PDB-2bwo: 5-Aminolevulinate Synthase from Rhodobacter capsulatus in complex...

ID or keywords:

Entry

Database: PDB / ID: 2bwo

Title

5-Aminolevulinate Synthase from Rhodobacter capsulatus in complex with succinyl-CoA

Components

5-AMINOLEVULINATE SYNTHASE

Keywords

TRANSFERASE / TETRAPYRROLE BIOSYNTHESIS / HEME BIOSYNTHESIS / PYRIDOXAL PHOSPHATE DEPENDENT / ACYLTRANSFERASE

Function / homology

Function and homology information

5-aminolevulinate synthase / 5-aminolevulinate synthase activity / hemoglobin biosynthetic process / protoporphyrinogen IX biosynthetic process / pyridoxal phosphate binding
Similarity search - Function

Biological species

RHODOBACTER CAPSULATUS (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / OTHER / Resolution: 2.8 Å

Authors

Astner, I. / Schulze, J.O. / van den Heuvel, J.J. / Jahn, D. / Schubert, W.-D. / Heinz, D.W.

Citation

Journal: Embo J. / Year: 2005
Title: Crystal Structure of 5-Aminolevulinate Synthase, the First Enzyme of Heme Biosynthesis, and its Link to Xlsa in Humans.
Authors: Astner, I. / Schulze, J.O. / Van Den Heuvel, J.J. / Jahn, D. / Schubert, W.-D. / Heinz, D.W.

History

Deposition	Jul 15, 2005	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Sep 27, 2005	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	Dec 23, 2015	Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other / Refinement description / Source and taxonomy / Structure summary

Remark 650

HELIX DETERMINATION METHOD: AUTHOR PROVIDED.

Remark 700

SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2bwo.cif.gz	311.9 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2bwo_validation.pdf.gz	1.2 MB	Display	wwPDB validaton report
Full document	2bwo_full_validation.pdf.gz	1.2 MB	Display
Data in XML	2bwo_validation.xml.gz	61.4 KB	Display
Data in CIF	2bwo_validation.cif.gz	81.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/bw/2bwo ftp://data.pdbj.org/pub/pdb/validation_reports/bw/2bwo	HTTPS FTP

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Related structure data

Related structure data	2bwnC 2bwpC C: citing same article (ref.)
Similar structure data	2bwp-1 4wyc-d 2bwp-2 3tfu-d 4xew-d 3tft-d 4xjo-d 4wye-d 6cgm-d 3lv2-d 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

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: 5-AMINOLEVULINATE SYNTHASE

B: 5-AMINOLEVULINATE SYNTHASE

D: 5-AMINOLEVULINATE SYNTHASE

E: 5-AMINOLEVULINATE SYNTHASE

hetero molecules

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

1

A: 5-AMINOLEVULINATE SYNTHASE

B: 5-AMINOLEVULINATE SYNTHASE

hetero molecules

defined by author&software
89.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: 5-AMINOLEVULINATE SYNTHASE

