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- PDB-6huy: HmdII from Desulfurobacterium thermolithotrophum reconstitued wit... -

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Basic information

Entry
Database: PDB / ID: 6huy
TitleHmdII from Desulfurobacterium thermolithotrophum reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydrofolate form A
Components(Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related ...) x 2
KeywordsOXIDOREDUCTASE / Hydrogenase / H2-activation / Lateral gene-transfer / cofactor biosynthesis / tetrahydromethanopterin / tetrahydrofolate / paralog / sulfur-reducing bacteria / metalloenzyme
Function / homology
Function and homology information


H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein / H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase, C-terminal / HMD, C-terminal domain superfamily / : / H2-forming N5,N10-methylene-tetrahydromethanopterin dehydrogenase / HMD N-terminal domain / 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold ...H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein / H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase, C-terminal / HMD, C-terminal domain superfamily / : / H2-forming N5,N10-methylene-tetrahydromethanopterin dehydrogenase / HMD N-terminal domain / 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
iron-guanylyl pyridinol cofactor / 5,10-Methenyltetrahydrofolate / Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
Similarity search - Component
Biological speciesDesulfurobacterium thermolithotrophum DSM 11699 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsWatanabe, T. / Wagner, T. / Huang, G. / Kahnt, J. / Ataka, K. / Ermler, U. / Shima, S.
Funding support Germany, China, 2items
OrganizationGrant numberCountry
Max Planck Society Germany
Ministry of Education (China) China
CitationJournal: Angew. Chem. Int. Ed. Engl. / Year: 2019
Title: The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
Authors: Watanabe, T. / Wagner, T. / Huang, G. / Kahnt, J. / Ataka, K. / Ermler, U. / Shima, S.
History
DepositionOct 9, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 9, 2019Provider: repository / Type: Initial release
Revision 1.1Feb 6, 2019Group: Data collection / Database references / Category: citation / citation_author / Item: _citation.title / _citation_author.identifier_ORCID
Revision 1.2Mar 13, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Jan 24, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr2_label_seq_id
Revision 1.4Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
B: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
C: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
D: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,28822
Polymers164,0084
Non-polymers4,28018
Water10,971609
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A: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
B: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,20211
Polymers82,0042
Non-polymers2,1989
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14460 Å2
ΔGint-110 kcal/mol
Surface area25600 Å2
MethodPISA
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C: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
D: Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,08611
Polymers82,0042
Non-polymers2,0829
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14670 Å2
ΔGint-108 kcal/mol
Surface area25630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.769, 131.829, 168.263
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related ... , 2 types, 4 molecules ACBD

#1: Protein Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein


Mass: 40994.000 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: synthetic gene
Source: (gene. exp.) Desulfurobacterium thermolithotrophum DSM 11699 (bacteria)
Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host: Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): /
References: UniProt: F0S2B6, 5,10-methenyltetrahydromethanopterin hydrogenase
#2: Protein Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related protein


Mass: 41010.000 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: synthetic gene
Source: (gene. exp.) Desulfurobacterium thermolithotrophum DSM 11699 (bacteria)
Tissue: / / Cell: / / Cell line: / / Gene: Dester_1504 / Organ: / / Details (production host): / / Cell (production host): / / Organ (production host): / / Production host: Escherichia coli BL21(DE3) (bacteria) / Tissue (production host): / / References: UniProt: F0S2B6

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Non-polymers , 6 types, 627 molecules

#3: Chemical ChemComp-FE9 / iron-guanylyl pyridinol cofactor


Mass: 686.323 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H23FeN6O13PS
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-GUE / 5,10-Methenyltetrahydrofolate


