data_5903 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,13C and 15N backbone resonance assignment of the Hyaluronan-binding domain of CD44 ; _BMRB_accession_number 5903 _BMRB_flat_file_name bmr5903.str _Entry_type original _Submission_date 2003-08-15 _Accession_date 2003-08-15 _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 Takeda Mitsuhiro . . 2 Terasawa Hiroaki . . 3 Sakakura Masayosh . . 4 Yamaguchi Yoshiki . . 5 Kajiwara Masahiro . . 6 Kawashima Hiroto . . 7 Miyasaka Masayuki . . 8 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 144 "13C chemical shifts" 284 "15N chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-04-07 original BMRB . stop_ _Original_release_date 2003-08-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the Hyaluronan-binding domain of CD44 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15017146 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takeda Mitsuhiro . . 2 Terasawa Hiroaki . . 3 Sakakura Masayoshi . . 4 Yamaguchi Yoshiki . . 5 Kajiwara Masahiro . . 6 Kawashima Hiroto . . 7 Miyasaka Masayuki . . 8 Shimada Ichio . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 97 _Page_last 98 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_CD44 _Saveframe_category molecular_system _Mol_system_name 'CD44 hyaluronan-binding domain' _Abbreviation_common CD44 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CD44 hyaluronan binding domain' $CD44_hyaluronan-binding_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CD44_hyaluronan-binding_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CD44 hyaluronan-binding domain' _Abbreviation_common CD44 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 160 _Mol_residue_sequence ; MAQIDLNITCRFAGVFHVEK NGRYSISRTEAADLCKAFNS TLPTMAQMEKALSIGFETCR YGFIEGHVVIPRIHPNSICA ANNTGVYILTSNTSQYDTYC FNASAPPEEDCTSVTDLPNA FDGPITITIVNRDGTRYVQK GEYRTNPEDIYPSNPTDDDV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 MET 2 -1 ALA 3 21 GLN 4 22 ILE 5 23 ASP 6 24 LEU 7 25 ASN 8 26 ILE 9 27 THR 10 28 CYS 11 29 ARG 12 30 PHE 13 31 ALA 14 32 GLY 15 33 VAL 16 34 PHE 17 35 HIS 18 36 VAL 19 37 GLU 20 38 LYS 21 39 ASN 22 40 GLY 23 41 ARG 24 42 TYR 25 43 SER 26 44 ILE 27 45 SER 28 46 ARG 29 47 THR 30 48 GLU 31 49 ALA 32 50 ALA 33 51 ASP 34 52 LEU 35 53 CYS 36 54 LYS 37 55 ALA 38 56 PHE 39 57 ASN 40 58 SER 41 59 THR 42 60 LEU 43 61 PRO 44 62 THR 45 63 MET 46 64 ALA 47 65 GLN 48 66 MET 49 67 GLU 50 68 LYS 51 69 ALA 52 70 LEU 53 71 SER 54 72 ILE 55 73 GLY 56 74 PHE 57 75 GLU 58 76 THR 59 77 CYS 60 78 ARG 61 79 TYR 62 80 GLY 63 81 PHE 64 82 ILE 65 83 GLU 66 84 GLY 67 85 HIS 68 86 VAL 69 87 VAL 70 88 ILE 71 89 PRO 72 90 ARG 73 91 