data_27186 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for APLF acidic domain ; _BMRB_accession_number 27186 _BMRB_flat_file_name bmr27186.str _Entry_type original _Submission_date 2017-07-21 _Accession_date 2017-07-21 _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 'van Ingen' Hugo . . 2 Corbeski Ivan . . 3 Dolinar Klemen . . 4 Wienk Hans . . 5 Boelens Rolf . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 "13C chemical shifts" 190 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-11-21 update BMRB 'update entry citation' 2018-06-21 original author 'original release' stop_ _Original_release_date 2017-07-21 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29905837 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Corbeski Ivan . . 2 Dolinar Klemen . . 3 Wienk Hans . . 4 Boelens Rolf . . 5 'van Ingen' Hugo . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_volume 46 _Journal_issue 14 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7138 _Page_last 7152 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'APLF acidic domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'APLF acidic domain' $APLF_acidic_domain stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_APLF_acidic_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common APLF_acidic_domain _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 65 _Mol_residue_sequence ; GSLDEDNDNVGQPNEYDLND SFLDDEEEDYEPTDEDSDWE PGKEDEEKEDVEELLKEAKR FMKRK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 447 GLY 2 448 SER 3 449 LEU 4 450 ASP 5 451 GLU 6 452 ASP 7 453 ASN 8 454 ASP 9 455 ASN 10 456 VAL 11 457 GLY 12 458 GLN 13 459 PRO 14 460 ASN 15 461 GLU 16 462 TYR 17 463 ASP 18 464 LEU 19 465 ASN 20 466 ASP 21 467 SER 22 468 PHE 23 469 LEU 24 470 ASP 25 471 ASP 26 472 GLU 27 473 GLU 28 474 GLU 29 475 ASP 30 476 TYR 31 477 GLU 32 478 PRO 33 479 THR 34 480 ASP 35 481 GLU 36 482 ASP 37 483 SER 38 484 ASP 39 485 TRP 40 486 GLU 41 487 PRO 42 488 GLY 43 489 LYS 44 490 GLU 45 491 ASP 46 492 GLU 47 493 GLU 48 494 LYS 49 495 GLU 50 496 ASP 51 497 VAL 52 498 GLU 53 499 GLU 54 500 LEU 55 501 LEU 56 502 LYS 57 503 GLU 58 504 ALA 59 505 LYS 60 506 ARG 61 507 PHE 62 508 MET 63 509 LYS 64 510 ARG 65 511 LYS 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 $APLF_acidic_domain 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 $APLF_acidic_domain 'recombinant technology' . Escherichia coli . pLIC 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $APLF_acidic_domain . uM 200 300 '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _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' 300 . mM pH 7 . pH pressure 1 . atm temperature 300 . 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 water H 1 protons ppm 4.7 external direct . . . 