data_15787 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N chemical shift assignments for HINT1 protein ; _BMRB_accession_number 15787 _BMRB_flat_file_name bmr15787.str _Entry_type original _Submission_date 2008-05-29 _Accession_date 2008-05-29 _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 Shapiro Michael J. . 2 Bai Guoyun . . 3 Feng Bo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 116 "13C chemical shifts" 347 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-14 update BMRB 'added PubMed ID' 2009-05-22 update BMRB 'complete entry citation' 2009-01-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone assignment of HINT1 protein, a mouse histidine triad nucleotide binding protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bai Guoyun . . 2 Feng Bo . . 3 Wang 'Jia Bei' . . 4 Varney Kristen M. . 5 Shapiro Michael . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 3 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 57 _Page_last 59 _Year 2009 _Details . loop_ _Keyword assignment HINT NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HINT1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HINT1 $HINT1 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_HINT1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HINT1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; MADEIAKAQVAQPGGDTIFG KIIRKEIPAKIIFEDDRCLA FHDISPQAPTHFLVIPKKHI SQISVADDDDESLLGHLMIV GKKCAADLGLKRGYRMVVNE GADGGQSVYHIHLHVLGGRQ MNWPPG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 GLU 5 ILE 6 ALA 7 LYS 8 ALA 9 GLN 10 VAL 11 ALA 12 GLN 13 PRO 14 GLY 15 GLY 16 ASP 17 THR 18 ILE 19 PHE 20 GLY 21 LYS 22 ILE 23 ILE 24 ARG 25 LYS 26 GLU 27 ILE 28 PRO 29 ALA 30 LYS 31 ILE 32 ILE 33 PHE 34 GLU 35 ASP 36 ASP 37 ARG 38 CYS 39 LEU 40 ALA 41 PHE 42 HIS 43 ASP 44 ILE 45 SER 46 PRO 47 GLN 48 ALA 49 PRO 50 THR 51 HIS 52 PHE 53 LEU 54 VAL 55 ILE 56 PRO 57 LYS 58 LYS 59 HIS 60 ILE 61 SER 62 GLN 63 ILE 64 SER 65 VAL 66 ALA 67 ASP 68 ASP 69 ASP 70 ASP 71 GLU 72 SER 73 LEU 74 LEU 75 GLY 76 HIS 77 LEU 78 MET 79 ILE 80 VAL 81 GLY 82 LYS 83 LYS 84 CYS 85 ALA 86 ALA 87 ASP 88 LEU 89 GLY 90 LEU 91 LYS 92 ARG 93 GLY 94 TYR 95 ARG 96 MET 97 VAL 98 VAL 99 ASN 100 GLU 101 GLY 102 ALA 103 ASP 104 GLY 105 GLY 106 GLN 107 SER 108 VAL 109 TYR 110 HIS 111 ILE 112 HIS 113 LEU 114 HIS 115 VAL 116 LEU 117 GLY 118 GLY 119 ARG 120 GLN 121 MET 122 ASN 123 TRP 124 PRO 125 PRO 126 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 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 DBJ BAB22484 "unnamed protein product [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 