PDB-5qcu: Crystal structure of BACE complex with BMC022

ID or keywords:

Entry

Database: PDB / ID: 5qcu

Title

Crystal structure of BACE complex with BMC022

Components

Beta-secretase 1

Keywords

HYDROLASE / Hydroloase / D3R / BACE / Ligand Docking

Function / homology

Function and homology information

memapsin 2 / Golgi-associated vesicle lumen / signaling receptor ligand precursor processing / beta-aspartyl-peptidase activity / amyloid precursor protein catabolic process / amyloid-beta formation / membrane protein ectodomain proteolysis / cellular response to manganese ion / amyloid-beta metabolic process / prepulse inhibition ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.951 Å

Model details

Structures for D3R docking challenge

Authors

Rondeau, J.M. / Shao, C. / Yang, H. / Burley, S.K.

Citation

Journal: J.Comput.Aided Mol.Des. / Year: 2020
Title: D3R grand challenge 4: blind prediction of protein-ligand poses, affinity rankings, and relative binding free energies.
Authors: Parks, C.D. / Gaieb, Z. / Chiu, M. / Yang, H. / Shao, C. / Walters, W.P. / Jansen, J.M. / McGaughey, G. / Lewis, R.A. / Bembenek, S.D. / Ameriks, M.K. / Mirzadegan, T. / Burley, S.K. / Amaro, R.E. / Gilson, M.K.

History

Deposition	Dec 1, 2017	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 3, 2020	Provider: repository / Type: Initial release
Revision 1.1	Dec 30, 2020	Group: Structure summary / Category: audit_author / Item: _audit_author.identifier_ORCID
Revision 1.2	Feb 10, 2021	Group: Database references / Category: citation_author / Item: _citation_author.identifier_ORCID

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	5qcu.cif.gz	463.3 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	5qcu_validation.pdf.gz	1.1 MB	Display	wwPDB validaton report
Full document	5qcu_full_validation.pdf.gz	1.1 MB	Display
Data in XML	5qcu_validation.xml.gz	46 KB	Display
Data in CIF	5qcu_validation.cif.gz	67.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qc/5qcu ftp://data.pdbj.org/pub/pdb/validation_reports/qc/5qcu	HTTPS FTP

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Group deposition

ID	G_1002044 (26 entries) 5qco 5qcp 5qcq 5qcr 5qcs 5qct 5qcu 5qcv 5qcw 5qcx
Title	Crystal Structures of Beta-Secretase 1 with Bound Ligands
Type	undefined
Description	Crystal Structures of Complexes of Beta-Secretase 1 and Ligands

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Related structure data

Similar structure data	2wf0-d 4d88-d 2f3f-2 5qco-1 5qd2-3 5i3w-d 5qd2-1 5qd7-1 4b70-d 5ygx-d 5qd5-1 3dv5-2 4d83-2 4d8c-2 3k5d-3 5qd3-1 5qd6-1 3qbh-3 3qbh-1 3k5f-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) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#115 - Jul 2009 beta-Secretase similarity (5) #79 - Jul 2006 Amyloid-beta Precursor Protein similarity (5)

Deposited unit

A: Beta-secretase 1

B: Beta-secretase 1

C: Beta-secretase 1

hetero molecules

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

1

A: Beta-secretase 1

hetero molecules

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

2

B: Beta-secretase 1

hetero molecules

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

3

C: Beta-secretase 1

hetero molecules

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

Unit cell

Length a, b, c (Å)	81.173, 102.482, 100.443
Angle α, β, γ (deg.)	90.000, 103.670, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	chain A
2	1	(chain B and (resid -2 through 157 or resid 170 through 385))
3	1	(chain C and (resid -2 through 157 or resid 170 through 385))

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details	Auth asym-ID	Auth seq-ID
1	1	1	chain A	A	-2 - 385
2	1	1	(chain B and (resid -2 through 157 or resid 170 through 385))	B	-2 - 157
2	2	1	(chain B and (resid -2 through 157 or resid 170 through 385))	B	170 - 385
3	1	1	(chain C and (resid -2 through 157 or resid 170 through 385))	C	-2 - 157
3	2	1	(chain C and (resid -2 through 157 or resid 170 through 385))	C	170 - 385

