data_1639 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential 1H NMR Assignments and Secondary Structure of an IgG-Binding Domain from Protein G ; _BMRB_accession_number 1639 _BMRB_flat_file_name bmr1639.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Lian Lu-Yun . . 2 Yang J. C. . 3 Derrick J. P. . 4 Sutcliffe Michael J. . 5 Roberts G. C.K. . 6 Murphy J. P. . 7 Goward C. R. . 8 Atkinson T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 350 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Lian, Lu-Yun, Yang, J. C., Derrick, J. P., Sutcliffe, Michael J., Roberts, G.C.K., Murphy, J. P., Goward, C. R., Atkinson, T., "Sequential 1H NMR Assignments and Secondary Structure of an IgG-Binding Domain from Protein G," Biochemistry 30, 5335-5340 (1991). ; _Citation_title ; Sequential 1H NMR Assignments and Secondary Structure of an IgG-Binding Domain from Protein G ; _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 Lian Lu-Yun . . 2 Yang J. C. . 3 Derrick J. P. . 4 Sutcliffe Michael J. . 5 Roberts G. C.K. . 6 Murphy J. P. . 7 Goward C. R. . 8 Atkinson T. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5335 _Page_last 5340 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_IgG_Fc_region-binding_protein _Saveframe_category molecular_system _Mol_system_name 'IgG Fc region-binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'IgG Fc region-binding protein' $IgG_Fc_region-binding_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IgG_Fc_region-binding_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'IgG Fc region-binding protein' _Name_variant 'protein G, IgG-binding domain' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; LTPAVTTYKLVINGKTLKGE TTTEAVDAATAEKVFKQYAN DNGVDGEWTYDDATKTFTVT EKPE ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 THR 3 PRO 4 ALA 5 VAL 6 THR 7 THR 8 TYR 9 LYS 10 LEU 11 VAL 12 ILE 13 ASN 14 GLY 15 LYS 16 THR 17 LEU 18 LYS 19 GLY 20 GLU 21 THR 22 THR 23 THR 24 GLU 25 ALA 26 VAL 27 ASP 28 ALA 29 ALA 30 THR 31 ALA 32 GLU 33 LYS 34 VAL 35 PHE 36 LYS 37 GLN 38 TYR 39 ALA 40 ASN 41 ASP 42 ASN 43 GLY 44 VAL 45 ASP 46 GLY 47 GLU 48 TRP 49 THR 50 TYR 51 ASP 52 ASP 53 ALA 54 THR 55 LYS 56 THR 57 PHE 58 THR 59 VAL 60 THR 61 GLU 62 LYS 63 PRO 64 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-06-03 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 1FCC "Crystal Structure Of The C2 Fragment Of Streptococcal Protein G In Complex With The Fc Domain Of Human Igg" 87.50 56 100.00 100.00 1.81e-29 PDB 1UWX "P1.2 Serosubtype Antigen Derived From N. Meningitidis Pora In Complex With Fab Fragment" 98.44 63 98.41 100.00 3.37e-34 PDB 2IGG "Determination Of The Solution Structures Of Domains Ii And Iii Of Protein G From Streptococcus By 1h Nmr" 100.00 64 100.00 100.00 1.08e-35 EMBL CAA37410 "Protein G' [Streptococcus sp. 