data_3466 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton Nuclear Magnetic Resonance Sequential Assignments and Secondary Structure of an Immunoglobulin Light Chain-Binding Domain of Protein L ; _BMRB_accession_number 3466 _BMRB_flat_file_name bmr3466.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Wikstrom Mats . . 2 Sjobring Ulf . . 3 Kastern Willian . . 4 Bjorck Lars . . 5 Drakenberg Torbjorn . . 6 Forsen Sture . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 440 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-22 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Wikstrom, Mats, Sjobring, Ulf, Kastern, Willian, Bjorck, Lars, Drakenberg, Torbjorn, Forsen, Sture, "Proton Nuclear Magnetic Resonance Sequential Assignments and Secondary Structure of an Immunoglobulin Light Chain-Binding Domain of Protein L," Biochemistry 32 (13), 3381-3386 (1993). ; _Citation_title ; Proton Nuclear Magnetic Resonance Sequential Assignments and Secondary Structure of an Immunoglobulin Light Chain-Binding Domain of Protein L ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wikstrom Mats . . 2 Sjobring Ulf . . 3 Kastern Willian . . 4 Bjorck Lars . . 5 Drakenberg Torbjorn . . 6 Forsen Sture . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 32 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3381 _Page_last 3386 _Year 1993 _Details . save_ ################################## # Molecular system description # ################################## save_system_protein_L _Saveframe_category molecular_system _Mol_system_name 'protein L' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'protein L' $protein_L stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_protein_L _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'protein L' _Name_variant 'B1 domain' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 78 _Mol_residue_sequence ; XNKEETPETPETDSEEEVTI KANLIFANGSTQTAEFKGTF EKATSEAYAYADTLKKDNGE YTVDVADKGYTLNIKFAG ; loop_ _Residue_seq_code _Residue_label 1 X 2 ASN 3 LYS 4 GLU 5 GLU 6 THR 7 PRO 8 GLU 9 THR 10 PRO 11 GLU 12 THR 13 ASP 14 SER 15 GLU 16 GLU 17 GLU 18 VAL 19 THR 20 ILE 21 LYS 22 ALA 23 ASN 24 LEU 25 ILE 26 PHE 27 ALA 28 ASN 29 GLY 30 SER 