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- PDB-8vdu: Crystal structure of hybrid insulin peptide (InsC8-15-IAPP74-80) ... -

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Basic information

Entry
Database: PDB / ID: 8vdu
TitleCrystal structure of hybrid insulin peptide (InsC8-15-IAPP74-80) bound to HLA-DQ8
Components
  • (MHC class II HLA-DQ- ...) x 2
  • Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)
KeywordsIMMUNE SYSTEM / pMHC II complex
Function / homology
Function and homology information


antigen processing and presentation of peptide or polysaccharide antigen via MHC class II / MHC class II protein complex / adaptive immune response / endosome membrane / lysosomal membrane
Similarity search - Function
MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site ...MHC class II, beta chain, N-terminal / Class II histocompatibility antigen, beta domain / Class II histocompatibility antigen, beta domain / MHC class II, alpha chain, N-terminal / Class II histocompatibility antigen, alpha domain / Class II histocompatibility antigen, alpha domain / MHC class II, alpha/beta chain, N-terminal / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / MHC class II HLA-DQ-beta-1 / MHC class II HLA-DQ-alpha chain
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å
AuthorsTran, T.M. / Lim, J.J. / Loh, T.Y. / Mannering, I.S. / Rossjohn, J. / Reid, H.H.
Funding support Australia, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP1123586. Australia
National Health and Medical Research Council (NHMRC, Australia)APP1123586 Australia
CitationJournal: J.Biol.Chem. / Year: 2024
Title: A structural basis of T cell cross-reactivity to native and spliced self-antigens presented by HLA-DQ8.
Authors: Tran, M.T. / Lim, J.J. / Loh, T.J. / Mannering, S.I. / Rossjohn, J. / Reid, H.H.
History
DepositionDec 17, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 7, 2024Provider: repository / Type: Initial release
Revision 1.1Aug 14, 2024Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Sep 4, 2024Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.3Nov 20, 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
A: MHC class II HLA-DQ-alpha chain
B: MHC class II HLA-DQ-beta-1
C: Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)
D: MHC class II HLA-DQ-alpha chain
E: MHC class II HLA-DQ-beta-1
F: Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)
G: MHC class II HLA-DQ-alpha chain
H: MHC class II HLA-DQ-beta-1
I: Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)
J: MHC class II HLA-DQ-alpha chain
K: MHC class II HLA-DQ-beta-1
L: Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)182,22518
Polymers180,76212
Non-polymers1,4626
Water181
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)72.319, 138.116, 101.832
Angle α, β, γ (deg.)90.000, 102.498, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 0 through 36 or (resid 37...
d_2ens_1(chain "D" and (resid 0 through 36 or (resid 37...
d_3ens_1(chain "G" and (resid 0 through 48 or (resid 49...
d_4ens_1(chain "J" and (resid 0 through 36 or (resid 37...
d_1ens_2(chain "B" and (resid 3 through 21 or (resid 22...
d_2ens_2(chain "E" and (resid 3 through 21 or (resid 22...
d_3ens_2(chain "H" and (resid 3 through 47 or (resid 48...
d_4ens_2(chain "K" and (resid 3 through 21 or (resid 22...
d_1ens_3(chain "C" and (resid 1 through 2 or (resid 3...
d_2ens_3(chain "F" and ((resid 1 and (name N or name...
d_3ens_3(chain "I" and ((resid 1 and (name N or name...
d_4ens_3chain "L"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1ASPASPALAALAAA0 - 1572 - 160
d_12ens_1GLUGLUGLUGLUAA159 - 181162 - 184
d_21ens_1ASPASPALAALADD0 - 1572 - 160
d_22ens_1GLUGLUGLUGLUDD159 - 181162 - 184
d_31ens_1ASPASPGLUGLUGG0 - 1812 - 184
d_41ens_1ASPASPALAALAJJ0 - 1572 - 160
d_42ens_1GLUGLUGLUGLUJJ159 - 181162 - 184
d_11ens_2SERSERALAALABB3 - 1903 - 190
d_21ens_2SERSERSERSEREE3 - 1043 - 104
d_22ens_2HISHISGLUGLUEE111 - 162111 - 162
d_23ens_2ARGARGALAALAEE167 - 190167 - 190
d_31ens_2SERSERSERSERHH3 - 1043 - 104
d_32ens_2HISHISGLUGLUHH111 - 162111 - 162
d_33ens_2ARGARGALAALAHH167 - 190167 - 190
d_41ens_2SERSERSERSERKK3 - 1043 - 104
d_42ens_2HISHISGLUGLUKK111 - 162111 - 162
d_43ens_2ARGARGALAALAKK167 - 190167 - 190
d_11ens_3GLNGLNCYSCYSCC1 - 132 - 14
d_21ens_3GLNGLNCYSCYSFF1 - 132 - 14
d_31ens_3GLNGLNCYSCYSII1 - 132 - 14
d_41ens_3GLNGLNCYSCYSLL1 - 132 - 14