'group G']" 75.00 185 97.92 100.00 1.95e-22 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $IgG_Fc_region-binding_protein . 1306 Bacteria . Streptococcus sp. G148 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 $IgG_Fc_region-binding_protein 'not available' . Escherichia coli TG2 . 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 4.2 . na temperature 298 . 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 'IgG Fc region-binding protein' _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 THR H H 8.75 . 1 2 . 2 THR HA H 4.72 . 1 3 . 2 THR HB H 4.18 . 1 4 . 2 THR HG2 H 1.33 . 1 5 . 3 PRO HA H 4.45 . 1 6 . 3 PRO HB2 H 1.97 . 2 7 . 3 PRO HB3 H 2.37 . 2 8 . 3 PRO HG2 H 2.05 . 1 9 . 3 PRO HG3 H 2.05 . 1 10 . 3 PRO HD2 H 3.79 . 2 11 . 3 PRO HD3 H 3.95 . 2 12 . 4 ALA H H 8.45 . 1 13 . 4 ALA HA H 4.41 . 1 14 . 4 ALA HB H 1.11 . 1 15 . 5 VAL H H 7.97 . 1 16 . 5 VAL HA H 4.33 . 1 17 . 5 VAL HB H 1.91 . 1 18 . 5 VAL HG1 H .87 . 1 19 . 5 VAL HG2 H .87 . 1 20 . 6 THR H H 8.47 . 1 21 . 6 THR HA H 4.54 . 1 22 . 6 THR HB H 4.08 . 1 23 . 6 THR HG2 H .83 . 1 24 . 7 THR H H 8.24 . 1 25 . 7 THR HA H 4.85 . 1 26 . 7 THR HB H 3.99 . 1 27 . 7 THR HG2 H 1.28 . 1 28 . 8 TYR H H 9.37 . 1 29 . 8 TYR HA H 5.38 . 1 30 . 8 TYR HB2 H 3.42 . 2 31 . 8 TYR HB3 H 2.95 . 2 32 . 8 TYR HD1 H 7.28 . 1 33 . 8 TYR HD2 H 7.28 . 1 34 . 8 TYR HE1 H 7.13 . 1 35 . 8 TYR HE2 H 7.13 . 1 36 . 9 LYS H H 9.15 . 1 37 . 9 LYS HA H 5.29 . 1 38 . 9 LYS HB2 H 1.99 . 2 39 . 9 LYS HB3 H 2.02 . 2 40 . 9 LYS HG2 H 1.5 . 2 41 . 9 LYS HG3 H 1.41 . 2 42 . 9 LYS HD2 H 1.64 . 1 43 . 9 LYS HD3 H 1.64 . 1 44 . 9 LYS HE2 H 2.85 . 2 45 . 9 LYS HE3 H 2.88 . 2 46 . 10 LEU H H 8.7 . 1 47 . 10 LEU HA H 5.05 . 1 48 . 10 LEU HB2 H 1.19 . 2 49 . 10 LEU HB3 H .95 . 2 50 . 10 LEU HG H .86 . 1 51 . 10 LEU HD1 H .44 . 2 52 . 10 LEU HD2 H .54 . 2 53 . 11 VAL H H 9.21 . 1 54 . 11 VAL HA H 4.31 . 1 55 . 11 VAL HB H 2 . 1 56 . 11 VAL HG1 H .88 . 1 57 . 11 VAL HG2 H .88 . 1 58 . 12 ILE H H 8.74 . 1 59 . 12 ILE HA H 4.3 . 1 60 . 12 ILE HB H 1.65 . 1 61 . 12 ILE HG12 H 1.41 . 1 62 . 12 ILE HG13 H 1.41 . 1 63 . 12 ILE HG2 H .76 . 1 64 . 12 ILE HD1 H .69 . 1 65 . 13 ASN H H 8.96 . 1 66 . 13 ASN HA H 5.23 . 1 67 . 13 ASN HB2 H 2.6 . 2 68 . 13 ASN HB3 H 2.95 . 2 69 . 13 ASN HD21 H 7.21 . 2 70 . 