SUPPLEMENTARY INFORMATION
|
|
- Marsha Harper
- 5 years ago
- Views:
Transcription
1 Supplementary Table S1 Kinetic Analyses of the AMSH-LP mutants AMSH-LP K M (μm) k cat x 10-3 (s -1 ) WT 71.8 ± ± 65.4 T353A 76.8 ± ± 3.7 F355A 58.9 ± ± 0.30 proximal S358A 75.1 ± ± 5.3 binding C402S 33.9 ± ± 0.12 F407A 30.2 ± ± 1.7 E329A 209 ± ± 19.7 distal F332A 897 ± ± 60.9 binding M370A 1277 ± ±.8 E292A N.D. N.D. active S357A 71.2 ± ± 0.89 site D360A N.D. N.D. N.D., not detectable; the mean values±s.e.m. in three independent experiments are shown. 1
2 Supplementary Table S2 Data collection, phasing, and refinement statistics AMSH-LP E292A K63-Ub 2 AMSH-LP Native Native Zn SAD Data Collection X-ray source PF-AR NW12A PF-AR NW12A Wavelength (Å) Space group P2 1 P6 5 P6 5 Unit cell parameter a = 38.1 Å b = 97.4 Å c = 87.9 Å β = 97.5 a = b = 81.9 Å c = 64.7 Å a = b = 82.1 Å c = 64.9 Å Resolution (Å) ( ) ( ) ( ) Unique reflections 83,683 76,845 17,081 Total relections 3,804,643 1,738,510 1,312,874 Completeness (%) 97.3 (90.7) 99.4 (98.3) 99.0 (.0) I / σ(i) 16.9 (3.20) 34.3 (14.1) 162 (147) R sym (0.267) (0.158) (0.153) Phasing Statistics Number of zinc sites 2 Phasing power R culis Mean overall figure of merit (Centric/Acentric) 0.118/0.565 Refinement Statistics Number of atoms: protein; ligand/ion 72; ; 328 Rmsd bond length (Å) Rmsd bond angle ( ) Average B factors (Å 2 ) :protein; liand/ion 13.9; ; 23.3 Residues in core region (%) Residues in additionally allowed region (%) Residues in generously allowed region (%) Residues in disallowed region (%) R work, R free 0.185, , The numbers in parentheses are for the highest resolution shell. Rsym = Σ Iavg - Ii /ΣIi. Rcullis = Σ FPH - FP - FH(calc) /Σ FPH. Rwork = Σ Fo - Fc /ΣFo for reflections of working set. Rfree = Σ Fo - Fc /ΣFo for reflections of test set (5% of total unique reflections). 2
3 Supplementary Figure Legends Supplementary Figure S1 Specific cleavage of Lys63-linked polyubiquitin chains by the AMSH-LP DUB domain and by full-length AMSH-LP. a, The AMSH-LP DUB domain can cleave Lys63-linked polyubiquitin chains but not Lys48-linked chains. Reaction mixtures were analyzed by SDS-PAGE after 20-hour reactions. b, Full-length AMSH-LP can cleave Lys63-linked polyubiquitin chains but not Lys48-linked chains. In contrast, the USP family DUB, UBPY, can cleave both Lys48- and Lys63-linked polyubiquitin chains. Reaction mixtures were analyzed by SDS-PAGE after 20-hour reactions. Supplementary Figure S2 Comparison of AfJAMM and the AMSH-LP DUB domain. a, Sequence alignment of AfJAMM and the AMSH-LP DUB domain. The secondary structure of AMSH-LP is shown above the alignment. Identical residues are highlighted by red background. Gray, orange, and green bars below the alignment correspond to the JAMM core, Ins-1, and Ins-2, respectively. b, Crystal structures of AfJAMM and the AMSH-LP DUB domain are shown as cartoon models in a similar orientation. Zn 2+ and the coordinating water molecule in the active site are shown as grey and red spheres, respectively. Residues involved in Zn 2+ coordination are shown as stick models. Ins-1 and Ins-2 of AMSH-LP are colored orange and green, respectively. Supplementary Figure S3 Comparison of the DUB domains of AMSH-LP and AMSH. a, Sequence alignment of the DUB domains of AMSH-LP and AMSH from representative organisms. The drawing schemes are the same as in Fig. 5a. b, Conservation of the DUB domains of AMSH and AMSH-LP is mapped on the AMSH-LP surface. The drawing schemes are the same as in Fig. 5b. 3
4 Supplementary Figure S4 The closed active site of AMSH-LP. AMSH-LP and K63-Ub 2 are shown as molecular surface and cartoon representations, respectively. The side chains of Asp321 and Phe407, which cover the active site, are colored orange and green, respectively. The proximal and distal ubiquitins are colored pink and cyan, respectively. Supplementary Figure S5 Cleavage of Lys48-linked polyubiquitin chains by the DUB domain of AMSH-LP mutants Supplementary Figure S6 Sequence alignment of 10 human JAMM proteins (6 DUBs and 4 non-dub proteins). Common sequences for JAMM DUBs are surrounded by rectangles. The secondary structure of AMSH-LP and putative signature sequences (φ; aliphatic residues, X; any residues) are shown above the alignment. MYSM1 has a 23-residue insertion between α3 and β7. Supplementary Figure S7 Sequence alignment of the DUB domains of AMSH-LP, AMSH, and POH1/Rpn11 from the representative organisms The secondary structure of AMSH-LP is shown above the alignment. % and more than 60% identical residues are highlighted by red and yellow backgrounds, respectively. Gray, orange, and green bars below the alignment correspond to the JAMM core, Ins-1, and Ins-2, respectively. Green squares indicate the residues involved in Zn 2+ coordination. Pink and cyan triangles indicate residues that form hydrophobic interactions with the proximal and distal ubiquitins, respectively. Pink and cyan circles indicate residues that form hydrogen bonds with the proximal and distal ubiquitins, respectively. Open circles indicate that only the main chain atoms are involved in the hydrogen bonding, whereas filled circles indicate that only the side chain atoms or both the side chain and main chain atoms are involved in the hydrogen bonding. 4
