PDB-9l89: Structure of human TREX1-DNA complex with K160R disease-associate...

Basic information

• Entry: Database: PDB / ID: 9l89
• Title: Structure of human TREX1-DNA complex with K160R disease-associated mutation

Components

• DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')
• Three-prime repair exonuclease 1

• Keywords: IMMUNE SYSTEM/DNA / nuclease / DNase / innate immunity / autoimmunity / cancer / IMMUNE SYSTEM-DNA complex

Function / homology

Function:

Regulation by TREX1 / adenyl deoxyribonucleotide binding / MutSalpha complex binding / oligosaccharyltransferase complex / exodeoxyribonuclease III / double-stranded DNA 3'-5' DNA exonuclease activity / MutLalpha complex binding / 3'-5'-DNA exonuclease activity / IRF3-mediated induction of type I IFN / DNA catabolic process / DNA binding, bending / WW domain binding / DNA metabolic process / negative regulation of cGAS/STING signaling pathway / nuclear replication fork / mismatch repair / 3'-5' exonuclease activity / negative regulation of innate immune response / protein-DNA complex / nuclear envelope / single-stranded DNA binding / double-stranded DNA binding / DNA recombination / DNA replication / DNA repair / endoplasmic reticulum membrane / magnesium ion binding / protein homodimerization activity / metal ion binding / cytosol / cytoplasm

Domain/homology:

Three-prime repair exonuclease 1/2 / Exonuclease, RNase T/DNA polymerase III / EXOIII / Ribonuclease H superfamily / Ribonuclease H-like superfamily

Component:

DNA / DNA (> 10) / Three-prime repair exonuclease 1

• Biological species: Homo sapiens (human); synthetic construct (others)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å
• Authors: Zhu, J. / Wang, L. / Lin, C. / Zhou, W.

Funding support

China, 1items

Organization	Grant number	Country
National Natural Science Foundation of China (NSFC)	32270920	China

• Citation: Journal: Immunity / Year: 2026; Title: Distinct recognition pattern for double-stranded DNA allows TREX1 to maintain immune homeostasis; Authors: Zhu, J. / Wang, L. / Lin, C. / Zhou, W.

History

Deposition	Dec 27, 2024	Deposition site: PDBJ / Processing site: PDBC
Revision 1.0	Apr 29, 2026	Provider: repository / Type: Initial release

Assembly

Deposited unit

A: Three-prime repair exonuclease 1

B: Three-prime repair exonuclease 1

C: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

D: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

E: Three-prime repair exonuclease 1

F: Three-prime repair exonuclease 1

G: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

H: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

Summary:

• 131 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	130,877	8
Polymers	130,877	8
Non-polymers	0	0
Water	4,594	255

1

A: Three-prime repair exonuclease 1

B: Three-prime repair exonuclease 1

C: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

D: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

Summary:

• defined by author&software
• Evidence: gel filtration
• 65.4 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	65,438	4
Polymers	65,438	4
Non-polymers	0	0
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	6460 Å2
ΔGint	-10 kcal/mol
Surface area	20860 Å2
Method	PISA

2

E: Three-prime repair exonuclease 1

F: Three-prime repair exonuclease 1

G: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

H: DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

Summary:

• defined by author&software
• 65.4 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	65,438	4
Polymers	65,438	4
Non-polymers	0	0
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	6650 Å2
ΔGint	-10 kcal/mol
Surface area	21320 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	43.777, 91.293, 158.241
Angle α, β, γ (deg.)	90.00, 90.86, 90.00
Int Tables number	4
Space group name H-M	P1211

Components

#1: Protein

A B E F
Three-prime repair exonuclease 1 / 3'-5' exonuclease TREX1 / Deoxyribonuclease III / DNase III

Details:

Mass: 26008.922 Da / Num. of mol.: 4 / Mutation: K160R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TREX1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9NSU2, exodeoxyribonuclease III

#2: DNA chain

C D G H
DNA (5'-D(P*GP*TP*TP*GP*GP*CP*CP*CP*TP*CP*TP*TP*TP*AP*GP*GP*GP*CP*CP*AP*TP*C)-3')

Details:

Mass: 6710.313 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

#3: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 255 / Source method: isolated from a natural source / Formula: H₂O

