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- PDB-4whx: X-ray Crystal Structure of an Amino Acid Aminotransferase from Bu... -

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Basic information

Entry
Database: PDB / ID: 4whx
TitleX-ray Crystal Structure of an Amino Acid Aminotransferase from Burkholderia pseudomallei Bound to the Co-factor Pyridoxal Phosphate
ComponentsBranched-chain-amino-acid transaminase
KeywordsTRANSFERASE / SSGCID / Burkholderia pseudomallei / pyridoxal phosphate / aminotransferase / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


L-leucine-2-oxoglutarate transaminase activity / branched-chain-amino-acid transaminase / L-valine-2-oxoglutarate transaminase activity / L-isoleucine-2-oxoglutarate transaminase activity / L-leucine biosynthetic process / L-valine biosynthetic process / isoleucine biosynthetic process
Similarity search - Function
Branched-chain amino acid aminotransferase I / Branched-chain aminotransferase / Aminotransferase, class IV, conserved site / Aminotransferases class-IV signature. / Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain / D-amino Acid Aminotransferase; Chain A, domain 2 / D-amino Acid Aminotransferase, subunit A, domain 2 / Branched-chain-amino-acid aminotransferase-like, N-terminal / Aminotransferase class IV / Aminotransferase-like, PLP-dependent enzymes ...Branched-chain amino acid aminotransferase I / Branched-chain aminotransferase / Aminotransferase, class IV, conserved site / Aminotransferases class-IV signature. / Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain / D-amino Acid Aminotransferase; Chain A, domain 2 / D-amino Acid Aminotransferase, subunit A, domain 2 / Branched-chain-amino-acid aminotransferase-like, N-terminal / Aminotransferase class IV / Aminotransferase-like, PLP-dependent enzymes / Branched-chain-amino-acid aminotransferase-like, C-terminal / Amino-transferase class IV / D-amino Acid Aminotransferase; Chain A, domain 1 / Alpha-Beta Barrel / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ALANINE / Branched-chain-amino-acid aminotransferase / Branched-chain-amino-acid aminotransferase
Similarity search - Component
Biological speciesBurkholderia pseudomallei 576 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.05 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID) / Fairman, J.W. / Dranow, D.M. / Taylor, B.M. / Lorimer, D. / Edwards, T.E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: to be published
Title: X-ray Crystal Structure of an Amino Acid Aminotransferase from Burkholderia pseudomallei Bound to the Co-factor Pyridoxal Phosphate
Authors: SSGCID / Fairman, J.W. / Dranow, D.M. / Taylor, B.M. / Lorimer, D. / Edwards, T.E.
History
DepositionSep 23, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 8, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 5, 2014Group: Structure summary
Revision 2.0Sep 20, 2017Group: Author supporting evidence / Derived calculations ...Author supporting evidence / Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary
Category: entity / entity_src_gen ...entity / entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list / software / struct_keywords
Item: _chem_comp.formula / _chem_comp.name ..._chem_comp.formula / _chem_comp.name / _entity.formula_weight / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation / _struct_keywords.text
Revision 2.1Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.2Dec 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / refine_hist
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Branched-chain-amino-acid transaminase
B: Branched-chain-amino-acid transaminase
C: Branched-chain-amino-acid transaminase
D: Branched-chain-amino-acid transaminase
E: Branched-chain-amino-acid transaminase
F: Branched-chain-amino-acid transaminase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)207,82912
Polymers207,3486
Non-polymers4816
Water16,898938
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27710 Å2
ΔGint-108 kcal/mol
Surface area53690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.140, 230.350, 77.530
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Detailsbiological unit is the same as asym.

