PDB-9zax: Crystal structure of Phosphoglycerate mutase from Trichomonas vag...

ID or keywords:

Entry

Database: PDB / ID: 9zax

Title

Crystal structure of Phosphoglycerate mutase from Trichomonas vaginalis in complex with 3-phosphoglyceric acid

Components

Phosphoglycerate mutase

Keywords

ISOMERASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / TRANSFERASE / Phosphoglycerate mutase

Function / homology

Function and homology information

phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) / phosphoglycerate mutase activity / canonical glycolysis / cytosol
Similarity search - Function

Biological species

Trichomonas vaginalis G3 (eukaryote)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.1 Å

Authors

Seattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	75N93022C00036	United States
National Institutes of Health/Office of the Director	S10OD030394	United States

Citation

Journal: To be published
Title: Crystal structure of Phosphoglycerate mutase from Trichomonas vaginalis in complex with 3-phosphoglyceric acid
Authors: Seibold, S. / Lovell, S. / Battaile, K.P.

History

Deposition	Nov 19, 2025	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Dec 3, 2025	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	9zax.cif.gz	384.6 KB	Display	PDBx/mmCIF format
PDB format	pdb9zax.ent.gz	311.8 KB	Display	PDB format
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Validation report

Summary document	9zax_validation.pdf.gz	1.6 MB	Display	wwPDB validaton report
Full document	9zax_full_validation.pdf.gz	1.6 MB	Display
Data in XML	9zax_validation.xml.gz	47.6 KB	Display
Data in CIF	9zax_validation.cif.gz	60.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/za/9zax ftp://data.pdbj.org/pub/pdb/validation_reports/za/9zax	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	#50 - Feb 2004 Glycolytic Enzymes similarity (9) #257 - May 2021 Fetal Hemoglobin similarity (8) #225 - Sep 2018 Phytase similarity (1)

Deposited unit

A: Phosphoglycerate mutase

B: Phosphoglycerate mutase

C: Phosphoglycerate mutase

D: Phosphoglycerate mutase

hetero molecules

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

1

Idetical with deposited unit
defined by author
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	74.639, 93.061, 95.485
Angle α, β, γ (deg.)	90.00, 92.86, 90.00
Int Tables number	4
Space group name H-M	P12₁1

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Phosphoglycerate mutase Mass: 29929.199 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trichomonas vaginalis G3 (eukaryote) / Gene: TVAG_165570 / Plasmid: TrvaA.01013.a.B1 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: A2DUN8, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

#1: Protein

Phosphoglycerate mutase

Mass: 29929.199 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Trichomonas vaginalis G3 (eukaryote) / Gene: TVAG_165570 / Plasmid: TrvaA.01013.a.B1 / Production host:

Escherichia coli BL21(DE3) (bacteria)
References: UniProt: A2DUN8, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)

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Non-polymers , 5 types, 474 molecules

#2: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#3: Chemical	ChemComp-3PG / 3-PHOSPHOGLYCERIC ACID Mass: 186.057 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₃H₇O₇P / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	ChemComp-PG4 / TETRAETHYLENE GLYCOL Mass: 194.226 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₈H₁₈O₅ / Comment: precipitant*YM
#5: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO₄
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 455 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
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: 2.77 Å³/Da / Density % sol: 55.54 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: Index F7 : 250 mM AMSO4, 0.1M Bis-Tris pH 6.5, 25% PEG 3350. TrvaA.01013.a.B1.PW39315 at 18.8 mg/mL. plate SS Clover F4 IDX F7 BK 5 pg 18, overnight soak in 2mM 3PG in crystallant. Puck: PSL- ...Details: Index F7 : 250 mM AMSO4, 0.1M Bis-Tris pH 6.5, 25% PEG 3350. TrvaA.01013.a.B1.PW39315 at 18.8 mg/mL. plate SS Clover F4 IDX F7 BK 5 pg 18, overnight soak in 2mM 3PG in crystallant. Puck: PSL-1001, Cryo: 20% (v/v) PEG 200 + 80% crystallant.

Crystal

Density Matthews: 2.77 Å³/Da / Density % sol: 55.54 %

Crystal grow

Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: Index F7 : 250 mM AMSO4, 0.1M Bis-Tris pH 6.5, 25% PEG 3350. TrvaA.01013.a.B1.PW39315 at 18.8 mg/mL. plate SS Clover F4 IDX F7 BK 5 pg 18, overnight soak in 2mM 3PG in crystallant. Puck: PSL- ...

