data_11589 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A GB1-gp41 fusion protein containing hydrophobic pocket binding domain residues of gp41 ; _BMRB_accession_number 11589 _BMRB_flat_file_name bmr11589.str _Entry_type original _Submission_date 2015-03-06 _Accession_date 2015-03-06 _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 Walsh Joseph D . 2 Chu Shidong . . 3 Zhang Shao-Qing . . 4 Gochin Miriam . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 162 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-12-11 original BMRB . stop_ _Original_release_date 2015-01-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25792539 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Walsh Joseph D . 2 Chu Shidong . . 3 Zhang Shao-Qing . . 4 Gochin Miriam . . stop_ _Journal_abbreviation 'Protein Eng. Des. Sel.' _Journal_name_full 'Protein engineering, design & selection : PEDS' _Journal_volume 28 _Journal_issue 4 _Journal_ISSN 1741-0126 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 107 _Page_last 116 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name GB1(i635) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gp41 hydrophobic pocket binding domain' $GB1(i635) stop_ _System_molecular_weight 10696.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GB1(i635) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GB1(i635) _Molecular_mass 10696.3 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; MGSSHHHHHHSGGSMQYKLI LNGKTLKGETTTEAVDAATA EKVFKQYANDNGVDGEWTYD DATKTFTVTEGGSGGSNKSL EQKANHETWEAWDREI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLY 3 3 SER 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 SER 12 12 GLY 13 13 GLY 14 14 SER 15 15 MET 16 16 GLN 17 17 TYR 18 18 LYS 19 19 LEU 20 20 ILE 21 21 LEU 22 22 ASN 23 23 GLY 24 24 LYS 25 25 THR 26 26 LEU 27 27 LYS 28 28 GLY 29 29 GLU 30 30 THR 31 31 THR 32 32 THR 33 33 GLU 34 34 ALA 35 35 VAL 36 36 ASP 37 37 ALA 38 38 ALA 39 39 THR 40 40 ALA 41 41 GLU 42 42 LYS 43 43 VAL 44 44 PHE 45 45 LYS 46 46 GLN 47 47 TYR 48 48 ALA 49 49 ASN 50 50 ASP 51 51 ASN 52 52 GLY 53 53 VAL 54 54 ASP 55 55 GLY 56 56 GLU 57 57 TRP 58 58 THR 59 59 TYR 60 60 ASP 61 61 ASP 62 62 ALA 63 63 THR 64 64 LYS 65 65 THR 66 66 PHE 67 67 THR 68 68 VAL 69 69 THR 70 70 GLU 71 71 GLY 72 72 GLY 73 73 SER 74 74 GLY 75 75 GLY 76 76 SER 77 77 ASN 78 78 LYS 79 79 SER 80 80 LEU 81 81 GLU 82 82 GLN 83 83 LYS 84 84 ALA 85 85 ASN 86 86 HIS 87 87 GLU 88 88 THR 89 89 TRP 90 90 GLU 91 91 ALA 92 92 TRP 93 93 ASP 94 94 ARG 95 95 GLU 96 96 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GB1(i635) 'E. coli' 562 Eubacteria . Escherichia coli 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 $GB1(i635) 'recombinant technology' . Escherichia coli . pRK603 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GB1(i635) . mM 1.3 2.1 '[U-100% 13C; U-100% 15N]' MES 10 mM . . 