PDB-6nfj: Structure of Beta-Klotho in Complex with FGF19 C-terminal peptide

ID or keywords:

Entry

Database: PDB / ID: 6nfj

Title

Structure of Beta-Klotho in Complex with FGF19 C-terminal peptide

Components

Beta-klotho
Fibroblast growth factor 19
Nanobody 30

Keywords

SIGNALING PROTEIN / Klotho / FGF19 / Nanobody / receptor tyrosine kinase / signaling

Function / homology

Function and homology information

negative regulation of bile acid biosynthetic process / betaKlotho-mediated ligand binding / positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway / fibroblast growth factor receptor binding / FGFR4 ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / neural crest cell migration / bile acid and bile salt transport / PI-3K cascade:FGFR4 / fibroblast growth factor binding ...
Similarity search - Function

Biological species

Homo sapiens (human)

Lama glama (llama)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.19 Å

Authors

Kuzina, E. / Schlessinger, J. / Lee, S.

Citation

Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2019
Title: Structures of ligand-occupied beta-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity.
Authors: Kuzina, E.S. / Ung, P.M. / Mohanty, J. / Tome, F. / Choi, J. / Pardon, E. / Steyaert, J. / Lax, I. / Schlessinger, A. / Schlessinger, J. / Lee, S.

History

Deposition	Dec 20, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 3, 2019	Provider: repository / Type: Initial release
Revision 1.1	Apr 17, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2	Apr 24, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3	Oct 11, 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 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4	Oct 30, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	6nfj.cif.gz	751.6 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	6nfj_validation.pdf.gz	475.5 KB	Display	wwPDB validaton report
Full document	6nfj_full_validation.pdf.gz	490.1 KB	Display
Data in XML	6nfj_validation.xml.gz	63.3 KB	Display
Data in CIF	6nfj_validation.cif.gz	85.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/nf/6nfj ftp://data.pdbj.org/pub/pdb/validation_reports/nf/6nfj	HTTPS FTP

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Related structure data

Related structure data	5vaqS S: Starting model for refinement
Similar structure data	4a7z-d 6sxh-d 6t4h-d 6xwx-3 2ibm-1 3zpg-1 4a7k-d 5fsg-d 2bty-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) 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
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Deposited unit

A: Beta-klotho

B: Nanobody 30

C: Fibroblast growth factor 19

D: Beta-klotho

E: Nanobody 30

F: Fibroblast growth factor 19

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

1

A: Beta-klotho

B: Nanobody 30

C: Fibroblast growth factor 19

defined by author
Evidence: gel filtration
131 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: Beta-klotho

E: Nanobody 30

F: Fibroblast growth factor 19

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

Unit cell

Length a, b, c (Å)	130.090, 143.900, 141.050
Angle α, β, γ (deg.)	90.00, 90.90, 90.00
Int Tables number	5
Space group name H-M	C121

#1: Protein	Beta-klotho / BetaKlotho / Klotho beta-like protein Mass: 110389.242 Da / Num. of mol.: 2 / Mutation: N308Q, N611Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KLB / Cell line (production host): 293-EBNA / Production host: Homo sapiens (human) / References: UniProt: Q86Z14
#2: Antibody	Nanobody 30 Mass: 14700.269 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): WK6
#3: Protein/peptide	Fibroblast growth factor 19 / FGF-19 Mass: 5553.230 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: O95750
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: 2.53 Å³/Da / Density % sol: 51.31 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 21% PEG1500, 0.1M Ammonium sulphate, 0.2M NDSB-201, 0.1M Tris-HCl pH 7.5

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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: 0.9792 Å
Detector	Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 14, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9792 Å / Relative weight: 1
Reflection	Resolution: 3.19→59.42 Å / Num. obs: 42869 / % possible obs: 99.23 % / Redundancy: 3.8 % / Net I/σ(I): 3.4
Reflection shell	Resolution: 3.2→3.31 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 0.81 / CC_1/2: 0.519 / % possible all: 95.87

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Processing

Software

Name	Version	Classification
PHENIX	(1.13_2998: ???)	refinement
PHASER		phasing
XDS		data scaling
XDS		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5VAQ

5vaq

Resolution: 3.19→59.42 Å / SU ML: 0.6 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 38.64

