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- PDB-6no7: Crystal Structure of the full-length wild-type PKA RIa Holoenzyme -

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Basic information

Entry
Database: PDB / ID: 6no7
TitleCrystal Structure of the full-length wild-type PKA RIa Holoenzyme
Components
  • cAMP-dependent protein kinase catalytic subunit alpha
  • cAMP-dependent protein kinase type I-alpha regulatory subunit
KeywordsSIGNALING PROTEIN / PKA / RIa holoenzyme / ATP-dependent
Function / homology
Function and homology information


PKA-mediated phosphorylation of CREB / PKA-mediated phosphorylation of key metabolic factors / sperm head-tail coupling apparatus / ROBO receptors bind AKAP5 / HDL assembly / PKA activation in glucagon signalling / DARPP-32 events / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / channel activator activity ...PKA-mediated phosphorylation of CREB / PKA-mediated phosphorylation of key metabolic factors / sperm head-tail coupling apparatus / ROBO receptors bind AKAP5 / HDL assembly / PKA activation in glucagon signalling / DARPP-32 events / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / channel activator activity / Factors involved in megakaryocyte development and platelet production / Regulation of glycolysis by fructose 2,6-bisphosphate metabolism / mitochondrial protein catabolic process / PKA activation / nucleotide-activated protein kinase complex / cell communication by electrical coupling involved in cardiac conduction / Hedgehog 'off' state / high-density lipoprotein particle assembly / Rap1 signalling / negative regulation of cAMP/PKA signal transduction / cAMP-dependent protein kinase inhibitor activity / cAMP-dependent protein kinase / regulation of protein processing / cAMP-dependent protein kinase activity / sarcomere organization / protein localization to lipid droplet / cAMP-dependent protein kinase complex / regulation of bicellular tight junction assembly / cellular response to parathyroid hormone stimulus / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / negative regulation of interleukin-2 production / PKA activation / regulation of osteoblast differentiation / cellular response to cold / sperm capacitation / negative regulation of glycolytic process through fructose-6-phosphate / Triglyceride catabolism / ciliary base / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / Vasopressin regulates renal water homeostasis via Aquaporins / protein kinase A regulatory subunit binding / negative regulation of activated T cell proliferation / protein kinase A catalytic subunit binding / intracellular potassium ion homeostasis / mesoderm formation / RET signaling / cAMP/PKA signal transduction / Interleukin-3, Interleukin-5 and GM-CSF signaling / immunological synapse / plasma membrane raft / axoneme / PKA activation in glucagon signalling / Regulation of MECP2 expression and activity / DARPP-32 events / regulation of cardiac conduction / regulation of macroautophagy / cardiac muscle cell proliferation / regulation of cardiac muscle contraction / sperm flagellum / postsynaptic modulation of chemical synaptic transmission / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / vascular endothelial cell response to laminar fluid shear stress / renal water homeostasis / cAMP binding / Hedgehog 'off' state / Ion homeostasis / negative regulation of TORC1 signaling / regulation of proteasomal protein catabolic process / sperm midpiece / multivesicular body / cellular response to epinephrine stimulus / calcium channel complex / positive regulation of gluconeogenesis / protein serine/threonine/tyrosine kinase activity / Mitochondrial protein degradation / cellular response to glucagon stimulus / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / acrosomal vesicle / CD209 (DC-SIGN) signaling / positive regulation of calcium-mediated signaling / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / regulation of heart rate / FCGR3A-mediated IL10 synthesis / protein export from nucleus / positive regulation of phagocytosis / AURKA Activation by TPX2 / positive regulation of protein export from nucleus / negative regulation of smoothened signaling pathway / neural tube closure / Regulation of insulin secretion / neuromuscular junction / cellular response to glucose stimulus / Degradation of GLI1 by the proteasome / positive regulation of cholesterol biosynthetic process / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome
Similarity search - Function
cAMP-dependent protein kinase regulatory subunit / cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain / Regulatory subunit of type II PKA R-subunit / RIIalpha, Regulatory subunit portion of type II PKA R-subunit / : / Cyclic nucleotide-binding domain signature 2. / cAMP-dependent protein kinase catalytic subunit / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain ...cAMP-dependent protein kinase regulatory subunit / cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain / Regulatory subunit of type II PKA R-subunit / RIIalpha, Regulatory subunit portion of type II PKA R-subunit / : / Cyclic nucleotide-binding domain signature 2. / cAMP-dependent protein kinase catalytic subunit / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / Extension to Ser/Thr-type protein kinases / Jelly Rolls / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / RmlC-like jelly roll fold / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Jelly Rolls / 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 / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / cAMP-dependent protein kinase type I-alpha regulatory subunit / cAMP-dependent protein kinase catalytic subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
Bos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.55 Å
AuthorsLu, T. / Wu, J. / Taylor, S.S.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM34921 United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2019
Title: Two PKA RI alpha holoenzyme states define ATP as an isoform-specific orthosteric inhibitor that competes with the allosteric activator, cAMP.
Authors: Lu, T.W. / Wu, J. / Aoto, P.C. / Weng, J.H. / Ahuja, L.G. / Sun, N. / Cheng, C.Y. / Zhang, P. / Taylor, S.S.
History
DepositionJan 15, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 24, 2019Provider: repository / Type: Initial release
Revision 1.1Jul 31, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Aug 14, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.3Aug 28, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Oct 11, 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
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.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
Revision 1.6Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: cAMP-dependent protein kinase catalytic subunit alpha
B: cAMP-dependent protein kinase type I-alpha regulatory subunit
C: cAMP-dependent protein kinase catalytic subunit alpha
D: cAMP-dependent protein kinase type I-alpha regulatory subunit
E: cAMP-dependent protein kinase catalytic subunit alpha
F: cAMP-dependent protein kinase type I-alpha regulatory subunit
G: cAMP-dependent protein kinase catalytic subunit alpha
H: cAMP-dependent protein kinase type I-alpha regulatory subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)335,93114
Polymers334,8208
Non-polymers1,1126
Water00
1
A: cAMP-dependent protein kinase catalytic subunit alpha
B: cAMP-dependent protein kinase type I-alpha regulatory subunit
C: cAMP-dependent protein kinase catalytic subunit alpha
D: cAMP-dependent protein kinase type I-alpha regulatory subunit


