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- PDB-5iso: STRUCTURE OF FULL LENGTH HUMAN AMPK (NON-PHOSPHORYLATED AT T-LOOP... -

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Basic information

Entry
Database: PDB / ID: 5iso
TitleSTRUCTURE OF FULL LENGTH HUMAN AMPK (NON-PHOSPHORYLATED AT T-LOOP) IN COMPLEX WITH A SMALL MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE (991)
Components
  • (5'-AMP-activated protein kinase subunit ...) x 2
  • 5'-AMP-activated protein kinase catalytic subunit alpha-2
KeywordsTRANSFERASE / NUCLEOTIDE-BINDING / ACTIVATOR / NON-PHOSPHORYLATION
Function / homology
Function and homology information


nail development / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity / : / regulation of stress granule assembly / histone H2BS36 kinase activity / AMPK inhibits chREBP transcriptional activation activity / positive regulation of peptidyl-lysine acetylation / lipid droplet disassembly / Lipophagy ...nail development / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase / [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity / : / regulation of stress granule assembly / histone H2BS36 kinase activity / AMPK inhibits chREBP transcriptional activation activity / positive regulation of peptidyl-lysine acetylation / lipid droplet disassembly / Lipophagy / import into nucleus / cAMP-dependent protein kinase regulator activity / protein kinase regulator activity / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of TOR signaling / negative regulation of hepatocyte apoptotic process / Carnitine metabolism / nucleotide-activated protein kinase complex / protein localization to lipid droplet / response to muscle activity / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / Nuclear events mediated by NFE2L2 / lipid biosynthetic process / regulation of glycolytic process / cAMP-dependent protein kinase activity / negative regulation of tubulin deacetylation / Macroautophagy / AMP-activated protein kinase activity / positive regulation of protein localization / cholesterol biosynthetic process / AMP binding / cellular response to nutrient levels / positive regulation of macroautophagy / fatty acid homeostasis / regulation of macroautophagy / positive regulation of protein kinase activity / cellular response to glucose starvation / Activation of AMPK downstream of NMDARs / regulation of microtubule cytoskeleton organization / positive regulation of autophagy / energy homeostasis / negative regulation of TORC1 signaling / cellular response to calcium ion / protein serine/threonine/tyrosine kinase activity / positive regulation of glycolytic process / Translocation of SLC2A4 (GLUT4) to the plasma membrane / ADP binding / cellular response to glucose stimulus / TP53 Regulates Metabolic Genes / regulation of circadian rhythm / Wnt signaling pathway / autophagy / cytoplasmic stress granule / cellular response to prostaglandin E stimulus / fatty acid biosynthetic process / rhythmic process / cellular response to xenobiotic stimulus / glucose homeostasis / cellular response to oxidative stress / positive regulation of cold-induced thermogenesis / spermatogenesis / Regulation of TP53 Activity through Phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / nuclear speck / axon / negative regulation of gene expression / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / neuronal cell body / chromatin binding / positive regulation of gene expression / negative regulation of apoptotic process / protein kinase binding / Golgi apparatus / signal transduction / nucleoplasm / ATP binding / membrane / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
PRKAA2, UBA-like autoinhibitory domain / 5'-AMP-activated protein kinase catalytic subunit alpha-2, C-terminal / : / AMP-activated protein kinase, alpha subunit, autoinhibitory domain / Association with the SNF1 complex (ASC) domain / ASC domain superfamily / 5'-AMP-activated protein kinase beta subunit, interaction domain / 5'-AMP-activated protein kinase beta subunit, interation domain / AMPK, C-terminal adenylate sensor domain / Adenylate sensor of SNF1-like protein kinase ...PRKAA2, UBA-like autoinhibitory domain / 5'-AMP-activated protein kinase catalytic subunit alpha-2, C-terminal / : / AMP-activated protein kinase, alpha subunit, autoinhibitory domain / Association with the SNF1 complex (ASC) domain / ASC domain superfamily / 5'-AMP-activated protein kinase beta subunit, interaction domain / 5'-AMP-activated protein kinase beta subunit, interation domain / AMPK, C-terminal adenylate sensor domain / Adenylate sensor of SNF1-like protein kinase / AMP-activated protein kinase, glycogen-binding domain / Glycogen recognition site of AMP-activated protein kinase / KA1 domain/Ssp2, C-terminal / CBS domain superfamily / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain / CBS domain profile. / Immunoglobulin E-set / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Chem-992 / ADENOSINE MONOPHOSPHATE / STAUROSPORINE / 5'-AMP-activated protein kinase subunit gamma-1 / 5'-AMP-activated protein kinase catalytic subunit alpha-2 / 5'-AMP-activated protein kinase subunit beta-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.63 Å
AuthorsXiao, B. / Hubbard, J.A. / Gamblin, S.J.
CitationJournal: To Be Published
Title: STRUCTURE OF FULL LENGTH HUMAN AMPK (NON-PHOSPHORYLATED AT T-LOOP) IN COMPLEX WITH A SMALL MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE (991)
Authors: Xiao, B. / Hubbard, J.A. / Gamblin, S.J.
History
DepositionMar 15, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Mar 29, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 12, 2019Group: Data collection / Database references / Structure summary
Category: audit_author / citation_author ...audit_author / citation_author / database_PDB_rev / database_PDB_rev_record
Item: _audit_author.name / _citation_author.name
Revision 1.2Oct 16, 2019Group: Data collection / Category: reflns_shell
Revision 1.3Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 5'-AMP-activated protein kinase catalytic subunit alpha-2
B: 5'-AMP-activated protein kinase subunit beta-1
E: 5'-AMP-activated protein kinase subunit gamma-1
C: 5'-AMP-activated protein kinase catalytic subunit alpha-2
D: 5'-AMP-activated protein kinase subunit beta-1
F: 5'-AMP-activated protein kinase subunit gamma-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)268,84716
Polymers264,9676
Non-polymers3,88010
Water1,44180
1
A: 5'-AMP-activated protein kinase catalytic subunit alpha-2
B: 5'-AMP-activated protein kinase subunit beta-1
E: 5'-AMP-activated protein kinase subunit gamma-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4238
Polymers132,4833
Non-polymers1,9405
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16640 Å2
ΔGint-100 kcal/mol
Surface area42190 Å2
MethodPISA
2
C: 5'-AMP-activated protein kinase catalytic subunit alpha-2
D: 5'-AMP-activated protein kinase subunit beta-1
F: 5'-AMP-activated protein kinase subunit gamma-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4238
Polymers132,4833
Non-polymers1,9405
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16280 Å2
ΔGint-97 kcal/mol
Surface area40810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)75.420, 129.390, 139.280
Angle α, β, γ (deg.)90.00, 92.73, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AC

