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- PDB-4cff: Structure of full length human AMPK in complex with a small molec... -

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Basic information

Entry
Database: PDB / ID: 4cff
TitleStructure of full length human AMPK in complex with a small molecule activator, a thienopyridone derivative (A-769662)
Components
  • (5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT ...) x 2
  • 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2
KeywordsTRANSFERASE / NUCLEOTIDE-BINDING / STAUROSPORINE-BINDING / SERINE/THREONINE-PROTEIN KINASE / ACTIVATOR / CARBOHYDRATE BINDING MODULE (CBM)
Function / homology
Function and homology information


nail development / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity / regulation of stress granule assembly / AMPK inhibits chREBP transcriptional activation activity / histone H2BS36 kinase activity / cAMP-dependent protein kinase regulator activity / AMP-activated protein kinase activity / lipid droplet disassembly / Lipophagy ...nail development / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity / regulation of stress granule assembly / AMPK inhibits chREBP transcriptional activation activity / histone H2BS36 kinase activity / cAMP-dependent protein kinase regulator activity / AMP-activated protein kinase activity / lipid droplet disassembly / Lipophagy / regulation of carbon utilization / import into nucleus / nucleotide-activated protein kinase complex / negative regulation of hepatocyte apoptotic process / Energy dependent regulation of mTOR by LKB1-AMPK / Carnitine shuttle / protein kinase regulator activity / negative regulation of TOR signaling / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / Nuclear events mediated by NFE2L2 / regulation of glycolytic process / cAMP-dependent protein kinase activity / protein localization to lipid droplet / negative regulation of tubulin deacetylation / AMP binding / Macroautophagy / cholesterol biosynthetic process / lipid biosynthetic process / response to muscle activity / positive regulation of protein kinase activity / positive regulation of macroautophagy / regulation of macroautophagy / fatty acid homeostasis / cellular response to nutrient levels / cellular response to glucose starvation / energy homeostasis / Activation of AMPK downstream of NMDARs / positive regulation of protein localization / negative regulation of TORC1 signaling / positive regulation of gluconeogenesis / protein serine/threonine/tyrosine kinase activity / positive regulation of autophagy / cellular response to calcium ion / regulation of microtubule cytoskeleton organization / positive regulation of glycolytic process / TP53 Regulates Metabolic Genes / Translocation of SLC2A4 (GLUT4) to the plasma membrane / cellular response to glucose stimulus / regulation of circadian rhythm / ADP binding / autophagy / cellular response to xenobiotic stimulus / Wnt signaling pathway / cytoplasmic stress granule / fatty acid biosynthetic process / rhythmic process / glucose homeostasis / cellular response to prostaglandin E stimulus / positive regulation of cold-induced thermogenesis / cellular response to oxidative stress / spermatogenesis / Regulation of TP53 Activity through Phosphorylation / protein phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / regulation of cell cycle / nuclear speck / ciliary basal body / axon / negative regulation of gene expression / protein serine kinase activity / neuronal cell body / protein serine/threonine kinase activity / dendrite / chromatin binding / protein kinase binding / negative regulation of apoptotic process / protein-containing complex binding / Golgi apparatus / signal transduction / nucleoplasm / ATP binding / metal ion binding / nucleus / membrane / cytoplasm / cytosol
Similarity search - Function
PRKAA2, UBA-like autoinhibitory domain / 5'-AMP-activated protein kinase catalytic subunit alpha-2, C-terminal / Kinase associated domain 1, KA1 / : / AMP-activated protein kinase, alpha subunit, autoinhibitory domain / : / Association with the SNF1 complex (ASC) domain / ASC domain superfamily / : / 5'-AMP-activated protein kinase beta subunit, interaction domain ...PRKAA2, UBA-like autoinhibitory domain / 5'-AMP-activated protein kinase catalytic subunit alpha-2, C-terminal / Kinase associated domain 1, KA1 / : / AMP-activated protein kinase, alpha subunit, autoinhibitory domain / : / Association with the SNF1 complex (ASC) domain / ASC domain superfamily / : / 5'-AMP-activated protein kinase beta subunit, interaction domain / 5'-AMP-activated protein kinase beta subunit, interation domain / AMPK, C-terminal adenylate sensor domain / Adenylate sensor of SNF1-like protein kinase / AMP-activated protein kinase, glycogen-binding domain / Glycogen recognition site of AMP-activated protein kinase / KA1 domain/Ssp2, C-terminal / TATA-Binding Protein / Domain in cystathionine beta-synthase and other proteins. / CBS domain superfamily / CBS domain / CBS domain / CBS domain profile. / Immunoglobulin E-set / 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. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / Chem-C1V / STAUROSPORINE / 5'-AMP-activated protein kinase subunit gamma-1 / 5'-AMP-activated protein kinase catalytic subunit alpha-2 / 5'-AMP-activated protein kinase subunit beta-1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.924 Å
AuthorsXiao, B. / Sanders, M.J. / Carmena, D. / Bright, N.J. / Haire, L.F. / Underwood, E. / Patel, B.R. / Heath, R.B. / Walker, P.A. / Hallen, S. ...Xiao, B. / Sanders, M.J. / Carmena, D. / Bright, N.J. / Haire, L.F. / Underwood, E. / Patel, B.R. / Heath, R.B. / Walker, P.A. / Hallen, S. / Giordanetto, F. / Martin, S.R. / Carling, D. / Gamblin, S.J.
CitationJournal: Nat.Commun. / Year: 2013
Title: Structural Basis of Ampk Regulation by Small Molecule Activators.
Authors: Xiao, B. / Sanders, M.J. / Carmena, D. / Bright, N.J. / Haire, L.F. / Underwood, E. / Patel, B.R. / Heath, R.B. / Walker, P.A. / Hallen, S. / Giordanetto, F. / Martin, S.R. / Carling, D. / Gamblin, S.J.
History
DepositionNov 14, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 25, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 8, 2014Group: Database references
Revision 1.2Feb 12, 2014Group: Data collection / Other / Refinement description
Revision 1.3May 8, 2019Group: Data collection / Derived calculations ...Data collection / Derived calculations / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / struct_conn
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Oct 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: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2
B: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1
C: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2
D: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1
E: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1
F: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)272,49414
Polymers269,4516
Non-polymers3,0438
Water00
1
C: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2
D: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1
F: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,2477
Polymers134,7263
Non-polymers1,5214
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15440 Å2
ΔGint-88.9 kcal/mol
Surface area39230 Å2
MethodPISA
2
A: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2
B: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1
E: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,2477
Polymers134,7263
Non-polymers1,5214
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15770 Å2
ΔGint-90.7 kcal/mol
Surface area40700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.019, 134.787, 141.286
Angle α, β, γ (deg.)90.00, 93.04, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AC

