data_11459 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; One-disulfide variant of hen lysozyme: 1SS[6-127] ; _BMRB_accession_number 11459 _BMRB_flat_file_name bmr11459.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" 443 "15N chemical shifts" 125 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]' 11460 'One-disulfide variant of hen lysozyme: 1SS[30-115]' 11461 'One-disulfide variant of hen lysozyme: 1SS[64-80]' 11462 'One-disulfide variant of hen lysozyme: 1SS[76-94]' 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[6-127] _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 1SS[6-127] $1SS-6-127 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-6-127 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 1SS[6-127] _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRCELAAAMKRHGLDN YRGYSLGNWVAAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWANDGRTPGSRNLANIP ASALLSSDITASVNAAKKIV SDGNGMNAWVAWRNRAKGTD VQAWIRGCRL ; 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 CYS 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 ALA 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 ALA 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 CYS 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 1.28e-85 BMRB 11052 2SS(6-127_64-80) 100.00 130 98.46 98.46 1.27e-86 BMRB 11460 1SS[30-115] 100.00 130 96.92 96.92 9.78e-84 BMRB 11461 1SS[64-80] 100.00 130 96.92 96.92 9.78e-84 BMRB 11462 1SS[76-94] 100.00 130 96.92 96.92 9.78e-84 BMRB 15198 all-Ala-Hen_egg_white_lysoyzme 100.00 130 98.46 98.46 1.40e-85 BMRB 18365 WT-ALA 99.23 129 98.45 98.45 9.25e-85 BMRB 18366 W28G 99.23 129 97.67 97.67 3.18e-83 BMRB 18367 W62G 99.23 129 97.67 97.67 3.18e-83 BMRB 18368 W108G 99.23 129 97.67 97.67 3.18e-83 BMRB 18369 W111G 99.23 129 97.67 97.67 3.18e-83 BMRB 18370 W123G 99.23 129 97.67 97.67 3.18e-83 PDB 3ZVQ "Crystal Structure Of Proteolyzed Lysozyme" 53.85 70 97.14 97.14 5.82e-42 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[6-127] 7 CYS SG 1SS[6-127] 128 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-6-127 . . . . . . 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-6-127 '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-6-127 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_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _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' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' '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[6-127] _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 8.62 