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- PDB-4gs7: Structure of the Interleukin-15 quaternary complex -

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Basic information

Entry
Database: PDB / ID: 4gs7
TitleStructure of the Interleukin-15 quaternary complex
Components
  • Cytokine receptor common subunit gamma
  • Interleukin-15
  • Interleukin-15 receptor subunit alpha
  • Interleukin-2 receptor subunit beta
KeywordsIMMUNE SYSTEM / Cytokine / Cytokine Receptor / Immunoregulatory / anti-tumor / anti-viral / Reductive methylation
Function / homology
Function and homology information


extrathymic T cell selection / NK T cell proliferation / natural killer cell proliferation / interleukin-2 receptor complex / interleukin-2 receptor activity / mature B cell differentiation / positive regulation of natural killer cell differentiation / interleukin-15 receptor activity / interleukin-2 binding / CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation ...extrathymic T cell selection / NK T cell proliferation / natural killer cell proliferation / interleukin-2 receptor complex / interleukin-2 receptor activity / mature B cell differentiation / positive regulation of natural killer cell differentiation / interleukin-15 receptor activity / interleukin-2 binding / CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / tyrosine phosphorylation of STAT protein / positive regulation of tissue remodeling / positive regulation of T cell differentiation in thymus / natural killer cell differentiation / lymphocyte differentiation / Interleukin-9 signaling / Interleukin-21 signaling / interleukin-7-mediated signaling pathway / interleukin-9-mediated signaling pathway / interleukin-4-mediated signaling pathway / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation / interleukin-2-mediated signaling pathway / cytokine receptor binding / neutrophil activation / regulation of defense response to virus by host / interleukin-15-mediated signaling pathway / cellular homeostasis / positive regulation of natural killer cell proliferation / STAT3 nuclear events downstream of ALK signaling / Interleukin-15 signaling / cytokine receptor activity / Interleukin-2 signaling / negative regulation of cold-induced thermogenesis / regulation of T cell differentiation / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of B cell differentiation / positive regulation of immunoglobulin production / cytokine binding / positive regulation of interleukin-17 production / immunoglobulin mediated immune response / macrophage differentiation / cell surface receptor signaling pathway via JAK-STAT / Interleukin receptor SHC signaling / lymph node development / cell maturation / positive regulation of T cell proliferation / coreceptor activity / positive regulation of phagocytosis / Interleukin-7 signaling / cytoplasmic vesicle membrane / cytokine activity / positive regulation of cytokine production / response to nutrient levels / cytokine-mediated signaling pathway / positive regulation of immune response / positive regulation of inflammatory response / cell-cell signaling / negative regulation of neuron projection development / T cell differentiation in thymus / RAF/MAP kinase cascade / protein-containing complex assembly / Interleukin-4 and Interleukin-13 signaling / gene expression / nuclear membrane / receptor complex / endosome / nuclear speck / immune response / Golgi membrane / external side of plasma membrane / intracellular membrane-bounded organelle / positive regulation of cell population proliferation / endoplasmic reticulum membrane / negative regulation of apoptotic process / protein kinase binding / cell surface / Golgi apparatus / signal transduction / extracellular space / extracellular region / nucleoplasm / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Interleukin-15 / Interleukin-15, mammal / Interleukin-15 receptor subunit alpha / Interleukin-15/Interleukin-21 family / Interleukin-2 receptor subunit beta, N-terminal / Interleukin 15 / Interleukin-2 receptor subunit beta N-terminal domain 1 / Interleukin-15/Interleukin-21 / Rubrerythrin, domain 2 - #230 / : ...Interleukin-15 / Interleukin-15, mammal / Interleukin-15 receptor subunit alpha / Interleukin-15/Interleukin-21 family / Interleukin-2 receptor subunit beta, N-terminal / Interleukin 15 / Interleukin-2 receptor subunit beta N-terminal domain 1 / Interleukin-15/Interleukin-21 / Rubrerythrin, domain 2 - #230 / : / : / Cytokine receptor-like factor 2-like, D2 domain / Cytokine receptor-like factor 2, domain 1 / Short hematopoietin receptor family 1 signature. / Interleukin-6 receptor alpha chain, binding / Short hematopoietin receptor, family 1, conserved site / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Four-helical cytokine-like, core / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Rubrerythrin, domain 2 / Growth Hormone; Chain: A; / Single Sheet / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
ACETATE ION / Interleukin-2 receptor subunit beta / Cytokine receptor common subunit gamma / Interleukin-15 / Interleukin-15 receptor subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsRing, A.M. / Ozkan, E. / Feng, D. / Garcia, K.C.
CitationJournal: Nat.Immunol. / Year: 2012
Title: Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15.
Authors: Ring, A.M. / Lin, J.X. / Feng, D. / Mitra, S. / Rickert, M. / Bowman, G.R. / Pande, V.S. / Li, P. / Moraga, I. / Spolski, R. / Ozkan, E. / Leonard, W.J. / Garcia, K.C.
History
DepositionAug 27, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 7, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 14, 2012Group: Database references
Revision 1.2Dec 5, 2012Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / 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_ref_seq_dif / 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.comp_id / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Mar 26, 2025Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
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: Interleukin-15
B: Interleukin-2 receptor subunit beta
C: Cytokine receptor common subunit gamma
D: Interleukin-15 receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,79510
Polymers70,3834
Non-polymers1,4126
Water4,576254
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7350 Å2
ΔGint9 kcal/mol
Surface area28960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.949, 74.610, 129.211
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 4 molecules ABCD

