PDB-5ao2: Crystal structure of human SAMHD1 (amino acid residues 115-583) R...

ID or keywords:

Entry

Database: PDB / ID: 5ao2

Title

Crystal structure of human SAMHD1 (amino acid residues 115-583) R164A variant bound to dGTP

Components

DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1

Keywords

HYDROLASE / DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE / HIV RESTRICTION FACTOR

Function / homology

Function and homology information

Nucleotide catabolism /

Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity /

dGTP binding / triphosphoric monoester hydrolase activity / dATP catabolic process /

dGTPase activity / tetraspanin-enriched microdomain / dGTP catabolic process / DNA strand resection involved in replication fork processing ...
Similarity search - Function

Biological species

HOMO SAPIENS (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.966 Å

Authors

Schwefel, D. / Taylor, I.A.

Citation

Journal: Plos Pathog. / Year: 2015
Title: Phospho-Dependent Regulation of Samhd1 Oligomerisation Couples Catalysis and Restriction.
Authors: Arnold, L.H. / Groom, H.C.T. / Kunzelmann, S. / Schwefel, D. / Caswell, S.J. / Ordonez, P. / Mann, M.C. / Rueschenbaum, S. / Goldstone, D.C. / Pennell, S. / Howell, S.A. / Stoye, J.P. / ...

History

Deposition	Sep 9, 2015	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Oct 14, 2015	Provider: repository / Type: Initial release
Revision 1.1	Jan 10, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	5ao2.cif.gz	685.8 KB	Display	PDBx/mmCIF format
PDB format	pdb5ao2.ent.gz	564.8 KB	Display	PDB format
PDBx/mmJSON format	5ao2.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ao/5ao2 ftp://data.pdbj.org/pub/pdb/validation_reports/ao/5ao2	HTTPS FTP

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Related structure data

Related structure data	5ao0C 5ao1C 5ao3C 5ao4C 3u1nS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	6u6x-d 6u6y-d 5ao1-d 4rxo-d 0283 4q7h-d 2ib5-d 4pn3-d 5ao3-d 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
Related items in Molecule of the Month	#152 - Aug 2012 cAMP-dependent Protein Kinase similarity (2)

Deposited unit

A: DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1

B: DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1

C: DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1

D: DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1

hetero molecules

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

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	69.706, 199.320, 81.804
Angle α, β, γ (deg.)	90.00, 100.79, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1 / DNTPASE / DENDRITIC CELL-DERIVED IFNG-INDUCED PROTEIN / DCIP / MONOCYTE PROTEIN 5 / MOP-5 / SAM ...DNTPASE / DENDRITIC CELL-DERIVED IFNG-INDUCED PROTEIN / DCIP / MONOCYTE PROTEIN 5 / MOP-5 / SAM DOMAIN AND HD DOMAIN-CONTAINING PROTEIN 1 / SAMHD1 Mass: 56797.988 Da / Num. of mol.: 4 / Fragment: UNP RESIDUES 115-583 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA2 References: UniProt: Q9Y3Z3, Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases
#2: Chemical	ChemComp-FE / FE (III) ION / Iron Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe
#3: Chemical	ChemComp-DGT / 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE / Deoxyguanosine triphosphate Mass: 507.181 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₃P₃
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	R164A VARIANT

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.57 Å³/Da / Density % sol: 52.08 % / Description: NONE
Crystal grow	Details: 0.2 M SODIUM CITRATE, 0.1 M BIS TRIS PROPANE-HCL, 20% PEG 3350, PH 8.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92
Detector	Type: DECTRIS
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.92 Å / Relative weight: 1
Reflection	Resolution: 2.97→30 Å / Num. obs: 43467 / % possible obs: 95.9 % / Observed criterion σ(I): -3 / Redundancy: 3.45 % / B_iso Wilson estimate: 64.01 Å² / R_merge(I) obs: 0.12 / Net I/σ(I): 13.06
Reflection shell	Resolution: 2.97→3.14 Å / Redundancy: 3.13 % / R_merge(I) obs: 0.74 / Mean I/σ(I) obs: 1.96 / % possible all: 81.3

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
XDS		data reduction
XDS		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3U1N

3u1n

Resolution: 2.966→29.564 Å / SU ML: 0.42 / σ(F): 2 / Phase error: 24.38 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2344	2197	5.1 %
R_work	0.1562	-	-
obs	0.1601	43459	96.01 %

Solvent computation

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

Displacement parameters

B_iso mean: 64.8 Å²

Refinement step

Cycle: LAST / Resolution: 2.966→29.564 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13474	0	128	4	13606

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.011	14451
X-RAY DIFFRACTION	f_angle_d	1.501	19512
X-RAY DIFFRACTION	f_dihedral_angle_d	17.831	5467
X-RAY DIFFRACTION	f_chiral_restr	0.068	2063
X-RAY DIFFRACTION	f_plane_restr	0.008	2497

