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- PDB-4s20: Structural basis for transcription reactivation by RapA -

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Basic information

Entry
Database: PDB / ID: 4s20
TitleStructural basis for transcription reactivation by RapA
Components
  • (DNA-directed RNA polymerase subunit ...) x 4
  • 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'
  • 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'
  • RNA polymerase-associated protein RapA
KeywordsTRANSFERASE/DNA/RNA / DNA-directed RNA polymerase / transcription transferase / DNA translocase / ATPase / TRANSFERASE-DNA-RNA complex
Function / homology
Function and homology information


bacterial-type RNA polymerase core enzyme binding / ATP-dependent chromatin remodeler activity / submerged biofilm formation / replication fork processing / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation ...bacterial-type RNA polymerase core enzyme binding / ATP-dependent chromatin remodeler activity / submerged biofilm formation / replication fork processing / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / helicase activity / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription initiation / cell motility / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / response to heat / intracellular iron ion homeostasis / nucleic acid binding / protein dimerization activity / response to antibiotic / DNA repair / DNA-templated transcription / positive regulation of DNA-templated transcription / ATP hydrolysis activity / DNA binding / ATP binding / membrane / cytoplasm / cytosol
Similarity search - Function
RNA polymerase recycling, bacterial, C-terminal / RNA polymerase-associated protein RapA / RapA, N-terminal Tudor like domain 1 / RapA, N-terminal Tudor-like domain 2 / RNA polymerase recycling family C-terminal / RapA N-terminal Tudor like domain / RapA N-terminal Tudor like domain 1 / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal ...RNA polymerase recycling, bacterial, C-terminal / RNA polymerase-associated protein RapA / RapA, N-terminal Tudor like domain 1 / RapA, N-terminal Tudor-like domain 2 / RNA polymerase recycling family C-terminal / RapA N-terminal Tudor like domain / RapA N-terminal Tudor like domain 1 / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / Helicase conserved C-terminal domain / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 / 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 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DNA / DNA (> 10) / RNA / : / DNA-directed RNA polymerase subunit beta / : / : / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit beta / RNA polymerase-associated protein RapA
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.7 Å
AuthorsLiu, B. / Zuo, Y. / Steitz, T.A.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2015
Title: Structural basis for transcription reactivation by RapA.
Authors: Liu, B. / Zuo, Y. / Steitz, T.A.
History
DepositionJan 16, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 4, 2015Provider: repository / Type: Initial release
Revision 1.1Feb 18, 2015Group: Database references
Revision 1.2Mar 4, 2015Group: Database references
Revision 1.3Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
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.ptnr3_label_seq_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 / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA-directed RNA polymerase subunit alpha
B: DNA-directed RNA polymerase subunit alpha
C: DNA-directed RNA polymerase subunit beta
D: DNA-directed RNA polymerase subunit beta'
E: DNA-directed RNA polymerase subunit omega
F: DNA-directed RNA polymerase subunit alpha
G: DNA-directed RNA polymerase subunit alpha
H: DNA-directed RNA polymerase subunit beta
I: DNA-directed RNA polymerase subunit beta'
J: DNA-directed RNA polymerase subunit omega
K: RNA polymerase-associated protein RapA
L: RNA polymerase-associated protein RapA
M: 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'
N: 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'
O: 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'
P: 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,017,74422
Polymers1,017,43416
Non-polymers3106
Water00
1
A: DNA-directed RNA polymerase subunit alpha
B: DNA-directed RNA polymerase subunit alpha
C: DNA-directed RNA polymerase subunit beta
D: DNA-directed RNA polymerase subunit beta'
E: DNA-directed RNA polymerase subunit omega
L: RNA polymerase-associated protein RapA
O: 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'
P: 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)508,87211
Polymers508,7178
Non-polymers1553
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38700 Å2
ΔGint-267 kcal/mol
Surface area177720 Å2
MethodPISA
2
F: DNA-directed RNA polymerase subunit alpha
G: DNA-directed RNA polymerase subunit alpha
H: DNA-directed RNA polymerase subunit beta
I: DNA-directed RNA polymerase subunit beta'
J: DNA-directed RNA polymerase subunit omega
K: RNA polymerase-associated protein RapA
M: 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'
N: 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)508,87211
Polymers508,7178
Non-polymers1553
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area37890 Å2
ΔGint-191 kcal/mol
Surface area178030 Å2
MethodPISA
Unit cell
Length a, b, c (Å)336.090, 158.930, 255.010
Angle α, β, γ (deg.)90.00, 101.28, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22F
13A
23G
14B
24F
15B
25G
16C
26H
17D
27I
18E
28J
19F
29G
110K
210L
111M
211O

