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- PDB-6bj8: TCR55 in complex with Pep20/HLA-B35 -

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Basic information

Entry
Database: PDB / ID: 6bj8
TitleTCR55 in complex with Pep20/HLA-B35
Components
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, B-35 alpha chain
  • TCR 55 alpha chain
  • TCR 55 beta chain
  • VAL-PRO-LEU-THR-GLU-ASP-ALA-GLU-LEU
KeywordsIMMUNE SYSTEM / agonist / complex
Function / homology
Function and homology information


regulation of interleukin-12 production / regulation of dendritic cell differentiation / regulation of T cell anergy / regulation of interleukin-6 production / TAP binding / protection from natural killer cell mediated cytotoxicity / detection of bacterium / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / secretory granule membrane ...regulation of interleukin-12 production / regulation of dendritic cell differentiation / regulation of T cell anergy / regulation of interleukin-6 production / TAP binding / protection from natural killer cell mediated cytotoxicity / detection of bacterium / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / secretory granule membrane / positive regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / negative regulation of receptor binding / DAP12 interactions / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / cellular response to iron ion / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / lumenal side of endoplasmic reticulum membrane / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / negative regulation of forebrain neuron differentiation / regulation of erythrocyte differentiation / peptide antigen assembly with MHC class I protein complex / ER to Golgi transport vesicle membrane / regulation of iron ion transport / response to molecule of bacterial origin / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / MHC class I protein complex / defense response / negative regulation of neurogenesis / positive regulation of receptor-mediated endocytosis / peptide antigen assembly with MHC class II protein complex / multicellular organismal-level iron ion homeostasis / MHC class II protein complex / cellular response to nicotine / specific granule lumen / positive regulation of cellular senescence / positive regulation of T cell mediated cytotoxicity / recycling endosome membrane / phagocytic vesicle membrane / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / negative regulation of epithelial cell proliferation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of immune response / Interferon gamma signaling / Modulation by Mtb of host immune system / positive regulation of T cell activation / Interferon alpha/beta signaling / sensory perception of smell / negative regulation of neuron projection development / positive regulation of protein binding / tertiary granule lumen / DAP12 signaling / MHC class II protein complex binding / late endosome membrane / protein-folding chaperone binding / iron ion transport / ER-Phagosome pathway / T cell differentiation in thymus / early endosome membrane / protein refolding / protein homotetramerization / intracellular iron ion homeostasis / adaptive immune response / amyloid fibril formation / learning or memory / cell surface receptor signaling pathway / immune response / Amyloid fiber formation / endoplasmic reticulum lumen / lysosomal membrane / Golgi membrane / external side of plasma membrane / innate immune response / signaling receptor binding / focal adhesion / Neutrophil degranulation / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / Golgi apparatus / cell surface / endoplasmic reticulum / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
: / : / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 ...: / : / T-cell receptor alpha chain, constant domain / Domain of unknown function (DUF1968) / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Immunoglobulin V-Type / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / Immunoglobulin V-set domain / MHC classes I/II-like antigen recognition protein / Immunoglobulin V-set domain / : / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Human nkt tcr beta chain / HLA class I histocompatibility antigen, B alpha chain / HLA class I histocompatibility antigen, B alpha chain / Beta-2-microglobulin / TRA@ protein
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsJude, K.M. / Sibener, L.V. / Yang, X. / Garcia, K.C.
Funding support United States, 8items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI07290 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)CA216926-01 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI57229 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI103867 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI096879 United States
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)NS071518 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)A1091580 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)CA199090-01 United States
CitationJournal: Cell / Year: 2018
Title: Isolation of a Structural Mechanism for Uncoupling T Cell Receptor Signaling from Peptide-MHC Binding.
Authors: Sibener, L.V. / Fernandes, R.A. / Kolawole, E.M. / Carbone, C.B. / Liu, F. / McAffee, D. / Birnbaum, M.E. / Yang, X. / Su, L.F. / Yu, W. / Dong, S. / Gee, M.H. / Jude, K.M. / Davis, M.M. / ...Authors: Sibener, L.V. / Fernandes, R.A. / Kolawole, E.M. / Carbone, C.B. / Liu, F. / McAffee, D. / Birnbaum, M.E. / Yang, X. / Su, L.F. / Yu, W. / Dong, S. / Gee, M.H. / Jude, K.M. / Davis, M.M. / Groves, J.T. / Goddard III, W.A. / Heath, J.R. / Evavold, B.D. / Vale, R.D. / Garcia, K.C.
History
DepositionNov 5, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 25, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 8, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Feb 20, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support
Revision 1.4Oct 4, 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: HLA class I histocompatibility antigen, B-35 alpha chain
B: Beta-2-microglobulin
D: TCR 55 alpha chain
H: TCR 55 beta chain
C: VAL-PRO-LEU-THR-GLU-ASP-ALA-GLU-LEU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,82236
Polymers94,9565
Non-polymers2,86631
Water11,115617
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18450 Å2
ΔGint-83 kcal/mol
Surface area36280 Å2
Unit cell
Length a, b, c (Å)194.492, 61.698, 92.145
Angle α, β, γ (deg.)90.00, 104.87, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 4 types, 4 molecules ABDH

