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- PDB-6duq: Structure of a Rho-NusG KOW domain complex -

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Basic information

Entry
Database: PDB / ID: 6duq
TitleStructure of a Rho-NusG KOW domain complex
Components
  • (Transcription ...) x 2
  • rU12
KeywordsTRANSCRIPTION/RNA / Rho / NusG / RecA / ATPase / TRANSCRIPTION / TRANSCRIPTION-RNA complex
Function / homology
Function and homology information


DNA-templated transcription elongation / ATP-dependent activity, acting on RNA / transcription elongation-coupled chromatin remodeling / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / helicase activity / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ribosome biogenesis ...DNA-templated transcription elongation / ATP-dependent activity, acting on RNA / transcription elongation-coupled chromatin remodeling / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / helicase activity / DNA-templated transcription termination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ribosome biogenesis / hydrolase activity / ATP hydrolysis activity / RNA binding / ATP binding / membrane / identical protein binding / cytosol
Similarity search - Function
Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / : ...Transcription termination factor Rho / Rho termination factor, N-terminal / Rho termination factor, RNA-binding domain / Transcription termination factor Rho, ATP binding domain / Rho termination factor, RNA-binding domain / Rho termination factor, N-terminal domain / Rho RNA-binding domain profile. / Rho termination factor, N-terminal domain / Rho termination factor, N-terminal domain superfamily / : / Transcription antitermination protein, NusG / Transcription antitermination protein, NusG, bacteria, conserved site / Transcription termination factor nusG signature. / NusG-like / Transcription termination factor nusG / Cold shock domain / Cold shock protein domain / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Nucleic acid-binding proteins / KOW (Kyprides, Ouzounis, Woese) motif. / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Translation protein SH3-like domain superfamily / KOW / KOW motif / Ribosomal protein L2, domain 2 / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / RNA / RNA (> 10) / Transcription termination/antitermination protein NusG / Transcription termination factor Rho / Transcription termination/antitermination protein NusG / Transcription termination factor Rho
Similarity search - Component
Biological speciesEscherichia coli M718 (bacteria)
Escherichia coli M605 (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.7 Å
AuthorsBerger, J.M. / Lawson, M.R.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM071747 United States
Other privateG. Harold and Leila Y. Mathers Foundation United States
CitationJournal: Mol. Cell / Year: 2018
Title: Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.
Authors: Lawson, M.R. / Ma, W. / Bellecourt, M.J. / Artsimovitch, I. / Martin, A. / Landick, R. / Schulten, K. / Berger, J.M.
History
DepositionJun 21, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 5, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Apr 17, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Jan 29, 2020Group: Derived calculations / Category: pdbx_struct_assembly_gen / Item: _pdbx_struct_assembly_gen.asym_id_list
Revision 1.5Mar 13, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.value / _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.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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
L: Transcription termination factor Rho
A: Transcription termination factor Rho
G: Transcription termination factor Rho
B: Transcription termination factor Rho
H: Transcription termination factor Rho
C: Transcription termination factor Rho
I: Transcription termination factor Rho
D: Transcription termination factor Rho
K: Transcription termination factor Rho
F: Transcription termination factor Rho
J: Transcription termination factor Rho
E: Transcription termination factor Rho
M: Transcription termination/antitermination protein NusG
N: Transcription termination/antitermination protein NusG
O: Transcription termination/antitermination protein NusG
P: Transcription termination/antitermination protein NusG
Q: Transcription termination/antitermination protein NusG
R: Transcription termination/antitermination protein NusG
S: Transcription termination/antitermination protein NusG
T: Transcription termination/antitermination protein NusG
U: Transcription termination/antitermination protein NusG
V: Transcription termination/antitermination protein NusG
W: Transcription termination/antitermination protein NusG
X: Transcription termination/antitermination protein NusG
Y: rU12
Z: rU12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)662,11662
Polymers655,90626
Non-polymers6,21036
Water0
1
L: Transcription termination factor Rho
G: Transcription termination factor Rho
H: Transcription termination factor Rho
I: Transcription termination factor Rho
K: Transcription termination factor Rho
J: Transcription termination factor Rho
P: Transcription termination/antitermination protein NusG
Q: Transcription termination/antitermination protein NusG
R: Transcription termination/antitermination protein NusG
V: Transcription termination/antitermination protein NusG
W: Transcription termination/antitermination protein NusG
X: Transcription termination/antitermination protein NusG
Z: rU12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)331,05831
Polymers327,95313
Non-polymers3,10518
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Transcription termination factor Rho
B: Transcription termination factor Rho
C: Transcription termination factor Rho
D: Transcription termination factor Rho
F: Transcription termination factor Rho
E: Transcription termination factor Rho
M: Transcription termination/antitermination protein NusG
N: Transcription termination/antitermination protein NusG
O: Transcription termination/antitermination protein NusG
S: Transcription termination/antitermination protein NusG
T: Transcription termination/antitermination protein NusG
U: Transcription termination/antitermination protein NusG
Y: rU12
hetero molecules


