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- PDB-4hre: Crystal Structure of p11/Annexin A2 Heterotetramer in Complex wit... -

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Basic information

Entry
Database: PDB / ID: 4hre
TitleCrystal Structure of p11/Annexin A2 Heterotetramer in Complex with SMARCA3 Peptide
Components
  • Annexin A2
  • Helicase-like transcription factor
  • Protein S100-A10
KeywordsCalcium-binding protein / Calcium Binding / Nucleus
Function / homology
Function and homology information


Dissolution of Fibrin Clot / AnxA2-p11 complex / membrane raft assembly / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / positive regulation of vacuole organization / phospholipase A2 inhibitor activity / positive regulation of low-density lipoprotein particle clearance / positive regulation of vesicle fusion / myelin sheath adaxonal region / negative regulation of low-density lipoprotein particle receptor catabolic process ...Dissolution of Fibrin Clot / AnxA2-p11 complex / membrane raft assembly / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / positive regulation of vacuole organization / phospholipase A2 inhibitor activity / positive regulation of low-density lipoprotein particle clearance / positive regulation of vesicle fusion / myelin sheath adaxonal region / negative regulation of low-density lipoprotein particle receptor catabolic process / positive regulation of plasma membrane repair / positive regulation of plasminogen activation / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / PCSK9-AnxA2 complex / cornified envelope / Schmidt-Lanterman incisure / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / vesicle budding from membrane / plasma membrane protein complex / calcium-dependent phospholipid binding / osteoclast development / negative regulation of receptor internalization / Dissolution of Fibrin Clot / S100 protein binding / collagen fibril organization / epithelial cell apoptotic process / positive regulation of receptor recycling / basement membrane / positive regulation of GTPase activity / positive regulation of exocytosis / positive regulation of focal adhesion assembly / regulation of neurogenesis / ATP-dependent activity, acting on DNA / cytoskeletal protein binding / fibrinolysis / positive regulation of stress fiber assembly / phosphatidylinositol-4,5-bisphosphate binding / Neutrophil degranulation / lipid droplet / positive regulation of substrate adhesion-dependent cell spreading / lung development / cell-matrix adhesion / response to activity / protein localization to plasma membrane / serine-type endopeptidase inhibitor activity / mRNA transcription by RNA polymerase II / helicase activity / sarcolemma / RING-type E3 ubiquitin transferase / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / RNA polymerase II transcription regulator complex / nuclear matrix / calcium-dependent protein binding / ubiquitin protein ligase activity / late endosome membrane / melanosome / E3 ubiquitin ligases ubiquitinate target proteins / : / chromatin organization / protease binding / midbody / angiogenesis / basolateral plasma membrane / transmembrane transporter binding / early endosome / cell adhesion / protein ubiquitination / membrane raft / lysosomal membrane / DNA repair / calcium ion binding / ubiquitin protein ligase binding / nucleolus / cell surface / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular space / DNA binding / RNA binding / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Protein S100-A10 / HIRAN domain / HIRAN domain / HIRAN / : / Annexin A2 / Annexin / Zinc finger, C3HC4 type (RING finger) / Annexin repeat, conserved site / Annexin repeat signature. ...Protein S100-A10 / HIRAN domain / HIRAN domain / HIRAN / : / Annexin A2 / Annexin / Zinc finger, C3HC4 type (RING finger) / Annexin repeat, conserved site / Annexin repeat signature. / Annexin / Annexin / Annexin repeats / Annexin repeat / Annexin superfamily / Annexin repeat profile. / S-100/ICaBP type calcium binding protein signature. / S100/Calcium binding protein 7/8-like, conserved site / Annexin V; domain 1 / S100/CaBP-9k-type, calcium binding, subdomain / S-100/ICaBP type calcium binding domain / S-100/ICaBP type calcium binding domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / EF-hand / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Recoverin; domain 1 / Ring finger / Zinc finger RING-type profile. / Helicase conserved C-terminal domain / Zinc finger, RING-type / EF-hand domain pair / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Annexin A2 / Protein S100-A10 / Helicase-like transcription factor
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7852 Å
AuthorsGao, P. / Patel, D.J.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2013
Title: SMARCA3, a Chromatin-Remodeling Factor, Is Required for p11-Dependent Antidepressant Action.
Authors: Oh, Y.S. / Gao, P. / Lee, K.W. / Ceglia, I. / Seo, J.S. / Zhang, X. / Ahn, J.H. / Chait, B.T. / Patel, D.J. / Kim, Y. / Greengard, P.
History
DepositionOct 27, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 6, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 20, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Annexin A2
C: Annexin A2
E: Protein S100-A10
F: Protein S100-A10
G: Helicase-like transcription factor
H: Helicase-like transcription factor
B: Annexin A2
D: Annexin A2
I: Protein S100-A10
J: Protein S100-A10
K: Helicase-like transcription factor
L: Helicase-like transcription factor


