data_26663 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N Chemical Shift Assignments for c-Myc-1-88, pS62 ; _BMRB_accession_number 26663 _BMRB_flat_file_name bmr26663.str _Entry_type original _Submission_date 2015-09-17 _Accession_date 2015-09-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'This assigned peptide contains a phosphorylated Ser 62 residue.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Helander Sara . . 2 Montecchio Meri . . 3 Sunnerhagen Maria . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 71 "13C chemical shifts" 236 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-12-17 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26662 'Backbone 1H, 13C and 15N Chemical Shift Assignments for c-Myc-1-88' stop_ _Original_release_date 2015-12-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26655473 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Helander Sara . . 2 Montecchio Meri . . 3 Pilstal Robert . . 4 Su Yulong . . 5 Kuruvilla Jacob . . 6 Elven Malin . . 7 Ziauddin Javed M.E. . 8 Anandapadamanaban Madhanagopal . . 9 Cristobal Susana . . 10 Lundstrom Patrik . . 11 Sears Rosalie . . 12 Wallner Bjorn . . 13 Sunnerhagen Maria . . stop_ _Journal_abbreviation Structure _Journal_volume 23 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2267 _Page_last 2279 _Year 2015 _Details . loop_ _Keyword 'intrinsically disordered' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name c-Myc _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label c-Myc $c-Myc stop_ _System_molecular_weight 10156 _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Myc fragment comprising residues 1-88 of intact c-Myc' save_ ######################## # Monomeric polymers # ######################## save_c-Myc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common c-Myc _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function ; Proto-oncogenic transcription factor, universal regulator of cell growth, apoptosis and proliferation in both normal and tumor cells. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; HHHHHHMPLNVSFTNRNYDL DYDSVQPYFYCDEEENFYQQ QQQSELQPPAPSEDIWKKFE LLPTPPLXPSRRSGLCSPSY VAVTPFSLRGDNDG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 HIS 2 -4 HIS 3 -3 HIS 4 -2 HIS 5 -1 HIS 6 0 HIS 7 1 MET 8 2 PRO 9 3 LEU 10 4 ASN 11 5 VAL 12 6 SER 13 7 PHE 14 8 THR 15 9 ASN 16 10 ARG 17 11 ASN 18 12 TYR 19 13 ASP 20 14 LEU 21 15 ASP 22 16 TYR 23 17 ASP 24 18 SER 25 19 VAL 26 20 GLN 27 21 PRO 28 22 TYR 29 23 PHE 30 24 TYR 31 25 CYS 32 26 ASP 33 27 GLU 34 28 GLU 35 29 GLU 36 30 ASN 37 31 PHE 38 32 TYR 39 33 GLN 40 34 GLN 41 35 GLN 42 36 GLN 43 37 GLN 44 