#1: Protein	Beta-secretase 1 / Aspartyl protease 2 / Asp 2 / Beta-site amyloid precursor protein cleaving enzyme 1 / Beta-site APP ...Aspartyl protease 2 / Asp 2 / Beta-site amyloid precursor protein cleaving enzyme 1 / Beta-site APP cleaving enzyme 1 / Memapsin-2 / Membrane-associated aspartic protease 2 Mass: 44777.336 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BACE1, BACE, KIAA1149 / Production host: Escherichia coli (E. coli) / References: UniProt: P56817, memapsin 2
#2: Chemical	ChemComp-E51 / (2R,4S)-N-butyl-4-[(5S,8S,10R)-5,10-dimethyl-3,3,6-trioxo-3lambda~6~-thia-7-azabicyclo[11.3.1]heptadeca-1(17),13,15-trien-8-yl]-4-hydroxy-2-methylbutanamide Mass: 494.687 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₂₆H₄₂N₂O₅S
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 600 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.02 Å³/Da / Density % sol: 59.3 %
Crystal grow	Temperature: 292 K / Method: hanging drop Details: CRYSTALS WERE GROWN AT 19C BY VAPOUR DIFFUSION IN HANGING DROPS USING 1.0M UNBUFFERED AMMONIUM SULFATE AS PRECIPITANT. PROTEIN STOCK WAS BACE MUT46B BATCH X 8.3MG/ML IN 10MM TRIS-HCL PH 7.4, ...Details: CRYSTALS WERE GROWN AT 19C BY VAPOUR DIFFUSION IN HANGING DROPS USING 1.0M UNBUFFERED AMMONIUM SULFATE AS PRECIPITANT. PROTEIN STOCK WAS BACE MUT46B BATCH X 8.3MG/ML IN 10MM TRIS-HCL PH 7.4, 25MM NACL, WITH A 4-FOLD EXCESS OF BMC022 ADDED FROM A 50MM STOCK SOLUTION IN DMSO (1.4% DMSO IN DROP). CRYO-PROTECTANT WAS 2.0M LI2SO4, 0.2M SUCROSE, 0.1M CITRATE PH 5.5.

Crystal

Density Matthews: 3.02 Å³/Da / Density % sol: 59.3 %

Crystal grow

Temperature: 292 K / Method: hanging drop
Details: CRYSTALS WERE GROWN AT 19C BY VAPOUR DIFFUSION IN HANGING DROPS USING 1.0M UNBUFFERED AMMONIUM SULFATE AS PRECIPITANT. PROTEIN STOCK WAS BACE MUT46B BATCH X 8.3MG/ML IN 10MM TRIS-HCL PH 7.4, ...

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Data collection

Diffraction	Mean temperature: 95 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00003
Detector	Type: MAR CCD 165 mm / Detector: CCD / Date: Nov 11, 2003
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.00003 Å / Relative weight: 1
Reflection	Resolution: 1.951→55.289 Å / Num. obs: 115047 / % possible obs: 99.09 % / R_merge(I) obs: 0.059

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
PHENIX	1.12_2829	refinement
CNX		refinement
CNX		phasing
SCALEPACK		data scaling
DENZO		date reduction
PDB_EXTRACT	3.24	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.951→55.289 Å / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 18.32 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1931	11513	10.01 %
R_work	0.167	103534	-
obs	0.1696	115047	99.09 %

Solvent computation

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

Displacement parameters

B_iso max: 163.55 Å² / B_iso mean: 43.1026 Å² / B_iso min: 20.25 Å²

Refinement step

Cycle: final / Resolution: 1.951→55.289 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8895	0	102	600	9597
B_iso mean	-	-	33.53	42.57	-
Num. residues	-	-	-	-	1130

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	9234
X-RAY DIFFRACTION	f_angle_d	0.935	12559
X-RAY DIFFRACTION	f_chiral_restr	0.062	1367
X-RAY DIFFRACTION	f_plane_restr	0.006	1610
X-RAY DIFFRACTION	f_dihedral_angle_d	14.556	5390