DBJ BAB28235 "unnamed protein product [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 GB AAC71076 "protein kinase C inhibitor [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 GB AAH70415 "Histidine triad nucleotide binding protein 1 [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 GB AAH80296 "Histidine triad nucleotide binding protein 1 [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 GB AAI68732 "Histidine triad nucleotide binding protein 1 [Rattus norvegicus]" 100.00 126 100.00 100.00 5.45e-86 GB EDL33521 "mCG1442, isoform CRA_b [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 REF NP_001103077 "histidine triad nucleotide-binding protein 1 [Rattus norvegicus]" 100.00 126 100.00 100.00 5.45e-86 REF NP_032274 "histidine triad nucleotide-binding protein 1 [Mus musculus]" 100.00 126 100.00 100.00 5.45e-86 REF XP_005350115 "PREDICTED: histidine triad nucleotide-binding protein 1 [Microtus ochrogaster]" 100.00 126 97.62 99.21 2.33e-84 SP P62959 "RecName: Full=Histidine triad nucleotide-binding protein 1; AltName: Full=17 kDa inhibitor of protein kinase C; AltName: Full=A" 100.00 126 100.00 100.00 5.45e-86 SP P70349 "RecName: Full=Histidine triad nucleotide-binding protein 1; AltName: Full=Adenosine 5'-monophosphoramidase; AltName: Full=Prote" 100.00 126 100.00 100.00 5.45e-86 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HINT1 'E. coli' 562 Eubacteria . Escherichia coli 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 $HINT1 'recombinant technology' . Escherichia coli . pET-28a(+) 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 $HINT1 0.2 mM '[U-98% 13C; U-98% 15N]' D2O 10 % '[U-99% 2H]' H2O 90 % 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _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_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 0.1 . M pH 7.3 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 CBCA(CO)NH' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 HINT1 _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 1 MET H H 8.17 . 1 2 1 1 MET C C 175.2 . 1 3 1 1 MET CA C 54.7 . 1 4 1 1 MET CB C 32.5 . 1 5 1 1 MET N N 123.3 . 1 6 2 2 ALA H H 8.17 . 1 7 2 2 ALA C C 175.6 . 1 8 2 2 ALA CA C 52.8 . 1 9 2 2 ALA CB C 18.8 . 1 10 2 2 ALA N N 125.7 . 1 11 3 3 ASP H H 8.29 . 1 12 3 3 ASP C C 175.6 . 1 13 3 3 ASP CA C 54.6 . 1 14 3 3 ASP CB C 40.9 . 1 15 3 3 ASP N N 120.0 . 1 16 4 4 GLU H H 8.22 . 1 17 4 4 GLU C C 175.7 . 1 18 4 4 GLU CA C 57.1 . 1 19 4 4 GLU CB C 29.6 . 1 20 4 4 GLU N N 121.3 . 1 21 5 5 ILE H H 8.00 . 1 22 5 5 ILE C C 176.6 . 1 23 5 5 ILE CA C 61.8 . 