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- PDB-4u2v: Bak BH3-in-Groove dimer (GFP) -

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Basic information

Entry
Database: PDB / ID: 4u2v
TitleBak BH3-in-Groove dimer (GFP)
ComponentsGreen fluorescent protein,Bcl-2 homologous antagonist/killer
KeywordsAPOPTOSIS / Bak / Bcl-2
Function / homology
Function and homology information


Activation and oligomerization of BAK protein / BAK complex / BH domain binding / endocrine pancreas development / Release of apoptotic factors from the mitochondria / establishment or maintenance of transmembrane electrochemical gradient / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / endoplasmic reticulum calcium ion homeostasis / regulation of mitochondrial membrane permeability ...Activation and oligomerization of BAK protein / BAK complex / BH domain binding / endocrine pancreas development / Release of apoptotic factors from the mitochondria / establishment or maintenance of transmembrane electrochemical gradient / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / endoplasmic reticulum calcium ion homeostasis / regulation of mitochondrial membrane permeability / response to UV-C / Bcl-2 family protein complex / negative regulation of release of cytochrome c from mitochondria / porin activity / positive regulation of IRE1-mediated unfolded protein response / pore complex / positive regulation of release of cytochrome c from mitochondria / positive regulation of proteolysis / animal organ regeneration / extrinsic apoptotic signaling pathway in absence of ligand / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / cellular response to unfolded protein / Pyroptosis / release of cytochrome c from mitochondria / intrinsic apoptotic signaling pathway / heat shock protein binding / apoptotic signaling pathway / regulation of mitochondrial membrane potential / bioluminescence / response to hydrogen peroxide / intrinsic apoptotic signaling pathway in response to DNA damage / generation of precursor metabolites and energy / cellular response to mechanical stimulus / positive regulation of protein-containing complex assembly / cellular response to UV / protein-folding chaperone binding / channel activity / response to ethanol / transmembrane transporter binding / mitochondrial outer membrane / response to xenobiotic stimulus / positive regulation of apoptotic process / negative regulation of cell population proliferation / protein heterodimerization activity / negative regulation of gene expression / apoptotic process / protein-containing complex binding / endoplasmic reticulum / protein homodimerization activity / mitochondrion / metal ion binding / identical protein binding / cytosol
Similarity search - Function
Blc2-like / Apoptosis Regulator Bcl-x / Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / Bcl-2 family / BCL (B-Cell lymphoma); contains BH1, BH2 regions ...Blc2-like / Apoptosis Regulator Bcl-x / Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / Bcl-2 family / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl2-like / Bcl-2, Bcl-2 homology region 1-3 / Apoptosis regulator proteins, Bcl-2 family / BCL2-like apoptosis inhibitors family profile. / Bcl-2-like superfamily / Green Fluorescent Protein / Green fluorescent protein / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
CACODYLATE ION / Green fluorescent protein / Bcl-2 homologous antagonist/killer
Similarity search - Component
Biological speciesAequorea victoria (jellyfish)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsBrouwer, J.M. / Colman, P.M. / Czabotar, P.E.
Funding support Australia, 3items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)1059331 Australia
National Health and Medical Research Council (NHMRC, Australia)1023055 Australia
National Health and Medical Research Council (NHMRC, Australia)1016701 Australia
CitationJournal: Mol.Cell / Year: 2014
Title: Bak Core and Latch Domains Separate during Activation, and Freed Core Domains Form Symmetric Homodimers.
Authors: Brouwer, J.M. / Westphal, D. / Dewson, G. / Robin, A.Y. / Uren, R.T. / Bartolo, R. / Thompson, G.V. / Colman, P.M. / Kluck, R.M. / Czabotar, P.E.
History
DepositionJul 18, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 10, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2014Group: Database references
Revision 1.2Sep 27, 2017Group: Author supporting evidence / Data collection ...Author supporting evidence / Data collection / Database references / Derived calculations / Other / Source and taxonomy
Category: citation / diffrn_source ...citation / diffrn_source / entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site ..._citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site / _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
Revision 1.3Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 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 / refine_hist
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein
Revision 1.5Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.6Oct 16, 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
B: Green fluorescent protein,Bcl-2 homologous antagonist/killer
D: Green fluorescent protein,Bcl-2 homologous antagonist/killer
C: Green fluorescent protein,Bcl-2 homologous antagonist/killer
A: Green fluorescent protein,Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)142,74112
Polymers141,6834
Non-polymers1,0588
Water3,639202
1
B: Green fluorescent protein,Bcl-2 homologous antagonist/killer
C: Green fluorescent protein,Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,0974
Polymers70,8422
Non-polymers2552
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5020 Å2
ΔGint-31 kcal/mol
Surface area28460 Å2
MethodPISA
2
D: Green fluorescent protein,Bcl-2 homologous antagonist/killer
A: Green fluorescent protein,Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,6458
Polymers70,8422
Non-polymers8036
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5680 Å2
ΔGint-43 kcal/mol
Surface area28470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.190, 63.840, 122.020
Angle α, β, γ (deg.)90.000, 98.350, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Green fluorescent protein,Bcl-2 homologous antagonist/killer / Apoptosis regulator BAK / Bcl-2-like protein 7 / Bcl2-L-7


