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- PDB-3q3n: Toluene 4 monooxygenase HD complex with p-nitrophenol -

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Basic information

Entry
Database: PDB / ID: 3q3n
TitleToluene 4 monooxygenase HD complex with p-nitrophenol
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
: / P-NITROPHENOL / 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: 1.84 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 / 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)116,34310
Polymers115,5764
Non-polymers7676
Water12,845713
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)232,68720
Polymers231,1528
Non-polymers1,53512
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555x,-y,-z1
Unit cell
Length a, b, c (Å)98.303, 116.016, 181.044
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221

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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, 719 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-NPO / P-NITROPHENOL


Mass: 139.109 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H5NO3
#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.: 713 / 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: 2.23 Å3/Da / Density % sol: 44.92 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 200 mM ammonium chloride, 16 mM p-nitrophenol, 18% 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: 1.8→30 Å / Num. obs: 92496 / % possible obs: 96.4 % / Redundancy: 6.7 % / Rmerge(I) obs: 0.073 / Χ2: 1.498 / Net I/σ(I): 10.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.8-1.834.50.44933970.888171.5
1.83-1.864.80.4238260.933180.6
1.86-1.95.30.38741800.942187.8
1.9-1.945.80.3744460.969193.4
1.94-1.986.20.33345751.006196.8
1.98-2.036.60.30846811.071198.8
2.03-2.086.90.27647581.152199.8
2.08-2.137.10.23847881.2181100
2.13-2.27.20.20347601.3021100
2.2-2.277.20.18547741.4611100
2.27-2.357.20.16147591.6141100
2.35-2.447.20.14147851.671100
2.44-2.557.20.11847951.7641100
2.55-2.697.20.09947741.8031100
2.69-2.867.20.08447931.8531100
2.86-3.087.10.0748222.0341100
3.08-3.397.10.05948282.22199.9
3.39-3.8870.04648361.94199.8
3.88-4.887.10.03648701.6199.9
4.88-306.80.03250491.342199.7

