data_17362 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments for E2-25K ; _BMRB_accession_number 17362 _BMRB_flat_file_name bmr17362.str _Entry_type original _Submission_date 2010-12-14 _Accession_date 2010-12-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone chemical shift assignments for E2-25K/HIP2' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wilson Randall C. . 2 Edmondson Stephen P. . 3 Twigg Pamela D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 171 "13C chemical shifts" 558 "15N chemical shifts" 171 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-14 update BMRB 'update entry citation' 2010-12-16 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17195 'UBA Domain of E2-25K' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The E2-25K ubiquitin-associated (UBA) domain aids in polyubiquitin chain synthesis and linkage specificity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21281599 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wilson Randall C. . 2 Edmondson Stephen P. . 3 Flatt Justin W. . 4 Helms Kimberli . . 5 Twigg Pamela D. . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_name_full 'Biochemical and biophysical research communications' _Journal_volume 405 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 662 _Page_last 666 _Year 2011 _Details . loop_ _Keyword E2-25K 'UBA domain' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name E2-25K _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'E2-25K monomer' $E2-25K stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E2-25K _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common E2-25K _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 207 _Mol_residue_sequence ; AMADIGSMANIAVQRIKREF KEVLKSEETSKNQIKVDLVD ENFTELRGEIAGPPDTPYEG GRYQLEIKIPETYPFNPPKV RFITKIWHPNISSVTGAICL DILKDQWAAAMTLRTVLLSL QALLAAAEPDDPQDAVVANQ YKQNPEMFKQTARLWAHVYA GAPVSSPEYTKKIENLCAMG FDRNAVIVALSSKSWDVETA TELLLSN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 ALA 2 -5 MET 3 -4 ALA 4 -3 ASP 5 -2 ILE 6 -1 GLY 7 0 SER 8 1 MET 9 2 ALA 10 3 ASN 11 4 ILE 12 5 ALA 13 6 VAL 14 7 GLN 15 8 ARG 16 9 ILE 17 10 LYS 18 11 ARG 19 12 GLU 20 13 PHE 21 14 LYS 22 15 GLU 23 16 VAL 24 17 LEU 25 18 LYS 26 19 SER 27 20 GLU 28 21 GLU 29 22 THR 30 23 SER 31 24 LYS 32 25 ASN 33 26 GLN 34 27 ILE 35 28 LYS 36 29 VAL 37 30 ASP 38 31 LEU 39 32 VAL 40 33 ASP 41 34 GLU 42 35 ASN 43 36 PHE 44 37 THR 45 38 GLU 46 39 LEU 47 40 ARG 48 41 GLY 49 42 GLU 50 43 ILE 51 44 ALA 52 45 GLY 53 46 PRO 54 47 PRO 55 48 ASP 56 49 THR 57 50 PRO 58 51 TYR 59 52 GLU 60 53 GLY 61 54 GLY 62 55 ARG 63 56 TYR 64 57 GLN 65 58 LEU 66 59 GLU 67 60 ILE 68 61 LYS 69 62 ILE 70 63 PRO 71 64 GLU 72 65 THR 73 66 TYR 74 67 PRO 75 68 PHE 76 69 ASN 77 70 PRO 78 71 PRO 79 72 LYS 80 73 VAL 81 74 ARG 82 75 PHE 83 76 ILE 84 77 THR 85 78 LYS 86 79 ILE 87 80 TRP 88 81 HIS 89 82 PRO 90 83 ASN 91 84 ILE 92 85 SER 93 86 SER 94 87 VAL 95 88 THR 96 89 GLY 97 90 ALA 98 91 ILE 99 92 CYS 100 93 LEU 101 94 ASP 102 95 ILE 103 96 LEU 104 97 LYS 105 98 ASP 106 99 GLN 107 100 TRP 108 101 ALA 109 102 ALA 110 103 ALA 111 104 MET 112 105 THR 113 106 LEU 114 107 ARG 115 108 THR 116 109 VAL 117 110 LEU 118 111 LEU 119 112 SER 120 113 LEU 121 114 GLN 122 115 ALA 123 116 LEU 124 117 LEU 125 118 ALA 126 119 ALA 127 120 ALA 128 121 GLU 129 122 PRO 130 123 ASP 131 124 ASP 132 125 PRO 133 126 GLN 134 127 ASP 135 128 ALA 136 129 VAL 137 130 VAL 138 131 ALA 139 132 ASN 140 133 GLN 141 134 TYR 142 135 LYS 143 136 GLN 144 137 ASN 145 138 PRO 146 139 GLU 147 140 MET 148 141 PHE 149 142 LYS 150 143 GLN 151 144 THR 152 145 ALA 153 146 ARG 154 147 LEU 155 148 TRP 156 149 ALA 157 150 HIS 158 151 VAL 159 152 TYR 160 153 ALA 161 154 GLY 162 155 ALA 163 156 PRO 164 157 VAL 165 158 SER 166 159 SER 167 160 PRO 168 161 GLU 169 162 TYR 170 163 THR 171 164 LYS 172 165 LYS 173 166 ILE 174 167 GLU 175 168 ASN 176 169 LEU 177 170 CYS 178 171 ALA 179 172 MET 180 173 GLY 181 174 PHE 182 175 ASP 183 176 ARG 184 177 ASN 185 178 ALA 186 179 VAL 187 180 ILE 188 181 VAL 189 182 ALA 190 183 LEU 191 184 SER 192 185 SER 193 186 LYS 194 187 SER 195 188 TRP 196 189 ASP 197 190 VAL 198 191 GLU 199 192 THR 200 193 ALA 201 194 THR 202 195 GLU 203 196 LEU 204 197 LEU 205 198 LEU 206 199 SER 207 200 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 