data_6222 #Corrected using PDB structure: 1T1TA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 7 V HA 5.06 4.27 # 13 K HA 3.78 4.62 # 15 I HA 4.08 3.27 # 18 Y HA 3.84 4.69 # 38 W HA 5.23 4.49 # 40 W HA 4.19 5.54 # 42 L HA 3.93 4.64 # 43 S HA 5.49 3.84 # 49 L HA 3.85 4.86 # 58 S HA 4.44 3.50 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 N/A N/A N/A N/A 0.08 # #bmr6222.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6222.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A N/A +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.446 N/A N/A N/A N/A 0.597 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.192 N/A N/A N/A N/A 0.376 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Kurtoxin ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee C. W. . 2 Min H. J. . 3 Cho E. M. . 4 Kohno T. . . 5 Eu Y. J. . 6 Kim J. I. . stop_ _BMRB_accession_number 6222 _BMRB_flat_file_name bmr6222.str _Entry_type new _Submission_date 2004-05-29 _Accession_date 2004-06-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 386 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution Structure of Kurtoxin ; _Citation_status 'in preparation' _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee C. W. . 2 Min H. J. . 3 Cho E. M. . 4 Kohno T. . . 5 Eu Y. J. . 6 Kim J. I. . stop_ _Journal_abbreviation ? _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year ? loop_ _Keyword "Cysteine stabilized alpha-beta" stop_ save_ ################################## # Molecular system description # ################################## save_neurotoxin _Saveframe_category molecular_system _Mol_system_name Kurtoxin _Abbreviation_common neurotoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Kurtoxin $Kurtoxin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1T1T ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_Kurtoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "scorpion toxin" _Name_variant . _Abbreviation_common kurtoxin _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 63 _Mol_residue_sequence ; KIDGYPVDYWNCKRICWYNN KYCNDLCKGLKADSGYCWGW TLSCYCQGLPDNARIKRSGR CRA ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 ILE 3 ASP 4 GLY 5 TYR 6 PRO 7 VAL 8 ASP 9 TYR 10 TRP 11 ASN 12 CYS 13 LYS 14 ARG 15 ILE 16 CYS 17 TRP 18 TYR 19 ASN 20 ASN 21 LYS 22 TYR 23 CYS 24 ASN 25 ASP 26 LEU 27 CYS 28 LYS 29 GLY 30 LEU 31 LYS 32 ALA 33 ASP 34 SER 35 GLY 36 TYR 37 CYS 38 TRP 39 GLY 40 TRP 41 THR 42 LEU 43 SER 44 CYS 45 TYR 46 CYS 47 GLN 48 GLY 49 LEU 50 PRO 51 ASP 52 ASN 53 ALA 54 