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- PDB-4wnc: Crystal structure of human wild-type GAPDH at 1.99 angstroms reso... -

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Basic information

Entry
Database: PDB / ID: 4wnc
TitleCrystal structure of human wild-type GAPDH at 1.99 angstroms resolution
ComponentsGlyceraldehyde-3-phosphate dehydrogenase
KeywordsOXIDOREDUCTASE / glycolytic / Rossman fold / NAD-binding
Function / homology
Function and homology information


peptidyl-cysteine S-trans-nitrosylation / Transferases; Transferring nitrogenous groups; Transferring other nitrogenous groups / negative regulation of endopeptidase activity / glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / : / aspartic-type endopeptidase inhibitor activity / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / Gluconeogenesis / Glycolysis / GAIT complex ...peptidyl-cysteine S-trans-nitrosylation / Transferases; Transferring nitrogenous groups; Transferring other nitrogenous groups / negative regulation of endopeptidase activity / glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / : / aspartic-type endopeptidase inhibitor activity / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / Gluconeogenesis / Glycolysis / GAIT complex / peptidyl-cysteine S-nitrosylase activity / regulation of macroautophagy / defense response to fungus / positive regulation of type I interferon production / lipid droplet / positive regulation of cytokine production / glycolytic process / cellular response to type II interferon / microtubule cytoskeleton organization / glucose metabolic process / NAD binding / disordered domain specific binding / NADP binding / antimicrobial humoral immune response mediated by antimicrobial peptide / microtubule cytoskeleton / neuron apoptotic process / nuclear membrane / microtubule binding / vesicle / killing of cells of another organism / positive regulation of canonical NF-kappaB signal transduction / negative regulation of translation / protein stabilization / ribonucleoprotein complex / intracellular membrane-bounded organelle / perinuclear region of cytoplasm / extracellular exosome / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Glyceraldehyde 3-phosphate dehydrogenase, active site / Glyceraldehyde 3-phosphate dehydrogenase active site. / Glyceraldehyde-3-phosphate dehydrogenase, type I / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain / Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain / Glyceraldehyde/Erythrose phosphate dehydrogenase family / Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Dihydrodipicolinate Reductase; domain 2 ...Glyceraldehyde 3-phosphate dehydrogenase, active site / Glyceraldehyde 3-phosphate dehydrogenase active site. / Glyceraldehyde-3-phosphate dehydrogenase, type I / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain / Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain / Glyceraldehyde/Erythrose phosphate dehydrogenase family / Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain / Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain / Dihydrodipicolinate Reductase; domain 2 / Dihydrodipicolinate Reductase; domain 2 / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Glyceraldehyde-3-phosphate dehydrogenase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.99 Å
AuthorsGarcin, E.D.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: A Dimer Interface Mutation in Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Its Binding to AU-rich RNA.
Authors: White, M.R. / Khan, M.M. / Deredge, D. / Ross, C.R. / Quintyn, R. / Zucconi, B.E. / Wysocki, V.H. / Wintrode, P.L. / Wilson, G.M. / Garcin, E.D.
History
DepositionOct 11, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 3, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 17, 2014Group: Database references
Revision 1.2Feb 11, 2015Group: Database references
Revision 1.3Nov 22, 2017Group: Database references / Derived calculations ...Database references / Derived calculations / Refinement description / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list / refine / software
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.type / _pdbx_struct_assembly_prop.value / _pdbx_struct_oper_list.symmetry_operation / _refine.pdbx_ls_cross_valid_method / _software.classification / _software.name
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 / 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.ptnr1_symmetry / _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.ptnr2_symmetry / _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.ptnr3_symmetry / _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.ptnr1_symmetry / _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_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
O: Glyceraldehyde-3-phosphate dehydrogenase
A: Glyceraldehyde-3-phosphate dehydrogenase
B: Glyceraldehyde-3-phosphate dehydrogenase
C: Glyceraldehyde-3-phosphate dehydrogenase
D: Glyceraldehyde-3-phosphate dehydrogenase
E: Glyceraldehyde-3-phosphate dehydrogenase
F: Glyceraldehyde-3-phosphate dehydrogenase
G: Glyceraldehyde-3-phosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)293,28422
Polymers288,7938
Non-polymers4,49114
Water43,2182399
1
O: Glyceraldehyde-3-phosphate dehydrogenase
B: Glyceraldehyde-3-phosphate dehydrogenase
C: Glyceraldehyde-3-phosphate dehydrogenase
F: Glyceraldehyde-3-phosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,76713
Polymers144,3974
Non-polymers2,3709
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18600 Å2
ΔGint-198 kcal/mol
Surface area44980 Å2
MethodPISA
2
A: Glyceraldehyde-3-phosphate dehydrogenase
D: Glyceraldehyde-3-phosphate dehydrogenase
E: Glyceraldehyde-3-phosphate dehydrogenase
G: Glyceraldehyde-3-phosphate dehydrogenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,5189
Polymers144,3974
Non-polymers2,1215
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18630 Å2
ΔGint-198 kcal/mol
Surface area45100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)132.537, 81.423, 147.802
Angle α, β, γ (deg.)90.000, 90.060, 90.000
Int Tables number4
Space group name H-MP1211
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

