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- PDB-6zbn: HIF Prolyl Hydroxylase 2 (PHD2/EGLN1) in complex with tert-butyl ... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6zbn
TitleHIF Prolyl Hydroxylase 2 (PHD2/EGLN1) in complex with tert-butyl 6-(5-hydroxy-4-(1H-1,2,3-triazol-1-yl)-1H-pyrazol-1-yl)nicotinate (IOX4)
ComponentsEgl nine homolog 1
KeywordsOXIDOREDUCTASE / Inhibitor / Complex / IOX4 / HIF / PHD2 / Hypoxia
Function / homology
Function and homology information


peptidyl-proline 4-dioxygenase activity / hypoxia-inducible factor-proline dioxygenase activity / hypoxia-inducible factor-proline dioxygenase / negative regulation of hypoxia-inducible factor-1alpha signaling pathway / peptidyl-proline dioxygenase activity / regulation protein catabolic process at postsynapse / intracellular oxygen homeostasis / regulation of modification of postsynaptic structure / labyrinthine layer development / 2-oxoglutarate-dependent dioxygenase activity ...peptidyl-proline 4-dioxygenase activity / hypoxia-inducible factor-proline dioxygenase activity / hypoxia-inducible factor-proline dioxygenase / negative regulation of hypoxia-inducible factor-1alpha signaling pathway / peptidyl-proline dioxygenase activity / regulation protein catabolic process at postsynapse / intracellular oxygen homeostasis / regulation of modification of postsynaptic structure / labyrinthine layer development / 2-oxoglutarate-dependent dioxygenase activity / heart trabecula formation / cardiac muscle tissue morphogenesis / L-ascorbic acid binding / response to nitric oxide / ventricular septum morphogenesis / regulation of angiogenesis / enzyme inhibitor activity / regulation of neuron apoptotic process / ferrous iron binding / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / cellular response to hypoxia / intracellular iron ion homeostasis / response to hypoxia / postsynaptic density / intracellular membrane-bounded organelle / glutamatergic synapse / enzyme binding / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus / cytoplasm / cytosol
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 signature. / Zinc finger, MYND-type / Zinc finger MYND-type profile. / Oxoglutarate/iron-dependent dioxygenase / Fe(2+) 2-oxoglutarate dioxygenase domain profile.
Similarity search - Domain/homology
: / Chem-QEE / Egl nine homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.01 Å
AuthorsFigg Jr, W.D. / McDonough, M.A. / Nakashima, Y. / 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
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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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)155,18119
Polymers152,7906
Non-polymers2,39213
Water5,188288
1
A: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8483
Polymers25,4651
Non-polymers3832
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8483
Polymers25,4651
Non-polymers3832
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,9404
Polymers25,4651
Non-polymers4753
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8483
Polymers25,4651
Non-polymers3832
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8483
Polymers25,4651
Non-polymers3832
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Egl nine homolog 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8483
Polymers25,4651
Non-polymers3832
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)77.062, 75.472, 127.555
Angle α, β, γ (deg.)90.000, 95.040, 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-QEE / ~{tert}-butyl 6-[5-oxidanyl-4-(1,2,3-triazol-1-yl)pyrazol-1-yl]pyridine-3-carboxylate / tert-butyl 6-(5-hydroxy-4-(1H-1,2,3-triazol-1-yl)-1H-pyrazol-1-yl)nicotinate