ARG 55 ILE 56 LYS 57 ARG 58 SER 59 GLY 60 ARG 61 CYS 62 ARG 63 ALA stop_ _Sequence_homology_query_date 2006-01-30 _Sequence_homology_query_revised_last_date 2006-01-24 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 1T1T "A Chain A, Solution Structure Of Kurtoxin" 100.00 63 100 100 8e-37 SWISS-PROT P58910 "KURT_PARTR Kurtoxin (Ktx)" 100.00 63 100 100 8e-37 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _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 Kurtoxin 12 CYS SG Kurtoxin 61 CYS SG single disulfide Kurtoxin 16 CYS SG Kurtoxin 37 CYS SG single disulfide Kurtoxin 23 CYS SG Kurtoxin 44 CYS SG single disulfide Kurtoxin 27 CYS SG Kurtoxin 46 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 $Kurtoxin "South African fattail scorpion" 170972 Eukaryota Metazoa Parabuthus "Parabuthus transvaalicus" 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 $Kurtoxin 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Kurtoxin 1 mM "[U-15N; U-13C]" CD3CN 25 % . D2O 10 % . H2O 65 % . stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version 2.5 loop_ _Task processing stop_ _Details "Boucher, W." save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task "data analysis" stop_ _Details "Kraulis, P. J." save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task "structure solution" "refinement" stop_ _Details "Brunger, A. T." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D NOESY 2D TOCSY DQF-COSY 3D 15N-separated NOESY HNHA E-COSY ; save_ ####################### # Sample conditions # ####################### save_sample_condition_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.2 pH temperature 288 1 K 'ionic strength' 0 . M pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Kurtoxin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 LYS H H 8.52 0.02 1 2 1 LYS HA H 4.21 0.02 1 3 1 LYS HB2 H 1.80 0.02 1 4 1 LYS HB3 H 1.80 0.02 1 5 1 LYS HG3 H 1.11 0.02 2 6 1 LYS HG2 H 0.85 0.02 2 7 1 LYS HD3 H 1.60 0.02 2 8 1 LYS HD2 H 1.44 0.02 2 9 1 LYS HE2 H 3.04 0.02 1 10 1 LYS HE3 H 3.04 0.02 1 11 1 LYS HZ H 7.73 0.02 1 12 2 ILE H H 9.01 0.02 1 13 2 ILE HA H 4.65 0.02 1 14 2 ILE HB H 1.78 0.02 1 15 2 ILE HG12 H 0.84 0.02 1 16 2 ILE HG13 H 0.84 0.02 1 17 2 ILE HD1 H 0.69 0.02 1 18 3 ASP H H 7.98 0.02 1 19 3 ASP HA H 5.21 0.02 1 20 3 ASP HB3 H 2.75 0.02 2 21 3 ASP HB2 H 2.51 0.02 2 22 4 GLY H H 7.74 0.02 1 23 4 GLY HA3 H 3.91 0.02 2 24 4 GLY HA2 H 3.51 0.02 2 25 5 TYR H H 8.83 0.02 1 26 5 TYR HA H 5.19 0.02 1 27 5 TYR HB3 H 3.06 0.02 2 28 5 TYR HB2 H 2.91 0.02 2 29 