370.18690.0009-0.0490.17090.01150.187346.0483-37.5357-12.0408
179.04920.12314.98435.7379-5.05017.26220.06610.18410.7527-0.0427-0.04370.078-0.5169-0.16980.03810.22780.06750.03270.29670.00680.285349.8778-36.0516-30.0273
180.30830.41980.18611.8216-0.30030.50650.0232-0.03220.00460.06820.03570.00090.06410.0248-0.05560.18530.0198-0.01960.212-0.02450.174135.5857-37.874-16.8917
192.9587-0.4144-0.70882.3431-0.19872.31810.0422-0.02420.03860.0863-0.06060.11860.0602-0.29660.01280.2503-0.0086-0.02190.2636-0.03610.221127.8523-47.1605-18.3097
200.1839-0.27510.30942.798-1.20073.03420.0351-0.04620.04860.10110.06450.1189-0.1963-0.2249-0.130.17830.03590.01550.2929-0.04810.27436.3176-2.9802-13.0383
210.41770.54560.44091.48421.18031.16650.01540.0171-0.014-0.02880.034-0.0383-0.00660.0033-0.03870.18860.0186-0.01010.2172-0.01230.201138.1647-10.2765-24.0071
220.2049-0.3074-0.60785.3542-2.04483.759-0.0130.0039-0.0668-0.22810.0514-0.19320.30360.1251-0.03380.14210.01710.00450.261-0.02180.239148.4263-11.9211-11.2168
233.92694.91153.73317.00794.98844.2649-0.12650.215-0.1062-0.14590.209-0.21940.04370.2989-0.10650.16230.01380.0120.20510.00620.149235.877-18.088-19.5485
240.40670.7946-0.79222.2595-1.24071.73150.0035-0.0666-0.08390.0143-0.00370.1227-0.0057-0.0031-0.00590.17050.0001-0.00960.2431-0.04990.237332.4363-12.1439-10.2455
254.82913.8972-6.04476.9963-2.07579.5519-0.27040.35230.224-0.87250.22320.78560.0703-1.01680.02750.30530.061-0.08540.36690.00540.361416.903-3.7821-22.3835
269.3884-2.91871.2035.8102-5.27279.2541-0.01830.361-0.1853-0.29640.15150.8357-0.0482-0.9411-0.22550.2580.0116-0.03510.4562-0.10890.425813.5315-8.1893-14.6339
270.5190.22470.05015.5073-0.56272.5498-0.0118-0.12250.1338-0.0349-0.0450.42660.0211-0.39290.06640.12420.02910.02220.3014-0.04970.295325.4046-8.768-11.2815
288.97561.66370.23286.2597-2.95177.53540.1398-1.04480.11921.08370.0260.2182-0.0074-0.5173-0.18220.31830.0211-0.01220.4556-0.0680.237122.1504-8.0522-3.5632
297.6676-1.3281-3.09162.04351.63413.1241-0.0817-0.6794-0.94380.88820.0958-0.12121.002-0.0617-0.03520.55680.0542-0.07220.39470.06250.399860.4293-49.74922.6845
300.64030.2025-0.63540.9290.19660.8169-0.00270.1079-0.2345-0.13360.0735-0.30310.09120.178-0.08390.24760.0806-0.02590.3928-0.06010.370776.1551-32.8977-28.0267
314.45811.60674.07130.93821.36753.1530.0177-0.36580.0440.0378-0.1830.07350.0887-0.40640.22930.21660.06070.01210.3295-0.0570.303269.4866-27.0234-28.0028
320.62121.2952-0.42912.79531.392.7807-0.0152-0.0776-0.0872-0.02480.0211-0.1386-0.04780.0628-0.02960.20780.0768-0.02490.3051-0.04380.275671.4873-31.4084-18.446
333.037-0.3242-0.81261.9236-0.71393.0268-0.0564-0.1674-0.1880.05080.0151-0.63340.26830.68830.05030.28740.1502-0.0440.4561-0.10060.47784.6637-42.1546-22.1936
342.0566-1.9892.78470.95330.30093.8261-0.0524-0.2178-0.03170.2584-0.24930.4872-0.1204-0.30210.37970.35630.0046-0.11770.7057-0.03480.598195.2977-18.498.1299
350.15530.42810.30881.79361.0541.14350.0516-0.0407-0.04490.19760.0047-0.14890.11780.0682-0.04960.21750.0365-0.04330.3011-0.01550.239257.222-26.87933.3891
360.465-0.3386-0.09950.77940.18640.22170.09970.1393-0.0428-0.0857-0.0601-0.03220.0363-0.0025-0.03860.20480.0303-0.04510.2972-0.03370.218658.9721-26.2954-5.292
