data_11462 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; One-disulfide variant of hen lysozyme: 1SS[76-94] ; _BMRB_accession_number 11462 _BMRB_flat_file_name bmr11462.str _Entry_type original _Submission_date 2011-12-04 _Accession_date 2011-12-05 _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 Noda Yasuo . . 2 Narama Kuniaki . . 3 Kasai Kenichi . . 4 Murakami Shusaku . . 5 Tachibana Hideki . . 6 Segawa Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 117 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-04-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 11051 'Disulfide-free variant of hen lysozyme: 0SS' 11052 'Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80]' 11459 'One-disulfide variant of hen lysozyme: 1SS[6-127]' 11460 'One-disulfide variant of hen lysozyme: 1SS[30-115]' 11461 'One-disulfide variant of hen lysozyme: 1SS[64-80]' stop_ _Original_release_date 2013-04-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22344587 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Noda Yasuo . . 2 Narama Kuniaki . . 3 Kasai Kenichi . . 4 Tachibana Hideki . . 5 Segawa Shin-Ichi . . stop_ _Journal_abbreviation Biopolymers _Journal_name_full Biopolymers _Journal_volume 97 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 539 _Page_last 549 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 1SS[76-94] _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 1SS[76-94] $1SS-76-94 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_1SS-76-94 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 1SS[76-94] _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRSELAAAMKRHGLDN YRGYSLGNWVAAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWANDGRTPGSRNLCNIP ASALLSSDITASVNCAKKIV SDGNGMNAWVAWRNRAKGTD VQAWIRGARL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 LYS 3 2 VAL 4 3 PHE 5 4 GLY 6 5 ARG 7 6 SER 8 7 GLU 9 8 LEU 10 9 ALA 11 10 ALA 12 11 ALA 13 12 MET 14 13 LYS 15 14 ARG 16 15 HIS 17 16 GLY 18 17 LEU 19 18 ASP 20 19 ASN 21 20 TYR 22 21 ARG 23 22 GLY 24 23 TYR 25 24 SER 26 25 LEU 27 26 GLY 28 27 ASN 29 28 TRP 30 29 VAL 31 30 ALA 32 31 ALA 33 32 ALA 34 33 LYS 35 34 PHE 36 35 GLU 37 36 SER 38 37 ASN 39 38 PHE 40 39 ASN 41 40 THR 42 41 GLN 43 42 ALA 44 43 THR 45 44 ASN 46 45 ARG 47 46 ASN 48 47 THR 49 48 ASP 50 49 GLY 51 50 SER 52 51 THR 53 52 ASP 54 53 TYR 55 54 GLY 56 55 ILE 57 56 LEU 58 57 GLN 59 58 ILE 60 59 ASN 61 60 SER 62 61 ARG 63 62 TRP 64 63 TRP 65 64 ALA 66 65 ASN 67 66 ASP 68 67 GLY 69 68 ARG 70 69 THR 71 70 PRO 72 71 GLY 73 72 SER 74 73 ARG 75 74 ASN 76 75 LEU 77 76 CYS 78 77 ASN 79 78 ILE 80 79 PRO 81 80 ALA 82 81 SER 83 82 ALA 84 83 LEU 85 84 LEU 86 85 SER 87 86 SER 88 87 ASP 89 88 ILE 90 89 THR 91 90 ALA 92 91 SER 93 92 VAL 94 93 ASN 95 94 CYS 96 95 ALA 97 96 LYS 98 97 LYS 99 98 ILE 100 99 VAL 101 100 SER 102 101 ASP 103 102 GLY 104 103 ASN 105 104 GLY 106 105 MET 107 106 ASN 108 107 ALA 109 108 TRP 110 109 VAL 111 110 ALA 112 111 TRP 113 112 ARG 114 113 ASN 115 114 ARG 116 115 ALA 117 116 LYS 118 117 GLY 119 118 THR 