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- PDB-5f1a: The Crystal Structure of Salicylate Bound to Human Cyclooxygenase-2 -

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Basic information

Entry
Database: PDB / ID: 5f1a
TitleThe Crystal Structure of Salicylate Bound to Human Cyclooxygenase-2
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE/INHIBITOR / Membrane Protein / Monotopic / Cyclooxygenase / Cyclooxygenase-2 / COX / PGHS / Salicylic acid / Salicylate / Inhibitor / Complex / OXIDOREDUCTASE-INHIBITOR complex
Function / homology
Function and homology information


Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of DHA-derived 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 / positive regulation of fibroblast growth factor production ...Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of DHA-derived 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 / 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 / regulation of neuroinflammatory response / positive regulation of synaptic plasticity / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / positive regulation of smooth muscle contraction / Nicotinamide salvaging / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / cyclooxygenase pathway / response to fatty acid / response to fructose / positive regulation of fever generation / prostaglandin secretion / response to vitamin D / cellular response to fluid shear stress / nuclear outer membrane / response to angiotensin / response to manganese ion / prostaglandin biosynthetic process / nuclear inner membrane / negative regulation of smooth muscle contraction / cellular response to ATP / positive regulation of cell migration involved in sprouting angiogenesis / maintenance of blood-brain barrier / bone mineralization / Interleukin-10 signaling / 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 / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / learning / caveola / positive regulation of smooth muscle cell proliferation / memory / regulation of blood pressure / positive regulation of protein import into nucleus / peroxidase activity / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / positive regulation of peptidyl-serine phosphorylation / response to estradiol / cellular response to heat / regulation of inflammatory response / cellular response to hypoxia / angiogenesis / Interleukin-4 and Interleukin-13 signaling / response to oxidative stress / response to lipopolysaccharide / response to xenobiotic stimulus / neuron projection / positive regulation of apoptotic process / negative regulation of cell population proliferation / endoplasmic reticulum lumen / heme binding / endoplasmic reticulum membrane / enzyme binding / endoplasmic reticulum / 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 / Haem peroxidase superfamily ...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
ACRYLIC ACID / PROTOPORPHYRIN IX CONTAINING CO / 2-HYDROXYBENZOIC ACID / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.38 Å
AuthorsLucido, M.J. / Orlando, B.J. / Malkowski, M.G.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM077176 United States
CitationJournal: Biochemistry / Year: 2016
Title: Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry.
Authors: Lucido, M.J. / Orlando, B.J. / Vecchio, A.J. / Malkowski, M.G.
History
DepositionNov 30, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2017Group: Author supporting evidence / Derived calculations / Refinement description
Category: pdbx_audit_support / pdbx_struct_oper_list / software
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.2Nov 20, 2019Group: Derived calculations / Category: pdbx_struct_conn_angle / struct_conn
Revision 1.3Dec 25, 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 / atom_site_anisotrop ...atom_site / atom_site_anisotrop / 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_struct_conn_angle / 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 / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _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 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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

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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
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,67220
Polymers127,3392
Non-polymers4,33318
Water7,044391
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12560 Å2
ΔGint4 kcal/mol
Surface area41680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)118.410, 132.660, 178.740
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number23
Space group name H-MI222

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Prostaglandin G/H synthase 2 / Cyclooxygenase-2 / COX-2 / PHS II / Prostaglandin H2 synthase 2 / PGHS-2 / Prostaglandin- ...Cyclooxygenase-2 / COX-2 / PHS II / Prostaglandin H2 synthase 2 / PGHS-2 / Prostaglandin-endoperoxide synthase 2


Mass: 63669.602 Da / Num. of mol.: 2 / Mutation: N594A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PTGS2, COX2 / Plasmid: pFastBac1 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf21
References: UniProt: P35354, prostaglandin-endoperoxide synthase

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Sugars , 4 types, 6 molecules

#2: Polysaccharide alpha-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-4)-alpha-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: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2/a4-b1_b4-c1_c4-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(4+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...alpha-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: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
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
#9: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 5 types, 403 molecules