31 THR 32 GLN 33 THR 34 ALA 35 GLU 36 PHE 37 LYS 38 GLY 39 THR 40 PHE 41 GLU 42 LYS 43 ALA 44 THR 45 SER 46 GLU 47 ALA 48 TYR 49 ALA 50 TYR 51 ALA 52 ASP 53 THR 54 LEU 55 LYS 56 LYS 57 ASP 58 ASN 59 GLY 60 GLU 61 TYR 62 THR 63 VAL 64 ASP 65 VAL 66 ALA 67 ASP 68 LYS 69 GLY 70 TYR 71 THR 72 LEU 73 ASN 74 ILE 75 LYS 76 PHE 77 ALA 78 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1HZ5 "Crystal Structures Of The B1 Domain Of Protein L From Peptostreptococcus Magnus, With A Tyrosine To Tryptophan Substitution" 80.77 72 98.41 100.00 2.21e-35 PDB 1HZ6 "Crystal Structures Of The B1 Domain Of Protein L From Peptostreptococcus Magnus With A Tyrosine To Tryptophan Substitution" 80.77 72 98.41 100.00 2.21e-35 PDB 2PTL "Three-Dimensional Solution Structure Of An Immunoglobulin Light Chain- Binding Domain Of Protein L. Comparison With The Igg-Bin" 98.72 78 100.00 100.00 3.21e-45 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $protein_L . 1260 Bacteria . Finegoldia magna 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 $protein_L 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6 . na temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details 'The chemical shift reference is not available at this time.' 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'protein L' _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 ASN HA H 4.78 . 1 2 . 2 ASN HB2 H 2.88 . 2 3 . 2 ASN HB3 H 2.77 . 2 4 . 2 ASN HD21 H 7.65 . 2 5 . 2 ASN HD22 H 6.91 . 2 6 . 3 LYS H H 8.57 . 1 7 . 3 LYS HA H 4.37 . 1 8 . 3 LYS HB2 H 1.89 . 2 9 . 3 LYS HB3 H 1.8 . 2 10 . 3 LYS HG2 H 1.45 . 1 11 . 3 LYS HG3 H 1.45 . 1 12 . 3 LYS HD2 H 1.75 . 1 13 . 3 LYS HD3 H 1.75 . 1 14 . 3 LYS HE2 H 3.01 . 1 15 . 3 LYS HE3 H 3.01 . 1 16 . 4 GLU H H 8.48 . 1 17 . 4 GLU HA H 4.32 . 1 18 . 4 GLU HB2 H 2.08 . 2 19 . 4 GLU HB3 H 1.98 . 2 20 . 4 GLU HG2 H 2.3 . 1 21 . 4 GLU HG3 H 2.3 . 1 22 . 5 GLU H H 8.41 . 1 23 . 5 GLU HA H 4.38 . 1 24 . 5 GLU HB2 H 2.08 . 2 25 . 5 GLU HB3 H 1.96 . 2 26 . 5 GLU HG2 H 2.28 . 1 27 . 5 GLU HG3 H 2.28 . 1 28 . 6 THR H H 8.31 . 1 29 . 6 THR HA H 4.65 . 1 30 . 6 THR HB H 4.19 . 1 31 . 6 THR HG2 H 1.27 . 1 32 . 7 PRO HA H 4.47 . 1 33 . 7 PRO HB2 H 2.32 . 2 34 . 7 PRO HB3 H 1.94 . 