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- PDB-5awf: Crystal structure of SufB-SufC-SufD complex from Escherichia coli -

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Basic information

Entry
Database: PDB / ID: 5awf
TitleCrystal structure of SufB-SufC-SufD complex from Escherichia coli
Components
  • FeS cluster assembly protein SufB
  • FeS cluster assembly protein SufD
  • Probable ATP-dependent transporter SufC
KeywordsTRANSPORT PROTEIN/PROTEIN BINDING / Iron-Sulfur Clusters / Iron-Sulfur Proteins / ABC proteins / ABC ATPase / TRANSPORT PROTEIN-PROTEIN BINDING complex
Function / homology
Function and homology information


iron-sulfur cluster assembly complex / iron-sulfur cluster assembly / response to radiation / 2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / ATP hydrolysis activity / ATP binding / cytosol
Similarity search - Function
SUF system FeS cluster assembly, SufB / SUF system FeS cluster assembly, SufBD, N-terminal / SufBD protein N-terminal region / SUF system FeS cluster assembly, SufD / SUF system FeS cluster assembly, SufBD / SUF system FeS cluster assembly, SufBD superfamily / SUF system FeS cluster assembly, SufBD core domain / FeS cluster assembly SUF system, ATPase SufC / ABC transporter-like, conserved site / ABC transporters family signature. ...SUF system FeS cluster assembly, SufB / SUF system FeS cluster assembly, SufBD, N-terminal / SufBD protein N-terminal region / SUF system FeS cluster assembly, SufD / SUF system FeS cluster assembly, SufBD / SUF system FeS cluster assembly, SufBD superfamily / SUF system FeS cluster assembly, SufBD core domain / FeS cluster assembly SUF system, ATPase SufC / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Probable ATP-dependent transporter SufC / Iron-sulfur cluster assembly protein SufB / Iron-sulfur cluster assembly protein SufD
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.957 Å
AuthorsHirabayashi, K. / Wada, K.
CitationJournal: J Biol Chem / Year: 2015
Title: Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.
Authors: Kei Hirabayashi / Eiki Yuda / Naoyuki Tanaka / Sumie Katayama / Kenji Iwasaki / Takashi Matsumoto / Genji Kurisu / F Wayne Outten / Keiichi Fukuyama / Yasuhiro Takahashi / Kei Wada /
Abstract: ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC ...ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC transporters and structural maintenance of chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel type of ABC protein, the SufBCD complex, functions in the biosynthesis of nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as eukaryotic chloroplasts. In this study, we determined the first crystal structure of the Escherichia coli SufBCD complex, which exhibits the common architecture of ABC proteins: two ABC ATPase components (SufC) with function-specific components (SufB-SufD protomers). Biochemical and physiological analyses based on this structure provided critical insights into Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S cluster in the SufBCD complex.
History
DepositionJul 3, 2015Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 11, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 17, 2016Group: Database references
Revision 1.2Feb 26, 2020Group: Data collection / Database references / Derived calculations
Category: citation / diffrn_source / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Aug 11, 2021Group: Database references / Structure summary / Category: audit_author / citation_author / database_2
Item: _audit_author.identifier_ORCID / _citation_author.identifier_ORCID ..._audit_author.identifier_ORCID / _citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FeS cluster assembly protein SufB
B: FeS cluster assembly protein SufD
C: Probable ATP-dependent transporter SufC
D: Probable ATP-dependent transporter SufC
E: FeS cluster assembly protein SufB
F: FeS cluster assembly protein SufD
G: Probable ATP-dependent transporter SufC
H: Probable ATP-dependent transporter SufC


Theoretical massNumber of molelcules
Total (without water)313,8238
Polymers313,8238
Non-polymers00
Water00
1
A: FeS cluster assembly protein SufB
B: FeS cluster assembly protein SufD
C: Probable ATP-dependent transporter SufC
D: Probable ATP-dependent transporter SufC


Theoretical massNumber of molelcules
Total (without water)156,9114
Polymers156,9114
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6420 Å2
ΔGint-30 kcal/mol
Surface area50980 Å2
MethodPISA
2
E: FeS cluster assembly protein SufB
F: FeS cluster assembly protein SufD
G: Probable ATP-dependent transporter SufC
H: Probable ATP-dependent transporter SufC


