data_17437 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone chemical shift assignments of the UBC domain of Ube2S ; _BMRB_accession_number 17437 _BMRB_flat_file_name bmr17437.str _Entry_type original _Submission_date 2011-01-31 _Accession_date 2011-01-31 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lorenz Sonja G. . 2 Wemmer David E. . 3 Kuriyan John . . 4 Pelton Jeffrey G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 262 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-03-09 original author . stop_ _Original_release_date 2011-03-09 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit e2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21376237 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wickliffe Katherine E. . 2 Lorenz Sonja . . 3 Wemmer David E. . 4 Kuriyan John . . 5 Rape Michael . . stop_ _Journal_abbreviation Cell _Journal_name_full Cell _Journal_volume 144 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 769 _Page_last 781 _Year 2011 _Details . loop_ _Keyword E2 'K11-linked chain' 'substrate-assisted catalysis' ubiquitin ubiquitination stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Ube2S _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ube2S $Ube2S stop_ _System_molecular_weight 17369 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ube2S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ube2S _Molecular_mass 17369 _Mol_thiol_state 'all free' loop_ _Biological_function 'ubiquitin conjugating enzyme (E2)' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; MNSNVENLPPHIIRLVYKEV TTLTADPPDGIKVFPNEEDL TDLQVTIEGPEGTPYAGGLF RMKLLLGKDFPASPPKGYFL TKIFHPNVGANGEICVNVLK RDWTAELGIRHVLLTIKCLL IHPNPESALNEEAGRLLLEN YEEYAARARLLTEIHG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 SER 4 ASN 5 VAL 6 GLU 7 ASN 8 LEU 9 PRO 10 PRO 11 HIS 12 ILE 13 ILE 14 ARG 15 LEU 16 VAL 17 TYR 18 LYS 19 GLU 20 VAL 21 THR 22 THR 23 LEU 24 THR 25 ALA 26 ASP 27 PRO 28 PRO 29 ASP 30 GLY 31 ILE 32 LYS 33 VAL 34 PHE 35 PRO 36 ASN 37 GLU 38 GLU 39 ASP 40 LEU 41 THR 42 ASP 43 LEU 44 GLN 45 VAL 46 THR 47 ILE 48 GLU 49 GLY 50 PRO 51 GLU 52 GLY 53 THR 54 PRO 55 TYR 56 ALA 57 GLY 58 GLY 59 LEU 60 PHE 61 ARG 62 MET 63 LYS 64 LEU 65 LEU 66 LEU 67 GLY 68 LYS 69 ASP 70 PHE 71 PRO 72 ALA 73 SER 74 PRO 75 PRO 76 LYS 77 GLY 78 TYR 79 PHE 80 LEU 81 THR 82 LYS 83 ILE 84 PHE 85 HIS 86 PRO 87 ASN 88 VAL 89 GLY 90 ALA 91 ASN 92 GLY 93 GLU 94 ILE 95 CYS 96 VAL 97 ASN 98 VAL 99 LEU 100 LYS 101 ARG 102 ASP 103 TRP 104 THR 105 ALA 106 GLU 107 LEU 108 GLY 109 ILE 110 ARG 111 HIS 112 VAL 113 LEU 114 LEU 115 THR 116 ILE 117 LYS 118 CYS 119 LEU 120 LEU 121 ILE 122 HIS 123 PRO 124 ASN 125 PRO 126 GLU 127 SER 128 ALA 129 LEU 130 ASN 131 GLU 132 GLU 133 ALA 134 GLY 135 ARG 136 LEU 137 LEU 138 LEU 139 GLU 140 ASN 141 TYR 142 GLU 143 GLU 144 TYR 145 ALA 146 ALA 147 ARG 148 ALA 149 ARG 150 LEU 151 LEU 152 THR 153 GLU 154 ILE 155 HIS 156 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1ZDN "Ubiquitin-Conjugating Enzyme E2s" 100.00 158 100.00 