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- PDB-3lk4: Crystal structure of CapZ bound to the uncapping motif from CD2AP -

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Basic information

Entry
Database: PDB / ID: 3lk4
TitleCrystal structure of CapZ bound to the uncapping motif from CD2AP
Components
  • CD2-associated protein
  • F-actin-capping protein subunit alpha-1
  • F-actin-capping protein subunit beta isoforms 1 and 2
KeywordsPROTEIN BINDING / CapZ / CD2AP / actin filaments / uncapping / actin-filament regulators / protein-protein comple / Actin capping / Actin-binding / Cytoplasm / Cytoskeleton
Function / homology
Function and homology information


Advanced glycosylation endproduct receptor signaling / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / RHOD GTPase cycle / RHOF GTPase cycle / response to glial cell derived neurotrophic factor / COPI-mediated anterograde transport / negative regulation of small GTPase mediated signal transduction / Factors involved in megakaryocyte development and platelet production / transforming growth factor beta1 production ...Advanced glycosylation endproduct receptor signaling / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / RHOD GTPase cycle / RHOF GTPase cycle / response to glial cell derived neurotrophic factor / COPI-mediated anterograde transport / negative regulation of small GTPase mediated signal transduction / Factors involved in megakaryocyte development and platelet production / transforming growth factor beta1 production / localization of cell / Rab protein signal transduction / F-actin capping protein complex / WASH complex / negative regulation of transforming growth factor beta1 production / negative regulation of filopodium assembly / response to transforming growth factor beta / slit diaphragm / podocyte differentiation / immunological synapse formation / endothelium development / nerve growth factor signaling pathway / collateral sprouting / protein heterooligomerization / cell-cell adhesion mediated by cadherin / renal albumin absorption / substrate-dependent cell migration, cell extension / membrane organization / cell junction assembly / phosphatidylinositol 3-kinase regulatory subunit binding / filopodium assembly / cell-cell junction organization / actin polymerization or depolymerization / barbed-end actin filament capping / regulation of cell morphogenesis / regulation of lamellipodium assembly / Nephrin family interactions / podosome / lamellipodium assembly / clathrin binding / maintenance of blood-brain barrier / cortical cytoskeleton / nuclear envelope lumen / D-glucose import / cell leading edge / filamentous actin / brush border / neurotrophin TRK receptor signaling pathway / centriolar satellite / protein secretion / lymph node development / adipose tissue development / stress-activated MAPK cascade / cytoskeleton organization / ruffle / actin filament polymerization / ERK1 and ERK2 cascade / phosphatidylinositol 3-kinase/protein kinase B signal transduction / hippocampal mossy fiber to CA3 synapse / liver development / trans-Golgi network membrane / actin filament organization / positive regulation of protein secretion / regulation of actin cytoskeleton organization / response to insulin / synapse organization / response to virus / cell morphogenesis / neuromuscular junction / protein catabolic process / regulation of synaptic plasticity / lipid metabolic process / Schaffer collateral - CA1 synapse / structural constituent of cytoskeleton / fibrillar center / response to wounding / Z disc / positive regulation of protein localization to nucleus / SH3 domain binding / male gonad development / actin filament binding / cell migration / actin cytoskeleton / late endosome / lamellipodium / T cell receptor signaling pathway / growth cone / actin cytoskeleton organization / protein-containing complex assembly / vesicle / negative regulation of neuron apoptotic process / response to oxidative stress / cell population proliferation / postsynaptic density / cadherin binding / inflammatory response / axon / cell division / dendrite / apoptotic process
Similarity search - Function
F-actin capping protein, alpha/beta subunit, N-terminal domain / F-actin capping protein, alpha subunit / F-actin capping protein, beta subunit / CD2-associated protein, first SH3 domain / CD2-associated protein, second SH3 domain / CD2-associated protein, third SH3 domain / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit ...F-actin capping protein, alpha/beta subunit, N-terminal domain / F-actin capping protein, alpha subunit / F-actin capping protein, beta subunit / CD2-associated protein, first SH3 domain / CD2-associated protein, second SH3 domain / CD2-associated protein, third SH3 domain / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / : / Ribosomal protein S3 C-terminal domain / Variant SH3 domain / Aspartate Aminotransferase, domain 1 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / SH3 domain / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Alpha-Beta Complex / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta isoforms 1 and 2 / CD2-associated protein