#1: Protein 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2 / AMPK SUBUNIT ALPHA-2 / ACETYL-COA CARBOXYLASE KINASE / ACACA KINASE / HYDROXYMETHYLGLUTARYL-COA ...AMPK SUBUNIT ALPHA-2 / ACETYL-COA CARBOXYLASE KINASE / ACACA KINASE / HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE / HMGCR KINASE


Mass: 64650.977 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: A 172 THR AND C 172 THR ARE PHOSPHORYLATED. / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli)
References: UniProt: P54646, non-specific serine/threonine protein kinase, EC: 2.7.11.27, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase

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5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT ... , 2 types, 4 molecules BDEF

#2: Protein 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1 / AMPK SUBUNIT BETA-1 / AMPKB


Mass: 32448.453 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: B 108 SER AND D 108 SER ARE PHOSPHORYLATED. / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q9Y478
#3: Protein 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1 / AMPK GAMMA1 / AMPK SUBUNIT GAMMA-1 / AMPKG


Mass: 37626.289 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P54619

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Non-polymers , 3 types, 8 molecules

#4: Chemical ChemComp-STU / STAUROSPORINE


Mass: 466.531 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C28H26N4O3 / Comment: antibiotic*YM
#5: Chemical ChemComp-C1V / 3-[4-(2-hydroxyphenyl)phenyl]-4-oxidanyl-6-oxidanylidene-7H-thieno[2,3-b]pyridine-5-carbonitrile


