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- PDB-6atf: HLA-DRB1*1402 in complex with Vimentin59-71 -

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Basic information

Entry
Database: PDB / ID: 6atf
TitleHLA-DRB1*1402 in complex with Vimentin59-71
Components
  • HLA class II histocompatibility antigen, DR alpha chain
  • MHC class II antigen
  • Vimentin59-71
KeywordsIMMUNE SYSTEM / HLA Class II
Function / homology
Function and homology information


keratin filament binding / lens fiber cell development / intermediate filament organization / myeloid dendritic cell antigen processing and presentation / antigen processing and presentation of endogenous peptide antigen via MHC class II / autolysosome membrane / regulation of T-helper cell differentiation / cellular response to muramyl dipeptide / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / structural constituent of eye lens ...keratin filament binding / lens fiber cell development / intermediate filament organization / myeloid dendritic cell antigen processing and presentation / antigen processing and presentation of endogenous peptide antigen via MHC class II / autolysosome membrane / regulation of T-helper cell differentiation / cellular response to muramyl dipeptide / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / structural constituent of eye lens / MHC class II receptor activity / positive regulation of CD4-positive, alpha-beta T cell activation / astrocyte development / antigen processing and presentation of peptide or polysaccharide antigen via MHC class II / positive regulation of memory T cell differentiation / Striated Muscle Contraction / microtubule organizing center / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / intermediate filament / polysaccharide binding / transport vesicle membrane / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / cell leading edge / Bergmann glial cell differentiation / Generation of second messenger molecules / immunological synapse / positive regulation of collagen biosynthetic process / PD-1 signaling / Caspase-mediated cleavage of cytoskeletal proteins / T cell receptor binding / phagocytic vesicle / regulation of mRNA stability / MHC class II antigen presentation / trans-Golgi network membrane / lumenal side of endoplasmic reticulum membrane / Late endosomal microautophagy / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / cellular response to type II interferon / structural constituent of cytoskeleton / cognition / peptide antigen assembly with MHC class II protein complex / nuclear matrix / MHC class II protein complex / Aggrephagy / Chaperone Mediated Autophagy / positive regulation of T cell mediated cytotoxicity / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / Interferon gamma signaling / endocytic vesicle membrane / double-stranded RNA binding / neuron projection development / positive regulation of T cell activation / negative regulation of neuron projection development / Downstream TCR signaling / peroxisome / MHC class II protein complex binding / late endosome membrane / early endosome membrane / scaffold protein binding / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / molecular adaptor activity / lysosome / cytoskeleton / endosome membrane / immune response / protein domain specific binding / lysosomal membrane / Golgi membrane / axon / focal adhesion / positive regulation of gene expression / cell surface / extracellular exosome / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Intermediate filament head, DNA-binding domain / : / Intermediate filament head (DNA binding) region / Intermediate filament protein, conserved site / Intermediate filament protein / Intermediate filament (IF) rod domain signature. / Intermediate filament, rod domain / Intermediate filament (IF) rod domain profile. / Intermediate filament protein / Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 ...Intermediate filament head, DNA-binding domain / : / Intermediate filament head (DNA binding) region / Intermediate filament protein, conserved site / Intermediate filament protein / Intermediate filament (IF) rod domain signature. / Intermediate filament, rod domain / Intermediate filament (IF) rod domain profile. / Intermediate filament protein / Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / Class II Histocompatibility Antigen, M Beta Chain; Chain B, domain 1 / MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / MHC classes I/II-like antigen recognition protein / : / 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 / Roll / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
TRIETHYLENE GLYCOL / HLA class II histocompatibility antigen DR beta chain / HLA class II histocompatibility antigen, DR alpha chain / Vimentin
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsScally, S.W. / Ting, Y.T. / Rossjohn, J.
Funding support Australia, 1items
OrganizationGrant numberCountry
NHMRC, ARC Australia
CitationJournal: Ann. Rheum. Dis. / Year: 2017
Title: Molecular basis for increased susceptibility of Indigenous North Americans to seropositive rheumatoid arthritis.
Authors: Scally, S.W. / Law, S.C. / Ting, Y.T. / Heemst, J.V. / Sokolove, J. / Deutsch, A.J. / Bridie Clemens, E. / Moustakas, A.K. / Papadopoulos, G.K. / Woude, D.V. / Smolik, I. / Hitchon, C.A. / ...Authors: Scally, S.W. / Law, S.C. / Ting, Y.T. / Heemst, J.V. / Sokolove, J. / Deutsch, A.J. / Bridie Clemens, E. / Moustakas, A.K. / Papadopoulos, G.K. / Woude, D.V. / Smolik, I. / Hitchon, C.A. / Robinson, D.B. / Ferucci, E.D. / Bernstein, C.N. / Meng, X. / Anaparti, V. / Huizinga, T. / Kedzierska, K. / Reid, H.H. / Raychaudhuri, S. / Toes, R.E. / Rossjohn, J. / El-Gabalawy, H. / Thomas, R.
History
DepositionAug 29, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 13, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _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 II histocompatibility antigen, DR alpha chain
B: MHC class II antigen
D: HLA class II histocompatibility antigen, DR alpha chain
E: MHC class II antigen
C: Vimentin59-71
F: Vimentin59-71
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,88719
Polymers92,8616
Non-polymers2,02613
Water18,3211017
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A: HLA class II histocompatibility antigen, DR alpha chain
B: MHC class II antigen
C: Vimentin59-71
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,62511
Polymers46,4313
Non-polymers1,1948
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8400 Å2
ΔGint-14 kcal/mol
Surface area18600 Å2
MethodPISA
2
D: HLA class II histocompatibility antigen, DR alpha chain
E: MHC class II antigen
F: Vimentin59-71
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,2628
Polymers46,4313
Non-polymers8325
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8920 Å2
ΔGint-8 kcal/mol
Surface area18590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.980, 77.770, 94.540
Angle α, β, γ (deg.)90.00, 109.52, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 2 types, 4 molecules ADBE

