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- PDB-4ivf: Crystal structure of glutathione transferase homolog from Loddero... -

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Basic information

Entry
Database: PDB / ID: 4ivf
TitleCrystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per subunit
ComponentsPutative uncharacterized protein
KeywordsTRANSFERASE / GST / glutathione S-transferase / Enzyme Function Initiative / EFI / Structural Genomics
Function / homology
Function and homology information


glutathione transferase
Similarity search - Function
Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily ...Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 - #10 / Glutathione S-transferase, C-terminal / Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Glutaredoxin / Glutaredoxin / Thioredoxin-like superfamily / Up-down Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
CITRIC ACID / GLUTATHIONE / glutathione transferase
Similarity search - Component
Biological speciesLodderomyces elongisporus (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsVetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. ...Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / Hillerich, B. / Love, J. / Seidel, R.D. / Imker, H.J. / Armstrong, R.N. / Gerlt, J.A. / Almo, S.C. / Enzyme Function Initiative (EFI)
CitationJournal: To be Published
Title: Crystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per subunit
Authors: Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / ...Authors: Vetting, M.W. / Toro, R. / Bhosle, R. / Al Obaidi, N.F. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Washington, E. / Scott Glenn, A. / Chowdhury, S. / Evans, B. / Hammonds, J. / Hillerich, B. / Love, J. / Seidel, R.D. / Imker, H.J. / Armstrong, R.N. / Gerlt, J.A. / Almo, S.C. / Enzyme Function Initiative (EFI)
History
DepositionJan 22, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 13, 2013Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2017Group: Refinement description / Category: software
Revision 1.2Sep 20, 2023Group: 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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Putative uncharacterized protein
B: Putative uncharacterized protein
C: Putative uncharacterized protein
D: Putative uncharacterized protein
E: Putative uncharacterized protein
F: Putative uncharacterized protein
G: Putative uncharacterized protein
H: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)217,01525
Polymers211,9068
Non-polymers5,10917
Water22,8971271
1
A: Putative uncharacterized protein
F: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,2066
Polymers52,9762
Non-polymers1,2294
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6960 Å2
ΔGint-35 kcal/mol
Surface area18390 Å2
MethodPISA
2
B: Putative uncharacterized protein
G: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,2066
Polymers52,9762
Non-polymers1,2294
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6940 Å2
ΔGint-34 kcal/mol
Surface area18080 Å2
MethodPISA
3
C: Putative uncharacterized protein
D: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,2066
Polymers52,9762
Non-polymers1,2294
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7000 Å2
ΔGint-34 kcal/mol
Surface area17900 Å2
MethodPISA
4
E: Putative uncharacterized protein
H: Putative uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,3987
Polymers52,9762
Non-polymers1,4215
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7360 Å2
ΔGint-33 kcal/mol
Surface area17780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.598, 112.476, 194.384
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
Putative uncharacterized protein


Mass: 26488.191 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lodderomyces elongisporus (fungus) / Strain: NRRL YB-4239 / Gene: LELG_04376 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A5E437
#2: Chemical
ChemComp-GSH / GLUTATHIONE


Mass: 307.323 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C10H17N3O6S
#3: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1271 / 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: 2.34 Å3/Da / Density % sol: 47.37 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: Protein (10 mM Hepes pH 7.5, 100 mM NaCl); Reservoir (0.17M Amm Acetate, 0.085 M Sodium Citrate pH 5.6, 25.5% Peg4000, 15% (V/V) glycerol); Cryoprotection (Reservoir taken to 20% glycerol), ...Details: Protein (10 mM Hepes pH 7.5, 100 mM NaCl); Reservoir (0.17M Amm Acetate, 0.085 M Sodium Citrate pH 5.6, 25.5% Peg4000, 15% (V/V) glycerol); Cryoprotection (Reservoir taken to 20% glycerol), vapor diffusion, sitting drop, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 31-ID / Wavelength: 0.9793 Å
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Oct 16, 2012 / Details: MIRRORS
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 2.2→194.384 Å / Num. all: 99618 / Num. obs: 99618 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Rsym value: 0.175 / Net I/σ(I): 7.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRsym value% possible all
2.2-2.326.10.71.187431142860.797.9
2.32-2.466.10.5431.482620135200.54398
2.46-2.6360.4151.877366128050.41598.3
2.63-2.8460.2962.571652119200.29698.3
2.84-3.1160.2143.465824110350.21498.6
3.11-3.4860.1544.559681100250.15498.7
3.48-4.0260.1314.85364689270.13199
4.02-4.926.20.1195.14728576240.11999.5
4.92-6.966.70.0926.44075660540.092100
6.96-40.0226.70.057102282734220.05798.6

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Processing

Software
NameVersionClassificationNB
MOSFLMdata reduction
SCALA3.3.20data scaling
PHENIX1.8.1_1168refinement
PDB_EXTRACT3.11data extraction
BALBESphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3GX0