5 Supplementary Figure S8 Sample images of tricine SDS-PAGE gels stained by coomassie brilliant blue for quantification of ubiquitin monomers produced by DUB reactions. 5
6 a b linkage Lys48 Lys63 linkage Lys48 Lys63 AMSH-LP DUB (kda) AMSH-LP DUB - AMSH-LP UBPY - AMSH-LP UBPY UBPY AMSH-LP polyubiquitin chain polyubiquitin chain ubiquitin monomer ubiquitin monomer Fukai, S. Supplementary Figure S1 6
7 a β1 α1 β2 β3 β4 β5 α2 β6 H.sapiens_AMSH-LP-ss A.fulgidus_JAMM-ss H.sapiens_AMSH-LP E G L R C V V L P E D L C H K F L Q L A E S N T V R G I E T C G I L C G K L T H N E F T I T H V I V P K Q S A G P D Y C D M E N V E E L F N V Q D Q H D L L T L G W I H T H P T A.fulgidus_JAMM.. G S S M K I S R G L L K T I L E A A K S A H.. P D E F I A L L S G S K.... D V M D E L I F L P F V S G S V S A V I H L D M L P I G M K V F G T V H S H P S α3 β7 β8 α4 β9 β10 β11 H.sapiens_AMSH-LP-ss A.fulgidus_JAMM-ss H.sapiens_AMSH-LP Q T A F L S S V D L H T H C S Y Q L M L P E A I A I V C S.. P K H K D T G I F R L T N A G M L E V S A C K K K G F H P H T K E P R L F S I C K H V L V K. D I K I I V L D L R A.fulgidus_JAMM P S C R P S E E D L S L F T R F G..... K Y H I I V C Y P Y D E N S W K C Y N R K G E E V E L E V V E K D b Ins-2 Ins-1 disordered region H.sapiens AMSH-LP A.fulgidus JAMM Fukai, S. Supplementary Figure S2 7
8 a β1 α1 β2 β3 β4 β5 α2 β H.sapiens_AMSH-LP E G L R C V V L P E D L C H K F L Q L A E S N T V R G I E T C G I L C G K L T H N E F T I T H V I V P K Q S A G P D Y C D M E N V E E L F N V Q D Q H D L L T L G W I H T H P T Q T M.musculus_AMSH-LP E G L R C V V L S R D L C H K F L L L A D S N T V R G I E T C G I L C G K L T H N E F T I T H V V V P K Q S A G P D Y C D V E N V E E L F N V Q D Q H G L L T L G W I H T H P T Q T X.tropicalis_AMSH-LP D G L R P V V L P R D L S Q R F L Q L A E A N T S R G I E T C G I L C G K L T H D E F T I T H V I V P K Q S A G P D Y C D M E N V E E L F N V Q D Q H N L L T L G W I H T H P T Q T H.sapiens_AMSH D G L R H V V V P G R L C P Q F L Q L A S A N T A R G V E T C G I L C G K L M R N E F T I T H V L I P K Q S A G S D Y C N T E N E E E L F L I Q D Q Q G L I T L G W I H T H P T Q T D.melanogaster_AMSH G S L R L V Y V P G D T M E V F L K L A L A N T S K N I E T C G V L A G H L S Q N Q L Y I T H I I T P Q Q Q G T P D S C N T M H E E Q I F D V Q D Q M Q L I T L G W I H T H P T Q T S.pombe_AMSH K P L R T I Y L P K L L K K V F L D V V K P N T K K N L E T C G I L C G K L R Q N A F F I T H L V I P L Q E A T S D T C G T T D E A S L F E F Q D K H N L L T L G W I H T H P T Q T α3 β7 β8 α4 β9 β10 β H.sapiens_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H K D T G I F R L T. N A G M L E V S A C K K K G. F H P H T. K E P R L F S I C K H V L V K. D I K I I V L D L R.. M.musculus_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H K D T G I F R L T. N A G M L E V S T C K K K G. F H P H T. K D P K L F S I C S H V L V K. D I K T T V L D L R.. X.tropicalis_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H N D T G I F R L T. S A G M L E V S A C K K K G. F H P H S. K E P R Q F N T C R H V T V Q. D A G I T V L D L R.. H.sapiens_AMSH A F L S S V D L H T H C S Y Q M M L P E S V A I V C S P K F Q E T G F F K L T. D H G L E E I S S C R Q K G. F H P H S. K D P P L F C S C S H V T V V. D R A V T I T D L R.. D.melanogaster_AMSH A F L S S V D L H T H C S Y Q I M M P E A L A I V C A P K Y N T T G F F I L T P H Y G L D Y I A Q C R Q S G. F H P H P. N D P P L F M E A Q H I R M D N Q A K I K V I D L R R. S.pombe_AMSH C F M S S V D L H T H C S Y Q L M L P E A I A I V M A P S K N T S G I F R L L D P E G L Q T I V K C R K P G L F H P H E G K V Y T M V A Q P G H V R E I. N S K L Q V V D L R V K b Ins-1 active site Ins-1 active site proximal ubiquitin 90 proximal ubiquitin distal ubiquitin Ins-2 distal ubiquitin binding site distal ubiquitin Ins-2 proximal ubiquitin binding site Fukai, S. Supplementary Figure S3 8
9 Phe407 Asp321 Lys63 Gly76 Fukai, S. Supplementary Figure S4 9
10 (kda) T353A Proximal binding F355A S358A AMSH-LP + K48-polyUb Distal binding C402S F407A E329A F332A M370A E292A S357A D360A wt K48-polyUb only Active site - AMSH-LP K48- polyub Ub Fukai, S. Supplementary Figure S5 10
11 β1 α1 β2 264 EXXG φ φ XG 303 AMSH-LP EGLRCVVLP---EDLCHKFLQLAESNTVRGI---ETCGILCGKLTH AMSH DGLRHVVVP---GRLCPQFLQLASANTARGV---ETCGILCGKLMR BRCC36 MAVQVVQAVQAVHLESDAFLVCLNHALSTEKE--EVMGLCIGELND Rpn11 VDTAEQVY-----ISSLALLKMLKHGRAGVPM--EVMGLMLGEFVD MYSM1 EEKQEPFQV---KVASEALLIMDLHAHVSMA---EVIGLLGGRYSE CSN5 PWTKDHHYFKYCKISALALLKMVMHARSGGNL--EVMGLMLGKVDG eif3γ eif3η Rpn8 CSN6 SAVKQVQID---GLVVLKIIKHYQEEGQGTE---VVQGVLLGLVVE PGGRVVRLH---PVILASIVDSYERRNEGAA---RVIGTLLGTVDK LAVQKVVVHP---LVLLSVVDHFNRIGKVGNQK-RVVGVLLGSWQK TGSVSVALHP---LVILNISDHWIRMRSQEGRPVQVIGALIGKQEG β6 α3 β7 β8 φgwihthp SXφD FRL 340 Y S YKT 395 AMSH-LP AMSH BRCC36 Rpn11 MYSM1 CSN5 eif3γ eif3η Rpn8 CSN6 LLTLGWIHTHPTQTAFLSSVDLHTHCSYQLMLP----EAIAIVCSPKHK------DTGIFRLTNAG LITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLP----ESVAIVCSPKFQ------ETGFFKLTDHG MRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNT-KTGRVLYTCFQSIQAQ EMVVGWYHSHPGFGCWLSGVDINTQQSFEALSE----RAVAVVVDPIQS-VKGKVVIDAFRLINAN FSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFS-23-QITCLVISEEIS------PDGSYRLPYKF ENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQE----PFVAVVIDPTRTISAGKVNLGAFRTYPKG HLHVGWYQSTYYG-SFVTRALLDSQFSYQHAIE... ELILGWYATGHDITEHSVLIHEYYSREAPNPIH... ERIVGWYHTGP----KLHKNDIAINELMKRYCP... LEFLGWYTTGG----PPDPSDIHVHKQVCEIIE... Fukai, S. Supplementary Figure S6 11
