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- PDB-3q3o: Toluene 4 monooxygenase HD complex with phenol -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 3q3o
TitleToluene 4 monooxygenase HD complex with phenol
Components(Toluene-4-monooxygenase system protein ...) x 4
KeywordsOXIDOREDUCTASE / aromatic hydrocarbon catabolism / iron / multi-component monooxygenase / aromatic hydroxylation
Function / homology
Function and homology information


toluene 4-monooxygenase / toluene 4-monooxygenase activity / toluene catabolic process / monooxygenase activity / metal ion binding
Similarity search - Function
Monooxygenase component MmoB/DmpM / Phenol Hydroxylase P2 Protein / TmoB-like / Toluene-4-monooxygenase system B / TmoB-like superfamily / Toluene-4-monooxygenase system protein B (TmoB) / Monooxygenase component MmoB/DmpM / Monooxygenase component MmoB/DmpM superfamily / MmoB/DmpM family / Methane/phenol monooxygenase, hydroxylase component ...Monooxygenase component MmoB/DmpM / Phenol Hydroxylase P2 Protein / TmoB-like / Toluene-4-monooxygenase system B / TmoB-like superfamily / Toluene-4-monooxygenase system protein B (TmoB) / Monooxygenase component MmoB/DmpM / Monooxygenase component MmoB/DmpM superfamily / MmoB/DmpM family / Methane/phenol monooxygenase, hydroxylase component / Propane/methane/phenol/toluene hydroxylase / Methane/Phenol/Alkene Hydroxylase / Ribonucleotide Reductase, subunit A / Ribonucleotide Reductase, subunit A / Ribonucleotide reductase-like / Ferritin-like superfamily / Ubiquitin-like (UB roll) / Roll / Alpha-Beta Complex / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / PHENOL / Toluene-4-monooxygenase system, hydroxylase component subunit alpha / Toluene-4-monooxygenase system, hydroxylase component subunit gamma / Toluene-4-monooxygenase system, effector component / Toluene-4-monooxygenase system, hydroxylase component subunit beta / Toluene-4-monooxygenase system, hydroxylase component subunit alpha
Similarity search - Component
Biological speciesPseudomonas mendocina (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.95 Å
AuthorsAcheson, J.F. / Bailey, L.J. / Fox, B.G.
CitationJournal: Biochemistry / Year: 2012
Title: Crystallographic analysis of active site contributions to regiospecificity in the diiron enzyme toluene 4-monooxygenase.
Authors: Bailey, L.J. / Acheson, J.F. / McCoy, J.G. / Elsen, N.L. / Phillips, G.N. / Fox, B.G.
History
DepositionDec 22, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 28, 2011Provider: repository / Type: Initial release
Revision 1.1Feb 8, 2012Group: Database references
Revision 1.2Feb 29, 2012Group: Database references
Revision 1.3Nov 8, 2017Group: Refinement description / Category: software
Revision 1.4Feb 21, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_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_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: Toluene-4-monooxygenase system protein A
B: Toluene-4-monooxygenase system protein E
C: Toluene-4-monooxygenase system protein B
E: Toluene-4-monooxygenase system protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,49113
Polymers115,5764
Non-polymers9159
Water11,007611
1
A: Toluene-4-monooxygenase system protein A
B: Toluene-4-monooxygenase system protein E
C: Toluene-4-monooxygenase system protein B
E: Toluene-4-monooxygenase system protein D
hetero molecules

A: Toluene-4-monooxygenase system protein A
B: Toluene-4-monooxygenase system protein E
C: Toluene-4-monooxygenase system protein B
E: Toluene-4-monooxygenase system protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)232,98126
Polymers231,1528
Non-polymers1,82918
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555x,-y,-z1
Buried area38650 Å2
ΔGint-152 kcal/mol
Surface area61190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.698, 116.393, 180.789
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11B-309-

1PE

21A-760-

HOH

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Components

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Toluene-4-monooxygenase system protein ... , 4 types, 4 molecules ABCE