Similarity search - Component
Biological speciesGallus gallus (chicken)
homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.99 Å
AuthorsHernandez-Valladares, M. / Kim, T. / Kannan, B. / Tung, A. / Cooper, J.A. / Robinson, R.C.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.
Authors: Hernandez-Valladares, M. / Kim, T. / Kannan, B. / Tung, A. / Aguda, A.H. / Larsson, M. / Cooper, J.A. / Robinson, R.C.
History
DepositionJan 27, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Apr 7, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 18, 2019Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Nov 1, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: F-actin-capping protein subunit alpha-1
B: F-actin-capping protein subunit beta isoforms 1 and 2
C: CD2-associated protein
D: F-actin-capping protein subunit alpha-1
E: F-actin-capping protein subunit beta isoforms 1 and 2
F: CD2-associated protein
G: F-actin-capping protein subunit alpha-1
H: F-actin-capping protein subunit beta isoforms 1 and 2
I: CD2-associated protein
J: F-actin-capping protein subunit alpha-1
K: F-actin-capping protein subunit beta isoforms 1 and 2
L: CD2-associated protein
M: F-actin-capping protein subunit alpha-1
N: F-actin-capping protein subunit beta isoforms 1 and 2
O: CD2-associated protein
P: F-actin-capping protein subunit alpha-1
Q: F-actin-capping protein subunit beta isoforms 1 and 2
R: CD2-associated protein
S: F-actin-capping protein subunit alpha-1
T: F-actin-capping protein subunit beta isoforms 1 and 2
U: CD2-associated protein
V: F-actin-capping protein subunit alpha-1
W: F-actin-capping protein subunit beta isoforms 1 and 2
X: CD2-associated protein
Y: F-actin-capping protein subunit alpha-1
Z: F-actin-capping protein subunit beta isoforms 1 and 2
0: CD2-associated protein
1: F-actin-capping protein subunit alpha-1
2: F-actin-capping protein subunit beta isoforms 1 and 2
3: CD2-associated protein
4: F-actin-capping protein subunit alpha-1
5: F-actin-capping protein subunit beta isoforms 1 and 2
6: CD2-associated protein
7: F-actin-capping protein subunit alpha-1
8: F-actin-capping protein subunit beta isoforms 1 and 2
9: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)811,55936
Polymers811,55936
Non-polymers00
Water52,2442900
1
A: F-actin-capping protein subunit alpha-1
B: F-actin-capping protein subunit beta isoforms 1 and 2
C: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10590 Å2
ΔGint-55 kcal/mol
Surface area23070 Å2
MethodPISA
2
D: F-actin-capping protein subunit alpha-1
E: F-actin-capping protein subunit beta isoforms 1 and 2
F: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10600 Å2
ΔGint-56 kcal/mol
Surface area23020 Å2
MethodPISA
3
G: F-actin-capping protein subunit alpha-1
H: F-actin-capping protein subunit beta isoforms 1 and 2
I: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10570 Å2
ΔGint-56 kcal/mol
Surface area23130 Å2
MethodPISA
4
J: F-actin-capping protein subunit alpha-1
K: F-actin-capping protein subunit beta isoforms 1 and 2
L: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10580 Å2
ΔGint-55 kcal/mol
Surface area23040 Å2
MethodPISA
5
M: F-actin-capping protein subunit alpha-1
N: F-actin-capping protein subunit beta isoforms 1 and 2
O: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10570 Å2
ΔGint-56 kcal/mol
Surface area23110 Å2
MethodPISA
6
P: F-actin-capping protein subunit alpha-1
Q: F-actin-capping protein subunit beta isoforms 1 and 2
R: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10580 Å2
ΔGint-55 kcal/mol
Surface area23090 Å2
MethodPISA
7
S: F-actin-capping protein subunit alpha-1
T: F-actin-capping protein subunit beta isoforms 1 and 2
U: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10590 Å2
ΔGint-55 kcal/mol
Surface area23000 Å2
MethodPISA
8
V: F-actin-capping protein subunit alpha-1
W: F-actin-capping protein subunit beta isoforms 1 and 2
X: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10580 Å2
ΔGint-55 kcal/mol
Surface area23120 Å2
MethodPISA
9
Y: F-actin-capping protein subunit alpha-1
Z: F-actin-capping protein subunit beta isoforms 1 and 2
0: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10600 Å2
ΔGint-56 kcal/mol
Surface area23160 Å2
MethodPISA
10
1: F-actin-capping protein subunit alpha-1
2: F-actin-capping protein subunit beta isoforms 1 and 2
3: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10600 Å2
ΔGint-56 kcal/mol
Surface area23080 Å2
MethodPISA
11
4: F-actin-capping protein subunit alpha-1
5: F-actin-capping protein subunit beta isoforms 1 and 2
6: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10590 Å2
ΔGint-56 kcal/mol
Surface area23010 Å2
MethodPISA
12
7: F-actin-capping protein subunit alpha-1
8: F-actin-capping protein subunit beta isoforms 1 and 2
9: CD2-associated protein


