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- PDB-6p64: Alpha-beta TCR Binding to Neoantigen KQWLVWLFL Presented by HLA-A206 -

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Basic information

Entry
Database: PDB / ID: 6p64
TitleAlpha-beta TCR Binding to Neoantigen KQWLVWLFL Presented by HLA-A206
Components
  • 302TIL TCR alpha chain
  • 302TIL TCR beta chain
  • Beta-2-microglobulin
  • MHC class I antigen
  • Neoantigen peptide KQWLVWLFL
KeywordsIMMUNE SYSTEM / Neoantigen / Peptide/MHC / T Cell Receptor
Function / homology
Function and homology information


N-terminal peptidyl-L-cysteine N-palmitoylation / O-acyltransferase activity / HHAT G278V doesn't palmitoylate Hh-Np / palmitoyltransferase activity / smoothened signaling pathway / antigen processing and presentation of peptide antigen via MHC class I / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / negative regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression ...N-terminal peptidyl-L-cysteine N-palmitoylation / O-acyltransferase activity / HHAT G278V doesn't palmitoylate Hh-Np / palmitoyltransferase activity / smoothened signaling pathway / antigen processing and presentation of peptide antigen via MHC class I / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / negative regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / transferrin transport / cellular response to iron ion / Endosomal/Vacuolar pathway / lumenal side of endoplasmic reticulum membrane / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / MHC class II protein complex / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / Hedgehog ligand biogenesis / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of iron ion transport / regulation of erythrocyte differentiation / HFE-transferrin receptor complex / response to molecule of bacterial origin / MHC class I peptide loading complex / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / MHC class I protein complex / positive regulation of T cell activation / peptide antigen binding / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / multicellular organismal-level iron ion homeostasis / specific granule lumen / phagocytic vesicle membrane / recycling endosome membrane / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / negative regulation of epithelial cell proliferation / MHC class II protein complex binding / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / positive regulation of cellular senescence / tertiary granule lumen / DAP12 signaling / T cell differentiation in thymus / negative regulation of neuron projection development / ER-Phagosome pathway / protein refolding / early endosome membrane / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / immune response / endoplasmic reticulum lumen / Amyloid fiber formation / Golgi membrane / lysosomal membrane / external side of plasma membrane / focal adhesion / Neutrophil degranulation / endoplasmic reticulum membrane / GTP binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / cell surface / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / metal ion binding / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function
: / Membrane bound O-acyl transferase, MBOAT / MBOAT, membrane-bound O-acyltransferase family / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin ...: / Membrane bound O-acyl transferase, MBOAT / MBOAT, membrane-bound O-acyltransferase family / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / 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 / Immunoglobulins / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Beta-2-microglobulin / HLA class I antigen / Protein-cysteine N-palmitoyltransferase HHAT / MHC class I antigen
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.05 Å
AuthorsDevlin, J.R. / Baker, B.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: To be Published
Title: A T cell receptor peptide/MHC complex at 3.05 Angstrom resolution
Authors: Devlin, J.R. / Baker, B.M. / Harari, A.
History
DepositionMay 31, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 3, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 16, 2022Group: Author supporting evidence / Database references / Category: database_2 / pdbx_audit_support
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization
Revision 1.2Oct 11, 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
Revision 1.3Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MHC class I antigen
B: Beta-2-microglobulin
F: MHC class I antigen
G: Beta-2-microglobulin
D: 302TIL TCR alpha chain
E: 302TIL TCR beta chain
I: 302TIL TCR alpha chain
J: 302TIL TCR beta chain
C: Neoantigen peptide KQWLVWLFL
H: Neoantigen peptide KQWLVWLFL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)193,33715
Polymers192,87710
Non-polymers4605
Water57632
1
A: MHC class I antigen
B: Beta-2-microglobulin
C: Neoantigen peptide KQWLVWLFL
hetero molecules

D: 302TIL TCR alpha chain
E: 302TIL TCR beta chain


Theoretical massNumber of molelcules
Total (without water)96,6237
Polymers96,4385
Non-polymers1842
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_765-x+2,-y+1,z+1/21
2
I: 302TIL TCR alpha chain
J: 302TIL TCR beta chain
hetero molecules

F: MHC class I antigen
G: Beta-2-microglobulin
H: Neoantigen peptide KQWLVWLFL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,7158
Polymers96,4385
Non-polymers2763
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Unit cell
Length a, b, c (Å)276.641, 276.641, 112.465
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Space group name HallP612(x,y,z+5/12)
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/6
#3: y,-x+y,z+5/6
#4: -y,x-y,z+1/3
#5: -x+y,-x,z+2/3
#6: x-y,-y,-z
#7: -x,-x+y,-z+2/3
#8: -x,-y,z+1/2
#9: y,x,-z+1/3
#10: -y,-x,-z+5/6
#11: -x+y,y,-z+1/2
#12: x,x-y,-z+1/6
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25