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	5397	X-RAY DIFFRACTION	11.587	TORSIONAL
1	2	B	5397	X-RAY DIFFRACTION	11.587	TORSIONAL
1	3	C	5397	X-RAY DIFFRACTION	11.587	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 (%)
1.9511-1.9732	0.2365	347	0.2009	3243	3590	94
1.9732-1.9965	0.2301	398	0.1952	3359	3757	98
1.9965-2.0208	0.2134	384	0.1828	3472	3856	98
2.0208-2.0464	0.2184	392	0.1785	3369	3761	98
2.0464-2.0733	0.224	376	0.1782	3395	3771	98
2.0733-2.1017	0.2061	373	0.1728	3394	3767	98
2.1017-2.1318	0.2039	398	0.1727	3434	3832	98
2.1318-2.1636	0.2114	367	0.1686	3368	3735	99
2.1636-2.1974	0.1918	370	0.1645	3458	3828	99
2.1974-2.2334	0.1996	409	0.1718	3413	3822	99
2.2334-2.2719	0.2114	367	0.1628	3466	3833	99
2.2719-2.3132	0.1924	393	0.1692	3443	3836	99
2.3132-2.3577	0.2117	385	0.1716	3413	3798	99
2.3577-2.4059	0.211	393	0.1796	3413	3806	99
2.4059-2.4582	0.1987	406	0.1765	3496	3902	100
2.4582-2.5153	0.2209	375	0.1718	3467	3842	100
2.5153-2.5782	0.206	377	0.174	3454	3831	100
2.5782-2.648	0.2019	386	0.1787	3485	3871	100
2.648-2.7259	0.2351	425	0.1933	3452	3877	100
2.7259-2.8139	0.2206	406	0.1966	3460	3866	100
2.8139-2.9144	0.2307	347	0.1969	3514	3861	100
2.9144-3.0311	0.2402	375	0.1957	3494	3869	100
3.0311-3.169	0.217	384	0.1936	3475	3859	100
3.169-3.3361	0.2149	371	0.1941	3541	3912	100
3.3361-3.5451	0.1819	378	0.1653	3510	3888	100
3.5451-3.8187	0.176	387	0.1459	3463	3850	100
3.8187-4.2029	0.1475	398	0.1317	3512	3910	100
4.2029-4.8108	0.1364	385	0.1215	3501	3886	100
4.8108-6.0599	0.1817	408	0.1529	3487	3895	100
6.0599-55.3114	0.2013	353	0.1857	3583	3936	99

