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- PDB-4pkh: Complex of ADP-actin With the N-terminal Actin-Binding Domain of ... -

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Basic information

Entry
Database: PDB / ID: 4pkh
TitleComplex of ADP-actin With the N-terminal Actin-Binding Domain of Tropomodulin
Components
  • Actin, alpha skeletal muscle
  • Gelsolin,Tropomodulin-1 chimera
KeywordsContractile Protein/Actin-Binding Protein / Tmod / Actin Filament / Pointed-End Capping Protein / Tropomyosin / Contractile Protein / Actin-binding Protein / Contractile Protein-Actin-Binding Protein complex
Function / homology
Function and homology information


pointed-end actin filament capping / lens fiber cell development / myofibril assembly / striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle ...pointed-end actin filament capping / lens fiber cell development / myofibril assembly / striated muscle atrophy / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / renal protein absorption / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / phosphatidylinositol 3-kinase catalytic subunit binding / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / actin cap / sequestering of actin monomers / regulation of podosome assembly / myosin II binding / negative regulation of viral entry into host cell / actin filament severing / actin filament capping / barbed-end actin filament capping / actin filament depolymerization / actin polymerization or depolymerization / cell projection assembly / cardiac muscle cell contraction / Striated Muscle Contraction / podosome / sarcoplasm / Sensory processing of sound by outer hair cells of the cochlea / relaxation of cardiac muscle / cytoskeletal motor activator activity / phagocytosis, engulfment / cortical actin cytoskeleton / tropomyosin binding / cortical cytoskeleton / myofibril / myosin heavy chain binding / mesenchyme migration / troponin I binding / hepatocyte apoptotic process / actin filament bundle / filamentous actin / actin filament bundle assembly / skeletal muscle thin filament assembly / striated muscle thin filament / skeletal muscle myofibril / cilium assembly / actin monomer binding / Caspase-mediated cleavage of cytoskeletal proteins / skeletal muscle fiber development / phagocytic vesicle / stress fiber / titin binding / phosphatidylinositol-4,5-bisphosphate binding / response to muscle stretch / actin filament polymerization / sarcomere / adult locomotory behavior / filopodium / muscle contraction / central nervous system development / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / protein destabilization / cellular response to type II interferon / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / lamellipodium / cell body / actin binding / blood microparticle / secretory granule lumen / ficolin-1-rich granule lumen / amyloid fibril formation / cytoskeleton / hydrolase activity / Amyloid fiber formation / protein domain specific binding / focal adhesion / calcium ion binding / Neutrophil degranulation / positive regulation of gene expression / magnesium ion binding / extracellular space / extracellular exosome / extracellular region / ATP binding / membrane / identical protein binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Tropomodulin / Tropomodulin / Actin; Chain A, domain 2 / Actin; Chain A, domain 2 / Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat ...Tropomodulin / Tropomodulin / Actin; Chain A, domain 2 / Actin; Chain A, domain 2 / Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Leucine-rich repeat domain superfamily / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / Roll / Alpha-Beta Complex / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Gelsolin / Tropomodulin-1 / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesHomo sapiens (human)
Oryctolagus cuniculus (rabbit)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å
AuthorsRao, J.N. / Dominguez, R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM073791 United States
CitationJournal: Science / Year: 2014
Title: Actin cytoskeleton. Mechanism of actin filament pointed-end capping by tropomodulin.
Authors: Rao, J.N. / Madasu, Y. / Dominguez, R.