Theoretical massNumber of molelcules
Total (without water)67,6303
Polymers67,6303
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10580 Å2
ΔGint-54 kcal/mol
Surface area23120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.728, 142.341, 192.999
Angle α, β, γ (deg.)90.00, 89.99, 90.00
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
111
121
12
22
32
42
52
62
72
82
92
102
112
122
13
23
33
43
53
63
73
83
93
103
113
123

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and resid 8:276
211chain D and resid 8:276
311chain G and resid 8:276
411chain J and resid 8:276
511chain M and resid 8:276
611chain P and resid 8:276
711chain S and resid 8:276
811chain V and resid 8:276
911chain Y and resid 8:276
1011chain 1 and resid 8:276
1111chain 4 and resid 8:276
1211chain 7 and resid 8:276
112chain B and resid 4:244
212chain E and resid 4:244
312chain H and resid 4:244
412chain K and resid 4:244
512chain N and resid 4:244
612chain Q and resid 4:244
712chain T and resid 4:244
812chain W and resid 4:244
912chain Z and resid 4:244
1012chain 2 and resid 4:244
1112chain 5 and resid 4:244
1212chain 8 and resid 4:244
113chain C and resid 475:503
213chain F and resid 475:503
313chain I and resid 475:503
413chain L and resid 475:503
513chain O and resid 475:503
613chain R and resid 475:503
713chain U and resid 475:503
813chain X and resid 475:503
913chain 0 and resid 475:503
1013chain 3 and resid 475:503
1113chain 6 and resid 475:503
1213chain 9 and resid 475:503

NCS ensembles :
ID
1
2
3

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Components

#1: Protein
F-actin-capping protein subunit alpha-1 / CapZ 36/32 / Beta-actinin subunit I


Mass: 33001.789 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: CAPZA1 / Plasmid: pET3d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Star (DE3) / References: UniProt: P13127
#2: Protein
F-actin-capping protein subunit beta isoforms 1 and 2 / CapZ B1 and B2 / CapZ 36/32 / Beta-actinin subunit II


Mass: 31403.449 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: CAPZA1, CAPZB / Plasmid: pET3d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Star (DE3) / References: UniProt: P14315
#3: Protein/peptide
CD2-associated protein / Cas ligand with multiple SH3 domains / Adapter protein CMS


Mass: 3224.673 Da / Num. of mol.: 12 / Source method: obtained synthetically / Details: peptide synthesis / Source: (synth.) homo sapiens (human) / References: UniProt: Q9Y5K6
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2900 / Source method: isolated from a natural source / Formula: H2O

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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: 2.02 Å3/Da / Density % sol: 39.16 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 30% PEG 400, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 105 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 14, 2008 / Details: phosphor screen, fiber-optic taper, CCD chip
RadiationMonochromator: double-crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 1.99→20 Å / Num. obs: 358158 / % possible obs: 82.6 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.054 / Rsym value: 0.054 / Net I/σ(I): 24.7
Reflection shellResolution: 2→2.1 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.418 / Mean I/σ(I) obs: 3.3 / Num. unique all: 16631 / Rsym value: 0.418 / % possible all: 76.8