Theoretical massNumber of molelcules
Total (without water)156,9114
Polymers156,9114
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6520 Å2
ΔGint-29 kcal/mol
Surface area51380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.475, 139.556, 124.684
Angle α, β, γ (deg.)90.00, 113.10, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein FeS cluster assembly protein SufB


Mass: 54800.070 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: sufB, ynhE, b1683, JW5273 / Production host: Escherichia coli (E. coli) / References: UniProt: P77522
#2: Protein FeS cluster assembly protein SufD


Mass: 46884.641 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: sufD, ynhC, b1681, JW1671 / Production host: Escherichia coli (E. coli) / References: UniProt: P77689
#3: Protein
Probable ATP-dependent transporter SufC


Mass: 27613.332 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: sufC, ynhD, b1682, JW1672 / Production host: Escherichia coli (E. coli) / References: UniProt: P77499

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.05 Å3/Da / Density % sol: 59.63 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: pentaerythritol propoxylate (5/4 PO/OH), sodium citrate, potassium chloride

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Apr 12, 2014
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.95→50 Å / Num. obs: 77331 / % possible obs: 98.5 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 15.8
Reflection shellResolution: 2.95→3.06 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.371 / Mean I/σ(I) obs: 2.8 / % possible all: 98.1

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
HKL-2000data scaling
PHENIXphasing
Cootmodel building
HKL-2000data reduction
RefinementMethod to determine structure: MIR / Resolution: 2.957→41.111 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.77 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2262 1990 2.58 %Random selection
Rwork0.1868 ---
obs0.1878 77254 98.2 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.957→41.111 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19914 0 0 0 19914
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00620287
X-RAY DIFFRACTIONf_angle_d1.24127438
X-RAY DIFFRACTIONf_dihedral_angle_d15.8137464
X-RAY DIFFRACTIONf_chiral_restr0.0483071
X-RAY DIFFRACTIONf_plane_restr0.0063597
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9569-3.03080.31431300.27945172X-RAY DIFFRACTION95
3.0308-3.11270.32141480.26295372X-RAY DIFFRACTION98
3.1127-3.20430.30651390.25295374X-RAY DIFFRACTION99
3.2043-3.30760.29641480.24185345X-RAY DIFFRACTION99
3.3076-3.42580.26921410.22445403X-RAY DIFFRACTION99
3.4258-3.56290.23781440.19795445X-RAY DIFFRACTION99
3.5629-3.72490.24861390.18995422X-RAY DIFFRACTION99
3.7249-3.92120.23891460.19375428X-RAY DIFFRACTION99
3.9212-4.16660.22231470.17955426X-RAY DIFFRACTION99
4.1666-4.4880.19441460.15585439X-RAY DIFFRACTION99
4.488-4.93890.17971380.13685421X-RAY DIFFRACTION99
4.9389-5.65210.18731420.16585460X-RAY DIFFRACTION99
5.6521-7.1150.23921460.20065428X-RAY DIFFRACTION99
7.115-41.11520.2011360.17435129X-RAY DIFFRACTION92
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)
