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- PDB-6nhh: Rhodobacter sphaeroides bc1 with azoxystrobin -

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Basic information

Entry
Database: PDB / ID: 6nhh
TitleRhodobacter sphaeroides bc1 with azoxystrobin
Components
  • Cytochrome b
  • Cytochrome c1
  • Ubiquinol-cytochrome c reductase iron-sulfur subunit
KeywordsOXIDOREDUCTASE / Mitochondrial respiratory chain complex / cytochrome bc1 / inhibitors / electron transfer
Function / homology
Function and homology information


respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 ...Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE / Chem-8SP / Chem-AZO / FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / STRONTIUM ION / : / : / : ...1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE / Chem-8SP / Chem-AZO / FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / STRONTIUM ION / : / : / : / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Cytochrome b / Cytochrome c1
Similarity search - Component
Biological speciesRhodobacter sphaeroides (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å
AuthorsXia, D. / Zhou, F. / Yu, C.A.
CitationJournal: J.Biol.Chem. / Year: 2019
Title: Crystal structure of bacterial cytochromebc1in complex with azoxystrobin reveals a conformational switch of the Rieske iron-sulfur protein subunit.
Authors: Esser, L. / Zhou, F. / Yu, C.A. / Xia, D.
History
DepositionDec 21, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 19, 2019Provider: repository / Type: Initial release
Revision 1.1Jun 26, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Aug 21, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome b
B: Cytochrome c1
C: Ubiquinol-cytochrome c reductase iron-sulfur subunit
E: Cytochrome b
F: Cytochrome c1
G: Ubiquinol-cytochrome c reductase iron-sulfur subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,76325
Polymers199,2106
Non-polymers7,55319
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area31530 Å2
ΔGint-386 kcal/mol
Surface area72000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.309, 154.655, 100.939
Angle α, β, γ (deg.)90.000, 95.360, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain E
12(chain B and resid 1 through 256)
22(chain F and resid 1 through 256)
13chain C
23chain G

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain AA3 - 2010
211chain EE3 - 2010
112(chain B and resid 1 through 256)B1 - 256
212(chain F and resid 1 through 256)F1 - 256
113chain CC13 - 1001
213chain GG13 - 1001

NCS ensembles :
ID
1
2
3

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Components

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Protein , 3 types, 6 molecules AEBFCG

#1: Protein Cytochrome b


Mass: 50087.422 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: Expressed as one natural part of a complex in the bacterium rhodobacter sphaeroides
Source: (natural) Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (bacteria)
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 / References: UniProt: A0A344Q9J3, UniProt: Q3IY10*PLUS
#2: Protein Cytochrome c1


Mass: 29589.158 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (bacteria)
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 / References: UniProt: A0A344Q9J2, UniProt: Q3IY11*PLUS
#3: Protein Ubiquinol-cytochrome c reductase iron-sulfur subunit


Mass: 19928.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (bacteria)
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
References: UniProt: A0A344Q9J4, UniProt: Q3IY09*PLUS, quinol-cytochrome-c reductase

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Sugars , 1 types, 2 molecules

#9: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 7 types, 17 molecules

#4: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical ChemComp-AZO / METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE / AZOXYSTROBIN


Mass: 403.387 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H17N3O5
#6: Chemical ChemComp-6PE / 1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE


Mass: 410.420 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H33NO8P
#7: Chemical ChemComp-8SP / O-[(R)-{[(2R)-2,3-bis(octanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine


Type: L-peptide linking / Mass: 511.543 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H42NO10P
#8: Chemical ChemComp-SR / STRONTIUM ION


Mass: 87.620 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Sr
#10: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#11: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2

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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: 3.5 Å3/Da / Density % sol: 64.86 % / Description: red plates
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 57 mg/ml protein incubated with 3.5 mM azoxystrobin (ChemService). Diluted with 50 mM Tris 7.5 pH, 200 mM NaCl, 200 mM Histidine, 0.5% b-OG, 10 % glycerol, 5 mM NaN3 and 1.25 mM NaAscorbate. ...Details: 57 mg/ml protein incubated with 3.5 mM azoxystrobin (ChemService). Diluted with 50 mM Tris 7.5 pH, 200 mM NaCl, 200 mM Histidine, 0.5% b-OG, 10 % glycerol, 5 mM NaN3 and 1.25 mM NaAscorbate. This solution is treated with 0.12-0.30% SMC and 5-8% PEG400 and 10 mM Sr(NO3)2
Temp details: constant

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 6, 2013
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 54693 / % possible obs: 100 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.198 / Rpim(I) all: 0.096 / Rrim(I) all: 0.197 / Χ2: 0.993 / Net I/σ(I): 4.4 / Num. measured all: 396134
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Num. unique obsCC1/2Rpim(I) allΧ2% possible allRmerge(I) obsRrim(I) all
3-3.076.836580.60.6860.943100
3.07-3.156.836080.7120.570.947100
3.15-3.236.936170.7280.4880.983100
3.23-3.33736410.8140.40.9711000.984
3.33-3.43736710.8520.341.0181000.8410.908
3.43-3.567.136070.9060.2591.0341000.6450.696
3.56-3.77.236440.950.1951.0271000.4860.524
3.7-3.877.236490.9720.1441.0351000.3610.389
3.87-4.077.336100.9830.1091.0461000.2740.295
4.07-4.337.436510.9890.0841.0241000.2140.23
4.33-4.667.436370.9920.0651.0221000.1670.179
4.66-5.137.636650.9950.0581.0041000.1490.16
5.13-5.877.636580.9930.0610.9891000.1560.168
5.87-7.397.736770.9960.0470.8941000.1210.13
7.39-507.637000.9990.020.96799.50.0510.055

