data_4287 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments of the Unstructured Yeast Target Membrane SNARE Sso1. ; _BMRB_accession_number 4287 _BMRB_flat_file_name bmr4287.str _Entry_type original _Submission_date 1998-12-18 _Accession_date 1998-12-18 _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 Fiebig Klaus M. . 2 Brunger Axel T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 366 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-05 original author . stop_ _Original_release_date 1999-10-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Fiebig, K. M., Rice, L. M., Pollock, E., and Brunger, A. T., "Folding Intermediates of SNARE Complex Assembly," Nat. Struct. Biol. 6, 117-123 (1999). ; _Citation_title 'Folding Intermediates of SNARE Complex Assembly' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99140290 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fiebig Klaus M. . 2 Rice Luke M. . 3 Pollock Elizabeth . . 4 Brunger Axel T. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 117 _Page_last 123 _Year 1999 _Details . loop_ _Keyword 'alpha-helix bundle' 'cellular trafficking' 'coiled coil' 'H1-H2 domain' 'membrane fusion' Sec9 Snc1 Sso1 'yeast SNARE' stop_ save_ ################################## # Molecular system description # ################################## save_Sso1p _Saveframe_category molecular_system _Mol_system_name Sso1 _Abbreviation_common Sso1p _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Sso1 $Sso1 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Membrane fusion protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sso1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Sso1 _Abbreviation_common Sso1 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 268 _Mol_residue_sequence ; GSHMSYNNPYQLETPFEESY ELDEGSSAIGAEGHDFVGFM NKISQINRDLDKYDHTINQV DSLHKRLLTEVNEEQASHLR HSLDNFVAQATDLQFKLKNE IKSAQRDGIHDTNKQAQAEN SRQRFLKLIQDYRIVDSNYK EENKEQAKRQYMIIQPEATE DEVEAAISDVGGQQIFSQAL LNANRRGEAKTALAEVQARH QELLKLEKSMAELTQLFNDM EELVIEQQENVDVIDKNVED AQLDVEQGVGHTDKAVKSAR KARKNKIR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 SER 6 3 TYR 7 4 ASN 8 5 ASN 9 6 PRO 10 7 TYR 11 8 GLN 12 9 LEU 13 10 GLU 14 11 THR 15 12 PRO 16 13 PHE 17 14 GLU 18 15 GLU 19 16 SER 20 17 TYR 21 18 GLU 22 19 LEU 23 20 ASP 24 21 GLU 25 22 GLY 26 23 SER 27 24 SER 28 25 ALA 29 26 ILE 30 27 GLY 31 28 ALA 32 29 GLU 33 30 GLY 34 31 HIS 35 32 ASP 36 33 PHE 37 34 VAL 38 35 GLY 39 36 PHE 40 37 MET 41 38 ASN 42 39 LYS 43 40 ILE 44 41 SER 45 42 GLN 46 43 ILE 47 44 ASN 48 45 ARG 49 46 ASP 50 47 LEU 51 48 ASP 52 49 LYS 53 50 TYR 54 51 ASP 55 52 HIS 56 53 THR 57 54 ILE 58 55 ASN 59 56 GLN 60 57 VAL 61 58 ASP 62 59 SER 