data_27703 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Myc bHLH-LZ domain in presence of 1.6 M GdmCl ; _BMRB_accession_number 27703 _BMRB_flat_file_name bmr27703.str _Entry_type original _Submission_date 2018-11-24 _Accession_date 2018-11-24 _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 Panova Stanislava V. . 2 Cliff Matthew J. . 3 Macek Pavel . . 4 Blackledge Martin . . 5 Jensen Malene Ringkjobing . 6 Nissink 'J. Willem' M. . 7 Embrey Kevin J. . 8 Davies Rick . . 9 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 84 "13C chemical shifts" 168 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-02 update BMRB 'update entry citation' 2019-08-15 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27701 'bHLHZip domain of Myc (in presence of 3.2 M GdmCl)' 27702 'bHLHZip domain of Myc (in presence of 2.4 M GdmCl)' 27704 'bHLHZip domain of Myc' stop_ _Original_release_date 2018-11-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31402220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Panova Stanislava V. . 2 Cliff Matthew J. . 3 Macek Pavel . . 4 Blackledge Martin . . 5 Jensen Malene Ringkjobing . 6 Nissink 'J. Willem' M. . 7 Embrey Kevin J. . 8 Davies Rick . . 9 Waltho Jonathan P. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 27 _Journal_issue 10 _Journal_ISSN 1878-4186 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1537 _Page_last 1546 _Year 2019 _Details . loop_ _Keyword IDP 'chemical denaturation' 'disordered protein' 'protein unfolding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bHLHZip domain of Myc' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'bHLHZip domain of Myc' $bHLHZip_domain_of_Myc stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bHLHZip_domain_of_Myc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common bHLHZip_domain_of_Myc _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; GSNVKRRTHNVLERQRRNEL KRSFFALRDQIPELENNEKA PKVVILKKATAYILSVQAEE QKLISEEDLLRKRREQLKHK LEQLRNS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 351 GLY 2 352 SER 3 353 ASN 4 354 VAL 5 355 LYS 6 356 ARG 7 357 ARG 8 358 THR 9 359 HIS 10 360 ASN 11 361 VAL 12 362 LEU 13 363 GLU 14 364 ARG 15 365 GLN 16 366 ARG 17 367 ARG 18 368 ASN 19 369 GLU 20 370 LEU 21 371 LYS 22 372 ARG 23 373 SER 24 374 PHE 25 375 PHE 26 376 ALA 27 377 LEU 28 378 ARG 29 379 ASP 30 380 GLN 31 381 ILE 32 382 PRO 33 383 GLU 34 384 LEU 35 385 GLU 36 386 ASN 37 387 ASN 38 388 GLU 39 389 LYS 40 390 ALA 41 391 PRO 42 392 LYS 43 393 VAL 44 394 VAL 45 395 ILE 46 396 LEU 47 397 LYS 48 398 LYS 49 399 ALA 50 400 THR 51 