E: 5-AMINOLEVULINATE SYNTHASE

hetero molecules

defined by author&software
89.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	67.935, 91.356, 247.644
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Refine code	Auth asym-ID	Auth seq-ID
1	1	1	2	A	3 - 320
2	1	1	2	B	3 - 320
3	1	1	2	D	3 - 320
4	1	1	2	E	3 - 320
1	2	1	2	A	328 - 338
2	2	1	2	B	328 - 338
3	2	1	2	D	328 - 338
4	2	1	2	E	328 - 338
1	3	1	6	A	339 - 356
2	3	1	6	B	339 - 356
3	3	1	6	D	339 - 356
4	3	1	6	E	339 - 356
1	4	1	2	A	357 - 380
2	4	1	2	B	357 - 380
3	4	1	2	D	357 - 380
4	4	1	2	E	357 - 380
1	5	1	2	A	381 - 399
2	5	1	2	B	381 - 399
3	5	1	2	D	381 - 399
4	5	1	2	E	381 - 399
1	1	2	2	B	3 - 320
2	1	2	2	A	3 - 320
3	1	2	2	D	3 - 320
4	1	2	2	E	3 - 320
1	2	2	2	B	328 - 338
2	2	2	2	A	328 - 338
3	2	2	2	D	328 - 338
4	2	2	2	E	328 - 338
1	3	2	6	B	339 - 356
2	3	2	6	A	339 - 356
3	3	2	6	D	339 - 356
4	3	2	6	E	339 - 356
1	4	2	2	B	357 - 380
2	4	2	2	A	357 - 380
3	4	2	2	D	357 - 380
4	4	2	2	E	357 - 380
1	5	2	6	B	381 - 399
2	5	2	6	A	381 - 399
3	5	2	6	D	381 - 399
4	5	2	6	E	381 - 399
1	1	3	2	D	3 - 320
2	1	3	2	A	3 - 320
3	1	3	2	B	3 - 320
4	1	3	2	E	3 - 320
1	2	3	2	D	328 - 338
2	2	3	2	A	328 - 338
3	2	3	2	B	328 - 338
4	2	3	2	E	328 - 338
1	3	3	6	D	339 - 356
2	3	3	6	A	339 - 356
3	3	3	6	B	339 - 356
4	3	3	6	E	339 - 356
1	4	3	2	D	357 - 380
2	4	3	2	A	357 - 380
3	4	3	2	B	357 - 380
4	4	3	2	E	357 - 380
1	5	3	6	D	381 - 399
2	5	3	6	A	381 - 399
3	5	3	6	B	381 - 399
4	5	3	6	E	381 - 399
1	1	4	2	E	3 - 320
2	1	4	2	A	3 - 320
3	1	4	2	B	3 - 320
4	1	4	2	D	3 - 320
1	2	4	2	E	328 - 338
2	2	4	2	A	328 - 338
3	2	4	2	B	328 - 338
4	2	4	2	D	328 - 338
1	3	4	6	E	339 - 356
2	3	4	6	A	339 - 356
3	3	4	6	B	339 - 356
4	3	4	6	D	339 - 356
1	4	4	2	E	357 - 380
2	4	4	2	A	357 - 380
3	4	4	2	B	357 - 380
4	4	4	2	D	357 - 380
1	5	4	6	E	381 - 399
2	5	4	6	A	381 - 399
3	5	4	6	B	381 - 399
4	5	4	6	D	381 - 399

NCS ensembles :

ID
1
2
3
4

#1: Protein	5-AMINOLEVULINATE SYNTHASE / 5-AMINOLEVULINIC ACID SYNTHASE / DELTA- AMINOLEVULINATE SYNTHASE / DELTA-ALA SYNTHETASE Mass: 43673.910 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: LYSINE 248 COVALENTLY BOUND TO PLP, CHAIN A / Source: (gene. exp.) RHODOBACTER CAPSULATUS (bacteria) Description: GERMAN COLLECTION OF MICROORGANISMS (DSM) DSM 1710 Plasmid: PQE30 / Production host: ESCHERICHIA COLI M15 (bacteria) / References: UniProt: P18079, 5-aminolevulinate synthase
#2: Chemical	ChemComp-SCA / SUCCINYL-COENZYME A Mass: 867.607 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₅H₄₀N₇O₁₉P₃S
#3: Chemical	ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate Mass: 247.142 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₈H₁₀NO₆P
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 110 / Source method: isolated from a natural source / Formula: H₂O
Sequence details	DIFFERENT STRAINS OF RHODOBACTER CAPSULATUS

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.21 Å³/Da / Density % sol: 44 %
Crystal grow	pH: 7.5 Details: 100 MM HEPES PH 7.5, 200 MM NA ACETATE, 8% (V/V) ISOPROPANOL, 20% PEG 4000