11.1203-0.549-0.45670.63210.1710.9392-0.2352-0.72890.19160.19960.4237-0.11560.01880.4360.01620.5237-0.0887-0.18390.7271-0.16990.700916.79570.5951130.3138
20.60450.36760.32480.70360.00861.5215-0.2038-0.07360.32290.05440.2449-0.3208-0.31870.54670.00190.4377-0.2033-0.07130.5229-0.05220.649912.750671.9262116.9827
30.47490.0036-0.39490.23680.30450.787-0.1044-0.019-0.02870.01160.04340.0398-0.16670.2629-0.00010.11220.006-0.06190.1612-0.01310.2803-2.731960.2236112.9758
40.20530.27920.30930.41310.33381.16280.15240.0433-0.01580.0119-0.1156-0.3968-0.2260.35830.00010.3368-0.02510.04110.54430.00660.442510.010452.65895.9388
50.6267-0.1601-0.02430.51820.40780.3439-0.2017-0.4430.16630.4308-0.0862-0.18490.06590.1595-0.00310.58530.02450.04260.6690.03310.3801-14.45239.7299140.2462
60.345-0.3563-0.02360.42220.13080.2030.37590.06610.29030.9957-0.29980.52220.2831-0.18850.00280.6938-0.03420.18370.91770.06380.7031-34.108241.2792139.5075
70.3844-0.5628-0.47270.91730.73590.6522-0.1667-0.0072-0.2570.6016-0.06610.03860.6403-0.03310.00390.6464-0.20910.16270.53990.11530.6475-30.897127.7213128.2255
80.8291-0.38080.80480.4548-0.28430.82620.0405-0.2889-0.29340.24380.07480.11770.3305-0.3141-00.4734-0.13820.1590.42240.05940.4657-28.037433.6264128.5301
90.6753-0.1325-0.19550.275-0.27310.4344-0.05480.0263-0.15320.20490.12170.3160.2939-0.1334-0.00010.3179-0.06770.06350.31570.03580.4367-23.679438.9816121.0164
100.41040.40110.06530.41050.08820.0312-0.0667-0.4286-0.278-0.04620.22430.3101-0.03120.0602-0.00420.3386-0.01540.03690.37160.01560.418-19.565544.1578118.0872
110.5374-0.11650.75810.2226-0.23691.0919-0.12890.0044-0.110.10050.1-0.01430.0914-0.05010.00020.21370.01460.05510.249-0.00680.3667-14.253848.8401113.6046
120.2605-0.36530.31530.4895-0.47490.51670.0456-0.10030.0419-0.1456-0.17390.0787-0.0826-0.5555-0.00010.30650.09110.00280.5916-0.03650.5628-36.848157.2639112.5085
130.74020.18360.55981.05830.47870.53490.7027-0.0162-0.6-0.04790.1527-0.38660.9140.45430.01470.82750.2645-0.17610.6942-0.03720.869.257926.325877.5938
140.54920.05740.41071.0150.71740.75280.0925-0.07440.0381-0.01220.1065-0.1864-0.04490.1703-00.27460.09790.10910.4172-0.02530.372410.442949.536279.653
151.03780.0290.77140.86060.34551.7490.39960.1479-0.0616-0.5451-0.2310.07660.03360.08010.00030.55740.1731-0.03380.4104-0.04780.3896-1.236237.941170.27
160.17610.2645-0.12420.3795-0.17260.38820.2467-0.17540.2894-0.1921-0.146-0.1538-0.2293-0.01890.00020.76240.23410.04820.8297-0.09940.95-40.640788.9628103.745
170.5308-0.32080.26541.1364-0.10350.12350.0569-0.1464-0.1499-0.2239-0.07180.2499-0.0466-0.43210.1223-0.15240.69740.04050.385-0.14520.4965-45.78566.270999.6036
180.1760.07540.07410.73260.1450.11280.26880.34950.1887-0.7394-0.09050.2647-0.2906-0.38610.00141.0340.385-0.02460.83330.01690.8042-45.892877.644690.3023
190.10060.1194-0.08060.3091-0.15970.21330.16990.30510.5933-0.587-0.16070.2526-0.2669-0.2282-0.00431.25960.34360.23450.84180.14341.0285-43.238491.431887.9409
201.043-1.16890.13011.2802-0.21251.0592-0.2415-0.16290.27620.24510.2718-0.3097-0.0810.286-0.00030.5635-0.299-0.1840.9860.07140.635710.6865138.959769.2649
210.91410.4976-0.05720.43340.47931.53890.06370.08860.06220.14710.0947-0.1620.00350.601800.5423-0.2038-0.13591.01290.10980.59615.8962132.800856.8676
