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- PDB-3qbv: Structure of designed orthogonal interaction between CDC42 and nu... -

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Basic information

Entry
Database: PDB / ID: 3qbv
TitleStructure of designed orthogonal interaction between CDC42 and nucleotide exchange domains of intersectin
Components
  • Cell division control protein 42 homolog
  • Intersectin-1
KeywordsPROTEIN BINDING/SIGNALING PROTEIN / Computationally designed / orthogonal interaction / GTPase / nucleotide exchange / cell membrane / GTP-binding / lipoprotein / membrane / methylation / nucleotide-binding / prenylation / cell junction / cell projection / endocytosis / phosphoprotein / SH3 domain / synapse / synaptosome / protein binding-signaling protein complex
Function / homology
Function and homology information


clathrin-dependent synaptic vesicle endocytosis / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction / cardiac neural crest cell migration involved in outflow tract morphogenesis ...clathrin-dependent synaptic vesicle endocytosis / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction / cardiac neural crest cell migration involved in outflow tract morphogenesis / positive regulation of synapse structural plasticity / dendritic cell migration / storage vacuole / apolipoprotein A-I receptor binding / positive regulation of epithelial cell proliferation involved in lung morphogenesis / neuron fate determination / modulation by host of viral process / organelle transport along microtubule / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly / Inactivation of CDC42 and RAC1 / cardiac conduction system development / GTP-dependent protein binding / regulation of filopodium assembly / establishment of Golgi localization / leading edge membrane / neuropilin signaling pathway / positive regulation of intracellular protein transport / cell junction assembly / filopodium assembly / establishment of epithelial cell apical/basal polarity / regulation of modification of postsynaptic structure / dendritic spine morphogenesis / mitogen-activated protein kinase kinase kinase binding / embryonic heart tube development / thioesterase binding / regulation of stress fiber assembly / RHO GTPases activate KTN1 / regulation of lamellipodium assembly / proline-rich region binding / nuclear migration / DCC mediated attractive signaling / adherens junction organization / sprouting angiogenesis / Wnt signaling pathway, planar cell polarity pathway / regulation of small GTPase mediated signal transduction / CD28 dependent Vav1 pathway / regulation of postsynapse organization / positive regulation of filopodium assembly / endosomal transport / regulation of mitotic nuclear division / establishment or maintenance of cell polarity / phagocytosis, engulfment / RHOV GTPase cycle / intracellular vesicle / NRAGE signals death through JNK / heart contraction / Myogenesis / RHOJ GTPase cycle / Golgi organization / RHOQ GTPase cycle / exocytosis / positive regulation of cytokinesis / RHO GTPases activate PAKs / CDC42 GTPase cycle / RHOU GTPase cycle / macrophage differentiation / RHOG GTPase cycle / RHO GTPases Activate WASPs and WAVEs / RAC3 GTPase cycle / RAC2 GTPase cycle / RHO GTPases activate IQGAPs / spindle midzone / negative regulation of protein-containing complex assembly / phagocytic vesicle / positive regulation of lamellipodium assembly / positive regulation of substrate adhesion-dependent cell spreading / clathrin-coated pit / positive regulation of stress fiber assembly / GPVI-mediated activation cascade / RAC1 GTPase cycle / EPHB-mediated forward signaling / substantia nigra development / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / guanyl-nucleotide exchange factor activity / small monomeric GTPase / G protein activity / filopodium / positive regulation of DNA replication / secretory granule / actin filament organization / integrin-mediated signaling pathway / RHO GTPases Activate Formins / regulation of actin cytoskeleton organization / FCGR3A-mediated phagocytosis / EGFR downregulation / positive regulation of JNK cascade / MAPK6/MAPK4 signaling / Schaffer collateral - CA1 synapse / protein localization
Similarity search - Function
Intersectin-1, AP2 binding region / Intersectin and clathrin adaptor AP2 binding region / Pleckstrin homology domain / Cdc42 / Cytoskeletal-regulatory complex EF hand / EH domain profile. / Eps15 homology domain / EH domain / Dbl Homology Domain; Chain A / Dbl homology (DH) domain ...Intersectin-1, AP2 binding region / Intersectin and clathrin adaptor AP2 binding region / Pleckstrin homology domain / Cdc42 / Cytoskeletal-regulatory complex EF hand / EH domain profile. / Eps15 homology domain / EH domain / Dbl Homology Domain; Chain A / Dbl homology (DH) domain / Guanine-nucleotide dissociation stimulator, CDC24, conserved site / Dbl homology (DH) domain signature. / Variant SH3 domain / Variant SH3 domain / Small GTPase Rho / small GTPase Rho family profile. / Dbl homology (DH) domain superfamily / RhoGEF domain / Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases / Dbl homology (DH) domain / Dbl homology (DH) domain profile. / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / C2 domain superfamily / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / SH3 domain / Small GTPase / Ras family / Rab subfamily of small GTPases / EF-hand, calcium binding motif / Src homology 3 domains / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / EF-hand domain / EF-hand domain pair / Small GTP-binding protein domain / PH-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Roll / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Cell division control protein 42 homolog / Intersectin-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å
AuthorsKapp, G.T. / Remenyi, A. / Lim, W.A. / Kortemme, T.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2012
Title: Control of protein signaling using a computationally designed GTPase/GEF orthogonal pair.
Authors: Kapp, G.T. / Liu, S. / Stein, A. / Wong, D.T. / Remenyi, A. / Yeh, B.J. / Fraser, J.S. / Taunton, J. / Lim, W.A. / Kortemme, T.
History
DepositionJan 14, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 8, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2012Group: Database references
Revision 1.2Apr 18, 2012Group: Database references
Revision 1.3Apr 25, 2012Group: Database references
Revision 1.4Sep 13, 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_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cell division control protein 42 homolog
B: Intersectin-1
C: Cell division control protein 42 homolog
D: Intersectin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,9286
Polymers121,0424
Non-polymers8862
Water2,072115
1
A: Cell division control protein 42 homolog
B: Intersectin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,9643
Polymers60,5212
Non-polymers4431
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2820 Å2
ΔGint-18 kcal/mol
Surface area24270 Å2
MethodPISA
2
C: Cell division control protein 42 homolog
D: Intersectin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,9643
Polymers60,5212
Non-polymers4431
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3010 Å2
ΔGint-16 kcal/mol
Surface area23530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.460, 80.062, 94.591
Angle α, β, γ (deg.)90.00, 108.23, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11B
21D
12A
22C

