data_4286 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments of the Unstructured Yeast Vesicular SNARE Snc1. ; _BMRB_accession_number 4286 _BMRB_flat_file_name bmr4286.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 Pollock Elizabeth . . 3 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" 438 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-01 original author . stop_ _Original_release_date 1999-10-01 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_Snc1p _Saveframe_category molecular_system _Mol_system_name Snc1 _Abbreviation_common Snc1p _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Snc1 $Snc1 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_Snc1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Snc1 _Abbreviation_common Snc1 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 98 _Mol_residue_sequence ; GSPEFMSSSTPFDPYALSEH DEERPQNVQSKSRTAELQAE IDDTVGIMRDNINKVAERGE RLTSIEDKADNLAVSAQGFK RGANRVRKAMWYKDLKMK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 SER 3 -1 PRO 4 0 GLU 5 1 PHE 6 2 MET 7 3 SER 8 4 SER 9 5 SER 10 6 THR 11 7 PRO 12 8 PHE 13 9 ASP 14 10 PRO 15 11 TYR 16 12 ALA 17 13 LEU 18 14 SER 19 15 GLU 20 16 HIS 21 17 ASP 22 18 GLU 23 19 GLU 24 20 ARG 25 21 PRO 26 22 GLN 27 23 ASN 28 24 VAL 29 25 GLN 30 26 SER 31 27 LYS 32 28 SER 33 29 ARG 34 30 THR 35 31 ALA 36 32 GLU 37 33 LEU 38 34 GLN 39 35 ALA 40 36 GLU 41 37 ILE 42 38 ASP 43 39 ASP 44 40 THR 45 41 VAL 46 42 GLY 47 43 ILE 48 44 MET 49 45 ARG 50 46 ASP 51 47 ASN 52 48 ILE 53 49 ASN 54 50 LYS 55 51 VAL 56 52 ALA 57 53 GLU 58 54 ARG 59 55 GLY 60 56 GLU 61 57 ARG 62 58 LEU 63 59 THR 64 60 SER 65 61 ILE 66 62 GLU 67 63 ASP 68 64 LYS 69 65 ALA 70 66 ASP 71 67 ASN 72 68 LEU 73 69 ALA 74 70 VAL 75 71 SER 76 72 ALA 77 73 GLN 78 74 GLY 79 75 PHE 80 76 LYS 81 77 ARG 82 78 GLY 83 79 ALA 84 80 ASN 85 81 ARG 86 82 VAL 87 83 ARG 88 84 LYS 89 85 ALA 90 86 MET 91 87 TRP 92 88 TYR 93 89 LYS 94 90 ASP 95 91 LEU 96 92 LYS 97 93 MET 98 94 LYS 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 3B5N "Structure Of The Yeast Plasma Membrane Snare Complex" 61.22 61 100.00 100.00 1.09e-33 DBJ GAA21395 "K7_Snc1p [Saccharomyces cerevisiae Kyokai no. 7]" 94.90 117 100.00 100.00 5.15e-61 EMBL CAY77620 "Snc1p [Saccharomyces cerevisiae EC1118]" 94.90 117 100.00 100.00 5.15e-61 GB AAA35069 "synaptobrevin [Saccharomyces cerevisiae]" 94.90 117 100.00 100.00 5.15e-61 GB AAC05002 "Snc1p: Vesicle-associated membrane protein,synaptobrevin homolog [Saccharomyces