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- PDB-6dy3: Caenorhabditis elegans N-acylethanolamine-hydrolyzing acid amidas... -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6dy3
TitleCaenorhabditis elegans N-acylethanolamine-hydrolyzing acid amidase (NAAA) ortholog
Components
  • N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
  • N-acylethanolamine-hydrolyzing acid amidase beta-subunit
KeywordsHYDROLASE / endocannabinoid / lipase
Function / homology
Function and homology information


Neurotransmitter release cycle / N-(long-chain-acyl)ethanolamine deacylase / N-(long-chain-acyl)ethanolamine deacylase activity / N-acylethanolamine metabolic process / fatty acid amide hydrolase activity / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / extrinsic component of membrane / lipid catabolic process / fatty acid metabolic process / lysosome
Similarity search - Function
Acid ceramidase-like / Acid ceramidase, N-terminal / beta subunit of N-acylethanolamine-hydrolyzing acid amidase / Choloylglycine hydrolase/NAAA C-terminal / Linear amide C-N hydrolases, choloylglycine hydrolase family
Similarity search - Domain/homology
N-acylethanolamine-hydrolyzing acid amidase
Similarity search - Component
Biological speciesCaenorhabditis elegans (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsGorelik, A. / Gebai, A. / Illes, K. / Piomelli, D. / Nagar, B.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)MOP-133535 Canada
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018
Title: Molecular mechanism of activation of the immunoregulatory amidase NAAA.
Authors: Gorelik, A. / Gebai, A. / Illes, K. / Piomelli, D. / Nagar, B.
History
DepositionJul 1, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 26, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 10, 2018Group: Data collection / Database references / Structure summary
Category: citation / entity
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _entity.formula_weight
Revision 1.2Oct 24, 2018Group: Data collection / Database references / Structure summary
Category: citation / citation_author / entity
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ..._citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _entity.formula_weight
Revision 1.3Nov 7, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Apr 17, 2019Group: Data collection / Structure summary / Category: entity / Item: _entity.pdbx_ec
Revision 1.5Jan 8, 2020Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / 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 / pdbx_validate_close_contact / 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 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
B: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
C: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
D: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
E: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
F: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
G: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
H: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)161,41110
Polymers160,2698
Non-polymers1,1412
Water6,305350
1
A: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
B: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6383
Polymers40,0672
Non-polymers5711
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5830 Å2
ΔGint-28 kcal/mol
Surface area14280 Å2
MethodPISA
2
C: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
D: N-acylethanolamine-hydrolyzing acid amidase beta-subunit


Theoretical massNumber of molelcules
Total (without water)40,0672
Polymers40,0672
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5160 Å2
ΔGint-42 kcal/mol
Surface area14020 Å2
MethodPISA
3
E: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
F: N-acylethanolamine-hydrolyzing acid amidase beta-subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,6383
Polymers40,0672
Non-polymers5711
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5790 Å2
ΔGint-25 kcal/mol
Surface area13760 Å2
MethodPISA
4
G: N-acylethanolamine-hydrolyzing acid amidase alpha-subunit
H: N-acylethanolamine-hydrolyzing acid amidase beta-subunit


Theoretical massNumber of molelcules
Total (without water)40,0672
Polymers40,0672
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4900 Å2
ΔGint-37 kcal/mol
Surface area13970 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.614, 89.614, 207.058
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number78
Space group name H-MP43

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Components

#1: Protein
N-acylethanolamine-hydrolyzing acid amidase alpha-subunit


Mass: 13369.171 Da / Num. of mol.: 4 / Fragment: residues 19-121
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: CELE_Y55D5A.3, Y55D5A.3 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q9GUI1, N-(long-chain-acyl)ethanolamine deacylase
#2: Protein
N-acylethanolamine-hydrolyzing acid amidase beta-subunit


Mass: 26698.195 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: CELE_Y55D5A.3, Y55D5A.3 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9GUI1
#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 350 / 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: 2.59 Å3/Da / Density % sol: 52.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 0.2 M KNO3, 0.1M BIS-TRIS propane pH 8 and 20 % PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.97 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: May 23, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 45129 / % possible obs: 100 % / Redundancy: 15.2 % / Net I/σ(I): 23.4
Reflection shellResolution: 2.7→2.8 Å

