PDB-7mj0: LarB, a carboxylase/hydrolase involved in synthesis of the cofact...

Basic information

• Entry: Database: PDB / ID: 7mj0
• Title: LarB, a carboxylase/hydrolase involved in synthesis of the cofactor for lactate racemase, in complex with adenosine monophosphate AMP
• Components: Pyridinium-3,5-biscarboxylic acid mononucleotide synthase
• Keywords: LYASE (CARBON-CARBON) / Carboxylase / Hydrolase

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:

ADENOSINE MONOPHOSPHATE / Pyridinium-3,5-biscarboxylic acid mononucleotide synthase

• Biological species: Lactobacillus plantarum (bacteria)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.01 Å
• Authors: Chatterjee, S. / Rankin, J.A. / Lagishetty, S. / 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: Proc.Natl.Acad.Sci.USA / Year: 2021; Title: The LarB carboxylase/hydrolase forms a transient cysteinyl-pyridine intermediate during nickel-pincer nucleotide cofactor biosynthesis.; Authors: Rankin, J.A. / Chatterjee, S. / Tariq, Z. / Lagishetty, S. / Desguin, B. / Hu, J. / Hausinger, R.P.

History

Deposition	Apr 19, 2021	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 29, 2021	Provider: repository / Type: Initial release
Revision 1.1	Oct 18, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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:

• 160 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	159,804	10
Polymers	159,061	6
Non-polymers	743	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 author&software
• Evidence: light scattering
• 214 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	213,665	20
Polymers	212,082	8
Non-polymers	1,583	12
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	23800 Å2
ΔGint	-273 kcal/mol
Surface area	53780 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 author&software
• 213 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	213,471	12
Polymers	212,082	8
Non-polymers	1,389	4
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	22310 Å2
ΔGint	-186 kcal/mol
Surface area	56110 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 author&software
• 212 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	212,082	8
Polymers	212,082	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	19220 Å2
ΔGint	-161 kcal/mol
Surface area	54670 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	121.284, 121.284, 213.406
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
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: 26510.227 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactobacillus plantarum (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-AMP / ADENOSINE MONOPHOSPHATE

Details:

Mass: 347.221 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₀H₁₄N₅O₇P / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP*YM

#3: Chemical

A-302 A-303 ChemComp-MG / MAGNESIUM ION

Details:

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

• Has ligand of interest: Y

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.47 ų/Da / Density % sol: 50.14 %
• Crystal grow: Temperature: 277 K / Method: vapor diffusion, sitting drop; Details: 20% PEG 3350, 100 mM Magnesium formate, 2 mM nitrilotriacetic acid (pH to 7.5 with sodium hydroxide), 0.7 mM zinc sulfate, 10 mM EDTA, 10 mM AMP

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.978 Å
• Detector: Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 19, 2019
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.978 Å / Relative weight: 1
• Reflection: Resolution: 3.01→40 Å / Num. obs: 32347 / % possible obs: 99.9 % / Redundancy: 9.7 % / R_merge(I) obs: 0.145 / R_pim(I) all: 0.049 / R_rim(I) all: 0.153 / Χ²: 0.84 / Net I/σ(I): 4.9

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	Rmerge(I) obs	Num. unique obs	CC1/2	Rpim(I) all	Χ2	% possible all	Rrim(I) all
3.09-3.21	9.6	0.988	2892	0.787	0.334	0.666	100
3.21-3.34	9.9	0.684	2933	0.908	0.228	0.703	100	0.722
3.34-3.49	9.9	0.468	2913	0.96	0.156	0.776	100	0.494
3.49-3.68	9.9	0.398	2942	0.965	0.132	0.82	100	0.42
3.68-3.91	9.9	0.254	2917	0.984	0.084	0.873	100	0.268
3.91-4.21	9.9	0.168	2945	0.994	0.056	0.825	100	0.177
4.21-4.63	9.8	0.109	2972	0.996	0.036	0.892	100	0.115
4.63-5.3	9.7	0.101	2985	0.997	0.034	1.06	100	0.106
5.3-6.67	9.6	0.101	3036	0.996	0.034	0.972	100	0.107
3.01-3.17	9.1		4619	0.699			99.9

Processing

Software

Name	Version	Classification
PHENIX	1.14_3260	refinement
HKL-2000		data scaling
PDB_EXTRACT	3.27	data extraction
HKL-2000		data reduction
MOLREP		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 1D7A

