data_30436 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of SH3 domain from Shank1 ; _BMRB_accession_number 30436 _BMRB_flat_file_name bmr30436.str _Entry_type original _Submission_date 2018-03-13 _Accession_date 2018-03-13 _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 Ishida H. . . 2 Vogel H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 58 "13C chemical shifts" 174 "15N chemical shifts" 58 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-05-03 update BMRB 'update entry citation' 2018-08-07 original author 'original release' stop_ _Original_release_date 2018-04-16 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30058071 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ishida Hiroaki . . 2 Skorobogatov Anton . . 3 Yamniuk Aaron P. . 4 Vogel Hans J. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 592 _Journal_issue 16 _Journal_ISSN 1873-3468 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2786 _Page_last 2797 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'SH3 and multiple ankyrin repeat domains protein 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 6626.528 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; MVPGRSFMAVKSYQAQAEGE ISLSKGEKIKVLSIGEGGFW EGQVKGRVGWFPSDCLEEVA N ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 553 MET 2 554 VAL 3 555 PRO 4 556 GLY 5 557 ARG 6 558 SER 7 559 PHE 8 560 MET 9 561 ALA 10 562 VAL 11 563 LYS 12 564 SER 13 565 TYR 14 566 GLN 15 567 ALA 16 568 GLN 17 569 ALA 18 570 GLU 19 571 GLY 20 572 GLU 21 573 ILE 22 574 SER 23 575 LEU 24 576 SER 25 577 LYS 26 578 GLY 27 579 GLU 28 580 LYS 29 581 ILE 30 582 LYS 31 583 VAL 32 584 LEU 33 585 SER 34 586 ILE 35 587 GLY 36 588 GLU 37 589 GLY 38 590 GLY 39 591 PHE 40 592 TRP 41 593 GLU 42 594 GLY 43 595 GLN 44 596 VAL 45 597 LYS 46 598 GLY 47 599 ARG 48 600 VAL 49 601 GLY 50 602 TRP 51 603 PHE 52 604 PRO 53 605 SER 54 606 ASP 55 607 CYS 56 608 LEU 57 609 GLU 58 610 GLU 59 611 VAL 60 612 ALA 61 613 ASN 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 _Gene_mnemonic $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens SHANK1 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 $entity_1 'recombinant technology' . Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 13C; U-99% 15N] Shank1 SH3 domain, 20 mM Bis-Tirs, 100 mM KCl, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' Bis-Tirs 20 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 15N] Shank1 SH3 domain, 20 mM Bis-Tris, 100 mM KCl, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 15N]' KCl 100 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details '1 mM Shank1 SH3 domain, 20 mM Bis-Tris, 100 mM KCl, 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM 'natural abundance' KCl 100 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 13C; U-99% 15N] Shank1 SH3 domain, 20 mM Bis-Tris, 100 mM KCl, 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' KCl 100 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _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_software_2 _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CYANA _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_2 