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- PDB-5bo4: Structure of SOCS2:Elongin C:Elongin B from DMSO-treated crystals -

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Basic information

Entry
Database: PDB / ID: 5bo4
TitleStructure of SOCS2:Elongin C:Elongin B from DMSO-treated crystals
Components
  • Suppressor of cytokine signaling 2
  • Transcription elongation factor B polypeptide 1
  • Transcription elongation factor B polypeptide 2
KeywordsSIGNALING PROTEIN / Ubiquitin Ligase / Suppressor of Cytokine Signalling
Function / homology
Function and homology information


negative regulation of growth hormone receptor signaling pathway / JAK pathway signal transduction adaptor activity / phosphorylation-dependent protein binding / cytokine receptor binding / negative regulation of receptor signaling pathway via JAK-STAT / target-directed miRNA degradation / elongin complex / growth hormone receptor binding / VCB complex / Cul5-RING ubiquitin ligase complex ...negative regulation of growth hormone receptor signaling pathway / JAK pathway signal transduction adaptor activity / phosphorylation-dependent protein binding / cytokine receptor binding / negative regulation of receptor signaling pathway via JAK-STAT / target-directed miRNA degradation / elongin complex / growth hormone receptor binding / VCB complex / Cul5-RING ubiquitin ligase complex / growth hormone receptor signaling pathway / negative regulation of multicellular organism growth / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / mammary gland alveolus development / regulation of signal transduction / cell surface receptor signaling pathway via JAK-STAT / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Growth hormone receptor signaling / Formation of HIV-1 elongation complex containing HIV-1 Tat / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV elongation complex in the absence of HIV Tat / cellular response to hormone stimulus / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / insulin-like growth factor receptor binding / lactation / RNA Polymerase II Pre-transcription Events / positive regulation of neuron differentiation / Negative regulation of FLT3 / Interleukin-7 signaling / transcription corepressor binding / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / regulation of cell growth / Vif-mediated degradation of APOBEC3G / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / Regulation of expression of SLITs and ROBOs / cytokine-mediated signaling pathway / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / response to estradiol / Neddylation / protein-containing complex assembly / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / intracellular signal transduction / protein ubiquitination / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / nucleoplasm / cytoplasm / cytosol
Similarity search - Function
SOCS box / Suppressor of cytokine signalling 2 / SOCS2, SH2 domain / suppressors of cytokine signalling / SOCS box / SOCS box-like domain superfamily / SOCS box domain / SOCS box domain profile. / SOCS_box / Elongin C; Chain C, domain 1 ...SOCS box / Suppressor of cytokine signalling 2 / SOCS2, SH2 domain / suppressors of cytokine signalling / SOCS box / SOCS box-like domain superfamily / SOCS box domain / SOCS box domain profile. / SOCS_box / Elongin C; Chain C, domain 1 / Elongin-C / Elongin B / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SH2 domain / SHC Adaptor Protein / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / SKP1/BTB/POZ domain superfamily / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Suppressor of cytokine signaling 2 / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.9 Å
AuthorsGadd, M.S. / Bulatov, E. / Ciulli, A.
Funding support1items
OrganizationGrant numberCountry
European Research Council
CitationJournal: Plos One / Year: 2015
Title: Serendipitous SAD Solution for DMSO-Soaked SOCS2-ElonginC-ElonginB Crystals Using Covalently Incorporated Dimethylarsenic: Insights into Substrate Receptor Conformational Flexibility in Cullin RING Ligases.
Authors: Gadd, M.S. / Bulatov, E. / Ciulli, A.
History
DepositionMay 27, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jul 8, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Data collection / Category: diffrn / diffrn_radiation / diffrn_source / Item: _diffrn_radiation.diffrn_id
Revision 1.2Oct 9, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength / pdbx_entry_details / pdbx_modification_feature / reflns / reflns_shell
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_radiation_wavelength.wavelength / _reflns.pdbx_Rsym_value / _reflns_shell.pdbx_Rsym_value

