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- PDB-6byz: Structure of Cysteine-free Human Insulin-Degrading Enzyme in comp... -

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Basic information

Entry
Database: PDB / ID: 6byz
TitleStructure of Cysteine-free Human Insulin-Degrading Enzyme in complex with Substrate-selective Macrocyclic Inhibitor 37
Components
  • ALA-ALA-ALA
  • Insulin-degrading enzyme
KeywordsHYDROLASE/INHIBITOR / Insulin / Glucagon / Diabetes / Exo-site / HYDROLASE / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


insulysin / beta-endorphin binding / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / cytosolic proteasome complex / insulin binding ...insulysin / beta-endorphin binding / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / cytosolic proteasome complex / insulin binding / regulation of aerobic respiration / peptide catabolic process / amyloid-beta clearance / peroxisomal matrix / amyloid-beta metabolic process / positive regulation of protein binding / Insulin receptor recycling / negative regulation of proteolysis / peptide binding / proteolysis involved in protein catabolic process / Peroxisomal protein import / protein catabolic process / antigen processing and presentation of endogenous peptide antigen via MHC class I / metalloendopeptidase activity / positive regulation of protein catabolic process / insulin receptor signaling pathway / peroxisome / amyloid-beta binding / virus receptor activity / endopeptidase activity / basolateral plasma membrane / Ub-specific processing proteases / external side of plasma membrane / protein-containing complex binding / cell surface / protein homodimerization activity / ATP hydrolysis activity / mitochondrion / proteolysis / extracellular space / extracellular exosome / zinc ion binding / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Peptidase M16, middle/third domain / Middle or third domain of peptidase_M16 / : / PQQ synthase PqqF-like, C-terminal lobe domain 4 / : / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal ...Peptidase M16, middle/third domain / Middle or third domain of peptidase_M16 / : / PQQ synthase PqqF-like, C-terminal lobe domain 4 / : / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-J18 / Insulin-degrading enzyme
Similarity search - Component
Biological speciesHomo sapiens (human)
Escherichia coli BL21 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95624845742 Å
AuthorsTan, G.A. / Seeliger, M.A. / Maianti, J.P. / Liu, D.R.
CitationJournal: Nat.Chem.Biol. / Year: 2019
Title: Substrate-selective inhibitors that reprogram the activity of insulin-degrading enzyme.
Authors: Maianti, J.P. / Tan, G.A. / Vetere, A. / Welsh, A.J. / Wagner, B.K. / Seeliger, M.A. / Liu, D.R.
History
DepositionDec 21, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 3, 2019Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support
Revision 1.2May 29, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.3Oct 4, 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: Insulin-degrading enzyme
B: Insulin-degrading enzyme
D: ALA-ALA-ALA
E: ALA-ALA-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)237,9948
Polymers236,4004
Non-polymers1,5944
Water7,008389
1
A: Insulin-degrading enzyme
D: ALA-ALA-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,9974
Polymers118,2002
Non-polymers7972
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area910 Å2
ΔGint5 kcal/mol
Surface area38480 Å2
MethodPISA
2
B: Insulin-degrading enzyme
E: ALA-ALA-ALA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,9974
Polymers118,2002
Non-polymers7972
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area910 Å2
ΔGint5 kcal/mol
Surface area38700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)264.486, 264.486, 91.094
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number170
Space group name H-MP65
Space group name HallP65
Symmetry operation#1: x,y,z
#2: x-y,x,z+5/6
#3: y,-x+y,z+1/6
#4: -y,x-y,z+2/3
#5: -x+y,-x,z+1/3
#6: -x,-y,z+1/2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...
21(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...
12CHAIN D
22CHAIN E

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNASNASN(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA4444
121LYSLYSLYSLYS(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA119119
131ASNASNHISHIS(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA43 - 101143 - 1011
141ASNASNHISHIS(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA43 - 101143 - 1011
151ASNASNHISHIS(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA43 - 101143 - 1011
161ASNASNHISHIS(CHAIN A AND (RESID 44 THROUGH 118 OR (RESID 119...AA43 - 101143 - 1011
211ASNASNASNASN(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB4444
221GLUGLUGLUGLU(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB124124
231ASNASNHISHIS(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB44 - 101144 - 1011
241ASNASNHISHIS(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB44 - 101144 - 1011
251ASNASNHISHIS(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB44 - 101144 - 1011
261ASNASNHISHIS(CHAIN B AND (RESID 44 THROUGH 123 OR (RESID 124...BB44 - 101144 - 1011
112ALAALAALAALACHAIN DDC1 - 31 - 3
212ALAALAALAALACHAIN EED1 - 31 - 3