Mass: 456.432 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H22N7O6
#6: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#7: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 609 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.38 Å3/Da / Density % sol: 63.31 % / Description: plate shape
Crystal growTemperature: 281 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: dHmdII reconstituted with the Fe-guanylylpyridinol cofactor from Methanothermobacter marburgensis was cocrystallized with methenyl-tetrahydrofolate using the sitting drop vapor diffusion ...Details: dHmdII reconstituted with the Fe-guanylylpyridinol cofactor from Methanothermobacter marburgensis was cocrystallized with methenyl-tetrahydrofolate using the sitting drop vapor diffusion method at 281 K under N2/H2 (95%/5%) in red light condition. The reconstituted dHmdII holoenzyme was mixed with methenyl-tetrahydrofolate at the final concentrations of 1.6 mM. Methenyl-tetrahydrofolate was dissolved in 10% DMSO, and the final concentration of DMSO in the protein solution was 1.6%. 0.7 ul of dHmdII at 21 mg/ml (with Fe-guanylylpryridinol and methenyl-tetrahydrofolate) was spotted on a 96-well 2-drop MRC Crystallization Plates (Molecular Dimensions, Suffolk, UK) and 0.7 ul of reservoir solution was mixed. After 10 days, the crystals appeared in 20% PEG 3000 (w/v), 100 mM Tri-Sodium Citrate pH 5.5 (from the kit Wizard, Jean Bioscience). Crystals were cryoprotected by a soak of few seconds in 20% PEG 3000 (w/v), 100 mM Tri-Sodium Citrate pH 5.5 and 20% glycerol before a flash freeze in liquid nitrogen.
Temp details: The temperature was fluctuating by +/- 1 degree

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 15, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.25→48.89 Å / Num. obs: 105630 / % possible obs: 99.9 % / Redundancy: 4.8 % / Biso Wilson estimate: 42.3 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.096 / Rpim(I) all: 0.049 / Rrim(I) all: 0.108 / Net I/σ(I): 9.7
Reflection shellResolution: 2.25→2.37 Å / Redundancy: 4.9 % / Rmerge(I) obs: 1.421 / Num. unique obs: 15270 / CC1/2: 0.623 / Rpim(I) all: 0.714 / Rrim(I) all: 1.595 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
SCALA3.3.22data scaling
PHASER2.6.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4YT4