1.0 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 HNCACB' '3D CBCA(CO)NH' '3D HBHA(CO)NH' 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 'APLF acidic domain' _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 1 448 2 SER HA H 4.611 . . 2 448 2 SER C C 174.880 . . 3 448 2 SER CA C 58.881 . . 4 448 2 SER CB C 64.107 . . 5 449 3 LEU H H 8.502 . . 6 449 3 LEU HA H 4.516 . . 7 449 3 LEU C C 177.359 . . 8 449 3 LEU CA C 55.885 . . 9 449 3 LEU CB C 42.295 . . 10 449 3 LEU N N 123.259 . . 11 450 4 ASP H H 8.193 . . 12 450 4 ASP C C 176.383 . . 13 450 4 ASP CA C 54.741 . . 14 450 4 ASP CB C 41.505 . . 15 450 4 ASP N N 120.019 . . 16 451 5 GLU H H 8.395 . . 17 451 5 GLU HA H 4.417 . . 18 451 5 GLU C C 176.175 . . 19 451 5 GLU CA C 56.722 . . 20 451 5 GLU CB C 30.695 . . 21 451 5 GLU N N 121.199 . . 22 452 6 ASP H H 8.487 . . 23 452 6 ASP HA H 4.744 . . 24 452 6 ASP C C 176.145 . . 25 452 6 ASP CA C 54.681 . . 26 452 6 ASP CB C 41.347 . . 27 452 6 ASP N N 122.134 . . 28 453 7 ASN H H 8.267 . . 29 453 7 ASN HA H 4.818 . . 30 453 7 ASN C C 175.122 . . 31 453 7 ASN CA C 53.626 . . 32 453 7 ASN CB C 39.606 . . 33 453 7 ASN N N 119.235 . . 34 454 8 ASP H H 8.394 . . 35 454 8 ASP HA H 4.728 . . 36 454 8 ASP C C 176.098 . . 37 454 8 ASP CA C 54.803 . . 38 454 8 ASP CB C 41.329 . . 39 454 8 ASP N N 120.666 . . 40 455 9 ASN H H 8.339 . . 41 455 9 ASN HA H 4.843 . . 42 455 9 ASN C C 175.315 . . 43 455 9 ASN CA C 53.529 . . 44 455 9 ASN CB C 39.153 . . 45 455 9 ASN N N 118.838 . . 46 456 10 VAL H H 8.032 . . 47 456 10 VAL HA H 4.234 . . 48 456 10 VAL C C 176.798 . . 49 456 10 VAL CA C 62.812 . . 50 456 10 VAL CB C 32.607 . . 51 456 10 VAL N N 119.851 . . 52 457 11 GLY H H 8.481 . . 53 457 11 GLY HA2 H 4.068 . . 54 457 11 GLY HA3 H 4.068 . . 55 457 11 GLY C C 173.791 . . 56 457 11 GLY CA C 45.369 . . 57 457 11 GLY N N 112.150 . . 58 458 12 GLN H H 8.208 . . 59 458 12 GLN C C 174.265 . . 60 458 12 GLN CA C 53.713 . . 61 458 12 GLN CB C 29.171 . . 62 458 12 GLN N N 120.834 . . 63 459 13 PRO HA H 4.538 . . 64 459 13 PRO C C 176.789 . . 65 459 13 PRO CA C 63.516 . . 66 459 13 PRO CB C 32.215 . . 67 460 14 ASN H H 8.548 . . 68 460 14 ASN C C 175.444 . . 69 460 14 ASN CA C 53.498 . . 70 460 14 ASN CB C 39.365 . . 71 460 14 ASN N N 118.920 . . 72 461 15 GLU H H 8.407 . . 73 461 15 GLU HA H 4.324 . . 74 461 15 GLU C C 176.136 . . 75 461 15 GLU CA C 57.064 . . 76 461 15 GLU CB C 30.375 . . 77 461 15 GLU N N 121.225 . . 78 462 16 TYR H H 8.043 . . 79 462 16 TYR HA H 4.691 . . 80 462 16 TYR C C 175.492 . . 81 462 16 TYR CA C 57.922 . . 82 462 16 TYR CB C 38.974 . . 83 462 16 TYR N N 119.791 . . 84 463 17 ASP H H 8.212 . . 85 463 17 ASP HA H 4.726 . . 86 463 17 ASP C C 176.169 . . 87 463 17 ASP CA C 54.509 . . 88 463 17 ASP CB C 41.568 . . 89 463 17 ASP N N 121.901 . . 90 464 18 LEU H H 8.095 . . 91 464 18 LEU HA H 4.419 . . 