1 24 5 5 ILE CB C 37.8 . 1 25 5 5 ILE N N 122.1 . 1 26 6 6 ALA H H 8.13 . 1 27 6 6 ALA C C 174.9 . 1 28 6 6 ALA CA C 52.8 . 1 29 6 6 ALA CB C 18.6 . 1 30 6 6 ALA N N 126.6 . 1 31 7 7 LYS H H 8.02 . 1 32 7 7 LYS C C 174.8 . 1 33 7 7 LYS CA C 56.4 . 1 34 7 7 LYS CB C 32.7 . 1 35 7 7 LYS N N 120.2 . 1 36 8 8 ALA H H 8.00 . 1 37 8 8 ALA C C 176.8 . 1 38 8 8 ALA CA C 52.3 . 1 39 8 8 ALA CB C 18.8 . 1 40 8 8 ALA N N 124.5 . 1 41 9 9 GLN H H 8.16 . 1 42 9 9 GLN C C 175.6 . 1 43 9 9 GLN CA C 55.5 . 1 44 9 9 GLN CB C 29.1 . 1 45 9 9 GLN N N 119.9 . 1 46 10 10 VAL H H 7.98 . 1 47 10 10 VAL C C 175.6 . 1 48 10 10 VAL CA C 61.8 . 1 49 10 10 VAL CB C 32.5 . 1 50 10 10 VAL N N 121.4 . 1 51 11 11 ALA H H 8.31 . 1 52 11 11 ALA C C 176.9 . 1 53 11 11 ALA CA C 51.9 . 1 54 11 11 ALA CB C 19.0 . 1 55 11 11 ALA N N 128.5 . 1 56 12 12 GLN H H 8.48 . 1 57 12 12 GLN CA C 53.1 . 1 58 12 12 GLN CB C 29.1 . 1 59 12 12 GLN N N 121.9 . 1 60 13 13 PRO C C 176.9 . 1 61 13 13 PRO CA C 63.5 . 1 62 13 13 PRO CB C 31.2 . 1 63 14 14 GLY H H 8.83 . 1 64 14 14 GLY C C 173.9 . 1 65 14 14 GLY CA C 45.2 . 1 66 14 14 GLY N N 112.0 . 1 67 15 15 GLY H H 8.15 . 1 68 15 15 GLY C C 173.6 . 1 69 15 15 GLY CA C 44.8 . 1 70 15 15 GLY N N 107.4 . 1 71 16 16 ASP H H 8.10 . 1 72 16 16 ASP C C 176.4 . 1 73 16 16 ASP CA C 53.4 . 1 74 16 16 ASP CB C 40.9 . 1 75 16 16 ASP N N 118.9 . 1 76 17 17 THR H H 7.62 . 1 77 17 17 THR CA C 60.8 . 1 78 17 17 THR CB C 73.0 . 1 79 17 17 THR N N 110.2 . 1 80 18 18 ILE C C 176.3 . 1 81 18 18 ILE CA C 63.0 . 1 82 18 18 ILE CB C 38.1 . 1 83 19 19 PHE H H 7.29 . 1 84 19 19 PHE C C 177.8 . 1 85 19 19 PHE CA C 56.1 . 1 86 19 19 PHE CB C 34.1 . 1 87 19 19 PHE N N 119.9 . 1 88 20 20 GLY H H 7.73 . 1 89 20 20 GLY C C 175.0 . 1 90 20 20 GLY CA C 47.2 . 1 91 20 20 GLY N N 111.2 . 1 92 21 21 LYS H H 7.13 . 1 93 21 21 LYS C C 178.5 . 1 94 21 21 LYS CA C 59.2 . 1 95 21 21 LYS CB C 32.2 . 1 96 21 21 LYS N N 119.8 . 1 97 22 22 ILE H H 7.43 . 1 98 22 22 ILE C C 179.6 . 1 99 22 22 ILE CA C 65.0 . 1 100 22 22 ILE CB C 37.6 . 1 101 22 22 ILE N N 121.6 . 1 102 23 23 ILE H H 8.35 . 1 103 23 23 ILE C C 176.9 . 1 104 23 23 ILE CA C 65.2 . 1 105 23 23 ILE CB C 37.8 . 1 106 23 23 ILE N N 123.8 . 1 107 24 24 ARG H H 7.74 . 1 108 24 24 ARG C C 174.5 . 1 109 24 24 ARG CA C 56.6 . 1 110 24 24 ARG CB C 30.9 . 1 111 24 24 ARG N N 115.8 . 1 112 25 25 LYS H H 7.83 . 1 113 25 25 LYS C C 176.0 . 1 114 25 25 LYS CA C 56.1 . 1 115 25 25 LYS CB C 27.5 . 1 116 25 25 LYS N N 115.2 . 1 117 26 26 GLU H H 8.58 . 1 118 26 26 GLU C C 176.7 . 1 119 26 26 GLU CA C 56.8 . 1 120 26 26 GLU CB C 30.5 . 1 121 26 26 GLU N N 118.3 . 