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Suppressor of cytokine signaling 2
B: Transcription elongation factor B polypeptide 2
C: Transcription elongation factor B polypeptide 1
D: Suppressor of cytokine signaling 2
E: Transcription elongation factor B polypeptide 2
F: Transcription elongation factor B polypeptide 1
G: Suppressor of cytokine signaling 2
H: Transcription elongation factor B polypeptide 2
I: Transcription elongation factor B polypeptide 1
J: Suppressor of cytokine signaling 2
K: Transcription elongation factor B polypeptide 2
L: Transcription elongation factor B polypeptide 1
M: Suppressor of cytokine signaling 2
N: Transcription elongation factor B polypeptide 2
O: Transcription elongation factor B polypeptide 1
P: Suppressor of cytokine signaling 2
Q: Transcription elongation factor B polypeptide 2
R: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)253,22618
Polymers253,22618
Non-polymers00
Water59433
1
A: Suppressor of cytokine signaling 2
B: Transcription elongation factor B polypeptide 2
C: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Suppressor of cytokine signaling 2
E: Transcription elongation factor B polypeptide 2
F: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
G: Suppressor of cytokine signaling 2
H: Transcription elongation factor B polypeptide 2
I: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
J: Suppressor of cytokine signaling 2
K: Transcription elongation factor B polypeptide 2
L: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
M: Suppressor of cytokine signaling 2
N: Transcription elongation factor B polypeptide 2
O: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
P: Suppressor of cytokine signaling 2
Q: Transcription elongation factor B polypeptide 2
R: Transcription elongation factor B polypeptide 1


Theoretical massNumber of molelcules
Total (without water)42,2043
Polymers42,2043
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)185.217, 185.217, 67.204
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31G
41J
51M
61P
12B
22E
32H
42K
52N
62Q
13C
23F
33I
43L
53O
63R

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A32 - 198
2114D32 - 198
3114G32 - 198
4114J32 - 198
5114M32 - 198
6114P32 - 198
1124B1 - 104
2124E1 - 104
3124H1 - 104
4124K1 - 104
5124N1 - 104
6124Q1 - 104
1134C17 - 112
2134F17 - 112
3134I17 - 112
4134L17 - 112
5134O17 - 112
6134R17 - 112

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.566268, 0.821767, -0.063556), (0.820238, -0.569425, -0.054451), (-0.080937, -0.021297, -0.996492)-0.5837, 119.328987, 56.068932
3given(-0.998944, -0.043313, 0.015336), (-0.043163, 0.999018, 0.009954), (-0.015752, 0.009282, -0.999833)96.522743, 53.272171, 29.06266
4given(-0.548441, -0.836172, -0.005386), (0.836188, -0.548438, -0.00208), (-0.001214, -0.005645, 0.999983)188.020981, 112.474457, -22.241369
5given(-0.997727, 0.021042, -0.06401), (0.024547, 0.998213, -0.054481), (0.062749, -0.055929, -0.996461)183.165405, 1.39315, 28.03113
6given(-0.552012, 0.830301, 0.076705), (-0.828796, -0.556448, 0.058847), (0.091543, -0.031088, 0.995316)0.2492, 218.961884, -46.292629
7given(1), (1), (1)
8given(0.490237, 0.871264, 0.023822), (0.869616, -0.487106, -0.080603), (-0.058623, 0.060231, -0.996462)-2.55777, 112.297821, 49.879238
9given(-0.997753, -0.060461, 0.028854), (-0.060379, 0.998169, 0.003729), (-0.029026, 0.001979, -0.999577)97.397926, 53.51656, 29.5243
10given(-0.58245, -0.8125, -0.024409), (0.81264, -0.582733, 0.0061), (-0.01918, -0.016283, 0.999683)188.822952, 116.743683, -20.166031
11given(-0.991361, -0.122077, 0.047966), (-0.125692, 0.98872, -0.08145), (-0.037482, -0.086775, -0.995523)198.44371, 18.936199, 42.489101
12given(-0.481164, 0.875576, -0.04299), (-0.874345, -0.475793, 0.095611), (0.06326, 0.083592, 0.99449)-0.51914, 209.501801, -58.218868
13given(1), (1), (1)
14given(0.493554, 0.86968, 0.007858), (0.866317, -0.490807, -0.092754), (-0.07681, 0.052586, -0.995658)-2.01457, 113.587151, 51.1674
15given(-0.998466, -0.052271, 0.01825), (-0.052119, 0.998603, 0.008702), (-0.018679, 0.007737, -0.999796)97.086327, 53.353619, 29.14953
16given(-0.573948, -0.818754, -0.014998), (0.818794, -0.574066, 0.004876), (-0.012602, -0.009482, 0.999876)188.623276, 115.670639, -21.13847
17given(-0.996819, -0.079039, 0.010192), (-0.079647, 0.992431, -0.093477), (-0.002726, -0.093991, -0.995569)194.649643, 14.02297, 39.7654
18given(-0.480748, 0.876794, -0.010669), (-0.873173, -0.477577, 0.097414), (0.080317, 0.056148, 0.995187)-2.22743, 209.648849, -55.62812

