data_5771 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins ; _BMRB_accession_number 5771 _BMRB_flat_file_name bmr5771.str _Entry_type original _Submission_date 2003-04-14 _Accession_date 2003-04-14 _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 Muskett Frederick W. . 2 May Felicity E.B. . 3 Westley Bruce R. . 4 Feeney James . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 266 "15N chemical shifts" 57 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-05-21 original BMRB . stop_ _Original_release_date 2003-04-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins ; _Citation_status 'in preparation' _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 Muskett Frederick W. . 2 May Felicity E.B. . 3 Westley Bruce R. . 4 Feeney James . . stop_ _Journal_abbreviation Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_tff3 _Saveframe_category molecular_system _Mol_system_name 'tff3 dimer' _Abbreviation_common tff3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'tff3 subunit 1' $tff3 'tff3 subunit 2' $tff3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'tff3 subunit 1' 1 'tff3 subunit 2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_tff3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human intestinal trefoil factor 3' _Abbreviation_common tff3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; EEYVGLSANQCAVPAKDRVD CGYPHVTPKECNNRGCCFDS RIPGVPWCFKPLQEAECTF ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLU 3 TYR 4 VAL 5 GLY 6 LEU 7 SER 8 ALA 9 ASN 10 GLN 11 CYS 12 ALA 13 VAL 14 PRO 15 ALA 16 LYS 17 ASP 18 ARG 19 VAL 20 ASP 21 CYS 22 GLY 23 TYR 24 PRO 25 HIS 26 VAL 27 THR 28 PRO 29 LYS 30 GLU 31 CYS 32 ASN 33 ASN 34 ARG 35 GLY 36 CYS 37 CYS 38 PHE 39 ASP 40 SER 41 ARG 42 ILE 43 PRO 44 GLY 45 VAL 46 PRO 47 TRP 48 CYS 49 PHE 50 LYS 51 PRO 52 LEU 53 GLN 54 GLU 55 ALA 56 GLU 57 CYS 58 THR 59 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1E9T 'High Resolution Solution Structure Of Human Intestinal Trefoil Factor' 98.31 59 100.00 100.00 7.74e-27 PDB 1PE3 'Solution Structure Of The Disulphide-Linked Dimer Of Human Intestinal Trefoil Factor (Tff3)' 100.00 59 100.00 100.00 2.07e-27 DBJ BAA95531 'trefoil factor 3, HITF, human intestinal trefoil factor [Homo sapiens]' 100.00 73 100.00 100.00 2.96e-28 DBJ BAB13731 'trefoil factor 3 [Homo sapiens]' 100.00 73 100.00 100.00 2.96e-28 GenBank AAA59981 'secretory protein' 100.00 80 100.00 100.00 1.77e-28 GenBank AAA83628 'intestinal trefoil factor' 100.00 80 100.00 100.00 1.77e-28 GenBank AAH17859 'TFF3 protein [Homo sapiens]' 