• Has protein modification: N

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.42 ų/Da / Density % sol: 49.09 %
• Crystal grow: Temperature: 289 K / Method: vapor diffusion, hanging drop; Details: 0.05 M Li2SO4, 27.5% PEG 3350, 0.1 M Bis-Tris pH 6.5

Data collection

• Diffraction: Mean temperature: 80 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: SSRF / Beamline: BL02U1 / Wavelength: 0.97918 Å
• Detector: Type: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Oct 22, 2023
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.97918 Å / Relative weight: 1
• Reflection: Resolution: 2.38→43.77 Å / Num. obs: 49774 / % possible obs: 100 % / Redundancy: 3.9 % / B_iso Wilson estimate: 29.4 Ų / CC_1/2: 0.927 / R_pim(I) all: 0.15 / Net I/σ(I): 4.3
• Reflection shell: Resolution: 2.38→2.42 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 1.9 / Num. unique obs: 4725 / CC_1/2: 0.413 / R_pim(I) all: 0.767 / % possible all: 100

Processing

Software

Name	Version	Classification
PHENIX	1.21.1_5127	refinement
XDS		data scaling
XDS		data reduction
PHENIX		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 7TQQ

7tqq

Resolution: 2.38→43.77 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.83 / Stereochemistry target values: ML

	Rfactor	Num. reflection	% reflection
Rfree	0.2548	2504	5.03 %
Rwork	0.2202	-	-
obs	0.2219	49774	99.01 %

• Solvent computation: Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
• Displacement parameters: B_iso mean: 43.16 Ų

Refinement step

Cycle: LAST / Resolution: 2.38→43.77 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6487	1306	0	255	8048

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.004	8112
X-RAY DIFFRACTION	f_angle_d	0.613	11312
X-RAY DIFFRACTION	f_dihedral_angle_d	20.62	3057
X-RAY DIFFRACTION	f_chiral_restr	0.04	1296
X-RAY DIFFRACTION	f_plane_restr	0.005	1241

LS refinement shell

Resolution (Å)	Rfactor Rfree	Num. reflection Rfree	Rfactor Rwork	Num. reflection Rwork	Refine-ID	% reflection obs (%)
2.38-2.42	0.3469	129	0.2784	2483	X-RAY DIFFRACTION	92
2.42-2.47	0.3115	151	0.2787	2498	X-RAY DIFFRACTION	96
2.47-2.53	0.3342	140	0.2737	2542	X-RAY DIFFRACTION	98
2.53-2.58	0.3105	142	0.2702	2626	X-RAY DIFFRACTION	99
2.59-2.65	0.3229	120	0.2617	2604	X-RAY DIFFRACTION	99
2.65-2.72	0.3053	141	0.2752	2651	X-RAY DIFFRACTION	100
2.72-2.8	0.2897	133	0.2459	2636	X-RAY DIFFRACTION	100
2.8-2.89	0.2761	124	0.2403	2671	X-RAY DIFFRACTION	100
2.89-3	0.256	159	0.2348	2598	X-RAY DIFFRACTION	100
3-3.11	0.2888	170	0.2271	2616	X-RAY DIFFRACTION	100
3.11-3.26	0.2388	122	0.2323	2663	X-RAY DIFFRACTION	100
3.26-3.43	0.2829	140	0.2185	2637	X-RAY DIFFRACTION	100
3.43-3.64	0.2474	118	0.2096	2714	X-RAY DIFFRACTION	100
3.64-3.92	0.2151	132	0.1977	2631	X-RAY DIFFRACTION	100
3.92-4.32	0.228	159	0.1857	2648	X-RAY DIFFRACTION	100
4.32-4.94	0.2224	149	0.1815	2649	X-RAY DIFFRACTION	100
4.94-6.22	0.2025	148	0.2021	2674	X-RAY DIFFRACTION	100
6.22-43.77	0.2326	127	0.2099	2729	X-RAY DIFFRACTION	99

