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- PDB-4ogr: crystal structure of P-TEFb complex with AFF4 and Tat -

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Basic information

Entry
Database: PDB / ID: 4ogr
Titlecrystal structure of P-TEFb complex with AFF4 and Tat
Components
  • AF4/FMR2 family member 4
  • Cyclin-T1
  • Cyclin-dependent kinase 9
  • Protein Tat
Keywordstransferase/viral protein / P-TEFb / cyclin-dependent kinase 9 / cyclin fold / intrinsically unstructured AFF4 / transcriptional regulation at HIV promoter / binds TAR / N-terminal acetylation of Tat / transferase-viral protein complex
Function / homology
Function and homology information


: / super elongation complex / trans-activation response element binding / P-TEFb complex / Interactions of Tat with host cellular proteins / 7SK snRNA binding / positive regulation of viral transcription / cyclin/CDK positive transcription elongation factor complex / regulation of muscle cell differentiation / regulation of mRNA 3'-end processing ...: / super elongation complex / trans-activation response element binding / P-TEFb complex / Interactions of Tat with host cellular proteins / 7SK snRNA binding / positive regulation of viral transcription / cyclin/CDK positive transcription elongation factor complex / regulation of muscle cell differentiation / regulation of mRNA 3'-end processing / positive regulation of protein localization to chromatin / modulation by virus of host chromatin organization / nucleus localization / host cell nucleolus / actinin binding / cyclin-dependent protein serine/threonine kinase activator activity / positive regulation by host of viral transcription / RNA polymerase binding / negative regulation of protein localization to chromatin / positive regulation of DNA-templated transcription, elongation / [RNA-polymerase]-subunit kinase / transcription elongation-coupled chromatin remodeling / replication fork processing / negative regulation of peptidyl-threonine phosphorylation / cellular response to cytokine stimulus / regulation of cyclin-dependent protein serine/threonine kinase activity / spermatid development / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / RNA-binding transcription regulator activity / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / regulation of DNA repair / cyclin-dependent kinase / Formation of HIV elongation complex in the absence of HIV Tat / cyclin-dependent protein serine/threonine kinase activity / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / molecular condensate scaffold activity / response to endoplasmic reticulum stress / cyclin binding / RNA polymerase II CTD heptapeptide repeat kinase activity / transcription elongation factor complex / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / TP53 Regulates Transcription of DNA Repair Genes / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / euchromatin / transcription coactivator binding / cytoplasmic ribonucleoprotein granule / PML body / fibrillar center / kinase activity / regulation of gene expression / DNA-binding transcription factor binding / Estrogen-dependent gene expression / cell population proliferation / host cell cytoplasm / transcription by RNA polymerase II / transcription cis-regulatory region binding / regulation of cell cycle / protein kinase activity / response to xenobiotic stimulus / cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding / cell division / protein domain specific binding / protein phosphorylation / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / DNA-templated transcription / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / chromatin binding / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of transcription by RNA polymerase II / DNA binding / extracellular region / nucleoplasm / ATP binding / membrane / metal ion binding / nucleus / cytosol
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2670 / AF-4 proto-oncoprotein N-terminal region / AF4/FMR2 family / AF4 interaction motif / AF4/FMR2, C-terminal homology domain / AF4 interaction motif / AFF4, C-terminal homology domain / Tat domain superfamily / Immunodeficiency virus transactivating regulatory protein (Tat) / : ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #2670 / AF-4 proto-oncoprotein N-terminal region / AF4/FMR2 family / AF4 interaction motif / AF4/FMR2, C-terminal homology domain / AF4 interaction motif / AFF4, C-terminal homology domain / Tat domain superfamily / Immunodeficiency virus transactivating regulatory protein (Tat) / : / Transactivating regulatory protein (Tat) / Cyclin-T2-like, C-terminal domain / Haspin like kinase domain / Cyclin/Cyclin-like subunit Ssn8 / Cyclin-like / Cyclin A; domain 1 / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Cyclin-like superfamily / Helix non-globular / Special / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE / Cyclin-T1 / Cyclin-dependent kinase 9 / Protein Tat / AF4/FMR2 family member 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Human immunodeficiency virus type 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsSchulze-Gahmen, U. / Alber, T.
CitationJournal: Elife / Year: 2014
Title: AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter.
Authors: Schulze-Gahmen, U. / Lu, H. / Zhou, Q. / Alber, T.
History
DepositionJan 16, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 7, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 2, 2014Group: Database references
Revision 1.2Nov 22, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 20, 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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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.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_seq_id / _struct_conn.ptnr2_label_asym_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: Cyclin-dependent kinase 9
B: Cyclin-T1
C: AF4/FMR2 family member 4
E: Cyclin-dependent kinase 9
F: Cyclin-T1
G: AF4/FMR2 family member 4
I: Cyclin-dependent kinase 9
K: Cyclin-T1
L: AF4/FMR2 family member 4
D: Protein Tat
H: Protein Tat
M: Protein Tat
hetero molecules