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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_2D_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_3 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_4 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_C(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_11 _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' 100 . mM pH 6.8 0.1 pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' '2D NOESY' '3D 1H-13C NOESY' '3D 1H-15N NOESY' '3D C(CO)NH' '3D H(CCO)NH' '3D HBHA(CO)NH' stop_ loop_ _Sample_label $sample_2 $sample_1 $sample_3 $sample_4 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_1 _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 1 553 1 MET C C 175.426 . . 2 553 1 MET CA C 55.239 . . 3 553 1 MET CB C 32.407 . . 4 554 2 VAL H H 8.337 . . 5 554 2 VAL C C 175.363 . . 6 554 2 VAL CA C 61.679 . . 7 554 2 VAL CB C 32.993 . . 8 554 2 VAL N N 123.726 . . 9 555 3 PRO C C 177.186 . . 10 555 3 PRO CA C 63.435 . . 11 555 3 PRO CB C 31.236 . . 12 556 4 GLY H H 8.796 . . 13 556 4 GLY C C 174.279 . . 14 556 4 GLY CA C 45.287 . . 15 556 4 GLY N N 109.939 . . 16 557 5 ARG H H 7.959 . . 17 557 5 ARG C C 175.240 . . 18 557 5 ARG CA C 55.824 . . 19 557 5 ARG CB C 31.822 . . 20 557 5 ARG N N 120.661 . . 21 558 6 SER H H 8.387 . . 22 558 6 SER C C 172.827 . . 23 558 6 SER CA C 57.581 . . 24 558 6 SER CB C 64.606 . . 25 558 6 SER N N 116.458 . . 26 559 7 PHE H H 8.825 . . 27 559 7 PHE C C 174.252 . . 28 559 7 PHE CA C 56.995 . . 29 559 7 PHE CB C 44.701 . . 30 559 7 PHE N N 120.810 . . 31 560 8 MET H H 9.256 . . 32 560 8 MET C C 175.431 . . 33 560 8 MET CA C 53.483 . . 34 560 8 MET CB C 35.334 . . 35 560 8 MET N N 120.205 . . 36 561 9 ALA H H 8.940 . . 37 561 9 ALA C C 178.491 . . 38 561 9 ALA CA C 51.726 . . 39 561 9 ALA CB C 17.772 . . 40 561 9 ALA N N 125.963 . . 41 562 10 VAL H H 9.154 . . 42 562 10 VAL C C 174.571 . . 43 562 10 VAL CA C 61.093 . . 44 562 10 VAL CB C 31.822 . . 45 562 10 VAL N N 121.450 . . 46 563 11 LYS H H 7.751 . . 47 563 11 LYS C C 173.829 . . 48 563 11 LYS CA C 54.653 . . 49 563 11 LYS CB C 35.920 . . 50 563 11 LYS N N 120.116 . . 51 564 12 SER H H 8.278 . . 52 564 12 SER C C 173.062 . . 53 564 12 SER CA C 57.581 . . 54 564 12 SER CB C 64.332 . . 55 564 12 SER N N 113.967 . . 56 565 13 TYR H H 8.927 . . 57 565 13 TYR C C 173.974 . . 58 565 13 TYR CA C 58.751 . . 59 565 13 TYR CB C 42.945 . . 60 565 13 TYR N N 121.511 . . 61 566 14 GLN H H 7.535 . . 62 566 14 GLN C C 173.218 . . 63 566 14 GLN CA C 52.897 . . 64 566 14 GLN CB C 28.976 . . 65 566 14 GLN N N 128.429 . . 66 567 15 ALA H H 8.302 . . 67 567 15 ALA C C 178.694 . . 68 567 15 ALA CA C 53.483 . . 69 567 15 ALA CB C 19.528 . . 70 567 15 ALA N N 127.480 . . 71 568 16 GLN H H 9.113 . . 72 568 16 GLN C C 174.677 . . 73 568 16 GLN CA C 55.239 . . 74 568 16 GLN CB C 31.236 . . 75 568 16 GLN N N 120.199 . . 76 569 17 ALA H H 7.216 . . 77 569 17 ALA C C 177.014 . . 78 569 17 ALA CA C 50.555 . . 79 569 17 ALA CB C 21.869 . . 80 569 17 ALA N N 120.538 . . 81 570 18 GLU H H 8.743 . . 82 570 18 GLU C C 177.369 . . 83 570 18 GLU CA C 58.166 . . 