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	0.1409	0.1418	0.2488	0.1831	0.2958	0.4921	0.0017	-0.2482	0.1537	0.4278	0.0637	0.274	-0.1223	0.0967	-0.0001	0.3157	-0.0141	0.0289	0.3141	0.003	0.3473	5.7392	22.7687	25.3746
2	0.1284	0.0368	-0.0428	0.151	-0.0398	0.0204	-0.2533	-0.7561	0.1767	0.3049	0.1002	-0.0249	-0.047	0.032	-0.0311	0.2033	0.0496	0.0634	0.4251	0.0028	0.3313	-7.1402	35.2703	21.8709
3	0.0464	-0.0194	-0.1124	0.0074	0.0544	0.3177	-0.1695	0.0552	-0.2759	0.0518	0.0866	0.3523	0.2854	0.0197	-0.1119	0.2535	-0.0384	0.0883	0.1762	0.0219	0.363	4.9779	12.4132	17.5383
4	0.2849	-0.104	0.1517	0.7246	0.3175	0.9486	0.0674	-0.1544	-0.0927	-0.0903	-0.179	-0.1724	0.0898	0.2689	0.0819	0.1123	-0.0021	0.0116	0.2047	0.0049	0.2608	7.0943	13.4005	15.6382
5	0.0631	0.0275	-0.078	0.633	-0.1084	0.0995	-0.0917	-0.3249	-0.064	0.4826	-0.054	-0.2122	-0.2894	0.1244	-0.0083	0.4195	0.0036	-0.0384	0.4488	-0.024	0.2232	8.5216	25.0089	28.6666
6	0.0881	0.0704	-0.0041	0.0454	0.0018	-0.0018	0.0125	-0.1111	0.6756	-0.0501	-0.0068	-0.594	-0.1354	0.2255	0.0003	0.2737	0.0268	-0.0249	0.4198	-0.0165	0.5445	16.7104	17.3649	25.0321
7	0.2492	0.0799	-0.0887	0.1562	-0.0433	0.0798	-0.1672	-0.3211	-0.1482	0.7598	0.2127	-0.1305	0.2712	-0.2767	-0.0007	0.676	-0.0727	-0.1044	0.4431	0.1145	0.3872	2.4286	26.9237	38.7785
8	0.4974	0.3661	-0.1855	0.3365	-0.1459	0.0883	-0.1645	0.048	0.2587	0.116	0.2279	0.5122	0.3788	-0.4617	0.0474	0.3508	-0.0222	0.0957	0.3328	-0.0294	0.2806	-7.6648	22.5107	29.8439
9	1.5026	-0.3233	0.405	1.5592	-0.5168	0.2358	-0.0148	-0.8312	0.317	1.0893	0.2284	-0.1711	0.2269	-0.0948	0.1824	0.8612	-0.0908	0.1303	0.4232	-0.2688	0.244	1.7151	35.1464	36.0947
10	0.0324	0.0473	-0.0216	0.0563	-0.0048	0.106	0.2228	-0.0208	0.0926	0.5365	0.0375	-0.4987	0.6896	0.5401	0.0005	0.5261	-0.0217	-0.122	0.6213	0.0108	0.3442	16.5896	17.8706	32.4667
11	0.0214	0.0307	-0.0564	0.2374	-0.006	0.4454	-0.0234	-0.0096	-0.0888	0.0391	-0.1374	-0.0209	0.0893	0.0857	0	0.2091	0.0058	0.0229	0.1953	-0.0021	0.3459	-0.641	24.4464	0.5709
12	0.1723	-0.1858	0.109	0.6572	-0.1785	0.077	-0.3565	-0.2918	-0.4533	-0.2274	0.3199	0.5623	0.0234	0.0414	0.0087	0.2429	-0.0846	0.0133	0.3568	0.0034	0.2543	-12.4468	12.167	10.1772
13	0.4483	-0.3208	0.2923	1.1489	-0.8963	0.6867	-0.1053	-0.2015	0.2055	0.873	0.0075	0.1724	-0.29	-0.192	-0.0683	0.2767	-0.0351	0.0553	0.2274	-0.0451	0.2563	-0.6151	39.3237	8.5421
14	0.1371	0.0485	0.0117	0.3631	0.0847	0.6035	0.2805	0.3055	-0.1548	-0.1611	-0.3532	-0.5519	-0.1541	0.1758	0.0132	0.2284	0.0106	-0.0057	0.379	0.0529	0.35	10.748	28.5872	7.979
15	0.2296	-0.0604	0.022	0.3555	-0.3173	0.2382	0.1525	0.1189	0.0781	-0.4396	-0.1441	-0.015	0.0698	0.0004	0.0282	0.1774	0.0294	0.0124	0.1873	-0.0456	0.2941	0.2231	22.5028	-3.562
16	0.0275	-0.0481	0.078	0.1897	0.0281	0.433	0.2335	0.0097	-0.3838	0.0048	-0.1409	-0.2775	-0.1994	0.1307	0.0355	0.158	-0.031	0.0638	0.2096	0.0001	0.3622	9.2452	29.7157	-4.4653