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Components

#1: Protein
Branched-chain-amino-acid transaminase


Mass: 34558.012 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia pseudomallei 576 (bacteria)
Gene: ilvE, BUC_1039 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: B7CIR9, UniProt: A0A0E1U3Z8*PLUS, branched-chain-amino-acid transaminase
#2: Chemical
ChemComp-ALA / ALANINE


Type: L-peptide linking / Mass: 89.093 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H7NO2
#3: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 938 / 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: 2.27 Å3/Da / Density % sol: 45.83 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: JCSG+ well H8 - 0.1 M BIS-TRIS pH 5.50, 0.2 M sodium chloride, 25% PEG3350, cryoprotected in 20% EG

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 13, 2014
RadiationMonochromator: Diamond[111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.05→50 Å / Num. obs: 115291 / % possible obs: 98 % / Observed criterion σ(I): -3 / Redundancy: 4.21 % / Biso Wilson estimate: 30.77 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.056 / Rrim(I) all: 0.064 / Χ2: 0.963 / Net I/σ(I): 17.99 / Num. measured all: 485486
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Highest resolution (Å)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.05-2.10.7820.5092.5836148860385590.57999.5
2.1-2.160.8480.413.1935352841283490.46699.3
2.16-2.220.90.324.1134312815980800.36399
2.22-2.290.9310.2615.0833183788777880.29798.7
2.29-2.370.9450.2285.8532550775076620.25998.9
2.37-2.450.9690.1817.3331161741672940.20698.4
2.45-2.540.9750.1528.7230183720270940.17398.5
2.54-2.650.9820.12310.829079695568270.1498.2
2.65-2.760.990.09513.5727660664265020.10897.9
2.76-2.90.9930.0816.3226476637762260.09197.6
2.9-3.060.9950.06220.8124996606559030.07197.3
3.06-3.240.9970.04826.0123640577656050.05597
3.24-3.470.9980.03831.5821826538652060.04396.7
3.47-3.740.9990.03237.0720391508349210.03796.8
3.74-4.10.9990.02842.4818684467745480.03297.2
4.1-4.580.9990.02448.3816919424841360.02897.4
4.58-5.290.9990.02348.8215011378336770.02697.2
5.29-6.480.9990.02345.4212835323131310.02696.9
6.48-9.1710.01950.69931252624360.02196.4
9.170.9990.01755.535149149213470.0290.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XDSdata scaling
XDSdata reduction
PHENIX(phenix.refine: dev_1769)refinement
PDB_EXTRACT3.15data extraction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.05→42.254 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 19.35 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1975 5630 4.88 %RANDOM
Rwork0.1622 109649 --
obs0.1639 115279 98 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 91.57 Å2 / Biso mean: 35.3044 Å2 / Biso min: 17.34 Å2
Refinement stepCycle: final / Resolution: 2.05→42.254 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14178 0 8 938 15124
Biso mean--47.6 37.79 -
Num. residues----1840
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00414534
X-RAY DIFFRACTIONf_angle_d0.90319751
X-RAY DIFFRACTIONf_chiral_restr0.0322210
X-RAY DIFFRACTIONf_plane_restr0.0032545
X-RAY DIFFRACTIONf_dihedral_angle_d13.6845123
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 (%)