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	0.1047	-0.1229	0.0218	0.3212	-0.1938	0.174	-0.2374	-0.168	0.2385	0.1865	0.025	-0.142	-0.2958	0.1068	-0.0044	0.3633	-0.0419	-0.0747	0.2819	-0.0078	0.3313	43.5983	10.3869	25.1485
2	0.8745	-0.1532	0.124	0.8473	-0.5239	0.8014	-0.134	0.1871	0.2632	-0.0852	0.0299	-0.0618	-0.1432	0.0842	-0.0001	0.3562	-0.0705	-0.0414	0.3005	0.0559	0.2874	42.3146	12.8514	12.0263
3	0.2634	-0.0472	0.224	0.3533	-0.1818	0.2319	-0.0135	0.0288	0.0423	0.2421	-0.0335	-0.1679	-0.0311	0.0238	0.0001	0.3033	-0.0253	-0.0201	0.2701	-0.0108	0.2127	44.0835	-4.8581	26.8247
4	0.4159	-0.178	-0.161	0.8001	-0.1847	0.908	-0.1037	0.271	0.0909	-0.0972	0.2211	0.293	-0.0886	-0.2383	0.013	0.2567	0.0108	-0.0052	0.3007	0.0488	0.3095	20.5332	-6.8131	20.1896
5	0.3114	0.1547	0.1304	0.3574	-0.3023	0.4602	-0.0635	-0.0056	-0.0555	0.1597	0.1025	0.1704	-0.0137	-0.0286	-0.0001	0.2875	-0	0.0478	0.2457	-0.0016	0.2479	24.7327	-9.1764	29.7383
6	0.378	0.1611	-0.1833	0.0765	-0.0454	0.3696	-0.0995	0.1564	0.326	0.1061	0.1404	0.1683	-0.223	-0.0381	-0.0016	0.3763	0.064	0.0249	0.2909	0.0195	0.4111	21.8662	3.5236	27.5896
7	0.3396	-0.1557	0.1807	0.8381	-0.5434	0.38	-0.0071	0.0312	0.0167	0.0144	0.0578	0.1297	-0.0544	-0.0936	-0.0001	0.3069	-0.0055	0.0332	0.2765	-0.0183	0.2271	33.9037	-12.8525	24.7811
8	0.2471	0.162	-0.0771	0.9607	-0.0129	0.048	0.3391	-0.5734	-0.2829	0.3058	-0.2787	-0.1552	0.0836	-0.3246	0.0215	0.3306	-0.0645	-0.0324	0.4448	0.0784	0.285	18.9475	11.0746	-1.4569
9	0.1618	-0.083	0.0158	0.2068	0.1133	0.12	0.1006	-0.1832	-0.205	-0.0011	-0.1108	0.1519	0.1005	-0.4412	-0	0.2734	-0.0841	-0.0085	0.5097	0.0858	0.3448	8.0508	7.5208	-7.105
10	0.5863	0.1954	0.0574	0.3605	-0.151	0.3248	0.1229	-0.3401	-0.3319	0.1258	-0.1331	0.1699	0.192	-0.6002	0.0013	0.234	-0.0064	-0.0069	0.5524	-0.0266	0.3251	5.5641	12.1818	-9.6507
11	0.8886	0.3919	-0.369	0.2573	0.1114	0.7632	0.1101	-0.2307	-0.0031	0.1046	-0.1401	0.0247	-0.158	-0.2319	0.0001	0.2701	0.0381	-0.0343	0.3268	0.0302	0.2629	19.1916	19.4468	-10.4547
12	0.82	0.4989	-0.1103	0.4121	-0.1483	0.6467	-0.1114	0.1825	-0.4452	-0.0448	0.0978	-0.0415	-0.0124	0.0252	-0.001	0.2462	0.0209	-0.0168	0.3166	-0.0482	0.3033	30.767	13.9659	-25.7094
13	0.8576	-0.0692	-0.31	0.6417	-0.1149	0.1578	-0.1185	0.3811	-0.7505	-0.2592	-0.0043	-0.0108	0.3998	0.0422	-0.0742	0.4653	0.016	0.1027	0.2753	-0.1939	0.8187	32.7589	-6.9563	-26.2955
14	0.541	-0.2644	0.0333	0.7044	-0.266	1.3505	-0.0689	0.2388	-0.698	-0.088	-0.1092	-0.2974	0.1944	0.4115	-0.3669	0.2091	0.1643	0.0235	0.0899	-0.0344	0.7026	35.2226	0.7854	-18.3973
15	0.3314	0.0284	-0.2236	0.0345	0.0175	0.2328	0.0903	0.0595	-0.2698	0.0157	-0.0699	-0.1418	-0.0851	-0.1553	0	0.2597	0.0031	-0.0513	0.2352	0.0093	0.3385	27.9543	14.1511	-17.0981
16	0.6711	0.1838	-0.193	0.3257	0.0847	0.1784	0.015	0.0857	-0.4094	-0.027	0.027	-0.0903	0.0022	0.0991	-0.0027	0.2586	0.028	-0.0449	0.2988	0.0452	0.3897	37.6851	14.1402	-20.7631
17	0.1467	-0.1431	-0.0734	0.1253	0.0636	0.3768	0.0092	0.1215	-0.0276	0.0056	-0.0746	0.3059	0.1386	-0.3968	-0.0001	0.2822	-0.035	0.0084	0.3726	0.014	0.3887	-1.5138	-48.4978	37.3691
18	0.0951	-0.0636	0.0794	0.1792	0.0736	0.1536	0.0036	-0.2982	-0.0356	0.1778	-0.1266	0.057	0.1624	-0.0076	-0	0.315	-0.0628	0.0684	0.3049	0.024	0.3043	-1.698	-51.8153	50.1863
19	0.5584	0.0705	-0.5532	0.2729	-0.104	0.813	-0.0265	-0.1865	-0.094	0.1729	-0.0903	0.1439	0.3406	-0.2991	-0.0041	0.3632	-0.0369	0.0261	0.2527	0.0515	0.297	2.568	-55.5987	48.8602
20	0.1782	0.1301	0.0514	0.1606	-0.0917	0.1796	-0.0566	-0.1416	-0.2761	0.0849	-0.0164	-0.1252	0.5144	0.1275	0.0001	0.345	0.0334	0.0064	0.236	0.0491	0.3365	13.082	-56.3121	39.9234
21	0.1343	0.1148	-0.0185	0.0886	-0.0299	0.0291	0.0206	0.0888	-0.0266	-0.127	-0.0117	0.1578	0.0393	-0.2789	-0.0003	0.2922	0.029	-0.0522	0.3066	0.0007	0.3084	4.4792	-42.3965	29.4855
22	0.496	0.0193	-0.2736	0.7561	-0.2378	0.3184	0.1251	-0.0832	0.0085	0.111	-0.0848	-0.0727	-0.1096	0.0998	-0.0001	0.2891	0.0078	-0.0096	0.3022	0.0371	0.2885	21.6803	-35.0597	38.3652
23	0.8951	0.0429	-0.3044	1.1126	0.2811	0.2002	0.2422	-0.1814	0.1593	0.5871	0.0551	0.1756	-0.5541	-0.1021	0.1331	0.5429	0.0341	0.1818	0.3415	-0.0019	0.3659	10.0876	-19.1314	47.5319
24	0.3298	0.1633	0.1584	0.4042	-0.2948	0.592	-0.0127	0.0941	-0.0301	0.0967	0.0724	0.2322	-0.1392	-0.1275	0.003	0.3028	0.0676	0.0807	0.2823	0.048	0.3719	11.0093	-25.8326	36.7534
25	0.2008	0.3281	-0.2833	0.6411	-0.5361	0.5177	0.0907	-0.0573	-0.0552	0.2025	-0.0501	0.0951	0.0316	-0.0822	0.002	0.2538	0.058	0.035	0.2512	0.0047	0.2484	11.8041	-34.7987	39.5672
26	0.2881	0.2209	-0.3002	0.4885	-0.0154	0.4412	0.093	-0.1052	0.1282	0.0952	-0.0048	-0.0125	-0.1006	0.0975	-0	0.2918	0.0384	0.0108	0.3013	0.0208	0.3016	18.951	-31.8145	31.3413

