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- PDB-2ynm: Structure of the ADPxAlF3-Stabilized Transition State of the Nitr... -

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Basic information

Entry
Database: PDB / ID: 2ynm
TitleStructure of the ADPxAlF3-Stabilized Transition State of the Nitrogenase-like Dark-Operative Protochlorophyllide Oxidoreductase Complex from Prochlorococcus marinus with Its Substrate Protochlorophyllide a
Components
  • (LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT ...) x 2
  • LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
KeywordsOXIDOREDUCTASE / IRON-SULFUR CLUSTER / METALLOENZYME / ELECTRON TRANSFER / CHLOROPHYLL SYNTHESIS / ATPASE / DYNAMIC SWITCH
Function / homology
Function and homology information


light-independent chlorophyll biosynthetic process / ferredoxin:protochlorophyllide reductase (ATP-dependent) / photosynthesis, dark reaction / oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor / oxidoreductase activity, acting on iron-sulfur proteins as donors / 4 iron, 4 sulfur cluster binding / ATP binding / metal ion binding
Similarity search - Function
Proto-chlorophyllide reductase 57 kD subunit B / Light-independent protochlorophyllide reductase, iron-sulphur ATP-binding protein / Light-independent protochlorophyllide reductase, N subunit / Light-independent protochlorophyllide reductase, B subunit / Protochlorophyllide reductase, ChlB, light independent / Light-independent protochlorophyllide reductase subunit B-like, C-terminal / Proto-chlorophyllide reductase, C-terminal / Proto-chlorophyllide reductase 57 kD subunit / NifH/frxC family / NifH/chlL conserved site ...Proto-chlorophyllide reductase 57 kD subunit B / Light-independent protochlorophyllide reductase, iron-sulphur ATP-binding protein / Light-independent protochlorophyllide reductase, N subunit / Light-independent protochlorophyllide reductase, B subunit / Protochlorophyllide reductase, ChlB, light independent / Light-independent protochlorophyllide reductase subunit B-like, C-terminal / Proto-chlorophyllide reductase, C-terminal / Proto-chlorophyllide reductase 57 kD subunit / NifH/frxC family / NifH/chlL conserved site / 4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family / NifH/frxC family signature 2. / NifH/frxC family signature 1. / NIFH_FRXC family profile. / Nitrogenase/oxidoreductase, component 1 / Nitrogenase component 1 type Oxidoreductase / Nitrogenase molybdenum iron protein domain / Helicase, Ruva Protein; domain 3 / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / ALUMINUM FLUORIDE / : / Protochlorophyllide / IRON/SULFUR CLUSTER / Light-independent protochlorophyllide reductase subunit N / Light-independent protochlorophyllide reductase subunit B / Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
Similarity search - Component
Biological speciesPROCHLOROCOCCUS MARINUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsKrausze, J. / Lange, C. / Heinz, D.W. / Moser, J.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2013
Title: Structure of Adp-Aluminium Fluoride-Stabilized Protochlorophyllide Oxidoreductase Complex.
Authors: Moser, J. / Lange, C. / Krausze, J. / Rebelein, J. / Schubert, W. / Ribbe, M.W. / Heinz, D.W. / Jahn, D.
History
DepositionOct 16, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 30, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2013Group: Database references
Revision 1.2Dec 20, 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 / pdbx_validate_chiral / struct_conn / 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_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_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_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_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.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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_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

Downloads & links

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Assembly

Deposited unit
A: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
B: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
C: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N
D: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)175,51623
Polymers171,5304
Non-polymers3,98619
Water6,882382
1
A: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
B: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
C: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N
D: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B
hetero molecules

A: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
B: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN
C: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N
D: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)351,03246
Polymers343,0598
Non-polymers7,97238
Water1448
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_554-x,y,-z-11
Buried area53700 Å2
ΔGint-233.5 kcal/mol
Surface area90140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)308.400, 74.110, 74.230
Angle α, β, γ (deg.)90.00, 91.24, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11D-2053-

HOH

Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.47548, -0.07883, 0.87619), (-0.07359, -0.99605, -0.04968), (0.87664, -0.04086, -0.4794)
Vector: 45.27161, 68.23617, -70.50817)

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN / DPOR SUBUNIT L / LI-POR SUBUNIT L


Mass: 32845.430 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PROCHLOROCOCCUS MARINUS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODON PLUS RIL
References: UniProt: Q7VD39, ferredoxin:protochlorophyllide reductase (ATP-dependent), EC: 1.18.-.-