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Processing

Software
NameVersionClassification
HKL-2000data collection
MOLREPphasing
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3LK2

3lk2


Resolution: 1.99→19.984 Å / SU ML: 0.3 / Isotropic thermal model: RANDOM / Cross valid method: THROUGHOUT / σ(F): 1.96 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2722 18001 5.03 %
Rwork0.2253 --
obs0.2277 358158 82.25 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.913 Å2 / ksol: 0.32 e/Å3
Displacement parametersBiso mean: 49.4 Å2
Baniso -1Baniso -2Baniso -3
1--2.1232 Å20.3329 Å2-0.8627 Å2
2--2.3544 Å2-0.7957 Å2
3----4.8098 Å2
Refinement stepCycle: LAST / Resolution: 1.99→19.984 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms51470 0 0 2900 54370
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00752442
X-RAY DIFFRACTIONf_angle_d1.0270986
X-RAY DIFFRACTIONf_dihedral_angle_d19.01219408
X-RAY DIFFRACTIONf_chiral_restr0.0737743
X-RAY DIFFRACTIONf_plane_restr0.0049325
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2185X-RAY DIFFRACTIONPOSITIONAL
12D2185X-RAY DIFFRACTIONPOSITIONAL0.033
13G2185X-RAY DIFFRACTIONPOSITIONAL0.041
14J2185X-RAY DIFFRACTIONPOSITIONAL0.036
15M2185X-RAY DIFFRACTIONPOSITIONAL0.043
16P2185X-RAY DIFFRACTIONPOSITIONAL0.026
17S2185X-RAY DIFFRACTIONPOSITIONAL0.038
18V2185X-RAY DIFFRACTIONPOSITIONAL0.043
19Y2185X-RAY DIFFRACTIONPOSITIONAL0.022
11012185X-RAY DIFFRACTIONPOSITIONAL0.022
11142185X-RAY DIFFRACTIONPOSITIONAL0.037
11272185X-RAY DIFFRACTIONPOSITIONAL0.042
21B1864X-RAY DIFFRACTIONPOSITIONAL
22E1864X-RAY DIFFRACTIONPOSITIONAL0.032
23H1864X-RAY DIFFRACTIONPOSITIONAL0.049
24K1864X-RAY DIFFRACTIONPOSITIONAL0.035
25N1864X-RAY DIFFRACTIONPOSITIONAL0.05
26Q1864X-RAY DIFFRACTIONPOSITIONAL0.024
27T1864X-RAY DIFFRACTIONPOSITIONAL0.033
28W1864X-RAY DIFFRACTIONPOSITIONAL0.05
29Z1864X-RAY DIFFRACTIONPOSITIONAL0.024
21021864X-RAY DIFFRACTIONPOSITIONAL0.024
21151864X-RAY DIFFRACTIONPOSITIONAL0.034
21281864X-RAY DIFFRACTIONPOSITIONAL0.049
31C225X-RAY DIFFRACTIONPOSITIONAL
32F225X-RAY DIFFRACTIONPOSITIONAL0.022
33I225X-RAY DIFFRACTIONPOSITIONAL0.03
34L225X-RAY DIFFRACTIONPOSITIONAL0.023
35O225X-RAY DIFFRACTIONPOSITIONAL0.028
36R225X-RAY DIFFRACTIONPOSITIONAL0.015
37U225X-RAY DIFFRACTIONPOSITIONAL0.022
38X225X-RAY DIFFRACTIONPOSITIONAL0.029
390225X-RAY DIFFRACTIONPOSITIONAL0.017
3103225X-RAY DIFFRACTIONPOSITIONAL0.013
3116225X-RAY DIFFRACTIONPOSITIONAL0.024
3129225X-RAY DIFFRACTIONPOSITIONAL0.029
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.9902-2.06120.33516090.2833116475
2.0612-2.14370.322216600.26593145476
2.1437-2.24110.330616370.27273154076
2.2411-2.35910.316617630.25923200478
2.3591-2.50660.316217670.2523356081
2.5066-2.69970.304118620.24553502885
2.6997-2.97060.2919720.24163661989
2.9706-3.39870.287919380.23593702590
