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- PDB-6ssa: Human Leukocyte Antigen Class I A02 Carrying LLWNGPMQV -

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Basic information

Entry
Database: PDB / ID: 6ssa
TitleHuman Leukocyte Antigen Class I A02 Carrying LLWNGPMQV
Components
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, A-2 alpha chain
  • LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
KeywordsIMMUNE SYSTEM / Yellow Fever / Altered Peptide Ligand / Human Major Histocompatibility Complex / X-ray 3D Structure Determination
Function / homology
Function and homology information


positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / TAP complex binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / CD8 receptor binding ...positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / TAP complex binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / Golgi medial cisterna / CD8 receptor binding / flavivirin / protection from natural killer cell mediated cytotoxicity / beta-2-microglobulin binding / endoplasmic reticulum exit site / TAP binding / detection of bacterium / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / T cell receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / Endosomal/Vacuolar pathway / T cell mediated cytotoxicity / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / lumenal side of endoplasmic reticulum membrane / regulation of iron ion transport / cellular response to iron(III) ion / negative regulation of iron ion transport / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / response to molecule of bacterial origin / HFE-transferrin receptor complex / transferrin transport / MHC class I peptide loading complex / cellular response to iron ion / negative regulation of receptor-mediated endocytosis / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / cellular response to nicotine / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / specific granule lumen / positive regulation of immune response / antigen processing and presentation of exogenous peptide antigen via MHC class II / peptide antigen binding / phagocytic vesicle membrane / positive regulation of type II interferon production / recycling endosome membrane / positive regulation of T cell activation / negative regulation of epithelial cell proliferation / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon alpha/beta signaling / Modulation by Mtb of host immune system / viral capsid / sensory perception of smell / positive regulation of cellular senescence / tertiary granule lumen / DAP12 signaling / MHC class II protein complex binding / T cell differentiation in thymus / late endosome membrane / T cell receptor signaling pathway / double-stranded RNA binding / nucleoside-triphosphate phosphatase / negative regulation of neuron projection development / E3 ubiquitin ligases ubiquitinate target proteins / antibacterial humoral response / ER-Phagosome pathway / protein refolding / early endosome membrane / clathrin-dependent endocytosis of virus by host cell / amyloid fibril formation / mRNA (guanine-N7)-methyltransferase / protein homotetramerization / methyltransferase cap1 / intracellular iron ion homeostasis / learning or memory / methyltransferase cap1 activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / protein dimerization activity / symbiont-mediated suppression of host innate immune response / defense response to Gram-positive bacterium / immune response / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / endoplasmic reticulum lumen
Similarity search - Function
Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A ...Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus capsid protein C / Flavivirus capsid protein C / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M superfamily, flavivirus / Envelope glycoprotein M, flavivirus / Flavivirus polyprotein propeptide superfamily / Flavivirus envelope glycoprotein M / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide / : / Flavivirus NS3 helicase, C-terminal helical domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus envelope glycoprotein E, stem/anchor domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / DEAD box, Flavivirus / Flavivirus DEAD domain / 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. / helicase superfamily c-terminal domain / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Immunoglobulin E-set / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Immunoglobulin-like fold / Immunoglobulins / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / HLA class I histocompatibility antigen, A alpha chain / Genome polyprotein / HLA class I histocompatibility antigen, A alpha chain / Beta-2-microglobulin
Similarity search - Component
Biological speciesHomo sapiens (human)
Yellow fever virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.11 Å
AuthorsRizkallah, P.J. / Bovay, A.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_179570 Switzerland
CitationJournal: Mol.Immunol. / Year: 2020
Title: Identification of a superagonist variant of the immunodominant Yellow fever virus epitope NS4b214-222by combinatorial peptide library screening.
Authors: Bovay, A. / Zoete, V. / Rizkallah, P.J. / Beck, K. / Delbreil, P. / Speiser, D.E. / Cole, D.K. / Fuertes Marraco, S.A.
History
DepositionSep 6, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 15, 2020Provider: repository / Type: Initial release
Revision 1.1Jul 22, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 24, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_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
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
D: HLA class I histocompatibility antigen, A-2 alpha chain
E: Beta-2-microglobulin
F: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
G: HLA class I histocompatibility antigen, A-2 alpha chain
H: Beta-2-microglobulin
I: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
J: HLA class I histocompatibility antigen, A-2 alpha chain
K: Beta-2-microglobulin
L: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)181,41433
Polymers179,55212
Non-polymers1,86221
Water20,5191139
1
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,2547
Polymers44,8883
Non-polymers3664
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4740 Å2
ΔGint-21 kcal/mol
Surface area19010 Å2
MethodPISA
2
D: HLA class I histocompatibility antigen, A-2 alpha chain
E: Beta-2-microglobulin
F: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,1786
Polymers44,8883
Non-polymers2903
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5220 Å2
ΔGint-18 kcal/mol
Surface area19360 Å2
MethodPISA
3
G: HLA class I histocompatibility antigen, A-2 alpha chain
H: Beta-2-microglobulin
I: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,4259
Polymers44,8883
Non-polymers5376
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5610 Å2
ΔGint-22 kcal/mol
Surface area18600 Å2
MethodPISA
4
J: HLA class I histocompatibility antigen, A-2 alpha chain
K: Beta-2-microglobulin
L: LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,55711
Polymers44,8883
Non-polymers6698
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6100 Å2
ΔGint-29 kcal/mol
Surface area19130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)117.908, 49.071, 169.011
Angle α, β, γ (deg.)90.000, 92.480, 90.000
Int Tables number3
Space group name H-MP121
Components on special symmetry positions
IDModelComponents
11A-454-

