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- PDB-5djq: The structure of CBB3 cytochrome oxidase. -

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Basic information

Entry
Database: PDB / ID: 5djq
TitleThe structure of CBB3 cytochrome oxidase.
Components
  • (Cbb3-type cytochrome c oxidase subunit ...) x 3
  • Putative uncharacterized protein
KeywordsOXIDOREDUCTASE / cbb3-cytochrome c oxidase / Pseudomonas_stutzeri
Function / homology
Function and homology information


aerobic respiration, using ferrous ions as electron donor / plasma membrane respirasome / plasma membrane respiratory chain complex IV / cytochrome complex / aerobic electron transport chain / cytochrome-c oxidase / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity ...aerobic respiration, using ferrous ions as electron donor / plasma membrane respirasome / plasma membrane respiratory chain complex IV / cytochrome complex / aerobic electron transport chain / cytochrome-c oxidase / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / respirasome / proton transmembrane transport / oxygen binding / electron transfer activity / iron ion binding / copper ion binding / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2250 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #130 / Cytochrome c oxidase, monohaem subunit/FixO / Cytochrome c oxidase cbb3-type, subunit I / Cytochrome c oxidase cbb3-type, subunit III / Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal / Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal domain superfamily / Cytochrome C oxidase, mono-heme subunit/FixO / N-terminal domain of cytochrome oxidase-cbb3, FixP / Cytochrome C Oxidase; Chain A ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2250 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #130 / Cytochrome c oxidase, monohaem subunit/FixO / Cytochrome c oxidase cbb3-type, subunit I / Cytochrome c oxidase cbb3-type, subunit III / Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal / Cbb3-type cytochrome c oxidase subunit CcoP, N-terminal domain superfamily / Cytochrome C oxidase, mono-heme subunit/FixO / N-terminal domain of cytochrome oxidase-cbb3, FixP / Cytochrome C Oxidase; Chain A / Cytochrome c oxidase-like, subunit I domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Cytochrome C oxidase, cbb3-type, subunit III / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Helix non-globular / Special / Up-down Bundle / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
COPPER (II) ION / HEXACYANOFERRATE(3-) / HEME C / PROTOPORPHYRIN IX CONTAINING FE / HYDROGEN PEROXIDE / PHOSPHATE ION / Cbb3-type cytochrome c oxidase subunit CcoN1 / Cbb3-type cytochrome c oxidase subunit II / Cbb3-type cytochrome c oxidase subunit CcoP1 / :
Similarity search - Component
Biological speciesPseudomonas stutzeri (bacteria)
Pseudomonas stutzeri ATCC 14405 = CCUG 16156 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.2 Å
AuthorsBuschmann, S. / Warkentin, E. / Xie, H. / Kohlstaedt, M. / Langer, J.D. / Ermler, U. / Michel, H.
Citation
Journal: Science / Year: 2010
Title: The structure of cbb3 cytochrome oxidase provides insights into proton pumping.
Authors: Buschmann, S. / Warkentin, E. / Xie, H. / Langer, J.D. / Ermler, U. / Michel, H.
#1: Journal: Mbio / Year: 2016
Title: Identification and Characterization of the Novel Subunit CcoM in the cbb33Cytochrome c Oxidase from Pseudomonas stutzeri ZoBell.
Authors: Kohlstaedt, M. / Buschmann, S. / Xie, H. / Resemann, A. / Warkentin, E. / Langer, J.D. / Michel, H.
History
DepositionSep 2, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jan 13, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2016Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cbb3-type cytochrome c oxidase subunit CcoN1
B: Cbb3-type cytochrome c oxidase subunit II
C: Cbb3-type cytochrome c oxidase subunit CcoP1
D: Cbb3-type cytochrome c oxidase subunit CcoN1
E: Cbb3-type cytochrome c oxidase subunit II
F: Cbb3-type cytochrome c oxidase subunit CcoP1
G: Cbb3-type cytochrome c oxidase subunit CcoN1
H: Cbb3-type cytochrome c oxidase subunit II
I: Cbb3-type cytochrome c oxidase subunit CcoP1
K: Cbb3-type cytochrome c oxidase subunit CcoN1
L: Cbb3-type cytochrome c oxidase subunit II
M: Cbb3-type cytochrome c oxidase subunit CcoP1
N: Putative uncharacterized protein
O: Putative uncharacterized protein
P: Putative uncharacterized protein
Q: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)467,59860
Polymers453,30616
Non-polymers14,29244
Water0
1
A: Cbb3-type cytochrome c oxidase subunit CcoN1
B: Cbb3-type cytochrome c oxidase subunit II
C: Cbb3-type cytochrome c oxidase subunit CcoP1
N: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,90015
Polymers113,3274
Non-polymers3,57311
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23800 Å2
ΔGint-310 kcal/mol
Surface area34060 Å2
MethodPISA
2
D: Cbb3-type cytochrome c oxidase subunit CcoN1
E: Cbb3-type cytochrome c oxidase subunit II
F: Cbb3-type cytochrome c oxidase subunit CcoP1
O: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,90015
Polymers113,3274
Non-polymers3,57311
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23930 Å2
ΔGint-311 kcal/mol
Surface area33910 Å2
MethodPISA
3
G: Cbb3-type cytochrome c oxidase subunit CcoN1
H: Cbb3-type cytochrome c oxidase subunit II
I: Cbb3-type cytochrome c oxidase subunit CcoP1
P: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,90015
Polymers113,3274
Non-polymers3,57311
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23760 Å2
ΔGint-309 kcal/mol
Surface area33950 Å2
MethodPISA
4
K: Cbb3-type cytochrome c oxidase subunit CcoN1
L: Cbb3-type cytochrome c oxidase subunit II
M: Cbb3-type cytochrome c oxidase subunit CcoP1
Q: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,90015
Polymers113,3274
Non-polymers3,57311
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23570 Å2
ΔGint-307 kcal/mol
Surface area34310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.475, 279.933, 175.192
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