13 ASN HD22 H 6.85 . 2 71 . 14 GLY H H 7.88 . 1 72 . 14 GLY HA2 H 4.11 . 2 73 . 14 GLY HA3 H 4.35 . 2 74 . 15 LYS H H 8.85 . 1 75 . 15 LYS HA H 4.17 . 1 76 . 15 LYS HB2 H 1.88 . 1 77 . 15 LYS HB3 H 1.88 . 1 78 . 15 LYS HG2 H 1.51 . 1 79 . 15 LYS HG3 H 1.51 . 1 80 . 15 LYS HD2 H 1.76 . 1 81 . 15 LYS HD3 H 1.76 . 1 82 . 15 LYS HE2 H 3.03 . 1 83 . 15 LYS HE3 H 3.03 . 1 84 . 16 THR H H 8.65 . 1 85 . 16 THR HA H 4.41 . 1 86 . 16 THR HB H 4.22 . 1 87 . 16 THR HG2 H 1.2 . 1 88 . 17 LEU H H 7.93 . 1 89 . 17 LEU HA H 4.32 . 1 90 . 17 LEU HB2 H 1.71 . 1 91 . 17 LEU HB3 H 1.71 . 1 92 . 17 LEU HG H 1.43 . 1 93 . 17 LEU HD1 H .86 . 2 94 . 17 LEU HD2 H .93 . 2 95 . 18 LYS H H 8.06 . 1 96 . 18 LYS HA H 4.85 . 1 97 . 18 LYS HB2 H 1.79 . 2 98 . 18 LYS HB3 H 1.86 . 2 99 . 18 LYS HG2 H 1.53 . 1 100 . 18 LYS HG3 H 1.53 . 1 101 . 18 LYS HD2 H 1.79 . 1 102 . 18 LYS HD3 H 1.79 . 1 103 . 18 LYS HE2 H 3.04 . 1 104 . 18 LYS HE3 H 3.04 . 1 105 . 19 GLY H H 8.3 . 1 106 . 19 GLY HA2 H 4.21 . 2 107 . 19 GLY HA3 H 4.26 . 2 108 . 20 GLU H H 8.4 . 1 109 . 20 GLU HA H 5.68 . 1 110 . 20 GLU HB2 H 2.02 . 2 111 . 20 GLU HB3 H 2.07 . 2 112 . 20 GLU HG2 H 2.31 . 2 113 . 20 GLU HG3 H 2.35 . 2 114 . 21 THR H H 8.81 . 1 115 . 21 THR HA H 4.78 . 1 116 . 21 THR HB H 4.02 . 1 117 . 21 THR HG2 H .63 . 1 118 . 22 THR H H 8.18 . 1 119 . 22 THR HA H 5.91 . 1 120 . 22 THR HB H 4.4 . 1 121 . 22 THR HG2 H 1.25 . 1 122 . 23 THR H H 9.1 . 1 123 . 23 THR HA H 4.71 . 1 124 . 23 THR HB H 3.91 . 1 125 . 23 THR HG2 H .52 . 1 126 . 24 GLU H H 8.08 . 1 127 . 24 GLU HA H 5.5 . 1 128 . 24 GLU HB2 H 1.79 . 2 129 . 24 GLU HB3 H 2.05 . 2 130 . 24 GLU HG2 H 2.35 . 2 131 . 24 GLU HG3 H 2.41 . 2 132 . 25 ALA H H 9.39 . 1 133 . 25 ALA HA H 5.03 . 1 134 . 25 ALA HB H 1.43 . 1 135 . 26 VAL H H 8.7 . 1 136 . 26 VAL HA H 4.43 . 1 137 . 26 VAL HB H 2.28 . 1 138 . 26 VAL HG1 H 1.05 . 1 139 . 26 VAL HG2 H 1.05 . 1 140 . 27 ASP H H 7.41 . 1 141 . 27 ASP HA H 4.82 . 1 142 . 27 ASP HB2 H 3.08 . 1 143 . 27 ASP HB3 H 3.08 . 1 144 . 28 ALA H H 8.45 . 1 145 . 28 ALA HA H 3.37 . 1 146 . 28 ALA HB H 1.23 . 1 147 . 29 ALA H H 8.14 . 1 148 . 29 ALA HA H 4 . 1 149 . 29 ALA HB H 1.35 . 1 150 . 30 THR H H 8.35 . 1 151 . 30 THR HA H 3.76 . 1 152 . 30 THR HB H 4.06 . 1 153 . 30 THR HG2 H 1.28 . 1 154 . 31 ALA H H 7.19 . 1 155 . 31 ALA HA H 3.19 . 1 156 . 31 ALA HB H .61 . 1 157 . 32 GLU H H 8.44 . 1 158 . 32 GLU HA H 2.64 . 1 159 . 32 GLU HB2 H 1.73 . 2 160 . 32 GLU HB3 H 1.82 . 2 161 . 32 GLU HG2 H 1.57 . 2 162 . 32 GLU HG3 H 1.92 . 2 163 . 33 LYS H H 7.11 . 1 164 . 33 LYS HA H 3.82 . 1 165 . 