PDB-8stc: S127A variant of LarB, a carboxylase/hydrolase involved in synthe...

Basic information

• Entry: Database: PDB / ID: 8stc
• Title: S127A variant of LarB, a carboxylase/hydrolase involved in synthesis of the cofactor for lactate racemase, in complex with Zinc and soaked with bicarbonate.
• Components: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase
• Keywords: LYASE / Carboxylase / Hydrolase / LYASE (CARBON-CARBON)

Function / homology

Function:

pyridinium-3,5-biscarboxylic acid mononucleotide synthase / 'de novo' IMP biosynthetic process / transferase activity / hydrolase activity / plasma membrane

Domain/homology:

Pyridinium-3,5-biscarboxylic acid mononucleotide synthase / PurE domain / AIR carboxylase / AIR carboxylase

Component:

Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

• Biological species: Lactiplantibacillus plantarum WCFS1 (bacteria)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
• Authors: Chatterjee, S. / Rankin, J.A. / Hu, J. / Hausinger, R.P.

Funding support

United States, 2items

Organization	Grant number	Country
National Science Foundation (NSF, United States)	CHE-1807073	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	GM128959	United States

• Citation: Journal: To be published; Title: S127A variant of LarB, a carboxylase/hydrolase involved in synthesis of the cofactor for lactate racemase, in complex with Zinc and soaked with bicarbonate.; Authors: Chatterjee, S. / Rankin, J.A. / Hu, J. / Hausinger, R.P.

History

Deposition	May 9, 2023	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 3, 2024	Provider: repository / Type: Initial release

Assembly

Deposited unit

A: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

B: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

C: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

D: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

E: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

F: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

Summary:

• 159 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	159,145	10
Polymers	158,965	6
Non-polymers	179	4
Water	0	0

1

A: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

B: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

A: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

B: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

A: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

B: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

A: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

B: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

Summary:

• defined by software
• Evidence: gel filtration
• 212 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	212,313	16
Polymers	211,954	8
Non-polymers	359	8
Water	0

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1
crystal symmetry operation	2_655	-x+1,-y,z	1
crystal symmetry operation	3_545	-y+1/2,x-1/2,z	1
crystal symmetry operation	4_555	y+1/2,-x+1/2,z	1

Calculated values:

Buried area	20770 Å2
ΔGint	-362 kcal/mol
Surface area	55090 Å2
Method	PISA

2

C: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

D: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

C: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

D: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

C: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

D: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

C: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

D: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

hetero molecules

Summary:

• defined by software
• Evidence: gel filtration
• 212 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	212,313	16
Polymers	211,954	8
Non-polymers	359	8
Water	0

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1
crystal symmetry operation	2_545	-x,-y-1,z	1
crystal symmetry operation	3_445	-y-1/2,x-1/2,z	1
crystal symmetry operation	4_545	y+1/2,-x-1/2,z	1

Calculated values:

Buried area	20880 Å2
ΔGint	-357 kcal/mol
Surface area	57220 Å2
Method	PISA

3

E: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

F: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

E: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

F: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

E: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

F: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

E: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

F: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

Summary:

• defined by software
• Evidence: gel filtration
• 212 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	211,954	8
Polymers	211,954	8
Non-polymers	0	0
Water	0

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1
crystal symmetry operation	2_655	-x+1,-y,z	1
crystal symmetry operation	3_545	-y+1/2,x-1/2,z	1
crystal symmetry operation	4_555	y+1/2,-x+1/2,z	1

Calculated values:

Buried area	14930 Å2
ΔGint	-126 kcal/mol
Surface area	64030 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	120.380, 120.380, 213.159
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	90
Space group name H-M	P4212

Components

#1: Protein

A B C D E F
Pyridinium-3,5-biscarboxylic acid mononucleotide synthase / P2CMN synthase / Lactate racemase accessory protein LarB / Lactate racemase activation protein LarB / Lactate racemase maturation protein LarB / Lactate racemization operon protein LarB / Nickel-pincer cofactor biosynthesis protein LarB / Nicotinic acid adenine dinucleotide carboxylase/hydrolase / NaAD carboxylase/hydrolase

Details:

Mass: 26494.227 Da / Num. of mol.: 6 / Mutation: S127A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactiplantibacillus plantarum WCFS1 (bacteria)
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1 / Gene: larB, lp_0105 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: F9UST0, pyridinium-3,5-biscarboxylic acid mononucleotide synthase

