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- PDB-6uxn: Crystal structure of BAK core domain BH3-groove-dimer in complex ... -

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Basic information

Entry
Database: PDB / ID: 6uxn
TitleCrystal structure of BAK core domain BH3-groove-dimer in complex with phosphatidylserine
ComponentsBcl-2 homologous antagonist/killer
KeywordsAPOPTOSIS / Pore-forming Protein
Function / homology
Function and homology information


Activation and oligomerization of BAK protein / BH domain binding / B cell negative selection / BAK complex / negative regulation of endoplasmic reticulum calcium ion concentration / response to fungus / response to mycotoxin / limb morphogenesis / Release of apoptotic factors from the mitochondria / apoptotic process involved in blood vessel morphogenesis ...Activation and oligomerization of BAK protein / BH domain binding / B cell negative selection / BAK complex / negative regulation of endoplasmic reticulum calcium ion concentration / response to fungus / response to mycotoxin / limb morphogenesis / Release of apoptotic factors from the mitochondria / apoptotic process involved in blood vessel morphogenesis / post-embryonic camera-type eye morphogenesis / endocrine pancreas development / establishment or maintenance of transmembrane electrochemical gradient / B cell apoptotic process / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / endoplasmic reticulum calcium ion homeostasis / regulation of mitochondrial membrane permeability / calcium ion transport into cytosol / fibroblast apoptotic process / response to UV-C / mitochondrial fusion / Bcl-2 family protein complex / myeloid cell homeostasis / porin activity / thymocyte apoptotic process / negative regulation of release of cytochrome c from mitochondria / pore complex / positive regulation of IRE1-mediated unfolded protein response / positive regulation of release of cytochrome c from mitochondria / vagina development / B cell homeostasis / positive regulation of calcium ion transport into cytosol / positive regulation of proteolysis / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / blood vessel remodeling / animal organ regeneration / cellular response to unfolded protein / Pyroptosis / heat shock protein binding / extrinsic apoptotic signaling pathway in absence of ligand / intrinsic apoptotic signaling pathway / release of cytochrome c from mitochondria / epithelial cell proliferation / response to gamma radiation / regulation of mitochondrial membrane potential / apoptotic signaling pathway / positive regulation of protein-containing complex assembly / establishment of localization in cell / response to hydrogen peroxide / cellular response to mechanical stimulus / intrinsic apoptotic signaling pathway in response to DNA damage / cellular response to UV / protein-folding chaperone binding / channel activity / response to ethanol / transmembrane transporter binding / mitochondrial outer membrane / regulation of cell cycle / positive regulation of apoptotic process / response to xenobiotic stimulus / protein heterodimerization activity / negative regulation of cell population proliferation / 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-8SP / Bcl-2 homologous antagonist/killer
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.49 Å
AuthorsCowan, A.D. / Colman, P.M. / Czabotar, P.E.
Funding support Australia, 3items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)1079706 Australia
National Health and Medical Research Council (NHMRC, Australia)1059290 Australia
National Health and Medical Research Council (NHMRC, Australia)1113133 Australia
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2020
Title: BAK core dimers bind lipids and can be bridged by them.
Authors: Cowan, A.D. / Smith, N.A. / Sandow, J.J. / Kapp, E.A. / Rustam, Y.H. / Murphy, J.M. / Brouwer, J.M. / Bernardini, J.P. / Roy, M.J. / Wardak, A.Z. / Tan, I.K. / Webb, A.I. / Gulbis, J.M. / ...Authors: Cowan, A.D. / Smith, N.A. / Sandow, J.J. / Kapp, E.A. / Rustam, Y.H. / Murphy, J.M. / Brouwer, J.M. / Bernardini, J.P. / Roy, M.J. / Wardak, A.Z. / Tan, I.K. / Webb, A.I. / Gulbis, J.M. / Smith, B.J. / Reid, G.E. / Dewson, G. / Colman, P.M. / Czabotar, P.E.
History
DepositionNov 7, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 2, 2020Provider: repository / Type: Initial release
Revision 1.1Sep 30, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 18, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 11, 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: Bcl-2 homologous antagonist/killer
B: Bcl-2 homologous antagonist/killer
C: Bcl-2 homologous antagonist/killer
D: Bcl-2 homologous antagonist/killer
E: Bcl-2 homologous antagonist/killer
F: Bcl-2 homologous antagonist/killer
G: Bcl-2 homologous antagonist/killer
H: Bcl-2 homologous antagonist/killer
I: Bcl-2 homologous antagonist/killer
J: Bcl-2 homologous antagonist/killer
K: Bcl-2 homologous antagonist/killer
L: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,13350
Polymers114,00812
Non-polymers11,12538
Water1,31573
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A: Bcl-2 homologous antagonist/killer
B: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,3369
Polymers19,0012
Non-polymers2,3347
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4360 Å2
ΔGint-54 kcal/mol
Surface area9630 Å2
MethodPISA
2
C: Bcl-2 homologous antagonist/killer
D: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,3097
Polymers19,0012
Non-polymers1,3075
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4560 Å2
ΔGint-58 kcal/mol
Surface area9040 Å2
MethodPISA
3
E: Bcl-2 homologous antagonist/killer
F: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9209
Polymers19,0012
Non-polymers1,9197
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4840 Å2
ΔGint-84 kcal/mol
Surface area9130 Å2
MethodPISA
4
G: Bcl-2 homologous antagonist/killer
H: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,9209
Polymers19,0012
Non-polymers1,9197
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4650 Å2
ΔGint-67 kcal/mol
Surface area9030 Å2
MethodPISA
5
I: Bcl-2 homologous antagonist/killer
J: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,6326
Polymers19,0012
Non-polymers1,6314
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4210 Å2
ΔGint-45 kcal/mol
Surface area9140 Å2
MethodPISA
6
K: Bcl-2 homologous antagonist/killer
L: Bcl-2 homologous antagonist/killer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,01610
Polymers19,0012
Non-polymers2,0158
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5080 Å2
ΔGint-93 kcal/mol
Surface area8950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)157.762, 91.089, 96.395
Angle α, β, γ (deg.)90.000, 107.070, 90.000
Int Tables number5
Space group name H-MC121

