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- PDB-6xwl: Cystathionine beta-synthase from Toxoplasma gondii -

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Basic information

Entry
Database: PDB / ID: 6xwl
TitleCystathionine beta-synthase from Toxoplasma gondii
ComponentsCystathionine beta-synthaseCystathionine beta synthase
KeywordsCYTOSOLIC PROTEIN / Transulfuration / hydrogen sulfide / homocysteine / CBS
Function / homology
Function and homology information


cystathionine beta-synthase / cysteine biosynthetic process via cystathionine / cystathionine beta-synthase activity / cysteine biosynthetic process from serine / cytoplasm
Similarity search - Function
Cystathionine beta-synthase / Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site / Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. / CBS domain superfamily / Domain in cystathionine beta-synthase and other proteins. / Pyridoxal-phosphate dependent enzyme / Tryptophan synthase beta subunit-like PLP-dependent enzyme / Pyridoxal-phosphate dependent enzyme / CBS domain / CBS domain / CBS domain profile.
Similarity search - Domain/homology
PYRIDOXAL-5'-PHOSPHATE / Cystathionine beta-synthase
Similarity search - Component
Biological speciesToxoplasma gondii ME49 (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.201 Å
AuthorsFernandez-Rodriguez, C. / Oyenarte, I. / Conter, C. / Gonzalez-Recio, I. / Quintana, I. / Martinez-Chantar, M. / Astegno, A. / Martinez-Cruz, L.A.
Funding support Spain, 4items
OrganizationGrant numberCountry
Ministry of Economy and Competitiveness (MINECO)BFU2013-47531-R Spain
Ministry of Economy and Competitiveness (MINECO)BES-2014-068464 Spain
Ministry of Economy and Competitiveness (MINECO)BFU2016-77408-R Spain
Ministry of Economy and Competitiveness (MINECO)BES-2017-080435 Spain
CitationJournal: Comput Struct Biotechnol J / Year: 2021
Title: Structural insight into the unique conformation of cystathionine beta-synthase from Toxoplasma gondii .
Authors: Fernandez-Rodriguez, C. / Oyenarte, I. / Conter, C. / Gonzalez-Recio, I. / Nunez-Franco, R. / Gil-Pitarch, C. / Quintana, I. / Jimenez-Oses, G. / Dominici, P. / Martinez-Chantar, M.L. / ...Authors: Fernandez-Rodriguez, C. / Oyenarte, I. / Conter, C. / Gonzalez-Recio, I. / Nunez-Franco, R. / Gil-Pitarch, C. / Quintana, I. / Jimenez-Oses, G. / Dominici, P. / Martinez-Chantar, M.L. / Astegno, A. / Martinez-Cruz, L.A.
History
DepositionJan 23, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 3, 2021Provider: repository / Type: Initial release
Revision 1.1Aug 4, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 24, 2024Group: 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
F: Cystathionine beta-synthase
A: Cystathionine beta-synthase
B: Cystathionine beta-synthase
C: Cystathionine beta-synthase
D: Cystathionine beta-synthase
E: Cystathionine beta-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)337,23212
Polymers335,7506
Non-polymers1,4836
Water0
1
F: Cystathionine beta-synthase
A: Cystathionine beta-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,4114
Polymers111,9172
Non-polymers4942
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9700 Å2
ΔGint-50 kcal/mol
Surface area36330 Å2
MethodPISA
2
B: Cystathionine beta-synthase
D: Cystathionine beta-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,4114
Polymers111,9172
Non-polymers4942
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9720 Å2
ΔGint-45 kcal/mol
Surface area36940 Å2
MethodPISA
3
C: Cystathionine beta-synthase
E: Cystathionine beta-synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,4114
Polymers111,9172
Non-polymers4942
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9890 Å2
ΔGint-48 kcal/mol
Surface area37110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)83.237, 83.237, 420.309
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 6 through 337 or (resid 338...
21(chain B and (resid 6 through 337 or (resid 338...
31(chain C and (resid 6 through 337 or (resid 338...
41(chain D and (resid 6 through 362 or resid 365...
51(chain E and (resid 6 through 337 or (resid 338...
61(chain F and (resid 6 through 362 or resid 365...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 6 through 337 or (resid 338...A6 - 337
121(chain A and (resid 6 through 337 or (resid 338...A338
131(chain A and (resid 6 through 337 or (resid 338...A6 - 1551
141(chain A and (resid 6 through 337 or (resid 338...A6 - 1551
151(chain A and (resid 6 through 337 or (resid 338...A6 - 1551
161(chain A and (resid 6 through 337 or (resid 338...A6 - 1551
211(chain B and (resid 6 through 337 or (resid 338...B6 - 337
221(chain B and (resid 6 through 337 or (resid 338...B338
231(chain B and (resid 6 through 337 or (resid 338...B6 - 513
311(chain C and (resid 6 through 337 or (resid 338...C6 - 337
321(chain C and (resid 6 through 337 or (resid 338...C338
331(chain C and (resid 6 through 337 or (resid 338...C6 - 513
341(chain C and (resid 6 through 337 or (resid 338...C6 - 513
351(chain C and (resid 6 through 337 or (resid 338...C6 - 513
361(chain C and (resid 6 through 337 or (resid 338...C6 - 513
411(chain D and (resid 6 through 362 or resid 365...D6 - 362
421(chain D and (resid 6 through 362 or resid 365...D365 - 373
431(chain D and (resid 6 through 362 or resid 365...D374
441(chain D and (resid 6 through 362 or resid 365...D6 - 513
451(chain D and (resid 6 through 362 or resid 365...D6 - 513
461(chain D and (resid 6 through 362 or resid 365...D6 - 513
471(chain D and (resid 6 through 362 or resid 365...D6 - 513
511(chain E and (resid 6 through 337 or (resid 338...E6 - 337
521(chain E and (resid 6 through 337 or (resid 338...E338
531(chain E and (resid 6 through 337 or (resid 338...E6 - 513
541(chain E and (resid 6 through 337 or (resid 338...E6 - 513
551(chain E and (resid 6 through 337 or (resid 338...E6 - 513
561(chain E and (resid 6 through 337 or (resid 338...E6 - 513
611(chain F and (resid 6 through 362 or resid 365...F6 - 362
621(chain F and (resid 6 through 362 or resid 365...F365 - 373
631(chain F and (resid 6 through 362 or resid 365...F374
641(chain F and (resid 6 through 362 or resid 365...F6 - 513
651(chain F and (resid 6 through 362 or resid 365...F6 - 513
661(chain F and (resid 6 through 362 or resid 365...F6 - 513
671(chain F and (resid 6 through 362 or resid 365...F6 - 513

