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- PDB-7ka0: Crystal structure of the complex of M. tuberculosis PheRS with co... -

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Basic information

Entry
Database: PDB / ID: 7ka0
TitleCrystal structure of the complex of M. tuberculosis PheRS with cognate precursor tRNA and phenylalanine
Components
  • (Phenylalanine--tRNA ligase ...) x 2
  • tRNA(Phe)
KeywordsLIGASE/RNA / aminoacylation / phenylalanyl tRNA synthetase / Structural Genomics / Ligase-tRNA complex / Center for Structural Genomics of Infectious Diseases / CSGID / LIGASE-RNA complex
Function / homology
Function and homology information


phenylalanine-tRNA ligase complex / phenylalanine-tRNA ligase / phenylalanine-tRNA ligase activity / phenylalanyl-tRNA aminoacylation / peptidoglycan-based cell wall / tRNA binding / magnesium ion binding / ATP binding / plasma membrane / cytoplasm
Similarity search - Function
Phenylalanine-tRNA ligase, class II, N-terminal / Phenylalanine-tRNA ligase alpha chain 1, bacterial / Aminoacyl tRNA synthetase class II, N-terminal domain / Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type / Phenylalanyl-tRNA synthetase, class IIc, alpha subunit / Phenylalanly tRNA synthetase, tRNA-binding-domain / tRNA synthetase, B5-domain / Phenylalanine-tRNA ligase, class IIc, beta subunit / tRNA synthetase B5 domain / B5 domain profile. ...Phenylalanine-tRNA ligase, class II, N-terminal / Phenylalanine-tRNA ligase alpha chain 1, bacterial / Aminoacyl tRNA synthetase class II, N-terminal domain / Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type / Phenylalanyl-tRNA synthetase, class IIc, alpha subunit / Phenylalanly tRNA synthetase, tRNA-binding-domain / tRNA synthetase, B5-domain / Phenylalanine-tRNA ligase, class IIc, beta subunit / tRNA synthetase B5 domain / B5 domain profile. / tRNA synthetase B5 domain / B3/4 domain / Ferrodoxin-fold anticodon-binding domain / Ferrodoxin-fold anticodon-binding domain superfamily / Ferredoxin-fold anticodon binding domain / Ferredoxin-fold anticodon binding (FDX-ACB) domain profile. / Ferredoxin-fold anticodon binding domain / B3/B4 tRNA-binding domain / Phenylalanyl-tRNA synthetase-like, B3/B4 / Phenylalanyl tRNA synthetase beta chain, core domain / Phenylalanyl tRNA synthetase beta chain CLM domain / B3/4 domain / Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm / Phenylalanyl-tRNA synthetase / tRNA synthetases class II core domain (F) / tRNA-binding domain / Putative tRNA binding domain / tRNA-binding domain profile. / Putative DNA-binding domain superfamily / Aminoacyl-tRNA synthetase, class II / Aminoacyl-transfer RNA synthetases class-II family profile. / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
ACETATE ION / : / TRIETHYLENE GLYCOL / PHENYLALANINE / : / RNA / RNA (> 10) / Phenylalanine--tRNA ligase beta subunit / Phenylalanine--tRNA ligase alpha subunit
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsChang, C. / Michalska, K. / Jedrzejczak, R. / Wower, J. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)HHSN272201700060C United States
CitationJournal: Nucleic Acids Res. / Year: 2021
Title: Mycobacterium tuberculosis Phe-tRNA synthetase: structural insights into tRNA recognition and aminoacylation.
Authors: Michalska, K. / Jedrzejczak, R. / Wower, J. / Chang, C. / Baragana, B. / Gilbert, I.H. / Forte, B. / Joachimiak, A.
History
DepositionSep 29, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 12, 2021Provider: repository / Type: Initial release
Revision 1.1Jun 2, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jun 16, 2021Group: Database references / Category: pdbx_database_related
Revision 1.3Oct 18, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Phenylalanine--tRNA ligase alpha subunit
B: Phenylalanine--tRNA ligase beta subunit
C: tRNA(Phe)
D: Phenylalanine--tRNA ligase alpha subunit
E: Phenylalanine--tRNA ligase beta subunit
F: tRNA(Phe)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)305,33647
Polymers302,2516
Non-polymers3,08641
Water16,286904
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area36410 Å2
ΔGint-331 kcal/mol
Surface area112060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)292.859, 109.980, 127.951
Angle α, β, γ (deg.)90.000, 100.160, 90.000
Int Tables number5
Space group name H-MC121