2 35 . 7 PRO HG2 H 2.02 . 1 36 . 7 PRO HG3 H 2.02 . 1 37 . 7 PRO HD2 H 3.86 . 2 38 . 7 PRO HD3 H 3.75 . 2 39 . 8 GLU H H 8.54 . 1 40 . 8 GLU HA H 4.33 . 1 41 . 8 GLU HB2 H 2.06 . 2 42 . 8 GLU HB3 H 1.97 . 2 43 . 8 GLU HG2 H 2.25 . 1 44 . 8 GLU HG3 H 2.25 . 1 45 . 9 THR H H 8.28 . 1 46 . 9 THR HA H 4.63 . 1 47 . 9 THR HB H 4.19 . 1 48 . 9 THR HG2 H 1.27 . 1 49 . 10 PRO HA H 4.45 . 1 50 . 10 PRO HB2 H 2.34 . 2 51 . 10 PRO HB3 H 1.92 . 2 52 . 10 PRO HG2 H 2.02 . 1 53 . 10 PRO HG3 H 2.02 . 1 54 . 10 PRO HD2 H 3.86 . 2 55 . 10 PRO HD3 H 3.75 . 2 56 . 11 GLU H H 8.6 . 1 57 . 11 GLU HA H 4.36 . 1 58 . 11 GLU HB2 H 2.11 . 2 59 . 11 GLU HB3 H 2 . 2 60 . 11 GLU HG2 H 2.34 . 1 61 . 11 GLU HG3 H 2.34 . 1 62 . 12 THR H H 8.18 . 1 63 . 12 THR HA H 4.4 . 1 64 . 12 THR HB H 4.25 . 1 65 . 12 THR HG2 H 1.22 . 1 66 . 13 ASP H H 8.42 . 1 67 . 13 ASP HA H 4.68 . 1 68 . 13 ASP HB2 H 2.79 . 2 69 . 13 ASP HB3 H 2.73 . 2 70 . 14 SER H H 8.33 . 1 71 . 14 SER HA H 4.5 . 1 72 . 14 SER HB2 H 3.94 . 2 73 . 14 SER HB3 H 3.88 . 2 74 . 15 GLU H H 8.5 . 1 75 . 15 GLU HA H 4.41 . 1 76 . 15 GLU HB2 H 2.16 . 2 77 . 15 GLU HB3 H 1.99 . 2 78 . 15 GLU HG2 H 2.38 . 1 79 . 15 GLU HG3 H 2.38 . 1 80 . 16 GLU H H 8.33 . 1 81 . 16 GLU HA H 4.26 . 1 82 . 16 GLU HB2 H 2.1 . 2 83 . 16 GLU HB3 H 2.01 . 2 84 . 16 GLU HG2 H 2.34 . 1 85 . 16 GLU HG3 H 2.34 . 1 86 . 17 GLU H H 8.37 . 1 87 . 17 GLU HA H 4.22 . 1 88 . 17 GLU HB2 H 2.11 . 2 89 . 17 GLU HB3 H 1.95 . 2 90 . 17 GLU HG2 H 2.25 . 1 91 . 17 GLU HG3 H 2.25 . 1 92 . 18 VAL H H 9.13 . 1 93 . 18 VAL HA H 4.77 . 1 94 . 18 VAL HB H 2.48 . 1 95 . 18 VAL HG1 H 1.14 . 2 96 . 18 VAL HG2 H .95 . 2 97 . 19 THR H H 8.11 . 1 98 . 19 THR HA H 5.06 . 1 99 . 19 THR HB H 3.92 . 1 100 . 19 THR HG2 H 1.04 . 1 101 . 20 ILE H H 9.36 . 1 102 . 20 ILE HA H 4.79 . 1 103 . 20 ILE HB H 1.87 . 1 104 . 20 ILE HG12 H 1.26 . 2 105 . 20 ILE HG13 H 1.1 . 2 106 . 20 ILE HG2 H .69 . 1 107 . 20 ILE HD1 H .44 . 1 108 . 21 LYS H H 8.73 . 1 109 . 21 LYS HA H 4.84 . 1 110 . 21 LYS HB2 H 1.92 . 1 111 . 21 LYS HB3 H 1.92 . 1 112 . 21 LYS HG2 H 1.48 . 2 113 . 21 LYS HG3 H 1.33 . 2 114 . 21 LYS HD2 H 1.75 . 1 115 . 21 LYS HD3 H 1.75 . 1 116 . 21 LYS HE2 H 3.01 . 1 117 . 21 LYS HE3 H 3.01 . 1 118 . 