ILE 74 92 HIS 75 93 PRO 76 94 ASN 77 95 SER 78 96 ILE 79 97 CYS 80 98 ALA 81 99 ALA 82 100 ASN 83 101 ASN 84 102 THR 85 103 GLY 86 104 VAL 87 105 TYR 88 106 ILE 89 107 LEU 90 108 THR 91 109 SER 92 110 ASN 93 111 THR 94 112 SER 95 113 GLN 96 114 TYR 97 115 ASP 98 116 THR 99 117 TYR 100 118 CYS 101 119 PHE 102 120 ASN 103 121 ALA 104 122 SER 105 123 ALA 106 124 PRO 107 125 PRO 108 126 GLU 109 127 GLU 110 128 ASP 111 129 CYS 112 130 THR 113 131 SER 114 132 VAL 115 133 THR 116 134 ASP 117 135 LEU 118 136 PRO 119 137 ASN 120 138 ALA 121 139 PHE 122 140 ASP 123 141 GLY 124 142 PRO 125 143 ILE 126 144 THR 127 145 ILE 128 146 THR 129 147 ILE 130 148 VAL 131 149 ASN 132 150 ARG 133 151 ASP 134 152 GLY 135 153 THR 136 154 ARG 137 155 TYR 138 156 VAL 139 157 GLN 140 158 LYS 141 159 GLY 142 160 GLU 143 161 TYR 144 162 ARG 145 163 THR 146 164 ASN 147 165 PRO 148 166 GLU 149 167 ASP 150 168 ILE 151 169 TYR 152 170 PRO 153 171 SER 154 172 ASN 155 173 PRO 156 174 THR 157 175 ASP 158 176 ASP 159 177 ASP 160 178 VAL 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 $CD44_hyaluronan-binding_domain 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 _Vector_name $CD44_hyaluronan-binding_domain 'recombinant technology' . . . . . 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 _Isotopic_labeling $CD44_hyaluronan-binding_domain 2.0 mM '[U-98% 13C; U-98% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ ####################### # Sample conditions # ####################### save_EX-condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.1 n/a temperature 298 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449500 DSS H 1 'methyl protons' ppm 0.0 internal . . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329051 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $EX-condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CD44 hyaluronan 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 GLN C C 174.8 0.2 1 2 . 4 ILE H H 8.67 0.01 1 3 . 4 ILE C C 173.1 0.2 1 4 . 4 ILE CA C 61.6 0.4 1 5 . 4 ILE N N 124.5 0.7 1 6 . 5 ASP H H 8.76 0.01 1 7 . 5 ASP C C 174.7 0.2 1 8 . 5 ASP CA C 52.7 0.4 1 9 . 5 ASP N N 128.9 0.7 1 10 . 6 LEU H H 9.46 0.01 1 11 . 6 LEU C C 174.5 0.2 1 12 . 6 LEU CA C 52.6 0.4 1 13 . 6 LEU N N 123.9 0.7 1 14 . 7 ASN H H 8.97 0.01 1 15 . 7 ASN C C 173.8 0.2 1 16 . 7 ASN CA C 52.7 0.4 1 17 . 7 ASN N N 124 0.7 1 18 . 8 ILE H H 8.34 0.01 1 19 . 8 ILE C C 176.2 0.2 1 20 . 8 ILE CA C 59.2 0.4 1 21 . 8 ILE N N 120.8 0.7 1 22 . 9 THR H H 7.99 0.01 1 23 . 9 THR C C 176.7 0.2 1 24 . 9 THR CA C 61.6 0.4 1 25 . 9 THR N N 112.1 0.7 1 26 . 10 CYS H H 8.97 0.01 1 27 . 10 CYS C C 172.5 0.2 1 28 . 