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- PDB-5w58: Crystal Complex of Cyclooxygenase-2: (S)-ARN-2508 (a dual COX and... -

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Basic information

Entry
Database: PDB / ID: 5w58
TitleCrystal Complex of Cyclooxygenase-2: (S)-ARN-2508 (a dual COX and FAAH inhibitor)
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE/INHIBITOR / cyclooxygenase / protein-inhibitor complex / prostaglandin / FAAH-COX dual inhibition / OXIDOREDUCTASE / OXIDOREDUCTASE-INHIBITOR complex
Function / homology
Function and homology information


Biosynthesis of DHA-derived SPMs / Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of electrophilic ω-3 PUFA oxo-derivatives / Synthesis of 15-eicosatetraenoic acid derivatives / cellular response to non-ionic osmotic stress / positive regulation of platelet-derived growth factor production / hair cycle / cellular response to homocysteine / Nicotinamide salvaging ...Biosynthesis of DHA-derived SPMs / Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of electrophilic ω-3 PUFA oxo-derivatives / Synthesis of 15-eicosatetraenoic acid derivatives / cellular response to non-ionic osmotic stress / positive regulation of platelet-derived growth factor production / hair cycle / cellular response to homocysteine / Nicotinamide salvaging / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / positive regulation of fibroblast growth factor production / prostaglandin-endoperoxide synthase / prostaglandin-endoperoxide synthase activity / negative regulation of synaptic transmission, dopaminergic / cellular response to lead ion / response to nematode / positive regulation of transforming growth factor beta production / negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress / positive regulation of prostaglandin biosynthetic process / positive regulation of synaptic plasticity / regulation of neuroinflammatory response / response to fructose / cyclooxygenase pathway / positive regulation of smooth muscle contraction / response to fatty acid / positive regulation of fever generation / response to vitamin D / cellular response to fluid shear stress / prostaglandin secretion / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / response to manganese ion / nuclear outer membrane / response to angiotensin / nuclear inner membrane / negative regulation of smooth muscle contraction / prostaglandin biosynthetic process / positive regulation of cell migration involved in sprouting angiogenesis / cellular response to ATP / maintenance of blood-brain barrier / bone mineralization / negative regulation of calcium ion transport / decidualization / negative regulation of cell cycle / positive regulation of vascular endothelial growth factor production / response to tumor necrosis factor / brown fat cell differentiation / response to glucocorticoid / positive regulation of vasoconstriction / keratinocyte differentiation / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / : / response to cytokine / learning / positive regulation of smooth muscle cell proliferation / peroxidase activity / caveola / memory / regulation of blood pressure / cellular response to mechanical stimulus / positive regulation of protein import into nucleus / positive regulation of nitric oxide biosynthetic process / positive regulation of peptidyl-serine phosphorylation / response to estradiol / regulation of cell population proliferation / cellular response to heat / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / neuron projection / positive regulation of apoptotic process / response to xenobiotic stimulus / negative regulation of cell population proliferation / positive regulation of cell population proliferation / heme binding / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / protein homodimerization activity / protein-containing complex / metal ion binding / cytoplasm
Similarity search - Function
: / Myeloperoxidase, subunit C / Haem peroxidase domain superfamily, animal type / Haem peroxidase, animal-type / Haem peroxidase domain superfamily, animal type / Animal haem peroxidase / Animal heme peroxidase superfamily profile. / Laminin / Laminin / EGF-like domain ...: / Myeloperoxidase, subunit C / Haem peroxidase domain superfamily, animal type / Haem peroxidase, animal-type / Haem peroxidase domain superfamily, animal type / Animal haem peroxidase / Animal heme peroxidase superfamily profile. / Laminin / Laminin / EGF-like domain / Haem peroxidase superfamily / EGF-like domain profile. / EGF-like domain / Ribbon / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
triacetyl-beta-chitotriose / Chem-FF8 / PROTOPORPHYRIN IX CONTAINING FE / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.267 Å
AuthorsXu, S. / Goodman, M.C. / Banerjee, S. / Piomelli, D. / Marnett, L.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)CA89450 United States
CitationJournal: J. Biol. Chem. / Year: 2018
Title: Dual cyclooxygenase-fatty acid amide hydrolase inhibitor exploits novel binding interactions in the cyclooxygenase active site.
Authors: Goodman, M.C. / Xu, S. / Rouzer, C.A. / Banerjee, S. / Ghebreselasie, K. / Migliore, M. / Piomelli, D. / Marnett, L.J.
History
DepositionJun 14, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 31, 2018Provider: repository / Type: Initial release
Revision 1.1Mar 14, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
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 / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _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
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: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,9918
Polymers67,3331
Non-polymers2,6597
Water4,936274
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A: Prostaglandin G/H synthase 2
hetero molecules

A: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,98316
Polymers134,6652
Non-polymers5,31714
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_544x,-y-1/2,-z-3/41
Buried area12720 Å2
ΔGint-4 kcal/mol
Surface area43320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)173.774, 173.774, 203.304
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122
Components on special symmetry positions
IDModelComponents
11A-860-

