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- PDB-6jpv: Structural analysis of AIMP2-DX2 and HSP70 interaction -

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Basic information

Entry
Database: PDB / ID: 6jpv
TitleStructural analysis of AIMP2-DX2 and HSP70 interaction
ComponentsHeat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
KeywordsCHAPERONE / HSP70 / AIMP2-DX2 / substrate binding domain
Function / homology
Function and homology information


type II pneumocyte differentiation / : / Selenoamino acid metabolism / denatured protein binding / cellular heat acclimation / negative regulation of inclusion body assembly / death receptor agonist activity / Viral RNP Complexes in the Host Cell Nucleus / C3HC4-type RING finger domain binding / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway ...type II pneumocyte differentiation / : / Selenoamino acid metabolism / denatured protein binding / cellular heat acclimation / negative regulation of inclusion body assembly / death receptor agonist activity / Viral RNP Complexes in the Host Cell Nucleus / C3HC4-type RING finger domain binding / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / Cytosolic tRNA aminoacylation / aminoacyl-tRNA synthetase multienzyme complex / ATP-dependent protein disaggregase activity / positive regulation of microtubule nucleation / misfolded protein binding / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of tumor necrosis factor-mediated signaling pathway / regulation of mitotic spindle assembly / aggresome / lysosomal transport / cellular response to steroid hormone stimulus / mRNA catabolic process / : / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of protein ubiquitination / Regulation of HSF1-mediated heat shock response / HSF1-dependent transactivation / response to unfolded protein / cellular response to unfolded protein / Mitochondrial unfolded protein response (UPRmt) / Attenuation phase / chaperone-mediated protein complex assembly / transcription regulator inhibitor activity / ATP metabolic process / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / inclusion body / heat shock protein binding / negative regulation of protein ubiquitination / centriole / Transcriptional and post-translational regulation of MITF-M expression and activity / protein folding chaperone / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / positive regulation of erythrocyte differentiation / positive regulation of RNA splicing / positive regulation of protein ubiquitination / positive regulation of interleukin-8 production / AUF1 (hnRNP D0) binds and destabilizes mRNA / negative regulation of transforming growth factor beta receptor signaling pathway / ATP-dependent protein folding chaperone / G protein-coupled receptor binding / negative regulation of cell growth / PKR-mediated signaling / histone deacetylase binding / positive regulation of NF-kappaB transcription factor activity / transcription corepressor activity / disordered domain specific binding / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / cellular response to heat / virus receptor activity / protein refolding / cellular response to oxidative stress / protein-containing complex assembly / molecular adaptor activity / vesicle / blood microparticle / ficolin-1-rich granule lumen / protein stabilization / nuclear speck / protein ubiquitination / cadherin binding / receptor ligand activity / translation / ribonucleoprotein complex / signaling receptor binding / negative regulation of cell population proliferation / focal adhesion / apoptotic process / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / positive regulation of gene expression / negative regulation of apoptotic process / perinuclear region of cytoplasm / enzyme binding / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / protein-containing complex / ATP hydrolysis activity / mitochondrion / extracellular space / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / membrane / plasma membrane / cytosol
Similarity search - Function
AIMP2, lysyl-tRNA synthetase binding domain / AIMP2, thioredoxin-like domain / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 / AIMP2 lysyl-tRNA synthetase binding domain / Thioredoxin-like domain / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. ...AIMP2, lysyl-tRNA synthetase binding domain / AIMP2, thioredoxin-like domain / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 / AIMP2 lysyl-tRNA synthetase binding domain / Thioredoxin-like domain / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Glutathione S-transferase, C-terminal domain / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal domain superfamily / ATPase, nucleotide binding domain / Sandwich / Mainly Beta
Similarity search - Domain/homology
Heat shock 70 kDa protein 1A / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15000649024 Å
AuthorsCho, H.Y. / Son, S.Y. / Jeon, Y.H.
Funding support Korea, Republic Of, 1items
OrganizationGrant numberCountry
National Research Foundation (Korea)NRF-2013M3A6A4045160 Korea, Republic Of
CitationJournal: Nat.Chem.Biol. / Year: 2020
Title: Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development.
Authors: Lim, S. / Cho, H.Y. / Kim, D.G. / Roh, Y. / Son, S.Y. / Mushtaq, A.U. / Kim, M. / Bhattarai, D. / Sivaraman, A. / Lee, Y. / Lee, J. / Yang, W.S. / Kim, H.K. / Kim, M.H. / Lee, K. / Jeon, Y.H. / Kim, S.
History
DepositionMar 28, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 2, 2019Provider: repository / Type: Initial release
Revision 1.1Nov 20, 2019Group: Database references / Category: citation / Item: _citation.pdbx_database_id_DOI / _citation.title
Revision 1.2Dec 18, 2019Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed
Revision 1.3Jan 1, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _citation_author.identifier_ORCID
Revision 1.4Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
B: Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2