#1: Protein Toluene-4-monooxygenase system protein A / Alpha hydroxylase


Mass: 58169.344 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas mendocina (bacteria) / Strain: KR1 / Gene: Q00456, tmoA / Plasmid: p58kABE / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21
References: UniProt: Q6Q8Q7, UniProt: Q00456*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of ...References: UniProt: Q6Q8Q7, UniProt: Q00456*PLUS, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
#2: Protein Toluene-4-monooxygenase system protein E / Beta hydroxylase


Mass: 36176.645 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas mendocina (bacteria) / Strain: KR1 / Gene: Q00460, tmoE / Plasmid: p58kABE / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21
References: UniProt: Q00460, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
#3: Protein Toluene-4-monooxygenase system protein B / Gamma hydroxylase


Mass: 9600.989 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas mendocina (bacteria) / Strain: KR1 / Gene: Q00457, tmoB / Plasmid: p58kABE / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21
References: UniProt: Q00457, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
#4: Protein Toluene-4-monooxygenase system protein D / Effector


Mass: 11629.032 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas mendocina (bacteria) / Strain: KR1 / Gene: Q00459, tmoD / Plasmid: pCDtet / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21(DE3)
References: UniProt: Q00459, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

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Non-polymers , 4 types, 620 molecules

#5: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe
#6: Chemical
ChemComp-IPH / PHENOL


Mass: 94.111 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H6O
#7: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400


Mass: 238.278 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 611 / 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: 2.25 Å3/Da / Density % sol: 44.11 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 200 mM ammonium chloride, 50 mM phenol, 20% PEG3350, 100 mM Bis-Tris, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 7, 2010 / Details: mirrors and beryllium lenses
RadiationMonochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 77602 / % possible obs: 94.1 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.05 / Χ2: 1.274 / Net I/σ(I): 13.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.9-1.934.10.31827310.902167.5
1.93-1.974.20.28829530.893171.7
1.97-2.014.30.26132250.924179
2.01-2.054.20.23834230.932184.3
2.05-2.094.30.21636721.007189.8
2.09-2.144.30.18938371.003194.3
2.14-2.194.30.16540201.043197.5
2.19-2.254.40.15540481.131198.8
2.25-2.324.50.13740891.203199.9
2.32-2.394.50.12541091.3081100
2.39-2.484.50.11240781.504199.9
2.48-2.584.60.09840851.5981100
2.58-2.74.60.08241261.526199.9
2.7-2.844.60.06641381.374199.9
2.84-3.024.70.05241051.3751100
3.02-3.254.70.04841361.62199.9
3.25-3.584.70.04441211.961199.8
3.58-4.094.80.03341821.499199.9
4.09-5.164.80.02541981.033199.8
5.16-504.60.02543261.013199