220.444-0.0314-0.31040.2870.15090.25070.1677-0.1197-0.0270.1189-0.1853-0.0661-0.05420.3089-0.00020.4895-0.1537-0.16050.51170.07160.3828-12.1907130.130856.3689
230.5052-0.0320.14770.0702-0.05060.6570.1723-0.195-0.15280.0861-0.0935-0.05010.05370.5077-0.00010.58470.0182-0.12460.78120.04140.6071-4.592114.066442.5473
240.10930.08060.08690.3060.00170.078-0.038-0.25920.25060.73180.13080.1986-0.47340.4205-0.00321.5058-0.2165-0.03031.59840.01710.5664-35.5113123.692294.828
250.4640.1099-0.18120.70010.04420.0850.0442-0.1316-0.1671-0.01180.4641-0.06070.20890.32680.15150.9416-0.288-0.17420.96140.13450.4492-25.7073124.656282.5541
260.4271-0.2065-0.26270.93390.61430.43770.0369-0.5665-0.14240.7137-0.19180.17410.0915-0.3382-0.00290.893-0.31720.13351.04480.08310.4451-49.0961122.468880.3102
270.6202-0.2929-0.14640.28540.03630.89420.2051-0.5466-0.01960.2566-0.21540.1594-0.0817-0.0984-0.00210.7707-0.3030.09580.72810.04570.3149-45.1512121.245676.8814
281.0612-0.1772-0.4150.4214-0.03280.58820.3217-0.2939-0.09940.4044-0.0208-0.1615-0.0080.10680.01770.6654-0.22720.05680.6510.02830.3215-39.4228122.130968.4442
290.91330.51060.38740.6485-0.16810.62820.1869-0.3562-0.18170.1182-0.1292-0.05130.04070.01290.00050.6246-0.205-0.020.4780.02540.3815-31.2276122.938162.4916
300.51910.360.07150.2722-0.09170.65630.0709-0.1758-0.12610.0986-0.09750.0365-0.24560.28780.00040.5362-0.1731-0.03640.50770.0270.3938-25.7726127.737157.9259
310.1997-0.25170.25430.3127-0.36060.5634-0.0881-0.3850.15730.20240.05790.062-0.151-0.1580.00040.5135-0.06830.03770.4645-0.04710.4108-44.5053141.178154.5474
320.4970.22680.21210.5945-0.03270.3065-0.0498-0.0295-0.250.29180.1189-0.22970.9614-0.03570.00141.22210.1903-0.07650.47120.10350.6403-18.346586.968132.0743
330.14120.24180.24050.83940.21510.56930.0138-0.1145-0.01120.27030.1082-0.47390.11320.61740.00240.39710.1039-0.05920.59190.00230.569-6.1993105.796727.7298
340.46850.64840.11231.0855-0.31921.3777-0.03860.10190.06870.06830.09310.11810.1930.2252-0.00010.4660.0415-0.00860.4030.00220.5441-19.1824105.515822.0193
350.0980.0970.13360.15580.14460.17320.0902-0.0225-0.17150.1504-0.3547-0.39960.4466-0.3364-0.00230.9506-0.00740.00740.46180.00480.7076-25.471986.105221.0162
360.3227-0.0536-0.39940.10710.09530.49950.1879-0.35230.1159-0.8454-0.02230.66670.1528-1.0142-0.00180.7721-0.0462-0.06890.94690.03440.7831-35.030187.181617.3868
370.00730.0074-0.146-0.002-0.0312.5822-0.36970.08241.288-0.6495-0.11910.3059-0.27260.9422-0.04391.6068-0.1325-0.04360.70330.22511.5955-35.0446170.461735.2458
380.2028-0.0658-0.11590.02350.03790.06860.04320.25170.3343-0.2798-0.3167-0.31450.33450.59330.00031.1952-0.1232-0.0220.97430.25341.2788-30.8695163.070434.5129
390.1240.1308-0.00680.1297-0.02610.0554-0.0281-0.00170.5538-0.2637-0.387-0.0024-0.34650.1452-0.00591.0793-0.0427-0.12060.4514-0.02221.0634-40.4172164.982944.5901
400.53920.1991-0.13570.0853-0.15060.8824-0.0498-0.10840.01780.0657-0.15390.4393-0.4864-0.1154-0.04290.67380.1944-0.04840.2907-0.06360.6336-52.7372147.842140.4941
410.1963-0.081-0.00760.17710.04640.02310.50370.135-0.2701-0.517-0.1423-0.39220.2265-0.1764-0.00010.8095-0.05070.09070.36760.05980.4998-46.2811139.043533.7096
420.0305-0.02740.01250.043-0.01840.0073-0.0972-0.02540.2593-0.24920.02540.1214-0.04260.4016-0.00070.8525-0.0739-0.06510.59060.09850.6173-45.0903148.012432.0602