'natural abundance' arginine 50 mM . . 'natural abundance' glutamate 50 mM . . 'natural abundance' H2O 90 % . . 'natural abundance' D2O 10 % . . U-2H stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Swiss Federal Institute of Technology' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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 'ionic strength' 0 . M pH 5.5 . pH pressure 1 . atm temperature 298 . K 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 water C 13 protons ppm 4.773 na indirect . . . 0.251449530 water H 1 protons ppm 4.773 internal direct . . . 1.0 water N 15 protons ppm 4.773 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 '2D 1H-15N HSQC' '3D HNCACB' 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 'gp41 hydrophobic pocket binding domain' _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 3 3 SER H H 8.46 . 1 2 3 3 SER CA C 58.25 . 1 3 3 3 SER CB C 63.77 . 1 4 3 3 SER N N 117.85 . 1 5 10 10 HIS H H 8.62 . 1 6 10 10 HIS CA C 55.56 . 1 7 10 10 HIS CB C 29.76 . 1 8 10 10 HIS N N 121.44 . 1 9 11 11 SER H H 8.49 . 1 10 11 11 SER CA C 58.28 . 1 11 11 11 SER CB C 63.93 . 1 12 11 11 SER N N 118.31 . 1 13 12 12 GLY H H 8.52 . 1 14 12 12 GLY CA C 45.33 . 1 15 12 12 GLY N N 111.27 . 1 16 13 13 GLY H H 8.31 . 1 17 13 13 GLY CA C 44.99 . 1 18 13 13 GLY N N 108.68 . 1 19 14 14 SER H H 8.13 . 1 20 14 14 SER CA C 58.58 . 1 21 14 14 SER CB C 64.14 . 1 22 14 14 SER N N 115.02 . 1 23 15 15 MET H H 8.46 . 1 24 15 15 MET CA C 54.54 . 1 25 15 15 MET CB C 35.37 . 1 26 15 15 MET N N 121.29 . 1 27 16 16 GLN H H 7.99 . 1 28 16 16 GLN CA C 55.79 . 1 29 16 16 GLN CB C 30.58 . 1 30 16 16 GLN N N 119.46 . 1 31 17 17 TYR H H 9.19 . 1 32 17 17 TYR CA C 57.19 . 1 33 17 17 TYR CB C 43.25 . 1 34 17 17 TYR N N 124.96 . 1 35 18 18 LYS H H 9.07 . 1 36 18 18 LYS CA C 55.07 . 1 37 18 18 LYS CB C 36.02 . 1 38 18 18 LYS N N 122.27 . 1 39 19 19 LEU H H 8.57 . 1 40 19 19 LEU CA C 52.62 . 1 41 19 19 LEU CB C 42.63 . 1 42 19 19 LEU N N 126.33 . 1 43 20 20 ILE H H 9.04 . 1 44 20 20 ILE CA C 60.19 . 1 45 20 20 ILE CB C 38.09 . 1 46 20 20 ILE N N 126.27 . 1 47 21 21 LEU H H 8.66 . 1 48 21 21 LEU CA C 54.45 . 1 49 21 21 LEU CB C 42.22 . 1 50 21 21 LEU N N 125.77 . 1 51 22 22 ASN H H 8.80 . 1 52 22 22 ASN CA C 51.07 . 1 53 22 22 ASN CB C 38.17 . 1 54 22 22 ASN N N 125.52 . 1 55 23 23 GLY H H 7.91 . 1 56 23 23 GLY CA C 44.74 . 1 57 23 23 GLY N N 109.96 . 