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- PDB-4kpf: Novel fluoroquinolones in complex with topoisomerase IV from S. p... -

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Basic information

Entry
Database: PDB / ID: 4kpf
TitleNovel fluoroquinolones in complex with topoisomerase IV from S. pneumoniae and E-site G-gate
Components
  • E-site1
  • E-site2
  • E-site3
  • E-site4
  • ParC55
  • ParE30
KeywordsISOMERASE/DNA/INHIBITOR / PROTEIN-DNA CLEAVAGE COMPLEX / ISOMERASE-DNA-INHIBITOR COMPLEX / TOPOISOMERASE IIA / Quinolone / ACHN-454
Function / homology
Function and homology information


DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA negative supercoiling activity / extrinsic component of plasma membrane / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / chromosome segregation / chromosome / DNA binding / ATP binding / metal ion binding / cytoplasm
Similarity search - Function
DNA topoisomerase IV subunit A, Gram-positive / DNA topoisomerase 4 subunit B, Firmicutes/Mollicutes / Rossmann fold - #670 / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / : / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA topoisomerase, type IIA, subunit B / DNA gyrase B subunit, C-terminal ...DNA topoisomerase IV subunit A, Gram-positive / DNA topoisomerase 4 subunit B, Firmicutes/Mollicutes / Rossmann fold - #670 / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / : / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA topoisomerase, type IIA, subunit B / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA topoisomerase, type IIA, subunit B, domain 2 / DNA gyrase B / DNA topoisomerase, type IIA / DNA topoisomerase, type IIA, conserved site / DNA topoisomerase II signature. / TopoisomeraseII / DNA topoisomerase, type IIA, subunit B, C-terminal / Toprim domain / DNA topoisomerase, type IIA-like domain superfamily / Toprim domain profile. / TOPRIM domain / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-1UV / DNA / DNA (> 10) / DNA topoisomerase 4 subunit A / DNA topoisomerase 4 subunit B
Similarity search - Component
Biological speciesStreptococcus pneumoniae (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.24 Å
AuthorsLaponogov, I. / Pan, X.-S. / Vesekov, D.A. / Cirz, R.T. / Wagman, A.S. / Moser, H.E. / Fisher, L.M. / Sanderson, M.R.
CitationJournal: Open Biol / Year: 2016
Title: Exploring the active site of the Streptococcus pneumoniae topoisomerase IV-DNA cleavage complex with novel 7,8-bridged fluoroquinolones.
Authors: Laponogov, I. / Pan, X.S. / Veselkov, D.A. / Cirz, R.T. / Wagman, A. / Moser, H.E. / Fisher, L.M. / Sanderson, M.R.
History
DepositionMay 13, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 26, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / Database references / Source and taxonomy
Category: citation / citation_author / pdbx_entity_src_syn
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 16, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ParC55
B: ParC55
C: ParE30
D: ParE30
E: E-site1
F: E-site2
G: E-site3
H: E-site4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)185,57616
Polymers184,6848
Non-polymers8938
Water25214
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21240 Å2
ΔGint-171 kcal/mol
Surface area56630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)157.860, 157.860, 210.780
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein ParC55


Mass: 56455.434 Da / Num. of mol.: 2 / Fragment: ParC55
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: ATCC BAA-334 / TIGR4 / Gene: parC, SP_0855 / Production host: Escherichia coli (E. coli) / References: UniProt: P72525
#2: Protein ParE30


Mass: 30415.703 Da / Num. of mol.: 2 / Fragment: ParE30
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: ATCC BAA-334 / TIGR4 / Gene: parE / Production host: Escherichia coli (E. coli) / References: UniProt: Q59961

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DNA chain , 4 types, 4 molecules EFGH

#3: DNA chain E-site1


Mass: 2121.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: DNA chain E-site2


Mass: 3348.209 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#5: DNA chain E-site3


Mass: 2113.410 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#6: DNA chain E-site4


Mass: 3358.211 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 3 types, 22 molecules