100.00 73 100.00 100.00 2.96e-28 GenBank AAL28111 'trefoil factor 3 [Homo sapiens]' 50.85 101 100.00 100.00 1.15e-09 GenBank AAX36110 'trefoil factor 3 [synthetic construct]' 100.00 74 100.00 100.00 2.51e-28 REF NP_003217 'trefoil factor 3 precursor [Homo sapiens]' 100.00 130 100.00 100.00 7.80e-29 REF XP_531572 'PREDICTED: trefoil factor 3 [Pan troglodytes]' 100.00 130 98.31 98.31 3.28e-28 SWISS-PROT Q07654 'Trefoil factor 3 precursor (Intestinal trefoil factor) (hP1.B)' 100.00 80 100.00 100.00 1.77e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $tff3 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $tff3 'recombinant technology' 'E. coli' Escherichia coli BL21 CodonPlus-RP . 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 $tff3 . mM 1.0 4.0 [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label . save_ save_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_1H-15N_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HNHA' _Sample_label . save_ save_1H-15N_(CLEANEX-PM)-FHSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N (CLEANEX-PM)-FHSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.01 M pH 6.8 0.1 n/a temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_tff3_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H NOESY' '1H-1H TOCSY' '1H-1H DQF-COSY' '1H-15N HSQC' '1H-15N NOESY-HSQC' '1H-15N TOCSY-HSQC' '1H-15N HNHA' '1H-15N (CLEANEX-PM)-FHSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'tff3 subunit 1' _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 GLU N N 122.3 . 1 2 . 2 GLU H H 8.31 . 1 3 . 2 GLU HA H 4.66 . 1 4 . 2 GLU HB2 H 2.95 . 1 5 . 2 GLU HB3 H 2.95 . 1 6 . 3 TYR N N 123.6 . 1 7 . 3 TYR H H 8.06 . 1 8 . 3 TYR HA H 4.04 . 1 9 . 3 TYR HB2 H 2.95 . 2 10 . 3 TYR HB3 H 1.98 . 2 11 . 3 TYR HD1 H 7.07 . 1 12 . 3 TYR HD2 H 7.07 . 1 13 . 4 VAL N N 112.3 . 1 14 . 4 VAL H H 7.93 . 1 15 . 4 VAL HA H 3.90 . 1 16 . 4 VAL HB H 2.00 . 1 17 . 4 VAL HG1 H 0.88 . 1 18 . 4 VAL HG2 H 0.88 . 1 19 . 6 LEU N N 121.8 . 1 20 . 6 LEU H H 7.87 . 1 21 . 6 LEU HA H 4.45 . 1 22 . 6 LEU HB2 H 1.53 . 1 23 . 6 LEU HB3 H 1.53 . 1 24 . 6 LEU HD1 H 0.74 . 1 25 . 6 LEU HD2 H 0.74 . 1 26 . 7 SER N N 117.5 . 1 27 . 7 SER H H 8.41 . 1 28 . 7 SER HA H 4.47 . 1 29 . 8 ALA N N 124.9 . 1 30 . 8 ALA H H 8.51 . 1 31 . 8 ALA HA H 4.09 . 1 32 . 8 ALA HB H 1.39 . 1 33 . 9 ASN N N 116.1 . 1 34 . 9 ASN H H 8.34 . 1 35 . 9 ASN HA H 4.50 . 1 36 . 9 ASN HB2 H 2.77 . 1 37 . 9 ASN HB3 H 2.77 . 1 38 . 9 ASN ND2 N 113.1 . 1 39 . 9 ASN HD21 H 7.62 . 2 40 . 9 ASN HD22 H 6.92 . 2 41 . 10 GLN N N 118.7 . 1 42 . 