10 CYS CA C 59.3 0.4 1 29 . 10 CYS N N 114.8 0.7 1 30 . 11 ARG H H 8.53 0.01 1 31 . 11 ARG C C 175.9 0.2 1 32 . 11 ARG CA C 55.2 0.4 1 33 . 11 ARG N N 121.4 0.7 1 34 . 12 PHE H H 9.81 0.01 1 35 . 12 PHE C C 174.1 0.2 1 36 . 12 PHE CA C 56.9 0.4 1 37 . 12 PHE N N 123.9 0.7 1 38 . 13 ALA H H 8.04 0.01 1 39 . 13 ALA C C 177.1 0.2 1 40 . 13 ALA CA C 53.2 0.4 1 41 . 13 ALA N N 128.4 0.7 1 42 . 14 GLY H H 8.86 0.01 1 43 . 14 GLY C C 173.9 0.2 1 44 . 14 GLY CA C 46.5 0.4 1 45 . 14 GLY N N 102.6 0.7 1 46 . 15 VAL H H 7.92 0.01 1 47 . 15 VAL C C 175.1 0.2 1 48 . 15 VAL CA C 62.0 0.4 1 49 . 15 VAL N N 123.1 0.7 1 50 . 16 PHE H H 9.18 0.01 1 51 . 16 PHE C C 172.1 0.2 1 52 . 16 PHE CA C 54.5 0.4 1 53 . 16 PHE N N 120.9 0.7 1 54 . 17 HIS H H 8.92 0.01 1 55 . 17 HIS C C 172.9 0.2 1 56 . 17 HIS CA C 55.1 0.4 1 57 . 17 HIS N N 122.3 0.7 1 58 . 18 VAL H H 8.39 0.01 1 59 . 18 VAL C C 172.4 0.2 1 60 . 18 VAL CA C 61.0 0.4 1 61 . 18 VAL N N 126.2 0.7 1 62 . 19 GLU H H 8.11 0.01 1 63 . 19 GLU C C 174.7 0.2 1 64 . 19 GLU CA C 53.8 0.4 1 65 . 19 GLU N N 126.2 0.7 1 66 . 20 LYS H H 9.91 0.01 1 67 . 20 LYS C C 175.2 0.2 1 68 . 20 LYS CA C 54.6 0.4 1 69 . 20 LYS N N 134.7 0.7 1 70 . 21 ASN H H 9.75 0.01 1 71 . 21 ASN C C 175.3 0.2 1 72 . 21 ASN CA C 54.3 0.4 1 73 . 21 ASN N N 122.9 0.7 1 74 . 22 GLY H H 8.95 0.01 1 75 . 22 GLY C C 173.6 0.2 1 76 . 22 GLY CA C 46.5 0.4 1 77 . 22 GLY N N 105.5 0.7 1 78 . 23 ARG H H 7.96 0.01 1 79 . 23 ARG C C 175.4 0.2 1 80 . 23 ARG CA C 54.5 0.4 1 81 . 23 ARG N N 116.8 0.7 1 82 . 24 TYR H H 8.48 0.01 1 83 . 24 TYR C C 177.5 0.2 1 84 . 24 TYR CA C 58.4 0.4 1 85 . 24 TYR N N 122.4 0.7 1 86 . 25 SER H H 8.02 0.01 1 87 . 25 SER C C 172.8 0.2 1 88 . 25 SER CA C 59 0.4 1 89 . 25 SER N N 119 0.7 1 90 . 26 ILE H H 9.35 0.01 1 91 . 26 ILE C C 174.9 0.2 1 92 . 26 ILE CA C 62 0.4 1 93 . 26 ILE N N 126.2 0.7 1 94 . 27 SER H H 8.18 0.01 1 95 . 27 SER C C 174.5 0.2 1 96 . 27 SER CA C 56.9 0.4 1 97 . 27 SER N N 123.9 0.7 1 98 . 28 ARG H H 9.02 0.01 1 99 . 28 ARG C C 179.2 0.2 1 100 . 28 ARG CA C 59.7 0.4 1 101 . 28 ARG N N 121.8 0.7 1 102 . 29 THR H H 7.76 0.01 1 103 . 29 THR C C 177.5 0.2 1 104 . 29 THR CA C 63.9 0.4 1 105 . 29 THR N N 107.7 0.7 1 106 . 30 GLU H H 8.08 0.01 1 107 . 30 GLU C C 177.6 0.2 1 108 . 30 GLU CA C 59.7 0.4 1 109 . 30 GLU N N 127.3 0.7 1 110 . 31 ALA H H 8.8 0.01 1 111 . 31 ALA C C 178.2 0.2 1 112 . 31 ALA CA C 56.1 0.4 1 113 . 31 ALA N N 124.1 0.7 1 114 . 32 ALA H H 7.05 0.01 1 115 . 32 ALA C C 180.9 0.2 1 116 . 32 ALA CA C 55.3 0.4 1 117 . 32 ALA N N 116.9 0.7 1 118 . 33 ASP H H 7.32 0.01 1 119 . 33 ASP C C 178.9 0.2 1 120 . 33 ASP CA C 57.3 0.4 1 121 . 33 ASP N N 120.6 0.7 1 122 . 34 LEU H H 9.53 0.01 1 123 . 