33 LYS HB2 H 1.88 . 1 166 . 33 LYS HB3 H 1.88 . 1 167 . 33 LYS HG2 H 1.36 . 1 168 . 33 LYS HG3 H 1.36 . 1 169 . 33 LYS HD2 H 1.57 . 2 170 . 33 LYS HD3 H 1.65 . 2 171 . 33 LYS HE2 H 2.94 . 1 172 . 33 LYS HE3 H 2.94 . 1 173 . 34 VAL H H 7.36 . 1 174 . 34 VAL HA H 3.66 . 1 175 . 34 VAL HB H 1.83 . 1 176 . 34 VAL HG1 H .96 . 2 177 . 34 VAL HG2 H .85 . 2 178 . 35 PHE H H 8.52 . 1 179 . 35 PHE HA H 4.85 . 1 180 . 35 PHE HB2 H 2.92 . 2 181 . 35 PHE HB3 H 3.46 . 2 182 . 35 PHE HD1 H 6.58 . 1 183 . 35 PHE HD2 H 6.58 . 1 184 . 35 PHE HE1 H 7.06 . 1 185 . 35 PHE HE2 H 7.06 . 1 186 . 35 PHE HZ H 7.21 . 1 187 . 36 LYS H H 9.19 . 1 188 . 36 LYS HA H 4.18 . 1 189 . 36 LYS HB2 H 1.72 . 1 190 . 36 LYS HB3 H 1.72 . 1 191 . 36 LYS HG2 H 1.6 . 1 192 . 36 LYS HG3 H 1.6 . 1 193 . 36 LYS HD2 H 1.75 . 1 194 . 36 LYS HD3 H 1.75 . 1 195 . 36 LYS HE2 H 3.05 . 1 196 . 36 LYS HE3 H 3.05 . 1 197 . 37 GLN H H 7.57 . 1 198 . 37 GLN HA H 4.11 . 1 199 . 37 GLN HB2 H 2.26 . 2 200 . 37 GLN HB3 H 2.3 . 2 201 . 37 GLN HG2 H 2.47 . 2 202 . 37 GLN HG3 H 2.5 . 2 203 . 37 GLN HE21 H 6.95 . 2 204 . 37 GLN HE22 H 7.89 . 2 205 . 38 TYR H H 8.25 . 1 206 . 38 TYR HA H 4.33 . 1 207 . 38 TYR HB2 H 3.37 . 1 208 . 38 TYR HB3 H 3.37 . 1 209 . 38 TYR HD1 H 7.01 . 1 210 . 38 TYR HD2 H 7.01 . 1 211 . 38 TYR HE1 H 6.73 . 1 212 . 38 TYR HE2 H 6.73 . 1 213 . 39 ALA H H 9.24 . 1 214 . 39 ALA HA H 3.84 . 1 215 . 39 ALA HB H 1.87 . 1 216 . 40 ASN H H 8.48 . 1 217 . 40 ASN HA H 4.53 . 1 218 . 40 ASN HB2 H 2.98 . 2 219 . 40 ASN HB3 H 3 . 2 220 . 40 ASN HD21 H 7.14 . 2 221 . 40 ASN HD22 H 7.79 . 2 222 . 41 ASP H H 8.83 . 1 223 . 41 ASP HA H 4.21 . 1 224 . 41 ASP HB2 H 2.83 . 2 225 . 41 ASP HB3 H 2.71 . 2 226 . 42 ASN H H 7.43 . 1 227 . 42 ASN HA H 4.72 . 1 228 . 42 ASN HB2 H 2.11 . 2 229 . 42 ASN HB3 H 2.77 . 2 230 . 42 ASN HD21 H 6.56 . 2 231 . 42 ASN HD22 H 6.75 . 2 232 . 43 GLY H H 7.78 . 1 233 . 43 GLY HA2 H 3.98 . 1 234 . 43 GLY HA3 H 3.98 . 1 235 . 44 VAL H H 8.24 . 1 236 . 44 VAL HA H 4.12 . 1 237 . 44 VAL HB H 1.88 . 1 238 . 44 VAL HG1 H .83 . 2 239 . 44 VAL HG2 H .73 . 2 240 . 45 ASP H H 8.57 . 1 241 . 45 ASP HA H 5 . 1 242 . 45 ASP HB2 H 2.82 . 2 243 . 45 ASP HB3 H 2.71 . 2 244 . 46 GLY H H 8.21 . 1 245 . 46 GLY HA2 H 3.87 . 2 246 . 46 GLY HA3 H 4.21 . 2 247 . 47 GLU H H 8.15 . 1 248 . 47 GLU HA H 4.84 . 1 249 . 47 GLU HB2 H 2.05 . 2 250 . 47 GLU HB3 H 2.16 . 2 251 . 47 GLU HG2 H 2.41 . 2 252 . 47 GLU HG3 H 2.48 . 2 253 . 48 TRP H H 9.39 . 1 254 . 48 TRP HA H 5.37 . 1 255 . 48 TRP HB2 H 3.22 . 2 256 . 48 TRP HB3 H 3.34 . 2 257 . 48 TRP HD1 H 7.6 . 1 258 . 