12 β1 α1 β2 β3 β4 β5 α2 β H.sapiens_AMSH-LP E G L R C V V L P E D L C H K F L Q L A E S N T V R G I E T C G I L C G K L T H N E F T I T H V I V P K Q S A G P D Y C D M E N V E E L F N V Q D Q H D L L T L G W I H T H P T Q T M.musculus_AMSH-LP E G L R C V V L S R D L C H K F L L L A D S N T V R G I E T C G I L C G K L T H N E F T I T H V V V P K Q S A G P D Y C D V E N V E E L F N V Q D Q H G L L T L G W I H T H P T Q T X.tropicalis_AMSH-LP D G L R P V V L P R D L S Q R F L Q L A E A N T S R G I E T C G I L C G K L T H D E F T I T H V I V P K Q S A G P D Y C D M E N V E E L F N V Q D Q H N L L T L G W I H T H P T Q T H.sapiens_AMSH D G L R H V V V P G R L C P Q F L Q L A S A N T A R G V E T C G I L C G K L M R N E F T I T H V L I P K Q S A G S D Y C N T E N E E E L F L I Q D Q Q G L I T L G W I H T H P T Q T D.melanogaster_AMSH G S L R L V Y V P G D T M E V F L K L A L A N T S K N I E T C G V L A G H L S Q N Q L Y I T H I I T P Q Q Q G T P D S C N T M H E E Q I F D V Q D Q M Q L I T L G W I H T H P T Q T S.pombe_AMSH K P L R T I Y L P K L L K K V F L D V V K P N T K K N L E T C G I L C G K L R Q N A F F I T H L V I P L Q E A T S D T C G T T D E A S L F E F Q D K H N L L T L G W I H T H P T Q T H.sapiens_POH1 D T A E Q V Y I S S L A L L K M L K H G R A G V P.. M E V M G L M L G E F V D. D Y T V R V I D V F A M P Q S G T G V S V E A V D P V F Q A K M L D M L K Q T G R P E M V V G W Y H S H P G F G D.melanogaster_Rpn11 D T A E Q V Y I S S L A L L K M L K H G R A G V P.. M E V M G L M L G E F V D. D Y T V Q V I D V F A M P Q T G T G V S V E A V D P V F Q A K M L D M L K Q T G R P E M V V G W Y H S H P G F G S.pombe_Rpn11 D N S E C V Y I S S L A L L K M L R H G R H G T P.. M E V M G L M L G E F V D. D F T V R V V D V F A M P Q S G T G V S V E A V D P V F Q K N M M D M L K Q T G R P E M V V G W Y H S H P G F G α3 β7 β8 α4 β9 β10 β H.sapiens_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H K D T G..... I F R L T. N A G M L E V S.. A C K K K G. F H P H T. K E P R L F S I C K H V L V K. D I K I I V L D L R M.musculus_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H K D T G..... I F R L T. N A G M L E V S.. T C K K K G. F H P H T. K D P K L F S I C S H V L V K. D I K T T V L D L R X.tropicalis_AMSH-LP A F L S S V D L H T H C S Y Q L M L P E A I A I V C S P K H N D T G..... I F R L T. S A G M L E V S.. A C K K K G. F H P H S. K E P R Q F N T C R H V T V Q. D A G I T V L D L R H.sapiens_AMSH A F L S S V D L H T H C S Y Q M M L P E S V A I V C S P K F Q E T G..... F F K L T. D H G L E E I S.. S C R Q K G. F H P H S. K D P P L F C S C S H V T V V. D R A V T I T D L R.. D.melanogaster_AMSH A F L S S V D L H T H C S Y Q I M M P E A L A I V C A P K Y N T T G..... F F I L T P H Y G L D Y I A.. Q C R Q S G. F H P H P. N D P P L F M E A Q H I R M D N Q A K I K V I D L R R. S.pombe_AMSH C F M S S V D L H T H C S Y Q L M L P E A I A I V M A P S K N T S G..... I F R L L D P E G L Q T I V.. K C R K P G L F H P H E G K V Y T M V A Q P G H V R E I. N S K L Q V V D L R V K H.sapiens_POH1 C W L S G V D I N T Q Q S F E A L S E R A V A V V V D P I Q S V K G K V V I D A F R L I. N A N M M V L G H E P R Q T T S. N L G H L. N K P S I Q A L I H G L N R H. Y Y S I T I N Y R K D.melanogaster_Rpn11 C W L S G V D I N T Q Q S F E A L S E R A V A V V V D P I Q S V K G K V V I D A F R L I. N P N M L V L G Q E P R Q T T S. N L G H L. Q K P S V Q A L I H G L N R H. Y Y S I S I N Y R K S.pombe_Rpn11 C W L S S V D I N T Q Q S F E Q L T P R A V A V V V D P I Q S V K G K V V I D A F R L I. N P S T L M M G Q E P R Q T T S. N L G H I. N K P S I Q A L I H G L G R H. Y Y S L R I N Y K K Fukai, S. Supplementary Figure S7 12
13 AMSH-LP (nm) time (min) K63-Ub 2 (µm) wt 10 Ub(µg) AMSH-LP (nm) time (min) K63-Ub 2 (µm) 400 E329A 10 Ub(µg) Ub Ub AMSH-LP (nm) time (min) K63-Ub 2 (µm) T353A 0 10 S358A 0 15 Ub(µg) AMSH-LP (nm) time (min) K63-Ub 2 (µm) F407A 0 15 S357A 0 15 Ub(µg) Ub Ub AMSH-LP (nm) time (min) K63-Ub 2 (µm) F355A 0 60 C402S 0 Ub(µg) AMSH-LP (nm) time (min) K63-Ub 2 (µm) F332A 15 M370A Ub(µg) Ub Ub Fukai, S. Supplementary Figure S8 13
SUPPLEMENTARY INFORMATION
Supplementary Table 1: Amplitudes of three current levels. Level 0 (pa) Level 1 (pa) Level 2 (pa) TrkA- TrkH WT 200 K 0.01 ± 0.01 9.5 ± 0.01 18.7 ± 0.03 200 Na * 0.001 ± 0.01 3.9 ± 0.01 12.5 ± 0.03 200
More informationSUPPLEMENTARY INFORMATION
doi:10.1038/nature11054 Supplementary Fig. 1 Sequence alignment of Na v Rh with NaChBac, Na v Ab, and eukaryotic Na v and Ca v homologs. Secondary structural elements of Na v Rh are indicated above the
More informationSUPPLEMENTARY INFORMATION
Table of Contents Page Supplementary Table 1. Diffraction data collection statistics 2 Supplementary Table 2. Crystallographic refinement statistics 3 Supplementary Fig. 1. casic1mfc packing in the R3
More informationSUPPLEMENTARY INFORMATION
Supplementary Results DNA binding property of the SRA domain was examined by an electrophoresis mobility shift assay (EMSA) using synthesized 12-bp oligonucleotide duplexes containing unmodified, hemi-methylated,
More informationSupplementary Figure 1. Biochemical and sequence alignment analyses the
Supplementary Figure 1. Biochemical and sequence alignment analyses the interaction of OPTN and TBK1. (a) Analytical gel filtration chromatography analysis of the interaction between TBK1 CTD and OPTN(1-119).