Theoretical massNumber of molelcules
Total (without water)254,45221
Polymers253,25712
Non-polymers1,1949
Water66737
1
A: Cyclin-dependent kinase 9
B: Cyclin-T1
C: AF4/FMR2 family member 4
D: Protein Tat
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,8177
Polymers84,4194
Non-polymers3983
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11570 Å2
ΔGint-100 kcal/mol
Surface area29930 Å2
MethodPISA
2
E: Cyclin-dependent kinase 9
F: Cyclin-T1
G: AF4/FMR2 family member 4
H: Protein Tat
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,8177
Polymers84,4194
Non-polymers3983
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10700 Å2
ΔGint-103 kcal/mol
Surface area28570 Å2
MethodPISA
3
I: Cyclin-dependent kinase 9
K: Cyclin-T1
L: AF4/FMR2 family member 4
M: Protein Tat
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,8177
Polymers84,4194
Non-polymers3983
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11560 Å2
ΔGint-96 kcal/mol
Surface area30100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)184.908, 184.908, 360.399
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A and segid A
21chain E and segid E
31chain I and segid I
12chain B and segid B
22chain F and segid F
32chain K and segid K
13chain C and segid C
23chain L and segid L
14chain D and segid D
24chain H and segid H
34chain M and segid M

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain A and segid AA0
211chain E and segid EE0
311chain I and segid II0
112chain B and segid BB0
212chain F and segid FF0
312chain K and segid KK0
113chain C and segid CC0
213chain L and segid LL0
114chain D and segid DD0
214chain H and segid HH0
314chain M and segid MM0

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 4 types, 12 molecules AEIBFKCGLDHM

#1: Protein Cyclin-dependent kinase 9 / / C-2K / Cell division cycle 2-like protein kinase 4 / Cell division protein kinase 9 / ...C-2K / Cell division cycle 2-like protein kinase 4 / Cell division protein kinase 9 / Serine/threonine-protein kinase PITALRE / Tat-associated kinase complex catalytic subunit


Mass: 38226.309 Da / Num. of mol.: 3 / Fragment: unp residues 1-330
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDK9, CDC2L4, TAK / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P50750, cyclin-dependent kinase, [RNA-polymerase]-subunit kinase
#2: Protein Cyclin-T1 / CycT1 / Cyclin-T


Mass: 30618.959 Da / Num. of mol.: 3 / Fragment: unp residues 1-264
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CCNT1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O60563
#3: Protein AF4/FMR2 family member 4 / ALL1-fused gene from chromosome 5q31 protein / Protein AF-5q31 / Major CDK9 elongation factor- ...ALL1-fused gene from chromosome 5q31 protein / Protein AF-5q31 / Major CDK9 elongation factor-associated protein


Mass: 8789.776 Da / Num. of mol.: 3 / Fragment: unp residues 2-73
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AFF4, AF5Q31, MCEF, HSPC092 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UHB7
#4: Protein Protein Tat / Transactivating regulatory protein


Mass: 6784.110 Da / Num. of mol.: 3 / Fragment: unp residues 1-57
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 (HXB3 ISOLATE)
Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P69698

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Non-polymers , 3 types, 46 molecules

#5: Chemical ChemComp-ADN / ADENOSINE / Adenosine


Mass: 267.241 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H13N5O4
#6: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 37 / 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: 3.51 Å3/Da / Density % sol: 64.97 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.3
Details: Crystallized from 25 mM HEPES pH 7.3, 0.2 M NaCl, 10 mM MgCl, 2.4 M Na formate, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 12, 2013
RadiationMonochromator: DOUBLE FLAT CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. all: 73424 / Num. obs: 73424 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 24.2 % / Biso Wilson estimate: 77.94 Å2 / Rmerge(I) obs: 0.222 / Χ2: 1.169 / Net I/σ(I): 12
Reflection shell
Resolution (Å)Redundancy (%)Num. unique allΧ2Diffraction-ID% possible allRmerge(I) obs
3-3.0523.835890.8791100
3.05-3.1123.936190.9151100
3.11-3.1724.135970.9531100
3.17-3.2324.235900.9681100
3.23-3.324.236461.0081100
3.3-3.3824.335901.0291100
3.38-3.4624.336161.091100
3.46-3.5624.436431.0831100
3.56-3.6624.536041.10911000.828
3.66-3.7824.636221.13811000.662
3.78-3.9124.536511.17411000.531
3.91-4.0724.636431.1811000.419
4.07-4.2624.636501.22411000.327
4.26-4.4824.536611.32511000.246
4.48-4.7624.536961.29511000.22
4.76-5.1324.336951.40111000.201
5.13-5.6424.237001.4711000.233
5.64-6.4623.937511.46111000.23
6.46-8.1323.538081.35411000.12
8.13-5022.440531.27611000.044