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 (%)
2.9664-3.0309	0.3643	70	0.2549	1555	X-RAY DIFFRACTION	57
3.0309-3.1013	0.3039	128	0.2506	2583	X-RAY DIFFRACTION	98
3.1013-3.1788	0.3548	108	0.2428	2586	X-RAY DIFFRACTION	94
3.1788-3.2646	0.334	158	0.221	2607	X-RAY DIFFRACTION	98
3.2646-3.3605	0.3037	145	0.2152	2674	X-RAY DIFFRACTION	100
3.3605-3.4688	0.2807	153	0.1954	2649	X-RAY DIFFRACTION	100
3.4688-3.5926	0.2351	145	0.1757	2644	X-RAY DIFFRACTION	100
3.5926-3.7362	0.2305	141	0.1498	2682	X-RAY DIFFRACTION	99
3.7362-3.9059	0.2048	129	0.1441	2713	X-RAY DIFFRACTION	99
3.9059-4.1113	0.2512	146	0.1314	2649	X-RAY DIFFRACTION	99
4.1113-4.3681	0.1919	136	0.1251	2664	X-RAY DIFFRACTION	99
4.3681-4.7041	0.1933	147	0.1199	2551	X-RAY DIFFRACTION	96
4.7041-5.1753	0.2206	150	0.1231	2662	X-RAY DIFFRACTION	99
5.1753-5.9189	0.2504	159	0.15	2678	X-RAY DIFFRACTION	100
5.9189-7.4375	0.2077	139	0.1668	2698	X-RAY DIFFRACTION	100
7.4375-29.5652	0.2004	143	0.1393	2667	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	0.0593	0.077	0.0096	0.1131	-0.0034	0.086	-0.0459	-0.0952	0.0578	0.0123	0.1132	0.1025	0.0032	-0.0978	0.0003	0.1995	0.0119	-0.029	0.2104	0.127	0.2102	13.3669	6.3508	13.6084
2	0.2044	-0.1759	0.0729	0.3605	-0.1444	0.0777	0.1305	0.0886	0.0367	-0.2692	-0.0369	0.1184	0.2468	-0.1623	0.0445	0.3242	-0.0678	-0.0792	0.3057	0.0555	0.2571	14.1596	-7.6116	6.3528
3	0.1583	-0.0254	-0.014	0.0283	0.0662	0.1777	-0.035	0.1432	-0.0115	-0.111	0.0169	0.1866	0.0157	-0.1995	-0.124	0.3578	-0.1469	-0.1974	0.4227	0.1502	0.3444	3.0762	0.683	-1.9844
4	0.0029	0.0077	0.002	0.1348	0.105	0.0903	0.0269	0.0987	0.0385	-0.1078	0.0592	-0.0122	0.048	-0.049	0.0765	0.2481	-0.0167	-0.0163	0.3279	0.0997	0.1992	16.8321	10.0096	2.5689
5	0.3496	0.0716	-0.0901	0.3008	-0.1721	0.1458	-0.0588	0.4787	-0.0433	-0.4811	0.159	-0.1104	0.2508	-0.0787	0.0523	0.3247	-0.0337	-0.0255	0.1324	0.1277	0.1839	24.8181	-0.1431	5.9969
6	0.1555	0.1192	0.0321	0.1112	0.0587	0.0592	-0.1816	0.0286	0.0968	-0.2866	0.2389	0.0924	-0.0165	0.0485	0.0178	0.3312	0.0616	0.0466	0.2209	0.0593	0.2433	41.3258	-9.0601	2.8158
7	0.0809	0.1674	0.0304	0.3796	0.1356	0.1177	0.0531	-0.0042	-0.1695	-0.0552	0.0345	-0.3432	0.2548	0.0886	0.0241	0.4192	0.0532	0.0435	0.2225	0.0984	0.2088	43.5313	-14.0034	-7.7088
8	0.0661	0.0683	0.0851	0.1632	0.0378	0.0845	0.0046	0.1686	0.1167	-0.2271	0.1256	0.0256	-0.1011	-0.0202	0.0839	0.1726	0.271	0.0906	0.2296	0.227	0.2764	26.7741	10.5859	-5.2772
9	0.0401	0.0029	0.0481	0.0332	-0.0186	0.1746	-0.1617	-0.0143	-0.0539	-0.0552	-0.1039	0.0067	-0.0325	0.0283	-0.1818	0.328	-0.0062	0.2357	0.2116	-0.1307	0.1086	49.611	-7.1386	-10.0841
10	0.2961	-0.0681	-0.053	0.3344	-0.0881	0.2129	0.1369	-0.1539	-0.0362	0.1044	-0.1693	-0.0882	-0.0298	0.1956	0.0032	0.2337	-0.0351	-0.054	0.2991	0.1116	0.2825	44.3517	2.3954	32.3122
11	0.0405	0.0253	-0.0551	0.2113	-0.1484	0.448	0.01	-0.0715	0.0881	0.1299	0.02	-0.239	-0.2281	0.2739	-0.0413	0.313	-0.0384	0.0277	0.2702	-0.0901	0.3162	38.9863	20.8597	37.3423
12	0.9006	-0.2004	-0.0615	0.1902	-0.1256	0.0636	-0.0464	-0.5375	-0.0286	0.1058	0.0968	0.049	0.1109	-0.2027	0.0531	0.2017	0.0071	-0.0108	0.2445	0.165	0.1823	22.6374	-10.4199	36.6373
