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- PDB-6vpm: TPX2 residues 7-20 fused to Aurora A residues 116-389 with C290 d... -

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Basic information

Entry
Database: PDB / ID: 6vpm
TitleTPX2 residues 7-20 fused to Aurora A residues 116-389 with C290 disulfide bonded to compound 8-34, and in complex with AMP-PNP
ComponentsTPX2 fragment - Aurora A kinase domain fusion
KeywordsTRANSFERASE / Ser/Thr kinase
Function / homology
Function and homology information


importin-alpha family protein binding / Interaction between PHLDA1 and AURKA / activation of protein kinase activity / regulation of centrosome cycle / negative regulation of microtubule depolymerization / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / spindle pole centrosome / chromosome passenger complex ...importin-alpha family protein binding / Interaction between PHLDA1 and AURKA / activation of protein kinase activity / regulation of centrosome cycle / negative regulation of microtubule depolymerization / axon hillock / spindle assembly involved in female meiosis I / cilium disassembly / spindle pole centrosome / chromosome passenger complex / microtubule nucleation / positive regulation of oocyte maturation / pronucleus / mitotic centrosome separation / germinal vesicle / meiotic spindle / protein localization to centrosome / anterior/posterior axis specification / centrosome localization / neuron projection extension / spindle organization / positive regulation of mitochondrial fission / mitotic spindle pole / SUMOylation of DNA replication proteins / mitotic spindle assembly / spindle midzone / intercellular bridge / regulation of G2/M transition of mitotic cell cycle / negative regulation of protein binding / centriole / protein serine/threonine/tyrosine kinase activity / positive regulation of mitotic nuclear division / positive regulation of mitotic cell cycle / regulation of mitotic spindle organization / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / molecular function activator activity / AURKA Activation by TPX2 / liver regeneration / regulation of cytokinesis / regulation of signal transduction by p53 class mediator / mitotic spindle organization / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / regulation of protein stability / kinetochore / response to wounding / spindle / spindle pole / G2/M transition of mitotic cell cycle / mitotic spindle / Regulation of PLK1 Activity at G2/M Transition / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / mitotic cell cycle / peptidyl-serine phosphorylation / microtubule cytoskeleton / midbody / protein autophosphorylation / basolateral plasma membrane / molecular adaptor activity / Regulation of TP53 Activity through Phosphorylation / microtubule / proteasome-mediated ubiquitin-dependent protein catabolic process / eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / non-specific serine/threonine protein kinase / protein kinase activity / postsynaptic density / ciliary basal body / protein phosphorylation / protein heterodimerization activity / cell division / negative regulation of gene expression / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / centrosome / ubiquitin protein ligase binding / negative regulation of apoptotic process / protein kinase binding / perinuclear region of cytoplasm / glutamatergic synapse / nucleoplasm
Similarity search - Function
TPX2 / Aurora-A binding / TPX2, C-terminal / TPX2 central domain / Targeting protein for Xklp2 (TPX2) domain / Aurora-A binding / Cell cycle regulated microtubule associated protein / Aurora kinase A / Aurora kinase / Transferase(Phosphotransferase) domain 1 ...TPX2 / Aurora-A binding / TPX2, C-terminal / TPX2 central domain / Targeting protein for Xklp2 (TPX2) domain / Aurora-A binding / Cell cycle regulated microtubule associated protein / Aurora kinase A / Aurora kinase / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / 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. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / MALONIC ACID / Chem-R74 / Aurora kinase A / Targeting protein for Xklp2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.58 Å
AuthorsLim, D.C. / Yaffe, M.B.
Funding support United States, 4items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)ES015339 United States
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)ES028374 United States
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)ES020466 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM104047 United States
CitationJournal: Sci.Signal. / Year: 2020
Title: Redox priming promotes Aurora A activation during mitosis.
Authors: Lim, D.C. / Joukov, V. / Rettenmaier, T.J. / Kumagai, A. / Dunphy, W.G. / Wells, J.A. / Yaffe, M.B.
History
DepositionFeb 3, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 5, 2020Provider: repository / Type: Initial release
Revision 1.1Apr 3, 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
Revision 1.2Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TPX2 fragment - Aurora A kinase domain fusion
B: TPX2 fragment - Aurora A kinase domain fusion
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,67110
Polymers67,9732
Non-polymers1,6988
Water9,044502
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6610 Å2
ΔGint-62 kcal/mol
Surface area25010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)50.730, 85.769, 152.492
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein TPX2 fragment - Aurora A kinase domain fusion / Targeting protein for Xklp2 / Aurora kinase A / Differentially expressed in cancerous and non- ...Targeting protein for Xklp2 / Aurora kinase A / Differentially expressed in cancerous and non-cancerous lung cells 2 / DIL-2 / Hepatocellular carcinoma-associated antigen 519 / Hepatocellular carcinoma-associated antigen 90 / Protein fls353 / Restricted expression proliferation-associated protein 100 / p100 / Aurora 2 / Aurora/IPL1-related kinase 1 / hARK1 / Breast tumor-amplified kinase / Serine/threonine-protein kinase 15 / Serine/threonine-protein kinase 6 / Serine/threonine-protein kinase aurora-A