#1: Protein
Glyceraldehyde-3-phosphate dehydrogenase / GAPDH / Peptidyl-cysteine S-nitrosylase GAPDH


Mass: 36099.168 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GAPDH, GAPD, CDABP0047, OK/SW-cl.12 / Plasmid: pET21a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pRIPL
References: UniProt: P04406, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), Transferases; Transferring nitrogenous groups; Transferring other nitrogenous groups
#2: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE


Mass: 663.425 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Comment: NAD*YM
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2399 / 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: 2.66 Å3/Da / Density % sol: 53.7 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5
Details: 20% (w/v) PEG6000, 0.1 M sodium acetate, 0.01 M ZnCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 1.116 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 5, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.116 Å / Relative weight: 1
ReflectionResolution: 1.99→50 Å / Num. obs: 216430 / % possible obs: 99.9 % / Redundancy: 3.7 % / Biso Wilson estimate: 17.27 Å2 / Rmerge(I) obs: 0.092 / Χ2: 1.311 / Net I/av σ(I): 11.221 / Net I/σ(I): 19.1 / Num. measured all: 795088
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
1.99-2.023.30.336106722.38799.9
2.02-2.063.60.31107892.05100
2.06-2.13.60.314107721.96499.8
2.1-2.143.70.236108121.498100
2.14-2.193.70.208107371.391100
2.19-2.243.70.196107631.449100
2.24-2.33.60.198107681.48799.9
2.3-2.363.70.154108361.137100
2.36-2.433.70.141107201.116100
2.43-2.513.70.131108421.171100
2.51-2.63.70.116108401.125100
2.6-2.73.70.118107371.14999.9
2.7-2.823.70.099108681.102100
2.82-2.973.70.088107941.04100
2.97-3.163.70.077108511.08299.9
3.16-3.43.70.07108401.067100
3.4-3.743.70.071108591.10899.9
3.74-4.293.70.065109011.08399.9
4.29-5.43.60.05109341.04199.9
5.4-503.70.04110951.03899.4

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Processing

Software
NameClassificationNB
PHENIXrefinement
Blu-Icedata collection
HKL-2000data scaling
SCALEPACKdata scaling
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1U8F