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.12 Å47.04 Å
Translation2.12 Å47.04 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
PHENIX1.6.4_486refinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.95→31.659 Å / Occupancy max: 1 / Occupancy min: 0.11 / SU ML: 0.23 / σ(F): 0 / Phase error: 20.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.192 3536 5.03 %
Rwork0.1499 --
obs0.1521 70254 92.55 %
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 49.799 Å2 / ksol: 0.359 e/Å3
Displacement parametersBiso max: 116.8 Å2 / Biso mean: 34.8964 Å2 / Biso min: 12.58 Å2
Baniso -1Baniso -2Baniso -3
1-10.1525 Å2-0 Å2-0 Å2
2---2.0294 Å20 Å2
3----8.1231 Å2
Refinement stepCycle: LAST / Resolution: 1.95→31.659 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8022 0 60 611 8693
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0068408
X-RAY DIFFRACTIONf_angle_d0.99311412
X-RAY DIFFRACTIONf_chiral_restr0.0731166
X-RAY DIFFRACTIONf_plane_restr0.0051490
X-RAY DIFFRACTIONf_dihedral_angle_d13.4863084
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.95-2.01970.25422760.18935064534071
2.0197-2.10050.23832890.16995849613882
2.1005-2.19610.22093190.16686426674590
2.1961-2.31190.23273830.15416690707394
2.3119-2.45670.19283520.14766868722096
2.4567-2.64630.20343560.15196964732097
2.6463-2.91240.22473910.16457060745198
2.9124-3.33340.21463840.16987151753599
3.3334-4.19820.17423900.138772337623100
4.1982-31.66310.15123960.13067413780999
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)
10.32470.1198-0.03210.2299-0.08860.26790.0145-0.2668-0.0450.09470.03590.10550.00470.1746-0.04950.1911-0.0051-0.01410.2688-0.02820.216835.28129.993626.958
20.571-0.4899-0.18640.43860.01030.12140.0026-0.1381-0.06870.03130.111-0.1733-0.02010.0553-0.09740.1908-0.0202-0.01560.15440.01220.194326.088.572925.8988
30.16390.31230.24880.55370.33620.8121-0.1318-0.14-0.0515-0.11610.02510.0316-0.1524-0.22720.09260.24560.0213-0.03060.2189-0.00370.17884.53636.2919-0.3176
40.11710.1342-0.08760.11980.51340.59010.0254-0.02560.0081-0.1554-0.0579-0.0372-0.3044-0.11870.03240.26940.0757-0.01660.15060.00250.15459.558218.309815.668
50.4955-0.1769-0.12410.18360.07340.5649-0.0237-0.0185-0.05840.0666-0.0179-0.0121-0.1134-0.10790.03710.22980.0193-0.00360.19520.01160.18747.37576.229118.8453
60.9827-0.0688-0.27990.30650.14340.455-0.046-0.39090.07740.124-0.0274-0.012-0.0061-0.25360.03990.1380.0679-0.01320.17540.00610.09338.796414.145735.1149
70.2379-0.1405-0.1340.68270.28360.8004-0.0176-0.1433-0.0055-0.0551-0.18550.1185-0.0157-0.42640.18580.18780.0881-0.05760.3827-0.05920.2001-7.466110.487925.0292
80.4185-0.2965-0.43650.27680.24130.5811-0.19020.0462-0.0408-0.0092-0.27120.35840.0432-0.87180.40030.18030.0756-0.06610.6764-0.19860.3465-20.10497.842727.8227
90.38530.04520.05960.65340.60441.24120.0511-0.1958-0.026-0.1269-0.23890.1268-0.3846-0.50820.21120.22630.2046-0.08410.3689-0.08940.1974-9.583526.539830.1944
100.6022-0.2404-0.39130.42630.58691.08630.09320.27630.1599-0.4669-0.05880.1363-0.5516-0.25620.16960.41830.2949-0.15680.2654-0.05310.1824-10.338830.932113.7264