More informationSUPPLEMENTARY INFORMATION
SUPPLEMENTARY INFORMATION doi:10.1038/nature11524 Supplementary discussion Functional analysis of the sugar porter family (SP) signature motifs. As seen in Fig. 5c, single point mutation of the conserved
More informationNitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein
Acta Cryst. (2015). D71, 274-282, doi:10.1107/s1399004714025243 Supporting information Volume 71 (2015) Supporting information for article: Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08
More informationSUPPLEMENTARY INFORMATION. doi: /nature07461
Figure S1 Electrophysiology. a ph-activation of. Two-electrode voltage clamp recordings of Xenopus oocytes expressing in comparison to waterinjected oocytes. Currents were recorded at 40 mv. The ph of
More informationSUPPLEMENTARY INFORMATION
Dph2 SeMet (iron-free) # Dph2 (iron-free) Dph2-[4Fe-4S] Data collection Space group P2 1 2 1 2 1 P2 1 2 1 2 1 P2 1 2 1 2 1 Cell dimensions a, b, c (Å) 58.26, 82.08, 160.42 58.74, 81.87, 160.01 55.70, 80.53,
More informationStabilizing the CH2 domain of an Antibody by Engineering in an Enhanced Aromatic Sequon
Stabilizing the CH2 domain of an Antibody by Engineering in an Enhanced Aromatic Sequon Wentao Chen,, Leopold Kong, Stephen Connelly, Julia M. Dendle,, Yu Liu,, Ian A. Wilson,#, Evan T. Powers, *, Jeffery
More informationSUPPLEMENTARY INFORMATION
Fig. 1 Influences of crystal lattice contacts on Pol η structures. a. The dominant lattice contact between two hpol η molecules (silver and gold) in the type 1 crystals. b. A close-up view of the hydrophobic
More informationFW 1 CDR 1 FW 2 CDR 2
Supplementary Figure 1 Supplementary Figure 1: Interface of the E9:Fas structure. The two interfaces formed by V H and V L of E9 with Fas are shown in stereo. The Fas receptor is represented as a surface
More informationSUPPLEMENTARY INFORMATION
SUPPLEMENTARY INFORMATION doi:10.1038/nature11539 Supplementary Figure 1 Schematic representation of plant (A) and mammalian (B) P 2B -ATPase domain organization. Actuator (A-), nucleotide binding (N-),
More informationSupplementary Information. The protease GtgE from Salmonella exclusively targets. inactive Rab GTPases
Supplementary Information The protease GtgE from Salmonella exclusively targets inactive Rab GTPases Table of Contents Supplementary Figures... 2 Supplementary Figure 1... 2 Supplementary Figure 2... 3
More informationSUPPLEMENTARY INFORMATION
Supplementary materials Figure S1 Fusion protein of Sulfolobus solfataricus SRP54 and a signal peptide. a, Expression vector for the fusion protein. The signal peptide of yeast dipeptidyl aminopeptidase
More informationSupplementary figure 1. Comparison of unbound ogm-csf and ogm-csf as captured in the GIF:GM-CSF complex. Alignment of two copies of unbound ovine
Supplementary figure 1. Comparison of unbound and as captured in the GIF:GM-CSF complex. Alignment of two copies of unbound ovine GM-CSF (slate) with bound GM-CSF in the GIF:GM-CSF complex (GIF: green,
More informationTable 1. Crystallographic data collection, phasing and refinement statistics. Native Hg soaked Mn soaked 1 Mn soaked 2
Table 1. Crystallographic data collection, phasing and refinement statistics Native Hg soaked Mn soaked 1 Mn soaked 2 Data collection Space group P2 1 2 1 2 1 P2 1 2 1 2 1 P2 1 2 1 2 1 P2 1 2 1 2 1 Cell
More informationTHE CRYSTAL STRUCTURE OF THE SGT1-SKP1 COMPLEX: THE LINK BETWEEN
THE CRYSTAL STRUCTURE OF THE SGT1-SKP1 COMPLEX: THE LINK BETWEEN HSP90 AND BOTH SCF E3 UBIQUITIN LIGASES AND KINETOCHORES Oliver Willhoft, Richard Kerr, Dipali Patel, Wenjuan Zhang, Caezar Al-Jassar, Tina
More informationSupplementary Figures
1 Supplementary Figures Supplementary Figure 1 Type I FGFR1 inhibitors (a) Chemical structures of a pyrazolylaminopyrimidine inhibitor (henceforth referred to as PAPI; PDB-code of the FGFR1-PAPI complex:
More informationSupplementary Materials for
www.advances.sciencemag.org/cgi/content/full/1/7/e1500263/dc1 Supplementary Materials for Newton s cradle proton relay with amide imidic acid tautomerization in inverting cellulase visualized by neutron
More informationSUPPLEMENTARY INFORMATION
www.nature.com/nature 1 Figure S1 Sequence alignment. a Structure based alignment of the plgic of E. chrysanthemi (ELIC), the acetylcholine binding protein from the snail Lymnea stagnalis (AchBP, PDB code
More informationSI Text S1 Solution Scattering Data Collection and Analysis. SI references
SI Text S1 Solution Scattering Data Collection and Analysis. The X-ray photon energy was set to 8 kev. The PILATUS hybrid pixel array detector (RIGAKU) was positioned at a distance of 606 mm from the sample.
