PDB-5pzu: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph...

ID or keywords:

Entry

Database: PDB / ID: 5pzu

Title

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid

Components

Fructose-1,6-bisphosphatase 1

Fructose 1,6-bisphosphatase

Keywords

HYDROLASE/HYDROLASE INHIBITOR / D3R docking / HYDROLASE-HYDROLASE INHIBITOR complex

Function / homology

Function and homology information

cellular response to raffinose / sucrose biosynthetic process / cellular hypotonic salinity response / cellular response to phorbol 13-acetate 12-myristate / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / negative regulation of Ras protein signal transduction / fructose 1,6-bisphosphate metabolic process / cellular response to magnesium ion / fructose 6-phosphate metabolic process ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.901 Å

Model details

For D3R project

Authors

Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G. / Yang, H. / Shao, C. / Burley, S.K.

Citation

Journal: To be published
Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.

History

Deposition	Apr 18, 2017	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jan 9, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jan 16, 2019	Group: Data collection / Category: diffrn_radiation / Item: _diffrn_radiation.pdbx_diffrn_protocol
Revision 1.2	Feb 6, 2019	Group: Data collection / Database references / Structure summary Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.3	Feb 10, 2021	Group: Structure summary / Category: audit_author / Item: _audit_author.identifier_ORCID
Revision 1.4	Mar 6, 2024	Group: Advisory / Data collection ...Advisory / Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_unobs_or_zero_occ_atoms / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5pzu.cif.gz	507.4 KB	Display	PDBx/mmCIF format
PDB format	pdb5pzu.ent.gz	417.8 KB	Display	PDB format
PDBx/mmJSON format	5pzu.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/pz/5pzu ftp://data.pdbj.org/pub/pdb/validation_reports/pz/5pzu	HTTPS FTP

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Group deposition

ID	G_1002030 (23 entries) 5pzq 5pzr 5pzs 5pzt 5pzu 5pzv 5pzw 5pzx 5pzy 5pzz
Title	Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with allosteric inhibitors
Type	undefined
Description	Fructose-1,6-bisphosphatase 1 with inhibitors

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Related structure data

Similar structure data	5pzw-d 5pzx-2 2wbb-1 5q07-1 5pzz-1 5q04-2 5q0b-d 5q00-1 2vt5-1 5q02-d 6lw2-d 1fta-d 4mjo-2 5pzy-2 5q05-2 2y5l-1 4mjo-1 1fpe-1 3kbz-d 5pzv-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

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (1)

Deposited unit

A: Fructose-1,6-bisphosphatase 1

B: Fructose-1,6-bisphosphatase 1

C: Fructose-1,6-bisphosphatase 1

D: Fructose-1,6-bisphosphatase 1

hetero molecules

149 kDa, 4 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)	67.657, 83.267, 277.759
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	(chain A and (resid 9 through 61 or resid 72...
2	1	(chain B and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))
3	1	(chain C and (resid 9 through 61 or resid 72...
4	1	(chain D and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))

NCS domain segments:

Ens-ID: 1

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	ASP	ASP	GLY	GLY	(chain A and (resid 9 through 61 or resid 72...	A	A	9 - 61	10 - 62
1	2	LYS	LYS	TYR	TYR	(chain A and (resid 9 through 61 or resid 72...	A	A	72 - 139	73 - 140
1	3	LYS	LYS	GLY	GLY	(chain A and (resid 9 through 61 or resid 72...	A	A	141 - 156	142 - 157
1	4	ASN	ASN	SER	SER	(chain A and (resid 9 through 61 or resid 72...	A	A	158 - 335	159 - 336
2	1	ASP	ASP	TYR	TYR	(chain B and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	B	B	9 - 139	10 - 140
2	2	LYS	LYS	GLY	GLY	(chain B and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	B	B	141 - 156	142 - 157
2	3	ASN	ASN	SER	SER	(chain B and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	B	B	158 - 335	159 - 336
3	1	ASP	ASP	GLY	GLY	(chain C and (resid 9 through 61 or resid 72...	C	C	9 - 61	10 - 62
3	2	LYS	LYS	TYR	TYR	(chain C and (resid 9 through 61 or resid 72...	C	C	72 - 139	73 - 140
3	3	LYS	LYS	GLY	GLY	(chain C and (resid 9 through 61 or resid 72...	C	C	141 - 156	142 - 157
3	4	ASN	ASN	SER	SER	(chain C and (resid 9 through 61 or resid 72...	C	C	158 - 335	159 - 336
4	1	ASP	ASP	TYR	TYR	(chain D and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	D	D	9 - 139	10 - 140
4	2	LYS	LYS	GLY	GLY	(chain D and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	D	D	141 - 156	142 - 157
4	3	ASN	ASN	SER	SER	(chain D and (resid 9 through 139 or resid 141 through 156 or resid 158 through 335))	D	D	158 - 335	159 - 336

