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- PDB-6f5m: Crystal structure of highly glycosylated human leukocyte elastase... -

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Basic information

Entry
Database: PDB / ID: 6f5m
TitleCrystal structure of highly glycosylated human leukocyte elastase in complex with a thiazolidinedione inhibitor
ComponentsNeutrophil elastase
KeywordsHYDROLASE / human leukocyte elastase / human neutrophil elastase / parabolic inhibition / glycosylation
Function / homology
Function and homology information


leukocyte elastase / biosynthetic process of antibacterial peptides active against Gram-negative bacteria / neutrophil-mediated killing of fungus / Expression of NOTCH2NL genes / negative regulation of chemotaxis / acute inflammatory response to antigenic stimulus / positive regulation of leukocyte tethering or rolling / response to yeast / leukocyte migration involved in inflammatory response / negative regulation of interleukin-8 production ...leukocyte elastase / biosynthetic process of antibacterial peptides active against Gram-negative bacteria / neutrophil-mediated killing of fungus / Expression of NOTCH2NL genes / negative regulation of chemotaxis / acute inflammatory response to antigenic stimulus / positive regulation of leukocyte tethering or rolling / response to yeast / leukocyte migration involved in inflammatory response / negative regulation of interleukin-8 production / negative regulation of chemokine production / Antimicrobial peptides / pyroptotic inflammatory response / Activation of Matrix Metalloproteinases / cytokine binding / neutrophil-mediated killing of gram-negative bacterium / Collagen degradation / extracellular matrix disassembly / Pyroptosis / phagocytosis / response to UV / phagocytic vesicle / Degradation of the extracellular matrix / transcription repressor complex / positive regulation of MAP kinase activity / secretory granule / Regulation of Complement cascade / positive regulation of interleukin-8 production / positive regulation of smooth muscle cell proliferation / protein catabolic process / positive regulation of immune response / negative regulation of inflammatory response / specific granule lumen / intracellular calcium ion homeostasis / transcription corepressor activity / azurophil granule lumen / peptidase activity / heparin binding / protease binding / : / endopeptidase activity / response to lipopolysaccharide / defense response to bacterium / serine-type endopeptidase activity / intracellular membrane-bounded organelle / Neutrophil degranulation / negative regulation of transcription by RNA polymerase II / cell surface / Golgi apparatus / proteolysis / extracellular space / extracellular exosome / extracellular region / cytosol / cytoplasm
Similarity search - Function
: / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin ...: / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / Chem-CQH / Neutrophil elastase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsHochscherf, J. / Pietsch, M. / Tieu, W. / Kuan, K. / Hautmann, S. / Abell, A. / Guetschow, M. / Niefind, K.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationNI 643/4-1 Germany
Citation
Journal: Acta Crystallogr F Struct Biol Commun / Year: 2018
Title: Crystal structure of highly glycosylated human leukocyte elastase in complex with an S2' site binding inhibitor.
Authors: Hochscherf, J. / Pietsch, M. / Tieu, W. / Kuan, K. / Abell, A.D. / Gutschow, M. / Niefind, K.
#1: Journal: J. Mol. Biol. / Year: 2011
Title: Unexpected active-site flexibility in the structure of human neutrophil elastase in complex with a new dihydropyrimidone inhibitor.
Authors: Hansen, G. / Gielen-Haertwig, H. / Reinemer, P. / Schomburg, D. / Harrenga, A. / Niefind, K.
#2: Journal: Bioorg. Med. Chem. Lett. / Year: 2012
Title: 5-benzylidenerhodanine and 5-benzylidene-2-4-thiazolidinedione based antibacterials.
Authors: Zvarec, O. / Polyak, S.W. / Tieu, W. / Kuan, K. / Dai, H. / Pedersen, D.S. / Morona, R. / Zhang, L. / Booker, G.W. / Abell, A.D.
History
DepositionDec 1, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 8, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 15, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.page_first ..._citation.journal_abbrev / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
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_special_symmetry / 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.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _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 2.1Jan 17, 2024Group: 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
Revision 2.2Nov 20, 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: Neutrophil elastase
B: Neutrophil elastase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)51,57615
Polymers46,6382
Non-polymers4,93813
Water79344
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A: Neutrophil elastase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,7368
Polymers23,3191
Non-polymers2,4177
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Neutrophil elastase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,8397
Polymers23,3191
Non-polymers2,5206
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)204.557, 204.557, 62.155
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number155
Space group name H-MH32
Components on special symmetry positions
IDModelComponents
11A-518-