1 122 27 27 ILE H H 6.89 . 1 123 27 27 ILE CA C 56.7 . 1 124 27 27 ILE CB C 39.9 . 1 125 27 27 ILE N N 115.2 . 1 126 28 28 PRO C C 174.8 . 1 127 28 28 PRO CA C 62.28 . 1 128 28 28 PRO CB C 32.0 . 1 129 29 29 ALA H H 7.72 . 1 130 29 29 ALA C C 175.4 . 1 131 29 29 ALA CA C 50.7 . 1 132 29 29 ALA CB C 22.3 . 1 133 29 29 ALA N N 121.5 . 1 134 30 30 LYS H H 9.11 . 1 135 30 30 LYS C C 176.2 . 1 136 30 30 LYS CA C 55.0 . 1 137 30 30 LYS CB C 31.3 . 1 138 30 30 LYS N N 123.7 . 1 139 31 31 ILE H H 8.02 . 1 140 31 31 ILE C C 171.3 . 1 141 31 31 ILE CA C 61.9 . 1 142 31 31 ILE CB C 38.2 . 1 143 31 31 ILE N N 126.2 . 1 144 32 32 ILE H H 9.03 . 1 145 32 32 ILE C C 174.6 . 1 146 32 32 ILE CA C 61.5 . 1 147 32 32 ILE CB C 40.3 . 1 148 32 32 ILE N N 127.0 . 1 149 33 33 PHE H H 7.52 . 1 150 33 33 PHE C C 171.4 . 1 151 33 33 PHE CA C 57.6 . 1 152 33 33 PHE CB C 43.2 . 1 153 33 33 PHE N N 121.0 . 1 154 34 34 GLU H H 7.47 . 1 155 34 34 GLU C C 172.9 . 1 156 34 34 GLU CA C 55.5 . 1 157 34 34 GLU CB C 32.5 . 1 158 34 34 GLU N N 128.4 . 1 159 35 35 ASP H H 8.73 . 1 160 35 35 ASP C C 175.6 . 1 161 35 35 ASP CA C 52.4 . 1 162 35 35 ASP CB C 40.85 . 1 163 35 35 ASP N N 126.1 . 1 164 36 36 ASP H H 8.18 . 1 165 36 36 ASP C C 176.2 . 1 166 36 36 ASP CA C 55.7 . 1 167 36 36 ASP CB C 39.9 . 1 168 36 36 ASP N N 121.5 . 1 169 37 37 ARG H H 8.85 . 1 170 37 37 ARG C C 177.1 . 1 171 37 37 ARG CA C 56.4 . 1 172 37 37 ARG CB C 34.4 . 1 173 37 37 ARG N N 117.4 . 1 174 38 38 CYS H H 9.02 . 1 175 38 38 CYS C C 169.1 . 1 176 38 38 CYS CA C 57.3 . 1 177 38 38 CYS CB C 31.7 . 1 178 38 38 CYS N N 121.0 . 1 179 39 39 LEU H H 8.79 . 1 180 39 39 LEU C C 173.1 . 1 181 39 39 LEU CA C 54.5 . 1 182 39 39 LEU CB C 47.1 . 1 183 39 39 LEU N N 118.7 . 1 184 40 40 ALA H H 9.23 . 1 185 40 40 ALA C C 176.6 . 1 186 40 40 ALA CA C 49.3 . 1 187 40 40 ALA CB C 24.0 . 1 188 40 40 ALA N N 125.1 . 1 189 41 41 PHE H H 8.72 . 1 190 41 41 PHE C C 175.3 . 1 191 41 41 PHE CA C 55.0 . 1 192 41 41 PHE CB C 41.4 . 1 193 41 41 PHE N N 119.6 . 1 194 42 42 HIS H H 8.10 . 1 195 42 42 HIS C C 175.1 . 1 196 42 42 HIS CA C 58.2 . 1 197 42 42 HIS CB C 32.0 . 1 198 42 42 HIS N N 120.5 . 1 199 43 43 ASP H H 8.59 . 1 200 43 43 ASP C C 176.0 . 1 201 43 43 ASP CA C 55.4 . 1 202 43 43 ASP CB C 42.6 . 1 203 43 43 ASP N N 123.8 . 1 204 44 44 ILE H H 8.15 . 1 205 44 44 ILE C C 175.8 . 1 206 44 44 ILE CA C 62.5 . 1 207 44 44 ILE CB C 38.6 . 1 208 44 44 ILE N N 122.4 . 1 209 45 45 SER H H 9.43 . 1 210 45 45 SER CA C 54.0 . 1 211 45 45 SER CB C 62.2 . 1 212 45 45 SER N N 121.2 . 1 213 46 46 PRO C C 175.3 . 1 214 46 46 PRO CA C 62.0 . 