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- PDB-3ciq: A regulatable switch mediates self-association in an immunoglobul... -

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Basic information

Entry
Database: PDB / ID: 3ciq
TitleA regulatable switch mediates self-association in an immunoglobulin fold
ComponentsBeta-2-microglobulin
KeywordsIMMUNE SYSTEM / class-1 MHC / amyloid / protein folding / dialysis-related amyloidosis / beta-2 microglobulin / Disease mutation / Glycation / Glycoprotein / Immune response / Immunoglobulin domain / MHC I / Pyrrolidone carboxylic acid / Secreted
Function / homology
Function and homology information


: / : / positive regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / negative regulation of receptor binding / DAP12 interactions / cellular response to iron ion / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC ...: / : / positive regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / negative regulation of receptor binding / DAP12 interactions / cellular response to iron ion / Endosomal/Vacuolar pathway / 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 / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / MHC class II protein complex / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / response to molecule of bacterial origin / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / antigen processing and presentation of exogenous peptide antigen via MHC class II / MHC class I protein complex / positive regulation of immune response / peptide antigen binding / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / positive regulation of receptor-mediated endocytosis / multicellular organismal-level iron ion homeostasis / positive regulation of T cell activation / cellular response to nicotine / specific granule lumen / recycling endosome membrane / phagocytic vesicle membrane / positive regulation of cellular senescence / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / negative regulation of epithelial cell proliferation / Interferon gamma signaling / MHC class II protein complex binding / positive regulation of protein binding / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / tertiary granule lumen / DAP12 signaling / negative regulation of neuron projection development / iron ion transport / T cell differentiation in thymus / ER-Phagosome pathway / protein refolding / early endosome membrane / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / Amyloid fiber formation / endoplasmic reticulum lumen / Golgi membrane / external side of plasma membrane / lysosomal membrane / focal adhesion / Neutrophil degranulation / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane / cytosol
Similarity search - Function
Beta-2-Microglobulin / : / 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 ...Beta-2-Microglobulin / : / 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 / Mainly Beta
Similarity search - Domain/homology
COPPER (II) ION / L(+)-TARTARIC ACID / Beta-2-microglobulin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsCalabrese, M.F. / Eakin, C.M. / Wang, J.M. / Miranker, A.D.
Citation
Journal: Nat.Struct.Mol.Biol. / Year: 2008
Title: A regulatable switch mediates self-association in an immunoglobulin fold.
Authors: Calabrese, M.F. / Eakin, C.M. / Wang, J.M. / Miranker, A.D.
#1: Journal: Nat.Struct.Mol.Biol. / Year: 2006
Title: A native to amyloidogenic transition regulated by a backbone trigger
Authors: Eakin, C.M. / Berman, A.J. / Miranker, A.D.
#2: Journal: J.Mol.Biol. / Year: 2007
Title: Formation of a stable oligomer of beta-2 microglobulin requires only transient encounter with Cu(II)
Authors: Calabrese, M.F. / Miranker, A.D.
History
DepositionMar 11, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 2, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 20, 2021Group: Database references / Derived calculations / Category: database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 6, 2024Group: Data collection / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-2-microglobulin
B: Beta-2-microglobulin
C: Beta-2-microglobulin
D: Beta-2-microglobulin
E: Beta-2-microglobulin
F: Beta-2-microglobulin
G: Beta-2-microglobulin
H: Beta-2-microglobulin
I: Beta-2-microglobulin
J: Beta-2-microglobulin
K: Beta-2-microglobulin
L: Beta-2-microglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,57325