401 ALA 52 402 TYR 53 403 ILE 54 404 LEU 55 405 SER 56 406 VAL 57 407 GLN 58 408 ALA 59 409 GLU 60 410 GLU 61 411 GLN 62 412 LYS 63 413 LEU 64 414 ILE 65 415 SER 66 416 GLU 67 417 GLU 68 418 ASP 69 419 LEU 70 420 LEU 71 421 ARG 72 422 LYS 73 423 ARG 74 424 ARG 75 425 GLU 76 426 GLN 77 427 LEU 78 428 LYS 79 429 HIS 80 430 LYS 81 431 LEU 82 432 GLU 83 433 GLN 84 434 LEU 85 435 ARG 86 436 ASN 87 437 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $bHLHZip_domain_of_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 $bHLHZip_domain_of_Myc 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET 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 $bHLHZip_domain_of_Myc 1 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM 'natural abundance' TSP 1 mM 'natural abundance' GdmCl 1.6 M 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR _Saveframe_category software _Name CCPNMR _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_(H)N(CA)NNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name (H)N(CA)NNH _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' 1.6 0.05 M pH 6.5 0.1 pH pressure 1 . atm temperature 278 . 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 TSP C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0 internal indirect . . . 1 TSP N 15 'methyl protons' ppm 0 internal 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 $CCPNMR stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' (H)N(CA)NNH 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 'bHLHZip domain of 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 1 352 2 SER H H 8.79 0.003 1 2 352 2 SER CA C 58.57348 0.6 1 3 352 2 SER CB C 64.18179 0.6 1 4 352 2 SER N N 115.967 0.13 1 5 353 3 ASN H H 8.775 0.006 1 6 353 3 ASN CA C 53.53561 0.6 1 7 353 3 ASN CB C 38.95631 0.6 1 8 353 3 ASN N N 121.895 0.09 1 9 354 4 VAL H H 8.189 0.006 1 10 354 4 VAL CA C 62.87074 0.6 1 11 354 4 VAL CB C 32.86842 0.6 1 12 354 4 VAL N N 121.003 0.05 1 13 355 5 LYS H H 8.512 0.006 1 14 355 5 LYS CA C 56.54995 0.6 1 15 355 5 LYS CB C 33.14021 0.6 1 16 355 5 LYS N N 126.192 0.1 1 17 356 6 ARG H H 8.481 0.007 1 18 356 6 ARG CA C 56.4762 0.6 1 19 356 6 ARG CB C 31.08499 0.6 1 20 356 6 ARG N N 123.695 0.13 1 21 357 7 ARG H H 8.598 0.004 1 22 357 7 ARG CA C 56.52288 0.6 1 23 357 7 ARG CB C 30.89517 0.6 1 24 357 7 ARG N N 123.651 0.08 1 25 358 8 THR H H 8.312 0.005 1 26 358 8 THR CA C 61.97633 0.6 1 27 358 8 THR CB C 70.16569 0.6 1 28 358 8 THR N N 115.647 0.05 1 29 359 9 HIS H H 8.643 0.053 1 30 359 9 HIS CA C 55.89597 0.6 1 31 359 9 HIS CB C 29.6858 0.6 1 32 359 9 