Mass: 33986.734 Da / Num. of mol.: 2 / Fragment: kinase domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: TPX2, C20orf1, C20orf2, DIL2, HCA519, AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2
References: UniProt: Q9ULW0, UniProt: O14965, non-specific serine/threonine protein kinase

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Non-polymers , 5 types, 510 molecules

#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-AMP / ADENOSINE MONOPHOSPHATE


Mass: 347.221 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#4: Chemical ChemComp-R74 / N~2~-[(2H-1,3-benzodioxol-5-yl)acetyl]-N-[(pyridin-4-yl)methyl]-L-cysteinamide


Mass: 373.426 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H19N3O4S
#5: Chemical ChemComp-MLA / MALONIC ACID / DICARBOXYLIC ACID C3 / PROPANEDIOLIC ACID / METHANEDICARBOXYLIC ACID


Mass: 104.061 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 502 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.44 Å3/Da / Density % sol: 49.6 % / Mosaicity: 0.441 °
Crystal growTemperature: 298 K / Method: evaporation / pH: 5.5
Details: 0.1 M sodium malonate pH 5.5, 7.5% PEG 3350, 11% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å
DetectorType: RIGAKU SATURN 944 / Detector: CCD / Date: Mar 27, 2013 / Details: mirrors
RadiationMonochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.58→50 Å / Num. obs: 81955 / % possible obs: 89.2 % / Redundancy: 11.3 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 21.9
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.58-1.643.80.61272430.6990.350.7150.67280
1.64-1.74.40.46672480.8510.2430.5320.71180.1
1.7-1.785.50.31874330.9320.1440.3520.79781.9
1.78-1.876.80.25777010.9740.1020.2780.83484.6
1.87-1.998.90.17184150.9880.0570.1811.13892.4
1.99-2.1411.30.1385570.9930.0390.1360.99793.7
2.14-2.3613.40.11385630.9960.0310.1171.08893.4
2.36-2.717.50.09188380.9970.0210.0931.04895.8
2.701-3.418.70.06389750.9990.0140.0651.03696.5
3.403-5018.80.04589820.9990.010.0461.01693.1

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
SCALEPACKdata scaling
PDB_EXTRACT3.25data extraction
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: D_1000246826

