PDB-2v67: Crystal structure of Chlamydomonas reinhardtii Rubisco with a lar...

ID or keywords:

Entry

Database: PDB / ID: 2v67

Title

Crystal structure of Chlamydomonas reinhardtii Rubisco with a large- subunit supressor mutation T342I

Components

(RIBULOSE BISPHOSPHATE CARBOXYLASE ...) x 2

Keywords

OXIDOREDUCTASE / LARGE SUBUNIT LOOP 6 MUTATION / CO2/O2 SPECIFICITY / CARBON DIOXIDE FIXATION / PHOTOSYNTHESIS / TRANSIT PEPTIDE / PHOTORESPIRATION / METAL-BINDING / HYDROXYLATION / METHYLATION / CHLOROPLAST / CALVIN CYCLE / MONOOXYGENASE / LYASE / RUBISCO / PLASTID / MAGNESIUM / ACETYLATION

Function / homology

Function and homology information

photorespiration / ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / chloroplast / monooxygenase activity / magnesium ion binding
Similarity search - Function

Biological species

CHLAMYDOMONAS REINHARDTII (plant)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2 Å

Authors

Karkehabadi, S. / Satagopan, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I.

Citation

Journal: Biochemistry / Year: 2007
Title: Structural Analysis of Altered Large-Subunit Loop-6-Carboxy-Terminus Interactions that Influence Catalytic Efficiency and Co2 O2 Specificity of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase
Authors: Karkehabadi, S. / Satagopan, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I.

History

Deposition	Jul 13, 2007	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Aug 7, 2007	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Dec 13, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_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 / _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	2v67.cif.gz	991 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2v67_validation.pdf.gz	2.8 MB	Display	wwPDB validaton report
Full document	2v67_full_validation.pdf.gz	2.8 MB	Display
Data in XML	2v67_validation.xml.gz	194.9 KB	Display
Data in CIF	2v67_validation.cif.gz	270.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/v6/2v67 ftp://data.pdbj.org/pub/pdb/validation_reports/v6/2v67	HTTPS FTP

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Related structure data

Related structure data	2v63C 2v68C 2v69C 2v6aC 1gk8S 1ir2 1uw9 1uwa 1uzd 1uzh S: Starting model for refinement C: citing same article (ref.)
Similar structure data	1ir2-1 2vdh-d 1rcx-d 2vdi-d 1ir2-2 2v68-d 1uw9-d 1gk8-1 8ruc-1 1uwa-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	#11 - Nov 2000 Rubisco similarity (18)

Deposited unit

A: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

B: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

C: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

D: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

E: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

F: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

G: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

H: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN

I: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

J: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

K: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

L: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

M: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

N: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

O: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

P: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1

hetero molecules

559 kDa, 16 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)	120.094, 178.558, 122.495
Angle α, β, γ (deg.)	90.00, 117.83, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Refine code: 1