Polymers142,66112
Non-polymers91313
Water1,36976
1
G: Beta-2-microglobulin
H: Beta-2-microglobulin
I: Beta-2-microglobulin
J: Beta-2-microglobulin
K: Beta-2-microglobulin
L: Beta-2-microglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,86213
Polymers71,3306
Non-polymers5317
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9810 Å2
ΔGint-35 kcal/mol
Surface area30650 Å2
MethodPISA
2
A: Beta-2-microglobulin
B: Beta-2-microglobulin
C: Beta-2-microglobulin
D: Beta-2-microglobulin
E: Beta-2-microglobulin
F: Beta-2-microglobulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,71212
Polymers71,3306
Non-polymers3816
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9920 Å2
ΔGint-32 kcal/mol
Surface area30680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.594, 68.047, 96.218
Angle α, β, γ (deg.)104.38, 94.15, 117.77
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLNGLNSERSER2AA8 - 119 - 12
21GLNGLNSERSER2BB8 - 119 - 12
31GLNGLNSERSER2CC8 - 119 - 12
41GLNGLNSERSER2DD8 - 119 - 12
51GLNGLNSERSER2EE8 - 119 - 12
61GLNGLNSERSER2FF8 - 119 - 12
71GLNGLNSERSER2GG8 - 119 - 12
81GLNGLNSERSER2HH8 - 119 - 12
91GLNGLNSERSER2II8 - 119 - 12
101GLNGLNSERSER2JJ8 - 119 - 12
111GLNGLNSERSER2KK8 - 119 - 12
121GLNGLNSERSER2LL8 - 119 - 12
12SERSERVALVAL1AA20 - 2721 - 28
22SERSERVALVAL1BB20 - 2721 - 28
32SERSERVALVAL1CC20 - 2721 - 28
42SERSERVALVAL1DD20 - 2721 - 28
52SERSERVALVAL1EE20 - 2721 - 28
62SERSERVALVAL1FF20 - 2721 - 28
72SERSERVALVAL1GG20 - 2721 - 28
82SERSERVALVAL1HH20 - 2721 - 28
92SERSERVALVAL1II20 - 2721 - 28
102SERSERVALVAL1JJ20 - 2721 - 28
112SERSERVALVAL1KK20 - 2721 - 28
122SERSERVALVAL1LL20 - 2721 - 28
13VALVALLEULEU1AA37 - 4038 - 41
23VALVALLEULEU1BB37 - 4038 - 41
33VALVALLEULEU1CC37 - 4038 - 41
43VALVALLEULEU1DD37 - 4038 - 41
53VALVALLEULEU1EE37 - 4038 - 41
63VALVALLEULEU1FF37 - 4038 - 41
73VALVALLEULEU1GG37 - 4038 - 41
83VALVALLEULEU1HH37 - 4038 - 41
93VALVALLEULEU1II37 - 4038 - 41
103VALVALLEULEU1JJ37 - 4038 - 41
113VALVALLEULEU1KK37 - 4038 - 41
123VALVALLEULEU1LL37 - 4038 - 41
14VALVALPHEPHE1AA49 - 5650 - 57
24VALVALPHEPHE1BB49 - 5650 - 57
34VALVALPHEPHE1CC49 - 5650 - 57
44VALVALPHEPHE1DD49 - 5650 - 57
54VALVALPHEPHE1EE49 - 5650 - 57
64VALVALPHEPHE1FF49 - 5650 - 57
74VALVALPHEPHE1GG49 - 5650 - 57
84VALVALPHEPHE1HH49 - 5650 - 57
94VALVALPHEPHE1II49 - 5650 - 57
104VALVALPHEPHE1JJ49 - 5650 - 57
114VALVALPHEPHE1KK49 - 5650 - 57
124VALVALPHEPHE1LL49 - 5650 - 57
15PHEPHETHRTHR1AA62 - 6863 - 69
25PHEPHETHRTHR1BB62 - 6863 - 69
35PHEPHETHRTHR1CC62 - 6863 - 69
45PHEPHETHRTHR1DD62 - 6863 - 69
55PHEPHETHRTHR1EE62 - 6863 - 69
65PHEPHETHRTHR1FF62 - 6863 - 69
75PHEPHETHRTHR1GG62 - 6863 - 69
85PHEPHETHRTHR1HH62 - 6863 - 69
95PHEPHETHRTHR1II62 - 6863 - 69
105PHEPHETHRTHR1JJ62 - 6863 - 69
115PHEPHETHRTHR1KK62 - 6863 - 69
125PHEPHETHRTHR1LL62 - 6863 - 69
16TYRTYRASNASN1AA78 - 8379 - 84
26TYRTYRASNASN1BB78 - 8379 - 84
36TYRTYRASNASN1CC78 - 8379 - 84
46TYRTYRASNASN1DD78 - 8379 - 84
56TYRTYRASNASN1EE78 - 8379 - 84
66TYRTYRASNASN1FF78 - 8379 - 84
76TYRTYRASNASN1GG78 - 8379 - 84
86TYRTYRASNASN1HH78 - 8379 - 84
96TYRTYRASNASN1II78 - 8379 - 84
106TYRTYRASNASN1JJ78 - 8379 - 84
116TYRTYRASNASN1KK78 - 8379 - 84
126TYRTYRASNASN1LL78 - 8379 - 84
17LYSLYSLYSLYS4AA41 - 4842 - 49
27LYSLYSLYSLYS4BB41 - 4842 - 49
37LYSLYSLYSLYS4CC41 - 4842 - 49
47LYSLYSLYSLYS4DD41 - 4842 - 49
57LYSLYSLYSLYS4EE41 - 4842 - 49
67LYSLYSLYSLYS4FF41 - 4842 - 49
77LYSLYSLYSLYS4GG41 - 4842 - 49
87LYSLYSLYSLYS4HH41 - 4842 - 49
97LYSLYSLYSLYS4II41 - 4842 - 49
107LYSLYSLYSLYS4JJ41 - 4842 - 49
117LYSLYSLYSLYS4KK41 - 4842 - 49
127LYSLYSLYSLYS4LL41 - 4842 - 49
18SERSERSERSER2AA57 - 6158 - 62
28SERSERSERSER2BB57 - 6158 - 62
38SERSERSERSER2CC57 - 6158 - 62
48SERSERSERSER2DD57 - 6158 - 62
58SERSERSERSER2EE57 - 6158 - 62
68SERSERSERSER2FF57 - 6158 - 62
78SERSERSERSER2GG57 - 6158 - 62
88SERSERSERSER2HH57 - 6158 - 62
98SERSERSERSER2II57 - 6158 - 62
108SERSERSERSER2JJ57 - 6158 - 62
118SERSERSERSER2KK57 - 6158 - 62
128SERSERSERSER2LL57 - 6158 - 62
19HISHISGLNGLN4AA84 - 8985 - 90
29HISHISGLNGLN4BB84 - 8985 - 90
39HISHISGLNGLN4CC84 - 8985 - 90
49HISHISGLNGLN4DD84 - 8985 - 90
59HISHISGLNGLN4EE84 - 8985 - 90
69HISHISGLNGLN4FF84 - 8985 - 90
79HISHISGLNGLN4GG84 - 8985 - 90
89HISHISGLNGLN4HH84 - 8985 - 90
99HISHISGLNGLN4II84 - 8985 - 90
109HISHISGLNGLN4JJ84 - 8985 - 90
119HISHISGLNGLN4KK84 - 8985 - 90
129HISHISGLNGLN4LL84 - 8985 - 90