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRVALVALAA6 - 2326 - 232
21THRTHRVALVALBB6 - 2326 - 232
12THRTHRVALVALAA6 - 2326 - 232
22THRTHRVALVALFF6 - 2326 - 232
13THRTHRVALVALAA6 - 2326 - 232
23THRTHRVALVALGG6 - 2326 - 232
14THRTHRVALVALBB6 - 2326 - 232
24THRTHRVALVALFF6 - 2326 - 232
15THRTHRVALVALBB6 - 2326 - 232
25THRTHRVALVALGG6 - 2326 - 232
16TYRTYRGLUGLUCC3 - 13423 - 1342
26TYRTYRGLUGLUHH3 - 13423 - 1342
17THRTHRGLYGLYDD12 - 137612 - 1376
27THRTHRGLYGLYII12 - 137612 - 1376
18ALAALAGLUGLUEE2 - 761 - 75
28ALAALAGLUGLUJJ2 - 761 - 75
19THRTHRVALVALFF6 - 2326 - 232
29THRTHRVALVALGG6 - 2326 - 232
110PROPROLEULEUKK2 - 9628 - 968
210PROPROLEULEULL2 - 9628 - 968
111DADADGDGMM1 - 151 - 15
211DADADGDGOO1 - 151 - 15

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11

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Components

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DNA-directed RNA polymerase subunit ... , 4 types, 10 molecules ABFGCHDIEJ

#1: Protein
DNA-directed RNA polymerase subunit alpha / RNAP subunit alpha / RNA polymerase subunit alpha / Transcriptase subunit alpha


Mass: 36558.680 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoA, ECDH10B_3470 / Production host: Escherichia coli (E. coli)
References: UniProt: B1X6E7, UniProt: P0A7Z4*PLUS, DNA-directed RNA polymerase
#2: Protein DNA-directed RNA polymerase subunit beta / RNAP subunit beta / RNA polymerase subunit beta / Transcriptase subunit beta


Mass: 150820.875 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoB, O3K_23925 / Production host: Escherichia coli (E. coli)
References: UniProt: K0AVA1, UniProt: P0A8V2*PLUS, DNA-directed RNA polymerase
#3: Protein DNA-directed RNA polymerase subunit beta' / RNAP subunit beta' / RNA polymerase subunit beta' / Transcriptase subunit beta'


Mass: 156537.031 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoC, O3O_01425 / Production host: Escherichia coli (E. coli) / References: UniProt: K0BCS5, DNA-directed RNA polymerase
#4: Protein DNA-directed RNA polymerase subunit omega / RNAP omega subunit / RNA polymerase omega subunit / Transcriptase subunit omega


Mass: 10118.352 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoZ, O3O_25075 / Production host: Escherichia coli (E. coli) / References: UniProt: K0BU55, DNA-directed RNA polymerase

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Protein / DNA chain / RNA chain , 3 types, 6 molecules KLMONP