4yt4


Resolution: 2.25→24.983 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.47
Details: For the last refinement cycle, the hydrogens have been generated in riding position. In the final deposited model, these hydrogens were omitted.
RfactorNum. reflection% reflection
Rfree0.2122 5111 4.85 %
Rwork0.1869 --
obs0.1881 105367 99.77 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 55.2 Å2
Refinement stepCycle: LAST / Resolution: 2.25→24.983 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10949 0 270 609 11828
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00711439
X-RAY DIFFRACTIONf_angle_d0.87915526
X-RAY DIFFRACTIONf_dihedral_angle_d17.1286992
X-RAY DIFFRACTIONf_chiral_restr0.0461815
X-RAY DIFFRACTIONf_plane_restr0.0051958
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.25-2.27560.31441520.33873316X-RAY DIFFRACTION100
2.2756-2.30230.32741790.32343286X-RAY DIFFRACTION100
2.3023-2.33040.31221500.30693348X-RAY DIFFRACTION100
2.3304-2.35980.36491780.31053292X-RAY DIFFRACTION100
2.3598-2.39090.3191500.28573319X-RAY DIFFRACTION100
2.3909-2.42360.31551630.28623292X-RAY DIFFRACTION100
2.4236-2.45820.30941700.27833327X-RAY DIFFRACTION100
2.4582-2.49490.3041520.25943332X-RAY DIFFRACTION100
2.4949-2.53380.27551840.25813273X-RAY DIFFRACTION100
2.5338-2.57530.30211590.25683335X-RAY DIFFRACTION100
2.5753-2.61970.29381940.24173295X-RAY DIFFRACTION100
2.6197-2.66720.24281880.2243282X-RAY DIFFRACTION100
2.6672-2.71850.28111730.21993330X-RAY DIFFRACTION100
2.7185-2.77390.24021630.21693351X-RAY DIFFRACTION100
2.7739-2.83410.24761810.21443298X-RAY DIFFRACTION100
2.8341-2.90.25681840.21153322X-RAY DIFFRACTION100
2.9-2.97240.21751650.20843317X-RAY DIFFRACTION100
2.9724-3.05260.26321530.20483365X-RAY DIFFRACTION100
3.0526-3.14230.28531800.2013334X-RAY DIFFRACTION100
3.1423-3.24350.23851720.19683290X-RAY DIFFRACTION99
3.2435-3.35920.2331640.19653334X-RAY DIFFRACTION100
3.3592-3.49330.21611690.19223342X-RAY DIFFRACTION100
3.4933-3.65180.22961720.16493365X-RAY DIFFRACTION100
3.6518-3.84370.18321510.16063390X-RAY DIFFRACTION100
3.8437-4.08360.16511900.14973338X-RAY DIFFRACTION100
4.0836-4.39730.16171780.13973362X-RAY DIFFRACTION100
4.3973-4.83690.14861850.13253372X-RAY DIFFRACTION100
4.8369-5.53020.16511780.14453419X-RAY DIFFRACTION100
5.5302-6.94260.18611490.16793477X-RAY DIFFRACTION100
6.9426-24.98470.17231850.173553X-RAY DIFFRACTION99
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)
13.9704-0.0452-0.41314.40570.65483.07720.08950.07290.65560.4157-0.1653-0.9149-0.57360.80410.07310.6461-0.2088-0.02940.65890.17340.9119-91.466-64.331959.5407
22.6934-0.0205-1.06323.5355-0.30422.84660.00380.14340.87490.0689-0.0339-0.9901-0.75480.51950.08390.675-0.20030.04570.64780.23740.9326-91.1665-58.332655.2181
34.38190.0161-1.50364.68060.62452.89160.23810.08550.92730.4685-0.3366-0.6414-0.6360.3626-0.08730.5918-0.1370.04370.41560.07920.6603-104.8629-62.638863.5742
43.7026-0.1504-0.71133.4435-0.31982.1640.24430.36010.60980.087-0.1334-0.0931-0.40920.0099-0.07980.4521-0.06630.02350.40970.16180.4383-107.9387-68.871359.1489
51.7707-0.2782-0.08413.0988-0.47990.82810.0570.42610.1247-0.3168-0.048-0.1837-0.05850.0161-0.01340.3032-0.01570.01630.5090.02870.2792-101.7995-88.500454.7851
62.86020.5591-0.32614.7129-1.47662.5372-0.11250.4804-0.0208-0.0703-0.2028-1.201-0.00850.33670.11590.33250.04820.03680.6592-0.02480.7952-85.5757-105.287457.8029
73.94420.6811-0.55772.5383-0.24881.3320.0217-0.2179-0.33410.4692-0.0195-0.5418-0.06350.39010.02950.4621-0.0681-0.0990.43430.02220.3879-100.038-94.979472.0945
81.19891.48751.72731.89482.29462.81480.2146-0.86920.60150.3229-0.1089-0.1907-0.39710.1618-0.03020.5496-0.0808-0.02120.55020.01680.5679-107.6295-80.233170.178
92.2396-0.43720.00473.1184-0.4452.59630.10320.2699-0.4106-0.4483-0.0175-0.60650.33970.4594-0.11490.51240.1291-0.02090.5031-0.23230.6-95.1593-125.527257.2302
102.9196-0.0084-0.75553.17310.35842.68560.03890.3174-0.4895-0.0291-0.0174-0.06280.3723-0.03390.0380.41470.0337-0.10730.364-0.08390.4501-106.298-124.206865.471
