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- PDB-3u5m: Crystal structure of TRIM33 PHD-Bromo in the free state -

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Basic information

Entry
Database: PDB / ID: 3u5m
TitleCrystal structure of TRIM33 PHD-Bromo in the free state
ComponentsE3 ubiquitin-protein ligase TRIM33
KeywordsTRANSCRIPTION / TRIM33 / PHD / Bromodomain / TGF-beta / epigenetics / histone
Function / homology
Function and homology information


co-SMAD binding / regulation of transforming growth factor beta receptor signaling pathway / Germ layer formation at gastrulation / R-SMAD binding / negative regulation of BMP signaling pathway / Downregulation of SMAD2/3:SMAD4 transcriptional activity / RING-type E3 ubiquitin transferase / ubiquitin-protein transferase activity / protein ubiquitination / negative regulation of DNA-templated transcription ...co-SMAD binding / regulation of transforming growth factor beta receptor signaling pathway / Germ layer formation at gastrulation / R-SMAD binding / negative regulation of BMP signaling pathway / Downregulation of SMAD2/3:SMAD4 transcriptional activity / RING-type E3 ubiquitin transferase / ubiquitin-protein transferase activity / protein ubiquitination / negative regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleoplasm / nucleus
Similarity search - Function
B-box, C-terminal / B-Box C-terminal domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, PHD-type, conserved site / PHD-finger ...B-box, C-terminal / B-Box C-terminal domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, PHD-type, conserved site / PHD-finger / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Zinc finger PHD-type signature. / Ring finger / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Bromodomain-like / Histone Acetyltransferase; Chain A / Zinc finger, FYVE/PHD-type / Zinc finger RING-type profile. / Zinc finger, RING-type / Bromodomain / bromo domain / Bromodomain / Bromodomain (BrD) profile. / Bromodomain-like superfamily / Zinc finger, RING/FYVE/PHD-type / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
E3 ubiquitin-protein ligase TRIM33
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.08 Å
AuthorsWang, Z. / Patel, D.J.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2011
Title: A poised chromatin platform for TGF-beta access to master regulators
Authors: Xi, Q. / Wang, Z. / Zaromytidou, A.I. / Zhang, X.H. / Chow-Tsang, L.F. / Liu, J.X. / Kim, H. / Barlas, A. / Manova-Todorova, K. / Kaartinen, V. / Studer, L. / Mark, W. / Patel, D.J. / Massague, J.
History
DepositionOct 11, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 18, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase TRIM33
B: E3 ubiquitin-protein ligase TRIM33
C: E3 ubiquitin-protein ligase TRIM33
D: E3 ubiquitin-protein ligase TRIM33
E: E3 ubiquitin-protein ligase TRIM33
F: E3 ubiquitin-protein ligase TRIM33
G: E3 ubiquitin-protein ligase TRIM33
H: E3 ubiquitin-protein ligase TRIM33
I: E3 ubiquitin-protein ligase TRIM33
J: E3 ubiquitin-protein ligase TRIM33
K: E3 ubiquitin-protein ligase TRIM33
L: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)288,01448
Polymers285,96312
Non-polymers2,05136
Water00
1
A: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
7
G: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
8
H: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
9
I: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0415
Polymers23,8301
Non-polymers2114
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
10
J: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
11
K: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
12
L: E3 ubiquitin-protein ligase TRIM33
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9613
Polymers23,8301
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)79.527, 79.781, 134.160
Angle α, β, γ (deg.)89.90, 89.96, 59.97
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
E3 ubiquitin-protein ligase TRIM33 / Ectodermin homolog / RET-fused gene 7 protein / Protein Rfg7 / Transcription intermediary factor 1- ...Ectodermin homolog / RET-fused gene 7 protein / Protein Rfg7 / Transcription intermediary factor 1-gamma / TIF1-gamma / Tripartite motif-containing protein 33


Mass: 23830.262 Da / Num. of mol.: 12
Fragment: The C-terminal PHD and Bromo dual domains of TRIM33, UNP residues 882-1087
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRIM33, KIAA1113, RFG7, TIF1G / Plasmid: pRSFDuet-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q9UPN9, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#2: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca

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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: 52.27 %
Crystal growTemperature: 273 K / Method: vapor diffusion, hanging drop
Details: 0.2M CaCl2, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 273K

