data_4218 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of toxin 2 from centruroides noxius hoffmann,a beta scorpion neurotoxin acting on sodium channels ; _BMRB_accession_number 4218 _BMRB_flat_file_name bmr4218.str _Entry_type original _Submission_date 1998-07-01 _Accession_date 1998-07-01 _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 PINTAR A. . . 2 POSSANI L. D. . 3 DELEPIERRE M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 336 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 update BMRB 'Updating non-standard residue' 2008-03-24 update BMRB . 2000-05-04 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of toxin 2 from centruroides noxius Hoffmann, a beta-scorpion neurotoxin acting on sodium channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99182423 _PubMed_ID 10080898 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 PINTAR A. . . 2 POSSANI L. D. . 3 DELEPIERRE M. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular biology' _Journal_volume 287 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 359 _Page_last 367 _Year 1999 _Details . loop_ _Keyword 'Centruroides noxius' neurotoxin 'scorpion toxin' 'sodium channels' stop_ save_ ################################## # Molecular system description # ################################## save_system-T2CNH _Saveframe_category molecular_system _Mol_system_name 'Toxin 2 from Centruroides noxius hoffmann' _Abbreviation_common T2CNH _Enzyme_commission_number 5.3.4.1 loop_ _Mol_system_component_name _Mol_label T2CNH $T2CNH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_T2CNH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Toxin 2 from Centruroides noxius hoffmann' _Abbreviation_common T2CNH _Molecular_mass . _Mol_thiol_state 'all disulfide bond' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; KEGYLVDKNTGCKYECLKLG DNDYCLRECKQQYGKGAGGY CYAFACWCTHLYEQAIVWPL PNKRCSX ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 GLU 3 GLY 4 TYR 5 LEU 6 VAL 7 ASP 8 LYS 9 ASN 10 THR 11 GLY 12 CYS 13 LYS 14 TYR 15 GLU 16 CYS 17 LEU 18 LYS 19 LEU 20 GLY 21 ASP 22 ASN 23 ASP 24 TYR 25 CYS 26 LEU 27 ARG 28 GLU 29 CYS 30 LYS 31 GLN 32 GLN 33 TYR 34 GLY 35 LYS 36 GLY 37 ALA 38 GLY 39 GLY 40 TYR 41 CYS 42 TYR 43 ALA 44 PHE 45 ALA 46 CYS 47 TRP 48 CYS 49 THR 50 HIS 51 LEU 52 TYR 53 GLU 54 GLN 55 ALA 56 ILE 57 VAL 58 TRP 59 PRO 60 LEU 61 PRO 62 ASN 63 LYS 64 ARG 65 CYS 66 SER 67 