PDB-7km6: APOBEC3B antibody 5G7 Fv-clasp

ID or keywords:

Entry

Database: PDB / ID: 7km6

Title

APOBEC3B antibody 5G7 Fv-clasp

Components

(5G7 human monoclonal FAB ...) x 2

Keywords

IMMUNE SYSTEM

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.67 Å

Authors

Tang, H. / Shi, K. / Aihara, H.

Funding support

United States,

China, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	GM118047	United States
National Natural Science Foundation of China (NSFC)	31470160	China

Citation

Journal: Viruses / Year: 2021
Title: Structural Characterization of a Minimal Antibody against Human APOBEC3B.
Authors: Tang, H. / Demir, O. / Kurniawan, F. / Brown, W.L. / Shi, K. / Moeller, N.H. / Carpenter, M.A. / Belica, C. / Orellana, K. / Du, G. / LeBeau, A.M. / Amaro, R.E. / Harris, R.S. / Aihara, H.

History

Deposition	Nov 2, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 12, 2021	Provider: repository / Type: Initial release
Revision 1.1	Oct 18, 2023	Group: 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

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7km6.cif.gz	298.3 KB	Display	PDBx/mmCIF format
PDB format	pdb7km6.ent.gz	240.9 KB	Display	PDB format
PDBx/mmJSON format	7km6.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	7km6_validation.pdf.gz	436 KB	Display	wwPDB validaton report
Full document	7km6_full_validation.pdf.gz	435.9 KB	Display
Data in XML	7km6_validation.xml.gz	30 KB	Display
Data in CIF	7km6_validation.cif.gz	43.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/km/7km6 ftp://data.pdbj.org/pub/pdb/validation_reports/km/7km6	HTTPS FTP

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Related structure data

Related structure data	5xcqS S: Starting model for refinement
Similar structure data	5xcx-d 5xcu-2 5xcs-d 7km6-2 5xcv-2 6240 5xcu-1 1v4a-d 3qb0-3 6rrc-2 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details)

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1)

Deposited unit

L: 5G7 human monoclonal FAB light chain

H: 5G7 human monoclonal FAB heavy chain

l: 5G7 human monoclonal FAB light chain

h: 5G7 human monoclonal FAB heavy chain

hetero molecules

78.3 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

L: 5G7 human monoclonal FAB light chain

H: 5G7 human monoclonal FAB heavy chain

hetero molecules

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

2

l: 5G7 human monoclonal FAB light chain

h: 5G7 human monoclonal FAB heavy chain

hetero molecules

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

Unit cell

Length a, b, c (Å)	54.074, 68.823, 88.759
Angle α, β, γ (deg.)	90.000, 107.050, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain H and (resid 1 through 21 or resid 23...
2	1	(chain h and (resid 1 through 21 or resid 23...
1	2	(chain L and (resid 1 through 13 or resid 15...
2	2	(chain l and (resid 1 through 13 or resid 15...