92 464 18 LEU C C 177.386 . . 93 464 18 LEU CA C 55.631 . . 94 464 18 LEU CB C 42.419 . . 95 464 18 LEU N N 122.693 . . 96 465 19 ASN H H 8.408 . . 97 465 19 ASN HA H 4.770 . . 98 465 19 ASN C C 175.130 . . 99 465 19 ASN CA C 53.722 . . 100 465 19 ASN CB C 39.423 . . 101 465 19 ASN N N 119.080 . . 102 466 20 ASP H H 8.246 . . 103 466 20 ASP HA H 4.702 . . 104 466 20 ASP C C 176.325 . . 105 466 20 ASP CA C 54.716 . . 106 466 20 ASP CB C 41.372 . . 107 466 20 ASP N N 121.009 . . 108 467 21 SER H H 8.138 . . 109 467 21 SER HA H 4.496 . . 110 467 21 SER C C 174.204 . . 111 467 21 SER CA C 58.640 . . 112 467 21 SER CB C 64.089 . . 113 467 21 SER N N 115.748 . . 114 468 22 PHE H H 8.176 . . 115 468 22 PHE HA H 4.756 . . 116 468 22 PHE C C 175.551 . . 117 468 22 PHE CA C 57.916 . . 118 468 22 PHE CB C 39.535 . . 119 468 22 PHE N N 121.943 . . 120 469 23 LEU H H 8.062 . . 121 469 23 LEU HA H 4.464 . . 122 469 23 LEU C C 176.774 . . 123 469 23 LEU CA C 55.099 . . 124 469 23 LEU CB C 42.867 . . 125 469 23 LEU N N 123.650 . . 126 470 24 ASP H H 8.208 . . 127 470 24 ASP HA H 4.721 . . 128 470 24 ASP C C 175.939 . . 129 470 24 ASP CA C 54.614 . . 130 470 24 ASP CB C 41.445 . . 131 470 24 ASP N N 121.584 . . 132 471 25 ASP H H 8.242 . . 133 471 25 ASP HA H 4.718 . . 134 471 25 ASP C C 176.314 . . 135 471 25 ASP CA C 54.610 . . 136 471 25 ASP CB C 41.578 . . 137 471 25 ASP N N 120.869 . . 138 472 26 GLU H H 8.332 . . 139 472 26 GLU HA H 4.396 . . 140 472 26 GLU C C 176.323 . . 141 472 26 GLU CA C 56.912 . . 142 472 26 GLU CB C 30.413 . . 143 472 26 GLU N N 121.079 . . 144 473 27 GLU H H 8.334 . . 145 473 27 GLU HA H 4.397 . . 146 473 27 GLU C C 176.487 . . 147 473 27 GLU CA C 56.686 . . 148 473 27 GLU CB C 30.668 . . 149 473 27 GLU N N 120.921 . . 150 474 28 GLU H H 8.415 . . 151 474 28 GLU HA H 4.391 . . 152 474 28 GLU C C 175.935 . . 153 474 28 GLU CA C 56.594 . . 154 474 28 GLU CB C 30.821 . . 155 474 28 GLU N N 122.502 . . 156 475 29 ASP H H 8.382 . . 157 475 29 ASP HA H 4.731 . . 158 475 29 ASP C C 175.586 . . 159 475 29 ASP CA C 54.314 . . 160 475 29 ASP CB C 41.532 . . 161 475 29 ASP N N 121.877 . . 162 476 30 TYR H H 8.112 . . 163 476 30 TYR HA H 4.686 . . 164 476 30 TYR C C 175.140 . . 165 476 30 TYR CA C 57.880 . . 166 476 30 TYR CB C 39.418 . . 167 476 30 TYR N N 121.365 . . 168 477 31 GLU H H 8.184 . . 169 477 31 GLU C C 173.887 . . 170 477 31 GLU CA C 53.826 . . 171 477 31 GLU CB C 30.439 . . 172 477 31 GLU N N 125.580 . . 173 478 32 PRO HA H 4.561 . . 174 478 32 PRO C C 177.154 . . 175 478 32 PRO CA C 63.170 . . 176 478 32 PRO CB C 32.267 . . 177 479 33 THR H H 8.323 . . 178 479 33 THR HA H 4.520 . . 179 479 33 THR C C 174.487 . . 180 479 33 THR CA C 61.625 . . 181 479 33 THR CB C 70.286 . . 182 479 33 THR N N 114.240 . . 183 480 34 ASP H H 8.404 . . 184 480 34 ASP HA H 4.703 . . 