100.00 4.35e-108 DBJ BAB93484 "ubiquitin carrier protein [Homo sapiens]" 100.00 222 100.00 100.00 1.54e-108 DBJ BAC25019 "unnamed protein product [Mus musculus]" 100.00 223 99.36 99.36 7.01e-108 DBJ BAC25523 "unnamed protein product [Mus musculus]" 100.00 223 99.36 99.36 6.15e-108 DBJ BAE27035 "unnamed protein product [Mus musculus]" 100.00 223 99.36 99.36 6.15e-108 DBJ BAE32323 "unnamed protein product [Mus musculus]" 100.00 223 99.36 99.36 6.15e-108 GB AAA58446 "ubiquitin carrier protein [Homo sapiens]" 100.00 225 100.00 100.00 1.41e-108 GB AAH04236 "Ubiquitin-conjugating enzyme E2S [Homo sapiens]" 100.00 222 100.00 100.00 1.54e-108 GB AAH07554 "Ubiquitin-conjugating enzyme E2S [Homo sapiens]" 100.00 222 100.00 100.00 1.54e-108 GB AAH12255 "Ubiquitin-conjugating enzyme E2S [Mus musculus]" 100.00 223 99.36 99.36 6.15e-108 GB AAH30171 "Ubiquitin-conjugating enzyme E2S [Mus musculus]" 100.00 223 99.36 99.36 6.15e-108 PIR B42856 "ubiquitin carrier protein E2 - human" 100.00 247 100.00 100.00 9.06e-109 REF NP_001069940 "ubiquitin-conjugating enzyme E2 S [Bos taurus]" 100.00 223 100.00 100.00 1.26e-108 REF NP_001091235 "ubiquitin-conjugating enzyme E2 S-A [Xenopus laevis]" 100.00 223 99.36 99.36 6.15e-108 REF NP_001099694 "ubiquitin-conjugating enzyme E2 S [Rattus norvegicus]" 100.00 223 99.36 99.36 5.17e-108 REF NP_001252933 "ubiquitin-conjugating enzyme E2 S [Macaca mulatta]" 100.00 222 100.00 100.00 1.05e-108 REF NP_001273893 "ubiquitin-conjugating enzyme E2 S [Canis lupus familiaris]" 100.00 223 100.00 100.00 8.08e-109 SP A1L3K1 "RecName: Full=Ubiquitin-conjugating enzyme E2 S-A; AltName: Full=E2 ubiquitin-conjugating enzyme S-A; AltName: Full=Ubiquitin c" 100.00 223 99.36 99.36 6.15e-108 SP B5DFI8 "RecName: Full=Ubiquitin-conjugating enzyme E2 S; AltName: Full=E2 ubiquitin-conjugating enzyme S; AltName: Full=Ubiquitin carri" 100.00 223 99.36 99.36 5.17e-108 SP Q16763 "RecName: Full=Ubiquitin-conjugating enzyme E2 S; AltName: Full=E2 ubiquitin-conjugating enzyme S; AltName: Full=E2-EPF; AltName" 100.00 222 100.00 100.00 1.54e-108 SP Q1RML1 "RecName: Full=Ubiquitin-conjugating enzyme E2 S; AltName: Full=E2 ubiquitin-conjugating enzyme S; AltName: Full=Ubiquitin carri" 100.00 223 100.00 100.00 1.62e-108 SP Q921J4 "RecName: Full=Ubiquitin-conjugating enzyme E2 S; AltName: Full=E2 ubiquitin-conjugating enzyme S; AltName: Full=Ubiquitin carri" 100.00 223 99.36 99.36 6.15e-108 TPG DAA19381 "TPA: ubiquitin-conjugating enzyme E2 S [Bos taurus]" 100.00 223 100.00 100.00 1.62e-108 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ube2S Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $Ube2S 'recombinant technology' . Escherichia coli . 