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- PDB-6jmt: Crystal structure of GIT/PIX complex -

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Basic information

Entry
Database: PDB / ID: 6jmt
TitleCrystal structure of GIT/PIX complex
Components
  • ARF GTPase-activating protein GIT2
  • beta PIX
KeywordsCELL ADHESION / GIT2 / PIX / Complex
Function / homology
Function and homology information


presynaptic actin cytoskeleton organization / RHOV GTPase cycle / negative regulation of microtubule nucleation / Ephrin signaling / RHOQ GTPase cycle / RHOU GTPase cycle / RHOA GTPase cycle / NRAGE signals death through JNK / EGFR downregulation / RAC1 GTPase cycle ...presynaptic actin cytoskeleton organization / RHOV GTPase cycle / negative regulation of microtubule nucleation / Ephrin signaling / RHOQ GTPase cycle / RHOU GTPase cycle / RHOA GTPase cycle / NRAGE signals death through JNK / EGFR downregulation / RAC1 GTPase cycle / G alpha (12/13) signalling events / storage vacuole / astrocyte cell migration / positive regulation of growth hormone secretion / postsynaptic actin cytoskeleton organization / gamma-tubulin binding / lamellipodium assembly / regulation of synaptic vesicle exocytosis / small GTPase-mediated signal transduction / behavioral response to pain / mitotic spindle pole / Golgi organization / calyx of Held / Rho protein signal transduction / GABA-ergic synapse / hematopoietic progenitor cell differentiation / ruffle / presynaptic modulation of chemical synaptic transmission / GTPase activator activity / guanyl-nucleotide exchange factor activity / positive regulation of GTPase activity / lamellipodium / cell cortex / kinase activity / growth cone / postsynapse / neuron projection / positive regulation of apoptotic process / focal adhesion / centrosome / neuronal cell body / protein-containing complex binding / protein kinase binding / protein-containing complex / nucleoplasm / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
ARF GTPase-activating protein GIT1, C-terminal / G protein-coupled receptor kinase-interacting protein 1 C term / GIT, Spa2 homology (SHD) domain / Spa2 homology domain (SHD) of GIT / Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins / Unstructured region one on RhoGEF 6 and 7 / Rho guanine nucleotide exchange factor 6/7, coiled-coil domain / betaPIX coiled coil / Rho guanine nucleotide exchange factor 7, SH3 domain / RhoGEF 6/7, PH domain ...ARF GTPase-activating protein GIT1, C-terminal / G protein-coupled receptor kinase-interacting protein 1 C term / GIT, Spa2 homology (SHD) domain / Spa2 homology domain (SHD) of GIT / Helical motif in the GIT family of ADP-ribosylation factor GTPase-activating proteins / Unstructured region one on RhoGEF 6 and 7 / Rho guanine nucleotide exchange factor 6/7, coiled-coil domain / betaPIX coiled coil / Rho guanine nucleotide exchange factor 7, SH3 domain / RhoGEF 6/7, PH domain / Unstructured region two on RhoGEF 6 and 7 / Arf GTPase activating protein / ArfGAP domain superfamily / Putative GTPase activating protein for Arf / ARF GTPase-activating proteins domain profile. / Putative GTP-ase activating proteins for the small GTPase, ARF / ARFGAP/RecO-like zinc finger / Domain of unknown function DUF3447 / Guanine-nucleotide dissociation stimulator, CDC24, conserved site / Dbl homology (DH) domain signature. / Variant SH3 domain / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain 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. / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / PH-like domain superfamily
Similarity search - Domain/homology
ARF GTPase-activating protein GIT2 / Rho guanine nucleotide exchange factor 7 / ARF GTPase-activating protein GIT2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsZhu, J. / Lin, L. / Xia, Y. / Zhang, R. / Zhang, M.
CitationJournal: Mol.Cell / Year: 2020
Title: GIT/PIX Condensates Are Modular and Ideal for Distinct Compartmentalized Cell Signaling.
Authors: Zhu, J. / Zhou, Q. / Xia, Y. / Lin, L. / Li, J. / Peng, M. / Zhang, R. / Zhang, M.
History
DepositionMar 13, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 20, 2020Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 22, 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: ARF GTPase-activating protein GIT2
D: ARF GTPase-activating protein GIT2
B: ARF GTPase-activating protein GIT2
C: ARF GTPase-activating protein GIT2
E: ARF GTPase-activating protein GIT2
F: ARF GTPase-activating protein GIT2
I: beta PIX
J: beta PIX
K: beta PIX
L: beta PIX
M: beta PIX
N: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)258,11918
Polymers257,72712
Non-polymers3926
Water0
1
A: ARF GTPase-activating protein GIT2
L: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1610 Å2
ΔGint-19 kcal/mol
Surface area17440 Å2
MethodPISA
2
D: ARF GTPase-activating protein GIT2
N: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1660 Å2
ΔGint-17 kcal/mol
Surface area17380 Å2
MethodPISA
3
B: ARF GTPase-activating protein GIT2
M: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1610 Å2
ΔGint-18 kcal/mol
Surface area17450 Å2
MethodPISA
4
C: ARF GTPase-activating protein GIT2
I: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1540 Å2
ΔGint-17 kcal/mol
Surface area16460 Å2
MethodPISA
5
E: ARF GTPase-activating protein GIT2
J: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1630 Å2
ΔGint-16 kcal/mol
Surface area16570 Å2
MethodPISA
6
F: ARF GTPase-activating protein GIT2
K: beta PIX
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,0203
Polymers42,9542
Non-polymers651
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1500 Å2
ΔGint-18 kcal/mol
Surface area17390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)168.963, 322.681, 44.469
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
ARF GTPase-activating protein GIT2 / G protein-coupled receptor kinase-interactor 2