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1CN2 "Solution Structure Of Toxin 2 From Centruroides Noxius Hoffmann, A Beta Scorpion Neurotoxin Acting On Sodium Channels, Nmr, 15 " 98.51 67 100.00 100.00 1.39e-39 PDB 2YBR "Crystal Structure Of The Human Derived Single Chain Antibody Fragment (scfv) 9004g In Complex With Cn2 Toxin From The Scorpion " 98.51 66 100.00 100.00 1.35e-39 PDB 2YC1 "Crystal Structure Of The Human Derived Single Chain Antibody Fragment (scfv) 9004g In Complex With Cn2 Toxin From The Scorpion " 98.51 66 100.00 100.00 1.35e-39 GB AAB21461 "toxin 2, Cn2 [Centruroides noxius=scorpions, Hoffmann, venom, Peptide, 66 aa]" 98.51 66 96.97 96.97 5.16e-37 GB AAB36086 "Na+ channel-specific toxin 2, partial [Centruroides noxius]" 98.51 84 100.00 100.00 5.80e-40 GB AAR08045 "beta-toxin [Centruroides noxius]" 97.01 64 98.46 98.46 2.04e-36 SP P01495 "RecName: Full=Beta-mammal toxin Cn2; Short=Toxin 2; AltName: Full=Toxin II.9.2.2; Flags: Precursor" 98.51 84 100.00 100.00 5.80e-40 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 13:32:02 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 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 N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Secretion $T2CNH 'Mexican scorpion' 6878 Eukaryota Metazoa Centruroides noxius heart venom 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 $T2CNH 'purified from the natural source' . . . . . 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 $T2CNH 1 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 . n/a pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . $entry_citation $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name T2CNH _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 LYS HA H 4.091 0.03 1 2 . 1 LYS HB2 H 1.775 0.03 2 3 . 1 LYS HB3 H 1.508 0.03 2 4 . 1 LYS HG2 H 0.992 0.03 1 5 . 1 LYS HG3 H 0.992 0.03 1 6 . 1 LYS HD2 H 1.591 0.03 1 7 . 1 LYS HD3 H 1.591 0.03 1 8 . 2 GLU H H 8.007 0.03 1 9 . 2 GLU HA H 4.605 0.03 1 10 . 2 GLU HB2 H 2.138 0.03 2 11 . 2 GLU HB3 H 1.865 0.03 2 12 . 2 GLU HG2 H 2.338 0.03 2 13 . 2 GLU HG3 H 2.233 0.03 2 14 . 3 GLY H H 7.245 0.03 1 15 . 3 GLY HA2 H 3.352 0.03 2 16 . 3 GLY HA3 H 1.827 0.03 2 17 . 4 TYR H H 9.181 0.03 1 18 . 4 TYR HA H 4.932 0.03 1 19 . 4 TYR HB2 H 3.152 0.03 2 20 . 4 TYR HB3 H 3.048 0.03 2 21 . 4 TYR HE1 H 7.355 0.03 1 22 . 4 TYR HE2 H 7.355 0.03 1 23 . 4 TYR HD1 H 7.602 0.03 1 24 . 4 TYR HD2 H 7.602 0.03 1 25 . 