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Processing

Software
NameVersionClassification
HKL-2000data reduction
SCALEPACKdata scaling
PHENIXdev_3339refinement
PDB_EXTRACT3.24data extraction
MOLREPphasing
RefinementResolution: 3→39.285 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 0.82 / Phase error: 30.58
RfactorNum. reflection% reflection
Rfree0.2816 1996 3.66 %
Rwork0.2639 --
obs0.2646 54537 99.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 235.11 Å2 / Biso mean: 73.7896 Å2 / Biso min: 6.55 Å2
Refinement stepCycle: final / Resolution: 3→39.285 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13436 0 911 0 14347
Biso mean--38.67 --
Num. residues----1722
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A4052X-RAY DIFFRACTION2.937TORSIONAL
12E4052X-RAY DIFFRACTION2.937TORSIONAL
21B2442X-RAY DIFFRACTION2.937TORSIONAL
22F2442X-RAY DIFFRACTION2.937TORSIONAL
31C1632X-RAY DIFFRACTION2.937TORSIONAL
32G1632X-RAY DIFFRACTION2.937TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.0001-3.07510.37081420.38283736387899
3.0751-3.15820.38611400.352337123852100
3.1582-3.25110.31011430.32237523895100
3.2511-3.3560.35131430.313537503893100
3.356-3.47580.29681420.298837363878100
3.4758-3.61490.28571430.280437453888100
3.6149-3.77930.30631410.267837423883100
3.7793-3.97840.25651420.233737183860100
3.9784-4.22740.24791430.225337783921100
4.2274-4.55330.2051430.22137623905100
4.5533-5.01070.27691430.208137583901100
5.0107-5.73390.30591420.234237553897100
5.7339-7.21670.28731430.258437803923100
7.2167-39.28860.25741460.276638173963100
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)
10.0162-0.02880.02560.0428-0.04150.0291-0.21430.1475-0.3857-0.1526-0.1944-0.81880.88730.422300.931-0.04480.18891.43590.3591.076936.38350.326621.1868
20.222-0.20710.0547-0.0307-0.31080.63550.0428-0.1325-0.1353-0.0139-0.09460.0247-0.11790.0189-0.05990.2704-0.0386-0.00430.66050.06840.4158.341.289738.6942
30.2119-0.0214-0.18090.74690.18780.17150.2006-0.3367-0.15640.2162-0.27280.0601-0.23230.1033-0.05370.4519-0.0649-0.03351.09930.14680.36517.72294.942760.3801
42.6785-0.9749-1.00660.6384-0.18311.3008-0.5506-0.1412-0.48540.1353-0.4253-0.2609-0.04250.7076-1.73110.38570.027-0.12721.51390.3470.734331.6535-7.71857.75
50.31730.07830.23760.2471-0.18160.43060.0577-0.03570.0166-0.03930.0603-0.05420.01850.14730.18290.49240.250.13440.58140.07160.1882-1.11866.974446.7473
60.28020.00660.01890.2599-0.1830.3953-0.181-0.2332-0.31480.07880.1012-0.38470.0646-0.4109-0.0120.4041-0.0922-0.10040.81450.12760.8198-22.2918-15.841334.3475
71.2138-0.11640.12311.50710.13670.7497-0.0787-0.0808-0.14750.05640.04340.2185-0.1012-0.3003-00.4234-0.0159-0.01421.2680.13720.6962-25.4822-7.657939.8694
80.02870.0434-0.06590.023-0.0990.21590.014-0.0530.1941-0.10030.1004-0.15950.2279-0.16130.00830.2885-0.02320.02240.80640.040.6118-8.9017-19.350133.1761
90.10160.1322-0.15390.76330.16110.39990.10080.3435-1.3137-0.30730.0350.28230.2035-0.02760.00010.6492-0.01940.0381.2441-0.02370.96343.3681-11.00817.1195
100.2996-0.2322-0.10980.15790.07710.029-0.42960.47770.9321-0.70610.29190.2183-0.40980.07230.33340.9017-0.2991-0.52580.62110.22790.8955-25.97244.0321-8.8664
110.02020.02270.00340.0253-0.01740.0243-0.2465-0.10990.37140.0386-0.1124-0.5744-0.46130.3681-00.7802-0.0249-0.1161.62130.35591.015736.001818.196336.7264
120.01310.0366-0.08930.0175-0.17380.30380.06150.0472-0.0224-0.0081-0.0949-0.0526-0.1504-0.09-0.01720.3634-0.00680.02030.67510.14850.388910.159124.976517.7606
13-0.0370.19860.00130.07870.02840.23220.09280.1044-0.074-0.0527-0.31580.32150.01370.1039-1.76770.2674-0.11350.03010.18190.22270.061815.65417.448413.8087
