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- PDB-7ry1: human Hsp90_MC domain structure -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7ry1
Titlehuman Hsp90_MC domain structure
ComponentsHeat shock protein HSP 90-alphaHeat shock response
KeywordsCHAPERONE / Hsp90 / hexamer
Function / homology
Function and homology information


sperm mitochondrial sheath / dATP binding / Scavenging by Class F Receptors / sulfonylurea receptor binding / CTP binding / positive regulation of protein polymerization / vRNP Assembly / UTP binding / sperm plasma membrane / positive regulation of tau-protein kinase activity ...sperm mitochondrial sheath / dATP binding / Scavenging by Class F Receptors / sulfonylurea receptor binding / CTP binding / positive regulation of protein polymerization / vRNP Assembly / UTP binding / sperm plasma membrane / positive regulation of tau-protein kinase activity / protein insertion into mitochondrial outer membrane / chaperone-mediated autophagy / telomerase holoenzyme complex assembly / Rho GDP-dissociation inhibitor binding / Uptake and function of diphtheria toxin / mitochondrial transport / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / PIWI-interacting RNA (piRNA) biogenesis / TPR domain binding / non-chaperonin molecular chaperone ATPase / regulation of postsynaptic membrane neurotransmitter receptor levels / dendritic growth cone / Sema3A PAK dependent Axon repulsion / regulation of protein ubiquitination / skeletal muscle contraction / positive regulation of cell size / HSF1-dependent transactivation / telomere maintenance via telomerase / response to unfolded protein / protein unfolding / chaperone-mediated protein complex assembly / HSF1 activation / regulation of protein-containing complex assembly / Attenuation phase / RHOBTB2 GTPase cycle / positive regulation of lamellipodium assembly / eNOS activation / axonal growth cone / DNA polymerase binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / positive regulation of cardiac muscle contraction / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Signaling by ERBB2 / Recruitment of mitotic centrosome proteins and complexes / cardiac muscle cell apoptotic process / positive regulation of telomerase activity / positive regulation of defense response to virus by host / response to salt stress / endocytic vesicle lumen / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Anchoring of the basal body to the plasma membrane / protein tyrosine kinase binding / activation of innate immune response / response to cold / positive regulation of interferon-beta production / nitric-oxide synthase regulator activity / lysosomal lumen / Constitutive Signaling by Overexpressed ERBB2 / ESR-mediated signaling / AURKA Activation by TPX2 / VEGFR2 mediated vascular permeability / response to cocaine / brush border membrane / ATP-dependent protein folding chaperone / Signaling by ERBB2 TMD/JMD mutants / neuron migration / Constitutive Signaling by EGFRvIII / DDX58/IFIH1-mediated induction of interferon-alpha/beta / Signaling by ERBB2 ECD mutants / tau protein binding / Signaling by ERBB2 KD Mutants / Regulation of necroptotic cell death / Regulation of actin dynamics for phagocytic cup formation / Downregulation of ERBB2 signaling / cellular response to virus / VEGFA-VEGFR2 Pathway / histone deacetylase binding / Aggrephagy / Chaperone Mediated Autophagy / positive regulation of protein import into nucleus / response to estrogen / positive regulation of protein catabolic process / The role of GTSE1 in G2/M progression after G2 checkpoint / regulation of protein localization / positive regulation of nitric oxide biosynthetic process / disordered domain specific binding / Regulation of PLK1 Activity at G2/M Transition / unfolded protein binding / melanosome
Similarity search - Function
Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / 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
Similarity search - Domain/homology
Chem-MDC / Heat shock protein HSP 90-alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.523 Å
AuthorsPeng, S. / Deng, J. / Matts, R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)1R15CA219907-01 United States
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2022
Title: Crystal structure of the middle and C-terminal domains of Hsp90 alpha labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target.
Authors: Peng, S. / Woodruff, J. / Pathak, P.K. / Matts, R.L. / Deng, J.
History
DepositionAug 24, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 11, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Heat shock protein HSP 90-alpha
B: Heat shock protein HSP 90-alpha
C: Heat shock protein HSP 90-alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)150,1876
Polymers149,0363
Non-polymers1,1503
Water0
1
A: Heat shock protein HSP 90-alpha
B: Heat shock protein HSP 90-alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,1244
Polymers99,3582
Non-polymers7672
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3670 Å2
ΔGint-26 kcal/mol
Surface area42350 Å2
MethodPISA
2
C: Heat shock protein HSP 90-alpha
hetero molecules

