PDB-4h2h: Crystal structure of an enolase (mandalate racemase subgroup, tar...

ID or keywords:

Entry

Database: PDB / ID: 4h2h

Title

Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)

Components

Mandelate racemase/muconate lactonizing enzyme

Keywords

ISOMERASE / Enolase / mandelate racemase subgroup / enzyme function initiative / EFI / Structural Genomics

Function / homology

Function and homology information

4-hydroxyproline betaine 2-epimerase / amino-acid betaine catabolic process / amino-acid racemase activity / racemase and epimerase activity, acting on amino acids and derivatives / magnesium ion binding
Similarity search - Function

Biological species

Pelagibaca bermudensis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.7 Å

Authors

Vetting, M.W. / Morisco, L.L. / Wasserman, S.R. / Sojitra, S. / Imker, H.J. / Gerlt, J.A. / Almo, S.C. / Enzyme Function Initiative (EFI)

Citation

Journal: Nature / Year: 2013
Title: Discovery of new enzymes and metabolic pathways by using structure and genome context.
Authors: Zhao, S. / Kumar, R. / Sakai, A. / Vetting, M.W. / Wood, B.M. / Brown, S. / Bonanno, J.B. / Hillerich, B.S. / Seidel, R.D. / Babbitt, P.C. / Almo, S.C. / Sweedler, J.V. / Gerlt, J.A. / ...

History

Deposition	Sep 12, 2012	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Oct 10, 2012	Provider: repository / Type: Initial release
Revision 1.1	Sep 18, 2013	Group: Database references
Revision 1.2	Nov 6, 2013	Group: Database references
Revision 1.3	Sep 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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_asym_id / _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_asym_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_ref_seq_dif.details / _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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Download

PDBx/mmCIF format	4h2h.cif.gz	1.1 MB	Display	PDBx/mmCIF format
PDB format	pdb4h2h.ent.gz	941.7 KB	Display	PDB format
PDBx/mmJSON format	4h2h.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	4h2h_validation.pdf.gz	547.8 KB	Display	wwPDB validaton report
Full document	4h2h_full_validation.pdf.gz	577.9 KB	Display
Data in XML	4h2h_validation.xml.gz	124.4 KB	Display
Data in CIF	4h2h_validation.cif.gz	179 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/h2/4h2h ftp://data.pdbj.org/pub/pdb/validation_reports/h2/4h2h	HTTPS FTP

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Related structure data

Related structure data	2pmqSC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	2pmq-1 4izg-1 4j1o-1 4e8g-1 3fv9-d 3cyj-1 4dwd-1 3fvd-1 3eez-1 2pce-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
Other databases	TargetTrack: EFI-502101

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (2)

Deposited unit

A: Mandelate racemase/muconate lactonizing enzyme

B: Mandelate racemase/muconate lactonizing enzyme

C: Mandelate racemase/muconate lactonizing enzyme

D: Mandelate racemase/muconate lactonizing enzyme

E: Mandelate racemase/muconate lactonizing enzyme

F: Mandelate racemase/muconate lactonizing enzyme

G: Mandelate racemase/muconate lactonizing enzyme

H: Mandelate racemase/muconate lactonizing enzyme

hetero molecules

335 kDa, 8 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)	91.035, 152.824, 113.027
Angle α, β, γ (deg.)	90.00, 105.20, 90.00
Int Tables number	4
Space group name H-M	P12₁1

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein	Mandelate racemase/muconate lactonizing enzyme Mass: 40701.141 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pelagibaca bermudensis (bacteria) / Strain: HTCC2601 / Gene: R2601_01638 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q0FPQ4

#1: Protein

Mandelate racemase/muconate lactonizing enzyme

Mass: 40701.141 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Pelagibaca bermudensis (bacteria) / Strain: HTCC2601 / Gene: R2601_01638 / Plasmid: pET / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q0FPQ4

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Non-polymers , 6 types, 2148 molecules