3.3987-4.27510.237418550.20063551686
4.2751-19.98480.206119380.17353624788
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)
10.3788-0.22080.40872.4473-0.51230.6558-0.01710.1497-0.19280.60650.13430.1288-0.0439-0.41070.0485-0.0870.0432-0.00390.22960.04290.1709-13.247599.5705107.3952
21.19231.4572-0.53143.28790.34480.6249-0.77530.303-0.8872-1.94840.0334-0.25330.1728-0.8729-1.0063-0.04960.2032-0.91720.4763-0.0553-0.5308-21.770787.625386.2054
31.25490.09340.10641.77171.37540.823-0.0740.2254-0.1184-0.8673-0.0260.1546-0.4021-0.0778-0.06150.5974-0.009-0.13520.1763-0.00980.1458-5.159584.353984.1928
40.4166-0.3091-0.21880.56830.07630.1333-0.53030.13960.13690.42620.0907-0.6431-0.3177-0.0705-0.0120.23180.0949-0.12660.2553-0.08960.398124.016878.3442110.9537
50.1496-0.09190.12540.1454-0.14140.0896-0.21-0.0158-0.04420.5631-0.0039-0.4423-0.22420.33420.00020.23250.0412-0.07070.23140.03640.1984-3.905293.524110.7678
60.47220.7440.04591.04140.18160.084-0.5413-0.3330.560.56520.4001-0.5268-0.10730.0207-0.00010.41570.1728-0.30160.3221-0.18030.483514.0434102.4211118.8675
70.59280.5162-0.31021.0906-0.30691.746-0.1941-0.11960.11170.34820.0647-0.5485-1.0357-0.14340.02610.28510.134-0.22020.1733-0.10110.341620.902390.1567118.7683
81.9885-0.31120.53472.67110.41650.2427-0.2707-0.26290.01820.2450.135-0.17820.0797-0.1452-0.0650.16480.0948-0.08140.2013-0.01080.184211.814582.5195112.3659
90.0911-0.03840.18140.0263-0.11840.4850.00570.0477-0.1414-0.0663-0.02120.05980.2373-0.05540.00560.19260.19820.08220.4095-0.16370.6583-25.111793.1965108.7835
100.03920.0236-0.0830.0147-0.03360.1873-0.556-0.1530.08020.2980.75540.0514-0.2838-0.70580.00020.53080.192-0.16950.45480.00210.24420.624794.5541121.3905
110.2610.2124-0.01490.1727-0.14050.36360.06410.1983-0.10280.0279-0.04750.1129-0.4607-0.3709-00.25170.1369-0.00830.35760.00730.1863-13.365299.466943.1424
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983.1593-0.3643-0.81343.2805-0.5090.7089-0.3162-0.3919-0.0030.29590.19460.1873-0.090.16360.06180.34610.1150.12350.18230.03280.18714.392-11.533715.8806
992.17760.278-1.18071.0714-0.92341.2244-0.50010.2330.97260.71870.52880.1239-0.19980.0699-0.0850.63660.2238-0.09510.47260.20141.007141.3213-22.222912.3091
1000.1767-0.2507-0.0961.0622-0.27810.3342-0.5807-0.2482-0.13240.89550.6237-0.2030.17320.5888-0.13020.78840.22460.20920.39860.04220.249315.5827-23.566124.9095
1010.53650.364-0.06490.1898-0.02380.1647-0.01440.0713-0.07030.05520.0795-0.05720.51190.1718-0.05120.82150.13560.08510.38150.01390.227829.4966-28.5147-53.3602
1021.6997-0.3273-0.68510.71320.15661.3187-0.1411-0.35390.0227-0.11060.1048-0.00450.36120.43030.06650.47790.04680.15350.2498-0.01130.124938.1988-16.561-74.4602
1031.89940.8428-0.52542.1531-0.41050.1929-0.21770.2664-0.0182-0.44820.2670.06750.1321-0.1645-0.00840.6627-0.07110.08250.1806-0.02090.114421.601-13.3599-76.6399