#1: Protein HLA class I histocompatibility antigen, B-35 alpha chain / MHC class I antigen B*35


Mass: 31940.246 Da / Num. of mol.: 1 / Fragment: UNP residues 25-300
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-B, HLAB / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P30685, UniProt: P01889*PLUS
#2: Protein Beta-2-microglobulin


Mass: 11748.160 Da / Num. of mol.: 1 / Fragment: UNP residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P61769
#3: Protein TCR 55 alpha chain


Mass: 22890.752 Da / Num. of mol.: 1 / Mutation: T161C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRA@ / Production host: Escherichia coli (E. coli) / References: UniProt: Q6IRV4
#4: Protein TCR 55 beta chain


Mass: 27390.535 Da / Num. of mol.: 1 / Mutation: A187C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: K7N5M4

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Protein/peptide , 1 types, 1 molecules C

#5: Protein/peptide VAL-PRO-LEU-THR-GLU-ASP-ALA-GLU-LEU


Mass: 986.073 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 3 types, 648 molecules

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


Mass: 92.094 Da / Num. of mol.: 27 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 617 / 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: 2.81 Å3/Da / Density % sol: 56.27 %
Crystal growTemperature: 295 K / Method: vapor diffusion
Details: 0.04 M potassium phosphate monobasic, 16% w/v PEG8000, 20% v/v glycerol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 23, 2017
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 1.75→50 Å / Num. obs: 103605 / % possible obs: 97.14 % / Redundancy: 2.9 % / Biso Wilson estimate: 19.44 Å2 / CC1/2: 0.988 / Rmerge(I) obs: 0.063 / Rpim(I) all: 0.0423 / Rrim(I) all: 0.0763 / Net I/σ(I): 10.84
Reflection shellResolution: 1.75→1.813 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.4594 / Mean I/σ(I) obs: 2.34 / Num. unique obs: 10087 / CC1/2: 0.696 / Rpim(I) all: 0.3183 / Rrim(I) all: 0.5622 / % possible all: 94.81

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSNov 1, 2016data reduction
XDSNov 1, 2016data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1A1N

