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- PDB-7u8h: Discovery of a KRAS G12V Inhibitor in vivo Tool Compound starting... -

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Basic information

Entry
Database: PDB / ID: 7u8h
TitleDiscovery of a KRAS G12V Inhibitor in vivo Tool Compound starting from an HSQC-NMR based Fragment Hit
ComponentsGTPase KRas
KeywordsSIGNALING PROTEIN / KRAS / P21 / GTP-BINDING PROTEIN / ONCOGENES / BINDER / HYDROLASE / INHIBITOR OF SOS-MEDIATED
Function / homology
Function and homology information


response to mineralocorticoid / GMP binding / forebrain astrocyte development / LRR domain binding / regulation of synaptic transmission, GABAergic / negative regulation of epithelial cell differentiation / response to isolation stress / response to gravity / epithelial tube branching involved in lung morphogenesis / type I pneumocyte differentiation ...response to mineralocorticoid / GMP binding / forebrain astrocyte development / LRR domain binding / regulation of synaptic transmission, GABAergic / negative regulation of epithelial cell differentiation / response to isolation stress / response to gravity / epithelial tube branching involved in lung morphogenesis / type I pneumocyte differentiation / Rac protein signal transduction / positive regulation of Rac protein signal transduction / Signaling by RAS GAP mutants / Signaling by RAS GTPase mutants / Activation of RAS in B cells / myoblast proliferation / skeletal muscle cell differentiation / RAS signaling downstream of NF1 loss-of-function variants / RUNX3 regulates p14-ARF / positive regulation of glial cell proliferation / SOS-mediated signalling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / cardiac muscle cell proliferation / Signalling to RAS / Activated NTRK2 signals through FRS2 and FRS3 / SHC-related events triggered by IGF1R / Estrogen-stimulated signaling through PRKCZ / glial cell proliferation / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / SHC-mediated cascade:FGFR2 / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / SHC-mediated cascade:FGFR4 / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / Signaling by FGFR4 in disease / FRS-mediated FGFR3 signaling / Signaling by CSF3 (G-CSF) / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / FRS-mediated FGFR1 signaling / p38MAPK events / Signaling by FGFR3 in disease / protein-membrane adaptor activity / Tie2 Signaling / striated muscle cell differentiation / Signaling by FGFR2 in disease / GRB2 events in EGFR signaling / Signaling by FLT3 fusion proteins / SHC1 events in EGFR signaling / FLT3 Signaling / Signaling by FGFR1 in disease / EGFR Transactivation by Gastrin / NCAM signaling for neurite out-growth / CD209 (DC-SIGN) signaling / homeostasis of number of cells within a tissue / Downstream signal transduction / GRB2 events in ERBB2 signaling / Insulin receptor signalling cascade / Ras activation upon Ca2+ influx through NMDA receptor / SHC1 events in ERBB2 signaling / response to glucocorticoid / Constitutive Signaling by Overexpressed ERBB2 / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / VEGFR2 mediated cell proliferation / small monomeric GTPase / FCERI mediated MAPK activation / liver development / female pregnancy / RAF activation / Signaling by ERBB2 TMD/JMD mutants / Signaling by SCF-KIT / Constitutive Signaling by EGFRvIII / Signaling by high-kinase activity BRAF mutants / regulation of long-term neuronal synaptic plasticity / MAP2K and MAPK activation / Signaling by ERBB2 ECD mutants / visual learning / Signaling by ERBB2 KD Mutants / cytoplasmic side of plasma membrane / cytokine-mediated signaling pathway / Regulation of RAS by GAPs / Signaling by CSF1 (M-CSF) in myeloid cells / RAS processing / Negative regulation of MAPK pathway / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / GDP binding / Signaling by BRAF and RAF1 fusions / positive regulation of cellular senescence / DAP12 signaling / MAPK cascade / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
Similarity search - Function
Small GTPase, Ras-type / Small GTPase Ras domain profile. / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases ...Small GTPase, Ras-type / Small GTPase Ras domain profile. / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
1H-benzimidazol-2-ylmethanethiol / GUANOSINE-5'-DIPHOSPHATE / Chem-LX6 / GTPase KRas
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.702 Å
AuthorsPhan, J. / Fesik, S.W.
Funding support1items
OrganizationGrant numberCountry
Other government
CitationJournal: J.Med.Chem. / Year: 2022
Title: Fragment Optimization of Reversible Binding to the Switch II Pocket on KRAS Leads to a Potent, In Vivo Active KRAS G12C Inhibitor.
Authors: Broker, J. / Waterson, A.G. / Smethurst, C. / Kessler, D. / Bottcher, J. / Mayer, M. / Gmaschitz, G. / Phan, J. / Little, A. / Abbott, J.R. / Sun, Q. / Gmachl, M. / Rudolph, D. / Arnhof, H. ...Authors: Broker, J. / Waterson, A.G. / Smethurst, C. / Kessler, D. / Bottcher, J. / Mayer, M. / Gmaschitz, G. / Phan, J. / Little, A. / Abbott, J.R. / Sun, Q. / Gmachl, M. / Rudolph, D. / Arnhof, H. / Rumpel, K. / Savarese, F. / Gerstberger, T. / Mischerikow, N. / Treu, M. / Herdeis, L. / Wunberg, T. / Gollner, A. / Weinstabl, H. / Mantoulidis, A. / Kramer, O. / McConnell, D.B. / W Fesik, S.
History
DepositionMar 8, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2022Provider: repository / Type: Initial release
Revision 1.1Nov 23, 2022Group: 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 1.2Jan 4, 2023Group: Database references / Source and taxonomy / Structure summary
Category: entity / entity_name_com ...entity / entity_name_com / entity_src_gen / struct / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _entity.pdbx_description / _entity.pdbx_ec ..._entity.pdbx_description / _entity.pdbx_ec / _entity.pdbx_mutation / _entity_src_gen.pdbx_gene_src_gene / _struct.title / _struct_ref.db_code / _struct_ref.pdbx_db_accession / _struct_ref.pdbx_db_isoform / _struct_ref_seq.pdbx_db_accession / _struct_ref_seq_dif.details / _struct_ref_seq_dif.pdbx_seq_db_accession_code
Revision 1.3Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTPase KRas
B: GTPase KRas
C: GTPase KRas
D: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,36718
Polymers77,4844
Non-polymers2,88314
Water11,385632
1
A: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,1815
Polymers19,3711
Non-polymers8104
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,1815
Polymers19,3711
Non-polymers8104
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,0034
Polymers19,3711
Non-polymers6323
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,0034
Polymers19,3711
Non-polymers6323
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)94.835, 98.480, 149.888
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11D-323-