Theoretical massNumber of molelcules
Total (without water)167,4104
Polymers167,4104
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
E: cAMP-dependent protein kinase catalytic subunit alpha
F: cAMP-dependent protein kinase type I-alpha regulatory subunit
G: cAMP-dependent protein kinase catalytic subunit alpha
H: cAMP-dependent protein kinase type I-alpha regulatory subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,52210
Polymers167,4104
Non-polymers1,1126
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)139.778, 184.811, 183.406
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
cAMP-dependent protein kinase catalytic subunit alpha / PKA C-alpha


Mass: 40757.352 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRKACA, PKACA / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P17612, cAMP-dependent protein kinase
#2: Protein
cAMP-dependent protein kinase type I-alpha regulatory subunit


Mass: 42947.621 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Gene: PRKAR1A / Production host: Escherichia coli (E. coli) / References: UniProt: P00514
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
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: 3.54 Å3/Da / Density % sol: 65.25 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7
Details: mixing 1 ul of the protein solution (7.5 mg/ml) and 1 ul of the reservoir solution (100 mM imidazole/MES pH=7.0, 100 mM NPS, 16.8% v/v Ethylene glycol, 8.4 % w/v PEG 8000).

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 20, 2017
RadiationMonochromator: Double-crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.55→50 Å / Num. obs: 58193 / % possible obs: 87 % / Redundancy: 2.7 % / Rmerge(I) obs: 0.126 / Net I/σ(I): 7.6
Reflection shellResolution: 3.55→3.63 Å / Redundancy: 2 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 1.7 / Num. unique obs: 2567 / % possible all: 80.7

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
HKL-2000data reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2QCS