63 60 LEU 64 61 HIS 65 62 LYS 66 63 ARG 67 64 LEU 68 65 LEU 69 66 THR 70 67 GLU 71 68 VAL 72 69 ASN 73 70 GLU 74 71 GLU 75 72 GLN 76 73 ALA 77 74 SER 78 75 HIS 79 76 LEU 80 77 ARG 81 78 HIS 82 79 SER 83 80 LEU 84 81 ASP 85 82 ASN 86 83 PHE 87 84 VAL 88 85 ALA 89 86 GLN 90 87 ALA 91 88 THR 92 89 ASP 93 90 LEU 94 91 GLN 95 92 PHE 96 93 LYS 97 94 LEU 98 95 LYS 99 96 ASN 100 97 GLU 101 98 ILE 102 99 LYS 103 100 SER 104 101 ALA 105 102 GLN 106 103 ARG 107 104 ASP 108 105 GLY 109 106 ILE 110 107 HIS 111 108 ASP 112 109 THR 113 110 ASN 114 111 LYS 115 112 GLN 116 113 ALA 117 114 GLN 118 115 ALA 119 116 GLU 120 117 ASN 121 118 SER 122 119 ARG 123 120 GLN 124 121 ARG 125 122 PHE 126 123 LEU 127 124 LYS 128 125 LEU 129 126 ILE 130 127 GLN 131 128 ASP 132 129 TYR 133 130 ARG 134 131 ILE 135 132 VAL 136 133 ASP 137 134 SER 138 135 ASN 139 136 TYR 140 137 LYS 141 138 GLU 142 139 GLU 143 140 ASN 144 141 LYS 145 142 GLU 146 143 GLN 147 144 ALA 148 145 LYS 149 146 ARG 150 147 GLN 151 148 TYR 152 149 MET 153 150 ILE 154 151 ILE 155 152 GLN 156 153 PRO 157 154 GLU 158 155 ALA 159 156 THR 160 157 GLU 161 158 ASP 162 159 GLU 163 160 VAL 164 161 GLU 165 162 ALA 166 163 ALA 167 164 ILE 168 165 SER 169 166 ASP 170 167 VAL 171 168 GLY 172 169 GLY 173 170 GLN 174 171 GLN 175 172 ILE 176 173 PHE 177 174 SER 178 175 GLN 179 176 ALA 180 177 LEU 181 178 LEU 182 179 ASN 183 180 ALA 184 181 ASN 185 182 ARG 186 183 ARG 187 184 GLY 188 185 GLU 189 186 ALA 190 187 LYS 191 188 THR 192 189 ALA 193 190 LEU 194 191 ALA 195 192 GLU 196 193 VAL 197 194 GLN 198 195 ALA 199 196 ARG 200 197 HIS 201 198 GLN 202 199 GLU 203 200 LEU 204 201 LEU 205 202 LYS 206 203 LEU 207 204 GLU 208 205 LYS 209 206 SER 210 207 MET 211 208 ALA 212 209 GLU 213 210 LEU 214 211 THR 215 212 GLN 216 213 LEU 217 214 PHE 218 215 ASN 219 216 ASP 220 217 MET 221 218 GLU 222 219 GLU 223 220 LEU 224 221 VAL 225 222 ILE 226 223 GLU 227 224 GLN 228 225 GLN 229 226 GLU 230 227 ASN 231 228 VAL 232 229 ASP 233 230 VAL 234 231 ILE 235 232 ASP 236 233 LYS 237 234 ASN 238 235 VAL 239 236 GLU 240 237 ASP 241 238 ALA 242 239 GLN 243 240 LEU 244 241 ASP 245 242 VAL 246 243 GLU 247 244 GLN 248 245 GLY 249 246 VAL 250 247 GLY 251 248 HIS 252 249 THR 253 250 ASP 254 251 LYS 255 252 ALA 256 253 VAL 257 254 LYS 258 255 SER 259 256 ALA 260 257 ARG 261 258 LYS 262 259 ALA 263 260 ARG 264 261 LYS 265 262 ASN 266 263 LYS 267 264 ILE 268 265 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1FIO "Crystal Structure Of Yeast T-Snare Protein Sso1" 72.76 196 100.00 100.00 4.94e-136 DBJ GAA26746 "K7_Sso1p [Saccharomyces cerevisiae Kyokai no. 7]" 98.88 290 100.00 100.00 0.00e+00 EMBL CAA47959 "Sso1 protein [Saccharomyces cerevisiae]" 