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
111LYSLYSLEULEUchain 'C'CI1 - 91 - 9
221LYSLYSLEULEUchain 'H'HJ1 - 91 - 9
132GLYGLYTHRTHR(chain 'A' and (resid 1 through 190 or resid 200...AA1 - 1902 - 191
142THRTHRTRPTRP(chain 'A' and (resid 1 through 190 or resid 200...AA200 - 217201 - 218
152ARGARGTHRTHR(chain 'A' and (resid 1 through 190 or resid 200...AA219 - 225220 - 226
162THRTHRVALVAL(chain 'A' and (resid 1 through 190 or resid 200...AA228 - 247229 - 248
172GLUGLUTRPTRP(chain 'A' and (resid 1 through 190 or resid 200...AA254 - 274255 - 275
282GLYGLYTHRTHRchain 'F'FC1 - 1902 - 191
292THRTHRTRPTRPchain 'F'FC200 - 217201 - 218
2102ARGARGTHRTHRchain 'F'FC219 - 225220 - 226
2112THRTHRVALVALchain 'F'FC228 - 247229 - 248
2122GLUGLUTRPTRPchain 'F'FC254 - 274255 - 275
1133METMETMETMETchain 'B'BB0 - 991 - 100
2143METMETMETMETchain 'G'GD0 - 991 - 100
1154ASPASPASPASP(chain 'E' and resid 2 through 245)EF2 - 2452 - 245
2164ASPASPASPASPchain 'J'JH2 - 2452 - 245
1175THRTHRLYSLYSchain 'D'DE4 - 564 - 56
1185ASNASNLYSLYSchain 'D'DE63 - 13063 - 130
1195LYSLYSLYSLYSchain 'D'DE134 - 182134 - 182
1205PHEPHEPROPROchain 'D'DE185 - 203185 - 203
2215THRTHRLYSLYS(chain 'I' and (resid 4 through 56 or resid 63...IG4 - 564 - 56
2225ASNASNLYSLYS(chain 'I' and (resid 4 through 56 or resid 63...IG63 - 13063 - 130
2235LYSLYSLYSLYS(chain 'I' and (resid 4 through 56 or resid 63...IG134 - 182134 - 182
2245PHEPHEPROPRO(chain 'I' and (resid 4 through 56 or resid 63...IG185 - 203185 - 203

NCS ensembles :
ID
1
2
3
4
5

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Components

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Protein , 4 types, 8 molecules AFBGDIEJ

#1: Protein MHC class I antigen / HLA-A*02:06


Mass: 32001.398 Da / Num. of mol.: 2 / Fragment: UNP residues 25-299
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A / Production host: Escherichia coli (E. coli) / Strain (production host): XL1 Blue / References: UniProt: U5YJP1, UniProt: Q53Z42*PLUS
#2: Protein Beta-2-microglobulin


Mass: 11879.356 Da / Num. of mol.: 2 / Fragment: UNP residues 21-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / Strain (production host): XL1 Blue / References: UniProt: P61769
#3: Protein 302TIL TCR alpha chain


Mass: 23541.119 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Rosetta2
#4: Protein 302TIL TCR beta chain


Mass: 27783.045 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Rosetta2

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Protein/peptide , 1 types, 2 molecules CH

#5: Protein/peptide Neoantigen peptide KQWLVWLFL


Mass: 1233.521 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q5VTY9*PLUS

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Non-polymers , 2 types, 37 molecules

#6: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.31 Å3/Da / Density % sol: 62.8 %
Crystal growTemperature: 295.5 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 8 mg/mL protein, 12.5% PEG3350, 0.1 M MOPS, pH 7.0, 0.25 M lithium nitrate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.98 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 10, 2018
RadiationMonochromator: Cryogenically-cooled single crystal Si(220) side bounce
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 3.04879832067→49.38 Å / Num. obs: 48454 / % possible obs: 99.6 % / Redundancy: 5.3 % / Biso Wilson estimate: 58.6177609415 Å2 / CC1/2: 0.99 / Rmerge(I) all: 0.16 / Rrim(I) all: 0.18 / Χ2: 0.936 / Net I/σ(I): 9.2
Reflection shellResolution: 3.04879832067→3.1 Å / Redundancy: 5.2 % / Rmerge(I) all: 1.07 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 2388 / CC1/2: 0.538 / Rrim(I) all: 1.19 / Χ2: 0.936 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 1TVH, 5JZI, & 5C0B

