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- PDB-4gdk: Crystal Structure of Human Atg12~Atg5 Conjugate in Complex with a... -

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Basic information

Entry
Database: PDB / ID: 4gdk
TitleCrystal Structure of Human Atg12~Atg5 Conjugate in Complex with an N-terminal Fragment of Atg16L1
Components
  • Autophagy protein 5
  • Autophagy-related protein 16-1
  • Ubiquitin-like protein ATG12
KeywordsPROTEIN BINDING / protein-protein conjugate / protein-protein complex / ubiquitin-like protein / autophagy / E3 ligase / ubiquitin-like fold / structural protein / isopeptide bond / Cytoplasm and autophagosomal membranes
Function / homology
Function and homology information


otolith development / regulation of autophagosome maturation / positive regulation of viral translation / response to fluoride / C-terminal protein lipidation / regulation of cytokine production involved in immune response / Atg8-family ligase activity / Atg12-Atg5-Atg16 complex / antigen processing and presentation of endogenous antigen / negative regulation of dendrite extension ...otolith development / regulation of autophagosome maturation / positive regulation of viral translation / response to fluoride / C-terminal protein lipidation / regulation of cytokine production involved in immune response / Atg8-family ligase activity / Atg12-Atg5-Atg16 complex / antigen processing and presentation of endogenous antigen / negative regulation of dendrite extension / vacuole-isolation membrane contact site / phagophore / negative regulation of autophagic cell death / ubiquitin-like protein transferase activity / negative regulation of defense response to virus / cellular response to nitrosative stress / ventricular cardiac muscle cell development / microautophagy / positive regulation of stress granule assembly / glycophagy / regulation of cilium assembly / transferase complex / aggrephagy / dendrite arborization / mucus secretion / mitochondria-associated endoplasmic reticulum membrane contact site / response to fungus / xenophagy / corpus callosum development / protein localization to phagophore assembly site / negative thymic T cell selection / phagophore assembly site membrane / autophagy of mitochondrion / piecemeal microautophagy of the nucleus / negative stranded viral RNA replication / regulation of release of sequestered calcium ion into cytosol / endolysosome membrane / cellular response to nitrogen starvation / response to iron(II) ion / positive regulation of mucus secretion / regulation of reactive oxygen species metabolic process / negative regulation of cardiac muscle cell apoptotic process / negative regulation of phagocytosis / axonal transport / negative regulation of type I interferon production / Receptor Mediated Mitophagy / Macroautophagy / chaperone-mediated autophagy / heart contraction / autophagosome membrane / blood vessel remodeling / autophagosome assembly / axoneme / autophagosome maturation / regulation of postsynaptic membrane neurotransmitter receptor levels / postsynaptic modulation of chemical synaptic transmission / mitophagy / membrane-membrane adaptor activity / positive regulation of autophagy / sperm midpiece / cardiac muscle cell apoptotic process / negative regulation of protein ubiquitination / post-translational protein modification / autophagosome / negative regulation of innate immune response / hippocampus development / PINK1-PRKN Mediated Mitophagy / Negative regulators of DDX58/IFIH1 signaling / macroautophagy / Schaffer collateral - CA1 synapse / autophagy / protein tag activity / phagocytic vesicle membrane / vasodilation / protein transport / chromatin organization / GTPase binding / defense response to virus / postsynapse / protein ubiquitination / response to xenobiotic stimulus / axon / innate immune response / intracellular membrane-bounded organelle / glutamatergic synapse / protein-containing complex / nucleoplasm / identical protein binding / membrane / cytosol / cytoplasm
Similarity search - Function
Ubiquitin-like protein Atg12 / Ubiquitin-like autophagy protein Apg12 / Autophagy protein Apg5, helix rich domain / Ubiquitin-like (UB roll) - #620 / Autophagy-related protein 5 / Autophagy protein Atg5, helix rich domain / Autophagy protein Atg5, UblA domain / : / : / : ...Ubiquitin-like protein Atg12 / Ubiquitin-like autophagy protein Apg12 / Autophagy protein Apg5, helix rich domain / Ubiquitin-like (UB roll) - #620 / Autophagy-related protein 5 / Autophagy protein Atg5, helix rich domain / Autophagy protein Atg5, UblA domain / : / : / : / Autophagy protein ATG5, UblB domain / Autophagy protein ATG5, alpha-helical bundle region / Autophagy protein ATG5, UblA domain / Autophagy-related protein 16 / Autophagy-related protein 16 domain / Autophagy protein 16 (ATG16) / Serum Albumin; Chain A, Domain 1 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin-like domain superfamily / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Roll / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Ubiquitin-like protein ATG12 / Autophagy-related protein 16-1 / Autophagy protein 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsOtomo, C. / Metlagel, Z. / Takaesu, G. / Otomo, T.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2013
Title: Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy.
Authors: Otomo, C. / Metlagel, Z. / Takaesu, G. / Otomo, T.
History
DepositionJul 31, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 5, 2012Provider: repository / Type: Initial release
Revision 1.1Jan 2, 2013Group: Database references
Revision 1.2Jan 16, 2013Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_conn.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _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: Ubiquitin-like protein ATG12
B: Autophagy protein 5
C: Autophagy-related protein 16-1
D: Ubiquitin-like protein ATG12
E: Autophagy protein 5
F: Autophagy-related protein 16-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,9038
Polymers94,8576
Non-polymers462
Water1,36976
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)43.757, 113.153, 210.685
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Ubiquitin-like protein ATG12 / Autophagy-related protein 12 / APG12-like