HOH

21B-517-

HOH

31B-521-

HOH

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Neutrophil elastase / Bone marrow serine protease / Elastase-2 / Human leukocyte elastase / HLE / Medullasin / PMN elastase


Mass: 23318.982 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08246, leukocyte elastase

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Sugars , 3 types, 4 molecules

#2: 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)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 894.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-4/a4-b1_a6-e1_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]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: 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)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1056.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_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]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE

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Non-polymers , 4 types, 53 molecules

#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Formula: C2H3O2
#7: Chemical ChemComp-CQH / 5-[[4-[[(2~{S})-4-methyl-1-oxidanylidene-1-[(2-propylphenyl)amino]pentan-2-yl]carbamoyl]phenyl]methyl]-2-oxidanylidene-1,3-thiazol-1-ium-4-olate


Mass: 479.591 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H29N3O4S
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 44 / 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: 2.68 Å3/Da / Density % sol: 54.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: HLE from human blood was purchased from SERVA as a lyophilisate in the presence of sodium acetate puffer, pH 5.5. The lyophilisate was disolved in water so that the HLE concentration was 5 ...Details: HLE from human blood was purchased from SERVA as a lyophilisate in the presence of sodium acetate puffer, pH 5.5. The lyophilisate was disolved in water so that the HLE concentration was 5 mg/ml (170 micromolar) and the acetate concentration 250 millimolar. 120 microliter dissolved HNE lysophilisate was mixed with 6 microliter inhibitor solution (10 mM in DMSO). 1 microliter of the resulting HLE/inhibitor mixture was mixed with 0.5 microliter reservoir solution which was composed of 20 % PEG MME 5000, 0.2 M potassium sulphate. Repeated seeding was necessary to get usable crystals. In the final seeding step the reservoir was composed of 20 % PEG MME 5000, 0.2 M sodium sulphate.
PH range: 5-7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Oct 20, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.7→45.6 Å / Num. obs: 13722 / % possible obs: 99.94 % / Redundancy: 20.7 % / Biso Wilson estimate: 62.04 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.2407 / Rsym value: 0.2407 / Net I/σ(I): 15.4
Reflection shellResolution: 2.7→2.83 Å / Redundancy: 21.6 % / Mean I/σ(I) obs: 1.2 / Num. unique obs: 1808 / CC1/2: 0.442 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1PPG

