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- PDB-7pqo: Catalytic fragment of MASP-1 in complex with P1 site mutant ecotin -

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Basic information

Entry
Database: PDB / ID: 7pqo
TitleCatalytic fragment of MASP-1 in complex with P1 site mutant ecotin
Components
  • Ecotin
  • Mannan-binding lectin serine protease 1
KeywordsIMMUNE SYSTEM / serine protease / complement / inhibitor
Function / homology
Function and homology information


Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / negative regulation of complement activation / complement activation, lectin pathway / zymogen activation / Scavenging by Class A Receptors / Initial triggering of complement / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type endopeptidase inhibitor activity / defense response ...Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / negative regulation of complement activation / complement activation, lectin pathway / zymogen activation / Scavenging by Class A Receptors / Initial triggering of complement / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type endopeptidase inhibitor activity / defense response / calcium-dependent protein binding / peptidase activity / outer membrane-bounded periplasmic space / serine-type endopeptidase activity / calcium ion binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein homodimerization activity / extracellular space / extracellular region / nucleoplasm / identical protein binding / cytosol
Similarity search - Function
Ecotin, C-terminal / Proteinase inhibitor I11, ecotin / Proteinase inhibitor I11, ecotin, gammaproteobacteria / Ecotin superfamily / Ecotin / Peptidase S1A, complement C1r/C1S/mannan-binding / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. ...Ecotin, C-terminal / Proteinase inhibitor I11, ecotin / Proteinase inhibitor I11, ecotin, gammaproteobacteria / Ecotin superfamily / Ecotin / Peptidase S1A, complement C1r/C1S/mannan-binding / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / EGF-like domain signature 2. / EGF-like domain / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Ecotin / Mannan-binding lectin serine protease 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Escherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.39 Å
AuthorsHarmat, V. / Fodor, K. / Heja, D.
Funding support Hungary, 6items
OrganizationGrant numberCountry
Ministry of Human Capacities2018-1.2.1-NKP-2018-00005 Hungary
National Research Development and Innovation Office (NKFIH)OTKA K 119386 Hungary
National Research Development and Innovation Office (NKFIH)OTKA K 119374 Hungary
National Research Development and Innovation Office (NKFIH)OTKA K 135289 Hungary
European Regional Development FundVEKOP-2.3.3-15-2017-00018 Hungary
European Regional Development FundVEKOP-2.3.2-16-2017-00014 Hungary
Citation
Journal: J.Biol.Chem. / Year: 2022
Title: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.
Authors: Nagy, Z.A. / Heja, D. / Bencze, D. / Kiss, B. / Boros, E. / Szakacs, D. / Fodor, K. / Wilmanns, M. / Kocsis, A. / Dobo, J. / Gal, P. / Harmat, V. / Pal, G.
#1: Journal: Acta Crystallogr D Biol Crystallogr / Year: 2012
Title: Towards automated crystallographic structure refinement with phenix.refine.
Authors: Afonine, P.V. / Grosse-Kunstleve, R.W. / Echols, N. / Headd, J.J. / Moriarty, N.W. / Mustyakimov, M. / Terwilliger, T.C. / Urzhumtsev, A. / Zwart, P.H. / Adams, P.D.
#2: Journal: Acta Crystallogr D Biol Crystallogr / Year: 2010
Title: PHENIX: a comprehensive Python-based system for macromolecular structure solution.
Authors: Paul D Adams / Pavel V Afonine / Gábor Bunkóczi / Vincent B Chen / Ian W Davis / Nathaniel Echols / Jeffrey J Headd / Li-Wei Hung / Gary J Kapral / Ralf W Grosse-Kunstleve / Airlie J McCoy ...Authors: Paul D Adams / Pavel V Afonine / Gábor Bunkóczi / Vincent B Chen / Ian W Davis / Nathaniel Echols / Jeffrey J Headd / Li-Wei Hung / Gary J Kapral / Ralf W Grosse-Kunstleve / Airlie J McCoy / Nigel W Moriarty / Robert Oeffner / Randy J Read / David C Richardson / Jane S Richardson / Thomas C Terwilliger / Peter H Zwart /
Abstract: Macromolecular X-ray crystallography is routinely applied to understand biological processes at a molecular level. However, significant time and effort are still required to solve and complete many ...Macromolecular X-ray crystallography is routinely applied to understand biological processes at a molecular level. However, significant time and effort are still required to solve and complete many of these structures because of the need for manual interpretation of complex numerical data using many software packages and the repeated use of interactive three-dimensional graphics. PHENIX has been developed to provide a comprehensive system for macromolecular crystallographic structure solution with an emphasis on the automation of all procedures. This has relied on the development of algorithms that minimize or eliminate subjective input, the development of algorithms that automate procedures that are traditionally performed by hand and, finally, the development of a framework that allows a tight integration between the algorithms.
#3: Journal: Acta Crystallogr D Biol Crystallogr / Year: 2010
Title: XDS.
Authors: Kabsch, W.
#4: Journal: Acta Crystallogr D Biol Crystallogr / Year: 2010
Title: Molecular replacement with MOLREP.
Authors: Vagin, A. / Teplyakov, A.
#5: Journal: PLoS Pathog / Year: 2019
Title: Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.
Authors: Nagy, Z.A. / Szakacs, D. / Boros, E. / Heja, D. / Vigh, E. / Sandor, N. / Jozsi, M. / Oroszlan, G. / Dobo, J. / Gal, P. / Pal, G.
History
DepositionSep 17, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 18, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 8, 2022Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.title
Revision 1.2Jan 31, 2024Group: 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
Revision 1.3Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Mannan-binding lectin serine protease 1
K: Ecotin
A: Mannan-binding lectin serine protease 1
B: Mannan-binding lectin serine protease 1
I: Ecotin
J: Ecotin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)191,94514
Polymers191,2776
Non-polymers6688
Water00
1
C: Mannan-binding lectin serine protease 1
K: Ecotin
hetero molecules