140.425-0.0142-0.23380.0506-0.1080.3843-0.00170.08980.1165-0.3837-0.10150.0624-0.0099-0.1581-0.07490.64470.02390.03161.17180.14160.43421.165316.7812-3.0126
150.14650.01970.13090.1645-0.13260.16560.0354-0.0098-0.0493-0.10630.01070.0347-0.02730.11380.12620.5472-0.03890.15930.73730.12230.351418.176719.3269-5.9608
160.20180.22190.10370.38220.14660.0652-0.0599-0.0997-0.0029-0.1839-0.3154-0.2248-0.0766-0.0415-1.47510.674-0.21310.40691.32750.24910.582939.210126.35470.0542
170.2826-0.0939-0.09370.0932-0.04370.12140.0623-0.01850.00620.0086-0.0286-0.00940.01940.01880.07370.715-0.1369-0.09690.68970.08330.09283.426716.00434.576
180.17720.15980.06420.37160.17320.1079-0.08130.06830.0221-0.02470.2907-0.2035-0.066-0.260.09610.6270.1045-0.08260.59450.22590.6076-16.765541.35913.0834
190.3680.0372-0.24080.09810.04960.2612-0.0144-0.14790.329-0.17860.0630.150.26340.14560.05120.62640.113-0.05810.88290.21760.5389-20.451235.90767.9187
200.1042-0.0016-0.27870.00180.0050.76640.14350.03640.22080.0550.0673-0.2102-0.1707-0.19090.04630.839-0.232-0.08110.38110.17220.793717.922441.957623.0096
210.05080.0392-0.02780.14350.03920.0202-0.42470.02640.24890.14950.2667-0.03210.262-0.01210.00330.52850.04290.00460.5754-0.12580.5744.478533.679934.698
221.2830.17180.81890.56840.18030.5280.0641-0.394-0.27020.48980.09110.28910.4168-0.2612-0.09240.73180.03890.25870.29180.06960.5501-31.490122.433253.897
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 33 )A3 - 33
2X-RAY DIFFRACTION2chain 'A' and (resid 34 through 295 or resseq 1001 or resseq 1002)A34 - 295
3X-RAY DIFFRACTION2chain 'A' and (resid 34 through 295 or resseq 1001 or resseq 1002)A1001
4X-RAY DIFFRACTION2chain 'A' and (resid 34 through 295 or resseq 1001 or resseq 1002)A1002
5X-RAY DIFFRACTION3chain 'A' and (resid 296 through 405 )A296 - 405
6X-RAY DIFFRACTION4chain 'A' and (resid 406 through 432 )A406 - 432
7X-RAY DIFFRACTION5chain 'A' and resid 1003A1003
8X-RAY DIFFRACTION6chain 'B' and (resid 1 through 46 )B1 - 46
9X-RAY DIFFRACTION7chain 'B' and (resid 47 through 183 )B47 - 183
10X-RAY DIFFRACTION8chain 'B' and (resid 184 through 256 )B184 - 256
11X-RAY DIFFRACTION9chain 'C' and (resid 13 through 51 )C13 - 51
12X-RAY DIFFRACTION10chain 'C' and (resid 52 through 187 or resid 1001)C52 - 187
13X-RAY DIFFRACTION10chain 'C' and (resid 52 through 187 or resid 1001)C1001
14X-RAY DIFFRACTION11chain 'E' and (resid 3 through 33 )E3 - 33
15X-RAY DIFFRACTION12chain 'E' and (resid 34 through 118 )E34 - 118
16X-RAY DIFFRACTION13chain 'E' and (resid 119 through 269 or resseq 1001 or resseq 1002)E119 - 269
17X-RAY DIFFRACTION13chain 'E' and (resid 119 through 269 or resseq 1001 or resseq 1002)E1001
18X-RAY DIFFRACTION13chain 'E' and (resid 119 through 269 or resseq 1001 or resseq 1002)E1002
19X-RAY DIFFRACTION14chain 'E' and (resid 270 through 327 )E270 - 327
20X-RAY DIFFRACTION15chain 'E' and (resid 328 through 405 )E328 - 405
21X-RAY DIFFRACTION16chain 'E' and (resid 406 through 432 )E406 - 432
22X-RAY DIFFRACTION17chain 'E' and resid 1003E1003
23X-RAY DIFFRACTION18chain 'F' and (resid 1 through 46 )F1 - 46
24X-RAY DIFFRACTION19chain 'F' and (resid 47 through 222 )F47 - 222
25X-RAY DIFFRACTION20chain 'F' and (resid 223 through 256 )F223 - 256
26X-RAY DIFFRACTION21chain 'G' and (resid 13 through 51 )G13 - 51
27X-RAY DIFFRACTION22chain 'G' and (resid 52 through 187 or resid 1001)G52 - 187
28X-RAY DIFFRACTION22chain 'G' and (resid 52 through 187 or resid 1001)G1001

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