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- PDB-6i7q: Structure of pVHL-elongin B-elongin C (VCB) in complex with hydro... -

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Basic information

Entry
Database: PDB / ID: 6i7q
TitleStructure of pVHL-elongin B-elongin C (VCB) in complex with hydroxylated-HIF-2alpha (523-542) in the C2221 form
Components
  • Elongin-B
  • Elongin-C
  • Endothelial PAS domain-containing protein 1
  • von Hippel-Lindau disease tumor suppressor
KeywordsGENE REGULATION / E3 UBIQUITIN LIGASE / von Hippel Lindau / Prolyl hydroxylation / HIF / TUMOR SUPPRESSOR / CANCER / PROTEOSOMAL DEGRADATION / UBIQUITIN
Function / homology
Function and homology information


RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Elongation / myoblast fate commitment / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / Cellular response to hypoxia / PTK6 Expression ...RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Elongation / myoblast fate commitment / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / Cellular response to hypoxia / PTK6 Expression / Transcriptional regulation of pluripotent stem cells / regulation of protein neddylation / regulation of cellular response to hypoxia / negative regulation of receptor signaling pathway via JAK-STAT / RHOBTB3 ATPase cycle / norepinephrine metabolic process / transcription elongation factor activity / target-directed miRNA degradation / surfactant homeostasis / elongin complex / epithelial cell maturation / Replication of the SARS-CoV-1 genome / Regulation of gene expression by Hypoxia-inducible Factor / VCB complex / Cul5-RING ubiquitin ligase complex / intracellular membraneless organelle / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / SUMOylation of ubiquitinylation proteins / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / blood vessel remodeling / embryonic placenta development / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / ubiquitin-like ligase-substrate adaptor activity / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / visual perception / lung development / negative regulation of autophagy / regulation of heart rate / protein serine/threonine kinase binding / Pexophagy / transcription corepressor binding / erythrocyte differentiation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / TP53 Regulates Transcription of DNA Repair Genes / mitochondrion organization / transcription initiation at RNA polymerase II promoter / positive regulation of cell differentiation / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Inactivation of CSF3 (G-CSF) signaling / mRNA transcription by RNA polymerase II / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / multicellular organismal-level iron ion homeostasis / Evasion by RSV of host interferon responses / transcription coactivator binding / Regulation of expression of SLITs and ROBOs / cell morphogenesis / ubiquitin-protein transferase activity / transcription corepressor activity / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of cold-induced thermogenesis / microtubule cytoskeleton / Neddylation / regulation of gene expression / response to oxidative stress / DNA-binding transcription activator activity, RNA polymerase II-specific / protein-containing complex assembly / angiogenesis / Replication of the SARS-CoV-2 genome / transcription regulator complex / cellular response to hypoxia / protein-macromolecule adaptor activity / amyloid fibril formation / DNA-binding transcription factor binding / ubiquitin-dependent protein catabolic process / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / RNA polymerase II-specific DNA-binding transcription factor binding / DNA-binding transcription factor activity, RNA polymerase II-specific / response to hypoxia / cilium / protein stabilization / nuclear speck / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein heterodimerization activity / negative regulation of cell population proliferation / negative regulation of gene expression
Similarity search - Function
von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / HIF-1 alpha, transactivation domain, C-terminal / HIF-1 alpha C terminal transactivation domain / Hypoxia-inducible factor 1-alpha bHLH domain / Hypoxia-inducible factor, alpha subunit-like / Hypoxia-inducible factor-1 / Nuclear translocator / von Hippel-Lindau disease tumour suppressor, beta/alpha domain ...von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / HIF-1 alpha, transactivation domain, C-terminal / HIF-1 alpha C terminal transactivation domain / Hypoxia-inducible factor 1-alpha bHLH domain / Hypoxia-inducible factor, alpha subunit-like / Hypoxia-inducible factor-1 / Nuclear translocator / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / Elongin-C / Elongin B / PAC motif / Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain) / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / PAS domain / helix loop helix domain / Myc-type, basic helix-loop-helix (bHLH) domain / Myc-type, basic helix-loop-helix (bHLH) domain profile. / Helix-loop-helix DNA-binding domain superfamily / PAS fold / PAS fold / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / PAS domain / PAS repeat profile. / SKP1/BTB/POZ domain superfamily / PAS domain / PAS domain superfamily / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
von Hippel-Lindau disease tumor suppressor / Elongin-B / Elongin-C / Endothelial PAS domain-containing protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Bos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.798 Å
AuthorsChowdhury, R. / Aguilera, L.S. / Schofield, C.J.
Citation
Journal: To Be Published
Title: HIF-2alpha-pVHL-elongin B-elongin C complex
Authors: Chowdhury, R. / Schofield, C.J.
#1: Journal: Nature / Year: 2002
Title: Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.
Authors: Hon, W.C. / Wilson, M.I. / Harlos, K. / Claridge, T.D. / Schofield, C.J. / Pugh, C.W. / Maxwell, P.H. / Ratcliffe, P.J. / Stuart, D.I. / Jones, E.Y.
History
DepositionNov 17, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 27, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 20, 2021Group: Database references / Derived calculations ...Database references / Derived calculations / Refinement description / Source and taxonomy / Structure summary
Category: entity / entity_name_com ...entity / entity_name_com / pdbx_entity_src_syn / pdbx_struct_mod_residue / refine / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _pdbx_entity_src_syn.organism_common_name ..._entity.pdbx_description / _pdbx_entity_src_syn.organism_common_name / _refine.solvent_model_details / _struct_ref.db_code / _struct_ref.db_name / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_db_accession
Revision 1.2Jan 24, 2024Group: 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
B: Elongin-B
C: Elongin-C
H: Endothelial PAS domain-containing protein 1
V: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,0765
Polymers44,9844
Non-polymers921
Water5,765320
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6660 Å2
ΔGint-46 kcal/mol
Surface area18480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.827, 86.758, 136.376
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