HOH

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Components

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Protein , 2 types, 8 molecules ADGJBEHK

#1: Protein
HLA class I histocompatibility antigen, A-2 alpha chain / MHC class I antigen A*2


Mass: 31951.316 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-A, HLAA / Production host: Escherichia coli (E. coli) / References: UniProt: P01892, UniProt: P04439*PLUS
#2: Protein
Beta-2-microglobulin


Mass: 11879.356 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M, CDABP0092, HDCMA22P / Production host: Escherichia coli (E. coli) / References: UniProt: P61769

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Protein/peptide , 1 types, 4 molecules CFIL

#3: Protein/peptide
LEU-LEU-TRP-ASN-GLY-PRO-MET-GLN-VAL


Mass: 1057.266 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Yellow fever virus / References: UniProt: P03314*PLUS

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Non-polymers , 5 types, 1160 molecules

#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C4H10O3
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1139 / 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: 2.72 Å3/Da / Density % sol: 54.79 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.1 M Sodium Cacodylate pH 6.5, 0.2 M Ammonium Sulphate, 20 % PEG 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 14, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.925
11-h,-k,l20.075
ReflectionResolution: 2→117.77 Å / Num. obs: 131906 / % possible obs: 99.9 % / Redundancy: 3.6 % / CC1/2: 0.983 / Rmerge(I) obs: 0.15 / Rpim(I) all: 0.088 / Rrim(I) all: 0.174 / Net I/σ(I): 5 / Num. measured all: 476741 / Scaling rejects: 309
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2-2.053.51.4483420296830.3930.8491.6851.7100
8.94-117.773.20.078527316280.9230.0510.0948.699.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRR rigid body: 0.794
Highest resolutionLowest resolution
Rotation70.08 Å2.06 Å

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Processing

Software
NameVersionClassificationNB
XDSdata reduction
Aimless0.5.32data scaling
MOLREPphasing
REFMAC5.8.0253refinement
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5N6B