C: Mannan-binding lectin serine protease 1
K: Ecotin
hetero molecules


  • defined by author&software
  • Evidence: gel filtration
  • 128 kDa, 4 polymers
Theoretical massNumber of molelcules
Total (without water)127,93210
Polymers127,5184
Non-polymers4146
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z1
Buried area12200 Å2
ΔGint-65 kcal/mol
Surface area47980 Å2
MethodPISA
2
A: Mannan-binding lectin serine protease 1
B: Mannan-binding lectin serine protease 1
I: Ecotin
J: Ecotin
hetero molecules


  • defined by author&software
  • Evidence: gel filtration
  • 128 kDa, 4 polymers
Theoretical massNumber of molelcules
Total (without water)127,9799
Polymers127,5184
Non-polymers4605
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10650 Å2
ΔGint-57 kcal/mol
Surface area46490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)251.066, 251.066, 211.585
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number97
Space group name H-MI422
Space group name HallI42
Symmetry operation#1: x,y,z
#2: -y,x,z
#3: y,-x,z
#4: x,-y,-z
#5: -x,y,-z
#6: -x,-y,z
#7: y,x,-z
#8: -y,-x,-z
#9: x+1/2,y+1/2,z+1/2
#10: -y+1/2,x+1/2,z+1/2
#11: y+1/2,-x+1/2,z+1/2
#12: x+1/2,-y+1/2,-z+1/2
#13: -x+1/2,y+1/2,-z+1/2
#14: -x+1/2,-y+1/2,z+1/2
#15: y+1/2,x+1/2,-z+1/2
#16: -y+1/2,-x+1/2,-z+1/2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
12
22
32

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
111GLUGLUCYSCYS(chain 'A' and (resid 300 through 302 or resid 306...AC300 - 3017 - 8
121PROPROGLUGLU(chain 'A' and (resid 300 through 302 or resid 306...AC306 - 31313 - 20
131PHEPHEPROPRO(chain 'A' and (resid 300 through 302 or resid 306...AC320 - 43927 - 146
141ILEILEASNASN(chain 'A' and (resid 300 through 302 or resid 306...AC449 - 699156 - 406
211GLUGLUCYSCYS(chain 'B' and (resid 300 through 310 or (resid 311...BD300 - 3017 - 8
221PROPROGLUGLU(chain 'B' and (resid 300 through 310 or (resid 311...BD306 - 31313 - 20
231PHEPHEPROPRO(chain 'B' and (resid 300 through 310 or (resid 311...BD320 - 43927 - 146
241ILEILEASNASN(chain 'B' and (resid 300 through 310 or (resid 311...BD449 - 699156 - 406
311GLUGLUCYSCYS(chain 'C' and (resid 300 through 302 or resid 306...CA300 - 3017 - 8
321PROPROGLUGLU(chain 'C' and (resid 300 through 302 or resid 306...CA306 - 31313 - 20
331PHEPHEPROPRO(chain 'C' and (resid 300 through 302 or resid 306...CA320 - 43927 - 146
341ILEILEASNASN(chain 'C' and (resid 300 through 302 or resid 306...CA449 - 699156 - 406
152VALVALARGARG(chain 'I' and (resid 4 through 7 or (resid 8...IE4 - 14224 - 162
252VALVALARGARG(chain 'J' and (resid 4 through 9 or (resid 10...JF4 - 14224 - 162
352VALVALARGARG(chain 'K' and ((resid 4 through 5 and (name N...KB4 - 14224 - 162