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Protein , 3 types, 3 molecules BCV

#1: Protein Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 13179.780 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Plasmid: pGEX-4T-3 / Cell line (production host): BL21(DE3) / Production host: Escherichia coli (E. coli) / References: UniProt: Q15370
#2: Protein Elongin-C / EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / ...EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / Transcription elongation factor B polypeptide 1


Mass: 10930.498 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Gene: ELOC, TCEB1 / Plasmid: Plasmid / Details (production host): pBB75 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q2KII4
#4: Protein von Hippel-Lindau disease tumor suppressor / Protein G7 / pVHL


Mass: 18558.162 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Plasmid: pGEX-4T-3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P40337

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Protein/peptide , 1 types, 1 molecules H

#3: Protein/peptide Endothelial PAS domain-containing protein 1 / EPAS-1 / Basic-helix-loop-helix-PAS protein MOP2 / Class E basic helix-loop-helix protein 73 / ...EPAS-1 / Basic-helix-loop-helix-PAS protein MOP2 / Class E basic helix-loop-helix protein 73 / bHLHe73 / HIF-1-alpha-like factor / HLF / Hypoxia-inducible factor 2-alpha / HIF2-alpha / Member of PAS protein 2 / PAS domain-containing protein 2


Mass: 2315.529 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q99814

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Non-polymers , 2 types, 321 molecules

#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 320 / Source method: isolated from a natural source / Formula: H2O

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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: 2.77 Å3/Da / Density % sol: 55.56 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.8
Details: 0.1M Cacodyl-Na pH 5.8, 0.1M Mg formate, 50 mM Cystamine, 22 % PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97627 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 4, 2017 / Details: MIRRORS
RadiationMonochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97627 Å / Relative weight: 1
ReflectionResolution: 1.798→59.56 Å / Num. obs: 45358 / % possible obs: 100 % / Redundancy: 9.7 % / Biso Wilson estimate: 24.5 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.087 / Rpim(I) all: 0.043 / Rrim(I) all: 0.097 / Net I/σ(I): 11.9
Reflection shellResolution: 1.798→1.85 Å / Redundancy: 9.8 % / Rmerge(I) obs: 1.042 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 3301 / CC1/2: 0.643 / Rpim(I) all: 1.171 / Rrim(I) all: 1.166 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
DIALSdata reduction
DIALSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1LQB