2qcs


Resolution: 3.55→47.632 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 37.27 / Stereochemistry target values: TWIN_LSQ_F
RfactorNum. reflection% reflectionSelection details
Rfree0.2687 2816 5.57 %Random selection
Rwork0.2558 ---
obs0.2591 50530 87.05 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.55→47.632 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20062 0 66 0 20128
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00520577
X-RAY DIFFRACTIONf_angle_d1.21327821
X-RAY DIFFRACTIONf_dihedral_angle_d11.42912299
X-RAY DIFFRACTIONf_chiral_restr0.0622978
X-RAY DIFFRACTIONf_plane_restr0.0063587
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5501-3.61830.35661120.3592228X-RAY DIFFRACTION70
3.6183-3.69220.39191390.34752278X-RAY DIFFRACTION71
3.6922-3.77240.3011170.34952339X-RAY DIFFRACTION73
3.7724-3.86010.32891140.32422350X-RAY DIFFRACTION74
3.8601-3.95650.35051260.30942353X-RAY DIFFRACTION74
3.9565-4.06340.28161380.28082451X-RAY DIFFRACTION76
4.0634-4.18290.32791310.29172473X-RAY DIFFRACTION77
4.1829-4.31780.27091370.27262488X-RAY DIFFRACTION78
4.3178-4.47190.27461290.25932560X-RAY DIFFRACTION80
4.4719-4.65070.25911500.25422616X-RAY DIFFRACTION82
4.6507-4.86210.27951560.25112703X-RAY DIFFRACTION85
4.8621-5.1180.26671520.24962837X-RAY DIFFRACTION88
5.118-5.4380.28961480.26112905X-RAY DIFFRACTION90
5.438-5.85680.33541500.28333028X-RAY DIFFRACTION94
5.8568-6.44430.30041620.2723059X-RAY DIFFRACTION94
6.4443-7.37230.26391640.2313075X-RAY DIFFRACTION94
7.3723-9.27120.19481530.21413110X-RAY DIFFRACTION94
9.2712-41.54140.22091620.22833126X-RAY DIFFRACTION91
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)
10.06210.1884-0.13561.0805-0.32641.19770.01150.62030.70590.13550.4723-0.697-0.81760.2165-0.46391.3385-0.11280.59192.0861-0.1681.73633.693742.725218.7044
20.9608-0.7388-0.04241.18110.20562.0645-0.50331.1077-0.1022-0.17480.3798-0.9269-0.22221.0589-0.06440.5559-0.18650.51561.2025-0.40791.942531.709929.611119.2519
33.76571.36651.32654.49071.43052.1391-0.1840.2896-0.36710.8548-0.05260.49280.2040.03940.40020.6501-0.05510.01130.9274-0.05991.30277.494247.160541.6428
42.03060.3087-1.89190.9361-0.48831.7342-0.0419-0.24030.71840.517-0.2957-1.0529-0.40370.30610.34371.23880.215-0.21642.88130.40831.557452.2352-19.204753.9217
50.242-0.3231-0.09050.33880.07810.79130.59-0.393-0.1723-0.1068-0.2047-0.8907-0.00310.7126-0.14650.6957-0.2479-0.4061.86060.15842.495456.0935-16.297644.9629
61.5674-0.106-0.13070.3425-0.47590.7851-0.5604-0.5194-0.9747-0.2271-0.8311-1.40920.93910.9058-0.45020.08860.269-0.10522.03910.92612.401843.8383-34.874735.5541
70.73070.65880.9345.04670.99451.20570.2263-0.31-0.21370.5763-0.39741.47270.3115-0.49770.26781.9668-0.5376-0.46960.9807-0.27493.307753.6216-0.362942.9782
80.7257-0.15491.01260.7858-1.00812.36060.0846-1.2575-0.37650.6835-0.1572-0.9201-0.14040.45410.07151.09940.2943-0.26571.3799-0.18011.396433.604-11.444429.6287
91.62670.5105-0.65771.5415-0.46820.9004-0.54930.5521-0.0696-0.4707-0.0532-0.85330.00950.7914-0.05950.07650.0535-0.09411.3833-0.01251.5530.6799-12.310817.0488
102.9703-0.38390.68022.1675-0.5293.9821-0.1892-0.87410.1878-0.4063-0.0339-0.30370.1342-0.76480.04670.53630.0785-0.12161.15010.17971.32357.3796-34.451937.0702
114.44190.2261-3.80260.0025-0.11723.3359-0.0393-0.28681.3148-0.129-0.18840.4598-1.0357-0.45330.07911.44150.60990.082.59840.16842.0229-23.41618.1173-20.7967
120.7814-0.1139-0.4440.29480.44321.24350.73940.34850.2946-0.1513-0.07670.414-0.1318-0.3889-0.31241.09430.3093-0.23742.289-0.27641.9954-27.21824.9021-12.1781
131.87070.21720.53410.89720.44231.09380.45961.9908-0.3689-0.5521-0.79850.03960.1057-2.2008-0.09610.58220.2161-0.1593.3948-0.38420.9908-15.1829-15.4251-17.5555
142.47430.19980.7091.54530.21640.2216-0.1858-0.08350.6379-0.4445-0.2899-0.514-0.41520.52540.00431.41190.4875-0.29242.3954-0.27142.2359-24.59416.0833-1.2075