1041.02290.9851-0.62531.8837-1.39841.19650.25390.48170.51720.29760.2180.4234-0.42-0.2807-0.41770.52240.10880.09020.14040.11270.272-7.8788-7.4191-50.1786
1050.3563-0.3149-0.64290.91820.30251.29470.1031-0.1201-0.00830.6632-0.18760.20180.37720.19140.06890.8340.03860.12480.2149-0.02560.226120.0215-22.5418-50.1169
1061.14870.9667-0.45810.7323-0.32490.4809-0.2588-0.0476-0.3046-0.34420.095-0.03390.22320.22530.14090.57490.10660.13720.17090.07360.20282.0477-31.5154-42.2036
1070.8710.3857-0.15721.6276-1.25410.9534-0.24040.02230.0747-0.05770.12670.14620.16140.12330.08460.44170.09030.1240.07690.04830.1909-4.8264-19.2522-42.2948
1081.96470.0883-0.63671.2617-0.09630.8921-0.0457-0.0030.1227-0.06710.12060.0782-0.41660.1094-0.11230.53470.06040.10570.09350.0220.15934.2943-11.5692-48.5839
1094.09862.0122-0.32674.07010.0737.80810.62860.62060.27550.2270.5060.37190.11270.8838-0.69860.90860.2107-0.050.5810.00930.468141.2634-22.1024-51.8491
1100.1512-0.0640.04870.30760.35560.7473-0.2518-0.14620.0452-0.20530.33080.03910.31640.72560.01040.61020.0430.16990.3391-0.02380.195815.4091-23.6617-39.515
1110.41520.5051-0.10640.7394-0.00320.5060.0189-0.01960.0506-0.10070.0012-0.24260.03330.28870.05520.02590.0450.00020.207-0.02020.173128.0886-28.509875.0663
1120.73070.38230.85880.663-0.79893.6879-0.00980.24330.1335-0.2744-0.2045-0.38450.39011.29330.39240.08370.09990.10360.60950.06050.207236.6333-16.536453.8769
1130.94430.06020.12010.6204-1.50262.549-0.01410.14950.1131-0.1083-0.047-0.01950.15030.2170.06250.09060.03860.05580.18530.01230.161520.0187-13.322751.8251
1141.5049-1.01990.11151.0299-0.37890.47850.0410.15130.21350.00770.03660.279-0.0219-0.2925-0.13370.04780.03470.06060.26390.03750.333-9.2614-7.409778.5245
1153.23981.29370.81314.6382.46752.42280.22910.02620.32160.8617-0.20980.34050.5450.3201-0.00610.17540.00460.08250.1695-0.00980.156518.5992-22.602478.2684
1161.60390.4718-1.1412-0.1243-0.41920.8211-0.163-0.1307-0.1303-0.09090.0534-0.05680.09160.21370.08850.09130.03830.06370.12350.01740.22840.6836-31.560286.3136
1172.4515-0.749-0.84011.17920.6630.63250.25840.0462-0.02260.8431-0.18550.28511.2214-0.1808-0.6301-0.5670.17990.17930.0042-0.01670.1663-6.1644-19.28386.3003
1181.04640.0553-0.70490.7145-0.36681.23120.06230.00520.21270.02990.1035-0.0125-0.14650.171-0.29180.06260.04590.05630.14280.00530.18172.9333-11.607779.952
1190.8792-1.34320.07543.6957-0.02060.607-0.545-0.13110.4972-0.26760.4842-1.3486-0.14720.234-0.00130.12030.0358-0.02590.4520.04280.851139.878-22.200176.527
1200.7256-0.5042-0.29950.94190.30951.8948-0.0536-0.31740.05870.44460.0903-0.42640.03140.8545-0.04780.04190.02810.01240.415-0.02670.288914.0905-23.767888.9904
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 8:45)
2X-RAY DIFFRACTION2(chain A and resid 46:148)
3X-RAY DIFFRACTION3(chain A and resid 149:249)
4X-RAY DIFFRACTION4(chain A and resid 250:276)