372.18211.5095-0.88842.0303-0.20271.5880.1165-0.1172-0.31750.1913-0.151-0.29740.21110.08330.02620.27850.0545-0.09330.4023-0.01830.315265.6134-31.34968.6536
384.92742.8789-5.47273.8499-1.60339.69680.1947-0.783-1.15140.3562-0.1339-0.4480.78350.71270.02570.51040.0796-0.2160.47730.09160.575171.9662-38.19416.8919
391.90640.5395-1.13451.78940.35952.59720.1573-0.1342-0.20020.157-0.0326-0.2930.20440.3515-0.12280.28760.0602-0.10870.4092-0.01220.268968.5871-29.25999.5425
406.1369-2.747-6.13494.88352.06486.52350.2926-0.63490.3488-0.0166-0.2507-0.5778-0.410.92790.00790.33860.0411-0.13340.4628-0.00780.335573.3953-23.465914.367
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 2 through 37 )
2X-RAY DIFFRACTION2chain 'B' and (resid 38 through 68 )
3X-RAY DIFFRACTION3chain 'B' and (resid 69 through 168 )
4X-RAY DIFFRACTION4chain 'B' and (resid 169 through 270 )
5X-RAY DIFFRACTION5chain 'A' and (resid 33 through 47 )
6X-RAY DIFFRACTION6chain 'A' and (resid 48 through 68 )
7X-RAY DIFFRACTION7chain 'A' and (resid 69 through 123 )
8X-RAY DIFFRACTION8chain 'A' and (resid 124 through 143 )
9X-RAY DIFFRACTION9chain 'A' and (resid 144 through 169 )
10X-RAY DIFFRACTION10chain 'A' and (resid 170 through 204 )
11X-RAY DIFFRACTION11chain 'A' and (resid 205 through 221 )
12X-RAY DIFFRACTION12chain 'A' and (resid 222 through 261 )
13X-RAY DIFFRACTION13chain 'A' and (resid 262 through 276 )
14X-RAY DIFFRACTION14chain 'D' and (resid 4 through 28 )
15X-RAY DIFFRACTION15chain 'D' and (resid 29 through 68 )
16X-RAY DIFFRACTION16chain 'D' and (resid 69 through 121 )
17X-RAY DIFFRACTION17chain 'D' and (resid 122 through 141 )
18X-RAY DIFFRACTION18chain 'D' and (resid 142 through 199 )
19X-RAY DIFFRACTION19chain 'D' and (resid 200 through 270 )
20X-RAY DIFFRACTION20chain 'C' and (resid 33 through 68 )
21X-RAY DIFFRACTION21chain 'C' and (resid 69 through 123 )
22X-RAY DIFFRACTION22chain 'C' and (resid 124 through 143 )
23X-RAY DIFFRACTION23chain 'C' and (resid 144 through 169 )
24X-RAY DIFFRACTION24chain 'C' and (resid 170 through 190 )
25X-RAY DIFFRACTION25chain 'C' and (resid 191 through 204 )
26X-RAY DIFFRACTION26chain 'C' and (resid 205 through 221 )
27X-RAY DIFFRACTION27chain 'C' and (resid 222 through 261 )
28X-RAY DIFFRACTION28chain 'C' and (resid 262 through 276 )
29X-RAY DIFFRACTION29chain 'F' and (resid 4 through 28 )
30X-RAY DIFFRACTION30chain 'F' and (resid 29 through 95 )
31X-RAY DIFFRACTION31chain 'F' and (resid 96 through 133 )
32X-RAY DIFFRACTION32chain 'F' and (resid 134 through 168 )
33X-RAY DIFFRACTION33chain 'F' and (resid 169 through 270 )
34X-RAY DIFFRACTION34chain 'E' and (resid 18 through 33 )
35X-RAY DIFFRACTION35chain 'E' and (resid 34 through 97 )
36X-RAY DIFFRACTION36chain 'E' and (resid 98 through 169 )
37X-RAY DIFFRACTION37chain 'E' and (resid 170 through 204 )
38X-RAY DIFFRACTION38chain 'E' and (resid 205 through 221 )
39X-RAY DIFFRACTION39chain 'E' and (resid 222 through 260 )
40X-RAY DIFFRACTION40chain 'E' and (resid 261 through 276 )

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