PDB-8tvd: Fab 221-11 in complex with OspA

ID or keywords:

Entry

Database: PDB / ID: 8tvd

Title

Fab 221-11 in complex with OspA

Components

Heavy chain of Fab 221-11
Light chain of Fab 221-11
Outer surface protein A

Keywords

IMMUNE SYSTEM/Membrane Protein / monoclonal antibody / IMMUNE SYSTEM / IMMUNE SYSTEM-Membrane Protein complex

Function / homology

Outer surface lipoprotein, Borrelia / Outer surface lipoprotein domain superfamily / Borrelia lipoprotein / cell outer membrane / Prokaryotic membrane lipoprotein lipid attachment site profile. / cell surface / membrane / Outer surface protein A

Function and homology information

Biological species

Homo sapiens (human)

Borreliella burgdorferi B31 (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.077 Å

Authors

Rudolph, M.J. / Mantis, N.

Funding support

United States, 1items

Citation

Journal: To Be Published
Title: Fab 221-11 in complex with OspA
Authors: Rudolph, M.J. / Mantis, N.

History

Deposition	Aug 18, 2023	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 28, 2024	Provider: repository / Type: Initial release
Revision 1.1	Oct 30, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

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Others	Other downloads

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Validation report

Summary document	8tvd_validation.pdf.gz	480.8 KB	Display	wwPDB validaton report
Full document	8tvd_full_validation.pdf.gz	495.6 KB	Display
Data in XML	8tvd_validation.xml.gz	45.6 KB	Display
Data in CIF	8tvd_validation.cif.gz	61.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/tv/8tvd ftp://data.pdbj.org/pub/pdb/validation_reports/tv/8tvd	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	#21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1) #261 - Sep 2021 DNA-Sequencing Nanopores similarity (1) #22 - Oct 2001 Photosystem I similarity (1) #262 - Oct 2021 Fifty Years of Open Access to PDB Structures similarity (1) #29 - May 2002 Penicillin-binding Proteins similarity (1) #95 - Nov 2007 Multidrug Resistance Transporters similarity (1)

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)
#261 - Sep 2021
DNA-Sequencing Nanopores
similarity (1)
#22 - Oct 2001
Photosystem I
similarity (1)
#262 - Oct 2021
Fifty Years of Open Access to PDB Structures
similarity (1)
#29 - May 2002
Penicillin-binding Proteins
similarity (1)
#95 - Nov 2007
Multidrug Resistance Transporters
similarity (1)

Deposited unit

L: Light chain of Fab 221-11

H: Heavy chain of Fab 221-11

E: Outer surface protein A

A: Light chain of Fab 221-11

B: Heavy chain of Fab 221-11

C: Outer surface protein A

hetero molecules

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

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	107.812, 107.812, 316.850
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	91
Space group name H-M	P4₁22

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Protein , 1 types, 2 molecules EC

#3: Protein	Outer surface protein A Mass: 26821.172 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Borreliella burgdorferi B31 (bacteria) / Gene: ospA / Production host: Escherichia coli B (bacteria) / References: UniProt: P0CL66

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Antibody , 2 types, 4 molecules LAHB

#1: Antibody	Light chain of Fab 221-11 Mass: 22921.387 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)
#2: Antibody	Heavy chain of Fab 221-11 Mass: 23803.768 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)

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Non-polymers , 3 types, 18 molecules

#4: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO₄
#5: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	N
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: 3.15 Å³/Da / Density % sol: 61.01 %
Crystal grow	Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 4% pentaerythritol ethoxylate, 2.2 M ammonium sulfate, and 100 mM sodium acetate pH 4.6. 2.0 M Tri-ammonium citrate and 5% MPD.

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 24-ID-E / Wavelength: 0.979 Å

Detector

Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 14, 2021

Radiation

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

Radiation wavelength

Wavelength: 0.979 Å / Relative weight: 1

Reflection

Resolution: 3.05→50 Å / Num. obs: 35457 / % possible obs: 99.4 % / Redundancy: 15.2 % / CC_1/2: 0.6 / Net I/σ(I): 2.3