1 215 46 46 PRO CB C 32.3 . 1 216 47 47 GLN H H 8.35 . 1 217 47 47 GLN C C 175.2 . 1 218 47 47 GLN CA C 61.8 . 1 219 47 47 GLN CB C 32.7 . 1 220 47 47 GLN N N 125.8 . 1 221 48 48 ALA H H 8.32 . 1 222 48 48 ALA CA C 51.9 . 1 223 48 48 ALA CB C 19.0 . 1 224 48 48 ALA N N 128.7 . 1 225 49 49 PRO C C 177.0 . 1 226 49 49 PRO CA C 65.5 . 1 227 49 49 PRO CB C 32.1 . 1 228 50 50 THR H H 7.9 . 1 229 50 50 THR C C 172.0 . 1 230 50 50 THR CA C 62.2 . 1 231 50 50 THR CB C 69.6 . 1 232 50 50 THR N N 111.1 . 1 233 51 51 HIS H H 10.02 . 1 234 51 51 HIS C C 173.0 . 1 235 51 51 HIS CA C 52.8 . 1 236 51 51 HIS CB C 33.6 . 1 237 51 51 HIS N N 129.1 . 1 238 52 52 PHE H H 9.23 . 1 239 52 52 PHE C C 170.0 . 1 240 52 52 PHE CA C 54.2 . 1 241 52 52 PHE CB C 42.3 . 1 242 52 52 PHE N N 125.1 . 1 243 53 53 LEU H H 8.88 . 1 244 53 53 LEU C C 176.2 . 1 245 53 53 LEU CA C 52.3 . 1 246 53 53 LEU CB C 45.3 . 1 247 53 53 LEU N N 120.4 . 1 248 54 54 VAL H H 8.87 . 1 249 54 54 VAL C C 175.8 . 1 250 54 54 VAL CA C 60.8 . 1 251 54 54 VAL CB C 33.2 . 1 252 54 54 VAL N N 119.4 . 1 253 55 55 ILE H H 9.21 . 1 254 55 55 ILE CA C 56.2 . 1 255 55 55 ILE CB C 38.8 . 1 256 55 55 ILE N N 120.1 . 1 257 56 56 PRO C C 177.3 . 1 258 56 56 PRO CA C 61.0 . 1 259 57 57 LYS H H 7.93 . 1 260 57 57 LYS C C 175.7 . 1 261 57 57 LYS CA C 58.9 . 1 262 57 57 LYS CB C 32.0 . 1 263 57 57 LYS N N 121.9 . 1 264 58 58 LYS H H 8.15 . 1 265 58 58 LYS C C 174.4 . 1 266 58 58 LYS CA C 55.6 . 1 267 58 58 LYS CB C 33.5 . 1 268 58 58 LYS N N 121.5 . 1 269 59 59 HIS H H 8.60 . 1 270 59 59 HIS C C 173.7 . 1 271 59 59 HIS CA C 56.3 . 1 272 59 59 HIS CB C 29.8 . 1 273 59 59 HIS N N 124.2 . 1 274 60 60 ILE H H 6.23 . 1 275 60 60 ILE C C 176.6 . 1 276 60 60 ILE CA C 60.0 . 1 277 60 60 ILE CB C 40.7 . 1 278 60 60 ILE N N 130.8 . 1 279 61 61 SER H H 9.03 . 1 280 61 61 SER C C 172.9 . 1 281 61 61 SER CA C 60.9 . 1 282 61 61 SER CB C 62.8 . 1 283 61 61 SER N N 124.8 . 1 284 62 62 GLN H H 6.75 . 1 285 62 62 GLN C C 174.7 . 1 286 62 62 GLN CA C 54.2 . 1 287 62 62 GLN CB C 32.1 . 1 288 62 62 GLN N N 113.8 . 1 289 63 63 ILE H H 9.37 . 1 290 63 63 ILE C C 176.3 . 1 291 63 63 ILE CA C 62.8 . 1 292 63 63 ILE CB C 37.5 . 1 293 63 63 ILE N N 126.6 . 1 294 64 64 SER H H 8.50 . 1 295 64 64 SER C C 176.0 . 1 296 64 64 SER CA C 60.5 . 1 297 64 64 SER CB C 61.8 . 1 298 64 64 SER N N 115.3 . 1 299 65 65 VAL H H 7.22 . 1 300 65 65 VAL C C 175.8 . 1 301 65 65 VAL CA C 59.9 . 1 302 65 65 VAL CB C 30.9 . 1 303 65 65 VAL N N 114.4 . 1 304 66 66 ALA H H 7.56 . 1 305 66 66 ALA C C 175.5 . 1 306 66 66 ALA CA C 52.3 . 1 307 66 66 ALA CB C 18.6 . 