5 LEU H H 7.720 0.03 1 26 . 5 LEU HA H 4.587 0.03 1 27 . 5 LEU HB2 H 1.854 0.03 2 28 . 5 LEU HB3 H 1.702 0.03 2 29 . 5 LEU HG H 1.421 0.03 1 30 . 5 LEU HD1 H 0.651 0.03 2 31 . 5 LEU HD2 H 0.067 0.03 2 32 . 6 VAL H H 7.104 0.03 1 33 . 6 VAL HA H 5.213 0.03 1 34 . 6 VAL HB H 2.059 0.03 1 35 . 6 VAL HG1 H 1.059 0.03 2 36 . 6 VAL HG2 H 0.808 0.03 2 37 . 7 ASP H H 8.581 0.03 1 38 . 7 ASP HA H 4.909 0.03 1 39 . 7 ASP HB2 H 3.190 0.03 2 40 . 7 ASP HB3 H 2.497 0.03 2 41 . 8 LYS H H 9.090 0.03 1 42 . 8 LYS HA H 3.977 0.03 1 43 . 8 LYS HB2 H 1.903 0.03 2 44 . 8 LYS HB3 H 1.863 0.03 2 45 . 8 LYS HG2 H 1.584 0.03 2 46 . 8 LYS HG3 H 1.475 0.03 2 47 . 8 LYS HD2 H 1.753 0.03 1 48 . 8 LYS HD3 H 1.753 0.03 1 49 . 9 ASN H H 8.778 0.03 1 50 . 9 ASN HA H 4.728 0.03 1 51 . 9 ASN HB2 H 3.016 0.03 2 52 . 9 ASN HB3 H 2.842 0.03 2 53 . 10 THR H H 7.868 0.03 1 54 . 10 THR HA H 4.473 0.03 1 55 . 10 THR HB H 4.566 0.03 1 56 . 10 THR HG2 H 1.172 0.03 1 57 . 11 GLY H H 8.817 0.03 1 58 . 11 GLY HA2 H 4.301 0.03 2 59 . 11 GLY HA3 H 3.574 0.03 2 60 . 12 CYS H H 8.100 0.03 1 61 . 12 CYS HA H 4.988 0.03 1 62 . 12 CYS HB2 H 3.591 0.03 2 63 . 12 CYS HB3 H 2.904 0.03 2 64 . 14 TYR H H 9.240 0.03 1 65 . 14 TYR HA H 4.643 0.03 1 66 . 14 TYR HB2 H 2.884 0.03 1 67 . 14 TYR HB3 H 2.884 0.03 1 68 . 14 TYR HE1 H 6.618 0.03 1 69 . 14 TYR HE2 H 6.618 0.03 1 70 . 14 TYR HD1 H 7.061 0.03 1 71 . 14 TYR HD2 H 7.061 0.03 1 72 . 16 CYS H H 8.192 0.03 1 73 . 16 CYS HA H 4.846 0.03 1 74 . 16 CYS HB2 H 3.327 0.03 2 75 . 16 CYS HB3 H 3.163 0.03 2 76 . 17 LEU H H 8.266 0.03 1 77 . 17 LEU HA H 4.671 0.03 1 78 . 17 LEU HG H 1.252 0.03 1 79 . 17 LEU HD1 H 0.524 0.03 2 80 . 17 LEU HD2 H 0.373 0.03 2 81 . 19 LEU H H 8.310 0.03 1 82 . 19 LEU HA H 3.690 0.03 1 83 . 19 LEU HB2 H 1.718 0.03 2 84 . 19 LEU HB3 H 1.393 0.03 2 85 . 19 LEU HG H 1.492 0.03 1 86 . 19 LEU HD1 H 0.734 0.03 2 87 . 19 LEU HD2 H 0.124 0.03 2 88 . 20 GLY H H 9.046 0.03 1 89 . 20 GLY HA2 H 4.337 0.03 2 90 . 20 GLY HA3 H 3.682 0.03 2 91 . 21 ASP H H 8.581 0.03 1 92 . 21 ASP HA H 4.676 0.03 1 93 . 21 ASP HB2 H 2.806 0.03 2 94 . 21 ASP HB3 H 2.693 0.03 2 95 . 22 ASN H H 9.166 0.03 1 96 . 22 ASN HA H 4.842 0.03 1 97 . 22 ASN HB2 H 3.023 0.03 2 98 . 22 ASN HB3 H 2.675 0.03 2 99 . 23 ASP H H 9.057 0.03 1 100 . 23 ASP HA H 4.555 0.03 1 101 . 23 ASP HB2 H 2.793 0.03 1 102 . 23 ASP HB3 H 2.793 0.03 1 103 . 24 TYR H H 8.065 0.03 1 104 . 24 TYR HA H 4.353 0.03 1 105 . 24 TYR HB2 H 3.282 0.03 2 106 . 