#1: Protein Interleukin-15 / IL-15


Mass: 13080.885 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL15 / Production host: Escherichia coli (E. coli) / References: UniProt: P40933
#2: Protein Interleukin-2 receptor subunit beta / IL-2 receptor subunit beta / IL-2R subunit beta / IL-2RB / High affinity IL-2 receptor subunit beta ...IL-2 receptor subunit beta / IL-2R subunit beta / IL-2RB / High affinity IL-2 receptor subunit beta / p70-75 / p75


Mass: 25152.584 Da / Num. of mol.: 1 / Mutation: N29Q, N43Q, N71Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL2RB / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P14784
#3: Protein Cytokine receptor common subunit gamma / Interleukin-2 receptor subunit gamma / IL-2 receptor subunit gamma / IL-2R subunit gamma / IL-2RG / ...Interleukin-2 receptor subunit gamma / IL-2 receptor subunit gamma / IL-2R subunit gamma / IL-2RG / gammaC / p64


Mass: 24390.262 Da / Num. of mol.: 1 / Mutation: N75Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL2RG / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P31785
#4: Protein Interleukin-15 receptor subunit alpha / IL-15 receptor subunit alpha / IL-15R-alpha / IL-15RA / Soluble interleukin-15 receptor subunit ...IL-15 receptor subunit alpha / IL-15R-alpha / IL-15RA / Soluble interleukin-15 receptor subunit alpha / sIL-15 receptor subunit alpha / sIL-15R-alpha / sIL-15RA


Mass: 7758.956 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL15RA / Production host: Escherichia coli (E. coli) / References: UniProt: Q13261

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Sugars , 2 types, 4 molecules

#5: 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: isolated from a genetically manipulated source
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
#8: 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: isolated from a genetically manipulated source
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, 256 molecules

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


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 254 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.43 Å3/Da / Density % sol: 49.37 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.75
Details: 22.5% PEG3350, 0.1M BIS-TRIS propane, 0.2M sodium acetate, pH 8.75, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 8, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.35→40.23 Å / Num. obs: 29215