1tvh

5jzi

5c0b


Resolution: 3.05→49.38 Å / SU ML: 0.302158877854 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 20.1124472601
RfactorNum. reflection% reflectionSelection details
Rfree0.218829744142 1880 4.08296231947 %Random Selection
Rwork0.194273139606 ---
obs0.195257806136 46045 94.6940874036 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 66.9632652374 Å2
Refinement stepCycle: LAST / Resolution: 3.05→49.38 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13222 0 30 32 13284
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0031739078233213614
X-RAY DIFFRACTIONf_angle_d0.67989597371618476
X-RAY DIFFRACTIONf_chiral_restr0.04843552598851928
X-RAY DIFFRACTIONf_plane_restr0.008122822040082401
X-RAY DIFFRACTIONf_dihedral_angle_d18.04466264685020
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0488-3.13120.3379369301771240.3062012107582956X-RAY DIFFRACTION83.8551592704
3.1312-3.22330.3215785537951300.2859817630223112X-RAY DIFFRACTION88.3860414395
3.2233-3.32740.2919201117321350.2557062232553207X-RAY DIFFRACTION90.4955320877
3.3274-3.44630.2300102206871340.2449047882973223X-RAY DIFFRACTION91.3966784645
3.4463-3.58420.2128902564641460.2215601346753335X-RAY DIFFRACTION94.4128017358
3.5842-3.74730.2298547117981470.2058262859263396X-RAY DIFFRACTION95.2931683701
3.7473-3.94470.2407764602271490.1975841363923435X-RAY DIFFRACTION97.1537001898
3.9447-4.19180.2000320844251470.1732417459223508X-RAY DIFFRACTION97.8580990629
4.1918-4.51520.1733468773551500.1569716801473536X-RAY DIFFRACTION98.8203753351
4.5152-4.96920.1739698691081530.1477234025263534X-RAY DIFFRACTION98.4512683578
4.9692-5.68740.1780717436141530.1636956467423550X-RAY DIFFRACTION98.3271375465
5.6874-7.1620.2548222994981540.2004781221043633X-RAY DIFFRACTION98.9031078611
7.162-49.38780.2158039083671580.1838773962163740X-RAY DIFFRACTION97.0134395222
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)
13.38394321619-1.150021817240.4547889239632.90736036463-0.3480301096992.1853558007-0.115783216938-0.271498368540.044191394995-0.04533818654670.108504169180.089829176876-0.123911582092-0.06812847989270.008914790735660.34663746440.0651599568837-0.02406872357270.2710855504270.0545774324280.278465419943225.514913528100.406792679122.937493556
22.795238022720.949411593335-0.6980194265744.866610219-0.7959827379752.05669965822-0.108872127031-0.25712260813-0.0373202465702-0.2714119042030.08454016940381.348279219210.277612970688-0.2554207789820.01154681079610.4584658487210.0367945977950.03633253422860.4843904761410.1908310334110.866334830142208.01999692879.698039426123.989821522
33.24775124797-0.86750483419-0.6775579267871.74265353396-0.3203198446551.97551875448-0.5550117826710.484086773314-0.419063844883-0.625689100532-0.0885466102492-1.540226406480.4243774126660.6362635808120.6144776686830.760802608550.1135921518480.3660246078660.8951726235070.04370787615161.14051635925250.91311484136.641567189123.405294078
42.46530480686-0.7445309375840.03611739032213.74992797324-1.011805918171.074880170110.2934828521240.04694900389440.2918800561740.1906523974710.2906405268411.89905181091-0.0617535570791-0.339772619737-0.5100731847850.5854236465670.2046694587570.1234779976920.6464780476530.1693314758571.00108965647170.958683083115.18759524679.0086419181
52.69985504370.28484479406-0.169225473633.18666314261-1.714043229742.995733322170.0739173684465-0.3566525498080.04968601491020.6281447884640.0339598363933-0.0417675037534-0.0336580463945-0.0664037571443-0.09920391413320.7100709696480.1920372371270.0148839878830.425804672176-0.08251574611570.304165305405193.459120318113.03404511185.8519700702
64.31951197182-2.54637401053-3.311767620564.073258917571.655048717544.518537854360.2730988043680.279462259060.17793357921-0.333351185026-0.177922779816-0.0189377094768-0.518346341343-0.321912854362-0.09200267519060.3981601605950.0265331516302-0.006720718703190.2423200735890.04015805351130.32485522788211.38532166162.079459920845.8807031126
76.34300111198-1.03680202824-0.1414703576642.361199074050.2547807276421.35259943335-0.17512926358-0.474281315079-0.6815882247260.4727900906490.1312814203670.4248132384360.2264000298440.1303309800440.004162522839170.7764336619750.02961620647050.115515965340.3793531093330.0788074025050.363760950692208.94965489254.875546578180.497648272
