data_15879 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Protein folding on a highly rugged landscape: Experimental observation of glassy dynamics and structural frustration ; _BMRB_accession_number 15879 _BMRB_flat_file_name bmr15879.str _Entry_type new _Submission_date 2008-07-18 _Accession_date 2008-07-18 _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 Sadqi Mourad . . 2 'de Alba' Eva . . 3 Perez-Jimenez Raul . . 4 Sanchez-Ruiz Jose M. . 5 Munoz Victor . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 198 "13C chemical shifts" 23 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-02 update BMRB 'edit assembly name' 2010-04-22 update BMRB 'update atom names of NAL' 2009-03-23 update BMRB 'complete entry citation' 2009-03-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A designed protein as experimental model of primordial folding' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19240216 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sadqi Mourad . . 2 'de Alba' Eva . . 3 Perez-Jimenez Raul . . 4 Sanchez-Ruiz Jose M. . 5 Munoz Victor . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. U.S.A.' _Journal_volume 106 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4127 _Page_last 4132 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FSD_mod _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FSD_mod $FSD_mod 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_FSD_mod _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FSD_mod _Molecular_mass 3854.456 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 29 _Mol_residue_sequence ; GQQYTAXIKGRTFRNEKELR DFIEKFXGR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLN 3 GLN 4 TYR 5 THR 6 ALA 7 NAL 8 ILE 9 LYS 10 GLY 11 ARG 12 THR 13 PHE 14 ARG 15 ASN 16 GLU 17 LYS 18 GLU 19 LEU 20 ARG 21 ASP 22 PHE 23 ILE 24 GLU 25 LYS 26 PHE 27 DNS 28 GLY 29 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-23 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 PDB 2K6R "Protein Folding On A Highly Rugged Landscape: Experimental Observation Of Glassy Dynamics And Structural Frustration" 100.00 29 100.00 100.00 1.01e-08 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NAL _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common BETA-(2-NAPHTHYL)-ALANINE _BMRB_code . _PDB_code NAL _Standard_residue_derivative NAL _Molecular_mass 215.248 _Mol_paramagnetic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 20:02:23 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C N 0 . ? C2 C2 C N 0 . ? C3 C3 C N 0 . ? C4 C4 C N 0 . ? C4A