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid -2 through 32 )	A	-2 - 32
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 33 through 143 )	A	33 - 143
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 144 through 192 )	A	144 - 192
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 193 through 270 )	A	193 - 270
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 271 through 309 )	A	271 - 309
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 310 through 340 )	A	310 - 340
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 341 through 385 )	A	341 - 385
8	X-RAY DIFFRACTION	8	chain 'B' and (resid -2 through 24 )	B	-2 - 24
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 25 through 53 )	B	25 - 53
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 54 through 116 )	B	54 - 116
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 117 through 183 )	B	117 - 183
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 184 through 233 )	B	184 - 233
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 234 through 271 )	B	234 - 271
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 272 through 327 )	B	272 - 327
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 328 through 349 )	B	328 - 349
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 350 through 385 )	B	350 - 385
17	X-RAY DIFFRACTION	17	chain 'C' and (resid -2 through 32 )	C	-2 - 32
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 33 through 53 )	C	33 - 53
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 54 through 116 )	C	54 - 116
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 117 through 149 )	C	117 - 149
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 150 through 183 )	C	150 - 183
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 184 through 233 )	C	184 - 233
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 234 through 276 )	C	234 - 276
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 277 through 317 )	C	277 - 317
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 318 through 349 )	C	318 - 349
26	X-RAY DIFFRACTION	26	chain 'C' and (resid 350 through 385 )	C	350 - 385

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