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- PDB-7c8z: Crystal structure of salicylate 5-hydroxylase NagGH (a Rieske non... -

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Basic information

Entry
Database: PDB / ID: 7c8z
TitleCrystal structure of salicylate 5-hydroxylase NagGH (a Rieske non-heme iron-dependent monooxgenase)
Components
  • Salicylate 5-hydroxylase, large oxygenase component
  • Salicylate 5-hydroxylase, small oxygenase component
KeywordsOXIDOREDUCTASE / salicylate 5-hydroxylase / Rieske non-heme iron-dependent oxygenase / iron-sulfur cluster / non-heme iron
Function / homology
Function and homology information


salicylate 5-hydroxylase / salicylate 5-hydroxylase (NADH) activity / salicylic acid catabolic process / catalytic complex / 2 iron, 2 sulfur cluster binding / iron ion binding
Similarity search - Function
Ring-hydroxylating dioxygenase, large/alpha subunit AhdA1c-like, C-terminal / SnoaL-like domain / Ring-hydroxylating dioxygenase beta subunit / Aromatic-ring-hydroxylating dioxygenase, alpha subunit / Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain / Ring hydroxylating alpha subunit (catalytic domain) / Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site / Bacterial ring hydroxylating dioxygenases alpha-subunit signature. / SnoaL-like domain / Rieske [2Fe-2S] domain ...Ring-hydroxylating dioxygenase, large/alpha subunit AhdA1c-like, C-terminal / SnoaL-like domain / Ring-hydroxylating dioxygenase beta subunit / Aromatic-ring-hydroxylating dioxygenase, alpha subunit / Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain / Ring hydroxylating alpha subunit (catalytic domain) / Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site / Bacterial ring hydroxylating dioxygenases alpha-subunit signature. / SnoaL-like domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / NTF2-like domain superfamily
Similarity search - Domain/homology
: / FE2/S2 (INORGANIC) CLUSTER / Salicylate 5-hydroxylase, large oxygenase component / Salicylate 5-hydroxylase, small oxygenase component
Similarity search - Component
Biological speciesRalstonia sp. (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsLi, D.F. / Hou, Y.J.
CitationJournal: Appl.Environ.Microbiol. / Year: 2021
Title: Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases.
Authors: Hou, Y.J. / Guo, Y. / Li, D.F. / Zhou, N.Y.
History
DepositionJun 4, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 6, 2021Provider: repository / Type: Initial release
Revision 1.1Jul 21, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Nov 29, 2023Group: 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Salicylate 5-hydroxylase, large oxygenase component
C: Salicylate 5-hydroxylase, large oxygenase component
E: Salicylate 5-hydroxylase, large oxygenase component
G: Salicylate 5-hydroxylase, large oxygenase component
B: Salicylate 5-hydroxylase, small oxygenase component
D: Salicylate 5-hydroxylase, small oxygenase component
F: Salicylate 5-hydroxylase, small oxygenase component
H: Salicylate 5-hydroxylase, small oxygenase component
hetero molecules


Theoretical massNumber of molelcules
Total (without water)280,06216
Polymers279,1358
Non-polymers9278
Water5,873326
1
A: Salicylate 5-hydroxylase, large oxygenase component
C: Salicylate 5-hydroxylase, large oxygenase component
E: Salicylate 5-hydroxylase, large oxygenase component
B: Salicylate 5-hydroxylase, small oxygenase component
D: Salicylate 5-hydroxylase, small oxygenase component
F: Salicylate 5-hydroxylase, small oxygenase component
hetero molecules


Theoretical massNumber of molelcules
Total (without water)210,04612
Polymers209,3516
Non-polymers6956
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area28270 Å2
ΔGint-208 kcal/mol
Surface area53270 Å2
MethodPISA
2
G: Salicylate 5-hydroxylase, large oxygenase component
H: Salicylate 5-hydroxylase, small oxygenase component
hetero molecules

G: Salicylate 5-hydroxylase, large oxygenase component
H: Salicylate 5-hydroxylase, small oxygenase component
hetero molecules

G: Salicylate 5-hydroxylase, large oxygenase component
H: Salicylate 5-hydroxylase, small oxygenase component
hetero molecules


Theoretical massNumber of molelcules
Total (without water)210,04612
Polymers209,3516
Non-polymers6956
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area28450 Å2
ΔGint-210 kcal/mol
Surface area53180 Å2
MethodPISA
Unit cell
Length a, b, c (Å)188.156, 188.156, 147.586
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63
Components on special symmetry positions
IDModelComponents
11H-227-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain C
31chain E
41chain G
12chain B
22chain D
32chain F
42chain H