Theoretical massNumber of molelcules
Total (without water)33,7382
Polymers33,7382
Non-polymers00
Water5,963331
1
A: Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2

B: Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2


Theoretical massNumber of molelcules
Total (without water)33,7382
Polymers33,7382
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_554-x+1/2,-y,z-1/21
Buried area3130 Å2
ΔGint-20 kcal/mol
Surface area16040 Å2
MethodPISA
Unit cell
Length a, b, c (Å)41.111, 77.054, 88.711
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21

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
11SERSERGLUGLU(chain 'A' and (resid 394 through 534 or resid 536 through 545))AA394 - 5341 - 141
12VALVALHISHIS(chain 'A' and (resid 394 through 534 or resid 536 through 545))AA536 - 545143 - 152
21SERSERGLUGLU(chain 'B' and (resid 394 through 534 or resid 536 through 545))BB394 - 5341 - 141
22VALVALHISHIS(chain 'B' and (resid 394 through 534 or resid 536 through 545))BB536 - 545143 - 152

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Components

#1: Protein Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 / Heat shock 70 kDa protein 1 / HSP70.1 / Multisynthase complex auxiliary component p38 / Protein JTV-1


Mass: 16869.021 Da / Num. of mol.: 2
Fragment: HSP70 substrate binding domain/peptide sequences of DX2
Source method: isolated from a genetically manipulated source
Details: SF file contains Friedel pairs.,SF file contains Friedel pairs.
Source: (gene. exp.) Homo sapiens (human) / Gene: HSPA1A, HSP72, HSPA1, HSX70, AIMP2, JTV1, PRO0992 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIPL / References: UniProt: P0DMV8, UniProt: Q13155
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 331 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsSubstrate binding domain of HSP70: S394-S537 Peptide from AIMP2-DX2: M538-G546

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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: 2.09 Å3/Da / Density % sol: 41.03 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: PEG1500, Succinic Acid, Sodium Dihydrogen Phosphate, Glycine

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 18, 2018
RadiationMonochromator: DCM Si (111) Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.15→28.08 Å / Num. obs: 15918 / % possible obs: 99.72 % / Redundancy: 7.7 % / Biso Wilson estimate: 18.93 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.1036 / Rpim(I) all: 0.04137 / Rrim(I) all: 0.1118 / Net I/σ(I): 14.26
Reflection shellResolution: 2.15→2.227 Å / Redundancy: 8 % / Rmerge(I) obs: 0.2348 / Mean I/σ(I) obs: 8.73 / Num. unique obs: 1551 / CC1/2: 0.97 / Rpim(I) all: 0.08955 / Rrim(I) all: 0.2517 / % possible all: 99.87

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Processing

Software
NameVersionClassification
PHENIX1.12_2829refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIX1.12_2829phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4WV5

