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- PDB-6gg3: Crystal structure of M2 PYK in complex with Alanine. -

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Basic information

Entry
Database: PDB / ID: 6gg3
TitleCrystal structure of M2 PYK in complex with Alanine.
ComponentsPyruvate kinase PKM
KeywordsTRANSFERASE / Glycolysis / Pyruvate Kinase Activity
Function / homology
Function and homology information


pyruvate kinase / pyruvate kinase activity / histone H3T11 kinase activity / programmed cell death / Pyruvate metabolism / positive regulation of cytoplasmic translation / canonical glycolysis / Glycolysis / positive regulation of sprouting angiogenesis / potassium ion binding ...pyruvate kinase / pyruvate kinase activity / histone H3T11 kinase activity / programmed cell death / Pyruvate metabolism / positive regulation of cytoplasmic translation / canonical glycolysis / Glycolysis / positive regulation of sprouting angiogenesis / potassium ion binding / rough endoplasmic reticulum / Regulation of pyruvate metabolism / glycolytic process / non-specific protein-tyrosine kinase / cellular response to insulin stimulus / MHC class II protein complex binding / extracellular vesicle / : / protein tyrosine kinase activity / secretory granule lumen / vesicle / ficolin-1-rich granule lumen / transcription coactivator activity / non-specific serine/threonine protein kinase / cilium / cadherin binding / intracellular membrane-bounded organelle / mRNA binding / Neutrophil degranulation / magnesium ion binding / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / mitochondrion / RNA binding / extracellular exosome / extracellular region / ATP binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Pyruvate kinase, C-terminal domain / Pyruvate Kinase; Chain: A, domain 1 / Pyruvate kinase, active site / Pyruvate kinase active site signature. / Pyruvate kinase / Pyruvate kinase, barrel / Pyruvate kinase, insert domain superfamily / Pyruvate kinase, barrel domain / Pyruvate kinase, C-terminal / Pyruvate kinase, C-terminal domain superfamily ...Pyruvate kinase, C-terminal domain / Pyruvate Kinase; Chain: A, domain 1 / Pyruvate kinase, active site / Pyruvate kinase active site signature. / Pyruvate kinase / Pyruvate kinase, barrel / Pyruvate kinase, insert domain superfamily / Pyruvate kinase, barrel domain / Pyruvate kinase, C-terminal / Pyruvate kinase, C-terminal domain superfamily / Pyruvate kinase, alpha/beta domain / Pyruvate kinase-like, insert domain superfamily / Phosphoenolpyruvate-binding domains / Pyruvate kinase-like domain superfamily / Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily / TIM Barrel / Alpha-Beta Barrel / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ALANINE / PHOSPHATE ION / Pyruvate kinase PKM
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.72 Å
AuthorsMcNae, I.W. / Yuan, M. / Walkinshaw, M.D.
CitationJournal: Biochem.J. / Year: 2018
Title: An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor.
Authors: Yuan, M. / McNae, I.W. / Chen, Y. / Blackburn, E.A. / Wear, M.A. / Michels, P.A.M. / Fothergill-Gilmore, L.A. / Hupp, T. / Walkinshaw, M.D.
History
DepositionMay 2, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 4, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pyruvate kinase PKM
B: Pyruvate kinase PKM
C: Pyruvate kinase PKM
D: Pyruvate kinase PKM
E: Pyruvate kinase PKM
F: Pyruvate kinase PKM
G: Pyruvate kinase PKM
H: Pyruvate kinase PKM
I: Pyruvate kinase PKM
J: Pyruvate kinase PKM
K: Pyruvate kinase PKM
L: Pyruvate kinase PKM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)724,37935
Polymers722,25912
Non-polymers2,12023
Water00
1
A: Pyruvate kinase PKM
B: Pyruvate kinase PKM
C: Pyruvate kinase PKM
D: Pyruvate kinase PKM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)241,40011
Polymers240,7534
Non-polymers6477
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15870 Å2
ΔGint-105 kcal/mol
Surface area72740 Å2
MethodPISA
2
E: Pyruvate kinase PKM
F: Pyruvate kinase PKM
G: Pyruvate kinase PKM
H: Pyruvate kinase PKM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)241,48912
Polymers240,7534
Non-polymers7368
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15610 Å2
ΔGint-106 kcal/mol
Surface area72590 Å2
MethodPISA
3
I: Pyruvate kinase PKM
J: Pyruvate kinase PKM
K: Pyruvate kinase PKM
L: Pyruvate kinase PKM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)241,48912
Polymers240,7534
Non-polymers7368
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15230 Å2
ΔGint-107 kcal/mol
Surface area65390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)160.722, 199.364, 243.234
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28I
19A
29J
110A
210K
111A
211L
112B
212C
113B
213D
114B
214E
115B
215F
116B
216G
117B
217H
118B
218I
119B
219J
120B
220K
121B
221L
122C
222D
123C
223E
124C
224F
125C
225G
126C
226H
127C
227I
128C
228J
129C
229K
130C
230L
131D
231E
132D
232F
133D
233G
134D
234H
135D
235I
136D
236J
137D
237K
138D
238L
139E
239F
140E
240G
141E
241H
142E
242I
143E
243J
144E
244K
145E
245L
146F
246G
147F
247H
148F
248I
149F
249J
150F
250K
151F
251L
152G
252H
153G
253I
154G
254J
155G
255K
156G
256L
157H
257I
158H
258J
159H
259K
160H
260L
161I
261J
162I
262L
163J
263L
164K
264L