113.11820.2564-0.25315.119-0.66773.69230.1408-0.16890.17040.50940.0472-0.28030.1425-0.0428-0.32460.37910.049-0.13170.3850.02140.341-102.0191-110.578776.0454
121.46640.11390.07953.5423-0.94821.2950.05220.20050.04150.0341-0.101-0.7338-0.01860.28130.06350.27250.0143-0.02260.4751-0.02530.4144-93.7445-96.088861.7077
133.3437-0.9479-1.52333.4675-0.18564.30950.30770.37730.1703-0.31910.0486-0.0263-0.36010.0787-0.13130.3495-0.0627-0.0560.424-0.03460.3765-108.4031-92.54155.7781
140.6279-0.9108-0.29683.36131.88561.3293-0.32990.3953-0.7813-0.225-0.19940.69690.3701-0.47640.08830.4332-0.0745-0.05590.5761-0.02720.6491-115.7667-104.170962.2448
152.77890.2105-0.24743.13990.13882.02060.1795-0.07770.6984-0.0998-0.01530.5433-0.3082-0.21030.03690.59820.13270.06250.4867-0.10890.8652-107.8958-74.1117108.4109
162.6248-0.1428-0.75812.31150.34482.2937-0.0201-0.09740.7575-0.09140.02660.4878-0.7217-0.3689-0.05460.63820.1460.05910.4713-0.18240.9197-108.1927-68.0558112.7358
174.329-0.0717-1.3663.8047-0.61483.16580.09390.22140.9242-0.2995-0.03020.3899-0.4635-0.4474-0.17920.56690.070.05060.3966-0.02160.6256-94.508-72.4335104.4386
181.65170.4326-0.31122.3950.00411.09080.1202-0.30770.35840.2101-0.03910.1138-0.22030.0277-0.08470.33490.01520.00970.3355-0.08280.3112-94.4779-87.3734114.1069
191.9981-0.0243-0.25641.9486-0.13241.50550.093-0.0026-0.2801-0.0361-0.02840.30690.0153-0.1912-0.05330.3370.0295-0.04070.35850.00060.3995-103.7196-109.1304102.3681
205.306-2.25861.81651.0541-0.75181.33920.14010.51880.345-0.22830.08610.1333-0.00490.0804-0.11420.45880.0007-0.05110.46430.01110.4615-92.3853-90.023597.5288
212.50960.1346-0.2513.185-0.23862.8144-0.0424-0.2321-0.71440.166-0.0090.68120.2744-0.13220.01140.5561-0.0155-0.02980.4050.19370.7799-104.337-135.2467111.2613
222.59180.0405-0.7632.08270.14292.6759-0.195-0.2111-0.91860.0773-0.07940.20760.82790.18080.19770.66520.0547-0.07060.40850.11250.7458-94.1439-139.4877106.8096
233.2499-1.2798-0.73012.9833-0.16712.31850.14870.213-0.3139-0.292-0.19190.19290.1767-0.02850.05870.40330.0284-0.11480.3321-0.00830.391-96.3498-126.12196.5307
241.54220.2013-0.26272.87390.05521.78350.0491-0.1480.09550.1358-0.01070.4886-0.1261-0.2612-0.03680.28490.00930.01550.3844-0.02070.3716-106.3811-98.7815110.5914
253.87041.0183-0.89582.5445-0.63924.22950.2033-0.36610.00120.25710.014-0.06930.09030.4698-0.26670.38130.0909-0.07160.2974-0.0240.3441-91.0152-102.2799112.452
265.20960.9452-2.37975.4898-0.91123.7259-0.4357-0.165-1.3118-0.0933-0.2419-0.38060.62230.71330.60880.41860.1042-0.0840.49920.04280.7043-83.3863-113.7196104.2247
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 19 )
2X-RAY DIFFRACTION2chain 'A' and (resid 20 through 74 )
3X-RAY DIFFRACTION3chain 'A' and (resid 75 through 104 )
4X-RAY DIFFRACTION4chain 'A' and (resid 105 through 157 )
5X-RAY DIFFRACTION5chain 'A' and (resid 158 through 262 )
6X-RAY DIFFRACTION6chain 'A' and (resid 263 through 292 )
7X-RAY DIFFRACTION7chain 'A' and (resid 293 through 332 )
8X-RAY DIFFRACTION8chain 'A' and (resid 333 through 350 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 41 )
10X-RAY DIFFRACTION10chain 'B' and (resid 42 through 157 )
11X-RAY DIFFRACTION11chain 'B' and (resid 158 through 173 )
12X-RAY DIFFRACTION12chain 'B' and (resid 174 through 292 )
13X-RAY DIFFRACTION13chain 'B' and (resid 293 through 332 )
14X-RAY DIFFRACTION14chain 'B' and (resid 333 through 357 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1 through 19 )
16X-RAY DIFFRACTION16chain 'C' and (resid 20 through 74 )
17X-RAY DIFFRACTION17chain 'C' and (resid 75 through 104 )
18X-RAY DIFFRACTION18chain 'C' and (resid 105 through 231 )
19X-RAY DIFFRACTION19chain 'C' and (resid 232 through 332 )
20X-RAY DIFFRACTION20chain 'C' and (resid 333 through 351 )
21X-RAY DIFFRACTION21chain 'D' and (resid 1 through 41 )
22X-RAY DIFFRACTION22chain 'D' and (resid 42 through 103 )
23X-RAY DIFFRACTION23chain 'D' and (resid 104 through 204 )
24X-RAY DIFFRACTION24chain 'D' and (resid 205 through 292 )
25X-RAY DIFFRACTION25chain 'D' and (resid 293 through 332 )
26X-RAY DIFFRACTION26chain 'D' and (resid 333 through 355 )

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