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(0.64475729747, 0.53308039822, -0.547825990979), (0.709044367871, -0.149356211451, 0.689165296929), (0.285559296379, -0.832777287835, -0.474276161236)9.53172136091, 59.0375960008, 70.1775887204
2given(-0.359885526516, 0.929022433065, 0.0860216639338), (0.932760853051, 0.360334057259, 0.010796212027), (-0.0209666120122, 0.0841230410815, -0.996234769088)-15.0490600399, 9.35395256389, -2.02767091171
3given(-0.278121397693, -0.757051765562, -0.591203105882), (-0.3500667681, 0.653042981986, -0.671556491704), (0.894484066944, 0.0201863304643, -0.446643891759)44.3078197751, -23.6935637463, 42.3178663184
4given(0.63514675913, 0.526992951732, -0.564683117502), (0.730293887353, -0.171670301723, 0.661211120295), (0.251514278843, -0.832350729159, -0.493895567106)9.72343115357, 60.0604867806, 69.9781993157
5given(-0.329518124273, 0.940654076101, 0.0811647392024), (0.942525198801, 0.332773603608, -0.0301326793734), (-0.0553539104267, 0.066570547966, -0.996245103749)-14.7214602387, 10.7185699259, -2.04022182044
6given(-0.303642622367, -0.749146428277, -0.588711123457), (-0.354152093013, 0.662355767528, -0.660197797813), (0.884521030217, 0.00802908594342, -0.46643121774)43.5625280492, -23.9239068717, 42.7319203811
7given(0.697290465711, 0.550009802707, -0.459646846345), (0.637169334635, -0.181882537918, 0.748955259947), (0.328330999801, -0.815112237257, -0.477274339603)8.37777997899, 57.6351409898, 70.9612827411
8given(-0.353240686224, 0.931121383257, 0.0907413204558), (0.93526366696, 0.349149107413, 0.0581100168433), (0.0224252282216, 0.105393882341, -0.994177669586)-15.4766059117, 8.76024669946, -1.77696702319
9given(-0.263567325418, -0.763378086399, -0.589733975771), (-0.37278189305, 0.644459703222, -0.667611676903), (0.889699907377, 0.0438815237844, -0.454432048479)44.2868966531, -24.1893736781, 42.1048462957

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Components

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MHC class II HLA-DQ- ... , 2 types, 8 molecules ADGJBEHK

#1: Protein
MHC class II HLA-DQ-alpha chain / DQA1*03:01 (DQ8-alpha chain)


Mass: 21124.516 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DQA1 / Plasmid: pZip3 / Cell line (production host): High Five (BTI-Tn-5B1-4) / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): DH10B / References: UniProt: Q30069
#2: Protein
MHC class II HLA-DQ-beta-1 / DQB1*03:02 (DQ8-beta chain)


Mass: 22605.383 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-DQB1 / Plasmid: pZip3 / Cell line (production host): High Five (BTI-Tn-5B1-4) / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): DH10B / References: UniProt: O19707

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Protein/peptide , 1 types, 4 molecules CFIL

#3: Protein/peptide
Hybrid insulin peptide (HIP; InsC8-15-IAPP74-80)


Mass: 1460.632 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pZip3 / Cell line (production host): High Five (BTI-Tn-5B1-4) / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): DH10B

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Sugars , 2 types, 4 molecules

#4: Polysaccharide beta-D-mannopyranose-(3-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(3-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb3-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+3)][b-D-Manp]{}}}}LINUCSPDB-CARE
#5: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 3 molecules

#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.75 Å3/Da / Density % sol: 55.22 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 0.2 M Monopotassium phosphate, 17% PEG 8K

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 26, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 3.5→49.4 Å / Num. obs: 28794 / % possible obs: 97.9 % / Redundancy: 4.2 % / Biso Wilson estimate: 45.35 Å2 / CC1/2: 0.907 / Net I/σ(I): 4.6
Reflection shellResolution: 3.5→3.5 Å / Mean I/σ(I) obs: 2 / Num. unique obs: 4228 / CC1/2: 0.414