History
DepositionMay 14, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 30, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 6, 2014Group: Database references
Revision 1.2Sep 6, 2017Group: Advisory / Author supporting evidence ...Advisory / Author supporting evidence / Database references / Derived calculations / Other / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / entity_src_nat / pdbx_audit_support / pdbx_database_status / pdbx_struct_oper_list / pdbx_validate_close_contact / pdbx_validate_symm_contact
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _entity_src_nat.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 2023Group: 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 / refine_hist / struct_conn
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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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_conn.ptnr2_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Actin, alpha skeletal muscle
B: Gelsolin,Tropomodulin-1 chimera
D: Actin, alpha skeletal muscle
E: Gelsolin,Tropomodulin-1 chimera
F: Actin, alpha skeletal muscle
G: Gelsolin,Tropomodulin-1 chimera
I: Actin, alpha skeletal muscle
J: Gelsolin,Tropomodulin-1 chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)253,87524
Polymers251,6858
Non-polymers2,19016
Water9,872548
1
A: Actin, alpha skeletal muscle
B: Gelsolin,Tropomodulin-1 chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,4696
Polymers62,9212
Non-polymers5474
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6100 Å2
ΔGint-66 kcal/mol
Surface area22640 Å2
MethodPISA
2
D: Actin, alpha skeletal muscle
E: Gelsolin,Tropomodulin-1 chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,4696
Polymers62,9212
Non-polymers5474
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-55 kcal/mol
Surface area20630 Å2
MethodPISA
3
F: Actin, alpha skeletal muscle
G: Gelsolin,Tropomodulin-1 chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,4696
Polymers62,9212
Non-polymers5474
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4330 Å2
ΔGint-61 kcal/mol
Surface area22930 Å2
MethodPISA
4
I: Actin, alpha skeletal muscle
J: Gelsolin,Tropomodulin-1 chimera
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,4696
Polymers62,9212
Non-polymers5474
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3440 Å2
ΔGint-58 kcal/mol
Surface area20910 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.222, 135.136, 140.549
Angle α, β, γ (deg.)90.00, 94.41, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Actin, alpha skeletal muscle / / Alpha-actin-1


Mass: 42096.953 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: Skeletal Muscle / References: UniProt: P68135
#2: Protein
Gelsolin,Tropomodulin-1 chimera / AGEL / Actin-depolymerizing factor / ADF / Brevin / Erythrocyte tropomodulin / E-Tmod


Mass: 20824.406 Da / Num. of mol.: 4
Fragment: Gelsolin (UNP residues 12-136), GGSGGSGGS linker, Tmod1 Actin-binding site 1 (UNP residues 50-101)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GSN, TMOD1, D9S57E, TMOD / Plasmid: pTYB11 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P06396, UniProt: P28289