'SMT3- based system (LifeSensors)' ; gene was sub-cloned into a vector encoding a cleavable N-terminal hexa-His/SMT3- tag by ligation-free methods ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ube2S 804 uM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 75mM mM 'natural abundance' D2O 7.5 % 'natural abundance' DSS 30 uM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 92.5 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ube2S 400 uM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 75mM mM 'natural abundance' D2O 7.5 % 'natural abundance' DSS 30 uM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 92.5 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ube2S 1.00 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 75mM mM 'natural abundance' D2O 7.5 % 'natural abundance' DSS 30 uM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 92.5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_3 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 185 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $citation_1 $citation_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Ube2S _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 ASN H H 8.555 0.02 1 2 2 2 ASN CA C 53.272 0.2 1 3 2 2 ASN CB C 38.974 0.2 1 4 2 2 ASN N N 119.051 0.1 1 5 3 3 SER H H 8.519 0.02 1 6 3 3 SER CA C 58.508 0.2 1 7 3 3 SER CB C 63.770 0.2 1 8 3 3 SER N N 116.869 0.1 1 9 4 4 ASN H H 8.564 0.02 1 10 4 4 ASN CA C 53.675 0.2 1 11 4 4 ASN CB C 38.725 0.2 1 12 4 4 ASN N N 120.872 0.1 1 13 5 5 VAL H H 8.055 0.02 1 14 5 5 VAL CA C 62.914 0.2 1 15 5 5 VAL CB C 32.553 0.2 1 16 5 5 VAL N N 119.650 0.1 1 17 6 6 GLU H H 8.342 0.02 1 18 6 6 GLU CA C 56.596 0.2 1 19 6 6 GLU CB C 30.225 0.2 1 20 6 6 GLU N N 122.698 0.1 1 21 7 7 ASN H H 8.280 0.02 1 22 7 7 ASN CA C 53.276 0.2 1 23 7 7 ASN CB C 38.947 0.2 1 24 7 7 ASN N N 118.755 0.1 1 25 8 8 LEU H H 8.170 0.02 1 26 8 8 LEU N N 121.856 0.1 1 27 10 10 PRO CA C 65.805 0.2 1 28 10 10 PRO CB C 32.262 0.2 1 29 11 11 HIS H H 8.459 0.02 1 30 11 11 HIS CA C 59.204 0.2 1 31 11 11 HIS CB C 29.421 0.2 1 32 11 11 HIS N N 113.796 0.1 1 33 12 12 ILE H H 7.027 0.02 1 34 12 12 ILE CA C 61.574 0.2 1 35 12 12 ILE CB C 36.090 0.2 1 36 12 12 ILE N N 122.358 0.1 1 37 13 13 ILE H H 7.727 0.02 1 38 13 13 ILE CA C 64.603 0.2 1 39 13 13 ILE CB C 36.933 0.2 1 40 13 13 ILE N N 121.387 0.1 1 41 14 14 ARG H H 7.773 0.02 1 42 14 14 ARG CA C 59.642 0.2 1 43 14 14 ARG CB C 30.185 0.2 1 44 14 14 ARG N N 116.718 0.1 1 45 15 15 LEU H H 7.380 0.02 1 46 15 15 LEU CA C 58.284 0.2 1 47 15 15 LEU CB C 42.417 0.2 1 48 15 15 LEU N N 120.649 0.1 1 49 16 16 VAL H H 8.629 0.02 1 50 16 16 VAL CA C 66.930 0.2 1 51 16 16 VAL CB C 31.747 0.2 1 52 16 16 VAL N N 121.469 0.1 1 53 17 17 TYR H H 8.938 0.02 1 54 17 17 TYR CA C 62.091 0.2 1 55 17 17 TYR CB C 37.994 0.2 1 56 17 17 TYR N N 119.955 0.1 1 57 18 18 LYS H H 8.133 0.02 1 58 18 18 LYS CA C 59.658 0.2 1 59 18 18 LYS CB C 32.256 0.2 1 60 18 18 LYS N N 120.129 0.1 1 61 19 19 GLU H H 8.134 0.02 1 62 19 19 GLU CA C 59.926 0.2 1 63 19 19 GLU CB C 29.599 0.2 1 64 19 19 GLU N N 120.426 0.1 1 65 20 20 VAL H H 9.258 0.02 1 66 20 20 VAL CA C 67.585 0.2 1 67 20 20 VAL CB C 31.349 0.2 1 68 20 20 VAL N N 119.164 0.1 1 69 21 21 THR H H 8.159 0.02 1 70 21 21 THR CA C 66.913 0.2 1 71 21 21 THR CB C 68.440 0.2 1 72 21 21 THR N N 116.211 0.1 1 73 22 22 THR