NCS ensembles :
ID
1
2

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Components

#1: Protein Insulin-degrading enzyme / Abeta-degrading protease / Insulin protease / Insulinase / Insulysin


Mass: 117968.664 Da / Num. of mol.: 2
Mutation: C110L, E111Q, C171S, C178A, C257V, C414L, C573N, C590S, C789S, C812A, C819A, C904S, C966N, C974A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IDE / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P14735, insulysin
#2: Protein/peptide ALA-ALA-ALA


Mass: 231.249 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: Polypeptide co-purified with Human Insulin-Degrading enzyme
Source: (natural) Escherichia coli BL21(DE3) (bacteria)
#3: Chemical ChemComp-J18 / [(8R,9S,10S)-9-(2',3'-dimethyl[1,1'-biphenyl]-4-yl)-6-{[2-(trifluoromethyl)phenyl]sulfonyl}-1,6-diazabicyclo[6.2.0]decan-10-yl]methanol


Mass: 558.655 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C30H33F3N2O3S / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES


Mass: 238.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 389 / 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: 4.13 Å3/Da / Density % sol: 70.24 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 0.1 M HEPES, 12% Tacsimate, 20% PEGMME-5000, 10% 1,4-dioxane

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 1.116 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 9, 2015
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.116 Å / Relative weight: 1
ReflectionResolution: 2.956→48.48 Å / Num. obs: 148881 / % possible obs: 99.8 % / Redundancy: 12.4 % / Biso Wilson estimate: 63.5189271246 Å2 / Net I/σ(I): 16.34
Reflection shellResolution: 2.956→3.062 Å / Mean I/σ(I) obs: 1.91 / Num. unique obs: 7521 / % possible all: 98.88