#1: Protein 5'-AMP-activated protein kinase catalytic subunit alpha-2 / AMPK subunit alpha-2 / Acetyl-CoA carboxylase kinase / ACACA kinase / Hydroxymethylglutaryl-CoA ...AMPK subunit alpha-2 / Acetyl-CoA carboxylase kinase / ACACA kinase / Hydroxymethylglutaryl-CoA reductase kinase / HMGCR kinase


Mass: 62408.602 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRKAA2, AMPK, AMPK2 / Production host: Escherichia coli (E. coli)
References: UniProt: P54646, non-specific serine/threonine protein kinase, [acetyl-CoA carboxylase] kinase, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase

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5'-AMP-activated protein kinase subunit ... , 2 types, 4 molecules BDEF

#2: Protein 5'-AMP-activated protein kinase subunit beta-1 / AMPKb


Mass: 32448.453 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: B 108 SER is phosphorylated, and renamed to SEP. THE 16 RESIDUES (MGLNDIFEAQKIEWHE) AT THE N-TERMINAL OF BETA-1 ARE EXPRESSION TAG
Source: (gene. exp.) Homo sapiens (human) / Gene: PRKAB1, AMPK / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y478
#3: Protein 5'-AMP-activated protein kinase subunit gamma-1 / AMPKg


Mass: 37626.289 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRKAG1 / Production host: Escherichia coli (E. coli) / References: UniProt: P54619

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Non-polymers , 4 types, 90 molecules

#4: Chemical ChemComp-STU / STAUROSPORINE / Staurosporine


Mass: 466.531 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C28H26N4O3 / Comment: anticancer, antifungal, antibiotic, alkaloid*YM
#5: Chemical ChemComp-992 / 5-[[6-chloranyl-5-(1-methylindol-5-yl)-1H-benzimidazol-2-yl]oxy]-2-methyl-benzoic acid


Mass: 431.871 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H18ClN3O3
#6: Chemical
ChemComp-AMP / ADENOSINE MONOPHOSPHATE / Adenosine monophosphate