1 308 66 66 ALA N N 127.3 . 1 309 67 67 ASP H H 9.38 . 1 310 67 67 ASP C C 176.6 . 1 311 67 67 ASP CA C 52.7 . 1 312 67 67 ASP CB C 43.4 . 1 313 67 67 ASP N N 123.9 . 1 314 68 68 ASP H H 8.65 . 1 315 68 68 ASP C C 178.3 . 1 316 68 68 ASP CA C 57.5 . 1 317 68 68 ASP CB C 39.5 . 1 318 68 68 ASP N N 122.5 . 1 319 69 69 ASP H H 8.68 . 1 320 69 69 ASP C C 176.8 . 1 321 69 69 ASP CA C 55.4 . 1 322 69 69 ASP CB C 40.0 . 1 323 69 69 ASP N N 117.6 . 1 324 70 70 ASP H H 8.19 . 1 325 70 70 ASP C C 175.5 . 1 326 70 70 ASP CA C 54.7 . 1 327 70 70 ASP CB C 40.7 . 1 328 70 70 ASP N N 119.1 . 1 329 71 71 GLU H H 7.60 . 1 330 71 71 GLU C C 177.3 . 1 331 71 71 GLU CA C 61.3 . 1 332 71 71 GLU CB C 30.1 . 1 333 71 71 GLU N N 121.3 . 1 334 72 72 SER H H 8.82 . 1 335 72 72 SER C C 175.1 . 1 336 72 72 SER CA C 62.1 . 1 337 72 72 SER CB C 61.6 . 1 338 72 72 SER N N 115.0 . 1 339 73 73 LEU H H 7.64 . 1 340 73 73 LEU C C 177.7 . 1 341 73 73 LEU CA C 57.5 . 1 342 73 73 LEU CB C 41.1 . 1 343 73 73 LEU N N 124.7 . 1 344 74 74 LEU H H 8.24 . 1 345 74 74 LEU C C 179.0 . 1 346 74 74 LEU CA C 57.5 . 1 347 74 74 LEU CB C 40.10 . 1 348 74 74 LEU N N 118.0 . 1 349 75 75 GLY H H 8.3 . 1 350 75 75 GLY C C 176.1 . 1 351 75 75 GLY CA C 47.3 . 1 352 75 75 GLY N N 105.4 . 1 353 76 76 HIS H H 8.74 . 1 354 76 76 HIS C C 176.0 . 1 355 76 76 HIS CA C 58.6 . 1 356 76 76 HIS CB C 28.0 . 1 357 76 76 HIS N N 122.7 . 1 358 77 77 LEU H H 7.97 . 1 359 77 77 LEU C C 178.3 . 1 360 77 77 LEU CA C 57.3 . 1 361 77 77 LEU CB C 40.1 . 1 362 77 77 LEU N N 115.9 . 1 363 78 78 MET H H 7.03 . 1 364 78 78 MET C C 177.3 . 1 365 78 78 MET CA C 58.8 . 1 366 78 78 MET CB C 33.5 . 1 367 78 78 MET N N 115.8 . 1 368 79 79 ILE H H 8.06 . 1 369 79 79 ILE C C 177.7 . 1 370 79 79 ILE CA C 60.9 . 1 371 79 79 ILE CB C 35.3 . 1 372 79 79 ILE N N 121.5 . 1 373 80 80 VAL H H 8.62 . 1 374 80 80 VAL C C 178.5 . 1 375 80 80 VAL CA C 66.4 . 1 376 80 80 VAL CB C 30.6 . 1 377 80 80 VAL N N 122.5 . 1 378 81 81 GLY H H 8.45 . 1 379 81 81 GLY C C 173.3 . 1 380 81 81 GLY CA C 48.0 . 1 381 81 81 GLY N N 108.8 . 1 382 82 82 LYS H H 8.17 . 1 383 82 82 LYS C C 179.0 . 1 384 82 82 LYS CA C 57.8 . 1 385 82 82 LYS CB C 31.3 . 1 386 82 82 LYS N N 123.3 . 1 387 83 83 LYS H H 8.38 . 1 388 83 83 LYS C C 178.9 . 1 389 83 83 LYS CA C 59.5 . 1 390 83 83 LYS CB C 31.9 . 1 391 83 83 LYS N N 125.9 . 1 392 84 84 CYS H H 8.70 . 1 393 84 84 CYS C C 177.3 . 1 394 84 84 CYS CA C 63.0 . 1 395 84 84 CYS CB C 27.4 . 1 396 84 84 CYS N N 118.3 . 1 397 85 85 ALA H H 8.18 . 1 398 85 85 ALA C C 178.1 . 1 399 85 85 ALA CA C 55.0 . 1 400 85 85 ALA CB C 17.9 . 1 401 85 85 ALA N N 121.6 . 