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- PDB-2v68: Crystal structure of Chlamydomonas reinhardtii Rubisco with large... -

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Basic information

Entry
Database: PDB / ID: 2v68
TitleCrystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations V331A, T342I
Components(RIBULOSE BISPHOSPHATE CARBOXYLASE ...RuBisCO) x 2
KeywordsOXIDOREDUCTASE / 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
Ribulose bisphosphate carboxylase, small subunit / Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase / Ribulose bisphosphate carboxylase, small subunit / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain / RuBisCO large subunit, N-terminal domain / Ribulose bisphosphate carboxylase small subunit, domain / Ribulose bisphosphate carboxylase, small subunit superfamily / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase large subunit, type I ...Ribulose bisphosphate carboxylase, small subunit / Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase / Ribulose bisphosphate carboxylase, small subunit / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain / RuBisCO large subunit, N-terminal domain / Ribulose bisphosphate carboxylase small subunit, domain / Ribulose bisphosphate carboxylase, small subunit superfamily / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase large subunit, type I / Ribulose bisphosphate carboxylase, large chain, active site / Ribulose bisphosphate carboxylase large chain active site. / Ribulose bisphosphate carboxylase, large subunit, ferrodoxin-like N-terminal / Ribulose bisphosphate carboxylase large chain, N-terminal domain / Ribulose bisphosphate carboxylase, large subunit, C-terminal / RuBisCO / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain superfamily / RuBisCO large subunit, N-terminal domain superfamily / Ribulose bisphosphate carboxylase large chain, catalytic domain / Alpha-Beta Plaits / TIM Barrel / Alpha-Beta Barrel / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
2-CARBOXYARABINITOL-1,5-DIPHOSPHATE / Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 / Ribulose bisphosphate carboxylase large chain
Similarity search - Component
Biological speciesCHLAMYDOMONAS REINHARDTII (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsKarkehabadi, S. / Satagopan, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I.
CitationJournal: 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
DepositionJul 13, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 7, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4Dec 13, 2023Group: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)557,80281
Polymers551,71716
Non-polymers6,08565
Water41,0022276
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area125120 Å2
ΔGint-731 kcal/mol
Surface area150520 Å2
MethodPQS
Unit cell
Length a, b, c (Å)120.421, 178.236, 122.758
Angle α, β, γ (deg.)90.00, 117.72, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
12B
22A
13C
23A
14D
24A
15E
25A
16F
26A
17G
27A
18H
28A
19I
110J
210I
111K
211I
112L
212I
113M
213I
114N
214I
115O
215I
116P
216I