1u8f


Resolution: 1.99→49.361 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 16.65 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.179 2000 0.93 %
Rwork0.1387 213842 -
obs0.139 215842 99.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 158.82 Å2 / Biso mean: 24.7573 Å2 / Biso min: 5.79 Å2
Refinement stepCycle: final / Resolution: 1.99→49.361 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20184 0 440 2399 23023
Biso mean--31.18 33.1 -
Num. residues----2664
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00920909
X-RAY DIFFRACTIONf_angle_d1.18228361
X-RAY DIFFRACTIONf_chiral_restr0.0693215
X-RAY DIFFRACTIONf_plane_restr0.0063628
X-RAY DIFFRACTIONf_dihedral_angle_d12.9287475
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9861-2.03570.18961350.1634146421477796
2.0357-2.09080.20121370.1614151251526299
2.0908-2.15230.19721400.1471520015340100
2.1523-2.22180.18881440.13931522415368100
2.2218-2.30120.18471450.1434151931533899
2.3012-2.39330.18031440.13311535715501100
2.3933-2.50220.21371450.13771527915424100
2.5022-2.63410.18631420.13451531315455100
2.6341-2.79920.24021390.1471530415443100
2.7992-3.01520.18661430.14971536815511100
3.0152-3.31860.16011450.14231534215487100
3.3186-3.79870.22531440.13331541515559100
3.7987-4.78530.11911450.11221547015615100
4.7853-49.37660.15471520.1462156101576299
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)
10.4660.1539-0.09881.54430.56951.3449-0.0266-0.0539-0.02910.10220.04930.16580.1184-0.0296-0.01790.0953-0.0150.02880.09320.02440.1552-52.931-24.5069-52.9216
21.68510.60341.29470.33520.51391.78420.03690.0362-0.1339-0.03210.0139-0.00670.1719-0.0269-0.0740.1223-0.00550.00130.06280.00760.1152-38.3618-18.0588-70.9521
30.75240.20110.05160.81350.11071.1186-0.00840.09380.0129-0.12740.03980.1255-0.0011-0.0804-0.02550.0832-0.01-0.01990.07180.01390.1209-49.0681-11.1559-74.7701
40.2589-0.0541-0.22531.3949-0.89291.8138-0.00570.0504-0.0123-0.07060.0903-0.03190.1251-0.1174-0.07410.0703-0.00420.01040.0855-0.01410.1484-13.1219-58.2843-132.0227
51.4016-0.45041.16290.4841-0.59532.19850.0431-0.0071-0.16370.02080.00540.00360.250.0811-0.05020.14270.0180.04220.07230.00440.1516-30.1345-50.4911-117.3887
64.2854-3.67855.06693.6274-4.3737.30060.0529-0.038-0.34460.01070.05920.15540.28280.0007-0.08810.10690.01240.05620.08850.00470.1855-31.7541-53.3159-116.0299
71.0263-0.65710.05090.9178-0.00230.548-0.0413-0.1565-0.0030.13980.067-0.0449-0.03350.0001-0.02120.0970.00770.01050.08190.00440.1064-20.6757-44.8249-111.2296
80.257-0.06580.29211.17990.73011.5198-0.02450.03990.0175-0.0510.09120.015-0.11270.11530.0280.0755-0.00610.01990.08630.01040.1484-52.954523.0222-58.1413
90.8008-0.3719-0.56880.69540.43371.24160.006-0.02580.12910.02720.0099-0.0105-0.1996-0.0761-0.09320.12040.0217-0.02570.0814-0.00550.1392-35.986415.2301-43.495
103.3419-2.52-3.3123.00633.0364.59740.0479-0.02790.37560.01480.048-0.1599-0.2486-0.0226-0.19510.11070.0218-0.02740.1007-0.00660.184-34.371118.0509-42.1442
110.8665-0.5861-0.02330.9958-0.08610.5562-0.0631-0.1412-0.0080.15710.08080.04490.0296-0.01430.03880.10220.01510.02130.0869-0.00340.1083-45.45869.5566-37.3366
120.4866-0.30590.37370.67410.28532.40550.00390.0412-0.04290.0192-0.0941-0.04130.1389-0.1636-0.01640.08190.00730.01680.1591-0.00540.1219-11.3712-18.6079-43.1363