HIS N N 120.931 0.31 1 33 360 10 ASN H H 8.675 0.029 1 34 360 10 ASN CA C 53.63498 0.6 1 35 360 10 ASN CB C 39.02362 0.6 1 36 360 10 ASN N N 121.126 0.15 1 37 361 11 VAL H H 8.315 0.007 1 38 361 11 VAL CA C 63.27529 0.6 1 39 361 11 VAL CB C 32.67662 0.6 1 40 361 11 VAL N N 121.465 0.08 1 41 362 12 LEU H H 8.393 0.009 1 42 362 12 LEU CA C 55.84236 0.6 1 43 362 12 LEU CB C 42.19143 0.6 1 44 362 12 LEU N N 125.428 0.23 1 45 363 13 GLU H H 8.439 0.003 1 46 363 13 GLU CA C 57.31194 0.6 1 47 363 13 GLU CB C 30.33319 0.6 1 48 363 13 GLU N N 122.251 0.17 1 49 364 14 ARG H H 8.417 0.012 1 50 364 14 ARG CA C 57.10108 0.6 1 51 364 14 ARG CB C 30.58872 0.6 1 52 364 14 ARG N N 122.272 0.17 1 53 365 15 GLN H H 8.504 0.006 1 54 365 15 GLN CA C 56.80322 0.6 1 55 365 15 GLN CB C 29.4721 0.6 1 56 365 15 GLN N N 121.71 0.18 1 57 366 16 ARG H H 8.502 0.007 1 58 366 16 ARG CA C 56.95035 0.6 1 59 366 16 ARG CB C 30.85448 0.6 1 60 366 16 ARG N N 122.952 0.19 1 61 367 17 ARG H H 8.511 0.004 1 62 367 17 ARG CA C 57.23897 0.6 1 63 367 17 ARG CB C 30.65411 0.6 1 64 367 17 ARG N N 122.292 0.2 1 65 368 18 ASN H H 8.554 0.003 1 66 368 18 ASN CA C 53.80782 0.6 1 67 368 18 ASN CB C 38.85078 0.6 1 68 368 18 ASN N N 119.911 0.15 1 69 369 19 GLU H H 8.452 0.002 1 70 369 19 GLU CA C 57.23336 0.6 1 71 369 19 GLU CB C 30.26688 0.6 1 72 369 19 GLU N N 121.617 0.16 1 73 370 20 LEU H H 8.298 0.012 1 74 370 20 LEU CA C 55.80191 0.6 1 75 370 20 LEU CB C 42.31319 0.6 1 76 370 20 LEU N N 123.003 0.18 1 77 371 21 LYS H H 8.325 0.012 1 78 371 21 LYS CA C 56.76615 0.6 1 79 371 21 LYS CB C 33.01198 0.6 1 80 371 21 LYS N N 122.624 0.2 1 81 372 22 ARG H H 8.418 0.006 1 82 372 22 ARG CA C 56.5012 0.6 1 83 372 22 ARG CB C 30.79035 0.6 1 84 372 22 ARG N N 122.638 0.16 1 85 373 23 SER H H 8.396 0.004 1 86 373 23 SER CA C 58.84415 0.6 1 87 373 23 SER CB C 64.02012 0.6 1 88 373 23 SER N N 117.323 0.16 1 89 374 24 PHE H H 8.347 0.012 1 90 374 24 PHE CA C 58.84271 0.6 1 91 374 24 PHE CB C 39.87016 0.6 1 92 374 24 PHE N N 122.999 0.19 1 93 375 25 PHE H H 8.174 0.001 1 94 375 25 PHE CA C 58.1264 0.6 1 95 375 25 PHE CB C 39.85671 0.6 1 96 375 25 PHE N N 121.467 0.11 1 97 376 26 ALA H H 8.249 0.007 1 98 376 26 ALA CA C 52.83018 0.6 1 99 376 26 ALA CB C 19.49705 0.6 1 100 376 26 ALA N N 125.506 0.12 1 101 377 27 LEU H H 8.254 0.004 1 102 377 27 LEU CA C 55.88517 0.6 1 103 377 27 LEU CB C 42.30754 0.6 1 104 377 27 LEU N N 121.763 0.17 1 105 378 28 ARG H H 8.331 0.009 1 106 378 28 ARG CA C 56.41414 0.6 1 107 378 28 ARG CB C 30.88642 0.6 1 108 378 28 ARG N N 121.255 0.14 1 109 379 29 ASP H H 8.408 0.006 