17	0.089	0.0607	0.018	0.1593	-0.0109	0.1922	0.222	0.4183	-0.0579	-0.4255	-0.2045	-0.082	-0.1305	-0.1056	-0.0094	0.2731	0.0223	0.0329	0.2527	-0.0344	0.338	-10.0293	20.7786	-9.0938
18	0.3377	-0.2503	0.0484	0.5623	-0.3973	0.5568	-0.2146	-0.2126	-0.2164	0.0206	0.2618	0.1777	-0.1072	-0.1658	-0.0055	0.116	-0.006	0.0073	0.217	0.012	0.3102	-14.7803	25.2968	2.7996
19	0.3981	-0.2412	-0.144	0.5987	-0.094	0.3281	0.356	0.482	-0.293	-0.733	-0.0572	0.6181	0.0112	-0.5695	0.0197	0.3927	0.0436	-0.0961	0.2782	-0.0998	0.5251	-9.5827	12.61	-5.8646
20	0.1218	-0.0312	0.025	0.0634	-0.0809	0.0898	-0.1456	-0.1013	0.4143	-0.457	0.1787	-0.1883	-0.1921	0.0322	-0.0028	0.2801	-0.0126	0.035	0.2072	-0.0461	0.3065	5.0771	28.8652	-10.7598
21	0.2462	-0.1631	0.0164	0.1333	-0.0006	0.0054	-0.1114	0.0942	-0.737	-0.2347	-0.06	0.3276	0.6389	0.3196	-0.006	1.1481	0.1104	-0.0181	0.9081	0.06	0.5522	4.6052	5.507	39.5405
22	0.0274	0.0211	-0.0269	0.0424	-0.0059	0.0285	0.1227	-0.5306	0.1932	-0.1714	0.1016	0.0072	-0.2577	0.0195	0.0001	1.5089	-0.0897	0.0067	1.6958	-0.1027	1.4003	5.0208	11.8347	52.5983
23	0.1015	-0.1184	0.1356	0.1776	-0.2918	0.5876	0.0587	-0.1538	0.0174	0.3509	0.0333	0.227	0.1133	-0.2395	0.2923	0.6652	-0.0695	0.1186	0.4005	0.0486	0.1938	-0.5218	10.2149	40.554
24	0.6539	0.6087	0.0831	0.6365	-0.1466	0.6708	-0.3226	-0.2897	0.231	-0.0774	0.5848	0.2333	0.2921	-0.465	0.4735	0.3413	0.0069	0.0336	0.2476	-0.0752	0.2047	-8.9857	41.8414	-11.3499
25	0.0119	-0.0315	0.0607	0.0734	-0.1604	0.3473	0.1579	-0.0484	-0.1747	-0.2326	-0.0769	0.3646	0.3891	-0.2842	0.3384	1.5321	-0.3879	-0.3164	0.9168	-0.1985	0.7533	-16.0699	30.6343	-21.3395
26	0.3198	-0.2925	0.1771	0.3596	0.0255	0.7326	0.1061	0.1631	0.3655	-0.0629	0.3198	0.0442	-0.1278	-0.3175	1.4453	-0.3174	-0.0448	-0.2925	0.4207	0.1605	0.1498	-14.0937	36.3524	-9.6965
27	0.0224	0.1059	0.0966	0.5161	0.2781	0.3134	-0.2118	0.1536	0.0145	-0.0966	0.1817	0.0441	0.0195	-0.0574	-0.0127	0.2156	0.0102	-0.0041	0.2344	-0.0063	0.2378	-15.9864	-15.9061	54.1579
28	0.6055	0.3761	1.0077	0.2376	0.6438	1.7017	-0.2091	0.0589	0.5976	-0.0926	-0.0596	-0.1175	-0.4274	0.0848	-0.3024	0.222	-0.1055	-0.0184	0.2432	0.0792	0.4339	-5.9679	-1.2576	62.431
29	0.3631	0.4479	-0.1897	0.5931	0.0629	0.6964	-0.103	-0.0363	-0.0618	0.0494	0.0762	0.0922	0.2319	-0.0639	0.0006	0.1886	-0.0107	-0.0008	0.1777	0.0134	0.1856	-20.8776	-25.0028	61.8681
30	0.2778	-0.0076	0.0751	0.2741	-0.0466	0.025	-0.0024	0.1153	-0.0075	-0.5564	-0.02	0.0385	-0.0736	0.0384	0.0185	0.2465	0.0041	-0.005	0.2801	0.0689	0.2913	-16.6384	-13.0271	49.9617
31	0.6475	-0.1056	-0.4784	0.1196	0.1071	0.3567	0.0623	0.2463	0.4745	-0.5131	0.0234	0.187	0.0102	-0.3804	0.0525	0.2598	-0.0846	-0.1042	0.3038	0.0022	0.3902	-25.4848	-20.7131	48.9821
32	0.3995	0.3602	0.3412	1.5802	0.3608	0.3029	0.0175	0.6017	0.0296	-0.5775	0.1033	-0.3732	-0.0277	0.0712	0.1124	0.2184	-0.0467	0.0879	0.368	0.0563	0.2489	-1.7174	-13.4571	47.8165