Mass: 347.221 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 80 / 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: 2.55 Å3/Da / Density % sol: 51.79 % / Description: rods like
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 12% PEG3350, 300 mM Guanidine in 100mM PIPES buffer at pH 7.2.
PH range: 7.0-7.4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97949
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 29, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 2.63→47.37 Å / Num. obs: 78641 / % possible obs: 99.9 % / Redundancy: 3.2 % / Net I/σ(I): 14.6

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
xia2data reduction
XSCALEdata scaling
PHASER2.5.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4CFE

4cfe


Resolution: 2.63→19.974 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.35
RfactorNum. reflection% reflection
Rfree0.2296 3884 4.95 %
Rwork0.1779 --
obs0.1804 78449 99.12 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.63→19.974 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14548 0 270 80 14898
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00615193
X-RAY DIFFRACTIONf_angle_d0.84720676
X-RAY DIFFRACTIONf_dihedral_angle_d15.4689003
X-RAY DIFFRACTIONf_chiral_restr0.0522346
X-RAY DIFFRACTIONf_plane_restr0.0062556
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.63-2.6620.34811350.28292636X-RAY DIFFRACTION100
2.662-2.69560.36221590.26822709X-RAY DIFFRACTION100
2.6956-2.7310.34661310.26892654X-RAY DIFFRACTION100
2.731-2.76830.3121540.25882669X-RAY DIFFRACTION100
2.7683-2.80780.31951470.2582665X-RAY DIFFRACTION100
2.8078-2.84960.26681360.25242643X-RAY DIFFRACTION100
2.8496-2.8940.32371680.23152673X-RAY DIFFRACTION100
2.894-2.94130.28851400.22172650X-RAY DIFFRACTION100
2.9413-2.99180.24541450.21922689X-RAY DIFFRACTION100
2.9918-3.04610.34021370.22042675X-RAY DIFFRACTION100
3.0461-3.10440.26081330.22752682X-RAY DIFFRACTION100
3.1044-3.16760.25541130.2322715X-RAY DIFFRACTION100
3.1676-3.23620.28811220.21972684X-RAY DIFFRACTION100
3.2362-3.31110.29271300.21272691X-RAY DIFFRACTION100
3.3111-3.39350.2881360.21132681X-RAY DIFFRACTION100
3.3935-3.48480.21821330.20082670X-RAY DIFFRACTION100
3.4848-3.58680.27751380.19432698X-RAY DIFFRACTION100
3.5868-3.70180.23661540.18212608X-RAY DIFFRACTION99
3.7018-3.83330.23521440.17882665X-RAY DIFFRACTION99
3.8333-3.98560.22921610.16932646X-RAY DIFFRACTION99
3.9856-4.16540.22111420.15472647X-RAY DIFFRACTION99
4.1654-4.38280.23221370.15352655X-RAY DIFFRACTION99
4.3828-4.65420.18191390.14392650X-RAY DIFFRACTION98
4.6542-5.00830.17621120.13932688X-RAY DIFFRACTION98
5.0083-5.50270.20711340.15712621X-RAY DIFFRACTION98
5.5027-6.27720.23721400.17552657X-RAY DIFFRACTION97
6.2772-7.82870.22961000.16692634X-RAY DIFFRACTION96
7.8287-19.97420.15121640.13782610X-RAY DIFFRACTION95
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)
11.8567-0.45490.62548.2582-0.46151.5406-0.15630.0736-0.08520.13030.1799-0.3476-0.1925-0.1661-0.0340.46480.13550.04830.6466-0.01730.4159-44.1031-19.87084.4096
23.0018-0.00590.63433.576-0.77794.57440.0469-0.2986-0.62990.34980.29220.33180.0372-0.7625-0.30210.40140.1242-0.04350.6540.07810.6851-51.6259-39.222819.9759