Theoretical massNumber of molelcules
Total (without water)206,86112
Polymers206,86112
Non-polymers00
Water00
1
A: Annexin A2
C: Annexin A2
E: Protein S100-A10
F: Protein S100-A10
G: Helicase-like transcription factor
H: Helicase-like transcription factor


Theoretical massNumber of molelcules
Total (without water)103,4316
Polymers103,4316
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9630 Å2
ΔGint-89 kcal/mol
Surface area41470 Å2
MethodPISA
2
B: Annexin A2
D: Annexin A2
I: Protein S100-A10
J: Protein S100-A10
K: Helicase-like transcription factor
L: Helicase-like transcription factor


Theoretical massNumber of molelcules
Total (without water)103,4316
Polymers103,4316
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9940 Å2
ΔGint-91 kcal/mol
Surface area41380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)50.791, 74.346, 154.466
Angle α, β, γ (deg.)90.14, 96.56, 108.37
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Annexin A2 / Annexin II / Annexin-2 / Calpactin I heavy chain / Calpactin-1 heavy chain / Chromobindin-8 / ...Annexin II / Annexin-2 / Calpactin I heavy chain / Calpactin-1 heavy chain / Chromobindin-8 / Lipocortin II / Placental anticoagulant protein IV / PAP-IV / Protein I / p36


Mass: 38733.227 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Anxa2, Anx2, Cal1h / Production host: Escherichia coli (E. coli) / References: UniProt: P07356
#2: Protein
Protein S100-A10 / Calpactin I light chain / Calpactin-1 light chain / Cellular ligand of annexin II / S100 calcium- ...Calpactin I light chain / Calpactin-1 light chain / Cellular ligand of annexin II / S100 calcium-binding protein A10 / p10 protein / p11


Mass: 11176.019 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: S100A10, ANX2LG, CAL1L, CLP11 / Production host: Escherichia coli (E. coli) / References: UniProt: P60903
#3: Protein/peptide
Helicase-like transcription factor / DNA-binding protein/plasminogen activator inhibitor 1 regulator / HIP116 / RING finger protein 80 / ...DNA-binding protein/plasminogen activator inhibitor 1 regulator / HIP116 / RING finger protein 80 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3 / Sucrose nonfermenting protein 2-like 3


Mass: 1806.069 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / Source: (synth.) Homo sapiens (human)
References: UniProt: Q14527, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ...References: UniProt: Q14527, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 2.66 Å3/Da / Density % sol: 53.72 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 3.7
Details: 0.1 M citric acid, 25% PEG 3350, pH 3.7, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.075 Å / Relative weight: 1
ReflectionResolution: 2.7852→47.335 Å / Num. all: 50718 / Num. obs: 53292 / % possible obs: 95.17 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2

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Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1W7B and 4HRH