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Components

#1: Protein
Cystathionine beta-synthase / Cystathionine beta synthase


Mass: 55958.273 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Toxoplasma gondii ME49 (eukaryote) / Gene: TGME49_259180 / Production host: Toxoplasma gondii ME49 (eukaryote)
References: UniProt: A0A125YSJ9, cystathionine beta-synthase
#2: Chemical
ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate / Pyridoxal phosphate


Mass: 247.142 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C8H10NO6P / Feature type: SUBJECT OF INVESTIGATION
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: 2.51 Å3/Da / Density meas: 18 Mg/m3 / Density % sol: 50.95 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.7 / Details: 8% PEG 3350 0.1M MES pH=5.7 / PH range: 5.5-6.1

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Feb 10, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.855→420.309 Å / Num. obs: 44707 / % possible obs: 89.7 % / Redundancy: 10.2 % / CC1/2: 0.999 / Rmerge(I) obs: 0.115 / Rpim(I) all: 0.038 / Rrim(I) all: 0.121 / Net I/σ(I): 12.4 / Num. measured all: 457518
Reflection shell

Num. unique obs: 2211 / Diffraction-ID: 1 / Redundancy: 9.7 %

Resolution (Å)Rmerge(I) obsNum. measured allCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.855-3.241.299213740.6630.4361.3711.766.2
9.234-420.3090.044215050.9980.0150.04739.299.9

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
autoPROCdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1JBQ