#2: Chemical

A-301 C-301 ChemComp-ZN / ZINC ION

Details:

Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

#3: Chemical

A-302 D-301 ChemComp-MG / MAGNESIUM ION

Details:

Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

• Has ligand of interest: N

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.43 ų/Da / Density % sol: 49.36 %
• Crystal grow: Temperature: 277 K / Method: vapor diffusion, sitting drop; Details: 100 mM magnesium formate, 20% w/v PEG 3350, 2 mM nitrilotriacetic acid neutralized to a pH of ~7.5 with sodium hydroxide, and 0.7 mM zinc sulfate, soaked with 10 mM sodium bicarbonate at pH6 for 20 minutes during freezing

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 1.127 Å
• Detector: Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Nov 3, 2022
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 1.127 Å / Relative weight: 1
• Reflection: Resolution: 2.8→85.12 Å / Num. obs: 39278 / % possible obs: 99.7 % / Redundancy: 13.2 % / CC_1/2: 0.995 / Net I/σ(I): 13.4
• Reflection shell: Resolution: 2.8→2.91 Å / Mean I/σ(I) obs: 2 / Num. unique obs: 4351 / CC_1/2: 0.665

Processing

Software

Name	Version	Classification
PHENIX	(1.19_4092: ???)	refinement
iMOSFLM		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→42.91 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 27.85 / Stereochemistry target values: ML

	Rfactor	Num. reflection	% reflection
Rfree	0.2734	2020	5.15 %
Rwork	0.2367	-	-
obs	0.2386	39221	99.59 %

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

Refinement step

Cycle: LAST / Resolution: 2.8→42.91 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8009	0	4	0	8013

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.019	8251
X-RAY DIFFRACTION	f_angle_d	1.101	11332
X-RAY DIFFRACTION	f_dihedral_angle_d	12.748	2666
X-RAY DIFFRACTION	f_chiral_restr	0.058	1447
X-RAY DIFFRACTION	f_plane_restr	0.008	1495

LS refinement shell

Resolution (Å)	Rfactor Rfree	Num. reflection Rfree	Rfactor Rwork	Num. reflection Rwork	Refine-ID	% reflection obs (%)
2.8-2.87	0.3779	143	0.3304	2611	X-RAY DIFFRACTION	100
2.87-2.95	0.3281	140	0.3178	2599	X-RAY DIFFRACTION	100
2.95-3.03	0.348	142	0.2936	2555	X-RAY DIFFRACTION	98
3.03-3.13	0.3246	142	0.2767	2587	X-RAY DIFFRACTION	99
3.13-3.24	0.2606	127	0.2795	2663	X-RAY DIFFRACTION	100
3.24-3.37	0.3402	136	0.2818	2628	X-RAY DIFFRACTION	100
3.37-3.53	0.2833	133	0.2366	2657	X-RAY DIFFRACTION	100
3.53-3.71	0.2523	147	0.237	2632	X-RAY DIFFRACTION	100
3.71-3.95	0.2482	130	0.227	2667	X-RAY DIFFRACTION	100
3.95-4.25	0.2867	154	0.2219	2650	X-RAY DIFFRACTION	100
4.25-4.68	0.2364	158	0.1894	2670	X-RAY DIFFRACTION	100
4.68-5.35	0.2359	159	0.2093	2694	X-RAY DIFFRACTION	100
5.35-6.74	0.2846	130	0.2704	2708	X-RAY DIFFRACTION	98
6.74-42.91	0.277	179	0.2227	2880	X-RAY DIFFRACTION	100

