PDB-12ss: Crystal Structure of Superoxide dismutase from Cryptosporidium parvum

ID or keywords:

Entry

Database: PDB / ID: 12ss

Title

Crystal Structure of Superoxide dismutase from Cryptosporidium parvum

Components

Superoxide dismutase

Keywords

OXIDOREDUCTASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / Superoxide dismutase / Cryptosporidium parvum

Function / homology

Function and homology information

superoxide dismutase / superoxide dismutase activity / metal ion binding
Similarity search - Function

Biological species

Cryptosporidium parvum Iowa II (eukaryote)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.01 Å

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	75N93022C00036	United States
National Institutes of Health/Office of the Director	S10OD030394	United States

Citation

Journal: To be published
Title: Crystal Structure of Superoxide dismutase from Cryptosporidium parvum
Authors: Liu, L. / Ung, A.R. / Lovell, S. / Cooper, A. / Battaile, K.P.

History

Deposition	Apr 16, 2026	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 29, 2026	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	12ss.cif.gz	475.8 KB	Display	PDBx/mmCIF format
PDB format	pdb12ss.ent.gz	391.4 KB	Display	PDB format
PDBx/mmJSON format	12ss.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/2s/12ss ftp://data.pdbj.org/pub/pdb/validation_reports/2s/12ss	HTTPS FTP

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Related structure data

Similar structure data	Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#94 - Oct 2007 Superoxide Dismutase similarity (11)

Deposited unit

A: Superoxide dismutase

B: Superoxide dismutase

C: Superoxide dismutase

D: Superoxide dismutase

E: Superoxide dismutase

F: Superoxide dismutase

hetero molecules

142 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Superoxide dismutase

hetero molecules

C: Superoxide dismutase

hetero molecules

defined by author&software
Evidence: gel filtration, dimeric
47.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Superoxide dismutase

D: Superoxide dismutase

hetero molecules

defined by author&software
47.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: Superoxide dismutase

F: Superoxide dismutase

hetero molecules

defined by author&software
47.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	92.805, 92.805, 125.765
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	144
Space group name H-M	P3₁

#1: Protein	Superoxide dismutase Mass: 23549.318 Da / Num. of mol.: 6 / Fragment: P26-S221 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cryptosporidium parvum Iowa II (eukaryote) Gene: cgd5_3230 / Plasmid: CrpaA.01199.a.B2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A3FQJ9
#2: Chemical	ChemComp-MN / MANGANESE (II) ION Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 243 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y
Has protein modification	N

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.21 Å³/Da / Density % sol: 44.42 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: Berkeley D6: 25% (w/v) PEG 3350, 100 mM MES pH 5.5, 200 mM Ammonium acetate. ChtrB.20815.a.B1.PW39484 at 13.5 mg/mL. Metal assigned as Mn acquired from expression. P31 twinned, plate 20585 ...Details: Berkeley D6: 25% (w/v) PEG 3350, 100 mM MES pH 5.5, 200 mM Ammonium acetate. ChtrB.20815.a.B1.PW39484 at 13.5 mg/mL. Metal assigned as Mn acquired from expression. P31 twinned, plate 20585 D6 drop1, Puck: PSL-2101, Cryo: 20% PEG 200 + 80% crystallant

Crystal

Density Matthews: 2.21 Å³/Da / Density % sol: 44.42 %

Crystal grow

Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: Berkeley D6: 25% (w/v) PEG 3350, 100 mM MES pH 5.5, 200 mM Ammonium acetate. ChtrB.20815.a.B1.PW39484 at 13.5 mg/mL. Metal assigned as Mn acquired from expression. P31 twinned, plate 20585 ...

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
Detector	Type: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Jan 31, 2026
Radiation	Monochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9786 Å / Relative weight: 1
Reflection	Resolution: 2.01→46.4 Å / Num. obs: 161236 / % possible obs: 100 % / Redundancy: 10.7 % / CC_1/2: 0.999 / R_merge(I) obs: 0.126 / R_pim(I) all: 0.04 / R_rim(I) all: 0.132 / Χ²: 1.07 / Net I/σ(I): 14.8
Reflection shell	Resolution: 2.01→2.06 Å / % possible obs: 100 % / Redundancy: 10.9 % / R_merge(I) obs: 1.437 / Num. measured all: 65931 / Num. unique obs: 6024 / CC_1/2: 0.552 / R_pim(I) all: 0.454 / R_rim(I) all: 1.507 / Χ²: 0.91 / Net I/σ(I) obs: 1.8