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9537
Detector	Type: MARRESEARCH / Detector: CCD / Date: Oct 27, 2004 / Details: MIRRORS
Radiation	Monochromator: SILICON CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection	Resolution: 2.8→30 Å / Num. obs: 137995 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / R_merge(I) obs: 0.08 / Net I/σ(I): 13.5
Reflection shell	Resolution: 2.8→2.9 Å / Redundancy: 3.5 % / R_merge(I) obs: 0.36 / Mean I/σ(I) obs: 2.8 / % possible all: 99.7

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0005	refinement
DENZO		data reduction
SCALEPACK		data scaling
CNS		phasing

Refinement

Method to determine structure: OTHER / Resolution: 2.8→119.52 Å / Cor.coef. F_o:F_c: 0.957 / Cor.coef. F_o:F_c free: 0.92 / SU B: 26.87 / SU ML: 0.252 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.375 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS ATOMS MODELED WITH ZERO OCCUPANCY TO INDICATE THE PROBABLE LOCATION OF A CO-FACTOR IN THE ACTIVE STATE OF THE ENZYME.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.224	1876	4.9 %	RANDOM
R_work	0.16	-	-	-
obs	0.163	36616	99.3 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 26.65 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.04 Å²	0 Å²	0 Å²
2-	-	1.55 Å²	0 Å²
3-	-	-	-1.51 Å²

Refinement step

Cycle: LAST / Resolution: 2.8→119.52 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12209	0	283	110	12602

