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

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Basic information

Entry
Database: PDB / ID: 4cfe
TitleStructure of full length human AMPK in complex with a small molecule activator, a benzimidazole derivative (991)
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 / histone H2BS36 kinase activity / AMPK inhibits chREBP transcriptional activation activity / positive regulation of peptidyl-lysine acetylation / lipid droplet disassembly / Lipophagy ...nail development / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity / : / regulation of stress granule assembly / histone H2BS36 kinase activity / AMPK inhibits chREBP transcriptional activation activity / positive regulation of peptidyl-lysine acetylation / lipid droplet disassembly / Lipophagy / import into nucleus / cAMP-dependent protein kinase regulator activity / protein kinase regulator activity / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of TOR signaling / negative regulation of hepatocyte apoptotic process / Carnitine metabolism / nucleotide-activated protein kinase complex / protein localization to lipid droplet / response to muscle activity / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / Nuclear events mediated by NFE2L2 / lipid biosynthetic process / regulation of glycolytic process / cAMP-dependent protein kinase activity / negative regulation of tubulin deacetylation / Macroautophagy / AMP-activated protein kinase activity / positive regulation of protein localization / cholesterol biosynthetic process / AMP binding / cellular response to nutrient levels / positive regulation of macroautophagy / fatty acid homeostasis / regulation of macroautophagy / positive regulation of protein kinase activity / cellular response to glucose starvation / Activation of AMPK downstream of NMDARs / regulation of microtubule cytoskeleton organization / positive regulation of autophagy / energy homeostasis / negative regulation of TORC1 signaling / cellular response to calcium ion / protein serine/threonine/tyrosine kinase activity / positive regulation of glycolytic process / Translocation of SLC2A4 (GLUT4) to the plasma membrane / ADP binding / cellular response to glucose stimulus / TP53 Regulates Metabolic Genes / regulation of circadian rhythm / Wnt signaling pathway / autophagy / cytoplasmic stress granule / cellular response to prostaglandin E stimulus / fatty acid biosynthetic process / rhythmic process / cellular response to xenobiotic stimulus / glucose homeostasis / cellular response to oxidative stress / positive regulation of cold-induced thermogenesis / spermatogenesis / Regulation of TP53 Activity through Phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / nuclear speck / axon / negative regulation of gene expression / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / neuronal cell body / chromatin binding / positive regulation of gene expression / negative regulation of apoptotic process / protein kinase binding / Golgi apparatus / signal transduction / nucleoplasm / ATP binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm
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 / 5'-AMP-activated protein kinase beta subunit, interation domain / AMPK, C-terminal adenylate sensor 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 / CBS domain superfamily / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain / CBS domain profile. / Immunoglobulin E-set / 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. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-992 / ADENOSINE MONOPHOSPHATE / 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: 3.023 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 / Refinement description
Revision 1.3May 8, 2019Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / struct_conn
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Dec 20, 2023Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / 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

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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)273,33216
Polymers269,4516
Non-polymers3,88010
Water55831
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)136,6668
Polymers134,7263
Non-polymers1,9405
Water543
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)136,6668
Polymers134,7263
Non-polymers1,9405
Water543
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)76.030, 134.141, 140.558
Angle α, β, γ (deg.)90.00, 92.42, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(0.988, 0.07, 0.135), (0.062, -0.996, 0.062), (0.139, -0.053, -0.989)-175.2662, -10.40475, 1953.21326
2given(0.992, 0.046, 0.12), (0.039, -0.997, 0.064), (0.123, -0.058, -0.991)-160.10246, 0.78274, 1964.40759
3given(0.992, 0.074, 0.098), (0.071, -0.997, 0.034), (0.1, -0.027, -0.995)-139.79034, 13.70968, 1978.54529
4given(0.51, 0.085, 0.856), (-0.147, -0.972, 0.184), (0.848, -0.22, -0.483)-646.41418, -20.43999, 1066.29578
5given(0.994, 0.066, 0.091), (0.062, -0.997, 0.043), (0.094, -0.037, -0.995)-132.96349, 10.07762, 1983.2821
6given(0.987, 0.029, 0.158), (0.017, -0.997, 0.079), (0.16, -0.075, -0.984)-196.08771, -4.3016, 1939.13306
7given(0.985, 0.069, 0.16), (0.053, -0.993, 0.102), (0.166, -0.092, -0.982)-199.09406, -46.87558, 1934.01746

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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, [acetyl-CoA carboxylase] kinase, [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 , 4 types, 41 molecules