	R_factor	Num. reflection	% reflection
R_free	0.3196	3849	4.64 %
R_work	0.2796	-	-
obs	0.2815	42869	97.78 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Refinement step

Cycle: LAST / Resolution: 3.19→59.42 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	14271	0	0	0	14271

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	14697
X-RAY DIFFRACTION	f_angle_d	0.446	20110
X-RAY DIFFRACTION	f_dihedral_angle_d	10.539	8294
X-RAY DIFFRACTION	f_chiral_restr	0.04	2187
X-RAY DIFFRACTION	f_plane_restr	0.003	2586

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 (%)
3.1935-3.2339	0.4363	124	0.3928	2456	X-RAY DIFFRACTION	81
3.2339-3.2764	0.3843	126	0.3917	2889	X-RAY DIFFRACTION	97
3.2764-3.3213	0.3897	143	0.3711	2912	X-RAY DIFFRACTION	98
3.3213-3.3687	0.4444	146	0.3757	3013	X-RAY DIFFRACTION	99
3.3687-3.419	0.4101	152	0.3644	2958	X-RAY DIFFRACTION	99
3.419-3.4724	0.3632	148	0.3529	2975	X-RAY DIFFRACTION	99
3.4724-3.5294	0.3669	145	0.3507	2963	X-RAY DIFFRACTION	99
3.5294-3.5902	0.3854	149	0.3431	3032	X-RAY DIFFRACTION	99
3.5902-3.6555	0.3667	144	0.3382	2854	X-RAY DIFFRACTION	99
3.6555-3.7258	0.3455	141	0.3117	3104	X-RAY DIFFRACTION	99
3.7258-3.8018	0.3207	140	0.3056	2894	X-RAY DIFFRACTION	99
3.8018-3.8845	0.3617	147	0.2852	2975	X-RAY DIFFRACTION	98
3.8845-3.9748	0.367	135	0.2791	2919	X-RAY DIFFRACTION	98
3.9748-4.0742	0.3232	148	0.2679	2958	X-RAY DIFFRACTION	99
4.0742-4.1843	0.3209	135	0.257	2953	X-RAY DIFFRACTION	99
4.1843-4.3074	0.2716	144	0.2544	2938	X-RAY DIFFRACTION	98
4.3074-4.4464	0.3132	145	0.242	2925	X-RAY DIFFRACTION	98
4.4464-4.6053	0.289	146	0.2311	2959	X-RAY DIFFRACTION	98
4.6053-4.7896	0.2793	144	0.2349	2860	X-RAY DIFFRACTION	96
4.7896-5.0075	0.2674	144	0.2377	2932	X-RAY DIFFRACTION	98
5.0075-5.2713	0.25	140	0.2446	2957	X-RAY DIFFRACTION	99
5.2713-5.6014	0.3445	142	0.2562	2997	X-RAY DIFFRACTION	99
5.6014-6.0335	0.3135	141	0.2605	2981	X-RAY DIFFRACTION	99
6.0335-6.6399	0.3023	147	0.2727	2970	X-RAY DIFFRACTION	99
6.6399-7.599	0.2659	147	0.2665	2964	X-RAY DIFFRACTION	99
7.599-9.5675	0.2685	138	0.2383	2945	X-RAY DIFFRACTION	97
9.5675-59.4244	0.3202	148	0.2707	2907	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	2.0447	0.4454	-0.1664	2.4228	-0.2164	1.3102	-0.0432	-0.0294	-0.0668	-0.4894	-0.0951	-0.0025	0.2455	-0.0101	0.1183	0.4603	0.0768	0.0659	0.3404	0.0352	1.4786	-37.541	60.807	24.0188
2	1.2181	-0.5353	0.3265	0.8008	-0.2581	0.3353	0.0886	-0.042	0.2612	-0.5532	0.0403	-0.0577	-0.1779	-0.0583	-0.0894	0.2939	0.0673	0.2896	0.3505	-0.0999	1.1362	-7.2693	37.2667	40.8877
3	2.5213	-1.9195	0.4783	1.863	-0.6926	0.4156	-0.1364	-0.0046	-0.081	0.0888	-0.0553	-0.4335	-0.0105	0.1634	0.0819	0.4508	0.2345	0.1254	0.13	0.0075	0.6925	3.6242	20.0295	37.7959
4	0.9703	-0.7298	0.2779	1.6693	0.1613	0.6891	0.1938	0.298	0.0563	-0.5887	-0.2384	-0.4625	-0.0927	0.1575	0.0015	0.0497	0.2861	-0.0003	0.1033	0.1094	0.7202	-3.1882	25.6818	43.0687