430.13090.1411-0.00080.3636-0.1110.0951-0.32190.41310.4997-0.26570.19930.1143-0.5998-0.0276-0.0011.3096-0.0764-0.07550.64820.19510.7777-44.2746154.261527.2091
440.02220.03930.06730.06410.12010.21690.00530.51220.2239-0.5294-0.05470.209-0.27270.7751-0.00831.3119-0.1517-0.16140.93760.31751.1426-42.4347160.424324.9349
450.1672-0.0744-0.09230.08310.12510.1960.5188-0.119-0.1336-0.2194-0.422-0.2841-0.06130.23040.01571.90310.0077-0.04270.95750.30951.1751-35.2279168.75221.6322
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 34 through 164 )
2X-RAY DIFFRACTION2chain 'A' and (resid 165 through 312 )
3X-RAY DIFFRACTION3chain 'A' and (resid 313 through 439 )
4X-RAY DIFFRACTION4chain 'A' and (resid 440 through 495 )
5X-RAY DIFFRACTION5chain 'B' and (resid 8 through 54 )
6X-RAY DIFFRACTION6chain 'B' and (resid 55 through 77 )
7X-RAY DIFFRACTION7chain 'B' and (resid 78 through 124 )
8X-RAY DIFFRACTION8chain 'B' and (resid 125 through 207 )
9X-RAY DIFFRACTION9chain 'B' and (resid 208 through 261 )
10X-RAY DIFFRACTION10chain 'B' and (resid 262 through 290 )
11X-RAY DIFFRACTION11chain 'B' and (resid 291 through 366 )
12X-RAY DIFFRACTION12chain 'B' and (resid 367 through 421 )
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 66 )
14X-RAY DIFFRACTION14chain 'C' and (resid 67 through 130 )
15X-RAY DIFFRACTION15chain 'C' and (resid 131 through 243 )
16X-RAY DIFFRACTION16chain 'D' and (resid 1 through 62 )
17X-RAY DIFFRACTION17chain 'D' and (resid 63 through 162 )
18X-RAY DIFFRACTION18chain 'D' and (resid 163 through 204 )
19X-RAY DIFFRACTION19chain 'D' and (resid 205 through 235 )
20X-RAY DIFFRACTION20chain 'E' and (resid 36 through 193 )
21X-RAY DIFFRACTION21chain 'E' and (resid 194 through 312 )
22X-RAY DIFFRACTION22chain 'E' and (resid 313 through 439 )
23X-RAY DIFFRACTION23chain 'E' and (resid 440 through 495 )
24X-RAY DIFFRACTION24chain 'F' and (resid 8 through 26 )
25X-RAY DIFFRACTION25chain 'F' and (resid 27 through 54 )
26X-RAY DIFFRACTION26chain 'F' and (resid 55 through 124 )
27X-RAY DIFFRACTION27chain 'F' and (resid 125 through 207 )
28X-RAY DIFFRACTION28chain 'F' and (resid 208 through 261 )
29X-RAY DIFFRACTION29chain 'F' and (resid 262 through 325 )
30X-RAY DIFFRACTION30chain 'F' and (resid 326 through 366 )
31X-RAY DIFFRACTION31chain 'F' and (resid 367 through 421 )
32X-RAY DIFFRACTION32chain 'G' and (resid 1 through 62 )
33X-RAY DIFFRACTION33chain 'G' and (resid 63 through 130 )
34X-RAY DIFFRACTION34chain 'G' and (resid 131 through 209 )
35X-RAY DIFFRACTION35chain 'G' and (resid 210 through 229 )
36X-RAY DIFFRACTION36chain 'G' and (resid 230 through 243 )
37X-RAY DIFFRACTION37chain 'H' and (resid 1 through 33 )
38X-RAY DIFFRACTION38chain 'H' and (resid 34 through 48 )
39X-RAY DIFFRACTION39chain 'H' and (resid 49 through 83 )
40X-RAY DIFFRACTION40chain 'H' and (resid 84 through 130 )
41X-RAY DIFFRACTION41chain 'H' and (resid 131 through 147 )
42X-RAY DIFFRACTION42chain 'H' and (resid 148 through 161 )
43X-RAY DIFFRACTION43chain 'H' and (resid 162 through 191 )
44X-RAY DIFFRACTION44chain 'H' and (resid 192 through 209 )
45X-RAY DIFFRACTION45chain 'H' and (resid 210 through 236 )

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