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- PDB-6o9e: Structure of HIV-1 Reverse Transcriptase in complex with DNA and ... -

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Basic information

Entry
Database: PDB / ID: 6o9e
TitleStructure of HIV-1 Reverse Transcriptase in complex with DNA and INDOPY-1
Components
  • (Reverse transcriptase ...) x 2
  • DNA (38-MER)
KeywordsTRANSFERASE/DNA / Human immunodeficiency virus 1 / Protein/DNA / nucleotide-competing reverse transcriptase inhibitor / TRANSFERASE / TRANSFERASE-DNA complex
Function / homology
Function and homology information


RNA-directed DNA polymerase activity / HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase ...RNA-directed DNA polymerase activity / HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / telomerase activity / viral penetration into host nucleus / RNA stem-loop binding / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / host cell / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / symbiont-mediated suppression of host gene expression / symbiont entry into host cell / viral translational frameshifting / lipid binding / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / proteolysis / DNA binding / zinc ion binding / membrane
Similarity search - Function
HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. ...HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / Immunodeficiency lentiviral matrix, N-terminal / gag gene protein p17 (matrix protein) / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Retropepsin-like catalytic domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / RNase H type-1 domain profile. / Ribonuclease H domain / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Reverse transcriptase domain / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase (RT) catalytic domain profile. / Retrovirus capsid, C-terminal / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Nucleotidyltransferase; domain 5 / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / Alpha-Beta Plaits / Roll / DNA/RNA polymerase superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
sucrose / Chem-IY1 / AMMONIUM ION / DI(HYDROXYETHYL)ETHER / DNA / DNA (> 10) / Gag-Pol polyprotein
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsRuiz, F.X. / Hoang, A. / Das, K. / Arnold, E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)MERIT Award R37 AI027690 United States
CitationJournal: J.Med.Chem. / Year: 2019
Title: Structural Basis of HIV-1 Inhibition by Nucleotide-Competing Reverse Transcriptase Inhibitor INDOPY-1.
Authors: Ruiz, F.X. / Hoang, A. / Das, K. / Arnold, E.
History
DepositionMar 13, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 23, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 6, 2019Group: Data collection / Database references / Category: citation / citation_author / Item: _citation.title / _citation_author.identifier_ORCID
Revision 1.2Nov 27, 2019Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_asym.entity_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _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
A: Reverse transcriptase p66
B: Reverse transcriptase p51
C: Reverse transcriptase p66
D: Reverse transcriptase p51
F: DNA (38-MER)
E: DNA (38-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)254,10524
Polymers251,4366
Non-polymers2,66818
Water2,000111
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A: Reverse transcriptase p66
B: Reverse transcriptase p51
E: DNA (38-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,39815
Polymers125,7183
Non-polymers1,68012
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15040 Å2
ΔGint-92 kcal/mol
Surface area46290 Å2
MethodPISA
2
C: Reverse transcriptase p66
D: Reverse transcriptase p51
F: DNA (38-MER)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)126,7079
Polymers125,7183
Non-polymers9896
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12790 Å2
ΔGint-64 kcal/mol
Surface area47350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.762, 127.663, 131.610
Angle α, β, γ (deg.)90.00, 101.50, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Reverse transcriptase ... , 2 types, 4 molecules ACBD

#1: Protein Reverse transcriptase p66


Mass: 63874.133 Da / Num. of mol.: 2 / Mutation: C280S, D498N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 / Production host: Escherichia coli (E. coli)
References: UniProt: P03366, RNA-directed DNA polymerase, DNA-directed DNA polymerase, retroviral ribonuclease H
#2: Protein Reverse transcriptase p51


Mass: 50096.539 Da / Num. of mol.: 2 / Mutation: C280S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 / Production host: Escherichia coli (E. coli) / References: UniProt: P03366, HIV-1 retropepsin

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DNA chain / Sugars , 2 types, 4 molecules FE

#3: DNA chain DNA (38-MER)


Mass: 11747.539 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: Polysaccharide beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: sucrose
DescriptorTypeProgram
DFrufb2-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][b-D-Fruf]{[(2+1)][a-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 7 types, 127 molecules

#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-NH4 / AMMONIUM ION


Mass: 18.038 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: H4N
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C3H8O3
#8: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#9: Chemical ChemComp-IY1 / 5-methyl-1-(4-nitrophenyl)-2-oxo-2,5-dihydro-1H-pyrido[3,2-b]indole-3-carbonitrile / Indopy-1


Mass: 344.324 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H12N4O3 / Feature type: SUBJECT OF INVESTIGATION
#10: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


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


Mass: 18.015 Da / Num. of mol.: 111 / Source method: isolated from a natural source / Formula: H2O

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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: 3.01 Å3/Da / Density % sol: 59.11 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 10-12% PEG 8000, 50 MM BISTRIS-PROPANE PH 7.2, 50 MM AMMONIUM SULFATE, 5% GLYCEROL, 5% SUCROSE