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Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHENIXdev_1419refinement
PDB_EXTRACT3.14data extraction
HKL-2000data collection
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 4IMY

4imy


Resolution: 3→49.015 Å / FOM work R set: 0.8212 / SU ML: 0.37 / σ(F): 1.35 / Phase error: 24.18 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2323 2406 3.28 %
Rwork0.2047 70893 -
obs0.2056 73299 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 299.92 Å2 / Biso mean: 86.67 Å2 / Biso min: 34.72 Å2
Refinement stepCycle: LAST / Resolution: 3→49.015 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16054 0 63 37 16154
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00416500
X-RAY DIFFRACTIONf_angle_d0.80522375
X-RAY DIFFRACTIONf_chiral_restr0.032496
X-RAY DIFFRACTIONf_plane_restr0.0032845
X-RAY DIFFRACTIONf_dihedral_angle_d14.3366097
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5912X-RAY DIFFRACTION9.872TORSIONAL
12E5912X-RAY DIFFRACTION9.872TORSIONAL
13I5912X-RAY DIFFRACTION9.872TORSIONAL
21B4754X-RAY DIFFRACTION9.872TORSIONAL
22F4754X-RAY DIFFRACTION9.872TORSIONAL
23K4754X-RAY DIFFRACTION9.872TORSIONAL
31C604X-RAY DIFFRACTION9.872TORSIONAL
32L604X-RAY DIFFRACTION9.872TORSIONAL
41D894X-RAY DIFFRACTION9.872TORSIONAL
42H894X-RAY DIFFRACTION9.872TORSIONAL
43M894X-RAY DIFFRACTION9.872TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 17 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
3-3.06120.33691380.314540694207
3.0612-3.12780.35271390.312541024241
3.1278-3.20050.32091410.303540894230
3.2005-3.28050.30651380.293841164254
3.2805-3.36920.32061410.271841184259
3.3692-3.46830.26091380.252140884226
3.4683-3.58030.27081400.236941214261
3.5803-3.70820.24791410.225641334274
3.7082-3.85660.25021400.214741424282
3.8566-4.0320.26081400.199741264266
4.032-4.24450.19491410.180541504291
4.2445-4.51030.2131420.16341894331
4.5103-4.85820.17561410.165541744315
4.8582-5.34660.17931420.17241964338
5.3466-6.1190.2371430.202142354378
6.119-7.70440.22161470.204343074454
7.7044-49.0210.20881540.176745384692
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)
15.19871.1793-2.25265.9654-3.26612.38070.3021-0.50810.47070.260.09920.5098-0.64740.0498-0.4440.4713-0.05660.02790.67060.08380.678670.7832-19.3597-13.0615
21.1315-0.16450.1461.8916-0.69134.11190.032-0.05690.0414-0.11150.12380.1816-0.2902-0.2213-0.15570.4564-0.04430.04180.46790.11120.539449.154-16.0231-29.3354
34.00775.4508-1.14497.6995-1.68590.3868-1.56681.1457-2.4357-1.72080.9932-1.6321.08210.13260.61410.6981-0.16440.12260.98670.00611.249560.0742-40.65010.2175
42.63471.9433-0.69763.6560.17372.53560.1411-0.2719-0.03530.4305-0.1221-0.1112-0.13350.3297-0.02910.4458-0.0534-0.00660.62170.08130.440647.7267-31.75298.2902
55.33360.27182.89556.84514.674.5428-0.20730.16930.04160.38430.311-0.2651-0.1055-0.1622-0.08270.6363-0.1691-0.1010.66660.08140.716946.7766-36.8923-38.3322
64.41761.00750.93074.75173.55596.67260.158-0.8280.0330.41390.02220.3224-0.0391-0.1338-0.19270.6536-0.01280.18870.68460.08180.529729.5927-45.545712.4967
73.2575-0.5062-1.54613.9154-0.62934.49780.1031-0.29140.37990.63-0.04280.2287-0.4-0.8369-0.07090.5427-0.12490.12650.68140.00210.644137.0363-26.049611.7786
82.58342.45541.0894.21110.48021.81910.0083-0.1812-0.55870.35010.0078-0.64670.20580.387-0.01340.54350.14480.02130.7315-0.00310.7026103.865-26.5407-16.2995