C: Heat shock protein HSP 90-alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)100,1244
Polymers99,3582
Non-polymers7672
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
Buried area5440 Å2
ΔGint-29 kcal/mol
Surface area43280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)159.850, 311.964, 88.150
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resseq 293 or resseq 295:296 or (resid...
21(chain B and (resseq 293 or resseq 295:296 or (resid...
31(chain C and (resseq 293 or resseq 295:296 or (resid...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRTHRTHR(chain A and (resseq 293 or resseq 295:296 or (resid...AA2934
12PROPROILEILE(chain A and (resseq 293 or resseq 295:296 or (resid...AA295 - 2966 - 7
13TRPTRPTRPTRP(chain A and (resseq 293 or resseq 295:296 or (resid...AA2978
14THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
15THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
16THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
17THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
18THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
19THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
110THRTHRASPASP(chain A and (resseq 293 or resseq 295:296 or (resid...AA293 - 6994 - 410
21THRTHRTHRTHR(chain B and (resseq 293 or resseq 295:296 or (resid...BB2934
22PROPROILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB295 - 2966 - 7
23TRPTRPTRPTRP(chain B and (resseq 293 or resseq 295:296 or (resid...BB2978
24THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
25THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
26THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
27THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
28THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
29THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
210THRTHRILEILE(chain B and (resseq 293 or resseq 295:296 or (resid...BB293 - 6984 - 409
31THRTHRTHRTHR(chain C and (resseq 293 or resseq 295:296 or (resid...CC2934
32PROPROILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC295 - 2966 - 7
33TRPTRPTRPTRP(chain C and (resseq 293 or resseq 295:296 or (resid...CC2978
34THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
35THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
36THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
37THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
38THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
39THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409
310THRTHRILEILE(chain C and (resseq 293 or resseq 295:296 or (resid...CC293 - 6984 - 409

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Components

#1: Protein Heat shock protein HSP 90-alpha / Heat shock response / Heat shock 86 kDa / HSP 86 / HSP86 / Lipopolysaccharide-associated protein 2 / LAP-2 / LPS- ...Heat shock 86 kDa / HSP 86 / HSP86 / Lipopolysaccharide-associated protein 2 / LAP-2 / LPS-associated protein 2 / Renal carcinoma antigen NY-REN-38


Mass: 49678.781 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HSP90AA1, HSP90A, HSPC1, HSPCA / Production host: Escherichia coli (E. coli)
References: UniProt: P07900, non-chaperonin molecular chaperone ATPase
#2: Chemical ChemComp-MDC / N-[2-(1-MALEIMIDYL)ETHYL]-7-DIETHYLAMINOCOUMARIN-3-CARBOXAMIDE


Mass: 383.398 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C20H21N3O5 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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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: 3.69 Å3/Da / Density % sol: 66.64 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1M Succinic acid PH 6.5, 12% PEG3350, 20mM CaCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97951 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 4, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97951 Å / Relative weight: 1
ReflectionResolution: 3.5→50 Å / Num. obs: 27438 / % possible obs: 99.9 % / Redundancy: 6.4 % / Biso Wilson estimate: 127.52 Å2 / Rmerge(I) obs: 0.148 / Rpim(I) all: 0.063 / Rrim(I) all: 0.161 / Χ2: 0.688 / Net I/σ(I): 3.9 / Num. measured all: 176259
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.5-3.636.41.36627080.5360.5811.4870.466100
3.63-3.776.30.84426860.7090.3620.920.484100
3.77-3.946.10.64527160.8120.2830.7060.511100
3.94-4.156.30.44527090.9220.1920.4850.55799.9
4.15-4.416.70.29127220.9550.1210.3160.647100
4.41-4.756.60.22427210.9780.0930.2430.695100
4.75-5.236.30.18127260.9830.0780.1980.77499.9
5.23-5.986.80.17727590.9870.0730.1920.716100
5.98-7.536.60.11627890.9940.0480.1250.757100
7.53-506.10.05529020.9980.0230.061.24699.8

