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- PDB-6zbo: HIF Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 1-(6-morpho... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6zbo
TitleHIF Prolyl Hydroxylase 2 (PHD2/EGLN1) in Complex with 1-(6-morpholinopyrimidin-4-yl)-4-(1H-1,2,3-triazol-1-yl)-1H-pyrazol-5-ol (Molidustat)
ComponentsEgl nine homolog 1
KeywordsOXIDOREDUCTASE / PHD2 / Inhibitor / Complex / Molidustat / HIF
Function / homology
Function and homology information


hypoxia-inducible factor-proline dioxygenase activity / hypoxia-inducible factor-proline dioxygenase / peptidyl-proline 4-dioxygenase activity / peptidyl-proline dioxygenase activity / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / negative regulation of cyclic-nucleotide phosphodiesterase activity / regulation protein catabolic process at postsynapse / intracellular oxygen homeostasis / labyrinthine layer development / 2-oxoglutarate-dependent dioxygenase activity ...hypoxia-inducible factor-proline dioxygenase activity / hypoxia-inducible factor-proline dioxygenase / peptidyl-proline 4-dioxygenase activity / peptidyl-proline dioxygenase activity / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / negative regulation of cyclic-nucleotide phosphodiesterase activity / regulation protein catabolic process at postsynapse / intracellular oxygen homeostasis / labyrinthine layer development / 2-oxoglutarate-dependent dioxygenase activity / cardiac muscle tissue morphogenesis / heart trabecula formation / regulation of modification of postsynaptic structure / L-ascorbic acid binding / response to nitric oxide / ventricular septum morphogenesis / regulation of angiogenesis / ferrous iron binding / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / negative regulation of DNA-binding transcription factor activity / cellular response to hypoxia / intracellular iron ion homeostasis / postsynaptic density / response to hypoxia / intracellular membrane-bounded organelle / glutamatergic synapse / enzyme binding / positive regulation of transcription by RNA polymerase II / nucleus / cytosol / cytoplasm
Similarity search - Function
Prolyl 4-hydroxylase alpha subunit, Fe(2+) 2OG dioxygenase domain / 2OG-Fe(II) oxygenase superfamily / Prolyl 4-hydroxylase, alpha subunit / Prolyl 4-hydroxylase alpha subunit homologues. / MYND finger / Zinc finger, MYND-type / Zinc finger MYND-type signature. / Zinc finger MYND-type profile. / Oxoglutarate/iron-dependent dioxygenase / Fe(2+) 2-oxoglutarate dioxygenase domain profile.
Similarity search - Domain/homology
: / Chem-QEQ / Egl nine homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.79 Å
AuthorsFigg Jr, W.D. / McDonough, M.A. / Nakashima, Y. / Holt-Martyn, J.P. / Schofield, C.J.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust United Kingdom
Cancer Research UK United Kingdom
CitationJournal: Chemmedchem / Year: 2021
Title: Structural Basis of Prolyl Hydroxylase Domain Inhibition by Molidustat.
Authors: Figg Jr., W.D. / McDonough, M.A. / Chowdhury, R. / Nakashima, Y. / Zhang, Z. / Holt-Martyn, J.P. / Krajnc, A. / Schofield, C.J.
History
DepositionJun 8, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 7, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 6, 2021Group: Data collection / Database references / Structure summary
Category: citation / citation_author ...citation / citation_author / database_2 / diffrn_source / pdbx_contact_author / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site
Revision 1.2Dec 8, 2021Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.3Jan 24, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Egl nine homolog 1
B: Egl nine homolog 1
C: Egl nine homolog 1
D: Egl nine homolog 1
E: Egl nine homolog 1
F: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)155,46631
Polymers152,7906
Non-polymers2,67625
Water11,205622
1
A: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9416
Polymers25,4651
Non-polymers4765
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9055
Polymers25,4651
Non-polymers4404
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8704
Polymers25,4651
Non-polymers4053
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9055
Polymers25,4651
Non-polymers4404
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9055
Polymers25,4651
Non-polymers4404
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9416
Polymers25,4651
Non-polymers4765
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)77.119, 75.151, 127.215
Angle α, β, γ (deg.)90.000, 95.310, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Egl nine homolog 1 / Hypoxia-inducible factor prolyl hydroxylase 2 / HIF-PH2 / HIF-prolyl hydroxylase 2 / HPH-2 / Prolyl ...Hypoxia-inducible factor prolyl hydroxylase 2 / HIF-PH2 / HIF-prolyl hydroxylase 2 / HPH-2 / Prolyl hydroxylase domain-containing protein 2 / PHD2 / SM-20