#3: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 548 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.6 Å3/Da / Density % sol: 52.77 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.18 M sodium fluoride, 11% w/v PEG3350, 1% v/v PEG1000, 1% v/v PEG400
PH range: 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 1.0781 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Mar 6, 2013
RadiationMonochromator: channel cut Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0781 Å / Relative weight: 1
ReflectionResolution: 2.15→46 Å / Num. obs: 138122 / % possible obs: 98.7 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.077 / Net I/σ(I): 17.03
Reflection shellResolution: 2.15→2.28 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2 / % possible all: 99.4

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.8.4_1496)refinement
HKL-2000data scaling
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1EQY

1eqy


Resolution: 2.15→44.9 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 36.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3262 2017 1.46 %
Rwork0.2742 --
obs0.2749 138063 98.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.15→44.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15772 0 120 548 16440
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01816281
X-RAY DIFFRACTIONf_angle_d1.72922082
X-RAY DIFFRACTIONf_dihedral_angle_d18.3396008
X-RAY DIFFRACTIONf_chiral_restr0.0712411
X-RAY DIFFRACTIONf_plane_restr0.012836
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1473-2.2010.38961400.33879456X-RAY DIFFRACTION96
2.201-2.26050.36791570.32989754X-RAY DIFFRACTION99
2.2605-2.3270.3831220.33819754X-RAY DIFFRACTION99
2.327-2.40210.39321670.33079724X-RAY DIFFRACTION99
2.4021-2.4880.39241430.31859706X-RAY DIFFRACTION99
2.488-2.58760.35591390.31329726X-RAY DIFFRACTION99
2.5876-2.70530.39881350.3079747X-RAY DIFFRACTION99
2.7053-2.84790.34651520.29199670X-RAY DIFFRACTION98
2.8479-3.02630.33391470.28669711X-RAY DIFFRACTION98
3.0263-3.25990.34741380.27649597X-RAY DIFFRACTION98
3.2599-3.58790.31071470.25719631X-RAY DIFFRACTION97
3.5879-4.10670.29821340.24179715X-RAY DIFFRACTION98
4.1067-5.17280.2751460.23129869X-RAY DIFFRACTION100
5.1728-44.92070.30581500.27199986X-RAY DIFFRACTION99
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)
11.7014-0.4959-0.66571.95581.01194.32480.2064-0.60660.27240.5531-0.17370.3798-0.4049-0.085-0.07270.3747-0.03760.15710.3738-0.09290.2889-24.90211.9513186.4066
22.4848-0.2745-0.44582.14210.81213.11430.1201-0.59450.26020.31710.03050.0769-0.24690.064-0.12090.2208-0.02220.05760.2382-0.0460.2145-17.21217.4456177.8672
31.051-0.8868-0.47181.51470.78851.34740.0277-0.08360.3207-0.25730.02360.266-0.6493-0.6799-0.07270.52960.31610.06810.6865-0.06950.7315-36.342827.0267174.3462
40.4575-0.69710.12362.00570.57451.222-0.1176-0.18170.7049-0.0188-0.020.0288-0.3888-0.3322-0.24610.84220.42440.1620.441-0.0170.8514-35.199932.1559170.6161
51.5992-0.414-1.48070.94030.44411.38020.49850.70190.7076-0.2967-0.25110.0436-0.9394-0.515-0.31340.47720.48870.28950.21730.22270.726-26.406620.8758157.4264
62.76580.0639-1.39041.1360.28633.59190.1104-0.0922-0.01860.0333-0.0190.06750.16560.1649-0.12010.22720.01820.00130.2255-0.0760.2531-17.68623.8646168.5909