1YLA "Ubiquitin-Conjugating Enzyme E2-25 Kda (Huntington Interacting Protein 2)" 97.58 202 100.00 100.00 1.12e-146 PDB 2BEP "Crystal Structure Of Ubiquitin Conjugating Enzyme E2-25k" 75.36 159 99.36 100.00 4.50e-110 PDB 2BF8 "Crystal Structure Of Sumo Modified Ubiquitin Conjugating Enzyme E2-25k" 75.36 159 99.36 100.00 4.50e-110 PDB 2O25 "Ubiquitin-Conjugating Enzyme E2-25 Kda Complexed With Sumo-1- Conjugating Enzyme Ubc9" 97.58 202 100.00 100.00 1.12e-146 PDB 3E46 "Crystal Structure Of Ubiquitin-Conjugating Enzyme E2-25kda (Huntington Interacting Protein 2) M172a Mutant" 101.45 253 98.10 98.10 5.17e-147 PDB 3F92 "Crystal Structure Of Ubiquitin-Conjugating Enzyme E2-25kda (Huntington Interacting Protein 2) M172a Mutant Crystallized At Ph 8" 101.45 253 98.10 98.10 5.17e-147 PDB 3K9O "The Crystal Structure Of E2-25k And Ubb+1 Complex" 97.10 201 99.50 99.50 7.05e-145 PDB 3K9P "The Crystal Structure Of E2-25k And Ubiquitin Complex" 97.58 217 100.00 100.00 9.06e-147 DBJ BAA24927 "huntingtin interacting protein-2 [Mus musculus]" 96.62 200 99.50 99.50 9.71e-144 DBJ BAA78555 "E2 ubiquitin-conjugating enzyme [Homo sapiens]" 96.62 200 100.00 100.00 6.03e-145 DBJ BAB24523 "unnamed protein product [Mus musculus]" 56.04 116 100.00 100.00 2.25e-76 DBJ BAC29296 "unnamed protein product [Mus musculus]" 96.62 200 100.00 100.00 6.03e-145 DBJ BAC33269 "unnamed protein product [Mus musculus]" 96.62 200 100.00 100.00 6.03e-145 EMBL CAG32430 "hypothetical protein RCJMB04_25e17 [Gallus gallus]" 96.62 200 99.50 100.00 1.84e-144 GB AAB19536 "E2(25K) [Bos taurus]" 96.62 200 99.50 100.00 1.82e-144 GB AAC50633 "huntingtin interacting protein [Homo sapiens]" 96.62 200 100.00 100.00 6.03e-145 GB AAH02013 "Ubiquitin-conjugating enzyme E2K (UBC1 homolog, yeast) [Mus musculus]" 96.62 200 100.00 100.00 6.03e-145 GB AAH22804 "Ubiquitin-conjugating enzyme E2K (UBC1 homolog, yeast) [Homo sapiens]" 96.62 200 100.00 100.00 6.03e-145 GB AAH41728 "Ube2k protein [Xenopus laevis]" 96.62 200 97.00 99.00 1.14e-141 REF NP_001005662 "ubiquitin-conjugating enzyme E2 K [Xenopus (Silurana) tropicalis]" 96.62 200 97.50 99.00 3.08e-142 REF NP_001008611 "ubiquitin-conjugating enzyme E2 K [Danio rerio]" 96.62 200 97.00 99.50 1.26e-141 REF NP_001026711 "ubiquitin-conjugating enzyme E2 K [Gallus gallus]" 96.62 200 99.50 100.00 1.84e-144 REF NP_001072139 "ubiquitin-conjugating enzyme E2 K [Sus scrofa]" 96.62 200 100.00 100.00 6.03e-145 REF NP_001080290 "ubiquitin-conjugating enzyme E2K [Xenopus laevis]" 96.62 200 97.00 99.00 1.14e-141 SP P61085 "RecName: Full=Ubiquitin-conjugating enzyme E2 K; AltName: Full=E2 ubiquitin-conjugating enzyme K; AltName: Full=Huntingtin-inte" 96.62 200 100.00 100.00 6.03e-145 SP P61086 "RecName: Full=Ubiquitin-conjugating enzyme E2 K; AltName: Full=E2 ubiquitin-conjugating enzyme K; AltName: Full=Huntingtin-inte" 96.62 200 100.00 100.00 6.03e-145 SP P61087 "RecName: Full=Ubiquitin-conjugating enzyme E2 K; AltName: Full=E2 ubiquitin-conjugating enzyme K; AltName: Full=Huntingtin-inte" 96.62 200 100.00 100.00 6.03e-145 TPG DAA28715 "TPA: ubiquitin-conjugating enzyme E2K [Bos taurus]" 96.62 200 100.00 100.00 6.03e-145 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $E2-25K 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 $E2-25K 'recombinant technology' . Escherichia coli . pET30a 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 $E2-25K 0.35 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' DSS 0.12 mM 'natural abundance' 'sodium azide' 0.9 '% v/v' 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E2-25K 0.50 mM '[U-13C; U-15N]' DSS 0.12 mM 'natural abundance' 'sodium azide' 0.9 '% v/v' 'natural abundance' 'sodium phosphate' 50 mM '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_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 273 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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 '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'E2-25K monomer' _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 1 8 MET H H 7.68 . 1 2 1 8 MET CA C 56.9 . 1 3 1 8 MET CB C 32.6 . 1 4 1 8 MET N N 126.21 . 1 5 2 9 ALA C C 177.8 . 1 6 2 9 ALA CA C 52.7 . 1 7 2 9 ALA CB C 17.4 . 1 8 3 10 ASN H H 8.03 . 1 9 3 10 ASN C C 175.7 . 1 10 3 10 ASN CA C 53.1 . 1 11 3 10 ASN CB C 37.9 . 