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
Detector	Type: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Jun 7, 2025
Radiation	Monochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9786 Å / Relative weight: 1
Reflection	Resolution: 2.1→48.83 Å / Num. obs: 76013 / % possible obs: 99.8 % / Redundancy: 4.3 % / CC_1/2: 0.994 / R_merge(I) obs: 0.14 / R_pim(I) all: 0.077 / R_rim(I) all: 0.16 / Χ²: 1.02 / Net I/σ(I): 8.3 / Num. measured all: 327122
Reflection shell	Resolution: 2.1→2.14 Å / % possible obs: 99.9 % / Redundancy: 4.2 % / R_merge(I) obs: 0.95 / Num. measured all: 19062 / Num. unique obs: 4503 / CC_1/2: 0.51 / R_pim(I) all: 0.523 / R_rim(I) all: 1.089 / Χ²: 1.06 / Net I/σ(I) obs: 1.7

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Processing

Software

Name	Version	Classification
PHENIX	(2.0_5882: ???)	refinement
Aimless		data scaling
XDS		data reduction
PHASER		phasing
PDB_EXTRACT		data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.1→48.83 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 21.54 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2126	3501	4.61 %
R_work	0.1779	-	-
obs	0.1796	75976	99.73 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 2.1→48.83 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7180	0	139	455	7774

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.004	7479
X-RAY DIFFRACTION	f_angle_d	0.716	10105
X-RAY DIFFRACTION	f_dihedral_angle_d	18.095	2777
X-RAY DIFFRACTION	f_chiral_restr	0.045	1104
X-RAY DIFFRACTION	f_plane_restr	0.006	1272