38 SER 45 39 GLU 46 40 LEU 47 41 GLN 48 42 PRO 49 43 PRO 50 44 ALA 51 45 PRO 52 46 SER 53 47 GLU 54 48 ASP 55 49 ILE 56 50 TRP 57 51 LYS 58 52 LYS 59 53 PHE 60 54 GLU 61 55 LEU 62 56 LEU 63 57 PRO 64 58 THR 65 59 PRO 66 60 PRO 67 61 LEU 68 62 SEP 69 63 PRO 70 64 SER 71 65 ARG 72 66 ARG 73 67 SER 74 68 GLY 75 69 LEU 76 70 CYS 77 71 SER 78 72 PRO 79 73 SER 80 74 TYR 81 75 VAL 82 76 ALA 83 77 VAL 84 78 THR 85 79 PRO 86 80 PHE 87 81 SER 88 82 LEU 89 83 ARG 90 84 GLY 91 85 ASP 92 86 ASN 93 87 ASP 94 88 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P01106 MYC_HUMAN . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $c-Myc 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 $c-Myc 'recombinant technology' . Escherichia coli . pETMCSIII 'Phosphorylation at Ser62 was pursued using a CDK2/CyclinA2 kinase protocol described in the Citation.' 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 $c-Myc 80-250 uM '[U-99% 13C; U-99% 15N]' DTT 5 mM 'natural abundance' glycerol 5 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' HEPES 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'Analysis of data processing' stop_ _Details . save_ 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'With cryoprobe' 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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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_1 save_ save_3D_HACAN_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HACAN' _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' 120 . mM pH 7.0 . 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_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(CA)CO' '3D CBCA(CO)NH' '3D HACAN' 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 c-Myc _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 8 PRO CA C 62.982 . . 2 2 8 PRO CB C 32.040 . . 3 2 8 PRO N N 111.882 . . 4 3 9 LEU H H 8.348 . . 5 3 9 LEU C C 177.163 . . 6 3 9 LEU CA C 55.379 . . 7 3 9 LEU CB C 42.636 . . 8 3 9 LEU N N 121.847 . . 9 4 10 ASN H H 8.412 . . 10 4 10 ASN C C 175.120 . . 11 4 10 ASN CA C 53.242 . . 12 4 10 ASN CB C 38.596 . . 13 4 10 ASN N N 118.783 . . 14 5 11 VAL H H 7.956 . . 15 5 11 VAL C C 175.897 . . 16 5 11 VAL CA C 62.219 . . 17 5 11 VAL CB C 32.865 . . 18 5 11 VAL N N 119.324 . . 19 6 12 SER H H 8.307 . . 20 6 12 SER C C 174.313 . . 21 6 12 SER CA C 58.308 . . 22 6 12 SER CB C 63.797 . . 23 6 12 SER N N 118.368 . . 24 7 13 PHE H H 8.262 . . 25 7 13 PHE C C 175.967 . . 26 7 13 PHE CA C 57.923 . . 27 7 13 PHE CB C 39.472 . . 28 7 13 PHE N N 122.037 . . 29 8 14 THR H H 8.065 . . 30 8 14 THR C C 174.128 . . 31 8 14 THR CA C 62.080 . . 