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'B' and (resseq 1229:1443 or resseq 1450:1469 or resseq 1562:1578 )
211chain 'D' and (resseq 1229:1443 or resseq 1450:1469 or resseq 1562:1578 )
112chain 'A' and (resseq 1:29 or resseq 31:178 )
212chain 'C' and (resseq 1:29 or resseq 31:178 )

NCS ensembles :
ID
1
2

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Components

#1: Protein Cell division control protein 42 homolog / G25K GTP-binding protein


Mass: 19784.725 Da / Num. of mol.: 2 / Fragment: UNP Residues 1-178 / Mutation: F56R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDC42 / Plasmid: PGKC006 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA2 / References: UniProt: P60953
#2: Protein Intersectin-1 / SH3 domain-containing protein 1A / SH3P17


Mass: 40736.305 Da / Num. of mol.: 2 / Fragment: DH AND PH DOMAINS (UNP Residues 1229-1571) / Mutation: S1373E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITSN1, ITSN, SH3D1A / Plasmid: PGKI009 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA2 / References: UniProt: Q15811
#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 115 / 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: 2.54 Å3/Da / Density % sol: 51.56 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 100mm TRIS pH 7.5, 25% PEG 3350, 150mm ammonium sulfate, and 1mM DTT, temperature 295k, VAPOR DIFFUSION, HANGING DROP

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.115872
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 29, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.115872 Å / Relative weight: 1
ReflectionResolution: 2.65→50 Å / Num. obs: 35386 / Redundancy: 3.9 % / Rsym value: 0.069 / Net I/σ(I): 20
Reflection shellResolution: 2.65→2.74 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 2.7 / Rsym value: 0.412 / % possible all: 97