1 58 24 24 LYS H H 9.21 . 1 59 24 24 LYS CA C 59.09 . 1 60 24 24 LYS CB C 32.55 . 1 61 24 24 LYS N N 121.21 . 1 62 25 25 THR H H 8.79 . 1 63 25 25 THR CA C 61.82 . 1 64 25 25 THR CB C 69.62 . 1 65 25 25 THR N N 108.83 . 1 66 26 26 LEU H H 7.32 . 1 67 26 26 LEU CA C 54.98 . 1 68 26 26 LEU CB C 43.57 . 1 69 26 26 LEU N N 124.96 . 1 70 27 27 LYS H H 8.11 . 1 71 27 27 LYS CA C 53.88 . 1 72 27 27 LYS CB C 34.72 . 1 73 27 27 LYS N N 123.94 . 1 74 28 28 GLY H H 8.38 . 1 75 28 28 GLY CA C 45.06 . 1 76 28 28 GLY N N 109.46 . 1 77 29 29 GLU H H 8.36 . 1 78 29 29 GLU CA C 54.61 . 1 79 29 29 GLU CB C 33.63 . 1 80 29 29 GLU N N 118.77 . 1 81 30 30 THR H H 8.71 . 1 82 30 30 THR CA C 60.53 . 1 83 30 30 THR CB C 69.42 . 1 84 30 30 THR N N 116.02 . 1 85 31 31 THR H H 8.05 . 1 86 31 31 THR CA C 59.88 . 1 87 31 31 THR CB C 73.22 . 1 88 31 31 THR N N 111.83 . 1 89 32 32 THR H H 8.93 . 1 90 32 32 THR CA C 62.20 . 1 91 32 32 THR CB C 69.83 . 1 92 32 32 THR N N 114.71 . 1 93 33 33 GLU H H 8.00 . 1 94 33 33 GLU CA C 54.75 . 1 95 33 33 GLU CB C 30.86 . 1 96 33 33 GLU N N 124.46 . 1 97 34 34 ALA H H 9.26 . 1 98 34 34 ALA CA C 50.93 . 1 99 34 34 ALA CB C 23.68 . 1 100 34 34 ALA N N 125.15 . 1 101 35 35 VAL H H 8.39 . 1 102 35 35 VAL CA C 63.17 . 1 103 35 35 VAL CB C 31.95 . 1 104 35 35 VAL N N 114.46 . 1 105 36 36 ASP H H 7.32 . 1 106 36 36 ASP CA C 52.67 . 1 107 36 36 ASP CB C 42.00 . 1 108 36 36 ASP N N 114.71 . 1 109 37 37 ALA H H 8.38 . 1 110 37 37 ALA CA C 54.54 . 1 111 37 37 ALA CB C 17.52 . 1 112 37 37 ALA N N 121.60 . 1 113 38 38 ALA H H 8.02 . 1 114 38 38 ALA CA C 54.80 . 1 115 38 38 ALA CB C 17.92 . 1 116 38 38 ALA N N 120.40 . 1 117 39 39 THR H H 8.28 . 1 118 39 39 THR CA C 66.96 . 1 119 39 39 THR CB C 67.72 . 1 120 39 39 THR N N 116.58 . 1 121 40 40 ALA H H 7.02 . 1 122 40 40 ALA CA C 54.80 . 1 123 40 40 ALA CB C 17.24 . 1 124 40 40 ALA N N 123.58 . 1 125 41 41 GLU H H 8.30 . 1 126 41 41 GLU CA C 59.75 . 1 127 41 41 GLU CB C 28.90 . 1 128 41 41 GLU N N 116.50 . 1 129 42 42 LYS H H 7.00 . 1 130 42 42 LYS CA C 59.70 . 1 131 42 42 LYS CB C 32.26 . 1 132 42 42 LYS N N 116.92 . 1 133 43 43 VAL H H 7.30 . 1 134 43 43 VAL CA C 65.90 . 1 135 43 43 VAL CB C 31.69 . 1 136 43 43 VAL N N 120.65 . 1 137 44 44 PHE H H 8.43 . 1 138 44 44 PHE CA C 56.36 . 1 139 44 44 PHE CB C 37.31 . 1 140 44 44 PHE N N 120.63 . 1 141 45 45 LYS H H 9.12 . 1 142 45 45 LYS CA C 59.85 . 1 143 45 45 LYS CB C 31.62 . 1 144 45 45 LYS N N 122.96 . 1 145 46 46 GLN H H 7.42 . 1 146 46 46 GLN CA C 58.80 . 1 147 46 46 GLN CB C 28.21 . 1 148 46 46 GLN N N 119.65 . 1 149 47 47 TYR H H 8.21 . 1 150 47 47 TYR CA C 61.79 . 