10 GLN H H 8.01 . 1 43 . 10 GLN HA H 4.22 . 1 44 . 10 GLN HB2 H 2.40 . 2 45 . 10 GLN HB3 H 2.19 . 2 46 . 10 GLN HG2 H 2.78 . 1 47 . 10 GLN HG3 H 2.78 . 1 48 . 10 GLN NE2 N 111.6 . 1 49 . 10 GLN HE21 H 7.50 . 2 50 . 10 GLN HE22 H 6.81 . 2 51 . 11 CYS N N 113.3 . 1 52 . 11 CYS H H 7.58 . 1 53 . 11 CYS HA H 5.33 . 1 54 . 11 CYS HB2 H 3.52 . 2 55 . 11 CYS HB3 H 2.70 . 2 56 . 12 ALA N N 129.1 . 1 57 . 12 ALA H H 7.32 . 1 58 . 12 ALA HA H 4.57 . 1 59 . 12 ALA HB H 1.38 . 1 60 . 13 VAL N N 123.7 . 1 61 . 13 VAL H H 7.56 . 1 62 . 13 VAL HA H 4.23 . 1 63 . 13 VAL HB H 1.79 . 1 64 . 13 VAL HG1 H 1.22 . 2 65 . 13 VAL HG2 H 0.94 . 2 66 . 14 PRO HD2 H 4.05 . 2 67 . 14 PRO HD3 H 3.73 . 2 68 . 15 ALA N N 125.9 . 1 69 . 15 ALA H H 8.52 . 1 70 . 15 ALA HA H 4.22 . 1 71 . 15 ALA HB H 1.34 . 1 72 . 16 LYS N N 112.8 . 1 73 . 16 LYS H H 8.30 . 1 74 . 16 LYS HA H 4.06 . 1 75 . 16 LYS HB2 H 1.74 . 1 76 . 16 LYS HB3 H 1.74 . 1 77 . 16 LYS HG2 H 1.35 . 1 78 . 16 LYS HG3 H 1.35 . 1 79 . 17 ASP N N 118.2 . 1 80 . 17 ASP H H 7.74 . 1 81 . 17 ASP HA H 4.75 . 1 82 . 17 ASP HB2 H 2.79 . 2 83 . 17 ASP HB3 H 2.33 . 2 84 . 18 ARG N N 119.7 . 1 85 . 18 ARG H H 6.90 . 1 86 . 18 ARG HA H 4.18 . 1 87 . 18 ARG HB2 H 1.50 . 2 88 . 18 ARG HB3 H 1.15 . 2 89 . 18 ARG HG2 H 1.60 . 2 90 . 18 ARG HG3 H 0.42 . 2 91 . 18 ARG HD2 H 2.33 . 2 92 . 18 ARG HD3 H 1.82 . 2 93 . 18 ARG NE N 107.7 . 1 94 . 18 ARG HE H 5.49 . 1 95 . 19 VAL N N 126.4 . 1 96 . 19 VAL H H 9.65 . 1 97 . 19 VAL HA H 4.17 . 1 98 . 19 VAL HB H 1.99 . 1 99 . 19 VAL HG1 H 0.99 . 1 100 . 19 VAL HG2 H 0.99 . 1 101 . 20 ASP N N 126.6 . 1 102 . 20 ASP H H 8.67 . 1 103 . 20 ASP HA H 4.48 . 1 104 . 20 ASP HB2 H 2.69 . 2 105 . 20 ASP HB3 H 2.54 . 2 106 . 21 CYS N N 125.5 . 1 107 . 21 CYS H H 8.99 . 1 108 . 21 CYS HA H 4.36 . 1 109 . 21 CYS HB2 H 3.32 . 2 110 . 21 CYS HB3 H 2.91 . 2 111 . 22 GLY N N 107.0 . 1 112 . 22 GLY H H 8.94 . 1 113 . 22 GLY HA2 H 3.68 . 1 114 . 22 GLY HA3 H 3.68 . 1 115 . 23 TYR N N 120.0 . 1 116 . 23 TYR H H 7.56 . 1 117 . 23 TYR HA H 4.95 . 1 118 . 23 TYR HD1 H 6.95 . 1 119 . 23 TYR HD2 H 6.95 . 1 120 . 24 PRO HD2 H 3.70 . 2 121 . 25 HIS N N 115.7 . 1 122 . 25 HIS H H 8.41 . 1 123 . 25 HIS HA H 4.49 . 1 124 . 25 HIS HB2 H 3.31 . 1 125 . 25 HIS HB3 H 3.31 . 1 126 . 26 VAL N N 117.8 . 1 127 . 26 VAL H H 7.41 . 1 128 . 26 VAL HA H 4.28 . 1 129 . 26 VAL HB H 1.89 . 1 130 . 26 VAL HG1 H 1.04 . 1 131 . 26 VAL HG2 H 1.04 . 1 132 . 27 THR N N 114.5 . 1 133 . 27 THR H H 7.67 . 1 134 . 27 THR HA H 4.66 . 1 135 . 27 THR HB H 4.30 . 1 136 . 27 THR HG2 H 1.06 . 1 137 . 28 PRO HA H 3.25 . 