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	CC star	R_pim(I) all	R_rim(I) all	Χ²	% possible all
3.05-3.1	16.1	2.961	1719	0.571	0.853	0.756	3.058	0.318	100
3.1-3.16	14.9	2.447	1758	0.551	0.843	0.653	2.534	0.321	100
3.16-3.22	16	2.269	1739	0.617	0.873	0.58	2.343	0.337	100
3.22-3.29	17.4	2.025	1738	0.661	0.892	0.495	2.086	0.343	99.9
3.29-3.36	17.2	1.68	1748	0.789	0.939	0.413	1.731	0.374	99.9
3.36-3.43	16.2	1.38	1756	0.802	0.944	0.351	1.425	0.451	99.9
3.43-3.52	17.4	1.147	1740	0.881	0.968	0.281	1.182	0.472	99.9
3.52-3.62	17.6	1.015	1753	0.88	0.967	0.247	1.046	0.478	100
3.62-3.72	17.3	0.866	1753	0.903	0.974	0.213	0.893	0.579	100
3.72-3.84	17	0.715	1760	0.905	0.975	0.179	0.738	0.65	99.9
3.84-3.98	16.4	0.613	1765	0.934	0.983	0.157	0.634	0.765	99.7
3.98-4.14	15.7	0.528	1755	0.933	0.982	0.139	0.547	0.896	99.8
4.14-4.33	14.5	0.435	1763	0.943	0.985	0.121	0.453	1.222	99.2
4.33-4.56	12.2	0.357	1753	0.943	0.985	0.109	0.374	1.623	98.5
4.56-4.84	11.6	0.322	1766	0.886	0.969	0.102	0.339	1.812	98.2
4.84-5.21	13.1	0.308	1757	0.924	0.98	0.092	0.323	1.851	98.8
5.21-5.74	14.8	0.288	1799	0.961	0.99	0.081	0.301	1.871	99
5.74-6.57	15.5	0.259	1820	0.977	0.994	0.071	0.269	1.869	99.5
6.57-8.27	12.8	0.203	1859	0.969	0.992	0.065	0.215	2.325	99.1
8.27-50	10.3	0.127	1956	0.982	0.996	0.046	0.136	2.97	97.3

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Processing

Software

Name	Version	Classification
PHENIX	(1.11.1_2575: ???)	refinement
HKL-2000		data reduction
HKL-2000		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.077→48.732 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 2.09 / Phase error: 28.66 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.286	1735	4.9 %
R_work	0.2343	-	-
obs	0.2369	35384	99.04 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.077→48.732 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10053	0	31	11	10095

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	10270
X-RAY DIFFRACTION	f_angle_d	0.589	13903
X-RAY DIFFRACTION	f_dihedral_angle_d	2.498	6530
X-RAY DIFFRACTION	f_chiral_restr	0.044	1609
X-RAY DIFFRACTION	f_plane_restr	0.004	1741

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 (%)
3.077-3.1672	0.3915	130	0.3588	2666	X-RAY DIFFRACTION	95
3.1672-3.2694	0.3736	137	0.3398	2759	X-RAY DIFFRACTION	100
3.2694-3.3862	0.3498	154	0.3072	2759	X-RAY DIFFRACTION	100
3.3862-3.5217	0.3402	149	0.2789	2771	X-RAY DIFFRACTION	100
3.5217-3.682	0.288	125	0.2476	2795	X-RAY DIFFRACTION	100
3.682-3.876	0.2837	154	0.243	2787	X-RAY DIFFRACTION	100
3.876-4.1188	0.2814	146	0.2345	2807	X-RAY DIFFRACTION	100
4.1188-4.4366	0.2703	139	0.2028	2790	X-RAY DIFFRACTION	99
4.4366-4.8827	0.2636	138	0.183	2798	X-RAY DIFFRACTION	98
4.8827-5.5883	0.2392	142	0.1917	2820	X-RAY DIFFRACTION	99
5.5883-7.0373	0.3279	167	0.2403	2868	X-RAY DIFFRACTION	99
7.0373-48.732	0.2457	154	0.2191	3029	X-RAY DIFFRACTION	98