1 12 3 10 ASN N N 116.73 . 1 13 4 11 ILE H H 8.04 . 1 14 4 11 ILE C C 176.9 . 1 15 4 11 ILE CA C 63.0 . 1 16 4 11 ILE CB C 36.8 . 1 17 4 11 ILE N N 121.24 . 1 18 5 12 ALA H H 8.19 . 1 19 5 12 ALA C C 179.2 . 1 20 5 12 ALA CA C 55.5 . 1 21 5 12 ALA CB C 18.2 . 1 22 5 12 ALA N N 124.59 . 1 23 6 13 VAL H H 7.70 . 1 24 6 13 VAL C C 177.3 . 1 25 6 13 VAL CA C 65.3 . 1 26 6 13 VAL CB C 30.7 . 1 27 6 13 VAL N N 116.82 . 1 28 7 14 GLN H H 7.96 . 1 29 7 14 GLN C C 177.8 . 1 30 7 14 GLN CA C 58.3 . 1 31 7 14 GLN CB C 27.4 . 1 32 7 14 GLN N N 117.82 . 1 33 8 15 ARG H H 8.32 . 1 34 8 15 ARG C C 175.9 . 1 35 8 15 ARG CA C 57.5 . 1 36 8 15 ARG CB C 32.5 . 1 37 8 15 ARG N N 119.43 . 1 38 9 16 ILE H H 8.53 . 1 39 9 16 ILE CA C 60.0 . 1 40 9 16 ILE CB C 40.6 . 1 41 9 16 ILE N N 120.29 . 1 42 10 17 LYS C C 179.5 . 1 43 10 17 LYS CA C 60.25 . 1 44 10 17 LYS CB C 30.9 . 1 45 11 18 ARG H H 7.45 . 1 46 11 18 ARG C C 179.4 . 1 47 11 18 ARG CA C 58.7 . 1 48 11 18 ARG CB C 29.0 . 1 49 11 18 ARG N N 118.84 . 1 50 12 19 GLU H H 8.86 . 1 51 12 19 GLU C C 179.9 . 1 52 12 19 GLU CA C 59.0 . 1 53 12 19 GLU CB C 29.4 . 1 54 12 19 GLU N N 121.96 . 1 55 13 20 PHE H H 9.40 . 1 56 13 20 PHE C C 174.6 . 1 57 13 20 PHE CA C 60.9 . 1 58 13 20 PHE CB C 38.9 . 1 59 13 20 PHE N N 122.99 . 1 60 14 21 LYS H H 7.53 . 1 61 14 21 LYS C C 178.1 . 1 62 14 21 LYS CA C 58.8 . 1 63 14 21 LYS CB C 31.0 . 1 64 14 21 LYS N N 118.59 . 1 65 15 22 GLU H H 8.07 . 1 66 15 22 GLU C C 179.4 . 1 67 15 22 GLU CA C 58.3 . 1 68 15 22 GLU CB C 28.6 . 1 69 15 22 GLU N N 118.16 . 1 70 16 23 VAL H H 7.97 . 1 71 16 23 VAL C C 178.8 . 1 72 16 23 VAL CA C 66.2 . 1 73 16 23 VAL CB C 30.2 . 1 74 16 23 VAL N N 118.73 . 1 75 17 24 LEU H H 7.94 . 1 76 17 24 LEU CA C 57.2 . 1 77 17 24 LEU CB C 40.8 . 1 78 17 24 LEU N N 121.65 . 1 79 18 25 LYS C C 176.5 . 1 80 18 25 LYS CA C 55.2 . 1 81 18 25 LYS CB C 31.1 . 1 82 19 26 SER H H 7.84 . 1 83 19 26 SER CA C 59.0 . 1 84 19 26 SER CB C 64.1 . 1 85 19 26 SER N N 117.18 . 1 86 20 27 GLU C C 176.5 . 1 87 20 27 GLU CA C 56.3 . 1 88 20 27 GLU CB C 29.2 . 1 89 21 28 GLU H H 8.37 . 1 90 21 28 GLU C C 177.2 . 1 91 21 28 GLU CA C 56.2 . 1 92 21 28 GLU CB C 29.5 . 1 93 21 28 GLU N N 121.83 . 1 94 22 29 THR H H 8.11 . 1 95 22 29 THR CA C 60.8 . 1 96 22 29 THR CB C 69.4 . 1 97 22 29 THR N N 115.11 . 1 98 23 30 SER C C 174.5 . 1 99 23 30 SER CA C 57.9 . 1 100 23 30 SER CB C 63.3 . 1 101 24 31 LYS H H 8.51 . 1 102 24 31 LYS C C 175.9 . 1 103 24 31 LYS CA C 55.9 . 1 104 24 31 LYS CB C 29.3 . 1 105 24 31 LYS N N 122.90 . 1 106 25 32 ASN H H 8.28 . 1 107 25 32 ASN C C 178.3 . 1 108 25 32 ASN CA C 53.6 . 1 109 25 32 ASN CB C 36.9 . 1 110 25 32 ASN N N 116.61 . 1 111 26 33 GLN H H 8.48 . 1 112 26 33 GLN C C 178.4 . 1 113 26 33 GLN CA C 56.6 . 1 114 26 33 GLN CB C 30.2 . 1 115 26 33 GLN N N 116.13 . 1 116 27 34 ILE H H 7.37 . 1 117 27 34 ILE CA C 61.4 . 1 118 27 34 ILE CB C 39.6 . 1 119 27 34 ILE N N 112.92 . 1 120 28 35 LYS C C 173.8 . 1 121 28 35 LYS CA C 55.2 . 1 122 28 35 LYS CB C 35.3 . 1 123 29 36 VAL H H 8.05 . 1 124 29 36 VAL C C 171.8 . 1 125 29 36 VAL CA C 59.8 . 1 126 29 36 VAL CB C 34.4 . 1 127 29 36 VAL N N 118.47 . 1 128 30 37 ASP H H 8.79 . 1 129 30 37 ASP C C 174.7 . 1 130 30 37 ASP CA C 52.4 . 1 131 30 37 ASP CB C 44.6 . 1 132 30 37 ASP N N 122.51 . 1 133 31 38 LEU H H 8.68 . 1 134 31 38 LEU C C 176.7 . 1 135 31 38 LEU CA C 54.5 . 1 136 31 38 LEU CB C 41.1 . 1 137 31 38 LEU N N 121.59 . 1 138 32 39 VAL H H 8.11 . 1 139 32 39 VAL C C 175.3 . 1 140 32 39 VAL CA C 61.6 . 1 141 32 39 VAL CB C 31.7 . 1 142 32 39 VAL N N 121.22 . 1 143 33 40 ASP H H 8.37 . 1 144 33 40 ASP C C 176.9 . 1 145 33 40 ASP CA C 54.4 . 1 146 33 40 ASP CB C 40.7 . 1 147 33 40 ASP N N 124.25 . 1 148 34 41 GLU H H 8.33 . 1 149 34 41 GLU C C 175.7 . 1 150 34 41 GLU CA C 55.6 . 1 151 34 41 GLU CB C 32.0 . 1 152 34 41 GLU N N 122.95 . 1 153 35 42 ASN H H 8.16 . 1 154 35 42 ASN CA C 56.8 . 1 155 35 42 ASN CB C 38.9 . 1 156 35 42 ASN N N 121.29 . 1 157 36 43 PHE C C 175.7 . 1 158 36 43 PHE CA C 57.5 . 1 159 36 43 PHE CB C 40.3 . 1 160 37 44 THR H H 7.96 . 1 161 37 44 THR CA C 61.5 . 1 162 37 44 THR CB C 69.1 . 1 163 37 44 THR N N 116.62 . 1 164 38 45 GLU C C 176.0 . 1 165 38 45 GLU CA C 54.2 . 1 166 38 45 GLU CB C 29.7 . 1 167 39 46 LEU H H 9.11 . 1 168 39 46 LEU C C 175.4 . 