#1: Protein HLA class II histocompatibility antigen, DR alpha chain / MHC class II antigen DRA


Mass: 21919.594 Da / Num. of mol.: 2 / Fragment: UNP residues 26-206
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DRA, HLA-DRA1 / Production host: Homo sapiens (human) / References: UniProt: P01903
#2: Protein MHC class II antigen


Mass: 23072.367 Da / Num. of mol.: 2 / Fragment: UNP residues 30-219
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DRB1 / Production host: Homo sapiens (human) / References: UniProt: A0A0A1I7H6

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Protein/peptide , 1 types, 2 molecules CF

#3: Protein/peptide Vimentin59-71


Mass: 1438.657 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: UniProt: P08670*PLUS

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Sugars , 2 types, 4 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 1026 molecules

#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: C2H6O2
#7: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1017 / 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: 2.5 Å3/Da / Density % sol: 50.78 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.3
Details: 26% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane pH 7.3

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 5, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 1.9→33.482 Å / Num. obs: 72027 / % possible obs: 99.7 % / Redundancy: 3.6 % / Rpim(I) all: 0.056 / Net I/σ(I): 10.6
Reflection shellResolution: 1.9→2 Å / Redundancy: 3.5 % / Mean I/σ(I) obs: 3.3 / Num. unique obs: 10379 / Rpim(I) all: 0.23 / % possible all: 98.9

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
MOSFLMdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4MCY