2.05-2.07330.29181800.23083661384199
2.0733-2.09770.2661970.224237013898100
2.0977-2.12330.28241930.22483615380899
2.1233-2.15010.29281830.21993663384699
2.1501-2.17840.30511800.21013667384799
2.1784-2.20830.23751780.20193665384399
2.2083-2.23980.23461740.19083656383099
2.2398-2.27330.21752160.18613646386299
2.2733-2.30880.23052070.18633583379099
2.3088-2.34660.22221940.17833646384099
2.3466-2.38710.23741780.17763655383398
2.3871-2.43050.22151980.17583662386099
2.4305-2.47720.23221930.17593608380198
2.4772-2.52780.21021950.17583646384199
2.5278-2.58270.22181780.17763674385298
2.5827-2.64280.23381880.17713619380798
2.6428-2.70890.22861790.17683642382198
2.7089-2.78210.2281850.16773627381298
2.7821-2.8640.20441970.16943640383798
2.864-2.95640.21511710.16573645381698
2.9564-3.0620.22831630.17093628379197
3.062-3.18460.18251890.16723633382297
3.1846-3.32950.18521740.16693653382797
3.3295-3.50490.20011840.16513608379297
3.5049-3.72440.18292090.15533607381697
3.7244-4.01180.16431880.14823660384897
4.0118-4.41510.15311800.12623691387197
4.4151-5.0530.15651940.12063703389797
5.053-6.36280.16731990.1453729392897
6.3628-42.26250.16441860.14693816400295
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)
11.3450.1201-0.23061.46870.19891.98490.0785-0.22510.0220.17780.0303-0.31630.00560.2068-0.12860.2013-0.0066-0.04090.309-0.04220.340450.3181-18.3357-5.1255
24.0499-0.4452-0.40773.21290.67655.0989-0.00460.0986-0.2581-0.0767-0.1146-0.14710.17360.18860.11850.1148-0.0269-0.00030.1940.02040.246350.5722-19.7099-11.4977
32.1224-0.1060.08060.4178-0.06790.17330.0598-0.22530.25010.1168-0.0019-0.0397-0.02140.0797-0.05740.2466-0.02950.0310.2458-0.04560.303930.7297-16.3287-9.9165
42.51810.27810.63750.8321-0.38741.35110.1123-0.45060.20110.2409-0.0841-0.0636-0.07190.0054-0.01540.2976-0.04820.02040.3246-0.09190.263525.536-16.81194.9137
52.31651.2045-0.63110.6686-0.04952.77680.05140.05610.0689-0.1480.1085-0.3155-0.01340.5557-0.13490.2080.01260.07050.3083-0.01920.399952.1112-15.1428-26.2826
62.1815-0.1773-1.01942.21490.57732.72770.04640.37110.2532-0.30420.0035-0.1551-0.09120.0518-0.06750.2749-0.01350.07640.2810.03780.298443.1873-16.7299-40.3615
71.41110.86460.24582.05320.18312.7897-0.0519-0.09710.15550.06830.0582-0.1028-0.06810.26540.01140.1664-0.01050.02970.21490.03170.344646.4828-14.7161-27.6403
80.8196-0.3809-0.66364.05431.91032.218-0.06890.1994-0.2844-0.0101-0.1026-0.460.4568-0.02420.20940.33980.01880.14970.3893-0.01940.479249.6933-30.0115-37.941
90.89870.55690.15271.0210.05411.0448-0.0250.1211-0.1937-0.01620.057-0.19440.06760.126-0.01520.2042-0.00480.02070.1865-0.0090.261435.3905-34.545-24.8788
102.83050.6784-0.7442.4631-0.77113.5291-0.06610.2357-0.0723-0.1727-0.0480.12270.199-0.15840.09470.2272-0.00930.04580.2806-0.03880.255929.5989-35.2931-40.7887
112.03610.752-0.23331.5409-1.28141.46030.08840.255-0.416-0.2279-0.1104-0.18020.23690.09720.04410.36220.0260.05390.2688-0.0860.337832.909-44.1354-36.7031
121.58471.9339-1.07155.6431-1.63351.3255-0.24010.41760.0218-0.93260.1391-0.27730.0792-0.05410.0950.4980.01150.12860.4649-0.0320.298441.0245-32.3417-50.5866
131.3231-0.3841-0.17571.1613-0.19981.7299-0.0017-0.32360.1930.3160.01050.2812-0.0111-0.4408-0.08270.3048-0.03770.12340.3943-0.05910.3337-9.9357-14.6909-0.8942