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Components

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Phenylalanine--tRNA ligase ... , 2 types, 4 molecules ADBE

#1: Protein Phenylalanine--tRNA ligase alpha subunit / Phenylalanyl-tRNA synthetase alpha subunit / PheRS


Mass: 37415.266 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: pheS, Rv1649, MTCY06H11.14 / Plasmid: pMCSG53 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): gold / References: UniProt: P9WFU3, phenylalanine-tRNA ligase
#2: Protein Phenylalanine--tRNA ligase beta subunit / Phenylalanyl-tRNA synthetase beta subunit / PheRS


Mass: 88867.234 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: pheT, Rv1650, MTCY06H11.15 / Plasmid: pMCSG53 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): gold / References: UniProt: P9WFU1, phenylalanine-tRNA ligase

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RNA chain , 1 types, 2 molecules CF

#3: RNA chain tRNA(Phe)


Mass: 24842.811 Da / Num. of mol.: 2 / Source method: obtained synthetically
Source: (synth.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
References: GenBank: 1251771558

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Non-polymers , 8 types, 945 molecules

#4: Chemical ChemComp-PHE / PHENYLALANINE / Phenylalanine


Type: L-peptide linking / Mass: 165.189 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H11NO2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#7: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL / Polyethylene glycol


Mass: 150.173 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H14O4
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mg
#9: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#10: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: K
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 904 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 3.36 Å3/Da / Density % sol: 63.34 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.2 M lithium sulfate, 0.1 M HEPES, 25% PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97934 Å
DetectorType: DECTRIS PILATUS3 X 6M / Detector: PIXEL / Date: Aug 17, 2018
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 155793 / % possible obs: 98.9 % / Redundancy: 6.4 % / Rmerge(I) obs: 0.147 / Rpim(I) all: 0.061 / Rrim(I) all: 0.159 / Χ2: 0.948 / Net I/σ(I): 7.3 / Num. measured all: 1002495
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.4-2.445.51.20776770.6730.5481.330.82898.2
2.44-2.495.71.14877080.6810.5141.2620.81498.7
2.49-2.535.71.04977020.7310.4691.1530.83598.4
2.53-2.595.50.88676200.7450.4060.9780.83396.9
2.59-2.646.40.8177920.8390.3430.8820.85299.3
2.64-2.76.60.69877940.8980.2890.7570.85499.6
2.7-2.776.70.60978500.9220.250.6590.85799.5
2.77-2.856.70.51377840.9410.2120.5560.8799.6
2.85-2.936.60.41277980.9590.1710.4470.8999.2
2.93-3.026.50.33778190.9650.1410.3660.92299.3
3.02-3.136.20.25677050.9730.110.2790.95897.8
3.13-3.266.50.21577400.980.090.2340.99598.3
3.26-3.416.90.17677970.990.0710.1911.03799.5
3.41-3.586.90.13978550.9920.0560.151.12299.5
3.58-3.816.80.1178480.9940.0450.1191.16399.5
3.81-4.16.40.0977890.9940.0380.0981.13798.5
4.1-4.526.80.07878100.9950.0320.0841.16998.9
4.52-5.1770.07178650.9960.0280.0761.10399.5
5.17-6.516.40.06578370.9960.0270.070.89398.2
6.51-506.80.04980030.9970.020.0530.70699

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
SBC-Collectdata collection
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
HKL-3000phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3PCO