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LTE

4lte


Resolution: 2.95624845742→48.4799486587 Å / SU ML: 0.373683544509 / Cross valid method: FREE R-VALUE / σ(F): 1.35094572484 / Phase error: 20.7089500279
RfactorNum. reflection% reflection
Rfree0.202629282797 1997 2.61156425106 %
Rwork0.160914089223 --
obs0.162016770659 148838 99.8008515774 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 60.7670774468 Å2
Refinement stepCycle: LAST / Resolution: 2.95624845742→48.4799486587 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15653 0 108 389 16150
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0059791629266616159
X-RAY DIFFRACTIONf_angle_d0.84266370304421883
X-RAY DIFFRACTIONf_chiral_restr0.05146325262692352
X-RAY DIFFRACTIONf_plane_restr0.005130630524142824
X-RAY DIFFRACTIONf_dihedral_angle_d16.47715718859845
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A0X-RAY DIFFRACTIONPOSITIONAL0
12B0X-RAY DIFFRACTIONPOSITIONAL0
21D0X-RAY DIFFRACTIONPOSITIONAL0
22E0X-RAY DIFFRACTIONPOSITIONAL0
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9562-2.99230.407796021691360.3531803515014960X-RAY DIFFRACTION95.1633986928
2.9923-3.03020.3265378121911400.3116859355635232X-RAY DIFFRACTION100
3.0302-3.070.3257448735531320.2875085835865161X-RAY DIFFRACTION100
3.07-3.11210.3306850457581360.2590860055795182X-RAY DIFFRACTION100
3.1121-3.15650.2877650012781440.2398973767425190X-RAY DIFFRACTION100
3.1565-3.20360.3060135671681380.2335797395095113X-RAY DIFFRACTION100
3.2036-3.25370.2725377882231330.229279646695335X-RAY DIFFRACTION100
3.2537-3.3070.2375242132721380.2187655168245106X-RAY DIFFRACTION100
3.307-3.3640.2342795407981420.2094309723885189X-RAY DIFFRACTION100
3.364-3.42520.29405447431340.1943553994995193X-RAY DIFFRACTION100
3.4252-3.4910.2599513715151360.1873063027655282X-RAY DIFFRACTION100
3.491-3.56230.2267638803461360.1699136524485053X-RAY DIFFRACTION100
3.5623-3.63970.2187017020221460.1652504019695201X-RAY DIFFRACTION100
3.6397-3.72440.2159448713231400.1609326448545186X-RAY DIFFRACTION100
3.7244-3.81750.2299579201931400.1584270524235212X-RAY DIFFRACTION100
3.8175-3.92060.1977323038761380.1542575759725184X-RAY DIFFRACTION99.9812136014
3.9206-4.03590.2019090364771400.1477741298815139X-RAY DIFFRACTION100
4.0359-4.16610.1729538327551400.1310327812715231X-RAY DIFFRACTION100
4.1661-4.3150.1405580744471380.1244878234825198X-RAY DIFFRACTION100
4.315-4.48760.1498189959871380.1169605176025157X-RAY DIFFRACTION100
4.4876-4.69170.1764347182071420.1129996168155178X-RAY DIFFRACTION100
4.6917-4.93880.1523989124651400.1155552872825218X-RAY DIFFRACTION100
4.9388-5.24790.160945965541350.125397148515163X-RAY DIFFRACTION100
5.2479-5.65250.1812605179191400.1427068114465187X-RAY DIFFRACTION100
5.6525-6.22030.225118917321400.1624850415765184X-RAY DIFFRACTION100
6.2203-7.1180.1985455551691440.1642390531985171X-RAY DIFFRACTION100
7.118-8.95870.1613550493861440.1322234404785201X-RAY DIFFRACTION100
8.9587-48.48640.1356518672931370.1412349856165145X-RAY DIFFRACTION99.3043805227
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)
11.06775252224-0.1621945458190.09571959983120.998152473412-0.05791586055590.573702242013-0.0470390159868-0.01430137704320.2039290190680.013483707005-0.0301103088935-0.075451644322-0.213029036433-0.0525923393878-0.006733938715530.2981365818720.0180588015884-0.0749220708110.12208892556-0.0258832551360.267293846147114.031859634-32.079998324722.5646030851
20.259115964440.2155124762570.1573850918440.371714627485-0.1830474343620.428587499047-0.0509775292607-0.2014965848470.1119420280020.256024414198-0.0101847704716-0.101521589749-0.185676258642-0.06450633791053.60344785853E-50.433244492540.0259992296942-0.06547673949360.411506182319-0.07831524797230.328540903226115.31291611-43.525086800342.3163028899
30.35220190322-0.2204586227750.2404747449220.175369802523-0.1182737418490.1767587225450.0961212566332-0.123581703664-0.08424781830520.280835314239-0.11738370967-0.1427418378520.075324891074-0.1353889260781.27647280931E-70.3822013279650.02575403563220.04586409013440.4000589967990.02788817260650.336359823235112.81820587-59.912513636741.0966159358
41.3747135737-0.08446974299320.1291042645260.844818940602-0.4861217091820.580078614444-0.0848712407417-0.2671499832640.06977926648680.1480718003070.0123035292363-0.0901695138623-0.040352455396-0.0398986742242-0.0006213308614760.2741029920530.00235184791541-0.04103782943250.2386224632-0.02597622424420.194080744228116.051225233-54.517579292440.7848271904
50.948963137596-0.06860137726890.1241696603480.5436877902920.2413276840070.755191977684-0.0565178951588-0.0251217830473-0.1225707477230.00833991124070.0451709632919-0.02728433398430.03937639625380.0323914224068-2.33955778175E-60.257622090368-0.03068769517150.02010554424260.2073923136940.004830172240940.315002767604105.595431672-70.686900937721.5417230394
60.233743845482-0.0984717425530.274909835230.5675199907940.238407425630.5632402662150.0140423589860.0353170656811-0.139760546796-0.118162740295-0.06875222783620.111004248995-0.126560200519-0.186932339456-0.007033781235040.202752053448-0.06175079419830.00919941959740.256774084147-0.01346757514710.43684351180589.8233599227-65.903301330720.5895356711
