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- PDB-6x6h: Structure of Shiga toxin 2 with a C-terminal peptide of ribosomal... -

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Basic information

Entry
Database: PDB / ID: 6x6h
TitleStructure of Shiga toxin 2 with a C-terminal peptide of ribosomal P stalk proteins
Components
  • (rRNA N-glycosylase) x 2
  • P11 peptide
  • Shiga toxin 2 B subunit
KeywordsTOXIN / Shiga toxin / ribosome-inactivating protein / C-terminal peptide of ribosomal P stalk proteins
Function / homology
Function and homology information


symbiont-mediated hemolysis of host erythrocyte / rRNA N-glycosylase / rRNA N-glycosylase activity / toxin activity / negative regulation of translation / extracellular region
Similarity search - Function
Shiga-like toxin, subunit A / Shiga-like toxin, beta subunit / Shiga-like toxin beta subunit / Ribosome-inactivating protein conserved site / Shiga/ricin ribosomal inactivating toxins active site signature. / Enterotoxin / Ribosome-inactivating protein / Ribosome-inactivating protein, subdomain 1 / Ribosome-inactivating protein, subdomain 2 / Ribosome-inactivating protein superfamily / Ribosome inactivating protein
Similarity search - Domain/homology
ACETIC ACID / rRNA N-glycosylase / Shiga toxin 2 B subunit
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.88 Å
AuthorsRudolph, M.J.
CitationJournal: J.Biol.Chem. / Year: 2020
Title: Structural basis for the interaction of Shiga toxin 2a with a C-terminal peptide of ribosomal P stalk proteins.
Authors: Rudolph, M.J. / Davis, S.A. / Tumer, N.E. / Li, X.P.
History
DepositionMay 28, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 9, 2020Provider: repository / Type: Initial release
Revision 2.0Sep 16, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / citation / citation_author / entity_poly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_validate_close_contact / pdbx_validate_torsion / struct_conf / struct_conn / struct_ref_seq / struct_sheet_range
Item: _atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id ..._atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id / _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _entity_poly.pdbx_strand_id / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.pdb_strand_id / _pdbx_struct_sheet_hbond.range_1_auth_asym_id / _pdbx_struct_sheet_hbond.range_2_auth_asym_id / _pdbx_struct_special_symmetry.auth_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_torsion.auth_asym_id / _struct_conf.beg_auth_asym_id / _struct_conf.end_auth_asym_id / _struct_conn.ptnr1_auth_asym_id / _struct_ref_seq.pdbx_strand_id / _struct_sheet_range.beg_auth_asym_id / _struct_sheet_range.end_auth_asym_id
Revision 2.1Nov 25, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.2Oct 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
Revision 2.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A1: rRNA N-glycosylase
A2: rRNA N-glycosylase
B: Shiga toxin 2 B subunit
C: Shiga toxin 2 B subunit
D: Shiga toxin 2 B subunit
E: Shiga toxin 2 B subunit
F: Shiga toxin 2 B subunit
P: P11 peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,01421
Polymers71,3718
Non-polymers64313
Water8,575476
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)82.148, 85.226, 98.841
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP22121
Components on special symmetry positions
IDModelComponents
11A1-401-

HOH

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Components

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Protein , 2 types, 6 molecules A1BCDEF

#1: Protein rRNA N-glycosylase / Stx2A


Mass: 27061.381 Da / Num. of mol.: 1
Fragment: N-terminal portion, disulfide linked to C-terminal fragment
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_29255, DOT81_27455, DOY22_27375, DQG35_26865, ED607_26125, ED648_25265, EHV81_26780, EHV90_26725, EHW09_26775, F7G01_26395, GJD97_09695, GN312_26720
Production host: Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase
#3: Protein
Shiga toxin 2 B subunit / Shiga toxin 2 subunit B / Shiga toxin 2B / Shiga toxin 2v subunit A / Shiga toxin Stx2 subunit B / ...Shiga toxin 2 subunit B / Shiga toxin 2B / Shiga toxin 2v subunit A / Shiga toxin Stx2 subunit B / Shiga toxin Stx2a subunit B / Stx2 holotoxin B subunit / Stx2 holotoxin subunit B / Stx2B / Stx2B protein


Mass: 7824.590 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: stxII, stx2B, stx2b, stx2B_2, stx2dB, stx2vB, stxB2, vtx2B, BvCmsHHP019_02074, BvCmsNSP072_02053, BvCmsOUP014_04264, C9098_23370, C9Z37_23105, C9Z78_24425, D6004_26885, D7K33_26370, D9X77_ ...Gene: stxII, stx2B, stx2b, stx2B_2, stx2dB, stx2vB, stxB2, vtx2B, BvCmsHHP019_02074, BvCmsNSP072_02053, BvCmsOUP014_04264, C9098_23370, C9Z37_23105, C9Z78_24425, D6004_26885, D7K33_26370, D9X77_26970, DAH30_25515, DM155_24460, DNR35_15450, EBM08_12130, F7F11_25580, HW43_14770, UN91_26180
Production host: Escherichia coli (E. coli) / References: UniProt: Q7DJJ2