More informationENZYME MECHANISMS, PROTEASES, STRUCTURAL BIOLOGY
Supplementary Information SUBJECT AREAS: ENZYME MECHANISMS, PROTEASES, STRUCTURAL BIOLOGY Correspondence and requests for materials should be addressed to N.T. (ntanaka@pharm.showa-u.ac.jp) or W.O. (owataru@vos.nagaokaut.ac.jp)
More informationStructural insights into Aspergillus fumigatus lectin specificity - AFL binding sites are functionally non-equivalent
Acta Cryst. (2015). D71, doi:10.1107/s1399004714026595 Supporting information Volume 71 (2015) Supporting information for article: Structural insights into Aspergillus fumigatus lectin specificity - AFL
More informationTable S1. Overview of used PDZK1 constructs and their binding affinities to peptides. Related to figure 1.
Table S1. Overview of used PDZK1 constructs and their binding affinities to peptides. Related to figure 1. PDZK1 constru cts Amino acids MW [kda] KD [μm] PEPT2-CT- FITC KD [μm] NHE3-CT- FITC KD [μm] PDZK1-CT-
More informationSupplemental Information
Supplemental Information Combinatorial Readout of Unmodified H3R2 and Acetylated H3K14 by the Tandem PHD Finger of MOZ Reveals a Regulatory Mechanism for HOXA9 Transcription Yu Qiu 1, Lei Liu 1, Chen Zhao
More informationSupplementary Information. Structural basis for precursor protein-directed ribosomal peptide macrocyclization
Supplementary Information Structural basis for precursor protein-directed ribosomal peptide macrocyclization Kunhua Li 1,3, Heather L. Condurso 1,3, Gengnan Li 1, Yousong Ding 2 and Steven D. Bruner 1*
More informationPlasmid Relevant features Source. W18N_D20N and TrXE-W18N_D20N-anti
Table S1. E. coli plasmids Plasmid Relevant features Source pdg680 T. reesei XynII AA 2-190 with C-terminal His 6 tag optimized for E. coli expression in pjexpress401 Wan et al. (in press) psbn44d psbn44h
More informationSUPPLEMENTARY INFORMATION
doi:10.1038/nature10955 Supplementary Figures Supplementary Figure 1. Electron-density maps and crystallographic dimer structures of the motor domain. (a f) Stereo views of the final electron-density maps
More informationStructure and evolution of the spliceosomal peptidyl-prolyl cistrans isomerase Cwc27
Acta Cryst. (2014). D70, doi:10.1107/s1399004714021695 Supporting information Volume 70 (2014) Supporting information for article: Structure and evolution of the spliceosomal peptidyl-prolyl cistrans isomerase
More informationNature Structural & Molecular Biology: doi: /nsmb Supplementary Figure 1
Supplementary Figure 1 Crystallization. a, Crystallization constructs of the ET B receptor are shown, with all of the modifications to the human wild-type the ET B receptor indicated. Residues interacting
More informationDiphthamide biosynthesis requires a radical iron-sulfur enzyme. Pennsylvania State University, University Park, Pennsylvania 16802, USA
Diphthamide biosynthesis requires a radical iron-sulfur enzyme Yang Zhang, 1,4 Xuling Zhu, 1,4 Andrew T. Torelli, 1 Michael Lee, 2 Boris Dzikovski, 1 Rachel Koralewski, 1 Eileen Wang, 1 Jack Freed, 1 Carsten
More informationSupplementary figure 1 Application of tmfret in LeuT. (a) To assess the feasibility of using tmfret for distance-dependent measurements in LeuT, a
Supplementary figure 1 Application of tmfret in LeuT. (a) To assess the feasibility of using tmfret for distance-dependent measurements in LeuT, a series of tmfret-pairs comprised of single cysteine mutants
More informationSUPPLEMENTARY INFORMATION
doi:10.1038/nature12045 Supplementary Table 1 Data collection and refinement statistics. Native Pt-SAD X-ray source SSRF BL17U SPring-8 BL41XU Wavelength (Å) 0.97947 1.07171 Space group P2 1 2 1 2 1 P2
More informationSupporting Information
Supporting Information Ottmann et al. 10.1073/pnas.0907587106 Fig. S1. Primary structure alignment of SBT3 with C5 peptidase from Streptococcus pyogenes. The Matchmaker tool in UCSF Chimera (http:// www.cgl.ucsf.edu/chimera)
More informationSUPPLEMENTARY INFORMATION
Supplementary Table 1: Data collection, phasing and refinement statistics ChbC/Ta 6 Br 12 Native ChbC Data collection Space group P4 3 2 1 2 P4 3 2 1 2 Cell dimensions a, c (Å) 132.75, 453.57 132.81, 452.95
More informationCryo-EM data collection, refinement and validation statistics
1 Table S1 Cryo-EM data collection, refinement and validation statistics Data collection and processing CPSF-160 WDR33 (EMDB-7114) (PDB 6BM0) CPSF-160 WDR33 (EMDB-7113) (PDB 6BLY) CPSF-160 WDR33 CPSF-30
More informationNature Structural and Molecular Biology: doi: /nsmb Supplementary Figure 1
Supplementary Figure 1 Quantitation of the binding of pro53 peptide to sorla Vps10p measured by the AP reporter assay. The graph shows tracings of the typical chromogenic AP reaction observed with AP-pro53
More informationCrystal Structure of Fibroblast Growth Factor 9 (FGF9) Reveals Regions. Implicated in Dimerization and Autoinhibition
JBC Papers in Press. Published on November 1, 2000 as Manuscript M006502200 Crystal Structure of Fibroblast Growth Factor 9 (FGF9) Reveals Regions Implicated in Dimerization and Autoinhibition 1 Copyright
More informationSUPPLEMENTARY INFORMATION
doi:10.1038/nature11085 Supplementary Tables: Supplementary Table 1. Summary of crystallographic and structure refinement data Structure BRIL-NOP receptor Data collection Number of crystals 23 Space group
More informationSupplementary Figure 1 Crystal packing of ClR and electron density maps. Crystal packing of type A crystal (a) and type B crystal (b).