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Processing

Software
NameVersionClassification
AMoREphasing
PHENIXdev_847refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1KI1

1ki1


Resolution: 2.65→45.848 Å / SU ML: 0.9 / Isotropic thermal model: ISOTROPIC / σ(F): 1.35 / Phase error: 28.88 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2842 3499 9.91 %
Rwork0.2411 --
obs0.2456 35295 99.6 %
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.111 Å2 / ksol: 0.324 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--5.7378 Å2-0 Å20.1387 Å2
2---5.0701 Å2-0 Å2
3---10.8079 Å2
Refinement stepCycle: LAST / Resolution: 2.65→45.848 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6897 0 56 115 7068
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0067070
X-RAY DIFFRACTIONf_angle_d1.0019625
X-RAY DIFFRACTIONf_dihedral_angle_d15.2162466
X-RAY DIFFRACTIONf_chiral_restr0.0651139
X-RAY DIFFRACTIONf_plane_restr0.0051246
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11B1822X-RAY DIFFRACTIONPOSITIONAL0.024
12D1822X-RAY DIFFRACTIONPOSITIONAL0.024
21A1270X-RAY DIFFRACTIONPOSITIONAL0.02
22C1270X-RAY DIFFRACTIONPOSITIONAL0.02
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.65-2.68630.32031240.3051207X-RAY DIFFRACTION95
2.6863-2.72470.33421290.27231229X-RAY DIFFRACTION97
2.7247-2.76540.35191400.30771277X-RAY DIFFRACTION100
2.7654-2.80860.37361150.28091271X-RAY DIFFRACTION99
2.8086-2.85460.29021410.26781302X-RAY DIFFRACTION100
2.8546-2.90380.37791110.26341242X-RAY DIFFRACTION100
2.9038-2.95660.30821490.26621304X-RAY DIFFRACTION100
2.9566-3.01350.33141380.24481250X-RAY DIFFRACTION100
3.0135-3.0750.34991400.25561270X-RAY DIFFRACTION100
3.075-3.14180.29521380.24291268X-RAY DIFFRACTION100
3.1418-3.21490.3111250.25141278X-RAY DIFFRACTION100
3.2149-3.29530.33211650.26221247X-RAY DIFFRACTION100
3.2953-3.38430.30451460.24531284X-RAY DIFFRACTION100
3.3843-3.48390.30311190.2511301X-RAY DIFFRACTION100
3.4839-3.59630.25011430.21881254X-RAY DIFFRACTION100
3.5963-3.72480.27251480.2371260X-RAY DIFFRACTION100
3.7248-3.87380.27041600.22441278X-RAY DIFFRACTION100
3.8738-4.050.25441530.21221253X-RAY DIFFRACTION100
4.05-4.26340.2461400.21211285X-RAY DIFFRACTION100
4.2634-4.53030.26761650.21221259X-RAY DIFFRACTION100
4.5303-4.87970.21521460.21731269X-RAY DIFFRACTION100
4.8797-5.37010.27651310.2171295X-RAY DIFFRACTION100
5.3701-6.14560.38261660.30191268X-RAY DIFFRACTION100
6.1456-7.73680.28981350.28431314X-RAY DIFFRACTION100
7.7368-45.85430.23941320.22091331X-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)
10.02950.0042-0.02090.0211-0.01670.1035-0.10420.00220.0463-0.05770.0106-0.033-0-0.0748-0.09110.33690.027-0.05580.329-0.13220.194833.485113.941330.299
20.00810.00250.00510.0108-0.00430.0034-0.0033-0.01610.03130.08620.06150.02070.07590.00090.00010.2661-0.05730.1120.3719-0.0820.609232.53414.541739.6208