24 TYR HB3 H 3.420 0.03 2 107 . 24 TYR HE1 H 6.888 0.03 1 108 . 24 TYR HE2 H 6.888 0.03 1 109 . 24 TYR HD1 H 7.119 0.03 1 110 . 24 TYR HD2 H 7.119 0.03 1 111 . 25 CYS H H 8.215 0.03 1 112 . 25 CYS HA H 4.246 0.03 1 113 . 25 CYS HB2 H 2.495 0.03 2 114 . 25 CYS HB3 H 2.732 0.03 2 115 . 26 LEU H H 8.261 0.03 1 116 . 26 LEU HA H 3.741 0.03 1 117 . 26 LEU HB2 H 1.754 0.03 2 118 . 26 LEU HB3 H 2.061 0.03 2 119 . 26 LEU HG H 1.584 0.03 1 120 . 26 LEU HD1 H 1.066 0.03 2 121 . 26 LEU HD2 H 1.191 0.03 2 122 . 27 ARG H H 8.054 0.03 1 123 . 27 ARG HA H 3.882 0.03 1 124 . 27 ARG HB2 H 1.843 0.03 2 125 . 27 ARG HB3 H 1.999 0.03 2 126 . 27 ARG HG2 H 1.184 0.03 2 127 . 27 ARG HG3 H 1.590 0.03 2 128 . 28 GLU H H 8.379 0.03 1 129 . 28 GLU HA H 3.873 0.03 1 130 . 28 GLU HB2 H 1.435 0.03 2 131 . 28 GLU HB3 H 1.680 0.03 2 132 . 28 GLU HG2 H 1.982 0.03 1 133 . 28 GLU HG3 H 1.982 0.03 1 134 . 29 CYS H H 8.712 0.03 1 135 . 29 CYS HA H 4.343 0.03 1 136 . 29 CYS HB2 H 2.797 0.03 2 137 . 29 CYS HB3 H 2.992 0.03 2 138 . 30 LYS H H 7.995 0.03 1 139 . 30 LYS HA H 4.542 0.03 1 140 . 30 LYS HB2 H 1.657 0.03 2 141 . 30 LYS HB3 H 1.788 0.03 2 142 . 30 LYS HG2 H 1.584 0.03 1 143 . 30 LYS HG3 H 1.584 0.03 1 144 . 31 GLN H H 8.212 0.03 1 145 . 31 GLN HA H 3.915 0.03 1 146 . 31 GLN HB2 H 2.112 0.03 1 147 . 31 GLN HB3 H 2.112 0.03 1 148 . 31 GLN HG2 H 2.391 0.03 1 149 . 31 GLN HG3 H 2.391 0.03 1 150 . 32 GLN H H 7.480 0.03 1 151 . 32 GLN HA H 4.138 0.03 1 152 . 32 GLN HB2 H 1.265 0.03 2 153 . 32 GLN HB3 H 1.590 0.03 2 154 . 32 GLN HG2 H 1.761 0.03 1 155 . 32 GLN HG3 H 1.761 0.03 1 156 . 33 TYR H H 8.324 0.03 1 157 . 33 TYR HA H 4.989 0.03 1 158 . 33 TYR HB2 H 2.657 0.03 2 159 . 33 TYR HB3 H 3.385 0.03 2 160 . 33 TYR HE1 H 6.873 0.03 1 161 . 33 TYR HE2 H 6.873 0.03 1 162 . 33 TYR HD1 H 7.240 0.03 1 163 . 33 TYR HD2 H 7.240 0.03 1 164 . 34 GLY H H 7.878 0.03 1 165 . 34 GLY HA2 H 4.710 0.03 2 166 . 34 GLY HA3 H 3.915 0.03 2 167 . 35 LYS H H 8.274 0.03 1 168 . 35 LYS HA H 3.871 0.03 1 169 . 35 LYS HB2 H 1.904 0.03 1 170 . 35 LYS HB3 H 1.904 0.03 1 171 . 35 LYS HG2 H 1.516 0.03 3 172 . 35 LYS HG3 H 1.516 0.03 3 173 . 36 GLY H H 8.693 0.03 1 174 . 36 GLY HA2 H 4.085 0.03 2 175 . 36 GLY HA3 H 3.747 0.03 2 176 . 37 ALA H H 7.735 0.03 1 177 . 37 ALA HA H 4.627 0.03 1 178 . 37 ALA HB H 1.386 0.03 1 179 . 38 GLY H H 7.831 0.03 1 180 . 38 GLY HA2 H 4.540 0.03 2 181 . 38 GLY HA3 H 3.498 0.03 2 182 . 39 GLY H H 7.921 0.03 1 183 . 