Mass: 10282.029 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APG12, APG12L, ATG12 / Plasmid: pACYC Duet-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O94817
#2: Protein Autophagy protein 5 / APG5-like / Apoptosis-specific protein


Mass: 32489.195 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APG5L, ASP, ATG5 / Plasmid: pACYC Duet-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9H1Y0
#3: Protein/peptide Autophagy-related protein 16-1 / APG16-like 1


Mass: 4657.435 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: APG16L, ATG16L1, UNQ9393/PRO34307 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q676U5
#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 76 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHERE IS AN ISOPEPTIDE LINKAGE BETWEEN RESIDUE GLY140 OF ATG12 AND LYS130 OF ATG5. THE ATG12~ATG5 ...THERE IS AN ISOPEPTIDE LINKAGE BETWEEN RESIDUE GLY140 OF ATG12 AND LYS130 OF ATG5. THE ATG12~ATG5 CONJUGATE WAS GENERATED BY CO-EXPRESSING ATG12 AND ATG5 FROM PACYC DUET-1 AND ATG7 AND ATG10 FROM PCDF DUET-1 IN E. COLI.
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: 2.75 Å3/Da / Density % sol: 55.26 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PROTEIN: 10 MG/ML in 0.01M HEPES pH 7.0, 0.3 M NaCl, 0.001 M DTT; RESERVOIR: 0.1M Hepes pH7.5, 0.2 M lithium citrate, 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 16, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 29676 / % possible obs: 99.9 % / Redundancy: 6.9 % / Rmerge(I) obs: 0.1 / Χ2: 1.002 / Net I/σ(I): 9.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.7-2.86.10.63628661.0161100
2.8-2.917.10.49429401.0281100
2.91-3.047.30.34928850.9931100
3.04-3.27.30.23329381.0241100
3.2-3.47.30.162294911100
3.4-3.667.20.12229501.0341100
3.66-4.0370.09729500.953199.9
4.03-4.626.80.07729631.0091100
4.62-5.816.80.07630310.9851100
5.81-506.60.05632040.981199.6

