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- PDB-5eya: TRIM25 RING domain in complex with Ubc13-Ub conjugate -

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Basic information

Entry
Database: PDB / ID: 5eya
TitleTRIM25 RING domain in complex with Ubc13-Ub conjugate
Components
  • Polyubiquitin-B
  • Tripartite motif-containing 25 variant
  • Ubiquitin-conjugating enzyme E2 N
KeywordsSIGNALING PROTEIN/Transferase / Complex / E3 ligase / ubiquitination / SIGNALING PROTEIN-Transferase complex
Function / homology
Function and homology information


: / RIG-I binding / regulation of viral entry into host cell / UBC13-MMS2 complex / ubiquitin conjugating enzyme complex / suppression of viral release by host / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / host-mediated suppression of symbiont invasion / DNA double-strand break processing ...: / RIG-I binding / regulation of viral entry into host cell / UBC13-MMS2 complex / ubiquitin conjugating enzyme complex / suppression of viral release by host / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / host-mediated suppression of symbiont invasion / DNA double-strand break processing / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / response to vitamin D / Modulation of host responses by IFN-stimulated genes / postreplication repair / symbiont entry into host cell via disruption of host cell glycocalyx / TRAF6 mediated IRF7 activation / E2 ubiquitin-conjugating enzyme / positive regulation of double-strand break repair / symbiont entry into host cell via disruption of host cell envelope / cytoplasmic pattern recognition receptor signaling pathway / virus tail / ligase activity / RSV-host interactions / ubiquitin conjugating enzyme activity / TRAF6 mediated NF-kB activation / positive regulation of intracellular signal transduction / viral release from host cell / protein K63-linked ubiquitination / protein monoubiquitination / ubiquitin ligase complex / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / protein K48-linked ubiquitination / regulation of DNA repair / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / positive regulation of DNA-binding transcription factor activity / TICAM1, RIP1-mediated IKK complex recruitment / negative regulation of TORC1 signaling / ERAD pathway / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / IKK complex recruitment mediated by RIP1 / PINK1-PRKN Mediated Mitophagy / antiviral innate immune response / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / positive regulation of DNA repair / cellular response to leukemia inhibitory factor / Termination of translesion DNA synthesis / ubiquitin binding / double-strand break repair via homologous recombination / NOD1/2 Signaling Pathway / TAK1-dependent IKK and NF-kappa-B activation / DDX58/IFIH1-mediated induction of interferon-alpha/beta / Nonhomologous End-Joining (NHEJ) / Evasion by RSV of host interferon responses / ISG15 antiviral mechanism / CLEC7A (Dectin-1) signaling / Formation of Incision Complex in GG-NER / G2/M DNA damage checkpoint / positive regulation of NF-kappaB transcription factor activity / FCERI mediated NF-kB activation / PKR-mediated signaling / RING-type E3 ubiquitin transferase / Interleukin-1 signaling / Aggrephagy / SARS-CoV-1 activates/modulates innate immune responses / response to estrogen / Ovarian tumor domain proteases / protein polyubiquitination / cytoplasmic stress granule / Interferon gamma signaling / ubiquitin-protein transferase activity / Downstream TCR signaling / Antigen processing: Ubiquitination & Proteasome degradation / ubiquitin protein ligase activity / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / T cell receptor signaling pathway / Processing of DNA double-strand break ends / regulation of protein localization / TRAF3-dependent IRF activation pathway / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / response to oxidative stress / transcription coactivator activity / positive regulation of canonical NF-kappaB signal transduction / protein ubiquitination / nuclear body / cadherin binding / innate immune response / ubiquitin protein ligase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein-containing complex / RNA binding / extracellular exosome / zinc ion binding / nucleoplasm / ATP binding / nucleus / cytosol
Similarity search - Function
TRIM25, PRY/SPRY domain / : / zinc finger of C3HC4-type, RING / Zinc finger, RING-type, eukaryotic / RING-type zinc-finger / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / Pectate lyase superfamily protein ...TRIM25, PRY/SPRY domain / : / zinc finger of C3HC4-type, RING / Zinc finger, RING-type, eukaryotic / RING-type zinc-finger / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / Pectate lyase superfamily protein / Rhamnogalacturonase A/epimerase, pectate lyase-like / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Zinc/RING finger domain, C3HC4 (zinc finger) / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Herpes Virus-1 / Ubiquitin-conjugating enzyme/RWD-like / Pectin lyase fold / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / Pectin lyase fold/virulence factor / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin family / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Tail fiber / Ubiquitin-conjugating enzyme E2 N / E3 ubiquitin/ISG15 ligase TRIM25 / RING-type E3 ubiquitin transferase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.4 Å
AuthorsPornillos, O. / Sanchez, J.G.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM112508 United States
CitationJournal: Cell Rep / Year: 2016
Title: Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway.
Authors: Sanchez, J.G. / Chiang, J.J. / Sparrer, K.M. / Alam, S.L. / Chi, M. / Roganowicz, M.D. / Sankaran, B. / Gack, M.U. / Pornillos, O.
History
DepositionNov 24, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 17, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 9, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 N
F: Tripartite motif-containing 25 variant
G: Tripartite motif-containing 25 variant
B: Ubiquitin-conjugating enzyme E2 N
C: Polyubiquitin-B
D: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,79310
Polymers70,5316
Non-polymers2624
Water3,243180
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)53.047, 75.779, 169.101
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B
12chain C
22chain D
13chain F
23chain G