5 TYR HD1 H 7.50 0.02 1 30 5 TYR HD2 H 7.50 0.02 1 31 5 TYR HE1 H 6.75 0.02 1 32 5 TYR HE2 H 6.75 0.02 1 33 6 PRO HA H 4.75 0.02 1 34 6 PRO HB2 H 1.72 0.02 1 35 6 PRO HB3 H 1.72 0.02 1 36 6 PRO HG3 H 2.14 0.02 2 37 6 PRO HG2 H 2.08 0.02 2 38 6 PRO HD2 H 3.55 0.02 1 39 6 PRO HD3 H 3.55 0.02 1 40 7 VAL H H 7.22 0.02 1 41 7 VAL HA H 5.10 0.02 1 42 7 VAL HB H 1.87 0.02 1 43 7 VAL HG2 H 0.59 0.02 2 44 7 VAL HG1 H 0.55 0.02 2 45 8 ASP H H 8.20 0.02 1 46 8 ASP HA H 4.53 0.02 1 47 8 ASP HB3 H 3.41 0.02 2 48 8 ASP HB2 H 2.57 0.02 2 49 9 TYR H H 7.77 0.02 1 50 9 TYR HA H 3.82 0.02 1 51 9 TYR HB3 H 2.57 0.02 2 52 9 TYR HB2 H 2.37 0.02 2 53 9 TYR HD1 H 6.21 0.02 1 54 9 TYR HD2 H 6.21 0.02 1 55 9 TYR HE1 H 6.52 0.02 1 56 9 TYR HE2 H 6.52 0.02 1 57 10 TRP H H 7.96 0.02 1 58 10 TRP HA H 4.47 0.02 1 59 10 TRP HB3 H 3.48 0.02 2 60 10 TRP HB2 H 3.28 0.02 2 61 10 TRP HD1 H 7.19 0.02 1 62 10 TRP HE1 H 10.16 0.02 1 63 10 TRP HE3 H 7.56 0.02 1 64 10 TRP HZ2 H 7.48 0.02 1 65 10 TRP HZ3 H 7.20 0.02 1 66 10 TRP HH2 H 7.24 0.02 1 67 11 ASN H H 8.19 0.02 1 68 11 ASN HA H 4.11 0.02 1 69 11 ASN HB2 H 3.81 0.02 1 70 11 ASN HB3 H 2.49 0.02 1 71 11 ASN HD21 H 6.72 0.02 2 72 11 ASN HD22 H 7.15 0.02 2 73 12 CYS H H 8.42 0.02 1 74 12 CYS HA H 4.20 0.02 1 75 12 CYS HB3 H 2.74 0.02 2 76 12 CYS HB2 H 2.56 0.02 2 77 13 LYS H H 8.16 0.02 1 78 13 LYS HA H 3.82 0.02 1 79 13 LYS HB3 H 1.54 0.02 2 80 13 LYS HB2 H 1.22 0.02 2 81 13 LYS HG2 H 1.42 0.02 1 82 13 LYS HG3 H 1.42 0.02 1 83 13 LYS HD3 H 0.74 0.02 2 84 13 LYS HD2 H 0.64 0.02 2 85 13 LYS HE2 H 2.78 0.02 1 86 13 LYS HE3 H 2.78 0.02 1 87 14 ARG H H 8.21 0.02 1 88 14 ARG HA H 4.32 0.02 1 89 14 ARG HB2 H 1.84 0.02 1 90 14 ARG HB3 H 1.84 0.02 1 91 14 ARG HG2 H 1.59 0.02 2 92 14 ARG HG3 H 1.73 0.02 2 93 14 ARG HD2 H 3.16 0.02 1 94 14 ARG HD3 H 3.16 0.02 1 95 14 ARG HE H 7.25 0.02 1 96 15 ILE H H 7.96 0.02 1 97 15 ILE HA H 4.12 0.02 1 98 15 ILE HB H 1.53 0.02 1 99 15 ILE HG2 H 1.74 0.02 1 100 15 ILE HG12 H 1.53 0.02 1 101 15 ILE HG13 H 1.53 0.02 1 102 15 ILE HD1 H 1.31 0.02 1 103 16 CYS H H 8.40 0.02 1 104 16 CYS HA H 4.96 0.02 1 105 16 CYS HB2 H 3.90 0.02 1 106 16 CYS HB3 H 3.27 0.02 1 107 17 TRP H H 8.57 0.02 1 108 17 TRP HA H 4.48 0.02 1 109 17 TRP HB3 H 1.81 0.02 1 110 17 TRP HB2 H 1.81 0.02 1 111 17 TRP HD1 H 7.07 0.02 1 112 17 TRP HE1 H 10.01 0.02 1 113 17 TRP HE3 H 6.79 0.02 1 114 17 TRP HZ2 H 7.43 0.02 1 115 17 TRP HZ3 H 7.06 0.02 1 116 17 TRP HH2 H 7.17 0.02 1 117 18 TYR H H 6.73 0.02 1 118 18 TYR HA H 3.88 0.02 1 119 18 TYR HB3 H 3.09 0.02 2 120 18 TYR HB2 H 2.85 0.02 