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- PDB-6v6f: Crystal structure of Q61L KRAS(GMPPNP)-NF1(GRD)-SPRED1(EVH1) complex -

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Basic information

Entry
Database: PDB / ID: 6v6f
TitleCrystal structure of Q61L KRAS(GMPPNP)-NF1(GRD)-SPRED1(EVH1) complex
Components
  • GTPase KRas
  • Neurofibromin
  • Sprouty-related, EVH1 domain-containing protein 1
KeywordsONCOPROTEIN / Neurofibromin / RAS / Legius syndrome / RasGAP / GAP / SPRED / K-Ras / EVH1 / GRD
Function / homology
Function and homology information


negative regulation of lens fiber cell differentiation / stem cell factor receptor binding / negative regulation of intracellular signal transduction / FGFRL1 modulation of FGFR1 signaling / positive regulation of mast cell apoptotic process / negative regulation of Rac protein signal transduction / regulation of glial cell differentiation / observational learning / negative regulation of Schwann cell migration / Schwann cell migration ...negative regulation of lens fiber cell differentiation / stem cell factor receptor binding / negative regulation of intracellular signal transduction / FGFRL1 modulation of FGFR1 signaling / positive regulation of mast cell apoptotic process / negative regulation of Rac protein signal transduction / regulation of glial cell differentiation / observational learning / negative regulation of Schwann cell migration / Schwann cell migration / amygdala development / vascular associated smooth muscle cell migration / Schwann cell proliferation / negative regulation of mast cell proliferation / vasculogenesis involved in coronary vascular morphogenesis / mast cell apoptotic process / gamma-aminobutyric acid secretion, neurotransmission / vascular associated smooth muscle cell proliferation / glutamate secretion, neurotransmission / negative regulation of Schwann cell proliferation / negative regulation of leukocyte migration / mast cell proliferation / forebrain morphogenesis / regulation of cell-matrix adhesion / hair follicle maturation / regulation of blood vessel endothelial cell migration / cell communication / camera-type eye morphogenesis / smooth muscle tissue development / negative regulation of neurotransmitter secretion / negative regulation of oligodendrocyte differentiation / sympathetic nervous system development / myeloid leukocyte migration / peripheral nervous system development / negative regulation of cell migration involved in sprouting angiogenesis / myelination in peripheral nervous system / phosphatidylcholine binding / negative regulation of Ras protein signal transduction / metanephros development / phosphatidylethanolamine binding / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of long-term synaptic potentiation / collagen fibril organization / regulation of postsynapse organization / endothelial cell proliferation / positive regulation of DNA damage response, signal transduction by p53 class mediator / regulation of bone resorption / artery morphogenesis / neural tube development / negative regulation of epithelial to mesenchymal transition / response to mineralocorticoid / GMP binding / adrenal gland development / negative regulation of neuroblast proliferation / forebrain astrocyte development / LRR domain binding / negative regulation of protein import into nucleus / regulation of synaptic transmission, GABAergic / negative regulation of epithelial cell differentiation / pigmentation / response to isolation stress / spinal cord development / negative regulation of astrocyte differentiation / response to gravity / negative regulation of vascular associated smooth muscle cell migration / epithelial tube branching involved in lung morphogenesis / negative regulation of endothelial cell proliferation / type I pneumocyte differentiation / negative regulation of osteoclast 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 / oligodendrocyte differentiation / regulation of MAPK cascade / myoblast proliferation / skeletal muscle cell differentiation / RAS signaling downstream of NF1 loss-of-function variants / RUNX3 regulates p14-ARF / positive regulation of GTPase activity / positive regulation of glial cell proliferation / negative regulation of cell-matrix adhesion / protein serine/threonine kinase inhibitor activity / SOS-mediated signalling / extrinsic apoptotic signaling pathway via death domain receptors / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / neuroblast proliferation / SHC1 events in ERBB4 signaling / regulation of angiogenesis / cardiac muscle cell proliferation / Signalling to RAS / Activated NTRK2 signals through FRS2 and FRS3 / SHC-related events triggered by IGF1R / phosphatase binding / regulation of ERK1 and ERK2 cascade / Schwann cell development / Estrogen-stimulated signaling through PRKCZ / glial cell proliferation
Similarity search - Function
c-Kit-binding domain / SPRE, EVH1 domain / KBD domain profile. / Sprouty / Sprouty protein (Spry) / Sprouty (SPR) domain profile. / : / PH domain-like / Ras GTPase-activating protein / Ras GTPase-activating protein, conserved site ...c-Kit-binding domain / SPRE, EVH1 domain / KBD domain profile. / Sprouty / Sprouty protein (Spry) / Sprouty (SPR) domain profile. / : / PH domain-like / Ras GTPase-activating protein / Ras GTPase-activating protein, conserved site / Ras GTPase-activating proteins (rasGAP) domain signature. / GTPase-activator protein for Ras-like GTPase / Ras GTPase-activating proteins (rasGAP) domain profile. / GTPase-activator protein for Ras-like GTPases / Ras GTPase-activating domain / WH1/EVH1 domain / WH1 domain / Divergent CRAL/TRIO domain / WH1 domain profile. / WASP homology region 1 / CRAL-TRIO lipid binding domain profile. / Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) / CRAL-TRIO lipid binding domain / CRAL-TRIO lipid binding domain superfamily / Rho GTPase activation protein / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / 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 / PH-like domain superfamily / Armadillo-type fold / Roll / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
FORMIC ACID / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GTPase KRas / Neurofibromin / Sprouty-related, EVH1 domain-containing protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.542 Å
AuthorsYan, W. / Simanshu, D.K.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)HHSN261200800001E United States
CitationJournal: Cell Rep / Year: 2020
Title: Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR.
Authors: Yan, W. / Markegard, E. / Dharmaiah, S. / Urisman, A. / Drew, M. / Esposito, D. / Scheffzek, K. / Nissley, D.V. / McCormick, F. / Simanshu, D.K.
History
DepositionDec 5, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 15, 2020Provider: repository / Type: Initial release
Revision 1.1Aug 5, 2020Group: Database references / Derived calculations / Category: citation / citation_author / struct_conn
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _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
Revision 1.2Oct 11, 2023Group: 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: Sprouty-related, EVH1 domain-containing protein 1
B: Neurofibromin
C: GTPase KRas
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,53410
Polymers69,7383
Non-polymers7967
Water45025
1
B: Neurofibromin
C: GTPase KRas
hetero molecules