#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-NI / NICKEL (II) ION Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#4: Chemical	ChemComp-0XW / (2S,4R)-4-hydroxy-1,1-dimethylpyrrolidinium-2-carboxylate / Betonicine / L-4-Hydroxyproline betaine Mass: 159.183 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₇H₁₃NO₃
#5: Chemical	... ChemComp-IOD / IODIDE ION Mass: 126.904 Da / Num. of mol.: 61 / Source method: obtained synthetically / Formula: I
#6: Chemical	ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL Mass: 118.174 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₆H₁₄O₂ / Comment: precipitant*YM
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 2066 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.33 Å³/Da / Density % sol: 47.21 %
Crystal grow	Temperature: 298 K / pH: 7.5 Details: Protein (15 mM Hepes pH 8.0, 150 mM NaCl, 10% glycerol, 50 mM MgCl2, 5 mM EDTA, 2 mM NiCl2; Reservoir (0.1 M HEPES:NaOH pH 7.5 70% (v/v) MPD); Soak 2 minutes in (Reservoir + 50 mM MgCl2, 200 ...Details: Protein (15 mM Hepes pH 8.0, 150 mM NaCl, 10% glycerol, 50 mM MgCl2, 5 mM EDTA, 2 mM NiCl2; Reservoir (0.1 M HEPES:NaOH pH 7.5 70% (v/v) MPD); Soak 2 minutes in (Reservoir + 50 mM MgCl2, 200 mM 4-OH Proline Betaine ) Cryoprotection (Soaking solution), sitting drop vapor diffuction, temperature 298K

Crystal

Density Matthews: 2.33 Å³/Da / Density % sol: 47.21 %

Crystal grow

Temperature: 298 K / pH: 7.5
Details: Protein (15 mM Hepes pH 8.0, 150 mM NaCl, 10% glycerol, 50 mM MgCl2, 5 mM EDTA, 2 mM NiCl2; Reservoir (0.1 M HEPES:NaOH pH 7.5 70% (v/v) MPD); Soak 2 minutes in (Reservoir + 50 mM MgCl2, 200 ...

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 31-ID / Wavelength: 0.9793
Detector	Type: RAYONIX MX225HE / Detector: CCD / Date: Apr 14, 2012 / Details: MIRRORS
Radiation	Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9793 Å / Relative weight: 1
Reflection	Resolution: 1.7→109.072 Å / Num. obs: 325934 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / R_sym value: 0.085 / Net I/σ(I): 8.9
Reflection shell	Resolution: 1.7→1.79 Å / Redundancy: 3.6 % / R_merge(I) obs: 0.577 / Mean I/σ(I) obs: 1.3 / R_sym value: 0.577 / % possible all: 99.9

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Processing

Software

Name	Version	Classification
SCALA	3.3.16	data scaling
PHENIX	1.8_1069	refinement
PDB_EXTRACT	3.11	data extraction
MOSFLM		data reduction
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2PMQ

2pmq

Resolution: 1.7→25.68 Å / Occupancy max: 1 / Occupancy min: 0.11 / SU ML: 0.17 / σ(F): 0 / Phase error: 19 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.192	16434	5.04 %
R_work	0.159	-	-
obs	0.16	325787	99.9 %
all	-	325787	-

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso mean: 23.53 Å²

Refinement step

Cycle: LAST / Resolution: 1.7→25.68 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	22160	0	183	2066	24409

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.011	23114
X-RAY DIFFRACTION	f_angle_d	1.109	31597
X-RAY DIFFRACTION	f_dihedral_angle_d	12.802	8323
X-RAY DIFFRACTION	f_chiral_restr	0.074	3501
X-RAY DIFFRACTION	f_plane_restr	0.006	4139