39 GLY HA2 H 4.884 0.03 2 184 . 39 GLY HA3 H 4.615 0.03 2 185 . 40 TYR H H 8.941 0.03 1 186 . 40 TYR HA H 4.837 0.03 1 187 . 40 TYR HB2 H 3.305 0.03 2 188 . 40 TYR HB3 H 3.102 0.03 2 189 . 40 TYR HE1 H 6.547 0.03 1 190 . 40 TYR HE2 H 6.547 0.03 1 191 . 40 TYR HD1 H 6.866 0.03 1 192 . 40 TYR HD2 H 6.866 0.03 1 193 . 41 CYS H H 9.296 0.03 1 194 . 41 CYS HA H 5.212 0.03 1 195 . 41 CYS HB2 H 3.872 0.03 2 196 . 41 CYS HB3 H 2.991 0.03 2 197 . 42 TYR H H 9.460 0.03 1 198 . 42 TYR HA H 4.953 0.03 1 199 . 42 TYR HB2 H 2.956 0.03 2 200 . 42 TYR HB3 H 2.734 0.03 2 201 . 42 TYR HE1 H 6.401 0.03 1 202 . 42 TYR HE2 H 6.401 0.03 1 203 . 42 TYR HD1 H 6.828 0.03 1 204 . 42 TYR HD2 H 6.828 0.03 1 205 . 43 ALA H H 9.052 0.03 1 206 . 43 ALA HA H 3.482 0.03 1 207 . 43 ALA HB H 1.031 0.03 1 208 . 44 PHE H H 6.233 0.03 1 209 . 44 PHE HA H 4.130 0.03 1 210 . 44 PHE HB2 H 3.289 0.03 1 211 . 44 PHE HB3 H 3.289 0.03 1 212 . 44 PHE HD1 H 7.330 0.03 1 213 . 44 PHE HD2 H 7.330 0.03 1 214 . 44 PHE HE1 H 7.370 0.03 1 215 . 44 PHE HE2 H 7.370 0.03 1 216 . 45 ALA H H 8.121 0.03 1 217 . 45 ALA HA H 5.496 0.03 1 218 . 45 ALA HB H 1.320 0.03 1 219 . 46 CYS H H 8.713 0.03 1 220 . 46 CYS HA H 5.295 0.03 1 221 . 46 CYS HB2 H 2.840 0.03 2 222 . 46 CYS HB3 H 2.702 0.03 2 223 . 47 TRP H H 9.739 0.03 1 224 . 47 TRP HA H 4.622 0.03 1 225 . 47 TRP HB2 H 2.813 0.03 2 226 . 47 TRP HB3 H 2.580 0.03 2 227 . 47 TRP HD1 H 6.168 0.03 1 228 . 47 TRP HE3 H 5.508 0.03 1 229 . 47 TRP HE1 H 10.173 0.03 1 230 . 47 TRP HZ3 H 6.648 0.03 1 231 . 47 TRP HZ2 H 7.124 0.03 1 232 . 47 TRP HH2 H 7.050 0.03 1 233 . 48 CYS H H 8.637 0.03 1 234 . 48 CYS HA H 5.671 0.03 1 235 . 48 CYS HB2 H 3.283 0.03 2 236 . 48 CYS HB3 H 2.231 0.03 2 237 . 49 THR H H 8.051 0.03 1 238 . 49 THR HA H 4.537 0.03 1 239 . 49 THR HB H 4.090 0.03 1 240 . 49 THR HG2 H 1.184 0.03 1 241 . 50 HIS H H 8.830 0.03 1 242 . 50 HIS HA H 4.082 0.03 1 243 . 50 HIS HB2 H 3.468 0.03 2 244 . 50 HIS HB3 H 3.424 0.03 2 245 . 50 HIS HD2 H 7.221 0.03 1 246 . 50 HIS HE1 H 8.586 0.03 1 247 . 51 LEU H H 8.163 0.03 1 248 . 51 LEU HA H 4.182 0.03 1 249 . 51 LEU HB2 H 0.926 0.03 2 250 . 51 LEU HB3 H 0.698 0.03 2 251 . 51 LEU HG H 0.878 0.03 1 252 . 51 LEU HD1 H 0.034 0.03 2 253 . 51 LEU HD2 H -0.401 0.03 2 254 . 52 TYR H H 7.849 0.03 1 255 . 52 TYR HA H 4.585 0.03 1 256 . 52 TYR HB2 H 3.287 0.03 2 257 . 52 TYR HB3 H 3.181 0.03 2 258 . 52 TYR HE1 H 7.001 0.03 1 259 . 52 TYR HE2 H 7.001 0.03 1 260 . 