35.14240.61310.75937.5026-1.39175.497-0.34270.67310.7918-1.6520.52750.10370.12660.2998-0.19870.8636-0.1549-0.09410.7614-0.01680.6152-24.6471-41.93497.9868
47.1986-1.0809-0.00152.2421-4.21029.98460.4022-1.087-0.14431.03180.05150.892-1.066-0.0346-0.51930.85240.0053-0.02860.7129-0.11690.6744-19.9192-58.254742.8087
55.39180.00050.52132.5867-0.1482.3877-0.2204-0.58950.78420.6470.0162-0.0293-0.7081-0.2710.19571.0430.2608-0.25290.6643-0.14030.622-27.6564-24.337645.0893
60.841-0.66452.37083.0912-1.62476.252-0.5314-0.30230.21980.55160.1984-0.407-0.7391-0.01230.29470.62310.1445-0.04660.612-0.01590.539-43.7456-0.09166.9132
75.1749-1.5192-0.98963.63660.60320.8869-0.1816-0.24180.02740.31760.1150.1887-0.3627-0.36750.05630.62060.1-0.13320.560.04060.4619-27.5724-38.973538.7046
85.7282-3.1767-5.32476.98483.26644.92770.1150.5771-0.1528-0.7322-0.41090.1761-0.7586-0.08240.16430.5609-0.0427-0.07910.5550.02950.4748-12.4719-46.136418.919
93.3133-3.00492.62097.7769-4.55726.0755-0.5716-0.43150.54250.8953-0.0053-0.8589-0.82270.3420.53070.67630.0558-0.22390.5608-0.01490.563-5.1984-44.623548.5082
103.9684-1.9135-1.85998.91043.78356.9255-0.17040.26720.3335-0.1383-0.0061-0.2059-0.20690.05950.20750.3795-0.0312-0.08830.41970.05860.4381-8.6746-45.843824.7624
114.0884-4.0976.10687.8367-5.62799.28490.69371.2488-1.0253-0.8847-0.1163-0.46911.82441.8795-0.39860.73760.24280.03271.1091-0.16760.74530.5284-65.272217.295
127.4636-0.5373-1.39483.73741.11676.3566-0.0282-0.0044-0.67390.29270.033-0.00760.8093-0.02590.02950.67810.0771-0.1210.41480.0640.4493-5.3121-65.688545.0444
133.0443-2.49250.34344.52080.59826.1941-0.01370.4163-0.84750.02080.1155-0.2641.21240.3326-0.15210.76080.1309-0.01280.5511-0.09280.6875-4.9698-66.850225.1996
142.97921.8274-0.19355.1584-2.61574.8702-0.28650.2799-0.10340.0677-0.0003-0.4780.5512-0.0360.29560.4985-0.1215-0.02450.5546-0.0710.515-9.0828-1.288963.7487
153.0033-0.3614-0.55672.9524-0.29943.4885-0.06660.46920.1778-0.12910.03460.2607-0.0278-0.52060.05550.3539-0.1009-0.03060.72010.04790.652-14.277916.016245.2813
161.7341.38930.92382.53460.43934.49380.681-0.1870.42571.470.0360.5712-0.2718-0.3875-0.79551.10430.20420.30720.87570.16220.975310.85923.488557.2276
179.8713-1.4062-1.57874.72484.70214.692-0.53710.7190.3544-0.80540.37951.054-1.8281-0.91890.0750.91230.17590.06470.95320.20670.844117.553937.415329.0299
186.60312.4161-0.4483.69320.31882.3597-0.29591.1559-1.17-0.48680.1672-0.19650.3904-0.37820.08140.6777-0.09440.14710.8881-0.2470.749114.15532.201124.906
191.7206-0.0401-2.28751.589-0.69462.6988-1.39770.2281-1.1379-0.42190.2905-0.51711.7428-0.44970.98021.4924-0.24780.38420.6925-0.08161.0832-8.9808-20.995364.1908
205.55161.9860.45624.2821.1583.4589-0.04370.70620.0345-0.35110.050.33120.0699-0.6882-0.00450.35540.03960.0770.73740.07410.492112.12816.955930.7531
217.29634.11794.4285.89072.93475.47310.2363-0.94370.13761.1452-0.3690.64120.7320.19520.20080.67290.13540.19430.80740.06320.449424.231726.224351.34
222.3283.7315-2.4587.9456-3.6035.3008-0.15350.4814-0.3757-0.37220.0732-0.73120.05910.44240.05740.38170.050.07620.7770.02540.49834.67624.308322.7471
233.32170.92290.29436.92511.26933.8210.0119-0.4613-0.17920.89220.0612-0.13570.00340.3254-0.04670.5040.14040.05290.66910.10080.39828.686226.122545.9983