1ppg


Resolution: 2.7→45.553 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 26.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2336 1046 7.62 %
Rwork0.1758 --
obs0.1804 13721 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.7→45.553 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3272 0 329 44 3645
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0023685
X-RAY DIFFRACTIONf_angle_d0.5425047
X-RAY DIFFRACTIONf_dihedral_angle_d11.6432164
X-RAY DIFFRACTIONf_chiral_restr0.044617
X-RAY DIFFRACTIONf_plane_restr0.003627
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7-2.84230.35681290.29791814X-RAY DIFFRACTION100
2.8423-3.02040.30321390.27321807X-RAY DIFFRACTION100
3.0204-3.25350.3021420.23081795X-RAY DIFFRACTION100
3.2535-3.58080.27591630.1871793X-RAY DIFFRACTION100
3.5808-4.09870.22351610.16141788X-RAY DIFFRACTION100
4.0987-5.16280.18351440.13141829X-RAY DIFFRACTION100
5.1628-45.55980.20791680.15861849X-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)
13.1651.2823-0.132.2605-0.35671.04230.02940.313-0.3775-0.18430.248-0.08860.15290.3853-00.42680.0401-0.01550.54330.01960.509643.379324.92124.8767
20.99630.54140.10551.2539-0.13940.46760.23420.5988-0.78990.1149-0.0525-1.07370.66140.4122-0.00090.5010.04540.00940.6661-0.00370.688950.2717.947424.8139
34.0192-0.33120.04773.2315-0.15321.74390.08060.03880.50550.0067-0.0414-0.2224-0.42470.36190.00010.4196-0.07230.00740.49960.07350.467346.313832.604229.7795
40.36260.57120.41841.02010.971.2832-0.54570.49890.3497-1.00290.43890.1525-1.1674-0.23670.00320.84260.0967-0.09650.68480.11730.662533.348338.224516.5296
54.4070.5892-0.91363.45250.75934.74640.01560.2788-0.1827-0.0346-0.08830.33120.229-0.1200.4715-0.0001-0.07280.50180.03620.440629.655225.148420.3002
61.9512-1.67041.39592.4976-0.59832.4887-0.10410.42410.5141-0.03270.19790.1284-0.22090.1225-0.00010.5188-0.00560.05340.54020.09470.490934.73235.190424.2331
74.195-0.4995-0.20223.5328-0.67980.31650.0189-0.2265-0.03080.69330.1962-0.15660.0868-0.04500.62240.037-0.03170.40480.05980.455633.58159.367847.2871
80.3946-0.2835-0.28151.623-0.75260.84230.2017-0.41360.00190.64380.1194-0.77920.33550.62980.03410.67480.0362-0.12620.52130.08450.615943.03266.739547.9531
92.317-0.2622-0.47022.21850.40691.6967-0.0152-0.1065-0.54210.16680.13170.14670.3267-0.172200.56580.0077-0.02150.50270.04560.569828.65612.866842.2471
100.232-0.05790.19440.9725-0.71320.62670.3176-0.6734-0.3421.3089-0.17510.7608-0.3846-0.46870.00290.8805-0.0190.30230.8190.04950.856616.486611.69254.5081
110.91070.17970.34350.115-0.06140.33880.271-0.46411.1648-0.62570.001-0.2481-0.24380.13020.00020.6921-0.08930.00160.5692-0.07880.851838.130222.63450.8312
121.0473-0.3717-1.33842.2358-0.00751.82-0.3103-0.2157-0.10910.01740.11570.6278-0.4321-1.0385-0.00010.69050.09730.05180.80110.03950.709817.961319.335451.0658
132.6592-0.58441.92671.44080.79942.53560.137-0.52060.25590.86850.10830.2626-0.1678-0.643600.81880.02070.11340.5910.04680.622924.496717.22151.3892
140.0914-0.0135-0.03770.2909-0.02360.17880.0420.4633-0.28230.3171-0.60460.2917-0.0657-1.3605-0.00090.99670.1060.12210.71970.07450.749422.308228.087146.5234
151.99090.1545-1.57280.43130.49462.1466-0.36110.1403-0.36371.15730.24261.48960.3011-0.26830.00040.6194-0.0715-0.02930.6160.07480.750718.51153.758344.4036
161.7966-1.2222-0.68472.78661.60620.9261-0.58772.45721.0528-1.70271.1102-0.5228-1.27610.13770.09531.14390.15330.01821.05180.24610.711537.640532.74244.6071
170.18920.14910.02020.17970.15130.2972-0.50640.4116-2.67040.44310.4139-2.36932.58040.7894-0.00031.40920.4162-0.03651.06740.05561.660959.67819.015433.1715
180.31420.09430.06730.02820.02010.01440.2909-2.0422-1.11691.0818-0.34620.9004-0.8101-0.8512-0.00211.32020.13090.09771.49690.38731.019822.229811.121668.4391
190.05050.1589-0.43340.5005-1.36443.7205-0.2701-0.4183-0.42570.6710.4464-2.33580.11582.04620.39360.53230.1267-0.24290.9653-0.35521.58147.2405-1.730840.1192
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 16 through 62A)
2X-RAY DIFFRACTION2chain 'A' and (resid 62B through 80 )
3X-RAY DIFFRACTION3chain 'A' and (resid 81 through 123 )
4X-RAY DIFFRACTION4chain 'A' and (resid 124 through 140 )
5X-RAY DIFFRACTION5chain 'A' and (resid 141 through 197 )
6X-RAY DIFFRACTION6chain 'A' and (resid 198 through 243 )
7X-RAY DIFFRACTION7chain 'B' and (resid 16 through 62A)
8X-RAY DIFFRACTION8chain 'B' and (resid 62B through 80 )
9X-RAY DIFFRACTION9chain 'B' and (resid 81 through 123 )
10X-RAY DIFFRACTION10chain 'B' and (resid 124 through 140 )
11X-RAY DIFFRACTION11chain 'B' and (resid 141 through 155 )
12X-RAY DIFFRACTION12chain 'B' and (resid 156 through 184 )
13X-RAY DIFFRACTION13chain 'B' and (resid 185 through 215 )
14X-RAY DIFFRACTION14chain 'B' and (resid 216 through 225 )
15X-RAY DIFFRACTION15chain 'B' and (resid 226 through 243 )
16X-RAY DIFFRACTION16chain 'A' and (resid 401 through 405)
17X-RAY DIFFRACTION17chain 'A' and (resid 406 through 409)
18X-RAY DIFFRACTION18chain 'B' and (resid 401 through 406)
19X-RAY DIFFRACTION19chain 'B' and (resid 407 through 410)

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