1 169 39 46 LEU CA C 52.8 . 1 170 39 46 LEU CB C 44.6 . 1 171 39 46 LEU N N 122.03 . 1 172 40 47 ARG H H 8.98 . 1 173 40 47 ARG C C 175.9 . 1 174 40 47 ARG CA C 53.0 . 1 175 40 47 ARG CB C 30.8 . 1 176 40 47 ARG N N 122.88 . 1 177 41 48 GLY H H 9.08 . 1 178 41 48 GLY C C 171.4 . 1 179 41 48 GLY CA C 43.0 . 1 180 41 48 GLY N N 112.18 . 1 181 42 49 GLU H H 8.81 . 1 182 42 49 GLU C C 174.3 . 1 183 42 49 GLU CA C 54.9 . 1 184 42 49 GLU CB C 32.7 . 1 185 42 49 GLU N N 121.17 . 1 186 43 50 ILE H H 8.6 . 1 187 43 50 ILE C C 174.7 . 1 188 43 50 ILE CA C 58 . 1 189 43 50 ILE CB C 41 . 1 190 43 50 ILE N N 116.14 . 1 191 44 51 ALA H H 8.29 . 1 192 44 51 ALA C C 178.7 . 1 193 44 51 ALA CA C 50.3 . 1 194 44 51 ALA CB C 19.1 . 1 195 44 51 ALA N N 125.46 . 1 196 45 52 GLY H H 8.73 . 1 197 45 52 GLY CA C 43.5 . 1 198 45 52 GLY N N 107.63 . 1 199 47 54 PRO C C 176.0 . 1 200 47 54 PRO CA C 62.0 . 1 201 47 54 PRO CB C 30.9 . 1 202 48 55 ASP H H 8.97 . 1 203 48 55 ASP C C 174.7 . 1 204 48 55 ASP CA C 55.2 . 1 205 48 55 ASP CB C 38.4 . 1 206 48 55 ASP N N 115.48 . 1 207 49 56 THR H H 7.34 . 1 208 49 56 THR CA C 59.0 . 1 209 49 56 THR CB C 70.5 . 1 210 49 56 THR N N 105.97 . 1 211 51 58 TYR C C 176.6 . 1 212 51 58 TYR CA C 55.5 . 1 213 51 58 TYR CB C 37.6 . 1 214 52 59 GLU H H 7.48 . 1 215 52 59 GLU C C 175.4 . 1 216 52 59 GLU CA C 57.4 . 1 217 52 59 GLU CB C 29.1 . 1 218 52 59 GLU N N 123.36 . 1 219 53 60 GLY H H 9.36 . 1 220 53 60 GLY C C 173.9 . 1 221 53 60 GLY CA C 44.0 . 1 222 53 60 GLY N N 115.14 . 1 223 54 61 GLY H H 8.29 . 1 224 54 61 GLY C C 172.9 . 1 225 54 61 GLY CA C 42.7 . 1 226 54 61 GLY N N 106.17 . 1 227 55 62 ARG H H 8.47 . 1 228 55 62 ARG C C 173.9 . 1 229 55 62 ARG CA C 54.6 . 1 230 55 62 ARG CB C 31.3 . 1 231 55 62 ARG N N 121.85 . 1 232 56 63 TYR H H 8.72 . 1 233 56 63 TYR C C 174.1 . 1 234 56 63 TYR CA C 57.1 . 1 235 56 63 TYR CB C 39.4 . 1 236 56 63 TYR N N 121.32 . 1 237 57 64 GLN H H 9.55 . 1 238 57 64 GLN CA C 54.1 . 1 239 57 64 GLN CB C 29.6 . 1 240 57 64 GLN N N 121.44 . 1 241 58 65 LEU C C 174.7 . 1 242 58 65 LEU CA C 52.8 . 1 243 58 65 LEU CB C 44.6 . 1 244 59 66 GLU H H 9.08 . 1 245 59 66 GLU C C 173.9 . 1 246 59 66 GLU CA C 54.5 . 1 247 59 66 GLU CB C 32.4 . 1 248 59 66 GLU N N 124.82 . 1 249 60 67 ILE H H 8.04 . 1 250 60 67 ILE C C 173.6 . 1 251 60 67 ILE CA C 59.58 . 1 252 60 67 ILE CB C 38.92 . 1 253 60 67 ILE N N 126.29 . 1 254 61 68 LYS H H 9.24 . 1 255 61 68 LYS C C 173.5 . 1 256 61 68 LYS CA C 53.93 . 1 257 61 68 LYS CB C 33.38 . 1 258 61 68 LYS N N 126.97 . 1 259 62 69 ILE H H 8.67 . 1 260 62 69 ILE CA C 60.3 . 1 261 62 69 ILE CB C 35.5 . 1 262 62 69 ILE N N 125.47 . 1 263 63 70 PRO C C 176.9 . 1 264 63 70 PRO CA C 61.6 . 1 265 63 70 PRO CB C 31.7 . 1 266 64 71 GLU H H 9.10 . 1 267 64 71 GLU C C 176.5 . 1 268 64 71 GLU CA C 58.3 . 1 269 64 71 GLU CB C 28.3 . 1 270 64 71 GLU N N 119.63 . 1 271 65 72 THR H H 6.99 . 1 272 65 72 THR C C 174.6 . 1 273 65 72 THR CA C 59.9 . 1 274 65 72 THR CB C 67.9 . 1 275 65 72 THR N N 102.82 . 1 276 66 73 TYR H H 7.61 . 1 277 66 73 TYR CA C 57.5 . 1 278 66 73 TYR CB C 39.5 . 1 279 66 73 TYR N N 126.91 . 1 280 67 74 PRO C C 174.6 . 1 281 67 74 PRO CA C 62.7 . 1 282 67 74 PRO CB C 31.6 . 1 283 68 75 PHE H H 8.78 . 1 284 68 75 PHE C C 175.2 . 1 285 68 75 PHE CA C 59.8 . 1 286 68 75 PHE CB C 37.1 . 1 287 68 75 PHE N N 125.36 . 1 288 69 76 ASN H H 7.07 . 1 289 69 76 ASN CA C 49.7 . 1 290 69 76 ASN CB C 40.1 . 1 291 69 76 ASN N N 115.73 . 1 292 71 78 PRO C C 174.6 . 1 293 71 78 PRO CA C 61.1 . 1 294 71 78 PRO CB C 31.1 . 1 295 72 79 LYS H H 8.61 . 1 296 72 79 LYS C C 176.7 . 1 297 72 79 LYS CA C 54.4 . 1 298 72 79 LYS CB C 31.1 . 1 299 72 79 LYS N N 120.65 . 1 300 73 80 VAL H H 8.85 . 1 301 73 80 VAL C C 175.9 . 1 302 73 80 VAL CA C 59.5 . 1 303 73 80 VAL CB C 33.2 . 1 304 73 80 VAL N N 126.13 . 1 305 74 81 ARG H H 8.32 . 1 306 74 81 ARG C C 175.4 . 1 307 74 81 ARG CA C 54.1 . 1 308 74 81 ARG CB C 33.4 . 1 309 74 81 ARG N N 123.53 . 1 310 75 82 PHE H H 9.45 . 1 311 75 82 PHE C C 174.7 . 1 312 75 82 PHE CA C 59.3 . 1 313 75 82 PHE CB C 37.6 . 1 314 75 82 PHE N N 124.72 . 1 315 76 83 ILE H H 8.09 . 1 316 76 83 ILE C C 177.5 . 1 317 76 83 ILE CA C 61.5 . 1 318 76 83 ILE CB C 38.3 . 1 319 76 83 ILE N N 121.37 . 1 320 77 84 THR H H 7.27 . 1 321 77 84 THR C C 173.3 . 1 322 77 84 THR CA C 62.7 . 