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- PDB-5f6k: Crystal structure of the MLL3-Ash2L-RbBP5 complex -

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Basic information

Entry
Database: PDB / ID: 5f6k
TitleCrystal structure of the MLL3-Ash2L-RbBP5 complex
Components
  • Histone-lysine N-methyltransferase 2C
  • Retinoblastoma-binding protein 5
  • Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2
  • peptide ARTKQTARK
KeywordsTRANSFERASE/PROTEIN BINDING / histone methylation / histone methyltransferase / MLL-family proteins / SET domain / TRANSFERASE-PROTEIN BINDING complex
Function / homology
Function and homology information


[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / histone H3K4 trimethyltransferase activity / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / histone methyltransferase complex / acyltransferase activity / histone methyltransferase activity ...[histone H3]-lysine4 N-methyltransferase / histone H3K4 monomethyltransferase activity / histone H3K4 trimethyltransferase activity / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / histone H3K4 methyltransferase activity / histone methyltransferase complex / acyltransferase activity / histone methyltransferase activity / Formation of WDR5-containing histone-modifying complexes / hemopoiesis / MLL1 complex / nucleosomal DNA binding / response to electrical stimulus / transcription initiation-coupled chromatin remodeling / Deactivation of the beta-catenin transactivating complex / Formation of the beta-catenin:TCF transactivating complex / euchromatin / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / PKMTs methylate histone lysines / beta-catenin binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / response to estrogen / structural constituent of chromatin / nucleosome / Neddylation / histone binding / methylation / positive regulation of cell growth / transcription coactivator activity / transcription cis-regulatory region binding / protein heterodimerization activity / DNA damage response / positive regulation of cell population proliferation / nucleolus / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / nucleoplasm / metal ion binding / nucleus / cytosol
Similarity search - Function
Histone-lysine N-methyltransferase 2C / KMT2C, ePHD1 / KMT2C, ePHD2 / : / : / : / DHHC domain profile. / HMG-I/HMG-Y, DNA-binding, conserved site / HMG-I and HMG-Y DNA-binding domain (A+T-hook). / : ...Histone-lysine N-methyltransferase 2C / KMT2C, ePHD1 / KMT2C, ePHD2 / : / : / : / DHHC domain profile. / HMG-I/HMG-Y, DNA-binding, conserved site / HMG-I and HMG-Y DNA-binding domain (A+T-hook). / : / ASH2, PHD zinc finger / Set1/Ash2 histone methyltransferase complex subunit ASH2-like, WH / Histone methyltransferase complex subunit ASH2 / SPRY domain / Retinoblastoma-binding protein 5/Swd1 / FY-rich, N-terminal / F/Y-rich N-terminus / PHD-like zinc-binding domain / FYR domain FYRN motif profile. / "FY-rich" domain, N-terminal region / FY-rich, C-terminal / F/Y rich C-terminus / FYR domain FYRC motif profile. / "FY-rich" domain, C-terminal region / Beta-clip-like / SET domain / Cysteine-rich motif following a subset of SET domains / Post-SET domain / Post-SET domain profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / PHD-zinc-finger like domain / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / SPRY domain / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain superfamily / SET domain / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. / SET domain profile. / SET domain / PHD-finger / Ring finger / Zinc finger PHD-type signature. / Beta Complex / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Histone H3 signature 1. / Zinc finger, PHD-type / PHD zinc finger / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Zinc finger RING-type profile. / Zinc finger, RING-type / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Zinc finger, FYVE/PHD-type / Histone-fold / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / Jelly Rolls / WD40/YVTN repeat-like-containing domain superfamily / Sandwich / Mainly Beta
Similarity search - Domain/homology
S-ADENOSYL-L-HOMOCYSTEINE / Retinoblastoma-binding protein 5 / Histone H3.3C / Histone-lysine N-methyltransferase 2C / Set1/Ash2 histone methyltransferase complex subunit ASH2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.411 Å
AuthorsLi, Y. / Lei, M. / Chen, Y.
Funding support China, 1items
OrganizationGrant numberCountry
Strategic Priority Research Program of the Chinese Academy of SciencesXDB08010201 China
CitationJournal: Nature / Year: 2016
Title: Structural basis for activity regulation of MLL family methyltransferases.
Authors: Li, Y. / Han, J. / Zhang, Y. / Cao, F. / Liu, Z. / Li, S. / Wu, J. / Hu, C. / Wang, Y. / Shuai, J. / Chen, J. / Cao, L. / Li, D. / Shi, P. / Tian, C. / Zhang, J. / Dou, Y. / Li, G. / Chen, Y. / Lei, M.
History
DepositionDec 6, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 24, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 20, 2016Group: Database references
Revision 1.2Nov 8, 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 / citation / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2
B: Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2
C: Histone-lysine N-methyltransferase 2C
D: Retinoblastoma-binding protein 5
E: Histone-lysine N-methyltransferase 2C
F: Retinoblastoma-binding protein 5
M: peptide ARTKQTARK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)86,55211
Polymers85,6537
Non-polymers9004
Water4,053225
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2
E: Histone-lysine N-methyltransferase 2C
F: Retinoblastoma-binding protein 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,7455
Polymers42,2953
Non-polymers4502
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
B: Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2
C: Histone-lysine N-methyltransferase 2C
D: Retinoblastoma-binding protein 5
M: peptide ARTKQTARK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8086
Polymers43,3584
Non-polymers4502
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)80.342, 236.076, 44.416
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 2 types, 4 molecules ABCE