NCS ensembles :
ID
1
2

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Components

#1: Protein Mannan-binding lectin serine protease 1 / Complement factor MASP-3 / Complement-activating component of Ra-reactive factor / Mannose-binding ...Complement factor MASP-3 / Complement-activating component of Ra-reactive factor / Mannose-binding lectin-associated serine protease 1 / MASP-1 / Mannose-binding protein-associated serine protease / Ra-reactive factor serine protease p100 / RaRF / Serine protease 5


Mass: 45519.047 Da / Num. of mol.: 3 / Mutation: GLU 499 LYS is a natural variant
Source method: isolated from a genetically manipulated source
Details: ASMT expression tag is followed by residue 298 of the sequence. The enzyme is activated: the peptide bond between residues 448 and 449 is hydrolyzed.
Source: (gene. exp.) Homo sapiens (human) / Gene: MASP1, CRARF, CRARF1, PRSS5 / Plasmid: pET-17B / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): pLYSS
References: UniProt: P48740, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
#2: Protein Ecotin


Mass: 18240.020 Da / Num. of mol.: 3 / Mutation: M84R
Source method: isolated from a genetically manipulated source
Details: ecotin, M84R mutant
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: eco, eti, b2209, JW2197 / Production host: Escherichia coli (E. coli) / References: UniProt: P23827
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
Has ligand of interestN
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: 4.36 Å3/Da / Density % sol: 71.78 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 3.7M NaCl, 0.1M HEPES, pH 7.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Nov 9, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8726 Å / Relative weight: 1
ReflectionResolution: 3.4→40 Å / Num. obs: 45525 / % possible obs: 97.1 % / Redundancy: 7.49 % / Biso Wilson estimate: 114.18 Å2 / CC1/2: 0.997 / Rrim(I) all: 0.021 / Net I/σ(I): 13.02
Reflection shellResolution: 3.4→3.49 Å / Redundancy: 5.54 % / Mean I/σ(I) obs: 0.74 / Num. unique obs: 3058 / CC1/2: 0.595 / Rrim(I) all: 2.55 / % possible all: 90.1

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PHENIX1.17.1_3660refinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB structure 1AZZ and SP and CCP1-CCP2 fragments of PDB structure 3GOV were used.