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYASNASNchain AAA3 - 1513 - 151
21GLYGLYASNASNchain BBD3 - 1513 - 151
12METMETGLYGLYchain CCE1 - 761 - 76
22METMETGLYGLYchain DDF1 - 761 - 76
13ZNZNZNZNchain FFG - H101 - 102
23ZNZNZNZNchain GGI - J101 - 102

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Ubiquitin-conjugating enzyme E2 N / Bendless-like ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme N / Ubc13 / UbcH13 / ...Bendless-like ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme N / Ubc13 / UbcH13 / Ubiquitin carrier protein N / Ubiquitin-protein ligase N


Mass: 17183.807 Da / Num. of mol.: 2 / Mutation: C87K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2N, BLU / Production host: Escherichia coli (E. coli)
References: UniProt: P61088, E2 ubiquitin-conjugating enzyme
#2: Protein Tripartite motif-containing 25 variant


Mass: 9504.903 Da / Num. of mol.: 2 / Fragment: UNP residues 12-97
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q59GW5, UniProt: Q14258*PLUS
#3: Protein Polyubiquitin-B


Mass: 8576.831 Da / Num. of mol.: 2 / Fragment: UNP residues 1-76
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG47
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 180 / 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: 2.41 Å3/Da / Density % sol: 48.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.2 M Li citrate, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.97 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 23, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. obs: 27181 / % possible obs: 98.2 % / Redundancy: 8.1 % / Rmerge(I) obs: 0.179 / Rpim(I) all: 0.066 / Rrim(I) all: 0.191 / Χ2: 0.736 / Net I/av σ(I): 9.625 / Net I/σ(I): 3.9 / Num. measured all: 220683
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.4-2.494.80.74323380.7240.3310.8210.45586.4
2.49-2.596.40.7426000.7550.3060.8050.47195.8
2.59-2.77.90.70527250.8580.2650.7550.48499.9
2.7-2.858.90.57527150.9140.2050.6110.525100
2.85-3.0290.41327340.9560.1460.4380.565100
3.02-3.2690.26627370.9850.0940.2820.648100
3.26-3.588.90.17827730.9930.0630.1890.777100
3.58-4.18.80.1327770.9950.0460.1381.148100
4.1-5.178.70.11928030.9920.0430.1270.97100
5.17-508.20.06629790.9990.0240.071.024100