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PROPROGLUGLUchain AAA9 - 42328 - 442
21PROPROGLUGLUchain CCB9 - 42328 - 442
31PROPROGLUGLUchain EEC9 - 42328 - 442
41PROPROGLUGLUchain GGD9 - 42328 - 442
12METMETILEILEchain BBE1 - 1611 - 161
22METMETILEILEchain DDF1 - 1611 - 161
32METMETILEILEchain FFG1 - 1611 - 161
42METMETILEILEchain HHH1 - 1611 - 161

NCS ensembles :
ID
1
2

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Components

#1: Protein
Salicylate 5-hydroxylase, large oxygenase component / S5H large oxygenase component / Salicylate 5-hydroxylase / oxygenase component NagG / Salicylate 5- ...S5H large oxygenase component / Salicylate 5-hydroxylase / oxygenase component NagG / Salicylate 5-monooxygenase / hydroxylase large subunit


Mass: 50949.426 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Ralstonia sp. (bacteria) / Gene: nagG / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O52379, salicylate 5-hydroxylase
#2: Protein
Salicylate 5-hydroxylase, small oxygenase component / S5H small oxygenase component / Salicylate 5-hydroxylase / oxygenase component NagH / Salicylate 5- ...S5H small oxygenase component / Salicylate 5-hydroxylase / oxygenase component NagH / Salicylate 5-monooxygenase / hydroxylase small subunit


Mass: 18834.398 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Ralstonia sp. (bacteria) / Gene: nagH / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O52380, salicylate 5-hydroxylase
#3: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe2S2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 326 / 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: 2.7 Å3/Da / Density % sol: 58.82 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 2% tascimate, 0.1M imidazole, pH 7.0 and 10% (w/v) PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 9, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→47.3 Å / Num. obs: 91061 / % possible obs: 100 % / Redundancy: 6.4 % / CC1/2: 0.994 / Rmerge(I) obs: 0.156 / Rpim(I) all: 0.067 / Rrim(I) all: 0.17 / Net I/σ(I): 12.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.6-2.646.40.94345150.4210.4041.027100
14.24-47.35.20.0325660.9980.0150.03596.2

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
XDSdata reduction
Aimless0.7.3data scaling
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5AEU