4wv5


Resolution: 2.15000649024→28.0785408959 Å / SU ML: 0.257560777566 / Cross valid method: FREE R-VALUE / σ(F): 1.35779936231 / Phase error: 22.9145895941
RfactorNum. reflection% reflectionSelection details
Rfree0.23478720108 2154 7.69203299646 %Random selection
Rwork0.173762231727 ---
obs0.17847200903 15894 94.6239102521 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 25.3642749192 Å2
Refinement stepCycle: LAST / Resolution: 2.15000649024→28.0785408959 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2359 0 0 331 2690
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.006880919159852398
X-RAY DIFFRACTIONf_angle_d0.9575778231763244
X-RAY DIFFRACTIONf_chiral_restr0.0559951226453377
X-RAY DIFFRACTIONf_plane_restr0.00582881842173430
X-RAY DIFFRACTIONf_dihedral_angle_d18.19063440421501
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.15-2.20.2638592076221120.1822787155151323X-RAY DIFFRACTION73.4390992835
2.2-2.2550.2330753598281190.1936072986461457X-RAY DIFFRACTION79.5557799091
2.255-2.31590.2572158287831270.1889482890321584X-RAY DIFFRACTION86.7647058824
2.3159-2.38410.269949248481460.1784277243471675X-RAY DIFFRACTION91.5075376884
2.3841-2.4610.2992541412351410.1913281428491745X-RAY DIFFRACTION96.0774325013
2.461-2.54890.3111983364151520.1904684523571797X-RAY DIFFRACTION98.6835443038
2.5489-2.65080.2937042448871510.1860061541931813X-RAY DIFFRACTION99.8982706002
2.6508-2.77140.2810013494941520.1844138668521820X-RAY DIFFRACTION99.8481012658
2.7714-2.91740.2314381537151520.1890999160771828X-RAY DIFFRACTION99.8487140696
2.9174-3.09990.25534646581530.1831940920211814X-RAY DIFFRACTION99.6958945768
3.0999-3.33890.2144666234521520.1685701991271799X-RAY DIFFRACTION99.2370295015
3.3389-3.67430.2183056406821450.1540161847741822X-RAY DIFFRACTION99.2431886983
3.6743-4.20440.1854949306331490.1502899391121802X-RAY DIFFRACTION99.3380855397
4.2044-5.29130.1892164266871520.1476471215971792X-RAY DIFFRACTION98.9816700611
5.2913-28.08090.2225312818481510.1940991122191778X-RAY DIFFRACTION97.5227502528
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)
11.77884450176-0.814271882398-1.490756458856.292562516384.080035419714.67381333651-0.0987149500286-0.00683156194868-0.0896445824362-0.0347879359709-0.3025509909320.7295034321970.133280704096-0.3206402846370.302533628610.0977832294423-0.0294161600288-0.0001530643225580.14901121680.01849735246230.165118260552-9.47613986407-9.21916932182110.289183073
21.17345392268-0.305918440722-2.253720429021.034395613421.685401939615.599530809890.07241228911680.0266598111335-0.0745040798497-0.342033903966-0.2880746083110.670578568938-0.660957912907-1.488961457460.2793251324430.1949265590840.128177404506-0.06311492887530.6383256599130.05753026240410.472455623529-14.3421544748-6.73347803518106.838925159
33.561505535231.06778420168-3.517954830195.199063643520.8492654030234.21329068817-0.6754623017921.697514456210.166110689918-0.6097150755820.42834827365-0.08320254854460.486205878661-0.45414135640.4933694722390.8644399520410.295812686151-0.04667470051830.899263913653-0.04003958401760.383029070793-0.734238492554-16.099231069190.2586945679
48.369080204195.305474114585.932947874874.063807717883.999303872554.280797126640.283634163781.23336142320.299482666944-0.239393665811.04137497018-0.469513973481-0.04341257127121.0286526108-0.9542607062630.5678879700360.1376184658130.1645476867270.7275811610510.05680205739960.51020421789413.4762757764-18.829503005196.9927160983
58.75390201988-5.97351033716-5.929871674818.868962006155.727417927584.819913255470.00906354250828-0.4104204147850.3715938968690.2344610403810.0908829210534-0.5946504997790.5875376362890.181936761256-0.05744725401850.255669551156-0.0484430199625-0.02716305829250.31968671754-0.03085149304160.17038036578115.5675129127-11.2004919429112.851964662
68.710468159112.54283610811-1.278486460415.701230332844.997613998728.22375864613-0.598122673266-0.1851466186730.594461823774-0.7370933313960.01750312017080.815634078019-0.9893820304310.3989389096120.4108485345390.366272220730.0189392897379-0.09839864212190.292354360042-0.05241079698530.16543687664110.78228899361.96211975939127.547342205
73.4100109347-3.56240701289-2.44669710624.537660531383.99888601755.64189643967-0.01488511076710.08351384129120.4164626693360.01863388528570.0606289508288-0.189160628909-0.04947195645950.181263060802-0.03851727577330.133239304771-0.0153684641899-0.01234042819060.1232766634320.002318452701520.10523316369311.566804680911.613861821896.0099593298
81.631559387450.137740066932-0.09464477862694.423950991172.636671102884.01276115093-0.05229407237230.211464841984-0.107571833362-0.06247060035470.01736728880540.276573172852-0.1055820823080.06511069721950.06719114731090.06142944729170.0121633336935-0.006068716193810.1178518850440.0002088469572360.0935777883785.865408172582.3656202133883.0539226477