131.53640.24231.01750.58210.491.3309-0.0301-0.1657-0.03610.12960.0505-0.05160.09920.07080.0550.13010.0348-0.00170.13210.01250.1114-27.0572-1.6299-35.6837
140.8384-0.43840.2910.9163-0.18730.5935-0.0566-0.13790.18910.11710.0099-0.1559-0.08680.06540.00110.0927-0.0042-0.0150.1195-0.01750.1395-16.75416.3335-38.6176
150.55540.44780.02873.0587-1.00151.3915-0.0121-0.0651-0.0070.20150.0473-0.1563-0.11520.0214-0.04320.0981-0.0058-0.01010.1047-0.03230.1375-13.2685-12.8662-122.5349
161.2225-0.4194-0.64451.61280.73912.2966-0.05860.07730.1243-0.19060.082-0.1262-0.23110.09960.00190.1555-0.04670.00950.07660.00660.1616-12.8624-4.5543-139.4149
171.17550.4391-0.67810.3281-0.26581.04110.04380.02190.1542-0.03610.0384-0.0071-0.17260.0539-0.08980.141-0.00010.02220.07440.00590.1046-27.1967-18.1957-144.2645
186.47394.2792-5.30163.4981-3.38324.9440.11250.05670.3605-0.00670.0480.1334-0.2971-0.0272-0.14740.113-0.00860.0040.0836-0.00220.1412-28.5286-15.3374-145.8742
191.9722-0.0116-0.8731.2219-0.56363.7853-0.02730.15650.0663-0.12310.0195-0.0086-0.1835-0.1043-0.00630.0741-0.020.01730.0529-0.00930.1031-25.7216-22.5235-151.2817
200.80660.28950.04440.88460.15591.183-0.02440.095-0.0372-0.11140.0614-0.14140.01960.1487-0.02940.0865-0.01290.04750.087-0.01310.1335-14.1909-24.6283-147.8287
211.912-0.108-1.44374.56521.25322.7558-0.03220.0879-0.0147-0.2499-0.17470.24130.19230.22970.14010.1190.06190.01030.1950.02640.0719-57.5304-19.4968-120.4208
224.5252-3.0008-0.51716.5223-0.57291.77990.08260.02480.0249-0.1742-0.06010.1504-0.1746-0.13160.00340.09840.04860.00980.1860.00480.0548-53.5404-16.4859-130.7996
231.0716-0.65540.67930.9055-0.29812.3822-0.10440.08260.15760.1255-0.0534-0.0509-0.32440.34140.11540.1071-0.03730.01150.18310.01320.1233-53.5331-13.7888-111.0933
248.3657-1.2672-3.96825.43980.96475.9416-0.0887-0.1189-0.21880.1618-0.0190.28650.06590.08280.09050.0730.0395-0.00410.1260.00130.0483-57.2712-23.4444-102.2053
251.71250.3223-1.1990.6696-0.70971.47790.0435-0.10550.04030.16730.02820.0726-0.145-0.1065-0.05150.13220.01960.0180.117-0.01470.103-39.5171-33.8866-110.7092
264.41931.1826-4.47370.8013-1.18424.55520.0198-0.36430.24730.19180.07570.0532-0.24480.022-0.16640.11970.07990.03120.2242-0.03040.1299-38.2573-33.1685-107.4926
271.25430.3436-0.15881.4768-0.10561.7196-0.0035-0.2862-0.0480.29620.02770.0798-0.0383-0.095-0.03430.0910.02640.03970.15780.01740.1247-40.6635-42.0644-109.3895
280.8797-0.5216-0.2780.98040.38470.4709-0.0585-0.0947-0.20760.1054-0.0030.16390.077-0.11980.04880.0963-0.00040.05020.14060.01680.1676-52.1747-41.4531-113.5069
290.84430.3756-0.1461.01570.94752.6013-0.04280.07910.2504-0.31180.0306-0.0019-0.62630.17970.01920.2897-0.08030.01410.21510.03260.2456-13.690216.1859-75.4716
301.487-0.7505-1.32051.47661.36932.26390.03150.12150.0596-0.19810.0105-0.0483-0.16230.0925-0.07160.1165-0.0175-0.00440.13120.02570.096-30.3048-0.7042-78.7562
314.1654-1.5275-5.1091.28421.89887.01470.11530.31470.23-0.22150.0016-0.0626-0.2695-0.0167-0.120.1306-0.04420.00480.17030.04060.1206-32.02060.0661-81.723
321.12350.41080.09270.817-0.06331.3415-0.03380.1613-0.0966-0.12940.0614-0.16350.04230.23850.0050.09420.00380.03660.1419-0.00720.1258-20.4268-8.68-78.7067
332.1463-1.6618-0.46344.392-0.30912.40030.04230.0109-0.3773-0.0382-0.05710.26170.3023-0.2140.02810.2473-0.14690.01050.26860.00220.1836-55.5775-48.6263-146.4516
343.90282.79491.70224.9698-0.35551.629-0.04190.0154-0.2259-0.18880.16720.3130.3929-0.52740.00070.2306-0.11860.03480.24820.00620.197-53.4935-51.8119-135.5512