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Components

#1: Protein
Suppressor of cytokine signaling 2 / SOCS-2 / Cytokine-inducible SH2 protein 2 / CIS-2 / STAT-induced STAT inhibitor 2 / SSI-2


Mass: 19377.250 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SOCS2, CIS2, SSI2, STATI2 / Plasmid: pLIC / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O14508
#2: Protein
Transcription elongation factor B polypeptide 2 / Elongin 18 kDa subunit / Elongin-B / EloB / RNA polymerase II transcription factor SIII subunit B / SIII p18


Mass: 11852.389 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TCEB2 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15370
#3: Protein
Transcription elongation factor B polypeptide 1 / Elongin 15 kDa subunit / Elongin-C / EloC / RNA polymerase II transcription factor SIII subunit C / SIII p15


Mass: 10974.616 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TCEB1 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15369
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 33 / 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: 2.58 Å3/Da / Density % sol: 52.31 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.2 / Details: PEG 3350, CaOAc, Sodium cacodylate, Glycerol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1.0432, 0.9537
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jan 31, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
11.04321
20.95371
ReflectionRedundancy: 119.8 % / Number: 5659871 / Rsym value: 0.12 / D res high: 3.1 Å / D res low: 160.97 Å / Num. obs: 47227 / % possible obs: 100
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)IDRmerge(I) obsRsym valueRedundancy
9.854.5310.0450.045128.7
6.939.810.050.05131.7
5.666.9310.1110.111131.6
4.95.6610.1090.109131.5
4.384.910.0920.092129.8
44.3810.1110.111123.5
3.71410.1710.171117.3
3.473.7110.2650.265113.1
3.273.4710.4370.437110.2
3.13.2710.7440.744107.8
ReflectionResolution: 2.9→46.3 Å / Num. obs: 56676 / % possible obs: 99.2 % / Redundancy: 3.9 % / Biso Wilson estimate: 59.6 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.067 / Rpim(I) all: 0.039 / Rrim(I) all: 0.124 / Net I/av σ(I): 5.176 / Net I/σ(I): 15.6 / Num. measured all: 219197 / Scaling rejects: 1
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) allNet I/σ(I) obs% possible all
2.9-2.983.90.6222.31734044490.6730.36120.9100
12.64-46.33.70.02244.223376350.9990.013107.792.6