3gx0


Resolution: 2.2→37.126 Å / Occupancy max: 1 / Occupancy min: 0.41 / FOM work R set: 0.8365 / SU ML: 0.26 / σ(F): 0 / σ(I): 0 / Phase error: 23.23 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2234 4984 5.01 %RANDOM
Rwork0.1559 ---
obs0.1592 99532 98.2 %-
all-99532 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 98.71 Å2 / Biso mean: 24.4895 Å2 / Biso min: 2.01 Å2
Refinement stepCycle: LAST / Resolution: 2.2→37.126 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14481 0 333 1271 16085
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00715197
X-RAY DIFFRACTIONf_angle_d1.01820619
X-RAY DIFFRACTIONf_chiral_restr0.0752185
X-RAY DIFFRACTIONf_plane_restr0.0052655
X-RAY DIFFRACTIONf_dihedral_angle_d13.6365587
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.2250.30111540.21233082323697
2.225-2.25120.30671560.22563111326798
2.2512-2.27860.28581750.21183046322198
2.2786-2.30750.321790.20213107328698
2.3075-2.33780.27141640.20413091325597
2.3378-2.36980.27741570.18963129328698
2.3698-2.40370.2941580.19753086324497
2.4037-2.43960.27521870.2053111329898
2.4396-2.47770.29191780.19713062324098
2.4777-2.51830.29391470.19633139328698
2.5183-2.56170.27471840.193088327298
2.5617-2.60830.27531830.1783116329998
2.6083-2.65840.26121660.17683110327698
2.6584-2.71270.2351640.1693111327598
2.7127-2.77160.28331480.16573147329598
2.7716-2.83610.2551660.16363112327898
2.8361-2.9070.2331690.16333128329798
2.907-2.98560.27671650.16443156332198
2.9856-3.07340.23231400.16633148328898
3.0734-3.17250.25371550.16133145330098
3.1725-3.28580.22911690.15383176334598
3.2858-3.41730.20181700.14233167333798
3.4173-3.57270.17322030.12943122332599
3.5727-3.76090.16791660.12353183334998
3.7609-3.99630.18021840.12533156334099
3.9963-4.30440.17771610.12273241340299
4.3044-4.73680.16931470.11923254340199
4.7368-5.42040.17321540.123532723426100
5.4204-6.82220.22691430.149433463489100
6.8222-37.13110.17771920.16193406359899
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)
12.70630.15540.39751.820.17372.63370.11510.06290.1818-0.1591-0.00610.0623-0.1699-0.1359-0.06860.09140.00980.01480.19060.03370.11993.330695.224168.3915
26.15252.41811.96258.58861.97275.5003-0.1506-0.16520.50670.58370.0330.2519-0.3285-0.14940.09610.14850.0357-0.0060.2274-0.01870.1417-3.816495.964783.859
30.9939-0.3938-0.4321.407-0.15091.39140.02980.4522-0.0417-0.0547-0.05250.11660.0363-0.49810.02210.10210.00750.01580.28080.00130.10920.051585.504370.9047
42.8819-0.4553-0.99694.2780.6982.64890.04520.76950.0057-0.5501-0.0571-0.09430.2702-0.2029-0.0080.1721-0.02590.03850.4374-0.0740.092613.056580.649258.5985
50.41230.08030.55774.15612.41853.8229-0.05910.1816-0.1786-0.0839-0.1179-0.07980.02710.00240.10860.1084-0.00520.03170.2537-0.06970.058917.827679.63471.6484
62.89430.44450.26954.09061.84247.5422-0.118-0.23980.28530.1461-0.07740.1816-0.3006-0.05720.20940.0663-0.0006-0.0170.1327-0.01180.169816.974696.349890.077
70.8825-0.1091-0.33660.88170.47433.49180.0151-0.10260.05490.0397-0.0196-0.21110.12610.2083-0.04640.077-0.0194-0.02620.11040.0020.163926.436589.679982.9498
84.3567-0.7810.89281.74330.98461.70150.250.45490.2695-0.32790.1886-0.3975-0.1510.1604-0.35810.1847-0.04630.08780.3307-0.00940.202225.477185.757762.093
94.421.54741.97331.50140.07043.1572-0.1655-0.05410.2871-0.14530.1037-0.0019-0.4263-0.27720.03580.08570.0302-0.01650.13210.02630.183417.86795.888875.0205
103.6077-0.5811.68021.23720.40423.8974-0.07820.1120.1823-0.10580.0431-0.2462-0.40170.16410.04910.0833-0.01570.00410.13040.05160.226126.794197.513571.0937
115.33172.2562-4.32522.3132-0.45494.92430.70350.11041.0828-0.0897-0.48630.0269-0.9094-0.2229-0.65380.2368-0.0080.01090.30110.0760.26729.801103.248468.0962
121.9093-1.1185-0.93171.35710.27810.58330.0469-0.17551.1120.11250.1214-0.511-0.34240.20620.14530.228-0.052-0.00210.0950.07070.725259.085568.598367.2