1 323 77 84 THR CB C 69.9 . 1 324 77 84 THR N N 119.04 . 1 325 78 85 LYS H H 8.19 . 1 326 78 85 LYS C C 173.9 . 1 327 78 85 LYS CA C 56.0 . 1 328 78 85 LYS CB C 31.5 . 1 329 78 85 LYS N N 126.37 . 1 330 79 86 ILE H H 8.13 . 1 331 79 86 ILE C C 173.5 . 1 332 79 86 ILE CA C 60.42 . 1 333 79 86 ILE CB C 37.46 . 1 334 79 86 ILE N N 122.67 . 1 335 80 87 TRP H H 8.0061 . 1 336 80 87 TRP C C 173.9 . 1 337 80 87 TRP CA C 53.8 . 1 338 80 87 TRP CB C 29.7 . 1 339 80 87 TRP N N 129.87 . 1 340 81 88 HIS H H 10.56 . 1 341 81 88 HIS CA C 55.3 . 1 342 81 88 HIS CB C 34.8 . 1 343 81 88 HIS N N 131.08 . 1 344 82 89 PRO C C 176.3 . 1 345 82 89 PRO CA C 64.7 . 1 346 82 89 PRO CB C 31.2 . 1 347 83 90 ASN H H 11.27 . 1 348 83 90 ASN CA C 55.0 . 1 349 83 90 ASN CB C 40.2 . 1 350 83 90 ASN N N 117.37 . 1 351 84 91 ILE C C 174.3 . 1 352 84 91 ILE CA C 57.9 . 1 353 84 91 ILE CB C 41.1 . 1 354 85 92 SER H H 9.08 . 1 355 85 92 SER C C 177.1 . 1 356 85 92 SER CA C 58.2 . 1 357 85 92 SER CB C 62.5 . 1 358 85 92 SER N N 118.68 . 1 359 86 93 SER H H 9.93 . 1 360 86 93 SER C C 173.8 . 1 361 86 93 SER CA C 61.2 . 1 362 86 93 SER CB C 62.9 . 1 363 86 93 SER N N 129.97 . 1 364 87 94 VAL H H 7.99 . 1 365 87 94 VAL C C 177.8 . 1 366 87 94 VAL CA C 63.9 . 1 367 87 94 VAL CB C 33.0 . 1 368 87 94 VAL N N 121.56 . 1 369 88 95 THR H H 8.19 . 1 370 88 95 THR C C 176.2 . 1 371 88 95 THR CA C 60.9 . 1 372 88 95 THR CB C 71.0 . 1 373 88 95 THR N N 106.42 . 1 374 89 96 GLY H H 7.84 . 1 375 89 96 GLY C C 173.6 . 1 376 89 96 GLY CA C 45.7 . 1 377 89 96 GLY N N 109.76 . 1 378 90 97 ALA H H 7.73 . 1 379 90 97 ALA C C 176.3 . 1 380 90 97 ALA CA C 52.2 . 1 381 90 97 ALA CB C 18.2 . 1 382 90 97 ALA N N 121.87 . 1 383 91 98 ILE H H 8.71 . 1 384 91 98 ILE C C 175.5 . 1 385 91 98 ILE CA C 59.8 . 1 386 91 98 ILE CB C 41.3 . 1 387 91 98 ILE N N 119.43 . 1 388 92 99 CYS H H 8.85 . 1 389 92 99 CYS C C 171.9 . 1 390 92 99 CYS CA C 57.0 . 1 391 92 99 CYS CB C 26.0 . 1 392 92 99 CYS N N 127.95 . 1 393 93 100 LEU H H 7.48 . 1 394 93 100 LEU C C 176.0 . 1 395 93 100 LEU CA C 53.9 . 1 396 93 100 LEU CB C 44.2 . 1 397 93 100 LEU N N 126.03 . 1 398 94 101 ASP H H 9.29 . 1 399 94 101 ASP C C 179.8 . 1 400 94 101 ASP CA C 58.1 . 1 401 94 101 ASP CB C 42.5 . 1 402 94 101 ASP N N 130.61 . 1 403 95 102 ILE H H 8.51 . 1 404 95 102 ILE C C 173.2 . 1 405 95 102 ILE CA C 63.7 . 1 406 95 102 ILE CB C 37.2 . 1 407 95 102 ILE N N 117.32 . 1 408 96 103 LEU H H 7.30 . 1 409 96 103 LEU C C 176.5 . 1 410 96 103 LEU CA C 53.0 . 1 411 96 103 LEU CB C 40.1 . 1 412 96 103 LEU N N 113.34 . 1 413 97 104 LYS H H 7.92 . 1 414 97 104 LYS C C 175.7 . 1 415 97 104 LYS CA C 55.8 . 1 416 97 104 LYS CB C 31.5 . 1 417 97 104 LYS N N 123.11 . 1 418 98 105 ASP H H 8.59 . 1 419 98 105 ASP C C 176.5 . 1 420 98 105 ASP CA C 55.2 . 1 421 98 105 ASP CB C 39.9 . 1 422 98 105 ASP N N 119.69 . 1 423 99 106 GLN H H 7.73 . 1 424 99 106 GLN C C 174.3 . 1 425 99 106 GLN CA C 53.9 . 1 426 99 106 GLN CB C 27.0 . 1 427 99 106 GLN N N 115.35 . 1 428 100 107 TRP H H 7.21 . 1 429 100 107 TRP CA C 58.3 . 1 430 100 107 TRP CB C 29.6 . 1 431 100 107 TRP N N 121.66 . 1 432 101 108 ALA C C 177.3 . 1 433 101 108 ALA CA C 49.3 . 1 434 101 108 ALA CB C 21.2 . 1 435 102 109 ALA H H 8.01 . 1 436 102 109 ALA C C 176.3 . 1 437 102 109 ALA CA C 53.1 . 1 438 102 109 ALA CB C 17.4 . 1 439 102 109 ALA N N 120.39 . 1 440 103 110 ALA H H 7.05 . 1 441 103 110 ALA C C 178.4 . 1 442 103 110 ALA CA C 51.7 . 1 443 103 110 ALA CB C 18.0 . 1 444 103 110 ALA N N 115.84 . 1 445 104 111 MET H H 7.58 . 1 446 104 111 MET C C 172.5 . 1 447 104 111 MET CA C 56.7 . 1 448 104 111 MET CB C 31.0 . 1 449 104 111 MET N N 120.31 . 1 450 105 112 THR H H 7.45 . 1 451 105 112 THR CA C 62.5 . 1 452 105 112 THR CB C 72.5 . 1 453 105 112 THR N N 103.677 . 1 454 106 113 LEU C C 178.1 . 1 455 106 113 LEU CA C 57.5 . 1 456 106 113 LEU CB C 41.5 . 1 457 107 114 ARG H H 8.44 . 1 458 107 114 ARG C C 176.9 . 1 459 107 114 ARG CA C 59.9 . 1 460 107 114 ARG CB C 28.7 . 1 461 107 114 ARG N N 117.15 . 1 462 108 115 THR H H 7.88 . 1 463 108 115 THR C C 178.1 . 1 464 108 115 THR CA C 65.8 . 1 465 108 115 THR CB C 67.5 . 1 466 108 115 THR N N 113.83 . 1 467 109 116 VAL H H 8.50 . 1 468 109 116 VAL C C 177.1 . 1 469 109 116 VAL CA C 66.7 . 1 470 109 116 VAL CB C 30.7 . 1 471 109 116 VAL N N 124.41 . 