22 ALA H H 9.31 . 1 119 . 22 ALA HA H 5.48 . 1 120 . 22 ALA HB H 1.36 . 1 121 . 23 ASN H H 9.19 . 1 122 . 23 ASN HA H 5.18 . 1 123 . 23 ASN HB2 H 3.2 . 2 124 . 23 ASN HB3 H 2.53 . 2 125 . 23 ASN HD21 H 7.58 . 2 126 . 23 ASN HD22 H 6.78 . 2 127 . 24 LEU H H 9.36 . 1 128 . 24 LEU HA H 4.94 . 1 129 . 24 LEU HB2 H 1.87 . 1 130 . 24 LEU HB3 H 1.87 . 1 131 . 24 LEU HG H 1.76 . 1 132 . 24 LEU HD1 H 1.04 . 2 133 . 24 LEU HD2 H .93 . 2 134 . 25 ILE H H 9.06 . 1 135 . 25 ILE HA H 4.44 . 1 136 . 25 ILE HB H 1.71 . 1 137 . 25 ILE HG12 H 1.41 . 2 138 . 25 ILE HG13 H .95 . 2 139 . 25 ILE HG2 H 1.02 . 1 140 . 25 ILE HD1 H .78 . 1 141 . 26 PHE H H 8.59 . 1 142 . 26 PHE HA H 4.94 . 1 143 . 26 PHE HB2 H 3.37 . 2 144 . 26 PHE HB3 H 3.08 . 2 145 . 26 PHE HD1 H 7 . 1 146 . 26 PHE HD2 H 7 . 1 147 . 26 PHE HE1 H 6.67 . 1 148 . 26 PHE HE2 H 6.67 . 1 149 . 26 PHE HZ H 6.91 . 1 150 . 27 ALA H H 9.28 . 1 151 . 27 ALA HA H 4.27 . 1 152 . 27 ALA HB H 1.52 . 1 153 . 28 ASN H H 7.97 . 1 154 . 28 ASN HA H 4.68 . 1 155 . 28 ASN HB2 H 3.35 . 2 156 . 28 ASN HB3 H 2.91 . 2 157 . 28 ASN HD21 H 7.66 . 2 158 . 28 ASN HD22 H 6.98 . 2 159 . 29 GLY H H 8.34 . 1 160 . 29 GLY HA2 H 3.73 . 2 161 . 29 GLY HA3 H 4.4 . 2 162 . 30 SER H H 8 . 1 163 . 30 SER HA H 4.63 . 1 164 . 30 SER HB2 H 4.14 . 2 165 . 30 SER HB3 H 4.05 . 2 166 . 31 THR H H 8.32 . 1 167 . 31 THR HA H 5.73 . 1 168 . 31 THR HB H 4.16 . 1 169 . 31 THR HG2 H 1.19 . 1 170 . 32 GLN H H 9.1 . 1 171 . 32 GLN HA H 4.82 . 1 172 . 32 GLN HB2 H 2.31 . 2 173 . 32 GLN HB3 H 2.22 . 2 174 . 32 GLN HG2 H 2.57 . 2 175 . 32 GLN HG3 H 2.5 . 2 176 . 32 GLN HE21 H 7.52 . 2 177 . 32 GLN HE22 H 6.79 . 2 178 . 33 THR H H 8.78 . 1 179 . 33 THR HA H 5.55 . 1 180 . 33 THR HB H 4.05 . 1 181 . 33 THR HG2 H 1.26 . 1 182 . 34 ALA H H 9.21 . 1 183 . 34 ALA HA H 4.6 . 1 184 . 34 ALA HB H 1.14 . 1 185 . 35 GLU H H 7.94 . 1 186 . 35 GLU HA H 5.16 . 1 187 . 35 GLU HB2 H 1.95 . 2 188 . 35 GLU HB3 H 1.7 . 2 189 . 35 GLU HG2 H 2.1 . 1 190 . 35 GLU HG3 H 2.1 . 1 191 . 36 PHE H H 8.96 . 1 192 . 36 PHE HA H 4.61 . 1 193 . 36 PHE HB2 H 3.16 . 2 194 . 36 PHE HB3 H 2.6 . 2 195 . 36 PHE HD1 H 7.1 . 1 196 . 36 PHE HD2 H 7.1 . 1 197 . 36 PHE HE1 H 6.95 . 1 198 . 36 PHE HE2 H 6.95 . 1 199 . 