Resolution: 1.58→22.87 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 21.67
RfactorNum. reflection% reflection
Rfree0.203 2000 2.44 %
Rwork0.17 --
obs0.17 81814 89.2 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 33.14 Å2
Refinement stepCycle: LAST / Resolution: 1.58→22.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4550 0 114 502 5166
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.58-1.620.26131260.23815029X-RAY DIFFRACTION80
1.62-1.660.22611250.22054999X-RAY DIFFRACTION80
1.66-1.710.26521290.21025144X-RAY DIFFRACTION81
1.71-1.770.26921290.2015135X-RAY DIFFRACTION82
1.77-1.830.25091310.20895277X-RAY DIFFRACTION83
1.83-1.910.26591390.23195505X-RAY DIFFRACTION86
1.91-1.990.21281490.17795966X-RAY DIFFRACTION94
1.99-2.10.19581490.1675954X-RAY DIFFRACTION94
2.1-2.230.20871490.16385950X-RAY DIFFRACTION93
2.23-2.40.18841500.16895957X-RAY DIFFRACTION93
2.4-2.640.2051540.17426137X-RAY DIFFRACTION96
2.64-3.020.21761570.17756260X-RAY DIFFRACTION97
3.02-3.810.18581560.1616229X-RAY DIFFRACTION96
3.81-22.870.18471570.15066272X-RAY DIFFRACTION93
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)
10.1536-0.2197-0.0150.3540.10021.0213-0.0171-0.2488-0.3699-00.045-0.0629-0.207-0.15040.06560.21170.0287-0.10370.24750.02190.4239-11.832931.4041-25.4786
21.0680.01270.98991.77480.41240.7865-0.1086-0.12090.0814-0.00730.08420.0792-0.066-0.0810.00010.16550.00970.00960.1750.0220.1745-11.07823.8994-27.1469
30.6604-0.00650.10080.00020.0850.4131-0.1294-0.21070.4275-0.52410.16310.6488-0.3049-0.36030.01370.30970.0086-0.12320.24320.03410.4063-30.408716.9243-43.3919
40.63010.23540.45980.67570.25870.2914-0.1508-0.1005-0.0676-0.19350.171-0.06150.0944-0.02430.00370.2517-0.03990.00280.21350.01450.1836-13.35539.3547-41.7763
50.41540.4980.00290.57680.44270.7792-0.0263-0.1021-0.0481-0.0302-0.05410.0562-0.01870.3043-0.00010.2408-0.0115-0.00870.23460.0310.2155-14.992614.4058-35.6589
60.0214-0.0244-0.12780.228-0.05410.2680.08810.01610.18740.07480.035-0.2301-0.16970.3479-00.34510.02680.00750.3410.01580.2959-3.7187-10.9937-24.3839
70.55790.706-0.00680.93250.22290.555-0.1228-0.0953-0.0441-0.0040.0769-0.03410.06270.07180.00010.2348-0.0086-0.02050.19880.01550.1922-23.14612.4076-37.5869
80.0927-0.00170.01220.1182-0.08030.0478-0.40840.0952-0.09060.3860.1620.66010.6371-0.08360.00020.26720.0060.02420.26390.03880.3314-31.1853-3.3969-30.0083
90.8631.0566-0.40990.9125-0.06610.6298-0.22930.1082-0.3481-0.40660.1743-0.03860.26980.0376-0.05950.3364-0.0344-0.01350.2178-0.01670.2452-24.0349-3.6091-45.3685
100.36620.4707-0.03120.6393-0.18290.2503-0.31320.5276-0.0869-0.90390.2646-0.24760.03130.16970.00570.5092-0.13610.06550.3552-0.02050.2009-15.38545.7527-53.4605
110.0097-0.0068-0.03190.01540.02610.0421-0.4514-0.1489-0.47740.41960.0542-0.0870.30930.45930.00090.3190.0918-0.02080.28860.04030.245-4.536119.1672-15.7809
