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- PDB-3hae: Rational development of high-affinity T-cell receptor-like antibodies -

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Basic information

Entry
Database: PDB / ID: 3hae
TitleRational development of high-affinity T-cell receptor-like antibodies
Components
  • Antibody heavy chain
  • Antibody light chain
  • Beta-2-microglobulin
  • HLA class I histocompatibility antigen, A-2 alpha chain
  • NYESO-1 peptide
KeywordsIMMUNE SYSTEM / Fab / Major Histocompatability Complex / Immunity / Disulfide bond / Glycoprotein / Host-virus interaction / Immune response / Membrane / MHC I / Phosphoprotein / Transmembrane / Disease mutation / Glycation / Immunoglobulin domain / Pyrrolidone carboxylic acid / Secreted
Function / homology
Function and homology information


tRNA threonylcarbamoyladenosine metabolic process / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / Golgi medial cisterna / 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 / CD8 receptor binding / antigen processing and presentation of exogenous peptide antigen via MHC class I ...tRNA threonylcarbamoyladenosine metabolic process / positive regulation of memory T cell activation / T cell mediated cytotoxicity directed against tumor cell target / TAP complex binding / Golgi medial cisterna / 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 / CD8 receptor binding / antigen processing and presentation of exogenous peptide antigen via MHC class I / beta-2-microglobulin binding / endoplasmic reticulum exit site / TAP binding / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / protection from natural killer cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / detection of bacterium / T cell receptor binding / 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 / 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 / positive regulation of type II interferon production / 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 / Interferon alpha/beta signaling / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / antibacterial humoral response / positive regulation of cellular senescence / tertiary granule lumen / DAP12 signaling / T cell differentiation in thymus / T cell receptor signaling pathway / E3 ubiquitin ligases ubiquitinate target proteins / 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 / defense response to Gram-positive bacterium / immune response / endoplasmic reticulum lumen / Amyloid fiber formation / signaling receptor binding / Golgi membrane / lysosomal membrane / innate immune response / external side of plasma membrane / focal adhesion / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / cell surface / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / RNA binding
Similarity search - Function
CTAG/Pcc1 family / Transcription factor Pcc1 / 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 / : ...CTAG/Pcc1 family / Transcription factor Pcc1 / 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
HLA class I histocompatibility antigen, A alpha chain / HLA class I histocompatibility antigen, A alpha chain / Beta-2-microglobulin / Cancer/testis antigen 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsStewart-Jones, G. / Wadle, A. / Hombach, A. / Shenderov, E. / Held, G. / Fischer, E.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2009
Title: Rational development of high-affinity T-cell receptor-like antibodies
Authors: Stewart-Jones, G. / Wadle, A. / Hombach, A. / Shenderov, E. / Held, G. / Fischer, E. / Kleber, S. / Stenner-Liewen, F. / Bauer, S. / McMichael, A. / Knuth, A. / Abken, H. / Hombach, A.A. / ...Authors: Stewart-Jones, G. / Wadle, A. / Hombach, A. / Shenderov, E. / Held, G. / Fischer, E. / Kleber, S. / Stenner-Liewen, F. / Bauer, S. / McMichael, A. / Knuth, A. / Abken, H. / Hombach, A.A. / Cerundolo, V. / Jones, E.Y. / Renner, C.
History
DepositionMay 1, 2009Deposition site: RCSB / Processing site: PDBJ
SupersessionMay 19, 2009ID: 3GJG
Revision 1.0May 19, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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 / _struct_ref_seq_dif.details

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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
D: HLA class I histocompatibility antigen, A-2 alpha chain
E: Beta-2-microglobulin
J: HLA class I histocompatibility antigen, A-2 alpha chain
K: Beta-2-microglobulin
P: HLA class I histocompatibility antigen, A-2 alpha chain
Q: Beta-2-microglobulin
C: NYESO-1 peptide
F: NYESO-1 peptide
M: NYESO-1 peptide
R: NYESO-1 peptide
L: Antibody light chain
G: Antibody light chain
N: Antibody light chain
S: Antibody light chain
H: Antibody heavy chain
I: Antibody heavy chain
O: Antibody heavy chain
T: Antibody heavy chain