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	1	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	2	PHE	PHE	ALA	ALA	B	B	13 - 438	13 - 438
2	1	2	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	2	GLU	GLU	CAP	CAP	B	B - Z	440 - 477	440
2	2	2	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	3	PHE	PHE	LEU	LEU	C	C	13 - 437	13 - 437
2	1	3	PHE	PHE	LEU	LEU	A	A	13 - 437	13 - 437
1	2	3	GLY	GLY	CAP	CAP	C	C - GA	442 - 477	442
2	2	3	GLY	GLY	CAP	CAP	A	A - R	442 - 477	442
1	1	4	PHE	PHE	ALA	ALA	D	D	13 - 438	13 - 438
2	1	4	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	4	GLU	GLU	GLU	GLU	D	D	440	440
2	2	4	GLU	GLU	GLU	GLU	A	A	440	440
1	1	5	PHE	PHE	ALA	ALA	E	E	13 - 438	13 - 438
2	1	5	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	5	GLU	GLU	CAP	CAP	E	E - VA	440 - 477	440
2	2	5	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	6	PHE	PHE	ALA	ALA	F	F	13 - 438	13 - 438
2	1	6	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	6	GLU	GLU	CAP	CAP	F	F - DB	440 - 477	440
2	2	6	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	7	PHE	PHE	ALA	ALA	G	G	13 - 438	13 - 438
2	1	7	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	7	GLU	GLU	CAP	CAP	G	G - KB	440 - 477	440
2	2	7	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	8	PHE	PHE	ALA	ALA	H	H	13 - 438	13 - 438
2	1	8	PHE	PHE	ALA	ALA	A	A	13 - 438	13 - 438
1	2	8	GLU	GLU	CAP	CAP	H	H - SB	440 - 477	440
2	2	8	GLU	GLU	CAP	CAP	A	A - R	440 - 477	440
1	1	9	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	9	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	10	MME	MME	CYS	CYS	J	J	1 - 83	1 - 83
2	1	10	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	10	ASP	ASP	ALA	ALA	J	J	85 - 129	85 - 129
2	2	10	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	11	MME	MME	CYS	CYS	K	K	1 - 83	1 - 83
2	1	11	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	11	ASP	ASP	ALA	ALA	K	K	85 - 129	85 - 129
2	2	11	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	12	MME	MME	CYS	CYS	L	L	1 - 83	1 - 83
2	1	12	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	12	ASP	ASP	ALA	ALA	L	L	85 - 129	85 - 129
2	2	12	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	13	MME	MME	CYS	CYS	M	M	1 - 83	1 - 83
2	1	13	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	13	ASP	ASP	ALA	ALA	M	M	85 - 129	85 - 129
2	2	13	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	14	MME	MME	CYS	CYS	N	N	1 - 83	1 - 83
2	1	14	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	14	ASP	ASP	ALA	ALA	N	N	85 - 129	85 - 129
2	2	14	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	15	MME	MME	CYS	CYS	O	O	1 - 83	1 - 83
2	1	15	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	15	ASP	ASP	ALA	ALA	O	O	85 - 129	85 - 129
2	2	15	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129
1	1	16	MME	MME	CYS	CYS	P	P	1 - 83	1 - 83
2	1	16	MME	MME	CYS	CYS	I	I	1 - 83	1 - 83
1	2	16	ASP	ASP	ALA	ALA	P	P	85 - 129	85 - 129
2	2	16	ASP	ASP	ALA	ALA	I	I	85 - 129	85 - 129

NCS ensembles :

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RIBULOSE BISPHOSPHATE CARBOXYLASE ... , 2 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein	RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN / RUBISCO LARGE SUBUNIT / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE LARGE CHAIN Mass: 52708.895 Da / Num. of mol.: 8 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Plasmid: PLS-T342I / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: P00877, ribulose-bisphosphate carboxylase
#2: Protein	RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1 / RUBISCO SMALL SUBUNIT 1 / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE SMALL CHAIN Mass: 16283.806 Da / Num. of mol.: 8 / Fragment: RESIDUES 46-185 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Plasmid: PLS-T342I / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: P00873, ribulose-bisphosphate carboxylase

#1: Protein

RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN / RUBISCO LARGE SUBUNIT / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE LARGE CHAIN

Mass: 52708.895 Da / Num. of mol.: 8 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Plasmid: PLS-T342I / Production host:

ESCHERICHIA COLI (E. coli)
References: UniProt: P00877, ribulose-bisphosphate carboxylase

#2: Protein

RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1 / RUBISCO SMALL SUBUNIT 1 / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE SMALL CHAIN

Mass: 16283.806 Da / Num. of mol.: 8 / Fragment: RESIDUES 46-185
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Plasmid: PLS-T342I / Production host:

ESCHERICHIA COLI (E. coli)
References: UniProt: P00873, ribulose-bisphosphate carboxylase

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Sugars , 1 types, 8 molecules

#4: Sugar	ChemComp-CAP / 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE Type: saccharide / Mass: 356.115 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₆H₁₄O₁₃P₂

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Non-polymers , 3 types, 2852 molecules

#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#5: Chemical	... ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 58 / Source method: obtained synthetically / Formula: C₂H₆O₂
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 2786 / Source method: isolated from a natural source / Formula: H₂O

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Details

Compound details	ENGINEERED RESIDUE IN CHAIN A, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN B, THR 342 TO ILE ...ENGINEERED RESIDUE IN CHAIN A, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN B, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN C, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN D, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN E, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN F, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN G, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN H, THR 342 TO ILE
Sequence details	THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877) HAS A VARIANT (LEU46PRO) WHICH OCCURS IN ...THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877) HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR AND 2137. THE CHAINS I-P ARE ENCODED BY TWO GENES; RBCS 1, UNP P00873 AND RBCS 2, UNP P08475, THAT DIFFER IN POSITIONS 22, 47, 128, AND 132. JUDGING FROM THE ELECTRON DENSITY, THE TWO GENES ARE EXPRESSED AT APPROXIMATELY EQUAL LEVEL. SEQUENCE RBCS 1, UNP P00873 HAS BEEN USED IN THIS CASE.