#1: Protein Set1/Ash2 histone methyltransferase complex subunit ASH2,Set1/Ash2 histone methyltransferase complex subunit ASH2 / ASH2-like protein


Mass: 20597.355 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 380-496, 539-598
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ASH2L, ASH2L1 / Plasmid: pET28b-sumo / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q9UBL3
#2: Protein Histone-lysine N-methyltransferase 2C / Lysine N-methyltransferase 2C / Homologous to ALR protein / Myeloid/lymphoid or mixed-lineage ...Lysine N-methyltransferase 2C / Homologous to ALR protein / Myeloid/lymphoid or mixed-lineage leukemia protein 3


Mass: 18442.082 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 4757-4911
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KMT2C, HALR, KIAA1506, MLL3 / Plasmid: PGEX6P / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta
References: UniProt: Q8NEZ4, histone-lysine N-methyltransferase

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Protein/peptide , 2 types, 3 molecules DFM

#3: Protein/peptide Retinoblastoma-binding protein 5 / RBBP-5 / Retinoblastoma-binding protein RBQ-3


Mass: 3255.321 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 330-356
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBBP5, RBQ3 / Plasmid: pET28b-sumo / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q15291
#4: Protein/peptide peptide ARTKQTARK


Mass: 1063.254 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q6NXT2*PLUS

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Non-polymers , 3 types, 229 molecules

#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Zn
#6: Chemical ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE / S-Adenosyl-L-homocysteine


Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: C14H20N6O5S
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 225 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.47 Å3/Da / Density % sol: 50.16 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 100 mM Na-Cacodylate, pH 6.5, 10% PEG 3350, 0.1 M MgCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 1.1272 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 10, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1272 Å / Relative weight: 1
ReflectionResolution: 2.4→100 Å / Num. obs: 33535 / % possible obs: 99.9 % / Redundancy: 7.1 % / Biso Wilson estimate: 35.78 Å2 / Rmerge(I) obs: 0.11 / Rpim(I) all: 0.044 / Rrim(I) all: 0.118 / Χ2: 2.063 / Net I/av σ(I): 32.656 / Net I/σ(I): 11.4 / Num. measured all: 239734
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.4-2.497.30.65432930.9390.2560.7031.1100
2.49-2.597.40.51533080.960.2010.5531.141100
2.59-2.77.40.40132650.9640.1560.4311.298100
2.7-2.857.30.28833100.9810.1130.311.535100
2.85-3.027.30.2133020.9860.0830.2261.833100
3.02-3.267.30.13933250.9920.0550.152.02100
3.26-3.597.20.133490.9960.040.1082.404100
3.59-4.16.90.07933610.9960.0320.0853.2299.9
4.1-5.176.90.05834150.9970.0240.0633.313100
5.17-1006.50.04936070.9980.0210.0542.91799.3