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LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT ... , 2 types, 2 molecules CD

#2: Protein LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N / DPOR SUBUNIT N / LI-POR SUBUNIT N


Mass: 47040.328 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PROCHLOROCOCCUS MARINUS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODON PLUS RIL
References: UniProt: Q7VD37, ferredoxin:protochlorophyllide reductase (ATP-dependent), EC: 1.18.-.-
#3: Protein LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B / DPOR SUBUNIT B / LI-POR SUBUNIT B


Mass: 58798.477 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PROCHLOROCOCCUS MARINUS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODON PLUS RIL
References: UniProt: Q7VD38, ferredoxin:protochlorophyllide reductase (ATP-dependent), EC: 1.18.-.-

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Non-polymers , 10 types, 401 molecules

#4: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#5: Chemical
ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES / HEPES


Mass: 238.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H18N2O4S / Comment: pH buffer*YM
#6: Chemical ChemComp-AF3 / ALUMINUM FLUORIDE / Aluminium fluoride


Mass: 83.977 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: AlF3
#7: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#9: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe4S4
#10: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#11: Chemical ChemComp-PMR / Protochlorophyllide / Protochlorophyllide


Mass: 612.957 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C35H32MgN4O5
#12: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#13: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 382 / Source method: isolated from a natural source / Formula: H2O

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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: 2.67 Å3/Da / Density % sol: 53.94 %
Description: INCOMPLETE HIGH-RESOLUTION DATA WERE INCLUDED. DATA SHOW REASONABLE COMPLETENESS UP TO 2.6 A.
Crystal growpH: 7.5
Details: CRYSTALLIZED FROM 3% (W/V) PEG 6000, 100MM KCL, 100MM TRIS, PH 8.5; THEN SOAKED WITH 13% (W/V) PEG 8000, 100MM HEPES, PH 7.5, 15% (V/V) GLYCEROL, 5MM DTT, 0.01MM PCHLIDE, 24MM DMSO

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.91841
DetectorType: RAYONIX / Detector: CCD / Date: Dec 17, 2010 / Details: MIRRORS
RadiationMonochromator: SI(111) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91841 Å / Relative weight: 1
ReflectionResolution: 2.1→34.51 Å / Num. obs: 81370 / % possible obs: 83.1 % / Observed criterion σ(I): 3 / Redundancy: 2.6 % / Biso Wilson estimate: 23.56 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 14.32
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 0.6 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 3 / % possible all: 48.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8.1_1168)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3FWY AND 2XDQ