4mcy


Resolution: 1.9→33.482 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 18.86
RfactorNum. reflection% reflection
Rfree0.2023 3632 5.04 %
Rwork0.1699 --
obs0.1715 72003 99.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.9→33.482 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6263 0 132 1026 7421
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0046626
X-RAY DIFFRACTIONf_angle_d0.9139006
X-RAY DIFFRACTIONf_dihedral_angle_d13.952416
X-RAY DIFFRACTIONf_chiral_restr0.037976
X-RAY DIFFRACTIONf_plane_restr0.0041173
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.899-1.9240.26511140.23952554X-RAY DIFFRACTION97
1.924-1.95030.24491380.22242590X-RAY DIFFRACTION99
1.9503-1.97820.25151270.20692629X-RAY DIFFRACTION99
1.9782-2.00770.24381380.1942619X-RAY DIFFRACTION100
2.0077-2.03910.23271470.19132627X-RAY DIFFRACTION100
2.0391-2.07250.22091490.19132570X-RAY DIFFRACTION100
2.0725-2.10830.2241560.1862640X-RAY DIFFRACTION100
2.1083-2.14660.2181490.17552599X-RAY DIFFRACTION100
2.1466-2.18790.20841220.17752629X-RAY DIFFRACTION100
2.1879-2.23250.20311440.17682635X-RAY DIFFRACTION100
2.2325-2.2810.20271420.17062606X-RAY DIFFRACTION100
2.281-2.33410.22261390.17232631X-RAY DIFFRACTION100
2.3341-2.39240.22851380.17622631X-RAY DIFFRACTION100
2.3924-2.45710.22581350.18172628X-RAY DIFFRACTION100
2.4571-2.52940.2381380.17792603X-RAY DIFFRACTION100
2.5294-2.6110.21631540.17012636X-RAY DIFFRACTION100
2.611-2.70430.21381370.17762635X-RAY DIFFRACTION100
2.7043-2.81250.19531370.17242617X-RAY DIFFRACTION100
2.8125-2.94040.19231390.17282669X-RAY DIFFRACTION100
2.9404-3.09540.24241260.16822655X-RAY DIFFRACTION100
3.0954-3.28910.191400.16232636X-RAY DIFFRACTION100
3.2891-3.54280.17931340.15452669X-RAY DIFFRACTION100
3.5428-3.89890.17181540.15042622X-RAY DIFFRACTION100
3.8989-4.46190.16131380.13512664X-RAY DIFFRACTION100
4.4619-5.61730.18071360.14432680X-RAY DIFFRACTION100
5.6173-33.48760.18131610.1842697X-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)
12.93740.15470.94811.5101-1.67672.3719-0.02620.0541-0.1246-0.01830.0161-0.01450.0409-0.00990.03150.09350.02860.00630.0835-0.02570.088244.87484.374114.3068
23.46980.13-1.04952.94241.17052.6927-0.04350.2013-0.71210.0450.037-0.18170.45250.139-0.06210.17220.00140.01370.0957-0.03990.207444.4942-5.4391106.3641
31.28680.43790.52562.0372.78646.12520.0271-0.0391-0.13920.1117-0.0979-0.04760.20360.14950.03710.1270.0108-0.01240.12890.0570.124854.82034.9213123.0097
43.21491.04251.31831.45520.48312.0635-0.25520.0680.2383-0.11450.06710.29840.0886-0.19810.17430.1347-0.0450.02710.09010.05170.077727.78391.9457119.2004
52.51431.06770.01040.48070.22022.0489-0.0580.0371-0.0873-0.0561-0.0027-0.02120.1388-0.09630.03410.11730.00680.01130.05660.00880.101129.3496-2.8826117.45
61.6990.6968-1.11592.0348-0.49190.87320.07940.1497-0.27490.1937-0.00550.11090.4523-0.6433-0.09030.2098-0.15240.02460.29580.03490.192617.0165-9.3731119.6624
71.64750.4442-1.72813.23970.16191.92280.0908-0.55050.2290.0965-0.2460.3560.1915-0.61890.20580.08770.0010.04430.24420.02070.116921.2619-0.7732124.9657
81.48420.2826-0.03620.872-0.26741.9618-0.03240.07210.04380.0167-0.0042-0.0407-0.17390.02450.03880.08340.005-0.00430.07990.01150.084751.500214.2851112.2493