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	GLU	GLU	SER	SER	(chain H and (resid 1 through 21 or resid 23...	H	B	1 - 21	2 - 22
1	2	1	ALA	ALA	SER	SER	(chain H and (resid 1 through 21 or resid 23...	H	B	23 - 30	24 - 31
1	3	1	TYR	TYR	ALA	ALA	(chain H and (resid 1 through 21 or resid 23...	H	B	32 - 92	33 - 93
1	4	1	GLU	GLU	HIS	HIS	(chain H and (resid 1 through 21 or resid 23...	H	B	1 - 170	2 - 171
1	5	1	TRP	TRP	ILE	ILE	(chain H and (resid 1 through 21 or resid 23...	H	B	128 - 148	129 - 149
1	6	1	GLU	GLU	HIS	HIS	(chain H and (resid 1 through 21 or resid 23...	H	B	1 - 170	2 - 171
1	7	1	GLN	GLN	LYS	LYS	(chain H and (resid 1 through 21 or resid 23...	H	B	156 - 158	157 - 159
1	8	1	GLN	GLN	HIS	HIS	(chain H and (resid 1 through 21 or resid 23...	H	B	160 - 170	161 - 171
2	1	1	GLU	GLU	SER	SER	(chain h and (resid 1 through 21 or resid 23...	h	D	1 - 21	2 - 22
2	2	1	ALA	ALA	SER	SER	(chain h and (resid 1 through 21 or resid 23...	h	D	23 - 30	24 - 31
2	3	1	TYR	TYR	ALA	ALA	(chain h and (resid 1 through 21 or resid 23...	h	D	32 - 92	33 - 93
2	4	1	MET	MET	HIS	HIS	(chain h and (resid 1 through 21 or resid 23...	h	D	0 - 170	1 - 171
2	5	1	TRP	TRP	ILE	ILE	(chain h and (resid 1 through 21 or resid 23...	h	D	128 - 148	129 - 149
2	6	1	MET	MET	HIS	HIS	(chain h and (resid 1 through 21 or resid 23...	h	D	0 - 170	1 - 171
2	7	1	GLN	GLN	LYS	LYS	(chain h and (resid 1 through 21 or resid 23...	h	D	156 - 158	157 - 159
2	8	1	GLN	GLN	HIS	HIS	(chain h and (resid 1 through 21 or resid 23...	h	D	160 - 170	161 - 171
1	1	2	ASP	ASP	VAL	VAL	(chain L and (resid 1 through 13 or resid 15...	L	A	1 - 13	2 - 14
1	2	2	VAL	VAL	THR	THR	(chain L and (resid 1 through 13 or resid 15...	L	A	15 - 20	16 - 21
1	3	2	MET	MET	ALA	ALA	(chain L and (resid 1 through 13 or resid 15...	L	A	0 - 164	1 - 165
1	4	2	MET	MET	ALA	ALA	(chain L and (resid 1 through 13 or resid 15...	L	A	0 - 164	1 - 165
1	5	2	LEU	LEU	TYR	TYR	(chain L and (resid 1 through 13 or resid 15...	L	A	89 - 93	90 - 94
1	6	2	GLN	GLN	TYR	TYR	(chain L and (resid 1 through 13 or resid 15...	L	A	95 - 98	96 - 99
1	7	2	MET	MET	MET	MET	(chain L and (resid 1 through 13 or resid 15...	L	A	0	1
1	8	2	ARG	ARG	TYR	TYR	(chain L and (resid 1 through 13 or resid 15...	L	A	148 - 151	149 - 152
1	9	2	ARG	ARG	TYR	TYR	(chain L and (resid 1 through 13 or resid 15...	L	A	148 - 151	149 - 152
1	10	2	SER	SER	PRO	PRO	(chain L and (resid 1 through 13 or resid 15...	L	A	153 - 157	154 - 158
2	1	2	ASP	ASP	VAL	VAL	(chain l and (resid 1 through 13 or resid 15...	l	C	1 - 13	2 - 14
2	2	2	VAL	VAL	THR	THR	(chain l and (resid 1 through 13 or resid 15...	l	C	15 - 20	16 - 21
2	3	2	SER	SER	SER	SER	(chain l and (resid 1 through 13 or resid 15...	l	C	22	23
2	4	2	ILE	ILE	ILE	ILE	(chain l and (resid 1 through 13 or resid 15...	l	C	2	3
2	5	2	SER	SER	LEU	LEU	(chain l and (resid 1 through 13 or resid 15...	l	C	28 - 89	29 - 90
2	6	2	LEU	LEU	TYR	TYR	(chain l and (resid 1 through 13 or resid 15...	l	C	89 - 98	90 - 99
2	7	2	SER	SER	SER	SER	(chain l and (resid 1 through 13 or resid 15...	l	C	9	10
2	8	2	MET	MET	LYS	LYS	(chain l and (resid 1 through 13 or resid 15...	l	C	0 - 165	1 - 166
2	9	2	MET	MET	LYS	LYS	(chain l and (resid 1 through 13 or resid 15...	l	C	0 - 165	1 - 166
2	10	2	ARG	ARG	TYR	TYR	(chain l and (resid 1 through 13 or resid 15...	l	C	148 - 151	149 - 152
2	11	2	SER	SER	PRO	PRO	(chain l and (resid 1 through 13 or resid 15...	l	C	153 - 157	154 - 158

NCS ensembles :

ID
1
2

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Antibody , 2 types, 4 molecules LlHh

#1: Antibody	5G7 human monoclonal FAB light chain Mass: 18769.143 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)
#2: Antibody	5G7 human monoclonal FAB heavy chain Mass: 19997.412 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli)

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Non-polymers , 4 types, 431 molecules