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 (%)
1.7-1.7193	0.2683	522	0.2359	10371	X-RAY DIFFRACTION	100
1.7193-1.7395	0.269	568	0.2362	10272	X-RAY DIFFRACTION	100
1.7395-1.7607	0.2591	535	0.2263	10326	X-RAY DIFFRACTION	100
1.7607-1.783	0.2583	559	0.2272	10190	X-RAY DIFFRACTION	100
1.783-1.8065	0.2581	573	0.221	10257	X-RAY DIFFRACTION	100
1.8065-1.8312	0.2387	558	0.2059	10341	X-RAY DIFFRACTION	100
1.8312-1.8574	0.2394	562	0.1958	10284	X-RAY DIFFRACTION	100
1.8574-1.8851	0.2186	541	0.1848	10284	X-RAY DIFFRACTION	100
1.8851-1.9145	0.2103	540	0.1737	10309	X-RAY DIFFRACTION	100
1.9145-1.9459	0.2186	555	0.1785	10285	X-RAY DIFFRACTION	100
1.9459-1.9795	0.2218	528	0.1758	10380	X-RAY DIFFRACTION	100
1.9795-2.0154	0.2127	564	0.1691	10250	X-RAY DIFFRACTION	100
2.0154-2.0542	0.2054	532	0.1608	10289	X-RAY DIFFRACTION	100
2.0542-2.0961	0.1886	529	0.1502	10303	X-RAY DIFFRACTION	100
2.0961-2.1417	0.1995	511	0.154	10363	X-RAY DIFFRACTION	100
2.1417-2.1915	0.195	546	0.153	10272	X-RAY DIFFRACTION	100
2.1915-2.2462	0.1983	569	0.1565	10313	X-RAY DIFFRACTION	100
2.2462-2.3069	0.193	544	0.1488	10304	X-RAY DIFFRACTION	100
2.3069-2.3748	0.1867	526	0.1527	10359	X-RAY DIFFRACTION	100
2.3748-2.4514	0.1887	530	0.1568	10325	X-RAY DIFFRACTION	100
2.4514-2.5389	0.1934	545	0.159	10338	X-RAY DIFFRACTION	100
2.5389-2.6404	0.1904	582	0.1551	10264	X-RAY DIFFRACTION	100
2.6404-2.7605	0.1961	539	0.165	10372	X-RAY DIFFRACTION	100
2.7605-2.9058	0.191	563	0.1603	10300	X-RAY DIFFRACTION	100
2.9058-3.0876	0.2033	562	0.1576	10309	X-RAY DIFFRACTION	100
3.0876-3.3256	0.1648	578	0.1423	10310	X-RAY DIFFRACTION	100
3.3256-3.6594	0.1707	528	0.1378	10393	X-RAY DIFFRACTION	100
3.6594-4.1869	0.1476	535	0.1257	10373	X-RAY DIFFRACTION	100
4.1869-5.2676	0.1616	521	0.1347	10408	X-RAY DIFFRACTION	100
5.2676-25.6847	0.1974	589	0.1737	10209	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	1.3604	0.315	-1.1171	1.6159	-0.471	0.9644	-0.1475	-0.0244	-0.1777	-0.0104	-0.0064	-0.0445	0.1568	0.0454	0.1067	0.1264	0.0015	0.0352	0.0879	-0.0156	0.1303	25.8192	-38.8171	16.2366
2	0.7137	-0.3124	-0.6032	0.402	0.4847	0.7656	-0.2398	-0.3751	-0.0462	0.2449	0.1912	-0.1833	0.384	0.4386	0.006	0.1706	0.1103	-0.0442	0.2774	0.0058	0.191	41.7471	-21.312	36.4527
3	0.6564	0.0084	-0.2724	0.8349	0.2506	0.6158	-0.0746	-0.0077	-0.1066	-0.0029	0.0074	-0.0658	0.13	0.0589	0.0443	0.0968	0.0124	0.0171	0.0839	0.0065	0.1123	32.5226	-26.7415	20.7017
4	1.538	-0.3271	-1.0073	1.6586	0.3289	0.8344	-0.1354	0.0733	-0.1798	-0.0043	0.0083	0.0095	0.1417	-0.0871	0.0871	0.1225	-0.0088	0.0288	0.1001	0.0097	0.1169	4.8534	-39.3548	37.3671
5	0.7138	0.251	-0.5965	0.4902	-0.5854	0.9039	-0.2708	0.3279	-0.0914	-0.3286	0.2615	0.2124	0.4654	-0.4524	-0.0542	0.1635	-0.1293	-0.0535	0.3081	0.0087	0.1961	-11.2109	-21.3977	17.5201
6	0.6577	-0.0316	-0.2211	0.8585	-0.3427	0.6106	-0.0668	0.0141	-0.0951	0.0075	0.0307	0.0542	0.0993	-0.0938	0.0339	0.0856	-0.0184	0.0132	0.1101	-0.0078	0.0971	-2.2448	-26.8181	33.0374
