PDB-9cyn: Flagellar filament sheath protein FlaA1

ID or keywords:

Entry

Database: PDB / ID: 9cyn

Title

Flagellar filament sheath protein FlaA1

Components

Endoflagellar filament sheath protein

Keywords

STRUCTURAL PROTEIN / flagellum / bacterial motility / flagellar filament

Function / homology

Flagellar filament outer layer protein FlaA / Flagellar filament outer layer protein Flaa / periplasmic flagellum / bacterial-type flagellum-dependent cell motility / outer membrane-bounded periplasmic space / Endoflagellar filament sheath protein

Function and homology information

Biological species

Leptospira borgpetersenii serovar Hardjo-bovis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.82 Å

Authors

San Martin, F. / Larrieux, N. / Trajtenberg, F. / Buschiazzo, A.

Funding support

Uruguay, 1items

Citation

Journal: Nat Commun / Year: 2026
Title: Core-sheath coupling controls flagellar curvature and motility in Leptospira.
Authors: Fabiana San Martin / Megan R Brady / Lenka Fule / Lucienne Nouchikian / Azalia Rodriguez / Magalie Duchateau / Sonia Mondino / Nicole Larrieux / Elsio A Wunder / Albert I Ko / Martial Rey / ...
Abstract: Spirochaete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike ...

History

Deposition	Aug 2, 2024	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 18, 2026	Provider: repository / Type: Initial release
Revision 1.1	Sep 9, 2026	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/cy/9cyn ftp://data.pdbj.org/pub/pdb/validation_reports/cy/9cyn	HTTPS FTP

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Related structure data

Related structure data	75268C 75269C 75270C 10lkC 10llC 10lmC C: citing same article (ref.)
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

Deposited unit

A: Endoflagellar filament sheath protein

B: Endoflagellar filament sheath protein

C: Endoflagellar filament sheath protein

hetero molecules

87.4 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Endoflagellar filament sheath protein

C: Endoflagellar filament sheath protein

hetero molecules

defined by author
Evidence: gel filtration, There is also a tendency to form large soluble polymers in vitro (observed by SEC and DLS)
58.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Endoflagellar filament sheath protein

hetero molecules

defined by author
29.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	81.417, 105.776, 108.734
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁
Space group name Hall	P2ac2ab
Symmetry operation	#1: x,y,z #2: x+1/2,-y+1/2,-z #3: -x,y+1/2,-z+1/2 #4: -x+1/2,-y,z+1/2

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details (eV)
d_1	ens_1	(chain "A" and ((resid 51 and (name N or name...
d_2	ens_1	(chain "B" and (resid 51 through 71 or resid 73...
d_3	ens_1	(chain "C" and ((resid 51 and (name N or name...

NCS domain segments:

Ens-ID: ens_1

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
d_1	1	GLU	GLU	TRP	TRP	A	A	51 - 71	6 - 26
d_1	2	VAL	VAL	ALA	ALA	A	A	73 - 82	28 - 37
d_1	3	TYR	TYR	TYR	TYR	A	A	90	45
d_1	4	PRO	PRO	ARG	ARG	A	A	92 - 101	47 - 56
d_1	5	VAL	VAL	ASP	ASP	A	A	103 - 112	58 - 67
d_1	6	ALA	ALA	VAL	VAL	A	A	121 - 232	76 - 187
d_1	7	VAL	VAL	SER	SER	A	A	238 - 250	193 - 205
d_1	8	PRO	PRO	ASP	ASP	A	A	252 - 278	207 - 233
d_2	1	GLU	GLU	TRP	TRP	B	B	51 - 71	6 - 26
d_2	2	VAL	VAL	TYR	TYR	B	B	73 - 90	28 - 45
d_2	3	PRO	PRO	ARG	ARG	B	B	92 - 101	47 - 56
d_2	4	VAL	VAL	ASP	ASP	B	B	103 - 112	58 - 67
d_2	5	ALA	ALA	VAL	VAL	B	B	121 - 232	76 - 187
d_2	6	VAL	VAL	SER	SER	B	B	238 - 250	193 - 205
d_2	7	PRO	PRO	ASP	ASP	B	B	252 - 278	207 - 233
d_3	1	GLU	GLU	TRP	TRP	C	C	51 - 71	6 - 26
d_3	2	VAL	VAL	TYR	TYR	C	C	73 - 90	28 - 45
d_3	3	PRO	PRO	ARG	ARG	C	C	92 - 101	47 - 56
d_3	4	VAL	VAL	ASP	ASP	C	C	103 - 112	58 - 67
d_3	5	ALA	ALA	ARG	ARG	C	C	121 - 152	76 - 107
d_3	6	SER	SER	VAL	VAL	C	C	166 - 232	121 - 187
d_3	7	VAL	VAL	SER	SER	C	C	238 - 250	193 - 205
d_3	8	PRO	PRO	ASP	ASP	C	C	252 - 278	207 - 233