#5: Protein RNA polymerase-associated protein RapA / ATP-dependent helicase HepA


Mass: 110672.734 Da / Num. of mol.: 2 / Mutation: R350C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rapA, hepA, yabA, b0059, JW0058 / Production host: Escherichia coli (E. coli)
References: UniProt: P60240, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
#6: DNA chain 5'-D(P*AP*CP*GP*AP*CP*TP*GP*AP*GP*CP*CP*GP*AP*TP*G)-3'


Mass: 4619.012 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: template
#7: RNA chain 5'-R(P*AP*UP*CP*GP*GP*CP*UP*CP*A)-3'


Mass: 2831.743 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: transcript

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Non-polymers , 2 types, 6 molecules

#8: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

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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: 3.28 Å3/Da / Density % sol: 62.53 %
Crystal growTemperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.1 M HEPES, pH 7.0, 50 mM magnesium chloride, 5.2% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 297K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 17, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 4.7→49.53 Å / Num. all: 68812 / Num. obs: 68399 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rsym value: 0.06 / Net I/σ(I): 7.2
Reflection shellResolution: 4.7→4.95 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 2 / Rsym value: 0.314 / % possible all: 99.1

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Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
REFMAC5.7.0032refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 4JKR & 3DMQ

4jkr

3dmq
PDB Unreleased entry


Resolution: 4.7→20 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.86 / SU B: 436.487 / SU ML: 2.166 / Cross valid method: THROUGHOUT / ESU R Free: 1.806
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.36926 3240 5 %RANDOM
Rwork0.27337 ---
obs0.27829 60931 93.19 %-
all-68399 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 292.879 Å2
Baniso -1Baniso -2Baniso -3
1--0.07 Å20 Å20.01 Å2
2---0.01 Å20 Å2
3---0.08 Å2
Refinement stepCycle: LAST / Resolution: 4.7→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms60144 1004 6 0 61154
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01961816
X-RAY DIFFRACTIONr_bond_other_d0.0020.0259655
X-RAY DIFFRACTIONr_angle_refined_deg1.1011.95783707
X-RAY DIFFRACTIONr_angle_other_deg0.8433137036
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.657528
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.80324.0852962
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.6761510963
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.04315565
X-RAY DIFFRACTIONr_chiral_restr0.0630.29445
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02169276
X-RAY DIFFRACTIONr_gen_planes_other0.0010.0213795
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it6.29314.17130313
X-RAY DIFFRACTIONr_mcbond_other6.29314.17130312
X-RAY DIFFRACTIONr_mcangle_it11.29721.24837774
X-RAY DIFFRACTIONr_mcangle_other11.29721.24837775
X-RAY DIFFRACTIONr_scbond_it4.50114.08931499
X-RAY DIFFRACTIONr_scbond_other4.50114.08831500
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other8.65321.05245934
X-RAY DIFFRACTIONr_long_range_B_refined18.98468311
X-RAY DIFFRACTIONr_long_range_B_other18.98468312
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A126110.08
12B126110.08
21A131400