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Processing

Software
NameVersionClassification
Blu-Icedata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.35→40.23 Å / SU ML: 0.28 / σ(F): 1.34 / Phase error: 22.4 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2268 1456 4.99 %
Rwork0.1816 --
obs0.1838 29198 99.16 %
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--2.1201 Å2-0 Å20 Å2
2---0.0306 Å20 Å2
3---2.1508 Å2
Refinement stepCycle: LAST / Resolution: 2.35→40.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4687 0 92 254 5033
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0034946
X-RAY DIFFRACTIONf_angle_d0.7076731
X-RAY DIFFRACTIONf_dihedral_angle_d15.7961812
X-RAY DIFFRACTIONf_chiral_restr0.052745
X-RAY DIFFRACTIONf_plane_restr0.003843
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.35-2.42910.32611480.24162605X-RAY DIFFRACTION95
2.4291-2.52640.29651350.22642708X-RAY DIFFRACTION99
2.5264-2.64130.26951500.20752746X-RAY DIFFRACTION99
2.6413-2.78050.23721410.19882754X-RAY DIFFRACTION100
2.7805-2.95470.25331420.19162779X-RAY DIFFRACTION100
2.9547-3.18270.26271420.18742772X-RAY DIFFRACTION100
3.1827-3.50290.20261500.16882782X-RAY DIFFRACTION100
3.5029-4.00940.2121450.15582806X-RAY DIFFRACTION100
4.0094-5.04980.18591500.14872847X-RAY DIFFRACTION100
5.0498-40.23550.21931530.2032943X-RAY DIFFRACTION99
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)
12.0856-2.3528-0.78255.24440.07628.31640.1795-0.357-0.18510.13720.0469-0.30660.02010.6415-0.24870.1881-0.0664-0.02050.2754-0.00770.312220.8483-17.86064.5388
22.36240.2329-0.32315.3630.33884.8126-0.13210.3791-0.0363-0.22310.33680.1825-0.0103-0.019-0.16720.1441-0.0343-0.05150.3864-0.02710.245417.7256-16.3224-8.6597
36.346-2.1449-0.60112.2158-0.94198.04070.2468-0.0633-0.54280.1210.02930.74190.0909-0.431-0.33310.1428-0.0762-0.01920.2682-0.00690.25412.0363-21.68882.0195
47.201-4.3154.54486.408-1.57955.2240.1310.50910.3096-0.3061-0.17060.52790.0593-0.41170.06760.3383-0.0589-0.02020.45780.06250.363913.0865-10.1908-13.817
54.9601-6.2489-4.17687.74185.2853.54220.0972-0.0120.734-0.22850.1636-0.5414-0.34390.3807-0.33720.2161-0.0221-0.02870.2589-0.00790.278320.9228-10.0203-2.0314
64.41451.4619-0.36665.44-1.08834.66950.2808-0.4284-0.32010.451-0.07830.13820.3727-0.1934-0.15430.1931-0.0144-0.03140.26880.04230.21583.8773-34.067521.3695
74.816-2.6154-0.42028.2339-0.39682.61420.19230.2469-0.40190.0294-0.2063-0.07230.0460.23810.07240.2318-0.0023-0.00520.2231-0.00220.177812.4607-27.116611.728
85.8674.64470.17099.3086-0.04293.21320.2364-0.3530.02810.2345-0.21380.6750.4221-0.29650.01560.265-0.0357-0.00470.31850.07460.2463-4.046-33.601319.9215
97.49540.11335.87450.48810.40184.54490.10680.2823-0.27080.01930.0045-0.14120.02180.3126-0.15920.1847-0.00670.01540.1876-0.00310.225927.0425-19.871526.4499
105.9598-0.44532.2882.88260.56584.6630.0434-0.4447-0.20820.43540.06460.015-0.0636-0.1988-0.08950.2478-0.005-0.00030.18930.0340.214126.1257-17.115737.211
119.1149-0.67376.19392.25110.29095.13530.3569-0.5007-0.49790.0808-0.1183-0.00740.3401-0.2928-0.25680.2170.01180.0490.23930.05380.205421.8387-20.991732.6466
123.1574-1.3713-1.66496.87590.35287.05820.00910.08090.5296-0.12430.0112-0.8473-0.50021.1084-0.04230.323-0.0834-0.0690.39360.06670.397538.363211.6456-3.5226