120 119 ASP 121 120 VAL 122 121 GLN 123 122 ALA 124 123 TRP 125 124 ILE 126 125 ARG 127 126 GLY 128 127 ALA 129 128 ARG 130 129 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-06 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 BMRB 11051 0SS-variant 100.00 130 98.46 98.46 8.38e-86 BMRB 11459 1SS[6-127] 100.00 130 96.92 96.92 9.78e-84 BMRB 11460 1SS[30-115] 100.00 130 96.92 96.92 8.58e-84 BMRB 11461 1SS[64-80] 100.00 130 96.92 96.92 8.58e-84 BMRB 15198 all-Ala-Hen_egg_white_lysoyzme 100.00 130 97.69 98.46 2.88e-85 BMRB 18365 WT-ALA 99.23 129 97.67 98.45 2.67e-84 BMRB 18366 W28G 99.23 129 96.90 97.67 8.78e-83 BMRB 18367 W62G 99.23 129 96.90 97.67 8.78e-83 BMRB 18368 W108G 99.23 129 96.90 97.67 8.78e-83 BMRB 18369 W111G 99.23 129 96.90 97.67 8.78e-83 BMRB 18370 W123G 99.23 129 96.90 97.67 8.78e-83 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide 1SS[76-94] 77 CYS SG 1SS[76-94] 95 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $1SS-76-94 . . . . . . 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 $1SS-76-94 'recombinant technology' 'E. coli' Escherichia coli . pYK1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The pH was adjusted by adding DCl and NaOD' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $1SS-76-94 1 mM '[U-99% 15N]' 'dichloroacetic acid' 60 mM [U-2H] DMSO-d6 95 % [U-2H] H2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.114 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-15N_HSQC-NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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 298 . K pH* 5.5 . pH pressure 1 . atm 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 DMSO-d6 H 1 'methyl protons' ppm 2.55 internal direct . . . 1 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_ _Experiment_label '3D 1H-15N HSQC-NOESY-HSQC' '2D 1H-15N HSQC' 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 1SS[76-94] _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 1 2 LYS H H 8.63 0.02 1 2 1 2 LYS N N 122.19 0.1 1 3 2 3 VAL H H 7.96 0.02 1 4 2 3 VAL N N 116.38 0.1 1 5 3 4 PHE H H 8.16 0.02 1 6 3 4 PHE N N 119.95 0.1 1 7 4 5 GLY H H 8.29 0.02 1 8 4 5 GLY N N 106.19 0.1 1 9 5 6 ARG H H 8.19 0.02 1 10 5 6 ARG N N 118.08 0.1 1 11 6 7 SER H H 8.23 0.02 1 12 6 7 SER N N 114.67 0.1 1 13 7 8 GLU H H 8.24 0.02 1 14 7 8 GLU N N 120.16 0.1 1 15 8 9 LEU H H 8.00 0.02 1 16 8 9 LEU N N 118.82 0.1 1 17 9 10 ALA H H 8.07 0.02 1 18 9 10 ALA N N 120.88 0.1 1 19 10 11 ALA H H 7.94 0.02 1 20 10 11 ALA N N 118.85 0.1 1 21 11 12 ALA H H 7.98 0.02 1 22 11 12 ALA N N 118.92 0.1 1 23 12 13 MET H H 7.95 0.02 1 24 12 13 MET N N 115.53 0.1 1 25 13 14 LYS H H 7.90 0.02 1 26 13 14 LYS N N 117.71 0.1 1 27 14 15 ARG H H 8.02 0.02 1 28 14 15 ARG N N 117.99 0.1 1 29 15 16 HIS H H 8.16 0.02 1 30 15 16 HIS N N 115.76 0.1 1 31 16 17 GLY H H 8.32 0.02 1 32 16 17 GLY N N 106.73 0.1 1 33 17 18 LEU H H 8.18 0.02 1 34 17 18 LEU N N 118.89 0.1 1 35 18 19 ASP H H 8.35 0.02 1 36 18 19 ASP N N 117.43 0.1 1 37 19 20 ASN H H 8.04 0.02 1 38 19 20 ASN N N 