34 LEU C C 178.7 0.2 1 124 . 34 LEU CA C 57.7 0.4 1 125 . 34 LEU N N 127.3 0.7 1 126 . 35 CYS H H 8.66 0.01 1 127 . 35 CYS C C 179.1 0.2 1 128 . 35 CYS CA C 56.6 0.4 1 129 . 35 CYS N N 115.2 0.7 1 130 . 36 LYS H H 8.2 0.01 1 131 . 36 LYS C C 180.5 0.2 1 132 . 36 LYS CA C 60.4 0.4 1 133 . 36 LYS N N 123.1 0.7 1 134 . 37 ALA H H 8.17 0.01 1 135 . 37 ALA C C 177.7 0.2 1 136 . 37 ALA CA C 55.6 0.4 1 137 . 37 ALA N N 125.8 0.7 1 138 . 38 PHE H H 7.67 0.01 1 139 . 38 PHE C C 177.0 0.2 1 140 . 38 PHE CA C 59.4 0.4 1 141 . 38 PHE N N 115.4 0.7 1 142 . 39 ASN H H 9.01 0.01 1 143 . 39 ASN C C 173.8 0.2 1 144 . 39 ASN CA C 54.6 0.4 1 145 . 39 ASN N N 123.4 0.7 1 146 . 40 SER H H 8.23 0.01 1 147 . 40 SER C C 171.8 0.2 1 148 . 40 SER CA C 58.7 0.4 1 149 . 40 SER N N 112.2 0.7 1 150 . 41 THR H H 9.09 0.01 1 151 . 41 THR C C 175.3 0.2 1 152 . 41 THR CA C 59.3 0.4 1 153 . 41 THR N N 112.6 0.7 1 154 . 42 LEU H H 9.08 0.01 1 155 . 42 LEU CA C 54.1 0.4 1 156 . 42 LEU N N 125.1 0.7 1 157 . 43 PRO C C 175.6 0.2 1 158 . 44 THR H H 8.46 0.01 1 159 . 44 THR C C 176.4 0.2 1 160 . 44 THR CA C 60.1 0.4 1 161 . 44 THR N N 111.9 0.7 1 162 . 45 MET H H 8.96 0.01 1 163 . 45 MET C C 178.1 0.2 1 164 . 45 MET CA C 57.7 0.4 1 165 . 45 MET N N 121.8 0.7 1 166 . 46 ALA H H 8.40 0.01 1 167 . 46 ALA C C 181.7 0.2 1 168 . 46 ALA CA C 55.0 0.4 1 169 . 46 ALA N N 121.1 0.7 1 170 . 47 GLN H H 7.70 0.01 1 171 . 47 GLN C C 180.0 0.2 1 172 . 47 GLN CA C 58.5 0.4 1 173 . 47 GLN N N 119.7 0.7 1 174 . 48 MET H H 8.11 0.01 1 175 . 48 MET C C 178.0 0.2 1 176 . 48 MET CA C 56.3 0.4 1 177 . 48 MET N N 120.1 0.7 1 178 . 49 GLU H H 8.8 0.01 1 179 . 49 GLU C C 179.9 0.2 1 180 . 49 GLU CA C 59.8 0.4 1 181 . 49 GLU N N 120.8 0.7 1 182 . 50 LYS H H 7.94 0.01 1 183 . 50 LYS C C 179.7 0.2 1 184 . 50 LYS CA C 58.4 0.4 1 185 . 50 LYS N N 121.9 0.7 1 186 . 51 ALA H H 7.81 0.01 1 187 . 51 ALA C C 179.9 0.2 1 188 . 51 ALA CA C 55.6 0.4 1 189 . 51 ALA N N 124.1 0.7 1 190 . 52 LEU H H 8.60 0.01 1 191 . 52 LEU C C 181.0 0.2 1 192 . 52 LEU CA C 58.3 0.4 1 193 . 52 LEU N N 122.2 0.7 1 194 . 53 SER H H 7.92 0.01 1 195 . 53 SER C C 175.2 0.2 1 196 . 53 SER CA C 61.5 0.4 1 197 . 53 SER N N 115.2 0.7 1 198 . 54 ILE H H 7.43 0.01 1 199 . 54 ILE C C 176.0 0.2 1 200 . 54 ILE CA C 60.5 0.4 1 201 . 54 ILE N N 115.4 0.7 1 202 . 55 GLY H H 7.76 0.01 1 203 . 55 GLY C C 174.1 0.2 1 204 . 55 GLY CA C 45.1 0.4 1 205 . 55 GLY N N 107.3 0.7 1 206 . 56 PHE H H 7.89 0.01 1 207 . 56 PHE C C 170.8 0.2 1 208 . 56 PHE CA C 57.3 0.4 1 209 . 56 PHE N N 125 0.7 1 210 . 57 GLU H H 6.89 0.01 1 211 . 57 GLU C C 174.7 0.2 1 212 . 57 GLU CA C 54.1 0.4 1 213 . 57 GLU N N 120.1 0.7 1 214 . 