#4: Chemical ChemComp-SAL / 2-HYDROXYBENZOIC ACID / SALICYLIC ACID


Mass: 138.121 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H6O3
#5: Chemical ChemComp-COH / PROTOPORPHYRIN IX CONTAINING CO


Mass: 619.575 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32CoN4O4
#7: Chemical ChemComp-AKR / ACRYLIC ACID


Mass: 72.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H4O2
#8: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 391 / 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: 2.76 Å3/Da / Density % sol: 55.37 %
Crystal growTemperature: 296 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 22-34% PAA-5100, 100mM HEPES (pH 7.5), 20mM MgCl2, 0.6% BOG

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1.033 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 23, 2014
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 2.34→34.75 Å / Num. obs: 59216 / % possible obs: 99.5 % / Redundancy: 4.1 % / Biso Wilson estimate: 34.51 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.112 / Rpim(I) all: 0.061 / Net I/σ(I): 9.1 / Num. measured all: 241855 / Scaling rejects: 49
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) all% possible all
2.34-2.440.722.11796145410.7010.40399.4
10.2-34.753.90.03422.430967840.9980.01997.4

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
Aimless0.3.11data scaling
PHASER2.5.6phasing
PHENIX1.9-1692refinement
PDB_EXTRACT3.15data extraction
Coot0.8.1model building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.38→33.324 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 21.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2181 2791 4.96 %
Rwork0.1737 53506 -
obs0.1759 56297 99.46 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 105.09 Å2 / Biso mean: 44.1034 Å2 / Biso min: 19.61 Å2
Refinement stepCycle: final / Resolution: 2.38→33.324 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8893 0 292 391 9576
Biso mean--62.45 41.77 -
Num. residues----1105
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0059502
X-RAY DIFFRACTIONf_angle_d0.92212915
X-RAY DIFFRACTIONf_chiral_restr0.0391368
X-RAY DIFFRACTIONf_plane_restr0.0051662
X-RAY DIFFRACTIONf_dihedral_angle_d14.9073481
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.38-2.4210.28581420.24892628277099
2.421-2.46510.25171500.24342640279099
2.4651-2.51250.27121470.22212619276699
2.5125-2.56370.26561340.21842653278799
2.5637-2.61940.28311490.21412629277899
2.6194-2.68040.23761330.198726682801100
2.6804-2.74740.24051160.19892675279199
2.7474-2.82160.19851080.1982682279099
2.8216-2.90460.27921330.20112641277499
2.9046-2.99830.2131420.19452661280399
2.9983-3.10540.24171360.19292641277799
3.1054-3.22960.22291690.18672670283999
3.2296-3.37640.22871740.18352610278499
3.3764-3.55430.22721380.168826752813100
3.5543-3.77670.19171370.151126892826100
3.7767-4.06780.19621070.144827422849100
4.0678-4.47630.2121070.142427242831100
4.4763-5.1220.17041580.13242691284999
5.122-6.44550.20151470.166327282875100
6.4455-33.32750.20711640.171628403004100
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)
10.4266-0.36021.19551.8559-0.7193.41020.3103-0.4017-0.55190.3074-0.038-0.14980.8199-0.2932-0.17050.6837-0.0273-0.01340.25140.02710.491325.67911.2086230.6416
20.2485-0.2495-0.15330.85140.3251.3290.1819-0.1026-0.50380.0945-0.15150.11630.40430.3261-0.11470.5660.2019-0.12290.43480.08980.663853.26459.4212241.9511
36.21181.33432.51040.85250.32342.2490.3220.4345-0.84790.139-0.0936-0.29450.56150.3705-0.15790.40690.08710.01150.30790.00810.334840.870516.2565229.1303
41.16360.13240.32240.73040.40891.79730.0383-0.3183-0.04110.2473-0.17620.14270.2378-0.3350.11870.2965-0.01640.05340.26930.01990.228328.353324.9099242.5273