H H 7.728 0.02 1 74 22 22 THR CA C 66.037 0.2 1 75 22 22 THR CB C 68.746 0.2 1 76 22 22 THR N N 117.351 0.1 1 77 23 23 LEU H H 8.159 0.02 1 78 23 23 LEU CA C 57.342 0.2 1 79 23 23 LEU CB C 42.997 0.2 1 80 23 23 LEU N N 122.773 0.1 1 81 24 24 THR H H 7.935 0.02 1 82 24 24 THR CA C 65.038 0.2 1 83 24 24 THR CB C 68.747 0.2 1 84 24 24 THR N N 110.750 0.1 1 85 25 25 ALA H H 7.238 0.02 1 86 25 25 ALA CA C 53.870 0.2 1 87 25 25 ALA CB C 19.432 0.2 1 88 25 25 ALA N N 122.782 0.1 1 89 26 26 ASP H H 7.802 0.02 1 90 26 26 ASP N N 115.672 0.1 1 91 28 28 PRO CA C 61.657 0.2 1 92 28 28 PRO CB C 31.461 0.2 1 93 29 29 ASP H H 8.288 0.02 1 94 29 29 ASP CA C 55.999 0.2 1 95 29 29 ASP CB C 40.756 0.2 1 96 29 29 ASP N N 120.285 0.1 1 97 30 30 GLY H H 8.677 0.02 1 98 30 30 GLY CA C 45.747 0.2 1 99 30 30 GLY N N 112.211 0.1 1 100 31 31 ILE H H 7.882 0.02 1 101 31 31 ILE CA C 59.747 0.2 1 102 31 31 ILE CB C 40.241 0.2 1 103 31 31 ILE N N 121.526 0.1 1 104 32 32 LYS H H 8.438 0.02 1 105 32 32 LYS CA C 54.706 0.2 1 106 32 32 LYS CB C 36.475 0.2 1 107 32 32 LYS N N 125.009 0.1 1 108 33 33 VAL H H 8.367 0.02 1 109 33 33 VAL CA C 60.562 0.2 1 110 33 33 VAL CB C 33.815 0.2 1 111 33 33 VAL N N 118.863 0.1 1 112 34 34 PHE H H 8.658 0.02 1 113 34 34 PHE N N 122.976 0.1 1 114 35 35 PRO CA C 62.914 0.2 1 115 35 35 PRO CB C 32.548 0.2 1 116 36 36 ASN H H 8.968 0.02 1 117 36 36 ASN CA C 52.156 0.2 1 118 36 36 ASN CB C 39.030 0.2 1 119 36 36 ASN N N 121.594 0.1 1 120 37 37 GLU H H 9.048 0.02 1 121 37 37 GLU CA C 58.894 0.2 1 122 37 37 GLU CB C 30.377 0.2 1 123 37 37 GLU N N 123.954 0.1 1 124 38 38 GLU H H 8.151 0.02 1 125 38 38 GLU CA C 57.097 0.2 1 126 38 38 GLU CB C 30.252 0.2 1 127 38 38 GLU N N 116.233 0.1 1 128 39 39 ASP H H 7.544 0.02 1 129 39 39 ASP CA C 53.758 0.2 1 130 39 39 ASP CB C 40.581 0.2 1 131 39 39 ASP N N 117.431 0.1 1 132 40 40 LEU H H 8.691 0.02 1 133 40 40 LEU CA C 56.126 0.2 1 134 40 40 LEU CB C 42.056 0.2 1 135 40 40 LEU N N 125.952 0.1 1 136 41 41 THR H H 8.004 0.02 1 137 41 41 THR CA C 62.622 0.2 1 138 41 41 THR CB C 69.177 0.2 1 139 41 41 THR N N 103.412 0.1 1 140 42 42 ASP H H 7.152 0.02 1 141 42 42 ASP CA C 52.722 0.2 1 142 42 42 ASP CB C 42.275 0.2 1 143 42 42 ASP N N 122.203 0.1 1 144 43 43 LEU H H 8.671 0.02 1 145 43 43 LEU CA C 53.819 0.2 1 146 43 43 LEU CB C 44.621 0.2 1 147 43 43 LEU N N 124.978 0.1 1 148 44 44 GLN H H 8.136 0.02 1 149 44 44 GLN CA C 55.387 0.2 1 150 44 44 GLN CB C 29.824 0.2 1 151 44 44 GLN N N 124.138 0.1 1 152 45 45 VAL H H 8.667 0.02 1 153 45 45 VAL CA C 59.643 0.2 1 154 45 45 VAL CB C 37.311 0.2 1 155 45 45 VAL N N 121.215 0.1 1 156 46 46 THR H H 9.394 0.02 1 157 46 46 THR CA C 60.372 0.2 1 158 46 46 THR CB C 71.317 0.2 1 159 46 46 THR N N 116.800 0.1 1 160 47 47 ILE H H 9.168 0.02 1 161 47 47 ILE CA C 59.441 0.2 1 162 47 47 ILE CB C 42.447 0.2 1 163 47 47 ILE N N 121.597 0.1 1 164 48 48 GLU H H 8.735 0.02 1 165 48 48 GLU CA C 55.607 0.2 1 166 48 48 GLU CB C 30.438 0.2 1 167 48 48 GLU N N 127.866 0.1 1 168 49 49 GLY H H 9.561 0.02 1 