141.4932-0.90931.04565.2715-0.98791.9123-0.0573-0.20540.3047-0.2064-0.12110.1201-0.0499-0.22410.12350.1483-0.03440.03750.3319-0.08720.3133-9.6918-13.4335-7.1939
150.3409-0.47090.030.87610.02690.01140.0821-0.1822-0.14030.3275-0.07670.3777-0.0123-0.1588-0.02820.3794-0.10650.10740.4580.02260.3497-10.6882-31.5056-1.5787
161.1596-0.0692-0.3011.0272-0.0830.97580.031-0.3121-0.12690.267-0.01490.09860.1752-0.1301-0.00270.3406-0.07530.05790.3440.03750.2271.7838-35.76830.7418
170.20320.4884-0.26711.68930.00061.10360.1303-0.1718-0.61710.2826-0.0116-0.09470.29130.1227-0.08480.51550.0004-0.06670.27340.11430.697617.8265-72.9266-11.0822
180.17590.2484-0.42381.5697-0.44811.07040.1414-0.4877-0.6140.38030.01220.03870.247-0.1311-0.05880.52-0.0825-0.02180.38380.23390.542516.4162-65.24063.6381
190.55070.2405-0.91751.9639-0.0841.58060.1964-0.1412-0.5257-0.00380.01510.00150.3492-0.0898-0.2240.4035-0.0571-0.03180.21260.120.543814.5817-68.2811-9.4465
200.61910.9926-0.33941.6207-0.49660.243-0.0581-0.3532-0.81440.05150.0233-0.5090.1370.1070.04810.39070.0798-0.02170.37430.16080.63732.0746-60.9465-4.4483
211.01860.3940.24660.9302-0.3230.62330.0143-0.1347-0.27510.1287-0.036-0.12490.1986-0.0630.02790.302-0.0094-0.00980.18080.03690.299726.0007-49.4905-12.1354
221.77950.3284-0.32562.2306-0.93291.67640.0198-0.4212-0.20960.3031-0.0361-0.19270.11240.08610.02660.35080.0034-0.07140.31920.07260.29932.0521-44.14651.5079
231.03911.2545-0.88913.7984-1.67991.11040.339-0.9738-0.63430.8133-0.4417-0.54620.0870.04080.07350.5879-0.0176-0.13290.54850.21090.434130.1458-57.21213.1123
241.18890.31440.59421.5428-0.27591.5310.04550.1665-0.5117-0.27940.0558-0.29650.2357-0.0679-0.1030.4553-0.01530.04940.2678-0.09870.577417.7637-68.8361-31.8766
250.73230.5778-0.36572.69090.28451.9492-0.09220.1706-0.5914-0.08180.0023-0.34650.27250.25940.0250.3433-0.00060.07450.2089-0.02040.539219.7853-68.5715-25.7111
261.3271-1.6179-0.30762.01950.36110.06610.09880.3402-0.5494-0.0545-0.19580.38730.2468-0.10020.06880.4264-0.1015-0.02390.3906-0.09080.48413.4009-60.4833-30.3371
271.3867-0.3202-0.17480.59190.06430.6774-0.01950.1158-0.3851-0.10650.00540.06920.2642-0.06710.0280.3285-0.04520.01580.203-0.00850.29549.5228-49.1152-22.7883
282.6875-0.31230.65811.6749-0.21962.0509-0.10140.33860.0964-0.1210.025-0.2060.09490.08490.08460.3414-0.08140.00870.3357-0.04420.25748.8765-44.6011-39.3877
291.3575-0.1573-0.42421.84540.77052.0523-0.0390.4102-0.1898-0.1294-0.05610.28280.1554-0.26940.10860.2711-0.0651-0.03080.3599-0.03640.25190.0317-42.8647-34.3744
301.9641-2.8682-1.28097.73621.62391.81160.1260.847-0.8062-1.085-0.15310.15910.2905-0.21240.05720.5828-0.13750.01910.5389-0.19920.47555.0181-56.8571-47.9243
312.3679-1.3770.56977.58611.17526.1777-0.0363-0.06930.3171-0.14660.08620.1617-0.6222-0.3207-0.04740.25810.04260.04470.41690.05410.437-19.6476-8.418-25.9548
321.329-0.17580.06171.4102-0.50651.5954-0.00130.13750.0529-0.1108-0.01320.20120.0497-0.2188-0.00610.1734-0.03910.00660.31480.03950.2805-11.4763-19.4539-31.3369
331.99460.12980.08441.782-0.16051.92460.0721-0.25550.04230.0845-0.04130.16250.1067-0.1763-0.04410.1715-0.02890.02780.33610.02250.2656-13.529-18.4085-23.4714
