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- PDB-6u39: 2.4 Angstrom crystal structure of the D129G Ca-CaM:CaV1.2 IQ doma... -

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Basic information

Entry
Database: PDB / ID: 6u39
Title2.4 Angstrom crystal structure of the D129G Ca-CaM:CaV1.2 IQ domain complex
Components
  • Calmodulin-1
  • Voltage-dependent L-type calcium channel subunit alpha-1C
KeywordsCALCIUM-BINDING PROTEIN/MEMBRANE PROTEIN / MEMBRANE PROTEIN / CALCIUM-BINDING PROTEIN-MEMBRANE PROTEIN complex
Function / homology
Function and homology information


voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / positive regulation of adenylate cyclase activity / membrane depolarization during atrial cardiac muscle cell action potential / calcium ion transmembrane transport via high voltage-gated calcium channel / Phase 2 - plateau phase / high voltage-gated calcium channel activity / membrane depolarization during AV node cell action potential / cardiac conduction ...voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / positive regulation of adenylate cyclase activity / membrane depolarization during atrial cardiac muscle cell action potential / calcium ion transmembrane transport via high voltage-gated calcium channel / Phase 2 - plateau phase / high voltage-gated calcium channel activity / membrane depolarization during AV node cell action potential / cardiac conduction / L-type voltage-gated calcium channel complex / membrane depolarization during cardiac muscle cell action potential / positive regulation of muscle contraction / cell communication by electrical coupling involved in cardiac conduction / regulation of ventricular cardiac muscle cell action potential / NCAM1 interactions / camera-type eye development / cardiac muscle cell action potential involved in contraction / embryonic forelimb morphogenesis / calcium ion transport into cytosol / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / voltage-gated calcium channel complex / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / negative regulation of ryanodine-sensitive calcium-release channel activity / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / alpha-actinin binding / RHO GTPases activate PAKs / regulation of heart rate by cardiac conduction / calcium ion import across plasma membrane / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / Long-term potentiation / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / detection of calcium ion / regulation of cardiac muscle contraction / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / voltage-gated calcium channel activity / cellular response to interferon-beta / Protein methylation / calcium channel inhibitor activity / Activation of AMPK downstream of NMDARs / presynaptic cytosol / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / eNOS activation / titin binding / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / sperm midpiece / regulation of calcium-mediated signaling / voltage-gated potassium channel complex / calcium channel complex / FCERI mediated Ca+2 mobilization / substantia nigra development / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / FCGR3A-mediated IL10 synthesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / calyx of Held / adenylate cyclase activator activity / sarcomere / VEGFR2 mediated cell proliferation / protein serine/threonine kinase activator activity / VEGFR2 mediated vascular permeability / regulation of cytokinesis / spindle microtubule / calcium channel regulator activity / positive regulation of receptor signaling pathway via JAK-STAT / Translocation of SLC2A4 (GLUT4) to the plasma membrane / Regulation of insulin secretion
Similarity search - Function
Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated ...Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated / : / Voltage-dependent channel domain superfamily / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair
Similarity search - Domain/homology
Calmodulin-1 / Voltage-dependent L-type calcium channel subunit alpha-1C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsWang, K. / Van Petegem, F.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR) Canada
CitationJournal: J. Physiol. (Lond.) / Year: 2020
Title: Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+binding and cause misfolding.
Authors: Wang, K. / Brohus, M. / Holt, C. / Overgaard, M.T. / Wimmer, R. / Van Petegem, F.
History
DepositionAug 21, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 19, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.2Oct 11, 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 / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Calmodulin-1
B: Voltage-dependent L-type calcium channel subunit alpha-1C
C: Calmodulin-1
D: Voltage-dependent L-type calcium channel subunit alpha-1C
E: Calmodulin-1
F: Voltage-dependent L-type calcium channel subunit alpha-1C
G: Calmodulin-1
H: Voltage-dependent L-type calcium channel subunit alpha-1C
I: Calmodulin-1
J: Voltage-dependent L-type calcium channel subunit alpha-1C
K: Calmodulin-1
L: Voltage-dependent L-type calcium channel subunit alpha-1C
M: Calmodulin-1
N: Voltage-dependent L-type calcium channel subunit alpha-1C
O: Calmodulin-1
P: Voltage-dependent L-type calcium channel subunit alpha-1C
Q: Calmodulin-1
R: Voltage-dependent L-type calcium channel subunit alpha-1C
S: Calmodulin-1
T: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)210,98549
Polymers209,82320
Non-polymers1,16229
Water36020
1
A: Calmodulin-1
B: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2010 Å2
ΔGint-51 kcal/mol
Surface area9530 Å2
MethodPISA
2
C: Calmodulin-1
D: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2490 Å2
ΔGint-65 kcal/mol
Surface area10080 Å2
MethodPISA
3
E: Calmodulin-1
F: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2000 Å2
ΔGint-59 kcal/mol
Surface area10080 Å2
MethodPISA
4
G: Calmodulin-1
H: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2070 Å2
ΔGint-50 kcal/mol
Surface area10020 Å2
MethodPISA
5
I: Calmodulin-1
J: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,0624
Polymers20,9822
Non-polymers802
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2030 Å2
ΔGint-51 kcal/mol
Surface area9610 Å2
MethodPISA
6
K: Calmodulin-1
L: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2190 Å2
ΔGint-61 kcal/mol
Surface area10220 Å2
MethodPISA
7
M: Calmodulin-1
N: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1920 Å2
ΔGint-48 kcal/mol
Surface area9610 Å2
MethodPISA
8
O: Calmodulin-1
P: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1890 Å2
ΔGint-49 kcal/mol
Surface area9680 Å2
MethodPISA
9
Q: Calmodulin-1
R: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2150 Å2
ΔGint-63 kcal/mol
Surface area9800 Å2
MethodPISA
10
S: Calmodulin-1
T: Voltage-dependent L-type calcium channel subunit alpha-1C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,1035
Polymers20,9822
Non-polymers1203
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1970 Å2
ΔGint-63 kcal/mol
Surface area9420 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.795, 161.656, 96.277
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
Calmodulin-1