98.88 290 100.00 100.00 0.00e+00 EMBL CAA54217 "orf2 [Saccharomyces cerevisiae]" 98.88 290 100.00 100.00 0.00e+00 EMBL CAA64255 "syntaxin-related protein [Saccharomyces cerevisiae]" 98.88 290 100.00 100.00 0.00e+00 EMBL CAA97949 "SSO1 [Saccharomyces cerevisiae]" 98.88 290 100.00 100.00 0.00e+00 EMBL CAY86728 "Sso1p [Saccharomyces cerevisiae EC1118]" 98.88 290 99.62 100.00 0.00e+00 GB AHY77951 "Sso1p [Saccharomyces cerevisiae YJM993]" 98.88 290 99.62 100.00 0.00e+00 GB AJP41919 "Sso1p [Saccharomyces cerevisiae YJM1078]" 98.88 290 99.62 100.00 0.00e+00 GB AJU23363 "Sso1p [Saccharomyces cerevisiae YJM1526]" 98.88 290 99.62 100.00 0.00e+00 GB AJU24051 "Sso1p [Saccharomyces cerevisiae YJM1549]" 98.88 290 99.62 100.00 0.00e+00 GB AJU24725 "Sso1p [Saccharomyces cerevisiae YJM1574]" 98.88 290 99.62 100.00 0.00e+00 REF NP_015092 "Sso1p [Saccharomyces cerevisiae S288c]" 98.88 290 100.00 100.00 0.00e+00 SP P32867 "RecName: Full=Protein SSO1" 98.88 290 100.00 100.00 0.00e+00 TPG DAA11204 "TPA: Sso1p [Saccharomyces cerevisiae S288c]" 98.88 290 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sso1 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Sso1 'recombinant technology' 'E. coli' Escherichia coli DH5-alpha plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sso1 1.2 mM 0.5 1.5 '[U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 95 loop_ _Task transformation stop_ _Details . save_ save_software_two _Saveframe_category software _Name XEasy _Version 1.3.11 loop_ _Task Assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model . _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 $sample_one save_ save_1H-15N-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-NOESY-HSQC _Sample_label $sample_one save_ save_1H-15N-TOCSY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-TOCSY-HSQC _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-TOCSY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 220 . n/a pH 4.5 0.2 n/a temperature 288 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Sso1 _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 SER N N 115.987 0.05 1 2 . 2 SER H H 8.765 0.02 1 3 . 2 SER HA H 4.878 0.02 1 4 . 2 SER HB2 H 4.007 0.02 1 5 . 2 SER HB3 H 4.007 0.02 1 6 . 3 HIS N N 120.844 0.05 1 7 . 3 HIS H H 8.807 0.02 1 8 . 3 HIS HA H 4.619 0.02 1 9 . 3 HIS HB2 H 3.325 0.02 2 10 . 3 HIS HB3 H 3.405 0.02 2 11 . 4 MET N N 122.232 0.05 1 12 . 4 MET H H 8.548 0.02 1 13 . 4 MET HA H 4.605 0.02 1 14 . 4 MET HB2 H 2.066 0.02 1 15 . 4 MET HB3 H 2.066 0.02 1 16 . 4 MET HG2 H 2.597 0.02 1 17 . 4 MET HG3 H 2.597 0.02 1 18 . 5 SER N N 117.597 0.05 1 19 . 5 SER H H 8.444 0.02 1 20 . 5 SER HA H 4.593 0.02 1 21 . 