36 PHE HZ H 6.63 . 1 200 . 37 LYS H H 8.79 . 1 201 . 37 LYS HA H 5.7 . 1 202 . 37 LYS HB2 H 1.77 . 2 203 . 37 LYS HB3 H 1.63 . 2 204 . 37 LYS HG2 H 1.48 . 2 205 . 37 LYS HG3 H 1.31 . 2 206 . 37 LYS HD2 H 1.61 . 1 207 . 37 LYS HD3 H 1.61 . 1 208 . 37 LYS HE2 H 2.89 . 1 209 . 37 LYS HE3 H 2.89 . 1 210 . 38 GLY H H 8.52 . 1 211 . 38 GLY HA2 H 4.16 . 2 212 . 38 GLY HA3 H 4.22 . 2 213 . 39 THR H H 8.06 . 1 214 . 39 THR HA H 4.78 . 1 215 . 39 THR HB H 4.37 . 1 216 . 39 THR HG2 H 1.42 . 1 217 . 40 PHE H H 9.52 . 1 218 . 40 PHE HA H 3.78 . 1 219 . 40 PHE HB2 H 3.22 . 2 220 . 40 PHE HB3 H 3.11 . 2 221 . 40 PHE HD1 H 6.96 . 1 222 . 40 PHE HD2 H 6.96 . 1 223 . 40 PHE HE1 H 6.78 . 1 224 . 40 PHE HE2 H 6.78 . 1 225 . 40 PHE HZ H 7.1 . 1 226 . 41 GLU H H 9.2 . 1 227 . 41 GLU HA H 3.99 . 1 228 . 41 GLU HB2 H 2.16 . 2 229 . 41 GLU HB3 H 2.03 . 2 230 . 41 GLU HG2 H 2.41 . 1 231 . 41 GLU HG3 H 2.41 . 1 232 . 42 LYS H H 7.64 . 1 233 . 42 LYS HA H 4.07 . 1 234 . 42 LYS HB2 H 1.94 . 1 235 . 42 LYS HB3 H 1.94 . 1 236 . 42 LYS HG2 H 1.52 . 1 237 . 42 LYS HG3 H 1.52 . 1 238 . 42 LYS HD2 H 1.79 . 1 239 . 42 LYS HD3 H 1.79 . 1 240 . 42 LYS HE2 H 3.07 . 1 241 . 42 LYS HE3 H 3.07 . 1 242 . 43 ALA H H 9.18 . 1 243 . 43 ALA HA H 3.99 . 1 244 . 43 ALA HB H 1.04 . 1 245 . 44 THR H H 7.54 . 1 246 . 44 THR HA H 3.41 . 1 247 . 44 THR HB H 3.97 . 1 248 . 44 THR HG2 H 1.11 . 1 249 . 45 SER H H 7.66 . 1 250 . 45 SER HA H 4.21 . 1 251 . 45 SER HB2 H 4.03 . 1 252 . 45 SER HB3 H 4.03 . 1 253 . 46 GLU H H 8.29 . 1 254 . 46 GLU HA H 3.94 . 1 255 . 46 GLU HB2 H 2.33 . 2 256 . 46 GLU HB3 H 2.11 . 2 257 . 46 GLU HG2 H 2.57 . 1 258 . 46 GLU HG3 H 2.57 . 1 259 . 47 ALA H H 7.44 . 1 260 . 47 ALA HA H 2.67 . 1 261 . 47 ALA HB H .8 . 1 262 . 48 TYR H H 7.58 . 1 263 . 48 TYR HA H 3.97 . 1 264 . 48 TYR HB2 H 3.11 . 2 265 . 48 TYR HB3 H 2.78 . 2 266 . 48 TYR HD1 H 7.26 . 1 267 . 48 TYR HD2 H 7.26 . 1 268 . 48 TYR HE1 H 6.67 . 1 269 . 48 TYR HE2 H 6.67 . 1 270 . 49 ALA H H 8.14 . 1 271 . 49 ALA HA H 4.22 . 1 272 . 49 ALA HB H 1.53 . 1 273 . 50 TYR H H 8.13 . 1 274 . 50 TYR HA H 4.47 . 1 275 . 50 TYR HB2 H 3.32 . 2 276 . 50 TYR HB3 H 3.11 . 2 277 . 50 TYR HD1 H 7.16 . 1 278 . 50 TYR HD2 H 7.16 . 1 279 . 50 TYR HE1 H 6.86 . 