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5F59, 3TOJ

5f59

3toj


Resolution: 2.411→44.416 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2284 1644 4.91 %Random selection
Rwork0.1804 31814 --
obs0.1827 33458 99.3 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 152.65 Å2 / Biso mean: 46.5872 Å2 / Biso min: 16.08 Å2
Refinement stepCycle: final / Resolution: 2.411→44.416 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5547 0 54 225 5826
Biso mean--52.53 41.67 -
Num. residues----694
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035743
X-RAY DIFFRACTIONf_angle_d0.6547743
X-RAY DIFFRACTIONf_chiral_restr0.027806
X-RAY DIFFRACTIONf_plane_restr0.002985
X-RAY DIFFRACTIONf_dihedral_angle_d13.0562138
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4106-2.48150.31971390.23612436257593
2.4815-2.56160.30111420.221825732715100
2.5616-2.65310.28341040.234326612765100
2.6531-2.75930.33251410.227826262767100
2.7593-2.88490.30621370.204726312768100
2.8849-3.0370.24671230.20626442767100
3.037-3.22720.24391420.201326482790100
3.2272-3.47630.24691430.190526502793100
3.4763-3.82590.22231340.171226872821100
3.8259-4.37910.16851360.143826892825100
4.3791-5.51560.17931630.137627022865100
5.5156-44.42350.211400.182867300799
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)
16.79561.6026-2.66672.22541.16962.79830.5298-0.12190.76430.52860.0410.5899-0.8258-0.3459-0.5970.44030.00170.15060.3354-0.06470.325988.321254.41365.0589
24.59620.783-0.95444.703-1.00884.6888-0.0497-0.13490.31550.4525-0.17130.8153-0.1378-0.49580.21520.2720.01240.0340.2939-0.02420.244983.371550.7355-2.8384
32.1135-0.62582.09783.61820.44934.52210.141-0.27820.10810.6651-0.31-0.16230.05010.00120.18470.3124-0.04650.03230.2930.00840.134894.362945.40435.077
42.41990.6597-0.68784.53290.12131.5254-0.02180.0335-0.1065-0.00390.0198-0.21780.1324-0.0199-0.00440.25260.00640.02110.2484-0.0020.115496.900442.9175-7.4765
57.25371.99432.17184.37511.43765.1560.1301-0.7017-0.33830.6257-0.0027-0.58850.15720.3672-0.19630.35550.0115-0.08860.28880.01320.1935102.510638.31534.8396
61.36590.4592-0.34523.17640.67242.82990.0926-0.3934-0.32820.612-0.1222-0.25950.32890.0180.02590.3533-0.0156-0.02770.31040.030.199196.153240.46814.7455
76.1166-0.7155-1.86341.59922.56617.45740.24780.8422-0.7855-0.8716-0.18110.60750.049-0.4274-0.04120.95690.1126-0.12470.3648-0.17110.525193.89546.7216-24.2522
84.9406-0.4671.59646.5232-1.02576.7826-0.10220.2768-0.1622-1.22960.0140.58620.4414-0.5162-0.04210.5526-0.0463-0.08890.3018-0.09110.417989.71266.9935-13.5975
92.4757-0.11960.51580.63910.02970.72410.17960.4257-0.3758-1.3494-0.1961-0.24650.28780.14310.08480.70860.12970.21530.3036-0.0180.4921100.859513.539-19.2751
104.7818-2.16610.45454.1152-0.13222.68630.26590.1102-0.5527-0.6327-0.1047-0.42650.51120.1369-0.19620.49680.07170.0740.23020.02350.4768102.17926.4465-9.9435
119.2706-5.6598-0.42888.7620.11043.1664-0.0634-0.2175-0.14230.2354-0.3444-0.985-0.10970.29880.27650.2584-0.0070.06110.2710.05410.4417106.125514.6702-4.8639
124.74910.490.04090.35721.19854.6510.02630.35230.1848-0.5846-0.0258-1.22420.13570.7107-0.11530.58260.10590.30710.37430.08420.6593111.7518.3584-18.4141
130.5828-0.71211.57882.0184-0.78155.4186-0.21570.2455-0.69830.116-0.0936-0.86450.01040.65280.03340.30040.02270.09590.29020.06740.678110.710521.6584-10.9273
143.8314-0.9896-0.44142.36950.64411.40580.02460.3863-0.2332-0.9745-0.1808-0.36370.1930.05920.10450.45880.07410.10580.25470.00130.3522101.255915.3061-16.6352