30.1457-0.04230.13390.0141-0.03630.1256-0.13790.0170.1575-0.0135-0.07430.0363-0.0593-0.0095-0.01570.25240.00340.0190.2960.01460.263727.490125.475227.655
40.0116-0.0077-0.01240.01390.01230.0394-0.03140.0559-0.0005-0.0653-0.0486-0.0243-0.0044-0.0306-0.10950.2679-0.10690.06490.2746-0.17770.142932.485.208625.2115
50.0135-0.0288-0.0360.15060.02310.1125-0.04490.06040.0073-0.01570.0762-0.14080.04870.1146-0.15050.2954-0.08140.13720.3483-0.12620.083441.00288.099221.9921
60.020.0131-0.00250.0178-0.01060.0093-0.11260.0790.01650.13170.0039-0.4527-0.12230.1179-0.00090.2967-0.02790.05940.4181-0.15380.53349.674712.450925.0645
70.0017-0.00310.0010.0027-0.00430.0075-0.0230.10180.077-0.01970.0527-0.0064-0.0068-0.0049-00.1966-0.04860.02710.19970.00730.142134.917723.122123.0368
80.2096-0.04820.05620.07970.05470.34390.24010.088-0.1340.05040.20550.0762-0.0511-0.32630.18070.0726-0.0291-0.0172-0.1008-0.15940.037219.56721.322536.9501
90.0520.002-0.0260.0494-0.04590.05890.05630.0484-0.0572-0.0149-0.04440.06690.0336-0.02390.04230.41960.1246-0.31150.4397-0.43850.843116.1875-20.38999.4201
100.1040.0244-0.05280.01010.01520.1350.08070.08390.0389-0.0880.01450.0014-0.0190.00920.05090.49750.01920.00920.9291-0.51780.555124.8308-12.31710.8437
110.13950.08990.08870.16120.13560.1329-0.0950.1375-0.0847-0.0923-0.03250.02810.0959-0.03470.00810.3980.1955-0.02680.7191-0.39280.44828.0636-16.53622.5799
120.01330.0045-0.00130.0679-0.0280.0119-0.0884-0.0155-0.0273-0.01130.0019-0.0161-0.0340.0248-0.1310.3740.06530.01090.34190.20460.1392-20.253-30.907330.3482
130.0101-0.00410.0010.01280.00530.0049-0.0337-0.019-0.02370.1001-0.01210.07210.04170.0043-0.00010.2789-0.0749-0.1280.3931-0.02720.675-19.1881-31.378539.681
140.0018-0.005-0.00050.00510.0026-0.0009-0.05120.0574-0.1222-0.0139-0.0946-0.03930.1152-0.0087-0.00010.24220.05480.02210.20410.01590.2026-14.2579-42.435627.6758
150.13070.01020.01330.0199-0.02470.033-0.12950.07180.0586-0.0989-0.0752-0.07240.14620.0621-0.38520.1943-0.0545-0.01460.24680.27530.1565-19.1312-22.145325.2072
160.2541-0.3922-0.26380.61340.41410.6487-0.12750.0927-0.0372-0.0515-0.00420.2160.0052-0.1282-0.32850.3523-0.0254-0.14970.43210.21870.1768-27.6896-25.185321.8366
170.00290.0014-0.00160.0049-0.00460.00370.031-0.0210.0258-0.02390.0118-0.00650.0192-0.012-0.00010.22130.0412-0.02010.36320.15290.682-44.6287-21.655731.5241
180.00110.00070.0011-0.00030.00050.0019-0.03310.0074-0.04560.0157-0.02260.050.0237-0.034800.6229-0.0487-0.30340.71120.0130.6475-35.482-30.705815.8447
190.13210.0167-0.00230.00940.00730.0177-0.05550.234-0.17360.03580.08310.18870.118-0.04110.00790.2372-0.0045-0.0050.21230.05330.162-26.2455-37.91525.4111
200.01930.01470.01830.00480.01530.02830.0378-0.0402-0.07490.1452-0.07470.12720.06490.0442-0.00010.2181-0.0413-0.01280.18510.07570.3064-13.0776-23.347148.1075
210.2094-0.0159-0.28090.0020.02280.37890.0996-0.10930.0586-0.00910.0971-0.1381-0.11080.00440.11360.2068-0.066-0.12170.2297-0.03530.31339.483-22.38727.3266