1 110 379 29 ASP CA C 54.76288 0.6 1 111 379 29 ASP CB C 41.25974 0.6 1 112 379 29 ASP N N 121.038 0.17 1 113 380 30 GLN H H 8.308 0.01 1 114 380 30 GLN CA C 55.89154 0.6 1 115 380 30 GLN CB C 29.84247 0.6 1 116 380 30 GLN N N 120.436 0.14 1 117 381 31 ILE H H 8.385 0.006 1 118 381 31 ILE CA C 59.23129 0.6 1 119 381 31 ILE CB C 38.48425 0.6 1 120 381 31 ILE N N 124.448 0.03 1 121 383 33 GLU H H 8.655 0.005 1 122 383 33 GLU CA C 56.94647 0.6 1 123 383 33 GLU CB C 30.30235 0.6 1 124 383 33 GLU N N 121.937 0.13 1 125 384 34 LEU H H 8.414 0.004 1 126 384 34 LEU CA C 55.40409 0.6 1 127 384 34 LEU CB C 42.54021 0.6 1 128 384 34 LEU N N 123.431 0.1 1 129 385 35 GLU H H 8.563 0 1 130 385 35 GLU CA C 56.66871 0.6 1 131 385 35 GLU CB C 30.39708 0.6 1 132 385 35 GLU N N 121.995 0.09 1 133 386 36 ASN H H 8.618 0.004 1 134 386 36 ASN CA C 53.48618 0.6 1 135 386 36 ASN CB C 39.02186 0.6 1 136 386 36 ASN N N 120.194 0.09 1 137 387 37 ASN H H 8.603 0.006 1 138 387 37 ASN CA C 53.51987 0.6 1 139 387 37 ASN CB C 39.10918 0.6 1 140 387 37 ASN N N 119.989 0.08 1 141 388 38 GLU H H 8.449 0.001 1 142 388 38 GLU CA C 57.15355 0.6 1 143 388 38 GLU CB C 30.27006 0.6 1 144 388 38 GLU N N 121.421 0.11 1 145 389 39 LYS H H 8.412 0.003 1 146 389 39 LYS CA C 56.33124 0.6 1 147 389 39 LYS CB C 33.18778 0.6 1 148 389 39 LYS N N 122.601 0.1 1 149 390 40 ALA H H 8.443 0.002 1 150 390 40 ALA CA C 50.80978 0.6 1 151 390 40 ALA CB C 18.10775 0.6 1 152 390 40 ALA N N 127.045 0.09 1 153 392 42 LYS H H 8.559 0.001 1 154 392 42 LYS CA C 56.76628 0.6 1 155 392 42 LYS CB C 33.05415 0.6 1 156 392 42 LYS N N 123.011 0.14 1 157 393 43 VAL H H 8.35 0.007 1 158 393 43 VAL CA C 62.77872 0.6 1 159 393 43 VAL CB C 33.0271 0.6 1 160 393 43 VAL N N 123.521 0.03 1 161 394 44 VAL H H 8.435 0.016 1 162 394 44 VAL CA C 62.63944 0.6 1 163 394 44 VAL CB C 33.04402 0.6 1 164 394 44 VAL N N 126.744 0.03 1 165 395 45 ILE H H 8.475 0.011 1 166 395 45 ILE CA C 60.77228 0.6 1 167 395 45 ILE CB C 38.50556 0.6 1 168 395 45 ILE N N 127.524 0.04 1 169 396 46 LEU H H 8.518 0.008 1 170 396 46 LEU CA C 54.97691 0.6 1 171 396 46 LEU CB C 42.47928 0.6 1 172 396 46 LEU N N 128.454 0.08 1 173 397 47 LYS H H 8.454 0.005 1 174 397 47 LYS CA C 56.57572 0.6 1 175 397 47 LYS CB C 33.14887 0.6 1 176 397 47 LYS N N 123.784 0.07 1 177 398 48 LYS H H 8.485 0.007 1 178 398 48 LYS CA C 56.56247 0.6 1 179 398 48 LYS CB C 33.24457 0.6 1 180 398 48 LYS N N 123.862 0.05 1 181 399 49 ALA H H 8.568 0.004 1 182 399 49 ALA CA C 53.01899 0.6 1 183 399 49 ALA CB C 19.39909 0.6 1 184 399 49 ALA N N 126.247 0.09 1 185 400 50 THR H H 