#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#5: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 416 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	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: 2.04 Å³/Da / Density % sol: 39.6 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion Details: 100 mM Bis-Tris/Hydrochloric acid pH 6.5, 400 mM sodium chloride, 30% (w/v) PEG 3350

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 24-ID-C / Wavelength: 0.9792 Å

Detector

Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 28, 2018

Radiation

Monochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.9792 Å / Relative weight: 1

Reflection

Resolution: 1.65→84.86 Å / Num. obs: 71357 / % possible obs: 97.5 % / Redundancy: 3.7 % / B_iso Wilson estimate: 24.66 Å² / CC_1/2: 0.996 / R_merge(I) obs: 0.088 / R_pim(I) all: 0.053 / R_rim(I) all: 0.104 / Net I/σ(I): 7.6

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. measured all	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Net I/σ(I) obs	% possible all
1.65-1.68	2.7	0.833	7310	2724	0.6	0.537	0.998	0.9	74.1
9.05-84.86	3.5	0.05	1657	479	0.997	0.031	0.059	20.8	99

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Processing

Software

Name	Version	Classification
PHENIX	1.19.2_4158	refinement
Aimless	0.5.32	data scaling
PDB_EXTRACT	3.27	data extraction
XDS		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5XCQ

5xcq

Resolution: 1.67→84.86 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 28.1 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2384	6391	4.68 %
R_work	0.1887	130094	-
obs	0.1909	71268	96.08 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso max: 129.51 Å² / B_iso mean: 33.5936 Å² / B_iso min: 17.26 Å²

Refinement step

Cycle: final / Resolution: 1.67→84.86 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5323	0	45	417	5785
B_iso mean	-	-	49.94	43.55	-
Num. residues	-	-	-	-	672

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.009	5657
X-RAY DIFFRACTION	f_angle_d	0.99	7649
X-RAY DIFFRACTION	f_chiral_restr	0.061	806
X-RAY DIFFRACTION	f_plane_restr	0.007	983
X-RAY DIFFRACTION	f_dihedral_angle_d	12.626	2123

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	H	1500	X-RAY DIFFRACTION	4.461	TORSIONAL
1	2	h	1500	X-RAY DIFFRACTION	4.461	TORSIONAL
2	1	L	1334	X-RAY DIFFRACTION	4.461	TORSIONAL
2	2	l	1334	X-RAY DIFFRACTION	4.461	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.67-1.69	0.3855	214	0.3748	4124	4338	90
1.69-1.71	0.3415	205	0.3569	4307	4512	96
1.71-1.73	0.3756	205	0.3422	4281	4486	96
1.73-1.75	0.3252	234	0.3243	4354	4588	96
1.75-1.77	0.3188	230	0.3179	4285	4515	96
1.77-1.8	0.3267	229	0.3164	4316	4545	96
1.8-1.82	0.3336	223	0.2974	4260	4483	95
1.82-1.85	0.3435	242	0.2974	4311	4553	96
1.85-1.88	0.3085	208	0.2969	4357	4565	96
1.88-1.91	0.3182	228	0.2896	4364	4592	96
1.91-1.94	0.3257	190	0.2685	4332	4522	96
1.94-1.98	0.2669	256	0.2559	4226	4482	95
1.98-2.02	0.2925	154	0.2328	4298	4452	95
2.02-2.06	0.2751	232	0.225	4119	4351	93
2.06-2.1	0.2352	203	0.2162	4308	4511	95
2.1-2.15	0.2287	250	0.2095	4439	4689	98
2.15-2.21	0.2646	234	0.2013	4419	4653	98
2.21-2.27	0.2318	210	0.196	4403	4613	98
2.27-2.33	0.2517	234	0.1946	4424	4658	98
2.33-2.41	0.2328	209	0.1873	4424	4633	98
2.41-2.49	0.2469	207	0.1852	4404	4611	98
2.49-2.59	0.234	175	0.1851	4432	4607	97
2.59-2.71	0.2237	221	0.1761	4353	4574	97
2.71-2.86	0.2051	187	0.1717	4347	4534	96
2.86-3.03	0.2238	177	0.1722	4238	4415	93
3.03-3.27	0.2337	202	0.1722	4413	4615	98
3.27-3.6	0.2075	216	0.1518	4442	4658	98
3.6-4.12	0.2095	138	0.1397	4450	4588	97
4.12-5.19	0.1689	202	0.1356	4379	4581	97
5.19-84.86	0.2303	276	0.1729	4285	4561	96