13	0.602	-0.6109	0.1672	0.7054	-0.0255	0.388	0.0929	-0.0509	-0.3258	0.0919	0.1297	0.2812	0.0898	-0.3747	0.0243	0.2289	0.0783	0.009	0.5426	0.1072	0.081	9.3738	-2.5279	49.4156
14	0.007	0.0086	0.0015	0.1112	-0.0895	0.1159	0.042	0.0587	-0.112	-0.0951	0.0997	-0.037	-0.0258	0.0871	0.0501	0.208	-0.0035	0.0258	0.267	-0.1249	0.2953	40.4176	43.9521	16.0953
15	0.0442	0.0173	-0.0115	0.1241	-0.0508	0.0184	0.0939	0.0675	0.0661	-0.0591	0.0257	0.107	0.0047	-0.0164	0.0162	0.4198	-0.0163	0.105	0.2102	-0.0083	0.3126	30.2456	61.605	6.8509
16	0.4481	0.1208	0.1214	0.5223	-0.0483	0.1106	0.0384	0.2958	0.0365	-0.3704	0.0909	-0.0649	-0.0793	0.1643	0.0514	0.2175	-0.0512	0.1032	0.209	-0.1127	0.2256	40.7848	43.0027	4.6057
17	0.0072	0.0004	-0.0202	0.0287	-0.0645	0.1587	0.0989	0.003	0.353	0.0341	0.0045	-0.1229	-0.2687	0.0296	0.0897	0.4013	0.0488	0.0295	0.0798	-0.0575	0.4061	24.2076	65.7692	12.5351
18	0.0097	-0.0037	0.0095	0.008	-0.0041	0.0023	-0.0349	-0.0051	-0.0246	0.0276	0.052	-0.0296	-0.1121	-0.0008	0.0001	0.4702	-0.0238	0.007	0.2211	-0.0628	0.4312	29.3749	66.417	19.379
19	0.408	0.1146	-0.2162	0.1189	-0.1971	0.304	0.1053	-0.0994	0.2572	0.0094	0.0708	0.0442	-0.3019	-0.0492	0.0886	0.3774	0.0941	-0.0674	0.221	0.0052	0.2569	13.5881	62.1904	7.9696
20	0.4266	0.1857	0.1463	0.5388	0.1676	0.078	-0.159	-0.0006	0.1565	-0.032	-0.0642	0.1003	-0.2167	-0.0487	-0.0349	0.5312	0.2031	-0.0388	0.3102	0.095	0.1303	13.8733	66.8995	-2.1673
21	0.1424	-0.0003	0.1038	0.1113	-0.0599	0.1241	0.0007	0.0852	0.0058	-0.1289	0.1139	-0.0146	0.0809	-0.0793	-0.0126	0.2833	0.2599	0.0314	0.2063	-0.2539	-0.114	26.9276	41.7167	-3.8411
22	0.0478	0.0135	-0.0121	0.0209	-0.004	0.0062	-0.0549	0.1051	0.02	-0.0901	-0.0168	0.0355	-0.0186	0.0229	-0.0108	0.5512	0.2827	-0.5839	0.5657	0.0573	0.1868	5.209	60.8702	-6.7432
23	0.0799	-0.0446	-0.0923	0.0278	0.0331	0.1921	0.1312	-0.2112	0.0622	0.0467	-0.1559	0.0639	0.1455	-0.2305	0.0089	0.1775	-0.0473	0.0331	0.2703	-0.1217	0.3044	10.3262	48.4091	32.5652
24	0.0139	-0.0073	-0.0202	0.0013	0.0177	0.0538	-0.042	-0.0309	-0.0203	0.0656	-0.0387	-0.0077	0.0347	-0.0029	-0.0688	-0.1169	-0.4054	0.2667	0.4351	-0.2039	0.3001	-0.6408	47.0857	44.6028
25	0.0026	-0.0114	0.0114	0.1124	-0.0841	0.0689	-0.0882	-0.2426	0.0467	0.1338	-0.1988	0.1349	0.1151	-0.2277	-0.0563	0.2841	-0.0764	0.085	0.388	-0.0876	0.348	11.9578	37.1903	38.0666
26	0.0266	0.0651	-0.0359	0.1776	-0.0455	0.2031	-0.0257	-0.0958	-0.156	0.2731	-0.1289	0.0542	0.3124	-0.1594	-0.0701	0.4792	-0.1289	0.021	0.2347	-0.0179	0.2587	14.29	27.3625	37.791
27	0.6566	-0.0292	-0.0124	0.1896	0.196	0.1756	-0.0669	-0.7595	-0.057	0.0067	0.0705	-0.1679	0.0366	0.1451	0.0036	0.2036	-0.0538	-0.0062	0.282	-0.1683	0.208	31.2363	58.2706	40.6126
28	0.1405	-0.0059	0.0922	0.4398	0.0817	0.0715	0.077	-0.2239	0.1137	0.1135	0.1372	-0.2077	-0.1146	0.3391	0.1363	0.0631	-0.0143	-0.1472	0.6196	-0.1855	0.0639	43.1065	50.9235	51.0879
29	0.4165	0.1041	-0.2786	0.1941	-0.1757	0.2518	-0.0345	0.0183	-0.2075	-0.0557	-0.0447	-0.1124	0.1188	0.0552	-0.0184	0.1347	0.1333	-0.1568	0.5924	-0.234	-0.0364	45.7308	45.8082	54.9216