Mass: 35420.773 Da / Num. of mol.: 4
Fragment: UNP P42212 residues 1-230, UNP Q16611 residues 68-148
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aequorea victoria (jellyfish), (gene. exp.) Homo sapiens (human)
Gene: GFP, BAK1, BAK, BCL2L7, CDN1 / Production host: Escherichia coli (E. coli) / References: UniProt: P42212, UniProt: Q16611
#2: Chemical
ChemComp-CAC / CACODYLATE ION / dimethylarsinate


Mass: 136.989 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H6AsO2
#3: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 202 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsResidue SER 65 of GFP underwent mutation into GLY 65. GLY 65, TYR 66, and GLY 67 circularized into ...Residue SER 65 of GFP underwent mutation into GLY 65. GLY 65, TYR 66, and GLY 67 circularized into one chromophore.

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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: 3.02 Å3/Da / Density % sol: 59.23 %
Crystal growTemperature: 281 K / Method: vapor diffusion, hanging drop
Details: 4.5% PEG 8000, 40% MPD, 100 mM tri-sodium citrate, 90 mM cacodylate acid pH 6.5 and 1% Octyl glucoside
PH range: 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.953726 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 9, 2013
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.953726 Å / Relative weight: 1
ReflectionResolution: 2.29→20 Å / Num. obs: 74519 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 40.25 Å2 / Rmerge F obs: 0.996 / Rmerge(I) obs: 0.161 / Rrim(I) all: 0.185 / Χ2: 1.053 / Net I/σ(I): 7.93 / Num. measured all: 307853
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.29-2.433.60.1732.6220.554499612135110633.01791.2
2.43-2.590.4531.740.854797411404113911.99499.9
2.59-2.80.6580.9921.564473910652106481.137100
2.8-3.070.8370.5632.9141200979497850.64599.9
3.07-3.430.9730.2336.9237199888188710.26699.9
3.43-3.950.9920.11213.132648788078730.12999.9
3.95-4.830.9970.05922.0926869667666710.06899.9
4.83-6.80.9970.05323.3620515522752160.06199.8
6.80.9990.0332.0811713303130010.03599

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACT3.14data extraction
PHASERphasing
PHENIX(phenix.refine: 1.8.4_1496)refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4BDU