5 SER HB2 H 3.949 0.02 1 22 . 5 SER HB3 H 3.949 0.02 1 23 . 6 TYR N N 122.309 0.05 1 24 . 6 TYR H H 8.327 0.02 1 25 . 6 TYR HA H 4.719 0.02 1 26 . 6 TYR HB2 H 3.052 0.02 2 27 . 6 TYR HB3 H 3.190 0.02 2 28 . 6 TYR HD1 H 7.220 0.02 1 29 . 6 TYR HD2 H 7.220 0.02 1 30 . 7 ASN N N 120.416 0.05 1 31 . 7 ASN H H 8.416 0.02 1 32 . 7 ASN HA H 4.707 0.02 1 33 . 7 ASN HB2 H 2.824 0.02 1 34 . 7 ASN HB3 H 2.824 0.02 1 35 . 8 ASN N N 121.081 0.05 1 36 . 8 ASN H H 8.273 0.02 1 37 . 8 ASN HA H 4.694 0.02 1 38 . 8 ASN HB2 H 2.812 0.02 1 39 . 8 ASN HB3 H 2.812 0.02 1 40 . 10 TYR N N 118.872 0.05 1 41 . 10 TYR H H 8.102 0.02 1 42 . 10 TYR HA H 4.669 0.02 1 43 . 10 TYR HB2 H 3.052 0.02 2 44 . 10 TYR HB3 H 3.254 0.02 2 45 . 10 TYR HD1 H 7.246 0.02 1 46 . 10 TYR HD2 H 7.246 0.02 1 47 . 11 GLN N N 121.057 0.05 1 48 . 11 GLN H H 7.989 0.02 1 49 . 11 GLN HA H 4.403 0.02 1 50 . 11 GLN HB2 H 2.066 0.02 2 51 . 11 GLN HB3 H 2.168 0.02 2 52 . 11 GLN HG2 H 2.407 0.02 1 53 . 11 GLN HG3 H 2.407 0.02 1 54 . 12 LEU N N 123.336 0.05 1 55 . 12 LEU H H 8.257 0.02 1 56 . 12 LEU HA H 4.416 0.02 1 57 . 12 LEU HB2 H 1.738 0.02 1 58 . 12 LEU HB3 H 1.738 0.02 1 59 . 12 LEU HD1 H 1.005 0.02 1 60 . 12 LEU HD2 H 1.005 0.02 1 61 . 13 GLU N N 121.470 0.05 1 62 . 13 GLU H H 8.475 0.02 1 63 . 13 GLU HA H 4.492 0.02 1 64 . 13 GLU HB2 H 2.079 0.02 2 65 . 13 GLU HB3 H 2.193 0.02 2 66 . 13 GLU HG2 H 2.471 0.02 1 67 . 13 GLU HG3 H 2.471 0.02 1 68 . 14 THR N N 117.201 0.05 1 69 . 14 THR H H 8.262 0.02 1 70 . 14 THR HA H 4.707 0.02 1 71 . 14 THR HB H 4.290 0.02 1 72 . 14 THR HG2 H 1.346 0.02 2 73 . 16 PHE N N 120.368 0.05 1 74 . 16 PHE H H 8.286 0.02 1 75 . 16 PHE HA H 4.681 0.02 1 76 . 16 PHE HB2 H 3.203 0.02 1 77 . 16 PHE HB3 H 3.203 0.02 1 78 . 16 PHE HD1 H 7.347 0.02 1 79 . 16 PHE HD2 H 7.347 0.02 1 80 . 17 GLU N N 122.266 0.05 1 81 . 17 GLU H H 8.271 0.02 1 82 . 17 GLU HA H 4.365 0.02 1 83 . 17 GLU HB2 H 2.028 0.02 2 84 . 17 GLU HB3 H 2.142 0.02 2 85 . 17 GLU HG2 H 2.420 0.02 1 86 . 17 GLU HG3 H 2.420 0.02 1 87 . 18 GLU N N 121.639 0.05 1 88 . 18 GLU H H 8.374 0.02 1 89 . 18 GLU HA H 4.378 0.02 1 90 . 18 GLU HB2 H 2.053 0.02 2 91 . 18 GLU HB3 H 2.117 0.02 2 92 . 18 GLU HG2 H 2.433 0.02 1 93 . 18 GLU HG3 H 2.433 0.02 1 94 . 19 SER N N 116.501 0.05 1 95 . 19 SER H H 8.347 0.02 1 96 . 19 SER HA H 4.504 0.02 1 97 . 19 SER HB2 H 3.936 0.02 1 98 . 19 SER HB3 H 3.936 0.02 1 99 . 20 TYR N N 122.107 0.05 1 100 . 20 TYR H H 8.178 0.02 1 101 . 20 TYR HA H 4.694 0.02 1 102 . 20 TYR HB2 H 3.065 0.02 2 103 . 20 TYR HB3 H 3.191 0.02 2 104 . 20 TYR HD1 H 7.195 0.02 1 105 . 20 TYR HD2 H 7.195 0.02 1 106 . 21 GLU N N 121.617 0.05 1 107 . 21 GLU H H 8.285 0.02 1 108 . 21 GLU HA H 4.403 0.02 1 109 . 21 GLU HB2 H 2.041 0.02 2 110 . 