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 20, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 113545 / % possible obs: 100 % / Redundancy: 19 % / Biso Wilson estimate: 73.6 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.162 / Rpim(I) all: 0.055 / Rrim(I) all: 0.171 / Net I/σ(I): 11.6
Reflection shellResolution: 2.4→2.44 Å / Redundancy: 19.5 % / Rmerge(I) obs: 6.118 / Mean I/σ(I) obs: 0.8 / Num. unique obs: 5622 / CC1/2: 0.311 / Rpim(I) all: 2.035 / Rrim(I) all: 6.45 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5D3G

5d3g


Resolution: 2.4→50 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 30.68
RfactorNum. reflection% reflection
Rfree0.2416 1998 1.76 %
Rwork0.203 --
obs0.2037 113316 99.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.4→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15836 1441 175 111 17563
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218076
X-RAY DIFFRACTIONf_angle_d0.48924857
X-RAY DIFFRACTIONf_dihedral_angle_d17.4916945
X-RAY DIFFRACTIONf_chiral_restr0.0392692
X-RAY DIFFRACTIONf_plane_restr0.0032923
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.460.43251410.40047836X-RAY DIFFRACTION99
2.46-2.52660.38151430.3657928X-RAY DIFFRACTION100
2.5266-2.60090.3691430.34217879X-RAY DIFFRACTION100
2.6009-2.68490.35251400.32247933X-RAY DIFFRACTION100
2.6849-2.78080.29861420.30517925X-RAY DIFFRACTION100
2.7808-2.89220.31461430.26637940X-RAY DIFFRACTION100
2.8922-3.02380.29521420.2477915X-RAY DIFFRACTION100
3.0238-3.18320.26241430.23867972X-RAY DIFFRACTION100
3.1832-3.38270.27861420.23497944X-RAY DIFFRACTION100
3.3827-3.64390.25611430.2067957X-RAY DIFFRACTION100
3.6439-4.01060.23531440.18627983X-RAY DIFFRACTION100
4.0106-4.59090.17491430.16667987X-RAY DIFFRACTION100
4.5909-5.78390.22441430.17898003X-RAY DIFFRACTION100
5.7839-500.22961460.17588116X-RAY DIFFRACTION100
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)
16.8496-2.9707-2.41857.41892.83832.23740.1974-0.57151.54180.73920.4467-1.3777-0.96860.3469-0.64611.7730.0133-0.1031.1531-0.15991.0776-22.527682.5125-15.3778
22.7881-1.2625-2.01932.58911.68314.61420.5054-0.10620.87760.1099-0.0068-0.2782-1.247-0.2807-0.35920.90230.10790.08830.54840.11180.9235-27.09376.7132-45.2128
38.1486-1.2954-1.48734.78251.13294.2554-0.03560.2597-0.28390.24840.2573-0.57950.06440.5768-0.20690.361-0.0716-0.02920.66430.0150.70885.961351.0731-68.1268
42.3225-0.1866-0.88225.48791.03533.0329-0.2315-0.3251-0.59160.97740.13760.48430.6126-0.40410.01410.80730.04010.18750.73190.24470.8538-35.553746.3831-33.7602
54.29821.5624-3.88921.6163-1.26615.5185-0.58990.5302-1.02260.13430.0570.22990.9612-0.46370.58930.8498-0.12830.10580.6056-0.05711.2394-18.843127.9944-55.2033
64.3978-1.24030.56844.1938-1.26894.945-0.26870.2655-0.25010.1695-0.062-0.11280.3110.1860.33320.4512-0.04190.03880.48640.12530.8018-20.761241.505-53.0647
71.73880.05510.70011.93362.352.4330.3362-1.316-0.39611.52860.3484-0.42560.98310.0456-0.64952.789-0.5776-0.3752.1860.27661.0388-16.3549-6.072122.6327
82.41881.24961.21425.2787-2.24822.93050.6321-1.0381-0.33470.7789-0.5612-1.09170.34070.2325-0.06011.9204-0.4478-0.091.68840.10750.8471-16.00925.80628.7052
92.05161.6061-0.00752.1797-0.232.39440.8484-1.31880.36821.7942-0.5166-0.0005-0.12250.1131-0.24372.4403-0.7162-0.03191.8915-0.1470.8176-18.506311.23569.577
107.5418-1.98920.43767.3940.35474.61730.38780.05390.56061.0811-0.2543-1.4348-0.6241.0656-0.12721.2259-0.385-0.15981.14590.05970.8097-2.020314.1425-14.0158
114.88520.6843-2.72743.60173.11418.34360.2374-0.25710.26040.5724-0.15220.0639-0.46510.1158-0.08180.7256-0.073-0.01080.42770.14740.5862-17.219913.4256-26.1193