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	6.0357	0.4197	-3.1302	4.7974	4.5242	6.3658	0.1419	-0.4422	-0.6281	0.4663	0.3071	-0.9534	1.03	1.3158	0.3984	0.8118	0.5451	-0.0119	1.3222	-0.5164	1.2782	44.771	-24.416	1.577
2	7.5365	-1.9939	-3.4209	7.9685	5.1878	5.3093	0.182	2.2152	-0.5676	-1.1272	-0.321	-0.2162	-0.1391	-0.3693	0.1834	0.6393	0.1393	-0.0615	1.1809	-0.1901	0.5726	36.744	-16.206	-0.497
3	6.7159	-1.9523	-1.0619	2.9033	2.4346	7.1796	0.0757	0.2534	0.4846	-0.4287	-0.2843	0.6399	-0.4599	-0.5313	0.1751	0.3358	0.0166	-0.0946	0.4046	-0.0305	0.694	30.955	-3.726	12.731
4	8.4489	1.7445	-0.2708	7.1325	0.8753	9.288	0.0287	0.5327	0.371	0.208	0.1296	-0.638	-0.5179	0.1671	-0.1542	0.2868	0.0554	-0.0214	0.2636	-0.0009	0.4809	40.14	-6.815	18.591
5	3.2004	-0.3348	-2.6705	4.6941	2.4753	9.4603	-0.2824	-1.8647	1.0828	0.5249	0.0304	0.3949	-0.9178	-0.0956	0.2901	0.7621	0.0277	-0.0228	1.081	-0.2757	0.6996	32.683	-7.218	47.294
6	4.3922	-0.7211	1.6878	6.3809	0.6981	3.3633	-0.2972	-1.0025	-0.6437	0.379	-0.0079	0.0073	0.3816	0.1048	0.324	0.3963	0.0384	0.1082	0.4222	0.1387	0.5908	39.303	-23.133	35.773
7	4.5832	-1.1804	-2.8305	7.2037	-0.6411	7.1035	0.1182	-0.3872	0.1929	-0.0294	-0.2312	-0.4153	-0.0895	0.516	0.1335	0.2482	-0.0321	0.0224	0.3088	-0.0123	0.4339	44.422	-17.53	26.004
8	8.2443	5.8395	6.1529	6.1314	4.56	8.7888	0.6556	0.0299	0.4543	-0.3068	-0.3303	1.2233	0.3598	-2.1149	0.0367	0.7353	-0.1278	-0.2044	1.5429	0.1865	0.8525	-4.493	-32.242	22.067
9	3.3309	-0.5543	-1.2633	3.1766	2.8182	7.0638	0.3506	1.1419	-0.6961	-1.1029	-0.3553	0.6106	0.304	-1.2495	-0.0053	0.601	-0.1816	-0.1226	1.1667	0.2127	0.576	1.528	-32.865	22.14
10	7.4564	0.8021	2.1513	6.2576	-1.0215	7.5597	-0.1109	0.8526	-0.1835	-0.9823	0.159	-0.2078	0.2982	0.0379	-0.0472	0.395	-0.0713	0.1051	0.4277	-0.0073	0.4564	15.575	-36.705	29.186
11	5.9675	1.2424	0.271	5.3778	-2.3639	6.7154	-0.0855	-0.2725	-0.6779	-0.0643	0.093	0.2436	0.6741	-0.2593	-0.0009	0.279	-0.0032	0.0551	0.3517	0.0466	0.4613	10.353	-41.634	39.731
12	4.0259	-3.0889	-1.1752	2.7774	-0.4967	5.661	0.3657	-2.3764	-1.4123	0.696	-0.4014	-0.5449	0.4585	1.0149	0.0471	0.9352	-0.2866	-0.2323	1.5583	0.5057	1.0294	19.823	-36.752	64.776
13	4.5838	1.8507	2.2336	4.5506	-1.0339	5.6623	0.2052	-2.7184	0.7188	0.7652	-0.689	0.4856	-0.3075	-0.5344	0.3288	0.5854	-0.0917	0.1261	1.2935	-0.2142	0.656	2.68	-30.681	60.562
14	7.5386	-3.6702	5.1791	9.0289	-0.46	4.2043	0.0041	-0.9412	-0.1802	0.4374	0.0428	1.0903	0.4251	-1.1957	-0.0574	0.4462	-0.0903	0.1008	0.6187	-0.0792	0.5566	-4.248	-34.871	47.724
15	5.6841	2.3447	1.1878	5.267	2.2181	8.7651	0.1424	-0.3354	-0.9582	0.3767	-0.1039	-0.0707	0.596	-0.3417	-0.0528	0.2945	-0.0284	0.0722	0.4381	-0.0061	0.5433	3.036	-38.424	47.324