3pco


Resolution: 2.4→48.04 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2147 7094 4.96 %
Rwork0.1767 135987 -
obs0.1786 143081 91.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 302.73 Å2 / Biso mean: 65.6908 Å2 / Biso min: 5.82 Å2
Refinement stepCycle: final / Resolution: 2.4→48.04 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17589 2826 184 904 21503
Biso mean--67.27 44.14 -
Num. residues----2477
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.430.25851280.22572483261151
2.43-2.460.29311790.21733319349867
2.46-2.490.31741460.22273449359570
2.49-2.520.2751810.21443529371071
2.52-2.550.25662080.21813551375973
2.55-2.590.27461900.20713758394877
2.59-2.620.27492250.21354183440884
2.62-2.660.24222530.21414378463190
2.66-2.70.26832330.21964613484694
2.7-2.750.24722620.22244774503697
2.75-2.790.27712430.22574866510998
2.79-2.850.27252550.22494912516799
2.85-2.90.26872850.21144836512199
2.9-2.960.25432530.20284857511099
2.96-3.020.24542680.19734895516399
3.02-3.090.22312260.1934833505998
3.09-3.170.22172520.2014754500696
3.17-3.260.26772400.200749525192100
3.26-3.350.2262350.207349485183100
3.35-3.460.23142640.18849255189100
3.46-3.580.21612520.17994881513399
3.58-3.730.19482690.165649225191100
3.73-3.90.19082740.15494908518299
3.9-4.10.16932330.14714868510198
4.1-4.360.15592810.14064881516299
4.36-4.70.16522640.1349375201100
4.7-5.170.17482800.13934923520399
5.17-5.920.19652520.15174919517199
5.92-7.450.22882280.17274979520798
7.45-48.040.19212350.16134954518997
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)
10.0056-0.0073-0.00140.00890.00010.0054-0.1022-0.05330.00730.0045-0.0468-0.1390.0518-0.0750.00010.5682-0.13640.05660.92740.43261.08126.0228-2.379766.4841
20.00190.0037-00.0088-0.00560.0159-0.06090.0289-0.09190.096-0.0708-0.2538-0.038-0.27300.6276-0.13730.15030.72480.03761.06727.19230.217856.4933
30.00940.01790.05420.04140.12250.4058-0.0453-0.1418-0.1022-0.0102-0.0554-0.0611-0.0156-0.2513-0.3730.2447-0.09740.04780.34790.21930.447230.47148.464261.1111
40.2362-0.16330.18470.1954-0.11270.1224-0.0220.02980.0646-0.0035-0.0164-0.02550.00490.10570.03860.1889-0.0483-0.00870.2120.05420.089384.077655.305225.3879
50.21680.20740.02460.23850.13820.2636-0.03080.07620.21290.0093-0.0902-0.15050.01040.0734-0.28580.2114-0.0475-0.02470.22780.08440.137685.87665.003924.5618
60.5017-0.39450.25580.4115-0.34990.4522-0.05490.03960.41310.1355-0.1499-0.26320.1630.0203-0.03840.346-0.0916-0.06870.20330.04960.225889.008573.234431.3254
70.09190.02370.07480.0369-0.02070.0955-0.00240.0546-0.02860.0874-0.0169-0.1084-0.0260.13730.00260.2416-0.0573-0.02730.23230.08010.172787.64751.44934.5899
82.80720.8292-1.82363.39163.53516.4588-0.1916-0.1723-0.27030.19630.17030.1138-0.0596-0.0414-0.02920.3798-0.1497-0.06860.5510.06020.303491.052767.606826.4187
90.0465-0.0040.06310.09250.02290.3128-0.22170.0510.1482-0.07360.1028-0.02440.27220.1025-0.05750.25690.0531-0.05950.40580.00430.4103129.578466.580746.6208
100.5346-0.0443-0.16810.39020.09290.1564-0.3860.17840.42840.05440.2103-0.215-0.01790.2002-0.26220.0157-0.2743-0.07510.35710.15350.5836124.349780.458528.4211
110.47680.26090.31060.27490.03580.4917-0.1040.32970.3125-0.1264-0.0554-0.1046-0.19210.272-0.38470.219-0.1794-0.02660.29890.21380.5194112.810282.849220.093
120.40270.12730.24150.2090.01240.0353-0.0370.132-0.0493-0.0727-0.0664-0.00530.03910.0923-0.1590.1634-0.01440.0220.18710.02810.054880.879343.771916.183
