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- PDB-2ve6: Crystal structure of a Murine MHC class I H2-Db molecule in compl... -

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Basic information

Entry
Database: PDB / ID: 2ve6
TitleCrystal structure of a Murine MHC class I H2-Db molecule in complex with a photocleavable peptide
Components
  • BETA-2-MICROGLOBULIN
  • H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
  • SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7
KeywordsIMMUNE SYSTEM / PHOTOCLEAVABLE PEPTIDE / AUXILIARY ANCHORING RESIDUE / GLYCOPROTEIN / TRANSMEMBRANE / PEPTIDE LOADING / IMMUNE RESPONSE / IMMUNOGLOBULIN DOMAIN / MHC / SEV9 / MHC I / MEMBRANE / SECRETED
Function / homology
Function and homology information


Endosomal/Vacuolar pathway / DAP12 interactions / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / DAP12 signaling / cellular response to iron(III) ion / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / MHC class Ib protein complex / response to molecule of bacterial origin ...Endosomal/Vacuolar pathway / DAP12 interactions / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / DAP12 signaling / cellular response to iron(III) ion / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / MHC class Ib protein complex / response to molecule of bacterial origin / regulation of erythrocyte differentiation / multicellular organismal-level iron ion homeostasis / regulation of membrane depolarization / T cell differentiation in thymus / antigen processing and presentation of peptide antigen via MHC class I / cellular defense response / Neutrophil degranulation / positive regulation of T cell mediated cytotoxicity / negative regulation of neuron projection development / lumenal side of endoplasmic reticulum membrane / regulation of iron ion transport / negative regulation of iron ion transport / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous peptide antigen via MHC class Ib / peptide antigen assembly with MHC class I protein complex / iron ion transport / HFE-transferrin receptor complex / MHC class I peptide loading complex / transferrin transport / negative regulation of receptor-mediated endocytosis / cellular response to iron ion / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / peptide antigen assembly with MHC class II protein complex / protein refolding / MHC class I protein complex / negative regulation of epithelial cell proliferation / cellular response to nicotine / negative regulation of neurogenesis / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / 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 T cell activation / sensory perception of smell / positive regulation of cellular senescence / MHC class II protein complex binding / late endosome membrane / cellular response to lipopolysaccharide / antimicrobial humoral immune response mediated by antimicrobial peptide / antibacterial humoral response / defense response to Gram-negative bacterium / amyloid fibril formation / protein homotetramerization / intracellular iron ion homeostasis / learning or memory / defense response to Gram-positive bacterium / immune response / external side of plasma membrane / innate immune response / lysosomal membrane / structural molecule activity / Golgi apparatus / protein homodimerization activity / : / identical protein binding / plasma membrane / cytosol
Similarity search - Function
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 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 / H-2 class I histocompatibility antigen, D-B alpha chain
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
SENDAI VIRUS
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å
AuthorsGrotenbreg, G.M. / Roan, N.R. / Guillen, E. / Meijers, R. / Wang, J.H. / Bell, G.W. / Starnbach, M.N. / Ploegh, H.L.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2008
Title: Discovery of Cd8+ T Cell Epitopes in Chlamydia Trachomatis Infection Through Use of Caged Class I Mhc Tetramers.
Authors: Grotenbreg, G.M. / Roan, N.R. / Guillen, E. / Meijers, R. / Wang, J.H. / Bell, G.W. / Starnbach, M.N. / Ploegh, H.L.
History
DepositionOct 17, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 22, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2May 15, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Other / Refinement description
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_rmsd_angle / pdbx_validate_torsion / struct_conn / struct_ncs_dom_lim
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_label_atom_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 2.1Dec 13, 2023Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 2.2Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
B: BETA-2-MICROGLOBULIN
C: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7
D: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
E: BETA-2-MICROGLOBULIN
F: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7
G: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
H: BETA-2-MICROGLOBULIN
I: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7
J: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
K: BETA-2-MICROGLOBULIN
L: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Theoretical massNumber of molelcules
Total (without water)179,62912
Polymers179,62912
Non-polymers00
Water3,117173
1
A: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
B: BETA-2-MICROGLOBULIN
C: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Theoretical massNumber of molelcules
Total (without water)44,9073
Polymers44,9073
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4970 Å2
ΔGint-25.2 kcal/mol
Surface area23790 Å2
MethodPQS
2
D: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
E: BETA-2-MICROGLOBULIN
F: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Theoretical massNumber of molelcules
Total (without water)44,9073
Polymers44,9073
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5220 Å2
ΔGint-31 kcal/mol
Surface area22750 Å2
MethodPQS
3
G: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
H: BETA-2-MICROGLOBULIN
I: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Theoretical massNumber of molelcules
Total (without water)44,9073
Polymers44,9073
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5080 Å2
ΔGint-30.5 kcal/mol
Surface area23890 Å2
MethodPQS
4
J: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN
K: BETA-2-MICROGLOBULIN
L: SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Theoretical massNumber of molelcules
Total (without water)44,9073
Polymers44,9073
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4950 Å2
ΔGint-26.1 kcal/mol
Surface area24310 Å2
MethodPQS
Unit cell
Length a, b, c (Å)52.240, 103.870, 168.810
Angle α, β, γ (deg.)90.00, 90.83, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
11A
21D
31G
41J
12B
22E
32H
42K
13C
23F
33I
43L