5n6b


Resolution: 2.11→70.07 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.897 / SU B: 11.481 / SU ML: 0.156 / SU R Cruickshank DPI: 0.0644 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.064 / ESU R Free: 0.05
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2713 4797 4.9 %RANDOM
Rwork0.2229 ---
obs0.2253 94051 87.63 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 84.39 Å2 / Biso mean: 25.161 Å2 / Biso min: 4.69 Å2
Baniso -1Baniso -2Baniso -3
1--13.21 Å2-0 Å2-11.36 Å2
2--0.49 Å2-0 Å2
3---12.73 Å2
Refinement stepCycle: final / Resolution: 2.11→70.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12660 0 120 1139 13919
Biso mean--42.08 31.67 -
Num. residues----1540
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01313276
X-RAY DIFFRACTIONr_bond_other_d0.0010.01711602
X-RAY DIFFRACTIONr_angle_refined_deg1.6551.65618002
X-RAY DIFFRACTIONr_angle_other_deg1.2971.58126911
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4451556
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.77821.332826
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.441152146
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8715116
X-RAY DIFFRACTIONr_chiral_restr0.0760.21606
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0215057
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023091
LS refinement shellResolution: 2.11→2.163 Å / Rfactor Rfree error: 0
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)
10.66960.0360.16010.56530.47821.6912-0.00510.10090.0509-0.01830.04490.01210.01290.1679-0.03980.054-0.00750.02060.0783-0.00090.069641.3-3.646629.6321
22.9683-2.69740.96453.4352-0.93020.59370.15620.18890.10210.0054-0.1561-0.0361-0.06640.1202-00.12750.03640.05930.07220.03350.032715.04610.52969.3394
31.77430.65091.22051.1320.44360.90650.0003-0.05820.0444-0.1354-0.0030.1123-0.01170.00560.00270.07640.0222-0.00180.05930.00590.100413.9598-4.059427.5197
40.78120.0010.18050.4239-0.69631.57070.077-0.089-0.0046-0.02780.08620.01910.0443-0.1835-0.16320.04950.0030.01930.07590.02280.080913.4444-27.785855.9792
52.30051.54380.57842.82090.61690.20290.0991-0.30260.0445-0.152-0.1334-0.05240.007-0.10840.03420.1133-0.05510.04620.1061-0.05910.04540.2466-14.153375.6896
62.4178-0.67611.12741.0226-0.85121.08520.07670.0694-0.0920.1024-0.0808-0.0933-0.0443-0.0230.00410.0535-0.0152-0.01190.0549-0.00380.115140.7864-28.666657.7717
70.75080.0465-0.11610.42130.55391.5010.0776-0.1006-0.0144-0.00120.04390.0256-0.05430.1339-0.12150.0784-0.0140.04410.0773-0.01210.058938.09241.1526140.5386
82.45551.866-0.76783.0834-1.02530.48550.1065-0.1683-0.0544-0.1336-0.08470.09110.00060.1124-0.02190.1406-0.03790.00220.08180.01750.023811.2949-12.564160.0609
92.6222-0.9097-1.38531.49821.01141.04110.04840.10250.03420.1642-0.0870.18670.03330.00360.03860.0548-0.01990.07990.1012-0.02090.127210.73312.1025142.2045
100.6847-0.0361-0.16830.6869-0.77261.61160.04890.0609-0.0302-0.04180.06120.10060.0166-0.1296-0.11020.0253-0.00260.03680.05510.0050.12710.368-22.9972114.0435
112.8448-1.9192-1.05613.1041.49950.74080.06920.1805-0.09320.1611-0.0834-0.00980.043-0.06930.01420.14760.0512-0.02210.0724-0.04330.029536.6521-37.213493.8859
121.82180.5099-1.23751.7114-0.42720.8510.0485-0.065-0.0133-0.1496-0.0364-0.0522-0.0410.0384-0.01210.0560.02260.05410.0721-0.00680.092237.7655-22.5672112.148
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A0 - 180
2X-RAY DIFFRACTION1C1 - 9
3X-RAY DIFFRACTION2A181 - 276
4X-RAY DIFFRACTION3B0 - 99
5X-RAY DIFFRACTION4D0 - 180
6X-RAY DIFFRACTION4F1 - 9
7X-RAY DIFFRACTION5D181 - 276
8X-RAY DIFFRACTION6E0 - 99
9X-RAY DIFFRACTION7G0 - 180
10X-RAY DIFFRACTION7I1 - 9
11X-RAY DIFFRACTION8G181 - 276
12X-RAY DIFFRACTION9H0 - 99
13X-RAY DIFFRACTION10J0 - 180
14X-RAY DIFFRACTION10L1 - 9
15X-RAY DIFFRACTION11J181 - 276
16X-RAY DIFFRACTION12K0 - 99

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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