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5U7Z

5u7z


Resolution: 2.7→44.824 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 22.01
RfactorNum. reflection% reflection
Rfree0.2153 1961 4.59 %
Rwork0.1684 --
obs0.1705 42696 95.62 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.7→44.824 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10931 0 76 350 11357
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00411281
X-RAY DIFFRACTIONf_angle_d0.61115332
X-RAY DIFFRACTIONf_dihedral_angle_d9.5236710
X-RAY DIFFRACTIONf_chiral_restr0.0441691
X-RAY DIFFRACTIONf_plane_restr0.0031968
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7001-2.76760.3056770.27411559X-RAY DIFFRACTION52
2.7676-2.84240.27941260.25142627X-RAY DIFFRACTION87
2.8424-2.9260.30221460.23983030X-RAY DIFFRACTION100
2.926-3.02040.29581490.22943052X-RAY DIFFRACTION100
3.0204-3.12840.27521490.20893033X-RAY DIFFRACTION100
3.1284-3.25360.24831460.23022X-RAY DIFFRACTION100
3.2536-3.40160.22761490.18653039X-RAY DIFFRACTION100
3.4016-3.58090.22831390.17263081X-RAY DIFFRACTION100
3.5809-3.80510.2161490.15833006X-RAY DIFFRACTION100
3.8051-4.09870.19831470.14573060X-RAY DIFFRACTION100
4.0987-4.51090.16821470.12613056X-RAY DIFFRACTION100
4.5109-5.16280.17131420.12493033X-RAY DIFFRACTION100
5.1628-6.50140.20191510.1653053X-RAY DIFFRACTION100
6.5014-44.82990.1921440.15653084X-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)
11.24230.6675-0.00280.3597-0.00350.00050.1398-0.01520.3313-0.28930.0449-0.5997-0.29740.432-0.14530.6362-0.0437-0.16760.5208-0.06890.64228.399284.1381-20.1248
22.2174-0.0027-0.06071.6314-0.00581.7392-0.08290.00310.6788-0.01630.10970.2129-0.7339-0.13720.18270.5293-0.0437-0.33220.1707-0.11920.99865.500891.2795-20.1421
32.1207-0.9949-0.05582.17950.4820.9025-0.25550.10350.2546-0.1609-0.0412-0.0932-0.29650.1128-0.1920.5487-0.1112-0.36530.2901-0.0180.94310.598790.5637-28.3324
40.34530.4418-0.11744.3091-0.60640.8136-0.25321.00810.2191-0.4688-0.0282-0.272-0.35230.42440.1320.5011-0.1224-0.17260.6767-0.06590.466311.664176.4509-35.0422
53.4571-0.76521.30322.5625-1.16651.5128-0.22290.41180.2766-0.04890.328-0.19020.08190.1596-0.07820.4295-0.141-0.11980.5098-0.14720.4828-2.337767.2088-35.1059
60.8133-0.9655-1.41452.30821.18883.8101-0.1370.10350.1034-0.05080.13130.4218-0.084-0.54290.0440.3530.0516-0.16260.3719-0.06890.866-9.465376.5329-25.8255
72.98111.282-2.20951.1435-1.60633.8496-0.09520.12620.3787-0.2201-0.14640.4724-0.3915-0.1241-0.06480.57130.1048-0.3520.3713-0.1540.7695-2.2285.8896-27.0198
80.5624-0.78640.85432.3797-1.79923.206-0.30260.3740.1936-0.3504-0.3302-0.156-0.25620.05380.12510.4252-0.0032-0.15180.5093-0.18730.47611.326977.4848-31.6068
91.57230.3015-0.81551-1.20441.6119-0.5378-0.0062-0.3285-0.3207-0.0306-0.10420.5778-0.0341-0.07410.3525-0.0375-0.02980.4939-0.22370.5059.051662.6841-28.2194
101.25060.40340.58211.2178-0.20881.1219-0.3207-0.17040.66430.14960.0682-0.0603-0.24030.12590.1640.3420.0611-0.14710.4065-0.31370.456712.334478.9024-13.7968
111.94640.85051.45240.60230.14122.2099-0.1249-0.1403-0.4680.12740.2843-0.0210.4334-0.01610.01560.26930.0679-0.04880.3818-0.21630.43951.880263.1824-19.9678
120.53150.04670.28091.038-0.30751.1283-0.1188-0.54360.66590.2247-0.01960.488-0.1266-0.26580.2070.40340.14430.00140.487-0.34890.5099-0.314576.0323-8.6217