4bdu


Resolution: 2.3→19.997 Å / FOM work R set: 0.7611 / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 30.51 / Stereochemistry target values: ML
Details: Despite the resolution of the GFP-Bak(alpha2-alpha5) tetramer crystal structure, one of the four GFP molecules has poor electron density; this is most likely due to an absence of crystal ...Details: Despite the resolution of the GFP-Bak(alpha2-alpha5) tetramer crystal structure, one of the four GFP molecules has poor electron density; this is most likely due to an absence of crystal contacts with this moiety.
RfactorNum. reflection% reflection
Rfree0.2502 3705 5 %
Rwork0.1983 70427 -
obs0.2009 74132 99.87 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 297.21 Å2 / Biso mean: 60.89 Å2 / Biso min: 21.18 Å2
Refinement stepCycle: final / Resolution: 2.3→19.997 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9824 0 74 202 10100
Biso mean--96.42 48.87 -
Num. residues----1227
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00910090
X-RAY DIFFRACTIONf_angle_d1.34513642
X-RAY DIFFRACTIONf_chiral_restr0.0531455
X-RAY DIFFRACTIONf_plane_restr0.0061771
X-RAY DIFFRACTIONf_dihedral_angle_d12.7713664
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 26

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3-2.33020.40961390.39022650278999
2.3302-2.36210.40621430.36527052848100
2.3621-2.39580.39481410.347326612802100
2.3958-2.43150.36681390.349526942833100
2.4315-2.46940.39971410.326126962837100
2.4694-2.50980.37051440.323926732817100
2.5098-2.5530.39061410.314627242865100
2.553-2.59930.32571420.299826902832100
2.5993-2.64920.36361410.294227032844100
2.6492-2.70320.32641420.272326742816100
2.7032-2.76180.33791400.260826962836100
2.7618-2.82590.31191440.255727012845100
2.8259-2.89640.32511440.251527082852100
2.8964-2.97440.33261380.245526772815100
2.9744-3.06160.3241490.239727272876100
3.0616-3.16010.32181400.214227002840100
3.1601-3.27260.25821410.197426772818100
3.2726-3.4030.26081410.187827372878100
3.403-3.5570.25811410.180527222863100
3.557-3.74340.23681440.16927162860100
3.7434-3.97630.17811450.162527152860100
3.9763-4.28050.18451420.139827262868100
4.2805-4.70620.17711440.129527182862100
4.7062-5.37560.17941430.134427482891100
5.3756-6.72950.2221460.166927522898100
6.7295-19.99740.16881500.136928372987100
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)
15.75482.031.8645.53083.57825.18990.27670.1150.33590.32510.00130.5826-0.2203-0.4135-0.21430.2923-0.03240.030.33230.01880.27817.669363.378658.8049
23.76780.7639-0.89115.47-1.57184.68030.0491-0.0334-0.0561-0.1156-0.0562-0.04270.3732-0.3403-0.00010.328-0.0596-0.03320.3093-0.00530.180211.157356.551755.7388
35.32621.67481.48776.51322.16884.76360.0935-0.00680.0190.052-0.00610.48560.2345-1.50740.02090.3519-0.052-0.02310.57790.08210.31861.355558.373654.3999
43.4841-1.9110.02514.5073-0.28490.8123-0.106-0.0076-1.1147-0.33350.08710.11751.3979-0.72090.01151.3497-0.2785-0.05970.50580.05440.44677.5239.077649.9936
53.5853-2.1666-0.62016.079-0.77117.23720.85530.7504-0.2212-1.1965-0.71751.14990.0395-0.863-0.13810.3481-0.0281-0.10580.5570.03330.43624.005258.754842.0851