1lqb


Resolution: 1.798→59.527 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2366 2171 4.89 %
Rwork0.1872 --
obs0.1896 44373 97.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Solvent model: BULK SOLVENT MODELLING METHOD USED : FLAT MODEL
Refinement stepCycle: LAST / Resolution: 1.798→59.527 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2938 0 6 320 3264
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0183090
X-RAY DIFFRACTIONf_angle_d1.3994210
X-RAY DIFFRACTIONf_dihedral_angle_d6.8082603
X-RAY DIFFRACTIONf_chiral_restr0.08471
X-RAY DIFFRACTIONf_plane_restr0.011556
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7984-1.83750.45051220.35072496X-RAY DIFFRACTION93
1.8375-1.88020.39421340.32032568X-RAY DIFFRACTION97
1.8802-1.92720.36171310.2882621X-RAY DIFFRACTION97
1.9272-1.97930.30031430.26242579X-RAY DIFFRACTION98
1.9793-2.03760.29411210.24052655X-RAY DIFFRACTION98
2.0376-2.10340.29511400.2232616X-RAY DIFFRACTION98
2.1034-2.17850.2391400.20232628X-RAY DIFFRACTION98
2.1785-2.26580.24921350.20052623X-RAY DIFFRACTION98
2.2658-2.36890.25421330.18672627X-RAY DIFFRACTION97
2.3689-2.49380.26271320.19112619X-RAY DIFFRACTION97
2.4938-2.650.24261310.18692611X-RAY DIFFRACTION97
2.65-2.85460.19721580.18072620X-RAY DIFFRACTION98
2.8546-3.14190.25471260.16982677X-RAY DIFFRACTION98
3.1419-3.59650.21081670.16342643X-RAY DIFFRACTION99
3.5965-4.5310.1781290.14152753X-RAY DIFFRACTION99
4.531-59.55970.22131290.18132866X-RAY DIFFRACTION100
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)
10.1646-0.23310.03460.3883-0.04040.0291-0.10640.0546-0.0709-0.23880.17310.3429-0.12180.0828-0.01270.318-0.1422-0.10490.30870.0930.24737.354413.1889.1572
20.0558-0.129-0.0410.32070.15890.0866-0.0660.1408-0.1333-0.1768-0.09980.3-0.2892-0.1042-0.11660.3424-0.127-0.09290.26510.09670.25485.949315.6568.1249
30.112-0.1029-0.14530.22120.22140.2566-0.10530.13060.05870.0123-0.08490.0794-0.0361-0.0084-0.10760.4328-0.0693-0.21720.30130.13650.41110.067420.93343.603
40.0268-0.0282-0.00170.0344-0.0053-0.0008-0.04770.11040.1783-0.0689-0.08150.001-0.08530.0145-0.07840.6574-0.182-0.4480.40690.39370.08452.952820.8488-3.6424
50.05950.0509-0.05060.3328-0.23620.16930.14480.04960.02740.10440.19120.01840.03580.00970.04270.4173-0.0536-0.0790.4601-0.14260.30732.69298.0514-2.4399
60.00180.00010.01010.00030.0020.00570.05350.20410.0456-0.1113-0.11460.01490.0523-0.1944-00.3415-0.0751-0.09210.29260.03990.33850.70364.67727.8814
70.206-0.1054-0.06440.0740.05950.0368-0.15860.2006-0.1841-0.34420.13780.0835-0.05930.0717-0.06130.3294-0.1472-0.09770.29270.06020.21929.236510.8537.7602
80.0102-0.0006-0.00290.0011-0.00270.0147-0.0219-0.00990.01180.0007-0.00960.0123-0.0086-0.02940.00011.11590.0074-0.12711.24580.12050.83525.487723.6087-12.7896
90.01380.01460.00410.15970.0070.0019-0.02120.0324-0.0099-0.0632-0.07610.06660.0082-0.07520.00190.8542-0.0954-0.0071.13230.04010.210211.356716.9287-8.0619
100.05480.00340.0108-0.0009-0.00090.00150.01580.09260.0344-0.07730.0312-0.0322-0.0033-0.02670.01380.5403-0.20540.03180.4625-0.00480.113721.333114.30252.1866
110.0045-0.00450.00160.0186-0.00620.0049-0.0420.0331-0.0083-0.075-0.01120.002-0.03480.0344-00.5436-0.02440.14510.4516-0.10860.351432.44546.626410.5607
120.00170.00080.0029-0.00010.00170.00240.0160.0324-0.0113-0.0296-0-0.01690.06910.005300.51020.11220.14080.44-0.13170.658936.15890.200818.539
130.5347-0.16780.2580.127-0.18390.3838-0.29570.08230.2484-0.39150.28920.0067-0.1818-0.1147-0.08030.285-0.1158-0.02380.22590.05870.247615.05924.811815.65