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.0465306374284, -0.95872148281, -0.280513846681), (-0.960208177278, 0.120343786335, -0.252027040969), (0.275381836855, 0.257624710557, -0.926171880614)	122.551376281, 129.664445361, -17.488529125
2	given	(0.39305670885, -0.876973744323, -0.276447961461), (-0.84941384292, -0.461429581766, 0.256083706094), (-0.352139953831, 0.134163306605, -0.92628163108)	81.8448684469, 129.058066368, 6.3656023099

#1: Protein	Endoflagellar filament sheath protein / FlaA1 Mass: 28881.410 Da / Num. of mol.: 3 / Fragment: residues 50-302 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Leptospira borgpetersenii serovar Hardjo-bovis (bacteria) Gene: flaA-2, LBJ_0704 / Variant: JB197 / Production host: Escherichia coli (E. coli) / Strain (production host): Lemo21 / References: UniProt: Q04UP1
#2: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO₄
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 410 / Source method: isolated from a natural source / Formula: H₂O
Has ligand of interest	Y
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.7 Å³/Da / Density % sol: 54.48 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: ammonium sulfate, sodium cacodylate

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.979507 Å
Detector	Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Sep 23, 2021
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.979507 Å / Relative weight: 1
Reflection	Resolution: 1.816→75.82 Å / Num. obs: 85228 / % possible obs: 100 % / Redundancy: 13.8 % / B_iso Wilson estimate: 36.39 Å² / CC_1/2: 0.998 / R_merge(I) obs: 0.106 / R_pim(I) all: 0.03 / R_rim(I) all: 0.11 / Χ²: 0.77 / Net I/σ(I): 13.1
Reflection shell	Resolution: 1.816→1.848 Å / Redundancy: 14 % / R_merge(I) obs: 5.769 / Mean I/σ(I) obs: 0.5 / Num. unique obs: 4238 / CC_1/2: 0.375 / R_pim(I) all: 1.596 / R_rim(I) all: 5.987 / Χ²: 0.59 / % possible all: 100

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Processing

Software

Name	Version	Classification
PHENIX	1.21.1_5286	refinement
Aimless	0.7.13	data scaling
XDS	20230630	data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.82→75.82 Å / SU ML: 0.2417 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.1656
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2

	R_factor	Num. reflection	% reflection
R_free	0.215	4230	4.97 %
R_work	0.1841	80949	-
obs	0.1856	85179	99.94 %

Solvent computation

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

Displacement parameters

B_iso mean: 50.15 Å²

Refinement step

Cycle: LAST / Resolution: 1.82→75.82 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5036	0	38	410	5484

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.0168	5231
X-RAY DIFFRACTION	f_angle_d	1.3121	7115
X-RAY DIFFRACTION	f_chiral_restr	0.095	758
X-RAY DIFFRACTION	f_plane_restr	0.0115	924
X-RAY DIFFRACTION	f_dihedral_angle_d	12.4374	1861

Refine LS restraints NCS

Ens-ID	Dom-ID	Asym-ID	Auth asym-ID	Refine-ID	Type	Rms dev position (Å)
ens_1	d_2	A	A	X-RAY DIFFRACTION	Torsion NCS	2.87512504701
ens_1	d_3	A	A	X-RAY DIFFRACTION	Torsion NCS	2.54500155035