Supplementary Figure 1 Crystal packing of ClR and electron density maps. Crystal packing of type A crystal (a) and type B crystal (b). Crystal contacts at B-C loop are magnified and stereo view of A-weighted
More informationNature Structural and Molecular Biology: doi: /nsmb Supplementary Figure 1. Definition and assessment of ciap1 constructs.
Supplementary Figure 1 Definition and assessment of ciap1 constructs. (a) ciap1 constructs used in this study are shown as primary structure schematics with domains colored as in the main text. Mutations
More informationExperimental and Computational Mutagenesis to Investigate the. Positioning of a General Base within an Enzyme Active Site
Experimental and Computational Mutagenesis to Investigate the Positioning of a General Base within an Enzyme Active Site Jason P. Schwans, Philip Hanoian, Benjamin J. Lengerich, Fanny Sunden, Ana Gonzalez
More informationNature Structural & Molecular Biology: doi: /nsmb Supplementary Figure 1
Supplementary Figure 1 Zn 2+ -binding sites in USP18. (a) The two molecules of USP18 present in the asymmetric unit are shown. Chain A is shown in blue, chain B in green. Bound Zn 2+ ions are shown as
More informationSupplementary Information
Supplementary Information The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis Marta C. Marques a, Cristina Tapia b, Oscar Gutiérrez-Sanz b, Ana Raquel Ramos a, Kimberly L.
More informationThe structure of a nucleolytic ribozyme that employs a catalytic metal ion. Yijin Liu, Timothy J. Wilson and David M.J. Lilley
SUPPLEMENTARY INFORMATION The structure of a nucleolytic ribozyme that employs a catalytic metal ion Yijin Liu, Timothy J. Wilson and David M.J. Lilley Cancer Research UK Nucleic Acid Structure Research
More informationSupplementary Figure 1 Crystal contacts in COP apo structure (PDB code 3S0R)
Supplementary Figure 1 Crystal contacts in COP apo structure (PDB code 3S0R) Shown in cyan and green are two adjacent tetramers from the crystallographic lattice of COP, forming the only unique inter-tetramer
More informationTable S1. Primers used for the constructions of recombinant GAL1 and λ5 mutants. GAL1-E74A ccgagcagcgggcggctgtctttcc ggaaagacagccgcccgctgctcgg
SUPPLEMENTAL DATA Table S1. Primers used for the constructions of recombinant GAL1 and λ5 mutants Sense primer (5 to 3 ) Anti-sense primer (5 to 3 ) GAL1 mutants GAL1-E74A ccgagcagcgggcggctgtctttcc ggaaagacagccgcccgctgctcgg
More informationSUPPLEMENTARY INFORMATION
doi:10.1038/nature10458 Active Site Remodeling in the Bifunctional Fructose-1,6- bisphosphate aldolase/phosphatase Juan Du, Rafael F. Say, Wei Lü, Georg Fuchs & Oliver Einsle SUPPLEMENTARY FIGURES Figure
More informationSUPPLEMENTARY INFORMATION
SUPPLEMENTARY INFORMATION doi:10.1038/nature11744 Supplementary Table 1. Crystallographic data collection and refinement statistics. Wild-type Se-Met-BcsA-B SmCl 3 -soaked EMTS-soaked Data collection Space
More informationNB-DNJ/GCase-pH 7.4 NB-DNJ+/GCase-pH 7.4 NB-DNJ+/GCase-pH 4.5
SUPPLEMENTARY TABLES Suppl. Table 1. Protonation states at ph 7.4 and 4.5. Protonation states of titratable residues in GCase at ph 7.4 and 4.5. Histidine: HID, H at δ-nitrogen; HIE, H at ε-nitrogen; HIP,
More informationCH 3 CH 2 OH +H 2 O CHO. 2e + 2H + + O 2 H 2 O +HCOOH
2 4 H CH 3 2e + 2H + + 2 H 2 2 H CH 2 H 2e + 2H + + 2 H 2 2 H +H 2 CH 2e + 2H + + 2 H 2 2 H +HCH Supplemental Figure S. The three-step 4DM reaction, each step requires two reducing equivalents from ADPH
More informationSUPPLEMENTARY INFORMATION
SUPPLEMENTARY INFORMATION Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis Sergio de Cima, Luis M. Polo, Carmen Díez-Fernández, Ana I. Martínez, Javier
More informationfor Molecular Biology and Neuroscience and Institute of Medical Microbiology, Rikshospitalet-Radiumhospitalet
SUPPLEMENTARY INFORMATION TO Structural basis for enzymatic excision of N -methyladenine and N 3 -methylcytosine from DNA Ingar Leiros,5, Marivi P. Nabong 2,3,5, Kristin Grøsvik 3, Jeanette Ringvoll 2,
More informationNature Structural & Molecular Biology doi: /nsmb Supplementary Figure 1. CRBN binding assay with thalidomide enantiomers.
Supplementary Figure 1 CRBN binding assay with thalidomide enantiomers. (a) Competitive elution assay using thalidomide-immobilized beads coupled with racemic thalidomide. Beads were washed three times
More informationRho1 binding site PtdIns(4,5)P2 binding site Both sites
localization Mutation site DMSO LatB WT F77A I115A I131A K134A Rho1 binding site PtdIns(4,5)P2 binding site Both sites E186A E199A N201A R84A-E186A-E199A L131A-K136A-E186A L131A-E186A-E199A K136A-E186A-E199A
More informationSupplemental Information. Molecular Basis of Spectral Diversity. in Near-Infrared Phytochrome-Based. Fluorescent Proteins
Chemistry & Biology, Volume 22 Supplemental Information Molecular Basis of Spectral Diversity in Near-Infrared Phytochrome-Based Fluorescent Proteins Daria M. Shcherbakova, Mikhail Baloban, Sergei Pletnev,
More informationThe structure of a nucleolytic ribozyme that employs a catalytic metal ion Liu, Yijin; Wilson, Timothy; Lilley, David
University of Dundee The structure of a nucleolytic ribozyme that employs a catalytic metal ion Liu, Yijin; Wilson, Timothy; Lilley, David Published in: Nature Chemical Biology DOI: 10.1038/nchembio.2333
More informationSUPPLEMENTARY INFORMATION
doi:1.138/nature1737 Supplementary Table 1 variant Description FSEC - 2B12 a FSEC - 6A1 a K d (leucine) c Leucine uptake e K (wild-type like) K (Y18F) K (TS) K (TSY) K288A mutant, lipid facing side chain
More informationSupplementary Information
Supplementary Information Resveratrol Serves as a Protein-Substrate Interaction Stabilizer in Human SIRT1 Activation Xuben Hou,, David Rooklin, Hao Fang *,,, Yingkai Zhang Department of Medicinal Chemistry
More informationStructure and RNA-binding properties. of the Not1 Not2 Not5 module of the yeast Ccr4 Not complex
Structure and RNA-binding properties of the Not1 Not2 Not5 module of the yeast Ccr4 Not complex Varun Bhaskar 1, Vladimir Roudko 2,3, Jerome Basquin 1, Kundan Sharma 4, Henning Urlaub 4, Bertrand Seraphin
More informationSupplementary information for:
SUPPLEMETARY IFRMATI Supplementary information for: Structure of a β 1 -adrenergic G protein-coupled receptor Tony Warne, Maria J. Serrano-Vega, Jillian G. Baker#, Rouslan Moukhametzianov, Patricia C.