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Cbb3-type cytochrome c oxidase subunit ... , 3 types, 12 molecules ADGKBEHLCFIM

#1: Protein
Cbb3-type cytochrome c oxidase subunit CcoN1 / Cytochrome CBB3 subunit CcoN1


Mass: 52829.637 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Pseudomonas stutzeri (bacteria) / References: UniProt: D9IA43, cytochrome-c oxidase
#2: Protein
Cbb3-type cytochrome c oxidase subunit II / Cytochrome c oxidase / cbb3-type / subunit O


Mass: 22842.102 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Pseudomonas stutzeri (bacteria) / References: UniProt: D9IA44
#3: Protein
Cbb3-type cytochrome c oxidase subunit CcoP1 / Cbb3-Cox subunit CcoP1 / C-type cytochrome CcoP1 / Cyt c(P1) / Cytochrome c oxidase subunit III


Mass: 33691.051 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Pseudomonas stutzeri (bacteria) / References: UniProt: D9IA45

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Protein/peptide , 1 types, 4 molecules NOPQ

#4: Protein/peptide
Putative uncharacterized protein


Mass: 3963.710 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Pseudomonas stutzeri ATCC 14405 = CCUG 16156 (bacteria)
References: UniProt: H7ESS5

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Non-polymers , 7 types, 44 molecules

#5: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#6: Chemical
ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cu
#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca
#8: Chemical
ChemComp-PEO / HYDROGEN PEROXIDE / Hydrogen peroxide


Mass: 34.015 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: H2O2
#9: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#10: Chemical
ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#11: Chemical
ChemComp-FC6 / HEXACYANOFERRATE(3-) / FERRI(III)HEXACYANIDE


Mass: 211.949 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6FeN6

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.74 Å3/Da / Density % sol: 67.09 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 20mM TRIS(HCL), 0.1 M NACL, 0.058% ALPHA-UDM, 0.0125% DECANOYLSUCROSE, 0.018% ALPHA-DDM, 0.016 M K3FE(CN)6,