Theoretical massNumber of molelcules
Total (without water)331,05831
Polymers327,95313
Non-polymers3,10518
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)126.350, 126.320, 166.820
Angle α, β, γ (deg.)89.94, 89.90, 60.01
Int Tables number1
Space group name H-MP1

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Components

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Transcription ... , 2 types, 24 molecules LAGBHCIDKFJEMNOPQRSTUVWX

#1: Protein
Transcription termination factor Rho / ATP-dependent helicase Rho


Mass: 47396.562 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli M718 (bacteria) / Gene: rho, ECJG_05123 / Production host: Escherichia coli (E. coli)
References: UniProt: F4TMM7, UniProt: P0AG30*PLUS, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
#2: Protein
Transcription termination/antitermination protein NusG


Mass: 6657.404 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli M605 (bacteria) / Gene: nusG, ECIG_05396 / Production host: Escherichia coli (E. coli) / References: UniProt: F4T6L5, UniProt: P0AFG0*PLUS

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RNA chain , 1 types, 2 molecules YZ

#3: RNA chain rU12


Mass: 3629.032 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 3 types, 36 molecules

#4: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: BeF3

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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: 3.52 Å3/Da / Density % sol: 65.02 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 95 mM potassium glutamate, 50 mM Tris-HCl pH 8.0, 1 mM spermine, 0.5% PEG 8K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 25, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11587 Å / Relative weight: 1
ReflectionResolution: 3.68→40 Å / Num. obs: 94588 / % possible obs: 97.8 % / Redundancy: 2.2 % / Net I/σ(I): 8.9
Reflection shellResolution: 3.68→3.79 Å / Redundancy: 2.2 % / % possible all: 97.6

