PDB-9f0m: Crystal structure of Ta_Cel5A E133Q Y200F variant in complex with...

Basic information

• Entry: Database: PDB / ID: 9f0m
• Title: Crystal structure of Ta_Cel5A E133Q Y200F variant in complex with cellopentaose
• Components: cellulase
• Keywords: HYDROLASE / cellulase / TIM barrel
• Function / homology: glucan catabolic process / cellulase / Glycoside hydrolase, family 5 / Cellulase (glycosyl hydrolase family 5) / cellulase activity / Glycoside hydrolase superfamily / cellulase
• Biological species: Thermoascus aurantiacus ATCC 26904 (fungus)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.63 Å
• Authors: Dutoit, R.

Funding support

Belgium, 1items

Organization	Grant number	Country
Other government	BAG 20210875	Belgium

• Citation: Journal: To Be Published; Title: Crystal structure of Ta_Cel5A E133Q Y200F variant in complex with cellopentaose; Authors: Dutoit, R.

History

Deposition	Apr 17, 2024	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Apr 30, 2025	Provider: repository / Type: Initial release

Assembly

Deposited unit

A: cellulase

B: cellulase

hetero molecules

Summary:

• 69.9 kDa, 2 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	69,905	10
Polymers	67,687	2
Non-polymers	2,218	8
Water	17,006	944

1

A: cellulase

hetero molecules

Summary:

• defined by author
• Evidence: gel filtration, Ta_Cel5A eluted as a monomer using a Superdex 75 column conditioned with 50 mM Tris pH 8.0 NaCl 150 mM.
• 34.9 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	34,856	4
Polymers	33,844	1
Non-polymers	1,013	3
Water	18	1

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

2

B: cellulase

hetero molecules

Summary:

• defined by author
• 35 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	35,049	6
Polymers	33,844	1
Non-polymers	1,205	5
Water	18	1

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Unit cell

Length a, b, c (Å)	76.390, 85.420, 89.310
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P212121

Components

#1: Protein

A B cellulase

Details:

Mass: 33843.539 Da / Num. of mol.: 2 / Mutation: E133Q, Y200F
Source method: isolated from a genetically manipulated source
Details: E133Q and Y200F mutations, no tag
Source: (gene. exp.) Thermoascus aurantiacus ATCC 26904 (fungus)
Gene: eg1 / Plasmid: pET30b / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q8TG26, cellulase

#2: Polysaccharide

[C] [D] beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose

Details:

Type: oligosaccharide / Mass: 828.719 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source

Descriptor:

Descriptor	Type	Program
DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-ROH	Glycam Condensed Sequence	GMML 1.0
WURCS=2.0/1,5,4/[a2122h-1b_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1	WURCS	PDB2Glycan 1.1.0
[][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{}}}}}	LINUCS	PDB-CARE

#3: Chemical

A-501 A-502 B-501 B-502
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL

Details:

Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₃H₈O₃

#4: Chemical

B-503 B-504 ChemComp-SO4 / SULFATE ION

Details:

Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO₄

#5: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 944 / Source method: isolated from a natural source / Formula: H₂O

• Has ligand of interest: Y
• Has protein modification: Y

Experimental details

Experiment

• Experiment: Method: X-RAY DIFFRACTION / Number of used crystals: 1

Sample preparation

• Crystal: Density Matthews: 2.1 ų/Da / Density % sol: 41.5 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 ; Details: Reservoir solution: 0.1 M Tris pH 6.0, 1.3 M ammonium sulfate Drop: 2 ul of 465 uM protein mixed with 2 ul of reservoir solution, 0.2 ul cellohexaose 5 mM and 0.2 ul microseeds.