130.2246-0.104-0.00670.42670.04160.4681-0.01550.1832-0.1114-0.1769-0.1656-0.0570.0303-0.0075-0.71040.1911-0.0157-0.01750.1006-0.21920.040656.115226.048813.3115
140.00130.00460.00470.02540.03170.03790.11390.1147-0.0192-0.2071-0.1225-0.155-0.10490.0488-0.01780.41240.05150.18921.32970.12320.925518.990619.288840.6934
150.008-0.0038-0.00050.0024-0.001-0.0002-0.01560.02730.0514-0.00510.03170.02560.0968-0.009200.8318-0.06590.46141.38940.03351.48721.0138.618840.2276
160.0040.0005-0.00260.0001-0.00070.0082-0.00030.0304-0.00050.01330.0307-0.05450.0114-0.0204-00.95130.10550.34331.66810.09131.059335.893613.989230.9109
170.00190.0022-0.00310.0538-0.08370.1156-0.5513-0.346-0.3261-0.04570.06940.25560.0862-0.3359-0.31310.40470.01270.33860.59830.0040.722140.37327.772428.7445
180.01160.01480.01640.01560.01560.01620.0516-0.46090.1004-0.1615-0.0306-0.046-0.22160.092400.71820.04190.12381.1711-0.02830.855415.985425.609253.5751
190.0055-0.0008-0.00590.0026-0.00550.015-0.03710.065-0.0868-0.06530.09290.0843-0.03650.266801.36420.4810.14861.4245-0.17531.1898108.3240.11671.4339
200.0465-0.0036-0.06240.1264-0.10130.156-0.05890.1035-0.0932-0.1755-0.212-0.05590.26790.1949-0.29110.62110.33150.23330.4723-0.09760.435299.01979.88180.8368
210.11930.03130.03870.28160.11840.0896-0.00970.03870.03360.0235-0.02450.04670.018-0.041100.20320.0343-0.01790.1807-0.03790.122749.444757.531340.5198
220.3521-0.00590.11020.1841-0.00850.0330.05820.12050.303-0.1204-0.160.15310.0040.0259-0.01320.30120.0688-0.03290.17970.01520.173548.727571.8832.6677
230.0624-0.03340.07170.03940.01530.140.01810.0766-0.0113-0.1734-0.05610.0457-0.0995-0.083200.23650.0151-0.02960.2387-0.05660.167347.556451.723728.6287
244.00354.65275.12936.90357.42348.0011-0.15420.1999-0.3032-0.28670.2294-0.086-0.07760.077-0.03470.36440.0137-0.02470.2980.03410.17244.289667.402637.7833
250.0090.011-0.01110.0906-0.06710.1001-0.16480.20290.0285-0.08080.04230.32230.2249-0.1149-0.01170.32310.0089-0.11670.40440.0150.593216.223474.528422.0156
260.0127-0.0157-0.02730.02210.04180.0815-0.13970.10130.22510.1151-0.01970.31070.293-0.1425-0.00450.6631-0.2721-0.14120.70580.06531.0605-5.371360.697516.204
270.056-0.0078-0.02510.0908-0.10440.1515-0.2212-0.05150.21540.03470.13920.31210.0193-0.0724-0.11180.18630.0426-0.08810.23150.08030.668410.521470.709123.565
280.286-0.18530.09830.31390.04680.1434-0.1085-0.0615-0.02620.19840.11260.5861-0.0191-0.2234-0.06230.36940.12990.15240.3755-0.00120.90379.675379.710245.5519
290.3756-0.34810.23950.4514-0.03660.3111-0.1550.02250.13140.22220.05050.3955-0.2467-0.0788-0.43680.30770.16260.11520.1788-0.03230.619323.821684.46943.804
300.4126-0.13770.00830.2527-0.16810.030.0166-0.0144-0.03680.0951-0.14870.07920.0208-0.0655-0.12890.1712-0.00230.00580.07050.00070.011858.383140.019346.7531
310.0817-0.0109-0.02350.19410.02890.2059-0.0465-0.0424-0.03770.069-0.1203-0.2130.08590.2407-0.35740.24040.0149-0.02830.2330.13280.246486.22719.88249.293
320.0032-0.0037-0.00160.00550.0012-0.0004-0.0531-0.012-0.00030.032-0.0070.0114-0.051-0.026402.05910.03550.14582.28710.10312.5721115.749324.916621.7336
330.0050.0031-0.0070.0009-0.00340.00550.0409-0.04850.0523-0.0615-0.0377-0.03780.07820.075802.19640.10080.34392.47430.09842.6344116.012716.78221.3324
340.00090.0006-00.0006-0.00030.00030.03010.01310.0322-0.04910.0108-0.00170.03430.007802.13340.05890.32512.24190.02512.3755113.418.345820.9081