5aeu


Resolution: 2.6→47.28 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 23.82 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2375 1969 2.21 %
Rwork0.1923 87118 -
obs0.1933 89087 97.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 146.05 Å2 / Biso mean: 51.0469 Å2 / Biso min: 14.33 Å2
Refinement stepCycle: final / Resolution: 2.6→47.28 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17804 0 20 326 18150
Biso mean--50.39 43.73 -
Num. residues----2176
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A4664X-RAY DIFFRACTION2.358TORSIONAL
12C4664X-RAY DIFFRACTION2.358TORSIONAL
13E4664X-RAY DIFFRACTION2.358TORSIONAL
14G4664X-RAY DIFFRACTION2.358TORSIONAL
21B1968X-RAY DIFFRACTION2.358TORSIONAL
22D1968X-RAY DIFFRACTION2.358TORSIONAL
23F1968X-RAY DIFFRACTION2.358TORSIONAL
24H1968X-RAY DIFFRACTION2.358TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.6-2.6650.33111320.2901593794
2.665-2.73710.35581320.2806599395
2.7371-2.81760.29421420.2624604995
2.8176-2.90860.29171390.2433610196
2.9086-3.01250.29361410.2381611597
3.0125-3.13310.26561440.2167625098
3.1331-3.27560.21421370.2075626299
3.2756-3.44830.29081420.1981622699
3.4483-3.66430.22821390.1849633099
3.6643-3.94710.21961430.16856309100
3.9471-4.3440.21811420.1543634699
4.344-4.9720.17141450.14316360100
4.972-6.26190.22061440.17926393100
6.2619-47.30.22061470.19086447100
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)
10.9249-0.3155-0.31360.46490.241.066-0.069-0.1947-0.21050.44010.03490.3064-0.0798-0.31950.01540.22830.19510.1130.47550.06570.238736.552640.826672.6186
20.76660.25150.70030.66320.26930.8607-0.1649-0.14020.05750.0040.18670.2218-0.3144-0.40320.04290.38440.23450.04120.53110.01710.39626.784155.101157.2564
31.00910.5939-0.19550.82160.45710.7579-0.0353-0.6417-0.29760.63240.1694-0.0257-0.1742-0.2010.18260.48910.33140.13050.50990.02130.127648.390545.784581.7336
41.0538-0.1642-0.45691.0278-0.25791.7001-0.1479-0.3507-0.05680.31190.2083-0.0067-0.1098-0.02510.02530.39230.17060.0690.47910.05740.190450.452242.261982.5552
50.52370.16550.41510.5082-0.06761.1343-0.21990.0843-0.6696-0.09280.31280.59130.8702-0.52110.09090.6706-0.18170.11610.54120.08180.879633.89536.652551.0555
60.8671-0.1045-0.36650.36070.12680.5792-0.253-0.4436-0.29550.38690.19050.02430.389-0.14180.01340.47310.0740.17170.3320.1870.453558.358813.725373.1065
71.8616-0.8898-0.73941.93460.38991.5452-0.2876-0.4130.05650.72760.1677-0.13660.273-0.07410.09240.85950.21230.08540.67320.20960.410755.992122.432995.294
80.2163-0.16690.28180.4471-0.42110.5091-0.1133-0.3265-0.50140.07720.1245-0.04230.3436-0.12-0.08540.60140.14270.20450.0920.17430.630761.33631.257466.5821
90.2182-0.09370.22270.855-0.11450.2130.3170.3562-0.394-0.38030.2124-0.17980.37680.15850.10470.6035-0.01620.07920.4238-0.0890.621654.83954.126745.691
100.7241-0.15220.14780.17760.15670.8057-0.12730.3135-0.2957-0.16260.2011-0.02570.42890.09530.07580.6346-0.02310.16070.2888-0.02290.753264.4898-2.814750.9258
111.1222-0.2799-0.17840.5760.60560.8122-0.1488-0.1193-0.3450.03660.1120.1270.30470.02230.02230.45670.00690.08550.2280.04070.519963.34249.586851.3231
120.3817-0.2780.30080.3126-0.15180.23750.1980.1076-0.4313-0.063-0.02250.36910.8255-0.39250.05990.7662-0.19190.11140.4504-0.00460.815843.1791-2.843249.5748
130.4233-0.51770.36491.87280.01771.03890.2595-0.45490.11440.0961-0.02010.78780.196-0.55590.02750.37450.03910.09920.74670.07510.568420.969235.408956.5542
140.5402-0.0155-0.05630.65610.18310.5191-0.10110.0449-0.3388-0.12890.04250.33180.3955-0.25850.11210.3901-0.10750.00340.4757-0.05690.455134.965822.596432.7705
150.4257-0.17920.37271.0366-0.04310.76540.0710.0802-0.6031-0.2112-0.21740.13870.7336-0.10420.05460.7756-0.16090.07590.4798-0.09810.763345.75253.395632.918