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Components

#1: Protein
Beta-2-microglobulin


Mass: 11888.383 Da / Num. of mol.: 12 / Mutation: H13F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B2M / Production host: Escherichia coli (E. coli) / References: UniProt: P61769
#2: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Cu
#3: Chemical ChemComp-TLA / L(+)-TARTARIC ACID


Mass: 150.087 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H6O6
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 76 / Source method: isolated from a natural source / Formula: H2O
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: 2.59 Å3/Da / Density % sol: 52.58 %
Crystal growTemperature: 288 K / Method: vapor diffusion, sitting drop / pH: 7.4
Details: 28% PEG 3350, 200 mM ammonium tartrate dibasic, pH 7.40, VAPOR DIFFUSION, SITTING DROP, temperature 288K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X12B / Wavelength: 1.37
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.37 Å / Relative weight: 1
ReflectionResolution: 2.9→50 Å / Num. obs: 28565 / % possible obs: 95.3 % / Redundancy: 2.2 % / Rmerge(I) obs: 0.079
Reflection shellResolution: 2.9→3 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.363 / % possible all: 96.5

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→50 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.884 / SU B: 44.996 / SU ML: 0.384 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.468 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26393 1539 5.1 %RANDOM
Rwork0.22475 ---
obs0.2267 28565 94.77 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 57.443 Å2
Baniso -1Baniso -2Baniso -3
1--0.86 Å2-0.24 Å22.65 Å2
2---2.42 Å22.36 Å2
3---4.6 Å2
Refinement stepCycle: LAST / Resolution: 2.9→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9836 0 22 76 9934
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.02210132
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.8951.94213717
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.17251161
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.16823.89527
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.492151760
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.3241559
X-RAY DIFFRACTIONr_chiral_restr0.0680.21429
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.027779
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.180.23816
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2940.26816
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1090.2416
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0810.210
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1660.260
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0790.26
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.54626056
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it4.89939608
X-RAY DIFFRACTIONr_scbond_it3.7424707
X-RAY DIFFRACTIONr_scangle_it5.37234109
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A317tight positional0.010.05
2B317tight positional0.010.05
3C317tight positional0.010.05
4D317tight positional0.010.05
5E317tight positional0.010.05
6F317tight positional0.010.05
7G317tight positional0.010.05
8H317tight positional0.010.05
9I317tight positional0.010.05
10J317tight positional0.010.05
11K317tight positional0.010.05
12L317tight positional0.010.05
1A131medium positional0.250.5
2B131medium positional0.510.5
3C131medium positional0.230.5
4D131medium positional0.430.5