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Processing

Software

Name	Version	Classification
PHENIX	(2.1rc1_6025: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHASER		phasing
PDB_EXTRACT		data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.01→46.4 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 27.56 / Stereochemistry target values: TWIN_LSQ_F

	R_factor	Num. reflection	% reflection
R_free	0.1965	7734	4.8 %
R_work	0.1486	-	-
obs	0.1562	161236	100 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 2.01→46.4 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9352	0	17	243	9612

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.011	9708
X-RAY DIFFRACTION	f_angle_d	0.727	13204
X-RAY DIFFRACTION	f_dihedral_angle_d	15.317	3387
X-RAY DIFFRACTION	f_chiral_restr	0.045	1401
X-RAY DIFFRACTION	f_plane_restr	0.006	1687

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.01-2.02	0.355	164	0.2619	2690	X-RAY DIFFRACTION	94
2.02-2.03	0.3059	132	0.2446	2772	X-RAY DIFFRACTION	95
2.03-2.05	0.2253	112	0.2398	2732	X-RAY DIFFRACTION	96
2.05-2.06	0.2814	148	0.2541	3066	X-RAY DIFFRACTION	95
2.06-2.07	0.286	180	0.2426	2672	X-RAY DIFFRACTION	94
2.08-2.09	0.2969	128	0.2472	2708	X-RAY DIFFRACTION	95
2.09-2.1	0.2846	148	0.2352	2898	X-RAY DIFFRACTION	95
2.1-2.12	0.2608	140	0.2351	2768	X-RAY DIFFRACTION	95
2.12-2.13	0.2282	96	0.2253	2744	X-RAY DIFFRACTION	97
2.13-2.15	0.2304	120	0.224	2860	X-RAY DIFFRACTION	96
2.15-2.17	0.2746	92	0.2126	2816	X-RAY DIFFRACTION	97
2.17-2.18	0.2226	236	0.2	2678	X-RAY DIFFRACTION	92
2.18-2.2	0.2315	152	0.2047	2848	X-RAY DIFFRACTION	95
2.2-2.22	0.2209	204	0.21	2720	X-RAY DIFFRACTION	93
2.22-2.24	0.2103	180	0.2062	2718	X-RAY DIFFRACTION	94
2.24-2.25	0.2134	116	0.2043	2804	X-RAY DIFFRACTION	96
2.25-2.27	0.24	128	0.2022	2876	X-RAY DIFFRACTION	96
2.27-2.29	0.2335	112	0.1992	2784	X-RAY DIFFRACTION	96
2.29-2.31	0.2751	184	0.1917	2770	X-RAY DIFFRACTION	94
2.32-2.34	0.2728	148	0.194	2844	X-RAY DIFFRACTION	95
2.34-2.36	0.2131	200	0.1918	2676	X-RAY DIFFRACTION	93
2.36-2.38	0.1976	116	0.1861	2770	X-RAY DIFFRACTION	96
2.38-2.41	0.1989	160	0.1824	2792	X-RAY DIFFRACTION	95
2.41-2.43	0.2902	104	0.1816	2888	X-RAY DIFFRACTION	97
2.43-2.46	0.2395	160	0.1764	2752	X-RAY DIFFRACTION	95
2.46-2.49	0.1778	116	0.1746	2758	X-RAY DIFFRACTION	96
2.49-2.52	0.2214	148	0.1787	2858	X-RAY DIFFRACTION	95
2.52-2.55	0.2368	176	0.1608	2708	X-RAY DIFFRACTION	94
2.55-2.58	0.1762	128	0.1635	2862	X-RAY DIFFRACTION	96
2.58-2.61	0.187	100	0.171	2770	X-RAY DIFFRACTION	97
2.61-2.65	0.2587	172	0.1708	2834	X-RAY DIFFRACTION	94
2.65-2.69	0.2013	168	0.1681	2650	X-RAY DIFFRACTION	94
2.69-2.73	0.1887	132	0.1628	2908	X-RAY DIFFRACTION	96
2.73-2.77	0.1733	140	0.1524	2738	X-RAY DIFFRACTION	95
2.77-2.82	0.2031	128	0.1459	2818	X-RAY DIFFRACTION	96
2.82-2.86	0.1609	112	0.1441	2764	X-RAY DIFFRACTION	96
2.86-2.92	0.1969	152	0.1439	2808	X-RAY DIFFRACTION	95
2.92-2.97	0.2006	156	0.1448	2768	X-RAY DIFFRACTION	95
2.97-3.03	0.1987	92	0.1521	2832	X-RAY DIFFRACTION	97
3.03-3.1	0.2104	94	0.1533	2842	X-RAY DIFFRACTION	97
3.1-3.17	0.2304	176	0.1518	2752	X-RAY DIFFRACTION	94
3.17-3.25	0.2226	96	0.1569	2872	X-RAY DIFFRACTION	97
3.25-3.34	0.189	156	0.1472	2750	X-RAY DIFFRACTION	95
3.34-3.44	0.1728	132	0.1553	2846	X-RAY DIFFRACTION	96
3.44-3.55	0.2141	164	0.1461	2752	X-RAY DIFFRACTION	94
3.55-3.67	0.1786	148	0.1471	2770	X-RAY DIFFRACTION	95
3.67-3.82	0.2299	116	0.1439	2818	X-RAY DIFFRACTION	96
3.82-3.99	0.2304	156	0.134	2802	X-RAY DIFFRACTION	95
4-4.2	0.1807	152	0.1219	2724	X-RAY DIFFRACTION	95
4.21-4.47	0.1961	84	0.1136	2902	X-RAY DIFFRACTION	97
4.47-4.81	0.1162	144	0.1036	2750	X-RAY DIFFRACTION	95
4.81-5.3	0.1507	44	0.1088	2858	X-RAY DIFFRACTION	98
5.3-6.06	0.1937	142	0.1258	2814	X-RAY DIFFRACTION	95
6.06-7.63	0.1658	188	0.1417	2774	X-RAY DIFFRACTION	94
7.64-46.4	0.1957	162	0.147	2754	X-RAY DIFFRACTION	94