Theoretical massNumber of molelcules
Total (without water)362,21920
Polymers362,21920
Non-polymers00
Water00
1
A: HLA class I histocompatibility antigen, A-2 alpha chain
B: Beta-2-microglobulin
C: NYESO-1 peptide
L: Antibody light chain
H: Antibody heavy chain


Theoretical massNumber of molelcules
Total (without water)90,5555
Polymers90,5555
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9990 Å2
ΔGint-58 kcal/mol
Surface area36400 Å2
MethodPISA
2
D: HLA class I histocompatibility antigen, A-2 alpha chain
E: Beta-2-microglobulin
F: NYESO-1 peptide
G: Antibody light chain
I: Antibody heavy chain


Theoretical massNumber of molelcules
Total (without water)90,5555
Polymers90,5555
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10020 Å2
ΔGint-56 kcal/mol
Surface area36390 Å2
MethodPISA
3
J: HLA class I histocompatibility antigen, A-2 alpha chain
K: Beta-2-microglobulin
M: NYESO-1 peptide
N: Antibody light chain
O: Antibody heavy chain


Theoretical massNumber of molelcules
Total (without water)90,5555
Polymers90,5555
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
P: HLA class I histocompatibility antigen, A-2 alpha chain
Q: Beta-2-microglobulin
R: NYESO-1 peptide
S: Antibody light chain
T: Antibody heavy chain


Theoretical massNumber of molelcules
Total (without water)90,5555
Polymers90,5555
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)70.794, 105.596, 256.451
Angle α, β, γ (deg.)90.00, 92.26, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31J
41P
12A
22D
32J
42P
13B
23E
33K
43Q
14C
24F
34M
44R
15L
25G
35N
45S
16L
26G
36N
46S
17H
27I
37O
47T
18H
28I
38O
48T

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYGLNGLN2AA1 - 1801 - 180
21GLYGLYGLNGLN2DC1 - 1801 - 180
31GLYGLYGLNGLN2JE1 - 1801 - 180
41GLYGLYGLNGLN2PG1 - 1801 - 180
12ARGARGTRPTRP2AA181 - 274181 - 274
22ARGARGTRPTRP2DC181 - 274181 - 274
32ARGARGTRPTRP2JE181 - 274181 - 274
42ARGARGTRPTRP2PG181 - 274181 - 274
13METMETMETMET4BB0 - 991 - 100
23METMETMETMET4ED0 - 991 - 100
33METMETMETMET4KF0 - 991 - 100
43METMETMETMET4QH0 - 991 - 100
14SERSERVALVAL1CI1 - 91 - 9
24SERSERVALVAL1FJ1 - 91 - 9
34SERSERVALVAL1MK1 - 91 - 9
44SERSERVALVAL1RL1 - 91 - 9
15GLNGLNGLNGLN4LM1 - 1111 - 111
25GLNGLNGLNGLN4GN1 - 1111 - 111
35GLNGLNGLNGLN4NO1 - 1111 - 111
45GLNGLNGLNGLN4SP1 - 1111 - 111
16PROPROPROPRO4LM112 - 211112 - 211
26PROPROPROPRO4GN112 - 211112 - 211
36PROPROPROPRO4NO112 - 211112 - 211
46PROPROPROPRO4SP112 - 211112 - 211
17GLUGLUSERSER4HQ1 - 1191 - 119
27GLUGLUSERSER4IR1 - 1191 - 119
37GLUGLUSERSER4OS1 - 1191 - 119
47GLUGLUSERSER4TT1 - 1191 - 119
18ALAALAPROPRO4HQ120 - 219120 - 219
28ALAALAPROPRO4IR120 - 219120 - 219
38ALAALAPROPRO4OS120 - 219120 - 219
48ALAALAPROPRO4TT120 - 219120 - 219