122.971-1.4372-1.02042.69840.74534.68640.050.3417-0.17820.0750.0892-0.32210.23170.6872-0.17550.313-0.0224-0.06520.75420.06330.7027-2.8682-8.4066-47.8648
130.7885-0.825-0.40335.2477-0.89897.4563-0.05430.0795-0.05910.2988-0.0148-0.263-0.05680.79820.0610.32350.0018-0.05570.66310.12870.6464-4.0046-4.3036-42.9806
146.69992.60221.92427.4412-2.58615.43340.22550.3067-1.0897-0.7583-0.36820.49280.92750.4770.11320.5150.06470.06950.8184-0.01670.733-8.2886-13.5418-52.0089
154.53180.1101-0.18455.4494-0.38444.12550.3949-0.61580.15481.3419-0.26450.44340.3697-0.8464-0.21851.5107-0.4460.35451.3814-0.04980.7614-38.9799-1.7862-7.9883
161.76590.75081.84231.5903-0.05331.79590.6535-0.891-0.05551.1574-0.52090.80470.4303-1.3721-0.15411.5259-0.56070.50242.0462-0.12911.1518-47.6436-9.8252-11.3994
173.8237-1.63814.98476.587-1.70598.0344-0.119-0.21570.64040.2119-0.44030.8668-0.7416-1.35090.67611.0109-0.02490.32952.0523-0.15341.4713-58.4641-5.9171-25.2465
182.58360.6761-1.33031.92182.36736.30690.10450.0052-0.47790.3388-0.40170.0720.408-0.3770.3110.44040.02320.00830.67020.13950.7181-29.153-14.868-48.2375
198.01313.98352.80445.96351.31725.21990.27760.0496-0.3630.4553-0.3667-0.33470.0966-0.23740.11090.7463-0.09290.11090.69940.08840.6375-32.579-5.0636-28.9361
203.93870.238-0.79592.35920.50430.22760.5358-0.6387-0.41611.5794-0.5737-0.92770.7026-0.1358-0.03281.7689-0.1873-0.28691.18390.30691.0167-11.5925-6.2729-12.5123
217.0154-4.4942-0.79633.47073.19879.84150.3887-0.3713-1.15641.5646-1.04050.0021.046-1.10030.57171.3184-0.14780.19240.99220.12181.1196-10.9227-12.7494-23.9456
224.34430.648-2.72877.12567.2322.02250.8919-1.725-0.93132.2324-0.8852-0.82260.05850.9437-0.44312.3002-0.6499-0.49991.77520.15430.9333-8.03714.3441-1.7657
238.41461.4848-4.06316.8678-4.22067.12030.0243-0.88750.93281.12530.4003-0.715-0.77841.2678-0.45650.98490.0236-0.13110.9182-0.24741.1762-14.745574.0502-37.9446
243.55064.4093-1.38029.15963.21717.9246-0.3381-0.8088-0.69952.49180.6265-0.48730.68650.4168-0.29281.4130.4709-0.15881.61520.08121.05291.281852.0605-45.9961
253.6119-5.4302-2.82898.30591.74935.2693-0.2913-0.61151.26252.39480.2164-0.9026-0.12021.5481-0.05810.95950.0499-0.02751.0944-0.17611.1346-13.182671.0015-41.4946
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 83 )
2X-RAY DIFFRACTION2chain 'A' and (resid 84 through 421 )
3X-RAY DIFFRACTION3chain 'A' and (resid 422 through 553 )
4X-RAY DIFFRACTION4chain 'B' and (resid 4 through 174 )
5X-RAY DIFFRACTION5chain 'B' and (resid 175 through 325 )
6X-RAY DIFFRACTION6chain 'B' and (resid 326 through 428 )
7X-RAY DIFFRACTION7chain 'C' and (resid 1 through 59 )
8X-RAY DIFFRACTION8chain 'C' and (resid 60 through 114 )
9X-RAY DIFFRACTION9chain 'C' and (resid 115 through 269 )
10X-RAY DIFFRACTION10chain 'C' and (resid 270 through 325 )
11X-RAY DIFFRACTION11chain 'C' and (resid 326 through 421 )
12X-RAY DIFFRACTION12chain 'C' and (resid 422 through 473 )
13X-RAY DIFFRACTION13chain 'C' and (resid 474 through 527 )
14X-RAY DIFFRACTION14chain 'C' and (resid 528 through 553 )
15X-RAY DIFFRACTION15chain 'D' and (resid 6 through 83 )
16X-RAY DIFFRACTION16chain 'D' and (resid 84 through 174 )
17X-RAY DIFFRACTION17chain 'D' and (resid 175 through 238 )
18X-RAY DIFFRACTION18chain 'D' and (resid 239 through 363 )
19X-RAY DIFFRACTION19chain 'D' and (resid 364 through 427 )
20X-RAY DIFFRACTION20chain 'F' and (resid 0 through 16 )
21X-RAY DIFFRACTION21chain 'F' and (resid 17 through 26 )
22X-RAY DIFFRACTION22chain 'F' and (resid 27 through 33 )
23X-RAY DIFFRACTION23chain 'E' and (resid -1 through 10 )
24X-RAY DIFFRACTION24chain 'E' and (resid 11 through 20 )
25X-RAY DIFFRACTION25chain 'E' and (resid 21 through 33 )

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