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9918 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 6, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9918 Å / Relative weight: 1
ReflectionResolution: 3.2→14.982 Å / Num. obs: 108344 / % possible obs: 98.51 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.162 / Rsym value: 0.111 / Net I/σ(I): 11.4
Reflection shellResolution: 3.2→3.3 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.83 / Mean I/σ(I) obs: 2.4 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
Cootmodel building
Omodel building
XDSdata reduction
XSCALEdata scaling
SHARPphasing
RefinementResolution: 3.2→14.982 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 20.94 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2228 5480 5.06 %
Rwork0.187 --
obs0.1888 108344 98.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.2→14.982 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms31022 0 952 0 31974
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00933102
X-RAY DIFFRACTIONf_angle_d2.35545404
X-RAY DIFFRACTIONf_dihedral_angle_d17.37611306
X-RAY DIFFRACTIONf_chiral_restr0.0694723
X-RAY DIFFRACTIONf_plane_restr0.0115531
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.2360.28791800.26583462X-RAY DIFFRACTION100
3.236-3.27370.35531730.26633467X-RAY DIFFRACTION100
3.2737-3.31320.31821940.27463421X-RAY DIFFRACTION100
3.3132-3.35470.27972000.25813416X-RAY DIFFRACTION100
3.3547-3.39830.2652220.24353408X-RAY DIFFRACTION100
3.3983-3.44430.25931950.22673429X-RAY DIFFRACTION100
3.4443-3.49290.25531570.22043473X-RAY DIFFRACTION100
3.4929-3.54440.24421800.21493456X-RAY DIFFRACTION100
3.5444-3.5990.27181680.23273445X-RAY DIFFRACTION100
3.599-3.65720.30921660.23153438X-RAY DIFFRACTION99
3.6572-3.71930.26021690.21313468X-RAY DIFFRACTION100
3.7193-3.78580.2441880.20193421X-RAY DIFFRACTION100
3.7858-3.85740.23481980.20173398X-RAY DIFFRACTION99
3.8574-3.93480.22781800.1923472X-RAY DIFFRACTION99
3.9348-4.01870.2071740.18143450X-RAY DIFFRACTION99
4.0187-4.11030.21821770.17713454X-RAY DIFFRACTION99
4.1103-4.21090.18981650.17783445X-RAY DIFFRACTION99
4.2109-4.32210.22211740.17463424X-RAY DIFFRACTION99
4.3221-4.44610.2161960.17123432X-RAY DIFFRACTION99
4.4461-4.58560.20471680.17043462X-RAY DIFFRACTION99
4.5856-4.74450.21611780.16573415X-RAY DIFFRACTION98
4.7445-4.9280.18991730.16493439X-RAY DIFFRACTION98
4.928-5.14360.20521850.1693421X-RAY DIFFRACTION98
5.1436-5.40260.21861940.16923393X-RAY DIFFRACTION98
5.4026-5.72330.19971860.17513396X-RAY DIFFRACTION97
5.7233-6.13690.21441740.1723414X-RAY DIFFRACTION97
6.1369-6.70370.2271870.17723403X-RAY DIFFRACTION96
6.7037-7.56260.18251820.16413387X-RAY DIFFRACTION96
7.5626-9.15170.18812130.15693365X-RAY DIFFRACTION95
9.1517-14.98260.21671840.18513390X-RAY DIFFRACTION93
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)
12.66220.04141.03622.40830.51654.136-0.206-0.24020.27270.41380.0528-0.3745-0.40221.07610.10120.6364-0.0067-0.09870.78390.010.456113.1434123.2107174.4293