132.5427-1.68722.25441.3767-1.50663.5449-0.0604-0.01740.7153-0.080.30750.2666-0.3245-0.3865-0.16170.1840.00810.02790.25440.11510.498648.473665.18961.5759
142.7668-0.44071.20380.7141-0.29332.1288-0.02090.25420.297-0.0455-0.0529-0.1006-0.01280.2770.08270.11360.00390.00590.16010.03780.17462.800948.256361.9152
152.7601-0.92450.24271.9335-0.59791.98990.03680.3260.5780.0145-0.0237-0.5015-0.27560.5525-0.00790.1553-0.04920.01050.27590.03140.291171.424651.678858.7061
162.82440.1824-1.56790.29320.01654.16110.119-0.08340.8597-0.0918-0.1783-0.1005-0.60180.5195-0.27980.262-0.13970.04760.35370.2270.700769.147165.247754.9346
172.43180.5420.15892.4883-0.09921.40640.00910.0547-0.7107-0.03550.0457-0.2430.31180.0634-0.0420.21120.03550.02270.2066-0.02370.324118.043613.380878.2578
181.90860.51540.09171.05370.21741.76250.0779-0.1374-0.31020.1052-0.02930.01110.2502-0.2425-0.04780.1773-0.02930.01620.20580.06280.21720.774120.535388.0043
190.12640.31340.42281.83812.06363.20440.423-0.5591-0.67140.51110.0907-0.40750.4360.2633-0.37570.4454-0.0269-0.00250.3580.1410.493513.38917.558293.2376
201.3708-0.2909-0.40891.5645-0.34652.2751-0.05150.02890.0451-0.04110.03910.06930.0366-0.29620.01390.098-0.0005-0.01290.28490.02270.179-3.89636.741373.3686
215.151.613-0.94333.01421.50891.6699-0.08680.61610.0562-0.5027-0.02810.22630.1024-0.37810.08140.2225-0.0538-0.01690.3568-0.10960.18748.966527.270658.7792
221.93620.0672-0.25861.38760.10522.68630.0227-0.0675-0.12930.061-0.0851-0.09730.09750.01620.07830.0777-0.0131-0.00890.11870.03640.146417.607733.608978.9277
233.17510.13031.43550.8411-0.6862.1406-0.09840.05050.5080.00130.0290.1165-0.256-0.04850.06720.14480.03850.01720.13570.00760.21415.398643.821772.8993
242.17750.1250.05760.97140.14442.0905-0.0188-0.0493-0.2244-0.02360.0039-0.01830.1566-0.03170.00220.0971-0.00010.01840.05350.01750.090638.176933.285331.6331
250.59751.0247-0.41872.66751.72586.8727-0.0157-0.1682-0.15710.30230.0633-0.7476-0.38660.82920.06210.179-0.0458-0.09980.22820.0630.269551.878149.712634.7142
262.49890.77032.15151.00831.05253.3958-0.08850.1045-0.00120.04550.0219-0.0506-0.1711-0.12260.06280.11770.02150.00110.11840.0280.099930.796948.235222.0511
270.9613-0.38340.78240.73-0.03571.4214-0.09920.23890.1386-0.1525-0.0114-0.0878-0.15310.19220.07290.1637-0.0257-0.00270.18470.05670.097939.404947.824115.9654
281.39490.31650.11192.1238-0.10421.6174-0.01030.1663-0.2461-0.04130.0613-0.21560.23850.1252-0.0550.13650.0285-0.01130.1904-0.0590.133122.328368.24579.0563
293.4052-0.85050.34780.2315-0.47957.22950.02270.6302-0.7319-0.31680.0210.18620.49370.0099-0.05950.2102-0.0576-0.0380.2779-0.1260.25242.33265.870970.8919
301.4180.3360.69211.42740.56051.81130.0113-0.01650.01580.09360.01660.10780.1503-0.1029-0.03530.1042-0.01060.02660.1383-0.0140.07816.555378.712189.0636
312.3338-0.88140.01740.9274-0.03050.93650.0272-0.3947-0.27920.01360.09510.10040.18470.0559-0.13680.2134-0.03030.00850.1820.03650.14599.140567.196995.1479
323.104-0.1009-0.37621.62980.13691.72-0.11080.0366-0.40840.10740.0443-0.01350.27910.1130.03010.14410.00590.00170.13110.0150.103649.182434.163368.2077
331.92410.37121.26440.9527-0.12172.3130.02720.11850.0111-0.0114-0.0506-0.09320.0529-0.0292-0.00840.09380.00510.01880.11440.02640.078144.511141.781459.1321
341.998-0.06290.28284.1252-0.5817.1502-0.17080.21960.1614-0.5666-0.17380.5976-0.0062-0.17340.16970.15840.0226-0.00370.26680.03630.176734.644353.561764.5191
351.8236-0.22390.37290.9757-1.73414.06260.2619-0.13630.49350.01280.1673-0.1048-0.2707-0.2736-0.34180.16540.01460.0130.0938-0.00820.235747.234756.907669.174
366.0636-1.76332.66134.2136-1.89945.1829-0.1538-0.57580.08370.18720.0592-0.057-0.01660.0260.03910.11450.03190.01420.2084-0.04640.175762.657643.908283.5402
373.3859-0.46111.73950.4353-0.6641.4172-0.0943-0.34450.47940.13350.1425-0.1934-0.13310.08340.02910.14950.0311-0.04420.2712-0.11840.19148.605456.785981.5267