HOH

21A-1073-

HOH

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Prostaglandin G/H synthase 2 / Cyclooxygenase-2 / COX-2 / Glucocorticoid-regulated inflammatory cyclooxygenase / Gripghs / ...Cyclooxygenase-2 / COX-2 / Glucocorticoid-regulated inflammatory cyclooxygenase / Gripghs / Macrophage activation-associated marker protein P71/73 / PES-2 / PHS II / Prostaglandin H2 synthase 2 / PGHS-2 / Prostaglandin-endoperoxide synthase 2 / TIS10 protein


Mass: 67332.711 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Plasmid: pVL-1393-COX-2 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 3 types, 5 molecules

#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / triacetyl-beta-chitotriose


Type: oligosaccharide, Oligosaccharide / Class: Inhibitor / Mass: 627.594 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: oligosaccharide / References: triacetyl-beta-chitotriose
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,3,2/[a2122h-1b_1-5_2*NCC/3=O]/1-1-1/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}}LINUCSPDB-CARE
#3: 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
#4: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 3 types, 276 molecules

#5: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C34H32FeN4O4
#6: Chemical ChemComp-FF8 / (2S)-2-{2-fluoro-3'-[(hexylcarbamoyl)oxy][1,1'-biphenyl]-4-yl}propanoic acid


Mass: 387.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C22H26FNO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 274 / 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: 5.7 Å3/Da / Density % sol: 78.42 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: COX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM ...Details: COX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM DMSO stocks were added to protein samples. Mixing 3.5 uL of the protein-inhibitor complex with 3.5 uL crystallization solution containing 50 mM EPPS, pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550 against reservoir solutions comprised of 50 mM EPPS pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 2, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.267→132.1 Å / Num. obs: 71762 / % possible obs: 99.8 % / Redundancy: 14.6 % / Biso Wilson estimate: 47.97 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.155 / Rpim(I) all: 0.042 / Rrim(I) all: 0.161 / Net I/σ(I): 19.4
Reflection shellResolution: 2.27→2.32 Å / Redundancy: 14.2 % / CC1/2: 0.311 / Rpim(I) all: 1.136 / Rrim(I) all: 4.323 / % possible all: 96.5

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
Aimless0.5.21data scaling
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NT1