HOH

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
GTPase KRas / K-Ras 2 / Ki-Ras / c-K-ras / c-Ki-ras


Mass: 19370.891 Da / Num. of mol.: 4 / Mutation: G12V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KRAS, KRAS2, RASK2 / Production host: Escherichia coli (E. coli) / References: UniProt: P01116, small monomeric GTPase

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Non-polymers , 5 types, 646 molecules

#2: Chemical
ChemComp-2XO / 1H-benzimidazol-2-ylmethanethiol


Mass: 164.228 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H8N2S
#3: Chemical
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-LX6 / 2-amino-4,5,6,7-tetrahydro-1-benzothiophene-3-carbonitrile


Mass: 178.254 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H10N2S / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 632 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.26 Å3/Da / Density % sol: 45.53 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion
Details: 30% PEG3350, 0.1 M bicine pH 8.5, 0.2 M ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.98 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 7, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.7→30 Å / Num. obs: 76938 / % possible obs: 100 % / Redundancy: 7.9 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 20.7
Reflection shellResolution: 1.7→1.73 Å / Redundancy: 7.9 % / Rmerge(I) obs: 0.626 / Num. unique obs: 3773 / % possible all: 100

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
PHENIX1.8.1_1168refinement
PDB_EXTRACT3.27data extraction
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EPY