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 (%)
1.82-1.84	0.4362	146	0.433	2640	X-RAY DIFFRACTION	99.36
1.84-1.86	0.3793	145	0.3789	2665	X-RAY DIFFRACTION	99.89
1.86-1.88	0.3314	141	0.31	2662	X-RAY DIFFRACTION	99.93
1.88-1.91	0.3139	154	0.2915	2670	X-RAY DIFFRACTION	99.89
1.91-1.93	0.327	120	0.269	2656	X-RAY DIFFRACTION	99.93
1.93-1.96	0.2745	144	0.256	2680	X-RAY DIFFRACTION	100
1.96-1.98	0.3063	125	0.2644	2695	X-RAY DIFFRACTION	99.96
1.98-2.01	0.2723	137	0.2692	2644	X-RAY DIFFRACTION	100
2.01-2.05	0.2971	157	0.2433	2673	X-RAY DIFFRACTION	100
2.05-2.08	0.2749	126	0.2354	2697	X-RAY DIFFRACTION	99.86
2.08-2.12	0.27	107	0.215	2686	X-RAY DIFFRACTION	99.93
2.12-2.15	0.2556	149	0.1926	2673	X-RAY DIFFRACTION	99.93
2.15-2.2	0.2251	161	0.1913	2659	X-RAY DIFFRACTION	99.96
2.2-2.24	0.2227	148	0.1859	2645	X-RAY DIFFRACTION	100
2.24-2.29	0.2524	117	0.182	2716	X-RAY DIFFRACTION	99.96
2.29-2.34	0.1757	132	0.1724	2699	X-RAY DIFFRACTION	100
2.34-2.4	0.2263	139	0.1823	2678	X-RAY DIFFRACTION	99.96
2.4-2.47	0.2125	134	0.1925	2718	X-RAY DIFFRACTION	99.96
2.47-2.54	0.2426	156	0.2056	2653	X-RAY DIFFRACTION	100
2.54-2.62	0.2493	137	0.2023	2714	X-RAY DIFFRACTION	100
2.62-2.71	0.2621	138	0.2001	2710	X-RAY DIFFRACTION	99.93
2.71-2.82	0.2399	149	0.193	2671	X-RAY DIFFRACTION	100
2.82-2.95	0.2175	139	0.1878	2698	X-RAY DIFFRACTION	99.96
2.95-3.11	0.2078	151	0.1736	2716	X-RAY DIFFRACTION	100
3.11-3.3	0.1987	154	0.1765	2706	X-RAY DIFFRACTION	100
3.3-3.56	0.1897	139	0.1504	2727	X-RAY DIFFRACTION	100
3.56-3.91	0.175	138	0.1428	2751	X-RAY DIFFRACTION	100
3.91-4.48	0.1414	150	0.1441	2743	X-RAY DIFFRACTION	100
4.48-5.64	0.1905	150	0.1531	2774	X-RAY DIFFRACTION	100
5.64-75.82	0.2641	147	0.2216	2930	X-RAY DIFFRACTION	99.9