More informationStructural basis of PROTAC cooperative recognition for selective protein degradation
SUPPLEMENTARY INFORMATION Structural basis of PROTAC cooperative recognition for selective protein degradation Morgan S. Gadd 1, Andrea Testa 1, Xavier Lucas 1, Kwok-Ho Chan, Wenzhang Chen, Douglas J.
More informationSUPPLEMENTARY INFORMATION
Data collection Supplementary Table 1 Statistics of data collection, phasing and refinement Native Se-MAD Space group P2 1 2 1 2 1 P2 1 2 1 2 1 Cell dimensions a, b, c (Å) 50.4, 94.2, 115.4 49.8, 94.2,
More informationSUPPLEMENTARY INFORMATION
doi:10.108/nature11899 Supplementar Table 1. Data collection and refinement statistics (+TPMP, native) (-TPMP, native) (+TPMP, recombinant) (MgCl ) (MgSO ) Data collection Space group C P 1 C P 1 1 P 1
More informationSUPPLEMENTARY INFORMATION
Figure S1. Secondary structure of CAP (in the camp 2 -bound state) 10. α-helices are shown as cylinders and β- strands as arrows. Labeling of secondary structure is indicated. CDB, DBD and the hinge are
More informationSensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets
Supporting information Sensitive NMR Approach for Determining the Binding Mode of Tightly Binding Ligand Molecules to Protein Targets Wan-Na Chen, Christoph Nitsche, Kala Bharath Pilla, Bim Graham, Thomas
More informationSupplementary Information
Supplementary Information Structural analysis of leader peptide binding enables leaderfree cyanobactin processing Jesko Koehnke 1,2, Greg Mann 1,2, Andrew F Bent 1,2, Hannes Ludewig 1, Sally Shirran 1,
More informationSupporting Information. UV-induced ligand exchange in MHC class I protein crystals
Supporting Information for the article entitled UV-induced ligand exchange in MHC class I protein crystals by Patrick H.N. Celie 1, Mireille Toebes 2, Boris Rodenko 3, Huib Ovaa 3, Anastassis Perrakis
More informationSupplementary Figure 1. Aligned sequences of yeast IDH1 (top) and IDH2 (bottom) with isocitrate
SUPPLEMENTARY FIGURE LEGENDS Supplementary Figure 1. Aligned sequences of yeast IDH1 (top) and IDH2 (bottom) with isocitrate dehydrogenase from Escherichia coli [ICD, pdb 1PB1, Mesecar, A. D., and Koshland,
More informationSupplementary Information
Supplementary Information An engineered protein antagonist of K-Ras/B-Raf interaction Monique J. Kauke, 1,2 Michael W. Traxlmayr 1,2, Jillian A. Parker 3, Jonathan D. Kiefer 4, Ryan Knihtila 3, John McGee
More informationSUPPLEMENTARY FIGURES
SUPPLEMENTARY FIGURES Supplementary Figure 1 Protein sequence alignment of Vibrionaceae with either a 40-residue insertion or a 44-residue insertion. Identical residues are indicated by red background.
More informationBacterial protease uses distinct thermodynamic signatures for substrate recognition
Bacterial protease uses distinct thermodynamic signatures for substrate recognition Gustavo Arruda Bezerra, Yuko Ohara-Nemoto, Irina Cornaciu, Sofiya Fedosyuk, Guillaume Hoffmann, Adam Round, José A. Márquez,
More informationLipid Regulated Intramolecular Conformational Dynamics of SNARE-Protein Ykt6
Supplementary Information for: Lipid Regulated Intramolecular Conformational Dynamics of SNARE-Protein Ykt6 Yawei Dai 1, 2, Markus Seeger 3, Jingwei Weng 4, Song Song 1, 2, Wenning Wang 4, Yan-Wen 1, 2,
More informationDestruction of Amyloid Fibrils by Graphene through Penetration and Extraction of Peptides
Electronic Supplementary Material (ESI) for Nanoscale. This journal is The Royal Society of Chemistry 2015 Destruction of Amyloid Fibrils by Graphene through Penetration and Extraction of Peptides Zaixing
More informationSupporting Protocol This protocol describes the construction and the force-field parameters of the non-standard residue for the Ag + -site using CNS
Supporting Protocol This protocol describes the construction and the force-field parameters of the non-standard residue for the Ag + -site using CNS CNS input file generatemetal.inp: remarks file generate/generatemetal.inp
More informationStructure, mechanism and ensemble formation of the Alkylhydroperoxide Reductase subunits. AhpC and AhpF from Escherichia coli
Structure, mechanism and ensemble formation of the Alkylhydroperoxide Reductase subunits AhpC and AhpF from Escherichia coli Phat Vinh Dip 1,#, Neelagandan Kamariah 2,#, Malathy Sony Subramanian Manimekalai
More informationSUPPLEMENTARY INFORMATION
Supplementary Information Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins Nathan HyunJoong Joh 1, Andrew Min 1, Salem Faham 2, Julian P. Whitelegge 3, Duan Yang
More informationSUPPLEMENTARY INFORMATION
DOI:.38/ncb97 P ( μm, hours) 1 2 4 P DMSO Figure S1 unningham et al. E 97 65 27 MFN1 GFP-Parkin Opa1 ctin GPDH HEK293 GFP-Parkin 19 115 97 65 27 Mitochondrial Fraction SH-SY5Y GFP-Parkin Mito DMSO Mito
More informationSUPPLEMENTARY INFORMATION
Supplementary Figure 1: The HpUreI crystal used for collection of native diffraction data. The crystal belongs to spacegroup P4 2 2 1 2 and has an approximate maximal dimension of 0.25 mm. Supplementary
More informationCrystal lattice Real Space. Reflections Reciprocal Space. I. Solving Phases II. Model Building for CHEM 645. Purified Protein. Build model.