110.26290.05680.02620.118-0.04070.0193-0.254-0.06120.2229-0.1947-0.10650.0996-0.4644-0.01330.26740.93470.3656-0.24060.3612-0.07290.2328-4.025431.975-0.8781
120.2080.01230.00030.04480.1330.1710.13820.07880.1406-0.4075-0.0752-0.1419-0.6439-0.2795-0.03040.52140.1158-0.00250.19120.02360.216412.27228.64728.3593
130.5147-0.0171-0.1746-0.02180.06790.7881-0.00690.04410.2402-0.4002-0.022-0.0476-0.6109-0.29960.00680.51110.00520.02340.1373-0.01490.285522.017733.724816.9466
140.0379-0.01960.05980.01810.07860.1570.05290.1378-0.0248-0.035-0.0133-0.049-0.15590.0417-0.05080.2744-0.030.02580.14860.00490.199127.0869.32763.2931
150.6404-1.0083-0.36611.61190.53161.1583-0.05930.1251-0.3423-0.16170.24160.12750.31660.3046-0.1850.27450.0171-0.01430.2624-0.03840.254344.2192-6.20957.2485
160.0808-0.18480.18941.0290.23111.14890.0899-0.12220.14190.19340.1217-0.80770.23840.6378-0.25050.20940.01350.0070.476-0.07590.373755.47241.473215.3129
170.3563-0.0364-0.15980.28440.38991.11010.0511-0.07460.079-0.09270.0823-0.0522-0.23350.2283-0.13250.1604-0.08830.01910.1525-0.03990.161839.274515.617618.6117
180.59650.4051-0.35430.8569-0.05611.0592-0.02850.00850.1741-0.13790.1079-0.2284-0.27920.3332-0.11840.2515-0.1130.06230.2365-0.05910.213743.367211.81595.3979
191.1977-0.3546-0.61230.42840.61240.83490.36370.35820.4655-0.3933-0.0682-0.0518-0.74150.3402-0.2580.5929-0.16090.15970.1085-0.01750.393535.878436.32210.2496
200.31020.42880.13591.06730.0910.9288-0.11450.05270.2929-0.03050.1599-0.4856-0.30450.7003-0.10820.2459-0.18770.06320.4245-0.13130.398153.589419.999517.8058
210.3321-0.5172-0.09820.86660.11590.2480.0979-0.00520.1098-0.3028-0.40760.2885-0.3155-0.85270.23520.32540.3844-0.14920.5391-0.17730.3265-17.15734.415931.2855
220.0630.04380.02070.10960.10630.2139-0.10110.1279-0.0106-0.12170.04440.2861-0.1996-0.54240.13470.56070.5675-0.28940.7695-0.37580.6237-24.108941.557733.9007
230.0648-0.01260.0790.2530.00830.10720.18010.1032-0.0615-0.2379-0.23130.1972-0.1512-0.21190.06790.36040.4469-0.22030.8056-0.27550.4173-24.339529.858624.379
240.0776-0.0108-0.02670.46-0.00390.6332-0.1384-0.15460.5528-0.02690.0580.09220.0026-0.3160.11170.23450.2876-0.14091.1013-0.39090.6106-32.738928.91633.4473
251.16470.4969-0.47511.036-0.51760.6115-0.2502-0.3572-0.1597-0.1065-0.53890.23760.1052-0.21880.47830.15740.2348-0.00050.6735-0.30350.2871-20.55832.090541.6232
261.39720.1942-0.76772.51110.39581.5999-0.3156-0.86820.41450.028-0.29120.6351-0.0665-0.19580.43260.46220.3752-0.07570.9111-0.36490.5734-23.091339.197243.997
270.3123-0.5476-0.4180.9310.69830.5680.0244-0.1025-0.12830.1043-0.37250.3998-0.4921-0.91420.31780.33380.2611-0.07270.7239-0.25920.3805-18.273836.722239.5706
281.034-0.046-0.53190.24690.26080.5061-0.0981-0.3759-0.09160.222-0.16730.12820.21980.12830.23710.3758-0.0870.04390.535-0.04640.2547-4.3304-1.749338.1663
290.5114-0.2368-0.09490.35360.47341.8694-0.102-0.165-0.15760.08120.04210.14130.4-0.33720.06140.2161-0.01520.00070.2410.01050.20397.2281-7.784318.8451
301.9609-0.5047-1.14320.3688-0.12791.4391-0.4512-0.1127-0.56060.30640.19940.13260.68870.08960.23940.3756-0.00480.04030.15690.03490.2319.022-17.96122.4535