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.019	0.022	12678
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.614	1.972	17200
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.057	5	1589
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	32.917	23.236	550
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.04	15	2030
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.741	15	90
X-RAY DIFFRACTION	r_chiral_restr	0.139	0.2	1868
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	9661
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.216	0.2	6128
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.311	0.2	8706
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.138	0.2	451
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.272	0.2	65
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.246	0.2	10
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	2.552	2	8075
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	3.688	3	12605
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	3.497	2	5177
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	5.089	3	4595
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	1476	tight positional	0.04	0.05
1	2	B	1476	tight positional	0.03	0.05
1	3	D	1476	tight positional	0.03	0.05
1	4	E	1476	tight positional	0.03	0.05
2	1	B	1408	tight positional	0.02	0.05
2	2	A	1408	tight positional	0.02	0.05
2	3	D	1408	tight positional	0.02	0.05
2	4	E	1408	tight positional	0.02	0.05
3	1	D	1408	tight positional	0.02	0.05
3	2	A	1408	tight positional	0.02	0.05
3	3	B	1408	tight positional	0.02	0.05
3	4	E	1408	tight positional	0.02	0.05
4	1	E	1408	tight positional	0.02	0.05
4	2	A	1408	tight positional	0.02	0.05
4	3	B	1408	tight positional	0.02	0.05
4	4	D	1408	tight positional	0.02	0.05
1	1	A	1356	medium positional	0.47	0.5
1	2	B	1356	medium positional	0.43	0.5
1	3	D	1356	medium positional	0.46	0.5
1	4	E	1356	medium positional	0.43	0.5
2	1	B	1284	medium positional	0.39	0.5
2	2	A	1284	medium positional	0.44	0.5
2	3	D	1284	medium positional	0.45	0.5
2	4	E	1284	medium positional	0.4	0.5
3	1	D	1284	medium positional	0.45	0.5
3	2	A	1284	medium positional	0.44	0.5
3	3	B	1284	medium positional	0.39	0.5
3	4	E	1284	medium positional	0.4	0.5
4	1	E	1284	medium positional	0.4	0.5
4	2	A	1284	medium positional	0.44	0.5
4	3	B	1284	medium positional	0.39	0.5
4	4	D	1284	medium positional	0.45	0.5
1	1	A	135	loose positional	0.37	5
1	2	B	135	loose positional	0.59	5
1	3	D	135	loose positional	0.38	5
1	4	E	135	loose positional	0.4	5
2	1	B	275	loose positional	0.62	5
2	2	A	275	loose positional	0.54	5
2	3	D	275	loose positional	0.42	5
2	4	E	275	loose positional	0.51	5
3	1	D	275	loose positional	0.42	5
3	2	A	275	loose positional	0.54	5
3	3	B	275	loose positional	0.62	5
3	4	E	275	loose positional	0.51	5
4	1	E	275	loose positional	0.51	5
4	2	A	275	loose positional	0.54	5
4	3	B	275	loose positional	0.62	5
4	4	D	275	loose positional	0.42	5
1	1	A	1476	tight thermal	0.04	0.5
1	2	B	1476	tight thermal	0.04	0.5
1	3	D	1476	tight thermal	0.04	0.5
1	4	E	1476	tight thermal	0.04	0.5
2	1	B	1408	tight thermal	0.04	0.5
2	2	A	1408	tight thermal	0.04	0.5
2	3	D	1408	tight thermal	0.04	0.5
2	4	E	1408	tight thermal	0.04	0.5
3	1	D	1408	tight thermal	0.04	0.5
3	2	A	1408	tight thermal	0.04	0.5
3	3	B	1408	tight thermal	0.04	0.5
3	4	E	1408	tight thermal	0.04	0.5
4	1	E	1408	tight thermal	0.04	0.5
4	2	A	1408	tight thermal	0.04	0.5
4	3	B	1408	tight thermal	0.04	0.5
4	4	D	1408	tight thermal	0.04	0.5
1	1	A	1356	medium thermal	0.48	2
1	2	B	1356	medium thermal	0.47	2
1	3	D	1356	medium thermal	0.51	2
1	4	E	1356	medium thermal	0.49	2
2	1	B	1284	medium thermal	0.44	2
2	2	A	1284	medium thermal	0.46	2
2	3	D	1284	medium thermal	0.48	2
2	4	E	1284	medium thermal	0.46	2
3	1	D	1284	medium thermal	0.48	2
3	2	A	1284	medium thermal	0.46	2
3	3	B	1284	medium thermal	0.44	2
3	4	E	1284	medium thermal	0.46	2
4	1	E	1284	medium thermal	0.46	2
4	2	A	1284	medium thermal	0.46	2
4	3	B	1284	medium thermal	0.44	2
4	4	D	1284	medium thermal	0.48	2
1	1	A	135	loose thermal	3.27	10
1	2	B	135	loose thermal	2.99	10
1	3	D	135	loose thermal	3.63	10
1	4	E	135	loose thermal	3.1	10
2	1	B	275	loose thermal	2.14	10
2	2	A	275	loose thermal	2.33	10
2	3	D	275	loose thermal	2.58	10
2	4	E	275	loose thermal	2.21	10
3	1	D	275	loose thermal	2.58	10
3	2	A	275	loose thermal	2.33	10
3	3	B	275	loose thermal	2.14	10
3	4	E	275	loose thermal	2.21	10
4	1	E	275	loose thermal	2.21	10
4	2	A	275	loose thermal	2.33	10
4	3	B	275	loose thermal	2.14	10
4	4	D	275	loose thermal	2.58	10

LS refinement shell

Resolution: 2.81→2.88 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.36	136	-
R_work	0.26	2604	-
obs	-	-	96.99 %