8.147 0.002 1 186 400 50 THR CA C 62.22513 0.6 1 187 400 50 THR CB C 70.12286 0.6 1 188 400 50 THR N N 114.096 0.06 1 189 401 51 ALA H H 8.417 0.004 1 190 401 51 ALA CA C 53.21896 0.6 1 191 401 51 ALA CB C 19.30767 0.6 1 192 401 51 ALA N N 126.333 0.1 1 193 402 52 TYR H H 8.246 0.006 1 194 402 52 TYR CA C 58.82053 0.6 1 195 402 52 TYR CB C 38.88329 0.6 1 196 402 52 TYR N N 120.42 0.11 1 197 403 53 ILE H H 8.114 0.005 1 198 403 53 ILE CA C 61.66938 0.6 1 199 403 53 ILE CB C 38.78249 0.6 1 200 403 53 ILE N N 123.486 0.08 1 201 404 54 LEU H H 8.329 0.002 1 202 404 54 LEU CA C 55.83159 0.6 1 203 404 54 LEU CB C 42.31747 0.6 1 204 404 54 LEU N N 125.904 0.17 1 205 405 55 SER H H 8.355 0.002 1 206 405 55 SER CA C 58.90901 0.6 1 207 405 55 SER CB C 63.96537 0.6 1 208 405 55 SER N N 117.872 0.11 1 209 406 56 VAL H H 8.262 0.001 1 210 406 56 VAL CA C 63.0798 0.6 1 211 406 56 VAL CB C 32.72771 0.6 1 212 406 56 VAL N N 122.503 0.03 1 213 407 57 GLN H H 8.467 0.004 1 214 407 57 GLN CA C 56.98294 0.6 1 215 407 57 GLN CB C 29.31253 0.6 1 216 407 57 GLN N N 123.149 0.13 1 217 408 58 ALA H H 8.381 0.005 1 218 408 58 ALA CA C 53.51389 0.6 1 219 408 58 ALA CB C 19.173 0.6 1 220 408 58 ALA N N 125.044 0.11 1 221 409 59 GLU H H 8.446 0 1 222 409 59 GLU CA C 57.4144 0.6 1 223 409 59 GLU CB C 30.24936 0.6 1 224 409 59 GLU N N 120.342 0.1 1 225 410 60 GLU H H 8.461 0 1 226 410 60 GLU CA C 57.26381 0.6 1 227 410 60 GLU CB C 30.46438 0.6 1 228 410 60 GLU N N 121.605 0.12 1 229 411 61 GLN H H 8.414 0.007 1 230 411 61 GLN CA C 56.8211 0.6 1 231 411 61 GLN CB C 29.64604 0.6 1 232 411 61 GLN N N 121.037 0.18 1 233 412 62 LYS H H 8.332 0.01 1 234 412 62 LYS CA C 56.85881 0.6 1 235 412 62 LYS CB C 33.00332 0.6 1 236 412 62 LYS N N 122.858 0.14 1 237 413 63 LEU H H 8.305 0.01 1 238 413 63 LEU CA C 56.08756 0.6 1 239 413 63 LEU CB C 42.2092 0.6 1 240 413 63 LEU N N 123.455 0.23 1 241 414 64 ILE H H 8.252 0.009 1 242 414 64 ILE CA C 61.92209 0.6 1 243 414 64 ILE CB C 38.81967 0.6 1 244 414 64 ILE N N 122.686 0.15 1 245 415 65 SER H H 8.711 0.022 1 246 415 65 SER CA C 59.03047 0.6 1 247 415 65 SER CB C 64.35283 0.6 1 248 415 65 SER N N 120.698 0.08 1 249 416 66 GLU H H 8.697 0.009 1 250 416 66 GLU CA C 58.85207 0.6 1 251 416 66 GLU CB C 29.82934 0.6 1 252 416 66 GLU N N 123.197 0.15 1 253 417 67 GLU H H 8.529 0.012 1 254 417 67 GLU CA C 58.60489 0.6 1 255 417 67 GLU CB C 29.826 0.6 1 256 417 67 GLU N N 120.038 0.11 1 257 418 68 ASP H H 8.288 0.011 1 258 418 68 ASP CA C 56.30018 0.6 1 259 418 68 ASP CB C 40.9563 0.6 1 260 418 68 ASP N N 121.096 0.1 1 261 419 69 LEU H H 8.139 