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- PDB-4tw2: Crystal Structure of SCARB2 in Neural Condition (pH7.5) -

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Basic information

Entry
Database: PDB / ID: 4tw2
TitleCrystal Structure of SCARB2 in Neural Condition (pH7.5)
ComponentsScavenger receptor class B member 2
KeywordsPROTEIN BINDING / lipid binding tunnel
Function / homology
Function and homology information


regulation of glucosylceramide catabolic process / regulation of carbohydrate catabolic process / regulation of endosome organization / aminophospholipid transport / endosome to plasma membrane protein transport / regulation of lysosome organization / protein targeting to lysosome / phosphatidylcholine binding / cargo receptor activity / scavenger receptor activity ...regulation of glucosylceramide catabolic process / regulation of carbohydrate catabolic process / regulation of endosome organization / aminophospholipid transport / endosome to plasma membrane protein transport / regulation of lysosome organization / protein targeting to lysosome / phosphatidylcholine binding / cargo receptor activity / scavenger receptor activity / cholesterol binding / phosphatidylserine binding / receptor-mediated endocytosis / lysosomal lumen / sensory perception of sound / clathrin-coated endocytic vesicle membrane / positive regulation of neuron projection development / endocytic vesicle membrane / late endosome membrane / transmembrane signaling receptor activity / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / protein-folding chaperone binding / virus receptor activity / endosome membrane / Golgi membrane / lysosomal membrane / focal adhesion / endoplasmic reticulum membrane / enzyme binding / protein homodimerization activity / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Lysosome membrane protein II / CD36 family / CD36 family
Similarity search - Domain/homology
Lysosome membrane protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.889 Å
Model detailsThe protein was expressed in 293T cell
AuthorsDang, M.H. / Wang, X.X. / Rao, Z.H.
Funding support China, 1items
OrganizationGrant numberCountry
Institute of Biophysics, Chinese Academy of Science2014CB542800 China
CitationJournal: Protein Cell / Year: 2014
Title: Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71
Authors: Dang, M. / Wang, X. / Wang, Q. / Wang, Y. / Lin, J. / Sun, Y. / Li, X. / Zhang, L. / Lou, Z. / Wang, J. / Rao, Z.
History
DepositionJun 29, 2014Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jul 8, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 15, 2015Group: Derived calculations
Revision 1.2Jan 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Refinement description / Source and taxonomy
Category: diffrn_source / entity_src_gen ...diffrn_source / entity_src_gen / pdbx_struct_assembly / pdbx_struct_oper_list / software
Item: _diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_alt_source_flag ..._diffrn_source.pdbx_synchrotron_site / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation / _software.name
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_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_leaving_atom_flag / _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 3.0Nov 8, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_nonpoly_scheme / struct_conn / struct_ncs_dom_lim
Item: _atom_site.auth_seq_id / _chem_comp.pdbx_synonyms ..._atom_site.auth_seq_id / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nonpoly_scheme.pdb_seq_num / _struct_conn.ptnr2_auth_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 3.1Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Scavenger receptor class B member 2
B: Scavenger receptor class B member 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,29115
Polymers90,4382
Non-polymers6,85313
Water00
1
A: Scavenger receptor class B member 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,2848
Polymers45,2191
Non-polymers4,0657
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Scavenger receptor class B member 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,0087
Polymers45,2191
Non-polymers2,7896
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)57.796, 100.317, 105.173
Angle α, β, γ (deg.)90.000, 98.690, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ILE / Beg label comp-ID: ILE / End auth comp-ID: ASN / End label comp-ID: ASN / Auth seq-ID: 37 - 430 / Label seq-ID: 1 - 394

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1chain AAA
2chain BBB

NCS oper: (Code: given
Matrix: (-0.347561, -0.026515, -0.937282), (-0.022964, -0.99906, 0.036778), (-0.937376, 0.034306, 0.346625)
Vector: 38.501999, 42.9133, 25.6891)