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111PHEPHEALAALAAA13 - 43813 - 438
121GLUGLUCAPCAPAA - R440 - 477440
112PHEPHEALAALABB13 - 43813 - 438
212PHEPHEALAALAAA13 - 43813 - 438
122GLUGLUCAPCAPBB - Y440 - 477440
222GLUGLUCAPCAPAA - R440 - 477440
113PHEPHELEULEUCC13 - 43713 - 437
213PHEPHELEULEUAA13 - 43713 - 437
123GLYGLYCAPCAPCC - EA442 - 477442
223GLYGLYCAPCAPAA - R442 - 477442
114PHEPHEALAALADD13 - 43813 - 438
214PHEPHEALAALAAA13 - 43813 - 438
124GLUGLUCAPCAPDD - LA440 - 477440
224GLUGLUCAPCAPAA - R440 - 477440
115PHEPHEALAALAEE13 - 43813 - 438
215PHEPHEALAALAAA13 - 43813 - 438
125GLUGLUCAPCAPEE - RA440 - 477440
225GLUGLUCAPCAPAA - R440 - 477440
116PHEPHEALAALAFF13 - 43813 - 438
216PHEPHEALAALAAA13 - 43813 - 438
126GLUGLUCAPCAPFF - XA440 - 477440
226GLUGLUCAPCAPAA - R440 - 477440
117PHEPHEALAALAGG13 - 43813 - 438
217PHEPHEALAALAAA13 - 43813 - 438
127GLUGLUCAPCAPGG - EB440 - 477440
227GLUGLUCAPCAPAA - R440 - 477440
118PHEPHEALAALAHH13 - 43813 - 438
218PHEPHEALAALAAA13 - 43813 - 438
128GLUGLUCAPCAPHH - JB440 - 477440
228GLUGLUCAPCAPAA - R440 - 477440
119MMEMMECYSCYSII1 - 831 - 83
129ASPASPALAALAII85 - 12985 - 129
1110MMEMMECYSCYSJJ1 - 831 - 83
2110MMEMMECYSCYSII1 - 831 - 83
1210ASPASPALAALAJJ85 - 12985 - 129
2210ASPASPALAALAII85 - 12985 - 129
1111MMEMMECYSCYSKK1 - 831 - 83
2111MMEMMECYSCYSII1 - 831 - 83
1211ASPASPALAALAKK85 - 12985 - 129
2211ASPASPALAALAII85 - 12985 - 129
1112MMEMMECYSCYSLL1 - 831 - 83
2112MMEMMECYSCYSII1 - 831 - 83
1212ASPASPALAALALL85 - 12985 - 129
2212ASPASPALAALAII85 - 12985 - 129
1113MMEMMECYSCYSMM1 - 831 - 83
2113MMEMMECYSCYSII1 - 831 - 83
1213ASPASPALAALAMM85 - 12985 - 129
2213ASPASPALAALAII85 - 12985 - 129
1114MMEMMECYSCYSNN1 - 831 - 83
2114MMEMMECYSCYSII1 - 831 - 83
1214ASPASPALAALANN85 - 12985 - 129
2214ASPASPALAALAII85 - 12985 - 129
1115MMEMMECYSCYSOO1 - 831 - 83
2115MMEMMECYSCYSII1 - 831 - 83
1215ASPASPALAALAOO85 - 12985 - 129
2215ASPASPALAALAII85 - 12985 - 129
1116MMEMMECYSCYSPP1 - 831 - 83
2116MMEMMECYSCYSII1 - 831 - 83
1216ASPASPALAALAPP85 - 12985 - 129
2216ASPASPALAALAII85 - 12985 - 129

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.599, 0.7658, 0.2339), (0.7661, -0.6331, 0.111), (0.2331, 0.1127, -0.9659)-93.34, 145, 163.7
3given(0.09255, -0.771, -0.6301), (0.2925, 0.626, -0.7229), (0.09518, -0.1174, 0.2834)101.4, 99.72, 90.63
4given(-0.682, 0.488, 0.5447), (0.4875, -0.2518, 0.836), (0.5452, 0.8357, -0.06616)-122.1, 44.69, 31.28
5given(-0.8183, -0.4768, 0.321), (-0.4771, 0.2521, -0.8419), (0.3205, -0.8421, -0.4338)-23.45, 126.3, 201.2
6given(-0.7808, -0.2909, -0.5529), (-0.2873, -0.6188, 0.7311), (-0.5548, 0.7297, 0.3996)36.42, 69.41, -21.71
7given(0.08892, 0.2933, 0.9519), (-0.7711, 0.6252, -0.1207), (-0.6305, -0.7232, 0.2818)-124.8, 26.83, 110.6
8given(0.5, -0.01188, -0.8659), (-0.01142, -0.9999, 0.007126), (-0.8659, 0.006323, -0.5001)65.28, 169.6, 110.8
9given(0.5966, 0.7669, 0.2365), (0.7682, -0.631, 0.108), (0.2321, 0.1173, -0.9656)-93.66, 145.2, 163.3
10given(0.09544, -0.7703, -0.6305), (0.2872, 0.6278, -0.7235), (0.9531, -0.112, 0.2811)101.4, 99.69, 90.5
11given(-0.6806, 0.4924, 0.5425), (0.4913, -0.2424, 0.8365), (0.5434, 0.8359, -0.0769)-122.2, 43.92, 32.4
12given(-0.8157, -0.4778, 0.3262), (-0.4807, 0.2461, -0.8417), (0.3218, -0.8433, -0.4304)-23.94, 126.8, 200.9
13given(-0.7808, -0.2916, -0.5526), (-0.2829, -0.6235, 0.7289), (-0.5571, 0.7254, 0.4043)36.39, 69.98, -21.9
14given(0.08838, 0.2915, 0.9525), (-0.7739, 0.6222, -0.1186), (-0.6272, -0.7266, 0.2806)-124.8, 26.83, 110.9
15given(0.4999, -0.01129, -0.866), (-0.01038, -0.9999, 0.007043), (-0.866, 0.00547, -0.4999)65.25, 169.5, 110.8