Mass: 360.386 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H12N2O3S
#6: Chemical
ChemComp-AMP / ADENOSINE MONOPHOSPHATE


Mass: 347.221 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.7 Å3/Da / Density % sol: 54 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop
Details: CRYSTALS WERE GROWN BY THE HANGING DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 13% PEG3350, 0.1M MGCL2, 1% GLUCOSE, 0.15% CAPB IN 0.1M IMIDAZOLE AT PH 6.2.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92
DetectorType: DECTRIS PIXEL / Detector: PIXEL
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 3.92→20 Å / Num. obs: 23906 / % possible obs: 95 % / Redundancy: 3.2 % / Biso Wilson estimate: 124.87 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.8
Reflection shellResolution: 3.92→4.14 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.2 / % possible all: 83

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8.2_1309)refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2Y94, 2F15

2y94
PDB Unreleased entry

2f15


Resolution: 3.924→19.934 Å / SU ML: 0.5 / σ(F): 1.35 / Phase error: 27.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2637 1207 5.1 %
Rwork0.2082 --
obs0.2109 23906 94.1 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 87.9 Å2
Refinement stepCycle: LAST / Resolution: 3.924→19.934 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14270 0 214 0 14484
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00314842
X-RAY DIFFRACTIONf_angle_d0.68420166
X-RAY DIFFRACTIONf_dihedral_angle_d11.1665436
X-RAY DIFFRACTIONf_chiral_restr0.0482285
X-RAY DIFFRACTIONf_plane_restr0.0032489
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.9235-4.07930.30411130.2791953X-RAY DIFFRACTION73
4.0793-4.26320.28691150.25622374X-RAY DIFFRACTION89
4.2632-4.48560.27611240.23212536X-RAY DIFFRACTION94
4.4856-4.7630.28471440.21192579X-RAY DIFFRACTION97
4.763-5.1250.25411680.19692602X-RAY DIFFRACTION99
5.125-5.63020.24441330.21352605X-RAY DIFFRACTION97
5.6302-6.42090.31691260.22522699X-RAY DIFFRACTION100
6.4209-8.00170.24431480.21682655X-RAY DIFFRACTION99
8.0017-19.93390.24431360.17162696X-RAY DIFFRACTION98
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)
14.4060.6249-0.02616.9684-0.7543.412-0.4704-0.0827-0.3324-0.41770.7473-0.15550.79240.0771-0.30950.6739-0.2262-0.08980.70170.03020.4437-17.0593-1.2573205.8037
23.7549-0.7898-0.63363.6933-1.34062.420.08160.77790.25860.08660.04650.44040.1882-0.9641-0.03040.2175-0.2275-0.04040.6232-0.01710.65-21.821116.9787187.9308
33.9551.5913-0.74761.9214-0.41866.3440.25770.2281-0.42451.4155-0.01340.4580.5848-1.7625-0.08231.5048-0.16880.30240.8495-0.2651.0671.862627.1673198.5528
41.75062.78020.64484.693-0.11394.87230.49841.70860.16350.03910.92351.5249-0.387-0.7545-0.53520.55230.03730.02761.2101-0.00911.237411.406137.6981169.8069
53.78871.12740.20441.70630.01723.4831-0.16940.9093-1.0587-1.0028-0.0654-1.06541.4321-0.80530.00110.939-0.21980.31730.7232-0.38221.11536.58422.7333167.2647
68.3053-0.1101-0.18425.86040.09874.0251-0.34220.9512-0.50520.40580.045-0.25960.8730.5050.11761.0090.08720.08820.80130.07490.8728-18.594-21.5349209.4496