71.692-0.8685-1.12555.07041.06220.799-0.118-0.2262-0.00450.45560.3501-0.5280.6740.43510.13790.72570.2956-0.23830.3908-0.32260.6177-12.8119-13.2727159.5718
82.9759-0.0543-1.58193.17131.35583.4866-0.34020.0775-0.70730.1810.18590.02570.50870.0262-0.23230.3568-0.0408-0.11010.1849-0.10660.3975-19.0176-12.216151.2191
92.46540.45911.24332.81330.55131.04-0.06240.3447-0.55920.2245-0.04970.34950.8549-0.4248-0.07760.3974-0.1607-0.00440.3082-0.09990.3992-25.5216-14.7302156.5427
100.1360.1630.59752.20891.0742.68910.06461.1768-0.6580.0621-0.15890.30860.3966-0.44590.18230.23310.0016-0.09260.4201-0.17520.3407-25.3668-9.0282149.0989
114.05890.5722-0.99852.26130.84753.8041-0.08540.287-0.2623-0.02680.0182-0.23450.4656-0.03740.07130.27920.0104-0.08690.2149-0.03070.2507-19.4351-3.3138148.2522
121.10380.96770.2831.2390.98234.44180.08720.6148-0.26140.00390.03850.0910.2889-0.1978-0.12060.22450.0053-0.03720.3465-0.06120.2061-21.6243-1.3059152.4889
132.68770.32970.34253.1971-2.4872.0711-0.09330.4578-0.4551-0.1543-0.1135-0.07021.1344-0.4542-0.48860.5078-0.0755-0.09570.257-0.23930.5927-32.8393-9.6933142.7526
144.60630.47082.36271.44710.62881.3169-0.0077-0.5978-0.74320.2139-0.1258-0.04520.7329-0.8432-0.16030.4125-0.137-0.06650.4109-0.03850.4771-35.0601-8.6997163.4409
151.54610.6007-1.98592.25220.27743.0961-0.52660.1226-0.02510.0949-0.1276-0.17690.1069-0.69120.10360.47580.43110.11670.9405-0.41061.026-47.130.7799193.3308
164.1536-4.47530.26654.8282-0.35520.6076-0.3784-0.07980.71280.4647-0.091-0.0707-0.3199-0.36610.54240.6164-0.27650.16031.2459-0.18731.2917-37.648415.9463201.639
170.18880.36010.06061.7254-1.12521.7988-0.548-0.8755-0.31420.179-0.15620.84170.2161-0.12040.37920.7765-0.32790.25460.9115-0.03140.8291-19.07543.715197.8294
180.3972-0.9752-0.81094.1521-0.61446.543-0.6696-0.8562-0.6755-0.078-0.0868-0.01251.1550.2660.83510.6556-0.11450.00260.49290.11370.4257-0.2075-0.7381187.0038
192.1073-0.4354-1.00083.42430.96363.36180.03920.67690.0374-0.5172-0.09270.37690.1139-0.43940.01830.29810.0007-0.10970.45360.01390.28319.0359-9.2514126.1011
201.83720.0672-1.19223.0031-0.24842.10070.00540.35620.0031-0.4024-0.0146-0.12880.08610.1112-0.01550.25210.0162-0.03690.3239-0.02230.218117.4349-9.2701129.1907
211.95821.02440.08333.25761.38342.2002-0.11810.1197-0.43770.2112-0.22290.27870.8227-0.51520.04230.4289-0.1920.0980.2702-0.12570.36652.2503-26.2277142.5463
222.63010.7037-0.5772.54110.26763.3987-0.00430.2249-0.13970.16810.0084-0.08930.092-0.09460.03340.20370.018-0.02330.1936-0.04050.163712.4211-9.7883145.7191
232.30472.02560.58975.2636-4.6349.53670.0104-0.42850.1584-0.5894-0.4052-0.7567-0.04010.89330.20890.3547-0.05630.11950.2205-0.05510.467422.369311.8286151.2808
242.2737-0.0997-0.63861.88050.83553.04420.0957-0.33940.3469-0.00280.0158-0.1109-0.26080.173-0.04890.2114-0.02080.02830.1914-0.06130.22311.23645.6739160.6867
252.78311.42750.11887.53282.67786.2785-0.32280.0644-0.6092-0.38350.2538-0.82110.5893-0.68640.35120.9406-0.0240.1390.66430.2591.0592-18.0522.7253109.9245
260.02880.3250.38753.46754.40325.82510.38710.3702-0.38820.3802-0.14740.00950.3677-0.37310.31870.71090.1756-0.09070.73770.04880.677-18.491217.9857127.9804
272.03520.9867-0.77184.63472.82934.2038-0.1595-0.451-0.1686-0.6761-0.25070.0303-0.2444-0.92030.30070.62780.0764-0.18780.7638-0.06260.8365-17.050618.7427119.8484