169 49 49 GLY N N 112.447 0.1 1 170 50 50 PRO CA C 63.109 0.2 1 171 50 50 PRO CB C 32.194 0.2 1 172 51 51 GLU H H 8.938 0.02 1 173 51 51 GLU CA C 57.729 0.2 1 174 51 51 GLU CB C 29.764 0.2 1 175 51 51 GLU N N 124.606 0.1 1 176 52 52 GLY H H 9.167 0.02 1 177 52 52 GLY CA C 45.629 0.2 1 178 52 52 GLY N N 110.808 0.1 1 179 53 53 THR H H 7.498 0.02 1 180 53 53 THR N N 108.437 0.1 1 181 54 54 PRO CA C 63.764 0.2 1 182 54 54 PRO CB C 32.558 0.2 1 183 55 55 TYR H H 6.914 0.02 1 184 55 55 TYR CA C 55.845 0.2 1 185 55 55 TYR CB C 38.279 0.2 1 186 55 55 TYR N N 113.993 0.1 1 187 56 56 ALA H H 7.277 0.02 1 188 56 56 ALA CA C 53.700 0.2 1 189 56 56 ALA CB C 19.577 0.2 1 190 56 56 ALA N N 123.188 0.1 1 191 57 57 GLY H H 8.715 0.02 1 192 57 57 GLY CA C 45.294 0.2 1 193 57 57 GLY N N 111.735 0.1 1 194 58 58 GLY H H 8.257 0.02 1 195 58 58 GLY CA C 44.587 0.2 1 196 58 58 GLY N N 107.109 0.1 1 197 59 59 LEU H H 9.289 0.02 1 198 59 59 LEU CA C 54.098 0.2 1 199 59 59 LEU CB C 43.214 0.2 1 200 59 59 LEU N N 126.986 0.1 1 201 60 60 PHE H H 8.847 0.02 1 202 60 60 PHE CA C 57.359 0.2 1 203 60 60 PHE CB C 40.363 0.2 1 204 60 60 PHE N N 123.809 0.1 1 205 61 61 ARG H H 9.374 0.02 1 206 61 61 ARG CA C 55.492 0.2 1 207 61 61 ARG CB C 31.451 0.2 1 208 61 61 ARG N N 123.746 0.1 1 209 62 62 MET H H 9.451 0.02 1 210 62 62 MET CA C 54.413 0.2 1 211 62 62 MET CB C 37.355 0.2 1 212 62 62 MET N N 124.002 0.1 1 213 63 63 LYS H H 9.075 0.02 1 214 63 63 LYS CA C 54.453 0.2 1 215 63 63 LYS CB C 36.145 0.2 1 216 63 63 LYS N N 120.121 0.1 1 217 64 64 LEU H H 8.964 0.02 1 218 64 64 LEU CA C 52.784 0.2 1 219 64 64 LEU CB C 45.005 0.2 1 220 64 64 LEU N N 123.320 0.1 1 221 65 65 LEU H H 9.011 0.02 1 222 65 65 LEU CA C 52.982 0.2 1 223 65 65 LEU CB C 43.761 0.2 1 224 65 65 LEU N N 122.445 0.1 1 225 66 66 LEU H H 9.023 0.02 1 226 66 66 LEU CA C 55.461 0.2 1 227 66 66 LEU CB C 40.975 0.2 1 228 66 66 LEU N N 126.901 0.1 1 229 67 67 GLY H H 7.899 0.02 1 230 67 67 GLY CA C 44.227 0.2 1 231 67 67 GLY N N 108.891 0.1 1 232 68 68 LYS H H 8.390 0.02 1 233 68 68 LYS CA C 58.238 0.2 1 234 68 68 LYS CB C 32.265 0.2 1 235 68 68 LYS N N 116.508 0.1 1 236 69 69 ASP H H 8.524 0.02 1 237 69 69 ASP CA C 52.865 0.2 1 238 69 69 ASP CB C 40.553 0.2 1 239 69 69 ASP N N 116.136 0.1 1 240 70 70 PHE H H 7.702 0.02 1 241 70 70 PHE N N 124.895 0.1 1 242 71 71 PRO CA C 64.034 0.2 1 243 71 71 PRO CB C 32.299 0.2 1 244 72 72 ALA H H 8.551 0.02 1 245 72 72 ALA CA C 55.886 0.2 1 246 72 72 ALA CB C 18.189 0.2 1 247 72 72 ALA N N 128.435 0.1 1 248 73 73 SER H H 7.836 0.02 1 249 73 73 SER N N 111.632 0.1 1 250 75 75 PRO CA C 61.990 0.2 1 251 75 75 PRO CB C 32.552 0.2 1 252 76 76 LYS H H 7.917 0.02 1 253 76 76 LYS CA C 55.641 0.2 1 254 76 76 LYS CB C 34.429 0.2 1 255 76 76 LYS N N 118.364 0.1 1 256 77 77 GLY H H 8.335 0.02 1 257 77 77 GLY CA C 44.542 0.2 1 258 77 77 GLY N N 107.453 0.1 1 259 78 78 TYR H H 8.685 0.02 1 260 78 78 TYR CA C 56.075 0.2 1 261 78 78 TYR CB C 41.652 0.2 1 262 78 78 TYR N N 119.276 0.1 1 263 79 79 PHE H H 10.054 