1 151 47 47 TYR CB C 38.52 . 1 152 47 47 TYR N N 120.96 . 1 153 48 48 ALA H H 9.16 . 1 154 48 48 ALA CA C 56.19 . 1 155 48 48 ALA CB C 17.74 . 1 156 48 48 ALA N N 122.65 . 1 157 49 49 ASN H H 8.26 . 1 158 49 49 ASN CA C 56.99 . 1 159 49 49 ASN CB C 38.75 . 1 160 49 49 ASN N N 117.64 . 1 161 50 50 ASP H H 8.90 . 1 162 50 50 ASP CA C 56.90 . 1 163 50 50 ASP CB C 39.81 . 1 164 50 50 ASP N N 121.46 . 1 165 51 51 ASN H H 7.36 . 1 166 51 51 ASN CA C 53.73 . 1 167 51 51 ASN CB C 39.98 . 1 168 51 51 ASN N N 115.33 . 1 169 52 52 GLY H H 7.77 . 1 170 52 52 GLY CA C 46.77 . 1 171 52 52 GLY N N 108.21 . 1 172 53 53 VAL H H 8.10 . 1 173 53 53 VAL CA C 61.88 . 1 174 53 53 VAL CB C 33.13 . 1 175 53 53 VAL N N 120.71 . 1 176 54 54 ASP H H 8.43 . 1 177 54 54 ASP CA C 52.28 . 1 178 54 54 ASP CB C 43.11 . 1 179 54 54 ASP N N 127.21 . 1 180 55 55 GLY H H 7.97 . 1 181 55 55 GLY CA C 45.50 . 1 182 55 55 GLY N N 107.58 . 1 183 56 56 GLU H H 7.95 . 1 184 56 56 GLU CA C 55.48 . 1 185 56 56 GLU CB C 31.50 . 1 186 56 56 GLU N N 120.56 . 1 187 57 57 TRP H H 9.32 . 1 188 57 57 TRP CA C 57.70 . 1 189 57 57 TRP CB C 30.34 . 1 190 57 57 TRP N N 128.46 . 1 191 58 58 THR H H 9.24 . 1 192 58 58 THR CA C 60.49 . 1 193 58 58 THR CB C 72.18 . 1 194 58 58 THR N N 114.58 . 1 195 59 59 TYR H H 8.56 . 1 196 59 59 TYR CA C 56.83 . 1 197 59 59 TYR CB C 41.50 . 1 198 59 59 TYR N N 120.69 . 1 199 60 60 ASP H H 7.64 . 1 200 60 60 ASP CA C 51.75 . 1 201 60 60 ASP CB C 42.80 . 1 202 60 60 ASP N N 128.46 . 1 203 61 61 ASP H H 8.51 . 1 204 61 61 ASP CA C 56.23 . 1 205 61 61 ASP CB C 42.00 . 1 206 61 61 ASP N N 124.83 . 1 207 62 62 ALA H H 8.27 . 1 208 62 62 ALA CA C 54.98 . 1 209 62 62 ALA CB C 18.34 . 1 210 62 62 ALA N N 119.83 . 1 211 63 63 THR H H 6.96 . 1 212 63 63 THR CA C 60.33 . 1 213 63 63 THR CB C 70.07 . 1 214 63 63 THR N N 103.21 . 1 215 64 64 LYS H H 7.80 . 1 216 64 64 LYS CA C 56.85 . 1 217 64 64 LYS CB C 29.47 . 1 218 64 64 LYS N N 123.27 . 1 219 65 65 THR H H 7.35 . 1 220 65 65 THR CA C 62.15 . 1 221 65 65 THR CB C 71.88 . 1 222 65 65 THR N N 111.08 . 1 223 66 66 PHE H H 10.36 . 1 224 66 66 PHE CA C 57.23 . 1 225 66 66 PHE CB C 42.59 . 1 226 66 66 PHE N N 130.90 . 1 227 67 67 THR H H 9.05 . 1 228 67 67 THR CA C 61.55 . 1 229 67 67 THR CB C 70.98 . 1 230 67 67 THR N N 117.02 . 1 231 68 68 VAL H H 8.20 . 1 232 68 68 VAL CA C 57.87 . 1 233 68 68 VAL CB C 32.27 . 1 234 68 68 VAL N N 123.21 . 1 235 69 69 THR H H 8.35 . 1 236 69 69 THR CA C 60.84 . 1 237 69 69 THR CB C 70.37 . 1 238 69 69 THR N N 123.40 . 1 239 70 70 GLU H H 8.18 . 1 240 70 70 GLU CA C 56.33 . 1 241 70 70 GLU CB C 31.59 . 1 242 70 70 GLU N N 129.40 . 