0.02 1 2 1 2 LYS HA H 4.36 0.02 1 3 1 2 LYS HB2 H 1.53 0.02 2 4 1 2 LYS HB3 H 1.37 0.02 2 5 1 2 LYS HG2 H 1.27 0.02 2 6 1 2 LYS N N 122.17 0.1 1 7 2 3 VAL H H 7.94 0.02 1 8 2 3 VAL HA H 4.19 0.02 1 9 2 3 VAL HB H 1.93 0.02 1 10 2 3 VAL HG1 H 0.80 0.02 2 11 2 3 VAL N N 116.47 0.1 1 12 3 4 PHE H H 8.17 0.02 1 13 3 4 PHE HA H 4.60 0.02 1 14 3 4 PHE HB2 H 2.84 0.02 2 15 3 4 PHE HB3 H 3.07 0.02 2 16 3 4 PHE N N 120.15 0.1 1 17 4 5 GLY H H 8.31 0.02 1 18 4 5 GLY HA2 H 3.92 0.02 2 19 4 5 GLY N N 106.31 0.1 1 20 5 6 ARG H H 8.26 0.02 1 21 5 6 ARG HA H 4.31 0.02 1 22 5 6 ARG HB2 H 1.76 0.02 2 23 5 6 ARG HB3 H 1.62 0.02 2 24 5 6 ARG N N 117.97 0.1 1 25 6 7 CYS H H 8.48 0.02 1 26 6 7 CYS HA H 4.54 0.02 1 27 6 7 CYS HB2 H 3.14 0.02 2 28 6 7 CYS HB3 H 2.98 0.02 2 29 6 7 CYS N N 117.07 0.1 1 30 7 8 GLU H H 8.07 0.02 1 31 7 8 GLU N N 118.85 0.1 1 32 8 9 LEU H H 8.07 0.02 1 33 8 9 LEU HA H 4.25 0.02 1 34 8 9 LEU HB2 H 1.51 0.02 2 35 8 9 LEU N N 119.93 0.1 1 36 9 10 ALA H H 8.13 0.02 1 37 9 10 ALA HA H 4.21 0.02 1 38 9 10 ALA HB H 1.28 0.02 1 39 9 10 ALA N N 121.14 0.1 1 40 10 11 ALA H H 8.00 0.02 1 41 10 11 ALA HA H 4.22 0.02 1 42 10 11 ALA HB H 1.28 0.02 1 43 10 11 ALA N N 119.18 0.1 1 44 11 12 ALA H H 7.96 0.02 1 45 11 12 ALA HA H 4.19 0.02 1 46 11 12 ALA HB H 1.25 0.02 1 47 11 12 ALA N N 119.23 0.1 1 48 12 13 MET H H 7.98 0.02 1 49 12 13 MET HA H 4.31 0.02 1 50 12 13 MET HB2 H 1.89 0.02 2 51 12 13 MET HG2 H 2.48 0.02 2 52 12 13 MET N N 115.80 0.1 1 53 13 14 LYS H H 7.93 0.02 1 54 13 14 LYS HA H 4.23 0.02 1 55 13 14 LYS HB2 H 1.58 0.02 2 56 13 14 LYS HB3 H 1.70 0.02 2 57 13 14 LYS HG2 H 1.36 0.02 2 58 13 14 LYS N N 117.97 0.1 1 59 14 15 ARG H H 8.06 0.02 1 60 14 15 ARG N N 118.29 0.1 1 61 15 16 HIS H H 8.20 0.02 1 62 15 16 HIS HA H 4.62 0.02 1 63 15 16 HIS HB2 H 3.17 0.02 2 64 15 16 HIS HB3 H 3.05 0.02 2 65 15 16 HIS N N 115.97 0.1 1 66 16 17 GLY H H 8.34 0.02 1 67 16 17 GLY HA2 H 3.90 0.02 2 68 16 17 GLY HA3 H 3.78 0.02 2 69 16 17 GLY N N 106.84 0.1 1 70 17 18 LEU H H 8.19 0.02 1 71 17 18 LEU HA H 4.24 0.02 1 72 17 18 LEU HB2 H 1.50 0.02 2 73 17 18 LEU N N 118.97 0.1 1 74 18 19 ASP H H 8.36 0.02 1 75 18 19 ASP HA H 4.57 0.02 1 76 18 19 ASP HB2 H 2.74 0.02 2 77 18 19 ASP HB3 H 2.57 0.02 2 78 18 19 ASP N N 117.46 0.1 1 79 19 20 ASN H H 8.04 0.02 1 80 19 20 ASN HA H 4.54 0.02 1 81 19 20 ASN HB2 H 2.55 0.02 2 82 19 20 ASN HB3 H 2.43 0.02 2 83 19 20 ASN N N 116.63 0.1 1 84 20 21 TYR H H 7.86 0.02 1 85 20 21 TYR HA H 4.38 0.02 1 86 20 21 TYR HB2 H 2.94 0.02 2 87 20 21 TYR HB3 H 2.75 0.02 2 88 20 21 TYR N N 116.91 0.1 1 