1jbq


Resolution: 3.201→46.136 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 33.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.277 2137 4.99 %
Rwork0.253 40697 -
obs0.2544 42834 79.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 183.82 Å2 / Biso mean: 89.6753 Å2 / Biso min: 48.57 Å2
Refinement stepCycle: final / Resolution: 3.201→46.136 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21306 0 90 0 21396
Biso mean--100.25 --
Num. residues----2841
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A7110X-RAY DIFFRACTION5.413TORSIONAL
12B7110X-RAY DIFFRACTION5.413TORSIONAL
13C7110X-RAY DIFFRACTION5.413TORSIONAL
14D7110X-RAY DIFFRACTION5.413TORSIONAL
15E7110X-RAY DIFFRACTION5.413TORSIONAL
16F7110X-RAY DIFFRACTION5.413TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.24-3.27490.4331380.393478023
3.2749-3.35680.3243480.337495328
3.3568-3.44750.327460.3261104330
3.4475-3.5490.3343940.3189168151
3.549-3.66350.35351050.322238169
3.6635-3.79430.31982000.3032340798
3.7943-3.94620.32712000.29213296100
3.9462-4.12570.33761640.27813395100
4.1257-4.3430.28621900.25863401100
4.343-4.61490.28591710.24853435100
4.6149-4.97080.27612080.2473327100
4.9708-5.47030.29951730.25183387100
5.4703-6.26020.3671300.27253480100
6.2602-7.88090.24351770.24163383100
7.8809-46.130.1921930.1897334899
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)
12.46861.06240.85652.02191.07335.379-0.1954-0.4940.24840.1801-0.04930.16010.02260.06210.19480.21390.0446-0.17480.3701-0.13950.480837.8645-1.612913.4554
22.83150.87691.72130.9090.43023.90860.3815-1.28010.25030.3212-0.56170.39821.1538-0.99060.07350.42210.0369-0.03960.7527-0.18060.507324.982-10.57116.2618
30.52110.51390.68370.7662-0.19893.99520.45830.2758-0.39560.65920.03750.06542.73450.1649-0.3221.2513-0.0359-0.12050.51280.05211.089927.5467-36.1056-2.3847
45.67952.68852.71331.87963.21767.51530.6910.4575-1.3399-0.76640.0796-0.57861.20110.392-0.81191.44510.2229-0.00430.90990.07721.247331.5684-39.0156-29.5909
51.7552-1.05592.30990.8597-1.11573.38410.36970.0946-0.27170.1769-0.2328-0.42380.44090.94460.41971.83260.2927-0.08890.3037-0.01840.742231.1585-37.1545-10.3862
63.16022.3151-3.2952.0209-1.35597.45890.0004-0.9472-1.2069-0.1652-0.1174-0.20371.42150.89820.14951.81570.1098-0.27730.757-0.04571.02623.599-43.6628-9.4896
73.33930.5082.40032.05260.9633.615-0.2255-0.1430.2254-0.4536-0.20820.19080.0666-0.16570.1920.3579-0.0391-0.21370.2198-0.11230.352623.6454-10.7979-9.5816
83.94112.23930.95112.1659-0.04954.967-0.59250.34290.4681-0.21060.49420.2352-0.07830.13680.00630.5722-0.0739-0.22240.2717-0.03080.417324.6011-8.2321-22.3995
92.52920.78511.56832.4642-0.16923.0204-0.54761.13590.3571-0.77350.2989-0.0394-0.3431.2770.07150.5834-0.1956-0.20380.547-0.00850.460737.9824-2.8896-18.5551
101.91341.28040.83350.91610.3720.65270.3391.1319-1.07970.15350.2096-0.18281.22381.9096-0.22760.80590.45070.00131.349-0.25350.820859.1592-17.66950.1308
111.47621.7592-0.54144.9731.01985.7625-0.07750.2879-0.50671.35460.0231-1.19841.05230.6509-0.00431.37810.5185-0.08861.11010.07330.745259.4333-22.809127.5875
124.3674-2.65760.85342.87750.99881.97280.20820.1367-1.002-0.80230.0750.01090.88951.2728-0.20650.90460.5139-0.03351.2207-0.09670.837462.7791-19.49077.0238
131.9174-0.02461.07582.73111.21442.3799-0.3245-0.04411.0399-0.0208-0.20790.4357-0.5481-0.30290.39970.2416-0.0058-0.20040.28010.02560.78718.2611-36.746254.2453