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	1.5391	0.4338	-0.4214	0.5639	0.1642	1.5064	-0.0573	-0.2649	-0.1263	0.2046	0.1152	-0.1792	0.0378	0.2512	-0.06	0.2234	0.0652	-0.0175	0.3168	-0.0071	0.2985	34.2527	-1.4234	8.6119
2	6.5282	0.953	3.3886	4.9431	1.4628	4.2136	0.1502	-0.2896	-0.8467	0.1731	0.0878	-0.0254	0.6368	-0.1295	-0.2115	0.3296	0.0354	0.0482	0.2549	0.0318	0.3149	21.6694	-18.0934	7.7345
3	0.5121	-0.0823	-0.4198	2.2327	0.2167	2.0772	-0.0367	-0.0482	-0.1397	0.1069	-0.0139	0.0622	0.1815	0.1948	0.0471	0.2374	0.0337	-0.0049	0.2451	-0.0155	0.2636	23.5343	-8.2297	3.7184
4	8.4149	-2.2822	3.6116	1.8397	-1.7018	6.1615	0.1082	0.709	0.2127	-0.3774	-0.1095	-0.2003	-0.1295	0.3795	0.0238	0.3052	-0.0199	0.0398	0.2911	0.0148	0.2212	29.385	5.9455	-13.625
5	0.9066	0.1618	-1.27	0.4348	-0.4379	3.809	0.0607	0.1851	0.2026	0.1548	-0.0021	0.003	-0.3734	-0.2612	-0.0623	0.212	0.0315	-0.028	0.2391	-0.0001	0.2727	18.7028	5.6916	-4.577
6	1.2049	1.1017	0.0999	1.4067	-0.1308	4.1223	-0.0334	0.1697	-0.0358	-0.1428	0.0816	0.1333	0.0555	-0.1582	-0.0431	0.1887	0.0202	-0.0219	0.2556	-0.0051	0.2684	16.0041	-5.0019	-8.7407
7	0.7754	-0.3685	-1.1618	1.0237	0.197	1.8751	0.0776	0.0209	0.1912	0.0086	0.0052	-0.0282	-0.3068	-0.0242	-0.0737	0.2274	0.0281	-0.0169	0.2533	-0.0061	0.2781	24.3155	7.1787	4.1404
8	6.441	2.5169	2.9438	9.5598	-1.7096	2.454	0.0178	0.7423	-0.3391	-0.0833	0.3136	-0.5945	0.1345	0.6476	-0.3283	0.241	-0.0049	0.0377	0.3182	-0.0352	0.2433	31.1883	-2.4083	-10.7446
9	0.3385	-0.0565	-0.2923	2.1357	0.4873	2.2218	0.0285	-0.0621	-0.159	0.299	-0.0978	0.2497	0.6774	-0.403	0.0514	0.3894	-0.1016	0.0244	0.2355	-0.0203	0.2755	4.2631	26.0538	-13.7288
10	2.585	0.6544	-0.0848	3.6778	-0.3638	5.6807	0.0092	0.2144	0.0126	-0.2958	0.0222	-0.3401	0.0799	0.5444	-0.0486	0.1737	0.0012	0.0316	0.2253	0.0142	0.2185	19.5879	34.6305	-32.0563
11	0.8155	0.1073	0.2811	0.9373	0.714	3.0074	-0.0198	0.0342	0.0591	-0.0292	-0.004	-0.0082	-0.0508	-0.0981	0.0209	0.2146	0.0099	-0.0011	0.166	0.0043	0.2455	11.3499	37.0878	-22.2645
12	7.084	-4.7522	4.3428	8.9892	-1.6537	8.8348	0.4667	0.2949	-0.6931	-0.3307	-0.0097	0.2135	0.8095	0.1344	-0.4111	0.2491	0.0279	0.0416	0.1845	-0.0112	0.1811	13.7791	25.3639	-30.7391
13	1.8063	0.0598	1.0042	1.2741	-0.0102	2.3481	0.0013	-0.0098	0.0371	-0.0255	0.0241	-0.1297	-0.071	0.2273	-0.0218	0.1603	-0.0238	-0.0361	0.2742	-0.0136	0.259	7.6017	-10.5526	-21.6
14	2.3287	-0.8723	-1.2154	1.5922	0.1814	5.2636	-0.188	-0.4408	0.2649	0.224	-0.0275	-0.0066	-0.2897	-0.2287	0.2307	0.211	0.0445	-0.078	0.3421	-0.0603	0.3189	-5.7486	-1.7418	-17.3619
15	2.3339	0.963	1.5764	1.4924	0.7341	2.4921	-0.0224	-0.3374	0.196	0.1884	-0.0726	0.0202	-0.0147	-0.2074	0.0948	0.2118	0.0058	-0.0159	0.3066	-0.0411	0.2441	-1.6484	-10.2009	-18.1126