280.6879-0.07651.10852.06410.46161.87560.1983-0.28520.23180.28730.0625-0.7443-0.02330.1961-0.02410.6657-0.0105-0.06411.04950.08510.919-8.12445.6209112.1041
292.2546-0.3571-0.40791.2049-0.34221.7761-0.0487-0.53830.1633-0.15150.1059-0.9186-0.21360.69180.05030.71750.0285-0.11621.12330.10040.7892-12.245416.378494.6507
302.936-1.6193-0.14663.14521.31121.0725-0.0189-0.19310.23080.58930.34570.329-0.4738-0.03180.42291.4608-0.05930.06880.7183-0.08060.6683-29.028531.4371113.5378
311.58240.7495-0.31512.43930.08653.18480.0955-0.39690.47390.3612-0.30871.011-0.8386-0.67040.31481.08120.233-0.08890.915-0.11731.0358-37.765627.4553104.6166
320.752-1.23580.10812.30610.7183.17320.1081-0.50140.4189-0.7413-0.3426-0.2152-0.3423-0.6520.38151.26730.1375-0.17180.8618-0.04240.9531-27.722531.853101.5462
333.58440.87310.36330.8247-1.29523.2245-0.18550.23660.1797-1.06030.2164-0.3742-0.53730.36210.14110.84320.02220.03590.90080.01340.7717-12.977620.280184.2335
341.3066-0.43221.22022.8054-0.21041.1818-0.2257-0.11690.9242-0.6418-0.39550.258-0.43430.21640.24991.02610.1554-0.09970.9438-0.08920.7662-25.061520.416591.7614
351.18520.18861.49612.08690.73651.938-0.05120.291-0.05980.6231-0.1616-0.3292-0.13170.2915-0.01290.5681-0.0448-0.00990.95070.01570.6791-9.95183.905299.4244
361.22971.57530.48442.02350.64171.95920.03160.1844-0.48550.62610.0973-1.17130.63960.5684-0.35420.67270.25160.05060.85660.30731.705-3.2662-11.964392.9067
373.6394-0.1270.75822.05240.72422.93320.27180.932-0.2661-0.1616-0.2359-0.30850.3736-0.09150.05040.54650.10130.06740.9101-0.19010.9937-13.5012-7.967683.631
383.39761.3596-1.58762.5889-1.03253.05050.6285-0.06010.30740.6402-0.08650.61270.2617-0.5836-0.4780.6869-0.17550.02411.1253-0.05480.772-19.4187-4.344180.239
391.3462-1.2202-0.53461.4793-0.07141.04090.04980.17170.0488-0.8693-0.01470.4071-0.4014-0.1336-0.11121.3911-0.2644-0.29230.5317-0.15851.5645-46.380934.054118.3947
404.7432-0.10790.15610.07250.32242.1533-0.4614-1.2522-1.57840.1386-0.21080.02260.1673-0.77850.66440.8155-0.41260.10231.0348-0.08430.8975-38.206327.1808127.4994
412.9239-0.16741.83243.97042.27512.8790.14350.5209-0.2806-0.3304-0.3838-0.08120.1114-0.10890.36450.8768-0.01290.04281.19190.06510.66122.3081-10.018361.583
423.30971.04740.53452.0360.73793.23430.15780.29140.057-0.29930.0645-0.4391-0.4793-0.4546-0.08430.68550.0755-0.14950.77810.18640.71415.9687-25.462271.6386
433.56643.58352.33626.54911.00674.8343-0.06471.1582-0.1037-0.8929-0.2191-0.037-0.006-0.41520.21041.1004-0.0908-0.25561.09080.11350.90912.3059-25.92858.9293
442.54591.77560.4733.10721.20422.88870.09080.05340.1920.204-0.2439-0.00640.0252-0.38530.03960.861-0.04990.09620.9955-0.03010.80537.3286-26.814577.9174
454.09180.68070.08621.60591.54021.8899-0.2888-0.77980.85310.2874-0.0626-0.050.40830.67530.40310.77210.0353-0.17550.9640.17250.810624.8451-4.754674.6093
462.71530.7319-0.42472.1901-2.66264.41420.72231.10160.1074-0.7154-0.5348-0.49980.120.40180.0310.52550.32260.09771.2430.33491.258831.362910.292881.7727
477.0973-0.36092.03364.0887-1.8774.17221.065-0.06360.9369-0.3556-0.27780.3092-0.4313-0.8215-0.66630.73310.20050.11520.9481-0.16381.029619.528610.6991.5017