NCS ensembles :
ID
1
2
3
4
5
6
7
8

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Components

#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 / Fragment: UNP residues 25-300
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PETT22 b+ / Production host: Escherichia coli (E. coli) / References: UniProt: P01892, UniProt: P04439*PLUS
#2: Protein
Beta-2-microglobulin / Beta-2-microglobulin form pI 5.3


Mass: 11879.356 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PETT22 b+ / Production host: Escherichia coli (E. coli) / References: UniProt: P61769
#3: Protein/peptide
NYESO-1 peptide


Mass: 1090.335 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P78358*PLUS
#4: Antibody
Antibody light chain


Mass: 22740.143 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pHEN / Production host: Escherichia coli (E. coli) / Strain (production host): HB2151
#5: Antibody
Antibody heavy chain


Mass: 22893.605 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pHEN / Production host: Escherichia coli (E. coli) / Strain (production host): HB2151
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.64 Å3/Da / Density % sol: 53.48 %
Crystal growTemperature: 294 K / Method: vapor diffusion / pH: 6.9
Details: 12% PEG 8000, 50mM Mes, pH 6.9, VAPOR DIFFUSION, temperature 294K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.933 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: May 5, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 2.9→30 Å / Num. obs: 84609 / % possible obs: 97.8 % / Rmerge(I) obs: 0.118