Mass: 25464.955 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EGLN1, C1orf12, PNAS-118, PNAS-137 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q9GZT9, hypoxia-inducible factor-proline dioxygenase
#2: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#3: Chemical
ChemComp-QEQ / 2-(6-morpholin-4-ylpyrimidin-4-yl)-4-(1,2,3-triazol-1-yl)pyrazol-3-ol / 1-(6-morpholinopyrimidin-4-yl)-4-(1H-1,2,3-triazol-1-yl)-1H-pyrazol-5-ol


Mass: 314.303 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C13H14N8O2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 13 / Source method: isolated from a natural source / Formula: Cl
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 622 / 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: 2.4 Å3/Da / Density % sol: 48.8 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.2M Potassium thiocyanate pH 7, 21% PEG 3350, Sitting drop (300 nL), protein-to-well ratio 2:1, 298K

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Sep 15, 2019
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.79→63.13 Å / Num. obs: 134388 / % possible obs: 98.5 % / Redundancy: 7 % / Biso Wilson estimate: 36.96 Å2 / Rpim(I) all: 0.021 / Rrim(I) all: 0.056 / Net I/σ(I): 15 / Num. measured all: 937925
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
1.79-1.827.11.14654865330.5651.52197.1
4.86-63.177.249.55082670140.0140.03799.8

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation4.89 Å63.13 Å
Translation4.89 Å63.13 Å

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Processing

Software
NameVersionClassification
PHENIX1.19.1refinement
xia20.5.900data reduction
DIALS1.14.11data scaling
PHASER2.8.2phasing
Coot0.9.3model building
MolProbitymodel building
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3HQR