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Scavenger receptor class B member 2 / Lysosome membrane protein 2 / 85 kDa lysosomal membrane sialoglycoprotein / LGP85 / CD36 antigen- ...Lysosome membrane protein 2 / 85 kDa lysosomal membrane sialoglycoprotein / LGP85 / CD36 antigen-like 2 / Lysosome membrane protein II / LIMP II


Mass: 45219.070 Da / Num. of mol.: 2 / Fragment: ectodomain, UNP residues 37-430
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SCARB2, CD36L2, LIMP2, LIMPII / Plasmid: pFastBac_Bee
Details (production host): modified from pFastBac-one and can express recombinant protein with a melittin tag at the N-terminus and a 6x his-tag at the C-terminus
Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q14108

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Sugars , 6 types, 13 molecules

#2: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#3: 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.: 4 / 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
#4: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 3 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#7: 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.: 3 / 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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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: 3.34 Å3/Da / Density % sol: 63.19 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.1 mol/L HEPES (pH 7.5), 10% v/v 2-Propanol, 20% w/v Polyethylene glycol 4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B1 / Wavelength: 0.91998 Å
DetectorType: RIGAKU SATURN A200 / Detector: CCD / Date: Apr 13, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91998 Å / Relative weight: 1
ReflectionRedundancy: 3.7 % / Number: 106843 / Rmerge(I) obs: 0.105 / Χ2: 1.01 / D res high: 2.8 Å / D res low: 50 Å / Num. obs: 28574 / % possible obs: 99.1
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)IDRmerge(I) obsChi squaredRedundancy
6.035010.0591.0253.7
4.796.0310.0841.0523.8
4.184.7910.0920.9873.8
3.84.1810.1120.9573.8
3.533.810.1391.0013.8
3.323.5310.1770.983.8
3.153.3210.2391.0223.8
3.023.1510.3361.0113.8
2.93.0210.4621.0513.8
2.82.910.5351.0623.4
ReflectionResolution: 2.8→50 Å / Num. obs: 28574 / % possible obs: 99.1 % / Redundancy: 3.7 % / Biso Wilson estimate: 47.56 Å2 / Rmerge(I) obs: 0.105 / Net I/σ(I): 11.6
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
2.8-2.93.40.53526741.06293.1
2.9-3.023.80.46229011.05199.8
3.02-3.153.80.33628071.01199.9
3.15-3.323.80.23928721.02299.9
3.32-3.533.80.17728790.98100
3.53-3.83.80.13928801.001100
3.8-4.183.80.11228640.957100
4.18-4.793.80.09228910.98799.9
4.79-6.033.80.08428901.05299.8
6.03-503.70.05929161.02598.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
SCALEPACKdata reduction
Cootmodel building
PDB_EXTRACT3.14data extraction
PHASERphasing
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4F7B

4f7b


Resolution: 2.889→47.154 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 31.46 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2935 1297 5.11 %Random selection
Rwork0.2438 24102 --
obs0.2463 25399 95.12 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 145.27 Å2 / Biso mean: 53.3161 Å2 / Biso min: 15.34 Å2
Refinement stepCycle: final / Resolution: 2.889→47.154 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6368 0 454 0 6822
Biso mean--59.19 --
Num. residues----788
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0077027
X-RAY DIFFRACTIONf_angle_d1.3699607
X-RAY DIFFRACTIONf_chiral_restr0.0611151
X-RAY DIFFRACTIONf_plane_restr0.0051185
X-RAY DIFFRACTIONf_dihedral_angle_d14.8552587
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3636X-RAY DIFFRACTION6.082TORSIONAL
12B3636X-RAY DIFFRACTION6.082TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 9