89 21 22 ARG H H 8.13 0.02 1 90 21 22 ARG HA H 4.25 0.02 1 91 21 22 ARG HB2 H 1.73 0.02 2 92 21 22 ARG HB3 H 1.58 0.02 2 93 21 22 ARG N N 118.18 0.1 1 94 22 23 GLY H H 7.99 0.02 1 95 22 23 GLY HA2 H 3.71 0.02 2 96 22 23 GLY N N 106.05 0.1 1 97 23 24 TYR H H 8.02 0.02 1 98 23 24 TYR HA H 4.54 0.02 1 99 23 24 TYR HB2 H 2.95 0.02 2 100 23 24 TYR HB3 H 2.69 0.02 2 101 23 24 TYR N N 116.59 0.1 1 102 24 25 SER H H 8.28 0.02 1 103 24 25 SER HA H 4.39 0.02 1 104 24 25 SER HB2 H 3.67 0.02 2 105 24 25 SER N N 114.42 0.1 1 106 25 26 LEU H H 8.15 0.02 1 107 25 26 LEU HA H 4.35 0.02 1 108 25 26 LEU HB2 H 1.66 0.02 2 109 25 26 LEU HB3 H 1.56 0.02 2 110 25 26 LEU N N 120.92 0.1 1 111 26 27 GLY H H 8.20 0.02 1 112 26 27 GLY HA2 H 3.72 0.02 2 113 26 27 GLY N N 105.48 0.1 1 114 27 28 ASN H H 8.12 0.02 1 115 27 28 ASN HA H 4.61 0.02 1 116 27 28 ASN HB2 H 2.59 0.02 2 117 27 28 ASN HB3 H 2.46 0.02 2 118 27 28 ASN N N 117.07 0.1 1 119 28 29 TRP H H 8.17 0.02 1 120 28 29 TRP HA H 4.46 0.02 1 121 28 29 TRP HB2 H 3.22 0.02 2 122 28 29 TRP HB3 H 3.08 0.02 2 123 28 29 TRP N N 119.63 0.1 1 124 29 30 VAL H H 7.85 0.02 1 125 29 30 VAL HA H 3.98 0.02 1 126 29 30 VAL HB H 2.03 0.02 1 127 29 30 VAL HG1 H 0.85 0.02 2 128 29 30 VAL N N 115.99 0.1 1 129 30 31 ALA H H 7.97 0.02 1 130 30 31 ALA HA H 4.22 0.02 1 131 30 31 ALA HB H 1.28 0.02 1 132 30 31 ALA N N 122.67 0.1 1 133 31 32 ALA H H 7.90 0.02 1 134 31 32 ALA HA H 4.20 0.02 1 135 31 32 ALA HB H 1.27 0.02 1 136 31 32 ALA N N 118.97 0.1 1 137 32 33 ALA H H 7.96 0.02 1 138 32 33 ALA HA H 4.19 0.02 1 139 32 33 ALA HB H 1.25 0.02 1 140 32 33 ALA N N 119.23 0.1 1 141 33 34 LYS H H 7.85 0.02 1 142 33 34 LYS HA H 4.13 0.02 1 143 33 34 LYS HB2 H 1.54 0.02 2 144 33 34 LYS N N 115.99 0.1 1 145 34 35 PHE H H 7.92 0.02 1 146 34 35 PHE HA H 4.53 0.02 1 147 34 35 PHE HB2 H 3.13 0.02 2 148 34 35 PHE HB3 H 2.87 0.02 2 149 34 35 PHE N N 116.16 0.1 1 150 35 36 GLU H H 8.08 0.02 1 151 35 36 GLU HA H 4.32 0.02 1 152 35 36 GLU HB2 H 1.98 0.02 2 153 35 36 GLU HB3 H 1.84 0.02 2 154 35 36 GLU HG2 H 2.34 0.02 2 155 35 36 GLU N N 117.36 0.1 1 156 36 37 SER H H 7.94 0.02 1 157 36 37 SER HA H 4.34 0.02 1 158 36 37 SER HB2 H 3.61 0.02 2 159 36 37 SER N N 113.45 0.1 1 160 37 38 ASN H H 8.19 0.02 1 161 37 38 ASN HA H 4.56 0.02 1 162 37 38 ASN HB2 H 2.54 0.02 2 163 37 38 ASN HB3 H 2.43 0.02 2 164 37 38 ASN N N 118.74 0.1 1 165 38 39 PHE H H 8.06 0.02 1 166 38 39 PHE HA H 4.48 0.02 1 167 38 39 PHE HB2 H 3.08 0.02 2 168 38 39 PHE HB3 H 2.81 0.02 2 169 38 39 PHE N N 116.37 0.1 1 170 39 40 ASN H H 8.34 0.02 1 171 39 40 