21 GLU HB3 H 2.143 0.02 2 111 . 21 GLU HG2 H 2.420 0.02 1 112 . 21 GLU HG3 H 2.420 0.02 1 113 . 22 LEU N N 122.884 0.05 1 114 . 22 LEU H H 8.205 0.02 1 115 . 22 LEU HA H 4.429 0.02 1 116 . 22 LEU HB2 H 1.725 0.02 1 117 . 22 LEU HB3 H 1.725 0.02 1 118 . 22 LEU HD1 H 1.018 0.02 1 119 . 22 LEU HD2 H 1.018 0.02 1 120 . 23 ASP N N 121.060 0.05 1 121 . 23 ASP H H 8.412 0.02 1 122 . 23 ASP HA H 4.757 0.02 1 123 . 23 ASP HB2 H 2.799 0.02 2 124 . 23 ASP HB3 H 2.913 0.02 2 125 . 24 GLU N N 121.652 0.05 1 126 . 24 GLU H H 8.504 0.02 1 127 . 24 GLU HA H 4.429 0.02 1 128 . 24 GLU HB2 H 2.105 0.02 2 129 . 24 GLU HB3 H 2.243 0.02 2 130 . 24 GLU HG2 H 2.483 0.02 1 131 . 24 GLU HG3 H 2.483 0.02 1 132 . 25 GLY N N 109.590 0.05 1 133 . 25 GLY H H 8.564 0.02 1 134 . 25 GLY HA2 H 4.113 0.02 1 135 . 25 GLY HA3 H 4.113 0.02 1 136 . 26 SER N N 115.809 0.05 1 137 . 26 SER H H 8.268 0.02 1 138 . 26 SER HA H 4.618 0.02 1 139 . 26 SER HB2 H 4.037 0.02 1 140 . 26 SER HB3 H 4.037 0.02 1 141 . 27 SER N N 117.910 0.05 1 142 . 27 SER H H 8.447 0.02 1 143 . 27 SER HA H 4.605 0.02 1 144 . 27 SER HB2 H 4.050 0.02 1 145 . 27 SER HB3 H 4.050 0.02 1 146 . 28 ALA N N 126.003 0.05 1 147 . 28 ALA H H 8.337 0.02 1 148 . 28 ALA HA H 4.479 0.02 1 149 . 28 ALA HB H 1.511 0.02 1 150 . 29 ILE N N 119.668 0.05 1 151 . 29 ILE H H 8.101 0.02 1 152 . 29 ILE HA H 4.239 0.02 1 153 . 29 ILE HB H 1.991 0.02 1 154 . 29 ILE HG2 H 1.334 0.02 1 155 . 29 ILE HG12 H 1.612 0.02 1 156 . 29 ILE HG13 H 1.612 0.02 1 157 . 29 ILE HD1 H 1.031 0.02 1 158 . 30 GLY N N 112.870 0.05 1 159 . 30 GLY H H 8.513 0.02 1 160 . 30 GLY HA2 H 4.075 0.02 1 161 . 30 GLY HA3 H 4.075 0.02 1 162 . 31 ALA N N 123.981 0.05 1 163 . 31 ALA H H 8.225 0.02 1 164 . 31 ALA HA H 4.429 0.02 1 165 . 31 ALA HB H 1.511 0.02 1 166 . 32 GLU N N 119.577 0.05 1 167 . 32 GLU H H 8.546 0.02 1 168 . 32 GLU HA H 4.416 0.02 1 169 . 32 GLU HB2 H 2.079 0.02 2 170 . 32 GLU HB3 H 2.193 0.02 2 171 . 32 GLU HG2 H 2.445 0.02 1 172 . 32 GLU HG3 H 2.445 0.02 1 173 . 33 GLY N N 109.448 0.05 1 174 . 33 GLY H H 8.494 0.02 1 175 . 33 GLY HA2 H 4.088 0.02 1 176 . 33 GLY HA3 H 4.088 0.02 1 177 . 34 HIS N N 118.362 0.05 1 178 . 34 HIS H H 8.553 0.02 1 179 . 34 HIS HA H 4.820 0.02 1 180 . 34 HIS HB2 H 3.380 0.02 1 181 . 34 HIS HB3 H 3.380 0.02 1 182 . 35 ASP N N 120.736 0.05 1 183 . 35 ASP H H 8.632 0.02 1 184 . 35 ASP HA H 4.858 0.02 1 185 . 35 ASP HB2 H 2.862 0.02 1 186 . 35 ASP HB3 H 2.862 0.02 1 187 . 36 PHE N N 121.060 0.05 1 188 . 36 PHE H H 8.316 0.02 1 189 . 36 PHE HA H 4.719 0.02 1 190 . 36 PHE HB2 H 3.191 0.02 1 191 . 36 PHE HB3 H 3.191 0.02 1 192 . 36 PHE HD1 H 7.334 0.02 1 193 . 36 PHE HD2 H 7.334 0.02 1 194 . 37 VAL N N 122.804 0.05 1 195 . 