PDB-4kh0: The R state structure of E. coli ATCase with ATP and Magnesium bound

ID or keywords:

Entry

Database: PDB / ID: 4kh0

Title

The R state structure of E. coli ATCase with ATP and Magnesium bound

Components

Aspartate carbamoyltransferase regulatory chain
Aspartate carbamoyltransferase

Keywords

TRANSFERASE / pyrimidine nucleotide biosynthesis /

feedback inhibition / competing pathway product activation /

allostery

Function / homology

Function and homology information

Aspartate carbamoyltransferase regulatory subunit, N-terminal domain / Aspartate carbamoyltransferase regulatory subunit, C-terminal domain / Aspartate/ornithine carbamoyltransferase / SH3 type barrels. / Roll / Alpha-Beta Plaits /

Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.25 Å

Authors

Cockrell, G.M. / Zheng, Y. / Guo, W. / Peterson, A.W. / Kantrowitz, E.R.

Citation

Journal: Biochemistry / Year: 2013
Title: New Paradigm for Allosteric Regulation of Escherichia coli Aspartate Transcarbamoylase.
Authors: Cockrell, G.M. / Zheng, Y. / Guo, W. / Peterson, A.W. / Truong, J.K. / Kantrowitz, E.R.

History

Deposition	Apr 29, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Nov 27, 2013	Provider: repository / Type: Initial release
Revision 1.1	Nov 15, 2017	Group: Refinement description / Category: software
Revision 1.2	Sep 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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_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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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/kh/4kh0 ftp://data.pdbj.org/pub/pdb/validation_reports/kh/4kh0	HTTPS FTP

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Related structure data

Related structure data	4kgvC 4kgxC 4kgzC 4kh1C 1d09S C: citing same article (ref.) S: Starting model for refinement
Similar structure data	1r0b-d 1d09-1 2ipo-1 1xjw-1 1tth-1 1q95-d 4kgz-1 1f1b-1 8atc-1 3mpu-1 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#215 - Nov 2017 Aspartate Transcarbamoylase similarity (1)

Deposited unit

A: Aspartate carbamoyltransferase

B: Aspartate carbamoyltransferase regulatory chain

C: Aspartate carbamoyltransferase

D: Aspartate carbamoyltransferase regulatory chain

hetero molecules

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

1

A: Aspartate carbamoyltransferase

B: Aspartate carbamoyltransferase regulatory chain

C: Aspartate carbamoyltransferase

D: Aspartate carbamoyltransferase regulatory chain

hetero molecules

A: Aspartate carbamoyltransferase

B: Aspartate carbamoyltransferase regulatory chain

C: Aspartate carbamoyltransferase

D: Aspartate carbamoyltransferase regulatory chain

hetero molecules

A: Aspartate carbamoyltransferase

B: Aspartate carbamoyltransferase regulatory chain

C: Aspartate carbamoyltransferase

D: Aspartate carbamoyltransferase regulatory chain

hetero molecules

defined by author&software
317 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	121.133, 121.133, 155.107
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	150
Space group name H-M	P321

Components on special symmetry positions

ID	Model	Components
1	1	A-567- HOH

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Protein , 2 types, 4 molecules ACBD

#1: Protein	Aspartate carbamoyltransferase / / Aspartate transcarbamylase Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: ATCC 55124 / KO11 / Gene: pyrB, EKO11_4066, KO11_22860 / Production host: Escherichia coli (E. coli) / References: UniProt: E8Y328, aspartate carbamoyltransferase
#2: Protein	Aspartate carbamoyltransferase regulatory chain Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: ATCC 55124 / KO11 / Gene: pyrI, EKO11_4067, KO11_22855 / Production host: Escherichia coli (E. coli) / References: UniProt: E8Y329, aspartate carbamoyltransferase

#1: Protein

Aspartate carbamoyltransferase /

/ Aspartate transcarbamylase

Mass: 34337.105 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Strain: ATCC 55124 / KO11 / Gene: pyrB, EKO11_4066, KO11_22860 / Production host:

Escherichia coli (E. coli) / References: UniProt: E8Y328,

aspartate carbamoyltransferase

#2: Protein

Aspartate carbamoyltransferase regulatory chain

Mass: 17143.625 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Strain: ATCC 55124 / KO11 / Gene: pyrI, EKO11_4067, KO11_22855 / Production host:

Escherichia coli (E. coli) / References: UniProt: E8Y329,

aspartate carbamoyltransferase

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Non-polymers , 5 types, 477 molecules

#3: Chemical	ChemComp-PAL / N-(PHOSPHONACETYL)-L-ASPARTIC ACID Mass: 255.119 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₆H₁₀NO₈P
#4: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#5: Chemical	ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate Mass: 507.181 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₃P₃ / Comment: ATP, energy-carrying molecule*YM
#6: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#7: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 467 / 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: 3.19 Å³/Da / Density % sol: 61.45 %
Crystal grow	Temperature: 293 K / Method: microdialysis / pH: 5.9 Details: 50 mM maleic acid, 1 mM PALA, 3 mM sodium azide, pH 5.9, Microdialysis, temperature 293K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

NSLS

/ Beamline: X29A / Wavelength: 1.075 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 19, 2011

Radiation

Monochromator: Rosenbaum-Rock double crystal sagittal focusing monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.075 Å / Relative weight: 1

Reflection

Resolution: 2.25→50 Å / Num. all: 62983 / Num. obs: 62983 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 24.1 % / R_merge(I) obs: 0.085 / Net I/σ(I): 12

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Diffraction-ID	% possible all
2.25-2.33	22	0.741	1	100
2.33-2.42	22.4	0.537	1	100
2.42-2.53	22.4	0.361	1	100
2.53-2.67	22.4	0.26	1	100
2.67-2.83	22.4	0.184	1	100
2.83-3.05	22.4	0.124	1	100
3.05-3.36	22.3	0.083	1	100
3.36-3.85	22.2	0.058	1	100
3.85-4.85	30.4	0.096	1	100
4.85-50	31.3	0.059	1	100

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHENIX	1.8.1_1168	refinement
PDB_EXTRACT	3.11	data extraction
HKL-2000		data collection
HKL-2000		data reduction
HKL-2000		data scaling
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1D09

1d09

Resolution: 2.25→49.688 Å / Occupancy max: 1 / Occupancy min: 0 / SU ML: 0.23 / σ(F): 0 / Phase error: 22.03 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2077	3195	5.07 %
R_work	0.1682	-	-
obs	0.1702	62973	99.98 %
all	-	62973	-

Solvent computation

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

Displacement parameters

B_iso mean: 48.1575 Å²

Refinement step

Cycle: LAST / Resolution: 2.25→49.688 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7199	0	160	467	7826

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.01	7511
X-RAY DIFFRACTION	f_angle_d	1.136	10229
X-RAY DIFFRACTION	f_dihedral_angle_d	15.857	2810
X-RAY DIFFRACTION	f_chiral_restr	0.072	1174
X-RAY DIFFRACTION	f_plane_restr	0.004	1306