185 480 34 ASP C C 176.362 . . 186 480 34 ASP CA C 54.807 . . 187 480 34 ASP CB C 41.409 . . 188 480 34 ASP N N 122.682 . . 189 481 35 GLU H H 8.191 . . 190 481 35 GLU C C 176.389 . . 191 481 35 GLU CA C 56.840 . . 192 481 35 GLU CB C 30.576 . . 193 481 35 GLU N N 120.452 . . 194 482 36 ASP H H 8.368 . . 195 482 36 ASP HA H 4.774 . . 196 482 36 ASP C C 176.481 . . 197 482 36 ASP CA C 54.670 . . 198 482 36 ASP CB C 41.518 . . 199 482 36 ASP N N 121.448 . . 200 483 37 SER H H 8.219 . . 201 483 37 SER HA H 4.528 . . 202 483 37 SER C C 174.376 . . 203 483 37 SER CA C 58.508 . . 204 483 37 SER CB C 64.173 . . 205 483 37 SER N N 116.275 . . 206 484 38 ASP H H 8.390 . . 207 484 38 ASP HA H 4.776 . . 208 484 38 ASP C C 175.726 . . 209 484 38 ASP CA C 54.536 . . 210 484 38 ASP CB C 41.340 . . 211 484 38 ASP N N 122.303 . . 212 485 39 TRP H H 8.024 . . 213 485 39 TRP HA H 4.700 . . 214 485 39 TRP C C 175.503 . . 215 485 39 TRP CA C 57.872 . . 216 485 39 TRP CB C 29.955 . . 217 485 39 TRP N N 121.634 . . 218 486 40 GLU H H 7.794 . . 219 486 40 GLU C C 173.494 . . 220 486 40 GLU CA C 53.954 . . 221 486 40 GLU CB C 30.578 . . 222 486 40 GLU N N 125.062 . . 223 487 41 PRO HA H 4.284 . . 224 487 41 PRO C C 177.638 . . 225 487 41 PRO CA C 63.495 . . 226 487 41 PRO CB C 32.165 . . 227 488 42 GLY H H 8.550 . . 228 488 42 GLY HA2 H 4.059 . . 229 488 42 GLY HA3 H 4.059 . . 230 488 42 GLY C C 174.430 . . 231 488 42 GLY CA C 45.483 . . 232 488 42 GLY N N 109.392 . . 233 489 43 LYS H H 8.099 . . 234 489 43 LYS HA H 4.437 . . 235 489 43 LYS C C 176.991 . . 236 489 43 LYS CA C 56.606 . . 237 489 43 LYS CB C 33.229 . . 238 489 43 LYS N N 121.138 . . 239 490 44 GLU H H 8.639 . . 240 490 44 GLU HA H 4.402 . . 241 490 44 GLU C C 176.427 . . 242 490 44 GLU CA C 56.841 . . 243 490 44 GLU CB C 30.155 . . 244 490 44 GLU N N 121.891 . . 245 491 45 ASP H H 8.324 . . 246 491 45 ASP HA H 4.817 . . 247 491 45 ASP C C 176.345 . . 248 491 45 ASP CA C 54.622 . . 249 491 45 ASP CB C 41.547 . . 250 491 45 ASP N N 120.868 . . 251 492 46 GLU H H 8.260 . . 252 492 46 GLU HA H 4.391 . . 253 492 46 GLU C C 176.551 . . 254 492 46 GLU CA C 56.845 . . 255 492 46 GLU CB C 30.704 . . 256 492 46 GLU N N 121.077 . . 257 493 47 GLU H H 8.446 . . 258 493 47 GLU HA H 4.410 . . 259 493 47 GLU C C 176.430 . . 260 493 47 GLU CA C 56.688 . . 261 493 47 GLU CB C 30.270 . . 262 493 47 GLU N N 121.983 . . 263 494 48 LYS H H 8.271 . . 264 494 48 LYS HA H 4.438 . . 265 494 48 LYS C C 176.508 . . 266 494 48 LYS CA C 56.454 . . 267 494 48 LYS CB C 33.572 . . 268 494 48 LYS N N 122.730 . . 269 495 49 GLU H H 8.487 . . 270 495 49 GLU HA H 4.386 . . 271 495 49 GLU C C 176.546 . . 272 495 49 GLU CA C 56.608 . . 273 495 49 GLU CB C 30.709 . . 274 495 49 GLU N N 122.243 . . 275 496 50 ASP H H 8.391 . . 276 496 50 ASP HA H 4.780 . . 277 496 50 ASP C C 176.490 . . 