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	1.5956	1.0372	0.5852	2.3985	0.7976	1.4914	-0.0261	0.0358	0.0838	-0.0756	-0.04	0.1864	-0.106	-0.1028	0.0633	0.2098	0.0168	0.0158	0.217	0.0126	0.2397	7.0539	-9.2591	-35.4234
2	5.4024	1.177	2.026	6.8249	5.9396	9.4993	0.3986	0.2608	0.3881	0.0103	-0.809	0.8872	0.3603	-0.9671	0.4246	0.2903	0.0836	0.028	0.431	0.0066	0.4663	-11.1404	-26.9717	-42.2711
3	7.1627	-7.0098	7.5435	6.8527	-7.4357	8.0123	-0.1814	0.2505	0.2418	0.2229	-0.21	-0.088	-0.2242	0.0686	0.2179	0.318	-0.0193	0.0077	0.2612	-0.011	0.2395	10.0802	-37.9939	-33.3935
4	1.998	-0.2618	0.2087	1.9164	-0.2892	3.1599	0.0455	0.0342	0.0398	-0.0229	0.0277	-0.1279	0.0499	0.1767	-0.0663	0.1503	0.0169	-0.0092	0.1907	-0.0106	0.1912	24.5942	-21.0922	-31.917
5	0.0413	-0.2543	0.379	6.863	-7.3851	8.2812	-0.0505	-0.1078	-0.003	0.6047	0.1194	0.0853	-0.5794	0.0577	-0.0653	0.3259	0.037	-0.0242	0.3319	0.0395	0.2841	20.4044	-43.7933	-15.2049
6	4.4397	-4.807	5.1047	5.2628	-5.6205	5.9933	0.3548	0.2146	-0.2563	-0.2029	-0.0773	0.4023	0.53	-0.1772	-0.4056	0.4138	-0.0329	-0.005	0.3163	-0.059	0.2978	3.1772	-45.0142	-34.7095
7	3.7325	-3.3854	-3.7324	8.7154	3.6864	6.8498	-0.0602	1.146	-0.0198	-0.4515	-0.3702	0.6614	-0.0004	-0.3231	0.2332	0.2783	-0.0565	0.0329	0.3165	0.0291	0.2969	2.4903	-4.6481	-19.0553
8	7.1395	-5.8199	7.5092	5.4634	-5.4055	9.8444	-0.1636	-0.1017	0.5536	0.2844	0.0027	-0.3762	-0.4506	0.3815	0.1819	0.2337	-0.0227	0.0434	0.3759	-0.0132	0.3494	15.652	-8.9395	-9.0961
9	6.3042	-2.2071	-4.2022	7.3608	3.4354	7.4168	0.3779	-0.3296	0.8106	-0.094	0.1225	-0.4113	-0.7787	-0.3606	-0.4482	0.2625	0.0277	0.025	0.1694	-0.003	0.315	-1.8038	5.882	-9.5129
10	2.1713	-0.0533	0.4588	5.486	-0.3842	1.3029	0.0663	-0.1365	-0.2088	0.0054	-0.1141	-0.062	0.1174	0.0871	0.0177	0.169	0.0254	0.0076	0.2233	-0.0077	0.284	3.7627	-13.943	-3.9386
11	2.7453	-1.6599	1.3118	3.6189	-1.4695	3.5205	-0.0258	-0.09	0.2044	0.1889	0.0523	-0.1944	-0.1131	0.1613	-0.0191	0.2271	-0.0064	-0.0044	0.2908	-0.046	0.3306	7.4592	-3.296	-1.4955
12	4.2495	-1.4149	1.1712	3.6196	-0.4693	1.853	-0.0527	-0.3076	0.0473	0.2	0.1937	-0.2236	-0.1082	0.0239	-0.1594	0.2097	0.0088	0.0196	0.2256	-0.0096	0.2537	9.9499	-12.463	-4.3145
13	5.6214	-0.1759	1.8967	2.9667	0.2306	3.4995	-0.1585	0.3378	-0.1892	0.0337	-0.0093	0.405	-0.0865	-0.1834	0.1241	0.2289	0.0047	0.0208	0.2095	0.0181	0.213	-2.5725	-6.0581	-13.5327
14	4.9101	-6.5009	5.4828	8.6072	-7.2596	6.124	0.4694	0.3555	0.0121	-0.5071	-0.634	-0.2442	0.634	0.5468	0.0381	0.3604	0.0215	-0.0034	0.4242	0.0571	0.4207	22.8249	-23.1133	-5.3462
15	9.0361	-1.8262	-5.0923	5.9184	2.3066	3.1642	-0.0188	-1.1084	0.8114	0.2507	0.2216	-0.7018	-0.018	0.8107	-0.2	0.362	-0.0466	-0.0708	0.5323	0.0206	0.5127	25.4842	-24.1024	6.0821
16	7.3709	5.9562	7.152	5.9045	6.9137	8.6143	-0.0087	-0.1916	0.2369	-0.0391	-0.3534	0.2474	0.0535	-0.269	0.4102	0.29	0.0341	0.0011	0.2277	0.015	0.3137	2.0518	-35.6376	-9.2148
17	2.0078	-1.1924	-1.2731	6.5883	5.5035	6.419	0.0555	-0.1994	-0.0269	0.1132	0.015	-0.0403	0.2175	-0.1377	-0.0775	0.1445	-0.0361	0.0031	0.1753	0.014	0.2372	-12.6004	-25.1244	-7.9318
18	1.9788	0.0136	0.3202	1.644	0.4174	2.5355	0.0131	0.068	-0.0411	-0.0697	-0.0026	-0.0019	0.0228	-0.0342	0	0.1596	0.0068	0.0036	0.1972	-0.0204	0.2112	-11.2476	-17.6518	-12.0629
19	2.2835	0.4705	2.8903	1.9804	-2.1902	7.7783	0.5508	0.1024	-0.0121	-0.1955	-0.1203	0.5532	-0.8712	-0.3623	-0.3257	0.565	0.0793	0.1126	0.4955	-0.2391	0.5451	-9.6819	-49.567	-30.5428
20	4.5665	5.6567	4.9529	6.9932	6.149	5.3845	0.2355	-0.1175	-0.2079	0.2191	-0.0195	-0.3295	0.369	0.1637	-0.378	0.3373	0.0162	-0.0079	0.3359	0.0266	0.3412	9.8852	-41.7105	-7.0487