#4: Chemical ChemComp-STU / STAUROSPORINE / Staurosporine


Mass: 466.531 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C28H26N4O3 / Comment: anticancer, antifungal, antibiotic, alkaloid*YM
#5: Chemical ChemComp-992 / 5-[[6-chloranyl-5-(1-methylindol-5-yl)-1H-benzimidazol-2-yl]oxy]-2-methyl-benzoic acid


Mass: 431.871 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H18ClN3O3
#6: Chemical
ChemComp-AMP / ADENOSINE MONOPHOSPHATE / Adenosine monophosphate


Mass: 347.221 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 31 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE 19 RESIDUES (MSHHHHHHSSGLEVLFQGP) AT THE N-TERMINAL OF ALPHA-2 ARE EXPRESSION TAG. THE 16 ...THE 19 RESIDUES (MSHHHHHHSSGLEVLFQGP) AT THE N-TERMINAL OF ALPHA-2 ARE EXPRESSION TAG. THE 16 RESIDUES (MGLNDIFEAQKIEWHE) AT THE N- TERMINAL OF BETA-1 ARE EXPRESSION TAG

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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: 3.02→30 Å / Num. obs: 50545 / % possible obs: 93.4 % / Observed criterion σ(I): 2 / Redundancy: 2.7 % / Biso Wilson estimate: 96.99 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 21
Reflection shellResolution: 3.02→3.21 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 2.2 / % possible all: 95