131.6990.6041.06750.93340.33372.03020.0383-0.481-0.00210.3628-0.01820.37370.4201-0.4064-0.01120.35370.0189-0.00770.4732-0.18440.36633.222465.7776-6.5976
141.33490.482-0.12471.78050.17831.5082-0.2469-0.3526-0.47430.3186-0.0818-0.24690.21690.10920.31520.37980.1231-0.0920.3611-0.09770.414218.666260.5515-5.8955
150.88750.0444-0.08641.41910.0460.7923-0.1516-0.18080.32690.2884-0.1126-0.2414-0.2340.1639-0.06860.36280.0009-0.17120.3257-0.19670.43322.365576.2111-9.3551
160.52250.1218-0.07141.9869-0.32230.81640.13110.05920.6784-0.3896-0.0824-0.8651-0.13820.6484-0.06860.41310.00660.27490.6685-0.09141.151168.795385.6308-19.9793
171.5989-0.4972-0.05960.8459-0.16090.20450.1370.68320.5952-0.9155-0.1464-0.5149-0.33860.12840.08730.92280.18160.1610.44760.09930.473350.015896.9303-27.4668
181.40990.54530.04791.1443-0.07941.59750.4879-0.03770.5065-0.2136-0.2285-1.2668-0.53330.3274-0.03940.7162-0.05220.13320.3336-0.05861.027459.2632100.3824-17.8243
190.0608-0.1699-0.00590.6568-0.0072-0.00120.17570.0590.0451-0.3152-0.01760.45520.0823-0.2186-0.08730.69320.1533-0.07360.4015-0.04180.431841.131589.7921-23.7218
201.4391-0.2666-0.39791.80960.42591.1548-0.0408-0.19860.2627-0.06740.079-0.8961-0.09490.181-0.040.41860.1218-0.05190.3457-0.14030.623558.130679.9222-13.3785
210.7871-0.829-0.29162.1756-0.31190.5087-0.11130.04870.2771-0.09920.2266-0.2213-0.3952-0.0262-0.07330.52840.0738-0.11040.3231-0.10730.466442.352592.0028-13.1575
220.88020.4422-0.09410.3971-0.32191.09450.042-0.43450.49980.5650.1885-0.6675-0.27290.44070.860.56840.1083-0.36580.3904-0.33210.620853.232589.1786-2.6039
231.3598-0.7378-0.04032.4626-0.66611.2993-0.3997-0.23830.07710.75040.21680.02920.2098-0.25290.04380.5740.19-0.15770.4509-0.15630.344145.303881.4719-1.8773
242.0115-0.68650.57941.1114-0.05371.0738-0.19490.0216-0.32570.1975-0.12680.33950.1438-0.36230.34090.32810.01810.01080.3614-0.12950.395740.101970.254-9.4188
251.5385-0.0249-0.25261.11780.32070.8326-0.0456-0.01-0.32530.02570.0328-0.45780.32270.1960.03720.37830.1755-0.02810.3778-0.15720.549155.654368.9958-14.5309
265.8812-1.36010.95681.9115-0.19381.9199-0.27560.2526-0.47020.294-0.22450.09830.8313-0.66560.02910.5007-0.13960.07870.4043-0.25820.4189-23.616931.1716-40.5474
271.02170.85090.15451.86330.95621.3517-0.41230.3260.0085-0.5270.4444-0.2783-0.02820.39760.05180.4176-0.09650.02610.4178-0.18360.2842-13.067546.8539-43.6669
280.6955-0.34930.24731.0913-0.26534.3944-0.0447-0.0686-0.0940.35820.3539-0.88190.86470.2833-0.05250.34460.1232-0.03680.4483-0.18060.4097-5.838539.7667-36.2356
291.82440.19560.00150.9668-0.71721.3868-0.23620.21690.382-0.07880.00840.0377-0.2779-0.19270.19540.36850.0008-0.0310.3607-0.10840.3533-15.447453.9321-38.2964
301.75730.0325-0.56391.63560.21371.7102-0.16320.0195-0.21540.2787-0.19590.79360.5296-0.53720.18730.3908-0.15140.15560.4062-0.12530.4575-30.482142.1317-33.2534
312.23530.0295-0.37330.81180.26861.7036-0.2891-0.5629-0.14170.90690.11880.28770.5806-0.07640.13490.61820.01840.13560.417-0.03980.2741-20.912944.4676-23.6854
321.061-0.54831.13261.1675-0.3681.6496-0.6463-0.2289-0.04190.7103-0.29061.3852-0.3555-1.5863-0.71120.0215-0.27920.48880.7393-0.34740.8899-38.653946.3723-27.9725
331.24230.3985-0.25863.56882.27041.68020.18960.32180.0072-0.68660.18130.1513-0.42150.12020.10361.15370.0929-0.45350.43850.0460.537910.727131.671-24.1727
340.44670.37670.41930.65850.70210.75290.30040.712-0.4637-0.82530.15190.35870.2033-0.36230.41111.32670.0263-0.83090.5597-0.07510.55518.913115.0817-29.8218