#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-1UV / (3aS,4R)-4-amino-13-cyclopropyl-8-fluoro-10-oxo-3a,4,5,6,10,13-hexahydro-1H,3H-pyrrolo[2',1':3,4][1,4]oxazepino[5,6-h]quinoline-11-carboxylic acid


Mass: 373.378 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H20FN3O4
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 14 / 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: 4.11 Å3/Da / Density % sol: 70.04 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 50 mM Na Cacodylate, 4-7% isopropanol, optimized mixture of salts, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: May 6, 2011
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 3.24→41.828 Å / Num. all: 48832 / Num. obs: 48761 / % possible obs: 99.9 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 6.91 % / Rmerge(I) obs: 0.81 / Net I/σ(I): 19.16
Reflection shellResolution: 3.24→3.32 Å / Redundancy: 7.13 % / Rmerge(I) obs: 0.381 / Mean I/σ(I) obs: 5.91 / % possible all: 100

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Processing

Software
NameVersionClassification
GDEdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8_1069)refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.24→41.828 Å / SU ML: 0.21 / Cross valid method: THROUGHOUT / σ(F): 2 / Phase error: 16.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1845 2446 5.02 %random
Rwork0.1621 ---
obs0.1632 48732 99.86 %-
all-48761 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.24→41.828 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10339 730 60 14 11143
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00911413
X-RAY DIFFRACTIONf_angle_d1.24315668
X-RAY DIFFRACTIONf_dihedral_angle_d18.0574176
X-RAY DIFFRACTIONf_chiral_restr0.0761806
X-RAY DIFFRACTIONf_plane_restr0.0041917
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.24-3.30610.21451370.21052680X-RAY DIFFRACTION100
3.3061-3.3780.2621340.19892717X-RAY DIFFRACTION100
3.378-3.45650.2111510.1852674X-RAY DIFFRACTION100
3.4565-3.54290.20121400.18052682X-RAY DIFFRACTION100
3.5429-3.63870.17471410.17082694X-RAY DIFFRACTION100
3.6387-3.74570.16661450.16232713X-RAY DIFFRACTION100
3.7457-3.86650.17781420.15642707X-RAY DIFFRACTION100
3.8665-4.00460.17721410.14772668X-RAY DIFFRACTION100
4.0046-4.16480.15991450.14472727X-RAY DIFFRACTION100
4.1648-4.35410.15921370.13152692X-RAY DIFFRACTION100
4.3541-4.58340.13521550.12532712X-RAY DIFFRACTION100
4.5834-4.87020.15021400.13752736X-RAY DIFFRACTION100
4.8702-5.24560.17851470.15222737X-RAY DIFFRACTION100
5.2456-5.77220.18161440.1722730X-RAY DIFFRACTION100
5.7722-6.60470.21361490.18192769X-RAY DIFFRACTION100
6.6047-8.31050.18871430.16542781X-RAY DIFFRACTION100
8.3105-41.8310.21921550.17842867X-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)
18.23645.3637-5.65273.4309-3.63763.832-0.31720.4222-0.5177-0.20670.1961-0.30760.41490.02350.1640.6665-0.01-0.06380.666-0.06560.3953-73.953948.9022-44.3776
27.6483-0.67060.9416.63090.7018.3329-0.04860.3546-1.1403-0.6432-0.1336-0.42440.54750.08410.21830.6072-0.00880.18450.46990.02420.5205-89.863631.7628-27.1446