3hqr


Resolution: 1.79→53.71 Å / SU ML: 0.23 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2063 6820 5.09 %
Rwork0.1804 127164 -
obs0.1817 133984 98.25 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 147 Å2 / Biso mean: 58.0728 Å2 / Biso min: 27.63 Å2
Refinement stepCycle: final / Resolution: 1.79→53.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9467 0 241 625 10333
Biso mean--46.19 49.29 -
Num. residues----1206
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.79-1.810.40242200.3994076429696
1.81-1.830.36692320.36244175440797
1.83-1.850.30742300.32914136436697
1.85-1.880.30592320.29934214444697
1.88-1.90.25842100.28274093430397
1.9-1.930.3022210.26484259448097
1.93-1.960.27262020.2514156435897
1.96-1.990.24982170.23144197441497
1.99-2.020.23432220.22184187440998
2.02-2.050.25422150.22554218443398
2.05-2.080.27852310.22574196442798
2.08-2.120.25452500.2224172442298
2.12-2.160.2382330.21664179441298
2.16-2.210.25332250.21144290451598
2.21-2.260.21752140.19724199441398
2.26-2.310.23322250.18474215444098
2.31-2.370.18582760.17654173444999
2.37-2.430.19462630.17644259452299
2.43-2.50.24242180.17794294451299
2.5-2.580.24672270.18434224445199
2.58-2.670.24442110.19434309452099
2.67-2.780.23782140.1974287450199
2.78-2.910.23071900.19424322451299
2.91-3.060.21812360.18844262449899
3.06-3.250.23112530.18154282453599
3.25-3.50.20232020.18294352455499
3.5-3.860.19042400.16614318455899
3.86-4.410.14231960.136843694565100
4.41-5.560.14672450.132243504595100
5.56-53.710.21272700.18774401467199
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)
13.863-4.59622.41087.0515-3.50427.11790.19560.55240.5477-0.6756-0.1822-0.7417-0.28390.431800.3967-0.02080.09520.33280.03190.32736.6556-1.030728.8601
28.38164.0291-4.95883.357-3.47053.8598-0.2309-0.4987-0.990.8857-0.0165-1.62110.09090.81950.25130.56990.0833-0.2060.4957-0.09310.6946.7204-8.506648.9429
36.61041.68032.40211.5673-1.986.6799-0.3609-0.573-0.38770.30750.2783-0.42250.81030.36870.05850.83450.1914-0.01310.4657-0.03180.351337.8515-9.86356.9307
42.4060.05060.47134.14840.32191.84730.01760.02360.22790.20470.0422-0.1009-0.09520.0723-0.05510.3611-0.00070.00860.2685-0.00130.290830.549-5.303641.2463
56.92081.95425.10215.69033.04898.0261-0.09410.1251-0.5234-0.03760.3247-0.5398-0.22860.2002-0.26340.3777-0.00010.05250.2893-0.00530.34335.2763-18.432832.858
63.0842-0.8140.17944.56910.32970.74330.00110.1039-0.16960.26360.1949-0.08360.02310.1161-0.19550.37370.0082-0.02930.3138-0.02560.299932.6231-12.514637.8259
78.86712.9801-8.27216.5867-5.14328.82080.2617-0.61210.57010.5389-0.04150.9430.06630.2414-0.22550.52390.01870.11370.3691-0.00180.500413.80951.369547.6684
83.49440.4037-3.49953.33832.37036.22280.4014-1.04420.03140.8629-0.175-0.37540.09740.7753-0.18570.6793-0.1629-0.09580.5434-0.05410.409532.7817-42.310957.458
92.8765-2.31250.75176.6869-1.39394.0966-0.02130.2845-0.2548-0.1842-0.0681-0.34120.30250.24550.1620.4340.0155-0.05090.2862-0.00340.428733.3752-57.696439.8637
102.98570.6421-0.16813.0313-0.49512.13340.2002-0.3387-0.00530.3529-0.05590.0637-0.0391-0.0323-0.15060.4162-0.0188-0.04880.2939-0.02140.33923.7455-47.280146.9822
115.3124-2.726-3.40533.80572.39225.54220.26990.1326-0.04170.0923-0.1915-0.3222-0.43950.2722-0.12070.428-0.0425-0.04390.29840.01050.451632.9913-35.632840.2501
123.3861-1.4722-0.99254.2819-0.02781.66010.00220.10570.11750.1694-0.0544-0.1647-0.1482-0.02180.04290.4069-0.0192-0.03660.2852-0.01560.371429.1838-39.147842.3686
137.1197-0.8216-1.72951.5090.1610.78260.02250.0293-0.08560.21210.00410.36460.0501-0.1736-0.0170.4525-0.00840.01280.31160.01570.447513.6324-50.682746.3895
143.08793.26462.94866.89494.88064.08990.25780.8718-0.2004-0.4089-0.22240.64920.3025-0.6721-0.13510.6128-0.065-0.13960.7891-0.04980.5488-8.6948-49.658819.3415