350.0030.00310.00090.00210.00120.0024-0.0054-0.02110.01640.01950.0262-0.03990.02050.0142-01.3158-0.08960.221.7281-0.08051.761698.882513.728830.3507
360.0472-0.01150.05360.0025-0.00870.0733-0.42160.4264-0.2362-0.1712-0.0584-0.3380.08310.4024-0.04630.53340.06540.29220.60930.08330.71194.44937.380232.1075
370.0007-0.00060.00040.0004-0.0010.00170.00530.0095-0.0165-0.0042-0.00370.04430.0019-0.016702.4981-0.02080.09712.75560.04112.4641115.13727.00075.8905
380.0022-0.0013-0.00170.00280.00040.00130.04350.00030.032-0.00770.029-0.0248-0.01740.0073-02.30920.19310.26562.5825-0.09132.5469122.659116.20370.5879
390.01660.0038-0.00780.00490.00080.002-0.0741-0.0177-0.05530.0208-0.0124-0.0633-0.1834-0.015702.2978-0.11580.60372.57950.18882.9241119.122430.076713.6338
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 19 )A1 - 19
2X-RAY DIFFRACTION2chain 'A' and (resid 20 through 52 )A20 - 52
3X-RAY DIFFRACTION3chain 'A' and (resid 53 through 92 )A53 - 92
4X-RAY DIFFRACTION4chain 'A' and (resid 93 through 165 )A93 - 165
5X-RAY DIFFRACTION5chain 'A' and (resid 166 through 242 )A166 - 242
6X-RAY DIFFRACTION6chain 'A' and (resid 243 through 301 )A243 - 301
7X-RAY DIFFRACTION7chain 'A' and (resid 302 through 341 )A302 - 341
8X-RAY DIFFRACTION8chain 'A' and (resid 401 through 401 )A401
9X-RAY DIFFRACTION9chain 'B' and (resid -3 through 131 )B-3 - 131
10X-RAY DIFFRACTION10chain 'B' and (resid 132 through 290 )B132 - 290
11X-RAY DIFFRACTION11chain 'B' and (resid 291 through 486 )B291 - 486
12X-RAY DIFFRACTION12chain 'B' and (resid 487 through 700 )B487 - 700
13X-RAY DIFFRACTION13chain 'B' and (resid 701 through 831 )B701 - 831
14X-RAY DIFFRACTION14chain 'C' and (resid 5 through 19 )C5 - 19
15X-RAY DIFFRACTION15chain 'C' and (resid 20 through 24 )C20 - 24
16X-RAY DIFFRACTION16chain 'C' and (resid 25 through 29 )C25 - 29
17X-RAY DIFFRACTION17chain 'C' and (resid 30 through 49 )C30 - 49
18X-RAY DIFFRACTION18chain 'C' and (resid 50 through 70 )C50 - 70
19X-RAY DIFFRACTION19chain 'D' and (resid 2 through 59 )D2 - 59
20X-RAY DIFFRACTION20chain 'D' and (resid 60 through 92 )D60 - 92
21X-RAY DIFFRACTION21chain 'D' and (resid 93 through 211 )D93 - 211
22X-RAY DIFFRACTION22chain 'D' and (resid 212 through 301 )D212 - 301
23X-RAY DIFFRACTION23chain 'D' and (resid 302 through 341 )D302 - 341
24X-RAY DIFFRACTION24chain 'D' and (resid 401 through 401 )D401
25X-RAY DIFFRACTION25chain 'E' and (resid -3 through 61 )E-3 - 61
26X-RAY DIFFRACTION26chain 'E' and (resid 62 through 113 )E62 - 113
27X-RAY DIFFRACTION27chain 'E' and (resid 114 through 189 )E114 - 189
28X-RAY DIFFRACTION28chain 'E' and (resid 190 through 311 )E190 - 311
29X-RAY DIFFRACTION29chain 'E' and (resid 312 through 486 )E312 - 486
30X-RAY DIFFRACTION30chain 'E' and (resid 487 through 767 )E487 - 767
31X-RAY DIFFRACTION31chain 'E' and (resid 768 through 831 )E768 - 831
32X-RAY DIFFRACTION32chain 'F' and (resid 5 through 9 )F5 - 9
33X-RAY DIFFRACTION33chain 'F' and (resid 10 through 19 )F10 - 19
34X-RAY DIFFRACTION34chain 'F' and (resid 20 through 24 )F20 - 24
35X-RAY DIFFRACTION35chain 'F' and (resid 25 through 29 )F25 - 29
36X-RAY DIFFRACTION36chain 'F' and (resid 30 through 49 )F30 - 49
37X-RAY DIFFRACTION37chain 'F' and (resid 50 through 54 )F50 - 54
38X-RAY DIFFRACTION38chain 'F' and (resid 55 through 59 )F55 - 59
39X-RAY DIFFRACTION39chain 'F' and (resid 60 through 70 )F60 - 70

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