Mass: 40655.852 Da / Num. of mol.: 6 / Mutation: S255A/S256A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Git2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q80XR8, UniProt: Q9JLQ2*PLUS
#2: Protein/peptide
beta PIX


Mass: 2298.608 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9ES28*PLUS
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn

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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: 2.35 Å3/Da / Density % sol: 47.7 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / Details: NaF, Bis-Tris propane/citric acid pH 6.7, PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97775 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 17, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97775 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 59001 / % possible obs: 95.8 % / Redundancy: 8.1 % / Biso Wilson estimate: 46.7 Å2 / Rmerge(I) obs: 0.175 / Rpim(I) all: 0.061 / Rrim(I) all: 0.186 / Χ2: 0.921 / Net I/σ(I): 4.6
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.8-2.857.70.7629120.7870.2710.810.88997.6
2.85-2.98.20.68529310.8330.2350.7260.8997.7
2.9-2.968.20.63530390.8480.2190.6740.89397.7
2.96-3.028.10.58328730.860.2010.6180.88397.3
3.02-3.088.10.54429060.8640.190.5780.88696.9
3.08-3.158.10.43829380.8860.1530.4660.91695.1
3.15-3.238.10.38929360.9220.1350.4130.9396.7
3.23-3.327.90.32229190.9370.1140.3430.94197.4
3.32-3.427.60.26530200.9480.0960.2830.95197.4
3.42-3.537.70.23529030.9570.0850.2510.9697.2
3.53-3.658.30.229810.9660.0690.2120.98396.9
3.65-3.88.20.16829540.970.0580.1780.97196.8
3.8-3.978.20.14129600.9750.0490.150.98396.3
3.97-4.188.10.12428580.9790.0440.1320.94393.4
4.18-4.4480.10729900.9850.0380.1140.97195.1
4.44-4.798.10.128980.9870.0350.1060.9695.1
4.79-5.278.70.09829560.9830.0330.1040.89394.9
5.27-6.038.50.11129650.9830.0380.1180.86594.1
6.03-7.598.40.08829750.990.030.0930.87292.5
7.59-508.20.06430870.9940.0220.0680.84490.7

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Processing

Software
NameVersionClassification
HKL-3000data scaling
PHENIX1.8.4_1496refinement
PDB_EXTRACT3.24data extraction
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3JUE