A: Sprouty-related, EVH1 domain-containing protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,53410
Polymers69,7383
Non-polymers7967
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_645-x+1,y-1/2,-z1
Buried area4650 Å2
ΔGint-61 kcal/mol
Surface area27480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)72.011, 70.240, 79.700
Angle α, β, γ (deg.)90.000, 100.670, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein Sprouty-related, EVH1 domain-containing protein 1 / hSpred1


Mass: 12853.724 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SPRED1 / Production host: unidentified baculovirus / References: UniProt: Q7Z699
#2: Protein Neurofibromin / Neurofibromatosis-related protein NF-1


Mass: 37570.180 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NF1 / Production host: Escherichia coli (E. coli) / References: UniProt: P21359
#3: Protein GTPase KRas / K-Ras 2 / Ki-Ras / c-K-ras / c-Ki-ras


Mass: 19313.840 Da / Num. of mol.: 1 / Mutation: Q61L
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

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Non-polymers , 5 types, 32 molecules

#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#5: Chemical
ChemComp-FMT / FORMIC ACID


Mass: 46.025 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: CH2O2
#6: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3 / Feature type: SUBJECT OF INVESTIGATION
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 25 / 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: 2.84 Å3/Da / Density % sol: 56.7 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.8
Details: 100 mM Tris pH 7.8, 100 mM ammonium sulfate, 300 mM sodium formate, 3% PEG3350, 3.5% PGA-LM 10% detergent ANAPOE-80

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 9, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.54→78.321 Å / Num. obs: 25489 / % possible obs: 98.2 % / Redundancy: 3.387 % / Biso Wilson estimate: 68.213 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.069 / Rrim(I) all: 0.082 / Χ2: 1.066 / Net I/σ(I): 11.47 / Num. measured all: 86332
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.54-2.73.3410.8021.613184415539460.8010.95495
2.7-2.883.3150.5142.5112881393438860.9050.61598.8
2.88-3.113.5230.2594.8812742363836170.9740.30599.4
3.11-3.413.3440.1438.0311120336733250.9890.1798.8
3.41-3.813.4750.07713.8110537305830320.9950.09199.1
3.81-4.43.4140.04820.599074270326580.9970.05698.3
4.4-5.383.4170.0425.297746228922670.9970.04799
5.38-7.63.3070.04225.395801179117540.9970.0597.9
7.6-78.3213.2340.03233.373247102710040.9980.03897.8

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHASERphasing
PHENIX1.16refinement
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6V65