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Processing

Software
NameVersionClassification
PHENIX1.19_4092refinement
autoXDSdata reduction
Coot0.9.8.92model building
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.5→49.04 Å / SU ML: 0.387 / Cross valid method: FREE R-VALUE / σ(F): 100 / Phase error: 24.1523
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2457 1216 4.93 %
Rwork0.2075 23474 -
obs0.2094 24690 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 42.5 Å2
Refinement stepCycle: LAST / Resolution: 3.5→49.04 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12100 0 95 1 12196
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.002212516
X-RAY DIFFRACTIONf_angle_d0.625317103
X-RAY DIFFRACTIONf_chiral_restr0.0461933
X-RAY DIFFRACTIONf_plane_restr0.00412206
X-RAY DIFFRACTIONf_dihedral_angle_d12.74964419
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS0.759841712242
ens_1d_3AAX-RAY DIFFRACTIONTorsion NCS0.697423991026
ens_1d_4AAX-RAY DIFFRACTIONTorsion NCS0.797634636585
ens_2d_2BBX-RAY DIFFRACTIONTorsion NCS1.16255353424
ens_2d_3BBX-RAY DIFFRACTIONTorsion NCS1.13704789378
ens_2d_4BBX-RAY DIFFRACTIONTorsion NCS1.10075085038
ens_3d_2CCX-RAY DIFFRACTIONTorsion NCS0.973836068634
ens_3d_3CCX-RAY DIFFRACTIONTorsion NCS1.0900324725
ens_3d_4CCX-RAY DIFFRACTIONTorsion NCS0.933968022756
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5-3.640.29191240.2552627X-RAY DIFFRACTION100
3.64-3.810.27441570.24882573X-RAY DIFFRACTION99.82
3.81-4.010.28811360.22772575X-RAY DIFFRACTION99.78
4.01-4.260.26121270.20622615X-RAY DIFFRACTION99.96
4.26-4.590.22081090.18082605X-RAY DIFFRACTION99.96
4.59-5.050.22151420.16552608X-RAY DIFFRACTION100
5.05-5.780.22081250.19572603X-RAY DIFFRACTION100
5.78-7.270.25181300.2342646X-RAY DIFFRACTION100
7.27-49.040.21831660.19522622X-RAY DIFFRACTION99.82
Refinement TLS params.Method: refined / Origin x: 12.07 Å / Origin y: 24.425 Å / Origin z: 18.875 Å
111213212223313233
T0.175074803142 Å20.0264361078222 Å20.00812461546138 Å2-0.303727457575 Å2-0.00942121235874 Å2--0.262574850619 Å2
L-0.00162127450911 °20.0461059039098 °20.0288188063648 °2-0.346763564696 °20.0796276612713 °2--0.191232875438 °2
S-0.0298155850557 Å °-0.0724780689361 Å °-0.00739807234 Å °-0.0247024908231 Å °0.0475136219445 Å °0.0226792817671 Å °0.0337700589958 Å °0.0799456498393 Å °-0.0120480589304 Å °
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )A0 - 181
2X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )A601
3X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )A602
4X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )B3 - 191
5X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )C1 - 14
6X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )D0 - 181
7X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )E3 - 190
8X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )E201
9X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )F1 - 14
10X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )G0 - 181
11X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )H3 - 190
12X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )H201
13X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )I0 - 14
14X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )J0 - 181
15X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )J201
16X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )K3 - 191
17X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )K201
18X-RAY DIFFRACTION1( CHAIN A AND ( RESID 0:181 OR RESID 601:601 OR RESID 602:602 ) ) OR ( CHAIN B AND RESID 3:191 ) OR ( CHAIN C AND RESID 1:14 ) OR ( CHAIN D AND RESID 0:181 ) OR ( CHAIN E AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN F AND RESID 1:14 ) OR ( CHAIN G AND RESID 0:181 ) OR ( CHAIN H AND ( RESID 3:190 OR RESID 201:201 ) ) OR ( CHAIN I AND RESID 0:14 ) OR ( CHAIN J AND ( RESID 0:181 OR RESID 201:201 ) ) OR ( CHAIN K AND ( RESID 3:191 OR RESID 201:201 ) ) OR ( CHAIN L AND RESID 1:13 )L1 - 13

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