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	8.37376137798	-0.263744655221	-1.53735094154	2.70247765641	1.46108386379	2.72948423113	-0.186097520673	-0.644892039636	0.693872038379	0.469460865968	-0.168425312021	0.645744643391	0.0110763011642	-0.557251728263	0.406783602845	0.382678866689	-0.02293626441	0.0163558420718	0.478985434652	-0.0516484061709	0.481432323216	35.3317572597	67.7625918704	-2.04991538912
2	3.12545124025	0.744228146844	-0.051606686724	2.17281091951	0.00485205485477	1.02152681709	-0.249585523315	0.614214115461	-0.310465413752	-0.360502617764	0.211548882124	-0.540831439085	0.0519894419985	0.231775559557	0.0818843490769	0.306404355569	-0.0357712439493	0.0793673920952	0.505335915245	-0.0669618910174	0.366553760081	61.602225661	72.5750961067	-12.003802957
3	2.92369622935	0.939428519799	-0.137694386476	3.06998288059	0.169108504599	1.44229907194	0.143845638834	-0.50029372198	-0.204432988878	0.436949753815	-0.157522912687	-0.107554943892	0.133343579522	0.216835391056	-0.0208653219008	0.29254082908	0.0241580438109	-0.0157007976786	0.385255152587	-0.00561718696974	0.268752968567	55.1690030104	71.7436588887	2.11849824864
4	4.79500628674	4.81131067921	1.28291424319	8.58906324708	1.7895893671	1.67745560505	-0.469977841166	0.489985756641	0.1955399681	-0.883060816089	0.492035103271	0.11498238489	-0.228756455536	0.136130234757	-0.0589085841158	0.329792860053	-0.0477548751099	0.0439588077541	0.413487807295	-0.0007132312923	0.246111905528	55.949338006	76.1201125484	-13.167784579
5	6.73489342581	0.183187318151	-1.1298568014	3.14361931136	-1.47390704009	2.34621036355	0.224035345412	1.41894258468	-0.944249999374	-0.64638254822	0.0120616611664	0.00586814367788	0.125445148138	-0.081734483904	-0.202168435553	0.458754446244	-0.0382983273722	-0.00607184142297	0.659377582849	-0.10571164002	0.388828965525	44.093002131	64.0931784014	-19.2219285973
6	5.03265494319	2.19702873062	1.95119649056	2.90272820011	1.50525769165	3.12774620044	-0.240060015621	0.269005940841	0.186699503658	-0.251027089064	0.227194296958	0.241092975942	-0.14324532395	-0.0235058345789	0.00807616513198	0.247955389982	0.000977175130613	0.0012169742893	0.339330660256	0.0334187204514	0.274522053598	43.1556153387	77.7808482598	-10.1350805435
7	7.40566097176	2.77278853264	5.02549422685	1.96305266984	2.47811673279	6.56467219624	-0.104417981361	0.028995186429	0.16778996331	-0.116043057411	0.0285777379293	0.183663062567	-0.0614649671897	-0.268152575435	0.152166650077	0.255191774868	0.0126567242986	0.0181907416621	0.345785170465	0.0634934181642	0.341408382613	37.7485875264	75.9595575563	-7.31450700774
8	4.08046020458	2.51287350122	4.85836364282	3.34863791619	5.09541962314	7.94724455433	-0.0283138091911	0.384071718513	-0.183574524914	-0.259464334221	0.0525966965204	0.174315561685	0.248575397532	-0.297463013055	-0.199180461016	0.355413361613	-0.05152191614	-0.0300684487303	0.47681681368	0.0116946539998	0.36741517883	40.510847304	70.477277255	-15.9960422384
9	5.71525727897	5.37612556822	0.262660300083	8.55997279422	0.745497161408	3.8103450358	-0.0679576396252	0.0312218072111	0.585403659223	-0.379516997538	-0.0170486977123	0.392076429133	-0.530633155785	0.103458189137	0.0637426207312	0.314047329502	0.0167429701684	0.0346787168269	0.359372305957	0.00914560982378	0.281523147452	54.0223242279	82.9516391575	-1.89388674472
10	4.7460088754	4.26439461055	4.07598631788	7.49896011641	2.45062169346	3.69704169556	0.194313072504	-0.297794089475	-0.00738251040369	0.194359405702	-0.246644919302	0.534875441499	0.272429803118	-0.354001731772	0.0108992418684	0.301809506171	-0.0417926188698	0.0554904575223	0.439456811928	-0.0130315486987	0.360131419676	28.0388358429	60.6829400259	-7.5694043634
11	5.31481500196	3.39025794132	-2.54431322548	4.83695534322	-2.43160154275	5.87130471078	0.170542109309	-0.147322678642	-0.361076733786	0.430923771317	-0.0320646839939	-0.258711843882	0.393787255853	0.185873495032	-0.078549050122	0.389570879911	0.0444691828029	-0.0733318502326	0.322137763276	-0.0456172003586	0.301770773572	56.56840235	89.0200568583	24.0836606146
12	2.07839523386	-0.454832131711	1.50901413857	4.27385436286	-0.164339736956	3.07894559743	0.307422769561	-0.00946003692518	-0.164572399429	0.0627892927771	-0.181689745022	-0.0617360864782	0.314784516979	0.640583936087	-0.0710679232158	0.366914572603	0.0275172971929	-0.0248534066878	0.243829633144	-0.0871741712504	0.316197655411	52.2312793382	84.4241414324	17.2497097479