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 (%)
2.25-2.283	0.3058	124	0.2306	2585	X-RAY DIFFRACTION	100
2.283-2.3187	0.2775	151	0.2251	2513	X-RAY DIFFRACTION	100
2.3187-2.3567	0.3035	136	0.213	2594	X-RAY DIFFRACTION	100
2.3567-2.3973	0.2819	132	0.2055	2572	X-RAY DIFFRACTION	100
2.3973-2.4409	0.2469	136	0.1985	2555	X-RAY DIFFRACTION	100
2.4409-2.4879	0.2286	135	0.1798	2574	X-RAY DIFFRACTION	100
2.4879-2.5387	0.2612	148	0.1774	2559	X-RAY DIFFRACTION	100
2.5387-2.5939	0.238	143	0.186	2586	X-RAY DIFFRACTION	100
2.5939-2.6542	0.2452	134	0.1793	2566	X-RAY DIFFRACTION	100
2.6542-2.7206	0.214	136	0.1804	2588	X-RAY DIFFRACTION	100
2.7206-2.7941	0.2562	143	0.1755	2570	X-RAY DIFFRACTION	100
2.7941-2.8763	0.2255	135	0.1874	2593	X-RAY DIFFRACTION	100
2.8763-2.9692	0.2617	140	0.1959	2610	X-RAY DIFFRACTION	100
2.9692-3.0753	0.2645	144	0.193	2553	X-RAY DIFFRACTION	100
3.0753-3.1984	0.2651	141	0.1957	2586	X-RAY DIFFRACTION	100
3.1984-3.3439	0.2318	139	0.192	2624	X-RAY DIFFRACTION	100
3.3439-3.5202	0.2106	129	0.1741	2599	X-RAY DIFFRACTION	100
3.5202-3.7406	0.1952	121	0.159	2616	X-RAY DIFFRACTION	100
3.7406-4.0293	0.1951	166	0.1519	2601	X-RAY DIFFRACTION	100
4.0293-4.4346	0.1632	134	0.1422	2620	X-RAY DIFFRACTION	100
4.4346-5.0757	0.1642	137	0.1362	2649	X-RAY DIFFRACTION	100
5.0757-6.3928	0.2052	155	0.1718	2670	X-RAY DIFFRACTION	100
6.3928-49.7	0.1541	136	0.1542	2795	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	0.0188	0.0028	0.024	-0.001	0.0031	0.0272	0.024	0.1701	0.023	-0.2333	0.0774	0.1587	0.0117	-0.0476	0.2059	0.2538	0.0037	-0.1685	0.346	0.176	0.2115	41.1403	37.6464	1.0247
2	0.223	0.0674	-0.0042	0.0753	-0.0132	0.2504	0.127	0.0835	0.0406	-0.1213	0.0814	0.2144	0.0069	-0.1131	0.5763	0.0757	0.0628	-0.0529	0.0697	0.1396	0.1166	48.9417	42.7732	12.1488
3	0.0133	0.021	0.0054	0.0385	0.002	0.0131	0.0351	0.0117	-0.0861	-0.0461	0.0385	0.1005	0.0647	-0.0225	0.0724	0.1368	-0.0481	-0.2177	0.2237	0.1386	0.4127	30.3719	26.4998	10.4376
4	0.0056	0.0054	0.0079	0.0055	0.0085	0.0129	-0.0012	-0.0021	-0.0076	-0.0398	0.0243	0.0928	0.0227	-0.028	0.007	0.1032	-0.0146	-0.0902	0.2339	0.1621	0.4093	25.769	30.3382	13.6174
5	0.0024	-0.0025	0.0044	0.0459	0.0282	0.0405	-0.0135	-0.003	-0.0082	-0.02	-0.049	0.0937	-0.0037	-0.0591	-0.0211	0.1621	0.0145	0.0002	0.3684	0.2345	0.6433	22.0984	31.4709	21.5471
6	0.0671	-0.0332	0.0364	0.0461	-0.0531	0.0715	0.0249	-0.0469	-0.0952	-0.0013	0.0535	0.1286	0.0446	0.0412	0.0239	0.1067	-0.0291	-0.0159	0.274	0.1581	0.4072	31.7439	23.2992	21.3869
7	0.005	0.0132	-0.0123	0.0335	-0.0345	0.0387	0.0427	-0.0715	-0.1127	0.0884	-0.012	0.0924	-0.0803	0.0383	0.0116	0.2771	-0.1011	-0.0216	0.3333	0.1878	0.5741	31.9618	17.5205	24.3134
8	0.0232	0.0157	0.0188	0.0115	0.01	0.018	0.0165	-0.0092	-0.0698	-0.0091	0.0011	0.035	0.03	0.0004	-0.0054	0.1357	-0.0235	-0.1364	0.1407	0.1372	0.4603	38.0897	15.6771	16.125
9	0.0686	0.0027	-0.0307	0.0634	0.0159	0.0198	0.023	0.0964	-0.0643	-0.0635	0.0003	0.0277	-0.0202	0.0074	0.0879	0.2176	-0.0407	-0.2114	0.2317	0.0336	0.2417	41.6096	31.6618	-0.0091
10	0.0522	-0.0194	0.0269	0.0071	-0.0101	0.0137	0.02	0.0176	0.0225	-0.0018	-0.0023	-0.0083	-0.0204	-0.01	0.0022	0.3188	0.2331	-0.0156	0.4008	-0.0235	0.422	18.6255	81.6858	26.5883
11	0.0119	0.0072	-0.0132	0.0242	0.0202	0.0578	-0.0297	0.0095	-0.0323	-0.0068	-0.0508	0.0142	0.0377	-0.0248	-0.0461	0.4058	0.2777	-0.0051	0.4406	-0.0823	0.3397	20.0791	72.6136	32.344
12	0.0011	-0.0012	-0.0002	0.0012	0.0004	0.0002	0.0045	-0.0067	-0.0138	-0.0156	0.0168	-0.0008	0.0104	-0.0308	-0	0.4715	0.2717	-0.0232	0.5717	-0.138	0.4592	18.3234	65.5817	23.3722