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	1.5	-0.8254	-0.532	2.4218	-1.4548	4.3967	0.1365	-0.0246	-0.1067	-0.2703	-0.0575	-0.2597	0.219	0.9204	-0.079	-0.0344	-0.022	0.0445	0.1886	-0.058	0.1655	42.512	3.311	17.369
2	1.062	0.2538	-0.3726	1.2527	1.0034	2.839	0.1339	0.1348	0.1191	-0.1823	-0.076	0.1582	-0.3775	-0.4734	-0.0579	0.1648	0.0794	-0.0071	0.1674	0.0885	0.225	15.853	11.577	10.526
3	3.7623	-1.478	0.0811	1.9746	1.2231	3.5985	0.1954	0.3242	-0.2295	-0.3687	0.1553	-0.1867	-0.0115	0.5924	-0.3507	0.0866	-0.0303	0.0526	0.1485	-0.0453	0.0957	38.027	2.28	-0.699
4	2.1505	1.0181	-0.1208	3.0756	0.9541	2.0162	0.0479	-0.1411	0.2993	-0.3576	-0.1842	0.442	-0.8361	-0.7804	0.1364	0.3212	0.2004	0.0795	0.1952	0.0824	0.3168	9.992	28.628	24.247
5	0.9197	0.2157	-0.6157	1.8176	-0.3777	2.5717	0.0669	-0.0951	0.0544	0.1514	0.1133	-0.0757	-0.219	0.2288	-0.1802	0.109	-0.0157	0.0302	0.1226	-0.0009	0.1963	30.112	10.835	34.624
6	2.6555	-1.2255	0.8832	2.6321	0.0736	2.2221	-0.1409	-0.1634	0.2687	0.4376	0.2648	0.0953	-0.7754	-0.203	-0.1239	0.5521	0.0898	0.1923	0.0025	-0.028	0.1262	17.181	32.805	41.347
7	2.8385	1.0474	-1.928	2.4845	-0.2477	3.1581	0.092	-0.1294	-0.2615	0.6978	0.0491	-0.4356	0.2553	0.2251	-0.1411	0.2343	0.0608	-0.1021	-0.0387	-0.0358	0.1416	10.727	-31.567	51.451
8	0.7093	0.281	0.2717	2.5252	0.1108	1.3164	-0.0756	0.0534	0.0632	0.2351	-0.0658	0.2181	-0.1974	-0.2198	0.1414	0.1488	0.0297	0.0552	0.0775	-0.0312	0.1951	-9.636	-12.277	44.969
9	3.4892	0.1441	-0.7734	2.6645	0.2097	2.6979	-0.0369	-0.224	0.0423	1.2826	-0.0444	-0.2999	0.1813	0.1862	0.0813	0.6177	0.0189	-0.1128	-0.1014	0.0177	0.0302	4.004	-21.202	65.558
10	0.7591	-0.149	0.2604	2.1504	0.6956	1.4341	0.0129	0.1996	0.1163	-0.2792	-0.2795	0.2049	-0.1035	-0.3827	0.2665	-0.0333	0.0715	-0.0081	0.2137	-0.0291	0.2663	-22.483	-20.672	28.419
11	0.873	0.0796	0.0041	1.5707	0.366	1.9693	0.0656	0.2408	-0.0071	0.0127	-0.008	-0.0892	0.0543	0.1383	-0.0576	0.1046	0.0341	0.0327	0.1096	-0.0395	0.1926	4.211	-30.99	29.669
12	3.3723	-0.1509	1.1963	0.0859	0.2794	2.4645	0.2337	0.4198	0.4041	-0.239	-0.2951	0.2317	-0.081	-0.222	0.0615	0.0791	0.0396	0.0183	0.1843	-0.092	0.1944	-18.134	-33.769	15.706

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 52
2	X-RAY DIFFRACTION	2	A	53 - 296
3	X-RAY DIFFRACTION	3	A	297 - 397
4	X-RAY DIFFRACTION	4	B	1 - 52
5	X-RAY DIFFRACTION	5	B	53 - 296
6	X-RAY DIFFRACTION	6	B	297 - 397
7	X-RAY DIFFRACTION	7	D	1 - 52
8	X-RAY DIFFRACTION	8	D	53 - 296
9	X-RAY DIFFRACTION	9	D	297 - 397
10	X-RAY DIFFRACTION	10	E	1 - 52
11	X-RAY DIFFRACTION	11	E	53 - 296
12	X-RAY DIFFRACTION	12	E	297 - 398

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