1a1n


Resolution: 1.75→47.259 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 16.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1833 1856 1.79 %random
Rwork0.1585 ---
obs0.1589 103601 97.14 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.75→47.259 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6586 0 182 617 7385
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096994
X-RAY DIFFRACTIONf_angle_d0.9789489
X-RAY DIFFRACTIONf_dihedral_angle_d16.1894187
X-RAY DIFFRACTIONf_chiral_restr0.065986
X-RAY DIFFRACTIONf_plane_restr0.0061226
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.75-1.79730.23961370.2297491X-RAY DIFFRACTION94
1.7973-1.85020.23671440.20067927X-RAY DIFFRACTION99
1.8502-1.90990.22351430.17847862X-RAY DIFFRACTION99
1.9099-1.97820.18721450.16627901X-RAY DIFFRACTION98
1.9782-2.05740.21061420.15757777X-RAY DIFFRACTION97
2.0574-2.1510.19361430.15127880X-RAY DIFFRACTION98
2.151-2.26440.19511440.15267910X-RAY DIFFRACTION98
2.2644-2.40630.18551420.15137783X-RAY DIFFRACTION97
2.4063-2.59210.17171430.15487779X-RAY DIFFRACTION97
2.5921-2.85290.17741430.15587867X-RAY DIFFRACTION98
2.8529-3.26570.17521420.14797779X-RAY DIFFRACTION96
3.2657-4.1140.15531450.14517933X-RAY DIFFRACTION98
4.114-47.27630.18371430.16567856X-RAY DIFFRACTION95
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)
12.6643-0.0459-1.25691.32450.10532.9989-0.0465-0.058-0.30730.0025-0.05450.06410.2481-0.03920.09190.1352-0.0031-0.02410.15120.00790.1666-30.76428.9276-2.6558
26.26120.3785-4.57240.7509-0.55175.04960.10540.3732-0.1658-0.0688-0.01430.04070.0665-0.3135-0.03350.14040.0046-0.03550.1375-0.01930.1581-32.345133.0246-13.4819
32.460.0181-1.10822.31151.45684.02010.1492-0.18980.0730.12650.0189-0.0937-0.07320.2531-0.16750.1246-0.0106-0.02680.1587-0.00280.152-20.187637.9817-7.4753
41.38990.5074-0.24821.1368-0.44381.4760.1564-0.06450.13770.0326-0.0029-0.0437-0.1860.1283-0.16330.1341-0.0155-0.00340.1534-0.03150.1537-22.936744.8475-8.4135
51.8438-0.43471.46541.357-0.86961.6095-0.0074-0.5815-0.41420.16780.1780.06460.0552-0.1256-0.15880.258-0.0954-0.05010.40140.04290.225-14.509125.552221.8898
63.6302-0.18951.53280.74440.20210.9710.0297-0.1530.0130.04850.0446-0.10090.0237-0.0542-0.07750.205-0.0653-0.04030.33180.05410.2116-6.931127.439520.8784
74.07120.452-2.75172.8342-1.36282.29060.32050.0015-0.1585-0.2513-0.1834-0.22670.08980.1469-0.14550.23180.0311-0.05290.23340.07080.3135-12.154918.45682.9275
80.03330.3937-0.1524.6861-1.79490.68760.2403-0.7786-0.62090.87060.0130.48030.3478-0.2749-0.22590.4785-0.1717-0.06210.49590.24240.4584-22.211712.114121.7136
91.24460.1379-0.75321.7016-1.27874.1770.1452-0.2142-0.42720.0447-0.02430.230.1388-0.1566-0.11980.2749-0.0279-0.06820.27070.09890.3202-19.463716.64547.9282
100.78191.3536-1.15387.7983-7.16147.51150.1326-0.0737-0.4221-0.3630.0984-0.01980.8316-0.0862-0.21540.35030.0095-0.08620.16910.02550.3336-18.631112.8795-2.1369
110.7916-2.39870.40788.0919-2.45822.0664-0.21650.1694-0.5771-0.3293-0.11280.75370.3628-0.13870.30630.43-0.1042-0.08980.26390.07070.6331-25.01116.77594.3107
122.30220.9215-1.4131.8606-1.49252.18340.2282-0.1093-0.32590.1128-0.2796-0.0765-0.06210.26860.0480.17480.0031-0.02660.207600.1998-18.655928.2008-2.246
131.31720.12750.39397.4055-5.18535.68390.1957-0.1762-0.43580.18130.08130.5060.209-0.4191-0.2440.2438-0.0542-0.0780.24060.06720.3328-23.03515.94446.6492
140.0151-0.1089-0.2225.6305-2.6567.1834-0.0038-0.0988-0.2058-0.1115-0.0818-0.09010.72760.3910.15760.7298-0.0962-0.22120.50540.34770.6951-17.54071.434617.7543
151.22530.0799-0.30312.1427-1.48415.64070.0726-0.1931-0.6836-0.2842-0.2955-0.24890.97470.32160.17240.47990.0722-0.05370.22830.03530.3892-12.93349.8074-2.0416
163.5264-1.182-0.35513.8485-0.48223.2810.3015-0.2684-0.2560.2683-0.1255-0.2432-0.04660.3242-0.1550.39530.0225-0.13910.3130.16640.5137-11.93358.680410.6815
171.0422-0.28650.27751.648-0.3181.0718-0.0271-0.05480.1072-0.05080.0230.0349-0.11190.02160.00440.15510.02260.02380.1211-0.0080.1283-45.698959.1525-17.1411