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'L' and (resid 0 through 108 )	L	0 - 108
2	X-RAY DIFFRACTION	2	chain 'L' and (resid 109 through 125 )	L	109 - 125
3	X-RAY DIFFRACTION	3	chain 'L' and (resid 126 through 164 )	L	126 - 164
4	X-RAY DIFFRACTION	4	chain 'H' and (resid 1 through 111 )	H	1 - 111
5	X-RAY DIFFRACTION	5	chain 'H' and (resid 112 through 129 )	H	112 - 129
6	X-RAY DIFFRACTION	6	chain 'H' and (resid 130 through 170 )	H	130 - 170
7	X-RAY DIFFRACTION	7	chain 'l' and (resid 0 through 7 )	l	0 - 7
8	X-RAY DIFFRACTION	8	chain 'l' and (resid 8 through 25 )	l	8 - 25
9	X-RAY DIFFRACTION	9	chain 'l' and (resid 26 through 38 )	l	26 - 38
10	X-RAY DIFFRACTION	10	chain 'l' and (resid 39 through 54 )	l	39 - 54
11	X-RAY DIFFRACTION	11	chain 'l' and (resid 55 through 81 )	l	55 - 81
12	X-RAY DIFFRACTION	12	chain 'l' and (resid 82 through 96 )	l	82 - 96
13	X-RAY DIFFRACTION	13	chain 'l' and (resid 97 through 108 )	l	97 - 108
14	X-RAY DIFFRACTION	14	chain 'l' and (resid 109 through 118 )	l	109 - 118
15	X-RAY DIFFRACTION	15	chain 'l' and (resid 119 through 125 )	l	119 - 125
16	X-RAY DIFFRACTION	16	chain 'l' and (resid 126 through 165 )	l	126 - 165
17	X-RAY DIFFRACTION	17	chain 'h' and (resid 0 through 25 )	h	0 - 25
18	X-RAY DIFFRACTION	18	chain 'h' and (resid 26 through 122 )	h	26 - 122
19	X-RAY DIFFRACTION	19	chain 'h' and (resid 123 through 129 )	h	123 - 129
20	X-RAY DIFFRACTION	20	chain 'h' and (resid 130 through 170 )	h	130 - 170

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