0.02 1 264 79 79 PHE CA C 60.564 0.2 1 265 79 79 PHE CB C 39.420 0.2 1 266 79 79 PHE N N 122.525 0.1 1 267 80 80 LEU H H 9.411 0.02 1 268 80 80 LEU CA C 55.393 0.2 1 269 80 80 LEU CB C 41.580 0.2 1 270 80 80 LEU N N 125.864 0.1 1 271 81 81 THR H H 7.479 0.02 1 272 81 81 THR CA C 63.055 0.2 1 273 81 81 THR CB C 71.418 0.2 1 274 81 81 THR N N 118.554 0.1 1 275 82 82 LYS H H 8.470 0.02 1 276 82 82 LYS CA C 57.424 0.2 1 277 82 82 LYS CB C 32.020 0.2 1 278 82 82 LYS N N 127.550 0.1 1 279 83 83 ILE H H 8.216 0.02 1 280 83 83 ILE CA C 60.125 0.2 1 281 83 83 ILE CB C 41.485 0.2 1 282 83 83 ILE N N 120.974 0.1 1 283 84 84 PHE H H 8.326 0.02 1 284 84 84 PHE CA C 56.758 0.2 1 285 84 84 PHE CB C 40.034 0.2 1 286 84 84 PHE N N 127.814 0.1 1 287 85 85 HIS H H 9.474 0.02 1 288 85 85 HIS N N 129.962 0.1 1 289 86 86 PRO CA C 65.465 0.2 1 290 86 86 PRO CB C 32.673 0.2 1 291 87 87 ASN H H 11.438 0.02 1 292 87 87 ASN CA C 53.381 0.2 1 293 87 87 ASN CB C 41.128 0.2 1 294 87 87 ASN N N 116.818 0.1 1 295 88 88 VAL H H 7.374 0.02 1 296 88 88 VAL CA C 60.767 0.2 1 297 88 88 VAL CB C 34.067 0.2 1 298 88 88 VAL N N 118.605 0.1 1 299 89 89 GLY H H 9.372 0.02 1 300 89 89 GLY CA C 44.676 0.2 1 301 89 89 GLY N N 112.843 0.1 1 302 90 90 ALA H H 8.819 0.02 1 303 90 90 ALA CA C 55.122 0.2 1 304 90 90 ALA CB C 18.482 0.2 1 305 90 90 ALA N N 123.865 0.1 1 306 91 91 ASN H H 8.702 0.02 1 307 91 91 ASN CA C 52.427 0.2 1 308 91 91 ASN CB C 38.106 0.2 1 309 91 91 ASN N N 115.131 0.1 1 310 92 92 GLY H H 8.214 0.02 1 311 92 92 GLY CA C 45.544 0.2 1 312 92 92 GLY N N 107.109 0.1 1 313 93 93 GLU H H 8.944 0.02 1 314 93 93 GLU CA C 57.070 0.2 1 315 93 93 GLU CB C 29.771 0.2 1 316 93 93 GLU N N 123.339 0.1 1 317 94 94 ILE H H 7.828 0.02 1 318 94 94 ILE CA C 61.230 0.2 1 319 94 94 ILE CB C 38.731 0.2 1 320 94 94 ILE N N 124.667 0.1 1 321 95 95 CYS H H 7.953 0.02 1 322 95 95 CYS CA C 61.550 0.2 1 323 95 95 CYS CB C 30.109 0.2 1 324 95 95 CYS N N 128.950 0.1 1 325 96 96 VAL H H 8.216 0.02 1 326 96 96 VAL CA C 64.141 0.2 1 327 96 96 VAL CB C 31.935 0.2 1 328 96 96 VAL N N 126.966 0.1 1 329 97 97 ASN H H 9.194 0.02 1 330 97 97 ASN CA C 56.643 0.2 1 331 97 97 ASN CB C 38.038 0.2 1 332 97 97 ASN N N 122.796 0.1 1 333 102 102 ASP CA C 54.452 0.2 1 334 102 102 ASP CB C 40.596 0.2 1 335 103 103 TRP H H 7.581 0.02 1 336 103 103 TRP CA C 59.103 0.2 1 337 103 103 TRP CB C 30.198 0.2 1 338 103 103 TRP N N 119.480 0.1 1 339 104 104 THR H H 5.865 0.02 1 340 104 104 THR CA C 59.438 0.2 1 341 104 104 THR CB C 71.495 0.2 1 342 104 104 THR N N 117.751 0.1 1 343 105 105 ALA H H 8.096 0.02 1 344 105 105 ALA CA C 53.459 0.2 1 345 105 105 ALA CB C 18.667 0.2 1 346 105 105 ALA N N 120.079 0.1 1 347 106 106 GLU H H 7.748 0.02 1 348 106 106 GLU CA C 56.861 0.2 1 349 106 106 GLU CB C 29.523 0.2 1 350 106 106 GLU N N 114.810 0.1 1 351 107 107 LEU H H 7.004 0.02 1 352 107 107 LEU CA C 55.235 0.2 1 353 107 107 LEU CB C 40.894 0.2 1 354 107 107 LEU N N 120.908 0.1 1 355 108 108 GLY H H 7.467 0.02 1 356 108 108 GLY CA C 45.035 0.2 1 