34.1588-3.88051.18445.4096-2.1884.5724-0.4294-1.19260.83161.15121.5271-0.34280.9254-0.201-0.77840.59540.1823-0.05371.2059-0.22050.6187-40.36755.6852-39.2671
41.9162-1.648-1.38811.99731.18641.00270.1462-0.1295-1.1231-0.7731-0.38080.05761.31621.0270.30850.89390.33880.03031.2642-0.27480.9792-24.514245.0617-35.2419
52.04460.87011.05622.4250.74413.61550.1185-0.19870.13110.2892-0.1206-0.03660.05050.04640.00260.5504-0.11590.04670.71820.02680.3825-55.973365.4771-31.0729
66.87671.9949-5.45743.1634-1.24077.4557-0.67740.96250.09910.3690.7405-0.23990.6609-0.89110.02520.8501-0.027-0.11770.7256-0.12770.4429-87.233447.7684-44.3266
77.33161.62430.46527.74940.12583.94560.0756-0.00240.80740.18490.22390.149-0.8005-0.0229-0.38570.7193-0.18650.09810.56460.05140.4579-41.633296.9261-43.698
84.76883.71321.08028.38932.84842.4533-0.2457-0.0044-0.09440.0710.09410.34790.1029-0.47070.15050.5662-0.06660.01240.86180.07550.2964-67.781968.3562-51.9658
91.99460.2276-0.42311.8633-0.01952.1445-0.04280.47390.2723-0.40120.1411-0.1011-0.05670.3999-0.15650.5505-0.13260.01130.93330.03270.3721-51.340170.0423-53.4452
105.14543.20844.35781.97942.71354.8771-0.3305-0.19680.1105-0.31380.01460.0884-0.6362-0.16740.33090.58170.14690.0920.57980.10720.3863-76.561348.94345.7085
115.16793.8298-2.00615.41512.04658.2075-0.10090.10350.50430.04030.29250.4497-0.0679-0.4338-0.12670.38650.145-0.050.52690.07680.4069-97.052440.3958-13.611
128.7419-5.81850.60277.18142.77766.9131.04641.31970.1591-1.108-0.7314-0.6156-0.7945-0.8422-0.44050.7646-0.01690.16850.76480.040.4922-55.467376.84353.2338
135.03912.3334-1.32083.2755-0.42767.6460.1691-0.36710.59430.66690.35611.6021-0.9475-1.4837-0.58410.91650.1430.14610.96210.06721.3776-58.032695.5306-0.1005
143.73560.8956-1.02272.5853-0.42294.3581-0.0740.6023-0.0015-0.11120.1388-0.04490.1402-0.2245-0.12220.4636-0.0439-0.00390.70020.02340.3244-53.246558.9786-5.6338
156.44024.76934.77467.48083.44985.33320.8296-0.0335-0.38130.42240.1018-0.26480.5734-0.4086-0.60210.52660.03310.04570.87260.17280.4747-82.589437.37384.6747
167.5875-0.19591.74366.36950.64554.98430.2569-0.0205-0.5443-0.0640.1451-0.46820.49070.489-0.52730.47470.0082-0.09720.72430.03140.5036-19.622556.46929.2164
176.6565-0.7315-1.16771.2783-0.79171.955-0.363-0.2887-0.12940.20490.0311-0.18170.3860.00750.33280.7854-0.0935-0.05150.77180.03760.3773-56.900746.252214.136
181.93730.4959-0.59261.8942-0.4912.16970.2754-0.6889-0.04710.5150.0093-0.1796-0.08210.1334-0.33940.6729-0.08-0.09290.85110.04160.4001-48.547260.051817.1353
193.3848-0.4663-1.24840.8069-1.1312.74380.29781.2778-1.7703-0.522-0.22881.13871.04930.109-0.30851.12020.095-0.13840.9863-0.29141.4291-39.803238.8757-22.7145
203.40431.0587-3.28564.3081.62624.93560.01910.6745-0.5508-0.10730.068-0.43570.47681.27450.23160.87310.29910.16571.7636-0.23070.8985-24.915954.5029-46.5542
211.5384-0.54450.52081.3716-0.54952.96250.12050.0093-0.19780.3002-0.1718-0.55210.23030.72840.00570.65760.2358-0.11871.3446-0.03370.8447-22.198953.4469-24.0752
229.00311.51233.24654.3451-0.57555.61411.24680.45050.22680.2429-0.28521.65190.0015-0.7984-1.11450.65430.10160.10731.30170.02821.3491-69.712685.6985-14.446