C4A C N 0 . ? C5 C5 C N 0 . ? C6 C6 C N 0 . ? C7 C7 C N 0 . ? C8 C8 C N 0 . ? C8A C8A C N 0 . ? C9 C9 C N 0 . ? C10 C10 C S 0 . ? C11 C11 C N 0 . ? N N N N 0 . ? O2 O2 O N 0 . ? OXT OXT O N 0 . ? H1 H1 H N 0 . ? H3 H3 H N 0 . ? H4 H4 H N 0 . ? H5 H5 H N 0 . ? H6 H6 H N 0 . ? H7 H7 H N 0 . ? H8 H8 H N 0 . ? H91 H91 H N 0 . ? H92 H92 H N 0 . ? H10 H10 H N 0 . ? HN1 HN1 H N 0 . ? HN2 HN2 H N 0 . ? HXT HXT H N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C6 C5 ? ? SING C6 C7 ? ? SING C5 C4A ? ? DOUB C7 C8 ? ? DOUB C4A C4 ? ? SING C4A C8A ? ? SING C8 C8A ? ? SING C4 C3 ? ? DOUB C8A C1 ? ? DOUB C3 C2 ? ? SING C1 C2 ? ? SING C2 C9 ? ? SING C9 C10 ? ? SING C10 N ? ? SING C10 C11 ? ? DOUB C11 O2 ? ? SING C11 OXT ? ? SING C1 H1 ? ? SING C3 H3 ? ? SING C4 H4 ? ? SING C5 H5 ? ? SING C6 H6 ? ? SING C7 H7 ? ? SING C8 H8 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 H10 ? ? SING N HN1 ? ? SING N HN2 ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_DNS _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N~6~-{[5-(DIMETHYLAMINO)-1-NAPHTHYL]SULFONYL}-L-LYSINE _BMRB_code . _PDB_code DNS _Standard_residue_derivative DNS _Molecular_mass 379.474 _Mol_paramagnetic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 18:40:39 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C N 0 . ? N1 N1 N N 0 . ? C2 C2 C N 0 . ? C3 C3 C N 0 . ? C4 C4 C N 0 . ? C5 C5 C N 0 . ? C6 C6 C N 0 . ? C7 C7 C N 0 . ? C8 C8 C N 0 . ? S S S N 0 . ? OA OA O N 0 . ? OB OB O N 0 . ? NZ NZ N N 0 . ? CE CE C N 0 . ? CD CD C N 0 . ? CG CG C N 0 . ? CB CB C N 0 . ? CA CA C S 0 . ? C C C N 0 . ? OXT OXT O N 0 . ? O O O N 0 . ? N N N N 0 . ? C9 C9 C N 0 . ? C10 C10 C N 0 . ? C11 C11 C N 0 . ? C12 C12 C N 0 . ? H11A H11A H N 0 . ? H12 H12 H N 0 . ? H13 H13 H N 0 . ? H21 H21 H N 0 . ? H22 H22 H N 0 . ? H23 H23 H N 0 . ? H4 H4 H N 0 . ? H5 H5 H N 0 . ? H6 H6 H N 0 . ? HZ HZ H N 0 . ? HE3 HE3 H N 0 . ? HE2 HE2 H N 0 . ? HD3 HD3 H N 0 . ? HD2 HD2 H N 0 . ? HG3 HG3 H N 0 . ? HG2 HG2 H N 0 . ? HB3 HB3 H N 0 . ? HB2 HB2 H N 0 . ? HA HA H N 0 . ? HO HO H N 0 . ? H H H N 0 . ? H2 H2 H N 0 . ? H9 H9 H N 0 . ? H10 H10 H N 0 . ? H11 H11 H N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 N1 ? ? SING C1 H11A ? ? SING C1 H12 ? ? SING C1 H13 ? ? SING N1 C2 ? ? SING N1 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C2 H23 ? ? SING C3 C4 ? ? DOUB C3 C12 ? ? DOUB C4 C5 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 H5 ? ? DOUB C6 C7 ? ? SING C6 H6 ? ? SING C7 C8 ? ? SING C7 C12 ? ? SING C8 S ? ? DOUB C8 C9 ? ? DOUB S OA ? ? DOUB S OB ? ? SING S NZ ? ? SING