2 121 18 TYR HD1 H 6.48 0.02 1 122 18 TYR HD2 H 6.48 0.02 1 123 18 TYR HE1 H 6.33 0.02 1 124 18 TYR HE2 H 6.33 0.02 1 125 19 ASN H H 6.52 0.02 1 126 19 ASN HA H 4.99 0.02 1 127 19 ASN HB3 H 3.18 0.02 1 128 19 ASN HB2 H 2.80 0.02 1 129 20 ASN H H 8.80 0.02 1 130 20 ASN HA H 4.45 0.02 1 131 20 ASN HB3 H 3.13 0.02 2 132 20 ASN HB2 H 2.90 0.02 2 133 21 LYS H H 8.50 0.02 1 134 21 LYS HA H 4.07 0.02 1 135 21 LYS HB2 H 1.99 0.02 1 136 21 LYS HB3 H 1.99 0.02 1 137 21 LYS HG2 H 1.71 0.02 2 138 21 LYS HG3 H 1.76 0.02 2 139 21 LYS HD3 H 1.54 0.02 2 140 21 LYS HD2 H 1.46 0.02 2 141 21 LYS HE2 H 2.67 0.02 1 142 21 LYS HE3 H 2.67 0.02 1 143 22 TYR H H 7.84 0.02 1 144 22 TYR HA H 4.27 0.02 1 145 22 TYR HB3 H 2.92 0.02 2 146 22 TYR HB2 H 2.82 0.02 2 147 23 CYS H H 7.07 0.02 1 148 23 CYS HA H 4.22 0.02 1 149 23 CYS HB3 H 3.37 0.02 2 150 23 CYS HB2 H 3.19 0.02 2 151 24 ASN H H 9.07 0.02 1 152 24 ASN HA H 3.98 0.02 1 153 24 ASN HB3 H 2.95 0.02 2 154 24 ASN HB2 H 2.88 0.02 2 155 24 ASN HD21 H 6.73 0.02 1 156 24 ASN HD22 H 6.73 0.02 1 157 25 ASP H H 8.42 0.02 1 158 25 ASP HA H 4.61 0.02 1 159 25 ASP HB2 H 2.73 0.02 1 160 25 ASP HB3 H 2.73 0.02 1 161 26 LEU H H 7.79 0.02 1 162 26 LEU HA H 4.76 0.02 1 163 26 LEU HB2 H 1.72 0.02 1 164 26 LEU HB3 H 1.72 0.02 1 165 26 LEU HG H 1.58 0.02 1 166 26 LEU HD2 H 1.05 0.02 2 167 26 LEU HD1 H 0.76 0.02 2 168 27 CYS H H 8.72 0.02 1 169 27 CYS HA H 4.03 0.02 1 170 27 CYS HB3 H 2.69 0.02 1 171 27 CYS HB2 H 2.51 0.02 1 172 28 LYS H H 8.67 0.02 1 173 28 LYS HA H 4.22 0.02 1 174 28 LYS HB2 H 1.78 0.02 1 175 28 LYS HB3 H 1.78 0.02 1 176 28 LYS HG2 H 1.33 0.02 1 177 28 LYS HG3 H 1.33 0.02 1 178 28 LYS HD2 H 1.51 0.02 1 179 28 LYS HD3 H 1.51 0.02 1 180 28 LYS HE2 H 2.97 0.02 1 181 28 LYS HE3 H 2.97 0.02 1 182 28 LYS HZ H 7.50 0.02 1 183 29 GLY H H 8.08 0.02 1 184 29 GLY HA2 H 3.91 0.02 1 185 29 GLY HA3 H 3.91 0.02 1 186 30 LEU H H 7.23 0.02 1 187 30 LEU HA H 4.32 0.02 1 188 30 LEU HB2 H 1.88 0.02 1 189 30 LEU HB3 H 1.88 0.02 1 190 30 LEU HG H 1.75 0.02 1 191 30 LEU HD1 H 0.80 0.02 2 192 30 LEU HD2 H 1.56 0.02 2 193 31 LYS H H 7.69 0.02 1 194 31 LYS HA H 3.84 0.02 1 195 31 LYS HB2 H 2.03 0.02 1 196 31 LYS HB3 H 2.26 0.02 1 197 31 LYS HG3 H 1.39 0.02 2 198 31 LYS HG2 H 1.28 0.02 2 199 31 LYS HD3 H 1.66 0.02 2 200 31 LYS HD2 H 1.60 0.02 2 201 31 LYS HE2 H 2.99 0.02 1 202 31 LYS HE3 H 2.99 0.02 1 203 31 LYS HZ H 7.50 0.02 1 204 32 ALA H H 7.99 0.02 1 205 32 ALA HA H 4.70 0.02 1 206 32 ALA HB H 1.13 0.02 1 207 33 ASP H H 8.31 0.02 1 208 33 ASP HA H 4.65 0.02 1 209 33 ASP HB3 H 3.23 