84 570 18 GLU CB C 29.480 . . 85 570 18 GLU N N 121.703 . . 86 571 19 GLY H H 9.018 . . 87 571 19 GLY C C 175.043 . . 88 571 19 GLY CA C 45.287 . . 89 571 19 GLY N N 113.288 . . 90 572 20 GLU H H 7.796 . . 91 572 20 GLU C C 177.391 . . 92 572 20 GLU CA C 55.824 . . 93 572 20 GLU CB C 32.407 . . 94 572 20 GLU N N 118.837 . . 95 573 21 ILE H H 8.647 . . 96 573 21 ILE C C 173.827 . . 97 573 21 ILE CA C 59.337 . . 98 573 21 ILE CB C 41.189 . . 99 573 21 ILE N N 115.042 . . 100 574 22 SER H H 8.018 . . 101 574 22 SER C C 173.619 . . 102 574 22 SER CA C 57.581 . . 103 574 22 SER CB C 64.020 . . 104 574 22 SER N N 114.959 . . 105 575 23 LEU H H 9.285 . . 106 575 23 LEU C C 177.069 . . 107 575 23 LEU CA C 53.483 . . 108 575 23 LEU CB C 46.457 . . 109 575 23 LEU N N 120.075 . . 110 576 24 SER H H 9.029 . . 111 576 24 SER C C 172.799 . . 112 576 24 SER CA C 56.410 . . 113 576 24 SER CB C 64.218 . . 114 576 24 SER N N 119.068 . . 115 577 25 LYS H H 8.246 . . 116 577 25 LYS C C 177.104 . . 117 577 25 LYS CA C 58.751 . . 118 577 25 LYS CB C 32.407 . . 119 577 25 LYS N N 124.147 . . 120 578 26 GLY H H 9.064 . . 121 578 26 GLY C C 174.341 . . 122 578 26 GLY CA C 44.701 . . 123 578 26 GLY N N 114.471 . . 124 579 27 GLU H H 7.809 . . 125 579 27 GLU C C 174.970 . . 126 579 27 GLU CA C 56.995 . . 127 579 27 GLU CB C 30.651 . . 128 579 27 GLU N N 119.939 . . 129 580 28 LYS H H 8.390 . . 130 580 28 LYS C C 175.811 . . 131 580 28 LYS CA C 55.824 . . 132 580 28 LYS CB C 32.993 . . 133 580 28 LYS N N 121.657 . . 134 581 29 ILE H H 8.766 . . 135 581 29 ILE C C 174.987 . . 136 581 29 ILE CA C 59.337 . . 137 581 29 ILE CB C 41.189 . . 138 581 29 ILE N N 124.779 . . 139 582 30 LYS H H 8.196 . . 140 582 30 LYS C C 175.712 . . 141 582 30 LYS CA C 54.653 . . 142 582 30 LYS CB C 33.578 . . 143 582 30 LYS N N 127.554 . . 144 583 31 VAL H H 8.894 . . 145 583 31 VAL C C 175.282 . . 146 583 31 VAL CA C 64.020 . . 147 583 31 VAL CB C 31.822 . . 148 583 31 VAL N N 128.402 . . 149 584 32 LEU H H 9.551 . . 150 584 32 LEU C C 177.451 . . 151 584 32 LEU CA C 55.239 . . 152 584 32 LEU CB C 43.530 . . 153 584 32 LEU N N 128.246 . . 154 585 33 SER H H 7.668 . . 155 585 33 SER C C 171.062 . . 156 585 33 SER CA C 57.633 . . 157 585 33 SER CB C 64.606 . . 158 585 33 SER N N 111.589 . . 159 586 34 ILE H H 8.367 . . 160 586 34 ILE C C 176.332 . . 161 586 34 ILE CA C 60.508 . . 162 586 34 ILE CB C 38.261 . . 163 586 34 ILE N N 121.153 . . 164 587 35 GLY H H 8.058 . . 165 587 35 GLY C C 173.818 . . 166 587 35 GLY CA C 44.701 . . 167 587 35 GLY N N 114.680 . . 168 588 36 GLU H H 8.504 . . 169 588 36 GLU C C 178.427 . . 170 588 36 GLU CA C 55.824 . . 171 588 36 GLU CB C 30.651 . . 172 588 36 GLU N N 119.997 . . 173 589 37 GLY H H 8.981 . . 174 589 37 GLY C C 175.317 . . 175 589 37 GLY CA C 46.457 . . 176 589 37 GLY N N 109.301 . . 177 590 38 GLY H H 8.634 . . 178 590 38 GLY C C 173.829 . . 179 590 38 GLY CA C 44.701 . . 180 590 38 GLY N N 106.984 . . 181 591 39 PHE H H 7.686 . . 182 591 39 PHE C C 174.973 . . 183 591 39 PHE CA C 57.581 . . 184 591 39 PHE CB C 40.603 . . 185 591 39 PHE N N 120.477 . . 186 592 40 TRP H H 8.998 . . 187 592 40 TRP C C 171.759 . . 