5X-RAY DIFFRACTION5(chain B and resid 4:22)
6X-RAY DIFFRACTION6(chain B and resid 23:98)
7X-RAY DIFFRACTION7(chain B and resid 99:139)
8X-RAY DIFFRACTION8(chain B and resid 140:244)
9X-RAY DIFFRACTION9(chain C and resid 475:481)
10X-RAY DIFFRACTION10(chain C and resid 482:505)
11X-RAY DIFFRACTION11(chain D and resid 8:45)
12X-RAY DIFFRACTION12(chain D and resid 46:148)
13X-RAY DIFFRACTION13(chain D and resid 149:249)
14X-RAY DIFFRACTION14(chain D and resid 250:276)
15X-RAY DIFFRACTION15(chain E and resid 4:22)
16X-RAY DIFFRACTION16(chain E and resid 23:98)
17X-RAY DIFFRACTION17(chain E and resid 99:139)
18X-RAY DIFFRACTION18(chain E and resid 140:244)
19X-RAY DIFFRACTION19(chain F and resid 475:481)
20X-RAY DIFFRACTION20(chain F and resid 482:505)
21X-RAY DIFFRACTION21(chain G and resid 8:45)
22X-RAY DIFFRACTION22(chain G and resid 46:148)
23X-RAY DIFFRACTION23(chain G and resid 149:249)
24X-RAY DIFFRACTION24(chain G and resid 250:276)
25X-RAY DIFFRACTION25(chain H and resid 4:22)
26X-RAY DIFFRACTION26(chain H and resid 23:98)
27X-RAY DIFFRACTION27(chain H and resid 99:139)
28X-RAY DIFFRACTION28(chain H and resid 140:244)
29X-RAY DIFFRACTION29(chain I and resid 475:481)
30X-RAY DIFFRACTION30(chain I and resid 482:505)
31X-RAY DIFFRACTION31(chain J and resid 8:45)
32X-RAY DIFFRACTION32(chain J and resid 46:148)
33X-RAY DIFFRACTION33(chain J and resid 149:249)
34X-RAY DIFFRACTION34(chain J and resid 250:276)
35X-RAY DIFFRACTION35(chain K and resid 4:22)
36X-RAY DIFFRACTION36(chain K and resid 23:98)
37X-RAY DIFFRACTION37(chain K and resid 99:139)
38X-RAY DIFFRACTION38(chain K and resid 140:244)
39X-RAY DIFFRACTION39(chain L and resid 475:481)
40X-RAY DIFFRACTION40(chain L and resid 482:505)
41X-RAY DIFFRACTION41(chain M and resid 8:45)
42X-RAY DIFFRACTION42(chain M and resid 46:148)
43X-RAY DIFFRACTION43(chain M and resid 149:249)
44X-RAY DIFFRACTION44(chain M and resid 250:276)
45X-RAY DIFFRACTION45(chain N and resid 4:22)
46X-RAY DIFFRACTION46(chain N and resid 23:98)
47X-RAY DIFFRACTION47(chain N and resid 99:139)
48X-RAY DIFFRACTION48(chain N and resid 140:244)
49X-RAY DIFFRACTION49(chain O and resid 475:481)
50X-RAY DIFFRACTION50(chain O and resid 482:505)
51X-RAY DIFFRACTION51(chain P and resid 8:45)
52X-RAY DIFFRACTION52(chain P and resid 46:148)
53X-RAY DIFFRACTION53(chain P and resid 149:249)
54X-RAY DIFFRACTION54(chain P and resid 250:276)
55X-RAY DIFFRACTION55(chain Q and resid 4:22)
56X-RAY DIFFRACTION56(chain Q and resid 23:98)
57X-RAY DIFFRACTION57(chain Q and resid 99:139)
58X-RAY DIFFRACTION58(chain Q and resid 140:244)
59X-RAY DIFFRACTION59(chain R and resid 475:481)
60X-RAY DIFFRACTION60(chain R and resid 482:505)
61X-RAY DIFFRACTION61(chain S and resid 8:45)
62X-RAY DIFFRACTION62(chain S and resid 46:148)
63X-RAY DIFFRACTION63(chain S and resid 149:249)