1 472 110 117 LEU H H 8.25 . 1 473 110 117 LEU C C 178.4 . 1 474 110 117 LEU CA C 58.2 . 1 475 110 117 LEU CB C 40.2 . 1 476 110 117 LEU N N 119.48 . 1 477 111 118 LEU H H 8.41 . 1 478 111 118 LEU C C 177.9 . 1 479 111 118 LEU CA C 57.1 . 1 480 111 118 LEU CB C 39.9 . 1 481 111 118 LEU N N 117.69 . 1 482 112 119 SER H H 8.41 . 1 483 112 119 SER C C 174.6 . 1 484 112 119 SER CA C 61.8 . 1 485 112 119 SER CB C 63.7 . 1 486 112 119 SER N N 118.39 . 1 487 113 120 LEU H H 8.28 . 1 488 113 120 LEU C C 176.9 . 1 489 113 120 LEU CA C 54.4 . 1 490 113 120 LEU CB C 40.9 . 1 491 113 120 LEU N N 126.21 . 1 492 114 121 GLN H H 8.27 . 1 493 114 121 GLN C C 176.5 . 1 494 114 121 GLN CA C 55.6 . 1 495 114 121 GLN CB C 31.5 . 1 496 114 121 GLN N N 121.86 . 1 497 115 122 ALA H H 8.21 . 1 498 115 122 ALA C C 177.8 . 1 499 115 122 ALA CA C 52.7 . 1 500 115 122 ALA CB C 17.9 . 1 501 115 122 ALA N N 122.60 . 1 502 116 123 LEU H H 8.014 . 1 503 116 123 LEU CA C 53.7 . 1 504 116 123 LEU CB C 37.9 . 1 505 116 123 LEU N N 117.09 . 1 506 117 124 LEU C C 177.1 . 1 507 117 124 LEU CA C 57.4 . 1 508 117 124 LEU CB C 39.2 . 1 509 118 125 ALA H H 7.25 . 1 510 118 125 ALA C C 176.3 . 1 511 118 125 ALA CA C 51.8 . 1 512 118 125 ALA CB C 18.4 . 1 513 118 125 ALA N N 117.61 . 1 514 119 126 ALA H H 7.89 . 1 515 119 126 ALA C C 179.6 . 1 516 119 126 ALA CA C 50.9 . 1 517 119 126 ALA CB C 18.1 . 1 518 119 126 ALA N N 125.79 . 1 519 120 127 ALA H H 8.20 . 1 520 120 127 ALA C C 176.2 . 1 521 120 127 ALA CA C 51.3 . 1 522 120 127 ALA CB C 18.1 . 1 523 120 127 ALA N N 122.99 . 1 524 121 128 GLU H H 9.00 . 1 525 121 128 GLU CA C 51.5 . 1 526 121 128 GLU CB C 28.7 . 1 527 121 128 GLU N N 118.88 . 1 528 122 129 PRO C C 174.6 . 1 529 122 129 PRO CA C 63.5 . 1 530 122 129 PRO CB C 30.7 . 1 531 123 130 ASP H H 8.48 . 1 532 123 130 ASP C C 175.1 . 1 533 123 130 ASP CA C 54.4 . 1 534 123 130 ASP CB C 39.2 . 1 535 123 130 ASP N N 117.86 . 1 536 124 131 ASP H H 7.16 . 1 537 124 131 ASP CA C 51.1 . 1 538 124 131 ASP CB C 39.8 . 1 539 124 131 ASP N N 119.52 . 1 540 125 132 PRO C C 176.8 . 1 541 125 132 PRO CA C 62.3 . 1 542 125 132 PRO CB C 32.1 . 1 543 126 133 GLN H H 8.65 . 1 544 126 133 GLN C C 174.1 . 1 545 126 133 GLN CA C 54.3 . 1 546 126 133 GLN CB C 28.8 . 1 547 126 133 GLN N N 117.76 . 1 548 127 134 ASP H H 7.10 . 1 549 127 134 ASP C C 175.4 . 1 550 127 134 ASP CA C 52.0 . 1 551 127 134 ASP CB C 42.8 . 1 552 127 134 ASP N N 118.22 . 1 553 128 135 ALA H H 8.92 . 1 554 128 135 ALA C C 179.5 . 1 555 128 135 ALA CA C 54.5 . 1 556 128 135 ALA CB C 17.6 . 1 557 128 135 ALA N N 128.65 . 1 558 129 136 VAL H H 7.88 . 1 559 129 136 VAL C C 177.6 . 1 560 129 136 VAL CA C 65.3 . 1 561 129 136 VAL CB C 30.6 . 1 562 129 136 VAL N N 118.45 . 1 563 130 137 VAL H H 7.13 . 1 564 130 137 VAL CA C 64.84 . 1 565 130 137 VAL CB C 30.83 . 1 566 130 137 VAL N N 121.32 . 1 567 131 138 ALA C C 178.1 . 1 568 131 138 ALA CA C 54.8 . 1 569 131 138 ALA CB C 17.6 . 1 570 132 139 ASN H H 8.17 . 1 571 132 139 ASN C C 176.7 . 1 572 132 139 ASN CA C 55.7 . 1 573 132 139 ASN CB C 37.3 . 1 574 132 139 ASN N N 115.01 . 1 575 133 140 GLN H H 7.59 . 1 576 133 140 GLN C C 178.9 . 1 577 133 140 GLN CA C 59.1 . 1 578 133 140 GLN CB C 30.5 . 1 579 133 140 GLN N N 121.65 . 1 580 134 141 TYR H H 8.53 . 1 581 134 141 TYR C C 176.5 . 1 582 134 141 TYR CA C 60.9 . 1 583 134 141 TYR CB C 37.9 . 1 584 134 141 TYR N N 117.80 . 1 585 135 142 LYS H H 7.65 . 1 586 135 142 LYS C C 178.4 . 1 587 135 142 LYS CA C 58.3 . 1 588 135 142 LYS CB C 32.4 . 1 589 135 142 LYS N N 113.75 . 1 590 136 143 GLN H H 8.48 . 1 591 136 143 GLN C C 176.9 . 1 592 136 143 GLN CA C 56.7 . 1 593 136 143 GLN CB C 28.5 . 1 594 136 143 GLN N N 115.81 . 1 595 137 144 ASN H H 8.77 . 1 596 137 144 ASN CA C 50.8 . 1 597 137 144 ASN CB C 38.2 . 1 598 137 144 ASN N N 116.25 . 1 599 138 145 PRO C C 176.6 . 1 600 138 145 PRO CA C 64.7 . 1 601 138 145 PRO CB C 30.9 . 1 602 139 146 GLU H H 8.55 . 1 603 139 146 GLU C C 178.6 . 1 604 139 146 GLU CA C 58.7 . 1 605 139 146 GLU CB C 27.7 . 1 606 139 146 GLU N N 117.77 . 1 607 140 147 MET H H 7.53 . 1 608 140 147 MET C C 180.2 . 1 609 140 147 MET CA C 57.6 . 1 610 140 147 MET CB C 32.3 . 1 611 140 147 MET N N 121.01 . 1 612 141 148 PHE H H 9.06 . 1 613 141 148 PHE C C 176.2 . 1 614 141 148 PHE CA C 61.2 . 