188 592 40 TRP CA C 52.897 . . 189 592 40 TRP CB C 32.993 . . 190 592 40 TRP N N 123.241 . . 191 593 41 GLU H H 8.293 . . 192 593 41 GLU C C 177.122 . . 193 593 41 GLU CA C 52.897 . . 194 593 41 GLU CB C 31.236 . . 195 593 41 GLU N N 122.317 . . 196 594 42 GLY H H 9.366 . . 197 594 42 GLY C C 169.198 . . 198 594 42 GLY CA C 45.460 . . 199 594 42 GLY N N 114.351 . . 200 595 43 GLN H H 8.976 . . 201 595 43 GLN C C 175.295 . . 202 595 43 GLN CA C 53.483 . . 203 595 43 GLN CB C 32.407 . . 204 595 43 GLN N N 118.039 . . 205 596 44 VAL H H 9.067 . . 206 596 44 VAL C C 174.232 . . 207 596 44 VAL CA C 60.508 . . 208 596 44 VAL CB C 33.578 . . 209 596 44 VAL N N 126.855 . . 210 597 45 LYS H H 9.328 . . 211 597 45 LYS C C 176.467 . . 212 597 45 LYS CA C 57.581 . . 213 597 45 LYS CB C 30.651 . . 214 597 45 LYS N N 126.429 . . 215 598 46 GLY H H 8.627 . . 216 598 46 GLY C C 174.044 . . 217 598 46 GLY CA C 45.287 . . 218 598 46 GLY N N 107.293 . . 219 599 47 ARG H H 8.411 . . 220 599 47 ARG C C 174.361 . . 221 599 47 ARG CA C 55.239 . . 222 599 47 ARG CB C 31.236 . . 223 599 47 ARG N N 122.521 . . 224 600 48 VAL H H 8.262 . . 225 600 48 VAL C C 175.861 . . 226 600 48 VAL CA C 59.922 . . 227 600 48 VAL CB C 34.749 . . 228 600 48 VAL N N 121.262 . . 229 601 49 GLY H H 8.696 . . 230 601 49 GLY C C 170.779 . . 231 601 49 GLY CA C 45.872 . . 232 601 49 GLY N N 113.110 . . 233 602 50 TRP H H 8.600 . . 234 602 50 TRP C C 176.320 . . 235 602 50 TRP CA C 56.995 . . 236 602 50 TRP CB C 31.822 . . 237 602 50 TRP N N 120.595 . . 238 603 51 PHE H H 8.816 . . 239 603 51 PHE C C 171.103 . . 240 603 51 PHE CA C 55.824 . . 241 603 51 PHE CB C 38.261 . . 242 603 51 PHE N N 115.661 . . 243 604 52 PRO C C 178.349 . . 244 604 52 PRO CA C 62.264 . . 245 604 52 PRO CB C 31.236 . . 246 605 53 SER H H 8.312 . . 247 605 53 SER C C 175.528 . . 248 605 53 SER CA C 59.443 . . 249 605 53 SER CB C 60.694 . . 250 605 53 SER N N 121.310 . . 251 606 54 ASP H H 7.864 . . 252 606 54 ASP C C 176.821 . . 253 606 54 ASP CA C 54.653 . . 254 606 54 ASP CB C 39.432 . . 255 606 54 ASP N N 119.864 . . 256 607 55 CYS H H 7.478 . . 257 607 55 CYS C C 173.934 . . 258 607 55 CYS CA C 61.093 . . 259 607 55 CYS CB C 27.724 . . 260 607 55 CYS N N 114.331 . . 261 608 56 LEU H H 7.570 . . 262 608 56 LEU C C 176.377 . . 263 608 56 LEU CA C 54.068 . . 264 608 56 LEU CB C 44.701 . . 265 608 56 LEU N N 118.313 . . 266 609 57 GLU H H 8.692 . . 267 609 57 GLU C C 174.755 . . 268 609 57 GLU CA C 55.239 . . 269 609 57 GLU CB C 32.993 . . 270 609 57 GLU N N 118.912 . . 271 610 58 GLU H H 8.807 . . 272 610 58 GLU C C 176.324 . . 273 610 58 GLU CA C 56.995 . . 274 610 58 GLU CB C 30.065 . . 275 610 58 GLU N N 124.487 . . 276 611 59 VAL H H 8.178 . . 277 611 59 VAL C C 175.211 . . 278 611 59 VAL CA C 61.093 . . 279 611 59 VAL CB C 32.993 . . 280 611 59 VAL N N 122.453 . . 281 612 60 ALA H H 8.428 . . 282 612 60 ALA C C 176.673 . . 283 612 60 ALA CA C 52.312 . . 284 612 60 ALA CB C 18.942 . . 285 612 60 ALA N N 128.065 . . 286 613 61 ASN H H 7.989 . . 287 613 61 ASN C C 179.528 . . 288 613 61 ASN CA C 54.653 . . 289 613 61 ASN CB C 40.603 . . 290 613 61 ASN N N 123.589 . . stop_ save_