142.38611.20650.61453.94331.09732.8228-0.0541-0.5770.73540.6311-0.13250.44510.0135-0.33650.1340.35260.1196-0.01610.5421-0.14720.63715.6854-41.339566.279
155.00991.26420.04015.18160.61434.2966-0.0066-0.0425-0.1680.6555-0.2039-0.61690.71180.2270.19680.37840.00660.04140.41160.02420.489117.9923-58.05758.4105
164.19782.106-2.15411.3186-0.10994.3071-0.36510.4793-0.08030.1730.7809-0.49471.8664-0.3773-0.44441.30230.0433-0.30391.4258-0.52361.448138.7908-78.927133.4844
172.6621-2.19141.60751.9113-1.25871.01820.03760.0619-0.60630.08630.3123-0.09880.29790.8804-0.46580.42010.3212-0.20912.4206-0.69951.127936.9358-70.645817.5437
181.45150.63861.83611.14840.27482.61110.04090.8638-0.52990.39080.4213-0.73680.12661.65790.56650.82030.5693-0.42891.7546-0.42271.356834.9186-69.464837.1901
197.1918-2.18471.54710.6779-0.72673.28160.34721.7052-2.9032-0.3946-1.0381-0.0361.14950.8470.54511.09650.4904-0.08421.5953-0.42041.949933.1782-79.431738.3385
201.71050.2741-0.89493.45551.272.61-0.38010.0753-0.9725-0.1412-0.14550.46650.344-0.16020.41030.35590.03630.210.2690.06490.766818.2764-11.325683.7811
213.0764-0.4514-0.56512.40920.51413.23-0.03040.7397-0.6826-0.6752-0.19680.4084-0.0956-0.28250.20550.3213-0.09680.00930.4836-0.19290.624815.696-6.710671.7076
222.74191.54431.45112.42972.63015.4476-0.1976-0.73230.0033-0.73820.1841-0.2734-1.49950.0381-0.02740.55620.02890.15030.70740.02560.643625.230517.185490.36
230.36560.8592-0.1135.0096-3.32723.21720.6178-1.74021.4059-0.42750.26521.22170.13481.4186-0.5420.676-0.02110.03232.0769-0.93641.303538.652419.7251116.8977
241.5712-1.66380.05281.792-0.23460.7351-0.2737-1.14731.4246-0.050.6268-1.0561-0.84591.07660.09570.7768-0.7010.18511.6897-0.55111.220833.764225.6552100.3749
252.46571.12972.06953.61580.04022.9957-0.1622-0.02570.93750.305-0.64190.5573-0.6415-0.16520.69790.3493-0.0279-0.12220.5721-0.0750.80057.6724-43.234538.0933
262.2331.65251.3743.3236-0.14442.2774-0.30831.6027-0.0587-0.3720.53960.03090.73460.9304-0.10340.36070.0541-0.03930.838-0.31810.547916.8108-63.512836.2978
272.08750.27051.20911.41880.31392.2551-0.27411.36540.7592-0.62720.17520.4146-0.0890.65380.05320.1983-0.0958-0.34691.42130.24160.81411.4981-50.720424.6689
280.88790.16680.93873.41922.36284.0714-0.35641.68170.5888-1.05320.0075-0.07-1.01130.77120.68760.1951-0.3139-0.27391.31950.43340.715518.0924-40.479227.2861
293.39714.53761.16927.39531.32810.4363-0.57941.64780.06890.18080.9345-1.8126-0.58710.6532-0.12040.5798-0.1721-0.23071.12340.39291.020735.7505-37.955538.2483
300.1893-0.5939-0.20833.9644-0.94041.1839-0.36350.86871.19060.39490.112-1.5824-0.63581.23610.2030.4165-0.202-0.29391.80870.26411.701455.6101-34.803858.9154
313.2321.3758-0.38040.59680.20546.491-1.3487-0.36980.46070.58080.3394-0.83640.15570.96070.86110.94530.5413-0.3640.9443-0.17681.233548.2757-40.00773.7725
327.30433.0747-1.79283.3801-0.71340.4417-0.25182.290.0254-0.75191.35230.36070.2083-1.7294-0.69480.3242-0.08290.031.10230.36190.896745.713-39.646754.9144
332.69030.12440.72522.13761.23743.6409-0.4403-0.49280.5642-0.93960.25980.1872-0.35070.63610.4230.461-0.1286-0.18391.50490.43341.211450.4809-31.094153.9249
343.1605-0.0172-1.7362.80220.79614.1934-0.2725-1.0677-0.0166-0.3151-0.12690.4329-0.80280.3315-0.07680.0183-0.00330.12280.6968-0.06910.523512.45558.17101.99
352.2594-1.1818-0.50931.33240.79952.4449-0.515-1.7071-0.49180.77040.30460.62260.88030.58970.2379-0.09560.19280.41541.47840.42550.770814.5153-5.2961112.9175