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Data collection

DiffractionMean temperature: 197 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1.28215 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 18, 2011
RadiationMonochromator: SI mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.28215 Å / Relative weight: 1
ReflectionResolution: 3.08→27.36 Å / Num. obs: 50478 / % possible obs: 96.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 5.8 % / Biso Wilson estimate: 126.2 Å2 / Rsym value: 0.071 / Net I/σ(I): 30.2
Reflection shellResolution: 3.08→3.21 Å / Redundancy: 6 % / Mean I/σ(I) obs: 2.4 / Num. unique all: 5028 / Rsym value: 0.656 / % possible all: 95.7

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.1_743)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3O33

3o33


Resolution: 3.08→27.36 Å / SU ML: 1 / σ(F): 1.96 / Phase error: 33.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2935 1962 3.89 %Random
Rwork0.2074 ---
obs0.2106 50412 95.91 %-
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 84.996 Å2 / ksol: 0.277 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.0086 Å22.2508 Å2-2.502 Å2
2--5.2537 Å22.2831 Å2
3----5.2451 Å2
Refinement stepCycle: LAST / Resolution: 3.08→27.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17081 0 36 0 17117
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00917478
X-RAY DIFFRACTIONf_angle_d1.26323590
X-RAY DIFFRACTIONf_dihedral_angle_d18.0056592
X-RAY DIFFRACTIONf_chiral_restr0.0872567
X-RAY DIFFRACTIONf_plane_restr0.0063010
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0844-3.16140.4397970.37162444X-RAY DIFFRACTION67
3.1614-3.24680.3831320.34273546X-RAY DIFFRACTION98
3.2468-3.34220.37261560.31463526X-RAY DIFFRACTION98
3.3422-3.44980.39151390.28333596X-RAY DIFFRACTION98
3.4498-3.57290.35171310.23483484X-RAY DIFFRACTION98
3.5729-3.71560.24981490.24523569X-RAY DIFFRACTION98
3.7156-3.88430.35461380.18973493X-RAY DIFFRACTION98
3.8843-4.08840.27531440.21113602X-RAY DIFFRACTION99
4.0884-4.34360.24921480.18633519X-RAY DIFFRACTION99
4.3436-4.67750.2521430.17233607X-RAY DIFFRACTION99
4.6775-5.14540.21871590.15473480X-RAY DIFFRACTION99
5.1454-5.88350.4671530.26123583X-RAY DIFFRACTION99
5.8835-7.38830.2591350.20353620X-RAY DIFFRACTION99
7.3883-27.35550.28781380.18833381X-RAY DIFFRACTION94
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)
12.6648-1.5296-1.88644.44892.68274.91250.13680.24131.3262-0.2645-0.2314-0.1649-0.7346-0.49140.05371.39980.19780.0081.54350.11051.541631.454516.7734-19.115
26.27370.1754-1.12994.0529-1.90912.01620.55-1.52280.23870.7127-0.76890.3204-1.11510.67510.33161.55020.02970.10771.0869-0.11691.214944.586812.2317-21.6781
34.5721.6804-2.178.54251.78272.59360.72420.2336-0.4231-0.1065-0.81980.19910.18320.28580.06890.94430.1444-0.0621.3843-0.02641.107837.8862-4.6752-27.3857
43.95182.374-2.18184.5828-2.8534.01530.096-0.0987-0.3526-0.20730.02471.1340.3184-0.2035-0.09381.5655-0.0412-0.11391.25890.02581.46733.344924.3321-63.9664
57.0377-0.20620.15617.03271.61564.3947-1.3308-0.9671-0.32161.15230.141.11380.9298-0.87751.20541.3168-0.21910.16171.38060.1871.20370.64238.3133-66.7933
66.29182.4886-1.46041.8924-1.33783.4599-0.2244-0.2744-0.4248-0.6673-0.1547-0.2851-0.43970.13790.3391.43390.09640.02020.939-0.11751.226918.70140.647-72.284