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIXrefinement
PDB_EXTRACT3.15data extraction
HKL-2000data reduction
PHENIXphasing
RefinementResolution: 2.4→28.966 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 0.16 / Phase error: 24.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2275 1786 7.25 %
Rwork0.1891 22836 -
obs0.1919 24622 89.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 157.93 Å2 / Biso mean: 46.0471 Å2 / Biso min: 13.43 Å2
Refinement stepCycle: final / Resolution: 2.4→28.966 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4826 0 4 180 5010
Biso mean--26.67 37.82 -
Num. residues----612
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0064957
X-RAY DIFFRACTIONf_angle_d1.0986733
X-RAY DIFFRACTIONf_chiral_restr0.041757
X-RAY DIFFRACTIONf_plane_restr0.005878
X-RAY DIFFRACTIONf_dihedral_angle_d14.7661887
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1740X-RAY DIFFRACTION8.074TORSIONAL
12B1740X-RAY DIFFRACTION8.074TORSIONAL
21C902X-RAY DIFFRACTION8.074TORSIONAL
22D902X-RAY DIFFRACTION8.074TORSIONAL
31F856X-RAY DIFFRACTION8.074TORSIONAL
32G856X-RAY DIFFRACTION8.074TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 13

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.46490.3916980.28681261135966
2.4649-2.53740.27741160.25911473158976
2.5374-2.61920.26311230.23871585170883
2.6192-2.71270.26941320.23461686181887
2.7127-2.82130.27131340.2281713184789
2.8213-2.94960.27261390.2341784192392
2.9496-3.10490.28051420.21081799194193
3.1049-3.29920.25331420.21121823196594
3.2992-3.55350.23591470.20171870201796
3.5535-3.91030.23441470.17811899204697
3.9103-4.47440.18011530.14161950210398
4.4744-5.63040.17561520.14461935208797
5.6304-28.96850.18431610.16452058221997
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)
11.23940.27510.561.17020.43181.28260.0238-0.0522-0.6344-0.26680.0228-0.52280.5233-0.5701-0.02270.6622-0.5349-0.11540.1939-0.5398-0.2997-25.1007-11.242-15.6566
25.8962-0.7183-2.32581.70870.28661.3448-0.1455-0.37-0.71990.4969-0.0369-0.03520.80460.23560.03590.57990.0105-0.01370.36240.04230.3436-15.7739-11.9078-8.6204
33.21340.99790.28191.1776-0.05591.3672-0.38020.5116-0.32460.04130.2571-0.08740.4508-0.03120.07140.34940.0112-0.02340.3001-0.02520.1958-9.8921-4.1775-6.6646
43.24583.02230.9297.0249-1.76462.48570.391-0.36970.4776-0.0285-0.07560.3523-0.2447-1.2342-0.20010.3887-0.05050.02250.4389-0.05320.1905-26.3841.7104-13.973
53.1860.73291.25071.27650.1162.37170.0257-0.30520.3552-0.0216-0.08180.0643-0.08480.26820.10960.261-0.0135-0.01640.2654-0.05370.2596-12.36036.0226-9.6658
62.39660.12870.05351.82730.322.4171-0.21790.0350.2535-0.01370.1821-0.1790.15391.0626-0.0150.3107-0.0727-0.10830.29250.02220.1905-7.0174.3364-13.7274
73.8496-0.1298-1.13394.1144-1.74174.8180.0354-0.26960.86360.32890.3002-0.1415-0.4620.6576-0.09190.2486-0.0474-0.03640.5388-00.32563.51346.3811-2.9195
83.77121.8594-2.49513.86490.48744.96290.333-0.39870.03280.7563-0.1875-0.11750.43280.13810.04460.5251-0.00850.06850.2017-0.02730.397-21.3296-14.2552-32.3856
91.6394-0.85150.93171.969-0.32841.96270.00150.0557-0.18080.43650.0377-0.0182-0.0187-0.05610.06830.2588-0.0232-0.03560.1613-0.03410.2136-27.3211-4.0284-31.4164
