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- PDB-7k98: Preaminoacylation complex of M. tuberculosis PheRS with cognate p... -

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Basic information

Entry
Database: PDB / ID: 7k98
TitlePreaminoacylation complex of M. tuberculosis PheRS with cognate precursor tRNA and 5'-O-(N-phenylalanyl)sulfamoyl-adenosine (F-AMS)
Components
  • (Phenylalanine--tRNA ligase ...) x 2
  • tRNA(Phe)
KeywordsLIGASE/RNA / aminoacylation / phenylalanyl tRNA synthetase / adenylate analog / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID / LIGASE-RNA complex
Function / homology
Function and homology information


phenylalanine-tRNA ligase complex / phenylalanine-tRNA ligase / phenylalanyl-tRNA aminoacylation / phenylalanine-tRNA ligase activity / peptidoglycan-based cell wall / tRNA binding / magnesium ion binding / ATP binding / plasma membrane / cytoplasm
Similarity search - Function
Phenylalanyl-tRNA Synthetase; Chain B, domain 3 / Phenylalanyl-trna Synthetase, Chain B, domain 3 / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 - #10 / Ferrodoxin-fold anticodon-binding domain / 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 ...Phenylalanyl-tRNA Synthetase; Chain B, domain 3 / Phenylalanyl-trna Synthetase, Chain B, domain 3 / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 - #10 / Ferrodoxin-fold anticodon-binding domain / 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 / tRNA synthetase B5 domain / B5 domain profile. / tRNA synthetase B5 domain / Ferrodoxin-fold anticodon-binding domain / Ferrodoxin-fold anticodon-binding domain superfamily / Ferredoxin-fold anticodon binding domain / B3/4 domain / Ferredoxin-fold anticodon binding (FDX-ACB) domain profile. / Ferredoxin-fold anticodon binding domain / Phenylalanyl tRNA synthetase beta chain, core domain / Phenylalanyl tRNA synthetase beta chain CLM domain / Phenylalanine-tRNA ligase, class IIc, beta subunit / B3/B4 tRNA-binding domain / Phenylalanyl-tRNA synthetase-like, B3/B4 / B3/4 domain / Phenylalanyl-tRNA Synthetase; Chain B, domain 1 / 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 / Bira Bifunctional Protein; Domain 2 / BirA Bifunctional Protein; domain 2 / 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 proteins / 3-Layer(bba) Sandwich / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Alpha-Beta Plaits / Nucleic acid-binding, OB-fold / Beta Barrel / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
5'-O-(L-phenylalanylsulfamoyl)adenosine / : / 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 / molecular replacement / Resolution: 2.19 Å
AuthorsMichalska, K. / Chang, C. / Jedrzejczak, R. / Wower, J. / Baragana, B. / Forte, B. / Gilbert, I.H. / 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 28, 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
D: Phenylalanine--tRNA ligase alpha subunit
E: Phenylalanine--tRNA ligase beta subunit
C: tRNA(Phe)
F: tRNA(Phe)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)305,77926
Polymers304,1296
Non-polymers1,65020
Water12,106672
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area36480 Å2
ΔGint-326 kcal/mol
Surface area111380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)147.423, 65.302, 193.481
Angle α, β, γ (deg.)90.000, 109.290, 90.000
Int Tables number4
Space group name H-MP1211

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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: 37687.520 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) / Strain (production host): BL21-Gold (DE3) / References: UniProt: P9WFU3, phenylalanine-tRNA ligase
#2: Protein Phenylalanine--tRNA ligase beta subunit / Phenylalanyl-tRNA synthetase beta subunit / PheRS


Mass: 89533.961 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 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21-Gold (DE3) / 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 , 5 types, 692 molecules

#4: Chemical ChemComp-W5Y / 5'-O-(L-phenylalanylsulfamoyl)adenosine


Mass: 493.494 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H23N7O7S / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 672 / 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: 2.89 Å3/Da / Density % sol: 57.44 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop
Details: 30% PEG400, 0.2 M magnesium chloride, 0.1 M HEPES, pH 7.5, no cryoprotectant