485.50910.73812.95472.3793-0.04095.15770.6151-0.7257-0.62930.394-0.2089-0.3642-0.0524-0.726-0.31440.7242-0.11310.02580.98810.10950.723323.36531.057190.4469
494.1478-0.87032.01424.7527-6.09238.05010.0424-1.1593-0.23380.12740.96560.8779-0.0336-1.9947-1.1770.66420.09950.08721.0522-0.24491.125210.94635.046394.7816
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 78 )
2X-RAY DIFFRACTION2chain 'A' and (resid 79 through 165 )
3X-RAY DIFFRACTION3chain 'A' and (resid 166 through 246 )
4X-RAY DIFFRACTION4chain 'A' and (resid 247 through 273 )
5X-RAY DIFFRACTION5chain 'A' and (resid 274 through 320 )
6X-RAY DIFFRACTION6chain 'A' and (resid 321 through 375 )
7X-RAY DIFFRACTION7chain 'B' and (resid 54 through 61 )
8X-RAY DIFFRACTION8chain 'B' and (resid 62 through 74 )
9X-RAY DIFFRACTION9chain 'B' and (resid 75 through 85 )
10X-RAY DIFFRACTION10chain 'B' and (resid 86 through 102 )
11X-RAY DIFFRACTION11chain 'B' and (resid 103 through 121 )
12X-RAY DIFFRACTION12chain 'B' and (resid 122 through 160 )
13X-RAY DIFFRACTION13chain 'B' and (resid 161 through 168 )
14X-RAY DIFFRACTION14chain 'B' and (resid 169 through 177 )
15X-RAY DIFFRACTION15chain 'B' and (resid 1059 through 1071 )
16X-RAY DIFFRACTION16chain 'B' and (resid 1072 through 1081 )
17X-RAY DIFFRACTION17chain 'B' and (resid 1082 through 1091 )
18X-RAY DIFFRACTION18chain 'B' and (resid 1092 through 1099 )
19X-RAY DIFFRACTION19chain 'D' and (resid 5 through 59 )
20X-RAY DIFFRACTION20chain 'D' and (resid 60 through 145 )
21X-RAY DIFFRACTION21chain 'D' and (resid 146 through 295 )
22X-RAY DIFFRACTION22chain 'D' and (resid 296 through 375 )
23X-RAY DIFFRACTION23chain 'E' and (resid 53 through 60 )
24X-RAY DIFFRACTION24chain 'E' and (resid 61 through 177 )
25X-RAY DIFFRACTION25chain 'F' and (resid 5 through 28 )
26X-RAY DIFFRACTION26chain 'F' and (resid 29 through 55 )
27X-RAY DIFFRACTION27chain 'F' and (resid 56 through 78 )
28X-RAY DIFFRACTION28chain 'F' and (resid 79 through 145 )
29X-RAY DIFFRACTION29chain 'F' and (resid 146 through 181 )
30X-RAY DIFFRACTION30chain 'F' and (resid 182 through 206 )
31X-RAY DIFFRACTION31chain 'F' and (resid 207 through 246 )
32X-RAY DIFFRACTION32chain 'F' and (resid 247 through 273 )
33X-RAY DIFFRACTION33chain 'F' and (resid 274 through 295 )
34X-RAY DIFFRACTION34chain 'F' and (resid 296 through 320 )
35X-RAY DIFFRACTION35chain 'F' and (resid 321 through 375 )
36X-RAY DIFFRACTION36chain 'G' and (resid 52 through 60 )
37X-RAY DIFFRACTION37chain 'G' and (resid 61 through 138 )
38X-RAY DIFFRACTION38chain 'G' and (resid 139 through 177 )
39X-RAY DIFFRACTION39chain 'G' and (resid 1058 through 1063 )
40X-RAY DIFFRACTION40chain 'G' and (resid 1064 through 1074 )
41X-RAY DIFFRACTION41chain 'I' and (resid 5 through 165 )
42X-RAY DIFFRACTION42chain 'I' and (resid 166 through 196 )
43X-RAY DIFFRACTION43chain 'I' and (resid 197 through 216 )
44X-RAY DIFFRACTION44chain 'I' and (resid 217 through 320 )
45X-RAY DIFFRACTION45chain 'I' and (resid 321 through 375 )
46X-RAY DIFFRACTION46chain 'J' and (resid 52 through 60 )
47X-RAY DIFFRACTION47chain 'J' and (resid 61 through 102 )
48X-RAY DIFFRACTION48chain 'J' and (resid 103 through 149 )
49X-RAY DIFFRACTION49chain 'J' and (resid 150 through 177 )

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