Mass: 328.326 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C15H16N6O3 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 288 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.41 Å3/Da / Density % sol: 49 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.15M Potassium thiocyanate pH 7, 20.5% 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 X 16M / Detector: PIXEL / Date: Sep 26, 2019
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.01→76.76 Å / Num. obs: 97320 / % possible obs: 99.9 % / Redundancy: 6.8 % / Biso Wilson estimate: 46.843 Å2 / Rpim(I) all: 0.024 / Rrim(I) all: 0.063 / Net I/σ(I): 13.3 / Num. measured all: 666214
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
2.01-2.046.613184148500.7261.87498.8
5.45-76.827.143.73568950290.0120.03299.9

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation4.9 Å127.06 Å
Translation4.9 Å127.06 Å

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Processing

Software
NameVersionClassification
PHENIX1.19.1-4122-000refinement
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: 2.01→19.97 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 30.36 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2299 4821 4.97 %
Rwork0.2052 92131 -
obs0.2064 96952 99.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 172.75 Å2 / Biso mean: 74.1576 Å2 / Biso min: 35.22 Å2
Refinement stepCycle: final / Resolution: 2.01→19.97 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9348 0 259 288 9895
Biso mean--58.18 57.11 -
Num. residues----1196
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 (%)
2.01-2.030.38051600.373026318698
2.03-2.060.38471650.358330083173100
2.06-2.080.37971680.35553065323399
2.08-2.110.32881390.33623034317399
2.11-2.130.37051380.318330803218100
2.13-2.160.36951380.297130843222100
2.16-2.190.31191570.291930643221100
2.19-2.230.31631630.275130373200100
2.23-2.260.30221380.26973085322399
2.26-2.30.27071630.25243029319299
2.3-2.340.2911520.250430783230100
2.34-2.380.27441570.239730733230100
2.38-2.430.27151580.23830493207100
2.43-2.480.2461430.236430463189100
2.48-2.530.25291660.228130813247100
2.53-2.590.26691950.240330193214100
2.59-2.650.26441700.241130823252100
2.65-2.730.27541710.233530213192100
2.73-2.810.27911380.242431163254100
2.81-2.90.27461870.22730503237100
2.9-30.30361860.239730493235100
3-3.120.27421940.239230493243100
3.12-3.260.26281560.223831043260100
3.26-3.430.21941770.217730643241100
3.43-3.640.23781710.20930673238100
3.64-3.920.19431700.19230853255100
3.92-4.320.17071680.158731103278100
4.32-4.930.1651550.140131233278100
4.93-6.180.17171500.171831333283100
6.18-19.970.22151280.181232203348100
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)
10.6146-0.03610.09930.24830.03070.09830.76931.2448-0.1274-0.9308-0.0383-0.6904-0.18690.57610.02720.7993-0.00890.03570.75070.07980.571934.23861.273126.8156
20.8482-0.1906-0.69541.02920.15410.7241-0.08180.09730.20510.34610.1997-0.78440.01930.535200.592-0.0222-0.09390.5983-0.06860.633843.6715-7.390442.4948
32.5709-0.1091-1.20680.66480.71.2316-0.0447-0.22650.07260.42440.1389-0.4964-0.02220.1874-00.6794-0.026-0.09250.4961-0.02520.539736.9368-1.658947.5909
41.94910.4703-0.00232.00360.77362.50460.00250.1005-0.05680.19250.1108-0.15840.28440.055500.5418-0.0147-0.04510.42310.01980.4431.0219-10.358940.6028
50.29060.2750.00210.3270.14840.247-0.19340.64410.2169-0.4446-0.2625-0.321-0.97590.1859-0.00010.6950.0307-0.05790.6442-0.04850.489125.8163-16.783627.4963
61.33570.9151-0.42680.94860.31971.4712-0.00330.2523-0.13010.18610.2171-0.30250.29090.0966-00.53680.0158-0.08190.4624-0.0170.461932.6756-12.731837.9339
70.6762-0.1127-0.22510.2932-0.01750.07930.1045-0.4025-0.13430.4662-0.58320.5491-0.27870.4035-00.72780.00570.08730.59990.06990.750114.10811.937647.0698
80.00510.0087-0.01210.00920.00750.0678-0.1453-1.06760.2237-0.0177-0.18641.54870.0395-1.17110.00031.0955-0.03090.30980.7794-0.02310.9927-5.5721-18.442868.2996