1d7a

Resolution: 3.01→39.788 Å / SU ML: 0.45 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 29.55 / Stereochemistry target values: ML

	Rfactor	Num. reflection	% reflection
Rfree	0.2746	1673	5.18 %
Rwork	0.2353	30647	-
obs	0.2373	32320	99.89 %

• Solvent computation: Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
• Displacement parameters: B_iso max: 309.75 Ų / B_iso mean: 108.5008 Ų / B_iso min: 22.89 Ų

Refinement step

Cycle: final / Resolution: 3.01→39.788 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8501	0	48	0	8549
Biso mean	-	-	67.09	-	-
Num. residues	-	-	-	-	1213

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.01	8679
X-RAY DIFFRACTION	f_angle_d	1.15	11875
X-RAY DIFFRACTION	f_dihedral_angle_d	14.091	2946
X-RAY DIFFRACTION	f_chiral_restr	0.207	1494
X-RAY DIFFRACTION	f_plane_restr	0.008	1528

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0

Resolution (Å)	Rfactor Rfree	Num. reflection Rfree	Rfactor Rwork	Num. reflection Rwork	% reflection obs (%)
3.0103-3.0989	0.3608	157	0.3356	2474	100
3.0989-3.1989	0.3488	125	0.3181	2525	100
3.1989-3.3131	0.3178	142	0.2981	2498	100
3.3131-3.4457	0.3204	124	0.273	2511	100
3.4457-3.6024	0.3478	132	0.2593	2520	100
3.6024-3.7922	0.2923	141	0.2594	2529	100
3.7922-4.0296	0.2726	135	0.2376	2531	100
4.0296-4.3404	0.2347	157	0.2104	2526	100
4.3404-4.7765	0.222	149	0.1796	2544	100
4.7765-5.4662	0.2165	115	0.2136	2616	100
5.4662-6.881	0.3272	159	0.2624	2599	100
6.881-39.788	0.2516	137	0.2075	2774	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	6.7583	-3.3209	3.6406	3.8916	2.2945	9.383	0.336	-0.4101	-0.1487	0.3261	0.1989	-0.3407	0.2073	0.3014	-0.2751	1.3509	-0.2451	0.5081	0.7508	-0.2634	0.736	45.0561	-23.4659	5.6437
2	3.6406	-0.0991	1.3992	5.598	1.6413	1.9732	-0.1444	1.283	-0.9939	-1.1553	-0.3548	-0.7352	0.0654	0.1383	0.2713	1.6079	-0.0878	0.598	1.0359	-0.2123	0.917	44.0468	-19.2053	-4.3853
3	5.1599	-1.5094	-3.4958	2.4974	-0.7596	4.5112	-0.7659	1.1293	-0.9766	-1.2359	-0.1448	0.5953	1.3414	-0.5162	0.8634	0.7131	-0.1862	-0.0622	0.8186	-0.3664	0.7449	28.6997	-14.6395	8.3992
4	3.2022	-0.526	-0.1654	4.0716	0.6191	4.4015	-0.0563	0.3196	0.4255	-0.3663	-0.1578	0.289	-0.1443	-0.1989	0.132	0.2778	0.0065	-0.0732	0.2625	-0.047	0.4257	36.0665	-5.6736	15.4687
5	4.0217	-1.9321	-0.0396	3.1911	1.283	6.4204	0.3924	-1.3268	1.6076	0.9645	-0.2063	0.7091	-0.4516	0.0365	0.4074	0.8457	-0.2643	0.2923	1.1744	-0.949	1.0524	30.4109	-6.2873	44.8182
6	2.163	1.2882	0.2409	2.1837	-0.1527	2.4412	-0.1454	-2.0318	-0.2945	0.6948	-0.3068	0.0255	0.1212	0.4666	0.2951	0.5387	-0.0127	0.0357	0.9424	0.0324	0.4621	39.5708	-20.2453	40.8482
7	7.291	-0.0376	-1.5642	4.4826	0.4125	4.6701	-0.1292	-0.4008	-0.0086	0.0006	-0.1091	-0.4664	-0.0229	0.5077	0.2264	0.2425	-0.0342	0.0232	0.3713	0.0528	0.3589	45.0959	-18.0524	26.9497
8	7.1866	-3.4967	-2.9727	3.3019	-1.0333	5.1286	0.0585	-0.3372	0.2546	-0.4833	0.0715	1.1549	0.2624	-0.4794	0.1994	0.8135	0.1689	-0.372	0.6908	0.0627	1.0159	-1.7895	-31.9113	26.6353
9	3.0007	-0.5249	-0.4906	0.0974	0.0139	0.9341	0.2327	-0.1221	0.5632	-0.0927	0.3396	0.1731	-0.0834	-0.1932	-0.3632	1.2348	0.2006	-0.6575	1.5699	-0.1025	1.3278	-5.0973	-30.821	17.8307
10	2.9781	-0.1163	0.7087	0.0831	0.6915	6.4761	-0.0564	1.4524	-0.2307	-1.4451	0.2135	0.361	1.1928	0.106	-0.4274	1.8276	0.2059	-0.5319	1.257	0.0514	0.6976	2.4469	-37.1512	15.2405
11	3.3026	1.2362	1.495	4.4547	1.8197	4.2504	-0.0693	0.4331	0.4768	-2.0981	-0.1414	0.4416	-0.8437	-0.4321	0.3819	0.9536	0.0821	-0.0403	0.5309	0.0193	0.4957	12.8681	-32.7041	25.2331