1w7b

4hrh


Resolution: 2.7852→47.335 Å / SU ML: 0.39 / σ(F): 1.96 / Phase error: 38.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.296 2573 5.07 %RANDOM
Rwork0.249 ---
all0.2567 53292 --
obs0.2567 50718 95.17 %-
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 27.583 Å2 / ksol: 0.303 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-10.6168 Å20.3397 Å211.8367 Å2
2---1.2062 Å23.1344 Å2
3----10.5623 Å2
Refinement stepCycle: LAST / Resolution: 2.7852→47.335 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14088 0 0 0 14088
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00814324
X-RAY DIFFRACTIONf_angle_d1.24119223
X-RAY DIFFRACTIONf_dihedral_angle_d17.9375509
X-RAY DIFFRACTIONf_chiral_restr0.0962108
X-RAY DIFFRACTIONf_plane_restr0.0052463
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7852-2.83870.41051640.36572637X-RAY DIFFRACTION93
2.8387-2.89670.37921320.33942705X-RAY DIFFRACTION97
2.8967-2.95970.37871440.34092754X-RAY DIFFRACTION97
2.9597-3.02850.40381230.32342723X-RAY DIFFRACTION97
3.0285-3.10420.3731460.3082730X-RAY DIFFRACTION97
3.1042-3.18810.37241390.29922732X-RAY DIFFRACTION97
3.1881-3.28190.3461720.28162690X-RAY DIFFRACTION97
3.2819-3.38780.31511430.27012741X-RAY DIFFRACTION96
3.3878-3.50890.32591470.26692657X-RAY DIFFRACTION96
3.5089-3.64930.35871380.26192719X-RAY DIFFRACTION96
3.6493-3.81530.33281600.25682660X-RAY DIFFRACTION96
3.8153-4.01640.28621420.22972638X-RAY DIFFRACTION95
4.0164-4.26790.23531500.20582698X-RAY DIFFRACTION95
4.2679-4.59710.24341560.20132651X-RAY DIFFRACTION95
4.5971-5.05930.25611430.20762643X-RAY DIFFRACTION94
5.0593-5.79030.30041310.26222637X-RAY DIFFRACTION94
5.7903-7.29080.3211240.26262616X-RAY DIFFRACTION92
7.2908-47.34170.24471190.20952514X-RAY DIFFRACTION89
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)
10.3287-0.4464-0.29922.1751-1.51752.5294-0.4866-0.6650.01780.40060.3104-0.70720.83871.05930.48620.87390.0310.10790.80990.0760.488822.07657.1035-26.8372
21.9391-0.8811-1.39611.43761.03242.1441-0.0384-0.0406-0.16-0.0389-0.08940.1524-0.1193-0.01360.00060.28920.0260.06820.12570.05110.257718.15455.668-51.3894
31.5006-0.8267-0.9621.1033-0.35411.8004-0.34050.246-0.5255-0.83890.14160.44751.0716-0.35330.37660.7567-0.3306-0.10320.6873-0.01810.508615.8251.156716.9988
41.26730.4067-0.92661.7617-0.85981.6185-0.5402-0.1028-0.46570.44880.0964-0.18930.21060.1208-0.2727-0.1535-0.115-0.27910.3327-0.07760.148620.45671.347441.7844
55.83936.4863-0.93647.4189-1.43060.85570.1604-0.8284-0.90770.8331-0.5526-0.34450.21790.59440.23251.078-0.02590.12331.0744-0.08350.680527.4385-12.5322-1.272
60.67920.5908-0.13324.6585-0.80561.3570.63310.18930.45750.4362-1.1697-0.3977-0.2510.36390.38281.4343-0.6945-0.3591.41440.20661.456339.00830.2376-2.4127
73.45840.1514-2.73713.1896-1.77343.31210.0661-0.31450.7374-0.2592-0.4394-0.368-0.2310.89290.09051.01440.38160.35031.25480.4731.182337.5679-1.1232-12.5685