104.4390.7831-0.12543.4186-1.07573.46820.13390.01520.69650.651-0.0638-0.0694-0.0063-0.1203-0.07620.24050.0072-0.02840.1215-0.02580.2446-29.94313.1791-27.7136
112.63771.02871.21022.78970.03661.6844-0.07410.21190.35160.18620.0208-0.0493-0.11640.20280.13980.2142-0.0306-0.02050.15080.00270.184-25.49068.4828-32.0363
123.4809-0.85610.80773.77170.0223.9718-0.4567-0.3808-0.3428-0.15750.66190.02440.5405-0.6014-0.25050.2482-0.0227-0.02520.24050.02560.2658-32.8511-14.8656-37.2126
130.69070.35830.42951.5107-0.41640.46310.01820.11280.00290.0523-0.1635-0.01590.19490.17910.0810.27280.0387-0.0510.13640.00820.2402-25.3718-10.6232-48.1396
142.26770.4545-0.65183.432-1.30261.06370.5211-0.1880.3112-0.0736-0.1477-0.3373-0.5178-0.02470.04670.29880.00260.03810.0614-0.00760.2362-22.83252.5093-53.6208
152.97740.8296-0.2816.3267-5.63875.10240.31690.6492-0.1404-1.5191-0.1259-0.4031.1444-0.00990.46780.81540.017-0.00430.2930.07740.3305-27.237413.1204-55.0199
162.50220.1168-0.78761.4087-0.09771.7264-0.13280.1931-0.2404-0.3070.16390.0656-0.0024-0.3396-0.25430.19820.0028-0.080.16020.05040.1941-32.92977.1898-50.8113
175.3018-4.68962.85244.6898-3.39142.9134-0.2199-0.24180.7470.3714-0.0617-0.96130.24970.0976-0.05560.25090.0374-0.03560.2134-0.04660.213-20.62575.879-44.416
180.3817-0.7603-0.67195.27823.05493.0838-0.0816-0.05970.03040.4107-0.1445-0.89720.39650.41330.0880.26960.0474-0.03840.15940.04660.2333-19.1185-12.6513-42.3179
191.3741-2.10161.32196.1451-0.37692.15640.35860.0374-0.1044-0.8311-0.153-1.10690.38790.472-0.05290.7610.0346-0.14120.4326-0.06970.9046-13.2966-27.595-42.7984
204.56861.1487-0.85345.29330.4273.02530.5593-0.1748-0.7329-0.23760.13110.06320.36350.1764-0.22820.47690.1759-0.10870.38570.05840.2666-27.7847-12.9514-64.8463
216.3221-0.39-2.99482.08370.54783.0050.14210.4556-0.2221-0.33280.0855-0.05320.8210.198-0.22670.47410.0396-0.13830.3565-0.06390.3853-37.329-13.8731-71.7737
224.5198-0.69391.43882.1855-0.20481.94490.1994-0.1617-0.11110.16240.02210.09090.10490.1739-0.19480.2911-0.0146-0.03320.22340.04730.1729-43.1126-6.3425-74.0606
230.756-1.36770.7016.22943.46258.1974-0.30540.1457-0.041-0.58420.6646-0.1951-0.5841.0568-0.3020.1891-0.03350.0260.2567-0.01170.2395-26.5327-0.1885-67.1161
242.3087-0.19141.49641.6469-0.36472.1276-0.20720.19770.30820.0413-0.09380.0468-0.0771-0.19390.22280.18860.0244-0.00770.26630.01990.2024-40.67294.0182-71.4059
252.2232-0.28981.54172.3185-0.14481.0221-0.1239-0.55420.46580.3907-0.07760.2563-0.156-1.06020.12360.31390.1422-0.00250.5201-0.08710.3339-49.41486.0275-69.786
262.2869-0.431-0.24913.70580.95993.42530.08150.4236-0.1571-0.3492-0.07680.73070.1586-0.8619-0.12110.26470.0142-0.07480.60330.06260.2526-56.9979-0.8707-79.758
272.5166-0.742-0.22421.73910.94980.78730.0197-0.828-0.85120.4268-0.23990.22020.6895-0.2254-0.30470.4168-0.1546-0.14440.32820.07520.1472-43.034-13.1945-50.2718
280.21290.0502-0.05560.0126-0.01330.0127-0.0432-0.05180.09420.1733-0.05960.37870.0037-0.2351-0.13610.1198-0.36190.06160.93430.14740.5839-56.503-9.9688-45.3713
295.0212.45632.47552.40390.88312.9340.066-0.1202-0.25290.5786-0.2030.1198-0.026-0.64940.04360.2992-0.12060.02470.4396-0.00810.2395-46.0448-4.4769-45.4953
306.48170.8531.85680.5302-0.3681.49830.2013-0.19361.27360.18480.32030.34050.0205-0.6780.46330.2331-0.0046-0.15290.2712-0.02460.3217-44.21270.4526-51.8195