1 280 . 50 TYR HE2 H 6.86 . 1 281 . 51 ALA H H 8.27 . 1 282 . 51 ALA HA H 3.77 . 1 283 . 51 ALA HB H .89 . 1 284 . 52 ASP H H 8.73 . 1 285 . 52 ASP HA H 4.87 . 1 286 . 52 ASP HB2 H 3.09 . 2 287 . 52 ASP HB3 H 2.75 . 2 288 . 53 THR H H 7.95 . 1 289 . 53 THR HA H 4.27 . 1 290 . 53 THR HB H 4.39 . 1 291 . 53 THR HG2 H 1.51 . 1 292 . 54 LEU H H 7.62 . 1 293 . 54 LEU HA H 4.42 . 1 294 . 54 LEU HB2 H 2.12 . 1 295 . 54 LEU HB3 H 2.12 . 1 296 . 54 LEU HG H 1.41 . 1 297 . 54 LEU HD1 H 1.08 . 2 298 . 54 LEU HD2 H .68 . 2 299 . 55 LYS H H 7.87 . 1 300 . 55 LYS HA H 4.82 . 1 301 . 55 LYS HB2 H 2.11 . 2 302 . 55 LYS HB3 H 2.05 . 2 303 . 55 LYS HG2 H 1.52 . 1 304 . 55 LYS HG3 H 1.52 . 1 305 . 55 LYS HD2 H 1.92 . 1 306 . 55 LYS HD3 H 1.92 . 1 307 . 55 LYS HE2 H 3.05 . 1 308 . 55 LYS HE3 H 3.05 . 1 309 . 56 LYS H H 7.93 . 1 310 . 56 LYS HA H 4.02 . 1 311 . 56 LYS HB2 H 1.91 . 1 312 . 56 LYS HB3 H 1.91 . 1 313 . 56 LYS HG2 H 1.49 . 1 314 . 56 LYS HG3 H 1.49 . 1 315 . 56 LYS HD2 H 1.75 . 1 316 . 56 LYS HD3 H 1.75 . 1 317 . 56 LYS HE2 H 3.06 . 1 318 . 56 LYS HE3 H 3.06 . 1 319 . 57 ASP H H 7.63 . 1 320 . 57 ASP HA H 4.87 . 1 321 . 57 ASP HB2 H 2.64 . 2 322 . 57 ASP HB3 H 2.36 . 2 323 . 58 ASN H H 7.84 . 1 324 . 58 ASN HA H 4.94 . 1 325 . 58 ASN HB2 H 2.54 . 2 326 . 58 ASN HB3 H 2.16 . 2 327 . 58 ASN HD21 H 7.41 . 2 328 . 58 ASN HD22 H 7.25 . 2 329 . 59 GLY H H 8.49 . 1 330 . 59 GLY HA2 H 3.92 . 2 331 . 59 GLY HA3 H 4.52 . 2 332 . 60 GLU H H 8.05 . 1 333 . 60 GLU HA H 4.07 . 1 334 . 60 GLU HB2 H 2.04 . 2 335 . 60 GLU HB3 H 1.85 . 2 336 . 60 GLU HG2 H 2.39 . 2 337 . 60 GLU HG3 H 2.28 . 2 338 . 61 TYR H H 7.72 . 1 339 . 61 TYR HA H 5.72 . 1 340 . 61 TYR HB2 H 2.02 . 2 341 . 61 TYR HB3 H 1.47 . 2 342 . 61 TYR HD1 H 6.52 . 1 343 . 61 TYR HD2 H 6.52 . 1 344 . 61 TYR HE1 H 6.64 . 1 345 . 61 TYR HE2 H 6.64 . 1 346 . 62 THR H H 8.43 . 1 347 . 62 THR HA H 4.58 . 1 348 . 62 THR HB H 4.2 . 1 349 . 62 THR HG2 H 1.2 . 1 350 . 63 VAL H H 8.65 . 1 351 . 63 VAL HA H 4.87 . 1 352 . 63 VAL HB H 2.07 . 1 353 . 63 VAL HG1 H 1 . 2 354 . 63 VAL HG2 H .9 . 2 355 . 64 ASP H H 9.02 . 1 356 . 64 ASP HA H 5.08 . 1 357 . 64 ASP HB2 H 2.78 . 2 358 . 64 ASP HB3 H 2.7 . 2 359 . 65 VAL H H 8.68 . 1 360 . 65 VAL HA H 4.3 . 