21.98330.55790.98342.06490.23593.8099-0.0978-0.65940.09580.6510.059-0.142-0.0380.35830.07870.79060.2357-0.00250.83860.02440.3831102.0659116.2355187.4328
32.45310.69220.59913.58891.77614.3516-0.2596-0.28270.49440.32980.04530.3188-0.5544-0.02810.2640.63150.20720.01770.4926-0.00050.439492.262126.0368177.4889
41.68340.12321.02841.2672-0.01763.8986-0.1366-0.1445-0.22760.29870.1695-0.30420.67310.7712-0.14790.72820.27060.04140.71360.08520.5727106.0528102.9001165.6839
56.1569-1.11380.52274.21620.41184.5281-0.09960.4656-0.119-0.25950.1605-0.38490.18060.78810.00120.52530.0810.01880.6048-0.00030.3219103.2625108.5726147.344
61.9779-0.14320.74411.54860.02033.474-0.1871-0.5487-0.10450.91870.1971-0.05820.82990.5205-0.18551.37130.4359-0.02331.10790.20040.6769105.626998.5877191.2732
71.6681-0.44190.63642.9023-2.31738.02780.0378-0.1379-0.22350.09310.02850.25810.1648-0.3274-0.11640.3998-0.03510.06620.4568-0.0920.532977.244101.9561137.4029
82.94341.8346-0.53953.1425-2.95524.99110.2334-0.936-0.97511.9272-0.4477-0.13760.1952-0.1820.15221.85820.04090.26661.08660.49241.3859101.489249.0166154.4506
91.06151.35320.61934.4842-2.29483.8895-0.5181-0.4244-1.20410.00410.43770.91311.2329-0.81650.01441.6218-0.17310.44480.96450.34621.992691.07737.9007144.0738
104.62622.8384-1.28096.3826-4.77623.7873-0.33370.25430.09690.32881.172.14350.3863-1.4345-0.81240.9417-0.00090.13990.86950.42961.826885.928553.882141.0939
111.45660.07361.41253.5034-0.34451.3737-0.5012-0.1656-1.5326-0.5376-0.0404-1.73040.92990.61040.57931.2580.31050.39270.91950.18961.8957113.812846.5815135.3211
126.5098-4.36351.10155.4368-2.4313.7745-0.3286-0.1028-0.89280.3713-0.4077-1.47950.30150.96570.43460.79440.11490.01870.99440.2471.4832119.918664.9371133.688
131.5061-1.39820.45594.0406-0.4714.6974-0.70260.0726-1.8486-1.2207-0.1055-0.58282.1392-0.37030.3122.315-0.14680.77381.03820.0522.8366100.613724.1128136.3276
142.4067-0.0583-0.0083.0708-1.88222.6061-0.35090.6781-0.3574-1.42350.1705-0.68531.02-0.50340.19991.3004-0.18310.26731.1846-0.06120.7553114.816776.5301108.5198
151.9479-0.0571-0.24581.3627-1.0985.24170.17820.28380.2557-0.2972-0.164-0.0841-1.18490.2353-0.01541.14680.11120.02530.75560.03470.4199104.8445117.354975.4612
160.76980.86920.4391.5439-0.68484.55890.03950.9177-0.0273-0.7369-0.06320.0131-0.113-0.53670.03121.0890.2651-0.10031.226-0.14080.445196.1883104.822865.093
172.85160.2914-2.22231.6879-0.93856.1041-0.24360.3949-0.3668-0.3499-0.1369-0.28310.7940.41970.50770.86110.22430.04080.8049-0.16660.5345107.39196.304574.6756
180.77160.41480.19941.4786-1.56896.05710.16970.40480.2454-0.1795-0.17090.5159-0.6365-1.2377-0.12950.86560.2913-0.03390.8941-0.04830.594186.1228111.813987.8146
193.9912-0.8622-1.04523.8233-0.01134.90310.26870.00740.20760.2992-0.23780.0729-0.96890.0996-0.08491.07320.03810.01680.6206-0.09040.414994.3597111.4143105.3577
201.18390.4022-0.78191.7638-1.07914.09220.05031.27730.1179-0.49020.21470.4968-0.2042-2.1045-0.28691.28820.3605-0.22422.296-0.14740.899878.1252108.109863.4656
214.04460.24122.08091.35580.26627.0889-0.19080.1326-0.6057-0.19830.06930.06660.4718-0.1281-0.00630.80860.01610.17570.4134-0.08540.668789.753487.2612119.5089