51.46121.19840.07853.3734-0.1831.7597-0.09430.12390.54820.0559-0.09310.2344-0.38020.08140.16090.26520.0082-0.06760.21980.07690.338536.021245.2931228.0506
62.50820.0743-0.61382.86930.31854.1122-0.14010.13510.35490.1455-0.10030.1498-0.54630.15850.20450.2934-0.0711-0.11530.19610.02950.348939.528349.0679233.5236
71.45240.38740.72391.49020.02881.94140.00070.131-0.03280.04120.0005-0.14710.10350.5240.01390.19910.05080.01240.29450.02960.191346.376630.0716230.2671
87.1478-1.0543-2.90364.2205-1.88582.9449-0.1024-0.49350.83820.35950.10050.1372-0.33590.05810.01470.35-0.0425-0.04770.3134-0.09480.295440.447.951250.5421
91.47220.37491.07680.69750.51142.20320.1313-0.4262-0.17430.2805-0.10050.0830.3868-0.2168-0.04690.4247-0.05620.05330.34790.06420.258529.824820.142247.9261
102.28560.09480.40931.7525-0.5693.54250.1305-0.4932-0.43950.4911-0.2822-0.07110.4367-0.23950.15260.4818-0.0564-0.01270.28110.04390.245634.219418.4016247.5369
110.85480.76141.28750.64990.72822.4766-0.01140.09240.12880.1223-0.0258-0.05460.06030.5031-0.00720.25550.03730.01210.34230.05390.297846.642336.493231.6985
121.44770.17790.57280.58290.98552.4644-0.03670.2478-0.3525-0.17430.1602-0.36140.30431.1392-0.13830.44750.24590.06270.99110.0590.445656.139321.3962200.765
130.86571.55220.10266.94250.66361.79270.00820.2063-0.27860.0297-0.1545-0.7250.43150.87090.10350.37230.19220.05590.58410.0810.351644.757319.0575207.0212
140.5853-0.4258-0.82290.7907-0.09582.2182-0.01930.35570.1256-0.118-0.059-0.0925-0.6280.61940.00610.3266-0.1056-0.01070.56830.10940.276842.877238.8375196.5274
151.67641.0103-0.52831.4279-1.28773.1145-0.11120.2937-0.0532-0.24670.0275-0.14160.5540.30580.07820.34110.08980.0740.4148-0.04020.262528.518119.5479186.9561
168.49252.69580.02291.1258-0.18012.0127-0.19590.31080.2254-0.06150.09370.1836-0.0202-0.18370.08970.26180.06980.02640.2473-0.02270.230215.909424.4052206.5749
171.98980.5781-0.29750.7137-0.40462.08410.04020.3118-0.0797-0.1566-0.06530.00320.2847-0.08470.0340.29550.06850.0190.2185-0.05770.229823.538616.4036203.766
184.8863-0.0227-2.3452.5475-3.38715.6790.10220.88610.0403-0.71560.07140.24960.1744-0.8893-0.19250.4608-0.0015-0.01050.6819-0.08250.281414.034419.0287184.3181
190.69090.52910.04970.8847-0.23382.1544-0.08130.3631-0.1619-0.2838-0.0728-0.12770.21720.54250.16890.34440.1220.06320.4977-0.01530.310237.200720.9603193.1102
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 33 through 73 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 74 through 105a)A0
3X-RAY DIFFRACTION3chain 'A' and (resid 106 through 138 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 139 through 208 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 209 through 269 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 270 through 319 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 320 through 390 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 391 through 428 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 429 through 485 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 486 through 535 )A0
11X-RAY DIFFRACTION11chain 'A' and (resid 536 through 584 )A0
12X-RAY DIFFRACTION12chain 'B' and (resid 33 through 105a)B0
13X-RAY DIFFRACTION13chain 'B' and (resid 106 through 138 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 139 through 181 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 182 through 208 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 209 through 269 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 270 through 390 )B0
18X-RAY DIFFRACTION18chain 'B' and (resid 391 through 428 )B0
19X-RAY DIFFRACTION19chain 'B' and (resid 429 through 583 )B0

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