160.6407-0.55080.2330.8569-0.13940.42040.08720.3701-0.2867-0.2671-0.02420.47110.1992-0.60260.03970.3706-0.0627-0.06220.6704-0.02220.520527.195826.811125.5321
170.5635-0.12070.18220.1965-0.25380.3090.0555-0.01450.20190.09240.09260.1053-0.2742-0.29850.02430.26480.02460.03630.3872-0.00110.363334.752943.123937.4969
181.03950.1541-0.05990.4806-0.00020.5347-0.22680.0156-0.0452-0.21720.12350.0931-0.114-0.18560.03630.4078-0.0409-0.06250.69730.04840.56527.150546.015730.205
190.49120.2556-0.46191.3422-0.77760.9218-0.07930.19830.0399-0.06180.08880.0214-0.0991-0.38910.03230.3657-0.0334-0.10640.60320.08980.429331.575144.849925.2013
200.75740.0474-0.09680.7666-0.52570.9071-0.11210.2726-0.0936-0.02990.0360.0278-0.0053-0.32520.02080.21420.0425-0.01970.40550.03660.330139.462941.994434.2918
210.418-0.1480.49650.83360.22050.7967-0.0542-0.1863-0.08610.33490.15230.6546-0.079-0.7870.07740.22750.07020.00390.7020.07330.461218.202741.197444.9307
221.1365-0.0854-0.31260.36910.24591.0322-0.24130.5948-0.0786-0.55210.1687-0.12670.437-0.10280.03270.7170.05430.05920.5616-0.12040.29694.016288.175644.6057
230.6646-0.61010.59580.5889-0.47190.75070.04170.1471-0.2344-0.2899-0.04930.17060.6062-0.4723-0.00410.645-0.0889-0.03040.5516-0.09340.3796-16.167486.428554.5058
241.6884-0.14540.08691.00130.14510.8173-0.01040.1257-0.4993-0.2029-0.04510.39470.5136-0.56250.00990.7787-0.1651-0.05270.7708-0.18630.4145-21.834180.031845.7376
250.8872-0.1867-0.38541.0369-0.24971.0037-0.25670.35740.0573-0.3231-0.243-0.35430.42940.6976-0.28580.70890.29630.27690.4283-0.17370.11715.707382.717756.1382
260.7585-0.15270.08130.77040.17760.0705-0.06720.7108-0.008-0.29130.0025-0.2460.21940.3555-0.05910.93090.26270.28530.79-0.07110.362622.968190.372438.8525
271.47650.0587-0.35420.68520.5591.0247-0.0525-0.336-0.13120.16010.0486-0.0796-0.00540.1363-0.02860.27670.0516-0.00490.28980.03480.226372.581845.863864.1011
281.11240.4744-0.55081.4782-0.78060.4872-0.0487-0.11610.03760.25590.0388-0.1492-0.0901-0.1-0.0310.2059-0.01290.00170.19570.020.171774.571350.714153.9076
291.48530.708-0.6372.9872-0.66490.89450.1411-0.2896-0.07520.5367-0.17170.03710.0570.30680.01890.28840.0510.06370.21170.05870.184968.145342.162757.0687
301.04190.5466-0.16720.69570.05990.528-0.0311-0.1207-0.08630.0360.09360.022-0.1329-0.0676-0.01370.22890.02560.01520.25060.03510.222168.771246.704360.5026
311.21130.6383-0.15511.7899-0.2780.5573-0.02180.2542-0.0505-0.27710.1221-0.04640.04310.1612-0.03860.1833-0.0080.02320.2694-0.030.246976.951234.033436.8885
321.2459-0.1195-0.44340.6905-0.32850.4793-0.06780.0697-0.4699-0.12190.15350.09050.472-0.07020.0080.3259-0.03620.05340.1531-0.08830.363772.953417.890243.6768
331.95730.30610.53040.2301-0.07780.8103-0.06650.2214-0.6182-0.34710.0003-0.3260.25690.0739-0.05850.22540.0950.10050.1703-0.03380.330678.871633.024244.4893
340.9617-0.1564-0.17760.7566-0.22190.7281-0.01550.046-0.13410.0180.0536-0.0140.1862-0.00110.00630.2068-0.01780.06620.1835-0.01740.208471.699928.10945.3101
351.39360.51920.03810.8304-0.27981.11080.02130.08450.2746-0.03450.03150.1569-0.2104-0.1178-0.00360.2130.05190.01690.18610.02060.242558.529351.547536.2294
361.3601-0.0822-1.13070.08540.24691.6074-0.03010.47170.2843-0.09680.01530.0595-0.246-0.3532-0.17660.24160.01310.00180.22280.03530.170967.721347.471835.7777
371.1554-0.02550.18560.7926-0.39030.8443-0.06970.020.1671-0.09590.12590.1052-0.1147-0.1923-0.02530.20670.01960.01190.1816-0.0060.255959.712245.853438.8557
380.8279-0.352-0.36370.88570.35781.3875-0.1838-0.2958-0.0809-0.089-0.023-0.05160.02060.5678-0.01090.24060.0029-0.01380.28860.02020.229811.8246103.692587.3344