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Components

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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: 52680.844 Da / Num. of mol.: 8 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / 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 / 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: saccharideCarbohydrate / Mass: 356.115 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C6H14O13P2

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Non-polymers , 3 types, 2333 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 / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 49 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2276 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED 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 detailsTHE 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.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.03 Å3/Da / Density % sol: 39.01 % / Description: NONE
Crystal growpH: 7.5 / Details: pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 1.089
DetectorType: MARRESEARCH / Detector: CCD / Date: Sep 26, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.089 Å / Relative weight: 1
ReflectionResolution: 2.3→30 Å / Num. obs: 1285694 / % possible obs: 99.2 % / Redundancy: 20.3 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 10.8
Reflection shellResolution: 2.25→2.29 Å / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 3.1 / % possible all: 88.6

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GK8

1gk8


Resolution: 2.3→30 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.925 / SU B: 5.728 / SU ML: 0.143 / Cross valid method: THROUGHOUT / ESU R: 0.486 / ESU R Free: 0.22 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.203 10153 5 %RANDOM
Rwork0.172 ---
obs0.174 191997 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.46 Å2
Baniso -1Baniso -2Baniso -3
1-0.27 Å20 Å2-0.03 Å2
2---0.23 Å20 Å2
3----0.06 Å2
Refinement stepCycle: LAST / Resolution: 2.3→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms38202 0 372 2276 40850
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02239580
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.231.95953581
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.19654834
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.74523.1831866
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.625156359
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.23215320
X-RAY DIFFRACTIONr_chiral_restr0.0870.25667
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0230468
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.190.220011
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3020.226819
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1370.23037
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0550.210
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2420.299
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1770.29
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5621.524753
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.901238663
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.509317043
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.4244.514918
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A3642tight positional00.05
2B3637tight positional0.030.05
3C3624tight positional0.030.05
4D3642tight positional0.030.05
5E3641tight positional0.030.05
6F3638tight positional0.030.05
7G3640tight positional0.030.05
8H3642tight positional0.030.05
9I1039tight positional00.05
10J1039tight positional0.030.05
11K1037tight positional0.030.05
12L1039tight positional0.040.05
13M1039tight positional0.040.05
14N1037tight positional0.030.05
15O1037tight positional0.030.05
16P1039tight positional0.030.05
1A3642tight thermal00.5
2B3637tight thermal0.110.5
3C3624tight thermal0.120.5
4D3642tight thermal0.110.5
5E3641tight thermal0.120.5
6F3638tight thermal0.120.5
7G3640tight thermal0.120.5
8H3642tight thermal0.120.5
9I1039tight thermal00.5
10J1039tight thermal0.110.5
11K1037tight thermal0.10.5
12L1039tight thermal0.110.5
13M1039tight thermal0.130.5
14N1037tight thermal0.10.5
15O1037tight thermal0.110.5
16P1039tight thermal0.110.5
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.262 726 -
Rwork0.2 14110 -
obs--99.34 %

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