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Components

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


Mass: 9500.688 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BAK1, BAK, BCL2L7, CDN1 / Plasmid: pGEX-6P-3 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q16611
#2: Chemical
ChemComp-8SP / O-[(R)-{[(2R)-2,3-bis(octanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine


Type: L-peptide linking / Mass: 511.543 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: C22H42NO10P / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 73 / Source method: isolated from a natural source / Formula: H2O
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: 2.9 Å3/Da / Density % sol: 57.64 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: ammonium sulphate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9536 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 6, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9536 Å / Relative weight: 1
ReflectionResolution: 2.49→45.741 Å / Num. obs: 45501 / % possible obs: 99.1 % / Redundancy: 7 % / Biso Wilson estimate: 61.93 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.164 / Rrim(I) all: 0.177 / Χ2: 1.064 / Net I/σ(I): 9.31 / Num. measured all: 318495
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.49-2.646.9111.8051.1448539734270230.5121.94995.7
2.64-2.827.2361.2731.7550191694969360.6671.37299.8
2.82-3.057.0690.8992.5445504644564370.8360.97199.9
3.05-3.346.8060.4585.1440429594859400.9580.49699.9
3.34-3.736.660.2289.3635791538353740.9890.24799.8
3.73-4.37.3710.10218.2135232478547800.9980.1199.9
4.3-5.257.2210.0822.2229174404540400.9980.08699.9
5.25-7.386.6780.0820.0321016316031470.9980.08799.6
7.38-45.7416.9180.03536.3812619184318240.9990.03899

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation2.79 Å45.74 Å
Translation2.79 Å45.74 Å

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Processing

Software
NameVersionClassification
PHENIX1.14refinement
XDSdata reduction
XDSdata scaling
PHASER2.8.1phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6UXO