58 THR H H 7.94 0.01 1 215 . 58 THR C C 172.6 0.2 1 216 . 58 THR CA C 59.0 0.4 1 217 . 58 THR N N 110.9 0.7 1 218 . 59 CYS H H 8.96 0.01 1 219 . 59 CYS C C 175.2 0.2 1 220 . 59 CYS CA C 55.8 0.4 1 221 . 59 CYS N N 120.6 0.7 1 222 . 60 ARG H H 7.90 0.01 1 223 . 60 ARG C C 179.2 0.2 1 224 . 60 ARG CA C 52.9 0.4 1 225 . 60 ARG N N 119.8 0.7 1 226 . 61 TYR H H 8.41 0.01 1 227 . 61 TYR C C 176.4 0.2 1 228 . 61 TYR CA C 57.9 0.4 1 229 . 61 TYR N N 123.7 0.7 1 230 . 62 GLY H H 9.21 0.01 1 231 . 62 GLY C C 171.9 0.2 1 232 . 62 GLY CA C 44.8 0.4 1 233 . 62 GLY N N 106.2 0.7 1 234 . 63 PHE H H 7.86 0.01 1 235 . 63 PHE C C 175.3 0.2 1 236 . 63 PHE CA C 61.5 0.4 1 237 . 63 PHE N N 121.2 0.7 1 238 . 64 ILE H H 8.78 0.01 1 239 . 64 ILE C C 175.7 0.2 1 240 . 64 ILE CA C 60.9 0.4 1 241 . 64 ILE N N 111.4 0.7 1 242 . 65 GLU H H 9.20 0.01 1 243 . 65 GLU C C 177.1 0.2 1 244 . 65 GLU CA C 58.9 0.4 1 245 . 65 GLU N N 123.4 0.7 1 246 . 66 GLY H H 8.62 0.01 1 247 . 66 GLY C C 173.4 0.2 1 248 . 66 GLY CA C 46.0 0.4 1 249 . 66 GLY N N 117.1 0.7 1 250 . 67 HIS H H 7.13 0.01 1 251 . 67 HIS C C 172.3 0.2 1 252 . 67 HIS CA C 55.2 0.4 1 253 . 67 HIS N N 115.0 0.7 1 254 . 68 VAL H H 8.89 0.01 1 255 . 68 VAL C C 175.5 0.2 1 256 . 68 VAL CA C 62.8 0.4 1 257 . 68 VAL N N 123.5 0.7 1 258 . 69 VAL H H 8.67 0.01 1 259 . 69 VAL C C 175.2 0.2 1 260 . 69 VAL CA C 57.6 0.4 1 261 . 69 VAL N N 115.8 0.7 1 262 . 70 ILE H H 8.51 0.01 1 263 . 70 ILE CA C 57.7 0.4 1 264 . 70 ILE N N 117.3 0.7 1 265 . 71 PRO C C 174.3 0.2 1 266 . 72 ARG H H 8.46 0.01 1 267 . 72 ARG C C 175.0 0.2 1 268 . 72 ARG CA C 52.2 0.4 1 269 . 72 ARG N N 121.3 0.7 1 270 . 73 ILE H H 9.55 0.01 1 271 . 73 ILE C C 175.6 0.2 1 272 . 73 ILE CA C 62.6 0.4 1 273 . 73 ILE N N 126.3 0.7 1 274 . 74 HIS H H 9.13 0.01 1 275 . 74 HIS CA C 53.5 0.4 1 276 . 74 HIS N N 120.7 0.7 1 277 . 78 ILE H H 7.88 0.01 1 278 . 78 ILE C C 175.9 0.2 1 279 . 78 ILE CA C 61.6 0.4 1 280 . 78 ILE N N 115.9 0.7 1 281 . 79 CYS H H 7.55 0.01 1 282 . 79 CYS C C 171.9 0.2 1 283 . 79 CYS CA C 52.8 0.4 1 284 . 79 CYS N N 119.5 0.7 1 285 . 80 ALA H H 9.08 0.01 1 286 . 80 ALA C C 176.4 0.2 1 287 . 80 ALA CA C 52.8 0.4 1 288 . 80 ALA N N 124.5 0.7 1 289 . 81 ALA H H 8.24 0.01 1 290 . 81 ALA C C 175.6 0.2 1 291 . 81 ALA CA C 53.2 0.4 1 292 . 81 ALA N N 119.7 0.7 1 293 . 82 ASN H H 7.42 0.01 1 294 . 82 ASN C C 174.6 0.2 1 295 . 82 ASN CA C 55.1 0.4 1 296 . 82 ASN N N 110.4 0.7 1 297 . 83 ASN H H 7.78 0.01 1 298 . 83 ASN C C 174.8 0.2 1 299 . 83 ASN CA C 54.8 0.4 1 300 . 83 ASN N N 117.9 0.7 1 301 . 84 THR H H 8.32 0.01 1 302 . 84 THR C C 174.2 0.2 1 303 . 84 THR CA C 60.4 0.4 1 304 . 84 THR N N 108.2 0.7 1 305 . 85 GLY H H 9.01 0.01 1 306 . 