22F131400
31A126140.08
32G126140.08
41B126130.08
42F126130.08
51B131360
52G131360
61C708860.01
62H708860.01
71D683130.01
72I683130.01
81E44800.02
82J44800.02
91F126180.08
92G126180.08
101K539800.05
102L539800.05
111M10830.02
112O10830.02
LS refinement shellResolution: 4.7→4.815 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.433 180 -
Rwork0.393 3705 -
obs--80.97 %
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)
110.2865-6.24815.0047.3106-3.10175.4572-0.88481.7580.37231.0369-0.2779-0.0986-0.3663-0.97171.16271.16780.43620.4631.9266-0.01891.162619.152976.8544215.4675
211.9976-2.3570.52892.75221.12991.87281.42950.11211.2844-0.5452-0.6280.7501-0.6202-1.183-0.80152.20511.2602-0.28182.8210.52372.766-20.146196.5212208.5479
31.49070.3496-0.14132.65080.42813.52270.1308-0.1832-0.00850.518-0.2992-0.39230.6208-0.47780.16840.4956-0.1261-0.13390.51640.06911.321218.38565.6744262.0619
40.3518-0.3362-0.53032.8409-0.48453.2284-0.2686-0.00650.41940.17050.27570.60140.5984-1.9343-0.00710.37960.254-0.04972.7061-0.20971.7674-20.147263.9798262.87
53.3781-0.88041.92780.5199-0.172710.89510.4667-0.5737-0.04220.1479-0.1551-0.87350.403-0.45-0.31161.77650.158-0.22273.33-0.09793.5911-36.537255.2993230.4953
69.17354.6067-0.99743.9404-0.32380.87170.0092-0.5799-1.84410.0911-0.1798-1.258-0.7361-0.88660.17062.6101-0.075-0.10221.87170.14250.8822-18.30169.5718401.8641
710.7595-0.36362.87490.1523-0.2792.45230.6560.9015-0.48120.4032-0.00590.27120.9249-1.2272-0.65012.6134-0.74140.3112.98560.37032.9255-57.4204-9.8588393.8458
81.6834-0.5665-0.4832.2378-0.12061.99720.06660.18160.2134-0.16040.063-0.5206-0.2105-0.1122-0.12961.6259-0.0897-0.08110.44480.11531.1572-1.234320.7207358.2664
90.425-0.2087-0.11610.638-0.8082.1381-0.06180.6362-0.2832-0.22470.28880.61490.1693-1.0957-0.22691.1837-0.39-0.42181.7483-0.23641.7625-36.983422.1404343.233
104.72182.080.62112.58082.57593.36470.79010.4158-0.27720.2644-0.011-0.8699-0.28950.3166-0.77913.15510.0738-0.18743.77790.35234.6888-64.620430.8768367.9886
112.8392-0.8307-0.20731.6017-0.57252.77880.46590.06440.50080.0753-0.25990.3225-0.6302-0.5418-0.2061.2930.11650.07661.0891-0.3691.3618-31.956375.1416397.5719
123.20320.8306-0.08912.26381.04572.15830.4356-0.2170.0810.3284-0.47750.40070.7306-0.61350.04190.98070.0107-0.24861.3017-0.51041.26054.626811.4067214.1259
130.3618-0.43470.13730.8988-0.09770.0750.00440.27760.6797-1.1761-0.354-0.8022-0.24710.27010.34954.1085-0.22780.19513.985-0.03713.164-18.0630.2214349.027
147.8422-1.2321-0.41020.68890.77921.1533-0.3664-0.3234-0.4574-0.1346-0.13510.2211-0.02630.10240.50152.9222-0.1415-0.09432.3135-0.16232.674-14.991128.0206354.1978
158.0772-3.0819-2.696913.50427.19024.0028-2.3560.1482.68992.29582.0141.13391.67240.75340.3424.44410.41120.55064.0096-0.6222.2692-1.041455.9619264.492
163.63371.05790.49322.06163.79147.7333-0.64710.078-0.39240.1526-0.63240.3170.4522-1.27141.27952.7061-0.24420.21512.27110.22752.88794.198858.3214260.8477
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 232
2X-RAY DIFFRACTION2B6 - 232
3X-RAY DIFFRACTION3C3 - 1342
4X-RAY DIFFRACTION4D12 - 1376
5X-RAY DIFFRACTION5E2 - 76
6X-RAY DIFFRACTION6F6 - 232
7X-RAY DIFFRACTION7G6 - 232
8X-RAY DIFFRACTION8H3 - 1342
9X-RAY DIFFRACTION9I12 - 1376
10X-RAY DIFFRACTION10J2 - 76
11X-RAY DIFFRACTION11K2 - 962
12X-RAY DIFFRACTION12L2 - 962
13X-RAY DIFFRACTION13M1 - 15
14X-RAY DIFFRACTION14N1 - 9
15X-RAY DIFFRACTION15O1 - 15
16X-RAY DIFFRACTION16P1 - 9

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