52 TYR HD1 H 7.328 0.03 1 261 . 52 TYR HD2 H 7.328 0.03 1 262 . 53 GLU H H 8.712 0.03 1 263 . 53 GLU HA H 3.794 0.03 1 264 . 53 GLU HB2 H 2.055 0.03 1 265 . 53 GLU HB3 H 2.055 0.03 1 266 . 53 GLU HG2 H 2.440 0.03 1 267 . 53 GLU HG3 H 2.440 0.03 1 268 . 54 GLN H H 7.844 0.03 1 269 . 54 GLN HA H 4.335 0.03 1 270 . 54 GLN HB2 H 2.323 0.03 2 271 . 54 GLN HB3 H 2.024 0.03 2 272 . 54 GLN HG2 H 2.444 0.03 1 273 . 54 GLN HG3 H 2.444 0.03 1 274 . 55 ALA H H 7.375 0.03 1 275 . 55 ALA HA H 4.007 0.03 1 276 . 55 ALA HB H 0.837 0.03 1 277 . 56 ILE H H 8.597 0.03 1 278 . 56 ILE HA H 4.238 0.03 1 279 . 56 ILE HB H 1.868 0.03 1 280 . 56 ILE HG2 H 0.873 0.03 1 281 . 56 ILE HG12 H 1.298 0.03 1 282 . 56 ILE HG13 H 1.298 0.03 1 283 . 56 ILE HD1 H 0.930 0.03 1 284 . 57 VAL H H 8.197 0.03 1 285 . 57 VAL HA H 4.629 0.03 1 286 . 57 VAL HB H 2.307 0.03 1 287 . 57 VAL HG1 H 0.690 0.03 2 288 . 57 VAL HG2 H 0.116 0.03 2 289 . 58 TRP H H 8.552 0.03 1 290 . 58 TRP HA H 4.093 0.03 1 291 . 58 TRP HB2 H 3.029 0.03 2 292 . 58 TRP HB3 H 3.441 0.03 2 293 . 58 TRP HD1 H 7.316 0.03 1 294 . 58 TRP HE1 H 10.125 0.03 1 295 . 58 TRP HZ2 H 7.638 0.03 1 296 . 59 PRO HA H 3.686 0.03 1 297 . 59 PRO HB2 H 1.402 0.03 2 298 . 59 PRO HB3 H 1.313 0.03 2 299 . 59 PRO HG2 H 1.087 0.03 1 300 . 59 PRO HG3 H 1.087 0.03 1 301 . 59 PRO HD2 H 3.390 0.03 2 302 . 59 PRO HD3 H 3.190 0.03 2 303 . 60 LEU H H 8.867 0.03 1 304 . 60 LEU HA H 4.581 0.03 1 305 . 60 LEU HB2 H 1.920 0.03 2 306 . 60 LEU HB3 H 1.638 0.03 2 307 . 60 LEU HG H 1.719 0.03 1 308 . 60 LEU HD1 H 0.959 0.03 2 309 . 60 LEU HD2 H 0.873 0.03 2 310 . 61 PRO HA H 4.188 0.03 1 311 . 61 PRO HB2 H 2.266 0.03 2 312 . 61 PRO HB3 H 1.887 0.03 2 313 . 61 PRO HG2 H 2.049 0.03 1 314 . 61 PRO HG3 H 2.049 0.03 1 315 . 61 PRO HD2 H 3.884 0.03 2 316 . 61 PRO HD3 H 3.739 0.03 2 317 . 62 ASN H H 8.309 0.03 1 318 . 62 ASN HA H 4.682 0.03 1 319 . 62 ASN HB2 H 2.868 0.03 1 320 . 62 ASN HB3 H 2.868 0.03 1 321 . 63 LYS H H 7.048 0.03 1 322 . 63 LYS HA H 4.517 0.03 1 323 . 64 ARG H H 8.581 0.03 1 324 . 64 ARG HA H 4.493 0.03 1 325 . 64 ARG HB2 H 1.819 0.03 2 326 . 64 ARG HB3 H 1.722 0.03 2 327 . 64 ARG HG2 H 1.612 0.03 1 328 . 64 ARG HG3 H 1.612 0.03 1 329 . 65 CYS H H 8.812 0.03 1 330 . 65 CYS HA H 4.769 0.03 1 331 . 65 CYS HB2 H 3.299 0.03 2 332 . 65 CYS HB3 H 3.142 0.03 2 333 . 66 SER H H 8.793 0.03 1 334 . 66 SER HA H 4.516 0.03 1 335 . 66 SER HB2 H 3.980 0.03 2 336 . 66 SER HB3 H 3.933 0.03 2 stop_ save_