6v65


Resolution: 2.542→78.321 Å / SU ML: 0.43 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 36.13
RfactorNum. reflection% reflection
Rfree0.2647 1997 7.85 %
Rwork0.2164 --
obs0.2202 25424 98.03 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 185.43 Å2 / Biso mean: 87.9056 Å2 / Biso min: 36.55 Å2
Refinement stepCycle: final / Resolution: 2.542→78.321 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4565 0 46 25 4636
Biso mean--66.36 71.5 -
Num. residues----579
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.5424-2.6060.47671300.4042152990
2.606-2.67650.4191430.3682167099
2.6765-2.75520.41181410.3506164698
2.7552-2.84420.39771440.3158168198
2.8442-2.94580.38541430.2945168499
2.9458-3.06380.32511430.277167499
3.0638-3.20320.30861430.2577167999
3.2032-3.37210.271420.2443167199
3.3721-3.58340.28341440.2238169599
3.5834-3.860.27451430.2179168999
3.86-4.24850.21841450.1819169498
4.2485-4.86310.21351440.1631168099
4.8631-6.12670.22181440.1897170599
6.1267-78.3210.22571480.1804173098
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)
10.5304-0.4144-0.14210.9501-0.41440.4761-0.07450.4224-0.0605-0.0932-0.1336-0.37460.4509-0.7732-00.8901-0.31950.07651.0801-0.05681.04532.7829.0149-1.7713
20.02170.004-0.01930.00950.0030.02010.11070.06810.08270.19380.27470.29610.00990.378801.522-0.06690.61751.47320.09411.833333.253441.496714.6086
30.41260.08970.18970.1032-0.16150.46970.15590.56840.20710.4459-0.10650.0547-0.0679-1.024600.8657-0.06210.11171.09880.03980.785834.281732.0867-3.2093
40.01720.02550.02320.03280.02970.0490.44422.10730.644-2.4203-0.19941.28190.46171.023801.28840.18560.03141.13190.12741.536352.309526.9593-17.7862
50.06880.1594-0.12760.3578-0.27670.171-0.21920.83120.6705-0.44340.9075-0.0654-0.1987-1.001100.81940.05010.25090.87890.13830.919540.243531.8204-7.9866
60.01670.04410.05470.30090.22760.17210.14081.14020.51630.45870.35830.8244-0.32580.1675-00.9099-0.03050.12381.35370.30361.375432.695537.0411-6.3848
70.1279-0.10320.03550.2404-0.17910.15040.6658-0.6224-0.97781.0059-0.86230.3988-0.68630.38730.0010.7682-0.23940.07011.12310.19221.112541.820825.64015.4871
80.1537-0.1283-0.02050.20890.14240.12890.2727-0.61080.57680.7165-0.7268-0.4588-0.41610.6457-00.869-0.3250.1091.2158-0.06061.193940.3332.11146.3794
90.2922-0.38240.16230.4819-0.19960.0547-0.5052-0.2770.207-0.7365-0.26410.1953-0.10980.139-00.9066-0.16050.29041.17210.02871.197633.059330.30323.9994
100.1861-0.16390.27220.1418-0.20710.3960.25610.3477-1.90350.0339-1.0083-0.0230.7260.0296-00.9209-0.06590.25311.34130.16421.234740.652720.0763-2.2488
111.10630.43490.7990.8966-0.02491.16560.13970.00950.72530.1749-0.00740.3089-0.33490.1836-01.0761-0.09750.23350.95840.02350.964617.692833.003116.0547
121.58861.7701-0.8082.5976-0.43770.6964-0.0004-0.0240.2221-0.12950.0129-0.199-0.39010.0967-00.64870.03570.09150.88040.08680.764411.192116.845612.4632
130.39680.3601-0.04940.5715-0.22950.1097-0.31640.08340.2273-0.33020.3868-0.1889-0.2098-1.26520.00020.8609-0.04980.0610.9009-0.12970.8958-15.6168-2.81214.1139
143.96830.8591-0.07292.6779-0.26151.8838-0.31780.6345-0.579-0.26360.1489-0.48680.15650.133900.6147-0.0175-0.01960.7366-0.0550.5094.92984.172511.6165
150.29180.2923-0.62620.6096-0.67031.24170.182-0.37130.5690.63840.0480.9548-0.4229-0.0516-01.3627-0.31270.18181.0913-0.26721.49517.565439.614618.3434
160.3626-0.47750.20861.25880.05170.27660.4280.47880.04460.2969-0.42231.29850.0001-0.6917-0.05880.74520.03660.00560.58150.01390.6972-12.21585.547635.4702