13	0.0334	0.0156	-0.0168	0.0068	-0.0073	0.0079	-0.0287	0.0646	-0.0628	-0.0364	-0.0437	-0.0397	-0.0332	-0.0567	-0.0088	0.4316	0.2666	-0.076	0.4876	-0.06	0.5576	17.7476	71.6904	19.6819
14	0.052	0.016	0.0178	0.0096	0.0045	0.0097	-0.0309	-0.1033	0.0176	0.0179	-0.0266	0.0019	0.0189	-0.0174	-0.0552	0.0581	0.0328	0.0388	0.3132	0.0423	0.4556	29.9762	50.7407	24.7625
15	0.0007	0.0016	0.0023	0.0085	0.0082	0.0063	0.0741	0.0055	0.0956	0.0625	0.0695	0.0337	-0.0283	-0.0564	-0.0001	0.4281	0.035	0.0438	0.327	-0.0757	0.2581	59.5182	60.9752	79.2552
16	0.0069	-0.0011	0.004	0.0068	0.0001	0.0017	0.0226	-0.0203	-0.0238	-0.0035	0.0105	0.0172	0.0174	-0.0112	-0	0.3042	0.0335	0.0297	0.336	0.0241	0.0989	59.7938	45.049	76.9549
17	0.0439	-0.0204	-0.0182	0.0505	0.0102	0.0535	0.0476	-0.0232	0.1488	-0.0597	0.0183	0.0292	-0.2536	-0.0503	0	0.2722	-0.0104	0.0378	0.2317	-0.0017	0.1536	59.005	52.282	67.8078
18	0.0037	0.0048	-0.0005	0.0085	-0.0034	0.0015	0.0243	0.0415	0.1616	-0.0614	0.0386	-0.0259	-0.0706	0.0329	0.0001	0.5842	-0.033	0.045	0.287	0.0323	0.3176	68.3099	68.8601	62.6296
19	0.0032	0.001	-0.0014	0.0087	-0.0028	0.0019	-0.041	0.0213	0.0167	-0.0516	-0.0192	-0.0126	-0.0762	0.0649	-0.0002	0.7913	0.0011	0.1211	0.4757	0.1007	0.6761	71.3065	74.3086	60.123
20	0.017	0.0042	-0.0083	0.0288	0.0137	0.0233	0.0677	0.0446	0.196	-0.0834	0.0561	-0.1799	-0.016	0.0463	0.0002	0.4771	-0.1103	0.1086	0.4205	-0.0158	0.3266	76.8078	60.8771	56.0503
21	0.0244	-0.0122	0.0084	0.0517	-0.0119	0.0052	-0.0239	-0.0585	0.0823	0.0077	-0.0011	-0.1744	-0.0796	-0.0208	-0.0053	0.3534	-0.0372	0.0524	0.3285	-0.0648	0.2174	73.1483	54.5435	71.8563
22	0.0682	-0.0473	-0.0243	0.1119	0.0551	0.1518	-0.1021	-0.0698	-0.0103	0.0956	-0.0937	0.0424	0.009	0.0117	-0.0202	0.5589	0.2942	-0.0259	0.5051	-0.0075	0.3157	24.1415	78.2136	45.1188
23	0.1025	-0.0086	-0.0132	0.1779	-0.0969	0.0536	-0.0484	-0.0704	0.0111	0.079	-0.1197	-0.0979	-0.1832	-0.0314	-0.0859	0.6211	0.1794	-0.1621	0.361	0.0224	0.332	39.1739	72.3432	54.8819

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 1 through 53 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 54 through 134 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 135 through 166 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 167 through 187 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 188 through 215 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 216 through 236 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 237 through 261 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 262 through 284 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 285 through 310 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 10 through 19 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 20 through 67 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 68 through 84 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 85 through 104 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 105 through 153 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 1 through 32 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 33 through 53 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 54 through 166 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 167 through 195 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 196 through 221 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 222 through 261 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 262 through 310 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 10 through 67 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 68 through 153 )

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