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Protein/peptide , 2 types, 2 molecules A2P

#2: Protein/peptide rRNA N-glycosylase / Stx2A


Mass: 4532.119 Da / Num. of mol.: 1
Fragment: C-terminal fragment, disulfide linked to N-terminal portion
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_ ...Gene: stx2A, stx2a, stxA2, ARC77_05630, BTQ04_04340, BvCmsNSP072_02052, D4011_27180, D4660_26220, D5I97_26890, D6X63_27810, DAH26_28715, DL455_26690, DMI53_27500, DMO02_27200, DN703_28545, DOE35_29255, DOT81_27455, DOY22_27375, DQG35_26865, ED607_26125, ED648_25265, EHV81_26780, EHV90_26725, EHW09_26775, F7G01_26395, GJD97_09695, GN312_26720
Production host: Escherichia coli (E. coli) / References: UniProt: A9ZMR8, rRNA N-glycosylase
#4: Protein/peptide P11 peptide


Mass: 654.712 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Escherichia coli (E. coli)

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Non-polymers , 4 types, 489 molecules

#5: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cl
#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-ACY / ACETIC ACID


Mass: 60.052 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H4O2
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 476 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
Has protein modificationY

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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: 2.43 Å3/Da / Density % sol: 49.33 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 4.5
Details: 100 mM Sodium Acetate pH 4.5, 100 mM NaCl, 30% PEG 200

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.979 Å
DetectorType: ADSC HF-4M / Detector: PIXEL / Date: Sep 6, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 1.875→50 Å / Num. obs: 57068 / % possible obs: 99.7 % / Redundancy: 28.1 % / Biso Wilson estimate: 23.38 Å2 / Rmerge(I) obs: 0.38 / Rpim(I) all: 0.072 / Rrim(I) all: 0.387 / Χ2: 0.786 / Net I/σ(I): 2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.88-1.9122.53.06528050.3390.6563.1380.63999.4
1.91-1.9525.12.47628200.4510.4982.5280.69299.6
1.95-1.9830.12.33728090.6170.4262.3760.66999.9
1.98-2.0330.72.17227990.7120.392.2070.666100
2.03-2.0730.31.87828460.7880.341.9090.687100
2.07-2.1230.61.47228390.8430.2661.4960.727100
2.12-2.1729.11.43428160.8570.2651.4580.71100
2.17-2.2326.51.1828330.8780.2311.2030.73799.9
2.23-2.2928.61.06328480.9130.1991.0820.76999.8
2.29-2.37300.91528360.9430.1660.930.72199.9
2.37-2.4528.90.81928140.9510.1520.8330.73199.9
2.45-2.5527.20.70528460.9650.1350.7180.74899.9
2.55-2.6724.10.57628450.9080.1180.5890.76999
2.67-2.8123.90.46928210.9740.0960.4790.80299.1
2.81-2.98310.38428610.990.0690.390.82599.8
2.98-3.2131.40.27628790.9940.0490.280.873100
3.21-3.5428.40.19628840.9960.0370.1990.97499.9
3.54-4.0529.90.12529130.9980.0230.1271.005100
4.05-5.126.10.08928920.9990.0170.0910.98198.6
5.1-5027.60.09830620.9990.0190.10.9598.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1R4P