357 108 108 GLY N N 104.200 0.1 1 358 109 109 ILE H H 10.244 0.02 1 359 109 109 ILE CA C 64.599 0.2 1 360 109 109 ILE CB C 37.574 0.2 1 361 109 109 ILE N N 121.445 0.1 1 362 110 110 ARG H H 9.572 0.02 1 363 110 110 ARG CA C 61.057 0.2 1 364 110 110 ARG CB C 30.532 0.2 1 365 110 110 ARG N N 121.807 0.1 1 366 111 111 HIS H H 7.853 0.02 1 367 111 111 HIS CA C 60.627 0.2 1 368 111 111 HIS CB C 31.997 0.2 1 369 111 111 HIS N N 115.863 0.1 1 370 112 112 VAL H H 7.879 0.02 1 371 112 112 VAL CA C 66.282 0.2 1 372 112 112 VAL CB C 31.408 0.2 1 373 112 112 VAL N N 121.029 0.1 1 374 113 113 LEU H H 8.081 0.02 1 375 113 113 LEU CA C 58.128 0.2 1 376 113 113 LEU CB C 40.912 0.2 1 377 113 113 LEU N N 118.590 0.1 1 378 114 114 LEU H H 8.168 0.02 1 379 114 114 LEU CA C 58.023 0.2 1 380 114 114 LEU CB C 40.995 0.2 1 381 114 114 LEU N N 118.837 0.1 1 382 115 115 THR H H 8.281 0.02 1 383 115 115 THR CA C 67.275 0.2 1 384 115 115 THR CB C 68.034 0.2 1 385 115 115 THR N N 118.863 0.1 1 386 116 116 ILE H H 8.131 0.02 1 387 116 116 ILE CA C 65.992 0.2 1 388 116 116 ILE CB C 37.440 0.2 1 389 116 116 ILE N N 123.284 0.1 1 390 117 117 LYS H H 7.999 0.02 1 391 117 117 LYS CA C 61.231 0.2 1 392 117 117 LYS CB C 32.451 0.2 1 393 117 117 LYS N N 119.706 0.1 1 394 118 118 CYS H H 8.141 0.02 1 395 118 118 CYS CA C 63.329 0.2 1 396 118 118 CYS CB C 26.487 0.2 1 397 118 118 CYS N N 115.167 0.1 1 398 119 119 LEU H H 8.117 0.02 1 399 119 119 LEU CA C 56.714 0.2 1 400 119 119 LEU CB C 42.515 0.2 1 401 119 119 LEU N N 122.022 0.1 1 402 120 120 LEU H H 7.703 0.02 1 403 120 120 LEU CA C 58.253 0.2 1 404 120 120 LEU CB C 41.238 0.2 1 405 120 120 LEU N N 118.902 0.1 1 406 121 121 ILE H H 7.137 0.02 1 407 121 121 ILE CA C 63.790 0.2 1 408 121 121 ILE CB C 39.668 0.2 1 409 121 121 ILE N N 117.032 0.1 1 410 122 122 HIS H H 8.562 0.02 1 411 122 122 HIS N N 116.776 0.1 1 412 125 125 PRO CA C 67.450 0.2 1 413 125 125 PRO CB C 31.328 0.2 1 414 126 126 GLU H H 8.162 0.02 1 415 126 126 GLU CA C 58.897 0.2 1 416 126 126 GLU CB C 30.377 0.2 1 417 126 126 GLU N N 116.221 0.1 1 418 127 127 SER H H 8.145 0.02 1 419 127 127 SER CA C 57.042 0.2 1 420 127 127 SER CB C 62.242 0.2 1 421 127 127 SER N N 116.162 0.1 1 422 128 128 ALA H H 7.754 0.02 1 423 128 128 ALA CA C 52.990 0.2 1 424 128 128 ALA CB C 19.521 0.2 1 425 128 128 ALA N N 123.597 0.1 1 426 129 129 LEU H H 7.961 0.02 1 427 129 129 LEU CA C 56.085 0.2 1 428 129 129 LEU CB C 43.576 0.2 1 429 129 129 LEU N N 123.584 0.1 1 430 130 130 ASN H H 7.827 0.02 1 431 130 130 ASN CA C 51.502 0.2 1 432 130 130 ASN CB C 37.734 0.2 1 433 130 130 ASN N N 116.830 0.1 1 434 131 131 GLU H H 8.790 0.02 1 435 131 131 GLU CA C 59.608 0.2 1 436 131 131 GLU CB C 29.639 0.2 1 437 131 131 GLU N N 124.136 0.1 1 438 132 132 GLU H H 8.330 0.02 1 439 132 132 GLU CA C 59.310 0.2 1 440 132 132 GLU CB C 29.773 0.2 1 441 132 132 GLU N N 120.899 0.1 1 442 133 133 ALA H H 7.189 0.02 1 443 133 133 ALA CA C 54.873 0.2 1 444 133 133 ALA CB C 16.332 0.2 1 445 133 133 ALA N N 119.217 0.1 1 446 