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Processing

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

2y94
PDB Unreleased entry

2f15


Resolution: 3.023→19.914 Å / SU ML: 0.45 / σ(F): 1.35 / Phase error: 28.51 / Stereochemistry target values: ML
Details: K SOL IS K_OVERALL B SOL IS B_OVERALL NCS RESIDUES D189-D194 AND B190-D193: INSUFFICIENT ELECTRON DENSITY TO BUILD SIDE CHAINS. PRESENT AS A GUIDE TO VISUALISE THE DIRECTION OF THE LOOP THAT ...Details: K SOL IS K_OVERALL B SOL IS B_OVERALL NCS RESIDUES D189-D194 AND B190-D193: INSUFFICIENT ELECTRON DENSITY TO BUILD SIDE CHAINS. PRESENT AS A GUIDE TO VISUALISE THE DIRECTION OF THE LOOP THAT LINKS CBM TO REGULATORY FRAGMENT
RfactorNum. reflection% reflection
Rfree0.2529 2550 5.1 %
Rwork0.2176 --
obs0.2194 50545 92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 27.78 Å2 / ksol: 0.078 e/Å3
Displacement parametersBiso mean: 78.14 Å2
Refinement stepCycle: LAST / Resolution: 3.023→19.914 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14021 0 270 31 14322
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00214647
X-RAY DIFFRACTIONf_angle_d0.65319908
X-RAY DIFFRACTIONf_dihedral_angle_d11.5975381
X-RAY DIFFRACTIONf_chiral_restr0.0432255
X-RAY DIFFRACTIONf_plane_restr0.0032444
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0235-3.08140.35981070.36772008X-RAY DIFFRACTION70
3.0814-3.14410.37421590.33862721X-RAY DIFFRACTION95
3.1441-3.21220.31071400.32492803X-RAY DIFFRACTION97
3.2122-3.28660.34011460.31082780X-RAY DIFFRACTION96
3.2866-3.36840.31361450.29732747X-RAY DIFFRACTION97
3.3684-3.4590.32311270.28562867X-RAY DIFFRACTION97
3.459-3.56020.28371510.26252747X-RAY DIFFRACTION96
3.5602-3.67450.30051510.24462754X-RAY DIFFRACTION95
3.6745-3.80490.29231300.24242778X-RAY DIFFRACTION95
3.8049-3.95610.25041450.2252705X-RAY DIFFRACTION94
3.9561-4.13470.24841550.2072618X-RAY DIFFRACTION91
4.1347-4.35050.25091480.19072704X-RAY DIFFRACTION94
4.3505-4.61990.21271460.17962788X-RAY DIFFRACTION95
4.6199-4.97150.21541440.16692768X-RAY DIFFRACTION95
4.9715-5.46240.19281350.17392756X-RAY DIFFRACTION94
5.4624-6.23150.23181430.19332730X-RAY DIFFRACTION94
6.2315-7.77260.24971630.2082622X-RAY DIFFRACTION90
7.7726-19.91440.24531150.22392099X-RAY DIFFRACTION71
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)
13.465-0.41840.04228.93810.63373.9364-0.3024-0.17560.11280.14230.3635-0.2735-0.3834-0.1549-0.04340.41380.16750.05880.520.00590.394484.301433.6773987.0304
23.3131-0.5078-0.50254.00440.30652.7729-0.2402-0.4578-0.39830.41240.50580.66150.0632-0.7833-0.1810.43950.22380.05950.83020.20960.624477.811213.95351002.6531
34.6218-1.54171.38531.89560.94414.92380.11250.2330.3584-1.01810.12120.45550.1357-1.1926-0.20520.8080.0745-0.23140.929-0.03950.6629503.35075.7296995.1052
43.90651.9468-2.04124.76450.85588.6955-0.6049-1.04910.35680.88870.0281.3864-0.3761-0.69920.54140.65080.33530.07540.8167-0.14560.8666509.3225-5.91061025.8088
53.9734-2.3299-1.37833.70441.05710.6906-0.0176-0.4660.6380.62090.0209-0.255-1.189-0.5216-0.11281.3010.4522-0.23880.9484-0.29170.6091501.916128.12521028.2664
67.0244-0.99651.19957.15990.22594.5288-0.5771-0.37790.5520.43520.4646-0.4427-0.5541-0.00490.12440.65160.04-0.11650.51660.13790.6343482.165854.586985.192
71.4359-0.099-0.38640.24470.16130.1793-0.019-0.03810.04080.131-0.03650.09950.0629-0.04050.10421.79210.3265-0.09080.967-0.7711.4686498.621343.23371030.0457
82.0582-0.8466-0.99382.61710.26770.507-0.1423-0.22310.17310.32510.32980.146-0.2395-0.5625-0.23320.75140.4347-0.14180.8047-0.0610.5052502.540313.27961021.1786
96.1543-1.795-1.81594.84341.30545.91580.46341.03150.1622-1.2686-0.37080.1945-1.4698-0.20860.04040.67790.1808-0.09430.58180.04390.4423517.17515.8291001.5163
101.0643-0.57651.02981.9407-2.49374.4746-0.5324-0.45040.23960.57180.1503-0.7067-0.67350.45850.30550.60880.2406-0.18120.73-0.1130.4671523.47747.37641031.9462
116.4380.6575-0.34378.49591.26435.81310.00570.21330.2542-0.1568-0.2068-0.2245-0.31860.45870.13970.41230.1188-0.09370.53070.00950.3822521.22836.39181007.8025
122.41171.42050.16993.43312.29054.40620.05450.4469-1.1148-0.9941-0.0720.14110.74121.1555-0.01270.9640.48630.00111.1437-0.280.898529.7182-13.8854999.9637
136.6625-1.9095-0.31244.7808-0.89474.73080.0368-0.5868-0.61490.29430.13360.2110.85920.0786-0.17470.69590.2728-0.16270.7180.08050.5059523.9025-13.5931028.3817
147.2861-1.2278-0.21586.68270.88194.0401-0.06550.3103-1.3991-0.4443-0.116-0.0571.42720.46640.22330.82180.2435-0.040.5692-0.10220.6039524.5201-14.77721007.9897