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassification
Aimless0.3.11data scaling
SOLVEphasing
RESOLVEmodel building
REFMAC5.8.0073refinement
PDB_EXTRACT3.15data extraction
XDSdata reduction
RefinementMethod to determine structure: SAD / Resolution: 2.9→46.3 Å / Cor.coef. Fo:Fc: 0.909 / Cor.coef. Fo:Fc free: 0.867 / WRfactor Rfree: 0.269 / WRfactor Rwork: 0.216 / FOM work R set: 0.7581 / SU B: 50.951 / SU ML: 0.423 / SU R Cruickshank DPI: 0.4467 / SU Rfree: 0.4473 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.447 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2872 2862 5 %RANDOM
Rwork0.2288 ---
obs0.2317 53812 99.15 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 172.18 Å2 / Biso mean: 77.311 Å2 / Biso min: 33.97 Å2
Baniso -1Baniso -2Baniso -3
1-2.05 Å21.02 Å20 Å2
2--2.05 Å20 Å2
3----6.65 Å2
Refinement stepCycle: final / Resolution: 2.9→46.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14871 0 0 33 14904
Biso mean---55.1 -
Num. residues----1994
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01915180
X-RAY DIFFRACTIONr_bond_other_d0.0010.0214103
X-RAY DIFFRACTIONr_angle_refined_deg1.0141.97920696
X-RAY DIFFRACTIONr_angle_other_deg0.712332258
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4551957
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.58923.574526
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.005152276
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.2381557
X-RAY DIFFRACTIONr_chiral_restr0.0520.22493
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02116933
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023258
X-RAY DIFFRACTIONr_mcbond_it4.0664.587939
X-RAY DIFFRACTIONr_mcbond_other4.0664.587938
X-RAY DIFFRACTIONr_mcangle_it6.4917.7049859
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A2169MEDIUM POSITIONAL0.410.5
12D2169MEDIUM POSITIONAL0.460.5
13G2169MEDIUM POSITIONAL0.490.5
14J2169MEDIUM POSITIONAL0.440.5
15M2169MEDIUM POSITIONAL0.490.5
16P2169MEDIUM POSITIONAL0.490.5
11A2169MEDIUM THERMAL8.082
12D2169MEDIUM THERMAL19.162
13G2169MEDIUM THERMAL10.022
14J2169MEDIUM THERMAL13.942
15M2169MEDIUM THERMAL8.42
16P2169MEDIUM THERMAL9.952
21B757MEDIUM POSITIONAL0.270.5
22E757MEDIUM POSITIONAL0.270.5
23H757MEDIUM POSITIONAL0.220.5
24K757MEDIUM POSITIONAL0.230.5
25N757MEDIUM POSITIONAL0.320.5
26Q757MEDIUM POSITIONAL0.30.5
21B757MEDIUM THERMAL11.062
22E757MEDIUM THERMAL11.812
23H757MEDIUM THERMAL14.942
24K757MEDIUM THERMAL10.092
25N757MEDIUM THERMAL12.52
26Q757MEDIUM THERMAL13.332
31C1008MEDIUM POSITIONAL0.310.5
32F1008MEDIUM POSITIONAL0.380.5
33I1008MEDIUM POSITIONAL0.30.5
34L1008MEDIUM POSITIONAL0.30.5
35O1008MEDIUM POSITIONAL0.380.5
36R1008MEDIUM POSITIONAL0.460.5
31C1008MEDIUM THERMAL9.312
32F1008MEDIUM THERMAL18.822
33I1008MEDIUM THERMAL13.442
34L1008MEDIUM THERMAL9.692
35O1008MEDIUM THERMAL10.132
36R1008MEDIUM THERMAL12.532
LS refinement shellResolution: 2.9→2.975 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.414 203 -
Rwork0.335 4013 -
all-4216 -
obs--99.67 %
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)
10.2407-0.20420.80410.8847-0.07823.2739-0.0041-0.03660.0090.2105-0.05060.14710.1891-0.3360.05470.34740.10.06520.5469-0.06390.716780.1336142.62576.0033