#1: Protein	Fructose-1,6-bisphosphatase 1 / Fructose 1,6-bisphosphatase / Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6- ...Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6-bisphosphatase 1 (FBP1) / mRNA Mass: 36859.418 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FBP1, hCG_1640493 / Production host: Escherichia coli (E. coli) References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
#2: Chemical	ChemComp-94D / {5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl}phosphonic acid Mass: 302.287 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₁H₁₅N₂O₄PS
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 1386 / 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: 2.74 Å³/Da / Density % sol: 55.12 %
Crystal grow	Temperature: 300 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1M HEPES pH 7.0, 0.1M AMMONIUM ACETATE, 12% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.987 Å
Detector	Type: MAR CCD 165 mm / Detector: CCD / Date: Mar 17, 2006
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.987 Å / Relative weight: 1
Reflection	Resolution: 1.901→28.961 Å / Num. obs: 123340 / % possible obs: 99.23 %

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification	NB
PHENIX	1.11.1_2575	refinement
PDB_EXTRACT	3.23	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.901→28.961 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 21.97 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2344	6225	5.05 %
R_work	0.1881	117115	-
obs	0.1904	123340	99.23 %

Solvent computation

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

Displacement parameters

B_iso max: 94.7 Å² / B_iso mean: 23.6265 Å² / B_iso min: 4.65 Å²

Refinement step

Cycle: final / Resolution: 1.901→28.961 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9729	0	76	1386	11191
B_iso mean	-	-	19	36.97	-
Num. residues	-	-	-	-	1271

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	10077
X-RAY DIFFRACTION	f_angle_d	0.948	13628
X-RAY DIFFRACTION	f_chiral_restr	0.057	1536
X-RAY DIFFRACTION	f_plane_restr	0.006	1743
X-RAY DIFFRACTION	f_dihedral_angle_d	11.953	6138