1 243 71 71 GLY H H 8.88 . 1 244 71 71 GLY CA C 45.35 . 1 245 71 71 GLY N N 113.21 . 1 246 72 72 GLY H H 8.31 . 1 247 72 72 GLY CA C 45.14 . 1 248 72 72 GLY N N 108.66 . 1 249 73 73 SER H H 8.38 . 1 250 73 73 SER CA C 58.55 . 1 251 73 73 SER CB C 63.89 . 1 252 73 73 SER N N 115.49 . 1 253 74 74 GLY H H 8.58 . 1 254 74 74 GLY CA C 45.38 . 1 255 74 74 GLY N N 111.08 . 1 256 75 75 GLY H H 8.31 . 1 257 75 75 GLY CA C 45.15 . 1 258 75 75 GLY N N 108.71 . 1 259 76 76 SER H H 8.27 . 1 260 76 76 SER CA C 58.35 . 1 261 76 76 SER CB C 63.79 . 1 262 76 76 SER N N 115.49 . 1 263 77 77 ASN H H 8.51 . 1 264 77 77 ASN CA C 53.36 . 1 265 77 77 ASN CB C 38.58 . 1 266 77 77 ASN N N 120.77 . 1 267 78 78 LYS H H 8.27 . 1 268 78 78 LYS CA C 56.47 . 1 269 78 78 LYS CB C 33.01 . 1 270 78 78 LYS N N 121.83 . 1 271 80 80 LEU H H 8.21 . 1 272 80 80 LEU CA C 55.53 . 1 273 80 80 LEU CB C 42.04 . 1 274 80 80 LEU N N 123.56 . 1 275 81 81 GLU H H 8.24 . 1 276 81 81 GLU CA C 56.78 . 1 277 81 81 GLU CB C 30.00 . 1 278 81 81 GLU N N 121.05 . 1 279 82 82 GLN H H 8.26 . 1 280 82 82 GLN CA C 56.06 . 1 281 82 82 GLN CB C 29.17 . 1 282 82 82 GLN N N 121.15 . 1 283 83 83 LYS H H 8.24 . 1 284 83 83 LYS CA C 56.27 . 1 285 83 83 LYS CB C 32.88 . 1 286 83 83 LYS N N 122.21 . 1 287 84 84 ALA H H 8.23 . 1 288 84 84 ALA CA C 52.36 . 1 289 84 84 ALA CB C 19.10 . 1 290 84 84 ALA N N 124.39 . 1 291 85 85 ASN H H 8.28 . 1 292 85 85 ASN CA C 53.23 . 1 293 85 85 ASN CB C 38.66 . 1 294 85 85 ASN N N 117.60 . 1 295 86 86 HIS H H 8.33 . 1 296 86 86 HIS CA C 55.40 . 1 297 86 86 HIS CB C 29.09 . 1 298 86 86 HIS N N 118.65 . 1 299 87 87 GLU H H 8.47 . 1 300 87 87 GLU CA C 56.61 . 1 301 87 87 GLU CB C 29.90 . 1 302 87 87 GLU N N 121.52 . 1 303 88 88 THR H H 8.19 . 1 304 88 88 THR CA C 62.13 . 1 305 88 88 THR CB C 69.60 . 1 306 88 88 THR N N 114.52 . 1 307 89 89 TRP H H 7.94 . 1 308 89 89 TRP CA C 57.12 . 1 309 89 89 TRP CB C 29.28 . 1 310 89 89 TRP N N 122.21 . 1 311 90 90 GLU H H 8.04 . 1 312 90 90 GLU CA C 56.28 . 1 313 90 90 GLU CB C 30.00 . 1 314 90 90 GLU N N 121.97 . 1 315 91 91 ALA H H 8.03 . 1 316 91 91 ALA CA C 52.54 . 1 317 91 91 ALA CB C 18.90 . 1 318 91 91 ALA N N 123.75 . 1 319 92 92 TRP H H 7.82 . 1 320 92 92 TRP CA C 57.23 . 1 321 92 92 TRP CB C 29.24 . 1 322 92 92 TRP N N 119.15 . 1 323 93 93 ASP H H 8.05 . 1 324 93 93 ASP CA C 53.90 . 1 325 93 93 ASP CB C 40.49 . 1 326 93 93 ASP N N 121.02 . 1 327 94 94 ARG H H 8.32 . 1 328 94 94 ARG CA C 56.26 . 1 329 94 94 ARG CB C 30.01 . 1 330 94 94 ARG N N 122.02 . 1 331 96 96 ILE H H 7.69 . 1 332 96 96 ILE CA C 62.83 . 1 333 96 96 ILE CB C 39.60 . 1 334 96 96 ILE N N 125.86 . 1 stop_ save_