381.21880.4516-0.28152.20080.96621.9106-0.0295-0.42210.01170.19070.0732-0.10110.0488-0.0772-0.04790.15320.0501-0.00660.2021-0.03830.101345.354348.701285.0981
394.6182-0.53472.47781.4123-0.42021.49630.1131-0.021-0.54950.16710.01140.04350.19090.2613-0.10960.2305-0.00250.02030.27250.07660.125346.236933.587181.9957
400.95350.2043-0.10520.9631-0.22541.3983-0.1797-0.02420.49930.0585-0.020.1141-0.7384-0.14860.05260.37410.0363-0.11040.0864-0.02130.260231.004364.596735.6087
411.93880.16741.0610.74980.38582.1741-0.0271-0.13240.07160.068-0.06960.0306-0.0841-0.30140.06970.10240.03420.00710.1482-0.01530.084123.564245.094136.8414
423.71612.308-0.87673.8281.85352.5986-0.34820.02670.72040.0196-0.01120.2735-0.4826-0.63010.20790.1810.0767-0.01360.1922-0.06210.150417.907852.056137.5337
431.32250.67950.23422.97360.22611.5526-0.0173-0.3570.36630.204-0.06750.3728-0.3866-0.6975-0.00680.19040.09840.01060.4077-0.07050.205914.708451.631644.1065
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 36 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 37 through 52 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 53 through 89 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 90 through 101 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 102 through 116 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 117 through 136 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 137 through 160 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 161 through 175 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 176 through 191 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 192 through 210 )A0
11X-RAY DIFFRACTION11chain 'A' and (resid 211 through 225 )A0
12X-RAY DIFFRACTION12chain 'B' and (resid 5 through 63 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 64 through 89 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 90 through 175 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 176 through 209 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 210 through 222 )B0
17X-RAY DIFFRACTION17chain 'C' and (resid 5 through 89 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 90 through 210 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 211 through 230 )C0
20X-RAY DIFFRACTION20chain 'D' and (resid 5 through 89 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 90 through 101 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 102 through 175 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 176 through 223 )D0
24X-RAY DIFFRACTION24chain 'E' and (resid 5 through 89 )E0
25X-RAY DIFFRACTION25chain 'E' and (resid 90 through 101 )E0
26X-RAY DIFFRACTION26chain 'E' and (resid 102 through 136 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 137 through 230 )E0
28X-RAY DIFFRACTION28chain 'F' and (resid 5 through 89 )F0
29X-RAY DIFFRACTION29chain 'F' and (resid 90 through 101 )F0
30X-RAY DIFFRACTION30chain 'F' and (resid 102 through 191 )F0
31X-RAY DIFFRACTION31chain 'F' and (resid 192 through 230 )F0
32X-RAY DIFFRACTION32chain 'G' and (resid 5 through 63 )G0
33X-RAY DIFFRACTION33chain 'G' and (resid 64 through 89 )G0
34X-RAY DIFFRACTION34chain 'G' and (resid 90 through 101 )G0
35X-RAY DIFFRACTION35chain 'G' and (resid 102 through 116 )G0
36X-RAY DIFFRACTION36chain 'G' and (resid 117 through 136 )G0
37X-RAY DIFFRACTION37chain 'G' and (resid 137 through 175 )G0
38X-RAY DIFFRACTION38chain 'G' and (resid 176 through 210 )G0
39X-RAY DIFFRACTION39chain 'G' and (resid 211 through 230 )G0
40X-RAY DIFFRACTION40chain 'H' and (resid 5 through 89 )H0
41X-RAY DIFFRACTION41chain 'H' and (resid 90 through 175 )H0
42X-RAY DIFFRACTION42chain 'H' and (resid 176 through 191 )H0
43X-RAY DIFFRACTION43chain 'H' and (resid 192 through 222 )H0

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