116.59 0.1 1 39 20 21 TYR H H 7.85 0.02 1 40 20 21 TYR N N 116.79 0.1 1 41 21 22 ARG H H 8.12 0.02 1 42 21 22 ARG N N 118.09 0.1 1 43 22 23 GLY H H 7.99 0.02 1 44 22 23 GLY N N 106.01 0.1 1 45 23 24 TYR H H 8.04 0.02 1 46 23 24 TYR N N 116.59 0.1 1 47 24 25 SER H H 8.28 0.02 1 48 24 25 SER N N 114.39 0.1 1 49 25 26 LEU H H 8.14 0.02 1 50 25 26 LEU N N 120.81 0.1 1 51 26 27 GLY H H 8.19 0.02 1 52 26 27 GLY N N 105.41 0.1 1 53 27 28 ASN H H 8.12 0.02 1 54 27 28 ASN N N 117.05 0.1 1 55 28 29 TRP H H 8.16 0.02 1 56 28 29 TRP N N 119.48 0.1 1 57 29 30 VAL H H 7.85 0.02 1 58 29 30 VAL N N 115.84 0.1 1 59 30 31 ALA H H 7.98 0.02 1 60 30 31 ALA N N 122.70 0.1 1 61 31 32 ALA H H 7.90 0.02 1 62 31 32 ALA N N 119.00 0.1 1 63 32 33 ALA H H 7.95 0.02 1 64 32 33 ALA N N 119.21 0.1 1 65 33 34 LYS H H 7.86 0.02 1 66 33 34 LYS N N 116.02 0.1 1 67 34 35 PHE H H 7.93 0.02 1 68 34 35 PHE N N 116.20 0.1 1 69 35 36 GLU H H 8.09 0.02 1 70 35 36 GLU N N 117.34 0.1 1 71 36 37 SER H H 7.94 0.02 1 72 36 37 SER N N 113.45 0.1 1 73 37 38 ASN H H 8.21 0.02 1 74 37 38 ASN N N 118.75 0.1 1 75 38 39 PHE H H 8.08 0.02 1 76 38 39 PHE N N 116.30 0.1 1 77 39 40 ASN H H 8.35 0.02 1 78 39 40 ASN N N 117.89 0.1 1 79 40 41 THR H H 7.76 0.02 1 80 40 41 THR N N 111.23 0.1 1 81 41 42 GLN H H 8.02 0.02 1 82 41 42 GLN N N 118.43 0.1 1 83 42 43 ALA H H 8.00 0.02 1 84 42 43 ALA N N 121.35 0.1 1 85 43 44 THR H H 7.76 0.02 1 86 43 44 THR N N 109.67 0.1 1 87 44 45 ASN H H 8.10 0.02 1 88 44 45 ASN N N 118.62 0.1 1 89 45 46 ARG H H 8.04 0.02 1 90 45 46 ARG N N 117.59 0.1 1 91 46 47 ASN H H 8.27 0.02 1 92 46 47 ASN N N 117.79 0.1 1 93 47 48 THR H H 7.74 0.02 1 94 47 48 THR N N 110.75 0.1 1 95 48 49 ASP H H 8.28 0.02 1 96 48 49 ASP N N 118.24 0.1 1 97 49 50 GLY H H 8.00 0.02 1 98 49 50 GLY N N 105.07 0.1 1 99 50 51 SER H H 7.96 0.02 1 100 50 51 SER N N 112.82 0.1 1 101 51 52 THR H H 7.87 0.02 1 102 51 52 THR N N 112.16 0.1 1 103 52 53 ASP H H 8.22 0.02 1 104 52 53 ASP N N 118.48 0.1 1 105 53 54 TYR H H 7.90 0.02 1 106 53 54 TYR N N 116.86 0.1 1 107 54 55 GLY H H 8.19 0.02 1 108 54 55 GLY N N 106.29 0.1 1 109 55 56 ILE H H 7.81 0.02 1 110 55 56 ILE N N 116.00 0.1 1 111 56 57 LEU H H 8.08 0.02 1 112 56 57 LEU N N 121.90 0.1 1 113 57 58 GLN H H 8.02 0.02 1 114 57 58 GLN N N 118.72 0.1 1 115 58 59 ILE H H 7.81 0.02 1 116 58 59 ILE N N 116.89 0.1 1 117 59 60 ASN H H 8.27 0.02 1 118 59 60 ASN N N 120.61 0.1 1 119 60 61 SER H H 7.98 0.02 1 120 60 61 SER N N 114.24 0.1 1 121 61 62 ARG H H 8.16 0.02 1 122 61 62 ARG N N 119.48 0.1 1 123 62 63 TRP H H 7.91 0.02 1 124 62 63 TRP N N 117.97 0.1 1 125 63 64 TRP H H 7.96 0.02 1 126 63 64 TRP N N 118.57 0.1 1 127 64 65 ALA H H 8.02 0.02 1 128 64 65 ALA N N 121.17 0.1 1 129 65 66 ASN H H 8.18 0.02 1 130 65 66 ASN N N 115.83 0.1 1 131 66 67 ASP H H 8.32 0.02 1 132 66 67 ASP N N 117.52 0.1 1 133 67 68 GLY H H 8.24 0.02 1 134 67 68 GLY N N 104.96 0.1 1 135 68 69 ARG H H 7.84 0.02 1 136 68 69 ARG N N 116.84 0.1 1 137 71 72 GLY H H 8.21 0.02 1 138 71 72 GLY N N 105.23 0.1 1 139 72 73 SER H H 7.92 0.02 1 