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	9.2859	2.7604	-4.5696	4.0992	-3.1358	3.5826	0.3543	-1.9583	0.7559	1.1694	-0.1724	0.0065	-0.9039	0.374	-0.3204	0.7665	-0.0477	0.1644	0.9704	-0.1902	0.5165	3.1236	-28.0922	-7.9133
2	3.9641	-1.2056	0.7728	4.8857	0.8844	6.2821	0.9987	-0.3347	0.7939	-0.3874	0.0761	0.0899	-0.9709	0.1774	-1.0063	1.1227	-0.0444	0.4037	1.1211	-0.0681	0.5799	-3.6845	-24.9775	-13.5374
3	2.172	2.1865	-1.2157	4.959	-0.1628	0.7267	-0.014	0.218	-0.0349	-0.2253	0.2553	-0.1666	0.2367	0.6396	-0.1267	0.5133	-0.0189	-0.134	0.9641	0.0645	0.3029	-4.9499	-46.797	-12.9442
4	7.1794	-2.193	-1.0473	9.0129	6.3786	8.6987	-0.0626	-1.1952	-0.8728	1.7605	0.9981	-2.0419	1.031	1.078	-0.9183	0.6074	0.1278	-0.2506	0.6844	0.035	0.5383	-5.9441	-60.3297	-2.9947
5	2.2955	-1.9331	1.0971	6.5204	1.9023	2.4436	0.1375	-0.169	-0.2035	-1.094	-0.0079	0.1611	-0.0512	0.2087	-0.1925	0.5458	-0.1514	0.0334	1.2314	0.009	0.3752	-5.8817	-58.2587	-8.6395
6	3.1503	1.6595	1.7337	7.2236	2.8021	2.4336	0.2868	-0.1795	-0.4564	0.629	0.1268	-0.2711	0.4324	-0.2327	-0.246	0.9611	-0.1187	-0.0545	0.6267	0.0723	0.3493	-8.9106	-69.3843	-8.2608
7	3.5096	-2.7736	1.1942	7.9329	-0.3034	3.8704	0.2364	0.4059	0.1478	-0.4412	-0.0381	0.3078	-0.4437	-0.1995	-0.2243	0.6172	-0.0811	0.1589	0.6735	0.164	0.3241	4.1767	-35.1893	-32.869
8	2.4886	-0.5296	-1.9557	3.9456	-5.1428	9.602	1.052	0.815	1.1879	-1.7914	-0.7669	-0.8775	0.0857	1.7612	-0.3428	1.0282	-0.0831	0.2969	1.1336	0.0781	0.8732	10.8652	-25.7834	-32.3533
9	0.8029	1.0218	-0.0131	2.1204	-0.885	1.065	0.2094	-0.8396	0.4269	-0.2254	-0.2159	-0.4227	-0.491	0.588	-0.0346	0.8231	-0.1972	0.2839	1.1453	-0.0951	0.5926	12.9958	-35.1901	-34.7875
10	5.6953	-3.7636	0.0819	3.0347	-1.3487	3.2179	0.3953	0.0899	0.6367	-0.2308	-0.3805	0.6538	-0.2235	0.4354	0.0187	0.4448	-0.2624	0.1934	0.735	0.072	0.8291	3.8422	-26.4315	-26.0911
11	4.0128	2.3522	0.1957	3.5166	0.5164	0.5768	-0.143	0.4181	-0.3586	-0.7378	0.1631	-0.3412	-0.1413	-0.5569	-0.0441	0.5249	-0.07	-0.0673	1.2142	-0.0089	0.3126	-3.118	-57.2803	-25.5267
12	3.8922	0.6793	-3.3472	2.2445	1.4151	4.7917	-0.1337	-0.7576	0.0684	0.1688	0.5867	0.1554	-0.3633	-0.0597	-0.483	0.6021	0.1047	-0.0483	1.0714	0.1423	0.3895	-4.3622	-55.1918	-23.117
13	0.0835	-0.8051	0.3067	9.3212	-0.8818	4.849	0.03	-0.1048	0.1879	-0.4726	0.6069	1.8756	1.2452	-1.0732	-0.393	0.6459	-0.026	-0.1081	1.3564	0.125	0.2899	-20.3185	-58.5861	-19.8393
14	7.0346	3.3192	-0.5405	2.6873	-0.2901	0.0516	-0.5828	0.9047	0.0884	-1.0282	0.2998	-0.3328	0.003	-0.9503	0.3435	0.6946	-0.1112	0.0377	1.3938	-0.0186	0.4425	-10.9175	-58.3335	-30.9346
15	4.1196	1.255	-2.2413	2.9567	2.4596	6.5162	1.252	-1.0677	1.5553	0.801	-0.9653	0.3384	-0.0111	-0.711	-0.3214	1.1394	-0.1951	0.7373	0.9396	-0.1059	1.4711	-8.8078	-6.2898	-15.1761
16	3.1008	0.4288	-0.9857	2.3468	-1.3488	0.9235	-0.129	1.4995	-0.5925	-0.4938	-0.1089	-0.6981	0.8222	-0.4836	0.3482	1.4504	-0.7248	1.3428	0.1114	-0.1819	2.103	10.8944	0.576	-24.9523
17	5.0369	1.0371	0.7355	2.8722	1.1472	4.2968	0.0678	-0.1004	0.164	0.6274	0.0153	0.1426	0.6846	0.0462	-0.2425	1.282	0.1202	0.5477	0.5063	-0.0106	1.051	32.7276	11.2641	-23.1237