Mass: 16663.312 Da / Num. of mol.: 10 / Mutation: D129G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CALM1, CALM, CAM, CAM1 / Production host: Escherichia coli (E. coli) / References: UniProt: P0DP23
#2: Protein/peptide
Voltage-dependent L-type calcium channel subunit alpha-1C / Calcium channel / L type / alpha-1 polypeptide / isoform 1 / cardiac muscle / Voltage-gated calcium ...Calcium channel / L type / alpha-1 polypeptide / isoform 1 / cardiac muscle / Voltage-gated calcium channel subunit alpha Cav1.2


Mass: 4318.968 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q13936
#3: Chemical...
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: Ca / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.59 Å3/Da / Density % sol: 52.54 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / Details: ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 27, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.3→49.041 Å / Num. obs: 159034 / % possible obs: 97.5 % / Redundancy: 2.93 % / Biso Wilson estimate: 68.18 Å2 / CC1/2: 0.999 / Net I/σ(I): 17.06
Reflection shell
Resolution (Å)Num. unique obsCC1/2Diffraction-ID
2.3-2.44257110.7991
2.44-2.61242850.9291
6.84-49.04160410.9981

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3G43

3g43


Resolution: 2.4→49.041 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.29 / Phase error: 31.89
RfactorNum. reflection% reflection
Rfree0.2827 6993 4.99 %
Rwork0.2318 --
obs0.2344 140090 97.54 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 169.25 Å2 / Biso mean: 85.4384 Å2 / Biso min: 40.19 Å2
Refinement stepCycle: final / Resolution: 2.4→49.041 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11328 0 29 20 11377
Biso mean--82.34 67.99 -
Num. residues----1596
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.4-2.42730.36142370.3135446898
2.4273-2.45580.37572330.2965441198
2.4558-2.48580.38962300.3021445797
2.4858-2.51720.32972380.2966445599
2.5172-2.55040.32142360.2839449999
2.5504-2.58530.33942380.2778450899
2.5853-2.62220.32332290.2816442798
2.6222-2.66140.36672370.2869449298
2.6614-2.70290.36782320.2912445898
2.7029-2.74730.33572340.2816445899
2.7473-2.79460.36272370.3004449798
2.7946-2.84540.40182390.2979447198
2.8454-2.90020.36342370.3035443698
2.9002-2.95940.3452310.2974443698
2.9594-3.02370.34442290.3059442097
3.0237-3.0940.35912360.3022447998
3.094-3.17140.35282390.3056450198
3.1714-3.25710.28862360.265446399
3.2571-3.35290.31472330.2467446598
3.3529-3.46110.35362290.2571437396
3.4611-3.58480.3352350.2552444098
3.5848-3.72830.30792160.2426420692
3.7283-3.89790.2712350.2164430095
3.8979-4.10330.25052250.2098437596
4.1033-4.36020.2512330.1932445798
4.3602-4.69660.23372330.1908446098
4.6966-5.16880.26812340.1902443097
5.1688-5.91570.31172320.2464438997
5.9157-7.44890.2672320.2419444298
7.4489-49.040.20142280.1811442497
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)
16.2054-2.65322.23393.7614-0.6836.21590.56030.2866-1.7957-0.2333-0.05370.29051.1840.0643-0.54180.7446-0.0768-0.01840.7029-0.24841.123114.3488-2.193339.4294
27.0228-4.1757-2.86543.21972.2111.9635-0.13350.1044-0.55870.0923-0.05030.55440.0676-0.0090.14160.56910.04940.05070.605-0.06750.697727.35194.225447.7085
37.41711.8020.1222.17982.51984.27360.88630.28371.08271.2379-0.15651.0371-0.11-0.3314-0.7720.84750.10390.19850.588-0.08831.000318.286310.69744.3165