1r4p


Resolution: 1.88→42.753 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.47 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2056 2793 4.9 %
Rwork0.1677 54209 -
obs0.1696 57002 99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 94.44 Å2 / Biso mean: 28.531 Å2 / Biso min: 12.63 Å2
Refinement stepCycle: final / Resolution: 1.88→42.753 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5005 0 34 476 5515
Biso mean--40.81 38.95 -
Num. residues----637
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0065200
X-RAY DIFFRACTIONf_angle_d0.6717040
X-RAY DIFFRACTIONf_chiral_restr0.052787
X-RAY DIFFRACTIONf_plane_restr0.004910
X-RAY DIFFRACTIONf_dihedral_angle_d11.0193090
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.88-1.90740.33311380.3006233787
1.9074-1.94210.30041310.27272678100
1.9421-1.97940.29031250.25062727100
1.9794-2.01980.29491320.22872696100
2.0198-2.06380.26881720.21522652100
2.0638-2.11180.22871380.22736100
2.1118-2.16460.21761330.18672689100
2.1646-2.22310.20881420.17542730100
2.2231-2.28850.21571290.17462716100
2.2885-2.36240.22121480.16652693100
2.3624-2.44680.22311390.16062715100
2.4468-2.54470.24261290.16482713100
2.5447-2.66050.19731320.1657274699
2.6605-2.80080.20551370.1652269999
2.8008-2.97620.19671370.162732100
2.9762-3.20590.16741330.16112766100
3.2059-3.52840.21031610.15542735100
3.5284-4.03870.17861570.13492769100
4.0387-5.0870.16121490.1274276099
5.087-42.7530.18941310.1785292098
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)
14.5585-2.8985-0.8093.20360.82140.84850.0214-0.03350.42040.00980.0116-0.3823-0.1750.1954-0.02930.1941-0.05250.00080.1940.0090.262128.859762.9577130.9505
24.2889-1.7891-1.5641.88381.07532.88510.0462-0.03110.3040.02470.0573-0.2429-0.24110.0771-0.10140.1367-0.0709-0.02840.14520.00780.197327.594458.8765134.7661
31.3325-0.17430.07231.9506-0.08821.98140.02-0.2504-0.01850.23190.00770.03760.1121-0.191-0.00560.183-0.0360.00460.2236-0.00120.150213.875954.7208142.5354
42.3466-1.6479-0.97082.62571.20961.62050.09590.2364-0.0321-0.0718-0.1124-0.0218-0.0058-0.138-0.00320.1405-0.032-0.01840.1840.0160.130921.533550.8413122.133
54.13453.23961.43436.38650.15992.17570.118-0.0294-0.13490.0155-0.08910.00520.1180.50710.04260.14850.05820.03120.1961-0.01030.172229.852748.14120.9887
65.40662.86832.07765.90172.11812.85320.2405-0.2397-0.09130.5732-0.1047-0.23050.1926-0.0839-0.13990.22990.0346-0.00830.1630.03460.161922.967627.551117.0601
77.5861-4.08174.73963.4118-2.17084.9530.02410.4356-0.0028-0.1251-0.1754-0.25530.12320.68990.14810.13650.00510.0280.230.00860.148133.899317.1781103.1935
89.08075.74674.42496.78614.11035.1901-0.05810.1583-0.1799-0.2509-0.0940.09170.09860.09110.17110.19350.03530.00690.1620.0140.154225.480415.384897.935
99.29365.7019-3.15713.8765-0.59077.17560.18860.0105-0.50430.0005-0.1607-0.23420.14790.40790.04450.19930.0482-0.02740.13580.03450.2531.71911.8841100.3852
103.67591.48760.50611.84471.78942.25850.1227-0.16350.01050.1012-0.05640.04250.08720.0276-0.05130.16410.0025-0.01250.13420.0440.146828.418517.8615108.7589
119.36911.67152.73329.4009-6.69066.45750.40921.5863-0.9808-0.891-0.5863-0.62331.04170.94260.34170.37040.0982-0.03660.4032-0.10240.337834.56816.6312100.2939
124.88670.9651-0.90993.6233.48734.07330.45-0.7542-0.29260.1577-0.0002-0.57490.07920.7533-0.3880.24220.0199-0.04150.2656-0.02660.302534.268215.0746113.6994
136.34911.95141.7392.6318-2.28318.12990.0578-0.3521-0.07680.5882-0.0662-0.01690.13280.80640.07650.28120.0439-0.02650.13760.04170.203430.918313.6917125.2411
146.24534.40045.16236.93055.93957.76670.15230.0032-0.50580.06710.0459-0.27250.72440.2931-0.14580.26180.037-0.00890.1520.0570.258228.04797.8086117.4489
157.63430.73672.05178.509-1.36184.8130.1239-0.6557-0.71890.39260.0377-0.17320.33780.1404-0.08510.27640.03150.02010.22260.06590.205327.80317.5983124.816
163.99690.50051.28195.9627-1.87364.4618-0.1412-0.2618-0.0790.32460.01920.1881-0.07650.00360.00360.1540.02030.04390.16410.01070.174424.132917.6689122.2463