237.206-1.86131.69164.55672.79936.7515-0.0122-0.70081.49681.36460.11220.5395-0.125-0.47680.17211.3397-0.14970.17710.7157-0.16180.9027-50.388391.392911.4458
242.044-0.3982-0.03561.5815-1.23943.44690.03810.46290.9722-0.0806-0.04340.1592-0.7540.11670.1161.0729-0.08080.16560.60030.12260.9562-48.343294.8307-10.6178
253.3952-1.37741.59974.92823.19864.09410.1542-0.2860.3539-0.09630.1518-0.4954-0.65790.723-0.25830.897-0.1640.19171.43250.0180.6292-35.963871.523-31.9594
264.8444-0.6499-3.64356.1699-0.05192.77470.0686-0.2210.18720.01850.414-0.6683-0.24231.0082-0.51530.9364-0.1371-0.09121.14-0.15370.5665-38.967474.1368-3.0223
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain "A" and resseq 343:382A343 - 382
2X-RAY DIFFRACTION2chain "A" and resseq 383:429A383 - 429
3X-RAY DIFFRACTION3chain "A" and resseq 18:30A18 - 30
4X-RAY DIFFRACTION4chain "A" and resseq 3:17A3 - 17
5X-RAY DIFFRACTION5chain "A" and resseq 31:154A31 - 154
6X-RAY DIFFRACTION6chain "A" and resseq 430:455A430 - 455
7X-RAY DIFFRACTION7chain "A" and resseq 239:322A239 - 322
8X-RAY DIFFRACTION8chain "A" and resseq 456:482A456 - 482
9X-RAY DIFFRACTION9chain "A" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )A155 - 238
10X-RAY DIFFRACTION9chain "A" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )A323 - 342
11X-RAY DIFFRACTION9chain "A" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )A483 - 845
12X-RAY DIFFRACTION10chain "B" and resseq 343:382B343 - 382
13X-RAY DIFFRACTION11chain "B" and resseq 383:429B383 - 429
14X-RAY DIFFRACTION12chain "B" and resseq 18:30B18 - 30
15X-RAY DIFFRACTION13chain "B" and resseq 3:17B3 - 17
16X-RAY DIFFRACTION14chain "B" and resseq 31:154B31 - 154
17X-RAY DIFFRACTION15chain "B" and resseq 430:455B430 - 455
18X-RAY DIFFRACTION16chain "B" and resseq 239:322B239 - 322
19X-RAY DIFFRACTION17chain "B" and resseq 456:482B456 - 482
20X-RAY DIFFRACTION18chain "B" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )B155 - 238
21X-RAY DIFFRACTION18chain "B" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )B323 - 342
22X-RAY DIFFRACTION18chain "B" and not ( resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482 )B483 - 833
23X-RAY DIFFRACTION19chain "C" and resseq 539:581C539 - 581
24X-RAY DIFFRACTION20chain "C" and resseq 610:634C610 - 634
25X-RAY DIFFRACTION21chain "C" and not ( resseq 539:581 or resseq 610:634 )C415 - 538
26X-RAY DIFFRACTION21chain "C" and not ( resseq 539:581 or resseq 610:634 )C582 - 609
27X-RAY DIFFRACTION21chain "C" and not ( resseq 539:581 or resseq 610:634 )C635 - 830
28X-RAY DIFFRACTION22chain "D" and resseq 539:581D539 - 581
29X-RAY DIFFRACTION23chain "D" and resseq 610:634D610 - 634
30X-RAY DIFFRACTION24chain "D" and not ( resseq 539:581 or resseq 610:634 )D415 - 538
31X-RAY DIFFRACTION24chain "D" and not ( resseq 539:581 or resseq 610:634 )D582 - 609
32X-RAY DIFFRACTION24chain "D" and not ( resseq 539:581 or resseq 610:634 )D635 - 832
33X-RAY DIFFRACTION25chain "E" or chain "F"E9 - 15
34X-RAY DIFFRACTION26chain "G" or chain "H"G9 - 15

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