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.978565 Å
• Detector: Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 2, 2021
• Radiation: Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.978565 Å / Relative weight: 1
• Reflection: Resolution: 1.63→48.01 Å / Num. obs: 73367 / % possible obs: 99.7 % / Redundancy: 13.5 % / CC_1/2: 0.999 / R_merge(I) obs: 0.113 / R_rim(I) all: 0.118 / Net I/σ(I): 18.59

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Rmerge(I) obs	Mean I/σ(I) obs	Num. unique obs	CC1/2	Rrim(I) all	% possible all
1.63-1.67	0.981	2.64	5167	0.859	1.021	95.8
1.67-1.72	0.844	3.47	5225	0.927	0.876	100
1.72-1.77	0.706	4.45	5114	0.95	0.734	100
1.77-1.82	0.572	5.75	4985	0.969	0.594	100
1.82-1.88	0.492	6.97	4765	0.977	0.512	100
1.88-1.95	0.502	8.6	4667	0.984	0.523	100
1.95-2.02	0.304	11.82	4506	0.99	0.317	100
2.02-2.1	0.266	14.67	4327	0.994	0.277	100
2.1-2.2	0.204	17.35	4156	0.995	0.212	100
2.2-2.3	0.201	19.37	4028	0.995	0.208	100
2.3-2.43	0.15	22.01	3767	0.997	0.155	100
2.43-2.58	0.131	24.2	3602	0.997	0.136	100
2.58-2.75	0.109	27.84	3395	0.997	0.114	100
2.75-2.97	0.087	32.4	3163	0.998	0.091	100
2.97-3.26	0.071	44.47	2927	0.999	0.073	100
3.26-3.64	0.06	48.73	2668	0.999	0.062	100
3.64-4.21	0.05	48.73	2359	0.999	0.052	100
4.21-5.15	0.046	49.71	2023	0.999	0.048	100
5.15-7.29	0.048	46.87	1594	0.999	0.05	100
7.29-48.01	0.041	52.51	929	0.999	0.042	99.5