16	1.9127	-0.2415	0.7392	3.0896	-0.095	5.9798	0.0817	0.0331	-0.0382	0.2158	0.2076	-0.3719	-0.1004	0.4071	-0.2563	0.2451	-0.034	0.0109	0.2435	-0.0934	0.3152	20.6341	51.1354	-1.2192
17	2.2585	0.8729	0.2666	0.4268	-0.4445	3.4123	0.1374	0.2533	0.6524	-1.1582	-0.2081	-0.0101	-0.5692	0.1157	-0.0272	0.7774	0.0031	0.05	0.2656	0.0435	0.4292	11.4527	65.8498	-13.3539
18	2.4214	-0.4635	0.9189	4.0832	3.1262	3.2904	-0.071	-0.0483	0.1889	-0.1493	-0.0181	0.1175	-0.158	-0.0152	0.0821	0.2602	-0.0192	0.0272	0.1909	-0.0105	0.2465	11.3156	55.1124	-4.4519
19	7.468	1.1802	0.0515	1.0751	1.6482	3.0269	0.5286	-0.6558	0.1507	0.5212	-0.3675	0.3643	0.3742	-0.3807	-0.1332	0.5708	-0.1032	0.1724	0.2907	-0.0082	0.3439	1.505	50.4046	15.886
20	1.7371	-0.5717	-0.937	0.2304	0.6498	3.4991	-0.0679	-0.1776	-0.2144	0.3453	-0.293	0.2704	0.5449	-0.4705	0.3494	0.3256	-0.1032	0.0978	0.2614	-0.0545	0.3795	0.1229	44.9335	2.6953
21	6.0023	-2.9917	-4.2883	2.7491	0.3772	5.5784	0.1042	-0.0481	0.2711	0.1999	-0.1247	0.6987	-0.4706	-0.2601	0.0396	0.2444	-0.0219	0.0691	0.253	-0.0747	0.4623	-5.8082	54.7932	2.2317
22	1.6136	-0.1327	-0.8802	2.2444	1.9907	3.4355	0.0489	-0.0393	0.0656	0.2854	-0.169	0.2645	0.2379	-0.1698	0.1031	0.2157	-0.0423	0.039	0.1593	-0.0181	0.2203	7.5447	46.6815	-2.2761
23	1.1628	-0.769	-0.4609	4.1041	3.8302	5.3406	-0.0515	0.0253	-0.0492	0.4512	-0.0374	0.1269	0.5063	-0.2596	0.0938	0.3566	-0.0452	0.0783	0.2229	-0.0205	0.224	7.0121	48.4161	9.6607
24	3.9097	-0.6544	-1.5637	3.6416	0.5062	4.7959	-0.0117	-0.1918	-0.2661	0.6752	0.0263	-0.1673	0.2608	0.272	-0.0164	0.3468	0.0584	-0.0417	0.2226	-0.0188	0.2892	-23.4376	2.6193	-14.2794
25	6.4223	-0.5316	-2.1343	1.2246	-1.1924	2.5751	-0.2555	0.2295	-0.3074	0.0926	0.127	0.2762	0.3468	-0.2799	0.1081	0.3485	-0.0348	0.0394	0.293	-0.0779	0.3761	-40.8143	2.0352	-17.7535
26	9.0786	-2.0991	4.5577	2.4639	0.2075	8.1734	0.1399	1.4892	0.0374	-0.2596	0.0998	-0.3884	-0.5369	1.2612	-0.2121	0.3625	-0.0671	0.0917	0.5312	-0.0583	0.4183	-15.7238	8.5358	-30.0092
27	2.1399	0.6914	-0.2327	2.7989	1.2538	4.492	0.001	0.3701	0.1399	-0.3539	0.0503	-0.2099	-0.3359	0.1464	-0.0527	0.2115	0.0158	0.0009	0.2738	0.0263	0.2594	-28.2203	17.4205	-32.512
28	2.9174	0.4381	1.305	1.651	-0.4291	4.7308	0.0437	0.2412	-0.0412	-0.301	-0.147	0.0737	0.2091	-0.0238	0.1189	0.3152	0.0589	-0.02	0.3318	-0.0316	0.3459	-37.755	13.2161	-31.0882
29	1.3532	-1.8603	-2.1861	3.9272	2.8092	5.9843	0.1716	0.111	0.029	-0.1622	-0.1263	-0.1672	-0.2359	-0.0026	-0.0622	0.2053	0.0191	0.001	0.2539	0.0137	0.285	-24.4045	12.7689	-22.5435
30	2.719	-1.4748	0.2766	4.8603	0.6532	3.0937	0.0196	0.1012	0.0421	-0.0311	-0.0314	-0.0573	-0.4224	-0.0885	0.0519	0.4185	-0.0256	0.0434	0.2592	-0.0442	0.3088	-32.5458	33.8705	-6.8767