4epy


Resolution: 1.702→29.819 Å / SU ML: 0.16 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.91 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1991 3861 5.02 %
Rwork0.1724 73027 -
obs0.1738 76888 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 110.52 Å2 / Biso mean: 28.4008 Å2 / Biso min: 5.68 Å2
Refinement stepCycle: final / Resolution: 1.702→29.819 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5297 0 184 634 6115
Biso mean--23.01 35.64 -
Num. residues----665
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0055834
X-RAY DIFFRACTIONf_angle_d0.9747934
X-RAY DIFFRACTIONf_chiral_restr0.06874
X-RAY DIFFRACTIONf_plane_restr0.0041019
X-RAY DIFFRACTIONf_dihedral_angle_d16.7892220
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.702-1.72260.25941290.2078258299
1.7226-1.74440.23811480.20492548100
1.7444-1.76730.2031290.19782612100
1.7673-1.79150.2181430.19142609100
1.7915-1.81710.20751290.19012528100
1.8171-1.84420.23411510.19172618100
1.8442-1.8730.21421080.19322577100
1.873-1.90370.22381300.18792606100
1.9037-1.93660.22521480.17632569100
1.9366-1.97180.18811420.17752583100
1.9718-2.00970.21591200.17992649100
2.0097-2.05070.21611110.17782571100
2.0507-2.09530.23021380.18032589100
2.0953-2.1440.2251460.17822596100
2.144-2.19760.19661320.17832598100
2.1976-2.2570.18311330.16922594100
2.257-2.32340.22911330.1732598100
2.3234-2.39840.22021570.17582588100
2.3984-2.4840.19151270.17682614100
2.484-2.58350.20051370.17022624100
2.5835-2.7010.2181480.18412604100
2.701-2.84320.22921410.18932620100
2.8432-3.02120.22491460.1792593100
3.0212-3.25420.21281680.16312621100
3.2542-3.58120.17761410.1642634100
3.5812-4.09830.1721160.15432677100
4.0983-5.15910.16091540.14182663100
5.1591-29.8190.16741560.18152762100
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)
11.6417-1.6251-0.0222.55210.09551.2827-0.1223-0.0632-0.00910.15520.1563-0.44360.04920.38250.01480.08670.0162-0.03310.18260.00030.262858.03834.64216.741
22.09981.3303-1.40694.5119-3.92863.50450.0605-0.50150.41390.50470.1457-0.6562-0.21670.7499-0.20720.3370.0183-0.0820.2886-0.0590.496660.49544.44522.501
33.5935-3.09861.65782.8493-1.8592.8389-0.1824-0.12850.44910.0975-0.1011-0.5205-0.17310.10430.25870.16530.04530.00740.19790.03360.363464.39929.816.831
42.1061-1.3549-0.54886.8833-3.58272.7353-0.1192-0.0496-0.384-0.3787-0.1495-0.19620.17050.07680.25750.1450.0336-0.02340.17790.02920.330361.42626.26814.452
51.7488-0.96272.97236.13650.51835.9354-0.05050.46040.3743-0.4531-0.0083-0.109-0.45890.0513-0.00130.2397-0.01610.01650.35590.08970.256555.38542.6942.885
64.0279-2.3893-4.43964.20794.34758.5911-0.12180.04130.04370.2380.0529-0.1050.24040.13970.07150.08190.0271-0.03520.1171-0.00250.101848.03936.59716.52
71.3326-0.1302-1.56411.17171.64516.68150.15380.62020.0732-0.1961-0.16290.1082-0.2215-0.58210.03740.1030.0333-0.03980.24630.00860.146943.3139.228.78
84.41920.1835-0.28363.3104-0.69791.6107-0.04880.13-0.18490.11130.05360.06630.0851-0.1940.00470.07130.02060.0110.10230.0080.165541.85533.3518.6
94.00644.23795.04945.95845.29877.0728-0.185-0.4823-0.20950.5782-0.1242-0.04140.2657-0.06530.14850.15410.06560.01980.20690.02230.165649.0631.44824.796
104.23590.68391.06646.46243.12353.0468-0.1590.192-0.79450.20380.09650.060.45490.25370.06590.1320.04370.05880.17580.00320.309553.17523.79414.702
112.85321.3824-0.35482.635-0.03420.97420.0432-0.0721-0.27660.38540.0591-0.23090.08430.043-0.08460.12850.0151-0.03170.09060.01640.128631.83353.88221.739
127.4815-1.5548-3.99414.97760.46272.4506-0.27470.90180.4307-0.54720.2026-0.8192-0.18820.77660.09440.3187-0.04570.07930.41140.02750.33142.71955.8858.735
132.01490.74340.56642.9651.18832.924-0.00280.3170.201-0.17190.1559-0.1754-0.09850.0307-0.05520.083-0.01190.00940.14060.0160.067735.24968.83215.247
142.70370.61130.46263.5069-0.34173.97570.0337-0.02410.24140.1304-0.11660.2815-0.1123-0.34940.02980.06290.02190.03220.13020.00250.107525.61766.60218.051