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	5998	X-RAY DIFFRACTION	9.598	TORSIONAL
1	2	B	5998	X-RAY DIFFRACTION	9.598	TORSIONAL
1	3	C	5998	X-RAY DIFFRACTION	9.598	TORSIONAL
1	4	D	5998	X-RAY DIFFRACTION	9.598	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.9012-1.9228	0.3622	165	0.3337	3100	3265	80
1.9228-1.9454	0.3172	210	0.2925	3869	4079	99
1.9454-1.9692	0.3298	199	0.2701	3832	4031	100
1.9692-1.9941	0.3214	207	0.2552	3923	4130	100
1.9941-2.0203	0.3235	224	0.254	3863	4087	100
2.0203-2.048	0.3082	213	0.2464	3873	4086	100
2.048-2.0772	0.3054	204	0.236	3883	4087	100
2.0772-2.1082	0.2898	219	0.229	3903	4122	100
2.1082-2.1412	0.2755	217	0.2161	3884	4101	100
2.1412-2.1763	0.2801	185	0.2198	3926	4111	100
2.1763-2.2138	0.2597	202	0.2154	3852	4054	100
2.2138-2.254	0.2927	198	0.232	3956	4154	100
2.254-2.2973	0.2659	198	0.2006	3871	4069	100
2.2973-2.3442	0.2337	194	0.1923	3945	4139	100
2.3442-2.3952	0.2342	219	0.1832	3877	4096	100
2.3952-2.4509	0.2344	191	0.1856	3938	4129	100
2.4509-2.5121	0.2591	221	0.1833	3902	4123	100
2.5121-2.58	0.2455	209	0.1847	3905	4114	100
2.58-2.6559	0.2479	203	0.1826	3911	4114	100
2.6559-2.7415	0.2388	221	0.179	3941	4162	100
2.7415-2.8394	0.2547	210	0.1711	3920	4130	100
2.8394-2.953	0.2299	203	0.1721	3938	4141	100
2.953-3.0873	0.2235	223	0.1664	3962	4185	100
3.0873-3.2498	0.1976	217	0.1571	3929	4146	100
3.2498-3.4531	0.1901	204	0.1587	3968	4172	100
3.4531-3.7192	0.2075	210	0.1581	3950	4160	100
3.7192-4.0926	0.1922	221	0.1596	3975	4196	100
4.0926-4.6826	0.1634	226	0.1443	4000	4226	100
4.6826-5.8915	0.1869	195	0.1607	4065	4260	100
5.8915-28.9646	0.2286	217	0.2038	4254	4471	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	0.0215	-0.0011	-0.0035	0.0043	0.0023	0.0139	0.0028	0.0363	-0.0069	0.0058	-0.0069	-0.0072	-0.0765	-0.0281	-0.0163	0.0887	-0.0048	0.0092	0.066	0.0008	0.0532	16.1201	42.4295	17.4257
2	0.0028	-0.0004	0.0054	-0.0007	0.0002	0.0041	0.0073	0.0278	-0.0374	-0.002	0.0218	-0.0353	-0.0281	0.0199	0	0.0863	-0.026	0.014	0.1395	-0.0005	0.1122	19.5052	39.922	10.4006
3	0.0077	0.0095	-0.009	0.017	-0.0024	0.0118	-0.0085	0.0432	0.0246	-0.0368	0.0224	-0.0118	-0.077	-0.0057	-0.0064	0.1182	-0.0244	0.0149	0.0933	0.011	0.0757	27.6642	48.4115	13.9968
4	0.0142	0.0025	0.0067	0.0001	0.0007	0.0032	-0.0045	0.0205	0.0185	-0.0097	-0.0127	-0.0178	-0.0047	-0.0035	-0.0144	0.0901	-0.068	0.0492	0.2168	0.0188	0.1582	49.9317	36.9011	2.9255
5	0.0159	0.0034	0.0046	0.0602	0.0094	0.0101	0.0224	0.0406	-0.0039	-0.0474	-0.0008	-0.0431	-0.0473	0.0302	0.0257	0.094	-0.0933	0.0594	0.1454	0.0083	0.0315	36.8844	45.5579	2.7022
6	0.0017	-0	-0.0032	0.0005	0.0014	0.0078	-0.02	0.0091	-0.0029	-0.0074	0.0011	-0.0037	0.0079	-0.0014	-0.001	0.0641	-0.0045	-0.0054	0.0582	-0.0223	0.1422	26.0646	5.1408	32.8162
7	0.0079	-0.0026	0.0073	0.0029	0.0049	0.0089	-0.0003	-0.0353	-0.0263	-0.008	0.0142	-0.0107	-0.0293	0.0227	-0.0035	0.0491	0.0034	-0.0099	0.0719	-0.0226	0.0667	34.2897	26.6888	37.3328
8	0.0012	-0.0007	0.0007	0.0012	-0.0005	0.0009	0.0159	-0.0045	0.0195	-0.0022	0.0107	-0.0131	-0.0118	-0.0087	0	0.0973	-0.0296	-0.0318	0.1451	-0.0054	0.1406	47.8092	18.4597	40.8708
9	0.0044	0.0042	0.0068	0.0071	0.0146	0.0299	0.0338	0.0008	0.0042	-0.0154	0.0318	-0.0118	-0.0244	0.0204	0.0027	0.0839	0.0146	0.0151	0.1468	-0.0272	0.1604	42.3193	22.5588	33.5127
10	0.0054	0.0045	-0.0098	0.0183	0.0078	0.0281	0.0302	-0.0104	-0.0075	0.0089	0.0018	-0.0187	-0.0147	-0.0107	0.0272	0.0493	0.0069	-0.0094	0.1192	-0.0258	0.0899	45.3734	11.7275	32.1601
11	0.0216	-0.011	-0.0104	0.0162	0.0078	0.0092	-0.0026	0.0333	-0.0162	0.0207	0.035	-0.0085	0.0194	0.0344	0.0282	0.0489	0.0104	0.011	0.0621	-0.0509	0.0882	31.6977	15.8392	19.6486
12	0.0383	-0.0054	0.0133	0.0164	0.0089	0.0139	0.0185	0.0804	-0.0182	-0.0216	0	-0.0249	-0.0073	0.062	-0.0071	-0.0075	0.0153	0.0541	0.1466	-0.0733	0.0015	47.6826	21.3687	11.6114