1 361 . 65 VAL HB H 2.06 . 1 362 . 65 VAL HG1 H .99 . 1 363 . 65 VAL HG2 H .99 . 1 364 . 66 ALA H H 9.32 . 1 365 . 66 ALA HA H 4.95 . 1 366 . 66 ALA HB H 1.36 . 1 367 . 67 ASP H H 9.13 . 1 368 . 67 ASP HA H 4.44 . 1 369 . 67 ASP HB2 H 2.94 . 2 370 . 67 ASP HB3 H 2.84 . 2 371 . 68 LYS H H 8.99 . 1 372 . 68 LYS HA H 3.88 . 1 373 . 68 LYS HB2 H 2.18 . 1 374 . 68 LYS HB3 H 2.18 . 1 375 . 68 LYS HG2 H 1.49 . 1 376 . 68 LYS HG3 H 1.49 . 1 377 . 68 LYS HD2 H 1.78 . 1 378 . 68 LYS HD3 H 1.78 . 1 379 . 68 LYS HE2 H 3.06 . 1 380 . 68 LYS HE3 H 3.06 . 1 381 . 69 GLY H H 7.68 . 1 382 . 69 GLY HA2 H 3.44 . 2 383 . 69 GLY HA3 H 4.56 . 2 384 . 70 TYR H H 7.72 . 1 385 . 70 TYR HA H 4.59 . 1 386 . 70 TYR HB2 H 3.6 . 2 387 . 70 TYR HB3 H 3.13 . 2 388 . 70 TYR HD1 H 7.54 . 1 389 . 70 TYR HD2 H 7.54 . 1 390 . 70 TYR HE1 H 6.84 . 1 391 . 70 TYR HE2 H 6.84 . 1 392 . 71 THR H H 7.8 . 1 393 . 71 THR HA H 5.3 . 1 394 . 71 THR HB H 3.71 . 1 395 . 71 THR HG2 H 1.04 . 1 396 . 72 LEU H H 9.18 . 1 397 . 72 LEU HA H 4.76 . 1 398 . 72 LEU HB2 H 1.6 . 1 399 . 72 LEU HB3 H 1.6 . 1 400 . 72 LEU HG H 1.42 . 1 401 . 72 LEU HD1 H .81 . 2 402 . 72 LEU HD2 H .47 . 2 403 . 73 ASN H H 8.77 . 1 404 . 73 ASN HA H 5.44 . 1 405 . 73 ASN HB2 H 3.13 . 2 406 . 73 ASN HB3 H 2.45 . 2 407 . 73 ASN HD21 H 7.31 . 2 408 . 73 ASN HD22 H 6.98 . 2 409 . 74 ILE H H 9.33 . 1 410 . 74 ILE HA H 4.46 . 1 411 . 74 ILE HB H 1.72 . 1 412 . 74 ILE HG12 H 1.36 . 2 413 . 74 ILE HG13 H .62 . 2 414 . 74 ILE HG2 H -.04 . 1 415 . 74 ILE HD1 H .37 . 1 416 . 75 LYS H H 8.5 . 1 417 . 75 LYS HA H 5.12 . 1 418 . 75 LYS HB2 H 1.77 . 2 419 . 75 LYS HB3 H 1.57 . 2 420 . 75 LYS HG2 H 1.26 . 1 421 . 75 LYS HG3 H 1.26 . 1 422 . 75 LYS HD2 H 1.62 . 1 423 . 75 LYS HD3 H 1.62 . 1 424 . 75 LYS HE2 H 2.92 . 1 425 . 75 LYS HE3 H 2.92 . 1 426 . 76 PHE H H 8.87 . 1 427 . 76 PHE HA H 4.79 . 1 428 . 76 PHE HB2 H 3.48 . 2 429 . 76 PHE HB3 H 3.09 . 2 430 . 76 PHE HD1 H 7.16 . 1 431 . 76 PHE HD2 H 7.16 . 1 432 . 76 PHE HE1 H 6.98 . 1 433 . 76 PHE HE2 H 6.98 . 1 434 . 76 PHE HZ H 6.92 . 1 435 . 77 ALA H H 9.02 . 1 436 . 77 ALA HA H 4.39 . 1 437 . 77 ALA HB H 1.6 . 1 438 . 78 GLY H H 8.26 . 1 439 . 78 GLY HA2 H 3.63 . 2 440 . 78 GLY HA3 H 3.97 . 2 stop_ save_