32 8 14 THR CB C 69.800 . . 33 8 14 THR N N 114.439 . . 34 9 15 ASN H H 8.326 . . 35 9 15 ASN C C 174.944 . . 36 9 15 ASN CA C 53.448 . . 37 9 15 ASN CB C 38.867 . . 38 9 15 ASN N N 120.776 . . 39 10 16 ARG H H 8.150 . . 40 10 16 ARG C C 175.460 . . 41 10 16 ARG CA C 56.135 . . 42 10 16 ARG CB C 30.652 . . 43 10 16 ARG N N 120.946 . . 44 11 17 ASN H H 8.374 . . 45 11 17 ASN C C 175.003 . . 46 11 17 ASN CA C 53.134 . . 47 11 17 ASN CB C 38.792 . . 48 11 17 ASN N N 119.379 . . 49 12 18 TYR H H 8.087 . . 50 12 18 TYR C C 175.374 . . 51 12 18 TYR CA C 58.048 . . 52 12 18 TYR N N 120.530 . . 53 13 19 ASP H H 8.277 . . 54 13 19 ASP C C 176.081 . . 55 13 19 ASP CA C 54.559 . . 56 13 19 ASP CB C 41.084 . . 57 13 19 ASP N N 120.971 . . 58 14 20 LEU H H 7.927 . . 59 14 20 LEU C C 176.810 . . 60 14 20 LEU CA C 55.268 . . 61 14 20 LEU CB C 42.343 . . 62 14 20 LEU N N 121.363 . . 63 15 21 ASP H H 8.229 . . 64 15 21 ASP C C 176.216 . . 65 15 21 ASP CA C 54.182 . . 66 15 21 ASP CB C 40.982 . . 67 15 21 ASP N N 120.057 . . 68 16 22 TYR H H 8.026 . . 69 16 22 TYR C C 175.753 . . 70 16 22 TYR CA C 58.572 . . 71 16 22 TYR CB C 38.847 . . 72 16 22 TYR N N 120.758 . . 73 17 23 ASP H H 8.280 . . 74 17 23 ASP C C 176.183 . . 75 17 23 ASP CA C 54.545 . . 76 17 23 ASP CB C 41.183 . . 77 17 23 ASP N N 120.697 . . 78 18 24 SER H H 7.966 . . 79 18 24 SER C C 174.477 . . 80 18 24 SER CA C 58.623 . . 81 18 24 SER CB C 63.832 . . 82 18 24 SER N N 115.342 . . 83 19 25 VAL H H 8.036 . . 84 19 25 VAL C C 175.882 . . 85 19 25 VAL CA C 62.310 . . 86 19 25 VAL CB C 32.578 . . 87 19 25 VAL N N 120.981 . . 88 20 26 GLN H H 8.257 . . 89 20 26 GLN C C 173.807 . . 90 20 26 GLN CA C 53.588 . . 91 20 26 GLN CB C 29.013 . . 92 20 26 GLN N N 124.310 . . 93 21 27 PRO C C 176.083 . . 94 21 27 PRO CA C 63.075 . . 95 21 27 PRO CB C 31.909 . . 96 22 28 TYR H H 7.986 . . 97 22 28 TYR C C 174.954 . . 98 22 28 TYR CA C 57.670 . . 99 22 28 TYR CB C 38.863 . . 100 22 28 TYR N N 119.496 . . 101 23 29 PHE H H 7.903 . . 102 23 29 PHE C C 174.565 . . 103 23 29 PHE CA C 57.523 . . 104 23 29 PHE CB C 40.267 . . 105 23 29 PHE N N 122.007 . . 106 24 30 TYR H H 8.138 . . 107 24 30 TYR C C 175.059 . . 108 24 30 TYR CA C 57.809 . . 109 24 30 TYR N N 122.115 . . 110 25 31 CYS H H 8.175 . . 111 25 31 CYS C C 173.805 . . 112 25 31 CYS CA C 57.882 . . 113 25 31 CYS CB C 28.723 . . 114 25 31 CYS N N 121.040 . . 115 26 32 ASP H H 8.455 . . 116 26 32 ASP C C 176.454 . . 117 26 32 ASP CA C 54.904 . . 118 26 32 ASP CB C 41.282 . . 119 26 32 ASP N N 123.432 . . 120 27 33 GLU H H 8.445 . . 121 27 33 GLU C C 177.091 . . 122 27 33 GLU CA C 57.590 . . 123 27 33 GLU CB C 30.220 . . 