151.2562-0.51920.34370.2147-0.14110.09350.04810.25530.283-0.76850.0297-0.4066-0.6304-0.0185-1.18761.13750.16030.48080.57350.10380.5753106.000221.0717-26.2477
166.1489-0.438-4.33134.2829-2.44539.6889-0.1331-0.1066-0.35680.1519-0.3269-0.1274-0.06060.38320.56120.3106-0.03480.03550.2658-0.00970.453682.737523.86381.6739
174.0667-3.1726-2.60795.263-0.36638.1170.241-0.03420.41980.9292-0.25540.5524-0.324-0.06260.08830.4192-0.02360.06060.5493-0.15060.523371.029726.67915.7037
181.88991.12860.16272.805-3.6276.56340.3905-0.4450.28990.26880.36720.4088-0.317-0.4063-0.71170.53320.03550.1710.3532-0.04320.517260.13329.125313.9087
196.48661.6426-0.6295.5017-0.74165.76910.1629-0.79410.8580.02990.0163-0.2775-0.55730.0898-0.1520.2485-0.02810.1230.3686-0.07740.512374.072529.07986.7228
202.42851.60392.28676.9456-0.09286.57740.6682-0.1761-0.7653-0.1301-0.65950.90840.2093-0.76340.01940.3359-0.02290.02240.3606-0.09970.671358.63027.10410.4082
216.00150.71621.57248.4531.21423.9552-0.0173-0.80580.4437-0.0942-0.24230.28130.3558-0.12420.12590.2909-0.0418-0.06470.3992-0.12660.45959.584313.79372.013
226.93561.91833.45817.14081.69522.0430.4128-0.4562-0.0720.72-0.46620.23840.62550.1410.15350.3182-0.01290.01180.28230.03230.463965.03211.90725.1379
232.24-2.1191.59415.4878-0.7398.298-0.3439-0.09060.21950.63410.40711.1693-0.6319-0.9597-0.1270.37750.05970.09270.45730.03280.592862.179427.31326.8119
242.665-3.2370.58314.2101-1.51432.45810.03850.69940.5617-0.55220.2963-0.1264-0.1590.2172-0.27680.3784-0.00850.01750.4327-0.05460.473173.507723.5974-2.8422
254.4385-4.8994-3.44595.82833.07765.25510.18040.65780.23970.2666-0.0642-1.5540.2723-0.2395-0.02750.3414-0.02220.09130.234-0.08170.568375.553219.6201-0.9679
266.33280.21721.07424.77420.41927.260.4283-0.27710.74190.00250.11240.5668-0.3699-0.7497-0.42540.41920.09510.10680.38250.01470.706862.512832.04015.5974
274.94380.9478-0.68274.4877-1.31120.4177-0.0745-0.25180.02570.40470.16570.3309-0.6644-0.3463-0.10470.79580.22370.08530.83120.0780.469151.73933.8581.1176
282.35352.8506-3.16816.7034-1.05966.64321.0025-2.3353-0.74280.7159-0.6128-0.44-0.9576-0.1092-0.62580.5746-0.0745-0.0950.67060.12240.741170.455312.340413.9829
295.97745.61381.66025.8153-0.01765.6478-0.2713-0.3286-0.2918-1.3721-0.2417-0.30430.59270.3580.30680.41760.13180.01550.3504-0.03470.520371.06187.17473.9376
309.46920.77390.77367.7548-0.75986.04240.0025-0.15320.99530.5862-0.52370.51490.0752-0.06470.35440.43520.0107-0.02930.2982-0.06850.677459.8841-2.83771.4854
315.3669-1.13352.49322.5406-1.12396.0194-0.3363-0.1833-0.76650.0480.15780.30860.4522-0.22440.20590.34560.0190.20690.52520.05040.4005117.743442.7608-13.5735
324.569-0.75670.37352.40910.52753.4501-0.0745-0.2892-0.79720.41990.3160.1620.4935-0.1564-0.23230.3350.02470.14560.3730.07150.3735126.440339.0308-12.5019
337.7985-0.18267.12393.2572-0.32376.87710.12820.27940.3387-0.0795-0.0787-0.45110.01130.6858-0.09780.39890.00940.0510.3769-0.01640.2236138.011360.1272-21.3008
349.2184-0.42141.75777.7249-2.78672.2496-0.577-0.02-0.058-0.38750.0654-0.1614-0.42190.10430.5610.38710.03390.03310.2357-0.03890.3626134.519552.8221-21.4037
354.20240.4668-1.21488.0871-1.59421.8955-0.3191-0.2717-0.41890.43510.2184-0.09740.0930.11770.07530.31450.03280.08890.39090.00740.2195131.842346.4278-16.3711
367.7006-2.2571-0.56839.026-1.70457.8971-0.11920.6005-0.1334-1.3225-0.20770.22030.1189-0.71390.12820.3924-0.01280.04310.4284-0.02830.2865121.259546.3469-24.1022
373.6925-0.93972.92473.72911.82884.6551-0.3435-0.092-1.1338-0.03040.30430.19640.4927-0.26310.24240.47690.04380.17380.27440.04620.5104130.451334.4808-15.7171