152.11750.47890.11458.1297-0.3184.37860.0639-0.3784-0.1685-0.01980.0569-0.4960.49240.2098-0.10980.4121-0.1333-0.1040.75440.05070.4671520.261353.9471047.1633
163.0965-0.3059-0.83764.1627-0.44553.29480.150.33120.2223-0.06340.04040.28070.0034-0.7341-0.14490.2715-0.0763-0.05720.71460.01690.6193514.834671.97391029.737
173.80793.85570.39135.5623-0.36160.37811.5067-0.46030.52291.427-0.21281.4631-1.5333-1.0629-1.07571.10950.26540.40770.86530.08751.1291537.943384.72291036.2363
185.33772.44142.20356.735-1.71126.15890.71321.14931.0193-0.5992-0.61761.6453-1.8587-1.1386-0.06530.79570.33740.06190.89420.06110.8728547.418593.70411013.6911
195.0521.0411.20922.75710.73273.4985-0.321.1209-1.4664-0.67390.1788-0.62910.9977-0.18010.13320.9883-0.19760.32640.7605-0.35521.1614543.077458.3831008.5432
206.17390.367-0.13217.40060.88713.9554-0.63460.1483-0.477-0.3372-0.036-0.93831.56420.73790.53671.16870.12740.24240.82420.27720.8052517.784732.96551051.4788
211.24490.4388-0.21040.7399-1.08311.7733-0.9693-0.28790.92880.25440.0334-0.9795-1.7309-0.09430.90492.01840.2083-0.24870.6573-0.30642.0697542.896842.87261009.7653
226.84023.23450.444.69810.97786.4409-0.15180.7314-0.0706-0.56590.27130.0496-0.0471-0.6559-0.11490.36460.02360.08690.52240.08850.6091541.742973.64061014.8864
238.13151.61811.17536.41840.60498.22360.2975-1.6652-0.25521.2711-0.57190.26651.61320.17290.35870.56530.12650.09180.63250.07280.4394553.694282.72161035.7604
242.60810.7828-0.33716.1162-2.43493.5376-0.65490.4128-0.9616-0.64290.2569-0.88350.40280.43210.34460.4014-0.00620.11650.5774-0.11620.6561563.009380.94351006.0947
254.96812.32780.24132.3296-1.72055.07720.1509-0.5326-0.64380.4566-0.2816-0.2013-0.31050.68080.24140.39760.133-0.02240.58470.11070.5879558.372782.35461029.9699
262.5855-2.7837-1.9544.01112.87724.92190.771-1.24161.23761.25630.37910.2983-1.12351.7141-1.02751.0599-0.36960.14590.998-0.26110.6408564.7731103.24581037.8403
277.02022.19080.68055.68760.91165.82560.03340.31050.94-0.25040.15830.3189-1.2262-0.1389-0.12510.61550.05570.13070.45130.03910.4745562.854101.65141008.6604
282.36741.7183-0.02586.43653.09375.62640.6111-0.74480.9328-0.1302-0.40560.4237-1.3616-0.0103-0.29480.948-0.13350.21320.7025-0.17240.6836560.2954103.61841029.3625
298.24214.28670.07969.8078-7.12596.78250.10530.05011.55332.27350.08380.3249-0.87090.1586-0.11750.88450.30950.01920.7227-0.11510.704526.0024-4.59991018.1393
308.54923.2684.9045.05032.03645.68110.63261.1957-1.7974-0.9229-0.4815-0.45970.3378-1.2923-0.12450.95330.00370.15010.9911-0.27180.9137563.292593.64041019.7403
311.5594-0.5911-1.80921.58141.50552.5932-0.10620.3958-0.15240.0291-0.0701-0.2108-0.212-0.28740.14740.2360.14120.0090.5140.05580.7213476.375427.2711989.1739
325.4833-0.3214-1.58828.67484.8713.1789-0.5194-0.86031.23750.5123-0.57360.50450.5037-1.02661.08790.38050.0001-0.00650.573-0.0980.4952512.299959.58791043.8502
334.8889-0.80336.793.015-1.72489.59870.03320.34570.44930.508-0.91721.4613-0.2937-1.06530.81640.7640.29260.29110.79340.20580.9558477.039442.3623987.9151
343.3966-0.0031-2.0222.1587-0.49832.69320.0520.6291-0.56780.5515-0.76080.0205-0.1783-0.39080.70660.9074-0.3604-0.24421.11390.17470.7728513.081244.65371046.4099
35-0.03430.02140.01020.08660.05810.02270.11970.08640.1994-0.26520.141-0.0949-0.2109-0.00611.2086-0.22860.2068-0.0918-0.314-0.0747-0.1898504.163647.61121011.2281
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 363:376)
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 190:193)
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 48:122)
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 363:373)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 396:551)
20X-RAY DIFFRACTION20(CHAIN D AND RESID 78:170)
21X-RAY DIFFRACTION21(CHAIN D AND RESID 189:194)
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 275:325)
29X-RAY DIFFRACTION29(CHAIN E AND RESID 1326:1328)
30X-RAY DIFFRACTION30(CHAIN F AND RESID 1326:1328)
31X-RAY DIFFRACTION31(CHAIN A AND RESID 1552)
32X-RAY DIFFRACTION32(CHAIN C AND RESID 1552)
33X-RAY DIFFRACTION33(CHAIN A AND RESID 1553)
34X-RAY DIFFRACTION34(CHAIN C AND RESID 1553)
35X-RAY DIFFRACTION35((CHAIN A AND RESID 2001:2013) OR (CHAIN B AND RESID 2001:2006) OR (CHAIN C AND RESID 2001:2006) OR (CHAIN D AND RESID 2001) OR (CHAIN E AND RESID 2001:2002) OR (CHAIN F AND RESID 2001:2003)

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