93.3862-1.3576-0.00690.90960.19761.24380.02780.2289-0.074-0.0646-0.05010.1312-0.0972-0.11370.02340.1272-0.029-0.00150.1-0.03470.111614.67417.252798.5826
102.32760.6905-0.53930.72180.1296.9659-0.03180.0330.1230.00110.07380.0173-0.18860.1387-0.01240.06010.0131-0.00780.0676-0.00090.080627.834935.3216114.5136
113.6831-0.02030.98763.1217-0.91943.28260.04030.1190.6620.0419-0.04110.1262-0.505-0.0877-0.04280.16030.013-0.0090.08830.03780.192128.206745.1556106.5348
121.37070.3844-0.67122.3568-2.83866.3124-0.0512-0.11050.17840.17430.04870.0811-0.1556-0.2789-0.02440.11410.0120.01670.1287-0.05760.118717.730534.7548123.7334
132.88050.5629-1.34211.3746-0.25921.6637-0.21010.1277-0.2167-0.1240.0065-0.2866-0.05960.14140.20110.1068-0.0427-0.03890.1283-0.01370.056344.911437.7896119.4162
142.5030.7740.01250.5633-0.29771.6464-0.07380.06580.0776-0.0863-0.0070.0076-0.23450.04660.05220.1415-0.0067-0.00670.0659-0.00570.077443.346742.5925117.6392
152.78081.6257-0.23122.9815-0.55022.14830.2056-0.422-0.050.1365-0.2842-0.2508-0.3550.69310.09590.1455-0.0741-0.02010.2504-0.01150.121952.930644122.6793
161.22630.0271-0.02061.12050.26782.2714-0.00640.0203-0.0719-0.01530.0069-0.03170.06320.0538-0.01150.06660.00620.00490.0834-0.00620.076924.622524.9498114.8585
172.47081.1179-1.21331.9143-0.69712.6823-0.05610.2325-0.03530.04390.06040.14010.1647-0.23140.02460.08750.0132-0.00460.0981-0.02960.08216.490426.0611108.9023
183.2446-1.53010.0310.9146-0.27790.92690.04870.30190.1171-0.0514-0.0914-0.14690.07910.09150.03930.1244-0.02530.00460.11820.03160.114157.933132.626398.6132
193.02571.63382.73322.99513.21075.4895-0.0230.1596-0.25370.18480.262-0.30390.07130.403-0.25650.11070.0222-0.01430.10550.01030.114956.27626.7543113.7522
202.13340.7958-1.16521.7834-1.63683.20180.11570.05310.27430.30780.17030.3597-0.2924-0.2484-0.30160.11780.01950.04110.119-0.01140.123616.424332.956113.9199
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 26 )
2X-RAY DIFFRACTION2chain 'A' and (resid 27 through 55 )
3X-RAY DIFFRACTION3chain 'A' and (resid 56 through 76 )
4X-RAY DIFFRACTION4chain 'A' and (resid 77 through 101 )
5X-RAY DIFFRACTION5chain 'A' and (resid 102 through 154 )
6X-RAY DIFFRACTION6chain 'A' and (resid 155 through 166 )
7X-RAY DIFFRACTION7chain 'A' and (resid 167 through 181 )
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 89 )
9X-RAY DIFFRACTION9chain 'B' and (resid 90 through 190 )
10X-RAY DIFFRACTION10chain 'D' and (resid 3 through 26 )
11X-RAY DIFFRACTION11chain 'D' and (resid 27 through 55 )
12X-RAY DIFFRACTION12chain 'D' and (resid 56 through 76 )
13X-RAY DIFFRACTION13chain 'D' and (resid 77 through 101 )
14X-RAY DIFFRACTION14chain 'D' and (resid 102 through 154 )
15X-RAY DIFFRACTION15chain 'D' and (resid 155 through 181 )
16X-RAY DIFFRACTION16chain 'E' and (resid 2 through 51 )
17X-RAY DIFFRACTION17chain 'E' and (resid 52 through 89 )
18X-RAY DIFFRACTION18chain 'E' and (resid 90 through 190 )
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 13 )
20X-RAY DIFFRACTION20chain 'F' and (resid 1 through 13 )

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