85 GLY C C 173.3 0.2 1 307 . 85 GLY CA C 43.8 0.4 1 308 . 85 GLY N N 109.4 0.7 1 309 . 86 VAL H H 8.73 0.01 1 310 . 86 VAL C C 173.8 0.2 1 311 . 86 VAL CA C 62.7 0.4 1 312 . 86 VAL N N 121.8 0.7 1 313 . 87 TYR H H 8.23 0.01 1 314 . 87 TYR C C 174.5 0.2 1 315 . 87 TYR CA C 58.5 0.4 1 316 . 87 TYR N N 131 0.7 1 317 . 88 ILE H H 7.42 0.01 1 318 . 88 ILE C C 174.6 0.2 1 319 . 88 ILE CA C 60.8 0.4 1 320 . 88 ILE N N 127.8 0.7 1 321 . 89 LEU H H 8.44 0.01 1 322 . 89 LEU C C 176.9 0.2 1 323 . 89 LEU CA C 53.5 0.4 1 324 . 89 LEU N N 129.9 0.7 1 325 . 90 THR H H 8.46 0.01 1 326 . 90 THR C C 174.4 0.2 1 327 . 90 THR CA C 63 0.4 1 328 . 90 THR N N 122.3 0.7 1 329 . 91 SER H H 7.87 0.01 1 330 . 91 SER CA C 57.2 0.4 1 331 . 91 SER N N 119.2 0.7 1 332 . 93 THR H H 8.19 0.01 1 333 . 93 THR C C 174.7 0.2 1 334 . 93 THR CA C 62.1 0.4 1 335 . 93 THR N N 113.7 0.7 1 336 . 94 SER H H 8.12 0.01 1 337 . 94 SER C C 173.3 0.2 1 338 . 94 SER CA C 58.2 0.4 1 339 . 94 SER N N 117.0 0.7 1 340 . 95 GLN H H 7.27 0.01 1 341 . 95 GLN C C 173.7 0.2 1 342 . 95 GLN CA C 54.8 0.4 1 343 . 95 GLN N N 119.3 0.7 1 344 . 96 TYR H H 8.65 0.01 1 345 . 96 TYR C C 174.6 0.2 1 346 . 96 TYR CA C 57.9 0.4 1 347 . 96 TYR N N 120.1 0.7 1 348 . 97 ASP H H 7.82 0.01 1 349 . 97 ASP C C 175.2 0.2 1 350 . 97 ASP CA C 54.5 0.4 1 351 . 97 ASP N N 120.6 0.7 1 352 . 98 THR H H 8.07 0.01 1 353 . 98 THR CA C 62.6 0.4 1 354 . 98 THR N N 111.5 0.7 1 355 . 99 TYR H H 8.61 0.01 1 356 . 99 TYR C C 174.7 0.2 1 357 . 99 TYR CA C 56.8 0.4 1 358 . 99 TYR N N 123.7 0.7 1 359 . 100 CYS H H 8.52 0.01 1 360 . 100 CYS C C 172.3 0.2 1 361 . 100 CYS CA C 51.6 0.4 1 362 . 100 CYS N N 114.2 0.7 1 363 . 101 PHE H H 9.95 0.01 1 364 . 101 PHE C C 172.8 0.2 1 365 . 101 PHE CA C 56.4 0.4 1 366 . 101 PHE N N 121.2 0.7 1 367 . 102 ASN H H 9.06 0.01 1 368 . 102 ASN C C 174.6 0.2 1 369 . 102 ASN CA C 51.7 0.4 1 370 . 102 ASN N N 129.0 0.7 1 371 . 103 ALA H H 8.75 0.01 1 372 . 103 ALA C C 177.6 0.2 1 373 . 103 ALA CA C 54.0 0.4 1 374 . 103 ALA N N 128.4 0.7 1 375 . 104 SER H H 8.13 0.01 1 376 . 104 SER C C 173.7 0.2 1 377 . 104 SER CA C 58.6 0.4 1 378 . 104 SER N N 112.7 0.7 1 379 . 105 ALA H H 6.90 0.01 1 380 . 105 ALA CA C 50.6 0.4 1 381 . 105 ALA N N 126.2 0.7 1 382 . 107 PRO C C 175.9 0.2 1 383 . 108 GLU H H 7.86 0.01 1 384 . 108 GLU C C 174.7 0.2 1 385 . 108 GLU CA C 55.3 0.4 1 386 . 108 GLU N N 116.7 0.7 1 387 . 109 GLU H H 8.31 0.01 1 388 . 109 GLU C C 173.2 0.2 1 389 . 109 GLU CA C 56.3 0.4 1 390 . 109 GLU N N 124.0 0.7 1 391 . 110 ASP H H 9.45 0.01 1 392 . 110 ASP C C 176.5 0.2 1 393 . 110 ASP CA C 53.2 0.4 1 394 . 110 ASP N N 127.9 0.7 1 395 . 111 CYS H H 9.34 0.01 1 396 . 