3fwy

2xdq


Resolution: 2.1→34.51 Å / SU ML: 0.26 / σ(F): 1.99 / Phase error: 26.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2331 4028 4.9 %
Rwork0.1989 --
obs0.2006 81361 83.09 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 41.4 Å2
Refinement stepCycle: LAST / Resolution: 2.1→34.51 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11195 0 226 382 11803
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00411694
X-RAY DIFFRACTIONf_angle_d1.01815850
X-RAY DIFFRACTIONf_dihedral_angle_d13.4584399
X-RAY DIFFRACTIONf_chiral_restr0.0531766
X-RAY DIFFRACTIONf_plane_restr0.0032023
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12470.3287690.26121387X-RAY DIFFRACTION43
2.1247-2.15060.3321750.25321557X-RAY DIFFRACTION49
2.1506-2.17780.3069930.23581697X-RAY DIFFRACTION53
2.1778-2.20650.2787940.23831768X-RAY DIFFRACTION56
2.2065-2.23670.2967870.24341896X-RAY DIFFRACTION59
2.2367-2.26870.3049980.23671955X-RAY DIFFRACTION62
2.2687-2.30250.31831100.24822079X-RAY DIFFRACTION65
2.3025-2.33850.32031030.26242179X-RAY DIFFRACTION68
2.3385-2.37680.25441250.26012265X-RAY DIFFRACTION71
2.3768-2.41780.28931190.24812381X-RAY DIFFRACTION75
2.4178-2.46170.29231270.25552498X-RAY DIFFRACTION78
2.4617-2.50910.33151340.24982616X-RAY DIFFRACTION82
2.5091-2.56030.29181470.25142791X-RAY DIFFRACTION86
2.5603-2.61590.29931490.25372807X-RAY DIFFRACTION90
2.6159-2.67680.29951580.2513026X-RAY DIFFRACTION94
2.6768-2.74370.2661660.25473163X-RAY DIFFRACTION98
2.7437-2.81780.2971640.24673115X-RAY DIFFRACTION98
2.8178-2.90070.28851670.24133157X-RAY DIFFRACTION98
2.9007-2.99430.29021660.22283155X-RAY DIFFRACTION99
2.9943-3.10120.2431650.22693154X-RAY DIFFRACTION98
3.1012-3.22530.24891670.21753169X-RAY DIFFRACTION99
3.2253-3.3720.24761680.20393182X-RAY DIFFRACTION98
3.372-3.54960.22721660.1883129X-RAY DIFFRACTION98
3.5496-3.77170.20311680.17213177X-RAY DIFFRACTION99
3.7717-4.06250.19481670.16023167X-RAY DIFFRACTION98
4.0625-4.47060.17431670.14423170X-RAY DIFFRACTION99
4.4706-5.11570.15931690.143203X-RAY DIFFRACTION99
5.1157-6.43840.2091700.16423212X-RAY DIFFRACTION99
6.4384-34.51480.15021700.15123278X-RAY DIFFRACTION98
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°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)
12.80240.03790.22861.78520.0942.3044-0.0294-0.34570.20020.1999-0.1663-0.0335-0.126-0.07080.19980.2104-0.1099-0.01690.24190.00520.246156.61242.9477-1.1298
24.3699-0.7732-0.5826.0694-0.92643.10410.0459-0.30190.08870.4719-0.1121.19690.0387-1.19950.0580.2881-0.08530.08520.789-0.07880.388634.471238.958-3.526
32.27791.88260.5153.8162.26364.47940.1534-0.24930.49740.1859-0.220.3241-0.182-0.32550.06230.1762-0.03830.01220.2839-0.00560.273447.383243.5911-5.3756
41.75170.21340.06270.4020.21870.8111-0.05440.07380.3572-0.0869-0.1268-0.0536-0.2820.28110.16660.262-0.0919-0.00930.23760.08940.353161.230244.9948-17.4511
53.7358-0.57320.0692.3644-0.89121.9045-0.0320.12310.1588-0.1834-0.1273-0.4342-0.04710.40930.10820.2906-0.15350.04570.36710.11410.442671.164746.6772-14.6454
61.57220.4972-0.69652.0482-0.2911.56080.114-0.45490.37030.3128-0.193-0.2706-0.2410.27030.09680.3447-0.1541-0.09730.30320.04220.385469.276743.74743.1418
73.5808-3.4001-1.48714.95051.49173.32810.42780.39740.6197-0.9466-0.2581-0.6087-0.61440.2733-0.13810.4113-0.13640.0320.42410.20590.478771.819446.0324-22.9408
82.1222-0.02610.77430.214-0.01691.51960.26830.631-0.24750.1053-0.2261-0.08940.19120.4176-0.01110.29820.1034-0.03680.23410.00590.335367.750321.177-22.1405
96.5066-1.78486.3710.9205-2.55247.73190.74731.2259-0.5743-0.5718-0.3435-0.03450.73030.6187-0.37110.42370.13660.00520.7199-0.0160.270859.159424.7312-39.4132