152.1226-0.13792.92090.2294-0.18324.22820.02730.62560.7997-0.7449-0.46210.1045-0.8680.34320.62391.14510.176-0.44831.3553-0.26551.4127-4.3298-1.22281.5487
162.9673-0.2579-0.73331.56190.89391.5791-0.3814-0.7915-0.17740.0627-0.29760.6638-0.0934-0.75850.37320.51090.1599-0.03381.46220.0230.9575-1.7357-10.093410.6567
172.70180.35821.71593.9491-0.88954.8338-0.2450.2057-0.0331-0.0823-0.0566-0.20710.15340.39490.22780.68130.06880.08521.4898-0.10890.955521.1528-14.0799-18.5575
183.93150.142.43621.21650.12852.3009-0.3151-0.2581-0.81160.2504-0.3233-0.02131.0044-0.17730.60611.14640.01020.261.81250.3991.5813-10.7769-8.854262.2288
191.5020.08850.09921.30161.35221.57950.4944-1.0173-1.4220.3322-0.35590.2631-0.0509-1.13860.10330.8208-0.140.18561.4263-0.01731.7424-15.3499-5.321453.4958
202.6876-0.0076-0.61492.4451-0.10222.09910.0937-1.07380.41250.349-0.3029-0.070.0543-0.75860.14950.5502-0.02580.14191.5007-0.07520.8606-3.033614.284658.1856
210.9749-1.7949-0.59673.50720.81820.7372-0.07480.005-0.27620.5117-0.35880.05990.5608-0.5094-0.0041.6738-0.3580.47420.7364-0.95512.3286-13.7155-16.353741.784
222.54980.0945-0.74521.7646-0.61561.7510.1068-0.8301-1.0239-0.0174-0.36190.37140.2095-0.70830.11310.5777-0.0814-0.18811.1086-0.39111.50976.87070.754437.844
233.05920.82350.6891.88710.1482.5469-0.92761.7990.26950.06880.23570.82750.2572-0.55620.13190.261-0.22850.06621.3351-0.26560.93749.04910.016628.5348
243.63890.6361-1.1491.7345-0.1632.537-0.44720.6175-0.08250.0126-0.2137-0.1988-0.06230.20170.64160.6263-0.1286-0.27191.4521-0.13091.251933.575413.533456.8632
257.2069-4.1012-3.16942.33911.96792.2077-0.42231.04590.7503-0.9726-0.1453-1.1207-0.30331.17980.24751.2698-0.31490.59221.90510.09343.302251.478867.797629.6437
260.0254-0.0418-0.15230.1328-0.06811.30911.00350.76830.9473-0.1835-0.1512-0.8331-0.45041.0846-0.49881.1364-0.49790.28212.348-0.01472.243555.850858.831825.3147
271.72170.6011-0.01410.84680.33011.17730.3356-0.32950.64810.09870.8158-1.05410.23440.81220.12830.1376-0.3182-0.12281.1316-0.89162.851544.25748.129842.7172
288.9663-2.25070.83551.6795-0.8670.4832-0.20290.65180.2901-0.4801-0.13160.1629-0.4641-0.22380.0552.0808-0.32290.28472.3695-0.09611.967554.196258.31089.4156
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'D' and (resid 93 through 118 )
2X-RAY DIFFRACTION2chain 'D' and (resid 119 through 250 )
3X-RAY DIFFRACTION3chain 'D' and (resid 251 through 372 )
4X-RAY DIFFRACTION4chain 'E' and (resid 15 through 49 )
5X-RAY DIFFRACTION5chain 'E' and (resid 58 through 128 )
6X-RAY DIFFRACTION6chain 'E' and (resid 129 through 318 )
7X-RAY DIFFRACTION7chain 'E' and (resid 336 through 350 )
8X-RAY DIFFRACTION8chain 'F' and (resid 93 through 118 )
9X-RAY DIFFRACTION9chain 'F' and (resid 119 through 250)
10X-RAY DIFFRACTION10chain 'F' and (resid 251 through 372 )
11X-RAY DIFFRACTION11chain 'G' and (resid 15 through 49 )
12X-RAY DIFFRACTION12chain 'G' and (resid 58 through 128 )
13X-RAY DIFFRACTION13chain 'G' and (resid 129 through 318 )
14X-RAY DIFFRACTION14chain 'G' and (resid 336 through 350 )
15X-RAY DIFFRACTION15chain 'H' and (resid 93 through 118 )
16X-RAY DIFFRACTION16chain 'H' and (resid 119 through 250 )
17X-RAY DIFFRACTION17chain 'H' and (resid 251 through 372 )
18X-RAY DIFFRACTION18chain 'A' and (resid 15 through 49 )
19X-RAY DIFFRACTION19chain 'A' and (resid 58 through 128 )
20X-RAY DIFFRACTION20chain 'A' and (resid 129 through 318 )
21X-RAY DIFFRACTION21chain 'A' and (resid 336 through 350 )
22X-RAY DIFFRACTION22chain 'B' and (resid 93 through 118 )
23X-RAY DIFFRACTION23chain 'B' and (resid 119 through 250 )
24X-RAY DIFFRACTION24chain 'B' and (resid 251 through 372)
25X-RAY DIFFRACTION25chain 'C' and (resid 15 through 49 )
26X-RAY DIFFRACTION26chain 'C' and (resid 58 through 128 )
27X-RAY DIFFRACTION27chain 'C' and (resid 129 through 318 )
28X-RAY DIFFRACTION28chain 'C' and (resid 336 through 350 )

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