0.02 2 210 33 ASP HB2 H 2.99 0.02 2 211 34 SER H H 7.96 0.02 1 212 34 SER HA H 4.63 0.02 1 213 34 SER HB3 H 4.03 0.02 2 214 34 SER HB2 H 3.97 0.02 2 215 35 GLY H H 8.72 0.02 1 216 35 GLY HA2 H 4.57 0.02 1 217 36 TYR H H 8.63 0.02 1 218 36 TYR HA H 4.87 0.02 1 219 36 TYR HB3 H 3.17 0.02 2 220 36 TYR HB2 H 3.02 0.02 2 221 36 TYR HD1 H 6.94 0.02 1 222 36 TYR HD2 H 6.94 0.02 1 223 36 TYR HE1 H 6.62 0.02 1 224 36 TYR HE2 H 6.62 0.02 1 225 37 CYS H H 9.69 0.02 1 226 37 CYS HA H 5.20 0.02 1 227 37 CYS HB3 H 3.01 0.02 2 228 37 CYS HB2 H 2.88 0.02 2 229 38 TRP H H 9.13 0.02 1 230 38 TRP HA H 5.27 0.02 1 231 38 TRP HB3 H 4.01 0.02 2 232 38 TRP HB2 H 3.02 0.02 2 233 38 TRP HD1 H 6.28 0.02 1 234 38 TRP HE1 H 9.99 0.02 1 235 38 TRP HE3 H 7.77 0.02 1 236 38 TRP HZ2 H 7.41 0.02 1 237 38 TRP HZ3 H 7.10 0.02 1 238 38 TRP HH2 H 7.16 0.02 1 239 39 GLY H H 8.40 0.02 1 240 39 GLY HA3 H 3.60 0.02 2 241 39 GLY HA2 H 3.40 0.02 2 242 40 TRP H H 6.27 0.02 1 243 40 TRP HA H 4.23 0.02 1 244 40 TRP HB3 H 3.24 0.02 1 245 40 TRP HB2 H 2.59 0.02 1 246 40 TRP HD1 H 7.84 0.02 1 247 40 TRP HE1 H 10.43 0.02 1 248 40 TRP HE3 H 7.35 0.02 1 249 40 TRP HZ2 H 7.35 0.02 1 250 40 TRP HZ3 H 7.00 0.02 1 251 40 TRP HH2 H 7.16 0.02 1 252 41 THR H H 7.12 0.02 1 253 41 THR HA H 4.57 0.02 1 254 41 THR HB H 4.48 0.02 1 255 41 THR HG2 H 1.24 0.02 1 256 42 LEU H H 7.97 0.02 1 257 42 LEU HA H 3.97 0.02 1 258 42 LEU HB3 H 1.82 0.02 2 259 42 LEU HB2 H 1.71 0.02 2 260 42 LEU HG H 1.45 0.02 1 261 42 LEU HD2 H 0.76 0.02 2 262 42 LEU HD1 H 0.48 0.02 2 263 43 SER H H 7.53 0.02 1 264 43 SER HA H 5.53 0.02 1 265 43 SER HB3 H 3.84 0.02 2 266 43 SER HB2 H 3.75 0.02 2 267 44 CYS H H 8.92 0.02 1 268 44 CYS HA H 5.37 0.02 1 269 44 CYS HB3 H 2.75 0.02 1 270 44 CYS HB2 H 2.48 0.02 1 271 45 TYR H H 9.23 0.02 1 272 45 TYR HA H 4.28 0.02 1 273 45 TYR HB3 H 2.17 0.02 2 274 45 TYR HB2 H 2.02 0.02 2 275 45 TYR HD1 H 5.49 0.02 1 276 45 TYR HD2 H 5.49 0.02 1 277 45 TYR HE1 H 6.22 0.02 1 278 45 TYR HE2 H 6.22 0.02 1 279 46 CYS H H 8.11 0.02 1 280 46 CYS HA H 5.36 0.02 1 281 46 CYS HB2 H 2.86 0.02 1 282 46 CYS HB3 H 2.26 0.02 1 283 47 GLN H H 8.56 0.02 1 284 47 GLN HA H 4.74 0.02 1 285 47 GLN HB2 H 1.92 0.02 1 286 47 GLN HB3 H 1.92 0.02 1 287 47 GLN HG3 H 2.14 0.02 2 288 47 GLN HG2 H 2.08 0.02 2 289 48 GLY H H 8.77 0.02 1 290 48 GLY HA3 H 4.05 0.02 2 291 48 GLY HA2 H 3.54 0.02 2 292 49 LEU H H 8.72 0.02 1 293 49 LEU HA H 3.89 0.02 1 294 49 LEU HB2 H 1.55 0.02 1 295 49 LEU HB3 H 1.55 0.02 1 296 49 LEU HG H 1.19 0.02 1 297 49 LEU HD2 H 0.75 0.02 1 298 49 LEU HD1 H 