5	3.9639	0.7811	4.6797	3.7469	0.4511	7.2783	0.7304	0.6097	-0.3332	-0.7438	0.4718	-0.2025	0.3445	-0.5667	-1.0479	1.1001	0.186	-0.1438	0.6515	-0.002	0.5949	-24.5044	3.2874	17.8606
6	2.3865	1.4942	1.9885	1.3178	1.5429	4.784	-0.275	0.0725	0.131	-0.5998	-0.6183	0.739	-0.1462	-0.3365	0.4988	1.1251	-0.2318	0.0715	0.5557	-0.2174	0.6019	-13.77	7.6644	27.4025
7	0.6856	-0.3763	-0.6175	1.3138	-0.6181	3.8966	-0.1608	-0.0559	-0.2166	0.1248	-0.0241	0.2529	0.1086	-0.311	0.0959	0.3949	0.0652	0.2525	0.8573	-0.2131	0.7351	-12.1574	16.1956	25.0901
8	3.1398	0.9709	1.8465	8.0474	5.9353	5.4636	-0.2561	0.0333	0.3904	-1.4333	-0.1429	-0.0912	-0.122	0.2799	0.1487	1.2582	0.3541	0.077	0.5065	-0.0478	0.5087	-17.1946	10.387	11.0351
9	3.0201	-4.0286	-4.0634	7.0686	4.7039	6.0851	-0.046	0.3214	-0.2669	-0.512	-0.6181	1.0018	-0.5321	-0.8566	0.493	1.0235	0.3239	-0.0508	0.6447	0.0697	1.7358	-21.2354	20.0697	18.6857
10	3.88	-2.0284	-3.2104	4.6843	1.4201	2.6788	0.2145	0.3775	0.5014	0.0286	-0.7048	0.9137	0.221	0.1662	0.4732	1.2401	0.348	-0.074	1.2466	-0.137	0.9918	-28.3642	15.0649	12.3786
11	2.5973	-1.3109	-2.7428	5.6124	2.8775	4.0411	-0.4443	-0.3661	-0.5932	2.1175	0.2767	0.7182	0.6423	-0.2169	0.4528	1.3034	0.4225	0.3074	0.7858	-0.1187	0.8791	-21.6557	14.2078	28.0289
12	9.6643	-1.3989	3.4218	7.3067	-3.2347	6.4149	0.2591	0.451	-1.394	-1.3248	-0.2963	0.8542	1.1857	0.034	-0.0122	1.5593	0.1414	0.0703	0.5152	-0.016	1.4365	-24.8949	9.8799	21.0833
13	3.2566	-2.5099	-2.5324	2.3385	3.0153	4.7657	0.3589	2.0092	-1.3024	-1.3711	-1.1355	0.7168	0.7876	-1.423	0.7079	1.0571	0.0778	0.021	1.1176	-0.4951	0.7121	-30.5645	5.9927	6.3288
14	5.4923	-2.6468	1.4202	3.2893	-2.7675	2.522	0.4674	0.4087	-1.4587	-1.1735	-0.5289	1.1592	1.7013	0.6738	0.2724	1.271	0.2879	0.2477	0.6333	-0.0771	1.0931	-18.9133	5.6617	12.9828
15	1.7354	-0.0559	1.1372	4.1836	-2.2294	1.895	0.4436	0.893	0.0125	-0.9644	-1.3655	-1.1592	0.5445	1.2358	0.77	1.1861	0.3476	0.0739	0.7884	0.3258	0.5688	-9.8459	17.9785	14.7164
16	4.2649	1.7672	4.2433	1.0557	2.0236	4.5895	0.4375	0.1357	-1.6	0.2627	0.6137	-0.3681	0.0187	0.5494	-0.9655	0.7787	0.3777	-0.0327	0.9052	-0.0512	0.8181	-13.9011	7.5984	14.5365
17	7.6395	-2.8147	2.0626	6.1441	0.2864	4.3916	-0.1198	0.4857	1.2046	0.2509	0.0404	-0.9488	0.382	1.5142	0.143	0.4683	0.2461	0.0997	0.7527	0.0863	1.3679	-12.6875	49.0925	29.3633
18	0.1966	-0.2715	0.6404	2.7058	-2.9032	3.8334	-0.0784	1.5716	0.1414	-0.6833	-0.4219	1.0922	0.0263	-0.0503	0.4501	0.6496	0.4194	-0.1539	1.1037	0.1054	1.0028	-0.071	36.5641	38.3769
19	2.2062	0.2043	-0.2061	2.329	0.0919	1.1889	-0.0567	-0.0748	0.3023	0.5125	0.0961	0.21	-0.1026	-0.0463	0.0203	0.1713	0.0392	-0.0442	0.3125	-0.0321	0.0436	-4.4792	96.4831	23.4382