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9793 Å
DetectorType: DECTRIS PILATUS3 X 6M / Detector: PIXEL / Date: Dec 9, 2018 / Details: mirrors
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 2.19→30 Å / Num. obs: 173141 / % possible obs: 96.9 % / Observed criterion σ(I): -3 / Redundancy: 6.4 % / Rmerge(I) obs: 0.094 / Rpim(I) all: 0.039 / Rrim(I) all: 0.102 / Χ2: 1.409 / Net I/av σ(I): 21.5 / Net I/σ(I): 21.5
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.2-2.2461.2231.5682630.5960.5341.3380.92993.6
2.24-2.285.91.11183140.6410.4831.2160.96793.1
2.28-2.325.90.97382660.6940.4241.0650.98193.4
2.32-2.375.50.76280510.760.3440.840.98491.2
2.37-2.425.90.71283680.8050.310.781.00393.9
2.42-2.486.30.64485270.8490.2690.71.00596.8
2.48-2.546.20.53286290.8950.2240.5791.04196.6
2.54-2.616.30.4487050.9270.1860.4791.08197.6
2.61-2.686.30.34887090.950.1480.3791.13598.7
2.68-2.776.40.28887460.960.1220.3131.20198.6
2.77-2.876.40.22488490.9750.0950.2441.30598.9
2.87-2.996.30.17488050.9830.0750.191.47798.7
2.99-3.1260.13985460.9860.060.1521.78195.8
3.12-3.297.10.11988880.9910.0480.1291.67999.4
3.29-3.497.10.187830.9930.040.1081.86199.1
3.49-3.7670.08688990.9950.0350.0931.82399.4
3.76-4.146.80.07589580.9950.0310.0811.93899.3
4.14-4.736.30.06586880.9960.0280.0711.95796.5
4.73-5.967.10.06390200.9970.0260.0681.85299.7
5.96-306.60.04991270.9980.020.0531.5698.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
HKL-3000data scaling
PHASERphasing
PHENIX1.18rc1_3777refinement
PDB_EXTRACT3.25data extraction
HKL-3000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3PCO

3pco


Resolution: 2.19→29.85 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 27.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2242 3498 2.02 %
Rwork0.1775 169565 -
obs0.1784 173063 96.44 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 182.87 Å2 / Biso mean: 61.1809 Å2 / Biso min: 21.05 Å2
Refinement stepCycle: final / Resolution: 2.19→29.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17796 3256 101 675 21828
Biso mean--49.86 51.8 -
Num. residues----2510
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONf_bond_d0.0070.09622119
X-RAY DIFFRACTIONf_angle_d0.91510.63830941
X-RAY DIFFRACTIONf_chiral_restr0.0520.2933642
X-RAY DIFFRACTIONf_plane_restr0.0060.0513539
X-RAY DIFFRACTIONf_dihedral_angle_d24.127179.9898639
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 25