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.01 Å29.78 Å
Translation2.01 Å29.78 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: 1.84→29.152 Å / Occupancy max: 1 / Occupancy min: 0.22 / SU ML: 0.2 / σ(F): 0 / Phase error: 19.26 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1877 4209 5.02 %
Rwork0.1513 --
obs0.1532 83883 93.56 %
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 48.055 Å2 / ksol: 0.367 e/Å3
Displacement parametersBiso max: 136.4 Å2 / Biso mean: 31.0919 Å2 / Biso min: 7.18 Å2
Baniso -1Baniso -2Baniso -3
1-8.4461 Å2-0 Å2-0 Å2
2---1.4958 Å20 Å2
3----6.9503 Å2
Refinement stepCycle: LAST / Resolution: 1.84→29.152 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8035 0 47 713 8795
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0068515
X-RAY DIFFRACTIONf_angle_d1.01211584
X-RAY DIFFRACTIONf_chiral_restr0.0731185
X-RAY DIFFRACTIONf_plane_restr0.0051518
X-RAY DIFFRACTIONf_dihedral_angle_d13.3483152
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 (%)
1.84-1.90580.28523530.22186331668475
1.9058-1.9820.22953860.18327174756085
1.982-2.07220.22314100.16377760817092
2.0722-2.18140.20724280.15167996842495
2.1814-2.31810.20173910.14998123851496
2.3181-2.4970.18664530.14788174862797
2.497-2.74810.19743940.14888419881398
2.7481-3.14530.18824270.16348429885699
3.1453-3.96120.18184910.14828507899899
3.9612-29.1560.15724760.13478761923799
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)
10.40990.0679-0.28450.0159-0.01370.39020.02580.1365-0.03450.0140.04630.0111-0.0597-0.1321-0.070.15520.0193-0.01020.1330.00720.123921.36588.3967-23.0203
20.06960.0656-0.11990.3649-0.43550.561-0.02670.15060.12170.232-0.157-0.1491-0.23250.54490.16430.3916-0.0842-0.08990.40590.0560.220654.03938.87472.6726
30.30370.0452-0.0220.1967-0.36720.69850.06340.02250.00250.1095-0.03490.0388-0.26260.084-0.02120.1901-0.03390.00190.1047-0.00780.113536.288814.9421-15.3241
40.16360.0776-0.19670.4161-0.55360.79490.0730.0046-0.00520.1174-0.1135-0.0161-0.27430.19840.03750.2375-0.0933-0.00280.15980.00680.11843.218519.6716-18.4333
50.10340.0380.0850.2145-0.38611.1492-0.00520.0454-0.0666-0.0057-0.04450.0134-0.08150.18810.04460.1601-0.0119-0.00540.1534-0.01590.141541.08014.9671-17.4216
61.5633-0.06750.34810.2812-0.29631.14270.110.28990.012-0.0362-0.1257-0.01070.04530.27230.02110.1413-0.0332-0.00550.1605-0.01060.107640.405514.2932-36.289
70.21670.2493-0.37070.567-0.55050.68870.01130.04450.011-0.0038-0.1698-0.09460.0040.29480.13990.1424-0.0171-0.00310.30660.01680.125852.66464.7861-24.7475
80.7560.13950.29440.9448-0.05151.37580.0420.1537-0.02540.0285-0.2212-0.1673-0.08090.52870.17480.1442-0.1276-0.03620.40710.08630.15861.91713.5648-25.9616
90.2404-0.2047-0.0980.4738-0.4040.83040.07830.06020.05410.1046-0.2093-0.0774-0.37790.41620.14960.2647-0.2025-0.04890.35520.06620.164357.92327.1612-30.4423
100.29490.2219-0.39130.331-0.48241.12540.1543-0.12140.09020.4249-0.1734-0.1096-0.65860.54140.15040.4743-0.3437-0.09990.37520.0370.171959.987730.4136-13.2023
110.2410.428-0.17271.0987-0.64080.45090.1539-0.22350.22970.4239-0.25180.126-0.68540.18370.0770.5496-0.178-0.01050.2076-0.02530.149341.870427.65740.7705
120.41370.1084-0.30360.1135-0.36211.15930.0445-0.0170.16210.2470.04530.1069-0.64220.1189-0.08770.4258-0.02110.03410.09010.00660.181330.821233.537-18.8177
130.39410.23680.00630.1613-0.10590.6310.03580.1398-0.0254-0.01150.0571-0.0478-0.1918-0.0378-0.06540.19050.04820.00920.10270.00560.112620.07967.2536-3.8545
143.49431.57190.70930.7893-0.19173.35570.0181-0.11490.1912-0.07940.05440.13740.5579-0.7626-0.06520.2413-0.0830.00520.33750.03840.16720.0579-6.5278-7.7441
153.17041.4236-0.59060.695-0.41111.04140.1811-0.02280.1845-0.10420.11960.56670.1975-0.5076-0.29560.16920.0218-0.03660.45280.08330.255-5.48114.1189-18.1019
160.2854-0.0051-0.16510.2735-0.26621.05040.06370.05250.08530.06380.0530.0592-0.2297-0.2632-0.11090.17550.09810.02140.17990.04430.149210.805515.5444-19.2437
170.8433-0.6792-0.42350.7010.01321.4168-0.05950.057-0.15060.13420.09710.1763-0.1476-0.5795-0.04740.19090.10720.05870.32130.0560.20360.01649.3617-7.1725
181.2762-0.8408-0.92930.69540.29621.50250.12110.00920.20460.06230.1075-0.0286-0.5407-0.1667-0.17440.330.13670.06230.19890.01580.171114.701920.4256-4.0836
193.2690.455-0.69490.6352-0.76420.92690.362-0.06060.58560.4652-0.02840.0692-0.5769-0.16-0.2070.57090.20260.190.05770.05280.28113.540137.0029-10.4206
200.3354-0.6063-0.43221.71310.40340.915-0.0060.29130.03510.047-0.09310.4318-0.0677-0.5324-0.04890.21170.19480.03960.43710.11290.2956-4.22720.3865-18.2179
210.31990.5446-0.1651.3104-0.2080.1514-0.04160.03210.19890.0852-0.1324-0.2014-0.45960.7030.1580.4051-0.3598-0.12730.51140.12770.292866.956835.4507-32.1873
220.57640.16450.01630.3041-0.33520.9018-0.14370.14460.0910.01270.0743-0.11630.03280.01180.06810.5771-0.6346-0.17890.93840.30040.535274.99240.0514-34.4327
230.41410.50080.7871.60920.57071.68390.01140.01190.10070.1223-0.2095-0.3652-0.28710.4290.17140.3708-0.3794-0.11660.66110.16020.329475.180129.2591-26.5605
240.3561.0092-1.07074.3663-2.62963.5664-0.1787-0.2074-0.2637-0.3626-0.3856-0.8835-0.05220.47620.48670.2628-0.2968-0.00640.74970.20150.334274.580631.9288-39.6414
251.81990.316-2.13641.3227-1.23733.133-0.35740.7810.0756-0.0856-0.332-0.30180.3152-0.05830.56920.4823-0.38630.03080.91850.27830.407771.790536.7641-44.3942
261.04760.684-0.45580.9163-0.62581.0607-0.09740.3519-0.0067-0.237-0.1716-0.2109-0.50740.75990.25390.3488-0.3486-0.04480.64470.18710.227568.487435.8481-40.3436
271.61050.3864-0.17030.9244-0.62890.4564-0.19820.4004-0.1219-0.3216-0.0098-0.14870.41440.21320.15540.23970.01710.02140.3238-0.00090.157347.6423-4.1669-29.8523
281.39410.3568-0.23550.6903-0.91751.3021-0.1268-0.0725-0.2486-0.18440.1198-0.08520.42980.08120.03580.27440.0538-0.00260.1593-0.0210.167239.7006-16.1574-18.4652
290.7011-0.0421-0.46070.9881-0.08380.3152-0.04740.1631-0.1614-0.22690.0231-0.0950.16920.3759-0.00840.22980.0239-0.00510.232-0.02050.161446.7331-9.1857-22.3201
300.40710.2143-0.26840.26770.16331.3983-0.11740.0966-0.1135-0.13070.1120.04020.47540.03110.02770.2482-0.0160.00710.1327-0.02420.159531.9652-15.3499-14.1556
310.31450.28880.36970.6177-0.12071.05550.10430.07920.1048-0.12730.08470.2810.0805-0.1649-0.13080.1998-0.0236-0.04120.19240.01540.21331.3076-5.9248-20.1332
321.68690.2086-1.84850.5204-0.61422.3385-0.07920.3514-0.3423-0.3782-0.02150.01180.33870.18780.03560.2702-0.0606-0.01080.2772-0.05620.072737.5175-6.8586-35.3271
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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