63.41090.54560.65152.7682-0.96623.4994-0.1368-0.0625-0.10030.12950.21030.04210.5186-0.2564-0.06230.39320.06450.00480.258-0.01180.205210.467154.901750.6264
72.44050.8382-2.75192.05-0.12326.97170.3252-0.11510.0449-0.2068-0.0147-0.0843-1.18160.6224-0.25260.5551-0.0203-0.02440.19250.06430.384728.253771.954611.162
83.6659-4.245.10575.3928-5.03448.78470.42130.6279-1.0293-0.99670.11510.91851.2788-0.0806-0.54170.7215-0.128-0.05010.4323-0.0420.433924.354256.84281.1292
96.70181.56330.12122.59452.94846.21390.06510.58760.6864-0.2997-0.0920.0191-0.7121-0.31510.06480.4412-0.0130.03050.270.07390.308924.198668.84163.7461
104.1121-3.5854-0.51075.31421.32232.00780.0519-0.4154-0.5032-0.36170.20980.77520.6643-0.4233-0.31710.5377-0.2432-0.07550.47440.05180.360424.995238.8853-38.4212
115.7953-4.26233.69974.7859-1.1183.99240.31160.14540.1256-0.4642-0.1982-0.03790.3961-0.04030.1020.3687-0.13420.03410.31320.04460.281929.877947.0163-38.5269
121.939-0.66620.62561.7086-0.96133.39270.045-0.3041-0.2704-0.21970.25990.48090.6027-0.667-0.30560.3201-0.0717-0.04650.47380.01790.295925.000244.5649-31.3675
133.6322-2.6591-1.28465.95130.52462.30180.18920.229-0.3794-0.2967-0.08370.76180.209-0.8903-0.09550.3741-0.1647-0.10670.650.10190.414717.358343.8918-36.4305
147.9199-1.52480.76742.0223-1.76517.0759-0.2348-0.10891.01960.16320.3609-0.1842-0.858-0.4998-0.03220.5349-0.0628-0.00660.3466-0.01030.394121.756763.0811-29.8798
153.33022.6525-0.04943.07160.89164.81070.5003-0.83030.17720.4621-0.58451.56150.5289-1.13710.15410.359-0.0784-0.03830.77120.09280.633215.484743.2921-24.0357
162.87970.3482-0.10742.8752-0.01532.04770.0348-0.0573-0.0898-0.17290.07740.27790.2616-0.534-0.05810.3651-0.1405-0.07230.46320.0250.281824.613347.1814-29.6563
172.0156-0.55420.06252.48340.10338.4452-0.2794-0.24350.03380.22250.36240.14611.14920.1433-0.00710.57550.00690.05530.21520.12840.441927.868330.116913.4429
187.11851.6579-1.83446.57290.17118.42970.0717-0.4644-0.07090.71790.00680.8938-0.3331-0.7117-0.12570.47030.16880.07570.38430.11760.389521.133838.555320.3435
192.2719-1.630.11284.5832-4.46218.84740.1276-0.1610.3848-0.1424-0.4327-1.864-0.35720.65180.28530.2664-0.1845-0.11370.51980.05360.789953.740152.8487-23.7165
202.5972-1.3608-0.17295.4838-0.34863.1578-0.11440.03190.0655-0.18370.0195-0.879-0.00330.55230.09650.2408-0.07290.01880.48070.00150.429548.380346.9053-22.2796
212.05170.2271-0.34596.4522-3.97034.1449-0.0065-0.3748-0.1130.4709-0.6023-1.2437-0.13150.93390.6240.3734-0.0591-0.13770.61110.05570.617555.404749.2224-15.425
227.15952.09752.74048.69142.06853.60920.1088-0.6308-1.21480.63720.1233-0.53691.01690.5263-0.35670.46850.05040.01170.48310.06610.411445.36831.2692-12.3039
234.15361.989-1.46637.2864-0.50012.75560.5891-0.73250.01661.5762-0.5755-0.755-0.09650.24880.00690.5072-0.0513-0.17460.48560.0830.315944.358848.5833-8.4141
243.1673-0.3898-0.39494.4190.44452.7076-0.0275-0.12270.0243-0.1098-0.1706-0.2978-0.14050.45480.14860.3174-0.0863-0.0160.35590.05530.259544.553749.7929-17.2174
256.1086-4.9203-6.03165.30995.62846.3717-0.0839-0.50730.04990.05040.0671-0.1492-0.03040.7816-0.05460.3635-0.0863-0.02390.2919-0.01290.344531.803962.231415.9047