1 402 86 86 ALA H H 7.36 . 1 403 86 86 ALA C C 181.7 . 1 404 86 86 ALA CA C 54.5 . 1 405 86 86 ALA CB C 17.5 . 1 406 86 86 ALA N N 120.0 . 1 407 87 87 ASP H H 8.21 . 1 408 87 87 ASP C C 178.0 . 1 409 87 87 ASP CA C 57.0 . 1 410 87 87 ASP CB C 39.7 . 1 411 87 87 ASP N N 123.1 . 1 412 88 88 LEU H H 7.89 . 1 413 88 88 LEU C C 176.9 . 1 414 88 88 LEU CA C 54.7 . 1 415 88 88 LEU CB C 41.2 . 1 416 88 88 LEU N N 119.2 . 1 417 89 89 GLY H H 7.80 . 1 418 89 89 GLY C C 173.3 . 1 419 89 89 GLY CA C 45.8 . 1 420 89 89 GLY N N 107.7 . 1 421 90 90 LEU H H 8.16 . 1 422 90 90 LEU C C 177.8 . 1 423 90 90 LEU CA C 53.9 . 1 424 90 90 LEU CB C 37.8 . 1 425 90 90 LEU N N 123.1 . 1 426 91 91 LYS H H 8.40 . 1 427 91 91 LYS C C 177.7 . 1 428 91 91 LYS CA C 57.5 . 1 429 91 91 LYS CB C 33.0 . 1 430 91 91 LYS N N 124.5 . 1 431 92 92 ARG H H 9.00 . 1 432 92 92 ARG C C 174.9 . 1 433 92 92 ARG CA C 55.4 . 1 434 92 92 ARG CB C 30.0 . 1 435 92 92 ARG N N 119.3 . 1 436 93 93 GLY H H 7.52 . 1 437 93 93 GLY C C 172.5 . 1 438 93 93 GLY CA C 44.4 . 1 439 93 93 GLY N N 106.5 . 1 440 94 94 TYR H H 8.30 . 1 441 94 94 TYR C C 172.0 . 1 442 94 94 TYR CA C 56.2 . 1 443 94 94 TYR CB C 38.3 . 1 444 94 94 TYR N N 113.0 . 1 445 95 95 ARG H H 9.66 . 1 446 95 95 ARG C C 173.4 . 1 447 95 95 ARG CA C 53.8 . 1 448 95 95 ARG CB C 35.4 . 1 449 95 95 ARG N N 120.8 . 1 450 96 96 MET H H 9.62 . 1 451 96 96 MET C C 175.7 . 1 452 96 96 MET CA C 53.4 . 1 453 96 96 MET CB C 35.0 . 1 454 96 96 MET N N 126.1 . 1 455 97 97 VAL H H 9.35 . 1 456 97 97 VAL C C 174.5 . 1 457 97 97 VAL CA C 60.3 . 1 458 97 97 VAL CB C 37.1 . 1 459 97 97 VAL N N 122.2 . 1 460 98 98 VAL H H 9.24 . 1 461 98 98 VAL C C 173.4 . 1 462 98 98 VAL CA C 61.6 . 1 463 98 98 VAL CB C 34.8 . 1 464 98 98 VAL N N 126.9 . 1 465 99 99 ASN H H 9.36 . 1 466 99 99 ASN C C 173.5 . 1 467 99 99 ASN CA C 51.6 . 1 468 99 99 ASN CB C 38.8 . 1 469 99 99 ASN N N 127.5 . 1 470 100 100 GLU H H 8.52 . 1 471 100 100 GLU C C 175.5 . 1 472 100 100 GLU CA C 53.6 . 1 473 100 100 GLU CB C 29.8 . 1 474 100 100 GLU N N 124.1 . 1 475 101 101 GLY H H 8.96 . 1 476 101 101 GLY C C 172.3 . 1 477 101 101 GLY CA C 44.3 . 1 478 101 101 GLY N N 115.4 . 1 479 102 102 ALA H H 8.64 . 1 480 102 102 ALA C C 182.4 . 1 481 102 102 ALA CA C 55.2 . 1 482 102 102 ALA CB C 18.0 . 1 483 102 102 ALA N N 125.4 . 1 484 103 103 ASP H H 9.38 . 1 485 103 103 ASP C C 177.5 . 1 486 103 103 ASP CA C 56.7 . 1 487 103 103 ASP CB C 38.4 . 1 488 103 103 ASP N N 119.6 . 1 489 104 104 GLY H H 6.92 . 1 490 104 104 GLY C C 172.8 . 1 491 104 104 GLY CA C 45.7 . 1 492 104 104 GLY N N 102.2 . 