244.14850.0743-3.60484.8859-0.03183.33781.4888-1.31131.32341.1888-0.04850.2332-1.95641.3382-1.50191.1775-0.26530.22021.3201-0.33470.865935.149346.937153.7052
255.52422.15482.33186.21852.82557.98190.03690.06690.8561-0.33730.06070.5018-1.2359-0.1105-0.05050.7490.09770.19320.61510.1760.574432.084945.249425.0313
268.72540.66942.54098.59543.01126.66570.5146-0.62721.4126-0.0789-0.1093-0.1087-0.99830.0855-0.42780.86960.02640.30750.5801-0.07990.606530.239646.590645.3644
276.95191.9947-3.5244.5431-3.68263.59411.00130.54591.3211.4949-0.5154-0.0896-1.52050.0115-0.64170.90850.10690.05620.75880.02850.7702-3.5259-56.725235.0894
289.98680.04366.39829.1273-4.47587.71531.0049-0.2175-0.5511-1.3704-0.0672-0.89191.38321.0576-0.88090.85210.01390.07490.7456-0.12240.623933.723337.176435.7347
297.85220.68883.80783.7437-1.45843.15360.60382.06950.67640.27730.1425-0.1981-0.4907-0.5703-0.33350.4620.16080.07770.76590.04210.5377-52.3559-25.9326.5292
304.7158-2.7096-1.62035.2945-0.22241.15890.6071-0.4331-0.3678-0.3430.0826-0.10840.8126-1.3481-0.50.3758-0.1863-0.04420.5915-0.01160.4962-16.51394.034659.7093
311.86353.1950.29385.55680.78271.1901-0.2211-1.41051.13220.85690.35610.5675-0.6685-0.5204-0.28450.69610.29280.26740.8532-0.19480.812-51.2102-10.97815.0351
327.0876-0.3936-3.85917.7511-4.10884.5115-0.26210.7604-1.5504-0.0699-0.3156-0.39093.755-3.03070.94460.9203-0.4894-0.04670.9108-0.02240.9313-15.9442-10.627663.0688
33-0.14160.0528-0.08490.2041-0.02760.0184-0.00270.0857-0.0808-0.02570.0028-0.07470.04440.06760.00920.30320.0248-0.11290.47230.04570.309-13.6473-10.20841.3848
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 9:100)
2X-RAY DIFFRACTION2(chain A and resid 101:276)
3X-RAY DIFFRACTION3(chain A and resid 277:346)
4X-RAY DIFFRACTION4(chain A and resid 363:377)
5X-RAY DIFFRACTION5(chain A and resid 397:551)
6X-RAY DIFFRACTION6(chain B and resid 77:193)
7X-RAY DIFFRACTION7(chain B and resid 201:270)
8X-RAY DIFFRACTION8(chain E and resid 27:47)
9X-RAY DIFFRACTION9(chain E and resid 48:128)
10X-RAY DIFFRACTION10(chain E and resid 129:183)
11X-RAY DIFFRACTION11(chain E and resid 184:203)
12X-RAY DIFFRACTION12(chain E and resid 204:274)
13X-RAY DIFFRACTION13(chain E and resid 275:324)
14X-RAY DIFFRACTION14(chain C and resid 9:100)
15X-RAY DIFFRACTION15(chain C and resid 101:276)
16X-RAY DIFFRACTION16(chain C and resid 277:345)
17X-RAY DIFFRACTION17(chain C and resid 363:374)
18X-RAY DIFFRACTION18(chain C and resid 396:550)
19X-RAY DIFFRACTION19(chain D and resid 78:193)
20X-RAY DIFFRACTION20(chain D and resid 202:270)
21X-RAY DIFFRACTION21(chain F and resid 27:47)
22X-RAY DIFFRACTION22(chain F and resid 48:128)
23X-RAY DIFFRACTION23(chain F and resid 129:183)
24X-RAY DIFFRACTION24(chain F and resid 184:203)
25X-RAY DIFFRACTION25(chain F and resid 204:274)
26X-RAY DIFFRACTION26(chain F and resid 275:325)
27X-RAY DIFFRACTION27(chain G and resid 1:4)
28X-RAY DIFFRACTION28(chain H and resid 1:4)
29X-RAY DIFFRACTION29(chain I and resid 1:1)
30X-RAY DIFFRACTION30(chain J and resid 1:1)
31X-RAY DIFFRACTION31(chain K and resid 1:1)
32X-RAY DIFFRACTION32(chain L and resid 1:1)
33X-RAY DIFFRACTION33(chain W and resid 1:80)

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