1azz

3gov


Resolution: 3.39→39.6 Å / SU ML: 0.6306 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 34.7676
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2969 2261 4.99 %
Rwork0.2568 43026 -
obs0.2588 45287 96.33 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 134.57 Å2
Refinement stepCycle: LAST / Resolution: 3.39→39.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11330 0 43 0 11373
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.002411656
X-RAY DIFFRACTIONf_angle_d0.550715990
X-RAY DIFFRACTIONf_chiral_restr0.04451805
X-RAY DIFFRACTIONf_plane_restr0.00482113
X-RAY DIFFRACTIONf_dihedral_angle_d6.23671689
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.39-3.460.391180.42712167X-RAY DIFFRACTION79.12
3.46-3.540.46181340.42972472X-RAY DIFFRACTION90.27
3.54-3.630.46581450.40122649X-RAY DIFFRACTION95.52
3.63-3.730.41071260.38922640X-RAY DIFFRACTION95.84
3.73-3.840.41531690.38552633X-RAY DIFFRACTION96.29
3.84-3.960.36981320.36132668X-RAY DIFFRACTION96.72
3.96-4.10.37961430.31432676X-RAY DIFFRACTION96.81
4.1-4.270.32351200.29262717X-RAY DIFFRACTION97.32
4.27-4.460.28171500.2412730X-RAY DIFFRACTION98.6
4.46-4.690.23171320.22442770X-RAY DIFFRACTION98.54
4.69-4.990.24281670.19922719X-RAY DIFFRACTION98.77
4.99-5.370.24911470.20392755X-RAY DIFFRACTION99.01
5.37-5.910.25511420.21332804X-RAY DIFFRACTION99.23
5.91-6.760.27211420.2242805X-RAY DIFFRACTION99.56
6.76-8.510.2691310.22882864X-RAY DIFFRACTION99.67
8.51-39.60.27311630.2182957X-RAY DIFFRACTION99.46
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)
14.21051275967-1.356393961351.411140389574.159443711582.271237792684.47281651876-0.4811187593360.6362818592051.845349342770.3446717486040.02106872049590.456045107856-0.1735247670170.1902904180070.4656642821890.9269581923350.1447680007860.2367556371791.65658166303-0.02267024772661.99871545863-11.3075059174103.53443355926.5207555304
26.22835486937-4.562020089081.043860683385.70444697902-1.576086747283.810072689560.262644017352-0.1470674250720.1282602126840.7620444247830.09123347636480.717336179385-0.252687960739-0.928993392381-0.3761836933091.020671522440.1415730118810.2128917224880.9191493572640.02044682733551.553562011124.192257893696.286403128232.5156990917
35.66959862122-0.280282240288-0.5201004445294.11475376732-0.09104730302854.630492566520.2379271648920.022102656887-0.05274480688960.0293214595681-0.236617955312-0.00525734087106-0.1718678021460.3705102256170.02099704928680.744788239470.0670435929610.03729335473440.7302428694590.02456033653610.43518637976653.995705470172.505822960228.5634258244
41.93551943915-0.435275987403-1.551207641941.106276182340.9341502698174.52214149354-0.504908979259-0.290926456528-0.5431337498710.2501004400150.09428056651530.2988109273040.2277900802671.064011668350.3075275978411.005231704670.1983133965450.1060206152750.9275569638870.09107176192920.70024170127764.654192210949.73637854366.17973525885
53.30873624005-1.353373553612.585210001063.8057628572.994178727196.704567046090.19434904150.250925793594-0.01099440115341.249004136680.5768623267340.1245127804432.214012931561.45908882425-0.8969322474241.723396551490.165107410410.1795329613691.14957975356-0.04202404309920.80490093608533.004588612217.5733423607-10.3271305481
61.466807373172.646019502892.865102064135.421424709776.111021515978.349006853510.108804380362-0.00875693109958-0.7382064001830.423384115575-0.229872435782-0.4183758097031.440986241850.4606427537460.02460182347731.597473222550.06852865761270.226403252271.00361127336-0.1746407666661.171735485434.276013979226.966199023626.1410466437
77.10778235093-0.87931163753-0.6789779249483.952405291380.5816645427135.48378940883-0.199294648371-0.434706250901-0.5251993486450.170951469583-0.0713928933891-0.09375831633250.2778552019080.08719684008970.2984332961890.57490963036-0.05005114372980.05129631380260.546400759408-0.02113430374860.65177677758527.202893183751.407928560254.4372654854
83.774213266292.36044213781-0.9466714772742.234397151980.1229469077640.956967016760.935747045316-0.5925420266170.954106451060.772202462271-1.43666116679-0.628678279553-1.10475221265-0.1333624138640.4745266172181.629834633880.3905943915410.02518090457071.347089939730.2369816993461.18197886306-36.6691077927135.48434776290.4750733044
90.0221769006637-0.328881505406-0.4898416344075.619450035565.024563321356.013780506070.09826553599070.0219061724437-0.1848833677881.10203694487-0.8345958158321.2708861020.0874756964088-0.8839073121680.7258769558561.330596760.3737763588510.4155930272671.016862667770.08671386192051.3661472755-39.896299748299.774759366186.2373304219
102.37684011840.032312309728-0.1056022237843.215654309550.06065183669991.812898822440.121866598685-0.447340278849-0.7899237276040.1823359099830.1109741603411.209127916090.210717590885-0.050904694176-0.2215027310720.819941609233-0.05194429961460.1515325376531.006252934360.07239148509022.27056849432-32.06702124268.875641586365.4192585528
115.70096156717-0.510412294271-0.5243711354195.777468494231.245822622642.157160481140.166114147511-0.5773462332610.418781244651-0.1365414634260.2016936822430.520535656617-0.438175182524-0.051640746838-0.3858190674250.758764850075-0.0535903300990.1508583765090.684837390427-0.04505628299730.8445070796632.9196023051773.993912102961.2661243751
124.78322611426-2.27563047284-0.1674091780882.548143952010.2611640118761.296075754370.4853767653630.142914432138-0.846143189824-0.700856348187-0.5041083222291.23098480126-0.271004079859-0.2111363798650.09466344220990.969886586913-0.0785330956124-0.2477381712780.948476327989-0.2692028181121.6577389669-7.2827762418457.672186413146.0948331999
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'C' and (resid 299 through 364 )
2X-RAY DIFFRACTION2chain 'C' and (resid 365 through 435 )
3X-RAY DIFFRACTION3chain 'C' and (resid 436 through 699 )
4X-RAY DIFFRACTION4chain 'K' and (resid 4 through 142 )
5X-RAY DIFFRACTION5chain 'A' and (resid 297 through 364 )
6X-RAY DIFFRACTION6chain 'A' and (resid 365 through 435 )
7X-RAY DIFFRACTION7chain 'A' and (resid 436 through 699 )
8X-RAY DIFFRACTION8chain 'B' and (resid 300 through 364 )
9X-RAY DIFFRACTION9chain 'B' and (resid 365 through 435 )
10X-RAY DIFFRACTION10chain 'B' and (resid 436 through 699 )
11X-RAY DIFFRACTION11chain 'I' and (resid 4 through 142 )
12X-RAY DIFFRACTION12chain 'J' and (resid 4 through 142 )

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