342.62190.9921-0.45972.7004-1.1441.0095-0.01210.49050.2415-0.0840.10360.004-0.0299-0.1868-0.090.32930.03150.01130.34580.03390.245-2.9761-7.6471-34.5322
352.08120.4088-0.79210.71280.36280.71580.04680.10240.1648-0.11820.0415-0.0327-0.0421-0.1709-0.06690.248-0.01240.0160.25150.0360.26899.4086-18.2848-23.0913
362.1693-0.76121.39040.89810.04091.86180.06740.2430.1565-0.17070.005-0.1072-0.04060.0745-0.06720.2535-0.00450.0740.26790.06040.250515.0116-17.9012-37.2692
374.24530.17051.81771.2301-0.12041.6931-0.00550.52580.2272-0.3857-0.01040.1079-0.0155-0.00330.04240.36080.02240.02340.39520.06680.20081.7921-13.3211-48.0954
380.84050.2712-0.10590.44120.14970.1115-0.17450.0843-0.0387-0.23240.04940.0370.11520.1168-0.07150.6801-0.03830.26140.5618-0.25340.599516.563-40.1287-10.4415
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 91 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 92 through 118 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 119 through 199 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 307 )A0
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 40 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 41 through 91 )B0
7X-RAY DIFFRACTION7chain 'B' and (resid 92 through 118 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 119 through 140 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 141 through 199 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 200 through 232 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 233 through 279 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 280 through 307 )B0
13X-RAY DIFFRACTION13chain 'C' and (resid 2 through 91 )C0
14X-RAY DIFFRACTION14chain 'C' and (resid 92 through 118 )C0
15X-RAY DIFFRACTION15chain 'C' and (resid 119 through 145 )C0
16X-RAY DIFFRACTION16chain 'C' and (resid 146 through 307 )C0
17X-RAY DIFFRACTION17chain 'D' and (resid 2 through 40 )D0
18X-RAY DIFFRACTION18chain 'D' and (resid 41 through 91 )D0
19X-RAY DIFFRACTION19chain 'D' and (resid 92 through 118 )D0
20X-RAY DIFFRACTION20chain 'D' and (resid 119 through 145 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 146 through 199 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 200 through 279 )D0
23X-RAY DIFFRACTION23chain 'D' and (resid 280 through 307 )D0
24X-RAY DIFFRACTION24chain 'E' and (resid 2 through 91 )E0
25X-RAY DIFFRACTION25chain 'E' and (resid 92 through 118 )E0
26X-RAY DIFFRACTION26chain 'E' and (resid 119 through 145 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 146 through 199 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 200 through 232 )E0
29X-RAY DIFFRACTION29chain 'E' and (resid 233 through 279 )E0
30X-RAY DIFFRACTION30chain 'E' and (resid 280 through 307 )E0
31X-RAY DIFFRACTION31chain 'F' and (resid 2 through 21 )F0
32X-RAY DIFFRACTION32chain 'F' and (resid 22 through 91 )F0
33X-RAY DIFFRACTION33chain 'F' and (resid 92 through 118 )F0
34X-RAY DIFFRACTION34chain 'F' and (resid 119 through 140 )F0
35X-RAY DIFFRACTION35chain 'F' and (resid 141 through 199 )F0
36X-RAY DIFFRACTION36chain 'F' and (resid 200 through 279 )F0
37X-RAY DIFFRACTION37chain 'F' and (resid 280 through 307 )F0
38X-RAY DIFFRACTION38chain 'G' and (resid 1 through 4 )G0

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