390.51070.11430.310.92140.0741.7199-0.09330.3834-0.3767-0.080.4119-0.12690.29330.1015-0.05260.3040.05530.03160.4004-0.02530.2248.456889.268278.0798
400.71730.0268-0.05081.2722-0.46331.2286-0.13970.1551-0.2909-0.3999-0.0253-0.44990.3640.5588-0.01060.37610.1010.08950.37320.01060.30918.882492.712972.7251
410.66380.6179-1.06371.0708-0.60162.56260.2591-0.1661-0.04910.0212-0.2129-0.09740.27390.76830.11670.2440.0487-0.02090.27650.02330.22415.925498.545286.0103
421.15240.1868-0.42161.3985-0.54332.6244-0.05070.07260.0282-0.1971-0.14410.0390.05250.13150.02610.2448-0.02620.0520.2260.01330.19157.1599103.006875.793
430.5739-0.1636-0.16450.6053-0.4071.3277-0.0188-0.0573-0.0949-0.054-0.1158-0.04090.2121-0.120.00920.24180.02720.01670.199-0.0010.16688.791596.675778.3847
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 88 )A9 - 88
2X-RAY DIFFRACTION2chain 'A' and (resid 89 through 176 )A89 - 176
3X-RAY DIFFRACTION3chain 'A' and (resid 177 through 243 )A177 - 243
4X-RAY DIFFRACTION4chain 'A' and (resid 244 through 423 )A244 - 423
5X-RAY DIFFRACTION5chain 'C' and (resid 9 through 32 )C9 - 32
6X-RAY DIFFRACTION6chain 'C' and (resid 33 through 115 )C33 - 115
7X-RAY DIFFRACTION7chain 'C' and (resid 116 through 151 )C116 - 151
8X-RAY DIFFRACTION8chain 'C' and (resid 152 through 208 )C152 - 208
9X-RAY DIFFRACTION9chain 'C' and (resid 209 through 243 )C209 - 243
10X-RAY DIFFRACTION10chain 'C' and (resid 244 through 318 )C244 - 318
11X-RAY DIFFRACTION11chain 'C' and (resid 319 through 383 )C319 - 383
12X-RAY DIFFRACTION12chain 'C' and (resid 384 through 423 )C384 - 423
13X-RAY DIFFRACTION13chain 'E' and (resid 9 through 32 )E9 - 32
14X-RAY DIFFRACTION14chain 'E' and (resid 33 through 88 )E33 - 88
15X-RAY DIFFRACTION15chain 'E' and (resid 89 through 151 )E89 - 151
16X-RAY DIFFRACTION16chain 'E' and (resid 152 through 197 )E152 - 197
17X-RAY DIFFRACTION17chain 'E' and (resid 198 through 243 )E198 - 243
18X-RAY DIFFRACTION18chain 'E' and (resid 244 through 288 )E244 - 288
19X-RAY DIFFRACTION19chain 'E' and (resid 289 through 318 )E289 - 318
20X-RAY DIFFRACTION20chain 'E' and (resid 319 through 383 )E319 - 383
21X-RAY DIFFRACTION21chain 'E' and (resid 384 through 423 )E384 - 423
22X-RAY DIFFRACTION22chain 'G' and (resid 9 through 88 )G9 - 88
23X-RAY DIFFRACTION23chain 'G' and (resid 89 through 115 )G89 - 115
24X-RAY DIFFRACTION24chain 'G' and (resid 116 through 169 )G116 - 169
25X-RAY DIFFRACTION25chain 'G' and (resid 170 through 383 )G170 - 383
26X-RAY DIFFRACTION26chain 'G' and (resid 384 through 423 )G384 - 423
27X-RAY DIFFRACTION27chain 'B' and (resid 1 through 80 )B1 - 80
28X-RAY DIFFRACTION28chain 'B' and (resid 81 through 99 )B81 - 99
29X-RAY DIFFRACTION29chain 'B' and (resid 100 through 119 )B100 - 119
30X-RAY DIFFRACTION30chain 'B' and (resid 120 through 161 )B120 - 161
31X-RAY DIFFRACTION31chain 'D' and (resid 1 through 32 )D1 - 32
32X-RAY DIFFRACTION32chain 'D' and (resid 33 through 79 )D33 - 79
33X-RAY DIFFRACTION33chain 'D' and (resid 80 through 100 )D80 - 100
34X-RAY DIFFRACTION34chain 'D' and (resid 101 through 161 )D101 - 161
35X-RAY DIFFRACTION35chain 'F' and (resid 1 through 79 )F1 - 79
36X-RAY DIFFRACTION36chain 'F' and (resid 80 through 100 )F80 - 100
37X-RAY DIFFRACTION37chain 'F' and (resid 101 through 161 )F101 - 161
38X-RAY DIFFRACTION38chain 'H' and (resid 1 through 32 )H1 - 32
39X-RAY DIFFRACTION39chain 'H' and (resid 33 through 48 )H33 - 48
40X-RAY DIFFRACTION40chain 'H' and (resid 49 through 79 )H49 - 79
41X-RAY DIFFRACTION41chain 'H' and (resid 80 through 100 )H80 - 100
42X-RAY DIFFRACTION42chain 'H' and (resid 101 through 120 )H101 - 120
43X-RAY DIFFRACTION43chain 'H' and (resid 121 through 161 )H121 - 161

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