3jue


Resolution: 2.8→44.053 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.15
RfactorNum. reflection% reflection
Rfree0.2536 2987 5.1 %
Rwork0.1941 --
obs0.1971 58572 94.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 144.92 Å2 / Biso mean: 45.21 Å2 / Biso min: 13.78 Å2
Refinement stepCycle: final / Resolution: 2.8→44.053 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16299 0 6 0 16305
Biso mean--42.22 --
Num. residues----2170
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00916644
X-RAY DIFFRACTIONf_angle_d1.18422659
X-RAY DIFFRACTIONf_chiral_restr0.0432575
X-RAY DIFFRACTIONf_plane_restr0.0062993
X-RAY DIFFRACTIONf_dihedral_angle_d14.0775850
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.8-2.84280.31431470.2599230187
2.8428-2.89180.34581350.2521264596
2.8918-2.94440.3331520.2483268196
2.9444-3.0010.32411530.2427260297
3.001-3.06220.30041430.2501263796
3.0622-3.12880.34481330.2455265995
3.1288-3.20160.30241170.2354264195
3.2016-3.28160.30391420.2205265197
3.2816-3.37030.27061420.2078271497
3.3703-3.46940.25021380.2068270397
3.4694-3.58140.31441380.2131265297
3.5814-3.70930.25281540.1899274097
3.7093-3.85770.25421560.1878259597
3.8577-4.03320.20531340.1795273696
4.0332-4.24570.20521530.16252593
4.2457-4.51140.24641330.1651270795
4.5114-4.85940.2131280.165269395
4.8594-5.34760.22121590.1684264595
5.3476-6.11970.2651390.1976267994
6.1197-7.70340.21781470.1735270293
7.7034-44.0530.2091440.1761267787
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)
10.263-0.091-0.00390.2925-0.1020.23190.12040.05690.1076-0.21420.01920.13510.2226-0.22580.00540.3077-0.035-0.03290.2666-0.0050.2188-54.757553.3988-14.9925
20.0691-0.00150.00010.19090.00820.0362-0.0864-0.1261-0.39090.1425-0.0369-0.31920.0698-0.1168-0.0060.35980.0551-0.10940.27140.0650.47-36.097447.9132-5.4083
30.3581-0.2261-0.12140.3708-0.03910.08210.0312-0.0927-0.0147-0.05180.0089-0.03650.01580.050900.22760.0113-0.01440.25930.01610.2152-40.659572.202-4.9396
40.1274-0.1887-0.11040.30680.16260.5289-0.0107-0.07020.02080.18280.05980.12690.04550.02580.00090.2150.0419-0.080.23280.03680.2169-53.904571.12382.1445
50.30610.04130.0120.28110.02650.35050.11550.09080.205-0.0985-0.02010.0209-0.0769-0.0883-0.00010.2664-0.00920.0020.25560.01780.2524-81.1838139.583-30.0036
60.26620.1172-0.12640.1883-0.12910.1177-0.304-0.0106-0.32840.15740.18190.1508-0.1406-0.0558-0.00570.22790.02240.07830.18720.01230.3005-75.9462119.9175-21.8432
70.37060.223-0.10790.1961-0.04440.02740.01910.0313-0.03770.0673-0.11880.0409-0.00620.0888-00.23280.00060.01270.1830.03120.2181-56.3207134.468-19.2428
80.26380.11240.01750.19910.23430.33190.0801-0.12940.0680.230.01050.12860.09890.10110.04020.2282-0.0826-0.02260.1160.10260.1933-62.6906143.4598-12.6763
90.37740.134-0.13750.3740.22290.2378-0.0445-0.0081-0.12290.02220.02960.00030.0155-0.025700.2167-0.0592-0.01920.2962-0.01330.1827-87.92677.03135.7461
100.15810.11380.09790.3784-0.09450.27370.04420.01860.115-0.04190.01730.1245-0.2921-0.32610.00010.26130.02-0.00150.2718-0.00630.2302-88.6534100.48121.2375