152.1569-0.3433-0.34731.84290.33342.7472-0.0277-0.152-0.01850.12720.07210.54970.1039-0.2863-0.01480.0749-0.00640.040.10740.01510.16255.1830.48226.196
160.020.1055-0.02255.85780.4340.44310.02420.17880.7639-0.24760.13070.4349-0.0657-0.1256-0.10250.16540.02450.0170.1560.04350.4425-0.06339.42921.048
175.03992.2612-0.79356.23133.4237.2419-0.33860.6572-0.8772-0.44620.1708-0.2171.24840.30830.15440.3585-0.03150.05040.3271-0.09050.30324.54821.66811.568
182.4733-0.59820.81682.1243-0.06393.2356-0.020.4946-0.0823-0.52870.0051-0.06810.22950.09030.00010.1693-0.02310.04550.1860.01270.071816.60229.98715.099
193.0470.0956-0.42012.4077-0.42542.698-0.03610.05820.2727-0.0076-0.0021-0.0389-0.08920.04070.01410.0764-0.01760.02350.0549-0.00230.087117.70438.53522.913
201.90880.7344-0.36622.9139-1.71223.1686-0.3667-0.2675-0.10760.66540.1201-0.2393-0.37130.1463-0.03110.34040.14990.09960.16810.05040.228532.36513.23925.341
212.92040.33991.23740.322-0.28051.26190.0314-0.34570.27850.57530.0594-0.30770.13460.3632-0.03370.76230.28360.21930.46390.11140.593726.2715.63836.083
221.6852-0.7334-2.01411.90340.47372.5416-0.1447-0.0463-0.2220.11540.0952-0.56250.0534-0.01240.08050.16550.03760.05380.16450.04630.275237.21417.82321.285
235.6837-0.88791.06953.5991.81734.3294-0.04150.78730.1003-0.30830.14291.1536-0.0576-0.9432-0.05510.42230.00650.03030.34040.10930.483622.93311.24216.372
240.13710.6095-0.58532.6653-2.58342.5138-0.342-0.2253-0.41240.25750.22220.60630.452-0.1841-0.12410.50520.11180.3937-0.05620.39030.416226.806-0.79628.976
252.70920.08791.06243.95-1.92819.6619-0.12050.2337-0.482-0.37370.090.73120.5779-0.6676-0.01260.5349-0.14220.00040.33010.08190.769222.896-0.19217.43
263.6937-0.27321.2643.019-2.67056.5271-0.28540.3059-0.3211-0.42670.16710.31960.261-0.12920.05180.41910.0660.10810.17220.0540.344930.7881.84116.748
270.0487-0.13040.2050.3636-0.53670.8116-0.1988-0.269-0.23270.03270.0449-0.08880.19210.10890.07610.90490.36710.4572-0.00940.44890.568333.31-6.31831.194
281.6547-0.21050.99954.78351.84966.6998-0.4545-0.68750.04790.87750.0725-0.4375-0.3698-0.05320.16150.57590.32680.0040.46370.18410.370337.8853.36131.081
295.0804-0.3476-2.00964.53960.03612.1414-0.298-0.2372-0.34290.05370.2074-0.80290.62690.52330.020.23510.07470.03850.19270.05220.35940.4467.78819.425
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 0:25 )A0 - 25
2X-RAY DIFFRACTION2( CHAIN A AND RESID 26:37 )A26 - 37
3X-RAY DIFFRACTION3( CHAIN A AND RESID 38:46 )A38 - 46
4X-RAY DIFFRACTION4( CHAIN A AND RESID 47:57 )A47 - 57
5X-RAY DIFFRACTION5( CHAIN A AND RESID 58:74 )A58 - 74
6X-RAY DIFFRACTION6( CHAIN A AND RESID 75:86 )A75 - 86
7X-RAY DIFFRACTION7( CHAIN A AND RESID 87:104 )A87 - 104
8X-RAY DIFFRACTION8( CHAIN A AND RESID 105:137 )A105 - 137
9X-RAY DIFFRACTION9( CHAIN A AND RESID 138:151 )A138 - 151
10X-RAY DIFFRACTION10( CHAIN A AND RESID 152:167 )A152 - 167
11X-RAY DIFFRACTION11( CHAIN B AND RESID 0:57 )B0 - 57
12X-RAY DIFFRACTION12( CHAIN B AND RESID 58:74 )B58 - 74
13X-RAY DIFFRACTION13( CHAIN B AND RESID 75:126 )B75 - 126
14X-RAY DIFFRACTION14( CHAIN B AND RESID 127:167 )B127 - 167
15X-RAY DIFFRACTION15( CHAIN C AND RESID 1:37 )C1 - 37
16X-RAY DIFFRACTION16( CHAIN C AND RESID 38:57 )C38 - 57
17X-RAY DIFFRACTION17( CHAIN C AND RESID 58:74 )C58 - 74
18X-RAY DIFFRACTION18( CHAIN C AND RESID 75:116 )C75 - 116
19X-RAY DIFFRACTION19( CHAIN C AND RESID 117:166 )C117 - 166
20X-RAY DIFFRACTION20( CHAIN D AND RESID 1:25 )D1 - 25
21X-RAY DIFFRACTION21( CHAIN D AND RESID 26:37 )D26 - 37
22X-RAY DIFFRACTION22( CHAIN D AND RESID 38:57 )D38 - 57
23X-RAY DIFFRACTION23( CHAIN D AND RESID 58:76 )D58 - 76
24X-RAY DIFFRACTION24( CHAIN D AND RESID 77:92 )D77 - 92
25X-RAY DIFFRACTION25( CHAIN D AND RESID 93:103 )D93 - 103
26X-RAY DIFFRACTION26( CHAIN D AND RESID 104:116 )D104 - 116
27X-RAY DIFFRACTION27( CHAIN D AND RESID 117:137 )D117 - 137
28X-RAY DIFFRACTION28( CHAIN D AND RESID 138:151 )D138 - 151
29X-RAY DIFFRACTION29( CHAIN D AND RESID 152:166 )D152 - 166

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