351.60830.94-0.71332.155-0.48972.9259-0.18630.1203-0.4202-0.4530.0817-0.16920.84720.01080.05280.3732-0.0480.01240.2227-0.04770.2567-50.5847-52.3749-156.9015
361.1482-0.34730.86090.9639-0.93981.6550.02680.1108-0.0575-0.2070.03710.06650.1943-0.1133-0.05610.1379-0.01290.01410.1285-0.02110.0936-35.6461-34.5196-152.6706
373.6365-1.46344.23651.3921-1.9845.99890.09980.2711-0.2174-0.2331-0.00970.040.3167-0.0318-0.08210.1422-0.03930.04260.1594-0.03910.1132-34.0001-35.2982-155.6113
382.3577-0.27750.29532.122-0.79613.5588-0.01080.18860.0345-0.23930.00520.0614-0.06040.00470.01980.0842-0.01660.00530.0946-0.02330.0896-36.3955-26.3565-154.1051
391.24290.5350.13941.18580.13571.1907-0.05530.15070.1013-0.10.07650.1867-0.0357-0.31030.0140.08690.0033-0.01210.16520.00640.131-48.5411-26.6571-152.1088
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'O' and (resid 3 through 151 )O0
2X-RAY DIFFRACTION2chain 'O' and (resid 152 through 227 )O0
3X-RAY DIFFRACTION3chain 'O' and (resid 228 through 335 )O0
4X-RAY DIFFRACTION4chain 'A' and (resid 3 through 151 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 152 through 199 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 200 through 227 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 228 through 335 )A0
8X-RAY DIFFRACTION8chain 'B' and (resid 3 through 151 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 152 through 199 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 200 through 227 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 228 through 335 )B0
12X-RAY DIFFRACTION12chain 'C' and (resid 3 through 151 )C0
13X-RAY DIFFRACTION13chain 'C' and (resid 152 through 227 )C0
14X-RAY DIFFRACTION14chain 'C' and (resid 228 through 335 )C0
15X-RAY DIFFRACTION15chain 'D' and (resid 3 through 112 )D0
16X-RAY DIFFRACTION16chain 'D' and (resid 113 through 151 )D0
17X-RAY DIFFRACTION17chain 'D' and (resid 152 through 199 )D0
18X-RAY DIFFRACTION18chain 'D' and (resid 200 through 227 )D0
19X-RAY DIFFRACTION19chain 'D' and (resid 228 through 254 )D0
20X-RAY DIFFRACTION20chain 'D' and (resid 255 through 335 )D0
21X-RAY DIFFRACTION21chain 'E' and (resid 3 through 34 )E0
22X-RAY DIFFRACTION22chain 'E' and (resid 35 through 69 )E0
23X-RAY DIFFRACTION23chain 'E' and (resid 70 through 136 )E0
24X-RAY DIFFRACTION24chain 'E' and (resid 137 through 151 )E0
25X-RAY DIFFRACTION25chain 'E' and (resid 152 through 199 )E0
26X-RAY DIFFRACTION26chain 'E' and (resid 200 through 227 )E0
27X-RAY DIFFRACTION27chain 'E' and (resid 228 through 254 )E0
28X-RAY DIFFRACTION28chain 'E' and (resid 255 through 335 )E0
29X-RAY DIFFRACTION29chain 'F' and (resid 3 through 151 )F0
30X-RAY DIFFRACTION30chain 'F' and (resid 152 through 199 )F0
31X-RAY DIFFRACTION31chain 'F' and (resid 200 through 227 )F0
32X-RAY DIFFRACTION32chain 'F' and (resid 228 through 335 )F0
33X-RAY DIFFRACTION33chain 'G' and (resid 3 through 34 )G0
34X-RAY DIFFRACTION34chain 'G' and (resid 35 through 69 )G0
35X-RAY DIFFRACTION35chain 'G' and (resid 70 through 151 )G0
36X-RAY DIFFRACTION36chain 'G' and (resid 152 through 199 )G0
37X-RAY DIFFRACTION37chain 'G' and (resid 200 through 227 )G0
38X-RAY DIFFRACTION38chain 'G' and (resid 228 through 254 )G0
39X-RAY DIFFRACTION39chain 'G' and (resid 255 through 335 )G0

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