1 138 . 28 PRO HD2 H 3.60 . 2 139 . 29 LYS N N 115.7 . 1 140 . 29 LYS H H 7.67 . 1 141 . 29 LYS HA H 3.90 . 1 142 . 29 LYS HB2 H 1.75 . 2 143 . 29 LYS HB3 H 1.61 . 2 144 . 29 LYS HG2 H 1.35 . 1 145 . 29 LYS HG3 H 1.35 . 1 146 . 30 GLU N N 119.5 . 1 147 . 30 GLU H H 7.47 . 1 148 . 30 GLU HA H 3.98 . 1 149 . 30 GLU HB2 H 2.08 . 2 150 . 30 GLU HB3 H 1.88 . 2 151 . 30 GLU HG2 H 2.23 . 1 152 . 30 GLU HG3 H 2.23 . 1 153 . 31 CYS N N 118.0 . 1 154 . 31 CYS H H 8.38 . 1 155 . 31 CYS HA H 3.89 . 1 156 . 31 CYS HB2 H 3.36 . 2 157 . 31 CYS HB3 H 3.10 . 2 158 . 32 ASN N N 117.4 . 1 159 . 32 ASN H H 8.21 . 1 160 . 32 ASN HA H 4.87 . 1 161 . 32 ASN HB2 H 3.89 . 2 162 . 32 ASN HB3 H 2.78 . 2 163 . 32 ASN ND2 N 109.7 . 1 164 . 32 ASN HD21 H 7.75 . 2 165 . 32 ASN HD22 H 7.12 . 2 166 . 33 ASN N N 121.3 . 1 167 . 33 ASN H H 8.55 . 1 168 . 33 ASN HA H 4.49 . 1 169 . 33 ASN HB2 H 2.95 . 2 170 . 33 ASN HB3 H 2.83 . 2 171 . 33 ASN ND2 N 110.6 . 1 172 . 33 ASN HD21 H 7.49 . 2 173 . 33 ASN HD22 H 6.70 . 2 174 . 34 ARG N N 117.5 . 1 175 . 34 ARG H H 7.44 . 1 176 . 34 ARG HA H 4.32 . 1 177 . 34 ARG HB2 H 2.06 . 2 178 . 34 ARG HB3 H 1.80 . 2 179 . 34 ARG HG2 H 1.65 . 2 180 . 34 ARG HG3 H 1.51 . 2 181 . 34 ARG HD2 H 2.72 . 1 182 . 34 ARG HD3 H 2.72 . 1 183 . 35 GLY N N 107.2 . 1 184 . 35 GLY H H 8.05 . 1 185 . 35 GLY HA2 H 4.12 . 2 186 . 35 GLY HA3 H 3.71 . 2 187 . 36 CYS N N 117.0 . 1 188 . 36 CYS H H 7.59 . 1 189 . 36 CYS HA H 4.64 . 1 190 . 37 CYS N N 120.3 . 1 191 . 37 CYS H H 8.55 . 1 192 . 37 CYS HA H 4.12 . 1 193 . 37 CYS HB2 H 2.17 . 2 194 . 37 CYS HB3 H 1.03 . 2 195 . 38 PHE N N 121.8 . 1 196 . 38 PHE H H 8.50 . 1 197 . 38 PHE HA H 5.99 . 1 198 . 38 PHE HB2 H 3.08 . 2 199 . 38 PHE HB3 H 2.64 . 2 200 . 38 PHE HD1 H 7.12 . 1 201 . 38 PHE HD2 H 7.12 . 1 202 . 38 PHE HE1 H 7.38 . 1 203 . 38 PHE HE2 H 7.38 . 1 204 . 39 ASP N N 128.3 . 1 205 . 39 ASP H H 9.08 . 1 206 . 39 ASP HA H 4.54 . 1 207 . 39 ASP HB2 H 3.04 . 2 208 . 39 ASP HB3 H 2.85 . 2 209 . 41 ARG N N 120.2 . 1 210 . 41 ARG H H 7.76 . 1 211 . 41 ARG HA H 3.84 . 1 212 . 41 ARG HB2 H 1.92 . 1 213 . 41 ARG HB3 H 1.92 . 1 214 . 41 ARG HG2 H 1.80 . 2 215 . 41 ARG HG3 H 1.72 . 2 216 . 41 ARG HD2 H 3.16 . 1 217 . 41 ARG HD3 H 3.16 . 1 218 . 42 ILE N N 119.5 . 1 219 . 42 ILE H H 8.09 . 1 220 . 42 ILE HA H 4.63 . 1 221 . 42 ILE HB H 1.67 . 1 222 . 42 ILE HG2 H 0.86 . 1 223 . 42 ILE HG12 H 1.37 . 2 224 . 42 ILE HG13 H 0.97 . 2 225 . 42 ILE HD1 H 0.70 . 1 226 . 43 PRO HA H 4.77 . 1 227 . 43 PRO HB2 H 2.41 . 2 228 . 43 PRO HB3 H 2.01 . 2 229 . 43 PRO HG2 H 2.10 . 2 230 . 44 GLY N N 107.7 . 1 231 . 