16	4.8729	-0.6639	0.4759	3.6159	2.285	1.613	-2.1767	-1.2102	-0.6167	1.5007	-0.3807	2.0086	1.7699	-2.4671	2.4684	2.4998	0.0739	0.7641	2.4862	-0.5614	1.6096	39.15	-19.245	118.168
17	5.4552	1.6511	-5.6227	3.273	-3.495	8.7105	0.0463	-1.6749	0.5663	1.156	-0.5897	1.6872	0.6229	1.1376	0.5787	2.2728	-0.5103	0.8638	1.8806	-0.0473	1.5976	47.114	-22.494	123.053
18	0.8831	-0.9152	-0.0215	1.4421	0.6062	4.4899	-0.588	-0.2829	-1.0682	0.0181	0.127	0.1709	1.7964	-0.5837	1.007	3.3396	-0.1171	1.4319	1.1319	0.0256	1.8389	54.639	-33.712	110.044
19	0.6616	1.4044	-1.0936	3.1411	-1.5677	4.4147	-0.1421	-1.0255	-1.358	0.4403	-1.7219	-0.7824	0.865	0.3522	-0.1399	2.892	0.0306	1.5314	1.7472	0.2629	1.7882	61.563	-30.055	108.075
20	2.6853	-2.6652	1.5679	8.3683	3.9392	6.2238	-0.6166	0.6292	-0.4061	-0.4587	-1.1408	-0.4907	1.2538	0.0028	0.9891	2.1707	-0.1351	0.9226	1.2894	0.2027	1.3995	63.374	-18.78	99.448
21	1.6781	0.6426	-1.3694	2.3094	1.6279	5.7913	0.1812	-0.4903	0.0304	0.1588	-0.1136	0.0058	0.8091	-0.0974	0.7467	3.0538	0.0763	1.3247	1.9039	-0.2408	1.4064	52.218	-25.095	100.756
22	9.5419	-3.678	-5.0741	2.2009	1.6003	8.1353	0.2157	-0.1375	0.049	-0.7187	-1.3929	0.1261	1.5822	1.1724	1.1093	1.8617	-0.0049	0.5768	1.8457	0.0541	0.9468	62.893	-29.12	72.57
23	8.1797	4.5323	5.0694	8.5372	2.7196	4.2014	-1.0568	0.7453	-0.7747	-0.2259	-1.1114	1.4989	1.8972	-0.5079	2.2028	1.4484	0.0651	0.4039	1.9346	-0.4026	1.137	55.463	-24.329	66.848
24	5.0011	1.3798	0.4447	0.6264	-1.2354	7.7503	0.4451	0.55	-1.3005	0.092	-1.3217	1.0677	2.794	-1.9323	1.0366	2.1264	-0.5952	0.7367	2.0695	-0.8489	1.607	43.751	-29.02	81.68
25	1.1572	0.1933	-0.2106	0.0439	-0.1481	1.1224	-0.7972	-0.6477	-0.7748	0.0441	-0.2202	0.6761	0.8486	-0.0503	-0.0451	1.9275	0.0029	1.0323	2.937	-1.4607	1.8348	45.153	-24.571	80.67
26	3.4491	-3.6015	0.9223	3.9804	0.3784	8.3572	-0.0892	-1.9104	0.3895	0.4579	-0.1608	0.5751	-0.3639	-1.4055	-0.1728	1.3404	-0.7209	0.6744	2.4524	-0.8824	1.6023	31.079	-19.088	88.889
27	7.7023	-7.3312	-3.7448	8.3106	1.5201	7.1914	-1.5224	-1.2604	0.0964	1.3402	1.6947	0.2532	1.5153	-1.2105	-0.2345	1.7996	-0.4984	0.6794	2.5177	-0.7617	1.3921	41.239	-19.654	92.315
28	8.6596	7.0963	1.6003	9.5135	-1.8054	2.9101	-0.9468	0.6773	0.3774	-0.015	-0.2997	0.7774	1.1835	-0.3961	0.5722	1.6164	-0.3537	0.5904	1.6293	-0.6247	1.2139	48.431	-12.246	91.078
29	0.132	-0.0018	-0.0942	1.1677	0.4111	0.23	0.2721	0.547	-0.1132	-0.53	-0.7971	-0.1559	0.4459	0.1918	0.0291	2.4406	-0.2968	1.325	2.3283	-0.6696	1.3418	51.422	-24.452	90.966
30	5.918	-2.3789	2.6632	6.4398	3.4511	5.0389	-0.8921	-0.3485	-0.2299	0.5093	-0.2407	0.2817	0.2308	-0.2133	-0.5679	0.3558	0.1375	-0.1807	0.4039	0.2902	-0.0033	14.345	-17.857	33.892
31	4.8753	-1.5545	1.5181	1.7967	1.5292	4.026	-0.1249	-1.022	-0.2719	-0.0501	-0.0881	0.1689	-0.242	-1.0883	0.2375	0.3941	0.7729	-0.1078	1.8206	-0.3273	0.1451	29.534	-22.372	26.758