NZ CE ? ? SING NZ HZ ? ? SING CE CD ? ? SING CE HE3 ? ? SING CE HE2 ? ? SING CD CG ? ? SING CD HD3 ? ? SING CD HD2 ? ? SING CG CB ? ? SING CG HG3 ? ? SING CG HG2 ? ? SING CB CA ? ? SING CB HB3 ? ? SING CB HB2 ? ? SING CA C ? ? SING CA N ? ? SING CA HA ? ? SING C OXT ? ? DOUB C O ? ? SING OXT HO ? ? SING N H ? ? SING N H2 ? ? SING C9 C10 ? ? SING C9 H9 ? ? DOUB C10 C11 ? ? SING C10 H10 ? ? SING C11 C12 ? ? SING C11 H11 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FSD_mod . . . . . . 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 $FSD_mod 'chemical synthesis' . . . . . 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 $FSD_mod 1 mM 'natural abundance' DSS 0.05 mM 'natural abundance' D2O 10 % '[U-99.9% 2H]' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' 'data analysis' 'chemical shift assignment' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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 temperature 323 . K pH 5.0 . pH pressure 1 . atm 'ionic strength' 0 . M 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 H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS C 13 'methyl carbon' ppm 0 internal 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-1H TOCSY' '2D 1H-1H NOESY' '2D DQF-COSY' 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 FSD_mod _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 2 GLN HA H 4.431 . 1 2 2 2 GLN CA C 55.356 . 1 3 3 3 GLN H H 8.498 . 1 4 3 3 GLN HA H 4.389 . 1 5 3 3 GLN HB2 H 2.041 . . 6 3 3 GLN HB3 H 1.973 . . 7 3 3 GLN HG2 H 2.337 . . 8 3 3 GLN HG3 H 2.337 . . 9 3 3 GLN CA C 56.006 . 1 10 4 4 TYR H H 8.236 . 1 11 4 4 TYR HA H 4.599 . 1 12 4 4 TYR HB2 H 3.055 . . 13 4 4 TYR HB3 H 2.974 . . 14 4 4 TYR HD1 H 7.061 . . 15 4 4 TYR HD2 H 7.061 . . 16 4 4 TYR HE1 H 6.804 . . 17 4 4 TYR HE2 H 6.804 . . 18 5 5 THR H H 7.881 . 1 19 5 5 THR HA H 4.216 . 1 20 5 5 THR HB H 4.144 . 1 21 5 5 THR HG2 H 1.128 . . 22 5 5 THR CA C 62.394 . 1 23 6 6 ALA H H 7.992 . 1 24 6 6 ALA HA H 4.332 . 1 25 6 6 ALA HB H 1.339 . . 26 6 6 ALA CA C 52.838 . 1 27 7 7 NAL H1 H 7.650 . . 28 7 7 NAL H3 H 7.308 . . 29 7 7 NAL H4 H 7.754 . . 30 7 7 NAL H8 H 7.754 . . 31 7 7 NAL H10 H 4.781 . . 32 7 7 NAL H91 H 3.273 . . 33 7 7 NAL H92 H 3.273 . . 34 7 7 NAL H H 7.992 . 1 35 7 7 NAL C10 C 58.007 . . 36 8 8 ILE H H 7.747 . 1 37 8 8 ILE HA H 4.166 . 1 38 8 8 ILE HB H 1.800 . 1 39 8 8 ILE HD1 H 0.724 . . 40 8 8 ILE HG12 H 1.361 . . 41 8 8 ILE HG13 H 1.058 . . 42 8 8 ILE HG2 H 0.823 . . 43 8 8 ILE CA C 60.997 . 1 44 9 9 LYS H H 8.044 . 1 45 9 9 LYS HA H 4.143 . 1 46 9 9 LYS HB2 H 1.847 . . 