182.61980.06250.56533.20930.30092.51790.02020.0575-0.14160.2026-0.10090.50940.0603-0.40050.04170.1781-0.01950.06640.1883-0.02420.2656-63.470376.3734-39.034
191.5325-0.0020.27580.7923-0.20390.8145-0.06290.1351-0.0898-0.12280.08570.06820.07720.0183-0.01910.17060.0010.00320.1245-0.01350.1503-47.691441.4516-33.3812
202.2634-0.4160.76992.7017-0.70711.5372-0.0966-0.1705-0.40970.1960.150.2880.2817-0.1038-0.05140.19860.00570.03310.16550.01340.1963-50.449437.1348-23.0837
211.0153-0.45280.54280.6642-0.07370.7562-0.00270.0799-0.1984-0.05440.02870.07290.07210.0435-0.02450.16380.00680.01790.12810.00530.1543-45.931440.674-28.5694
221.5474-0.37221.23142.0247-1.0542.99030.1783-0.1727-0.228-0.11140.1430.33270.2715-0.3621-0.28460.1702-0.0433-0.040.16090.03170.2411-64.384145.8987-41.5857
231.0259-0.51220.51866.03530.76222.2126-0.09650.07390.0728-0.30210.08330.1996-0.2383-0.04690.02680.14320.01070.02130.13410.02030.1883-59.837677.7644-49.6338
240.86920.5460.41361.8648-0.64220.67840.104-0.0942-0.1190.0354-0.08460.03330.0110.0382-0.01590.1852-0.01120.02210.12920.00820.1542-57.087662.5365-45.7493
252.45311.1468-0.49242.0497-0.48191.90620.1452-0.5073-0.23510.3224-0.22560.20510.09410.0350.08410.2076-0.01120.05030.16220.03630.2217-59.121261.5497-40.5329
260.3385-0.49690.42452.5604-0.15450.65430.07630.05210.13070.20590.10750.2475-0.094-0.1065-0.17180.1383-0.01380.02410.14250.00730.1443-55.283672.1903-46.7263
270.95652.3939-1.09079.492-4.82242.8513-0.02950.183-0.0751-0.06480.1126-0.00870.0132-0.001-0.04190.1764-0.00780.00930.17570.00540.1505-51.87268.3339-55.216
280.69381.63420.59994.55111.13511.3950.36150.2376-0.9321-0.31980.11120.14380.6061-0.2651-0.42420.3699-0.055-0.12420.2394-0.00630.3368-63.824343.0769-51.4997
291.78853.1084-1.20815.3927-2.38623.17420.03420.13730.3309-0.37230.19010.6459-0.0944-0.0799-0.20680.1846-0.0003-0.01270.17690.02910.162-56.450967.6416-57.0901
301.33070.2734-1.67340.094-0.19352.54340.01480.10290.0384-0.1178-0.0102-0.01790.16020.12040.0070.16340.03180.01710.21370.00480.1769-30.10139.8379-12.0024
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 56 )
2X-RAY DIFFRACTION2chain 'A' and (resid 57 through 84 )
3X-RAY DIFFRACTION3chain 'A' and (resid 85 through 118 )
4X-RAY DIFFRACTION4chain 'A' and (resid 119 through 174 )
5X-RAY DIFFRACTION5chain 'A' and (resid 175 through 197 )
6X-RAY DIFFRACTION6chain 'A' and (resid 198 through 276 )
7X-RAY DIFFRACTION7chain 'B' and (resid 2 through 11 )
8X-RAY DIFFRACTION8chain 'B' and (resid 12 through 19 )
9X-RAY DIFFRACTION9chain 'B' and (resid 20 through 30 )
10X-RAY DIFFRACTION10chain 'B' and (resid 31 through 41 )
11X-RAY DIFFRACTION11chain 'B' and (resid 42 through 51 )
12X-RAY DIFFRACTION12chain 'B' and (resid 52 through 61 )
13X-RAY DIFFRACTION13chain 'B' and (resid 62 through 71 )
14X-RAY DIFFRACTION14chain 'B' and (resid 72 through 77 )
15X-RAY DIFFRACTION15chain 'B' and (resid 78 through 90 )
16X-RAY DIFFRACTION16chain 'B' and (resid 91 through 97 )
17X-RAY DIFFRACTION17chain 'D' and (resid 2 through 112 )
18X-RAY DIFFRACTION18chain 'D' and (resid 113 through 202 )
19X-RAY DIFFRACTION19chain 'H' and (resid 3 through 37 )
20X-RAY DIFFRACTION20chain 'H' and (resid 38 through 63 )
21X-RAY DIFFRACTION21chain 'H' and (resid 64 through 108 )
22X-RAY DIFFRACTION22chain 'H' and (resid 109 through 123 )
23X-RAY DIFFRACTION23chain 'H' and (resid 124 through 139 )
24X-RAY DIFFRACTION24chain 'H' and (resid 140 through 161 )
25X-RAY DIFFRACTION25chain 'H' and (resid 162 through 187 )
26X-RAY DIFFRACTION26chain 'H' and (resid 188 through 201 )
27X-RAY DIFFRACTION27chain 'H' and (resid 202 through 214 )
28X-RAY DIFFRACTION28chain 'H' and (resid 215 through 232 )
29X-RAY DIFFRACTION29chain 'H' and (resid 233 through 244 )
30X-RAY DIFFRACTION30chain 'C' and (resid 1 through 9 )

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