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ILEILEVALVALAA13 - 53033 - 550
21ILEILEVALVALBB13 - 53033 - 550
12ILEILEVALVALAA13 - 53033 - 550
22ILEILEVALVALCC13 - 53033 - 550
13ILEILEPROPROAA13 - 53133 - 551
23ILEILEPROPRODD13 - 53133 - 551
14ILEILEPROPROAA13 - 53133 - 551
24ILEILEPROPROEE13 - 53133 - 551
15ILEILEVALVALAA13 - 53033 - 550
25ILEILEVALVALFF13 - 53033 - 550
16ILEILEVALVALAA13 - 53033 - 550
26ILEILEVALVALGG13 - 53033 - 550
17ILEILEVALVALAA13 - 53033 - 550
27ILEILEVALVALHH13 - 53033 - 550
18ILEILEVALVALAA13 - 53033 - 550
28ILEILEVALVALII13 - 53033 - 550
19ILEILEVALVALAA13 - 53033 - 550
29ILEILEVALVALJJ13 - 53033 - 550
110ILEILEPROPROAA13 - 53133 - 551
210ILEILEPROPROKK13 - 53133 - 551
111ILEILEVALVALAA13 - 53033 - 550
211ILEILEVALVALLL13 - 53033 - 550
112ALAALAPROPROBB8 - 53128 - 551
212ALAALAPROPROCC8 - 53128 - 551
113ALAALAPROPROBB8 - 53128 - 551
213ALAALAPROPRODD8 - 53128 - 551
114ALAALAPROPROBB8 - 53128 - 551
214ALAALAPROPROEE8 - 53128 - 551
115ALAALAPROPROBB8 - 53128 - 551
215ALAALAPROPROFF8 - 53128 - 551
116ALAALAPROPROBB8 - 53128 - 551
216ALAALAPROPROGG8 - 53128 - 551
117ALAALAPROPROBB8 - 53128 - 551
217ALAALAPROPROHH8 - 53128 - 551
118ILEILEVALVALBB13 - 53033 - 550
218ILEILEVALVALII13 - 53033 - 550
119ILEILEVALVALBB13 - 53033 - 550
219ILEILEVALVALJJ13 - 53033 - 550
120ALAALAPROPROBB8 - 53128 - 551
220ALAALAPROPROKK8 - 53128 - 551
121ALAALAPROPROBB8 - 53128 - 551
221ALAALAPROPROLL8 - 53128 - 551
122ALAALAPROPROCC8 - 53128 - 551
222ALAALAPROPRODD8 - 53128 - 551
123ALAALAPROPROCC8 - 53128 - 551
223ALAALAPROPROEE8 - 53128 - 551
124ALAALAPROPROCC8 - 53128 - 551
224ALAALAPROPROFF8 - 53128 - 551
125ALAALAPROPROCC8 - 53128 - 551
225ALAALAPROPROGG8 - 53128 - 551
126ALAALAPROPROCC8 - 53128 - 551
226ALAALAPROPROHH8 - 53128 - 551
127ILEILEPROPROCC13 - 53133 - 551
227ILEILEPROPROII13 - 53133 - 551
128ILEILEPROPROCC13 - 53133 - 551
228ILEILEPROPROJJ13 - 53133 - 551
129ALAALAPROPROCC8 - 53128 - 551
229ALAALAPROPROKK8 - 53128 - 551
130ALAALAPROPROCC8 - 53128 - 551
230ALAALAPROPROLL8 - 53128 - 551
131GLUGLUPROPRODD7 - 53127 - 551
231GLUGLUPROPROEE7 - 53127 - 551
132ALAALAPROPRODD8 - 53128 - 551