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.19-2.220.34511240.28235717584182
2.22-2.250.29021320.28016485661792
2.25-2.290.38721360.27496524666095
2.29-2.320.39391210.26876528664993
2.32-2.360.29651180.25886368648692
2.36-2.40.30341350.24996522665793
2.4-2.440.30391100.24656742685296
2.44-2.490.3331470.24076729687696
2.49-2.540.27561480.23576784693297
2.54-2.60.29181250.2416876700198
2.6-2.660.30581390.23536872701199
2.66-2.720.30811320.22796972710499
2.72-2.80.27731550.22446824697999
2.8-2.880.27781410.22146980712199
2.88-2.970.29831760.22496914709099
2.97-3.080.31071320.2256671680395
3.08-3.20.21021130.21166928704199
3.2-3.350.2461490.2027018716799
3.35-3.520.23061480.18766964711299
3.52-3.740.20851750.1666963713899
3.74-4.030.20481560.14677030718699
4.03-4.440.16571530.12556875702897
4.44-5.080.16751550.11966962711798
5.08-6.390.16931550.1471107265100
6.39-29.850.17671230.14267207733098
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)
14.97655.1458-5.41526.1761-4.51917.28560.6324-1.44550.26550.8653-0.37710.55090.01310.5027-0.30451.01790.16540.14410.8029-0.02970.6251-65.753611.531717.5197
26.25275.5091-5.07084.7652-4.31676.6756-0.45030.0453-0.65490.48170.3349-0.25480.70.16210.15970.91330.22350.17070.7643-0.02040.7294-64.60345.20219.7923
36.77026.8182-2.14428.4034-4.24753.8574-0.1624-0.59950.38340.20640.21870.62450.05150.2007-0.28590.72640.09840.080.6536-0.10950.4593-62.232116.56914.573
46.532-4.8495-6.7535.13465.19519.4118-0.42-0.43010.64770.55970.5535-0.40470.83920.4355-0.09520.4155-0.0622-0.03140.445-0.00990.4112-25.520114.5709-24.5381
51.0618-0.12741.16083.02170.10771.3852-0.0574-0.10480.0043-0.04470.1695-0.10510.10050.0278-0.09650.343-0.04890.0680.39280.00350.3575-21.79361.2318-56.6175
62.55680.84770.80145.1328-3.63853.4015-0.15770.15390.1232-0.2981-0.276-1.12360.62421.32520.440.5160.10370.15910.6796-0.09330.6165-2.3025-5.5449-66.5987
71.8082-0.2728-0.10141.6895-0.70563.0248-0.02440.12510.06580.03440.0373-0.0175-0.01880.1027-0.01630.3044-0.05710.09650.3308-0.03740.333-18.13985.5117-64.4926
83.21984.66783.64557.06794.32776.88780.13630.16610.16940.09120.0563-0.1054-0.34820.2535-0.26560.397-0.04080.12020.382-0.02720.4053-13.683318.8426-63.5495
92.79071.71841.13016.03531.36030.76670.00120.0922-0.0023-0.4884-0.06120.0339-0.1569-0.05340.04920.3222-0.0610.08570.34050.02950.2317-20.07493.6633-68.4287
101.6317-0.9114-0.2066.9834-4.67713.5597-0.08060.30850.10640.0822-0.0756-0.2862-0.1570.33130.25420.4582-0.1550.00610.6125-0.09550.4151-12.157313.6964-43.032
118.33863.86491.86592.27020.92461.08720.2545-0.41260.04970.1386-0.1741-0.0515-0.08940.1179-0.08720.38630.05750.09780.43860.0170.409913.539634.4834-77.1785
129.25826.34131.57925.85591.11050.86720.3026-0.4960.55010.4197-0.27780.112-0.0877-0.1151-0.03680.40970.02420.11270.4359-0.04160.487717.292438.3777-72.8199
132.7994-0.3561-1.49021.39930.20071.7536-0.2382-0.43-0.34510.06430.049-0.17490.3320.36470.16740.32170.0870.04710.50170.10480.363313.32210.0064-87.7751
140.36080.1512-0.82960.4256-0.31231.608-0.06990.13370.0135-0.06120.0459-0.03590.2448-0.07390.02010.3082-0.0167-0.00160.4284-0.04720.4007-13.59093.2296-73.7001
151.37861.17831.63820.44070.7335.08990.12420.0101-0.24860.01010.1506-0.35580.50980.66-0.32070.35160.09060.00120.5067-0.08270.475-8.999-7.8053-49.3986
161.03450.2486-0.6791.1099-0.48551.35990.04810.0389-0.04790.13520.0567-0.03680.12810.061-0.08980.42230.0329-0.08140.3285-0.03090.3416-26.5955-13.7949-21.092
176.30652.6948-0.17954.6271-1.36561.91230.4812-1.3473-0.38360.6327-0.9302-1.0237-0.19210.44740.37730.7270.2111-0.18431.80330.19140.764928.7156-4.6454-10.5858
187.97963.54011.01434.2538-0.5562.73630.069-0.2882-0.04880.0892-0.2471-0.6268-0.08420.77640.17830.58990.1384-0.14861.23090.03010.587521.3356-4.017-18.4306
199.2385-1.65340.38184.17092.83642.2705-1.3011-1.00730.42381.14740.8292-0.3546-0.4053-0.03520.53020.4107-0.0535-0.00080.27060.03010.2718-27.5083-6.6207-24.1164
201.5063-0.0920.7031.25870.01761.6818-0.0387-0.0128-0.10130.01030.01450.1136-0.0356-0.13720.02440.2572-0.0262-0.03180.3512-0.02820.3434-56.8084.2943-51.9891
218.16951.41836.45757.95514.38436.5579-0.0205-0.0135-0.0150.4813-0.17990.34910.3957-0.25410.1980.4231-0.0556-0.06660.4490.08670.3789-49.394-5.464-32.4269