176.2182.525-1.49014.8098-1.00018.45780.0836-0.965-1.27651.09860.23170.37751.00310.3296-0.07450.47130.0639-0.02930.27750.13370.424626.73663.9637129.2815
187.86144.45952.2493.13793.18566.76840.1147-0.6006-0.00851.1444-0.0314-0.1471-0.1088-0.0513-0.22450.3140.04360.0040.26190.0390.213822.405219.5419130.7938
192.8889-1.02740.25913.5521.79832.0034-0.1666-0.5418-0.30760.57110.14280.27290.0055-0.04360.03080.34610.00110.10410.30570.08380.20912.23420.882130.935
204.81384.3514.24667.1714.45423.8866-0.0239-0.40660.32660.7135-0.11150.9585-0.3875-0.4550.02250.49970.05480.17930.38390.15630.41747.997620.0895132.4812
212.1873-0.40170.88873.11441.47921.4289-0.0311-0.5877-0.21120.4081-0.0910.33480.1166-0.29950.12290.30160.0050.06550.30870.0510.18178.877523.9904127.0683
226.00995.9637-5.53845.7975-5.44175.06690.2682-0.70040.22650.6952-0.54830.1839-0.50210.00690.20890.30630.01490.01060.26470.00170.26837.218932.5117124.6977
234.05821.80161.12684.9779-0.19152.80250.0448-0.2768-0.02370.357-0.18210.1389-0.127-0.05920.03760.17190.05870.09150.1912-0.01950.15872.659632.4691115.5144
246.60570.31880.82815.96042.10463.7772-0.1059-0.01680.09530.1340.06090.3062-0.1266-0.33150.08080.16180.00670.03220.18480.020.15770.349233.2331113.6658
255.88271.1257-0.48052.46010.05242.6589-0.07960.0610.0669-0.09650.02660.15080.0165-0.16070.01560.1410.00330.00940.10440.00070.11785.971433.0131109.1874
265.82291.5107-4.12734.203-0.63866.09750.22730.14720.1809-0.0146-0.06470.1949-0.0825-0.0543-0.20270.14360.0271-0.06360.13570.05820.08414.001829.513496.6081
273.295-0.36671.10733.4763-0.10175.70410.04150.2286-0.0796-0.185-0.02580.1349-0.0019-0.0712-0.01680.10430.01290.00720.11640.00120.141816.575727.028196.3071
286.92380.70620.98976.4765-0.14886.73560.0791-0.12570.0975-0.1312-0.1821-0.7016-0.24370.6998-0.07140.15650.00090.0080.21920.01810.234627.374726.079598.3322
296.9934-1.4327-2.290.7794-0.72236.68010.1591-0.06451.3878-1.58960.605-0.6913-1.32080.7558-0.65010.536-0.07740.08040.27790.01480.461427.142462.886116.9258
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 27 )A1 - 27
2X-RAY DIFFRACTION2chain 'A' and (resid 28 through 76 )A28 - 76
3X-RAY DIFFRACTION3chain 'A' and (resid 77 through 164 )A77 - 164
4X-RAY DIFFRACTION4chain 'A' and (resid 165 through 225 )A165 - 225
5X-RAY DIFFRACTION5chain 'A' and (resid 226 through 242 )A226 - 242
6X-RAY DIFFRACTION6chain 'A' and (resid 258 through 297 )A258 - 297
7X-RAY DIFFRACTION7chain 'B' and (resid 1 through 13 )B1 - 13
8X-RAY DIFFRACTION8chain 'B' and (resid 14 through 23 )B14 - 23
9X-RAY DIFFRACTION9chain 'B' and (resid 24 through 32 )B24 - 32
10X-RAY DIFFRACTION10chain 'B' and (resid 33 through 52 )B33 - 52
11X-RAY DIFFRACTION11chain 'B' and (resid 53 through 63 )B53 - 63
12X-RAY DIFFRACTION12chain 'B' and (resid 64 through 70 )B64 - 70
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 13 )C1 - 13
14X-RAY DIFFRACTION14chain 'C' and (resid 14 through 23 )C14 - 23
15X-RAY DIFFRACTION15chain 'C' and (resid 24 through 32 )C24 - 32
16X-RAY DIFFRACTION16chain 'C' and (resid 33 through 52 )C33 - 52
17X-RAY DIFFRACTION17chain 'C' and (resid 53 through 63 )C53 - 63
18X-RAY DIFFRACTION18chain 'C' and (resid 64 through 70 )C64 - 70
19X-RAY DIFFRACTION19chain 'D' and (resid 1 through 23 )D1 - 23
20X-RAY DIFFRACTION20chain 'D' and (resid 24 through 32 )D24 - 32
21X-RAY DIFFRACTION21chain 'D' and (resid 33 through 63 )D33 - 63
22X-RAY DIFFRACTION22chain 'D' and (resid 64 through 70 )D64 - 70
23X-RAY DIFFRACTION23chain 'E' and (resid 1 through 18 )E1 - 18
24X-RAY DIFFRACTION24chain 'E' and (resid 19 through 32 )E19 - 32
25X-RAY DIFFRACTION25chain 'E' and (resid 33 through 70 )E33 - 70
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 18 )F1 - 18
27X-RAY DIFFRACTION27chain 'F' and (resid 19 through 63 )F19 - 63
28X-RAY DIFFRACTION28chain 'F' and (resid 64 through 70 )F64 - 70
29X-RAY DIFFRACTION29chain 'P' and (resid 6 through 11 )P6 - 11

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