12	3.3125	0.4104	0.2975	3.6395	0.512	2.7533	0.0591	0.0704	-0.3584	-0.5581	-0.2412	-0.7049	-0.0695	0.2758	0.3038	0.355	-0.0052	0.0729	0.3598	0.1061	0.4569	19.8811	-39.5453	35.369
13	2.7875	-0.0531	-0.7536	5.5249	-0.6148	3.7784	0.114	-0.1176	-0.4353	0.1266	-0.2903	0.3091	0.0502	0.1298	0.1789	0.2065	-0.0626	0.0483	0.3756	0.0582	0.3338	10.4953	-41.3687	39.3023
14	3.0996	-1.3959	1.4152	2.1005	0.3192	5.7886	0.1249	-0.4812	-0.2489	-0.2244	0.4489	-0.9769	0.856	-0.3775	-0.3682	1.3212	-0.4635	-0.4183	0.7545	0.4885	1.3748	20.7816	-37.1653	60.3419
15	2.2532	-1.2496	-1.2376	2.8538	-1.5911	3.0673	0.4098	-1.4417	-0.8015	1.1858	-0.1258	-1.0043	0.2308	0.6049	-0.0414	1.0015	-0.4405	-0.6147	1.6942	0.179	0.7462	20.2271	-37.3748	68.2952
16	2.7257	-0.338	-0.6524	4.3556	-4.0558	4.888	0.1077	-0.9851	0.2245	1.3394	-0.4434	-0.4525	0.0064	0.0178	0.3054	1.6523	-1.0073	-0.3687	2.637	0.3958	1.0087	14.2105	-38.2928	77.4106
17	1.712	-1.9568	2.1509	2.8395	-2.0218	4.79	0.6293	-1.7989	0.3711	1.257	-1.2579	0.2976	-0.175	-0.5299	0.4578	0.719	-0.4039	0.0227	1.4061	-0.2491	0.6474	6.4702	-31.4046	61.6654
18	3.2848	1.0548	3.0168	1.3746	0.319	3.1818	0.045	-1.7741	1.1387	0.6541	-0.6104	1.3003	-0.5932	-0.7157	0.3325	0.5001	-0.1483	0.0675	0.9414	-0.5408	1.0798	-4.6959	-27.4572	53.0851
19	4.4697	-1.3978	1.5259	5.7194	-0.5263	7.6763	0.237	-1.0373	0.2314	0.423	-0.0729	0.8119	0.3228	-0.7039	-0.1411	0.4353	-0.0871	0.0807	0.5835	-0.155	0.4522	-1.8886	-36.365	48.5587
20	4.7975	2.0293	0.9841	4.2	1.1655	7.8188	0.4844	-1.068	-0.6029	0.4018	-0.6601	-0.4555	0.6342	0.0964	0.204	0.3966	-0.0704	-0.0166	0.5372	0.0206	0.4195	5.2313	-39.5717	48.1299
21	3.6704	1.4114	-0.3566	2.6165	-1.1008	2.4753	0.2639	-0.0501	-0.113	-1.095	-1.1837	0.3081	0.2778	0.034	0.5868	2.5009	0.498	1.0312	2.1087	0.0674	1.4802	60.25	-25.9181	70.0246
22	2.6546	-1.4141	-1.9574	4.5218	3.3849	3.0247	-0.5183	0.2075	-1.1058	-0.1485	-0.7709	0.5547	1.5929	-0.2192	1.1257	2.5343	-0.501	1.089	1.8864	-0.8637	1.5208	43.8487	-29.7257	80.8797
23	1.7679	0.7528	0.0897	1.6564	-0.1516	2.5605	0.145	-0.2734	-0.1391	-0.7627	-0.5641	0.4828	0.3962	-0.7381	0.4701	2.1782	-0.5494	0.8199	2.3955	-1.2125	1.2432	39.7266	-21.5992	83.1555
24	4.8284	-0.5521	-3.5777	0.3003	-0.5413	6.4217	0.1331	0.6592	-0.0103	-0.1786	0.0569	-0.0819	-0.0348	-0.9248	-0.0238	1.731	-0.5832	1.4953	1.8884	-0.9899	1.4628	41.8828	-18.3476	90.7648
25	2.8852	-2.0605	-1.6406	1.954	2.4207	4.1452	-0.3274	-0.2532	-0.4508	0.3183	-0.0666	0.4845	0.5699	0.2615	0.2129	1.9633	-0.6006	0.9944	1.7662	-0.9033	1.5267	45.1005	-15.7324	90.9399
26	1.4889	-1.4847	-0.601	6.3577	3.6579	2.7217	-0.3434	-0.1332	0.1699	-0.2714	-0.5586	0.2757	1.0464	0.2601	0.2651	1.8742	-0.3969	1.2361	1.4305	-0.4443	1.5768	51.0743	-19.2451	91.4767
27	0.8579	-0.3012	1.3994	4.4301	4.1454	7.2978	0.2221	-1.0684	0.2781	0.0729	-0.5217	0.4193	0.4973	-0.7474	0.0159	2.2195	-0.5799	0.9796	2.1053	-0.3006	1.5781	40.982	-21.2815	117.9114
28	6.283	-2.7138	-6.3388	2.4794	2.026	9.4907	-0.1736	-0.7654	-0.7722	-0.4995	-0.953	-0.5136	1.3509	-1.2674	0.9755	2.3086	-0.2651	0.9848	1.8702	0.173	1.6055	49.9842	-28.172	117.9628
29	5.6984	-1.7307	-0.5988	2.4782	-2.8963	8.3349	-1.2452	1.6426	-0.7501	-0.476	0.7288	-0.2759	0.5341	-0.2524	0.4052	2.6256	-0.1019	1.3885	1.9332	0.3222	1.3281	56.8603	-25.3797	112.1913
30	0.3014	-0.2893	-0.0262	0.9606	0.2516	2.19	-0.2486	-0.4759	-0.304	0.406	-0.8795	-0.1202	1.3337	-0.1515	0.069	2.9233	-0.1354	2.3193	1.1211	0.7879	1.6602	60.3864	-25.5608	101.1533