ASN HA H 4.67 0.02 1 172 39 40 ASN HB2 H 2.70 0.02 2 173 39 40 ASN HB3 H 2.54 0.02 2 174 39 40 ASN N N 117.87 0.1 1 175 40 41 THR H H 7.77 0.02 1 176 40 41 THR HA H 4.18 0.02 1 177 40 41 THR HG2 H 1.10 0.02 1 178 40 41 THR N N 111.30 0.1 1 179 41 42 GLN H H 8.04 0.02 1 180 41 42 GLN HA H 4.27 0.02 1 181 41 42 GLN HB2 H 2.00 0.02 2 182 41 42 GLN HB3 H 1.82 0.02 2 183 41 42 GLN HG2 H 2.16 0.02 2 184 41 42 GLN N N 118.48 0.1 1 185 42 43 ALA H H 8.00 0.02 1 186 42 43 ALA HA H 4.33 0.02 1 187 42 43 ALA HB H 1.28 0.02 1 188 42 43 ALA N N 121.37 0.1 1 189 43 44 THR H H 7.75 0.02 1 190 43 44 THR HA H 4.24 0.02 1 191 43 44 THR HB H 4.06 0.02 1 192 43 44 THR HG2 H 1.10 0.02 1 193 43 44 THR N N 109.69 0.1 1 194 44 45 ASN H H 8.10 0.02 1 195 44 45 ASN HA H 4.58 0.02 1 196 44 45 ASN HB2 H 2.61 0.02 2 197 44 45 ASN N N 118.63 0.1 1 198 45 46 ARG H H 8.05 0.02 1 199 45 46 ARG HA H 4.27 0.02 1 200 45 46 ARG HB2 H 1.76 0.02 2 201 45 46 ARG HB3 H 1.56 0.02 2 202 45 46 ARG N N 117.64 0.1 1 203 46 47 ASN H H 8.26 0.02 1 204 46 47 ASN HA H 4.65 0.02 1 205 46 47 ASN HB2 H 2.67 0.02 2 206 46 47 ASN HB3 H 2.54 0.02 2 207 46 47 ASN N N 117.74 0.1 1 208 47 48 THR H H 7.73 0.02 1 209 47 48 THR HA H 4.19 0.02 1 210 47 48 THR HG2 H 1.08 0.02 1 211 47 48 THR N N 110.79 0.1 1 212 48 49 ASP H H 8.28 0.02 1 213 48 49 ASP HA H 4.60 0.02 1 214 48 49 ASP HB2 H 2.79 0.02 2 215 48 49 ASP HB3 H 2.63 0.02 2 216 48 49 ASP N N 118.27 0.1 1 217 49 50 GLY H H 8.01 0.02 1 218 49 50 GLY HA2 H 3.79 0.02 2 219 49 50 GLY N N 105.19 0.1 1 220 50 51 SER H H 7.95 0.02 1 221 50 51 SER HA H 4.46 0.02 1 222 50 51 SER HB2 H 3.65 0.02 2 223 50 51 SER N N 112.88 0.1 1 224 51 52 THR H H 7.86 0.02 1 225 51 52 THR HA H 4.30 0.02 1 226 51 52 THR HB H 4.10 0.02 1 227 51 52 THR HG2 H 1.08 0.02 1 228 51 52 THR N N 112.21 0.1 1 229 52 53 ASP H H 8.23 0.02 1 230 52 53 ASP HA H 4.58 0.02 1 231 52 53 ASP HB2 H 2.71 0.02 2 232 52 53 ASP HB3 H 2.48 0.02 2 233 52 53 ASP N N 118.54 0.1 1 234 53 54 TYR H H 7.89 0.02 1 235 53 54 TYR HA H 4.38 0.02 1 236 53 54 TYR HB2 H 2.94 0.02 2 237 53 54 TYR HB3 H 2.75 0.02 2 238 53 54 TYR N N 116.90 0.1 1 239 54 55 GLY H H 8.19 0.02 1 240 54 55 GLY HA2 H 3.78 0.02 2 241 54 55 GLY N N 106.38 0.1 1 242 55 56 ILE H H 7.80 0.02 1 243 55 56 ILE HA H 4.19 0.02 1 244 55 56 ILE HB H 1.76 0.02 1 245 55 56 ILE HG12 H 1.11 0.02 2 246 55 56 ILE N N 116.08 0.1 1 247 56 57 LEU H H 8.08 0.02 1 248 56 57 LEU HA H 4.31 0.02 1 249 56 57 LEU HB2 H 1.51 0.02 2 250 56 57 LEU N N 121.87 0.1 1 251 57 58 GLN H H 8.02 0.02 1 252 57 58 GLN HA H 4.27 0.02 1 253 