72.680.4725-2.21464.1753-3.20782.83640.1915-0.41250.5148-0.2544-0.0904-0.2662-0.62930.5667-0.10311.4103-0.11990.02051.453-0.13821.3766-1.14116.575-89.2334
87.4379-2.21270.01745.4982-0.23152.77820.05961.85610.77991.1084-0.59310.1995-0.5169-0.62220.67561.3403-0.33350.19241.19180.17491.2384-14.836411.3453-85.3348
93.8492-0.6024-0.97518.4888-0.98412.93140.269-0.5308-0.6844-0.1797-0.6276-0.43450.2996-0.50610.35360.9179-0.1451-0.08461.1955-0.04331.0629-7.6676-4.762-81.1275
104.89781.5935-4.27893.248-0.26715.1533-0.3361-0.23980.4375-0.2510.0738-0.18150.18590.35220.18381.22440.0797-0.01091.5516-0.0621.380550.53665.6891-66.8458
113.1282-0.91830.53716.7369-0.01931.93470.4495-0.220.7-1.9963-1.0251-0.6413-0.50480.83940.43061.1693-0.1280.22521.4072-0.05831.112740.024114.9284-63.9499
126.12483.0271-1.31495.89340.00492.7033-0.4794-0.486-0.5428-0.35110.17430.1837-0.0302-0.51120.32481.04860.2321-0.03441.10010.06851.146928.7430.6579-58.4471
134.265-0.9954-1.54743.18392.79573.9062-0.3465-0.005-0.12110.22480.3271-0.44070.89740.50.04831.75920.1458-0.08681.3926-0.01441.219727.112424.5433-44.3989
147.26921.8491-1.19783.7744-0.28184.3218-1.0450.07160.54810.47870.8378-0.1901-0.6240.63490.16621.22510.3164-0.06711.0183-0.19241.134629.178938.9796-40.1247
158.6584-2.9123-1.54444.30612.84473.05-0.2510.33910.07670.5929-0.09950.7811-0.21-0.06780.31081.28-0.14310.05130.9014-0.02181.002711.813540.9057-36.0503
163.51670.21053.42531.96011.04574.2215-0.144-0.2988-0.45290.02240.17820.43880.0517-0.32950.00041.32720.04980.08691.68070.10471.345819.7381-3.89370.0749
176.27320.75680.84137.39450.87034.497-0.1211-0.28680.0139-1.3377-0.18810.33731.1586-0.93060.19971.3569-0.1602-0.14461.33640.19071.112930.2412-13.15672.6752
184.65643.14731.99825.2606-0.14872.7381-0.3491-0.31780.34430.04630.3175-0.49550.27680.55590.00051.19810.24340.081.2147-0.08381.189941.2911.28158.5786
193.14421.64192.40193.80621.86553.12350.0816-0.5738-0.3980.0488-0.3768-0.00610.8750.00460.18121.561-0.027-0.11951.55250.08031.3162-8.36-14.8392-22.0569
209.2709-4.5115-0.23817.4131.62853.38580.73362.3906-0.58960.307-1.5844-0.32430.3329-0.16760.90241.6053-0.075-0.31471.2758-0.09891.27214.8953-10.3135-19.6742
213.1709-2.10410.61487.40992.50891.96820.4017-0.18210.3532-0.231-0.62210.5063-0.34520.38480.23261.0323-0.01510.04311.4620.02691.1855-2.036.6288-13.6557
223.0205-1.43980.83852.5692-3.12133.596-0.3239-0.34260.38241.04530.01990.6535-0.2248-0.37770.29671.7364-0.00940.12511.337-0.02921.36123.411346.0026-111.7124
235.7738-0.8147-0.44964.1250.95111.785-1.10360.98270.6635-0.34160.72220.7340.0292-0.9030.18371.4143-0.0348-0.02711.32930.40551.27150.590732.2949-109.1509
249.3164-1.40311.91333.0761-1.97814.715-0.23910.4128-0.19080.5786-0.1102-0.73390.60840.1570.2671.378-0.0854-0.06310.957-0.07361.251918.641729.7804-103.4226
254.85490.46753.25432.54570.38994.411-0.46630.6519-0.7851-0.35750.8817-0.72790.36430.4212-0.30351.4929-0.04410.07551.6009-0.16951.439310.2695-4.2144-108.5211
263.3558-1.75420.6667.6083-0.9583.67-0.021.3644-0.52730.8989-0.7807-1.37950.1445-0.34221.01510.82520.0633-0.0881.4241-0.05281.3126-1.281-13.3031-112.7062
275.6798-4.12392.99917.0714-1.54784.5156-0.61910.3120.6309-0.02930.50270.1429-0.0953-0.32920.08471.0908-0.2171-0.041.31070.0781.165-11.31690.9367-116.9255