20	2.0157	-1.1907	0.1053	0.9825	-0.0089	1.0889	-0.2768	-0.4752	-0.4194	0.5819	0.4933	-0.5197	0.0546	0.424	-0.0729	0.5753	0.0547	-0.263	0.5062	0.0446	0.6391	12.8357	80.4126	36.9921
21	3.8462	-0.8217	0.7234	2.5106	-0.7247	2.5032	-0.4901	-0.8901	0.0388	0.3918	0.3049	-0.3265	-0.0359	0.3146	0.1612	0.9755	0.3025	-0.0676	0.8802	-0.0866	1.2751	35.3358	60.0233	43.3014
22	0.2076	-0.8222	0.043	4.4457	-0.1622	1.1789	-0.2452	-0.0085	-0.0242	-0.1425	0.0696	0.0966	0.1195	-0.0263	0.0566	1.2284	0.0322	0.1881	0.469	0.0408	1.9093	20.0594	41.2936	23.9984
23	1.9935	0.2422	-0.0793	1.0216	-0.0633	1.2273	0.1289	0.362	0.1731	-0.2918	0.2444	0.139	-0.035	-0.7808	-0.1981	1.0072	-0.3522	0.2991	0.9684	0.116	0.4914	0.8056	38.0027	14.1808
24	4.7731	-0.7034	2.2643	2.3363	-1.3932	4.0426	-0.8612	-0.5573	1.2677	0.9523	0.0663	-0.3018	1.2662	0.0207	0.6629	1.2498	0.2955	0.2288	0.6674	-0.0822	1.0786	19.7254	48.5982	26.1487
25	7.5123	-1.2241	1.1167	2.2036	-0.2325	0.1671	-0.6526	0.6439	0.7457	-1.045	0.3836	-0.4997	1.1112	-0.4052	0.2537	1.3168	-0.2697	0.1932	0.5309	-0.2468	0.9558	14.9017	46.7915	11.3473
26	0.0484	0.107	-0.0087	0.238	-0.0193	0.0015	-0.2079	0.2029	0.6944	-0.196	0.0977	0.3923	-0.2014	-0.0433	0.3507	0.6774	-0.1516	-0.454	0.7525	0.4831	2.08	11.2475	56.0248	18.9431
27	5.5792	0.4775	-1.9298	3.8483	0.8785	0.9534	-0.3166	1.2377	0.2866	-0.0671	-0.1944	1.1848	0.2281	-0.7269	0.6261	0.8025	-0.3133	-0.3169	0.7318	-0.1576	0.8843	4.3427	51.0388	11.9938
28	3.6798	1.5557	0.0154	0.8924	0.1893	0.143	-0.1898	-0.4817	0.2385	0.8316	-0.0748	-0.1467	-0.983	0.615	0.1224	1.2694	0.1228	-0.0851	0.6388	0.0101	0.3246	10.931	48.6312	27.2501
29	6.375	2.1254	4.7744	2.9963	0.7846	6.9935	0.1398	1.6653	0.2551	-1.1673	0.0993	0.2556	-0.1122	0.4189	-0.2822	1.3372	0.027	-0.0347	1.1469	0.3874	0.503	1.8685	44.7451	13.0726
30	6.0209	1.4393	-0.9852	6.74	-1.7063	0.4994	0.6007	0.1286	-0.1535	-0.7042	-0.2559	0.6149	0.6932	-1.9334	-0.3825	0.6293	-0.2745	-0.0614	1.468	-0.3174	0.6925	9.6502	40.8233	9.2378
31	1.7152	-0.4615	-0.3423	0.4981	-0.2924	0.4636	-0.0615	-0.2672	0.4835	0.1929	0.0431	-0.0533	-0.5878	-0.3072	-0.1281	1.0865	0.3352	0.2424	0.8595	-0.3706	0.9694	21.8124	54.8173	17.4185
32	2.7737	-0.758	-1.5229	2.3028	-2.0118	4.0359	0.0207	0.1869	0.2541	0.0301	-0.4061	-0.3215	-0.0788	0.5949	0.2748	1.3176	-0.3843	0.5218	1.0873	0.2962	1.2352	23.5003	52.1171	10.5237
33	5.9139	-1.3342	7.3632	0.3076	-1.6813	9.2337	0.9552	-0.2058	-0.4048	-0.4886	0.1008	-0.504	1.437	-0.4079	-0.8849	0.8398	-0.0634	0.0697	0.8324	-0.3772	0.6714	17.4512	41.8554	14.9429
34	3.2643	-0.6349	3.2927	4.2427	1.4273	7.663	-0.6881	-0.0673	2.633	0.2727	-0.0938	-0.7815	0.0856	1.5106	0.9253	0.6703	0.1468	0.1338	0.9287	-0.028	1.625	19.9689	85.0487	29.7196
35	0.1191	0.149	-0.4356	1.2241	-0.0152	1.8622	0.0885	0.1429	-0.3576	-0.0684	-0.6569	0.1386	0.0195	0.7713	0.2102	1.5417	-0.0015	0.5695	1.6654	-0.1506	0.7733	32.4862	72.6535	38.4906