278 496 50 ASP CA C 54.503 . . 279 496 50 ASP CB C 41.360 . . 280 496 50 ASP N N 122.119 . . 281 497 51 VAL H H 8.102 . . 282 497 51 VAL HA H 4.192 . . 283 497 51 VAL C C 176.676 . . 284 497 51 VAL CA C 63.183 . . 285 497 51 VAL CB C 32.678 . . 286 497 51 VAL N N 120.508 . . 287 498 52 GLU H H 8.430 . . 288 498 52 GLU HA H 4.317 . . 289 498 52 GLU C C 177.538 . . 290 498 52 GLU CA C 58.006 . . 291 498 52 GLU CB C 30.182 . . 292 498 52 GLU N N 123.041 . . 293 499 53 GLU H H 8.292 . . 294 499 53 GLU HA H 4.296 . . 295 499 53 GLU C C 177.416 . . 296 499 53 GLU CA C 57.986 . . 297 499 53 GLU CB C 30.111 . . 298 499 53 GLU N N 121.229 . . 299 500 54 LEU H H 8.108 . . 300 500 54 LEU HA H 4.367 . . 301 500 54 LEU C C 178.423 . . 302 500 54 LEU CA C 56.594 . . 303 500 54 LEU CB C 42.321 . . 304 500 54 LEU N N 121.574 . . 305 501 55 LEU H H 8.082 . . 306 501 55 LEU HA H 4.380 . . 307 501 55 LEU C C 178.126 . . 308 501 55 LEU CA C 56.193 . . 309 501 55 LEU CB C 42.141 . . 310 501 55 LEU N N 121.195 . . 311 502 56 LYS H H 8.008 . . 312 502 56 LYS HA H 4.275 . . 313 502 56 LYS C C 177.618 . . 314 502 56 LYS CA C 57.942 . . 315 502 56 LYS CB C 32.900 . . 316 502 56 LYS N N 120.838 . . 317 503 57 GLU H H 8.224 . . 318 503 57 GLU HA H 4.322 . . 319 503 57 GLU C C 176.869 . . 320 503 57 GLU CA C 57.375 . . 321 503 57 GLU CB C 30.155 . . 322 503 57 GLU N N 120.378 . . 323 504 58 ALA H H 8.109 . . 324 504 58 ALA HA H 4.374 . . 325 504 58 ALA C C 178.548 . . 326 504 58 ALA CA C 53.445 . . 327 504 58 ALA CB C 19.187 . . 328 504 58 ALA N N 123.587 . . 329 505 59 LYS H H 8.086 . . 330 505 59 LYS HA H 4.356 . . 331 505 59 LYS C C 177.102 . . 332 505 59 LYS CA C 56.987 . . 333 505 59 LYS CB C 32.820 . . 334 505 59 LYS N N 118.885 . . 335 506 60 ARG H H 8.002 . . 336 506 60 ARG HA H 4.324 . . 337 506 60 ARG C C 176.370 . . 338 506 60 ARG CA C 56.906 . . 339 506 60 ARG CB C 30.799 . . 340 506 60 ARG N N 120.480 . . 341 507 61 PHE H H 8.108 . . 342 507 61 PHE HA H 4.775 . . 343 507 61 PHE C C 175.724 . . 344 507 61 PHE CA C 57.916 . . 345 507 61 PHE CB C 39.618 . . 346 507 61 PHE N N 119.837 . . 347 508 62 MET H H 8.039 . . 348 508 62 MET HA H 4.546 . . 349 508 62 MET C C 175.697 . . 350 508 62 MET CA C 55.736 . . 351 508 62 MET CB C 33.348 . . 352 508 62 MET N N 121.453 . . 353 509 63 LYS H H 8.216 . . 354 509 63 LYS HA H 4.411 . . 355 509 63 LYS C C 176.299 . . 356 509 63 LYS CA C 56.575 . . 357 509 63 LYS CB C 33.198 . . 358 509 63 LYS N N 122.681 . . 359 510 64 ARG H H 8.341 . . 360 510 64 ARG HA H 4.454 . . 361 510 64 ARG C C 175.373 . . 362 510 64 ARG CA C 56.441 . . 363 510 64 ARG CB C 31.139 . . 364 510 64 ARG N N 123.292 . . 365 511 65 LYS H H 7.984 . . 366 511 65 LYS C C 175.351 . . 367 511 65 LYS CA C 58.040 . . 368 511 65 LYS CB C 33.911 . . 369 511 65 LYS N N 127.850 . . stop_ save_