350.8986-0.42831.49780.2014-0.69722.5096-0.00920.25260.1832-1.1152-0.0875-0.34-0.38470.28750.13961.17920.09480.19610.4645-0.0060.483228.2059121.186-29.5519
364.07860.5012-0.88590.8637-0.14241.33970.7760.43550.0132-0.7181-0.24170.28330.1510.061-0.30880.71620.0854-0.15680.3296-0.02260.440229.6178104.6827-23.7025
371.57640.1429-0.44322.282-0.37181.56640.60520.0313-0.1323-1.2705-0.341-0.2399-0.2598-0.034-0.27771.0169-0.0085-0.12620.1895-0.18740.405924.9863112.2718-23.745
381.6164-0.58850.60963.0757-0.08332.30960.0821-0.2639-0.2993-0.83410.00720.6429-0.2036-0.3169-0.110.41220.0484-0.17750.3262-0.03150.394113.125122.8239-14.4709
390.8563-1.05160.1592.8663-0.2891.7056-0.0523-0.366-0.34740.07090.32070.33890.1194-0.1275-0.24170.32840.0255-0.12740.38570.04730.374919.7829111.9121-5.8039
401.5589-0.1097-0.48862.9093-1.09523.1087-0.0869-0.49070.16550.64230.2465-0.1955-0.57140.0781-0.14930.50580.0775-0.17160.3855-0.14410.410717.4697131.1496-4.1349
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 17 through 21 )
2X-RAY DIFFRACTION2chain 'A' and (resid 22 through 37 )
3X-RAY DIFFRACTION3chain 'A' and (resid 38 through 44 )
4X-RAY DIFFRACTION4chain 'A' and (resid 45 through 58 )
5X-RAY DIFFRACTION5chain 'A' and (resid 59 through 72 )
6X-RAY DIFFRACTION6chain 'A' and (resid 73 through 79 )
7X-RAY DIFFRACTION7chain 'A' and (resid 80 through 93 )
8X-RAY DIFFRACTION8chain 'A' and (resid 94 through 105 )
9X-RAY DIFFRACTION9chain 'A' and (resid 106 through 118 )
10X-RAY DIFFRACTION10chain 'B' and (resid 122 through 184 )
11X-RAY DIFFRACTION11chain 'B' and (resid 185 through 210 )
12X-RAY DIFFRACTION12chain 'B' and (resid 211 through 235 )
13X-RAY DIFFRACTION13chain 'B' and (resid 236 through 270 )
14X-RAY DIFFRACTION14chain 'B' and (resid 271 through 306 )
15X-RAY DIFFRACTION15chain 'B' and (resid 307 through 355 )
16X-RAY DIFFRACTION16chain 'C' and (resid 17 through 44 )
17X-RAY DIFFRACTION17chain 'C' and (resid 45 through 72 )
18X-RAY DIFFRACTION18chain 'C' and (resid 73 through 105 )
19X-RAY DIFFRACTION19chain 'C' and (resid 106 through 118 )
20X-RAY DIFFRACTION20chain 'D' and (resid 122 through 184 )
21X-RAY DIFFRACTION21chain 'D' and (resid 185 through 210 )
22X-RAY DIFFRACTION22chain 'D' and (resid 211 through 242 )
23X-RAY DIFFRACTION23chain 'D' and (resid 243 through 270 )
24X-RAY DIFFRACTION24chain 'D' and (resid 271 through 306 )
25X-RAY DIFFRACTION25chain 'D' and (resid 307 through 355 )
26X-RAY DIFFRACTION26chain 'E' and (resid 19 through 32 )
27X-RAY DIFFRACTION27chain 'E' and (resid 33 through 71 )
28X-RAY DIFFRACTION28chain 'E' and (resid 72 through 93 )
29X-RAY DIFFRACTION29chain 'E' and (resid 94 through 118 )
30X-RAY DIFFRACTION30chain 'F' and (resid 122 through 159 )
31X-RAY DIFFRACTION31chain 'F' and (resid 160 through 270 )
32X-RAY DIFFRACTION32chain 'F' and (resid 271 through 355 )
33X-RAY DIFFRACTION33chain 'G' and (resid 17 through 26 )
34X-RAY DIFFRACTION34chain 'G' and (resid 27 through 44 )
35X-RAY DIFFRACTION35chain 'G' and (resid 45 through 58 )
36X-RAY DIFFRACTION36chain 'G' and (resid 59 through 79 )
37X-RAY DIFFRACTION37chain 'G' and (resid 80 through 118 )
38X-RAY DIFFRACTION38chain 'H' and (resid 122 through 184 )
39X-RAY DIFFRACTION39chain 'H' and (resid 185 through 270 )
40X-RAY DIFFRACTION40chain 'H' and (resid 271 through 355 )

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