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.7→39.03 Å / SU ML: 0.77 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 40.59 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3 1473 1.58 %
Rwork0.287 --
obs0.288 93095 97.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.7→39.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms42502 242 384 0 43128
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00744350
X-RAY DIFFRACTIONf_angle_d0.77259954
X-RAY DIFFRACTIONf_dihedral_angle_d23.01416986
X-RAY DIFFRACTIONf_chiral_restr0.0456906
X-RAY DIFFRACTIONf_plane_restr0.0057660
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.7-3.81930.43281020.39788354X-RAY DIFFRACTION98
3.8193-3.95570.4164960.39438329X-RAY DIFFRACTION97
3.9557-4.11390.38181980.37778268X-RAY DIFFRACTION98
4.1139-4.30090.3712970.35588404X-RAY DIFFRACTION98
4.3009-4.52740.37351980.35448295X-RAY DIFFRACTION98
4.5274-4.81060.3391980.32548360X-RAY DIFFRACTION98
4.8106-5.18120.3025970.30318416X-RAY DIFFRACTION98
5.1812-5.70120.30261970.29058291X-RAY DIFFRACTION98
5.7012-6.52280.3702990.28278352X-RAY DIFFRACTION98
6.5228-8.20550.21121920.26958246X-RAY DIFFRACTION97
8.2055-39.0320.2644990.20688307X-RAY DIFFRACTION97
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)
13.8533-1.44421.33593.98940.75483.93170.260.1065-0.1827-0.5875-0.9425-0.67960.7737-0.99250.58121.52580.01420.18121.43270.03421.3334-116.5391-0.997239.683
22.0986-0.60.86133.2924-0.85142.4884-0.3517-0.477-0.1941-1.1509-0.0251.4162-1.1035-0.46310.22352.93110.58640.40191.33090.06471.7085-96.767145.835339.6688
33.30741.505-0.43011.9466-1.86084.59830.04040.20280.24570.259-0.285-0.3513-1.27590.37160.35281.7139-0.27340.04861.3084-0.17361.8157-47.497552.225239.4773
45.36240.2714-0.18882.3564-1.15421.08730.68870.95851.3057-0.3076-1.1279-0.22220.17611.4940.18211.80840.0631-0.25283.4666-0.51911.1799-16.812511.405339.6419
52.8274-0.0101-0.61093.36631.36383.8282-0.71240.05980.0719-0.31550.31960.59350.75130.70730.46861.84090.0717-0.18531.13580.17041.7319-36.1054-34.280839.5785
63.0231.4436-0.01992.96870.94133.2816-0.88560.9689-0.8709-0.08690.5912-0.74131.2763-1.00840.18332.6832-0.9558-0.35141.84260.23481.3883-86.5905-40.332239.6774
71.82410.28621.2683.3151-1.01333.1151-0.7583-0.1654-0.6567-0.08720.39860.4654-0.544-1.41790.36161.67380.16770.28221.9316-0.05351.7629-160.46889.0967123.0131
83.46962.15940.32215.2426-0.97010.6272-0.71141.35550.61220.32780.58791.2466-1.47281.1168-0.05442.6286-0.8680.32112.4143-0.31591.1376-109.819215.3352122.9977
92.2616-1.0201-1.02222.8071-0.35533.29910.2388-0.0938-0.6447-0.466-0.6877-0.3880.02581.28770.33321.03470.3003-0.07841.8668-0.0911.9836-79.7706-24.2102122.8631
101.9838-0.8443-1.06766.3817-0.58342.9647-0.102-0.4450.2475-1.6462-0.1492-1.64632.05830.53970.12973.32080.9892-0.47151.9134-0.22371.0284-99.883-71.1477123.0414
114.40770.30240.44763.340.93783.5286-0.32131.38920.46110.3949-0.5253-0.19411.2892-0.1830.77081.3402-0.3380.1421.79310.19351.3956-148.9037-77.2084123.0665
127-1.48831.05472.12830.58942.81380.65120.2664-1.8566-0.0854-0.87680.6944-0.4896-1.91460.03231.18110.25470.15423.50710.62331.348-179.5024-36.675123.1276
132.52880.92840.4284.43231.50453.30291.4524-2.1684-2.73620.0848-2.2229-2.4544-0.8835-1.636-0.01941.6019-1.0313-0.20311.45672.12973.3784-98.75018.050668.8884
145.9173-1.99683.09883.77690.49643.11490.3409-1.6441-0.9064-0.0041-0.1661-1.3269-0.4284-0.644-0.10751.678-0.01670.46151.41820.80871.4707-80.72334.544468.712
152.3196-2.8191.14763.0741-2.20993.1373-0.219-0.0793-0.17282.27330.22153.03480.2982-0.2753-0.07072.5992-0.36221.35730.9791-0.38733.1097-48.741732.234268.5868
165.65651.468-1.53673.7816-3.5962.87830.7303-0.1039-1.55651.265-0.18412.0425-0.41191.2851-0.39061.34-0.8239-0.06411.5851-1.32191.6212-34.69463.310368.6895
172.18410.0313-1.06390.38050.62171.42-2.0249-2.93313.84440.27741.0533-1.44971.05130.86690.20921.7554-1.0812-2.5785-0.3648-3.61752.8602-52.7432-23.313868.7835
182.8220.1289-2.02997.98812.50923.3234-0.575-0.38471.71481.26640.8565-0.06671.06080.0154-0.17041.9155-0.1161-0.84690.9853-0.02141.4485-84.757-20.943368.909
193.56661.21252.09060.95690.61563.1524-1.3776-1.8186-3.59610.30050.74621.2078-1.13350.60870.07041.03810.91871.95112.55641.16283.2525-143.7506-1.8607152.133