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIX1.8_1069refinement
PDB_EXTRACT3.11data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→44.058 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8291 / SU ML: 0.27 / σ(F): 1.34 / Phase error: 23.5 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2361 2000 6.76 %RANDOM
Rwork0.1756 ---
obs0.1796 29598 99.5 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 152.09 Å2 / Biso mean: 67.2963 Å2 / Biso min: 29.79 Å2
Refinement stepCycle: LAST / Resolution: 2.7→44.058 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6469 0 2 76 6547
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0036655
X-RAY DIFFRACTIONf_angle_d0.6619009
X-RAY DIFFRACTIONf_chiral_restr0.049960
X-RAY DIFFRACTIONf_plane_restr0.0031137
X-RAY DIFFRACTIONf_dihedral_angle_d11.3912516
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6999-2.76740.29571320.24351821195394
2.7674-2.84220.30391400.241119272067100
2.8422-2.92580.33271420.239419632105100
2.9258-3.02020.27661370.234319032040100
3.0202-3.12810.29321450.228919882133100
3.1281-3.25330.3121390.212919272066100
3.2533-3.40140.27621440.208319852129100
3.4014-3.58060.22641410.198319492090100
3.5806-3.80480.24761430.175319632106100
3.8048-4.09840.23351440.161419752119100
4.0984-4.51050.20141440.137920032147100
4.5105-5.16230.1971450.129919992144100
5.1623-6.50060.2331480.166720442192100
6.5006-44.06390.19631560.166121512307100
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)
10.0341-0.00450.0006-0.02540.0357-0.0155-0.51030.62330.7423-0.03610.2005-0.083-0.2888-0.15810.00010.98680.1994-0.06930.7893-0.00550.6569-2.512513.844918.9204
20.02210.06840.08150.04970.06820.02350.11450.7893-0.02190.1443-0.1785-0.06180.5336-0.0942-0.00030.89640.1093-0.01260.9108-0.09870.54921.7682.920310.6551
3-0.0113-0.0347-0.01440.044-0.11250.06480.19410.14740.1859-0.30270.11080.5726-0.6101-0.3147-0.00070.82920.108-0.01270.7490.07430.5769-7.390811.975822.3126
40.07150.02090.01670.0539-0.0114-0.0065-0.44020.1934-0.7556-0.09950.1192-0.3472-0.0945-0.19750.00120.8433-0.079900.6501-0.03380.3723-5.29661.390520.2514
50.0849-0.0451-0.04230.01560.02680.07050.05460.135-0.32990.18980.0824-0.66860.69560.45690.00010.96140.05110.08620.76240.00080.57761.166-2.817819.8833
60.2144-0.1390.09110.0296-0.107-0.0041-0.2305-0.24851.0198-0.150.3005-0.24390.1888-0.431900.8605-0.02850.11950.67840.04740.42754.45227.355728.6212
70.01430.01820.00570.0434-0.02680.01260.0990.08150.62830.112-0.21190.34070.07310.35230.00010.74470.15660.08580.69190.0660.6061.117916.255528.4386
80.1493-0.0878-0.21750.0449-0.07150.157-0.13490.39310.0409-0.38730.00990.02530.3120.08090.00020.75270.04320.04170.66460.00060.75056.5857.852619.9282
90.1870.001-0.05130.14160.05780.0612-0.0021-0.39970.12790.9841-0.0633-0.4858-0.27040.28740.00020.5288-0.0026-0.04170.4755-0.02960.672812.282615.088561.1666
10-0.02170.1077-0.09070.0699-0.11660.2198-0.2758-0.7208-0.06120.51-0.2067-0.0810.04510.2297-0.00010.44490.10610.03270.40560.07490.50119.1692-9.382164.5805
110.95650.28720.06022.0892-0.5891.128-0.00380.0141-0.0681-0.0316-0.0277-0.13130.1263-0.008700.25280.00390.00950.3442-0.02220.37082.625-7.102250.1627
121.2341-1.10650.48190.72730.21481.11160.1560.24980.0245-0.1332-0.02120.10430.0842-0.1981-0.00010.4259-0.00320.05070.4088-0.040.42992.9261-1.022341.1325
130.40780.25040.40350.22790.24370.333-0.13060.3694-0.6109-0.3144-0.3213-1.2110.25010.12530.14140.54530.16450.20550.6362-0.05980.823120.93273.792834.0264
140.2616-0.10190.13190.2791-0.08480.1390.1723-0.07150.3106-0.4909-0.5772-0.6661-0.21610.6925-0.20890.32420.12390.15770.57470.05890.952422.55485.255344.0898