120.09180.046-0.00080.10020.04020.0061-0.2180.16030.1684-0.2575-0.0708-1.0687-0.04140.1747-0.00310.2585-0.02820.03560.26010.0960.3686-0.384128.9126-31.2771
130.1022-0.0023-0.17670.5258-0.30650.6312-0.0335-0.08490.10450.4706-0.2542-0.5164-0.7060.312-0.13920.4397-0.0675-0.17790.322-0.00940.461913.120212.5967-1.1838
140.99780.52-0.4481.7505-1.52691.2793-0.12010.04920.0035-0.0645-0.5717-1.17-0.21920.4241-0.96140.30290.0099-0.1210.29050.04260.432215.90941.047-5.1029
150.22630.61790.19011.5089-0.11640.1766-0.03070.03330.0268-0.1077-0.0073-0.17360.02140.0315-0.00010.21540.0190.01490.21120.0150.21796.18585.5961-14.5744
160.1819-0.2189-0.11170.23480.06240.0844-0.0303-0.10190.02280.3193-0.0415-0.048-0.1614-0.082400.2165-0.013-0.02910.21120.0140.20061.53732.9296-3.8025
170.0970.14330.18950.1951-0.03870.3503-0.0345-0.07240.00280.4148-0.0528-0.6724-0.15230.1573-0.00190.1805-0.0109-0.03930.24430.04310.314410.98031.8032-7.2521
180.55410.1813-0.00650.3937-0.1910.84080.044-0.04-0.01830.0361-0.04690.03680.00650.0769-00.09670.01060.00150.16340.02210.1594-2.3824-16.6364-5.0892
190.05440.08880.00570.1473-0.10270.0814-0.2013-0.0835-0.0656-0.11820.2180.06040.08850.0534-0.00020.21840.02870.00030.24160.0350.2037-6.6643-5.4575-14.3058
200.22250.3394-0.23730.3645-0.23890.0840.106-0.0079-0.02650.01210.0479-0.0714-0.16950.07040.00850.2310.0237-0.01120.22180.02770.198-0.6437-6.7048-9.2333
210.15590.22410.03990.1870.01320.2253-0.1917-0.33530.12380.4940.12840.3976-0.22030.10030.00020.3140.0165-0.01580.33910.01460.3384-22.62832.6686-27.9466
220.1350.20240.11080.2566-0.03690.7944-0.04710.0677-0.01350.02570.00270.1778-0.14580.00740.00010.19720.0036-0.00010.25070.03170.1996-9.0293-14.8272-15.2765
230.14490.16830.11890.15440.09390.20190.17760.0429-0.2971-0.2498-0.1027-0.25190.28850.25790.03480.24970.08810.05460.34470.00380.2345-0.6676-24.1703-22.5951
240.42430.0559-0.01660.9643-0.01680.02320.0560.5510.1583-0.03140.2327-0.4527-0.0957-0.03730.0110.43620.12770.01890.4128-0.03340.2364-5.2559-20.7553-29.2848
250.1534-0.155-0.07080.1710.14260.10030.04850.1569-0.2234-0.3258-0.17390.17460.6051-0.16320.00060.32290.0195-0.00450.2679-0.01540.2542-9.3087-29.5582-18.712
260.00280.0203-0.02980.08150.04580.09820.07810.092-0.2227-0.1997-0.11080.65210.2287-0.2391-0.00040.1856-0.03280.00770.2623-0.03470.2958-14.578-25.5874-11
270.0716-0.02270.06780.0914-0.00740.05420.12820.404-0.211-0.2463-0.13840.3092-0.052-0.6634-0.00010.22520.0731-0.03120.37420.00870.2337-18.4906-15.2263-17.2823
280.010.016-0.0280.1050.0010.0013-0.06410.3253-0.00580.15740.3651.0302-0.0126-0.36880.00250.1676-0.00810.0230.26050.06050.3108-17.5723-16.0459-4.0547