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 (%)
2.1-2.13	0.2913	128	0.2552	2910	X-RAY DIFFRACTION	100
2.13-2.16	0.2945	126	0.2451	2903	X-RAY DIFFRACTION	100
2.16-2.19	0.2795	131	0.239	2906	X-RAY DIFFRACTION	100
2.19-2.23	0.2822	142	0.229	2876	X-RAY DIFFRACTION	100
2.23-2.26	0.2577	155	0.2234	2899	X-RAY DIFFRACTION	100
2.26-2.3	0.2501	115	0.2042	2860	X-RAY DIFFRACTION	100
2.3-2.34	0.2804	118	0.201	2948	X-RAY DIFFRACTION	100
2.34-2.39	0.2849	113	0.1973	2942	X-RAY DIFFRACTION	100
2.39-2.44	0.2249	120	0.1839	2848	X-RAY DIFFRACTION	100
2.44-2.49	0.2422	149	0.1829	2899	X-RAY DIFFRACTION	100
2.49-2.55	0.1918	157	0.1794	2870	X-RAY DIFFRACTION	100
2.55-2.61	0.2408	146	0.1853	2859	X-RAY DIFFRACTION	100
2.61-2.68	0.2143	131	0.1825	2923	X-RAY DIFFRACTION	100
2.68-2.76	0.2249	166	0.1792	2878	X-RAY DIFFRACTION	100
2.76-2.85	0.2109	182	0.1864	2839	X-RAY DIFFRACTION	100
2.85-2.95	0.2317	136	0.1841	2918	X-RAY DIFFRACTION	100
2.95-3.07	0.2218	110	0.1786	2912	X-RAY DIFFRACTION	100
3.07-3.21	0.2119	148	0.1839	2886	X-RAY DIFFRACTION	100
3.21-3.38	0.2244	151	0.1893	2889	X-RAY DIFFRACTION	100
3.38-3.59	0.2134	147	0.1755	2910	X-RAY DIFFRACTION	100
3.59-3.87	0.181	156	0.1539	2876	X-RAY DIFFRACTION	99
3.87-4.26	0.1482	125	0.1372	2903	X-RAY DIFFRACTION	99
4.26-4.87	0.1638	139	0.1338	2920	X-RAY DIFFRACTION	100
4.87-6.14	0.1932	129	0.1655	2954	X-RAY DIFFRACTION	100
6.14-48.83	0.2166	181	0.1882	2947	X-RAY DIFFRACTION	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	0.3652	1.0827	0.2005	4.3421	-0.1143	1.6658	0.0604	-0.1959	-0.1467	-0.0595	-0.1	-0.2787	0.0401	0.0152	0.0189	0.2576	-0.0111	-0.0076	0.2332	0.0422	0.2497	-3.3484	-17.3815	38.6864
2	3.6027	-1.1532	-0.7528	3.5077	1.7019	1.3414	-0.1428	-0.2516	0.0997	0.3496	0.2555	-0.2867	0.0328	0.4165	-0.1086	0.2554	0.012	-0.0128	0.2357	-0.0403	0.2302	12.4784	9.2703	40.0772
3	2.4214	-0.1201	0.012	2.6983	0.4601	1.8817	0.0602	-0.0109	-0.1289	0.1117	0.0001	-0.1892	0.2159	0.2014	-0.0688	0.2104	0.0133	-0.0294	0.162	-0.0087	0.1553	7.7444	-6.8285	33.5464
4	0.8571	-0.0945	-0.3315	1.7791	0.8136	1.3992	0.0193	-0.0374	0.0417	0.007	0.0403	-0.1382	-0.0213	0.0613	-0.05	0.1829	0.0133	-0.0104	0.1434	0.0013	0.1758	4.0032	3.3689	33.9937
5	2.8001	0.4049	0.5526	2.3907	1.3068	2.9099	0.1655	-0.2964	-0.0974	0.4069	0.0665	-0.3313	0.3807	0.1236	-0.2129	0.412	0.0271	-0.0493	0.2613	-0.0694	0.2649	5.4949	16.9611	53.6988
6	2.1374	0.6237	-0.497	2.0411	-0.0861	3.8852	-0.0033	0.347	0.0847	-0.3116	-0.0886	0.0479	-0.0205	-0.2772	0.0659	0.29	0.0425	0.0068	0.2215	-0.0237	0.2663	-4.1313	17.2295	35.3728
7	2.4034	2.3859	1.7098	6.4128	2.8413	2.4188	0.1549	-0.1934	0.2003	0.4045	-0.2525	0.4609	0.0941	-0.3602	0.0998	0.2198	-0.0143	0.0144	0.2258	-0.0072	0.2013	-9.6168	1.3055	40.7926
8	2.3988	1.0936	-0.9472	3.1262	0.5091	2.4209	0.022	-0.2066	0.0433	0.2271	-0.0223	0.0091	0.1065	0.1546	-0.0151	0.188	0.0245	-0.0389	0.1585	0.0089	0.1477	-3.1063	-4.1932	42.2436
9	6.3531	0.8157	0.3378	2.1892	-0.2935	3.5155	0.1544	-0.7034	0.2548	0.3822	-0.1894	-0.0049	0.049	0.1068	0.0281	0.3429	-0.0164	-0.0136	0.2437	0.042	0.1993	-3.0227	-11.3779	46.692
10	0.7795	-1.4044	-0.3434	4.7907	-0.8907	1.6972	-0.1683	0.3046	0.1877	0.4678	0.0113	-0.3102	-0.3467	0.1418	0.1391	0.318	0.016	-0.0446	0.2031	0.0373	0.241	-2.038	17.3514	9.0101
11	2.0802	-0.5577	-0.0783	2.9743	1.0786	0.9794	0.0267	0.0513	0.006	-0.1355	0.1141	-0.3541	-0.1241	0.206	-0.1459	0.1999	-0.0185	0.0267	0.1929	-0.006	0.1804	11.0458	-0.1046	12.3841
12	0.6507	0.3959	0.0118	1.8847	1.0173	1.4517	0.0068	0.0842	-0.0096	-0.039	0.0911	-0.1746	-0.023	0.1883	-0.0808	0.1995	0.0016	-0.0058	0.1736	-0.0001	0.1653	5.0374	-3.6314	14.1467
13	6.0451	-1.6567	1.5016	6.1045	-0.3161	4.8315	0.1845	0.6854	0.4602	-0.1989	0.0369	-0.4376	-0.3344	0.3795	-0.252	0.4222	-0.0644	0.1246	0.2988	-0.0516	0.3445	11.9118	-16.0186	-8.9495
14	0.9221	-0.9647	-0.1384	3.274	0.1483	0.8175	0.0427	0.0715	-0.0869	-0.1033	0.0198	0.054	-0.0003	-0.0547	-0.0684	0.1575	-0.0083	-0.0183	0.1755	-0.0027	0.1469	-2.6539	-7.3837	6.3785
15	4.2971	0.0337	0.9318	1.9327	-0.0805	3.916	0.209	0.4117	-0.0891	-0.3394	-0.0411	-0.0352	-0.015	0.1376	-0.1783	0.352	0.0118	0.0231	0.2523	0.0831	0.2158	-1.2045	11.1273	1.2426
16	6.8776	6.9575	-5.7088	7.4064	-5.0087	6.3729	0.5301	-0.1364	0.8079	0.424	-0.2378	0.6552	-0.6099	-0.1829	-0.3589	0.2892	0.0729	-0.0165	0.3354	-0.0328	0.4357	-33.6265	12.9578	30.9871
17	4.1948	-1.087	0.2145	1.3391	-1.0989	1.0395	-0.1217	-1.0041	0.0308	0.2886	0.1095	0.4933	-0.4237	-0.715	0.0592	0.2987	0.0105	0.0691	0.5385	-0.0781	0.3722	-40.0647	2.3431	40.878