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 through 58 )	A	44 - 58
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 59 through 107 )	A	59 - 107
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 108 through 125 )	A	108 - 125
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 126 through 246 )	A	126 - 246
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 44 through 82 )	B	44 - 82
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 83 through 162 )	B	83 - 162
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 163 through 246 )	B	163 - 246
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 44 through 58 )	C	44 - 58
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 59 through 74 )	C	59 - 74
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 75 through 96 )	C	75 - 96
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 97 through 125 )	C	97 - 125
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 126 through 199 )	C	126 - 199
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 200 through 250 )	C	200 - 250
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 43 through 58 )	D	43 - 58
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 59 through 82 )	D	59 - 82
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 83 through 96 )	D	83 - 96
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 97 through 141 )	D	97 - 141
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 142 through 169 )	D	142 - 169
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 170 through 207 )	D	170 - 207
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 208 through 246 )	D	208 - 246
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 49 through 107 )	E	49 - 107
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 108 through 126 )	E	108 - 126
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 127 through 168 )	E	127 - 168
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 169 through 188 )	E	169 - 188
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 189 through 207 )	E	189 - 207
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 208 through 246 )	E	208 - 246
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 46 through 85 )	F	46 - 85
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 86 through 125 )	F	86 - 125
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 126 through 141 )	F	126 - 141
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 142 through 246 )	F	142 - 246