310.9491-0.0634-0.4930.66150.34212.41790.02770.0842-0.15730.1464-0.21570.19940.2022-0.60160.15840.2346-0.03850.03840.284-0.03350.2368-1.4565-7.067217.925
320.58410.2372-0.39120.17430.12491.50780.0421-0.0633-0.2926-0.0154-0.02590.05160.1898-0.1303-0.08820.2749-0.0207-0.01560.23080.02630.20265.6353-8.779625.036
330.25670.41140.20091.1156-0.24881.0360.0767-0.0539-0.17670.00150.0783-0.18430.0746-0.0243-0.10190.29360.06180.00340.19180.02930.231317.1265-13.809521.1235
340.17870.33450.16571.56460.0290.3181-0.02940.20180.01390.2659-0.13960.36590.32320.10740.10530.37220.07250.05970.19820.04210.259918.1199-17.905313.6663
350.03510.0655-0.05820.2250.14760.33010.0420.0073-0.05450.00150.0038-0.13730.17-0.0191-0.06360.24660.0073-0.01920.17990.0110.223615.9498-7.198514.439
360.43330.2290.52880.5561-0.05050.9052-0.07550.060.03160.14270.145-0.43450.0470.5219-0.06680.29480.0026-0.07950.3584-0.00120.350321.3827-8.265824.5051
370.8582-0.0309-0.68760.49820.71021.449-0.0279-0.3282-0.2610.2676-0.0858-0.20260.6723-0.13470.03140.28020.0569-0.02240.35570.05320.182312.5599-6.833134.7196
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 2:31)A2 - 31
2X-RAY DIFFRACTION2(chain A and resid 32:63)A32 - 63
3X-RAY DIFFRACTION3(chain A and resid 64:83)A64 - 83
4X-RAY DIFFRACTION4(chain A and resid 84:192)A84 - 192
5X-RAY DIFFRACTION5(chain A and resid 193:242)A193 - 242
6X-RAY DIFFRACTION6(chain A and resid 243:272)A243 - 272
7X-RAY DIFFRACTION7(chain A and resid 273:358)A273 - 358
8X-RAY DIFFRACTION8(chain A and resid 359:368)A359 - 368
9X-RAY DIFFRACTION9(chain A and resid 369:450)A369 - 450
10X-RAY DIFFRACTION10(chain A and resid 451:492)A451 - 492
11X-RAY DIFFRACTION11(chain B and resid 2:10)B2 - 10
12X-RAY DIFFRACTION12(chain B and resid 11:47)B11 - 47
13X-RAY DIFFRACTION13(chain B and resid 48:75)B48 - 75
14X-RAY DIFFRACTION14(chain B and resid 76:94)B76 - 94
15X-RAY DIFFRACTION15(chain B and resid 95:108)B95 - 108
16X-RAY DIFFRACTION16(chain B and resid 109:120)B109 - 120
17X-RAY DIFFRACTION17(chain B and resid 121:236)B121 - 236
18X-RAY DIFFRACTION18(chain B and resid 237:265)B237 - 265
19X-RAY DIFFRACTION19(chain B and resid 266:292)B266 - 292
20X-RAY DIFFRACTION20(chain B and resid 293:306)B293 - 306
21X-RAY DIFFRACTION21(chain C and resid 2:22)C2 - 22
22X-RAY DIFFRACTION22(chain C and resid 23:35)C23 - 35
23X-RAY DIFFRACTION23(chain C and resid 36:43)C36 - 43
24X-RAY DIFFRACTION24(chain C and resid 44:50)C44 - 50
25X-RAY DIFFRACTION25(chain C and resid 51:56)C51 - 56
26X-RAY DIFFRACTION26(chain C and resid 57:68)C57 - 68
27X-RAY DIFFRACTION27(chain C and resid 69:83)C69 - 83
28X-RAY DIFFRACTION28(chain E and resid 2:10)E2 - 10
29X-RAY DIFFRACTION29(chain E and resid 11:26)E11 - 26
30X-RAY DIFFRACTION30(chain E and resid 27:40)E27 - 40
31X-RAY DIFFRACTION31(chain E and resid 41:47)E41 - 47
32X-RAY DIFFRACTION32(chain E and resid 48:56)E48 - 56
33X-RAY DIFFRACTION33(chain E and resid 57:61)E57 - 61
34X-RAY DIFFRACTION34(chain E and resid 62:66)E62 - 66
35X-RAY DIFFRACTION35(chain E and resid 67:86)E67 - 86
36X-RAY DIFFRACTION36(chain E and resid 87:95)E87 - 95
37X-RAY DIFFRACTION37(chain E and resid 96:103)E96 - 103

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