18	5.7001	-0.1195	2.4628	4.976	0.6628	2.2641	-0.5464	-0.7398	-0.0468	1.212	0.4719	1.0284	-0.0579	-0.2581	-0.141	1.1515	-0.243	0.0254	1.237	0.1039	0.3274	52.1755	-26.3892	-5.1241
19	1.8599	1.2505	1.8004	5.6384	1.5655	4.561	-0.2718	-0.6634	0.1631	0.3841	0.2385	1.2845	0.8355	-0.9227	0.0706	0.8201	-0.198	0.1829	0.9902	0.1541	0.4886	48.7891	-32.9706	-11.3641
20	0.9717	0.173	0.4965	0.8002	1.2253	2.1636	0.2887	-0.1243	-0.2956	0.063	0.0105	0.0027	-0.6072	-0.2036	0.2149	1.2226	-0.0969	-0.1813	0.9676	0.0891	-0.1512	57.26	-25.7757	-19.1952
21	9.1103	3.9092	2.0371	6.3283	0.5231	6.7888	0.3698	-0.4275	-0.4326	0.1063	-0.1864	0.1005	0.6138	-1.233	-0.1558	1.0993	-0.1994	-0.1075	0.8582	0.1713	0.4113	57.3948	-35.4925	-12.1453
22	2.8323	1.7799	2.095	3.2697	1.3088	2.6552	0.0022	0.0409	0.0298	0.0884	-0.0839	-0.0664	-0.3398	-0.4128	-0.0187	1.2084	-0.2678	0.0239	0.8475	-0.0708	0.3279	55.1387	-23.7061	-10.9289
23	5.5603	-2.2302	2.8784	5.7554	-6.3198	8.2143	-0.1174	0.3831	1.2646	0.591	0.1571	-0.6037	-1.5407	-0.4539	0.3552	1.8256	0.2825	-0.3338	0.7794	-0.1074	0.5568	63.1003	6.3727	-13.873
24	2.1307	-1.2199	-0.1354	1.6742	0.777	0.5121	0.6318	-1.228	1.5213	1.2735	-0.8393	1.6444	-0.7339	-0.7011	0.333	2.2473	-0.0327	0.6471	0.9986	-0.4706	1.6131	58.7475	13.4738	-3.5553
25	7.4341	-0.2344	2.0622	7.087	-3.0941	4.6347	-0.4774	-1.2365	0.0777	0.4123	-0.4476	0.3297	0.5142	-0.0015	0.8469	0.8155	-0.1159	-0.0906	0.9534	0.0074	0.3635	60.141	-4.6678	-9.8072
26	8.2065	-2.9427	1.139	7.086	-2.7491	3.163	0.5896	0.9335	2.0653	-0.8142	-1.1105	0.0728	-0.5815	-0.5726	0.7819	1.9891	0.1796	-0.1317	0.8809	0.016	0.8713	57.1991	16.12	-14.7718
27	0.7631	0.3145	-0.829	1.3945	-2.5333	4.6383	-0.0548	-0.1284	0.1458	1.4907	0.4586	-0.4985	-0.5982	0.2569	-0.307	2.2971	-0.0756	-0.2527	0.9258	-0.1271	0.8576	65.9249	11.6151	-4.3004
28	3.7817	0.9939	0.7831	5.486	0.083	4.1967	-0.5065	0.2256	0.3096	-0.6044	0.3272	0.4149	0.1166	-0.2758	0.2394	0.8244	-0.1549	-0.1093	0.5376	-0.0247	0.2866	46.1957	-23.7604	-32.5222
29	2.0352	0.3837	0.9188	2.5827	1.2064	1.9992	-0.1682	0.2147	0.2426	-0.8188	0.0674	0.3538	0.013	-0.7368	0.1035	0.8155	-0.0088	-0.05	0.9328	0.1145	0.3608	44.0489	-21.1592	-30.4244
30	9.3112	1.394	0.1204	2.5389	-0.368	0.4335	-0.2211	0.7006	0.3448	0.3246	0.2061	-0.2338	-0.1611	0.5241	0.0585	0.8854	0.0476	-0.1107	0.7636	0.0527	0.4252	63.1933	0.6316	-24.2336
31	2.725	2.1442	-3.7536	6.545	-0.2923	7.0625	0.0657	-0.904	-1.0671	0.1077	0.3415	-1.5	0.6527	0.3628	-0.6186	0.6052	0.0372	-0.2172	0.9798	0.1685	1.3473	67.5468	-58.4488	-10.096
32	8.1077	1.8942	2.9235	3.8169	-4.1679	8.0097	0.542	-0.5089	1.0111	-0.1782	-0.5311	-0.7579	0.6388	1.3459	0.0636	1.3466	-0.3879	0.2704	1.325	-0.2914	1.1279	67.666	-53.2024	-15.2973
33	9.0008	-1.2859	1.361	4.8445	-6.0313	9.6209	0.1518	-0.076	-0.6046	-0.0424	0.3443	-0.2506	0.367	0.5018	-0.453	0.7803	-0.2409	-0.0066	0.5473	-0.1957	0.5486	57.1345	-51.3722	-19.1121
34	6.7581	4.5116	1.4927	7.3164	1.0297	3.9101	0.0904	0.6474	-0.6396	0.1485	-0.1844	0.039	-0.7839	0.7562	0.1277	0.5778	-0.0982	-0.138	0.4773	0.04	0.8135	34.0605	-57.9961	-29.3508
35	9.39	-0.4065	2.8801	8.5206	-3.692	5.466	-0.374	0.0862	-1.4242	0.7949	0.1072	0.0047	-0.0202	-0.687	0.3218	0.7427	0.0804	0.211	0.5856	-0.0179	0.8268	18.2563	-72.7409	-24.8607