13	6.96405466604	0.0344296017118	-0.250468778127	2.54664167873	0.25164638275	4.04088958209	0.110284183769	-0.706536332689	0.0849432009752	0.32310229417	-0.100751019366	0.0191968808173	0.356505021249	0.0506338214253	-0.0126632643403	0.372013360709	0.0318056224679	-0.0036923502408	0.293659285187	-0.0454809805904	0.258913418757	53.6622552034	90.0079410548	28.3140335687
14	2.79596179986	0.0103017981314	-0.1797877299	3.55147713822	1.37722913839	4.7970052133	0.04867997815	-0.034046720935	0.236107863787	-0.154833907707	-0.0381093892944	-0.0215914776807	-0.316510321115	-0.167248099959	-0.00236879786793	0.274455169269	0.0439621924296	0.0229779715759	0.253449650809	-0.0214508737909	0.304377862126	48.4230176522	99.7114609097	21.273196082
15	4.94810758414	-0.78661956173	5.55251948106	6.38892861195	-1.00403848425	6.26444745435	-0.662013672556	0.758889168574	1.54829573494	0.512970632827	0.313151939012	-0.874623254173	-1.9781641194	1.58251293129	0.387521944848	0.744661660973	-0.129312989973	0.0575493584525	0.590503059144	-0.108846229568	0.758415841665	60.0781837572	111.543522998	26.419968246
16	6.55858029603	1.91334657236	-2.26191353846	3.65890464737	0.711954994333	5.95820440338	0.0393996717213	0.0938907614005	0.202003799556	0.044125282346	-0.15990319744	0.4454279543	0.295889449324	-0.883833867049	0.0763442942585	0.376384643815	-0.0461508670645	0.0365030764875	0.35209229414	-0.0544548077314	0.306775748127	42.476433995	92.4590560596	26.3036952066
17	5.38806129978	1.06997244528	-2.793783411	0.687721523026	-1.82325540177	4.67660434335	0.139935882062	0.140034762271	0.821832053535	0.0151507334963	0.100182744432	-0.0807578255823	-0.48662374497	0.405677958057	-0.24084394221	0.383929348533	0.0100834774912	0.0122599033353	0.328488084074	-0.0590847439799	0.418561884908	60.8478656016	102.010196582	15.1915398513
18	2.19842343471	0.0486313172012	-0.205978158776	6.01819688799	-0.199167473896	2.84743973886	-0.0984992453155	-0.143933827631	-0.161681760606	0.352668646383	0.112045595661	-0.36985300739	0.261587977509	0.152540926587	-0.0116528239693	0.279173029852	0.0423368982985	-0.0186055965279	0.303556396287	0.044541305539	0.280761200412	43.5426062777	52.7986464239	6.52480332766
19	2.83946029941	0.855166148876	-0.0158621544447	7.13796250942	-0.33413077657	1.33190870107	-0.124256147453	0.24241773844	-0.287276777016	-0.744936647308	0.0655870911409	-0.167810622264	0.843764061267	0.115194745709	0.0678053785661	0.516468064556	0.0311022453467	0.0440704014088	0.256172660933	-0.069990343098	0.332638647139	40.8263047553	44.4826655327	-3.33300939794
20	1.36271350972	-1.72117583981	-0.528002515233	5.2740087178	0.00924716667864	2.2060961632	-0.111193625615	-0.465519627085	0.00636238511449	0.522310875941	0.0951515262636	-0.473498405852	0.399920758045	0.279418932265	-0.0306376674648	0.392947084401	0.0408375512722	-0.0457534954457	0.430196204087	0.0733980389624	0.332932193228	43.7408728892	51.087868372	13.3158799258
21	3.05650804811	0.245155138191	0.99075659539	2.45422299207	-0.299395210809	6.54785217181	-0.00990210616758	-0.252411957455	-0.158109864583	0.109218870411	0.0406626773851	-0.0116055674807	-0.0460509180268	-0.252312005263	-0.0415951921844	0.239635719625	-0.00332761644963	0.0171505659304	0.263282486331	0.0536145940656	0.298203046379	32.7659019592	55.5046202307	9.91424181937
22	4.04608564412	4.02624805263	5.67621155278	9.65456492653	5.69991998547	8.29979003761	0.387739014541	-0.536617663823	-0.123510062259	0.944993697754	-0.562657135132	-0.332061881545	0.553300873216	-0.218045662452	-0.0898627342557	0.375132982911	-0.0570977190936	-0.000144053173053	0.391064477536	0.0520377868876	0.358640346914	39.4006485273	55.0134521039	16.0297489112
23	2.27104007695	0.425431539637	-1.1178504815	4.87912441488	-0.142074815141	3.35401307161	-0.198385315019	0.0949094742614	-0.2328697891	-0.61851859777	0.167607521545	0.303417579087	0.462701339381	-0.265413084408	0.0157229756786	0.345022099382	-0.0308190130703	-0.0893395996805	0.319774882198	0.0419271185056	0.334303856291	32.1208285602	49.2129274262	1.81831786026
24	2.22904981144	2.79734482629	-1.62526756011	3.46447380452	-2.27492998218	4.00155337368	0.265765088392	-2.00305059421	1.47575775116	0.346734195728	-0.29173992078	-0.225235765269	-0.592655733502	1.19100544042	0.0193456477851	0.424029631314	-0.052161196507	0.00175493441376	0.713711078864	-0.1433869209	0.497042476008	49.7318276028	74.9863503706	10.737099437