6uxo


Resolution: 2.49→45.741 Å / SU ML: 0.39 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 30.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2529 1987 4.39 %
Rwork0.2046 43224 -
obs0.2068 45211 98.6 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 186.82 Å2 / Biso mean: 66.0962 Å2 / Biso min: 30.31 Å2
Refinement stepCycle: final / Resolution: 2.49→45.741 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7626 0 585 73 8284
Biso mean--98.63 63.42 -
Num. residues----953
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.49-2.55210.37011190.3032259683
2.5521-2.62110.30231430.28963110100
2.6211-2.69830.33631440.2733121100
2.6983-2.78530.33161420.26963093100
2.7853-2.88490.30521430.26543112100
2.8849-3.00040.31471440.27263116100
3.0004-3.13690.36181420.2433135100
3.1369-3.30220.2631430.20123097100
3.3022-3.5090.25871450.20383144100
3.509-3.77990.23771430.19253117100
3.7799-4.160.18991430.16283138100
4.16-4.76140.2171450.16423123100
4.7614-5.99680.24791450.20013154100
5.9968-45.7410.22851460.1881316898
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)
14.3082-2.09412.32424.2335-2.41985.42980.6090.0823-0.898-0.02450.12030.11480.48410.1822-0.81180.4152-0.05820.1240.39-0.06630.4422-46.1121-17.951741.6284
23.8912-0.2413-1.51581.3271.39112.99740.088-0.40650.15980.28760.0927-0.49040.39910.9898-0.25090.49090.0252-0.00920.4433-0.03790.6195-37.3682-6.050250.1533
33.38780.41115.33213.9611.88748.8992-0.06790.8319-0.005-0.26930.1521-0.28320.16850.7518-0.0680.4272-0.06410.15950.4811-0.0590.4419-39.433-12.811634.9374
45.0135-1.19852.97027.3945-5.61827.8956-0.06110.49350.0194-0.7236-0.10920.0419-0.2431-0.07470.09210.50440.08530.02320.3749-0.12360.3667-55.6755-8.039633.6641
59.66766.1155-4.809710.1748-4.22134.50740.28630.43650.8620.13350.54491.3135-0.4125-0.4673-0.79670.36650.0519-0.02510.3514-0.0440.4149-29.8016-26.455241.4247
69.55760.1087-0.61138.1441-1.91042.19950.494-0.6139-0.96970.8377-0.126-0.36031.07460.3042-0.38730.5426-0.0488-0.11280.47490.00410.7646-23.2734-45.328349.1382
72.59312.61314.89364.94392.29747.28570.3271-0.25080.2920.4467-0.22830.2595-0.0948-1.36920.25760.3548-0.0060.00080.48170.01130.4745-24.6896-34.554350.9593
85.53783.1972-2.6898.0813-6.32216.49690.05550.28010.1096-0.59520.22360.50210.48080.0697-0.33750.3772-0.0156-0.09270.3995-0.12210.3989-28.3922-34.708734.6465
99.8763-7.78132.01562.0251-5.10182.0066-0.4022.71040.29971.07120.167-0.1432-2.05732.85290.270.5728-0.0788-0.00521.20980.24350.6302-9.5789-21.270224.2938
108.434-2.289-5.31768.12090.67516.13990.29240.4652-0.1334-0.4942-0.4836-0.0671-0.09740.36550.14210.27450.0502-0.08770.57150.06610.3572-17.3727-23.872334.9802
114.3728-1.6362-1.45318.91663.14873.21640.1423-0.06370.38270.45770.1263-0.2109-0.1852-0.0842-0.3140.3836-0.0344-0.02760.35180.05560.2441-48.0315-35.018544.7664
121.7715-0.691-0.195.8026-1.16687.4935-0.1423-0.01730.440.45530.1370.5732-0.1686-0.1560.03380.3741-0.0570.06090.3020.00350.558-59.3569-35.098149.0949
139.9503-6.1357-6.6779.86036.03794.4070.16340.05860.3493-0.69640.01040.0342-0.5470.0496-0.00490.33760.0072-0.06960.34610.05460.3258-53.2847-33.304534.9382
147.54075.3554.6499.64813.45272.57140.25460.0702-0.4770.2358-0.01880.05290.8974-0.1053-0.11850.5513-0.08960.1310.39520.00950.4842-45.8824-52.615334.3473
153.24735.65957.11774.45866.63563.2806-0.56290.60290.2099-0.81890.36170.5754-1.20050.30690.1970.4885-0.0726-0.06740.59660.0480.5369-54.0823-46.001532.1592
166.1455-3.5637-3.90729.82435.97228.74590.30750.20790.2949-0.6370.1709-0.8223-0.51870.2125-0.6530.3472-0.0667-0.00640.34440.09720.3892-63.7279-50.48641.3193