312.362-1.343-3.244.3542.87424.76410.432-0.47690.6171-0.3442-0.290.3998-0.5558-0.4566-0.03560.2696-0.0255-0.07330.7644-0.0550.529-54.1014-3.726-57.315
323.15820.9536-0.93362.1221-0.48582.40230.1952-0.04150.00210.10810.04640.70390.2834-0.8052-0.21020.2768-0.0905-0.0490.4677-0.02530.2461-50.4668-7.1051-55.9751
331.9167-0.6712-0.35891.1535-0.21090.7386-0.11210.5-0.4662-0.2235-0.0964-0.07180.3870.20520.00740.37420.0627-0.05120.35-0.01570.282-5.6298-11.2108-31.1325
346.9357-0.39911.85443.0903-0.96494.731-0.01140.68130.2617-0.5209-0.4317-0.16130.13830.69710.42390.39150.1347-0.01810.36890.02060.2679-6.5176-3.5537-35.1472
352.21240.0325-0.39010.54980.29311.4680.26660.20670.3651-0.1239-0.28-0.14060.09211.24990.10190.27360.106-0.09070.56050.04150.345-0.858-4.1838-26.2518
361.9798-0.4267-0.39651.46951.74693.10520.07180.05920.0061-0.1283-0.0527-0.0351-0.07450.635-0.05550.29150.0121-0.0570.22920.05170.2401-8.54541.1606-22.1886
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 17 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 18 through 30 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 31 through 57 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 58 through 67 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 68 through 100 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 101 through 122 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 123 through 151 )A0
8X-RAY DIFFRACTION8chain 'F' and (resid 6 through 10 )F0
9X-RAY DIFFRACTION9chain 'F' and (resid 11 through 30 )F0
10X-RAY DIFFRACTION10chain 'F' and (resid 31 through 43 )F0
11X-RAY DIFFRACTION11chain 'F' and (resid 44 through 66 )F0
12X-RAY DIFFRACTION12chain 'F' and (resid 67 through 81 )F0
13X-RAY DIFFRACTION13chain 'G' and (resid -2 through 30 )G0
14X-RAY DIFFRACTION14chain 'G' and (resid 31 through 43 )G0
15X-RAY DIFFRACTION15chain 'G' and (resid 44 through 48 )G0
16X-RAY DIFFRACTION16chain 'G' and (resid 49 through 58 )G0
17X-RAY DIFFRACTION17chain 'G' and (resid 59 through 66 )G0
18X-RAY DIFFRACTION18chain 'G' and (resid 67 through 78 )G0
19X-RAY DIFFRACTION19chain 'G' and (resid 79 through 83 )G0
20X-RAY DIFFRACTION20chain 'B' and (resid 3 through 17 )B0
21X-RAY DIFFRACTION21chain 'B' and (resid 18 through 30 )B0
22X-RAY DIFFRACTION22chain 'B' and (resid 31 through 57 )B0
23X-RAY DIFFRACTION23chain 'B' and (resid 58 through 67 )B0
24X-RAY DIFFRACTION24chain 'B' and (resid 68 through 100 )B0
25X-RAY DIFFRACTION25chain 'B' and (resid 101 through 132 )B0
26X-RAY DIFFRACTION26chain 'B' and (resid 133 through 151 )B0
27X-RAY DIFFRACTION27chain 'C' and (resid 1 through 16 )C0
28X-RAY DIFFRACTION28chain 'C' and (resid 17 through 22 )C0
29X-RAY DIFFRACTION29chain 'C' and (resid 23 through 34 )C0
30X-RAY DIFFRACTION30chain 'C' and (resid 35 through 44 )C0
31X-RAY DIFFRACTION31chain 'C' and (resid 45 through 54 )C0
32X-RAY DIFFRACTION32chain 'C' and (resid 55 through 76 )C0
33X-RAY DIFFRACTION33chain 'D' and (resid 1 through 22 )D0
34X-RAY DIFFRACTION34chain 'D' and (resid 23 through 34 )D0
35X-RAY DIFFRACTION35chain 'D' and (resid 35 through 65 )D0
36X-RAY DIFFRACTION36chain 'D' and (resid 66 through 76 )D0

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