37 VAL H H 8.385 0.02 1 196 . 37 VAL HA H 4.317 0.00 1 197 . 37 VAL HB H 1.864 0.02 1 198 . 38 GLY N N 110.500 0.05 1 199 . 38 GLY H H 8.522 0.02 1 200 . 38 GLY HA2 H 4.024 0.02 1 201 . 38 GLY HA3 H 4.024 0.02 1 202 . 39 PHE N N 124.583 0.05 1 203 . 39 PHE H H 7.709 0.02 1 204 . 39 PHE HA H 4.530 0.02 1 205 . 39 PHE HB2 H 3.039 0.02 2 206 . 39 PHE HB3 H 3.203 0.02 2 207 . 229 GLU N N 122.047 0.05 1 208 . 229 GLU H H 8.601 0.02 1 209 . 229 GLU HA H 4.467 0.02 1 210 . 229 GLU HB2 H 2.116 0.02 2 211 . 229 GLU HB3 H 2.218 0.02 2 212 . 229 GLU HG2 H 2.483 0.02 1 213 . 229 GLU HG3 H 2.483 0.02 1 214 . 230 ASN N N 120.248 0.05 1 215 . 230 ASN H H 8.635 0.02 1 216 . 230 ASN HA H 4.871 0.02 1 217 . 230 ASN HB2 H 2.900 0.02 2 218 . 230 ASN HB3 H 2.964 0.02 2 219 . 231 VAL N N 119.890 0.05 1 220 . 231 VAL H H 8.175 0.02 1 221 . 231 VAL HA H 4.277 0.02 1 222 . 231 VAL HB H 2.243 0.02 1 223 . 231 VAL HG1 H 1.056 0.02 1 224 . 231 VAL HG2 H 1.056 0.02 1 225 . 232 ASP N N 123.545 0.05 1 226 . 232 ASP H H 8.514 0.02 1 227 . 232 ASP HA H 4.820 0.02 1 228 . 232 ASP HB2 H 2.773 0.02 2 229 . 232 ASP HB3 H 2.875 0.02 2 230 . 233 VAL N N 120.393 0.05 1 231 . 233 VAL H H 8.133 0.02 1 232 . 233 VAL HA H 4.252 0.02 1 233 . 233 VAL HB H 2.231 0.02 1 234 . 233 VAL HG1 H 1.056 0.02 1 235 . 233 VAL HG2 H 1.056 0.02 1 236 . 234 ILE N N 124.329 0.05 1 237 . 234 ILE H H 8.228 0.02 1 238 . 234 ILE HA H 4.252 0.02 1 239 . 234 ILE HB H 1.991 0.02 1 240 . 234 ILE HG2 H 1.321 0.02 1 241 . 234 ILE HG12 H 1.599 0.02 1 242 . 234 ILE HG13 H 1.599 0.02 1 243 . 234 ILE HD1 H 1.031 0.02 1 244 . 235 ASP N N 124.290 0.05 1 245 . 235 ASP H H 8.467 0.02 1 246 . 235 ASP HA H 4.770 0.02 1 247 . 235 ASP HB2 H 2.774 0.02 2 248 . 235 ASP HB3 H 2.926 0.02 2 249 . 236 LYS N N 122.605 0.05 1 250 . 236 LYS H H 8.372 0.02 1 251 . 236 LYS HA H 4.403 0.02 1 252 . 236 LYS HB2 H 1.876 0.02 2 253 . 236 LYS HB3 H 1.978 0.02 2 254 . 236 LYS HG2 H 1.561 0.02 1 255 . 236 LYS HG3 H 1.561 0.02 1 256 . 237 ASN N N 119.766 0.05 1 257 . 237 ASN H H 8.608 0.02 1 258 . 237 ASN HA H 4.846 0.02 1 259 . 237 ASN HB2 H 2.951 0.02 1 260 . 237 ASN HB3 H 2.951 0.02 1 261 . 238 VAL N N 120.307 0.05 1 262 . 238 VAL H H 8.103 0.02 1 263 . 238 VAL HA H 4.239 0.02 1 264 . 238 VAL HB H 2.256 0.02 1 265 . 238 VAL HG1 H 1.081 0.02 1 266 . 238 VAL HG2 H 1.081 0.02 1 267 . 239 GLU N N 123.499 0.05 1 268 . 239 GLU H H 8.490 0.02 1 269 . 239 GLU HA H 4.429 0.02 1 270 . 239 GLU HB2 H 2.104 0.02 2 271 . 239 GLU HB3 H 2.230 0.02 2 272 . 239 GLU HG2 H 2.483 0.02 1 273 . 239 GLU HG3 H 2.483 0.02 1 274 . 240 ASP N N 121.226 0.05 1 275 . 240 ASP H H 8.421 0.02 1 276 . 240 ASP HA H 4.719 0.02 1 277 . 240 ASP HB2 H 2.811 0.02 2 278 . 