124 27 33 GLU N N 120.694 . . 125 28 34 GLU C C 176.449 . . 126 28 34 GLU N N 118.584 . . 127 29 35 GLU H H 8.304 . . 128 29 35 GLU C C 176.791 . . 129 29 35 GLU CA C 57.526 . . 130 29 35 GLU CB C 29.830 . . 131 29 35 GLU N N 120.852 . . 132 30 36 ASN H H 8.331 . . 133 30 36 ASN C C 175.615 . . 134 30 36 ASN CA C 53.817 . . 135 30 36 ASN CB C 38.986 . . 136 30 36 ASN N N 118.612 . . 137 31 37 PHE H H 8.141 . . 138 31 37 PHE C C 176.425 . . 139 31 37 PHE CA C 59.180 . . 140 31 37 PHE CB C 39.275 . . 141 31 37 PHE N N 120.843 . . 142 32 38 TYR H H 8.097 . . 143 32 38 TYR C C 176.455 . . 144 32 38 TYR CA C 59.120 . . 145 32 38 TYR CB C 38.502 . . 146 32 38 TYR N N 120.121 . . 147 33 39 GLN H H 8.137 . . 148 33 39 GLN C C 176.763 . . 149 33 39 GLN CB C 29.254 . . 150 33 39 GLN N N 120.631 . . 151 36 42 GLN N N 120.979 . . 152 37 43 GLN C C 176.327 . . 153 37 43 GLN CA C 56.216 . . 154 37 43 GLN CB C 29.276 . . 155 38 44 SER H H 8.307 . . 156 38 44 SER C C 174.656 . . 157 38 44 SER CA C 58.829 . . 158 38 44 SER CB C 63.740 . . 159 38 44 SER N N 116.689 . . 160 39 45 GLU H H 8.431 . . 161 39 45 GLU C C 176.348 . . 162 39 45 GLU CA C 56.628 . . 163 39 45 GLU CB C 30.082 . . 164 39 45 GLU N N 122.319 . . 165 40 46 LEU H H 8.149 . . 166 40 46 LEU C C 177.030 . . 167 40 46 LEU CA C 55.100 . . 168 40 46 LEU CB C 42.296 . . 169 40 46 LEU N N 122.510 . . 170 41 47 GLN H H 8.282 . . 171 41 47 GLN C C 173.318 . . 172 41 47 GLN CA C 53.298 . . 173 41 47 GLN CB C 29.116 . . 174 41 47 GLN N N 122.164 . . 175 42 48 PRO CA C 61.449 . . 176 42 48 PRO N N 113.878 . . 177 43 49 PRO C C 176.256 . . 178 43 49 PRO CA C 62.620 . . 179 43 49 PRO CB C 32.099 . . 180 43 49 PRO N N 110.593 . . 181 44 50 ALA H H 8.426 . . 182 44 50 ALA C C 175.720 . . 183 44 50 ALA CA C 50.293 . . 184 44 50 ALA CB C 18.246 . . 185 44 50 ALA N N 125.570 . . 186 45 51 PRO C C 177.024 . . 187 45 51 PRO CA C 63.089 . . 188 45 51 PRO CB C 32.358 . . 189 45 51 PRO N N 112.719 . . 190 46 52 SER H H 8.364 . . 191 46 52 SER C C 174.822 . . 192 46 52 SER CA C 58.467 . . 193 46 52 SER CB C 63.809 . . 194 46 52 SER N N 115.836 . . 195 47 53 GLU H H 8.501 . . 196 47 53 GLU C C 176.271 . . 197 47 53 GLU CA C 56.743 . . 198 47 53 GLU CB C 30.265 . . 199 47 53 GLU N N 122.600 . . 200 48 54 ASP H H 8.343 . . 201 48 54 ASP C C 177.038 . . 202 48 54 ASP CA C 54.580 . . 203 48 54 ASP CB C 40.862 . . 204 48 54 ASP N N 121.043 . . 205 49 55 ILE H H 7.874 . . 206 49 55 ILE C C 176.357 . . 207 49 55 ILE CA C 62.484 . . 208 49 55 ILE CB C 38.348 . . 209 49 55 ILE N N 120.184 . . 210 50 56 TRP H H 7.899 . . 211 50 56 TRP C C 176.673 . . 212 50 56 TRP CA C 57.503 . . 