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- PDB-3q2a: Toluene 4 monooxygenase HD complex with inhibitor p-aminobenzoate -

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Basic information

Entry
Database: PDB / ID: 3q2a
TitleToluene 4 monooxygenase HD complex with inhibitor p-aminobenzoate
Components(Toluene-4-monooxygenase system protein ...) x 4
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / aromatic hydrocarbon catabolism / iron / multi-component monooxygenase / aromatic hydroxylation / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
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
Chem-ETE / : / 4-AMINOBENZOIC ACID / 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: 1.99 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 19, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 21, 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 / 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)116,72712
Polymers115,5764
Non-polymers1,1518
Water12,683704
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)233,45424
Polymers231,1528
Non-polymers2,30216
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555x,-y,-z1
Buried area39330 Å2
ΔGint-206 kcal/mol
Surface area60740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.973, 115.437, 180.997
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
11A-523-

P6G

21A-585-

HOH

31A-703-

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: QOO456, 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: QOO460, 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: QOO457, 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 , 5 types, 712 molecules

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


Mass: 55.845 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe
#6: Chemical
ChemComp-PAB / 4-AMINOBENZOIC ACID / 4-Aminobenzoic acid


Mass: 137.136 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H7NO2
#7: Chemical ChemComp-P6G / HEXAETHYLENE GLYCOL / POLYETHYLENE GLYCOL PEG400 / Polyethylene glycol


Mass: 282.331 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H26O7 / Comment: precipitant*YM
#8: Chemical ChemComp-ETE / 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL


Mass: 208.252 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H20O5
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 704 / 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: 2.24 Å3/Da / Density % sol: 45 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 200 mM ammonium chloride, 200 mM p-aminobenzoate, 22% 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: Jan 1, 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: 1.85→30 Å / Num. obs: 78868 / % possible obs: 89.3 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.07 / Χ2: 0.88 / Net I/σ(I): 11.7
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.85-1.9250.39348190.817155.2
1.92-1.995.60.32460450.804169
1.99-2.085.90.26370970.831181.3
2.08-2.1960.19580580.889191.9
2.19-2.336.40.15485340.963197.4
2.33-2.516.70.12587131.04198.8
2.51-2.7670.09487951.007199.7
2.76-3.167.20.07588400.94199.9
3.16-3.987.30.06688501.108199.3
3.98-307.20.03991170.354199.5