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3Q6M

3q6m


Resolution: 3.523→47.421 Å / SU ML: 0.52 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 28.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.272 1995 7.28 %
Rwork0.2164 25399 -
obs0.2204 27394 98.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 319.62 Å2 / Biso mean: 141.4972 Å2 / Biso min: 72.89 Å2
Refinement stepCycle: final / Resolution: 3.523→47.421 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9949 0 84 0 10033
Biso mean--180.8 --
Num. residues----1207
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00410205
X-RAY DIFFRACTIONf_angle_d0.80613701
X-RAY DIFFRACTIONf_chiral_restr0.0471504
X-RAY DIFFRACTIONf_plane_restr0.0041743
X-RAY DIFFRACTIONf_dihedral_angle_d14.8996323
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5296X-RAY DIFFRACTION8.528TORSIONAL
12B5296X-RAY DIFFRACTION8.528TORSIONAL
13C5296X-RAY DIFFRACTION8.528TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.523-3.61080.38911180.3429149884
3.6108-3.70840.34111430.32621819100
3.7084-3.81740.33861440.30981829100
3.8174-3.94060.33221400.30291784100
3.9406-4.08140.32841420.29561816100
4.0814-4.24470.32931420.26141812100
4.2447-4.43770.29251450.24211828100
4.4377-4.67150.25231440.23511835100
4.6715-4.96390.28681420.22511815100
4.9639-5.34670.25791450.20321826100
5.3467-5.88380.25951460.21851861100
5.8838-6.73320.29031460.21851857100
6.7332-8.47520.26081470.18991861100
8.4752-47.420.21211510.142195899
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)
18.24581.44432.90412.4932-1.97439.3351-0.17321.55980.3043-3.2550.0777-0.55160.157-0.5309-0.0051.56740.1301-0.04281.39090.20071.12-11.4122-39.2473-7.6209
28.57382.31292.02352.44553.73839.7126-0.57340.5710.3546-2.14970.4276-0.5722-0.6730.27420.28241.0334-0.05460.14581.10140.13451.0015-16.6525-37.7801-0.537
39.24252.7445-1.98654.60513.8759.43210.5341-1.8296-0.39152.1534-0.79740.18551.95431.16170.26841.67830.1032-0.12581.11910.0421.2189-11.8231-43.441710.5408
46.17774.2925-1.87048.8379-0.33747.59780.7244-0.98041.18160.9001-0.48390.31730.10380.3436-0.1991.2537-0.0213-0.14831.0595-0.12350.9407-18.0828-33.685410.1674
59.39742.7957-2.7075.9321-0.58126.2202-0.22860.56090.0296-0.26420.08840.6558-0.2104-1.53510.18091.11720.0567-0.07741.4284-0.00181.0704-42.2292-51.63077.8703
62.4317-0.7195-2.05246.6608-0.44613.0531-0.0379-1.26880.57720.14640.66641.2331-0.8737-1.5379-0.47621.43390.39010.10322.07720.24921.3088-48.6351-49.209917.2611
76.55121.70775.98466.9501-0.18885.9011-1.5487-3.74771.1165-1.53980.23692.41430.308-0.31531.29321.49530.16450.71233.54210.74522.212-66.3199-62.335528.6932
88.4913.2317-0.18975.8115-4.07862.9536-0.351-1.3552-0.2905-0.61520.4654-0.53560.4285-1.0438-0.07951.2823-0.00660.11081.76820.36131.5282-47.8834-62.11326.3735
90.2219-1.170.90276.1623-2.47749.0856-0.4576-0.571-0.30980.51911.1933-0.2432-0.0665-1.3414-0.95331.5689-0.21340.03552.20910.25691.4388-53.4395-68.980629.486
104.4302-1.40541.13482.2934-1.03247.80991.00010.0467-0.33220.36380.36840.53491.5541-0.8609-1.31221.4086-0.2943-0.10611.68810.43451.813-50.9043-79.845728.0664
117.535.08450.49535.16090.27453.25410.124-1.53370.23571.486-0.3571-0.7420.19310.20160.22551.31420.0624-0.1591.09480.05391.05663.9861-66.799148.5569
124.19510.8976-2.64439.4813.58858.50320.1740.89180.2609-1.3578-0.2618-0.0385-1.6243-0.65080.07721.40950.08540.01620.89840.06711.21912.0828-62.952435.5788
135.6002-0.61623.71128.85381.19765.4095-0.36810.5286-0.306-0.30810.5801-0.9717-0.24870.1891-0.08881.0108-0.00630.03221-0.01310.85575.6948-72.83634.3449
148.07543.14762.66489.31720.78135.80680.3088-0.5091-0.99730.68120.20750.43611.4113-1.3436-0.4561.2921-0.2830.04791.18370.24461.1675-21.2165-85.52337.318