70.22460.21970.22580.6242-0.04740.4159-0.0828-0.03370.2105-0.27210.2377-0.02640.0365-0.00140.57631.34240.6115-0.96120.3075-0.38831.00765.1398-12.8651169.3653
82.45460.36970.61623.39660.72792.24660.13590.50880.1751-0.2370.0817-0.2451-0.0024-0.2766-0.25350.4381-0.04690.06710.6457-0.03480.76025.293918.0662173.3354
94.22420.10792.75562.10481.85357.3572-0.5082-0.9902-0.01430.55140.0133-0.00591.0764-0.51980.63480.74990.17020.06670.3899-0.05020.489716.89627.9545193.9775
101.47191.9386-2.17765.459-2.46064.6056-0.76580.2973-0.754-0.4090.5441-1.11520.61911.28360.07590.3374-0.06560.04470.6163-0.12210.654727.802725.0144165.2613
116.88911.49260.23317.50820.60114.56970.3613-0.5499-0.17170.6005-0.4606-0.27870.24351.0904-0.08420.30280.0116-0.07380.53110.1060.357721.651627.3315188.3564
120.156-0.5816-0.53972.21351.1483.4520.5937-0.48060.41241.7836-0.55540.6346-0.612-0.0259-0.26030.9204-0.68880.00830.4173-1.34741.002227.859748.5418195.8091
137.41451.98261.43845.81831.05725.6222-0.3066-0.24490.8683-0.36610.81361.0309-1.1742-0.2532-0.27310.64120.0491-0.01880.49820.02180.592425.507646.3513166.9653
148.5146-0.4586-0.6593.83122.86475.54520.05610.23111.6656-0.63040.05660.4105-1.687-0.2102-0.24810.916-0.16680.20220.7111-0.42970.631523.531448.6711187.2248
153.3805-0.0720.35284.035-0.58061.7844-0.46270.01010.29370.31410.8461-0.5593-0.58720.1634-0.27190.80260.30990.11870.6136-0.02380.6197-52.3716-22.9806145.0356
161.9794-0.0349-0.0463.6081-0.04682.25-0.2442-0.6349-0.40420.44150.31180.7623-0.1315-0.8683-0.03770.5640.42830.041.01240.2140.7101-58.793-42.4757160.4333
174.44890.5759-1.64941.53450.88435.4953-0.7447-0.19250.0674-0.70580.2308-0.2742-0.4767-2.2146-0.05461.16540.3015-0.19641.12280.00270.9946-33.0414-50.5351153.3778
182.709-2.4084-0.2883.98660.35490.7482-0.785-0.95610.15091.08830.38520.0063-0.0564-0.2579-0.71770.60920.98890.05271.1279-0.03520.7479-27.1152-61.7485183.7752
192.6713-1.4201-1.09522.67530.32421.3562-0.5367-0.40110.19091.16330.3025-0.2843-2.0335-0.8342-0.23691.51060.8678-0.31031.4643-0.46780.8203-35.1137-28.0283186.2517
208.27130.063-1.24736.03850.08755.1695-0.6104-1.00730.64690.540.6997-0.1536-0.8975-0.1369-0.20051.05980.1497-0.01120.73480.14960.9825-54.5692-1.5466142.8612
211.28771.31-0.24533.2498-0.00611.07150.06170.11150.2018-0.91090.2481-1.4956-0.47560.3606-0.84321.3339-0.29120.4469-0.3251-0.62121.3773-38.3416-12.5087185.4347
223.0516-0.7618-0.19831.2239-0.10222.1347-0.2398-0.5468-0.48730.71260.53220.1799-0.1403-1.0347-0.19480.74110.5774-0.10330.9211-0.01370.7812-34.2424-42.9845179.296
231.3363-0.2614-0.95080.9244-0.14762.2683-0.46250.31480.035-0.2684-0.3413-0.1057-0.35060.1154-0.92861.03450.5673-0.02070.64440.13450.5338-19.1597-50.1886159.7622
241.5521-0.76661.42361.0961-2.17915.6267-0.5491-0.86860.51010.42140.2716-0.7142-1.37720.43220.82460.73640.4241-0.21030.7622-0.02610.4795-13.3443-48.2615190.2376
254.51641.0643-0.3583.446-0.60594.71530.49420.66510.0539-0.0663-0.24040.6547-0.51950.6426-0.16990.57830.2459-0.20840.6045-0.09140.5162-15.203-49.5166166.0198
261.67492.5593-1.22533.9966-2.42367.4206-0.90490.6035-1.2481-1.6342-0.348-0.50671.4210.5959-1.62751.18120.3844-0.08091.0679-0.56111.2059-6.0313-69.5252158.5451