5E131medium positional0.390.5
6F131medium positional0.250.5
7G131medium positional0.420.5
8H131medium positional0.410.5
9I131medium positional0.270.5
10J131medium positional0.350.5
11K131medium positional0.250.5
12L131medium positional0.310.5
1A317tight thermal0.020.5
2B317tight thermal0.020.5
3C317tight thermal0.020.5
4D317tight thermal0.030.5
5E317tight thermal0.020.5
6F317tight thermal0.020.5
7G317tight thermal0.020.5
8H317tight thermal0.020.5
9I317tight thermal0.020.5
10J317tight thermal0.020.5
11K317tight thermal0.020.5
12L317tight thermal0.020.5
1A131medium thermal0.172
2B131medium thermal0.222
3C131medium thermal0.222
4D131medium thermal0.32
5E131medium thermal0.242
6F131medium thermal0.212
7G131medium thermal0.22
8H131medium thermal0.142
9I131medium thermal0.152
10J131medium thermal0.152
11K131medium thermal0.222
12L131medium thermal0.272
LS refinement shellResolution: 2.9→2.975 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.385 102 -
Rwork0.338 2170 -
obs--96.27 %
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)
13.5360.49860.43365.50141.67891.9032-0.0337-0.14970.564-0.04380.0031-0.3336-0.15260.36780.0306-0.2009-0.0949-0.02710.0385-0.01590.0403-20.449823.82278.7314
25.98682.9897-0.34824.28691.1412.4473-0.03660.1068-0.6424-0.2593-0.0643-0.17160.38180.24510.1009-0.14930.1126-0.0701-0.0323-0.0024-0.0756-23.4431-6.10656.8587
37.87691.78221.63631.8872-0.57235.15720.2065-0.3497-0.73260.0498-0.2268-0.22060.27010.90240.0202-0.2150.0418-0.12960.06480.1280.0088-27.8567-7.813425.9134
42.00111.3076-0.07523.1572-0.78422.51060.2008-0.00280.3328-0.1893-0.12470.22550.0379-0.0796-0.0761-0.3284-0.0244-0.0557-0.09930.0212-0.1558-55.75791.880320.8177
52.46771.1298-0.3192.53010.79295.30170.2802-0.20561.00680.21-0.29680.5315-0.077-0.54780.0166-0.2256-0.0220.0987-0.057-0.09860.1975-51.669220.041727.1602
63.1113-0.6965-0.62423.37571.34163.68480.2120.56140.9304-0.35890.18160.4077-0.1494-0.1336-0.3936-0.0965-0.0595-0.0854-0.05130.22770.166-38.272626.65371.1207
71.85810.12250.51094.27421.34065.0772-0.24080.0424-0.34930.4792-0.03061.2871-0.1037-0.50870.2713-0.04720.00780.1497-0.088-0.09840.2219-70.65987.6922-40.6373
80.5906-0.97770.05643.8530.83244.7963-0.5561-0.3671-0.17941.61340.41711.34650.3988-0.74250.1391.14930.10720.8650.06240.20590.3598-68.1399-6.8452-14.6919
93.3947-0.26071.38833.43861.07441.763-0.1446-0.185-0.44810.88240.11510.90640.3949-0.11080.02950.76340.040.4347-0.09510.13930.3335-57.7815-21.2587-22.423
102.01561.51610.60838.07770.82142.7012-0.2390.0611-0.20491.35740.5137-0.86920.37750.688-0.27460.42820.2127-0.13240.0764-0.0440.0134-32.6869-4.6803-23.0363
112.1439-2.9218-0.984410.50351.69474.297-0.29720.09320.03950.2460.3554-0.95420.43490.6632-0.0582-0.08010.05490.03480.0186-0.0546-0.0725-35.0148-0.7274-42.1436
121.7821-0.725-1.32252.2591-0.13443.6816-0.2355-0.1832-0.10270.72280.04950.3143-0.32250.1180.1860.08830.03410.0389-0.2114-0.0423-0.2406-55.952819.9549-35.9887
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA0 - 971 - 98
2X-RAY DIFFRACTION2BB0 - 971 - 98
3X-RAY DIFFRACTION3CC0 - 971 - 98
4X-RAY DIFFRACTION4DD0 - 971 - 98
5X-RAY DIFFRACTION5EE0 - 971 - 98
6X-RAY DIFFRACTION6FF0 - 971 - 98
7X-RAY DIFFRACTION7GG0 - 971 - 98
8X-RAY DIFFRACTION8HH0 - 971 - 98
9X-RAY DIFFRACTION9II0 - 971 - 98
10X-RAY DIFFRACTION10JJ0 - 971 - 98
11X-RAY DIFFRACTION11KK0 - 971 - 98
12X-RAY DIFFRACTION12LL0 - 971 - 98

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