220.9884-0.2329-0.17350.6424-0.78211.339-0.41620.869-0.1382-0.9026-0.74331.63310.2944-1.6632-0.75360.5942-0.3199-0.9721.7112-1.58041.97932.8504105.7126110.7925
230.36110.04890.52270.11960.09041.20560.0687-0.1115-0.5135-0.3273-0.43571.2271.0022-1.3306-0.38220.6157-1.20460.10392.0012-1.57222.691626.283295.1883124.4555
242.63350.53570.86463.0124-0.20620.30240.34020.2909-0.53970.2141-0.59470.62721.2315-0.80960.26840.9485-0.360.22691.0346-0.48481.481443.068492.3108123.7072
251.61890.47510.15321.0871-1.08411.2747-0.01420.10520.1254-0.1853-0.68061.7729-0.2717-1.37930.2130.61420.1408-0.221.5423-0.77531.891433.4654119.5809129.268
266.3874-1.57830.29131.83010.28022.7618-0.31090.46330.5083-0.7309-0.48370.7203-0.8875-0.5010.5090.82380.0732-0.3670.6878-0.23140.975250.5704128.1412125.8046
271.30730.49351.07380.25890.17161.43990.21370.028-0.28830.0133-0.76051.04260.4688-1.57160.24311.1556-0.46140.28212.578-1.07352.744413.4876103.5854134.7798
286.93031.0767-2.13363.1499-0.13033.40250.0277-0.2814-0.19950.2079-0.12730.26420.1728-0.08680.11060.52050.0167-0.06340.31860.02570.398268.5999126.7512147.8156
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 211 )
2X-RAY DIFFRACTION2chain 'A' and ((resid 212 through 370 ) or (resid 501 through 502) )
3X-RAY DIFFRACTION3chain 'A' and (resid 371 through 470 )
4X-RAY DIFFRACTION4chain 'B' and ((resid 6 through 114 ) or resid 211 )
5X-RAY DIFFRACTION5chain 'B' and (resid 115 through 202 )
6X-RAY DIFFRACTION6chain 'C' and (resid 1 through 106 )
7X-RAY DIFFRACTION7chain 'C' and (resid 107 through 303 )
8X-RAY DIFFRACTION8chain 'D' and (resid 8 through 211 )
9X-RAY DIFFRACTION9chain 'D' and ((resid 212 through 370 ) or (resid 501 through 502) )
10X-RAY DIFFRACTION10chain 'D' and (resid 371 through 470 )
11X-RAY DIFFRACTION11chain 'E' and ((resid 6 through 114 ) or resid 211 )
12X-RAY DIFFRACTION12chain 'E' and (resid 115 through 202 )
13X-RAY DIFFRACTION13chain 'F' and (resid 1 through 106 )
14X-RAY DIFFRACTION14chain 'F' and (resid 107 through 303 )
15X-RAY DIFFRACTION15chain 'G' and (resid 6 through 211 )
16X-RAY DIFFRACTION16chain 'G' and ((resid 212 through 370 ) or (resid 501 through 502) )
17X-RAY DIFFRACTION17chain 'G' and (resid 371 through 470 )
18X-RAY DIFFRACTION18chain 'H' and ((resid 6 through 114 ) or resid 211 )
19X-RAY DIFFRACTION19chain 'H' and (resid 115 through 202 )
20X-RAY DIFFRACTION20chain 'I' and (resid 1 through 106 )
21X-RAY DIFFRACTION21chain 'I' and (resid 107 through 303 )
22X-RAY DIFFRACTION22chain 'K' and (resid 6 through 211 )
23X-RAY DIFFRACTION23chain 'K' and ((resid 212 through 370 ) or (resid 501 through 502) )
24X-RAY DIFFRACTION24chain 'K' and (resid 371 through 470 )
25X-RAY DIFFRACTION25chain 'L' and ((resid 6 through 114 ) or resid 211 )
26X-RAY DIFFRACTION26chain 'L' and (resid 115 through 202 )
27X-RAY DIFFRACTION27chain 'M' and (resid 1 through 106 )
28X-RAY DIFFRACTION28chain 'M' and (resid 107 through 303 )

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