213 50 56 TRP CB C 29.243 . . 214 50 56 TRP N N 121.757 . . 215 51 57 LYS H H 7.753 . . 216 51 57 LYS C C 176.552 . . 217 51 57 LYS CA C 56.856 . . 218 51 57 LYS CB C 32.635 . . 219 51 57 LYS N N 121.586 . . 220 52 58 LYS H H 7.952 . . 221 52 58 LYS C C 176.487 . . 222 52 58 LYS CA C 56.742 . . 223 52 58 LYS CB C 32.774 . . 224 52 58 LYS N N 120.822 . . 225 53 59 PHE H H 8.072 . . 226 53 59 PHE C C 175.596 . . 227 53 59 PHE CA C 57.854 . . 228 53 59 PHE CB C 39.399 . . 229 53 59 PHE N N 120.248 . . 230 54 60 GLU H H 8.150 . . 231 54 60 GLU C C 175.708 . . 232 54 60 GLU CA C 56.449 . . 233 54 60 GLU CB C 30.489 . . 234 54 60 GLU N N 122.004 . . 235 55 61 LEU H H 8.161 . . 236 55 61 LEU C C 176.861 . . 237 55 61 LEU CA C 54.867 . . 238 55 61 LEU CB C 42.423 . . 239 55 61 LEU N N 122.868 . . 240 56 62 LEU H H 8.193 . . 241 56 62 LEU CA C 52.807 . . 242 56 62 LEU CB C 41.541 . . 243 56 62 LEU N N 124.637 . . 244 57 63 PRO C C 176.794 . . 245 57 63 PRO CA C 62.803 . . 246 57 63 PRO CB C 32.029 . . 247 57 63 PRO N N 111.058 . . 248 58 64 THR H H 8.254 . . 249 58 64 THR C C 172.469 . . 250 58 64 THR CA C 59.770 . . 251 58 64 THR CB C 69.869 . . 252 58 64 THR N N 117.425 . . 253 59 65 PRO CA C 61.445 . . 254 59 65 PRO N N 115.907 . . 255 60 66 PRO C C 176.703 . . 256 60 66 PRO CA C 62.568 . . 257 60 66 PRO CB C 32.047 . . 258 60 66 PRO N N 110.593 . . 259 61 67 LEU H H 8.328 . . 260 61 67 LEU C C 177.190 . . 261 61 67 LEU CA C 54.798 . . 262 61 67 LEU CB C 42.919 . . 263 61 67 LEU N N 122.521 . . 264 62 68 SEP H H 8.589 . . 265 62 68 SEP CA C 55.726 . . 266 62 68 SEP CB C 65.210 . . 267 62 68 SEP N N 118.880 . . 268 63 69 PRO C C 177.185 . . 269 63 69 PRO CA C 64.727 . . 270 63 69 PRO CB C 32.084 . . 271 63 69 PRO N N 113.314 . . 272 64 70 SER H H 8.413 . . 273 64 70 SER C C 175.348 . . 274 64 70 SER CA C 60.004 . . 275 64 70 SER CB C 62.814 . . 276 64 70 SER N N 114.396 . . 277 65 71 ARG H H 8.056 . . 278 65 71 ARG C C 176.627 . . 279 65 71 ARG CA C 56.046 . . 280 65 71 ARG CB C 30.220 . . 281 65 71 ARG N N 121.595 . . 282 66 72 ARG H H 8.091 . . 283 66 72 ARG C C 176.498 . . 284 66 72 ARG CA C 56.342 . . 285 66 72 ARG CB C 30.713 . . 286 66 72 ARG N N 120.852 . . 287 67 73 SER H H 8.333 . . 288 67 73 SER C C 175.082 . . 289 67 73 SER CA C 58.420 . . 290 67 73 SER N N 116.618 . . 291 68 74 GLY H H 8.413 . . 292 68 74 GLY C C 174.164 . . 293 68 74 GLY CA C 45.433 . . 294 68 74 GLY N N 110.628 . . 295 69 75 LEU H H 8.078 . . 296 69 75 LEU C C 177.382 . . 297 69 75 LEU CA C 55.256 . . 298 69 75 LEU CB C 42.470 . . 299 69 75 LEU N N 121.427 . . 300 70 76 CYS H H 8.344 . . 301 70 76 CYS C C 174.262 . . 