47 9 9 LYS HB3 H 1.763 . . 48 9 9 LYS HD2 H 1.714 . . 49 9 9 LYS HD3 H 1.714 . . 50 9 9 LYS HE2 H 3.015 . . 51 9 9 LYS HE3 H 3.015 . . 52 9 9 LYS HG2 H 1.458 . . 53 9 9 LYS HG3 H 1.418 . . 54 9 9 LYS CA C 56.732 . 1 55 10 10 GLY H H 8.197 . 1 56 10 10 GLY HA2 H 4.015 . . 57 10 10 GLY HA3 H 3.854 . . 58 10 10 GLY CA C 45.352 . 1 59 11 11 ARG H H 7.769 . 1 60 11 11 ARG HA H 4.357 . 1 61 11 11 ARG HB2 H 1.575 . . 62 11 11 ARG HB3 H 1.575 . . 63 11 11 ARG HD2 H 2.910 . . 64 11 11 ARG HD3 H 2.910 . . 65 11 11 ARG HE H 6.975 . 1 66 11 11 ARG HG2 H 1.333 . . 67 11 11 ARG HG3 H 1.333 . . 68 11 11 ARG CA C 55.356 . 1 69 12 12 THR H H 7.891 . 1 70 12 12 THR HA H 4.352 . 1 71 12 12 THR HB H 4.000 . 1 72 12 12 THR HG2 H 1.050 . . 73 12 12 THR CA C 61.230 . 1 74 13 13 PHE H H 8.194 . 1 75 13 13 PHE HA H 4.806 . 1 76 13 13 PHE HB2 H 3.159 . . 77 13 13 PHE HB3 H 2.908 . . 78 13 13 PHE HD1 H 7.147 . . 79 13 13 PHE HD2 H 7.147 . . 80 13 13 PHE HE1 H 6.939 . . 81 13 13 PHE HE2 H 6.939 . . 82 13 13 PHE HZ H 6.347 . 1 83 13 13 PHE CA C 56.923 . 1 84 14 14 ARG H H 9.143 . 1 85 14 14 ARG HA H 4.285 . 1 86 14 14 ARG HB2 H 1.947 . . 87 14 14 ARG HB3 H 1.857 . . 88 14 14 ARG HD2 H 3.271 . . 89 14 14 ARG HD3 H 3.271 . . 90 14 14 ARG HG2 H 1.836 . . 91 14 14 ARG HG3 H 1.790 . . 92 14 14 ARG CA C 57.406 . 1 93 15 15 ASN H H 7.696 . 1 94 15 15 ASN HA H 4.724 . 1 95 15 15 ASN HB2 H 3.225 . . 96 15 15 ASN HB3 H 3.100 . . 97 15 15 ASN HD21 H 7.574 . . 98 15 15 ASN HD22 H 6.895 . . 99 16 16 GLU H H 8.884 . 1 100 16 16 GLU HA H 3.998 . 1 101 16 16 GLU HB2 H 2.130 . . 102 16 16 GLU HB3 H 2.130 . . 103 16 16 GLU HG2 H 2.383 . . 104 16 16 GLU HG3 H 2.383 . . 105 16 16 GLU CA C 59.272 . 1 106 17 17 LYS H H 8.121 . 1 107 17 17 LYS HA H 4.035 . 1 108 17 17 LYS HB2 H 1.938 . . 109 17 17 LYS HB3 H 1.938 . . 110 17 17 LYS HE2 H 3.093 . . 111 17 17 LYS HE3 H 3.093 . . 112 17 17 LYS HG2 H 1.513 . . 113 17 17 LYS HG3 H 1.513 . . 114 17 17 LYS CA C 59.341 . 1 115 18 18 GLU H H 8.173 . 1 116 18 18 GLU HA H 4.228 . 1 117 18 18 GLU HB2 H 2.343 . . 118 18 18 GLU HB3 H 2.245 . . 119 18 18 GLU HG2 H 2.682 . . 120 18 18 GLU HG3 H 2.504 . . 121 18 18 GLU CA C 59.143 . 1 122 19 19 LEU H H 7.383 . 1 123 19 19 LEU HA H 3.646 . 1 124 19 19 LEU HB2 H 1.817 . . 125 19 19 LEU HB3 H 1.350 . . 126 19 19 LEU HD1 H 0.674 . . 127 19 19 LEU HD2 H 0.482 . . 128 19 19 LEU HG H 1.209 . 1 129 19 19 LEU CA C 57.594 . 1 130 20 20 ARG H H 8.353 . 1 131 20 20 ARG HA H 3.854 . 1 132 20 20 ARG HB2 H 1.993 . . 133 20 20 ARG HB3 H 1.993 . . 134 20 20 ARG HD2 H 3.188 . . 135 20 20 ARG HD3 H 3.188 . . 