cerevisiae]" 94.90 117 100.00 100.00 5.15e-61 GB AHY74337 "Snc1p [Saccharomyces cerevisiae YJM993]" 94.90 117 100.00 100.00 5.15e-61 GB AJO92283 "Snc1p [Saccharomyces cerevisiae YJM189]" 94.90 117 100.00 100.00 5.15e-61 GB AJO92361 "Snc1p [Saccharomyces cerevisiae YJM193]" 94.90 117 100.00 100.00 5.15e-61 REF NP_009372 "SNAP receptor SNC1 [Saccharomyces cerevisiae S288c]" 94.90 117 100.00 100.00 5.15e-61 SP P31109 "RecName: Full=Synaptobrevin homolog 1" 94.90 117 100.00 100.00 5.15e-61 TPG DAA06958 "TPA: SNAP receptor SNC1 [Saccharomyces cerevisiae S288c]" 94.90 117 100.00 100.00 5.15e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Snc1 '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_name $Snc1 'recombinant technology' . . . . . 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 $Snc1 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 Snc1 _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 117.492 0.05 1 2 . 2 SER H H 8.770 0.02 1 3 . 2 SER HA H 4.891 0.02 1 4 . 2 SER HB2 H 3.974 0.02 1 5 . 2 SER HB3 H 3.974 0.02 1 6 . 4 GLU N N 120.838 0.05 1 7 . 4 GLU H H 8.529 0.02 1 8 . 4 GLU HA H 4.509 0.02 1 9 . 4 GLU HB2 H 1.875 0.02 2 10 . 4 GLU HB3 H 1.951 0.02 2 11 . 5 PHE N N 120.514 0.05 1 12 . 5 PHE H H 8.208 0.02 1 13 . 5 PHE HA H 4.279 0.02 1 14 . 5 PHE HB2 H 3.128 0.02 2 15 . 5 PHE HB3 H 3.230 0.02 2 16 . 6 MET N N 122.279 0.05 1 17 . 6 MET H H 8.277 0.02 1 18 . 6 MET HA H 4.719 0.02 1 19 . 6 MET HB2 H 2.028 0.02 1 20 . 6 MET HB3 H 2.028 0.02 1 21 . 7 SER N N 117.497 0.05 1 22 . 7 SER H H 8.417 0.02 1 23 . 7 SER HA H 4.441 0.02 1 24 . 7 SER HB2 H 3.974 0.02 1 25 . 7 SER HB3 H 3.974 0.02 1 26 . 8 SER N N 117.805 0.05 1 27 . 8 SER H H 8.429 0.02 1 28 . 8 SER HA H 4.593 0.02 1 29 . 8 SER HB2 H 3.974 0.02 1 30 . 8 SER HB3 H 3.974 0.02 1 31 . 9 SER N N 117.316 0.05 1 32 . 9 SER H H 8.381 0.02 1 33 . 9 SER HA H 4.555 0.02 1 34 . 9 SER HB2 H 3.986 0.02 1 35 . 9 SER HB3 H 3.986 0.02 1 36 . 10 THR N N 118.260 0.05 1 37 . 10 THR H H 8.234 0.02 1 38 . 10 THR HA H 4.643 0.02 1 39 . 10 THR HB H 4.239 0.02 1 40 . 10 THR HG2 H 1.321 0.02 2 41 . 12 PHE N N 121.173 0.05 1 42 . 12 PHE H H 8.328 0.02 1 43 . 12 PHE HA H 4.479 0.02 1 44 . 12 PHE HB2 H 3.076 0.02 2 45 . 12 PHE HB3 H 3.178 0.02 2 46 . 12 PHE HD1 H 7.283 0.02 1 47 . 12 PHE HD2 H 7.283 0.02 1 48 . 13 ASP N N 124.591 0.05 1 49 . 13 ASP H H 8.186 0.02 1 50 . 13 ASP HA H 4.934 0.02 1 51 . 13 ASP HB2 H 2.622 0.02 2 52 . 13 ASP HB3 H 2.862 0.02 2 53 . 15 TYR N N 118.285 0.05 1 54 . 