232ALAALAPROPROFF8 - 53128 - 551
133ALAALAPROPRODD8 - 53128 - 551
233ALAALAPROPROGG8 - 53128 - 551
134ALAALAPROPRODD8 - 53128 - 551
234ALAALAPROPROHH8 - 53128 - 551
135ILEILEPROPRODD13 - 53133 - 551
235ILEILEPROPROII13 - 53133 - 551
136ILEILEPROPRODD13 - 53133 - 551
236ILEILEPROPROJJ13 - 53133 - 551
137ALAALAPROPRODD8 - 53128 - 551
237ALAALAPROPROKK8 - 53128 - 551
138ALAALAPROPRODD8 - 53128 - 551
238ALAALAPROPROLL8 - 53128 - 551
139ALAALAPROPROEE8 - 53128 - 551
239ALAALAPROPROFF8 - 53128 - 551
140ALAALAPROPROEE8 - 53128 - 551
240ALAALAPROPROGG8 - 53128 - 551
141ALAALAPROPROEE8 - 53128 - 551
241ALAALAPROPROHH8 - 53128 - 551
142ILEILEPROPROEE13 - 53133 - 551
242ILEILEPROPROII13 - 53133 - 551
143ILEILEPROPROEE13 - 53133 - 551
243ILEILEPROPROJJ13 - 53133 - 551
144ALAALAPROPROEE8 - 53128 - 551
244ALAALAPROPROKK8 - 53128 - 551
145ALAALAPROPROEE8 - 53128 - 551
245ALAALAPROPROLL8 - 53128 - 551
146ALAALAPROPROFF8 - 53128 - 551
246ALAALAPROPROGG8 - 53128 - 551
147ALAALAPROPROFF8 - 53128 - 551
247ALAALAPROPROHH8 - 53128 - 551
148ILEILEVALVALFF13 - 53033 - 550
248ILEILEVALVALII13 - 53033 - 550
149ILEILEVALVALFF13 - 53033 - 550
249ILEILEVALVALJJ13 - 53033 - 550
150ALAALAPROPROFF8 - 53128 - 551
250ALAALAPROPROKK8 - 53128 - 551
151ALAALAPROPROFF8 - 53128 - 551
251ALAALAPROPROLL8 - 53128 - 551
152ALAALAPROPROGG8 - 53128 - 551
252ALAALAPROPROHH8 - 53128 - 551
153ILEILEVALVALGG13 - 53033 - 550
253ILEILEVALVALII13 - 53033 - 550
154ILEILEVALVALGG13 - 53033 - 550
254ILEILEVALVALJJ13 - 53033 - 550
155ALAALAPROPROGG8 - 53128 - 551
255ALAALAPROPROKK8 - 53128 - 551
156ALAALAPROPROGG8 - 53128 - 551
256ALAALAPROPROLL8 - 53128 - 551
157ILEILEPROPROHH13 - 53133 - 551
257ILEILEPROPROII13 - 53133 - 551
158ILEILEPROPROHH13 - 53133 - 551
258ILEILEPROPROJJ13 - 53133 - 551
159ALAALAPROPROHH8 - 53128 - 551
259ALAALAPROPROKK8 - 53128 - 551
160ALAALAPROPROHH8 - 53128 - 551
260ALAALAPROPROLL8 - 53128 - 551
161ILEILEPROPROII13 - 53133 - 551
261ILEILEPROPROJJ13 - 53133 - 551
162ILEILEVALVALII13 - 53033 - 550
262ILEILEVALVALLL13 - 53033 - 550
163ILEILEVALVALJJ13 - 53033 - 550
263ILEILEVALVALLL13 - 53033 - 550
164ALAALAPROPROKK8 - 53128 - 551
264ALAALAPROPROLL8 - 53128 - 551