0.004 1 262 419 69 LEU CA C 57.32467 0.6 1 263 419 69 LEU CB C 42.03909 0.6 1 264 419 69 LEU N N 122.346 0.09 1 265 420 70 LEU H H 8.157 0.015 1 266 420 70 LEU CA C 57.28872 0.6 1 267 420 70 LEU CB C 41.90434 0.6 1 268 420 70 LEU N N 121.077 0.33 1 269 421 71 ARG H H 8.084 0.029 1 270 421 71 ARG CA C 58.58296 0.6 1 271 421 71 ARG CB C 30.34374 0.6 1 272 421 71 ARG N N 120.87 0.31 1 273 422 72 LYS H H 8.227 0.028 1 274 422 72 LYS CA C 58.40225 0.6 1 275 422 72 LYS CB C 32.80746 0.6 1 276 422 72 LYS N N 121.372 0.37 1 277 423 73 ARG H H 8.317 0.025 1 278 423 73 ARG CA C 56.43394 0.6 1 279 423 73 ARG CB C 30.8796 0.6 1 280 423 73 ARG N N 121.316 0.35 1 281 424 74 ARG H H 8.364 0.023 1 282 424 74 ARG CA C 56.43161 0.6 1 283 424 74 ARG CB C 30.64153 0.6 1 284 424 74 ARG N N 121.497 0.35 1 285 425 75 GLU H H 8.425 0.02 1 286 425 75 GLU CA C 57.47805 0.6 1 287 425 75 GLU CB C 30.13963 0.6 1 288 425 75 GLU N N 121.467 0.31 1 289 426 76 GLN H H 8.377 0.026 1 290 426 76 GLN CA C 57.26994 0.6 1 291 426 76 GLN CB C 29.49191 0.6 1 292 426 76 GLN N N 120.901 0.38 1 293 427 77 LEU H H 8.208 0.023 1 294 427 77 LEU CA C 56.49196 0.6 1 295 427 77 LEU CB C 42.22736 0.6 1 296 427 77 LEU N N 122.795 0.31 1 297 428 78 LYS H H 8.21 0.025 1 298 428 78 LYS CA C 57.48762 0.6 1 299 428 78 LYS CB C 33.15649 0.6 1 300 428 78 LYS N N 121.188 0.25 1 301 429 79 HIS H H 8.39 0.074 1 302 429 79 HIS CA C 56.49683 0.6 1 303 429 79 HIS CB C 29.35998 0.6 1 304 429 79 HIS N N 118.98 0.03 1 305 430 80 LYS H H 8.404 0.052 1 306 430 80 LYS CA C 56.95825 0.6 1 307 430 80 LYS CB C 32.98446 0.6 1 308 430 80 LYS N N 122.951 0.32 1 309 431 81 LEU H H 8.436 0.006 1 310 431 81 LEU CA C 55.79377 0.6 1 311 431 81 LEU CB C 42.25496 0.6 1 312 431 81 LEU N N 122.906 0.33 1 313 432 82 GLU H H 8.428 0.016 1 314 432 82 GLU CA C 57.25992 0.6 1 315 432 82 GLU CB C 30.25321 0.6 1 316 432 82 GLU N N 121.927 0.27 1 317 433 83 GLN H H 8.387 0.014 1 318 433 83 GLN CA C 56.55931 0.6 1 319 433 83 GLN CB C 29.49317 0.6 1 320 433 83 GLN N N 121.222 0.18 1 321 434 84 LEU H H 8.341 0.017 1 322 434 84 LEU CA C 55.94875 0.6 1 323 434 84 LEU CB C 42.28378 0.6 1 324 434 84 LEU N N 123.529 0.27 1 325 435 85 ARG H H 8.401 0.014 1 326 435 85 ARG CA C 56.67661 0.6 1 327 435 85 ARG CB C 30.96965 0.6 1 328 435 85 ARG N N 121.645 0.17 1 329 436 86 ASN H H 8.525 0.01 1 330 436 86 ASN CA C 53.48649 0.6 1 331 436 86 ASN CB C 39.27872 0.6 1 332 436 86 ASN N N 120.223 0.16 1 333 437 87 SER H H 7.995 0.006 1 334 437 87 SER CA C 60.43019 0.6 1 335 437 87 SER CB C 64.85775 0.6 1 336 437 87 SER N N 121.558 0.1 1 stop_ save_