18	5.3426	2.6448	-2.4682	6.0154	-3.1301	6.1717	0.2614	0.6023	0.5735	0.0388	0.1622	0.7928	-0.4215	-0.8398	-0.3253	0.2509	0.099	-0.0131	0.3578	-0.0161	0.4673	-42.149	11.2101	23.6793
19	2.0188	0.1802	-0.1902	1.6886	0.5397	2.0448	0.0743	-0.0268	-0.0098	-0.2359	-0.2557	0.0508	-0.057	-0.1181	0.1429	0.1992	0.0367	-0.0221	0.2836	-0.0104	0.3003	-31.8399	6.7666	24.9761
20	1.8282	0.3113	0.1632	1.6905	-0.7109	1.3949	0.1854	-0.2816	0.2126	0.1509	-0.1257	0.2435	-0.1634	-0.501	-0.1393	0.1849	-0.0029	0.0088	0.3006	-0.0349	0.2545	-30.0956	3.9666	34.9593
21	4.0202	1.0626	0.0372	0.7537	0.7319	1.1028	0.679	-1.0472	1.0666	0.2605	-0.7991	0.5023	0.0927	-0.1115	0.0043	0.8066	0.0559	0.1159	1.0536	-0.2566	0.7109	-38.0835	10.9607	57.0667
22	4.1607	1.369	0.0694	4.5654	0.1587	3.9189	0.2377	-0.9749	-0.0883	0.8385	-0.3519	0.5059	0.419	-0.353	0.116	0.4232	-0.0844	0.1091	0.6226	-0.0106	0.3004	-31.2665	1.7274	52.8845
23	2.1187	0.5953	0.0824	2.278	-0.5246	3.1014	0.0305	-0.2556	0.1724	0.0974	-0.0541	0.0372	-0.1547	-0.0248	0.0413	0.218	0.0239	0.0002	0.2757	-0.0345	0.2769	-22.8616	7.883	37.2291
24	3.7586	-0.0048	0.733	2.2881	1.2234	4.0508	0.1365	-0.247	0.7204	0.0206	-0.0897	0.1634	-0.7623	0.005	-0.0213	0.532	0.0472	0.0178	0.2533	-0.045	0.5938	-26.1079	23.5493	30.2633
25	2.2369	-0.4204	-0.0461	1.8555	-0.5287	2.3347	0.0044	0.269	-0.2652	-0.1183	-0.1197	0.1615	0.2122	-0.3759	0.0719	0.1834	-0.0069	-0.0072	0.3022	-0.0606	0.2757	-34.8435	-11.0098	14.4242
26	1.8967	0.1066	-0.198	1.2067	-0.165	0.0401	0.0952	0.3676	-0.0688	-0.089	-0.1343	0.2106	-0.0602	-0.2537	0.0179	0.1638	0.0413	-0.0127	0.3199	-0.0161	0.2404	-30.9049	-5.3689	12.8878
27	2.9897	-0.9688	0.1491	0.3698	0.0419	0.345	-0.1327	0.9539	-0.5774	-0.2347	-0.0777	0.2396	-0.3039	-0.1443	0.3244	0.7538	-0.0161	-0.0794	0.8612	-0.1205	0.5455	-34.5728	-12.6796	-12.5599
28	4.367	-1.7944	0.735	3.9331	-1.3522	4.5582	0.2637	1.0739	0.0778	-0.6045	-0.3678	0.1458	-0.0288	-0.5407	0.0626	0.4119	0.0464	0.0129	0.7431	0.0748	0.2872	-28.3274	-3.7211	-8.0056
29	1.6915	-0.0745	-0.5234	2.0043	-0.4059	2.1689	0.0571	0.2503	-0.0742	-0.1429	-0.1065	0.0623	-0.0055	-0.1561	0.0374	0.191	0.0277	-0.0083	0.3105	-0.0331	0.2403	-21.1937	-8.6446	8.3757
30	6.9248	-0.4746	-0.2569	3.5256	1.0134	4.2665	-0.1216	-0.0465	-0.8644	-0.1288	-0.0251	0.303	0.5194	-0.4038	0.1157	0.3698	-0.0472	-0.019	0.2521	-0.0749	0.5285	-25.1727	-24.6904	16.2563

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 3 through 15 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 17 through 37 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 38 through 66 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 67 through 105 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 106 through 138 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 139 through 158 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 159 through 179 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 180 through 201 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 202 through 238 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 3 through 15 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 17 through 66 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 67 through 105 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 106 through 123 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 124 through 201 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 202 through 237 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 7 through 24 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 25 through 37 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 38 through 53 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 54 through 79 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 80 through 105 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 106 through 123 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 124 through 138 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 139 through 201 )
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 202 through 237 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 7 through 66 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 67 through 105 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 106 through 123 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 124 through 138 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 139 through 200 )
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 201 through 238 )

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