83.882795374590.537777020016-0.2229741605092.531711284830.1009835236463.75915375429-0.3996256772140.877518414411-0.225142819773-0.891977577950.3251778378420.1154364526540.380194768737-0.2195119025740.05775538401170.912352357963-0.0304168308738-0.007493022235260.5709146052610.1120007453850.384687587492220.32106995767.9703236782108.994594513
92.478968455310.5489944671120.03755563680534.58604870199-1.244118921893.10993809181-0.0284008440060.1438699936340.0912525826283-0.20176096584-0.00353500478958-0.3129489534140.04403336020690.2062911947940.0317882261860.238604974114-0.02129752121440.07949943201760.2655043327040.01733945976050.244391231956228.9785395245.329243332136.830604597
103.05870337019-1.776039340030.5393484299261.331089349820.8285352463934.235253670320.2472294286730.911604077937-0.000451897528636-1.34222186381-0.0302959757538-0.150445249150.949580942857-0.608304425065-0.3912567683951.43347470315-0.2930960325890.2845831716561.32388851658-0.08093287151970.622921630001239.50847441143.9300474948105.49540982
117.32400478827-0.1675092693440.7281499541675.161665069630.1297243414724.249006281730.109721818996-0.203909696081-0.157124968590.5468808881660.02008216127140.2141804693820.14857096204-0.18103658599-0.106833820420.5077621608190.01006344136910.1249008447960.303263309459-0.0005056287151360.318982301491199.79002210869.614017064678.1748406859
124.25228879992.473285897952.496685180565.302011503722.010727649414.5508946232-0.13200063638-0.299201988536-0.07668197479790.3518056205020.1323180162790.434709731349-0.370061108011-0.3798317376310.04713900849180.5929792563380.1232698423910.1846788155070.4868470502740.1414464400950.428535062441182.53323517785.354938514993.2402146942
132.42841320201-0.1034604285071.446327872992.595483728470.4859390866725.90951171105-0.0733640287581-0.08396754741090.1384994916710.0615622065945-0.00766431888626-0.187116915415-0.2533205049640.08767325657090.08286983230510.243483594821-0.03273588124280.0497928864630.1819744434560.04378552141980.300196539004226.85657202648.131354731856.8233025001
145.316316598691.724420110290.2887272880183.52201880008-0.6485234676085.65979139399-0.241851838548-0.461358800893-0.1787666335940.4180457212730.3981772787011.14764446622-0.194199648417-0.495453561744-0.09832216906010.6280481911860.1586361388890.2956163033950.84275612870.1610965939951.11020798455164.56009690986.057993659394.2061459801
150.0006931879118020.00545445257392-0.001635441749250.0662521654928-0.04619037141840.0717446700157-0.01393600438560.05438216898360.0281340976258-0.0545614833999-0.01893920155860.0509120636852-0.1176132519940.0495121056001-0.01885006494530.2671569092870.118171170519-0.04703140733790.2724754338070.03476578983110.204420593776227.53584319107.954396485125.505541239
160.1439836979750.0547333807994-0.06922756447710.0225471841836-0.01580110417890.07188181496430.000659806278081-0.0533134652984-0.09251457768050.0386112058887-0.0374714754798-0.009590421073240.06031956671670.02330505217950.02414362181060.0393732685321-0.1300734121440.1218499703130.06375580735130.05039932066160.126252001495224.78614960646.5141722592143.970805985
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resid 1 through 180)
2X-RAY DIFFRACTION2(chain 'B' and resid 0 through 99)
3X-RAY DIFFRACTION3(chain 'G' and resid 0 through 99)
4X-RAY DIFFRACTION4(chain 'D' and resid 4 through 114)
5X-RAY DIFFRACTION5(chain 'E' and resid 1 through 115)
6X-RAY DIFFRACTION6(chain 'I' and resid 3 through 114)
7X-RAY DIFFRACTION7(chain 'J' and resid 116 through 245)
8X-RAY DIFFRACTION8(chain 'A' and resid 181 through 275)
9X-RAY DIFFRACTION9(chain 'F' and resid 1 through 180)
10X-RAY DIFFRACTION10(chain 'F' and resid 181 through 274)
11X-RAY DIFFRACTION11(chain 'I' and resid 115 through 204)
12X-RAY DIFFRACTION12(chain 'E' and resid 116 through 245)
13X-RAY DIFFRACTION13(chain 'J' and resid 2 through 115)
14X-RAY DIFFRACTION14(chain 'D' and resid 115 through 203)
15X-RAY DIFFRACTION15(chain 'C' and resid 1 through 9)
16X-RAY DIFFRACTION16(chain 'H' and resid 1 through 9)

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