140.00080.003-0.00590.00490.00260.0030.0123-0.08710.03780.01820.0216-0.0217-0.0294-0.0059-00.2487-0.0438-0.11780.35460.04240.519712.747137.62120.2629
150.1090.04080.13940.33520.05520.1791-0.15690.1054-0.0473-0.15920.26440.02140.00860.00780.21460.1698-0.0704-0.00010.1850.01710.196219.228114.538619.691
160.0189-0.0190.01540.0174-0.01530.01180.0218-0.1246-0.03880.1101-0.0093-0.0432-0.01740.03490.00730.35770.1293-0.05450.34980.07980.18213.2806-8.670461.9098
17-0.00010.00250.00180.00870.00280.0027-0.1664-0.0227-0.06860.0363-0.0059-0.03650.0681-0.00400.20120.03980.05340.20140.01130.27238.3643-16.725848.3821
180.0043-0.0068-0.00010.0031-0.0010.0071-0.10720.065-0.01840.02480.00220.0802-0.0152-0.095500.5514-0.11210.02310.375-0.06440.27034.5636-13.145235.1589
190.0109-0.0172-0.01140.01620.01650.0082-0.0071-0.1612-0.03440.04840.02840.0171-0.07-0.0927-00.31680.0809-0.00680.2631-0.0060.152113.38291.830358.8017
200.04610.0519-0.01630.0773-0.03680.0175-0.16050.02760.060.03730.14380.0294-0.06540.07950.00130.18110.02680.00260.23180.04890.18565.2503-6.291744.2268
210.44780.2434-0.14910.3444-0.18720.0764-0.1712-0.08160.04040.03720.0774-0.0434-0.0828-0.0016-0.05250.19110.0328-0.02440.17550.01820.163113.5589-4.228844.6926
220.06180.06440.12530.08840.11140.1823-0.13770.02640.12210.07750.0683-0.0547-0.19840.04380.0010.2470.0561-0.02510.1990.03770.252811.34012.604142.1134
230.01550.07280.04890.2050.16120.146-0.03290.0027-0.0038-0.00110.08710.0056-0.08-0.1065-0.00080.15720.0165-0.01650.24160.05140.213114.0543.700833.6225
240.0015-0.00310.00080.02420.00070.02240.06910.1004-0.07150.02670.0948-0.17140.05340.09330.00880.17530.0159-0.02430.3725-0.02760.52938.77513.815627.8986
250.0192-0.02740.00490.04380.0210.038-0.0003-0.10930.13070.11010.058-0.3075-0.16190.11690.00010.1923-0.0137-0.030.30110.00640.384533.893511.730130.6485
26-0.0027-0.003-0.00560.022-0.00230.0040.1003-0.09940.08110.0226-0.03960.0341-0.07210.0628-0.00010.514-0.11260.02710.2906-0.06010.389318.654513.458348.2393
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 1 through 9 )
2X-RAY DIFFRACTION2chain 'B' and (resid 10 through 23 )
3X-RAY DIFFRACTION3chain 'B' and (resid 24 through 35 )
4X-RAY DIFFRACTION4chain 'B' and (resid 36 through 45 )
5X-RAY DIFFRACTION5chain 'B' and (resid 46 through 55 )
6X-RAY DIFFRACTION6chain 'B' and (resid 56 through 65 )
7X-RAY DIFFRACTION7chain 'B' and (resid 66 through 79 )
8X-RAY DIFFRACTION8chain 'B' and (resid 80 through 84 )
9X-RAY DIFFRACTION9chain 'B' and (resid 85 through 89 )
10X-RAY DIFFRACTION10chain 'B' and (resid 90 through 94 )
11X-RAY DIFFRACTION11chain 'B' and (resid 95 through 99 )
12X-RAY DIFFRACTION12chain 'B' and (resid 100 through 105 )
13X-RAY DIFFRACTION13chain 'C' and (resid 16 through 45 )
14X-RAY DIFFRACTION14chain 'C' and (resid 46 through 58 )
15X-RAY DIFFRACTION15chain 'C' and (resid 59 through 112 )
16X-RAY DIFFRACTION16chain 'H' and (resid 526 through 530 )
17X-RAY DIFFRACTION17chain 'H' and (resid 532 through 536 )
18X-RAY DIFFRACTION18chain 'H' and (resid 537 through 542 )
19X-RAY DIFFRACTION19chain 'V' and (resid 60 through 70 )
20X-RAY DIFFRACTION20chain 'V' and (resid 71 through 78 )
21X-RAY DIFFRACTION21chain 'V' and (resid 79 through 121 )
22X-RAY DIFFRACTION22chain 'V' and (resid 122 through 141 )
23X-RAY DIFFRACTION23chain 'V' and (resid 142 through 169 )
24X-RAY DIFFRACTION24chain 'V' and (resid 170 through 177 )
25X-RAY DIFFRACTION25chain 'V' and (resid 178 through 193 )
26X-RAY DIFFRACTION26chain 'V' and (resid 194 through 210 )

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