33	0.0595	-0.0715	-0.0835	0.1862	0.2104	0.2146	-0.4587	0.0984	-0.3572	-0.0577	0.4273	-0.3244	0.3333	0.0419	0.0035	0.2237	-0.0166	0.0234	0.332	0.0405	0.3414	-4.7413	-16.4093	60.0559
34	0.3666	-0.504	0.1201	0.7437	-0.2215	0.1554	0.1628	0.5306	0.4204	-0.4225	-0.4339	-0.0886	0.2685	0.4961	-0.103	0.321	-0.0805	-0.0115	0.362	0.1236	0.3052	-7.1193	-2.9242	47.8195
35	0.4981	-0.0397	0.0486	0.9426	0.14	0.0351	0.2089	-0.0112	-0.1489	-0.2315	-0.2828	0.0067	0.4931	-0.3875	0.0043	0.3777	-0.0648	-0.0952	0.3922	0.0573	0.1355	-21.2835	-19.8303	42.7902
36	0.1417	0.1767	-0.1772	0.1702	-0.1968	0.3245	0.0316	0.099	-0.1836	0.0619	-0.0379	0.1815	0.0158	-0.0695	-0.0015	0.2303	-0.0144	-0.0102	0.2209	-0.0071	0.3096	-22.6026	-13.6433	79.1593
37	0.3503	0.2009	-0.3571	0.1188	-0.2868	1.5848	-0.2237	-0.2925	-0.1924	0.3107	0.4752	-0.0832	0.0621	-0.4718	0.0446	0.2808	0.079	-0.0449	0.2901	0.0368	0.3143	-8.9512	-26.1916	75.6204
38	-0.0465	0.0126	-0.0144	1.0454	0.8301	0.5985	0.0041	0.0622	0.0834	0.0184	-0.0921	0.0751	-0.1317	-0.0734	0.0001	0.1372	0.0154	-0.0213	0.2131	0.0307	0.218	-23.7262	-6.713	72.8047
39	0.008	0.0048	0.0628	0.1545	-0.1276	1.1336	-0.0985	-0.2655	-0.7825	0.1886	0.0453	0.3197	-0.1111	-0.6622	0.0004	0.1992	0.0295	0.0077	0.3418	0.0208	0.4511	-33.4629	-8.4208	78.5455
40	0.0301	0.0458	-0.0075	0.066	-0.0657	0.835	0.3185	-0.1547	0.2342	0.7625	-0.2965	0.1708	0.4419	0.1118	-0.1708	0.4941	-0.0144	-0.0052	0.1698	-0.012	0.3389	-19.3297	-17.0265	91.0063
41	0.4121	-0.22	0.0918	0.2717	0.1401	0.4167	-0.1734	0.0038	0.2399	0.2317	-0.0065	-0.1296	-0.3552	0.3279	-0.0114	0.1789	0.0214	-0.0698	0.2246	0.0297	0.2204	-9.0674	-12.4416	85.1372
42	0.7792	-0.1542	0.3054	0.889	0.8742	1.1467	0.0256	-0.5913	-0.6069	0.9748	-0.0157	0.1378	0.4237	-0.0982	-0.1373	0.5964	0.0562	-0.0691	0.2519	0.0944	0.3296	-17.1801	-25.282	88.8395
43	0.0871	0.0094	-0.0879	0.0414	0.0028	0.0745	0.2115	-0.0346	-0.1289	-0.1601	-0.1776	0.2442	0.3584	0.3367	0.0001	0.3654	0.0512	0.0391	0.3001	0.0735	0.5111	-32.9329	-9.3245	85.9183
44	2.6255	0.1208	1.8682	0.5648	0.0727	1.3927	0.0062	1.0046	-0.3464	-1.5808	0.2436	-0.6609	0.9178	0.765	0.226	1.0639	-0.0187	0.2519	1.1408	0.1292	0.6722	-3.7981	-29.96	36.992
45	0.6666	0.826	0.1334	1.1048	0.316	0.6774	-0.2368	0.4318	0.0311	-0.2416	0.3758	-0.5302	0.8312	1.1287	0.1552	0.4395	0.0761	0.1276	0.6921	0.0272	0.2956	-1.8514	-27.7021	44.644
46	3.1681	-0.062	0.3839	0.1054	-0.082	0.1135	-0.3446	0.3498	0.4419	-0.5134	0.0678	0.109	0.0508	-0.2297	-0.1971	0.5649	0.0299	-0.0256	0.2253	-0.0274	0.2036	-21.6305	3.5618	93.1004
47	0.9285	-0.224	-0.7983	0.0679	0.2755	1.1557	0.1757	-0.4884	-0.2843	-0.161	0.0557	0.2942	0.1393	0.6322	0.1973	2.1016	-0.1765	-0.2315	0.9329	0.244	0.8188	-22.5871	-5.582	105.7793
48	0.0314	0.0325	-0.0096	0.0929	-0.0099	0.0007	-0.0081	-0.5857	-0.0469	0.2251	0.5301	0.1587	0.3355	-0.1151	0.2015	0.4078	0.1668	-0.0226	0.5535	0.0442	0.2129	-16.3596	-1.861	94.5406