13	0.0037	-0.0147	0.0007	0.0558	0.0021	0.0269	-0.0249	0.0227	-0.0189	-0.0238	-0.0289	-0.0021	0.0069	-0.011	-0.0446	0.054	0.0401	0.0392	0.1753	-0.0857	0.1133	52.8974	13.056	14.3192
14	0.0026	-0.0044	0.001	0.0077	0.007	0.0038	0.0063	0.0225	0.0196	-0.0647	0.0334	0.013	-0.0614	0.0008	0	0.1113	0.01	0.0162	0.0611	-0.0035	0.0847	16.4267	46.7087	37.2598
15	0.0371	-0.0059	-0.0046	0.0224	-0.0024	0.0041	-0.022	-0.0243	0.0046	0.0194	0.0148	-0.0072	-0.0019	0.0133	-0.0121	0.1645	0.006	0.0248	0.0626	-0.0032	0.072	15.7027	52.7288	48.3303
16	0.0044	-0.0034	-0.0025	0.0059	0.0019	0.0029	0.0088	-0.009	0.0094	-0.0002	0.0082	-0.0076	0.0007	0.0139	0.0024	0.1237	0.0244	0.0458	0.0457	-0.0093	0.0589	9.9971	61.4092	45.3307
17	0.0228	-0.0126	0.0144	0.0274	-0.0022	0.0205	0.0376	0.0005	0.0312	-0.0046	-0.0056	0.0406	-0.0618	-0.0466	0	0.0847	0.0092	0.0186	0.0749	0.0023	0.0908	-3.4864	42.9756	46.9058
18	0.0038	0.0026	-0.004	0.0169	0.0028	0.0016	0.0217	-0.0321	0.0534	0.0323	0.0063	0.0149	-0.0279	-0.0318	0.0156	0.0893	0.0228	0.0114	0.0752	-0.0015	0.0772	-4.7888	48.9388	53.4585
19	0.0102	0.0033	-0.0205	0.013	0.0018	0.0236	0.0009	0.0581	-0.0594	-0.0625	-0.0103	-0.0243	-0.0003	0.0272	0	0.0663	-0.0035	0.0082	0.0689	0.0024	0.0988	12.904	13.9533	36.7456
20	0.0046	0.0041	0.0007	0.0028	-0.0022	0.0073	0.0063	0.0181	-0.0156	0.0028	0.0119	0.0193	0.0156	-0.0225	0	0.0993	-0.001	0.0182	0.0513	-0.0031	0.1159	5.9531	9.0665	41.1458
21	0.0041	-0.0015	-0.0059	0.0003	0.0005	0.0065	0.0197	-0.002	-0.0529	0.0034	-0.0186	-0.0086	0.0415	-0.0028	0	0.0716	0.0014	0.0102	0.0696	0.0149	0.0909	12.2985	16.9968	51.5996
22	0.009	0.0064	0.0018	0.0173	0.0006	0.0164	0.0267	-0.0081	-0.0057	0.0056	-0.0231	-0.0139	0.0133	-0.047	-0.0048	0.0793	-0.0017	0.0121	0.0853	0.0038	0.072	-2.646	21.7746	59.4438
23	0.0039	-0.0033	0.0008	0.0095	-0.0021	0.0037	-0.002	-0.0355	-0.0185	0.0249	-0.0166	0.0306	-0.0145	0.0032	-0.0083	0.1097	-0.0114	0.0072	0.0647	0.0158	0.0748	-2.9892	11.9507	61.6818

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 9 through 106 )	A	9 - 106
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 107 through 131 )	A	107 - 131
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 132 through 212 )	A	132 - 212
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 213 through 247 )	A	213 - 247
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 248 through 335 )	A	248 - 335
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 9 through 28 )	B	9 - 28
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 29 through 88 )	B	29 - 88
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 89 through 106 )	B	89 - 106
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 107 through 131 )	B	107 - 131
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 132 through 170 )	B	132 - 170
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 171 through 212 )	B	171 - 212
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 213 through 291 )	B	213 - 291
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 292 through 335 )	B	292 - 335
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 9 through 88 )	C	9 - 88
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 89 through 131 )	C	89 - 131
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 132 through 148 )	C	132 - 148
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 149 through 247 )	C	149 - 247
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 248 through 335 )	C	248 - 335
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 9 through 106 )	D	9 - 106
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 107 through 148 )	D	107 - 148
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 149 through 212 )	D	149 - 212
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 213 through 291 )	D	213 - 291
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 292 through 335 )	D	292 - 335

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