302 70 76 CYS CA C 58.231 . . 303 70 76 CYS CB C 28.205 . . 304 70 76 CYS N N 119.515 . . 305 71 77 SER H H 8.375 . . 306 71 77 SER C C 172.736 . . 307 71 77 SER CA C 56.439 . . 308 71 77 SER CB C 63.270 . . 309 71 77 SER N N 119.477 . . 310 72 78 PRO C C 176.810 . . 311 72 78 PRO CA C 63.401 . . 312 72 78 PRO CB C 32.199 . . 313 72 78 PRO N N 113.284 . . 314 73 79 SER H H 8.297 . . 315 73 79 SER C C 174.030 . . 316 73 79 SER CA C 58.375 . . 317 73 79 SER CB C 63.611 . . 318 73 79 SER N N 115.320 . . 319 74 80 TYR H H 8.090 . . 320 74 80 TYR C C 175.195 . . 321 74 80 TYR CA C 57.968 . . 322 74 80 TYR CB C 39.011 . . 323 74 80 TYR N N 122.388 . . 324 75 81 VAL H H 7.878 . . 325 75 81 VAL C C 174.917 . . 326 75 81 VAL CA C 61.760 . . 327 75 81 VAL CB C 33.165 . . 328 75 81 VAL N N 123.695 . . 329 76 82 ALA H H 8.282 . . 330 76 82 ALA C C 177.454 . . 331 76 82 ALA CA C 52.295 . . 332 76 82 ALA CB C 19.320 . . 333 76 82 ALA N N 128.283 . . 334 77 83 VAL H H 8.151 . . 335 77 83 VAL C C 176.161 . . 336 77 83 VAL CA C 62.022 . . 337 77 83 VAL CB C 32.941 . . 338 77 83 VAL N N 120.112 . . 339 78 84 THR H H 8.316 . . 340 78 84 THR C C 172.923 . . 341 78 84 THR CA C 59.553 . . 342 78 84 THR CB C 69.903 . . 343 78 84 THR N N 120.667 . . 344 79 85 PRO C C 176.718 . . 345 79 85 PRO CA C 63.299 . . 346 79 85 PRO CB C 32.133 . . 347 79 85 PRO N N 113.298 . . 348 80 86 PHE H H 8.214 . . 349 80 86 PHE C C 175.883 . . 350 80 86 PHE CA C 58.156 . . 351 80 86 PHE CB C 39.484 . . 352 80 86 PHE N N 119.943 . . 353 81 87 SER H H 8.104 . . 354 81 87 SER C C 174.175 . . 355 81 87 SER CA C 58.161 . . 356 81 87 SER CB C 63.970 . . 357 81 87 SER N N 117.053 . . 358 82 88 LEU H H 8.244 . . 359 82 88 LEU C C 177.333 . . 360 82 88 LEU CA C 55.195 . . 361 82 88 LEU CB C 42.377 . . 362 82 88 LEU N N 124.236 . . 363 83 89 ARG H H 8.256 . . 364 83 89 ARG C C 176.761 . . 365 83 89 ARG CA C 56.346 . . 366 83 89 ARG CB C 31.101 . . 367 83 89 ARG N N 121.397 . . 368 84 90 GLY H H 8.470 . . 369 84 90 GLY C C 174.022 . . 370 84 90 GLY CA C 45.242 . . 371 84 90 GLY N N 110.131 . . 372 85 91 ASP H H 8.324 . . 373 85 91 ASP C C 176.219 . . 374 85 91 ASP CA C 54.482 . . 375 85 91 ASP CB C 41.143 . . 376 85 91 ASP N N 120.263 . . 377 86 92 ASN H H 8.463 . . 378 86 92 ASN C C 174.871 . . 379 86 92 ASN CA C 53.329 . . 380 86 92 ASN CB C 39.123 . . 381 86 92 ASN N N 118.177 . . 382 87 93 ASP H H 8.288 . . 383 87 93 ASP C C 175.618 . . 384 87 93 ASP CA C 54.501 . . 385 87 93 ASP CB C 41.293 . . 386 87 93 ASP N N 120.885 . . 387 88 94 GLY H H 7.979 . . 388 88 94 GLY C C 179.108 . . 389 88 94 GLY CA C 46.237 . . 390 88 94 GLY N N 115.087 . . stop_ save_