136 20 20 ARG HG2 H 1.775 . . 137 20 20 ARG HG3 H 1.625 . . 138 20 20 ARG CA C 59.831 . 1 139 21 21 ASP H H 8.481 . 1 140 21 21 ASP HA H 4.395 . 1 141 21 21 ASP HB2 H 2.881 . . 142 21 21 ASP HB3 H 2.730 . . 143 21 21 ASP CA C 57.083 . 1 144 22 22 PHE H H 7.803 . 1 145 22 22 PHE HA H 4.315 . 1 146 22 22 PHE HB2 H 3.368 . . 147 22 22 PHE HB3 H 3.250 . . 148 22 22 PHE HD1 H 7.152 . . 149 22 22 PHE HD2 H 7.152 . . 150 22 22 PHE HE1 H 6.945 . . 151 22 22 PHE HE2 H 6.945 . . 152 23 23 ILE H H 8.248 . 1 153 23 23 ILE HA H 3.406 . 1 154 23 23 ILE HB H 1.828 . 1 155 23 23 ILE HD1 H 0.484 . . 156 23 23 ILE HG12 H 1.589 . . 157 23 23 ILE HG13 H 1.000 . . 158 23 23 ILE HG2 H 0.552 . . 159 23 23 ILE CA C 64.236 . 1 160 24 24 GLU H H 8.306 . 1 161 24 24 GLU HA H 3.912 . 1 162 24 24 GLU HB2 H 2.176 . . 163 24 24 GLU HB3 H 2.096 . . 164 24 24 GLU HG2 H 2.507 . . 165 24 24 GLU HG3 H 2.323 . . 166 24 24 GLU CA C 59.215 . 1 167 25 25 LYS H H 7.605 . 1 168 25 25 LYS HA H 4.055 . 1 169 25 25 LYS HB2 H 1.738 . . 170 25 25 LYS HB3 H 1.591 . . 171 25 25 LYS HD2 H 1.738 . . 172 25 25 LYS HD3 H 1.738 . . 173 25 25 LYS HE2 H 2.950 . . 174 25 25 LYS HE3 H 2.950 . . 175 25 25 LYS HG2 H 1.407 . . 176 25 25 LYS HG3 H 1.273 . . 177 25 25 LYS CA C 58.116 . 1 178 26 26 PHE H H 7.885 . 1 179 26 26 PHE HA H 4.317 . 1 180 26 26 PHE HB2 H 2.886 . . 181 26 26 PHE HB3 H 2.574 . . 182 26 26 PHE HD1 H 6.959 . . 183 26 26 PHE HD2 H 6.959 . . 184 26 26 PHE HE1 H 5.821 . . 185 26 26 PHE HE2 H 5.821 . . 186 27 27 DNS H11A H 2.447 . . 187 27 27 DNS H12 H 2.447 . . 188 27 27 DNS H13 H 2.447 . . 189 27 27 DNS H21 H 2.447 . . 190 27 27 DNS H22 H 2.447 . . 191 27 27 DNS H23 H 2.447 . . 192 27 27 DNS H4 H 8.069 . . 193 27 27 DNS H5 H 7.198 . . 194 27 27 DNS H6 H 7.644 . . 195 27 27 DNS HZ H 6.953 . . 196 27 27 DNS H9 H 7.408 . . 197 27 27 DNS H10 H 7.292 . . 198 27 27 DNS HA H 4.165 . . 199 27 27 DNS HB2 H 1.779 . . 200 27 27 DNS HB3 H 1.706 . . 201 27 27 DNS HD2 H 1.706 . . 202 27 27 DNS HD3 H 1.706 . . 203 27 27 DNS HE2 H 2.773 . . 204 27 27 DNS HE3 H 2.773 . . 205 27 27 DNS HG2 H 1.266 . . 206 27 27 DNS HG3 H 1.133 . . 207 27 27 DNS H H 7.846 . 1 208 27 27 DNS CA C 56.733 . . 209 28 28 GLY H H 7.788 . 1 210 28 28 GLY HA2 H 3.985 . . 211 28 28 GLY HA3 H 3.985 . . 212 28 28 GLY CA C 45.405 . 1 213 29 29 ARG H H 7.647 . 1 214 29 29 ARG HA H 4.242 . 1 215 29 29 ARG HB2 H 1.900 . . 216 29 29 ARG HB3 H 1.745 . . 217 29 29 ARG HD2 H 3.199 . . 218 29 29 ARG HD3 H 3.199 . . 219 29 29 ARG HE H 7.217 . 1 220 29 29 ARG HG2 H 1.625 . . 221 29 29 ARG HG3 H 1.625 . . stop_ save_