134 134 GLY H H 8.265 0.02 1 447 134 134 GLY CA C 47.597 0.2 1 448 134 134 GLY N N 102.717 0.1 1 449 135 135 ARG H H 8.125 0.02 1 450 135 135 ARG CA C 59.326 0.2 1 451 135 135 ARG CB C 30.028 0.2 1 452 135 135 ARG N N 120.370 0.1 1 453 136 136 LEU H H 8.173 0.02 1 454 136 136 LEU CA C 57.749 0.2 1 455 136 136 LEU CB C 43.190 0.2 1 456 136 136 LEU N N 118.277 0.1 1 457 137 137 LEU H H 7.833 0.02 1 458 137 137 LEU CA C 59.133 0.2 1 459 137 137 LEU CB C 41.834 0.2 1 460 137 137 LEU N N 118.388 0.1 1 461 138 138 LEU H H 6.893 0.02 1 462 138 138 LEU CA C 56.480 0.2 1 463 138 138 LEU CB C 43.376 0.2 1 464 138 138 LEU N N 113.263 0.1 1 465 139 139 GLU H H 8.507 0.02 1 466 139 139 GLU CA C 58.088 0.2 1 467 139 139 GLU CB C 31.597 0.2 1 468 139 139 GLU N N 117.674 0.1 1 469 140 140 ASN H H 9.150 0.02 1 470 140 140 ASN CA C 52.588 0.2 1 471 140 140 ASN CB C 37.679 0.2 1 472 140 140 ASN N N 118.427 0.1 1 473 141 141 TYR H H 9.144 0.02 1 474 141 141 TYR CA C 63.421 0.2 1 475 141 141 TYR CB C 38.655 0.2 1 476 141 141 TYR N N 126.860 0.1 1 477 142 142 GLU H H 8.720 0.02 1 478 142 142 GLU CA C 59.705 0.2 1 479 142 142 GLU CB C 29.055 0.2 1 480 142 142 GLU N N 115.598 0.1 1 481 143 143 GLU H H 7.614 0.02 1 482 143 143 GLU CA C 58.407 0.2 1 483 143 143 GLU CB C 29.667 0.2 1 484 143 143 GLU N N 121.083 0.1 1 485 144 144 TYR H H 7.795 0.02 1 486 144 144 TYR CA C 61.282 0.2 1 487 144 144 TYR CB C 36.566 0.2 1 488 144 144 TYR N N 121.321 0.1 1 489 145 145 ALA H H 8.664 0.02 1 490 145 145 ALA CA C 54.949 0.2 1 491 145 145 ALA CB C 17.393 0.2 1 492 145 145 ALA N N 121.449 0.1 1 493 146 146 ALA H H 7.830 0.02 1 494 146 146 ALA CA C 55.138 0.2 1 495 146 146 ALA CB C 18.117 0.2 1 496 146 146 ALA N N 119.580 0.1 1 497 147 147 ARG H H 7.830 0.02 1 498 147 147 ARG CA C 58.324 0.2 1 499 147 147 ARG CB C 29.100 0.2 1 500 147 147 ARG N N 119.590 0.1 1 501 148 148 ALA H H 8.439 0.02 1 502 148 148 ALA CA C 54.929 0.2 1 503 148 148 ALA CB C 17.719 0.2 1 504 148 148 ALA N N 120.467 0.1 1 505 149 149 ARG H H 8.521 0.02 1 506 149 149 ARG CA C 59.076 0.2 1 507 149 149 ARG CB C 30.570 0.2 1 508 149 149 ARG N N 120.932 0.1 1 509 150 150 LEU H H 7.854 0.02 1 510 150 150 LEU CA C 57.940 0.2 1 511 150 150 LEU CB C 41.747 0.2 1 512 150 150 LEU N N 121.334 0.1 1 513 151 151 LEU H H 7.664 0.02 1 514 151 151 LEU CA C 57.347 0.2 1 515 151 151 LEU CB C 41.275 0.2 1 516 151 151 LEU N N 116.157 0.1 1 517 152 152 THR H H 7.902 0.02 1 518 152 152 THR CA C 67.049 0.2 1 519 152 152 THR CB C 68.634 0.2 1 520 152 152 THR N N 120.878 0.1 1 521 153 153 GLU H H 8.304 0.02 1 522 153 153 GLU CA C 58.370 0.2 1 523 153 153 GLU CB C 29.550 0.2 1 524 153 153 GLU N N 124.238 0.1 1 525 154 154 ILE H H 7.894 0.02 1 526 154 154 ILE CA C 63.245 0.2 1 527 154 154 ILE CB C 39.359 0.2 1 528 154 154 ILE N N 118.884 0.1 1 529 155 155 HIS H H 8.213 0.02 1 530 155 155 HIS CA C 56.861 0.2 1 531 155 155 HIS CB C 32.108 0.2 1 532 155 155 HIS N N 118.243 0.1 1 533 156 156 GLY H H 8.230 0.02 1 534 156 156 GLY N N 115.689 0.1 1 stop_ save_