44 GLY H H 8.71 . 1 232 . 44 GLY HA2 H 3.99 . 2 233 . 44 GLY HA3 H 3.64 . 2 234 . 45 VAL N N 113.7 . 1 235 . 45 VAL H H 7.12 . 1 236 . 45 VAL HA H 4.68 . 1 237 . 45 VAL HG1 H 0.81 . 2 238 . 45 VAL HG2 H 0.67 . 2 239 . 46 PRO HA H 4.17 . 1 240 . 46 PRO HB2 H 2.34 . 2 241 . 46 PRO HB3 H 1.63 . 2 242 . 46 PRO HG2 H 1.92 . 2 243 . 46 PRO HG3 H 1.85 . 2 244 . 46 PRO HD2 H 3.75 . 2 245 . 46 PRO HD3 H 3.38 . 2 246 . 47 TRP N N 124.1 . 1 247 . 47 TRP H H 8.16 . 1 248 . 47 TRP HA H 5.06 . 1 249 . 47 TRP NE1 N 126.9 . 1 250 . 47 TRP HD1 H 7.12 . 1 251 . 47 TRP HE3 H 7.73 . 1 252 . 47 TRP HE1 H 9.72 . 1 253 . 47 TRP HZ3 H 7.31 . 1 254 . 47 TRP HZ2 H 7.44 . 1 255 . 48 CYS N N 118.3 . 1 256 . 48 CYS H H 8.47 . 1 257 . 48 CYS HA H 6.04 . 1 258 . 48 CYS HB2 H 3.55 . 2 259 . 48 CYS HB3 H 2.75 . 2 260 . 49 PHE N N 124.7 . 1 261 . 49 PHE H H 9.15 . 1 262 . 49 PHE HA H 5.84 . 1 263 . 49 PHE HB2 H 3.11 . 2 264 . 49 PHE HB3 H 2.54 . 2 265 . 49 PHE HD1 H 7.30 . 1 266 . 49 PHE HD2 H 6.86 . 1 267 . 50 LYS N N 121.6 . 1 268 . 50 LYS H H 8.42 . 1 269 . 50 LYS HA H 4.53 . 1 270 . 50 LYS HB2 H 2.00 . 1 271 . 50 LYS HB3 H 2.00 . 1 272 . 50 LYS HG2 H 1.59 . 1 273 . 50 LYS HG3 H 1.59 . 1 274 . 50 LYS HD2 H 1.78 . 1 275 . 50 LYS HD3 H 1.78 . 1 276 . 50 LYS HE2 H 3.11 . 1 277 . 50 LYS HE3 H 3.11 . 1 278 . 51 PRO HA H 4.76 . 1 279 . 51 PRO HD2 H 3.84 . 2 280 . 51 PRO HD3 H 3.73 . 2 281 . 52 LEU N N 120.0 . 1 282 . 52 LEU H H 8.61 . 1 283 . 52 LEU HA H 4.21 . 1 284 . 52 LEU HB2 H 1.77 . 1 285 . 52 LEU HB3 H 1.77 . 1 286 . 52 LEU HD1 H 0.95 . 1 287 . 52 LEU HD2 H 0.95 . 1 288 . 53 GLN N N 122.5 . 1 289 . 53 GLN H H 8.38 . 1 290 . 53 GLN HA H 4.27 . 1 291 . 53 GLN HB2 H 2.03 . 2 292 . 53 GLN HB3 H 1.89 . 2 293 . 53 GLN HG2 H 2.38 . 2 294 . 53 GLN HG3 H 2.23 . 2 295 . 53 GLN NE2 N 112.6 . 1 296 . 53 GLN HE21 H 7.52 . 2 297 . 53 GLN HE22 H 6.83 . 2 298 . 54 GLU N N 120.9 . 1 299 . 54 GLU H H 8.34 . 1 300 . 54 GLU HA H 4.29 . 1 301 . 54 GLU HB2 H 2.09 . 2 302 . 54 GLU HB3 H 1.97 . 2 303 . 55 ALA N N 125.3 . 1 304 . 55 ALA H H 8.27 . 1 305 . 55 ALA HA H 4.28 . 1 306 . 55 ALA HB H 1.33 . 1 307 . 56 GLU N N 121.2 . 1 308 . 56 GLU H H 8.48 . 1 309 . 57 CYS N N 120.1 . 1 310 . 57 CYS H H 8.38 . 1 311 . 57 CYS HA H 4.67 . 1 312 . 57 CYS HB2 H 3.06 . 2 313 . 57 CYS HB3 H 2.94 . 2 314 . 58 THR N N 116.5 . 1 315 . 58 THR H H 8.11 . 1 316 . 58 THR HA H 4.34 . 1 317 . 58 THR HB H 4.13 . 1 318 . 58 THR HG2 H 1.13 . 1 319 . 59 PHE N N 127.6 . 1 320 . 59 PHE H H 7.75 . 1 321 . 59 PHE HA H 4.44 . 1 322 . 59 PHE HB2 H 3.13 . 2 323 . 59 PHE HB3 H 2.91 . 2 stop_ save_