83.745-2.4633-1.25721.62190.86641.30690.041-1.0494-0.36050.27620.27280.05451.73510.0881-0.27061.64010.2142-0.00931.8917-0.08090.551330.7656-6.6051-19.4674
91.65630.5384-0.97744.0157-3.57963.34660.4069-0.28090.52320.6299-0.7947-0.3691-0.6817-0.08370.25110.96880.0390.24160.77750.25330.850532.42253.1403-21.4316
105.0412.24454.3058.15392.85323.89540.2118-0.82850.84660.27130.04240.3704-0.0396-0.0372-0.21610.8405-0.6072-0.06161.62250.09051.537429.79069.6428-6.6228
112.9186-0.2513-1.2123.2714-2.0471.92780.1710.3914-0.0857-0.2156-0.33060.34250.1945-0.293-0.12381.002-0.45390.0651.117-0.22890.426818.9134-5.1713-13.2559
122.3947-0.37780.26881.7251-0.88362.82110.08410.9295-0.5022-0.32950.26130.1920.5987-0.1407-0.05631.0751-0.3209-0.03040.75120.0170.723114.1224-14.5851-1.4543
131.38010.3241-0.63550.0786-0.14590.2961-0.0829-0.5374-0.34490.08670.65242.26870.7814-1.4221-0.59771.0937-0.09760.14181.52220.3231.26035.7973-6.34238.817
143.6158-0.58362.64837.1256-1.34312.67120.1409-0.21590.23540.9671-0.44410.5167-0.8105-0.87440.06681.0306-0.01850.47951.25170.2140.71755.2963-1.7823-2.2977
150.51120.0914-0.36660.4527-0.21430.31160.0687-0.03610.02520.2886-0.07090.0152-0.18430.1959-0.16381.548-0.70560.46280.8703-0.25480.528224.1908-5.55583.5614
160.0679-0.0197-0.09248.18311.7762.49530.2746-0.4720.13840.5051-0.5726-0.3356-1.2684-0.36760.19141.0055-0.11360.26491.08990.03850.865919.40753.6799-13.5509
177.1405-4.268.05772.7204-5.33952.00050.8592-1.2241-0.9772-0.430.39710.77251.7863-2.7477-1.36181.9508-0.60120.2331.4723-0.11930.609917.70.78425.0272
181.8673-1.7534-1.69892.17251.4371.7035-0.21690.6135-0.2375-0.8359-0.04290.31991.31830.0220.46290.8345-0.01840.0880.7992-0.03040.5223-5.786836.184193.8617
191.66970.2768-0.81862.3737-1.09590.8044-0.17370.303-0.125-0.20830.155-0.27860.1960.0690.03930.3581-0.01020.04530.2083-0.00840.3534.840146.8699.9438
202.781-0.7842-1.75522.0356-0.15633.3766-0.2044-0.0657-0.0535-0.0154-0.1337-0.11250.1850.0918-0.03060.5010.10570.1296-0.00930.06010.28061.368926.4908120.972
211.1910.7572-0.54262.7289-1.60462.03810.0568-0.105-0.00280.5804-0.07770.2268-0.26190.04820.02270.4970.1030.09210.2568-0.04690.3212-6.203339.6859126.2211
220.63190.2728-0.30081.1697-0.48410.7801-0.0193-0.7683-0.41590.67760.2769-0.42270.99730.4790.51610.7129-0.05050.03430.7208-0.19820.29773.106435.307449.6743
232.1651-0.4352-1.42491.29250.67062.26140.1269-0.015-0.0847-0.0517-0.13110.1136-0.3749-0.040.0050.037-0.0349-0.17620.21510.0190.2079-1.241733.458225.3246
240.1353-0.0925-0.28570.19210.40120.92960.33131.352-0.187-0.4502-0.5696-0.0394-0.0009-0.45160.16961.04340.1215-0.12690.90630.10630.7372-0.124317.714968.2118
257.9492-1.58556.22537.8285-0.20575.0149-0.2370.47980.1079-0.0215-0.39011.22790.3834-0.88640.35270.7379-0.39170.32271.68210.06371.185-14.57321.312575.82
264.1458-1.30962.87644.3205-3.80594.14470.06140.7193-0.6814-1.034-0.20810.52740.7015-0.2167-0.02381.11440.01010.13931.61340.01240.6446-8.642223.49789.6916