NCS domain segments:

Component-ID: 1 / Refine code: 5

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11SERSERLEULEUAA4 - 2724 - 272
21SERSERLEULEUDD4 - 2724 - 272
31SERSERLEULEUGG4 - 2724 - 272
41SERSERLEULEUJJ4 - 2724 - 272
12THRTHRTYRTYRBB4 - 944 - 94
22THRTHRTYRTYREE4 - 944 - 94
32THRTHRTYRTYRHH4 - 944 - 94
42THRTHRTYRTYRKK4 - 944 - 94
13PHEPHELEULEUCC1 - 91 - 9
23PHEPHELEULEUFF1 - 91 - 9
33PHEPHELEULEUII1 - 91 - 9
43PHEPHELEULEULL1 - 91 - 9

NCS ensembles :
ID
1
2
3

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Components

#1: Protein
H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN D-B ALPHA CHAIN / MHC CLASS I MOLECULE / H-2D(B)


Mass: 32184.816 Da / Num. of mol.: 4 / Fragment: RESIDUES 25-301
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: BL21 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P01899
#2: Protein
BETA-2-MICROGLOBULIN / B2M MICROGLOBULIN


Mass: 11678.388 Da / Num. of mol.: 4 / Fragment: RESIDUES 22-119
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: BL21 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P01887
#3: Protein/peptide
SENDAI VIRUS EPITOPE RESIDUES 324-332 MODIFIED AT P7


Mass: 1044.117 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: 3-AMINO-3-(2-NITRO)PHENYL-PROPIONIC ACID AT P7 / Source: (synth.) SENDAI VIRUS
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 173 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Nonpolymer details3-AMINO-3-(2-NITRO)PHENYL-PROPIONIC ACID (PRQ): PHOTOCLEAVABLE

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.5 Å3/Da / Density % sol: 51 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop
Details: CRYSTALS WERE GROWN AT ROOM TEMPERATURE USING THE HANGING-DROP, VAPOR-DIFFUSION METHOD WITH A WELL SOLUTION OF 15% (W/V) PEG 8000, 0.05 M K/NA PHOSPHATE, 50-100 MM BETA-OCTYL-GLUCOPYRANOSIDE ...Details: CRYSTALS WERE GROWN AT ROOM TEMPERATURE USING THE HANGING-DROP, VAPOR-DIFFUSION METHOD WITH A WELL SOLUTION OF 15% (W/V) PEG 8000, 0.05 M K/NA PHOSPHATE, 50-100 MM BETA-OCTYL-GLUCOPYRANOSIDE AND 0.1 M CACODYLATE AT PH 6.4.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1.07
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 25, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.07 Å / Relative weight: 1
ReflectionResolution: 2.65→20 Å / Num. obs: 50561 / % possible obs: 96.6 % / Observed criterion σ(I): 0 / Redundancy: 2 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.7