102.1747-1.06981.40251.5515-1.28391.29230.36520.4618-0.3025-0.1304-0.10640.09990.42350.3045-0.2190.29130.0426-0.06540.19290.00790.28458.255721.0069-23.1138
110.89020.2563-0.15521.1292-0.1830.12260.2368-0.1553-0.27020.0923-0.03570.08250.29880.01320.15660.5367-0.0583-0.14250.0770.14460.378558.742218.7385-4.4579
120.8961-0.94730.36832.5016-0.3822.28570.21670.1684-0.21270.12380.0276-0.55190.46310.5106-0.14270.28690.1018-0.1280.39780.03350.460477.637419.4444-12.7485
131.4436-0.5032-0.47642.39132.08732.0861-0.0144-0.3244-0.26630.3975-0.23570.38350.7363-0.09270.27610.5864-0.1557-0.01870.4080.21690.422555.633318.17021.5557
144.2457-1.0357-5.39031.78171.81897.01090.24310.23410.1319-0.4084-0.1129-0.4202-0.430.8794-0.21630.2887-0.00960.01080.76710.14310.288546.053335.8553-50.1604
152.3301-0.04071.19810.9960.44792.48550.301-0.2043-0.43360.0538-0.1783-0.00210.4428-0.1469-0.11460.229-0.0442-0.010.23740.05790.202829.417621.2296-25.3075
161.24591.00531.60891.321.62753.55470.28220.2994-0.6396-0.157-0.1782-0.08160.75080.245-0.12610.40130.1189-0.05830.4122-0.13110.415832.699511.553-42.5832
170.54060.1155-0.64640.30130.21591.24710.09160.4961-0.42560.03890.031-0.17670.70520.4454-0.07060.58530.2644-0.10250.7595-0.25560.424336.68439.6078-51.4388
180.64481.28550.65772.91712.20782.9862-0.11720.5339-0.1352-0.36260.2671-0.17050.31820.4723-0.15870.52110.1625-0.1041.0903-0.18830.317225.461918.3388-69.4876
190.6454-0.0807-0.07360.17710.06930.8879-0.00030.72890.0373-0.1791-0.11920.0015-0.06660.2627-0.08040.22560.05520.05020.90410.09120.10532.412734.4267-55.5766
201.9803-0.44960.28360.6082-0.08891.2747-0.00280.08890.5517-0.0174-0.1627-0.1016-0.30840.07550.10810.204-0.0486-0.01030.28210.0490.311632.243849.0006-27.6228
211.79560.21030.08950.6264-0.26661.001-0.0451-0.40510.7870.1637-0.07840.0553-0.402-0.25490.09980.27230.026-0.05030.3435-0.14840.41827.581655.347-21.8285
220.6315-0.37780.15150.677-0.27141.35920.0023-0.3410.07960.1071-0.0754-0.02510.0414-0.06210.07590.147-0.0466-0.00940.517-0.02870.17526.471536.8263-20.9951
234.5399-1.77571.99041.83550.23592.18310.2648-0.2873-0.67280.4012-0.0831-0.21540.71270.4016-0.0820.44780.013-0.11380.56050.08390.3527-9.78718.2404-27.7033
242.59190.7507-2.18597.46354.01614.95390.1986-0.6985-0.56810.85840.2935-0.60320.45610.8553-0.45040.5751-0.0765-0.17930.95290.18860.5681-6.78315.6533-10.0395
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 29:82)
2X-RAY DIFFRACTION2CHAIN A AND (RESSEQ 83:98)
3X-RAY DIFFRACTION3CHAIN A AND (RESSEQ 99:158)
4X-RAY DIFFRACTION4CHAIN A AND (RESSEQ 159:198)
5X-RAY DIFFRACTION5CHAIN A AND (RESSEQ 199:224)
6X-RAY DIFFRACTION6CHAIN A AND (RESSEQ 225:274)
7X-RAY DIFFRACTION7CHAIN A AND (RESSEQ 275:295)
8X-RAY DIFFRACTION8CHAIN B AND (RESSEQ 28:82)
9X-RAY DIFFRACTION9CHAIN B AND (RESSEQ 83:106)
10X-RAY DIFFRACTION10CHAIN B AND (RESSEQ 107:178)
11X-RAY DIFFRACTION11CHAIN B AND (RESSEQ 179:224)
12X-RAY DIFFRACTION12CHAIN B AND (RESSEQ 225:274)
13X-RAY DIFFRACTION13CHAIN B AND (RESSEQ 275:295)
14X-RAY DIFFRACTION14CHAIN C AND (RESSEQ -6:17)
15X-RAY DIFFRACTION15CHAIN C AND (RESSEQ 18:122)
16X-RAY DIFFRACTION16CHAIN C AND (RESSEQ 123:185)
17X-RAY DIFFRACTION17CHAIN C AND (RESSEQ 186:257)
18X-RAY DIFFRACTION18CHAIN C AND (RESSEQ 258:283)
19X-RAY DIFFRACTION19CHAIN C AND (RESSEQ 284:411)
20X-RAY DIFFRACTION20CHAIN D AND (RESSEQ 1:168)
21X-RAY DIFFRACTION21CHAIN D AND (RESSEQ 169:304)
22X-RAY DIFFRACTION22CHAIN D AND (RESSEQ 305:420)
23X-RAY DIFFRACTION23CHAIN D AND (RESSEQ 421:491)
24X-RAY DIFFRACTION24CHAIN D AND (RESSEQ 492:528)

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