111 CYS C C 175.3 0.2 1 397 . 111 CYS CA C 52.6 0.4 1 398 . 111 CYS N N 125.2 0.7 1 399 . 112 THR H H 8.18 0.01 1 400 . 112 THR C C 175.2 0.2 1 401 . 112 THR CA C 64.7 0.4 1 402 . 112 THR N N 119.7 0.7 1 403 . 113 SER H H 8.72 0.01 1 404 . 113 SER C C 173.7 0.2 1 405 . 113 SER CA C 60.1 0.4 1 406 . 113 SER N N 122.8 0.7 1 407 . 114 VAL H H 8.87 0.01 1 408 . 114 VAL C C 176.1 0.2 1 409 . 114 VAL CA C 62.7 0.4 1 410 . 114 VAL N N 129.0 0.7 1 411 . 115 THR H H 8.06 0.01 1 412 . 115 THR C C 172.7 0.2 1 413 . 115 THR CA C 60.8 0.4 1 414 . 115 THR N N 114.3 0.7 1 415 . 116 ASP H H 7.38 0.01 1 416 . 116 ASP C C 172.8 0.2 1 417 . 116 ASP CA C 53.0 0.4 1 418 . 116 ASP N N 117.5 0.7 1 419 . 117 LEU H H 8.85 0.01 1 420 . 117 LEU CA C 51.4 0.4 1 421 . 117 LEU N N 120.1 0.7 1 422 . 119 ASN H H 8.19 0.01 1 423 . 119 ASN C C 176.2 0.2 1 424 . 119 ASN CA C 51.2 0.4 1 425 . 119 ASN N N 113.7 0.7 1 426 . 120 ALA H H 7.17 0.01 1 427 . 120 ALA C C 175.4 0.2 1 428 . 120 ALA CA C 52.7 0.4 1 429 . 120 ALA N N 122.5 0.7 1 430 . 121 PHE H H 8.16 0.01 1 431 . 121 PHE C C 175.1 0.2 1 432 . 121 PHE CA C 54.1 0.4 1 433 . 121 PHE N N 119.7 0.7 1 434 . 122 ASP H H 8.50 0.01 1 435 . 122 ASP C C 176.1 0.2 1 436 . 122 ASP CA C 55.5 0.4 1 437 . 122 ASP N N 119.2 0.7 1 438 . 123 GLY H H 7.97 0.01 1 439 . 123 GLY CA C 45.4 0.4 1 440 . 123 GLY N N 109.2 0.7 1 441 . 124 PRO C C 177.0 0.2 1 442 . 125 ILE H H 8.21 0.01 1 443 . 125 ILE C C 177.0 0.2 1 444 . 125 ILE CA C 59.9 0.4 1 445 . 125 ILE N N 125.6 0.7 1 446 . 126 THR H H 8.34 0.01 1 447 . 126 THR C C 172.8 0.2 1 448 . 126 THR CA C 63.9 0.4 1 449 . 126 THR N N 122.8 0.7 1 450 . 127 ILE H H 9.44 0.01 1 451 . 127 ILE C C 174.7 0.2 1 452 . 127 ILE CA C 60.3 0.4 1 453 . 127 ILE N N 134.6 0.7 1 454 . 128 THR H H 9.16 0.01 1 455 . 128 THR C C 175.8 0.2 1 456 . 128 THR CA C 61.1 0.4 1 457 . 128 THR N N 123.9 0.7 1 458 . 129 ILE H H 9.44 0.01 1 459 . 129 ILE C C 174.8 0.2 1 460 . 129 ILE CA C 60.9 0.4 1 461 . 129 ILE N N 127.7 0.7 1 462 . 130 VAL H H 9.22 0.01 1 463 . 130 VAL C C 176.0 0.2 1 464 . 130 VAL CA C 61.9 0.4 1 465 . 130 VAL N N 128.1 0.7 1 466 . 131 ASN H H 8.58 0.01 1 467 . 131 ASN C C 177.3 0.2 1 468 . 131 ASN CA C 53.7 0.4 1 469 . 131 ASN N N 124.6 0.7 1 470 . 132 ARG H H 9.32 0.01 1 471 . 132 ARG C C 177.1 0.2 1 472 . 132 ARG CA C 58.4 0.4 1 473 . 132 ARG N N 124.0 0.7 1 474 . 133 ASP H H 7.99 0.01 1 475 . 133 ASP C C 176.9 0.2 1 476 . 133 ASP CA C 53.6 0.4 1 477 . 133 ASP N N 117.0 0.7 1 478 . 134 GLY H H 8.27 0.01 1 479 . 134 GLY C C 175.0 0.2 1 480 . 134 GLY CA C 44.8 0.4 1 481 . 134 GLY N N 109.3 0.7 1 482 . 135 THR H H 8.35 0.01 1 483 . 135 THR C C 174.1 0.2 1 484 . 135 THR CA C 63.4 0.4 1 485 . 