170.66480.1384-0.19591.55211.16951.08050.2269-0.02530.06640.5429-0.3639-0.22480.7680.5874-0.04830.46360.0657-0.47550.54860.12110.25082.47425.855434.9297
180.5532-0.5423-0.23060.43010.2450.54210.34590.4975-0.99710.38970.0449-0.23050.05670.56850.00790.71610.0272-0.04110.63630.06180.90845.98712.968930.5113
190.3313-0.0743-0.00750.26870.00340.1125-0.32590.048-0.8170.9811-0.5331-0.046-0.6783-0.4994-00.78270.09390.00420.54990.00610.8197-8.267-1.074736.6368
200.5370.40140.5560.51290.45530.57470.37340.1276-0.55531.5657-0.26690.1619-0.7178-0.8670.00550.78980.08180.00230.49760.06930.6332-8.8734.189435.8779
210.1403-0.1179-0.0780.4396-0.41130.6281-0.2436-0.13660.03610.18020.15590.6183-0.6673-0.327200.77480.1542-0.02650.65420.05010.6617-6.821815.002823.0201
220.8607-0.64960.79972.5232-0.00592.99640.07890.2740.80.13150.06130.4547-0.4835-0.051400.67140.0369-0.03730.53250.05720.6345-4.996719.593134.8452
231.1289-0.0484-0.21390.4143-0.0340.0690.5242-1.30410.39760.47090.1228-0.713-0.58730.71910.00360.8583-0.0746-0.05130.7122-0.11090.886311.647716.592443.1721
240.00730.00870.04620.1664-0.04060.36770.9274-0.38280.54280.2557-0.22840.4023-0.29220.073-00.6916-0.05410.0330.6718-0.0290.7814-1.326224.351345.7224
250.7764-1.0981-0.15812.5413-0.36860.27810.0599-0.34510.68831.32940.2560.2886-0.06390.00660.00540.76340.0749-0.09140.51220.02480.50652.281910.472744.6538
261.65510.06060.45850.62330.40550.951.4264-2.31590.1579-0.0322-0.33081.1162-0.0718-0.58920.0790.78180.00550.08340.72710.00330.8118-11.47239.029344.0045
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 13 through 24 )A13 - 24
2X-RAY DIFFRACTION2chain 'A' and (resid 25 through 30 )A25 - 30
3X-RAY DIFFRACTION3chain 'A' and (resid 31 through 48 )A31 - 48
4X-RAY DIFFRACTION4chain 'A' and (resid 49 through 55 )A49 - 55
5X-RAY DIFFRACTION5chain 'A' and (resid 56 through 64 )A56 - 64
6X-RAY DIFFRACTION6chain 'A' and (resid 65 through 75 )A65 - 75
7X-RAY DIFFRACTION7chain 'A' and (resid 76 through 88 )A76 - 88
8X-RAY DIFFRACTION8chain 'A' and (resid 89 through 96 )A89 - 96
9X-RAY DIFFRACTION9chain 'A' and (resid 97 through 105 )A97 - 105
10X-RAY DIFFRACTION10chain 'A' and (resid 106 through 124 )A106 - 124
11X-RAY DIFFRACTION11chain 'B' and (resid 1205 through 1250 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 1251 through 1309 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 1310 through 1331 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 1332 through 1461 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 1462 through 1528 )B0
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 10 )C1 - 10
17X-RAY DIFFRACTION17chain 'C' and (resid 11 through 24 )C11 - 24
18X-RAY DIFFRACTION18chain 'C' and (resid 25 through 37 )C25 - 37
19X-RAY DIFFRACTION19chain 'C' and (resid 38 through 46 )C38 - 46
20X-RAY DIFFRACTION20chain 'C' and (resid 47 through 61 )C47 - 61
21X-RAY DIFFRACTION21chain 'C' and (resid 62 through 74 )C62 - 74
22X-RAY DIFFRACTION22chain 'C' and (resid 75 through 116 )C75 - 116
23X-RAY DIFFRACTION23chain 'C' and (resid 117 through 126 )C117 - 126
24X-RAY DIFFRACTION24chain 'C' and (resid 127 through 137 )C127 - 137
25X-RAY DIFFRACTION25chain 'C' and (resid 138 through 151 )C138 - 151
26X-RAY DIFFRACTION26chain 'C' and (resid 152 through 168 )C152 - 168

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