273.026-2.3988-1.12552.93212.20312.086-0.0034-0.10030.0149-0.1672-0.03390.3937-0.3308-0.6978-0.10910.6988-0.1025-0.03311.2188-0.03951.2677-13.63134.270276.0814
289.44260.60812.37843.78191.62095.3113-0.01870.45420.1570.1716-0.8762-0.36170.2860.4950.08990.8212-0.10930.11091.07310.21330.51973.719528.722880.4163
295.1440.84430.52863.2791-0.21967.91281.0053-0.6028-0.17430.72160.1484-0.95770.56821.089-0.13870.77150.0874-0.01670.7939-0.17750.869713.556923.713869.7159
300.688-1.7629-1.74296.56075.59785.03940.2067-0.0982-0.1024-0.04190.3517-0.2361-0.23950.7994-0.2260.9814-0.09250.46021.3352-0.01220.796514.008333.883856.684
313.84364.0074-2.2874.5468-2.61011.8877-0.5151-0.36281.1546-0.8036-0.2544-0.7037-0.9045-0.240.76671.5426-0.322-0.2341.4888-0.00440.872313.266640.068369.531
322.44362.61881.37245.43083.00086.04730.00150.8654-0.0364-0.834-0.32680.1976-0.2197-0.77490.04360.51990.11510.14331.24630.09370.1025-0.028226.154663.5933
334.50070.75963.86341.56971.85174.31340.80210.12420.0215-0.26740.25961.3273-1.5933-2.3509-1.11071.14020.17140.06170.96330.19821.0786-1.756236.033980.4864
341.95393.36252.89967.3856.50865.7414-0.07450.83690.1635-0.5018-0.15360.035-0.33011.6720.41660.93180.1374-0.08181.18620.41430.43341.745734.815462.1202
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 2:40)
2X-RAY DIFFRACTION2chain 'A' and (resseq 41:339)
3X-RAY DIFFRACTION3chain 'C' and (resseq 2:41)
4X-RAY DIFFRACTION4chain 'C' and (resseq 42:339)
5X-RAY DIFFRACTION5chain 'E' and (resseq 1:15)
6X-RAY DIFFRACTION6chain 'E' and (resseq 16:26)
7X-RAY DIFFRACTION7chain 'E' and (resseq 27:37)
8X-RAY DIFFRACTION8chain 'E' and (resseq 38:42)
9X-RAY DIFFRACTION9chain 'E' and (resseq 43:55)
10X-RAY DIFFRACTION10chain 'E' and (resseq 56:67)
11X-RAY DIFFRACTION11chain 'E' and (resseq 68:91)
12X-RAY DIFFRACTION12chain 'F' and (resseq 1:47)
13X-RAY DIFFRACTION13chain 'F' and (resseq 48:56)
14X-RAY DIFFRACTION14chain 'F' and (resseq 57:67)
15X-RAY DIFFRACTION15chain 'F' and (resseq 68:91)
16X-RAY DIFFRACTION16chain 'G' and (resseq -2:6)
17X-RAY DIFFRACTION17chain 'H' and (resseq -2:6)
18X-RAY DIFFRACTION18chain 'B' and (resseq 2:38)
19X-RAY DIFFRACTION19chain 'B' and (resseq 39:118)
20X-RAY DIFFRACTION20chain 'B' and (resseq 119:198)
21X-RAY DIFFRACTION21chain 'B' and (resseq 199:339)
22X-RAY DIFFRACTION22chain 'D' and (resseq 2:39)
23X-RAY DIFFRACTION23chain 'D' and (resseq 40:339)
24X-RAY DIFFRACTION24chain 'I' and (resseq 1:17)
25X-RAY DIFFRACTION25chain 'I' and (resseq 18:37)
26X-RAY DIFFRACTION26chain 'I' and (resseq 38:51)
27X-RAY DIFFRACTION27chain 'I' and (resseq 52:67)
28X-RAY DIFFRACTION28chain 'I' and (resseq 68:91)
29X-RAY DIFFRACTION29chain 'J' and (resseq 1:44)
30X-RAY DIFFRACTION30chain 'J' and (resseq 45:56)
31X-RAY DIFFRACTION31chain 'J' and (resseq 57:67)
32X-RAY DIFFRACTION32chain 'J' and (resseq 68:91)
33X-RAY DIFFRACTION33chain 'K' and (resseq -2:6)
34X-RAY DIFFRACTION34chain 'L' and (resseq -2:6)

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