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.09 Å29.22 Å
Translation2.09 Å29.22 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
PHENIXdev_609refinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.99→29.217 Å / Occupancy max: 1 / Occupancy min: 0.16 / SU ML: 0.21 / σ(F): 0 / Phase error: 19.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1883 3308 5.03 %
Rwork0.1411 --
obs0.1434 65744 92.4 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 58.996 Å2 / ksol: 0.38 e/Å3
Displacement parametersBiso max: 178.65 Å2 / Biso mean: 36.4313 Å2 / Biso min: 12.6 Å2
Baniso -1Baniso -2Baniso -3
1-13.841 Å2-0 Å2-0 Å2
2---4.2084 Å20 Å2
3----9.6325 Å2
Refinement stepCycle: LAST / Resolution: 1.99→29.217 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8020 0 75 704 8799
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0078482
X-RAY DIFFRACTIONf_angle_d111530
X-RAY DIFFRACTIONf_chiral_restr0.0691178
X-RAY DIFFRACTIONf_plane_restr0.0051506
X-RAY DIFFRACTIONf_dihedral_angle_d13.4973132
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 (%)
1.99-2.06110.27362650.17534815508072
2.0611-2.14360.21592650.14595444570981
2.1436-2.24110.22443410.14695947628889
2.2411-2.35930.21823240.14656234655893
2.3593-2.5070.21173620.15066316667895
2.507-2.70040.20833620.14576541690397
2.7004-2.9720.20163440.14736649699399
2.972-3.40140.19023460.156730707699
3.4014-4.28330.17843300.12786789711999
4.2833-29.220.14553690.13266971734099
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)
10.29240.0748-0.18480.06630.01130.185-0.00050.116-0.02860.02520.0163-0.0179-0.1055-0.081-0.01380.15180.0183-0.01940.1596-0.00680.1361-27.63848.4416-22.6526
20.01350.0760.00790.47360.040.0050.06620.06530.01950.1871-0.117-0.08120.02980.10250.00480.3236-0.0444-0.0960.34660.05570.20424.8218.99182.7004
30.15650.08150.0590.06020.09310.3361-0.00450.0510.07970.0543-0.0750.0117-0.26120.07050.03520.2008-0.0287-0.00930.13970.00740.1429-13.224114.908-15.3297
40.219-0.0933-0.01570.30260.14210.0740.0907-0.01860.01080.1266-0.1325-0.0312-0.20650.1214-0.02960.3042-0.0999-0.02260.18380.02910.16-6.140819.5694-18.672
50.16820.0945-0.07090.263-0.03370.6026-0.0414-0.0529-0.0794-0.034-0.0963-0.0038-0.04450.0850.05310.1753-0.0093-0.00190.1840.01010.1955-8.25885.0131-17.6759
60.7983-0.046-0.11560.1891-0.16040.19630.04810.16470.0097-0.0215-0.1037-0.029-0.00890.03870.01570.1838-0.0467-0.01160.24040.00260.1778-8.560714.268-35.9723
70.1144-0.00010.06190.2101-0.05990.3461-0.042-0.0241-0.06130.0073-0.1381-0.07350.0070.18620.06870.1778-0.0166-0.00410.33020.03860.19773.43315.018-24.7532
80.27160.00770.00650.04990.00930.0021-0.02030.0184-0.03280.0871-0.1489-0.0642-0.11680.3102-0.23470.2005-0.1414-0.06290.45570.11470.222912.702413.6676-25.8925
90.322-0.02980.14580.1810.150.2233-0.0073-0.0765-0.00970.1065-0.1587-0.1041-0.23370.3242-0.30880.3097-0.1942-0.06760.38290.11510.20598.874727.1531-30.4842
100.00520.0054-0.00340.0048-0.00440.02280.0405-0.06740.01790.0209-0.0381-0.0168-0.11840.09060.14560.5117-0.2682-0.09410.36390.04730.247210.016931.2317-13.4348
110.20350.05830.20350.31190.16220.39970.0194-0.03990.06410.0377-0.07910.0566-0.20790.1273-0.0410.4515-0.1093-0.0250.174-0.01070.1711-7.964927.48760.5015
120.0174-0.00720.01620.02250.00540.0247-0.00170.00190.12060.14750.03740.106-0.37940.0259-0.03660.5530.0074-0.00380.17390.00450.2467-18.303333.4829-18.7852
130.27650.1126-0.18670.4159-0.09050.469-0.02910.0090.00670.01340.0082-0.0323-0.1697-0.07760.00570.22630.0377-0.00510.1766-0.0060.174-29.11137.3082-3.8464
140.68360.3931-0.63260.5186-0.35962.1702-0.004-0.04010.0101-0.06310.11550.10740.0839-0.3921-0.09070.2408-0.06450.00770.43530.03120.2342-49.2433-6.2622-8.1077
150.14770.33880.16990.92120.06030.94690.0059-0.0518-0.00180.01640.19560.22260.0557-0.5356-0.18390.22260.0702-0.02670.5970.08750.2891-54.69994.2117-18.1048
160.2636-0.161-0.03070.3314-0.26190.53670.0330.06030.05130.06680.03830.0269-0.2535-0.28410.0110.21090.10290.00290.25710.02180.1592-38.313515.75-19.1512
170.9224-0.2123-0.10740.06110.08450.3053-0.0580.0064-0.15450.00990.05280.026-0.0717-0.33490.00630.18160.11080.03990.41390.04110.2163-49.1229.4805-7.1315