202.73990.55492.27776.0695-2.25042.7412-0.5654-0.432-1.70431.03150.84530.0094-0.77430.0442-0.03341.65660.1321.07341.7135-0.08441.3914-111.7602-4.2504152.0018
211.90642.5607-1.09773.0257-0.89362.58661.135-1.64612.67580.7148-1.15882.17470.5039-0.06880.0051.58190.26350.94422.777-1.6143.1171-97.7127-33.1216151.9883
226.3578-1.7609-3.40874.7286-0.87033.45530.408-1.58550.9658-0.16760.10021.5950.72040.8713-0.36441.21960.5477-0.66741.8414-0.62341.3574-115.711-59.7662152.2458
232.4256-2.5774-0.34094.00581.74442.323-0.25040.31250.71612.37670.1334-3.36110.1376-0.36530.01782.1352-0.0769-1.75581.91390.41213.1454-147.8075-57.3684152.337
245.53962.0321.23084.35223.20842.99560.9213-0.53030.56211.5107-0.5228-1.60560.489-1.0127-0.21811.2675-0.0296-0.49042.18980.9031.2623-161.7685-28.3998152.3094
254.67911.1511-0.37960.2901-0.25783.42311.61090.5640.8005-0.00460.82350.7388-1.7159-0.0758-2.29593.5047-0.72110.12963.15521.45982.1416-101.332328.3886101.2577
260.64421.2121-0.3072.3997-0.10621.93260.2704-0.2001-0.5351-1.18011.4137-1.5190.19231.8342-1.31173.6460.73941.36273.3065-0.39382.3875-28.809424.6478101.2914
271.4341-1.6515-0.25841.90280.38992.99261.5995-0.5505-1.039-0.26240.35981.31641.649-0.2111-1.57493.2511-0.6031-1.46113.6993-0.96292.5089-68.9638-36.9351101.4126
282.1666-2.57920.22713.22580.05431.28681.06770.23711.6929-0.42010.061-1.5092-0.2830.7791-0.97172.6635-0.11851.24984.64311.09362.1202-127.449411.0169184.6065
292.85710.3583-0.28570.09240.23071.44130.55971.3181-2.09230.39710.9074-0.48481.930.626-1.14473.9824-0.10690.40532.9491-1.71862.7322-94.5032-53.6674184.7171
300.43741.5743-0.49585.6395-1.74510.55550.3317-0.22070.45610.21061.53041.3305-0.2417-0.8421-1.32173.77150.7047-1.62893.47720.39482.1976-167.4772-49.9055184.8685
314.809-0.1048-0.1442.04340.98035.77681.6946-0.64270.08240.74061.5764-0.7842-0.23210.983-3.42892.08860.332-0.014.6431-0.63623.2546-65.703944.8216101.467
323.08850.8966-0.43542.81120.10494.59481.5266-1.1607-0.48660.2691.5751-0.37791.095-0.2263-2.96563.9121-1.3292-0.64483.37820.42423.3359-33.4882-14.4043101.7748
330.3779-0.0005-0.84244.09471.68394.80961.1394-0.26280.27810.8811.95831.5426-0.6043-0.9223-2.9965.01780.91280.41292.58880.69933.8824-100.6366-13.3364101.5023
343.6492-0.7970.30141.67750.01422.41431.4656-0.51580.1831.36770.8877-2.00210.28830.3755-2.42254.32270.9424-0.87213.1041-0.87153.8169-94.7516-12.0919184.4906
352.6363-1.1753-1.34730.68720.00373.19651.4496-0.9101-0.87480.40471.48250.48690.8305-1.5474-2.81422.31430.4177-0.38935.1140.78123.7765-130.2133-69.9006185.1837
361.16840.01850.93040.00470.04661.45171.241-1.11930.8740.06871.36451.0112-1.4108-0.8665-2.48594.6009-1.28571.14423.4646-0.02443.8208-163.5308-10.2161184.8679
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND RESSEQ 1:128
2X-RAY DIFFRACTION2CHAIN 'B' AND RESSEQ 1:128
3X-RAY DIFFRACTION3CHAIN 'C' AND RESSEQ 1:128
4X-RAY DIFFRACTION4CHAIN 'D' AND RESSEQ 1:128
5X-RAY DIFFRACTION5CHAIN 'E' AND RESSEQ 1:128
6X-RAY DIFFRACTION6CHAIN 'F' AND RESSEQ 1:128
7X-RAY DIFFRACTION7CHAIN 'G' AND RESSEQ 1:128
8X-RAY DIFFRACTION8CHAIN 'H' AND RESSEQ 1:128
9X-RAY DIFFRACTION9CHAIN 'I' AND RESSEQ 1:128
10X-RAY DIFFRACTION10CHAIN 'J' AND RESSEQ 1:128
11X-RAY DIFFRACTION11CHAIN 'K' AND RESSEQ 1:128
12X-RAY DIFFRACTION12CHAIN 'L' AND RESSEQ 1:128
13X-RAY DIFFRACTION13CHAIN 'A' AND RESSEQ 129:417
14X-RAY DIFFRACTION14CHAIN 'B' AND RESSEQ 129:417
15X-RAY DIFFRACTION15CHAIN 'C' AND RESSEQ 129:417
16X-RAY DIFFRACTION16CHAIN 'D' AND RESSEQ 129:417
17X-RAY DIFFRACTION17CHAIN 'E' AND RESSEQ 129:417
18X-RAY DIFFRACTION18CHAIN 'F' AND RESSEQ 129:417
19X-RAY DIFFRACTION19CHAIN 'G' AND RESSEQ 129:417
20X-RAY DIFFRACTION20CHAIN 'H' AND RESSEQ 129:417
21X-RAY DIFFRACTION21CHAIN 'I' AND RESSEQ 129:417
22X-RAY DIFFRACTION22CHAIN 'J' AND RESSEQ 129:417
23X-RAY DIFFRACTION23CHAIN 'K' AND RESSEQ 129:417
24X-RAY DIFFRACTION24CHAIN 'L' AND RESSEQ 129:417
25X-RAY DIFFRACTION25CHAIN 'M'
26X-RAY DIFFRACTION26CHAIN 'N'
27X-RAY DIFFRACTION27CHAIN 'O'
28X-RAY DIFFRACTION28CHAIN 'P'
29X-RAY DIFFRACTION29CHAIN 'Q'
30X-RAY DIFFRACTION30CHAIN 'R'
31X-RAY DIFFRACTION31CHAIN 'S'
32X-RAY DIFFRACTION32CHAIN 'T'
33X-RAY DIFFRACTION33CHAIN 'U'
34X-RAY DIFFRACTION34CHAIN 'V'
35X-RAY DIFFRACTION35CHAIN 'W'
36X-RAY DIFFRACTION36CHAIN 'X'

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