Compound details

ENGINEERED RESIDUE IN CHAIN A, THR 342 TO ILE ENGINEERED RESIDUE IN CHAIN B, THR 342 TO ILE ...

Sequence details

THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877) HAS A VARIANT (LEU46PRO) WHICH OCCURS IN ...

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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 Å³/Da / Density % sol: 37.9 % / Description: NONE
Crystal grow	pH: 7.5 / Details: pH 7.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9392
Detector	Type: ADSC CCD / Detector: CCD / Date: May 15, 2003
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9392 Å / Relative weight: 1
Reflection	Resolution: 2→30 Å / Num. obs: 272649 / % possible obs: 89.2 % / Redundancy: 17.3 % / R_merge(I) obs: 0.13 / Net I/σ(I): 7.5
Reflection shell	Resolution: 2→2.03 Å / R_merge(I) obs: 0.69 / Mean I/σ(I) obs: 1.3 / % possible all: 89.9

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
DENZO		data reduction
SCALEPACK		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GK8

1gk8

Resolution: 2→30 Å / Cor.coef. F_o:F_c: 0.955 / Cor.coef. F_o:F_c free: 0.935 / SU B: 4.099 / SU ML: 0.112 / Cross valid method: THROUGHOUT / ESU R: 0.247 / ESU R Free: 0.176 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.208	13764	5 %	RANDOM
R_work	0.174	-	-	-
obs	0.176	258817	89 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 17.96 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.66 Å²	0 Å²	-0.09 Å²
2-	-	-0.17 Å²	0 Å²
3-	-	-	-0.58 Å²

Refinement step

Cycle: LAST / Resolution: 2→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	38235	0	408	2786	41429

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	39647
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.14	1.96	53653
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.84	5	4836
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	31.306	23.143	1858
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.907	15	6386
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.211	15	321
X-RAY DIFFRACTION	r_chiral_restr	0.081	0.2	5679
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.02	30445
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.19	0.2	19719
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.306	0.2	27013
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.129	0.2	3201
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined	0.053	0.2	14
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.302	0.2	96
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.162	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	0.574	1.5	24737
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.889	2	38692
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	1.469	3	17093
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	2.394	4.5	14961
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

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	3644	tight positional	0	0.05
2	B	3638	tight positional	0.03	0.05
3	C	3622	tight positional	0.03	0.05
4	D	3344	tight positional	0.03	0.05
5	E	3643	tight positional	0.03	0.05
6	F	3634	tight positional	0.03	0.05
7	G	3638	tight positional	0.03	0.05
8	H	3640	tight positional	0.02	0.05
9	I	1039	tight positional	0	0.05
10	J	1037	tight positional	0.03	0.05
11	K	1037	tight positional	0.03	0.05
12	L	1039	tight positional	0.03	0.05
13	M	1036	tight positional	0.03	0.05
14	N	1039	tight positional	0.03	0.05
15	O	1037	tight positional	0.03	0.05
16	P	1039	tight positional	0.03	0.05
1	A	3644	tight thermal	0	0.5
2	B	3638	tight thermal	0.09	0.5
3	C	3622	tight thermal	0.1	0.5
4	D	3344	tight thermal	0.09	0.5
5	E	3643	tight thermal	0.11	0.5
6	F	3634	tight thermal	0.13	0.5
7	G	3638	tight thermal	0.1	0.5
8	H	3640	tight thermal	0.1	0.5
9	I	1039	tight thermal	0	0.5
10	J	1037	tight thermal	0.09	0.5
11	K	1037	tight thermal	0.09	0.5
12	L	1039	tight thermal	0.1	0.5
13	M	1036	tight thermal	0.13	0.5
14	N	1039	tight thermal	0.12	0.5
15	O	1037	tight thermal	0.09	0.5
16	P	1039	tight thermal	0.11	0.5

LS refinement shell

Resolution: 2→2.05 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.284	957	-
R_work	0.24	19051	-
obs	-	-	88.98 %

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RIBULOSE BISPHOSPHATE CARBOXYLASE ... , 2 types, 16 molecules ABCDEFGHIJKLMNOP

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Sugars , 1 types, 8 molecules

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Non-polymers , 3 types, 2852 molecules

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RIBULOSE BISPHOSPHATE CARBOXYLASE ... , 2 types, 16 molecules ABCDEFGHIJKLMNOP

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