240 ASP HB3 H 2.913 0.02 2 279 . 241 ALA N N 124.415 0.05 1 280 . 241 ALA H H 8.274 0.02 1 281 . 241 ALA HA H 4.403 0.02 1 282 . 241 ALA HB H 1.536 0.02 1 283 . 242 GLN N N 118.769 0.05 1 284 . 242 GLN H H 8.379 0.02 1 285 . 242 GLN HA H 4.403 0.02 1 286 . 242 GLN HB2 H 2.155 0.02 2 287 . 242 GLN HB3 H 2.243 0.02 2 288 . 242 GLN HG2 H 2.509 0.02 1 289 . 242 GLN HG3 H 2.509 0.02 1 290 . 243 LEU N N 122.618 0.05 1 291 . 243 LEU H H 8.187 0.02 1 292 . 243 LEU HA H 4.416 0.02 1 293 . 243 LEU HB2 H 1.751 0.02 1 294 . 243 LEU HB3 H 1.751 0.02 1 295 . 243 LEU HD1 H 1.018 0.02 1 296 . 243 LEU HD2 H 1.018 0.02 1 297 . 244 ASP N N 120.933 0.05 1 298 . 244 ASP H H 8.411 0.02 1 299 . 244 ASP HA H 4.782 0.02 1 300 . 244 ASP HB2 H 2.812 0.02 2 301 . 244 ASP HB3 H 2.926 0.02 2 302 . 245 VAL N N 119.837 0.05 1 303 . 245 VAL H H 8.075 0.02 1 304 . 245 VAL HA H 4.239 0.02 1 305 . 245 VAL HB H 2.243 0.02 1 306 . 245 VAL HG1 H 1.068 0.02 1 307 . 245 VAL HG2 H 1.068 0.02 1 308 . 246 GLU N N 120.935 0.05 1 309 . 246 GLU H H 8.440 0.02 1 310 . 246 GLU HA H 4.429 0.02 1 311 . 246 GLU HB2 H 2.117 0.02 2 312 . 246 GLU HB3 H 2.243 0.02 2 313 . 246 GLU HG2 H 2.509 0.02 1 314 . 246 GLU HG3 H 2.509 0.02 1 315 . 247 GLN N N 122.571 0.05 1 316 . 247 GLN H H 8.403 0.02 1 317 . 247 GLN HA H 4.555 0.02 1 318 . 247 GLN HB2 H 2.130 0.02 2 319 . 247 GLN HB3 H 2.268 0.02 2 320 . 247 GLN HG2 H 2.496 0.02 1 321 . 247 GLN HG3 H 2.496 0.02 1 322 . 248 GLY N N 109.971 0.05 1 323 . 248 GLY H H 8.496 0.02 1 324 . 248 GLY HA2 H 4.125 0.02 1 325 . 248 GLY HA3 H 4.125 0.02 1 326 . 249 VAL N N 119.126 0.05 1 327 . 249 VAL H H 8.105 0.02 1 328 . 249 VAL HA H 4.264 0.02 1 329 . 249 VAL HB H 2.243 0.02 1 330 . 249 VAL HG1 H 1.056 0.02 1 331 . 249 VAL HG2 H 1.056 0.02 1 332 . 250 GLY N N 112.175 0.05 1 333 . 250 GLY H H 8.618 0.02 1 334 . 250 GLY HA2 H 4.075 0.02 1 335 . 250 GLY HA3 H 4.075 0.02 1 336 . 251 HIS N N 118.468 0.05 1 337 . 251 HIS H H 8.494 0.02 1 338 . 251 HIS HA H 4.896 0.02 1 339 . 251 HIS HB2 H 3.317 0.02 2 340 . 251 HIS HB3 H 3.443 0.02 2 341 . 252 THR N N 115.710 0.05 1 342 . 252 THR H H 8.354 0.02 1 343 . 252 THR HA H 4.517 0.02 1 344 . 252 THR HB H 4.365 0.02 1 345 . 252 THR HG2 H 1.334 0.02 2 346 . 253 ASP N N 123.286 0.05 1 347 . 253 ASP H H 8.614 0.02 1 348 . 253 ASP HA H 4.770 0.02 1 349 . 253 ASP HB2 H 2.837 0.02 1 350 . 253 ASP HB3 H 2.837 0.02 1 351 . 254 LYS N N 122.034 0.05 1 352 . 254 LYS H H 8.377 0.02 1 353 . 254 LYS HA H 4.403 0.02 1 354 . 254 LYS HB2 H 1.889 0.02 2 355 . 254 LYS HB3 H 1.991 0.02 2 356 . 254 LYS HG2 H 1.574 0.02 1 357 . 254 LYS HG3 H 1.574 0.02 1 358 . 255 ALA N N 124.827 0.05 1 359 . 255 ALA H H 8.366 0.02 1 360 . 255 ALA HA H 4.429 0.02 1 361 . 