57 58 GLN HB2 H 1.82 0.02 2 254 57 58 GLN HB3 H 1.97 0.02 2 255 57 58 GLN HG2 H 2.16 0.02 2 256 57 58 GLN N N 118.74 0.1 1 257 58 59 ILE H H 7.81 0.02 1 258 58 59 ILE HA H 4.19 0.02 1 259 58 59 ILE HB H 1.74 0.02 1 260 58 59 ILE HD1 H 0.83 0.02 4 261 58 59 ILE N N 116.98 0.1 1 262 59 60 ASN H H 8.27 0.02 1 263 59 60 ASN HA H 4.65 0.02 1 264 59 60 ASN HB2 H 2.66 0.02 2 265 59 60 ASN HB3 H 2.53 0.02 2 266 59 60 ASN N N 120.56 0.1 1 267 60 61 SER H H 7.98 0.02 1 268 60 61 SER HA H 4.24 0.02 1 269 60 61 SER HB2 H 3.57 0.02 2 270 60 61 SER N N 114.30 0.1 1 271 61 62 ARG H H 8.17 0.02 1 272 61 62 ARG HA H 4.20 0.02 1 273 61 62 ARG HB2 H 1.76 0.02 2 274 61 62 ARG HB3 H 1.55 0.02 2 275 61 62 ARG N N 119.53 0.1 1 276 62 63 TRP H H 7.90 0.02 1 277 62 63 TRP HA H 4.48 0.02 1 278 62 63 TRP HB2 H 2.93 0.02 2 279 62 63 TRP HB3 H 3.14 0.02 2 280 62 63 TRP N N 117.96 0.1 1 281 63 64 TRP H H 7.94 0.02 1 282 63 64 TRP HA H 4.54 0.02 1 283 63 64 TRP HB2 H 3.04 0.02 2 284 63 64 TRP HB3 H 3.19 0.02 2 285 63 64 TRP N N 118.56 0.1 1 286 64 65 ALA H H 8.01 0.02 1 287 64 65 ALA HA H 4.33 0.02 1 288 64 65 ALA HB H 1.28 0.02 1 289 64 65 ALA N N 121.21 0.1 1 290 65 66 ASN H H 8.18 0.02 1 291 65 66 ASN HA H 4.60 0.02 1 292 65 66 ASN HB2 H 2.69 0.02 2 293 65 66 ASN HB3 H 2.55 0.02 2 294 65 66 ASN N N 115.85 0.1 1 295 66 67 ASP H H 8.30 0.02 1 296 66 67 ASP HA H 4.58 0.02 1 297 66 67 ASP HB2 H 2.79 0.02 2 298 66 67 ASP HB3 H 2.63 0.02 2 299 66 67 ASP N N 117.45 0.1 1 300 67 68 GLY H H 8.24 0.02 1 301 67 68 GLY HA2 H 3.73 0.02 2 302 67 68 GLY N N 105.03 0.1 1 303 68 69 ARG H H 7.83 0.02 1 304 68 69 ARG HA H 4.42 0.02 1 305 68 69 ARG HB2 H 1.55 0.02 2 306 68 69 ARG N N 116.92 0.1 1 307 71 72 GLY H H 8.24 0.02 1 308 71 72 GLY HA2 H 3.78 0.02 2 309 71 72 GLY N N 105.44 0.1 1 310 72 73 SER H H 7.91 0.02 1 311 72 73 SER HA H 4.34 0.02 1 312 72 73 SER HB2 H 3.65 0.02 2 313 72 73 SER N N 112.78 0.1 1 314 73 74 ARG H H 8.20 0.02 1 315 73 74 ARG HA H 4.31 0.02 1 316 73 74 ARG HB2 H 1.76 0.02 2 317 73 74 ARG HB3 H 1.56 0.02 2 318 73 74 ARG N N 119.60 0.1 1 319 74 75 ASN H H 8.15 0.02 1 320 74 75 ASN HA H 4.56 0.02 1 321 74 75 ASN HB2 H 2.64 0.02 2 322 74 75 ASN HB3 H 2.50 0.02 2 323 74 75 ASN N N 117.49 0.1 1 324 75 76 LEU H H 7.99 0.02 1 325 75 76 LEU HA H 4.22 0.02 1 326 75 76 LEU HB2 H 1.65 0.02 2 327 75 76 LEU HB3 H 1.53 0.02 2 328 75 76 LEU N N 119.17 0.1 1 329 76 77 ALA H H 8.03 0.02 1 330 76 77 ALA HA H 4.20 0.02 1 331 76 77 ALA HB H 1.27 0.02 1 332 76 77 ALA N N 119.21 0.1 1 333 77 78 ASN H H 8.04 0.02 1 334 77 78 ASN HA H 4.56 0.02 