7	0.7138	0.5455	-0.5428	1.8594	0.6796	1.437	0.0194	0.0501	0.0296	-0.1648	0.0623	-0.3053	-0.0874	0.0004	-0.0375	0.1534	-0.0321	0.0323	0.1207	0.0404	0.1883	37.2198	14.9181	-4.8728
8	0.5776	0.1811	-0.3038	1.2118	-0.1741	0.5481	-0.0032	-0.0744	0.0443	-0.0488	-0.04	-0.1899	-0.0048	0.2007	0.0257	0.0741	-0.0149	-0.0156	0.1658	0.0065	0.1553	46.27	3.583	21.9966
9	0.4274	0.2229	-0.2684	0.6123	-0.0657	1.0373	0.0083	0.0141	0.101	-0.1298	0.0434	-0.1721	-0.1187	0.0708	-0.0398	0.142	-0.035	0.0332	0.1056	0.017	0.1891	39.442	16.6677	7.1621
10	0.9006	0.6926	-0.3935	2.1008	0.0956	1.4128	-0.0329	0.1382	0.0499	-0.3122	-0.0072	0.0189	-0.008	-0.061	0.0204	0.1466	-0.0131	0.011	0.1244	-0.0119	0.0804	29.8637	-13.5127	-9.3962
11	0.2503	-0.0947	-0.1541	1.2073	0.5003	0.2529	0.1774	0.3627	0.087	-0.616	-0.1832	0.1255	-0.2381	-0.3731	0.0549	0.2089	0.0612	-0.1404	0.4084	-0.041	0.0813	0.7643	-3.6641	-4.685
12	0.5782	-0.1701	-0.2687	0.7849	0.2561	0.6415	0.0143	0.1446	-0.0312	-0.1951	-0.0225	0.0293	0.0208	-0.1107	0.0159	0.1442	-0.0216	-0.0173	0.1501	-0.0089	0.0889	16.8635	-13.0353	-2.4466
13	0.9271	-0.8008	-0.3162	1.7685	0.258	1.0918	-0.0829	-0.0919	0.017	0.333	0.0478	0.0358	0.0613	-0.0636	0.0251	0.182	0.0327	0.0139	0.1237	0.0157	0.0795	-1.6157	-16.6403	63.1647
14	0.1709	0.1438	-0.095	0.8264	-0.4085	0.3863	0.0646	-0.1979	-0.0296	0.4672	-0.1186	-0.2212	-0.1189	0.2626	0.0195	0.2589	-0.0111	-0.1079	0.2877	0.0032	0.1631	29.7166	-4.5025	59.1569
15	0.5017	0.2731	-0.3151	0.7682	-0.2416	0.5309	-0.0039	-0.1205	-0.0074	0.2185	0.0194	-0.0506	0.0201	0.0772	-0.0082	0.1815	0.0417	-0.0341	0.1522	-0.0005	0.0997	13.3284	-14.232	57.0522
16	0.9016	-0.5977	-0.5866	2.189	-0.6533	1.4089	-0.0359	-0.0519	-0.0347	0.1348	0.067	0.2811	0.004	-0.0446	-0.0149	0.1537	0.0425	0.005	0.127	-0.0377	0.1518	-6.9041	13.6463	60.304
17	0.4521	-0.2983	-0.1596	1.4035	0.1464	0.5669	-0.0219	0.0249	0.0189	0.0759	-0.023	0.1857	0.0104	-0.1863	0.0325	0.0763	0.0158	-0.0128	0.1776	-0.0136	0.1427	-15.8748	3.1379	33.0452
18	0.4155	-0.2529	-0.169	0.7276	0.0751	1.0607	-0.023	-0.0215	0.0679	0.1384	0.0387	0.1238	-0.0761	-0.0798	-0.0205	0.1322	0.041	0.0116	0.121	-0.0228	0.1656	-9.0483	15.7787	48.2914
19	0.1268	-0.1209	-0.1825	0.772	0.2564	1.2611	0.2673	0.0278	0.3852	-0.0643	-0.0209	-0.0158	-0.485	-0.149	-0.0895	0.3648	0.0687	0.1377	0.1199	0.1116	0.3181	17.9746	39.4453	13.6029
20	0.5183	0.1468	-0.5148	0.5826	0.0312	0.4946	0.1248	0.2952	0.1935	-0.0872	-0.0074	0.091	-0.1901	-0.2204	-0.0429	0.1574	0.0781	-0.0132	0.2267	0.072	0.1678	2.4482	21.0828	12.7064
21	0.129	0.0001	-0.0903	0.0049	-0.0121	0.1113	0.2538	0.3998	0.519	-0.1503	0.0394	0.1832	-0.5942	-0.3529	0.09	0.4582	0.3055	0.0669	0.123	0.3812	0.2496	10.5111	39.385	3.2941
22	0.3792	-0.0482	-0.1741	0.975	-0.1321	1.6166	0.1353	-0.0621	0.308	0.0137	0.0152	-0.105	-0.4022	0.0964	-0.1156	0.2846	-0.0156	0.059	0.1277	-0.0549	0.2592	12.3001	38.8772	42.748
23	0.6633	-0.3178	-0.3413	0.6183	0.1045	0.709	0.0801	-0.2218	0.2267	0.0759	0.0281	-0.1401	-0.2099	0.1591	-0.0388	0.1765	-0.0617	-0.0239	0.1834	-0.0784	0.1921	25.8793	24.9206	45.3538