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1WBX

1wbx


Resolution: 2.65→19.66 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.873 / SU B: 34.083 / SU ML: 0.345 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.412 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.291 2558 5.1 %RANDOM
Rwork0.234 ---
obs0.237 48002 96.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 47.84 Å2
Baniso -1Baniso -2Baniso -3
1-0.53 Å20 Å20.92 Å2
2--2.57 Å20 Å2
3----3.07 Å2
Refinement stepCycle: LAST / Resolution: 2.65→19.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12628 0 0 173 12801
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.02113110
X-RAY DIFFRACTIONr_bond_other_d0.0020.029085
X-RAY DIFFRACTIONr_angle_refined_deg0.8951.94217796
X-RAY DIFFRACTIONr_angle_other_deg0.733.00321857
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.13651532
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.27423.55676
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.541152133
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.8421598
X-RAY DIFFRACTIONr_chiral_restr0.0550.21779
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0214619
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022779
X-RAY DIFFRACTIONr_nbd_refined0.1640.22579
X-RAY DIFFRACTIONr_nbd_other0.1610.28994
X-RAY DIFFRACTIONr_nbtor_refined0.1730.26006
X-RAY DIFFRACTIONr_nbtor_other0.0840.27124
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1050.2353
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1160.256
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1390.2134
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1440.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2141.510034
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.231212433
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.24236580
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.3724.55363
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1568medium positional0.370.5
12D1568medium positional0.50.5
13G1568medium positional0.470.5
14J1568medium positional0.330.5
21B529medium positional0.220.5
22E529medium positional0.280.5
23H529medium positional0.270.5
24K529medium positional0.230.5
31C44medium positional0.130.5
32F44medium positional0.140.5
33I44medium positional0.220.5
34L44medium positional0.150.5
11A2164loose positional0.735
12D2164loose positional0.895
13G2164loose positional0.885
14J2164loose positional0.725
21B728loose positional0.745
22E728loose positional0.95
23H728loose positional0.695
24K728loose positional0.645
31C80loose positional0.515
32F80loose positional0.375
33I80loose positional0.555
34L80loose positional0.535
11A1568medium thermal2.88
12D1568medium thermal3.2
13G1568medium thermal3.57
14J1568medium thermal3.4
21B529medium thermal2.51
22E529medium thermal3.76
23H529medium thermal4.79
24K529medium thermal2.56
31C44medium thermal13.02
32F44medium thermal14.27
33I44medium thermal12.64
34L44medium thermal14.62
11A2164loose thermal2.77
12D2164loose thermal3.16
13G2164loose thermal3.55
14J2164loose thermal3.39
21B728loose thermal2.51
22E728loose thermal3.81
23H728loose thermal4.79
24K728loose thermal2.65
31C80loose thermal12.8
32F80loose thermal14.34
33I80loose thermal12.45
34L80loose thermal14.66
LS refinement shellResolution: 2.65→2.72 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.35 167
Rwork0.339 3293
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)
12.5899-0.47541.39691.15280.14222.34540.0168-0.164-0.22120.0119-0.06320.1851-0.0181-0.30240.0463-0.2841-0.01120.0737-0.3053-0.0442-0.15452.508-11.98717.804
27.7268-3.7232-0.88844.57930.70451.6150.00660.06930.31370.02090.03660.1313-0.23770.0954-0.0433-0.2379-0.02980.0403-0.35220.0046-0.2379-5.9555.89222.038
311.70066.2516-1.13485.2873-1.39770.43170.07370.4026-0.82150.0220.4135-0.20580.3937-0.2096-0.4872-0.035-0.08740.062-0.03490.0155-0.00716.927-21.46229.066
41.4897-0.35340.75390.933-0.57411.4213-0.0517-0.05030.0524-0.07530.02960.0427-0.0196-0.08150.0222-0.22420.03340.0269-0.2614-0.068-0.1862-11.773-6.545-22.224
56.6766-3.68140.37516.8626-2.44582.2774-0.12590.2510.43-0.14990.0776-0.10390.0709-0.13740.0484-0.2619-0.0526-0.0481-0.2758-0.0526-0.21976.105-11.307-27.385
610.77343.6523-0.32830.68410.5130.0232-0.7658-0.54750.56671.14111.22792.2274-0.5063-0.0688-0.46210.00570.0588-0.01730.0194-0.10120.0263-26.211.512-34.27
72.1489-0.2017-1.52661.57151.20645.19-0.0454-0.7925-0.07650.12550.1369-0.265-0.04920.0383-0.09150.15490.0717-0.10760.35060.0461-0.0748-24.982-11.19562.563
812.3441-8.5742-3.675710.88215.9547.50210.09710.27850.0376-0.5596-0.12690.0481-0.72680.01020.02990.0848-0.04660.09010.5907-0.0703-0.0526-42.416-6.41357.138
910.603712.3865-1.229291.552326.935418.0756-0.4244-0.0963-0.5322-0.36551.4521-3.08190.6961.329-1.0278-0.00020.0010.0006-0.00110.0040.0005-10.407-18.45549.749
103.11490.1517-1.54861.1038-0.48693.5810.2146-0.5103-0.061-0.1524-0.0910.2395-0.0497-0.1292-0.12370.4803-0.2169-0.05950.2186-0.0471-0.0706-13.85744.21366.41
113.62311.5133-0.80846.41521.08133.26130.1238-0.1331-0.9743-0.1024-0.33560.39390.3512-0.20650.21180.7106-0.2634-0.17750.17920.09470.2724-18.0924.43763.053
1226.737-8.5238-0.52556.6133.943923.68780.98071.20332.51310.1709-1.3766-0.5635-0.27821.1290.39580.016-0.0448-0.02890.01380.00290.0029-0.79955.34455.037
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 276
2X-RAY DIFFRACTION2B1 - 99
3X-RAY DIFFRACTION3C1 - 9
4X-RAY DIFFRACTION4D1 - 276
5X-RAY DIFFRACTION5E1 - 99
6X-RAY DIFFRACTION6F1 - 9
7X-RAY DIFFRACTION7G1 - 276
8X-RAY DIFFRACTION8H1 - 99
9X-RAY DIFFRACTION9I1 - 9
10X-RAY DIFFRACTION10J1 - 276
11X-RAY DIFFRACTION11K1 - 99
12X-RAY DIFFRACTION12L1 - 9

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