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 8 through 45 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 46 through 64 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 65 through 78 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 79 through 114 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 115 through 129 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 130 through 150 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 151 through 165 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 166 through 209 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 210 through 222 )
10	X-RAY DIFFRACTION	10	chain 'A' and (resid 223 through 235 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 8 through 45 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 46 through 64 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 65 through 94 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 95 through 114 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 115 through 129 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 130 through 150 )
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 151 through 164 )
18	X-RAY DIFFRACTION	18	chain 'B' and (resid 165 through 208 )
19	X-RAY DIFFRACTION	19	chain 'B' and (resid 209 through 222 )
20	X-RAY DIFFRACTION	20	chain 'B' and (resid 223 through 234 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 1 through 5 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 6 through 16 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 17 through 22 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 1 through 5 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 6 through 16 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 17 through 22 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 8 through 44 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 45 through 64 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 65 through 114 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 115 through 129 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 130 through 150 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 151 through 187 )
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 188 through 208 )
34	X-RAY DIFFRACTION	34	chain 'E' and (resid 209 through 222 )
35	X-RAY DIFFRACTION	35	chain 'E' and (resid 223 through 234 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 7 through 45 )
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 46 through 64 )
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 65 through 129 )
39	X-RAY DIFFRACTION	39	chain 'F' and (resid 130 through 150 )
40	X-RAY DIFFRACTION	40	chain 'F' and (resid 151 through 163 )
41	X-RAY DIFFRACTION	41	chain 'F' and (resid 164 through 208 )
42	X-RAY DIFFRACTION	42	chain 'F' and (resid 209 through 222 )
43	X-RAY DIFFRACTION	43	chain 'F' and (resid 223 through 234 )
44	X-RAY DIFFRACTION	44	chain 'G' and (resid 1 through 16 )
45	X-RAY DIFFRACTION	45	chain 'G' and (resid 17 through 22 )
46	X-RAY DIFFRACTION	46	chain 'H' and (resid 1 through 5 )
47	X-RAY DIFFRACTION	47	chain 'H' and (resid 6 through 16 )
48	X-RAY DIFFRACTION	48	chain 'H' and (resid 17 through 22 )