152.2181-0.1125-0.4522.4331-0.41565.7883-0.1215-0.0601-0.21180.3740.00850.64120.2502-0.54830.13120.3756-0.06190.07130.39260.04960.63-14.4078-49.351141.5536
164.2738-1.9802-1.32096.9421.25513.55530.01960.2552-0.06090.00590.00570.19760.2088-0.0338-0.0090.2617-0.023-0.030.27340.03210.3194-1.6758-45.337935.4548
174.8514-0.6274-2.90575.76931.59765.4488-0.08070.62910.36760.55370.50371.87270.0256-1.3471-0.50820.41460.0736-0.03410.71240.07720.9131-17.6029-33.123936.9928
181.96510.3287-0.23894.9933-1.42022.45310.00340.15120.1454-0.08710.11490.3502-0.0359-0.1488-0.0990.2167-0.0167-0.03350.31380.0310.4049-4.9743-38.805132.2186
192.655-3.6531.88247.8372-1.46792.20420.0546-0.19070.06630.19-0.2655-0.24660.1145-0.59870.01770.4343-0.00670.00330.43860.00940.536412.7916-56.351738.1926
207.04021.02095.64158.85756.97418.9372-0.009-0.8627-0.28030.29930.08580.4114-0.1182-0.5947-0.21520.7842-0.04790.30250.55920.10310.6318-4.9695-18.262367.869
217.2799-1.0417-0.65260.39750.9584.11590.1358-0.4959-0.6120.45580.11340.56760.3297-0.3468-0.22030.5674-0.08830.14260.3830.11080.6717-3.3084-19.949858.6035
222.91041.2796-0.17197.4285-4.5886.867-0.40350.0831-0.0625-0.01710.24650.8561-0.15-1.00860.05370.59320.1780.22360.5796-0.05910.9899-11.95010.463851.7905
234.41920.79090.21254.6414-2.10894.2987-0.37320.21580.8920.03390.07820.6579-0.4178-0.15340.41350.67120.0410.1530.40620.02920.909-1.61235.458447.3631
242.18160.55590.33452.36040.58873.75510.1806-0.28970.05280.5575-0.05930.2542-0.2981-0.0964-0.16110.6131-0.0210.23440.358-0.00920.56162.4799-8.310759.8961
253.2218-0.35450.68522.42690.03192.0860.06220.05470.03710.05050.05310.7118-0.1992-0.374-0.07470.37390.02620.13310.3040.06380.5504-1.9147-12.302444.9865
266.9066-5.8542-0.17256.85291.81138.44390.1286-0.12270.53031.05440.0081-0.8170.5744-0.083-0.10040.4516-0.0097-0.01090.2790.01520.60131.6738-26.200944.734
274.0384-1.2491.55784.1037-1.09555.03240.17470.1138-0.10790.1183-0.09050.50940.0134-0.2694-0.10290.3585-0.01480.08950.22920.00880.51-2.5054-16.426646.9563
286.9017-0.3130.67232.01280.01350.99910.10010.0102-0.27310.49140.01510.2827-0.28380.062-0.06480.5682-0.02590.1120.3377-0.01420.407312.6756-7.254853.7364
293.59780.72371.3012.17850.26323.57210.11390.1090.5892-0.13410.08990.695-0.3845-0.6616-0.19220.59120.1082-0.08360.61290.29860.8453-8.7234-6.565113.0333
308.8944-1.35071.68464.6417-3.08635.2088-0.45390.67890.45340.1154-0.15560.14340.34150.1510.47420.7612-0.0335-0.21890.67970.00960.527-7.7271-22.23532.3129
315.10190.62573.21891.42622.41266.3916-0.05230.33030.5591-0.68320.17760.1068-0.66720.0252-0.01590.74290.0007-0.10840.60130.32710.63820.3806-5.53256.0672
322.41441.1856-0.72051.88390.15821.8936-0.08370.23830.2164-0.27210.13720.583-0.0369-0.3152-0.07650.45990.0372-0.13290.50380.17790.5732-4.6793-19.021417.2316
339.45063.86595.17237.98854.26833.9224-0.2498-0.05570.56730.53410.16790.6149-0.85410.2310.00510.44290.0113-0.03590.42520.14240.49052.8924-12.984129.4007
342.62171.13450.66432.59840.3042.74220.018-0.04340.3139-0.0450.23670.4406-0.0607-0.3478-0.23430.42910.0498-0.08740.46820.17550.5562-2.6153-15.055418.1392
356.9038-5.5436-0.46489.51710.05430.81660.16080.4476-0.2833-0.3946-0.09681.0628-0.00720.4993-0.15040.6711-0.0560.03550.73030.08050.472417.2488-16.1223.3702
367.78984.48152.59753.8745-0.81745.03620.03350.6601-1.6528-0.0248-0.0227-1.22660.50890.73760.020.7250.0195-0.04950.55-0.22070.729325.1133-47.02288.6396
373.53973.1408-3.26816.2806-3.44456.5635-0.37851.1073-0.4618-0.74280.5639-0.97940.09260.8438-0.13350.5381-0.10640.07851.078-0.21180.477638.7605-31.84945.3614
381.5809-1.4267-1.14795.1762-1.74264.3582-0.19081.13430.0327-0.94270.2983-0.3532-0.19940.7896-0.0770.7011-0.10850.07830.9654-0.0920.337430.5567-27.6333-0.0593