220.023-0.0150.00950.0551-0.03870.03760.0457-0.1010.00920.23230.0044-0.10990.00190.1662-0.00250.1858-0.02830.01390.19750.03630.1996-7.3307-14.80150.2779
230.016-0.00170.00440.01130.00890.00360.10110.14850.0342-0.00230.08630.21090.0344-0.01140.00040.33110.0208-0.07160.27830.10130.2745-0.8129-17.894724.2489
240.06080.03460.01190.020.01440.0412-0.00830.0435-0.1824-0.04160.0772-0.06360.02850.024700.25150.06880.02550.13540.01860.21443.4735-34.730528.2886
250.0453-0.02340.03570.0112-0.01950.0246-0.0430.0602-0.02610.0899-0.0490.0528-0.00620.0741-00.1210.0257-0.00510.15260.01660.1946-15.9459-17.234341.1177
260.10.02910.01030.00230.0070.14120.00790.1280.14410.0415-0.0405-0.0205-0.21790.0904-0.08350.236-0.01120.04330.14210.17570.3368-10.2543-6.983128.23
270.0085-00.01120.0081-0.00360.0087-0.06550.02770.01350.0142-0.01540.0539-0.0958-0.0187-0.00010.7532-0.01930.07980.6480.25880.6529-6.7646-0.27998.3955
28-0.0004-0.00080.00040.005-0.00580.00520.00570.04620.00470.0166-0.03440.0044-0.0050.02010.00010.83550.10560.12840.7580.12420.4322-9.4366-0.28314.2034
290.00040.00090.00330.00010.00260.0042-0.02950.0372-0.0287-0.06280.05260.04620.15420.0337-0.00880.94640.117-0.22560.69630.21840.6382-10.1235-2.72531.3589
300.00460.00790.00580.02820.0130.00730.0639-0.00210.005-0.00190.02450.0074-0.0292-0.00290.00011.17770.216-0.03621.2870.24811.3021-19.36548.113512.0119
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:24)
2X-RAY DIFFRACTION2chain 'A' and (resseq 25:40)
3X-RAY DIFFRACTION3chain 'A' and (resseq 41:56)
4X-RAY DIFFRACTION4chain 'A' and (resseq 57:86)
5X-RAY DIFFRACTION5chain 'A' and (resseq 87:122)
6X-RAY DIFFRACTION6chain 'A' and (resseq 123:164)
7X-RAY DIFFRACTION7chain 'A' and (resseq 165:178)
8X-RAY DIFFRACTION8chain 'B' and (resseq 1229:1439)
9X-RAY DIFFRACTION9chain 'B' and (resseq 1440:1462)
10X-RAY DIFFRACTION10chain 'B' and (resseq 1463:1490)
11X-RAY DIFFRACTION11chain 'B' and (resseq 1491:1578)
12X-RAY DIFFRACTION12chain 'C' and (resseq 1:24)
13X-RAY DIFFRACTION13chain 'C' and (resseq 25:40)
14X-RAY DIFFRACTION14chain 'C' and (resseq 41:56)
15X-RAY DIFFRACTION15chain 'C' and (resseq 57:86)
16X-RAY DIFFRACTION16chain 'C' and (resseq 87:122)
17X-RAY DIFFRACTION17chain 'C' and (resseq 123:138)
18X-RAY DIFFRACTION18chain 'C' and (resseq 139:149)
19X-RAY DIFFRACTION19chain 'C' and (resseq 150:178)
20X-RAY DIFFRACTION20chain 'D' and (resseq 1229:1262)
21X-RAY DIFFRACTION21chain 'D' and (resseq 1263:1284)
22X-RAY DIFFRACTION22chain 'D' and (resseq 1285:1326)
23X-RAY DIFFRACTION23chain 'D' and (resseq 1327:1349)
24X-RAY DIFFRACTION24chain 'D' and (resseq 1350:1370)
25X-RAY DIFFRACTION25chain 'D' and (resseq 1371:1402)
26X-RAY DIFFRACTION26chain 'D' and (resseq 1403:1439)
27X-RAY DIFFRACTION27chain 'D' and (resseq 1440:1479)
28X-RAY DIFFRACTION28chain 'D' and (resseq 1480:1492)
29X-RAY DIFFRACTION29chain 'D' and (resseq 1493:1562)
30X-RAY DIFFRACTION30chain 'D' and (resseq 1563:1579)

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