45.77813.7596-1.58154.57911.96658.37610.5807-0.69680.42821.0548-0.62470.4536-0.2924-0.01630.05270.6972-0.02130.04550.5246-0.06240.651648.519411.984759.0472
58.3697-5.852-0.80866.06671.46241.4888-0.2656-0.55010.53890.38860.3788-0.52530.15890.3105-0.12780.46520.01620.06380.4364-0.02330.596434.09896.651450.8404
64.32550.76774.25786.24751.54064.3686-0.03730.65641.5146-0.1773-0.4448-0.2649-0.21550.70760.46230.54850.01420.02930.5804-0.0340.717246.92078.065746.6193
76.01510.0554-0.80799.30241.35974.41310.2705-0.04460.0540.3408-0.1268-0.6659-0.39370.1491-0.09670.54160.03320.11470.49840.07190.596617.601134.883360.5373
87.0887-4.95510.69364.9849-1.07230.8522-0.1702-0.6432-0.23750.2560.41270.147-0.1114-0.1747-0.24620.6917-0.11610.02460.57620.12130.761432.961142.85555.4943
95.39265.6827-5.72415.8894-5.86415.8201-0.43281.0255-0.058-0.18410.078-0.6528-0.1749-0.61670.40330.8987-0.0260.140.74030.05040.992324.390442.411949.1169
106.5117-0.32980.23269.53131.2626.3668-0.05980.3603-0.0657-0.20170.1159-0.2691-0.01210.1593-0.01730.4366-0.0660.02460.4969-0.00850.433756.850956.43667.0603
118.7-0.98534.58210.0752-1.63642.98140.13820.57370.0333-0.1933-0.396-0.01770.06930.13130.23180.61440.0763-0.02670.7382-0.10210.530543.289359.555818.3269
124.2694.6013-4.37787.743-6.3555.7591-0.28670.0431-2.03070.1559-0.782-0.73480.1098-0.59460.76180.6748-0.0558-0.04730.7823-0.0510.641450.70252.046421.3101
135.15771.67250.23365.4536-4.28277.73470.2970.1286-0.2442-0.42260.0732-0.01080.48990.025-0.41280.6310.1454-0.00190.5549-0.15280.548945.5363-10.782923.1961
146.4607-1.265-4.95950.83970.10415.15810.1858-0.6324-0.5418-0.0341-0.0983-0.1484-0.06830.3554-0.06150.6860.0828-0.18520.8836-0.1620.747933.7009-3.311712.5215
157.2275-4.07381.6767.7689-4.35132.4352-0.29830.61380.4824-0.25940.2275-0.1285-0.3375-0.68960.25081.0160.0101-0.03241.0463-0.08020.627244.6965-0.186514.6041
168.15650.87420.13524.1037-2.89178.25010.3155-0.1892-0.5181-0.4428-0.4273-0.34880.30320.53120.10390.57510.0392-0.11040.5166-0.0130.771216.07235.563-2.4206
177.82090.8155-4.0209-0.1041-0.22281.8026-0.25640.5241-0.5371-0.2457-0.0774-0.03550.128-0.49890.24380.6896-0.01-0.24160.9825-0.070.935428.9478-0.19158.0999
185.7023-5.28845.59014.8052-4.97445.2831-0.0815-2.01810.35860.61840.1965-0.92890.101-0.93180.13240.84860.1096-0.08550.869-0.08210.704616.29075.235911.0175
195.5938-2.0847-1.32855.27764.51345.65780.37960.1203-0.0439-0.89270.009-1.0197-0.6875-0.0768-0.31140.935-0.0845-0.07640.561-0.0620.7722.506348.3988-5.3765
209.23572.05541.10761.44260.21260.49620.1280.78410.4882-0.11770.03680.2862-0.03490.1413-0.23520.74980.0109-0.07360.6466-0.10270.762235.212535.5535-7.6217
218.8879-8.25936.85989.8086-6.80115.28480.6366-1.2048-0.411-0.65750.3907-0.46341.1606-1.1777-0.92650.9433-0.2154-0.0680.8407-0.18540.905623.67534.3345-1.978
226.0661.3488-0.66766.9077-0.9244.73910.5237-0.52960.45211.15870.0110.1281-0.1494-0.4771-0.54250.6437-0.0738-0.02370.65280.10320.640654.457853.137649.7493
238.1068-4.95423.41795.4505-1.47130.89220.08260.09130.7310.3803-0.2498-0.56590.01410.16180.21640.6268-0.11410.08180.64820.09110.651139.131145.610454.4461
248.38112.94793.89346.70160.94992.78190.46810.8194-0.76240.27460.52060.49740.8496-0.0932-0.96180.8428-0.1473-0.05620.6960.13820.705249.029139.789550.195