71.01709637965-0.144260371143-0.2724926777220.805699608677-0.3099259810790.603578190601-0.01925574233180.0729911330331-0.0149059725208-0.08150496878150.1085163709380.154158260441-0.0844932556537-0.139697459932.33785725581E-50.224349420175-0.0394002852467-0.07281538815550.273561984009-0.02327788762050.24708474387991.2132189088-56.59622813239.77496842437
80.4468861125840.09760940880.06087924875850.1686891534280.1787082959010.169965027952-0.113830294116-0.1970793004950.09593066564470.1225952973480.2179483954710.147428634537-0.0259288578096-0.1942855963536.27409310551E-50.4364702739690.0731700497824-0.04415963870890.335314039382-0.04492458023980.49298247809989.2045983224-36.29001725711.9864078512
91.13399345483-0.04604575775510.09128994343931.25619958944-0.1617743868280.661807302062-0.03877362711160.1744081085860.089753683008-0.1096354604660.06737840099130.0743582533527-0.0092404805102-0.08268759415710.0001661858583670.3132491962750.0140574942773-0.06168148398870.3391750347450.005535036254950.31097197615191.2486959512-46.3688403194.14726446132
100.3844959554390.2678246780620.2227903399430.7969583712580.2013669954641.5667649722-0.03240056709920.1310398872060.021373458503-0.1190830368190.03913804360680.0330258803273-0.088642875492-0.3522208084710.0008612065734440.471220252414-0.0242871385164-0.02051898608460.452760258654-0.04205416812390.35660096289499.6140065452-10.0351586357-32.4599228589
110.5369492375890.181912192639-0.2415747725530.05875824461290.06115903023180.919017356712-0.0736776905410.032937131797-0.155950444416-0.03724086107590.0127268739231-0.1220007378210.174607245790.035559987476-8.64841404022E-60.4891970291-0.0352371283895-0.01037664175730.423499241271-0.01643522824780.497841807393120.352568781-12.5283391653-23.330853624
120.192906036476-0.1037867942250.0101343938630.329683778763-0.238479736350.1805319314650.03898315847220.0125047640804-0.005576159374820.397153000546-0.02807598437890.1196311959130.1105597780340.14321256211-9.97950777018E-50.47604482765-0.0774338262293-0.03893247499910.328453701055-0.007344132965050.424637690359121.920991487-5.94271572027-8.12503485375
130.4643649901320.2605171498690.1015082905220.8630949002210.05653650414741.05260007437-0.04712918217090.0875408161833-0.1510159500260.005684891526350.00269388894652-0.1442749827830.186944215340.1255790601240.0006785822629860.42703168743-0.0176729013528-0.0174063507660.3022693199940.001616192321020.384909709077120.325653359-10.2022315389-12.3624359439
140.784748174220.0264050528584-0.2010723667490.807215648481-0.1088947287810.872874476385-0.02592351857850.00717928503602-0.05557925701230.176713606194-0.02550131056290.127918701329-0.05878981473150.0178124004646-4.82030259724E-50.468173076507-0.04830377748040.01468625018170.238529395645-0.02509260269710.351439221763105.7637944867.616494683282.27358298096
150.418962238367-0.114300370213-0.03749921344540.5230190764860.09492244641970.4833764589580.103658735110.002391870953660.09931982123160.0434787694076-0.1654689110780.0615327498841-0.263794304558-0.0001445340547989.827204856E-50.620851289671-0.039583377885-0.02846685549320.27541718288-0.05284957234850.391242320397106.94295889721.5550175172-6.32200981957
160.7208985343280.143892657984-0.4169709122940.8738800532280.05167857364020.400949144006-0.09567633536210.116711766977-0.0410892996558-0.0724342725842-0.02114810692490.193795789192-0.032723275892-0.06245577210741.555937816E-50.430585087533-0.00841252088315-0.04378061943990.304176634423-0.05881007148270.39874318775494.775003418420.4729451315-13.7218470221
170.31753704770.129993718334-0.2196409151640.586447188739-0.07701214945680.151762828622-0.1425268199620.310080379447-0.140542961192-0.3198093589620.05526510569520.0394498867484-0.162473682613-0.1500261628870.3492361694180.813774188527-0.104566485034-0.03432948471920.512603320056-0.139272140550.45349193661194.015384982317.1666147436-34.0253735836
180.588647866195-0.447020848893-0.3574826242811.379971530020.2902659974411.48801779107-0.104431162050.1829572917660.0158296610159-0.140072509828-0.001226240802220.260463887769-0.116274615546-0.3010751793510.009862571975360.428069906759-0.0439662850177-0.05514709567890.349068092981-0.07371377390190.35911508997487.980340821819.316701814-23.0829959743
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 44 through 275 )
2X-RAY DIFFRACTION2chain 'A' and (resid 276 through 329 )
3X-RAY DIFFRACTION3chain 'A' and (resid 330 through 380 )
4X-RAY DIFFRACTION4chain 'A' and (resid 381 through 514 )
5X-RAY DIFFRACTION5chain 'A' and (resid 515 through 675 )
6X-RAY DIFFRACTION6chain 'A' and (resid 676 through 734 )
7X-RAY DIFFRACTION7chain 'A' and (resid 735 through 823 )
8X-RAY DIFFRACTION8chain 'A' and (resid 824 through 876 )
9X-RAY DIFFRACTION9chain 'A' and (resid 877 through 1011 )
10X-RAY DIFFRACTION10chain 'B' and (resid 44 through 275 )
11X-RAY DIFFRACTION11chain 'B' and (resid 276 through 329 )
12X-RAY DIFFRACTION12chain 'B' and (resid 330 through 380 )
13X-RAY DIFFRACTION13chain 'B' and (resid 381 through 514 )
14X-RAY DIFFRACTION14chain 'B' and (resid 515 through 675 )
15X-RAY DIFFRACTION15chain 'B' and (resid 676 through 734 )
16X-RAY DIFFRACTION16chain 'B' and (resid 735 through 823 )
17X-RAY DIFFRACTION17chain 'B' and (resid 824 through 876 )
18X-RAY DIFFRACTION18chain 'B' and (resid 877 through 1011 )

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