48 TRP HE1 H 10.55 . 1 259 . 48 TRP HE3 H 7.6 . 1 260 . 48 TRP HZ2 H 7.33 . 1 261 . 48 TRP HZ3 H 6.65 . 1 262 . 48 TRP HH2 H 6.77 . 1 263 . 49 THR H H 9.33 . 1 264 . 49 THR HA H 4.88 . 1 265 . 49 THR HB H 4.31 . 1 266 . 49 THR HG2 H 1.26 . 1 267 . 50 TYR H H 8.66 . 1 268 . 50 TYR HA H 5.05 . 1 269 . 50 TYR HB2 H 2.6 . 2 270 . 50 TYR HB3 H 2.93 . 2 271 . 50 TYR HD1 H 6.05 . 1 272 . 50 TYR HD2 H 6.05 . 1 273 . 50 TYR HE1 H 6.47 . 1 274 . 50 TYR HE2 H 6.47 . 1 275 . 51 ASP H H 7.61 . 1 276 . 51 ASP HA H 4.64 . 1 277 . 51 ASP HB2 H 2.69 . 2 278 . 51 ASP HB3 H 2.34 . 2 279 . 52 ASP H H 8.62 . 1 280 . 52 ASP HA H 4.17 . 1 281 . 52 ASP HB2 H 2.6 . 2 282 . 52 ASP HB3 H 2.88 . 2 283 . 53 ALA H H 8.34 . 1 284 . 53 ALA HA H 4.17 . 1 285 . 53 ALA HB H 1.55 . 1 286 . 54 THR H H 7.02 . 1 287 . 54 THR HA H 4.43 . 1 288 . 54 THR HB H 4.43 . 1 289 . 54 THR HG2 H 1.04 . 1 290 . 55 LYS H H 7.88 . 1 291 . 55 LYS HA H 4.24 . 1 292 . 55 LYS HB2 H 2.08 . 1 293 . 55 LYS HB3 H 2.08 . 1 294 . 55 LYS HG2 H 1.91 . 1 295 . 55 LYS HG3 H 1.91 . 1 296 . 56 THR H H 7.42 . 1 297 . 56 THR HA H 5.5 . 1 298 . 56 THR HB H 3.79 . 1 299 . 56 THR HG2 H 1.01 . 1 300 . 57 PHE H H 10.45 . 1 301 . 57 PHE HA H 5.69 . 1 302 . 57 PHE HB2 H 3.23 . 2 303 . 57 PHE HB3 H 3.34 . 2 304 . 57 PHE HD1 H 7.74 . 1 305 . 57 PHE HD2 H 7.74 . 1 306 . 57 PHE HE1 H 7.11 . 1 307 . 57 PHE HE2 H 7.11 . 1 308 . 57 PHE HZ H 6.96 . 1 309 . 58 THR H H 9.19 . 1 310 . 58 THR HA H 5.31 . 1 311 . 58 THR HB H 3.85 . 1 312 . 58 THR HG2 H .98 . 1 313 . 59 VAL H H 8.54 . 1 314 . 59 VAL HA H 4.55 . 1 315 . 59 VAL HB H .05 . 1 316 . 59 VAL HG1 H .36 . 2 317 . 59 VAL HG2 H .42 . 2 318 . 60 THR H H 8.48 . 1 319 . 60 THR HA H 4.77 . 1 320 . 60 THR HB H 3.93 . 1 321 . 60 THR HG2 H 1.24 . 1 322 . 61 GLU H H 8.29 . 1 323 . 61 GLU HA H 4.54 . 1 324 . 61 GLU HB2 H 2.09 . 2 325 . 61 GLU HB3 H 2.21 . 2 326 . 61 GLU HG2 H 2.4 . 2 327 . 61 GLU HG3 H 2.48 . 2 328 . 62 LYS H H 8.73 . 1 329 . 62 LYS HA H 4.63 . 1 330 . 62 LYS HB2 H 1.89 . 2 331 . 62 LYS HB3 H 1.9 . 2 332 . 62 LYS HG2 H 1.57 . 1 333 . 62 LYS HG3 H 1.57 . 1 334 . 62 LYS HD2 H 1.76 . 1 335 . 62 LYS HD3 H 1.76 . 1 336 . 62 LYS HE2 H 3.04 . 1 337 . 62 LYS HE3 H 3.04 . 1 338 . 63 PRO HA H 4.46 . 1 339 . 63 PRO HB2 H 2 . 2 340 . 63 PRO HB3 H 2.32 . 2 341 . 63 PRO HG2 H 2.11 . 1 342 . 63 PRO HG3 H 2.11 . 1 343 . 63 PRO HD2 H 3.75 . 2 344 . 63 PRO HD3 H 3.95 . 2 345 . 64 GLU H H 7.99 . 1 346 . 64 GLU HA H 4.22 . 1 347 . 64 GLU HB2 H 1.96 . 2 348 . 64 GLU HB3 H 2.14 . 2 349 . 64 GLU HG2 H 2.38 . 2 350 . 64 GLU HG3 H 2.41 . 2 stop_ save_