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resseq 2:129)
2	X-RAY DIFFRACTION	2	chain 'A' and (resseq 130:209)
3	X-RAY DIFFRACTION	3	chain 'A' and (resseq 210:367)
4	X-RAY DIFFRACTION	4	chain 'B' and (resseq 2:129)
5	X-RAY DIFFRACTION	5	chain 'B' and (resseq 130:208)
6	X-RAY DIFFRACTION	6	chain 'B' and (resseq 209:367)
7	X-RAY DIFFRACTION	7	chain 'C' and (resseq 2:129)
8	X-RAY DIFFRACTION	8	chain 'C' and (resseq 130:233)
9	X-RAY DIFFRACTION	9	chain 'C' and (resseq 234:367)
10	X-RAY DIFFRACTION	10	chain 'D' and (resseq 2:129)
11	X-RAY DIFFRACTION	11	chain 'D' and (resseq 130:209)
12	X-RAY DIFFRACTION	12	chain 'D' and (resseq 210:367)
13	X-RAY DIFFRACTION	13	chain 'E' and (resseq 2:129)
14	X-RAY DIFFRACTION	14	chain 'E' and (resseq 130:210)
15	X-RAY DIFFRACTION	15	chain 'E' and (resseq 211:367)
16	X-RAY DIFFRACTION	16	chain 'F' and (resseq 2:129)
17	X-RAY DIFFRACTION	17	chain 'F' and (resseq 130:233)
18	X-RAY DIFFRACTION	18	chain 'F' and (resseq 234:367)
19	X-RAY DIFFRACTION	19	chain 'G' and (resseq 2:129)
20	X-RAY DIFFRACTION	20	chain 'G' and (resseq 130:310)
21	X-RAY DIFFRACTION	21	chain 'G' and (resseq 311:367)
22	X-RAY DIFFRACTION	22	chain 'H' and (resseq 2:129)
23	X-RAY DIFFRACTION	23	chain 'H' and (resseq 130:367)

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