140 72 73 SER N N 112.75 0.1 1 141 73 74 ARG H H 8.18 0.02 1 142 73 74 ARG N N 119.52 0.1 1 143 80 81 ALA H H 8.33 0.02 1 144 80 81 ALA N N 121.37 0.1 1 145 81 82 SER H H 7.92 0.02 1 146 81 82 SER N N 110.41 0.1 1 147 82 83 ALA H H 8.00 0.02 1 148 82 83 ALA N N 122.12 0.1 1 149 83 84 LEU H H 7.79 0.02 1 150 83 84 LEU N N 116.30 0.1 1 151 84 85 LEU H H 7.76 0.02 1 152 84 85 LEU N N 117.43 0.1 1 153 85 86 SER H H 7.84 0.02 1 154 85 86 SER N N 112.58 0.1 1 155 86 87 SER H H 7.90 0.02 1 156 86 87 SER N N 114.39 0.1 1 157 87 88 ASP H H 8.28 0.02 1 158 87 88 ASP N N 118.73 0.1 1 159 88 89 ILE H H 7.65 0.02 1 160 88 89 ILE N N 115.54 0.1 1 161 89 90 THR H H 7.86 0.02 1 162 89 90 THR N N 114.77 0.1 1 163 90 91 ALA H H 7.90 0.02 1 164 90 91 ALA N N 122.04 0.1 1 165 91 92 SER H H 8.09 0.02 1 166 91 92 SER N N 112.76 0.1 1 167 92 93 VAL H H 7.77 0.02 1 168 92 93 VAL N N 116.41 0.1 1 169 93 94 ASN H H 8.23 0.02 1 170 93 94 ASN N N 118.95 0.1 1 171 98 99 ILE H H 7.93 0.02 1 172 98 99 ILE N N 117.69 0.1 1 173 99 100 VAL H H 7.91 0.02 1 174 99 100 VAL N N 118.28 0.1 1 175 100 101 SER H H 7.94 0.02 1 176 100 101 SER N N 115.41 0.1 1 177 101 102 ASP H H 8.38 0.02 1 178 101 102 ASP N N 119.47 0.1 1 179 102 103 GLY H H 8.10 0.02 1 180 102 103 GLY N N 105.32 0.1 1 181 103 104 ASN H H 8.15 0.02 1 182 103 104 ASN N N 116.74 0.1 1 183 104 105 GLY H H 8.24 0.02 1 184 104 105 GLY N N 106.25 0.1 1 185 105 106 MET H H 8.06 0.02 1 186 105 106 MET N N 116.40 0.1 1 187 106 107 ASN H H 8.21 0.02 1 188 106 107 ASN N N 117.65 0.1 1 189 107 108 ALA H H 8.20 0.02 1 190 107 108 ALA N N 121.65 0.1 1 191 108 109 TRP H H 8.15 0.02 1 192 108 109 TRP N N 117.04 0.1 1 193 109 110 VAL H H 7.68 0.02 1 194 109 110 VAL N N 115.33 0.1 1 195 110 111 ALA H H 7.99 0.02 1 196 110 111 ALA N N 122.78 0.1 1 197 111 112 TRP H H 7.97 0.02 1 198 111 112 TRP N N 117.43 0.1 1 199 112 113 ARG H H 8.06 0.02 1 200 112 113 ARG N N 117.90 0.1 1 201 113 114 ASN H H 8.14 0.02 1 202 113 114 ASN N N 117.38 0.1 1 203 114 115 ARG H H 8.02 0.02 1 204 114 115 ARG N N 117.99 0.1 1 205 115 116 ALA H H 8.05 0.02 1 206 115 116 ALA N N 120.69 0.1 1 207 116 117 LYS H H 7.93 0.02 1 208 116 117 LYS N N 116.50 0.1 1 209 117 118 GLY H H 8.11 0.02 1 210 117 118 GLY N N 105.98 0.1 1 211 118 119 THR H H 7.86 0.02 1 212 118 119 THR N N 110.66 0.1 1 213 119 120 ASP H H 8.33 0.02 1 214 119 120 ASP N N 119.56 0.1 1 215 120 121 VAL H H 7.74 0.02 1 216 120 121 VAL N N 115.28 0.1 1 217 121 122 GLN H H 8.12 0.02 1 218 121 122 GLN N N 120.41 0.1 1 219 122 123 ALA H H 7.93 0.02 1 220 122 123 ALA N N 120.59 0.1 1 221 123 124 TRP H H 8.09 0.02 1 222 123 124 TRP N N 118.07 0.1 1 223 124 125 ILE H H 7.85 0.02 1 224 124 125 ILE N N 116.79 0.1 1 225 125 126 ARG H H 8.09 0.02 1 226 125 126 ARG N N 121.18 0.1 1 227 126 127 GLY H H 8.20 0.02 1 228 126 127 GLY N N 106.73 0.1 1 229 127 128 ALA H H 8.01 0.02 1 230 127 128 ALA N N 120.29 0.1 1 231 128 129 ARG H H 8.09 0.02 1 232 128 129 ARG N N 116.96 0.1 1 233 129 130 LEU H H 8.11 0.02 1 234 129 130 LEU N N 119.11 0.1 1 stop_ save_