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→25 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.853 / SU B: 32.96 / SU ML: 0.387 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.478 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.28284 4103 5 %RANDOM
Rwork0.20083 ---
obs0.2049 78384 98.42 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 2 Å2
Baniso -1Baniso -2Baniso -3
1-0.88 Å20 Å22.85 Å2
2---3.09 Å20 Å2
3---2.44 Å2
Refinement stepCycle: LAST / Resolution: 2.9→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25472 0 0 0 25472
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.02126180
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.8271.93735624
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.13153244
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.82623.631168
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.706154120
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.93415152
X-RAY DIFFRACTIONr_chiral_restr0.1240.23812
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0220160
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.250.211318
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3220.217563
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1670.2819
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2770.2110
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2830.25
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it01.516562
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0226144
X-RAY DIFFRACTIONr_scbond_it0311205
X-RAY DIFFRACTIONr_scangle_it04.59480
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
11A720tight positional0.070.05
12D720tight positional0.080.05
13J720tight positional0.070.05
14P720tight positional0.070.05
21A376tight positional0.060.05
22D376tight positional0.070.05
23J376tight positional0.060.05
24P376tight positional0.070.05
41C75tight positional0.060.05
42F75tight positional0.110.05
43M75tight positional0.090.05
44R75tight positional0.070.05
11A758medium positional0.620.5
12D758medium positional0.590.5
13J758medium positional0.540.5
14P758medium positional0.630.5
21A383medium positional0.460.5
22D383medium positional0.380.5
23J383medium positional0.420.5
24P383medium positional0.540.5
31B836medium positional0.530.5
32E836medium positional0.50.5
33K836medium positional0.560.5
34Q836medium positional0.550.5
51L837medium positional0.520.5
52G837medium positional0.480.5
53N837medium positional0.510.5
54S837medium positional0.470.5
61L758medium positional0.50.5
62G758medium positional0.550.5
63N758medium positional0.540.5
64S758medium positional0.520.5
71H878medium positional0.50.5
72I878medium positional0.520.5
73O878medium positional0.550.5
74T878medium positional0.50.5
81H721medium positional0.580.5
82I721medium positional0.510.5
83O721medium positional0.570.5
84T721medium positional0.510.5
11A720tight thermal00.5
12D720tight thermal00.5
13J720tight thermal00.5
14P720tight thermal00.5
21A376tight thermal00.5
22D376tight thermal00.5
23J376tight thermal00.5
24P376tight thermal00.5
41C75tight thermal00.5
42F75tight thermal00.5
43M75tight thermal00.5
44R75tight thermal00.5
11A758medium thermal02
12D758medium thermal02
13J758medium thermal02
14P758medium thermal02
21A383medium thermal02
22D383medium thermal02
23J383medium thermal02
24P383medium thermal02
31B836medium thermal02
32E836medium thermal02
33K836medium thermal02
34Q836medium thermal02
51L837medium thermal02
52G837medium thermal02
53N837medium thermal02
54S837medium thermal02
61L758medium thermal02
62G758medium thermal02
63N758medium thermal02
64S758medium thermal02
71H878medium thermal02
72I878medium thermal02
73O878medium thermal02
74T878medium thermal02
81H721medium thermal02
82I721medium thermal02
83O721medium thermal02
84T721medium thermal02
LS refinement shellResolution: 2.9→2.974 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.36 302 -
Rwork0.273 5419 -
obs--93.91 %
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)
13.75380.02350.82382.5657-1.29614.08780.02210.04680.09780.0682-0.01490.0302-0.102-0.0377-0.0072-0.4485-0.06190.0095-0.05640.0105-0.3594.58412.82127.71
28.62211.9778-5.84362.7469-2.85318.0825-0.0152-0.12160.26050.12490.19960.26060.0893-0.2477-0.1844-0.43130.0437-0.10830.0579-0.004-0.2441-28.9677.39437.597