135 THR N N 116.6 0.7 1 486 . 136 ARG H H 8.18 0.01 1 487 . 136 ARG C C 175.1 0.2 1 488 . 136 ARG CA C 54.3 0.4 1 489 . 136 ARG N N 124.7 0.7 1 490 . 137 TYR H H 8.84 0.01 1 491 . 137 TYR C C 173.8 0.2 1 492 . 137 TYR CA C 57.5 0.4 1 493 . 137 TYR N N 123.5 0.7 1 494 . 138 VAL H H 8.57 0.01 1 495 . 138 VAL C C 175.2 0.2 1 496 . 138 VAL CA C 61.1 0.4 1 497 . 138 VAL N N 123.4 0.7 1 498 . 139 GLN H H 9.48 0.01 1 499 . 139 GLN C C 173.0 0.2 1 500 . 139 GLN CA C 54.3 0.4 1 501 . 139 GLN N N 128.3 0.7 1 502 . 140 LYS H H 8.64 0.01 1 503 . 140 LYS C C 177.5 0.2 1 504 . 140 LYS CA C 53.9 0.4 1 505 . 140 LYS N N 124.7 0.7 1 506 . 141 GLY H H 9.15 0.01 1 507 . 141 GLY C C 169.5 0.2 1 508 . 141 GLY CA C 46.8 0.4 1 509 . 141 GLY N N 115.4 0.7 1 510 . 142 GLU H H 8.00 0.01 1 511 . 142 GLU C C 170.5 0.2 1 512 . 142 GLU CA C 54.8 0.4 1 513 . 142 GLU N N 119.2 0.7 1 514 . 143 TYR H H 8.79 0.01 1 515 . 143 TYR C C 174.0 0.2 1 516 . 143 TYR CA C 57.2 0.4 1 517 . 143 TYR N N 117.2 0.7 1 518 . 144 ARG H H 8.96 0.01 1 519 . 144 ARG C C 175.8 0.2 1 520 . 144 ARG CA C 57.0 0.4 1 521 . 144 ARG N N 128.5 0.7 1 522 . 145 THR H H 8.83 0.01 1 523 . 145 THR C C 174.9 0.2 1 524 . 145 THR CA C 61.8 0.4 1 525 . 145 THR N N 112.1 0.7 1 526 . 146 ASN H H 8.81 0.01 1 527 . 146 ASN CA C 49.9 0.4 1 528 . 146 ASN N N 125.6 0.7 1 529 . 147 PRO C C 178.0 0.2 1 530 . 148 GLU H H 7.95 0.01 1 531 . 148 GLU C C 177.7 0.2 1 532 . 148 GLU CA C 58.1 0.4 1 533 . 148 GLU N N 115.8 0.7 1 534 . 149 ASP H H 7.83 0.01 1 535 . 149 ASP C C 176.1 0.2 1 536 . 149 ASP CA C 55.5 0.4 1 537 . 149 ASP N N 115.6 0.7 1 538 . 150 ILE H H 7.13 0.01 1 539 . 150 ILE C C 175.7 0.2 1 540 . 150 ILE CA C 63.7 0.4 1 541 . 150 ILE N N 120.9 0.7 1 542 . 151 TYR H H 7.95 0.01 1 543 . 151 TYR CA C 54.8 0.4 1 544 . 151 TYR N N 120.7 0.7 1 545 . 152 PRO C C 177.6 0.2 1 546 . 153 SER H H 8.75 0.01 1 547 . 153 SER C C 174.1 0.2 1 548 . 153 SER CA C 58.7 0.4 1 549 . 153 SER N N 118.0 0.7 1 550 . 154 ASN H H 8.54 0.01 1 551 . 154 ASN CA C 51.3 0.4 1 552 . 154 ASN N N 121.8 0.7 1 553 . 155 PRO C C 177.2 0.2 1 554 . 156 THR H H 8.34 0.01 1 555 . 156 THR C C 174.6 0.2 1 556 . 156 THR CA C 61.6 0.4 1 557 . 156 THR N N 114.1 0.7 1 558 . 157 ASP H H 8.33 0.01 1 559 . 157 ASP C C 175.9 0.2 1 560 . 157 ASP CA C 54.6 0.4 1 561 . 157 ASP N N 122.9 0.7 1 562 . 158 ASP H H 8.35 0.01 1 563 . 158 ASP C C 175.9 0.2 1 564 . 158 ASP CA C 54.4 0.4 1 565 . 158 ASP N N 121.9 0.7 1 566 . 159 ASP H H 8.28 0.01 1 567 . 159 ASP C C 175.3 0.2 1 568 . 159 ASP CA C 54.5 0.4 1 569 . 159 ASP N N 120.8 0.7 1 570 . 160 VAL H H 7.63 0.01 1 571 . 160 VAL CA C 63.6 0.4 1 572 . 160 VAL N N 124.2 0.7 1 stop_ save_