0.31 0.02 1 299 50 PRO HA H 4.38 0.02 1 300 50 PRO HB2 H 1.89 0.02 2 301 50 PRO HB3 H 2.32 0.02 2 302 50 PRO HG2 H 2.01 0.02 1 303 50 PRO HG3 H 2.01 0.02 1 304 50 PRO HD2 H 3.38 0.02 1 305 50 PRO HD3 H 3.38 0.02 1 306 51 ASP H H 8.23 0.02 1 307 51 ASP HA H 4.18 0.02 1 308 51 ASP HB3 H 2.57 0.02 1 309 51 ASP HB2 H 2.42 0.02 1 310 52 ASN H H 7.77 0.02 1 311 52 ASN HA H 4.61 0.02 1 312 52 ASN HB3 H 3.08 0.02 1 313 52 ASN HB2 H 2.65 0.02 1 314 52 ASN HD22 H 7.50 0.02 2 315 52 ASN HD21 H 6.66 0.02 2 316 53 ALA H H 7.68 0.02 1 317 53 ALA HA H 4.04 0.02 1 318 53 ALA HB H 1.31 0.02 1 319 54 ARG H H 8.27 0.02 1 320 54 ARG HA H 4.28 0.02 1 321 54 ARG HB3 H 1.74 0.02 2 322 54 ARG HB2 H 1.65 0.02 2 323 54 ARG HG2 H 1.41 0.02 2 324 54 ARG HG3 H 1.65 0.02 2 325 54 ARG HD2 H 3.07 0.02 1 326 54 ARG HD3 H 3.07 0.02 1 327 54 ARG HE H 6.95 0.02 1 328 55 ILE H H 7.60 0.02 1 329 55 ILE HA H 5.12 0.02 1 330 55 ILE HB H 1.74 0.02 1 331 55 ILE HG2 H 0.76 0.02 1 332 55 ILE HG12 H 1.11 0.02 1 333 55 ILE HG13 H 1.11 0.02 1 334 55 ILE HD1 H 0.30 0.02 1 335 56 LYS H H 8.57 0.02 1 336 56 LYS HA H 4.01 0.02 1 337 56 LYS HB2 H 2.13 0.02 1 338 56 LYS HB3 H 2.13 0.02 1 339 56 LYS HG2 H 1.41 0.02 1 340 56 LYS HG3 H 1.41 0.02 1 341 56 LYS HD3 H 1.32 0.02 2 342 56 LYS HD2 H 1.25 0.02 2 343 56 LYS HE2 H 2.93 0.02 1 344 56 LYS HE3 H 2.93 0.02 1 345 56 LYS HZ H 7.51 0.02 1 346 57 ARG H H 9.27 0.02 1 347 57 ARG HA H 4.57 0.02 1 348 57 ARG HB2 H 1.70 0.02 1 349 57 ARG HB3 H 1.70 0.02 1 350 57 ARG HG3 H 1.91 0.02 2 351 57 ARG HG2 H 1.59 0.02 2 352 57 ARG HD2 H 3.15 0.02 1 353 57 ARG HD3 H 3.15 0.02 1 354 57 ARG HE H 7.34 0.02 1 355 58 SER H H 8.15 0.02 1 356 58 SER HA H 4.48 0.02 1 357 58 SER HB2 H 3.88 0.02 1 358 58 SER HB3 H 3.88 0.02 1 359 59 GLY H H 8.38 0.02 1 360 59 GLY HA3 H 4.14 0.02 2 361 59 GLY HA2 H 3.95 0.02 2 362 60 ARG H H 8.42 0.02 1 363 60 ARG HA H 4.45 0.02 1 364 60 ARG HB2 H 1.74 0.02 2 365 60 ARG HB3 H 1.81 0.02 2 366 60 ARG HG2 H 1.64 0.02 1 367 60 ARG HG3 H 1.64 0.02 1 368 60 ARG HD2 H 3.18 0.02 1 369 60 ARG HD3 H 3.18 0.02 1 370 60 ARG HE H 7.21 0.02 1 371 61 CYS H H 8.44 0.02 1 372 61 CYS HA H 4.82 0.02 1 373 61 CYS HB3 H 3.64 0.02 2 374 61 CYS HB2 H 2.75 0.02 2 375 62 ARG H H 9.07 0.02 1 376 62 ARG HA H 4.42 0.02 1 377 62 ARG HB2 H 2.15 0.02 1 378 62 ARG HB3 H 1.97 0.02 1 379 62 ARG HG3 H 1.86 0.02 2 380 62 ARG HG2 H 1.53 0.02 2 381 62 ARG HD2 H 3.18 0.02 1 382 62 ARG HD3 H 3.18 0.02 1 383 62 ARG HE H 7.28 0.02 1 384 63 ALA H H 7.34 0.02 1 385 63 ALA HA H 3.94 0.02 1 386 63 ALA HB H 1.13 0.02 1 stop_ save_