257.4925-4.92470.3396.4216-0.33227.82150.58490.69610.4791-0.8633-1.046-0.2237-0.0131.37830.4920.64290.12820.0360.69670.11320.705725.176766.624132.6314
264.5743-0.60522.20181.38410.93521.7776-0.0862-0.01150.7315-0.2855-0.41610.1636-0.4078-0.32340.52440.57060.07920.0110.91250.02670.605739.937760.144424.5212
273.0198-1.1096-2.0079.37235.11293.97190.2921.094-1.0111-0.3365-0.32510.47061.0343-0.29280.070.77530.1474-0.12050.8221-0.0040.568325.389257.379321.5908
284.0798-3.8279-5.27494.18124.94276.59130.7474-1.11020.496-0.23440.6661-0.6843-0.52321.1856-1.27581.0884-0.14110.02431.0519-0.14830.905949.597529.3816-2.0946
293.5067-2.16351.67588.3788-5.71779.21881.14370.7395-0.5315-1.5533-0.75910.75080.96210.3178-0.35210.910.043-0.09530.8041-0.06520.808550.331317.0175-9.6241
307.05852.57730.25850.68140.72350.7959-0.38510.717-0.898-0.47770.3974-0.1290.05630.1086-0.03810.6434-0.05060.00760.7289-0.08460.904538.869930.2886-8.4845
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and ((resid 501 through 502) or (resid 6 through 76))A0
2X-RAY DIFFRACTION2chain 'A' and ((resid 82 through 147) or (resid 503))A0
3X-RAY DIFFRACTION3chain 'B' and (resid 1612 through 1634)B1612 - 1634
4X-RAY DIFFRACTION4chain 'C' and ((resid 5 through 75) or (resid 501 through 502))C0
5X-RAY DIFFRACTION5chain 'C' and ((resid 82 through 148) or (resid 503))C0
6X-RAY DIFFRACTION6chain 'D' and (resid 1609 through 1634)D1609 - 1634
7X-RAY DIFFRACTION7chain 'E' and ((resid 501 through 502) or (resid 3 through 77))E0
8X-RAY DIFFRACTION8chain 'E' and ((resid 81 through 147) or (resid 503))E0
9X-RAY DIFFRACTION9chain 'F' and (resid 1614 through 1636)F1614 - 1636
10X-RAY DIFFRACTION10chain 'K' and ((resid 501 through 502) or (resid 4 through 77))K0
11X-RAY DIFFRACTION11chain 'K' and ((resid 81 through 147) or (resid 503))K0
12X-RAY DIFFRACTION12chain 'L' and (resid 1614 through 1637)L1614 - 1637
13X-RAY DIFFRACTION13chain 'S' and ((resid 501 through 502) or (resid 4 through 76))S0
14X-RAY DIFFRACTION14chain 'S' and ((resid 83 through 147) or (resid 503))S0
15X-RAY DIFFRACTION15chain 'T' and (resid 1613 through 1632)T1613 - 1632
16X-RAY DIFFRACTION16chain 'Q' and ((resid 501 through 502) or (resid 4 through 74))Q0
17X-RAY DIFFRACTION17chain 'Q' and ((resid 82 through 147) or (resid 503))Q0
18X-RAY DIFFRACTION18chain 'R' and (resid 1609 through 1633)R1609 - 1633
19X-RAY DIFFRACTION19chain 'M' and ((resid 501 through 502) or (resid 5 through 75))M0
20X-RAY DIFFRACTION20chain 'M' and ((resid 84 through 147) or (resid 503))M0
21X-RAY DIFFRACTION21chain 'N' and (resid 1612 through 1635)N1612 - 1635
22X-RAY DIFFRACTION22chain 'G' and ((resid 501 through 502) or (resid 4 through 76))G0
23X-RAY DIFFRACTION23chain 'G' and ((resid 84 through 146) or (resid 503))G0
24X-RAY DIFFRACTION24chain 'H' and (resid 1612 through 1635)H1612 - 1635
25X-RAY DIFFRACTION25chain 'I' and ((resid 501 through 502) or (resid 7 through 75))I0
26X-RAY DIFFRACTION26chain 'I' and (resid 82 through 147)I82 - 147
27X-RAY DIFFRACTION27chain 'J' and (resid 1610 through 1635)J1610 - 1635
28X-RAY DIFFRACTION28chain 'P' and (resid 1613 through 1633)P1613 - 1633
29X-RAY DIFFRACTION29chain 'O' and ((resid 501 through 502) or (resid 4 through 74))O0
30X-RAY DIFFRACTION30chain 'O' and ((resid 84 through 147) or (resid 503))O0

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