110.4121-0.27320.03930.27680.16320.32180.0213-0.05390.0522-0.01880.08-0.03740.067-0.01320.00010.21320.0186-0.02940.2065-0.01640.1894-65.046690.3282-6.3987
120.38660.0910.11210.1286-0.09070.31840.01470.1075-0.1056-0.1365-0.0198-0.03450.0255-0.003600.1990.0046-0.04340.1725-0.00360.1565-69.219782.0427-9.8177
130.0685-0.11730.12030.2409-0.15590.25280.0229-0.00940.0139-0.0001-0.2155-0.0152-0.22370.1921-0.00020.3635-0.0085-0.09670.37410.10860.3971-71.775731.24218.3552
140.3241-0.18550.24930.2167-0.30060.6777-0.32690.09480.27580.105-0.1425-0.237-0.29010.3173-0.10550.3056-0.162-0.16060.51140.2350.6358-62.710739.11011.3872
150.03250.0402-0.03020.0890.01380.1644-0.10940.2541-0.1878-0.1022-0.3628-0.63750.18750.1234-0.00790.35780.12440.02750.49620.01720.707-60.225414.0112-0.1107
160.11010.04410.07310.02270.02430.04790.1220.0866-0.5546-0.156-0.0369-0.09180.21020.05310.220.36020.1001-0.15190.00360.01761.0488-72.92927.93083.7543
170.553-0.2152-0.16150.08590.02440.1366-0.00690.2434-0.3364-0.0095-0.0412-0.1661-0.19640.17520.00010.36940.0353-0.01760.2419-0.04830.4657-90.733120.9973-6.1467
180.0452-0.01060.0360.12810.04590.03870.0456-0.05520.1313-0.2446-0.143-0.1714-0.07180.2129-0.010.2499-0.0136-0.03360.2587-0.00030.543-82.425134.8835-9.8872
190.13470.13710.09050.15050.09970.0628-0.09080.1499-0.0986-0.2674-0.1254-0.08320.083-0.2208-0.04980.3460.09910.03110.2078-0.28220.4283-93.33817.8294-10.5052
200.346-0.1566-0.04750.2331-0.04380.2792-0.03140.08130.0191-0.153-0.0280.12320.08050.5999-0.00380.269-0.0544-0.0730.3933-0.01620.2834-18.774814.753-37.1631
210.1710.12870.04310.17610.11980.3711-0.1466-0.35070.3280.0733-0.06160.1461-0.3330.3892-0.02890.4374-0.0801-0.04090.4047-0.14880.5431-27.036825.7027-27.8422
220.4528-0.11610.07170.2612-0.07860.7279-0.1418-0.1340.2996-0.00970.01030.32450.0151-0.3564-0.0418-0.03760.3113-0.09750.0733-0.14270.685-43.517112.7825-32.0669
230.01720.00840.05460.159-0.04760.1357-0.0945-0.24920.1492-0.07960.0230.15540.06030.02170.00010.36120.0467-0.01020.3173-0.05670.3563-35.8093-2.6108-20.1591
240.0166-0.0209-0.07880.1472-0.040.42780.09960.03850.0384-0.0538-0.16230.01620.03280.11850.00010.25910.05360.03890.3226-0.05170.2589-28.6119-0.4074-18.7291
250.15010.24270.17450.32060.29230.5083-0.03110.10040.0625-0.06370.02850.02660.02150.2203-00.2374-0.0436-0.00910.3165-0.00850.1977-101.548959.8526-12.6574
260.4161-0.10640.03080.2638-0.01520.23660.02760.00130.0445-0.03090.00040.1651-0.0642-0.130600.2361-0.0014-0.0330.2498-0.06480.234-124.14854.5983-7.5332
270.1425-0.2262-0.00640.29310.06510.28770.00690.085-0.04860.1062-0.07890.01740.0278-0.050400.29580.03270.00690.3131-0.05490.278-108.260434.252-0.6632
280.1887-0.13890.29250.126-0.25940.47090.025-0.0297-0.11820.16520.0114-0.127-0.0911-0.04430.00010.24530.03860.03680.2421-0.03860.1719-102.907339.73643.7897
290.01920.0196-0.0020.0295-0.00560.0033-0.17160.129-0.0988-0.1006-0.0835-0.0891-0.18880.0528-0.00040.38090.0416-0.08480.45170.0090.5278-85.223924.8839-21.6286
300.0570.02030.04890.02730.05560.1126-0.12910.11480.06350.2571-0.11990.0803-0.2190.1233-0.0040.4911-0.00830.03970.215-0.06730.3223-31.82352.2824-7.5082