Processing

Software

Name	Version	Classification
PHENIX	1.21_5207	refinement
XSCALE	20210323	data scaling
XDS	20210323	data reduction
PHASER	2.8.3	phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.63→42.71 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 16.67 / Stereochemistry target values: ML
Details: TLS were used in refinement TLS DETAILS. NUMBER OF TLS GROUPS: 15 ORIGIN: CENTER OF MASS TLS GROUP : 1 SELECTION: chain 'A' and (resid 2 through 20 ) ORIGIN FOR THE GROUP (A): -4.6308 16.5019 -9.7772 T TENSOR T11: 0.1927 T22: 0.1642 T33: 0.2009 T12: -0.0028 T13: -0.0230 T23: -0.0098 L TENSOR L11: 0.0558 L22: 0.1118 L33: 0.3906 L12: 0.0761 L13: 0.1538 L23: 0.2250 S TENSOR S11: 0.0676 S12: -0.0957 S13: -0.1023 S21: 0.0052 S22: -0.0523 S23: -0.0398 S31: 0.1943 S32: 0.0629 S33: 0.0001 TLS GROUP : 2 SELECTION: chain 'A' and (resid 21 through 84 ) ORIGIN FOR THE GROUP (A): -7.1860 16.9285 0.6502 T TENSOR T11: 0.2073 T22: 0.1618 T33: 0.1817 T12: -0.0039 T13: -0.0150 T23: 0.0314 L TENSOR L11: 0.3000 L22: 0.6249 L33: 0.6451 L12: 0.3691 L13: -0.0577 L23: 0.2460 S TENSOR S11: 0.0705 S12: -0.0710 S13: -0.0979 S21: 0.2006 S22: -0.0545 S23: -0.0257 S31: 0.2029 S32: -0.0568 S33: 0.0002 TLS GROUP : 3 SELECTION: chain 'A' and (resid 85 through 185 ) ORIGIN FOR THE GROUP (A): -9.8970 30.8504 -9.2245 T TENSOR T11: 0.1288 T22: 0.1286 T33: 0.1582 T12: 0.0064 T13: -0.0053 T23: -0.0041 L TENSOR L11: 0.5347 L22: 0.5469 L33: 0.4977 L12: 0.1294 L13: -0.0254 L23: 0.0947 S TENSOR S11: -0.0074 S12: -0.0272 S13: 0.0215 S21: 0.0219 S22: 0.0219 S23: 0.0611 S31: 0.0155 S32: -0.0197 S33: -0.0000 TLS GROUP : 4 SELECTION: chain 'A' and (resid 186 through 246 ) ORIGIN FOR THE GROUP (A): -3.9971 23.6931 -22.8305 T TENSOR T11: 0.1541 T22: 0.1469 T33: 0.1474 T12: -0.0046 T13: -0.0016 T23: -0.0111 L TENSOR L11: 0.4427 L22: 0.2773 L33: 0.1907 L12: -0.0903 L13: 0.0798 L23: 0.0186 S TENSOR S11: -0.0181 S12: 0.0763 S13: -0.0427 S21: -0.0485 S22: 0.0337 S23: -0.0124 S31: -0.0370 S32: 0.1025 S33: -0.0000 TLS GROUP : 5 SELECTION: chain 'A' and (resid 247 through 277 ) ORIGIN FOR THE GROUP (A): 1.3258 16.6523 -22.6549 T TENSOR T11: 0.1576 T22: 0.1645 T33: 0.1747 T12: 0.0269 T13: -0.0034 T23: -0.0317 L TENSOR L11: 0.1060 L22: 0.3129 L33: 0.3345 L12: -0.0810 L13: 0.1743 L23: 0.1541 S TENSOR S11: 0.0689 S12: 0.0255 S13: -0.0700 S21: 0.0461 S22: -0.0215 S23: -0.0349 S31: 0.0282 S32: 0.2609 S33: -0.0048 TLS GROUP : 6 SELECTION: chain 'A' and (resid 278 through 305 ) ORIGIN FOR THE GROUP (A): -1.6435 5.5827 -14.6457 T TENSOR T11: 0.2525 T22: 0.1632 T33: 0.2628 T12: 0.0408 T13: -0.0276 T23: -0.0134 L TENSOR L11: 0.0894 L22: 0.1110 L33: 0.5350 L12: -0.0173 L13: -0.0790 L23: 0.2398 S TENSOR S11: -0.1228 S12: -0.0741 S13: -0.4532 S21: 0.3292 S22: -0.0291 S23: -0.1298 S31: 0.6060 S32: 0.1017 S33: -0.0071 TLS GROUP : 7 SELECTION: chain 'B' and (resid 1 through 20 ) ORIGIN FOR THE GROUP (A): -39.0059 19.4217 -34.1021 T TENSOR T11: 0.1581 T22: 0.2108 T33: 0.1867 T12: 0.0040 T13: 0.0123 T23: 0.0033 L TENSOR L11: 0.1213 L22: 0.0800 L33: 0.4310 L12: 0.0097 L13: 0.2148 L23: -0.0853 S TENSOR S11: -0.0477 S12: -0.0284 S13: -0.0893 S21: 0.0283 S22: 0.0348 S23: 0.0230 S31: 0.2385 S32: -0.1119 S33: 0.0001 TLS GROUP : 8 SELECTION: chain 'B' and (resid 21 through 52 ) ORIGIN FOR THE GROUP (A): -38.2971 14.5567 -41.5819 T TENSOR T11: 0.2010 T22: 0.1815 T33: 0.1633 T12: -0.0385 T13: 0.0020 T23: -0.0153 L TENSOR L11: 0.1575 L22: 0.1244 L33: 0.4539 L12: 0.0216 L13: 0.1372 L23: -0.2981 S TENSOR S11: 0.0047 S12: 0.0640 S13: -0.1072 S21: -0.1262 S22: 0.0048 S23: 0.0246 S31: 0.2405 S32: -0.1639 S33: 0.0021 TLS GROUP : 9 SELECTION: chain 'B' and (resid 53 through 84 ) ORIGIN FOR THE GROUP (A): -32.2682 23.2516 -48.3338 T TENSOR T11: 0.1559 T22: 0.2003 T33: 0.1564 T12: -0.0159 T13: -0.0037 T23: -0.0140 L TENSOR L11: 0.0286 L22: 0.2819 L33: 0.4686 L12: -0.0237 L13: 0.0099 L23: 0.0556 S TENSOR S11: 0.0205 S12: 0.0669 S13: 0.0035 S21: -0.1042 S22: 0.0268 S23: -0.0124 S31: 0.0817 S32: 0.0170 S33: 0.0000 TLS GROUP : 10 SELECTION: chain 'B' and (resid 85 through 138 ) ORIGIN FOR THE GROUP (A): -29.3329 29.6624 -39.7053 T TENSOR T11: 0.1144 T22: 0.1594 T33: 0.1351 T12: -0.0046 T13: -0.0051 T23: 0.0061 L TENSOR L11: 0.0166 L22: 0.3761 L33: 0.5540 L12: 0.0602 L13: 0.0178 L23: 0.3342 S TENSOR S11: -0.0070 S12: 0.0420 S13: 0.0132 S21: -0.0208 S22: 0.0348 S23: -0.0105 S31: 0.0161 S32: -0.0149 S33: 0.0000 TLS GROUP : 11 SELECTION: chain 'B' and (resid 139 through 216 ) ORIGIN FOR THE GROUP (A): -32.0807 31.2161 -27.9941 T TENSOR T11: 0.1474 T22: 0.1457 T33: 0.1441 T12: 0.0040 T13: -0.0058 T23: 0.0033 L TENSOR L11: 0.1775 L22: 0.3135 L33: 0.6299 L12: 0.3057 L13: -0.1453 L23: 0.0916 S TENSOR S11: -0.0277 S12: -0.0295 S13: 0.0266 S21: 0.1021 S22: 0.0183 S23: -0.0435 S31: -0.0580 S32: -0.0669 S33: -0.0002 TLS GROUP : 12 SELECTION: chain 'B' and (resid 217 through 231 ) ORIGIN FOR THE GROUP (A): -37.0002 30.2209 -15.3864 T TENSOR T11: 0.2437 T22: 0.2093 T33: 0.1521 T12: -0.0160 T13: 0.0262 T23: 0.0097 L TENSOR L11: 0.0280 L22: 0.0301 L33: 0.0584 L12: 0.0314 L13: 0.0515 L23: 0.0143 S TENSOR S11: 0.0678 S12: -0.1291 S13: -0.0430 S21: 0.4576 S22: -0.0824 S23: 0.0546 S31: -0.0800 S32: -0.1094 S33: 0.0000 TLS GROUP : 13 SELECTION: chain 'B' and (resid 232 through 246 ) ORIGIN FOR THE GROUP (A): -38.4898 24.4467 -23.9162 T TENSOR T11: 0.2194 T22: 0.1712 T33: 0.1654 T12: -0.0126 T13: 0.0155 T23: -0.0070 L TENSOR L11: 0.0700 L22: 0.0398 L33: 0.1241 L12: 0.0597 L13: -0.0675 L23: -0.0260 S TENSOR S11: 0.0417 S12: -0.0871 S13: 0.0069 S21: 0.1881 S22: -0.1035 S23: 0.1380 S31: 0.0575 S32: -0.1808 S33: -0.0025 TLS GROUP : 14 SELECTION: chain 'B' and (resid 247 through 263 ) ORIGIN FOR THE GROUP (A): -43.8889 19.5534 -16.1059 T TENSOR T11: 0.2575 T22: 0.2404 T33: 0.1739 T12: -0.0431 T13: 0.0336 T23: -0.0024 L TENSOR L11: 0.0283 L22: 0.0270 L33: 0.0740 L12: -0.0218 L13: -0.0114 L23: -0.0163 S TENSOR S11: -0.0132 S12: -0.0626 S13: -0.0430 S21: 0.2340 S22: -0.0338 S23: 0.0866 S31: 0.1874 S32: -0.3468 S33: -0.0001 TLS GROUP : 15 SELECTION: chain 'B' and (resid 264 through 305 ) ORIGIN FOR THE GROUP (A): -42.0222 13.2385 -28.5887 T TENSOR T11: 0.2185 T22: 0.1841 T33: 0.1706 T12: -0.0530 T13: -0.0042 T23: 0.0118 L TENSOR L11: 0.1772 L22: 0.1531 L33: 0.5268 L12: 0.0156 L13: 0.1172 L23: -0.2397 S TENSOR S11: 0.0627 S12: 0.0128 S13: -0.0739 S21: -0.1086 S22: -0.0308 S23: 0.0591 S31: 0.2241 S32: -0.2015 S33: 0.0000