20.6360.0770.90792.59362.00252.79980.6725-0.0378-0.2852-0.0663-0.20610.11730.7673-0.075-0.46641.0449-0.0641-0.28950.27440.01030.799877.9184107.3378-10.0738
33.5893-3.13152.70614.5792-1.59342.42650.36050.1904-0.0931-0.1556-0.10270.11270.3860.1911-0.25780.7248-0.0204-0.12310.2544-0.07970.580583.8746116.0523.2982
41.1602-0.94940.4771.8652-2.17963.17240.00840.289-0.2242-0.22530.02370.14420.3302-0.4218-0.03210.06570.0509-0.03550.6036-0.41050.804969.364654.097444.1047
52.23040.2191-2.22962.3504-0.82083.965-0.1117-0.0378-0.03450.39140.24390.1655-0.2339-0.1209-0.13210.20170.26990.13160.6649-0.05930.643337.581770.256264.0375
62.6588-2.1693-1.04763.7156-0.06591.01110.1550.5412-0.20330.08990.07660.2212-0.1531-0.3636-0.23160.07590.20370.02630.7369-0.04120.580647.467171.16147.651
70.10170.17380.42521.8169-0.12252.4468-0.01580.0207-0.0079-0.16640.0333-0.1910.1630.2833-0.01750.16810.12790.09790.2285-0.00810.797512.483689.913323.8164
80.8106-1.36070.53543.8362-1.16644.7870.1598-0.1336-0.16650.36-0.27560.07980.30530.36390.11580.6534-0.05870.06140.27760.12520.761516.948754.699539.9493
92.0137-0.26051.24463.57250.82912.76220.1642-0.007-0.2344-0.1539-0.03770.13330.477-0.0095-0.12650.45670.18590.02090.09990.02860.56729.577462.657226.046
101.6342-0.8059-1.97880.76660.36263.4725-0.1962-0.14470.17230.27210.0131-0.2554-0.21670.17550.18310.48620.2069-0.44760.1418-0.19520.930684.386372.737828.2621
113.3567-1.61050.95561.7645-1.52141.4203-0.00240.3485-0.06990.14190.0304-0.0238-0.1515-0.1346-0.0280.34440.3233-0.25560.391-0.09130.695855.950495.620812.2414
122.4138-0.00990.26863.3482-1.24090.8841-0.1622-0.2467-0.12730.45940.47530.1718-0.0884-0.368-0.31310.53370.3187-0.27640.3395-0.02670.691560.135885.06826.0614
130.77430.98631.28191.32071.57332.2536-0.06720.0454-0.0942-0.06360.1582-0.2424-0.02230.1023-0.0910.34950.3110.12290.4553-0.02350.8256104.1946139.858121.1418
140.6769-0.74052.19941.1977-2.22347.94470.20960.06350.11620.1846-0.1496-0.58830.1236-0.2375-0.061.21650.2289-0.11230.39480.14870.805110.0841109.497439.7255
152.63343.74430.19137.42980.1731.81070.3817-0.3125-0.29440.3579-0.132-0.10750.61150.0262-0.24970.74710.3012-0.13440.35870.04590.5419102.4063112.419524.3992
161.32110.69450.47340.69271.04152.27280.10830.0222-0.12260.09210.0483-0.06230.21710.1881-0.15660.0690.0088-0.04720.34610.09050.762223.5339106.961853.4047
172.46490.2268-0.230.4181-0.83713.3238-0.2504-0.1454-0.0852-0.32260.1745-0.175-0.00310.49270.07590.5899-0.29880.20310.9191-0.06760.797654.7734121.028534.2444
183.11771.7832-0.09831.3465-0.7172.9943-0.08370.0090.0265-0.09680.2234-0.032-0.35390.438-0.13970.1419-0.22660.10180.7327-0.01840.616645.7434123.611549.5665
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A31 - 2054
2X-RAY DIFFRACTION2B2 - 104
3X-RAY DIFFRACTION3C17 - 112
4X-RAY DIFFRACTION4D32 - 2054
5X-RAY DIFFRACTION5E2 - 98
6X-RAY DIFFRACTION6F17 - 2021
7X-RAY DIFFRACTION7G31 - 2054
8X-RAY DIFFRACTION8H1 - 103
9X-RAY DIFFRACTION9I17 - 2019
10X-RAY DIFFRACTION10J32 - 2054
11X-RAY DIFFRACTION11K2 - 103
12X-RAY DIFFRACTION12L16 - 112
13X-RAY DIFFRACTION13M32 - 2054
14X-RAY DIFFRACTION14N2 - 104
15X-RAY DIFFRACTION15O17 - 112
16X-RAY DIFFRACTION16P32 - 2054
17X-RAY DIFFRACTION17Q2 - 103
18X-RAY DIFFRACTION18R17 - 2021

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