91.0250.52750.23150.57450.79271.41630.1954-0.16020.22280.24510.16351.1107-0.1496-0.6458-0.00010.89430.09910.44630.6920.11711.2034-7.243-10.234555.6035
100.4611-0.046-0.21780.338-0.2470.2724-0.0540.16081.12860.92090.02840.3978-0.7846-0.80650.00011.09410.10960.26040.69380.03451.1589-0.63944.126250.69
110.13410.05780.01950.27830.29760.30870.2031-0.34580.03780.207-0.17820.3885-0.1171-0.39980.00041.2296-0.0040.51830.7394-0.06130.9796-1.6141-6.042863.254
120.2568-0.0597-0.11390.0510.06120.14030.4587-0.44230.23180.8492-0.178-0.6988-0.29110.44890.00011.0239-0.05670.13070.6397-0.01950.8339.6963-12.612862.6068
131.13190.6182-1.21651.184-0.37281.32260.01750.22630.14150.17770.11181.1056-0.2572-0.325500.60980.0770.20760.57470.06440.9674-1.564-11.053645.1324
140.156-0.0054-0.05480.12560.18430.41740.5284-0.93280.45390.7530.19050.49940.7066-0.25450.00030.71810.01780.05840.5867-0.01130.8472.0568-26.142444.9334
150.24660.32880.34031.1997-0.52741.32320.0290.0989-0.0813-0.05760.15970.7675-0.0598-0.206400.65590.0140.1580.54680.02960.9126-2.2294-16.395447.0899
161.28550.1522-0.99711.80850.56581.00050.2335-0.36110.13710.7803-0.10930.4562-0.15340.179200.8606-0.03020.15920.57010.0770.599712.6921-6.859554.0106
170.151-0.16680.07540.22580.0620.37560.0521.1707-0.0964-0.77370.01270.91490.2045-0.2152-00.7051-0.0472-0.1540.9830.01230.8354-10.4886-48.173422.5718
180.366-0.03840.5020.5045-0.54651.0006-0.0629-0.5837-0.1050.87730.03260.35460.0439-0.725400.8135-0.02430.23070.7570.05810.989-14.8463-47.481748.3273
190.9783-0.2080.88321.4421-0.17820.78650.17410.4559-0.5907-0.1293-0.09660.73520.5863-0.254700.6197-0.0362-0.07060.6347-0.0560.8966-6.1957-56.01831.5973
201.19470.99480.44880.9162-0.00082.8127-0.15450.12290.26850.17860.12630.6673-0.4002-0.2156-00.4717-0.00460.0880.59170.03390.825-6.3548-38.906838.3261
211.34660.11120.17322.1729-0.98391.5218-0.00430.35560.24480.11250.04130.6321-0.47360.0722-00.4596-0.05430.01210.63050.05940.756-4.9518-38.483532.4276
220.5135-0.02180.09660.35010.24770.1946-0.13120.1018-0.32120.2398-0.1457-0.01240.1867-0.1005-00.65640.0275-0.01360.6329-0.0880.666912.2482-56.969438.2998
230.0758-0.037-0.07880.00160.03520.06270.1673-0.1907-0.4366-0.1192-0.0661-0.8201-0.33182.264801.072-0.0713-0.14371.24180.03750.734435.5245-45.476361.3077
242.65790.6193-0.0912.1337-0.8582.18410.0753-0.1149-0.29050.23350.0071-0.44470.10480.2432-00.5496-0.0076-0.08330.4780.00240.534131.8779-51.086245.4716
252.59490.5987-0.00993.73770.36463.03230.0896-0.07590.1073-0.0166-0.0351-0.1305-0.3130.063500.50280.0361-0.03740.4187-0.00770.40326.7056-43.341544.5005
260.2476-0.09540.07970.0402-0.03010.30630.1849-0.0327-0.16070.59110.13520.43890.30590.2897-0.00020.75670.05820.05860.7126-0.05550.8595.458-51.389949.3651
270.09340.0150.06470.0885-0.01710.0265-0.18390.35951.4965-0.08040.17330.7962-0.9221-0.24320.00060.97640.1311-0.18510.94490.28251.4596-3.409-0.541817.1378
285.10210.7294-4.57780.6949-1.7876.2687-0.2604-0.1303-0.2651-0.4855-0.64680.08980.2459-0.5315-1.29080.28770.1164-0.80051.45190.68111.2591-17.1213-16.1645.9372
290.09570.11570.04140.11520.05780.0603-0.3428-0.0009-0.1247-0.496-0.30120.1260.6282-0.349601.0187-0.0191-0.31761.13240.16311.0351-7.5941-22.58242.448
300.6136-0.403-0.7610.23870.48470.86760.29390.26670.6446-0.31030.09930.3518-0.2634-0.2964-01.01420.0619-0.24761.0070.42831.06720.5966-5.32336.0019
310.66970.26280.49661.82941.26911.4968-0.16970.21580.3075-0.25770.18360.7510.1896-0.4738-00.639-0.0032-0.19410.88180.30410.9318-4.3006-19.140817.3026
320.4537-0.1919-0.04410.86050.60131.51330.24660.340.5056-0.10170.06410.3726-0.1602-0.261900.60110.0228-0.11060.80690.25370.8662-1.8909-14.576120.4475