	Rfactor	Num. reflection	% reflection
Rfree	0.1744	3665	5 %
Rwork	0.1428	-	-
obs	0.1444	73338	99.65 %

• Solvent computation: Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
• Displacement parameters: B_iso mean: 19.18 Ų

Refinement step

Cycle: LAST / Resolution: 1.63→42.71 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	4749	0	146	944	5839

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	5245
X-RAY DIFFRACTION	f_angle_d	0.919	7215
X-RAY DIFFRACTION	f_dihedral_angle_d	13.856	2068
X-RAY DIFFRACTION	f_chiral_restr	0.06	810
X-RAY DIFFRACTION	f_plane_restr	0.008	917

LS refinement shell

Resolution (Å)	Rfactor Rfree	Num. reflection Rfree	Rfactor Rwork	Num. reflection Rwork	Refine-ID	% reflection obs (%)
1.63-1.65	0.2604	129	0.2068	2456	X-RAY DIFFRACTION	92
1.65-1.67	0.2387	139	0.1779	2645	X-RAY DIFFRACTION	100
1.67-1.7	0.221	138	0.1678	2650	X-RAY DIFFRACTION	100
1.7-1.72	0.1783	140	0.1622	2655	X-RAY DIFFRACTION	100
1.72-1.75	0.2164	141	0.1668	2668	X-RAY DIFFRACTION	100
1.75-1.78	0.216	137	0.1707	2622	X-RAY DIFFRACTION	100
1.78-1.81	0.2431	140	0.1902	2670	X-RAY DIFFRACTION	100
1.81-1.84	0.2995	140	0.2091	2661	X-RAY DIFFRACTION	100
1.84-1.88	0.2408	140	0.1896	2653	X-RAY DIFFRACTION	100
1.88-1.92	0.2004	141	0.1723	2667	X-RAY DIFFRACTION	100
1.92-1.96	0.1839	141	0.1577	2679	X-RAY DIFFRACTION	100
1.96-2	0.2163	139	0.1451	2655	X-RAY DIFFRACTION	100
2-2.05	0.1777	141	0.1428	2673	X-RAY DIFFRACTION	100
2.05-2.11	0.183	140	0.14	2664	X-RAY DIFFRACTION	100
2.11-2.17	0.1727	142	0.146	2685	X-RAY DIFFRACTION	100
2.17-2.24	0.1883	141	0.1463	2684	X-RAY DIFFRACTION	100
2.24-2.32	0.1936	141	0.1457	2674	X-RAY DIFFRACTION	100
2.32-2.41	0.1817	141	0.1414	2686	X-RAY DIFFRACTION	100
2.41-2.52	0.1677	142	0.1437	2691	X-RAY DIFFRACTION	100
2.52-2.66	0.1591	142	0.1374	2700	X-RAY DIFFRACTION	100
2.66-2.82	0.1912	142	0.1392	2696	X-RAY DIFFRACTION	100
2.82-3.04	0.1755	142	0.1423	2703	X-RAY DIFFRACTION	100
3.04-3.35	0.1586	144	0.1391	2741	X-RAY DIFFRACTION	100
3.35-3.83	0.1547	144	0.1275	2739	X-RAY DIFFRACTION	100
3.83-4.82	0.1315	146	0.11	2768	X-RAY DIFFRACTION	100
4.83-42.71	0.1403	152	0.1389	2888	X-RAY DIFFRACTION	100