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

ID	Refine TLS-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	chain 'A' and (resid 47 through 58 )	A	A	47 - 58	1 - 12
2	2	chain 'A' and (resid 59 through 107 )	A	A	59 - 107	13 - 61
3	3	chain 'A' and (resid 108 through 130 )	A	A	108 - 130	62 - 80
4	4	chain 'A' and (resid 131 through 148 )	A	A	131 - 148	81 - 98
5	5	chain 'A' and (resid 149 through 175 )	A	A	149 - 175	99 - 112
6	6	chain 'A' and (resid 176 through 211 )	A	A	176 - 211	113 - 148
7	7	chain 'A' and (resid 212 through 233 )	A	A	212 - 233	149 - 170
8	8	chain 'A' and (resid 234 through 250 )	A	A	234 - 250	171 - 187
9	9	chain 'A' and (resid 251 through 265 )	A	A	251 - 265	188 - 202
10	10	chain 'A' and (resid 266 through 278 )	A	A	266 - 278	203 - 215
11	11	chain 'B' and (resid 51 through 92 )	B	B	51 - 92	1 - 35
12	12	chain 'B' and (resid 93 through 121 )	B	B	93 - 121	36 - 63
13	13	chain 'B' and (resid 122 through 171 )	B	B	122 - 171	64 - 100
14	14	chain 'B' and (resid 172 through 223 )	B	B	172 - 223	101 - 152
15	15	chain 'B' and (resid 224 through 241 )	B	B	224 - 241	153 - 167
16	16	chain 'B' and (resid 242 through 258 )	B	B	242 - 258	168 - 184
17	17	chain 'B' and (resid 259 through 285 )	B	B	259 - 285	185 - 210
18	18	chain 'C' and (resid 46 through 92 )	C	C	46 - 92	1 - 40
19	19	chain 'C' and (resid 93 through 130 )	C	C	93 - 130	41 - 76
20	20	chain 'C' and (resid 131 through 178 )	C	C	131 - 178	77 - 112
21	21	chain 'C' and (resid 179 through 233 )	C	C	179 - 233	113 - 167
22	22	chain 'C' and (resid 234 through 250 )	C	C	234 - 250	168 - 183
23	23	chain 'C' and (resid 251 through 270 )	C	C	251 - 270	184 - 203
24	24	chain 'C' and (resid 271 through 286 )	C	C	271 - 286	204 - 218

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