388.63920.8463-1.04124.81110.1035.22330.00510.11960.37710.00260.18440.0333-0.0040.6046-0.25780.68140.10810.11930.4783-0.01280.6545143.604133.6969-19.6906
393.8877-0.12131.724.6238-3.62184.33360.36120.2372-0.42270.32070.49661.1524-0.4993-0.4108-0.86360.55220.06780.11740.3279-0.02190.46124.84561.8909-19.7057
405.7852-0.0598-3.79853.143-1.48396.18020.4008-0.7569-0.13010.7444-0.31270.00970.28340.9755-0.28440.42790.0125-0.05880.42230.04510.2834138.280271.9336-26.2256
414.54.5565.26524.72515.36346.170.53150.70620.543-1.5335-0.90111.3071-1.4498-1.32640.63370.88750.1334-0.01450.97250.0590.903760.563419.5736-3.4999
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 286 through 295 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 296 through 313 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 314 through 335 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 336 through 390 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 391 through 451 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 452 through 503 )A0
7X-RAY DIFFRACTION7chain 'B' and (resid 285 through 294 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 295 through 313 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 314 through 335 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 336 through 362 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 363 through 390 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 391 through 451 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 452 through 461 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 462 through 493 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 494 through 503 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 4754 through 4767 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 4768 through 4777 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 4778 through 4787 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 4788 through 4802 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 4803 through 4817 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 4818 through 4832 )C0
22X-RAY DIFFRACTION22chain 'C' and (resid 4833 through 4842 )C0
23X-RAY DIFFRACTION23chain 'C' and (resid 4843 through 4854 )C0
24X-RAY DIFFRACTION24chain 'C' and (resid 4855 through 4862 )C0
25X-RAY DIFFRACTION25chain 'C' and (resid 4863 through 4872 )C0
26X-RAY DIFFRACTION26chain 'C' and (resid 4873 through 4900 )C0
27X-RAY DIFFRACTION27chain 'C' and (resid 4901 through 4911 )C0
28X-RAY DIFFRACTION28chain 'D' and (resid 336 through 340 )D0
29X-RAY DIFFRACTION29chain 'D' and (resid 341 through 345 )D0
30X-RAY DIFFRACTION30chain 'D' and (resid 346 through 354 )D0
31X-RAY DIFFRACTION31chain 'E' and (resid 4755 through 4777 )E0
32X-RAY DIFFRACTION32chain 'E' and (resid 4778 through 4802 )E0
33X-RAY DIFFRACTION33chain 'E' and (resid 4803 through 4820 )E0
34X-RAY DIFFRACTION34chain 'E' and (resid 4821 through 4832 )E0
35X-RAY DIFFRACTION35chain 'E' and (resid 4833 through 4854 )E0
36X-RAY DIFFRACTION36chain 'E' and (resid 4855 through 4872 )E0
37X-RAY DIFFRACTION37chain 'E' and (resid 4873 through 4897 )E0
38X-RAY DIFFRACTION38chain 'E' and (resid 4898 through 4911 )E0
39X-RAY DIFFRACTION39chain 'F' and (resid 339 through 348 )F0
40X-RAY DIFFRACTION40chain 'F' and (resid 349 through 355 )F0
41X-RAY DIFFRACTION41chain 'M' and (resid 2 through 7 )M0

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