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN 'A' AND (RESID 115 THROUGH 205 )
2	X-RAY DIFFRACTION	2	CHAIN 'A' AND (RESID 206 THROUGH 260 )
3	X-RAY DIFFRACTION	3	CHAIN 'A' AND (RESID 261 THROUGH 291 )
4	X-RAY DIFFRACTION	4	CHAIN 'A' AND (RESID 292 THROUGH 323 )
5	X-RAY DIFFRACTION	5	CHAIN 'A' AND (RESID 324 THROUGH 438 )
6	X-RAY DIFFRACTION	6	CHAIN 'A' AND (RESID 439 THROUGH 469 )
7	X-RAY DIFFRACTION	7	CHAIN 'A' AND (RESID 470 THROUGH 504 )
8	X-RAY DIFFRACTION	8	CHAIN 'A' AND (RESID 505 THROUGH 558 )
9	X-RAY DIFFRACTION	9	CHAIN 'A' AND (RESID 559 THROUGH 582 )
10	X-RAY DIFFRACTION	10	CHAIN 'B' AND (RESID 115 THROUGH 323 )
11	X-RAY DIFFRACTION	11	CHAIN 'B' AND (RESID 324 THROUGH 372 )
12	X-RAY DIFFRACTION	12	CHAIN 'B' AND (RESID 373 THROUGH 482 )
13	X-RAY DIFFRACTION	13	CHAIN 'B' AND (RESID 483 THROUGH 582 )
14	X-RAY DIFFRACTION	14	CHAIN 'C' AND (RESID 115 THROUGH 205 )
15	X-RAY DIFFRACTION	15	CHAIN 'C' AND (RESID 206 THROUGH 232 )
16	X-RAY DIFFRACTION	16	CHAIN 'C' AND (RESID 233 THROUGH 372 )
17	X-RAY DIFFRACTION	17	CHAIN 'C' AND (RESID 373 THROUGH 411 )
18	X-RAY DIFFRACTION	18	CHAIN 'C' AND (RESID 412 THROUGH 435 )
19	X-RAY DIFFRACTION	19	CHAIN 'C' AND (RESID 436 THROUGH 469 )
20	X-RAY DIFFRACTION	20	CHAIN 'C' AND (RESID 470 THROUGH 504 )
21	X-RAY DIFFRACTION	21	CHAIN 'C' AND (RESID 505 THROUGH 558 )
22	X-RAY DIFFRACTION	22	CHAIN 'C' AND (RESID 559 THROUGH 582 )
23	X-RAY DIFFRACTION	23	CHAIN 'D' AND (RESID 115 THROUGH 260 )
24	X-RAY DIFFRACTION	24	CHAIN 'D' AND (RESID 261 THROUGH 291 )
25	X-RAY DIFFRACTION	25	CHAIN 'D' AND (RESID 292 THROUGH 323 )
26	X-RAY DIFFRACTION	26	CHAIN 'D' AND (RESID 324 THROUGH 372 )
27	X-RAY DIFFRACTION	27	CHAIN 'D' AND (RESID 373 THROUGH 481 )
28	X-RAY DIFFRACTION	28	CHAIN 'D' AND (RESID 482 THROUGH 558 )
29	X-RAY DIFFRACTION	29	CHAIN 'D' AND (RESID 559 THROUGH 582 )

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