221.18660.2133-0.2882.02540.29450.6258-0.0439-0.1187-0.21420.41580.05610.18590.1469-0.1093-0.02280.3815-0.034-0.00510.54680.0330.4557-91.415-16.7836-51.8837
230.76010.21990.59070.320.21210.6774-0.0678-0.0559-0.00260.04510.04250.0658-0.1034-0.11880.03970.37670.01170.01680.3849-0.00390.3425-54.345312.8067-40.1433
245.30720.3341-3.24750.9989-1.57417.28760.11020.08110.3413-0.2927-0.2080.1447-0.01941.97350.07150.5369-0.0294-0.15410.93250.03830.694713.50111.1943-46.6039
250.6259-1.87080.2795.4434-0.80170.10820.4709-0.36311.5197-0.0323-0.6762-1.20220.21661.48180.28550.5809-0.13920.03831.784-0.05290.852421.154813.7767-32.8204
265.8782-2.0345-2.13361.97750.93521.4482-0.331-0.81920.12710.40090.5273-0.63270.17191.2743-0.2150.56410.0361-0.07121.1054-0.16220.67183.816217.8311-13.8757
274.3734-1.3995-6.08380.46142.01348.9871-0.23980.052-0.18320.33130.25310.21361.25891.8024-0.06390.57730.1967-0.02711.25950.02950.83715.24215.0794-30.5338
285.90340.47763.46370.09740.67413.8485-0.3375-0.0905-0.4080.04420.1856-0.156-0.16960.73890.15890.54580.1179-0.00511.17950.13130.782818.83783.7545-46.7964
299.11160.02217.77340.71731.17489.70230.23860.1911-0.1082-0.308-0.111-0.0119-0.1025-0.8679-0.08630.70030.04180.12560.87290.10050.6139-72.1378-3.3287-21.2084
307.4823-6.0486-6.95724.92755.65746.4643-0.62030.0053-1.74570.7987-0.65011.20790.3801-0.98891.16480.5843-0.08460.15870.85860.050.896-70.8392-6.4282-5.3133
318.8443-4.006-0.03423.7411-0.14382.0196-0.8701-1.4084-0.24871.01740.77860.142-0.1664-0.25570.08880.71250.15690.04750.74170.05560.5213-46.1679-10.3560.9085
322.4955-2.64272.51692.7776-2.65892.636-0.8905-0.23961.12340.2592-0.2424-0.7345-0.986-0.72941.21330.76010.21860.0890.84730.02780.8844-64.81982.4267-6.6039
335.72531.0124-4.39471.0273-1.12333.49650.50650.28230.05250.02410.14110.2025-1.1903-0.7818-0.71840.85310.15250.24151.1093-0.13180.8718-80.76467.5053-6.2551
342.73272.78740.58856.0673-3.23665.35360.09630.16460.07590.08730.1609-0.0510.9064-0.829-0.23620.582-0.0012-0.02220.796-0.02020.6347-72.2685-1.07-33.5353
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 20 )A-1 - 20
2X-RAY DIFFRACTION2chain 'A' and (resid 21 through 55 )A21 - 55
3X-RAY DIFFRACTION3chain 'A' and (resid 56 through 91 )A56 - 91
4X-RAY DIFFRACTION4chain 'A' and (resid 92 through 110 )A92 - 110
5X-RAY DIFFRACTION5chain 'A' and (resid 111 through 142 )A111 - 142
6X-RAY DIFFRACTION6chain 'A' and (resid 143 through 169 )A143 - 169
7X-RAY DIFFRACTION7chain 'A' and (resid 170 through 260 )A170 - 260
8X-RAY DIFFRACTION8chain 'A' and (resid 261 through 285 )A261 - 285
9X-RAY DIFFRACTION9chain 'A' and (resid 286 through 318 )A286 - 318
10X-RAY DIFFRACTION10chain 'A' and (resid 319 through 341 )A319 - 341
11X-RAY DIFFRACTION11chain 'B' and (resid -2 through 99 )B-2 - 99
12X-RAY DIFFRACTION12chain 'B' and (resid 100 through 168 )B100 - 168
13X-RAY DIFFRACTION13chain 'B' and (resid 169 through 394 )B169 - 394
14X-RAY DIFFRACTION14chain 'B' and (resid 395 through 550 )B395 - 550
15X-RAY DIFFRACTION15chain 'B' and (resid 551 through 635 )B551 - 635
16X-RAY DIFFRACTION16chain 'B' and (resid 636 through 831 )B636 - 831
17X-RAY DIFFRACTION17chain 'D' and (resid -1 through 20 )D-1 - 20
18X-RAY DIFFRACTION18chain 'D' and (resid 21 through 91 )D21 - 91
19X-RAY DIFFRACTION19chain 'D' and (resid 92 through 110 )D92 - 110
20X-RAY DIFFRACTION20chain 'D' and (resid 111 through 318 )D111 - 318
21X-RAY DIFFRACTION21chain 'D' and (resid 319 through 341 )D319 - 341
22X-RAY DIFFRACTION22chain 'E' and (resid -4 through 290 )E-4 - 290
23X-RAY DIFFRACTION23chain 'E' and (resid 291 through 831 )E291 - 831
24X-RAY DIFFRACTION24chain 'C' and (resid 1 through 10 )C1 - 10
25X-RAY DIFFRACTION25chain 'C' and (resid 11 through 20 )C11 - 20
26X-RAY DIFFRACTION26chain 'C' and (resid 21 through 45 )C21 - 45
27X-RAY DIFFRACTION27chain 'C' and (resid 46 through 50 )C46 - 50
28X-RAY DIFFRACTION28chain 'C' and (resid 51 through 77 )C51 - 77
29X-RAY DIFFRACTION29chain 'F' and (resid 1 through 10 )F1 - 10
30X-RAY DIFFRACTION30chain 'F' and (resid 11 through 20 )F11 - 20
31X-RAY DIFFRACTION31chain 'F' and (resid 21 through 45 )F21 - 45
32X-RAY DIFFRACTION32chain 'F' and (resid 46 through 50 )F46 - 50
33X-RAY DIFFRACTION33chain 'F' and (resid 51 through 65 )F51 - 65
34X-RAY DIFFRACTION34chain 'F' and (resid 66 through 77 )F66 - 77

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