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64

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Components

#1: Protein
Pyruvate kinase PKM / Cytosolic thyroid hormone-binding protein / CTHBP / Opa-interacting protein 3 / OIP-3 / Pyruvate ...Cytosolic thyroid hormone-binding protein / CTHBP / Opa-interacting protein 3 / OIP-3 / Pyruvate kinase 2/3 / Pyruvate kinase muscle isozyme / Thyroid hormone-binding protein 1 / THBP1 / Tumor M2-PK / p58


Mass: 60188.250 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PKM, OIP3, PK2, PK3, PKM2 / Production host: Escherichia coli (E. coli) / References: UniProt: P14618, pyruvate kinase
#2: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: PO4
#3: Chemical
ChemComp-ALA / ALANINE


Type: L-peptide linking / Mass: 89.093 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C3H7NO2

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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: 2.7 Å3/Da / Density % sol: 54.41 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop
Details: 10-16% PEG 3350, 100 mM sodium Cacodylate, 50 mM MgCl2, 100 mM KCl
PH range: 7.2-7.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97624 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: May 4, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97624 Å / Relative weight: 1
ReflectionResolution: 3.72→199.3 Å / Num. obs: 82644 / % possible obs: 95.3 % / Redundancy: 4.2 % / Net I/σ(I): 7.5
Reflection shellResolution: 3.72→3.82 Å

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Processing

Software
NameVersionClassification
REFMAC5.8.0189refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4fxj