1 335 77 78 ASN HB2 H 2.63 0.02 2 336 77 78 ASN HB3 H 2.42 0.02 2 337 77 78 ASN N N 115.67 0.1 1 338 78 79 ILE H H 7.61 0.02 1 339 78 79 ILE HA H 4.35 0.02 1 340 78 79 ILE HB H 1.77 0.02 1 341 78 79 ILE HD1 H 0.90 0.02 1 342 78 79 ILE HG12 H 1.07 0.02 2 343 78 79 ILE N N 117.04 0.1 1 344 80 81 ALA H H 8.29 0.02 1 345 80 81 ALA HA H 4.18 0.02 1 346 80 81 ALA HB H 1.29 0.02 1 347 80 81 ALA N N 120.94 0.1 1 348 81 82 SER H H 7.90 0.02 1 349 81 82 SER HA H 4.21 0.02 1 350 81 82 SER HB2 H 3.71 0.02 2 351 81 82 SER HB3 H 3.62 0.02 2 352 81 82 SER N N 110.86 0.1 1 353 82 83 ALA H H 8.04 0.02 1 354 82 83 ALA HA H 4.25 0.02 1 355 82 83 ALA HB H 1.28 0.02 1 356 82 83 ALA N N 122.18 0.1 1 357 83 84 LEU H H 7.82 0.02 1 358 83 84 LEU HA H 4.24 0.02 1 359 83 84 LEU HB2 H 1.53 0.02 2 360 83 84 LEU N N 116.75 0.1 1 361 84 85 LEU H H 7.79 0.02 1 362 84 85 LEU HA H 4.32 0.02 1 363 84 85 LEU HB2 H 1.54 0.02 2 364 84 85 LEU N N 118.02 0.1 1 365 85 86 SER H H 7.89 0.02 1 366 85 86 SER HA H 4.30 0.02 1 367 85 86 SER HB2 H 3.65 0.02 2 368 85 86 SER N N 113.05 0.1 1 369 86 87 SER H H 7.94 0.02 1 370 86 87 SER HA H 4.33 0.02 1 371 86 87 SER HB2 H 3.70 0.02 2 372 86 87 SER N N 114.45 0.1 1 373 87 88 ASP H H 8.31 0.02 1 374 87 88 ASP HA H 4.61 0.02 1 375 87 88 ASP HB2 H 2.77 0.02 2 376 87 88 ASP HB3 H 2.60 0.02 2 377 87 88 ASP N N 119.10 0.1 1 378 88 89 ILE H H 7.74 0.02 1 379 88 89 ILE HA H 4.19 0.02 1 380 88 89 ILE HB H 1.81 0.02 1 381 88 89 ILE HD1 H 0.86 0.02 1 382 88 89 ILE HG12 H 1.11 0.02 2 383 88 89 ILE N N 116.19 0.1 1 384 89 90 THR H H 7.85 0.02 1 385 89 90 THR HA H 4.16 0.02 1 386 89 90 THR HB H 4.04 0.02 1 387 89 90 THR HG2 H 1.08 0.02 1 388 89 90 THR N N 114.72 0.1 1 389 90 91 ALA H H 7.96 0.02 1 390 90 91 ALA HA H 4.33 0.02 1 391 90 91 ALA HB H 1.29 0.02 1 392 90 91 ALA N N 122.19 0.1 1 393 91 92 SER H H 8.02 0.02 1 394 91 92 SER HA H 4.33 0.02 1 395 91 92 SER HB2 H 3.68 0.02 2 396 91 92 SER N N 112.81 0.1 1 397 92 93 VAL H H 7.83 0.02 1 398 92 93 VAL HA H 4.09 0.02 1 399 92 93 VAL HB H 2.04 0.02 1 400 92 93 VAL HG1 H 0.89 0.02 2 401 92 93 VAL N N 116.54 0.1 1 402 93 94 ASN H H 8.15 0.02 1 403 93 94 ASN HA H 4.52 0.02 1 404 93 94 ASN HB2 H 2.61 0.02 2 405 93 94 ASN HB3 H 2.52 0.02 2 406 93 94 ASN N N 118.98 0.1 1 407 94 95 ALA H H 8.03 0.02 1 408 94 95 ALA HA H 4.15 0.02 1 409 94 95 ALA HB H 1.29 0.02 1 410 94 95 ALA N N 121.15 0.1 1 411 95 96 ALA H H 8.01 0.02 1 412 95 96 ALA HA H 4.21 0.02 1 413 95 96 ALA HB H 1.30 0.02 1 414 95 96 ALA N N 118.74 0.1 1 415 96 97 LYS H H 7.80 0.02 1 416 96 97 LYS HA H 4.19 0.02 