136.30511.2035-0.72966.7737-0.34214.73640.05210.5965-0.137-0.8174-0.07740.3675-0.8306-0.64880.15780.51720.1354-0.05610.3540.06140.333424.997210.9697-11.6597
143.48470.8398-1.16835.87010.22595.36960.01470.29960.3559-0.2393-0.1135-0.3359-0.85270.1450.03980.30250.0008-0.02640.23790.07750.291232.453910.8909-7.5254
152.3014-0.0784-1.78241.9902-0.25527.62930.1985-0.22370.01350.4574-0.05520.2099-1.0368-0.2336-0.17780.2786-0.0158-0.00090.1895-0.06540.26424.32522.516925.9818
162.26861.05630.12334.87131.10617.8376-0.36110.10920.1831-0.23130.00990.175-1.2377-0.62410.38220.31370.06080.01960.2350.00230.214925.56590.8819.5183
177.4343-0.54840.20365.658-0.7738.59670.1509-0.2759-0.0230.7577-0.0177-0.5664-0.21220.6671-0.29810.3077-0.0217-0.02270.24420.04450.286438.1187-3.312228.3848
181.48920.30831.26132.0787-1.58985.5085-0.1092-0.10640.04820.1275-0.1192-0.052-0.36650.15020.22720.17340.00540.00740.213-0.01880.237929.4483-0.164124.1367
190.83720.3353-0.97982.69810.76261.63510.18350.8031-1.09140.39820.20850.43240.67710.9323-0.28070.88340.0952-0.25070.6791-0.25110.535521.6321-40.2268-21.8716
207.4371-4.4133-2.1065.76840.67520.98640.77920.4716-0.3319-1.1619-0.0985-0.14230.60651.0408-0.56980.42740.0374-0.03540.8216-0.23230.355326.2129-34.4869-23.5312
214.7689-5.33696.72765.9903-7.51689.49340.1074-0.57340.1721-0.08240.66320.06630.86180.693-0.69550.51340.1119-0.06390.6857-0.16940.451427.8327-36.2218-13.5634
223.7351-3.83551.14567.10260.7568.5930.01520.758-0.3381-0.8437-0.03640.1613-0.33090.7294-0.00980.315-0.0995-0.07460.6345-0.09010.25217.733-24.2212-21.3471
234.69-4.70963.36315.3627-4.55024.4910.5064-0.6047-1.6192-0.31740.77490.68930.3853-0.5567-0.84330.6660.0147-0.18840.4881-0.03070.594922.8653-40.4792-12.2288
249.487-6.82553.86386.0808-4.39873.76131.039-0.7251-1.668-1.7798-0.21551.56821.25860.041-0.84780.60380.0303-0.12440.5744-0.03410.569618.7617-41.0075-14.7438
253.4008-0.5024-0.3372.46544.11046.92110.46870.7420.2637-2.4176-0.59870.5254-1.18380.01250.21470.6380.0969-0.12350.5624-0.06390.318912.9127-19.4207-25.4261
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 0:18)
2X-RAY DIFFRACTION2CHAIN A AND (RESSEQ 19:54)
3X-RAY DIFFRACTION3CHAIN A AND (RESSEQ 55:76)
4X-RAY DIFFRACTION4CHAIN A AND (RESSEQ 77:95)
5X-RAY DIFFRACTION5CHAIN A AND (RESSEQ 96:112)
6X-RAY DIFFRACTION6CHAIN B AND (RESSEQ 6:63)
7X-RAY DIFFRACTION7CHAIN B AND (RESSEQ 64:76)
8X-RAY DIFFRACTION8CHAIN B AND (RESSEQ 77:102)
9X-RAY DIFFRACTION9CHAIN B AND (RESSEQ 103:138)
10X-RAY DIFFRACTION10CHAIN B AND (RESSEQ 139:186)
11X-RAY DIFFRACTION11CHAIN B AND (RESSEQ 187:207)
12X-RAY DIFFRACTION12CHAIN C AND (RESSEQ 32:63)
13X-RAY DIFFRACTION13CHAIN C AND (RESSEQ 64:82)
14X-RAY DIFFRACTION14CHAIN C AND (RESSEQ 83:128)
15X-RAY DIFFRACTION15CHAIN C AND (RESSEQ 129:151)
16X-RAY DIFFRACTION16CHAIN C AND (RESSEQ 152:169)
17X-RAY DIFFRACTION17CHAIN C AND (RESSEQ 170:180)
18X-RAY DIFFRACTION18CHAIN C AND (RESSEQ 181:227)
19X-RAY DIFFRACTION19CHAIN D AND (RESSEQ 1:10)
20X-RAY DIFFRACTION20CHAIN D AND (RESSEQ 11:20)
21X-RAY DIFFRACTION21CHAIN D AND (RESSEQ 21:26)
22X-RAY DIFFRACTION22CHAIN D AND (RESSEQ 27:41)
23X-RAY DIFFRACTION23CHAIN D AND (RESSEQ 42:48)
24X-RAY DIFFRACTION24CHAIN D AND (RESSEQ 49:62)
25X-RAY DIFFRACTION25CHAIN D AND (RESSEQ 63:67)

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