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°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)
1	0.0558	0.0761	0.1538	0.1118	0.225	0.3906	0.0676	-0.0957	-0.1023	0.0052	-0.0523	-0.0398	0.1943	0.0629	0.0001	0.1927	-0.0028	-0.023	0.1642	-0.0098	0.2009	-4.6308	16.5019	-9.7772
2	0.3	0.3691	-0.0577	0.6249	0.246	0.6451	0.0705	-0.071	-0.0979	0.2006	-0.0545	-0.0257	0.2029	-0.0568	0.0002	0.2073	-0.0039	-0.015	0.1618	0.0314	0.1817	-7.186	16.9285	0.6502
3	0.5347	0.1294	-0.0254	0.5469	0.0947	0.4977	-0.0074	-0.0272	0.0215	0.0219	0.0219	0.0611	0.0155	-0.0197	-0	0.1288	0.0064	-0.0053	0.1286	-0.0041	0.1582	-9.897	30.8504	-9.2245
4	0.4427	-0.0903	0.0798	0.2773	0.0186	0.1907	-0.0181	0.0763	-0.0427	-0.0485	0.0337	-0.0124	-0.037	0.1025	-0	0.1541	-0.0046	-0.0016	0.1469	-0.0111	0.1474	-3.9971	23.6931	-22.8305
5	0.106	-0.081	0.1743	0.3129	0.1541	0.3345	0.0689	0.0255	-0.07	0.0461	-0.0215	-0.0349	0.0282	0.2609	-0.0048	0.1576	0.0269	-0.0034	0.1645	-0.0317	0.1747	1.3258	16.6523	-22.6549
6	0.0894	-0.0173	-0.079	0.111	0.2398	0.535	-0.1228	-0.0741	-0.4532	0.3292	-0.0291	-0.1298	0.606	0.1017	-0.0071	0.2525	0.0408	-0.0276	0.1632	-0.0134	0.2628	-1.6435	5.5827	-14.6457
7	0.1213	0.0097	0.2148	0.08	-0.0853	0.431	-0.0477	-0.0284	-0.0893	0.0283	0.0348	0.023	0.2385	-0.1119	0.0001	0.1581	0.004	0.0123	0.2108	0.0033	0.1867	-39.0059	19.4217	-34.1021
8	0.1575	0.0216	0.1372	0.1244	-0.2981	0.4539	0.0047	0.064	-0.1072	-0.1262	0.0048	0.0246	0.2405	-0.1639	0.0021	0.201	-0.0385	0.002	0.1815	-0.0153	0.1633	-38.2971	14.5567	-41.5819
9	0.0286	-0.0237	0.0099	0.2819	0.0556	0.4686	0.0205	0.0669	0.0035	-0.1042	0.0268	-0.0124	0.0817	0.017	0	0.1559	-0.0159	-0.0037	0.2003	-0.014	0.1564	-32.2682	23.2516	-48.3338
10	0.0166	0.0602	0.0178	0.3761	0.3342	0.554	-0.007	0.042	0.0132	-0.0208	0.0348	-0.0105	0.0161	-0.0149	0	0.1144	-0.0046	-0.0051	0.1594	0.0061	0.1351	-29.3329	29.6624	-39.7053
11	0.1775	0.3057	-0.1453	0.3135	0.0916	0.6299	-0.0277	-0.0295	0.0266	0.1021	0.0183	-0.0435	-0.058	-0.0669	-0.0002	0.1474	0.004	-0.0058	0.1457	0.0033	0.1441	-32.0807	31.2161	-27.9941
12	0.028	0.0314	0.0515	0.0301	0.0143	0.0584	0.0678	-0.1291	-0.043	0.4576	-0.0824	0.0546	-0.08	-0.1094	0	0.2437	-0.016	0.0262	0.2093	0.0097	0.1521	-37.0002	30.2209	-15.3864
13	0.07	0.0597	-0.0675	0.0398	-0.026	0.1241	0.0417	-0.0871	0.0069	0.1881	-0.1035	0.138	0.0575	-0.1808	-0.0025	0.2194	-0.0126	0.0155	0.1712	-0.007	0.1654	-38.4898	24.4467	-23.9162
14	0.0283	-0.0218	-0.0114	0.027	-0.0163	0.074	-0.0132	-0.0626	-0.043	0.234	-0.0338	0.0866	0.1874	-0.3468	-0.0001	0.2575	-0.0431	0.0336	0.2404	-0.0024	0.1739	-43.8889	19.5534	-16.1059
15	0.1772	0.0156	0.1172	0.1531	-0.2397	0.5268	0.0627	0.0128	-0.0739	-0.1086	-0.0308	0.0591	0.2241	-0.2015	0	0.2185	-0.053	-0.0042	0.1841	0.0118	0.1706	-42.0222	13.2385	-28.5887

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 2 through 20 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 21 through 84 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 85 through 185 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 186 through 246 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 247 through 277 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 278 through 305 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 1 through 20 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 21 through 52 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 53 through 84 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 85 through 138 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 139 through 216 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 217 through 231 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 232 through 246 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 247 through 263 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 264 through 305 )