94.675019449913.007332487622.556876238142.850792445421.158698046983.040713816260.104849429188-0.105033928004-0.229005056706-0.0836357970373-0.0767180596296-0.234393692394-0.1433406054630.239869124610.03030983725920.0901217030703-0.002814117466060.02105258000610.1325998000270.01663055572330.11332948166615.95442525092.5001666305993.8569495101
102.891678218972.798042070982.078327566694.357188850832.815806024992.19892350602-0.1118457313260.0594788019499-0.5096937398730.2694650023660.284461388701-0.1708705461640.1164953132140.260859699925-0.3809391855390.108000767085-0.0304159877245-0.01461677211740.193401496653-0.02466840717920.1221330874597.54173131829-3.0460050512594.9518724133
111.81251207232-0.12699012935-0.5803296104031.645676742010.306420026343.514770473170.01625327006250.1070906083580.003706881777550.0369631903003-0.1599472653290.0508954442538-0.193896434124-0.5467328307040.02539620968590.0590618479517-0.02223974739920.0053789971330.09254336229070.004012965497560.1351830834711.735051813353.4516307575688.3962439564
125.745329401511.563903584032.857743568043.016855441540.7242179789096.72592192530.141177307252-0.2216026262240.1924417474280.551101286884-0.17871520333-0.0945253612680.01361418001340.303026225911-0.0532920624460.154457120571-0.0209792559497-0.002600291324430.114652592147-0.01288757187970.1448604523752.956682880372.3431699746898.5268498779
135.60074340953-2.93702121982-4.807538970125.053018415931.36658539267.5961784850.266980974996-1.274183570850.4179679510091.371319228060.083979538469-0.5982808434160.9060789584840.762574534553-0.2735142759610.499189425933-0.123371942-0.1403916071630.493666487733-0.0359823355280.29565312225923.701946343311.4508592633104.489663099
148.63240079007-0.211039031641.646061313769.329629940953.406721536566.655342494830.03476800388150.5513018728780.347710355023-0.530003005218-0.175246298232-0.8792814372350.1067338557770.8064387478810.0672037618680.255009338947-0.05053370063030.02229321862070.4342215623150.0417904341490.21493367930426.69662889939.5075000405587.2030962864
153.157101231941.71385326709-0.118919330935.041340643692.055890299943.203935616730.369360004177-0.5345871012140.1559256280440.8511533370450.275591175155-0.008604977081440.5011528211080.293453717330.2854172185760.1188175000210.0675629450278-0.1693135500450.157393894830.08663794297970.11863087092422.52624715441.1152643465468.8849722161
162.603883941190.1071076299470.7002526196196.22398348744.134239939514.790483334390.07374070930250.04968255559160.0211203312025-0.538946275458-0.1145844669030.107502346232-0.192786030336-0.04361352665290.02174444005060.07589084243430.01421839971050.001048554330230.07514206004880.001992812400540.08340105881511.79462589867-15.8559167453104.766431821
170.233805609147-0.09010812043340.8534066077335.154039054160.3912627421323.358433214420.242730426338-0.20593157520.035484977542-0.260030178769-0.251900289660.03058929127540.4998970745790.1246415912640.002886140697240.09139044976370.008547058577930.00983361063920.153059023758-0.01736830256330.155271704711.54096774952-19.7526573897106.833054591
181.79768756089-1.07785501539-0.704694916342.822542472541.107592600573.431013985730.0648593315286-0.03162338085280.05204356819390.03315652553470.0377507663244-0.0178466394589-0.09907995280240.143220790861-0.1034868700720.0459484391155-0.03258354501390.02741715578170.106781056602-0.01196553210360.134743065596-4.23003737175-5.64022423462111.495639434
193.1406899662-1.37428096051-1.266837301842.278122257231.008563498273.389401842320.09955570473670.1396780613090.200375684187-0.2030890569080.0304791519998-0.261440660149-0.347898930317-0.16329267417-0.06995231615950.1190755209820.00431262264490.03682925551350.1469362802690.02877079051880.08135988457842.5454626425-6.8094734179102.988823351
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 463 through 492 )
2X-RAY DIFFRACTION2chain 'B' and (resid 493 through 503 )
3X-RAY DIFFRACTION3chain 'B' and (resid 504 through 511 )
4X-RAY DIFFRACTION4chain 'B' and (resid 512 through 524 )
5X-RAY DIFFRACTION5chain 'B' and (resid 525 through 537 )
6X-RAY DIFFRACTION6chain 'B' and (resid 538 through 545 )
7X-RAY DIFFRACTION7chain 'A' and (resid 394 through 421 )
8X-RAY DIFFRACTION8chain 'A' and (resid 422 through 436 )
9X-RAY DIFFRACTION9chain 'A' and (resid 437 through 453 )
10X-RAY DIFFRACTION10chain 'A' and (resid 454 through 462 )
11X-RAY DIFFRACTION11chain 'A' and (resid 463 through 492 )
12X-RAY DIFFRACTION12chain 'A' and (resid 493 through 511 )
13X-RAY DIFFRACTION13chain 'A' and (resid 512 through 524 )
14X-RAY DIFFRACTION14chain 'A' and (resid 525 through 536 )
15X-RAY DIFFRACTION15chain 'A' and (resid 537 through 546 )
16X-RAY DIFFRACTION16chain 'B' and (resid 394 through 408 )
17X-RAY DIFFRACTION17chain 'B' and (resid 409 through 421 )
18X-RAY DIFFRACTION18chain 'B' and (resid 422 through 444 )
19X-RAY DIFFRACTION19chain 'B' and (resid 445 through 462 )

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