I. Solving Phases II. Model Building for CHEM 645 Purified Protein Solve Phase Build model and refine Crystal lattice Real Space Reflections Reciprocal Space ρ (x, y, z) pronounced rho F hkl 2 I F (h,
More informationNature Structural & Molecular Biology: doi: /nsmb Supplementary Figure 1
Supplementary Figure 1 Identification of the ScDcp2 minimal region interacting with both ScDcp1 and the ScEdc3 LSm domain. Pull-down experiment of untagged ScEdc3 LSm with various ScDcp1-Dcp2-His 6 fragments.
More informationStructures of holo wild-type human cellular retinol-binding protein II (hcrbpii) bound to retinol and retinal
Supporting information Volume 70 (2014) Supporting information for article: Structures of holo wild-type human cellular retinol-binding protein II (hcrbpii) bound to retinol and retinal Zahra Nossoni,
More informationThe structure of vanadium nitrogenase reveals an unusual bridging ligand
SUPPLEMENTARY INFORMATION The structure of vanadium nitrogenase reveals an unusual bridging ligand Daniel Sippel and Oliver Einsle Lehrstuhl Biochemie, Institut für Biochemie, Albert-Ludwigs-Universität
More informationStructure and Function of Neisseria gonorrhoeae MtrF Illuminates a Class of Antimetabolite Efflux Pumps
Cell Reports Supplemental Information Structure and Function of Neisseria gonorrhoeae MtrF Illuminates a Class of Antimetabolite Efflux Pumps Chih-Chia Su, Jani Reddy Bolla, Nitin Kumar, Abhijith Radhakrishnan,
More informationSupplementary Figure 3 a. Structural comparison between the two determined structures for the IL 23:MA12 complex. The overall RMSD between the two
Supplementary Figure 1. Biopanningg and clone enrichment of Alphabody binders against human IL 23. Positive clones in i phage ELISA with optical density (OD) 3 times higher than background are shown for
More informationStructural characterization of NiV N 0 P in solution and in crystal.
Supplementary Figure 1 Structural characterization of NiV N 0 P in solution and in crystal. (a) SAXS analysis of the N 32-383 0 -P 50 complex. The Guinier plot for complex concentrations of 0.55, 1.1,
More informationPurification, SDS-PAGE and cryo-em characterization of the MCM hexamer and Cdt1 MCM heptamer samples.
Supplementary Figure 1 Purification, SDS-PAGE and cryo-em characterization of the MCM hexamer and Cdt1 MCM heptamer samples. (a-b) SDS-PAGE analysis of the hexamer and heptamer samples. The eluted hexamer
More informationSUPPLEMENTARY INFORMATION
5 N 4 8 20 22 24 2 28 4 8 20 22 24 2 28 a b 0 9 8 7 H c (kda) 95 0 57 4 28 2 5.5 Precipitate before NMR expt. Supernatant before NMR expt. Precipitate after hrs NMR expt. Supernatant after hrs NMR expt.
More informationNature Structural & Molecular Biology: doi: /nsmb Supplementary Figure 1
Supplementary Figure 1 Chemical structure of LPS and LPS biogenesis in Gram-negative bacteria. a. Chemical structure of LPS. LPS molecule consists of Lipid A, core oligosaccharide and O-antigen. The polar
More informationIgE binds asymmetrically to its B cell receptor CD23
Supplementary Information IgE binds asymmetrically to its B cell receptor CD23 Balvinder Dhaliwal 1*, Marie O. Y. Pang 2, Anthony H. Keeble 2,3, Louisa K. James 2,4, Hannah J. Gould 2, James M. McDonnell
More informationSupplementary information
Supplementary information The structural basis of modularity in ECF-type ABC transporters Guus B. Erkens 1,2, Ronnie P-A. Berntsson 1,2, Faizah Fulyani 1,2, Maria Majsnerowska 1,2, Andreja Vujičić-Žagar
More informationFull wwpdb X-ray Structure Validation Report i
Full wwpdb X-ray Structure Validation Report i Mar 8, 2018 08:34 pm GMT PDB ID : 1RUT Title : Complex of LMO4 LIM domains 1 and 2 with the ldb1 LID domain Authors : Deane, J.E.; Ryan, D.P.; Maher, M.J.;
More informationSupporting Information
Supporting Information Micelle-Triggered b-hairpin to a-helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA HØctor Zamora-Carreras, [a] Beatriz Maestro,
More informationFull-length GlpG sequence was generated by PCR from E. coli genomic DNA. (with two sequence variations, D51E/L52V, from the gene bank entry aac28166),
Supplementary Methods Protein expression and purification Full-length GlpG sequence was generated by PCR from E. coli genomic DNA (with two sequence variations, D51E/L52V, from the gene bank entry aac28166),
More informationStructural insights into WcbI, a novel polysaccharide-biosynthesis enzyme
Volume 1 (2014) Supporting information for article: Structural insights into WcbI, a novel polysaccharide-biosynthesis enzyme Mirella Vivoli, Emily Ayres, Edward Beaumont, Michail N. Isupov and Nicholas
More informationFull wwpdb X-ray Structure Validation Report i
Full wwpdb X-ray Structure Validation Report i Mar 8, 2018 06:13 pm GMT PDB ID : 5G5C Title : Structure of the Pyrococcus furiosus Esterase Pf2001 with space group C2221 Authors : Varejao, N.; Reverter,
More informationImpact of the crystallization condition on importin-β conformation
Supporting information Volume 72 (2016) Supporting information for article: Impact of the crystallization condition on importin-β conformation Marcel J. Tauchert, Clément Hémonnot, Piotr Neumann, Sarah
More informationSupplemental Information. Expanded Coverage of the 26S Proteasome. Conformational Landscape Reveals. Mechanisms of Peptidase Gating
Cell Reports, Volume 24 Supplemental Information Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating Markus R. Eisele, Randi G. Reed, Till Rudack, Andreas
More informationSupplementary Information: Table S1. Potential energy and essential dynamics (ED) analysis of the MD simulations of the Bcl-2 complexes under study.
Supplementary Information: Table S1. Potential energy and essential dynamics (ED) analysis of the MD simulations of the Bcl-2 complexes under study. Bcl2 and complex Potential energy (kj/mol) ED 2D projection
More information