393.62710.32150.5942.6354-0.16911.415-0.01250.5683-0.2245-0.41530.10760.1494-0.04410.0602-0.11550.4559-0.0323-0.01930.4941-0.0470.26822.6841-29.483310.5392
402.1561-3.1885-0.14338.45060.69197.45930.01470.6670.1189-1.07560.119-0.6222-0.20641.5035-0.07840.3942-0.05880.01140.7676-0.08790.512541.4893-29.77818.1466
414.79544.6028-6.68294.7316-6.62879.4972-0.09990.63890.2366-0.50670.38970.85060.657-0.4543-0.21770.4007-0.0214-0.03740.3572-0.03150.337122.7754-36.75424.9704
424.84441.02930.87883.82080.8963.5456-0.09890.3441-0.2127-0.28610.1654-0.11730.06640.3447-0.03880.4406-0.020.02720.4337-0.05840.281628.2018-31.167914.4924
435.185-5.32116.02285.5777-6.42977.7111-0.15140.4428-0.5346-0.10210.52310.55760.2577-0.8048-0.28140.5447-0.0261-0.15910.78730.04960.46836.7673-25.35662.2349
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 188 through 215 )A188 - 215
2X-RAY DIFFRACTION2chain 'A' and (resid 216 through 230 )A216 - 230
3X-RAY DIFFRACTION3chain 'A' and (resid 231 through 266 )A231 - 266
4X-RAY DIFFRACTION4chain 'A' and (resid 267 through 329 )A267 - 329
5X-RAY DIFFRACTION5chain 'A' and (resid 330 through 353 )A330 - 353
6X-RAY DIFFRACTION6chain 'A' and (resid 354 through 392 )A354 - 392
7X-RAY DIFFRACTION7chain 'A' and (resid 393 through 407 )A393 - 407
8X-RAY DIFFRACTION8chain 'B' and (resid 183 through 215 )B183 - 215
9X-RAY DIFFRACTION9chain 'B' and (resid 216 through 266 )B216 - 266
10X-RAY DIFFRACTION10chain 'B' and (resid 267 through 329 )B267 - 329
11X-RAY DIFFRACTION11chain 'B' and (resid 330 through 353 )B330 - 353
12X-RAY DIFFRACTION12chain 'B' and (resid 354 through 382 )B354 - 382
13X-RAY DIFFRACTION13chain 'B' and (resid 383 through 407 )B383 - 407
14X-RAY DIFFRACTION14chain 'C' and (resid 189 through 205 )C189 - 205
15X-RAY DIFFRACTION15chain 'C' and (resid 206 through 282 )C206 - 282
16X-RAY DIFFRACTION16chain 'C' and (resid 283 through 329 )C283 - 329
17X-RAY DIFFRACTION17chain 'C' and (resid 330 through 342 )C330 - 342
18X-RAY DIFFRACTION18chain 'C' and (resid 343 through 392 )C343 - 392
19X-RAY DIFFRACTION19chain 'C' and (resid 393 through 405 )C393 - 405
20X-RAY DIFFRACTION20chain 'D' and (resid 188 through 197 )D188 - 197
21X-RAY DIFFRACTION21chain 'D' and (resid 198 through 215 )D198 - 215
22X-RAY DIFFRACTION22chain 'D' and (resid 216 through 230 )D216 - 230
23X-RAY DIFFRACTION23chain 'D' and (resid 231 through 266 )D231 - 266
24X-RAY DIFFRACTION24chain 'D' and (resid 267 through 303 )D267 - 303
25X-RAY DIFFRACTION25chain 'D' and (resid 304 through 342 )D304 - 342
26X-RAY DIFFRACTION26chain 'D' and (resid 343 through 353 )D343 - 353
27X-RAY DIFFRACTION27chain 'D' and (resid 354 through 382 )D354 - 382
28X-RAY DIFFRACTION28chain 'D' and (resid 383 through 405 )D383 - 405
29X-RAY DIFFRACTION29chain 'E' and (resid 189 through 230 )E189 - 230
30X-RAY DIFFRACTION30chain 'E' and (resid 231 through 266 )E231 - 266
31X-RAY DIFFRACTION31chain 'E' and (resid 267 through 297 )E267 - 297
32X-RAY DIFFRACTION32chain 'E' and (resid 298 through 342 )E298 - 342
33X-RAY DIFFRACTION33chain 'E' and (resid 343 through 353 )E343 - 353
34X-RAY DIFFRACTION34chain 'E' and (resid 354 through 392 )E354 - 392
35X-RAY DIFFRACTION35chain 'E' and (resid 393 through 405 )E393 - 405
36X-RAY DIFFRACTION36chain 'F' and (resid 189 through 205 )F189 - 205
37X-RAY DIFFRACTION37chain 'F' and (resid 206 through 229 )F206 - 229
38X-RAY DIFFRACTION38chain 'F' and (resid 230 through 282 )F230 - 282
39X-RAY DIFFRACTION39chain 'F' and (resid 283 through 329 )F283 - 329
40X-RAY DIFFRACTION40chain 'F' and (resid 330 through 342 )F330 - 342
41X-RAY DIFFRACTION41chain 'F' and (resid 343 through 353 )F343 - 353
42X-RAY DIFFRACTION42chain 'F' and (resid 354 through 392 )F354 - 392
43X-RAY DIFFRACTION43chain 'F' and (resid 393 through 405 )F393 - 405

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