1 615 141 148 PHE CB C 37.6 . 1 616 141 148 PHE N N 123.71 . 1 617 142 149 LYS H H 8.39 . 1 618 142 149 LYS C C 178.6 . 1 619 142 149 LYS CA C 59.9 . 1 620 142 149 LYS CB C 31.0 . 1 621 142 149 LYS N N 120.68 . 1 622 143 150 GLN H H 7.89 . 1 623 143 150 GLN C C 179.2 . 1 624 143 150 GLN CA C 57.6 . 1 625 143 150 GLN CB C 26.9 . 1 626 143 150 GLN N N 115.60 . 1 627 144 151 THR H H 8.63 . 1 628 144 151 THR C C 174.9 . 1 629 144 151 THR CA C 67.6 . 1 630 144 151 THR CB C 68.5 . 1 631 144 151 THR N N 120.65 . 1 632 145 152 ALA H H 9 . 1 633 145 152 ALA C C 180.5 . 1 634 145 152 ALA CA C 55.1 . 1 635 145 152 ALA CB C 16.8 . 1 636 145 152 ALA N N 124.70 . 1 637 146 153 ARG H H 8.16 . 1 638 146 153 ARG C C 177.9 . 1 639 146 153 ARG CA C 58.2 . 1 640 146 153 ARG CB C 29.4 . 1 641 146 153 ARG N N 119.25 . 1 642 147 154 LEU H H 7.88 . 1 643 147 154 LEU C C 180.2 . 1 644 147 154 LEU CA C 57.1 . 1 645 147 154 LEU CB C 39.2 . 1 646 147 154 LEU N N 122.89 . 1 647 148 155 TRP H H 9.222 . 1 648 148 155 TRP C C 181.0 . 1 649 148 155 TRP CA C 62.0 . 1 650 148 155 TRP CB C 27.6 . 1 651 148 155 TRP N N 120.79 . 1 652 149 156 ALA H H 9.02 . 1 653 149 156 ALA C C 179.7 . 1 654 149 156 ALA CA C 55.0 . 1 655 149 156 ALA CB C 17.5 . 1 656 149 156 ALA N N 128.49 . 1 657 150 157 HIS H H 8.6203 . 1 658 150 157 HIS C C 176.2 . 1 659 150 157 HIS CA C 57.4 . 1 660 150 157 HIS CB C 28.0 . 1 661 150 157 HIS N N 120.79 . 1 662 151 158 VAL H H 8.72 . 1 663 151 158 VAL C C 177.7 . 1 664 151 158 VAL CA C 65.1 . 1 665 151 158 VAL CB C 31.4 . 1 666 151 158 VAL N N 116.87 . 1 667 152 159 TYR H H 8.16 . 1 668 152 159 TYR C C 176.0 . 1 669 152 159 TYR CA C 58.4 . 1 670 152 159 TYR CB C 38.6 . 1 671 152 159 TYR N N 113.77 . 1 672 153 160 ALA H H 7.29 . 1 673 153 160 ALA C C 177.5 . 1 674 153 160 ALA CA C 50.4 . 1 675 153 160 ALA CB C 21.3 . 1 676 153 160 ALA N N 120.72 . 1 677 154 161 GLY H H 7.53 . 1 678 154 161 GLY C C 174.3 . 1 679 154 161 GLY CA C 45.5 . 1 680 154 161 GLY N N 106.96 . 1 681 155 162 ALA H H 8.03 . 1 682 155 162 ALA CA C 50.6 . 1 683 155 162 ALA CB C 17.1 . 1 684 155 162 ALA N N 124.19 . 1 685 156 163 PRO C C 175.9 . 1 686 156 163 PRO CA C 64.0 . 1 687 156 163 PRO CB C 31.4 . 1 688 157 164 VAL H H 7.73 . 1 689 157 164 VAL C C 177.9 . 1 690 157 164 VAL CA C 61.3 . 1 691 157 164 VAL CB C 32.6 . 1 692 157 164 VAL N N 117.88 . 1 693 158 165 SER H H 7.47 . 1 694 158 165 SER C C 173.5 . 1 695 158 165 SER CA C 55.9 . 1 696 158 165 SER CB C 64.2 . 1 697 158 165 SER N N 117.43 . 1 698 159 166 SER H H 8.14 . 1 699 159 166 SER CA C 54.6 . 1 700 159 166 SER CB C 62.5 . 1 701 159 166 SER N N 114.70 . 1 702 160 167 PRO C C 178.2 . 1 703 160 167 PRO CA C 64.0 . 1 704 160 167 PRO CB C 34.1 . 1 705 161 168 GLU H H 8.309 . 1 706 161 168 GLU C C 178.8 . 1 707 161 168 GLU CA C 58.5 . 1 708 161 168 GLU CB C 28.1 . 1 709 161 168 GLU N N 118.64 . 1 710 162 169 TYR H H 7.43 . 1 711 162 169 TYR C C 177.9 . 1 712 162 169 TYR CA C 57.3 . 1 713 162 169 TYR CB C 35.1 . 1 714 162 169 TYR N N 119.48 . 1 715 163 170 THR H H 7.90 . 1 716 163 170 THR C C 176.1 . 1 717 163 170 THR CA C 66.3 . 1 718 163 170 THR CB C 67.2 . 1 719 163 170 THR N N 114.73 . 1 720 164 171 LYS H H 7.841 . 1 721 164 171 LYS C C 178.4 . 1 722 164 171 LYS CA C 56.6 . 1 723 164 171 LYS CB C 30.8 . 1 724 164 171 LYS N N 121.36 . 1 725 165 172 LYS H H 7.24 . 1 726 165 172 LYS C C 178.2 . 1 727 165 172 LYS CA C 59.7 . 1 728 165 172 LYS CB C 32.6 . 1 729 165 172 LYS N N 118.05 . 1 730 166 173 ILE H H 7.78 . 1 731 166 173 ILE C C 178.3 . 1 732 166 173 ILE CA C 63.6 . 1 733 166 173 ILE CB C 38.0 . 1 734 166 173 ILE N N 118.27 . 1 735 167 174 GLU H H 8.47 . 1 736 167 174 GLU C C 179.5 . 1 737 167 174 GLU CA C 58.7 . 1 738 167 174 GLU CB C 28.1 . 1 739 167 174 GLU N N 119.20 . 1 740 168 175 ASN H H 8.31 . 1 741 168 175 ASN C C 177.5 . 1 742 168 175 ASN CA C 55.4 . 1 743 168 175 ASN CB C 37.4 . 1 744 168 175 ASN N N 118.15 . 1 745 169 176 LEU H H 7.48 . 1 746 169 176 LEU C C 180.7 . 1 747 169 176 LEU CA C 57.3 . 1 748 169 176 LEU CB C 41.6 . 1 749 169 176 LEU N N 119.76 . 1 750 170 177 CYS H H 8.90 . 1 751 170 177 CYS C C 178.3 . 1 752 170 177 CYS CA C 63.1 . 1 753 170 177 CYS CB C 26.2 . 1 754 170 177 CYS N N 120.20 . 1 755 171 178 ALA H H 8.01 . 1 756 171 178 ALA C C 178.3 . 1 757 171 178 ALA CA C 53.7 . 