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.8894-3.00510.3961800.35311607168758
3.0051-3.14180.42531490.330227982947100
3.1418-3.30750.32461610.297927932954100
3.3075-3.51460.31181380.279328072945100
3.5146-3.78590.30141520.2627952947100
3.7859-4.16660.27841660.227428222988100
4.1666-4.76910.23811470.196828232970100
4.7691-6.00660.24451490.206428162965100
6.0066-47.16060.29451550.22132841299699
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)
11.1738-0.1013-0.19521.5003-0.04121.9099-0.0216-0.0467-0.39850.2884-0.1635-0.03610.4319-0.12910.13410.2383-0.0043-0.1278-0.0136-0.02960.621110.8533-2.170234.6198
21.7295-0.14510.21951.4374-0.58461.9316-0.0095-0.045-0.71490.0998-0.08880.06340.9932-0.2052-0.35920.5764-0.0943-0.0240.1522-0.07710.68539.203-12.410532.1889
34.5045-1.77980.97672.86150.39682.60840.27280.3699-0.208-0.5527-0.2121-0.50010.51110.8415-0.17520.31250.2282-0.03760.32550.05350.65730.95454.082415.8856
40.45620.03070.26461.5555-0.71211.3369-0.1888-0.0459-0.5335-0.1841-0.2381-0.12590.75970.26220.0750.44850.13940.06520.1134-0.02050.671720.8466-9.397227.6354
52.05191.761-0.46821.5903-0.00812.09590.16130.1307-0.383-0.3391-0.357-0.27140.83430.6320.05380.540.27840.01780.29980.06480.68831.1169-8.800242.9627
62.59640.0938-1.28711.83580.53243.63140.0105-0.4782-0.23910.2402-0.10430.03210.38130.17330.15470.0819-0.0091-0.11670.16080.08940.541216.3235-2.298150.0794
70.6356-0.0526-1.42333.20331.56413.8391-0.0963-0.2004-0.02080.39440.1156-0.8970.3991.4011-0.30960.15890.077-0.08580.41550.10530.689731.38893.692235.0583
80.95250.3094-0.66912.0823-1.01932.4542-0.0502-0.0056-0.06140.0038-0.1125-0.17610.02820.09730.0330.0776-0.0888-0.1422-0.0973-0.05320.552818.26148.282935.8336
94.21142.219-1.30653.6993-0.41072.77180.1158-0.1941-0.60850.3545-0.25740.21510.611-0.42120.09140.1749-0.0086-0.1460.0562-0.09840.67854.2241-4.985342.1206
100.9685-0.02280.11322.1467-0.09261.66030.154-0.05210.55620.0464-0.08170.1591-0.7308-0.27430.04650.41140.10010.02090.05180.0170.87353.597751.262227.5717
113.6755-0.1050.13192.79970.37441.31490.05110.9980.4095-1.0958-0.2294-0.6832-0.2543-0.0170.20930.52490.09610.0760.2880.24160.446112.805538.95892.4697
120.5781-0.23460.19481.603-0.19191.15440.15250.13380.5035-0.3195-0.0173-0.1121-0.7455-0.3-0.32770.61720.17480.25010.14620.28640.79575.527553.184215.2987
130.80420.1130.3711.2112-0.52861.6290.31030.43840.268-0.2255-0.10940.3872-0.4176-0.7293-0.14690.25690.3397-0.0820.61440.11770.6193-13.697348.549723.3255
142.0710.1507-1.59735.7651-0.80283.57150.11511.32820.6458-1.15360.060.8536-0.2375-1.1447-0.01570.3850.2402-0.16620.67310.03280.5076-5.292940.24238.3422
152.0296-0.2229-0.321.81581.27552.92480.20080.15480.1368-0.2432-0.1530.1272-0.155-0.4052-0.04170.0790.0749-0.1250.0960.0860.4686-1.653435.899521.2167
161.46870.2958-0.0662.47461.50834.4632-0.0392-0.48550.47760.0218-0.33770.5721-0.8441-0.52920.24380.25220.1563-0.09650.3394-0.01230.6918-2.381949.834736.0332
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 37 through 88 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 89 through 131 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 132 through 167 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 168 through 231 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 232 through 251 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 252 through 311 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 312 through 334 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 335 through 403 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 404 through 430 )A0
10X-RAY DIFFRACTION10chain 'B' and (resid 37 through 131 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 132 through 167 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 168 through 231 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 232 through 311 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 312 through 334 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 335 through 403 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 404 through 430 )B0

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