290.111-0.0641-0.08490.1059-0.02820.0512-0.1255-0.328-0.192-0.00890.16060.13720.01520.1455-0.00020.1627-0.01410.01360.25110.0330.1991-10.6982-22.51631.0174
300.05510.0196-0.02440.0257-0.00960.00580.31560.8070.33460.0301-0.2160.0149-0.2319-0.27530.00020.26480.0479-0.00810.32840.02590.26834.495714.2341-17.732
310.0375-0.03040.00830.0405-0.00960.0323-0.167-0.20010.27510.63930.1802-0.0108-0.3773-0.1237-0.00120.37760.0326-0.0530.2694-0.02420.24141.105313.2804-6.1482
320.2863-0.07880.08870.1703-0.00830.0226-0.3525-0.45780.21030.25610.0450.1479-0.41950.3384-0.11980.59960.0557-0.16120.3998-0.04710.25727.21019.73235.8256
3321.99991.999921.99992.0001-0.2887.1496-4.8149-2.99942.5774-3.13973.66018.2996-2.29321.36680.06170.04041.34290.33310.73763.6828.416611.7868
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 125 THROUGH 144 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 145 THROUGH 217 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 218 THROUGH 229 )
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESID 230 THROUGH 258 )
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESID 259 THROUGH 282 )
6X-RAY DIFFRACTION6CHAIN 'A' AND (RESID 287 THROUGH 302 )
7X-RAY DIFFRACTION7CHAIN 'A' AND (RESID 303 THROUGH 333 )
8X-RAY DIFFRACTION8CHAIN 'A' AND (RESID 334 THROUGH 342 )
9X-RAY DIFFRACTION9CHAIN 'A' AND (RESID 343 THROUGH 373 )
10X-RAY DIFFRACTION10CHAIN 'A' AND (RESID 374 THROUGH 389 )
11X-RAY DIFFRACTION11CHAIN 'A' AND (RESID -1 THROUGH 10 )
12X-RAY DIFFRACTION12CHAIN 'A' AND (RESID 11 THROUGH 20 )
13X-RAY DIFFRACTION13CHAIN 'B' AND (RESID 125 THROUGH 135 )
14X-RAY DIFFRACTION14CHAIN 'B' AND (RESID 136 THROUGH 156 )
15X-RAY DIFFRACTION15CHAIN 'B' AND (RESID 157 THROUGH 187 )
16X-RAY DIFFRACTION16CHAIN 'B' AND (RESID 188 THROUGH 201 )
17X-RAY DIFFRACTION17CHAIN 'B' AND (RESID 202 THROUGH 217 )
18X-RAY DIFFRACTION18CHAIN 'B' AND (RESID 218 THROUGH 250 )
19X-RAY DIFFRACTION19CHAIN 'B' AND (RESID 251 THROUGH 258 )
20X-RAY DIFFRACTION20CHAIN 'B' AND (RESID 259 THROUGH 282 )
21X-RAY DIFFRACTION21CHAIN 'B' AND (RESID 287 THROUGH 302 )
22X-RAY DIFFRACTION22CHAIN 'B' AND (RESID 303 THROUGH 324 )
23X-RAY DIFFRACTION23CHAIN 'B' AND (RESID 325 THROUGH 333 )
24X-RAY DIFFRACTION24CHAIN 'B' AND (RESID 334 THROUGH 342 )
25X-RAY DIFFRACTION25CHAIN 'B' AND (RESID 343 THROUGH 353 )
26X-RAY DIFFRACTION26CHAIN 'B' AND (RESID 354 THROUGH 363 )
27X-RAY DIFFRACTION27CHAIN 'B' AND (RESID 364 THROUGH 373 )
28X-RAY DIFFRACTION28CHAIN 'B' AND (RESID 374 THROUGH 380 )
29X-RAY DIFFRACTION29CHAIN 'B' AND (RESID 381 THROUGH 389 )
30X-RAY DIFFRACTION30CHAIN 'B' AND (RESID -1 THROUGH 10 )
31X-RAY DIFFRACTION31CHAIN 'B' AND (RESID 11 THROUGH 15 )
32X-RAY DIFFRACTION32CHAIN 'B' AND (RESID 16 THROUGH 20 )
33X-RAY DIFFRACTION33CHAIN 'B' AND (RESID 116 THROUGH 116 )

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