1 758 171 178 ALA CB C 16.8 . 1 759 171 178 ALA N N 122.48 . 1 760 172 179 MET H H 7.26 . 1 761 172 179 MET C C 175.7 . 1 762 172 179 MET CA C 55.4 . 1 763 172 179 MET CB C 32.0 . 1 764 172 179 MET N N 115.26 . 1 765 173 180 GLY H H 7.79 . 1 766 173 180 GLY C C 173.5 . 1 767 173 180 GLY CA C 43.9 . 1 768 173 180 GLY N N 105.29 . 1 769 174 181 PHE H H 6.55 . 1 770 174 181 PHE C C 174.3 . 1 771 174 181 PHE CA C 56.4 . 1 772 174 181 PHE CB C 40.4 . 1 773 174 181 PHE N N 117.97 . 1 774 175 182 ASP H H 8.76 . 1 775 175 182 ASP C C 175.8 . 1 776 175 182 ASP CA C 53.9 . 1 777 175 182 ASP CB C 42.7 . 1 778 175 182 ASP N N 121.91 . 1 779 176 183 ARG H H 8.67 . 1 780 176 183 ARG C C 177.2 . 1 781 176 183 ARG CA C 60.0 . 1 782 176 183 ARG CB C 29.5 . 1 783 176 183 ARG N N 125.73 . 1 784 177 184 ASN H H 8.12 . 1 785 177 184 ASN C C 176.3 . 1 786 177 184 ASN CA C 56.0 . 1 787 177 184 ASN CB C 36.9 . 1 788 177 184 ASN N N 115.26 . 1 789 178 185 ALA H H 8.04 . 1 790 178 185 ALA C C 180.2 . 1 791 178 185 ALA CA C 54.4 . 1 792 178 185 ALA CB C 16.8 . 1 793 178 185 ALA N N 123.82 . 1 794 179 186 VAL H H 8.60 . 1 795 179 186 VAL C C 176.7 . 1 796 179 186 VAL CA C 66.1 . 1 797 179 186 VAL CB C 30.8 . 1 798 179 186 VAL N N 120.26 . 1 799 180 187 ILE H H 8.16 . 1 800 180 187 ILE C C 177.6 . 1 801 180 187 ILE CA C 66.2 . 1 802 180 187 ILE CB C 36.7 . 1 803 180 187 ILE N N 120.26 . 1 804 181 188 VAL H H 8.16 . 1 805 181 188 VAL C C 177.9 . 1 806 181 188 VAL CA C 67.0 . 1 807 181 188 VAL CB C 30.8 . 1 808 181 188 VAL N N 122.71 . 1 809 182 189 ALA H H 8.43 . 1 810 182 189 ALA C C 178.3 . 1 811 182 189 ALA CA C 55.0 . 1 812 182 189 ALA CB C 17.7 . 1 813 182 189 ALA N N 124.85 . 1 814 183 190 LEU H H 8.27 . 1 815 183 190 LEU C C 178.7 . 1 816 183 190 LEU CA C 57.0 . 1 817 183 190 LEU CB C 39.4 . 1 818 183 190 LEU N N 115.37 . 1 819 184 191 SER C C 174.60 . 1 820 184 191 SER CA C 61.80 . 1 821 184 191 SER CB C 63.70 . 1 822 185 192 SER H H 7.76 . 1 823 185 192 SER C C 174.6 . 1 824 185 192 SER CA C 60.0 . 1 825 185 192 SER CB C 62.9 . 1 826 185 192 SER N N 112.49 . 1 827 186 193 LYS H H 7.19 . 1 828 186 193 LYS C C 175.9 . 1 829 186 193 LYS CA C 52.3 . 1 830 186 193 LYS CB C 28.4 . 1 831 186 193 LYS N N 120.67 . 1 832 187 194 SER H H 7.90 . 1 833 187 194 SER C C 172.8 . 1 834 187 194 SER CA C 59.5 . 1 835 187 194 SER CB C 60.6 . 1 836 187 194 SER N N 112.47 . 1 837 188 195 TRP H H 8.69 . 1 838 188 195 TRP C C 172.3 . 1 839 188 195 TRP CA C 58.7 . 1 840 188 195 TRP CB C 24.1 . 1 841 188 195 TRP N N 110.48 . 1 842 189 196 ASP H H 7.25 . 1 843 189 196 ASP C C 174.9 . 1 844 189 196 ASP CA C 52.7 . 1 845 189 196 ASP CB C 41.4 . 1 846 189 196 ASP N N 119.81 . 1 847 190 197 VAL H H 8.75 . 1 848 190 197 VAL C C 178.4 . 1 849 190 197 VAL CA C 66.1 . 1 850 190 197 VAL CB C 30.8 . 1 851 190 197 VAL N N 127.29 . 1 852 191 198 GLU H H 8.75 . 1 853 191 198 GLU C C 179.2 . 1 854 191 198 GLU CA C 59.8 . 1 855 191 198 GLU CB C 28.2 . 1 856 191 198 GLU N N 122.79 . 1 857 192 199 THR H H 8.13 . 1 858 192 199 THR C C 178.1 . 1 859 192 199 THR CA C 64.8 . 1 860 192 199 THR CB C 67.8 . 1 861 192 199 THR N N 114.05 . 1 862 193 200 ALA H H 8.47 . 1 863 193 200 ALA C C 177.9 . 1 864 193 200 ALA CA C 54.8 . 1 865 193 200 ALA CB C 17.0 . 1 866 193 200 ALA N N 124.95 . 1 867 194 201 THR H H 8.09 . 1 868 194 201 THR C C 174.9 . 1 869 194 201 THR CA C 67.2 . 1 870 194 201 THR CB C 68.0 . 1 871 194 201 THR N N 114.33 . 1 872 195 202 GLU H H 7.31 . 1 873 195 202 GLU C C 179.1 . 1 874 195 202 GLU CA C 58.6 . 1 875 195 202 GLU CB C 28.4 . 1 876 195 202 GLU N N 119.42 . 1 877 196 203 LEU H H 7.31 . 1 878 196 203 LEU C C 179.5 . 1 879 196 203 LEU CA C 57.1 . 1 880 196 203 LEU CB C 40.8 . 1 881 196 203 LEU N N 119.90 . 1 882 197 204 LEU H H 7.84 . 1 883 197 204 LEU C C 178.6 . 1 884 197 204 LEU CA C 56.6 . 1 885 197 204 LEU CB C 39.6 . 1 886 197 204 LEU N N 121.36 . 1 887 198 205 LEU H H 7.76 . 1 888 198 205 LEU C C 177.3 . 1 889 198 205 LEU CA C 55.2 . 1 890 198 205 LEU CB C 41.6 . 1 891 198 205 LEU N N 117.84 . 1 892 199 206 SER H H 7.59 . 1 893 199 206 SER C C 173.0 . 1 894 199 206 SER CA C 58.4 . 1 895 199 206 SER CB C 63.3 . 1 896 199 206 SER N N 115.00 . 1 897 200 207 ASN H H 7.72 . 1 898 200 207 ASN CA C 54.3 . 1 899 200 207 ASN CB C 39.9 . 1 900 200 207 ASN N N 125.77 . 1 stop_ save_