92.99250.6547-0.26373.8394-0.25465.904-0.24530.4493-0.4338-0.51360.24820.10820.51920.14560.00960.55220.01140.02430.5424-0.11170.691592.8782-32.7884-35.8483
103.3991-0.0768-0.48653.6768-0.44542.721-0.0520.00830.0180.21450.1470.1144-0.36490.1293-0.09460.4104-0.07840.04510.6278-0.02250.4495104.01025.521-20.0124
113.8179-2.0866-2.99062.97520.44763.0806-0.44280.35642.2999-1.20431.48451.3214-1.7572-1.4676-0.92661.13520.03540.00110.8560.18111.3611103.559129.4987-31.1517
127.69175.855-0.19774.6819-0.853.6908-0.0872-0.48760.58260.1695-0.49781.8807-0.3207-1.12460.62520.5638-0.01130.08241.21380.23471.458877.261218.7995-25.1395
135.1768-0.2842-1.92046.8883-0.85784.7043-0.20120.61591.51540.30020.2971-0.213-0.3285-0.6614-0.15731.00080.0265-0.13190.82280.07711.13592.502624.3297-25.9146
141.55331.62560.73994.57010.54833.023-0.28190.26260.1116-0.4510.29410.1979-0.46770.2611-0.04770.6263-0.18860.02860.83740.05260.647103.637611.57-32.8202
157.69580.4777-4.12225.91441.02022.5548-0.08060.3386-0.283-0.64990.27990.2211-0.1583-0.6437-0.23690.5873-0.1861-0.0080.9002-0.07130.6944-5.372-71.9668-33.484
161.6974-0.1541-0.53061.32480.42423.6730.0890.07450.0621-0.13440.08040.079-0.3954-0.4626-0.16610.5533-0.05310.08560.766-0.00570.5809-0.7198-51.4159-17.0135
172.32950.93-0.92669.64311.56010.79710.6945-1.5465-0.50061.4439-0.8307-0.8695-0.1160.96060.20680.9076-0.4459-0.02061.1406-0.14660.965917.7667-69.2648-47.1228
184.14010.88620.35481.3748-0.3171.7415-0.34010.7539-0.205-0.42080.2412-0.05040.0954-0.33910.07630.7996-0.27590.04880.9196-0.06090.521513.9101-54.2379-54.6368
196.2364-0.89724.99275.0050.21414.1596-0.28360.9129-0.1271-0.28750.5702-0.4346-0.72810.0776-0.310.4962-0.1685-0.06120.8223-0.12370.725319.6982-55.9812-6.0124
203.87031.9866-1.90732.3325-1.79044.6315-0.40340.87490.2985-0.84440.5139-0.01840.42050.0147-0.04060.8611-0.12460.04570.86390.04160.551232.1731-43.6038-56.3622
214.10850.0562-0.78784.8735-0.02258.3026-0.20110.96020.1583-0.56160.11290.362-0.6647-0.35840.08370.8887-0.2732-0.07591.10060.16830.76512.3549-42.1193-57.6342
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 8:55)A8 - 55
2X-RAY DIFFRACTION2(chain A and resid 56:330)A56 - 330
3X-RAY DIFFRACTION3(chain B and resid 7:16)B7 - 16
4X-RAY DIFFRACTION4(chain B and resid 17:261)B17 - 261
5X-RAY DIFFRACTION5(chain C and resid 4:21)C4 - 21
6X-RAY DIFFRACTION6(chain C and resid 33:69)C33 - 69
7X-RAY DIFFRACTION7(chain D and resid 1:49)D1 - 49
8X-RAY DIFFRACTION8(chain E and resid 8:143)E8 - 143
9X-RAY DIFFRACTION9(chain E and resid 144:330)E144 - 330
10X-RAY DIFFRACTION10(chain F and resid 7:250)F7 - 250
11X-RAY DIFFRACTION11(chain F and resid 251:261)F251 - 261
12X-RAY DIFFRACTION12(chain G and resid 34:43)G34 - 43
13X-RAY DIFFRACTION13(chain G and resid 44:69)G44 - 69
14X-RAY DIFFRACTION14(chain H and resid 1:49)H1 - 49
15X-RAY DIFFRACTION15(chain I and resid 8:55)I8 - 55
16X-RAY DIFFRACTION16(chain I and resid 56:330)I56 - 330
17X-RAY DIFFRACTION17(chain K and resid 7:16)K7 - 16
18X-RAY DIFFRACTION18(chain K and resid 17:261)K17 - 261
19X-RAY DIFFRACTION19(chain L and resid 4:18)L4 - 18
20X-RAY DIFFRACTION20(chain L and resid 19:69)L19 - 69
21X-RAY DIFFRACTION21(chain M and resid 1:49)M1 - 49

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