1 417 96 97 LYS HB2 H 1.75 0.02 2 418 96 97 LYS HB3 H 1.61 0.02 2 419 96 97 LYS HG2 H 1.38 0.02 2 420 96 97 LYS N N 115.87 0.1 1 421 97 98 LYS H H 7.87 0.02 1 422 97 98 LYS HA H 4.25 0.02 1 423 97 98 LYS HB2 H 1.70 0.02 2 424 97 98 LYS HB3 H 1.58 0.02 2 425 97 98 LYS HG2 H 1.34 0.02 2 426 97 98 LYS N N 117.92 0.1 1 427 98 99 ILE H H 7.85 0.02 1 428 98 99 ILE HA H 4.19 0.02 1 429 98 99 ILE HB H 1.78 0.02 1 430 98 99 ILE HD1 H 0.84 0.02 1 431 98 99 ILE HG12 H 1.10 0.02 2 432 98 99 ILE N N 117.33 0.1 1 433 99 100 VAL H H 7.87 0.02 1 434 99 100 VAL HA H 4.23 0.02 1 435 99 100 VAL HB H 2.04 0.02 1 436 99 100 VAL HG1 H 0.87 0.02 2 437 99 100 VAL N N 118.13 0.1 1 438 100 101 SER H H 7.93 0.02 1 439 100 101 SER HA H 4.38 0.02 1 440 100 101 SER HB2 H 3.65 0.02 2 441 100 101 SER N N 115.44 0.1 1 442 101 102 ASP H H 8.35 0.02 1 443 101 102 ASP HA H 4.63 0.02 1 444 101 102 ASP HB2 H 2.75 0.02 2 445 101 102 ASP HB3 H 2.62 0.02 2 446 101 102 ASP N N 119.33 0.1 1 447 102 103 GLY H H 8.10 0.02 1 448 102 103 GLY HA2 H 3.78 0.02 2 449 102 103 GLY N N 105.42 0.1 1 450 103 104 ASN H H 8.14 0.02 1 451 103 104 ASN HA H 4.57 0.02 1 452 103 104 ASN HB2 H 2.59 0.02 2 453 103 104 ASN N N 116.75 0.1 1 454 104 105 GLY H H 8.25 0.02 1 455 104 105 GLY HA2 H 3.76 0.02 2 456 104 105 GLY N N 106.31 0.1 1 457 105 106 MET H H 8.06 0.02 1 458 105 106 MET HA H 4.39 0.02 1 459 105 106 MET HB2 H 1.90 0.02 2 460 105 106 MET N N 116.55 0.1 1 461 106 107 ASN H H 8.22 0.02 1 462 106 107 ASN HA H 4.56 0.02 1 463 106 107 ASN HB2 H 2.64 0.02 2 464 106 107 ASN HB3 H 2.58 0.02 2 465 106 107 ASN N N 117.64 0.1 1 466 107 108 ALA H H 8.24 0.02 1 467 107 108 ALA HA H 4.12 0.02 1 468 107 108 ALA HB H 1.19 0.02 1 469 107 108 ALA N N 121.93 0.1 1 470 108 109 TRP H H 8.15 0.02 1 471 108 109 TRP HA H 4.51 0.02 1 472 108 109 TRP HB2 H 3.25 0.02 2 473 108 109 TRP HB3 H 3.13 0.02 2 474 108 109 TRP N N 117.02 0.1 1 475 109 110 VAL H H 7.69 0.02 1 476 109 110 VAL HA H 4.00 0.02 1 477 109 110 VAL HB H 2.03 0.02 1 478 109 110 VAL HG1 H 0.88 0.02 2 479 109 110 VAL N N 115.60 0.1 1 480 110 111 ALA H H 7.99 0.02 1 481 110 111 ALA HA H 4.21 0.02 1 482 110 111 ALA HB H 1.28 0.02 1 483 110 111 ALA N N 122.69 0.1 1 484 111 112 TRP H H 7.98 0.02 1 485 111 112 TRP HA H 4.44 0.02 1 486 111 112 TRP HB2 H 3.23 0.02 2 487 111 112 TRP HB3 H 3.08 0.02 2 488 111 112 TRP N N 117.43 0.1 1 489 112 113 ARG H H 8.06 0.02 1 490 112 113 ARG HA H 4.17 0.02 1 491 112 113 ARG HB2 H 1.75 0.02 2 492 112 113 ARG HB3 H 1.58 0.02 2 493 112 113 ARG N N 117.85 0.1 1 494 113 114 ASN H H 8.12 0.02 