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'L' and (resid 2 through 38 )
2	X-RAY DIFFRACTION	2	chain 'L' and (resid 39 through 75 )
3	X-RAY DIFFRACTION	3	chain 'L' and (resid 76 through 139 )
4	X-RAY DIFFRACTION	4	chain 'L' and (resid 140 through 150 )
5	X-RAY DIFFRACTION	5	chain 'L' and (resid 151 through 172 )
6	X-RAY DIFFRACTION	6	chain 'L' and (resid 173 through 212 )
7	X-RAY DIFFRACTION	7	chain 'H' and (resid 1 through 44 )
8	X-RAY DIFFRACTION	8	chain 'H' and (resid 45 through 60 )
9	X-RAY DIFFRACTION	9	chain 'H' and (resid 61 through 91 )
10	X-RAY DIFFRACTION	10	chain 'H' and (resid 92 through 111 )
11	X-RAY DIFFRACTION	11	chain 'H' and (resid 112 through 151 )
12	X-RAY DIFFRACTION	12	chain 'H' and (resid 152 through 185 )
13	X-RAY DIFFRACTION	13	chain 'H' and (resid 186 through 199 )
14	X-RAY DIFFRACTION	14	chain 'H' and (resid 200 through 220 )
15	X-RAY DIFFRACTION	15	chain 'E' and (resid 34 through 110 )
16	X-RAY DIFFRACTION	16	chain 'E' and (resid 111 through 168 )
17	X-RAY DIFFRACTION	17	chain 'E' and (resid 169 through 272 )
18	X-RAY DIFFRACTION	18	chain 'A' and (resid 1 through 18 )
19	X-RAY DIFFRACTION	19	chain 'A' and (resid 19 through 38 )
20	X-RAY DIFFRACTION	20	chain 'A' and (resid 39 through 49 )
21	X-RAY DIFFRACTION	21	chain 'A' and (resid 50 through 75 )
22	X-RAY DIFFRACTION	22	chain 'A' and (resid 76 through 113 )
23	X-RAY DIFFRACTION	23	chain 'A' and (resid 114 through 143 )
24	X-RAY DIFFRACTION	24	chain 'A' and (resid 144 through 155 )
25	X-RAY DIFFRACTION	25	chain 'A' and (resid 156 through 174 )
26	X-RAY DIFFRACTION	26	chain 'A' and (resid 175 through 188 )
27	X-RAY DIFFRACTION	27	chain 'A' and (resid 189 through 212 )
28	X-RAY DIFFRACTION	28	chain 'B' and (resid 1 through 60 )
29	X-RAY DIFFRACTION	29	chain 'B' and (resid 61 through 127 )
30	X-RAY DIFFRACTION	30	chain 'B' and (resid 128 through 220 )
31	X-RAY DIFFRACTION	31	chain 'C' and (resid 24 through 48 )
32	X-RAY DIFFRACTION	32	chain 'C' and (resid 49 through 66 )
33	X-RAY DIFFRACTION	33	chain 'C' and (resid 67 through 121 )
34	X-RAY DIFFRACTION	34	chain 'C' and (resid 122 through 203 )
35	X-RAY DIFFRACTION	35	chain 'C' and (resid 204 through 272 )

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