364.1125-3.03140.28952.3165-0.10110.1899-0.1925-1.6439-0.15530.17470.2135-1.19170.6170.5355-0.08140.52310.25670.06421.1360.51841.05935.6301-10.23199.8474
372.49281.7324-1.94932.1449-0.45012.3623-0.7427-0.5055-0.5148-0.24510.3934-0.26740.17930.65480.34240.67850.04590.16770.93390.10391.03954.2397-11.548672.386
382.0083-0.288-0.97221.45220.51156.5878-1.24320.5975-0.8227-1.54620.5355-0.4495-0.97870.72240.7051.0034-0.47110.24940.719-0.10730.939943.086-6.158364.6448
392.9541-1.8411-0.76441.74161.19071.0479-0.0762-0.4959-0.16490.18120.49260.22090.1955-0.109-0.31030.21760.14510.08981.4050.45210.947848.8647-13.459185.6185
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'F' and (resid 6 through 254 )F6 - 254
2X-RAY DIFFRACTION2chain 'F' and (resid 255 through 319 )F255 - 319
3X-RAY DIFFRACTION3chain 'F' and (resid 320 through 375 )F320 - 375
4X-RAY DIFFRACTION4chain 'F' and (resid 376 through 428 )F376 - 428
5X-RAY DIFFRACTION5chain 'F' and (resid 429 through 461 )F429 - 461
6X-RAY DIFFRACTION6chain 'F' and (resid 462 through 513 )F462 - 513
7X-RAY DIFFRACTION7chain 'A' and (resid 6 through 139 )A6 - 139
8X-RAY DIFFRACTION8chain 'A' and (resid 140 through 253 )A140 - 253
9X-RAY DIFFRACTION9chain 'A' and (resid 254 through 319 )A254 - 319
10X-RAY DIFFRACTION10chain 'A' and (resid 320 through 375 )A320 - 375
11X-RAY DIFFRACTION11chain 'A' and (resid 376 through 431 )A376 - 431
12X-RAY DIFFRACTION12chain 'A' and (resid 432 through 513 )A432 - 513
13X-RAY DIFFRACTION13chain 'B' and (resid 6 through 139 )B6 - 139
14X-RAY DIFFRACTION14chain 'B' and (resid 140 through 285 )B140 - 285
15X-RAY DIFFRACTION15chain 'B' and (resid 286 through 349 )B286 - 349
16X-RAY DIFFRACTION16chain 'B' and (resid 350 through 375 )B350 - 375
17X-RAY DIFFRACTION17chain 'B' and (resid 376 through 428 )B376 - 428
18X-RAY DIFFRACTION18chain 'B' and (resid 429 through 461 )B429 - 461
19X-RAY DIFFRACTION19chain 'B' and (resid 462 through 513 )B462 - 513
20X-RAY DIFFRACTION20chain 'C' and (resid 6 through 139 )C6 - 139
21X-RAY DIFFRACTION21chain 'C' and (resid 140 through 285 )C140 - 285
22X-RAY DIFFRACTION22chain 'C' and (resid 286 through 386 )C286 - 386
23X-RAY DIFFRACTION23chain 'C' and (resid 387 through 428 )C387 - 428
24X-RAY DIFFRACTION24chain 'C' and (resid 429 through 513 )C429 - 513
25X-RAY DIFFRACTION25chain 'D' and (resid 6 through 69 )D6 - 69
26X-RAY DIFFRACTION26chain 'D' and (resid 70 through 139 )D70 - 139
27X-RAY DIFFRACTION27chain 'D' and (resid 140 through 245 )D140 - 245
28X-RAY DIFFRACTION28chain 'D' and (resid 246 through 319 )D246 - 319
29X-RAY DIFFRACTION29chain 'D' and (resid 320 through 349 )D320 - 349
30X-RAY DIFFRACTION30chain 'D' and (resid 350 through 375 )D350 - 375
31X-RAY DIFFRACTION31chain 'D' and (resid 376 through 428 )D376 - 428
32X-RAY DIFFRACTION32chain 'D' and (resid 429 through 461 )D429 - 461
33X-RAY DIFFRACTION33chain 'D' and (resid 462 through 513 )D462 - 513
34X-RAY DIFFRACTION34chain 'E' and (resid 6 through 163 )E6 - 163
35X-RAY DIFFRACTION35chain 'E' and (resid 164 through 319 )E164 - 319
36X-RAY DIFFRACTION36chain 'E' and (resid 320 through 349 )E320 - 349
37X-RAY DIFFRACTION37chain 'E' and (resid 350 through 404 )E350 - 404
38X-RAY DIFFRACTION38chain 'E' and (resid 405 through 437 )E405 - 437
39X-RAY DIFFRACTION39chain 'E' and (resid 438 through 513 )E438 - 513

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