172.4682-1.47973.57842.3534-0.42475.86360.23640.1369-0.3927-0.1589-0.2252-0.01280.37780.23920.00160.3264-0.0235-0.01720.5421-0.07430.6599-69.224-60.7631-2.8598
189.0565-6.5603-5.04689.6286.55233.6182-0.3879-0.6189-0.35570.40470.4826-0.05160.22370.7663-0.14150.4713-0.0486-0.03760.45080.15550.5571-64.472-56.038411.0227
197.03593.9399-6.82528.0583-1.90917.3082-0.0732-0.08230.14430.50890.01840.3004-0.0686-0.4147-0.01760.29950.0464-0.10290.6435-0.03310.4385-76.435-44.649712.2592
207.20572.8153-2.54069.3837-4.29654.17580.01710.28620.56040.25250.53220.7663-0.3102-0.6605-0.5820.35080.005-0.00670.4845-0.05780.4432-47.7703-57.7294.4572
213.5060.15440.14196.00442.75938.2970.16360.43450.0334-0.84250.2341-0.6143-0.71160.7694-0.3330.45530.04540.12390.4353-0.02420.4857-33.0407-56.1015-4.1361
225.44.5468-4.26459.632-6.36148.67980.0881-0.43220.22110.3717-0.1152-0.0605-0.13050.4217-0.05240.30760.0055-0.05280.4898-0.12280.39-40.02-57.999112.7179
233.2816-2.18754.16636.7976-5.196410.2292-0.1701-0.39040.14130.3813-0.12830.13870.31790.09610.27520.37720.07760.11390.40360.00090.3393-43.7441-69.853311.1658
248.27420.00184.27953.71360.41754.18410.3427-0.1219-0.68650.05680.11570.00470.2205-0.0161-0.57790.35140.02830.10570.3482-0.0050.3486-46.968-39.40854.5575
254.28061.0733-3.15862.79-2.4727.79820.15060.68230.2761-0.11870.37270.5487-0.2211-0.8898-0.46930.3668-0.0414-0.04550.43050.06620.6024-55.5636-27.486-4.1997
269.6613.23145.05333.49880.60454.23960.1719-0.8563-0.01550.4757-0.08560.1969-0.3013-0.6226-0.22610.4054-0.00480.14980.4235-0.00940.4073-50.3729-32.515712.8491
277.38080.81941.58428.74223.86174.96530.2008-0.40220.51560.6029-0.2139-0.0627-0.38320.1523-0.03140.4529-0.13550.02750.2980.05210.3335-38.671-29.619311.7834
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 67 through 100 )A67 - 100
2X-RAY DIFFRACTION2chain 'A' and (resid 101 through 148 )A101 - 148
3X-RAY DIFFRACTION3chain 'B' and (resid 69 through 100 )B69 - 100
4X-RAY DIFFRACTION4chain 'B' and (resid 101 through 146 )B101 - 146
5X-RAY DIFFRACTION5chain 'C' and (resid 67 through 100 )C67 - 100
6X-RAY DIFFRACTION6chain 'C' and (resid 101 through 124 )C101 - 124
7X-RAY DIFFRACTION7chain 'C' and (resid 125 through 147 )C125 - 147
8X-RAY DIFFRACTION8chain 'D' and (resid 69 through 100 )D69 - 100
9X-RAY DIFFRACTION9chain 'D' and (resid 101 through 106 )D101 - 106
10X-RAY DIFFRACTION10chain 'D' and (resid 107 through 145 )D107 - 145
11X-RAY DIFFRACTION11chain 'E' and (resid 69 through 106 )E69 - 106
12X-RAY DIFFRACTION12chain 'E' and (resid 107 through 147 )E107 - 147
13X-RAY DIFFRACTION13chain 'F' and (resid 69 through 100 )F69 - 100
14X-RAY DIFFRACTION14chain 'F' and (resid 101 through 124 )F101 - 124
15X-RAY DIFFRACTION15chain 'F' and (resid 125 through 147 )F125 - 147
16X-RAY DIFFRACTION16chain 'G' and (resid 68 through 106 )G68 - 106
17X-RAY DIFFRACTION17chain 'G' and (resid 107 through 147 )G107 - 147
18X-RAY DIFFRACTION18chain 'H' and (resid 69 through 100 )H69 - 100
19X-RAY DIFFRACTION19chain 'H' and (resid 101 through 145 )H101 - 145
20X-RAY DIFFRACTION20chain 'I' and (resid 67 through 100 )I67 - 100
21X-RAY DIFFRACTION21chain 'I' and (resid 101 through 148 )I101 - 148
22X-RAY DIFFRACTION22chain 'J' and (resid 68 through 106 )J68 - 106
23X-RAY DIFFRACTION23chain 'J' and (resid 107 through 146 )J107 - 146
24X-RAY DIFFRACTION24chain 'K' and (resid 67 through 100 )K67 - 100
25X-RAY DIFFRACTION25chain 'K' and (resid 101 through 147 )K101 - 147
26X-RAY DIFFRACTION26chain 'L' and (resid 69 through 106 )L69 - 106
27X-RAY DIFFRACTION27chain 'L' and (resid 107 through 146 )L107 - 146

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