4fxj


Resolution: 3.72→154.19 Å / Cor.coef. Fo:Fc: 0.919 / Cor.coef. Fo:Fc free: 0.915 / SU ML: 0.571 / Cross valid method: THROUGHOUT / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24879 3932 5 %RANDOM
Rwork0.2196 ---
obs0.22105 74293 94.65 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--2.47 Å20 Å20 Å2
2--6.3 Å2-0 Å2
3----3.84 Å2
Refinement stepCycle: 1 / Resolution: 3.72→154.19 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms45961 0 126 0 46087
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.01946814
X-RAY DIFFRACTIONr_bond_other_d0.0030.0245322
X-RAY DIFFRACTIONr_angle_refined_deg1.2991.97163242
X-RAY DIFFRACTIONr_angle_other_deg0.9223104970
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.99555981
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.9923.8211942
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.935158414
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.19215368
X-RAY DIFFRACTIONr_chiral_restr0.0720.27283
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02151824
X-RAY DIFFRACTIONr_gen_planes_other0.0010.029036
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.1218.80824020
X-RAY DIFFRACTIONr_mcbond_other3.1218.80824019
X-RAY DIFFRACTIONr_mcangle_it5.39413.21129969
X-RAY DIFFRACTIONr_mcangle_other5.39313.21129970
X-RAY DIFFRACTIONr_scbond_it2.7419.08822794
X-RAY DIFFRACTIONr_scbond_other2.7419.08822794
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.92813.52533274
X-RAY DIFFRACTIONr_long_range_B_refined8.23749269
X-RAY DIFFRACTIONr_long_range_B_other8.23749270
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A319600.04
12B319600.04
21A317900.03
22C317900.03
31A313840.03
32D313840.03
41A291820.03
42E291820.03
51A319680.03
52F319680.03
61A319900.03
62G319900.03
71A316980.04
72H316980.04
81A254080.04
82I254080.04
91A255280.04
92J255280.04
101A315200.04
102K315200.04
111A318620.04
112L318620.04
121B321640.03
122C321640.03
131B317040.03
132D317040.03
141B294740.03
142E294740.03
151B322000.04
152F322000.04
161B322580.04
162G322580.04
171B320380.04
172H320380.04
181B255340.04
182I255340.04
191B254420.04
192J254420.04
201B316400.04
202K316400.04
211B322600.03
212L322600.03
221C316260.03
222D316260.03
231C294080.03
232E294080.03
241C321700.02
242F321700.02
251C321580.03
252G321580.03
261C319440.04
262H319440.04
271C255180.04
272I255180.04
281C255100.05
282J255100.05
291C316700.04
292K316700.04
301C320020.03
302L320020.03
311D295720.03
312E295720.03
321D316320.04
322F316320.04
331D316620.04
332G316620.04
341D316280.03
342H316280.03
351D258740.04
352I258740.04
361D258200.04
362J258200.04
371D310440.04
372K310440.04
381D315940.03
382L315940.03
391E294380.04
392F294380.04
401E295140.03
402G295140.03
411E295440.03
412H295440.03
421E258860.04
422I258860.04
431E258840.04
432J258840.04
441E288920.04
442K288920.04
451E294560.03
452L294560.03
461F324360.03
462G324360.03
471F320500.04
472H320500.04
481F254160.05
482I254160.05
491F254720.04
492J254720.04
501F318440.03
502K318440.03
511F322500.03
512L322500.03
521G321000.04
522H321000.04
531G254380.05
532I254380.05
541G254740.04
542J254740.04
551G318360.03
552K318360.03
561G322540.04
562L322540.04
571H256060.04
572I256060.04
581H256460.04
582J256460.04
591H314840.04
592K314840.04
601H321220.04
602L321220.04
611I262140.03
612J262140.03
621I255000.04
622L255000.04
631J255100.04
632L255100.04
641K316860.04
642L316860.04
LS refinement shellResolution: 3.72→3.817 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.362 315 -
Rwork0.338 5457 -
obs--95.45 %
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)
10.42060.25650.59340.75160.19591.23590.1061-0.18320.0225-0.01940.0446-0.0910.2993-0.3247-0.15070.725-0.19750.0090.2414-0.00850.535834.7365395.688771.7042
20.18780.1432-0.38930.6272-0.29661.7346-0.0266-0.00880.07320.03430.1665-0.2151-0.2051-0.7921-0.13990.48550.1622-0.03890.7903-0.0620.501111.5398422.969564.2081
30.5428-0.1675-0.32480.87940.42890.34250.15450.2550.0548-0.0649-0.06840.0021-0.0295-0.1156-0.0860.59490.0609-0.01980.3978-0.00850.582729.3001411.43165.8343
40.9417-0.7420.48640.7641-0.50760.83290.48580.3009-0.2329-0.1334-0.37070.32110.3230.1965-0.1150.90220.0062-0.1920.2048-0.28280.830621.214376.780914.8261
50.2810.1422-0.38970.4452-0.26671.05630.0792-0.17990.06320.0835-0.12690.0097-0.14930.16590.04770.6449-0.112-0.01110.2246-0.06540.649178.9229410.648552.4253
60.6456-0.2439-0.25570.2699-0.01560.84370.1491-0.04780.1627-0.0058-0.0923-0.157-0.0998-0.0626-0.05680.620.01790.07930.11150.04130.770373.0483420.881717.1255
70.4047-0.4144-0.05350.9187-0.21890.2975-0.03760.0535-0.0006-0.0559-0.06910.03350.1789-0.04530.10670.82630.05830.05510.0386-0.0220.672591.2149362.33047.8796
80.81440.36780.20860.38540.42840.8326-0.0953-0.0061-0.08650.1297-0.0266-0.00230.4001-0.02310.12190.9742-0.05690.16640.0069-0.02190.661165.7526355.321733.8529
90.61450.1470.07380.31680.19760.91910.1104-0.308-0.2763-0.0629-0.172-0.3270.148-0.06310.06160.54250.0279-0.06280.21440.33751.1305130.8678375.473228.2148
100.39280.3816-0.05650.76350.25470.52460.3383-0.4504-0.26360.0888-0.5387-0.1884-0.1070.10820.20040.5153-0.2986-0.14930.66840.31620.727130.4979406.144654.4306
111.03630.22260.00740.26030.0281.1451-0.0278-0.05160.0643-0.1161-0.06470.1428-0.15770.09210.09260.5902-0.0483-0.04590.11270.11630.7519143.7272436.87248.1561
120.62070.12630.05180.4376-0.12550.4113-0.0780.0177-0.0591-0.21590.11830.02370.08150.0294-0.04030.5939-0.0696-0.06460.10260.10210.8388119.514416.0703-9.8741
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A13 - 602
2X-RAY DIFFRACTION2B8 - 602
3X-RAY DIFFRACTION3C8 - 602
4X-RAY DIFFRACTION4D6 - 602
5X-RAY DIFFRACTION5E7 - 602
6X-RAY DIFFRACTION6F8 - 602
7X-RAY DIFFRACTION7G8 - 602
8X-RAY DIFFRACTION8H8 - 602
9X-RAY DIFFRACTION9I13 - 602
10X-RAY DIFFRACTION10J13 - 602
11X-RAY DIFFRACTION11K8 - 602
12X-RAY DIFFRACTION12L8 - 602

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