64X-RAY DIFFRACTION64(chain S and resid 250:276)
65X-RAY DIFFRACTION65(chain T and resid 4:22)
66X-RAY DIFFRACTION66(chain T and resid 23:98)
67X-RAY DIFFRACTION67(chain T and resid 99:139)
68X-RAY DIFFRACTION68(chain T and resid 140:244)
69X-RAY DIFFRACTION69(chain U and resid 475:481)
70X-RAY DIFFRACTION70(chain U and resid 482:505)
71X-RAY DIFFRACTION71(chain V and resid 8:45)
72X-RAY DIFFRACTION72(chain V and resid 46:148)
73X-RAY DIFFRACTION73(chain V and resid 149:249)
74X-RAY DIFFRACTION74(chain V and resid 250:276)
75X-RAY DIFFRACTION75(chain W and resid 4:22)
76X-RAY DIFFRACTION76(chain W and resid 23:98)
77X-RAY DIFFRACTION77(chain W and resid 99:139)
78X-RAY DIFFRACTION78(chain W and resid 140:244)
79X-RAY DIFFRACTION79(chain X and resid 475:481)
80X-RAY DIFFRACTION80(chain X and resid 482:505)
81X-RAY DIFFRACTION81(chain Y and resid 8:45)
82X-RAY DIFFRACTION82(chain Y and resid 46:148)
83X-RAY DIFFRACTION83(chain Y and resid 149:249)
84X-RAY DIFFRACTION84(chain Y and resid 250:276)
85X-RAY DIFFRACTION85(chain Z and resid 4:22)
86X-RAY DIFFRACTION86(chain Z and resid 23:98)
87X-RAY DIFFRACTION87(chain Z and resid 99:139)
88X-RAY DIFFRACTION88(chain Z and resid 140:244)
89X-RAY DIFFRACTION89(chain 0 and resid 475:481)
90X-RAY DIFFRACTION90(chain 0 and resid 482:505)
91X-RAY DIFFRACTION91(chain 1 and resid 8:45)
92X-RAY DIFFRACTION92(chain 1 and resid 46:148)
93X-RAY DIFFRACTION93(chain 1 and resid 149:249)
94X-RAY DIFFRACTION94(chain 1 and resid 250:276)
95X-RAY DIFFRACTION95(chain 2 and resid 4:22)
96X-RAY DIFFRACTION96(chain 2 and resid 23:98)
97X-RAY DIFFRACTION97(chain 2 and resid 99:139)
98X-RAY DIFFRACTION98(chain 2 and resid 140:244)
99X-RAY DIFFRACTION99(chain 3 and resid 475:481)
100X-RAY DIFFRACTION100(chain 3 and resid 482:505)
101X-RAY DIFFRACTION101(chain 4 and resid 8:45)
102X-RAY DIFFRACTION102(chain 4 and resid 46:148)
103X-RAY DIFFRACTION103(chain 4 and resid 149:249)
104X-RAY DIFFRACTION104(chain 4 and resid 250:276)
105X-RAY DIFFRACTION105(chain 5 and resid 4:22)
106X-RAY DIFFRACTION106(chain 5 and resid 23:98)
107X-RAY DIFFRACTION107(chain 5 and resid 99:139)
108X-RAY DIFFRACTION108(chain 5 and resid 140:244)
109X-RAY DIFFRACTION109(chain 6 and resid 475:481)
110X-RAY DIFFRACTION110(chain 6 and resid 482:505)
111X-RAY DIFFRACTION111(chain 7 and resid 8:45)
112X-RAY DIFFRACTION112(chain 7 and resid 46:148)
113X-RAY DIFFRACTION113(chain 7 and resid 149:249)
114X-RAY DIFFRACTION114(chain 7 and resid 250:276)
115X-RAY DIFFRACTION115(chain 8 and resid 4:22)
116X-RAY DIFFRACTION116(chain 8 and resid 23:98)
117X-RAY DIFFRACTION117(chain 8 and resid 99:139)
118X-RAY DIFFRACTION118(chain 8 and resid 140:244)
119X-RAY DIFFRACTION119(chain 9 and resid 475:481)
120X-RAY DIFFRACTION120(chain 9 and resid 482:505)

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