330.1764-0.1320.02490.0885-0.03540.07260.15340.17840.6675-0.59220.5723-0.06190.12870.34320.00010.8273-0.1067-0.0441.07420.29550.697517.4236-16.31452.609
340.01160.0359-0.0150.0648-0.04050.02590.44210.5367-0.4486-0.0944-0.4485-0.7070.11170.7474-01.3338-0.0190.09860.9776-0.36551.123529.093-48.41584.2636
351.61240.17020.87451.28070.07871.7213-0.00940.7186-0.2118-0.70370.0302-0.45520.00560.6831-00.8221-0.12690.14991.0505-0.09740.560633.2444-30.52625.5828
361.6827-1.4296-0.00021.7577-0.18940.0686-0.35610.8145-0.7768-1.26290.41260.22290.36950.94090.15941.0124-0.20080.13791.4273-0.2470.367729.164-35.7024-1.2515
371.6388-0.6662-0.3472.43720.05221.4893-0.03160.4764-0.102-0.37720.08490.0231-0.01110.193300.5826-0.1002-0.00840.7864-0.04330.414926.1909-29.196912.1348
381.195-1.01840.43872.2434-0.54091.89040.0610.4005-0.1648-0.03730.0887-0.08780.21940.316300.5913-0.08840.01810.7081-0.06720.410427.2381-32.214717.0185
390.1306-0.02-0.05740.09150.0790.07980.22330.8621-0.3987-1.02690.2230.22990.0177-0.6471-0.00010.8874-0.0374-0.2431.0650.04170.60487.1977-25.82121.9417
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 189 through 205 )A189 - 205
2X-RAY DIFFRACTION2chain 'A' and (resid 206 through 230 )A206 - 230
3X-RAY DIFFRACTION3chain 'A' and (resid 231 through 283 )A231 - 283
4X-RAY DIFFRACTION4chain 'A' and (resid 284 through 342 )A284 - 342
5X-RAY DIFFRACTION5chain 'A' and (resid 343 through 353 )A343 - 353
6X-RAY DIFFRACTION6chain 'A' and (resid 354 through 391 )A354 - 391
7X-RAY DIFFRACTION7chain 'A' and (resid 392 through 406 )A392 - 406
8X-RAY DIFFRACTION8chain 'D' and (resid 187 through 197 )D187 - 197
9X-RAY DIFFRACTION9chain 'D' and (resid 198 through 231 )D198 - 231
10X-RAY DIFFRACTION10chain 'D' and (resid 232 through 266 )D232 - 266
11X-RAY DIFFRACTION11chain 'D' and (resid 267 through 283 )D267 - 283
12X-RAY DIFFRACTION12chain 'D' and (resid 284 through 297 )D284 - 297
13X-RAY DIFFRACTION13chain 'D' and (resid 298 through 342 )D298 - 342
14X-RAY DIFFRACTION14chain 'D' and (resid 343 through 353 )D343 - 353
15X-RAY DIFFRACTION15chain 'D' and (resid 354 through 382 )D354 - 382
16X-RAY DIFFRACTION16chain 'D' and (resid 383 through 405 )D383 - 405
17X-RAY DIFFRACTION17chain 'B' and (resid 189 through 215 )B189 - 215
18X-RAY DIFFRACTION18chain 'B' and (resid 216 through 266 )B216 - 266
19X-RAY DIFFRACTION19chain 'B' and (resid 267 through 297 )B267 - 297
20X-RAY DIFFRACTION20chain 'B' and (resid 298 through 342 )B298 - 342
21X-RAY DIFFRACTION21chain 'B' and (resid 343 through 391 )B343 - 391
22X-RAY DIFFRACTION22chain 'B' and (resid 392 through 406 )B392 - 406
23X-RAY DIFFRACTION23chain 'C' and (resid 184 through 197 )C184 - 197
24X-RAY DIFFRACTION24chain 'C' and (resid 198 through 266 )C198 - 266
25X-RAY DIFFRACTION25chain 'C' and (resid 267 through 391 )C267 - 391
26X-RAY DIFFRACTION26chain 'C' and (resid 392 through 405 )C392 - 405
27X-RAY DIFFRACTION27chain 'E' and (resid 189 through 215 )E189 - 215
28X-RAY DIFFRACTION28chain 'E' and (resid 216 through 229 )E216 - 229
29X-RAY DIFFRACTION29chain 'E' and (resid 230 through 266 )E230 - 266
30X-RAY DIFFRACTION30chain 'E' and (resid 267 through 297 )E267 - 297
31X-RAY DIFFRACTION31chain 'E' and (resid 298 through 342 )E298 - 342
32X-RAY DIFFRACTION32chain 'E' and (resid 343 through 392 )E343 - 392
33X-RAY DIFFRACTION33chain 'E' and (resid 393 through 406 )E393 - 406
34X-RAY DIFFRACTION34chain 'F' and (resid 188 through 197 )F188 - 197
35X-RAY DIFFRACTION35chain 'F' and (resid 198 through 266 )F198 - 266
36X-RAY DIFFRACTION36chain 'F' and (resid 267 through 283 )F267 - 283
37X-RAY DIFFRACTION37chain 'F' and (resid 284 through 342 )F284 - 342
38X-RAY DIFFRACTION38chain 'F' and (resid 343 through 391 )F343 - 391
39X-RAY DIFFRACTION39chain 'F' and (resid 392 through 405 )F392 - 405

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