283.9938-0.3323-3.40974.5219-0.37734.8448-0.00010.18380.33340.41220.36620.7930.1445-0.5724-0.4431.2722-0.10290.03361.6045-0.03371.3138-20.1415.751-41.557
292.80860.7902-0.68117.92020.26853.7060.61270.54561.10811.2655-0.67560.9864-0.6729-0.46610.22970.8909-0.02130.21551.52180.16541.403-8.429214.8548-45.5184
306.473-3.0897-1.89144.9920.28392.7768-0.70380.6382-0.74460.20.3659-0.1557-0.13690.37260.32971.283-0.25910.10251.2157-0.08651.23031.70060.5756-49.8009
312.7967-1.15491.19674.6505-2.83253.21420.62130.3264-0.89220.0668-0.59030.6967-0.1053-0.0875-0.0641.47710.15750.00641.2578-0.08421.390938.4688-15.1708-86.3407
324.74440.8495-0.46045.2014-1.3411.83010.249-1.535-1.6094-0.65-0.71050.01980.1368-0.10250.47441.47310.1234-0.05461.20540.23911.374224.6236-9.8713-90.2611
332.78062.00431.23388.4006-2.46283.40460.27080.37050.33270.1158-0.5905-0.4195-0.3778-0.3470.28080.94210.10550.10221.31240.03071.179831.98246.2281-94.7305
343.84590.46651.5235.52242.91333.6416-0.2892-0.04750.412-0.79960.6146-1.2234-0.31380.2189-0.42641.3395-0.09360.18191.3662-0.01721.327326.889246.26623.3987
357.0643-1.04781.55864.0774-0.32832.2464-1.0267-0.28690.84511.01620.4741-0.8005-0.35470.63460.60461.3848-0.2432-0.05551.1738-0.271.229129.28331.843-0.5916
368.07032.84551.43952.80042.1913.7719-0.0179-0.3915-0.0019-0.44130.0190.47990.1975-0.2417-0.03141.3060.0867-0.09761.02690.10411.212311.557630.2223-5.0577
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 883:932)
2X-RAY DIFFRACTION2chain 'A' and (resseq 933:975)
3X-RAY DIFFRACTION3chain 'A' and (resseq 976:1087)
4X-RAY DIFFRACTION4chain 'B' and (resseq 883:932)
5X-RAY DIFFRACTION5chain 'B' and (resseq 933:975)
6X-RAY DIFFRACTION6chain 'B' and (resseq 976:1087)
7X-RAY DIFFRACTION7chain 'C' and (resseq 883:932)
8X-RAY DIFFRACTION8chain 'C' and (resseq 933:975)
9X-RAY DIFFRACTION9chain 'C' and (resseq 976:1087)
10X-RAY DIFFRACTION10chain 'D' and (resseq 883:932)
11X-RAY DIFFRACTION11chain 'D' and (resseq 933:975)
12X-RAY DIFFRACTION12chain 'D' and (resseq 976:1087)
13X-RAY DIFFRACTION13chain 'E' and (resseq 883:932)
14X-RAY DIFFRACTION14chain 'E' and (resseq 933:975)
15X-RAY DIFFRACTION15chain 'E' and (resseq 976:1087)
16X-RAY DIFFRACTION16chain 'F' and (resseq 883:932)
17X-RAY DIFFRACTION17chain 'F' and (resseq 933:975)
18X-RAY DIFFRACTION18chain 'F' and (resseq 976:1087)
19X-RAY DIFFRACTION19chain 'G' and (resseq 883:932)
20X-RAY DIFFRACTION20chain 'G' and (resseq 933:975)
21X-RAY DIFFRACTION21chain 'G' and (resseq 976:1087)
22X-RAY DIFFRACTION22chain 'H' and (resseq 883:932)
23X-RAY DIFFRACTION23chain 'H' and (resseq 933:975)
24X-RAY DIFFRACTION24chain 'H' and (resseq 976:1087)
25X-RAY DIFFRACTION25chain 'I' and (resseq 883:932)
26X-RAY DIFFRACTION26chain 'I' and (resseq 933:975)
27X-RAY DIFFRACTION27chain 'I' and (resseq 976:1087)
28X-RAY DIFFRACTION28chain 'J' and (resseq 883:932)
29X-RAY DIFFRACTION29chain 'J' and (resseq 933:975)
30X-RAY DIFFRACTION30chain 'J' and (resseq 976:1087)
31X-RAY DIFFRACTION31chain 'K' and (resseq 883:932)
32X-RAY DIFFRACTION32chain 'K' and (resseq 933:975)
33X-RAY DIFFRACTION33chain 'K' and (resseq 976:1087)
34X-RAY DIFFRACTION34chain 'L' and (resseq 883:932)
35X-RAY DIFFRACTION35chain 'L' and (resseq 933:975)
36X-RAY DIFFRACTION36chain 'L' and (resseq 976:1087)

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