180.2886-0.0288-0.20430.0264-0.01320.2680.0248-0.01630.06360.06120.0395-0.0233-0.05180.00590.0080.32450.13440.02930.1905-0.01240.1468-34.224720.563-4.2345
190.2421-0.24480.00870.25060.00140.02390.0136-0.02080.09950.07760.0345-0.0796-0.0768-0.03850.16690.47360.17390.050.19730.00980.25-35.810337.4506-10.3051
200.3194-0.31280.13020.3652-0.10170.1188-0.0516-0.1039-0.01910.06660.05770.0731-0.0317-0.0668-0.04340.28970.21410.01570.47380.08360.3218-52.679421.0749-18.1031
210.0436-0.01970.00960.0123-0.00970.06410.0014-0.00090.0432-0.0031-0.00690.019-0.05650.0405-0.00470.4255-0.2939-0.09570.48270.12420.291517.724735.4802-32.279
223.25790.9915-0.16391.24190.19790.08370.096-0.257-0.07240.1146-0.09320.0064-0.0150.0880.00440.5602-0.345-0.11890.6610.19280.612325.689540.1269-34.6303
230.07030.0637-0.00010.0763-0.02950.04560.0199-0.03580.00850.0238-0.0253-0.0192-0.01940.04010.00950.4014-0.2912-0.11720.70790.21310.357225.862729.4504-26.4772
240.40550.1123-0.21970.1065-0.05360.13610.0267-0.0796-0.04730.0588-0.0669-0.083-0.00890.06030.00980.4039-0.2677-0.07650.5860.17630.341925.351632.0133-39.5828
250.47570.2448-0.45110.6198-0.30830.4392-0.06440.0187-0.02710.0432-0.028-0.03780.0210.05030.00320.4588-0.20060.03850.58750.21720.408222.884536.9361-44.4909
260.03340.00060.02490.0005-0.00840.1701-0.06870.06230.0329-0.10920.09480.0414-0.0323-0.0375-0.05170.4387-0.2539-0.07980.52070.16340.298418.328736.7769-40.0939
270.9640.25720.04560.4428-0.11190.0435-0.09480.2848-0.0781-0.15680.0373-0.08830.1087-0.01370.05020.22440.04420.03060.2538-0.00280.2058-1.5411-4.1943-29.816
280.35520.0279-0.09670.1209-0.36312.1366-0.09150.0196-0.1761-0.07290.0219-0.00680.50050.0260.05250.32560.03220.05310.1672-0.01330.2146-9.4935-16.1564-18.4201
290.58070.04080.27850.47520.15051.2462-0.04030.0875-0.0709-0.0625-0.0261-0.03420.17350.15310.03580.26750.05660.01910.26140.00070.2215-2.4832-9.1327-22.3238
300.1506-0.1509-0.51630.15460.52741.8005-0.09110.0483-0.15240.00830.0276-0.00370.5326-0.01850.08580.3083-0.02580.04240.18-0.01450.2361-17.2-15.3311-14.2349
310.00520.0282-0.03490.1523-0.18830.2330.01020.04160.0414-0.03180.05280.00880.0189-0.076-0.04330.1902-0.0078-0.00070.18620.00140.2176-17.9138-5.9308-20.0995
320.62-0.2145-0.52960.07530.18310.45230.04380.035-0.00360.0049-0.030.0610.0309-0.137-0.02060.2665-0.04680.01080.2505-0.0580.1736-12.3918-6.9852-34.7714
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 2:75)A2 - 75
2X-RAY DIFFRACTION2(chain A and resid 76:85)A76 - 85
3X-RAY DIFFRACTION3(chain A and resid 86:146)A86 - 146
4X-RAY DIFFRACTION4(chain A and resid 147:205)A147 - 205
5X-RAY DIFFRACTION5(chain A and resid 206:244)A206 - 244
6X-RAY DIFFRACTION6(chain A and resid 245:271)A245 - 271
7X-RAY DIFFRACTION7(chain A and resid 272:309)A272 - 309
8X-RAY DIFFRACTION8(chain A and resid 310:372)A310 - 372
9X-RAY DIFFRACTION9(chain A and resid 373:451)A373 - 451
10X-RAY DIFFRACTION10(chain A and resid 452:492)A452 - 492
11X-RAY DIFFRACTION11(chain B and resid 2:32)B2 - 32
12X-RAY DIFFRACTION12(chain B and resid 33:75)B33 - 75
13X-RAY DIFFRACTION13(chain B and resid 76:98)B76 - 98
14X-RAY DIFFRACTION14(chain B and resid 99:111)B99 - 111
15X-RAY DIFFRACTION15(chain B and resid 112:121)B112 - 121
16X-RAY DIFFRACTION16(chain B and resid 122:228)B122 - 228
17X-RAY DIFFRACTION17(chain B and resid 229:255)B229 - 255
18X-RAY DIFFRACTION18(chain B and resid 256:267)B256 - 267
19X-RAY DIFFRACTION19(chain B and resid 268:291)B268 - 291
20X-RAY DIFFRACTION20(chain B and resid 292:306)B292 - 306
21X-RAY DIFFRACTION21(chain C and resid 3:25)C3 - 25
22X-RAY DIFFRACTION22(chain C and resid 26:33)C26 - 33
23X-RAY DIFFRACTION23(chain C and resid 34:46)C34 - 46
24X-RAY DIFFRACTION24(chain C and resid 47:55)C47 - 55
25X-RAY DIFFRACTION25(chain C and resid 56:67)C56 - 67
26X-RAY DIFFRACTION26(chain C and resid 68:84)C68 - 84
27X-RAY DIFFRACTION27(chain E and resid 2:21)E2 - 21
28X-RAY DIFFRACTION28(chain E and resid 22:38)E22 - 38
29X-RAY DIFFRACTION29(chain E and resid 39:56)E39 - 56
30X-RAY DIFFRACTION30(chain E and resid 57:72)E57 - 72
31X-RAY DIFFRACTION31(chain E and resid 73:95)E73 - 95
32X-RAY DIFFRACTION32(chain E and resid 96:103)E96 - 103

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