268.60510.6783-3.60247.5969-3.18696.28380.4358-0.5712-0.26430.7838-0.040.4636-0.5977-0.2415-0.37080.5498-0.0874-0.01410.35250.06750.293717.382672.976622.8692
276.4831-0.5588-0.91017.3735-1.90724.3571-0.1122-0.5264-1.08360.51630.0570.34730.9495-0.69640.07540.6199-0.15760.01840.38410.09110.398421.020664.276518.0239
280.17620.0122-0.1110.04050.09920.9747-0.1778-0.0839-0.32670.21660.2199-0.44670.59512.1256-0.11090.62970.5015-0.37522.32960.0198-0.604439.469653.349251.1836
292.236-0.6944-0.17521.98680.77474.11970.09940.02270.2415-0.2109-0.0303-0.35410.13441.8364-0.04520.494-0.00760.01431.5885-0.02430.338337.032158.9439.5074
301.85650.34020.08670.96260.6421.69630.0729-0.1626-0.12560.03150.0776-0.1960.51371.8762-0.10880.64160.27740.00591.14470.03070.318533.105153.62645.3695
313.7136-0.0635-0.46686.72684.83653.6255-0.2383-0.0732-0.1196-0.05860.4812-0.0345-0.34190.9733-0.25320.27310.0239-0.02170.28280.08590.343232.654539.675810.2147
326.54640.71762.05435.5634-0.86486.8959-0.33250.68180.3765-0.44760.15260.2827-0.1972-0.39080.14050.4363-0.09590.02990.37590.08620.328622.299333.23231.5238
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'B' and (resid 1 through 24 )B0
2X-RAY DIFFRACTION2chain 'B' and (resid 25 through 81 )B0
3X-RAY DIFFRACTION3chain 'B' and (resid 82 through 128 )B0
4X-RAY DIFFRACTION4chain 'B' and (resid 129 through 147 )B0
5X-RAY DIFFRACTION5chain 'B' and (resid 148 through 170 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 171 through 227 )B0
7X-RAY DIFFRACTION7chain 'B' and (resid 228 through 1106 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 1107 through 1124 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 1125 through 1145 )B0
10X-RAY DIFFRACTION10chain 'D' and (resid 1 through 24 )D0
11X-RAY DIFFRACTION11chain 'D' and (resid 25 through 48 )D0
12X-RAY DIFFRACTION12chain 'D' and (resid 49 through 81 )D0
13X-RAY DIFFRACTION13chain 'D' and (resid 82 through 128 )D0
14X-RAY DIFFRACTION14chain 'D' and (resid 129 through 147 )D0
15X-RAY DIFFRACTION15chain 'D' and (resid 148 through 170 )D0
16X-RAY DIFFRACTION16chain 'D' and (resid 171 through 227 )D0
17X-RAY DIFFRACTION17chain 'D' and (resid 228 through 1106 )D0
18X-RAY DIFFRACTION18chain 'D' and (resid 1107 through 1145 )D0
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 24 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 25 through 81 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 82 through 128 )C0
22X-RAY DIFFRACTION22chain 'C' and (resid 129 through 147 )C0
23X-RAY DIFFRACTION23chain 'C' and (resid 148 through 175 )C0
24X-RAY DIFFRACTION24chain 'C' and (resid 176 through 1072 )C0
25X-RAY DIFFRACTION25chain 'C' and (resid 1073 through 1100 )C0
26X-RAY DIFFRACTION26chain 'C' and (resid 1101 through 1124 )C0
27X-RAY DIFFRACTION27chain 'C' and (resid 1125 through 1145 )C0
28X-RAY DIFFRACTION28chain 'A' and (resid 2 through 128 )A0
29X-RAY DIFFRACTION29chain 'A' and (resid 129 through 170 )A0
30X-RAY DIFFRACTION30chain 'A' and (resid 171 through 1072 )A0
31X-RAY DIFFRACTION31chain 'A' and (resid 1073 through 1100 )A0
32X-RAY DIFFRACTION32chain 'A' and (resid 1101 through 1145 )A0

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