36.7209-0.14260.22315.2610.25094.2927-0.20690.5464-0.7769-0.3111-0.05890.48950.4954-0.7340.2657-0.3898-0.17890.06310.0299-0.1128-0.196-14.671-5.61825.468
410.25216.3882-6.39886.6089-2.46144.8795-0.851.28920.93940.105-0.3146-0.8017-0.06510.51261.1646-0.47990.00240.0281-0.0396-0.1077-0.347512.80915.78826.195
54.45141.87360.76383.97480.88273.48150.0239-0.13950.56370.1691-0.12940.2676-0.3886-0.51240.1056-0.23850.05460.0733-0.0780.0051-0.256823.13432.18421.01
61.7380.2633-2.28384.4306-0.301813.5380.2670.20740.39120.2557-0.2959-0.2377-1.2788-0.29990.0288-0.15330.0787-0.0559-0.14760.0229-0.084145.67548.8547.241
75.0341.9928-1.10744.3613-1.10593.9799-0.20070.3906-0.2888-0.5480.102-0.59230.16590.05160.0987-0.3784-0.01560.0354-0.1758-0.0445-0.280932.28314.67611.217
85.43961.9055-0.82789.11471.89435.35-0.3929-0.1822-0.02610.45020.0309-0.729-0.311.06710.362-0.2554-0.0645-0.09910.11890.1587-0.198759.57741.45410.354
94.2836-0.1080.44351.49240.53794.3748-0.08520.26440.171-0.06510.0406-0.01780.024-0.08720.0447-0.45470.07760.0242-0.07660.0539-0.332432.4644.48271.318
108.40980.0508-5.63920.00070.0087.84230.0644-0.1425-0.0289-0.20570.0216-0.0014-0.16250.4314-0.086-0.3648-0.0435-0.1273-0.05570.0698-0.278166.0353.63760.215
119.3501-2.07912.51146.808-1.50944.6468-0.05130.1895-1.1517-0.2756-0.0808-0.25440.52680.32250.132-0.4340.04590.0737-0.09420.0374-0.173952.165-13.16167.37
128.9147-5.45952.5543.7026-0.71652.7326-1.01510.03850.70580.08590.2886-0.57490.5444-0.26650.7265-0.4707-0.06010.0805-0.02630.1325-0.286724.3176.47373.672
134.38480.2303-2.00862.96210.09632.8469-0.0131-0.2261-0.26890.2121-0.00760.45850.22350.01030.0207-0.42250.0259-0.0584-0.16690.0416-0.31474.3470.70286.872
144.1548-2.993-2.664717.72442.53533.6192-0.48060.1116-0.3536-0.0864-0.04291.34420.3188-0.56830.5236-0.2595-0.15440.17060.1642-0.1657-0.0066-22.3426.07597.065
154.1548-2.6154-0.75454.7588-0.63380.89620.2231-0.37390.29690.0378-0.0542-0.0965-0.1390.2632-0.1689-0.3989-0.05050.0081-0.1311-0.039-0.374314.04920.13283.821
163.53171.095-1.08963.6644-0.15979.1975-0.2265-0.59370.03830.4382-0.2640.52960.4053-0.34430.4905-0.22270.02930.1159-0.031-0.0873-0.0841-8.32332.389101.943
173.4847-0.25990.00722.2955-0.39165.85040.1779-0.07610.5029-0.15110.0362-0.1619-0.24390.0236-0.2141-0.3265-0.08060.1638-0.039-0.0115-0.084930.42560.19357.209
187.3248-2.4555-6.94641.82452.906412.00820.28870.18140.3793-0.2266-0.0892-0.0593-0.5352-0.7043-0.1994-0.3230.0408-0.0509-0.03850.0656-0.1299-3.06262.29268.987
195.08581.51450.75735.5774-0.95593.9698-0.1035-0.0006-0.1036-0.34290.18910.28030.1011-0.2456-0.0856-0.3380.00560.0497-0.11830.0261-0.341110.25344.36464.955
208.69411.2116-0.37192.5729-5.542412.55580.43020.7908-0.5839-0.1855-0.5883-0.60280.89941.78250.15810.05640.03170.1106-0.0712-0.1134-0.030738.77961.6354.354
214.7651.1412-1.28626.2516-0.17353.34640.12090.15680.5173-0.04890.01560.2516-0.486-0.2672-0.1365-0.1614-0.06980.163-0.12190.0578-0.156350.70972.08439.837
223.4310.5818-0.13086.1442.89394.5690.36190.47850.1806-0.93220.0123-0.7689-0.33930.3943-0.37420.0953-0.08930.1870.13380.08120.174.23474.28318.126
235.3731-1.9435-1.70952.94940.21883.9279-0.0383-0.1067-0.2198-0.1650.0229-0.04570.28990.41570.0154-0.229-0.02850.0316-0.1670.0183-0.24557.18351.09141.736
244.9763-0.1238-3.62710.7566-0.8523.35640.3055-0.3890.588-0.07410.1862-1.9877-0.16991.0306-0.4917-0.1891-0.16440.11950.4922-0.06740.187887.49569.02425.386
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 181
2X-RAY DIFFRACTION2A182 - 275
3X-RAY DIFFRACTION3B0 - 99
4X-RAY DIFFRACTION4C1 - 9
5X-RAY DIFFRACTION5H1 - 119
6X-RAY DIFFRACTION6H120 - 219
7X-RAY DIFFRACTION7L4 - 111
8X-RAY DIFFRACTION8L112 - 211
9X-RAY DIFFRACTION9D1 - 181
10X-RAY DIFFRACTION10D182 - 275
11X-RAY DIFFRACTION11E0 - 99
12X-RAY DIFFRACTION12F1 - 9
13X-RAY DIFFRACTION13G4 - 111
14X-RAY DIFFRACTION14G112 - 211
15X-RAY DIFFRACTION15I1 - 119
16X-RAY DIFFRACTION16I120 - 219
17X-RAY DIFFRACTION17J1 - 181
18X-RAY DIFFRACTION18J182 - 275
19X-RAY DIFFRACTION19K0 - 99
20X-RAY DIFFRACTION20M1 - 9
21X-RAY DIFFRACTION21O1 - 119
22X-RAY DIFFRACTION22O120 - 219
23X-RAY DIFFRACTION23N4 - 111
24X-RAY DIFFRACTION24N112 - 211

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