310.04750.04090.02610.0547-0.00630.05310.1736-0.29570.08430.0943-0.1778-0.18560.1488-0.08850.00110.2990.059-0.00710.2952-0.04640.2542-105.809940.462215.1397
320.02790.0150.02930.03080.03130.03620.0261-0.1392-0.0576-0.0132-0.2172-0.16740.06270.2039-0.00030.38530.1025-0.09510.3977-0.0230.2789-49.771770.720114.2691
330.01550.0251-0.02430.0598-0.06350.0543-0.02830.1404-0.3105-0.0722-0.05420.0577-0.0004-0.06910.00020.28970.0185-0.03250.27330.0140.1734-70.717486.1126-21.8524
340.0335-0.00410.01960.0276-0.02610.0337-0.1116-0.07380.01160.18970.0482-0.04740.18640.0964-0.00030.4229-0.13210.02770.18570.03050.2454-62.2284139.5378-0.8333
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 111 )A6 - 111
2X-RAY DIFFRACTION2chain 'A' and (resid 112 through 169 )A112 - 169
3X-RAY DIFFRACTION3chain 'A' and (resid 170 through 301 )A170 - 301
4X-RAY DIFFRACTION4chain 'A' and (resid 302 through 358 )A302 - 358
5X-RAY DIFFRACTION5chain 'D' and (resid 6 through 111 )D6 - 111
6X-RAY DIFFRACTION6chain 'D' and (resid 112 through 202 )D112 - 202
7X-RAY DIFFRACTION7chain 'D' and (resid 203 through 301 )D203 - 301
8X-RAY DIFFRACTION8chain 'D' and (resid 302 through 359 )D302 - 359
9X-RAY DIFFRACTION9chain 'B' and (resid 6 through 126 )B6 - 126
10X-RAY DIFFRACTION10chain 'B' and (resid 127 through 223 )B127 - 223
11X-RAY DIFFRACTION11chain 'B' and (resid 224 through 301 )B224 - 301
12X-RAY DIFFRACTION12chain 'B' and (resid 302 through 358 )B302 - 358
13X-RAY DIFFRACTION13chain 'C' and (resid 7 through 81 )C7 - 81
14X-RAY DIFFRACTION14chain 'C' and (resid 82 through 127 )C82 - 127
15X-RAY DIFFRACTION15chain 'C' and (resid 128 through 169 )C128 - 169
16X-RAY DIFFRACTION16chain 'C' and (resid 170 through 223 )C170 - 223
17X-RAY DIFFRACTION17chain 'C' and (resid 224 through 301 )C224 - 301
18X-RAY DIFFRACTION18chain 'C' and (resid 302 through 338 )C302 - 338
19X-RAY DIFFRACTION19chain 'C' and (resid 339 through 358 )C339 - 358
20X-RAY DIFFRACTION20chain 'E' and (resid 6 through 101 )E6 - 101
21X-RAY DIFFRACTION21chain 'E' and (resid 102 through 169 )E102 - 169
22X-RAY DIFFRACTION22chain 'E' and (resid 170 through 244 )E170 - 244
23X-RAY DIFFRACTION23chain 'E' and (resid 245 through 301 )E245 - 301
24X-RAY DIFFRACTION24chain 'E' and (resid 302 through 357 )E302 - 357
25X-RAY DIFFRACTION25chain 'F' and (resid 5 through 126 )F5 - 126
26X-RAY DIFFRACTION26chain 'F' and (resid 127 through 223 )F127 - 223
27X-RAY DIFFRACTION27chain 'F' and (resid 224 through 301 )F224 - 301
28X-RAY DIFFRACTION28chain 'F' and (resid 302 through 358 )F302 - 358
29X-RAY DIFFRACTION29chain 'I' and (resid 528 through 543 )I528 - 543
30X-RAY DIFFRACTION30chain 'J' and (resid 528 through 543 )J528 - 543
31X-RAY DIFFRACTION31chain 'K' and (resid 528 through 543 )K528 - 543
32X-RAY DIFFRACTION32chain 'L' and (resid 528 through 543 )L528 - 543
33X-RAY DIFFRACTION33chain 'M' and (resid 528 through 543 )M528 - 543
34X-RAY DIFFRACTION34chain 'N' and (resid 528 through 543 )N528 - 543

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