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 44:69 )	A	44 - 69
2	X-RAY DIFFRACTION	2	( CHAIN A AND RESID 70:125 )	A	70 - 125
3	X-RAY DIFFRACTION	3	( CHAIN A AND RESID 126:190 )	A	126 - 190
4	X-RAY DIFFRACTION	4	( CHAIN A AND RESID 191:246 )	A	191 - 246
5	X-RAY DIFFRACTION	5	( CHAIN B AND RESID 44:107 )	B	44 - 107
6	X-RAY DIFFRACTION	6	( CHAIN B AND RESID 108:162 )	B	108 - 162
7	X-RAY DIFFRACTION	7	( CHAIN B AND RESID 163:246 )	B	163 - 246
8	X-RAY DIFFRACTION	8	( CHAIN C AND RESID 46:71 )	C	46 - 71
9	X-RAY DIFFRACTION	9	( CHAIN C AND RESID 72:82 )	C	72 - 82
10	X-RAY DIFFRACTION	10	( CHAIN C AND RESID 83:190 )	C	83 - 190
11	X-RAY DIFFRACTION	11	( CHAIN C AND RESID 191:246 )	C	191 - 246
12	X-RAY DIFFRACTION	12	( CHAIN D AND RESID 43:82 )	D	43 - 82
13	X-RAY DIFFRACTION	13	( CHAIN D AND RESID 83:171 )	D	83 - 171
14	X-RAY DIFFRACTION	14	( CHAIN D AND RESID 172:190 )	D	172 - 190
15	X-RAY DIFFRACTION	15	( CHAIN D AND RESID 191:249 )	D	191 - 249
16	X-RAY DIFFRACTION	16	( CHAIN E AND RESID 46:68 )	E	46 - 68
17	X-RAY DIFFRACTION	17	( CHAIN E AND RESID 69:107 )	E	69 - 107
18	X-RAY DIFFRACTION	18	( CHAIN E AND RESID 108:125 )	E	108 - 125
19	X-RAY DIFFRACTION	19	( CHAIN E AND RESID 126:177 )	E	126 - 177
20	X-RAY DIFFRACTION	20	( CHAIN E AND RESID 178:220 )	E	178 - 220
21	X-RAY DIFFRACTION	21	( CHAIN E AND RESID 221:246 )	E	221 - 246
22	X-RAY DIFFRACTION	22	( CHAIN F AND RESID 49:82 )	F	49 - 82
23	X-RAY DIFFRACTION	23	( CHAIN F AND RESID 83:107 )	F	83 - 107
24	X-RAY DIFFRACTION	24	( CHAIN F AND RESID 108:128 )	F	108 - 128
25	X-RAY DIFFRACTION	25	( CHAIN F AND RESID 129:153 )	F	129 - 153
26	X-RAY DIFFRACTION	26	( CHAIN F AND RESID 154:168 )	F	154 - 168
27	X-RAY DIFFRACTION	27	( CHAIN F AND RESID 169:190 )	F	169 - 190
28	X-RAY DIFFRACTION	28	( CHAIN F AND RESID 191:218 )	F	191 - 218
29	X-RAY DIFFRACTION	29	( CHAIN F AND RESID 219:246 )	F	219 - 246
30	X-RAY DIFFRACTION	30	( CHAIN A AND RESID 302:302 ) OR ( CHAIN D AND RESID 301:301 )	A	302
31	X-RAY DIFFRACTION	30	( CHAIN A AND RESID 302:302 ) OR ( CHAIN D AND RESID 301:301 )	D	301
32	X-RAY DIFFRACTION	31	( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 )	A	301
33	X-RAY DIFFRACTION	31	( CHAIN A AND RESID 301:301 ) OR ( CHAIN C AND RESID 301:301 )	C	301