1 493 105 105 GLY H H 7.54 . 1 494 105 105 GLY C C 172.9 . 1 495 105 105 GLY CA C 44.4 . 1 496 105 105 GLY N N 107.8 . 1 497 106 106 GLN H H 8.12 . 1 498 106 106 GLN CA C 56.5 . 1 499 106 106 GLN CB C 28.0 . 1 500 106 106 GLN N N 121.4 . 1 501 108 108 VAL C C 176.9 . 1 502 109 109 TYR H H 9.41 . 1 503 109 109 TYR C C 174.2 . 1 504 109 109 TYR CA C 58.9 . 1 505 109 109 TYR CB C 35.0 . 1 506 109 109 TYR N N 132.7 . 1 507 110 110 HIS H H 7.95 . 1 508 110 110 HIS C C 175.5 . 1 509 110 110 HIS CA C 56.0 . 1 510 110 110 HIS CB C 35.0 . 1 511 110 110 HIS N N 125.1 . 1 512 111 111 ILE H H 8.94 . 1 513 111 111 ILE C C 171.7 . 1 514 111 111 ILE CA C 63.4 . 1 515 111 111 ILE CB C 37.8 . 1 516 111 111 ILE N N 129.2 . 1 517 112 112 HIS H H 7.91 . 1 518 112 112 HIS C C 176.7 . 1 519 112 112 HIS CA C 53.2 . 1 520 112 112 HIS CB C 31.1 . 1 521 112 112 HIS N N 116.2 . 1 522 113 113 LEU H H 9.03 . 1 523 113 113 LEU C C 175.4 . 1 524 113 113 LEU CA C 53.0 . 1 525 113 113 LEU CB C 45.7 . 1 526 113 113 LEU N N 127.0 . 1 527 114 114 HIS H H 9.64 . 1 528 114 114 HIS C C 176.2 . 1 529 114 114 HIS CA C 56.3 . 1 530 114 114 HIS CB C 34.7 . 1 531 114 114 HIS N N 126.1 . 1 532 115 115 VAL H H 9.20 . 1 533 115 115 VAL C C 173.4 . 1 534 115 115 VAL CA C 61.9 . 1 535 115 115 VAL CB C 31.0 . 1 536 115 115 VAL N N 122.8 . 1 537 116 116 LEU H H 8.80 . 1 538 116 116 LEU C C 175.1 . 1 539 116 116 LEU CA C 54.0 . 1 540 116 116 LEU CB C 44.0 . 1 541 116 116 LEU N N 124.8 . 1 542 117 117 GLY H H 9.08 . 1 543 117 117 GLY C C 170.7 . 1 544 117 117 GLY CA C 45.1 . 1 545 117 117 GLY N N 105.6 . 1 546 118 118 GLY H H 9.70 . 1 547 118 118 GLY C C 173.0 . 1 548 118 118 GLY CA C 44.5 . 1 549 118 118 GLY N N 109.4 . 1 550 119 119 ARG H H 7.58 . 1 551 119 119 ARG C C 172.0 . 1 552 119 119 ARG CA C 52.8 . 1 553 119 119 ARG CB C 31.9 . 1 554 119 119 ARG N N 113.9 . 1 555 120 120 GLN H H 8.32 . 1 556 120 120 GLN C C 175.8 . 1 557 120 120 GLN CA C 56.2 . 1 558 120 120 GLN CB C 29.1 . 1 559 120 120 GLN N N 118.7 . 1 560 121 121 MET H H 9.18 . 1 561 121 121 MET C C 177.3 . 1 562 121 121 MET CA C 52.0 . 1 563 121 121 MET CB C 27.4 . 1 564 121 121 MET N N 129.3 . 1 565 122 122 ASN H H 10.42 . 1 566 122 122 ASN C C 173.2 . 1 567 122 122 ASN CA C 53.0 . 1 568 122 122 ASN CB C 40.9 . 1 569 122 122 ASN N N 125.1 . 1 570 123 123 TRP H H 8.83 . 1 571 123 123 TRP CA C 53.8 . 1 572 123 123 TRP CB C 32.3 . 1 573 123 123 TRP N N 124.7 . 1 574 125 125 PRO C C 173.6 . 1 575 125 125 PRO CA C 61.2 . 1 576 125 125 PRO CB C 27.3 . 1 577 126 126 GLY H H 7.46 . 1 578 126 126 GLY CA C 45.7 . 1 579 126 126 GLY N N 117.3 . 1 stop_ save_