277.2216-0.6616-0.4525.5830.1874.88180.38810.1655-0.69270.0737-0.38990.21470.60510.0319-0.2840.62550.2162-0.14940.6441-0.00940.3638-12.3501-69.19186.8859
283.8887-0.87941.13514.90811.06916.25810.375-0.3189-1.2970.3410.43450.28742.1229-0.73750.6750.79850.2694-0.1420.2696-0.40080.8132-11.6892-70.8259166.798
296.794-2.50266.34612.9677-4.28878.37040.12720.5475-0.4492-0.40420.7193-0.4666-0.0635-0.6552-0.65770.7983-0.17490.16641.0488-0.48141.016625.542343.1854178.8102
304.97653.00982.2748.4368-4.00855.41980.2777-1.20050.550.37540.07481.1384-0.1767-0.35210.28770.60730.21480.09610.4170.11010.7076-11.0074-65.4967175.442
310.6329-0.01430.38870.0052-0.05960.6380.1475-0.49690.0464-0.0062-0.44280.18750.3895-0.88110.10021.9856-0.2734-0.57871.1161-0.06540.9751-24.62534.4214201.8174
323.8965-3.7339-1.09784.65571.34751.03440.51270.3026-0.6693-0.2885-0.38930.2134-0.1445-0.30520.01130.69870.4936-0.03962.02721.01381.8797-60.4293-29.2341147.1205
332.16760.7689-0.06510.5176-0.3370.4019-0.060.28990.0988-0.12430.26930.1368-0.0468-0.0115-0.00341.4231-1.1930.19591.44360.0710.5865-24.6519-9.9544207.0205
343.1397-0.6101-0.54322.16550.38790.1326-0.5364-0.95070.19770.67330.64330.6261-0.0146-0.33490.02360.97850.3361-0.07591.3284-0.42191.3505-60.2056-14.4727143.4783
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 8:100)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 101:276)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 277:346)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 363:375)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 396:551)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 78:173)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 187:193)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 203:270)
9X-RAY DIFFRACTION9(CHAIN E AND RESID 27:47)
10X-RAY DIFFRACTION10(CHAIN E AND RESID 48:127)
11X-RAY DIFFRACTION11(CHAIN E AND RESID 128:183)
12X-RAY DIFFRACTION12(CHAIN E AND RESID 184:203)
13X-RAY DIFFRACTION13(CHAIN E AND RESID 204:274)
14X-RAY DIFFRACTION14(CHAIN E AND RESID 275:325)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 10:100)
16X-RAY DIFFRACTION16(CHAIN C AND RESID 101:276)
17X-RAY DIFFRACTION17(CHAIN C AND RESID 277:346)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 363:376)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 396:551)
20X-RAY DIFFRACTION20(CHAIN D AND RESID 78:173)
21X-RAY DIFFRACTION21(CHAIN D AND RESID 189:196)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 203:270)
23X-RAY DIFFRACTION23(CHAIN F AND RESID 27:47)
24X-RAY DIFFRACTION24(CHAIN F AND RESID 48:121)
25X-RAY DIFFRACTION25(CHAIN F AND RESID 128:183)
26X-RAY DIFFRACTION26(CHAIN F AND RESID 184:203)
27X-RAY DIFFRACTION27(CHAIN F AND RESID 204:274)
28X-RAY DIFFRACTION28(CHAIN F AND RESID 275:324)
29X-RAY DIFFRACTION29(CHAIN E AND RESID 1326:1327)
30X-RAY DIFFRACTION30(CHAIN F AND RESID 1325:1326)
31X-RAY DIFFRACTION31(CHAIN A AND RESID 1552)
32X-RAY DIFFRACTION32(CHAIN C AND RESID 1552)
33X-RAY DIFFRACTION33(CHAIN B AND RESID 1271)
34X-RAY DIFFRACTION34(CHAIN C AND RESID 1553)

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