3nt1


Resolution: 2.267→66.048 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 21.44
RfactorNum. reflection% reflection
Rfree0.1886 2145 3 %
Rwork0.1691 --
obs0.1697 71469 99.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.267→66.048 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4512 0 181 276 4969
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0214842
X-RAY DIFFRACTIONf_angle_d1.276586
X-RAY DIFFRACTIONf_dihedral_angle_d20.891816
X-RAY DIFFRACTIONf_chiral_restr0.203702
X-RAY DIFFRACTIONf_plane_restr0.006838
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2669-2.31960.33361330.3334273X-RAY DIFFRACTION93
2.3196-2.37760.38851400.30214546X-RAY DIFFRACTION99
2.3776-2.44190.29071420.26574592X-RAY DIFFRACTION100
2.4419-2.51380.25341420.24894587X-RAY DIFFRACTION100
2.5138-2.59490.26711430.23744609X-RAY DIFFRACTION100
2.5949-2.68760.27231410.22224603X-RAY DIFFRACTION100
2.6876-2.79530.24861430.19714607X-RAY DIFFRACTION100
2.7953-2.92250.21981430.19074611X-RAY DIFFRACTION100
2.9225-3.07650.19781430.18434639X-RAY DIFFRACTION100
3.0765-3.26930.23561440.18064633X-RAY DIFFRACTION100
3.2693-3.52170.20771440.16634647X-RAY DIFFRACTION100
3.5217-3.87610.15441440.13664656X-RAY DIFFRACTION100
3.8761-4.43680.13271440.12754696X-RAY DIFFRACTION100
4.4368-5.58950.12941460.12484722X-RAY DIFFRACTION100
5.5895-66.07560.16821530.16454903X-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)
18.2723-0.8224-5.53163.41450.00697.2940.3181-0.63140.01140.5693-0.10510.2838-0.2635-0.0389-0.24450.73210.0048-0.05470.4693-0.02350.46252.8378-37.2447-48.8797
24.97324.8945-6.47614.8263-6.35738.4403-0.0891-0.85770.18611.1067-0.2917-0.103-0.29730.65440.29220.80120.0264-0.02570.56150.03210.46721.1996-45.3675-45.051
37.23632.18822.55998.99131.73228.3093-0.2359-0.39920.03841.1131-0.0634-0.86950.14460.57560.28930.53440.0047-0.15350.4150.03750.442814.9112-40.9254-52.3807
42.485-3.26542.88574.3315-3.86783.4305-0.1398-0.48640.23110.4946-0.3262-1.1321-0.45160.26060.49830.463-0.0771-0.12020.71310.08940.785220.7972-27.5298-60.1226
53.46662.9462-0.59065.1213.00318.2657-0.05160.19830.1548-0.22770.2432-0.4233-0.2650.8445-0.25060.3589-0.0577-0.05130.50610.05560.508819.8094-18.628-78.1673
68.54892.771-6.07517.5976-0.52654.6270.0575-0.8581-0.17480.5501-0.4222-1.12540.2260.54530.44040.4176-0.0171-0.11110.42020.03420.464811.8578-30.986-70.5564
71.4192-0.0499-0.42312.36110.02211.3796-0.1402-0.0731-0.33660.45950.05780.09840.060.09360.07410.50350.01680.01360.36020.01690.4059-6.2457-40.0033-62.6557
82.6834-2.79342.15654.3844-4.66975.7843-0.0368-0.4578-0.19391.03150.41060.6426-0.4607-0.183-0.43530.76480.06140.11620.499-0.01250.5119-10.0973-21.195-48.0751
96.6291-0.2133-4.95382.48720.72087.46290.4032-0.28260.22950.22480.09780.2654-0.79450.0996-0.50260.563-0.02420.0230.35530.00070.4993-3.6099-3.8786-67.0127
100.2312-0.3108-0.29741.5372-0.69421.441-0.0332-0.03550.01260.14440.08970.33470.1461-0.159-0.04680.4344-0.00690.020.37540.01930.452-11.7866-26.608-76.8486
112.2895-1.92851.23088.5461-0.53832.30340.00380.23370.1415-0.3135-0.00480.70770.0318-0.10430.01940.3237-0.0377-0.04680.39520.05720.4496-19.4835-24.7858-95.2331
125.7401-1.2772-0.80214.1014.67155.4092-0.1263-0.08430.2682-0.58750.06621.3398-0.4656-0.69730.32760.52720.0052-0.01960.58660.12090.79-28.2506-22.1953-84.1621
134.5038-6.32321.99089.4675-2.02852.21460.12470.0213-0.2354-0.23110.25251.6976-0.2007-0.3017-0.48350.49170.0093-0.03880.44030.06430.772-23.9442-19.5281-84.6121
140.75770.30030.25062.12470.26830.6588-0.0940.12750.093-0.17870.04180.2085-0.0634-0.03140.04270.395-0.0091-0.02040.35940.07090.3565-6.0484-25.2468-91.8528
155.12952.98182.60745.42624.62193.9442-0.11930.27950.1876-0.25740.2345-0.0445-0.44990.299-0.10180.4839-0.03530.03040.40190.06860.39312.1592-24.0357-80.9971
160.42570.2391-0.43983.54730.31791.0709-0.0354-0.11150.04070.02120.0395-0.0422-0.02340.1128-0.00230.454-0.0043-0.04190.36750.00840.3894-0.6539-28.8177-71.6522
174.7514-0.8283-0.391.3172.04484.16290.08130.06390.3406-0.0562-0.09260.2437-0.3706-0.2898-0.00460.51470.04440.01380.35570.05560.5846-15.3873-4.9506-82.0847
181.183-0.00430.17482.5381-0.23611.31710.0154-0.25320.11590.71050.0070.015-0.18640.0016-0.01290.60510.00010.01750.3828-0.03380.3416-2.8613-17.3955-55.4939
190.85240.11820.38120.5508-0.06171.7603-0.0330.09280.09940.0313-0.0004-0.0642-0.06470.15270.04380.3491-0.0140.0080.29120.03690.37752.6285-24.0095-83.8749
207.0216-4.6024-1.5496.936-2.14612.88690.0154-0.28350.52880.4440.3299-0.4598-0.71160.4729-0.41290.4892-0.0265-0.0120.393-0.0040.45082.0422-7.2338-80.8101
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 33:45)
2X-RAY DIFFRACTION2(chain A and resid 46:56)
3X-RAY DIFFRACTION3(chain A and resid 57:74)
4X-RAY DIFFRACTION4(chain A and resid 75:89)
5X-RAY DIFFRACTION5(chain A and resid 90:114)
6X-RAY DIFFRACTION6(chain A and resid 115:123)
7X-RAY DIFFRACTION7(chain A and resid 124:156)
8X-RAY DIFFRACTION8(chain A and resid 157:183)
9X-RAY DIFFRACTION9(chain A and resid 184:193)
10X-RAY DIFFRACTION10(chain A and resid 194:239)
11X-RAY DIFFRACTION11(chain A and resid 240:266)
12X-RAY DIFFRACTION12(chain A and resid 267:278)
13X-RAY DIFFRACTION13(chain A and resid 279:292)
14X-RAY DIFFRACTION14(chain A and resid 293:352)
15X-RAY DIFFRACTION15(chain A and resid 353:366)
16X-RAY DIFFRACTION16(chain A and resid 367:391)
17X-RAY DIFFRACTION17(chain A and resid 392:429)
18X-RAY DIFFRACTION18(chain A and resid 430:511)
19X-RAY DIFFRACTION19(chain A and resid 512:578)
20X-RAY DIFFRACTION20(chain A and resid 579:583)

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