31	3.4892	-0.9126	-2.2692	2.3753	0.6006	2.1199	-0.3619	-0.3693	-0.222	0.7785	0.0399	0.5923	0.6164	-0.3924	0.2983	0.7529	-0.0958	0.1687	0.406	-0.0126	0.4289	-44.9053	20.4026	9.6082
32	1.3694	-1.021	-0.1569	2.9104	0.8913	3.2493	-0.0844	-0.1286	-0.1235	0.4981	-0.0709	0.5024	0.1988	-0.3577	0.1544	0.3484	-0.0524	0.0787	0.2556	-0.0491	0.3486	-41.3362	23.3079	-0.6685

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 26 through 54 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 55 through 87 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 88 through 105 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 106 through 129 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 130 through 154 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 155 through 180 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 181 through 210 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 211 through 221 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 26 through 105 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 106 through 143 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 144 through 209 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 210 through 221 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 26 through 129 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 130 through 168 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 169 through 220 )
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 26 through 66 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 67 through 87 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 88 through 105 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 106 through 129 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 130 through 154 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 155 through 168 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 169 through 199 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 200 through 220 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 26 through 54 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 55 through 105 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 106 through 116 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 117 through 157 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 158 through 180 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 181 through 221 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 26 through 104 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 105 through 143 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 144 through 220 )

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