1 495 113 114 ASN HA H 4.55 0.02 1 496 113 114 ASN HB2 H 2.60 0.02 2 497 113 114 ASN HB3 H 2.47 0.02 2 498 113 114 ASN N N 117.22 0.1 1 499 114 115 ARG H H 8.00 0.02 1 500 114 115 ARG HA H 4.20 0.02 1 501 114 115 ARG HB2 H 1.77 0.02 2 502 114 115 ARG HB3 H 1.61 0.02 2 503 114 115 ARG N N 118.00 0.1 1 504 115 116 ALA H H 8.04 0.02 1 505 115 116 ALA HA H 4.22 0.02 1 506 115 116 ALA HB H 1.26 0.02 1 507 115 116 ALA N N 120.68 0.1 1 508 116 117 LYS H H 7.92 0.02 1 509 116 117 LYS HA H 4.21 0.02 1 510 116 117 LYS HB2 H 1.74 0.02 2 511 116 117 LYS HB3 H 1.60 0.02 2 512 116 117 LYS HG2 H 1.37 0.02 2 513 116 117 LYS N N 116.53 0.1 1 514 117 118 GLY H H 8.11 0.02 1 515 117 118 GLY HA2 H 3.89 0.02 2 516 117 118 GLY N N 105.96 0.1 1 517 118 119 THR H H 7.85 0.02 1 518 118 119 THR HA H 4.31 0.02 1 519 118 119 THR HB H 4.03 0.02 1 520 118 119 THR HG2 H 1.09 0.02 1 521 118 119 THR N N 110.78 0.1 1 522 119 120 ASP H H 8.34 0.02 1 523 119 120 ASP HA H 4.65 0.02 1 524 119 120 ASP HB2 H 2.78 0.02 2 525 119 120 ASP HB3 H 2.63 0.02 2 526 119 120 ASP N N 119.61 0.1 1 527 120 121 VAL H H 7.76 0.02 1 528 120 121 VAL HA H 4.08 0.02 1 529 120 121 VAL HB H 2.01 0.02 1 530 120 121 VAL HG1 H 0.86 0.02 2 531 120 121 VAL N N 115.60 0.1 1 532 121 122 GLN H H 8.12 0.02 1 533 121 122 GLN HA H 4.19 0.02 1 534 121 122 GLN HB2 H 1.92 0.02 2 535 121 122 GLN HB3 H 1.80 0.02 2 536 121 122 GLN HG2 H 2.18 0.02 2 537 121 122 GLN N N 120.36 0.1 1 538 122 123 ALA H H 7.94 0.02 1 539 122 123 ALA HA H 4.24 0.02 1 540 122 123 ALA HB H 1.20 0.02 1 541 122 123 ALA N N 120.64 0.1 1 542 123 124 TRP H H 8.06 0.02 1 543 123 124 TRP HA H 4.59 0.02 1 544 123 124 TRP HB2 H 3.19 0.02 2 545 123 124 TRP HB3 H 3.01 0.02 2 546 123 124 TRP N N 117.95 0.1 1 547 124 125 ILE H H 7.88 0.02 1 548 124 125 ILE HA H 4.19 0.02 1 549 124 125 ILE HB H 1.79 0.02 1 550 124 125 ILE HD1 H 0.85 0.02 4 551 124 125 ILE N N 117.03 0.1 1 552 125 126 ARG H H 8.10 0.02 1 553 125 126 ARG HA H 4.31 0.02 1 554 125 126 ARG HB2 H 1.73 0.02 2 555 125 126 ARG HB3 H 1.61 0.02 2 556 125 126 ARG N N 121.31 0.1 1 557 126 127 GLY H H 8.18 0.02 1 558 126 127 GLY HA2 H 3.79 0.02 2 559 126 127 GLY N N 106.14 0.1 1 560 127 128 CYS H H 8.31 0.02 1 561 127 128 CYS HA H 4.64 0.02 1 562 127 128 CYS HB2 H 3.14 0.02 2 563 127 128 CYS HB3 H 2.89 0.02 2 564 127 128 CYS N N 116.09 0.1 1 565 128 129 ARG H H 8.20 0.02 1 566 128 129 ARG HA H 4.33 0.02 1 567 128 129 ARG HB2 H 1.75 0.02 2 568 128 129 ARG N N 119.37 0.1 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 260 '260,260' '550,550,550' stop_ save_