150.06550.06880.09710.26850.4460.7353-0.6936-0.32280.7814-0.5917-0.4009-0.3514-1.17830.2585-0.10020.5496-0.1090.24450.47190.07320.912618.453622.561136.8463
160.1045-0.2076-0.22780.25060.28360.170.3313-0.11020.2946-0.0470.04260.6096-0.1487-0.4368-0.00030.4254-0.0028-0.00680.51770.08380.6687-0.443216.257239.8881
17-0.0063-0.0439-0.04620.11990.0516-0.0183-0.32170.7370.4251-0.24090.04880.0244-0.65380.0867-0.00130.7161-0.07070.05490.42760.120.78057.627228.580643.7118
180.4699-0.21740.49040.5028-0.39840.38880.07580.00510.31580.10590.0257-0.3587-0.05520.0342-0.00010.4180.03930.05870.33920.00540.44714.568316.644850.5298
190.3226-0.10240.26150.2848-0.16450.3739-0.1654-0.344-0.50520.72550.4257-0.6396-0.3476-0.52380.32240.7707-0.0906-0.12860.7810.00050.4653-0.67384.1765120.4149
200.08550.07540.02540.03210.03810.0087-0.2195-0.18111.73670.5116-0.672-0.87880.36580.5022-0.00010.6878-0.13580.0290.93590.12120.93227.11839.8466112.6264
210.053-0.08160.05880.0576-0.14870.06410.063-0.0709-0.3438-0.0741-0.09210.20850.7017-0.29450.00020.919-0.0043-0.05280.7099-0.09180.47862.1312-3.8726113.8407
220.5956-0.13160.28710.1921-0.18140.23880.0031-0.11480.1774-0.19780.33420.6714-0.0886-0.4494-00.79130.0044-0.05080.79950.01940.5305-4.6786.8307109.7554
230.0116-0.11490.08050.232-0.17780.18460.26120.59990.374-0.4288-0.254-0.3663-0.5832-0.424300.70090.23550.0610.70450.11510.5604-10.952513.766272.6408
240.48930.18150.34240.11110.25010.3543-0.51420.35870.2832-0.3042-0.066-0.11930.7744-0.9479-0.10960.6429-0.11280.06960.3776-0.00050.4358-1.5044-9.637369.1097
250.12060.0974-0.03680.51180.32131.1465-0.0209-0.1777-0.2269-0.09520.0972-0.07290.3512-0.2525-0.00160.52870.0538-0.07160.50070.04780.47610.4403-6.654880.5445
261.6258-0.18770.0272-0.0754-0.0341.24030.0245-0.4833-0.15140.20070.1171-0.25620.01760.01070.00040.46990.0133-0.06790.53080.08150.41533.9929-5.702390.088
271.2085-0.29570.05130.6533-0.25932.9096-0.022-0.20050.2001-0.10340.157-0.0404-0.3906-0.5408-00.49580.12190.02310.470.01450.4707-9.639911.573890.7578
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resseq 53:61)A53 - 61
2X-RAY DIFFRACTION2chain 'A' and (resseq 62:71)A62 - 71
3X-RAY DIFFRACTION3chain 'A' and (resseq 72:80)A72 - 80
4X-RAY DIFFRACTION4chain 'A' and (resseq 81:91)A81 - 91
5X-RAY DIFFRACTION5chain 'A' and (resseq 92:104)A92 - 104
6X-RAY DIFFRACTION6chain 'A' and (resseq 105:115)A105 - 115
7X-RAY DIFFRACTION7chain 'A' and (resseq 116:123)A116 - 123
8X-RAY DIFFRACTION8chain 'A' and (resseq 124:140)A124 - 140
9X-RAY DIFFRACTION9chain 'C' and (resseq 10:28)C10 - 28
10X-RAY DIFFRACTION10chain 'C' and (resseq 29:43)C29 - 43
11X-RAY DIFFRACTION11chain 'B' and (resseq 3:90)B3 - 90
12X-RAY DIFFRACTION12chain 'B' and (resseq 91:137)B91 - 137
13X-RAY DIFFRACTION13chain 'B' and (resseq 138:158)B138 - 158
14X-RAY DIFFRACTION14chain 'B' and (resseq 159:173)B159 - 173
15X-RAY DIFFRACTION15chain 'B' and (resseq 174:186)B174 - 186
16X-RAY DIFFRACTION16chain 'B' and (resseq 187:205)B187 - 205
17X-RAY DIFFRACTION17chain 'B' and (resseq 206:222)B206 - 222
18X-RAY DIFFRACTION18chain 'B' and (resseq 223:275)B223 - 275
19X-RAY DIFFRACTION19chain 'D' and (resseq 54:71)D54 - 71
20X-RAY DIFFRACTION20chain 'D' and (resseq 72:80)D72 - 80
21X-RAY DIFFRACTION21chain 'D' and (resseq 81:104)D81 - 104
22X-RAY DIFFRACTION22chain 'D' and (resseq 105:140)D105 - 140
23X-RAY DIFFRACTION23chain 'F' and (resseq 9:27)F9 - 27
24X-RAY DIFFRACTION24chain 'F' and (resseq 28:43)F28 - 43
25X-RAY DIFFRACTION25chain 'E' and (resseq 3:49)E3 - 49
26X-RAY DIFFRACTION26chain 'E' and (resseq 50:137)E50 - 137
27X-RAY DIFFRACTION27chain 'E' and (resseq 138:274)E138 - 274

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