255 ALA HB H 1.523 0.02 1 362 . 256 VAL N N 119.848 0.05 1 363 . 256 VAL H H 8.130 0.02 1 364 . 256 VAL HA H 4.214 0.02 1 365 . 256 VAL HB H 2.218 0.02 1 366 . 256 VAL HG1 H 1.081 0.02 1 367 . 256 VAL HG2 H 1.081 0.02 1 368 . 257 LYS N N 125.148 0.05 1 369 . 257 LYS H H 8.485 0.02 1 370 . 257 LYS HA H 4.467 0.02 1 371 . 257 LYS HB2 H 1.940 0.02 1 372 . 257 LYS HB3 H 1.940 0.02 1 373 . 257 LYS HG2 H 1.574 0.02 1 374 . 257 LYS HG3 H 1.574 0.02 1 375 . 258 SER N N 116.969 0.05 1 376 . 258 SER H H 8.348 0.02 1 377 . 258 SER HA H 4.883 0.02 1 378 . 258 SER HB2 H 4.012 0.02 1 379 . 258 SER HB3 H 4.012 0.02 1 380 . 259 ALA N N 126.552 0.05 1 381 . 259 ALA H H 8.438 0.02 1 382 . 259 ALA HA H 4.542 0.02 1 383 . 259 ALA HB H 1.548 0.02 1 384 . 260 ARG N N 120.568 0.05 1 385 . 260 ARG H H 8.349 0.02 1 386 . 260 ARG HA H 4.467 0.02 1 387 . 260 ARG HB2 H 1.927 0.02 1 388 . 260 ARG HB3 H 1.927 0.02 1 389 . 260 ARG HG2 H 1.801 0.02 1 390 . 260 ARG HG3 H 1.801 0.02 1 391 . 261 LYS N N 123.057 0.05 1 392 . 261 LYS H H 8.398 0.02 1 393 . 261 LYS HA H 4.416 0.02 1 394 . 261 LYS HB2 H 1.876 0.02 2 395 . 261 LYS HB3 H 1.940 0.02 2 396 . 261 LYS HG2 H 1.586 0.02 1 397 . 261 LYS HG3 H 1.586 0.02 1 398 . 262 ALA N N 125.682 0.05 1 399 . 262 ALA H H 8.385 0.02 1 400 . 262 ALA HA H 4.429 0.02 1 401 . 262 ALA HB H 1.523 0.02 1 402 . 263 ARG N N 121.384 0.05 1 403 . 263 ARG H H 8.420 0.02 1 404 . 263 ARG HA H 4.441 0.02 1 405 . 263 ARG HB2 H 1.940 0.02 1 406 . 263 ARG HB3 H 1.940 0.02 1 407 . 263 ARG HG2 H 1.788 0.02 1 408 . 263 ARG HG3 H 1.788 0.02 1 409 . 264 LYS N N 123.072 0.05 1 410 . 264 LYS H H 8.498 0.02 1 411 . 264 LYS HA H 4.467 0.02 1 412 . 264 LYS HB2 H 1.889 0.02 2 413 . 264 LYS HB3 H 1.965 0.02 2 414 . 264 LYS HG2 H 1.561 0.02 1 415 . 264 LYS HG3 H 1.561 0.02 1 416 . 265 ASN N N 120.446 0.05 1 417 . 265 ASN H H 8.555 0.02 1 418 . 265 ASN HA H 4.833 0.02 1 419 . 265 ASN HB2 H 2.900 0.02 1 420 . 265 ASN HB3 H 2.900 0.02 1 421 . 266 LYS N N 122.248 0.05 1 422 . 266 LYS H H 8.391 0.02 1 423 . 266 LYS HA H 4.467 0.02 1 424 . 266 LYS HB2 H 1.890 0.02 2 425 . 266 LYS HB3 H 1.978 0.02 2 426 . 266 LYS HG2 H 1.574 0.02 1 427 . 266 LYS HG3 H 1.574 0.02 1 428 . 267 ILE N N 123.084 0.05 1 429 . 267 ILE H H 8.357 0.02 1 430 . 267 ILE HA H 4.302 0.02 1 431 . 267 ILE HB H 1.927 0.02 1 432 . 267 ILE HG2 H 1.334 0.02 1 433 . 267 ILE HG12 H 1.612 0.02 1 434 . 267 ILE HG13 H 1.612 0.02 1 435 . 267 ILE HD1 H 1.043 0.02 1 436 . 268 ARG N N 129.315 0.05 1 437 . 268 ARG H H 8.027 0.02 1 438 . 268 ARG HA H 4.290 0.02 1 439 . 268 ARG HB2 H 1.877 0.02 2 440 . 268 ARG HB3 H 1.991 0.02 2 441 . 268 ARG HG2 H 1.713 0.02 1 442 . 268 ARG HG3 H 1.713 0.02 1 stop_ save_