156.0433-0.52483.32333.98640.19024.53070.23370.778-1.592-1.27580.19620.52692.3882-0.5235-0.32972.1863-0.58290.00681.5395-0.12481.6008-31.7964-95.637421.7012
163.468-3.37251.32223.7205-2.17516.5053-0.08550.90570.8317-0.9097-0.4939-1.69760.06570.24640.58921.5667-0.3398-0.21781.77920.34041.9524-27.898-80.434619.2727
176.3831-4.83441.04325.70933.18697.7856-0.24810.0463-0.5981-1.1031-0.5219-1.19190.9129-1.38330.9881.5171-0.3852-0.33421.7173-0.07121.3122-33.5798-82.410817.1537
186.2041-6.56620.83817.14650.22845.10820.19460.9604-0.7411-0.72330.0630.96450.6467-0.7906-0.17231.5018-0.7659-0.20792.14980.19511.5464-50.3907-85.744815.9042
198.9833-0.9231.80216.1737-1.26753.991-0.1657-1.3802-0.74031.3389-0.018-0.09590.2207-0.4890.41481.44210.15690.15291.18350.00631.1103-15.1872-44.157649.1903
208.088-2.28164.66539.09162.18438.4915-0.09521.2938-0.9566-1.03290.4111-0.46330.22351.00250.0441.2410.05630.10791.1243-0.1321.2004-14.1867-45.016833.67
219.49122.85690.43853.4608-0.02983.1149-0.56680.47580.0912-0.0996-0.06191.96670.1603-0.3120.60211.4358-0.0227-0.11920.9350.02981.0224-24.9274-38.786937.8057
224.77250.10020.958510.0721-3.72553.8757-0.3574-0.23730.34130.32720.03340.1251-0.5473-0.19640.37631.140.124-0.15970.9112-0.1711.0599-18.9096-13.623136.9987
232.973-0.4636-1.71146.8311-1.31552.08340.2370.61971.2617-0.0210.07791.5732-0.9783-0.8906-0.08361.64190.3087-0.59971.5508-0.13152.0272-26.32143.720923.4961
246.8750.4441-0.73468.7199-0.6265.0416-0.30890.60310.3736-0.9663-0.47061.1132-0.5238-0.91370.51451.50670.0562-0.11841.05550.13531.5705-17.04890.897118.4434
254.52742.8375-1.01453.83622.45025.8061-0.8130.4383-0.6157-0.3185-0.11290.36960.27130.67731.20871.9551-0.1053-0.11461.21690.07381.4211-10.0349-8.762117.3676
266.95613.0648-3.25352.34150.26066.91430.63450.49671.5869-0.3222-0.0738-0.1513-1.2781-0.1727-0.48312.37720.0879-0.38961.05640.00652.0749-4.980411.819415.9325
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 293 through 317 )A293 - 317
2X-RAY DIFFRACTION2chain 'A' and (resid 318 through 343 )A318 - 343
3X-RAY DIFFRACTION3chain 'A' and (resid 344 through 377 )A344 - 377
4X-RAY DIFFRACTION4chain 'A' and (resid 378 through 429 )A378 - 429
5X-RAY DIFFRACTION5chain 'A' and (resid 430 through 523 )A430 - 523
6X-RAY DIFFRACTION6chain 'A' and (resid 524 through 556 )A524 - 556
7X-RAY DIFFRACTION7chain 'A' and (resid 557 through 578 )A557 - 578
8X-RAY DIFFRACTION8chain 'A' and (resid 579 through 617 )A579 - 617
9X-RAY DIFFRACTION9chain 'A' and (resid 618 through 656 )A618 - 656
10X-RAY DIFFRACTION10chain 'A' and (resid 657 through 699 )A657 - 699
11X-RAY DIFFRACTION11chain 'B' and (resid 293 through 343 )B293 - 343
12X-RAY DIFFRACTION12chain 'B' and (resid 344 through 377 )B344 - 377
13X-RAY DIFFRACTION13chain 'B' and (resid 378 through 429 )B378 - 429
14X-RAY DIFFRACTION14chain 'B' and (resid 430 through 523 )B430 - 523
15X-RAY DIFFRACTION15chain 'B' and (resid 524 through 596 )B524 - 596
16X-RAY DIFFRACTION16chain 'B' and (resid 597 through 618 )B597 - 618
17X-RAY DIFFRACTION17chain 'B' and (resid 619 through 640 )B619 - 640
18X-RAY DIFFRACTION18chain 'B' and (resid 641 through 698 )B641 - 698
19X-RAY DIFFRACTION19chain 'C' and (resid 293 through 343 )C293 - 343
20X-RAY DIFFRACTION20chain 'C' and (resid 344 through 402 )C344 - 402
21X-RAY DIFFRACTION21chain 'C' and (resid 403 through 429 )C403 - 429
22X-RAY DIFFRACTION22chain 'C' and (resid 430 through 532 )C430 - 532
23X-RAY DIFFRACTION23chain 'C' and (resid 533 through 578 )C533 - 578
24X-RAY DIFFRACTION24chain 'C' and (resid 579 through 607 )C579 - 607
25X-RAY DIFFRACTION25chain 'C' and (resid 608 through 640 )C608 - 640
26X-RAY DIFFRACTION26chain 'C' and (resid 641 through 698 )C641 - 698

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