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	(chain A and resid 53:371)
2	X-RAY DIFFRACTION	2	(chain A and resid 372:691)
3	X-RAY DIFFRACTION	3	(chain A and resid 692:767)
4	X-RAY DIFFRACTION	4	(chain A and resid 768:968)
5	X-RAY DIFFRACTION	5	(chain B and resid 1:20)
6	X-RAY DIFFRACTION	6	(chain B and resid 21:27)
7	X-RAY DIFFRACTION	7	(chain B and resid 28:34)
8	X-RAY DIFFRACTION	8	(chain B and resid 35:47)
9	X-RAY DIFFRACTION	9	(chain B and resid 48:59)
10	X-RAY DIFFRACTION	10	(chain B and resid 60:69)
11	X-RAY DIFFRACTION	11	(chain B and resid 70:75)
12	X-RAY DIFFRACTION	12	(chain B and resid 76:82)
13	X-RAY DIFFRACTION	13	(chain B and resid 83:90)
14	X-RAY DIFFRACTION	14	(chain B and resid 91:96)
15	X-RAY DIFFRACTION	15	(chain B and resid 97:108)
16	X-RAY DIFFRACTION	16	(chain B and resid 109:121)
17	X-RAY DIFFRACTION	17	(chain C and resid 191:202)
18	X-RAY DIFFRACTION	18	(chain C and resid 203:213)
19	X-RAY DIFFRACTION	19	(chain D and resid 53:360)
20	X-RAY DIFFRACTION	20	(chain D and resid 361:608)
21	X-RAY DIFFRACTION	21	(chain D and resid 609:968)
22	X-RAY DIFFRACTION	22	(chain E and resid 1:7)
23	X-RAY DIFFRACTION	23	(chain E and resid 8:20)
24	X-RAY DIFFRACTION	24	(chain E and resid 21:34)
25	X-RAY DIFFRACTION	25	(chain E and resid 35:47)
26	X-RAY DIFFRACTION	26	(chain E and resid 48:59)
27	X-RAY DIFFRACTION	27	(chain E and resid 60:69)
28	X-RAY DIFFRACTION	28	(chain E and resid 70:79)
29	X-RAY DIFFRACTION	29	(chain E and resid 80:86)
30	X-RAY DIFFRACTION	30	(chain E and resid 87:95)
31	X-RAY DIFFRACTION	31	(chain E and resid 96:104)
32	X-RAY DIFFRACTION	32	(chain E and resid 105:109)
33	X-RAY DIFFRACTION	33	(chain E and resid 110:121)
34	X-RAY DIFFRACTION	34	(chain F and resid 191:202)
35	X-RAY DIFFRACTION	35	(chain F and resid 203:213)

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