15 TYR H H 8.101 0.02 1 55 . 15 TYR HA H 4.605 0.02 1 56 . 15 TYR HB2 H 2.989 0.02 2 57 . 15 TYR HB3 H 3.279 0.02 2 58 . 15 TYR HE1 H 7.233 0.02 1 59 . 15 TYR HE2 H 7.233 0.02 1 60 . 15 TYR HD1 H 7.587 0.02 1 61 . 15 TYR HD2 H 7.587 0.02 1 62 . 16 ALA N N 123.736 0.05 1 63 . 16 ALA H H 7.559 0.02 1 64 . 16 ALA HA H 4.315 0.02 1 65 . 16 ALA HB H 1.485 0.02 1 66 . 17 LEU N N 120.402 0.05 1 67 . 17 LEU H H 8.157 0.02 1 68 . 17 LEU HA H 4.403 0.02 1 69 . 17 LEU HB2 H 1.738 0.02 1 70 . 17 LEU HB3 H 1.738 0.02 1 71 . 17 LEU HD1 H 1.472 0.02 1 72 . 17 LEU HD2 H 1.472 0.02 1 73 . 18 SER N N 116.030 0.05 1 74 . 18 SER H H 8.260 0.02 1 75 . 18 SER HA H 4.530 0.02 1 76 . 18 SER HB2 H 3.948 0.02 1 77 . 18 SER HB3 H 3.948 0.02 1 78 . 19 GLU N N 122.146 0.05 1 79 . 19 GLU H H 8.373 0.02 1 80 . 19 GLU HA H 4.353 0.02 1 81 . 19 GLU HB2 H 2.003 0.02 2 82 . 19 GLU HB3 H 2.079 0.02 2 83 . 19 GLU HG2 H 2.369 0.02 1 84 . 19 GLU HG3 H 2.369 0.02 1 85 . 20 HIS N N 118.769 0.05 1 86 . 20 HIS H H 8.508 0.02 1 87 . 20 HIS HA H 4.795 0.02 1 88 . 20 HIS HB2 H 3.254 0.02 2 89 . 20 HIS HB3 H 3.380 0.02 2 90 . 21 ASP N N 121.491 0.05 1 91 . 21 ASP H H 8.472 0.02 1 92 . 21 ASP HA H 4.694 0.02 1 93 . 21 ASP HB2 H 2.774 0.02 1 94 . 21 ASP HB3 H 2.774 0.02 1 95 . 22 GLU N N 121.059 0.05 1 96 . 22 GLU H H 8.545 0.02 1 97 . 22 GLU HA H 4.365 0.02 1 98 . 22 GLU HB2 H 2.054 0.02 2 99 . 22 GLU HB3 H 2.180 0.02 2 100 . 22 GLU HG2 H 2.445 0.02 1 101 . 22 GLU HG3 H 2.445 0.02 1 102 . 23 GLU N N 121.357 0.05 1 103 . 23 GLU H H 8.405 0.02 1 104 . 23 GLU HA H 4.744 0.02 1 105 . 23 GLU HB2 H 2.066 0.02 2 106 . 23 GLU HB3 H 2.154 0.02 2 107 . 23 GLU HG2 H 2.433 0.02 1 108 . 23 GLU HG3 H 2.433 0.02 1 109 . 24 ARG N N 123.150 0.05 1 110 . 24 ARG H H 8.334 0.02 1 111 . 24 ARG HA H 4.391 0.02 1 112 . 24 ARG HB2 H 1.788 0.02 2 113 . 24 ARG HB3 H 1.890 0.02 2 114 . 24 ARG HG2 H 1.472 0.02 1 115 . 24 ARG HG3 H 1.472 0.02 1 116 . 26 GLN N N 120.420 0.05 1 117 . 26 GLN H H 8.649 0.02 1 118 . 26 GLN HA H 4.365 0.02 1 119 . 26 GLN HB2 H 2.028 0.02 2 120 . 26 GLN HB3 H 2.142 0.02 2 121 . 26 GLN HG2 H 2.458 0.02 1 122 . 26 GLN HG3 H 2.458 0.02 1 123 . 27 ASN N N 119.714 0.05 1 124 . 27 ASN H H 8.536 0.02 1 125 . 27 ASN HA H 4.807 0.02 1 126 . 27 ASN HB2 H 2.887 0.02 1 127 . 27 ASN HB3 H 2.887 0.02 1 128 . 28 VAL N N 120.416 0.05 1 129 . 28 VAL H H 8.163 0.02 1 130 . 28 VAL HA H 4.188 0.02 1 131 . 28 VAL HB H 2.180 0.02 1 132 . 28 VAL HG1 H 1.018 0.02 1 133 . 28 VAL HG2 H 1.018 0.02 1 134 . 29 GLN N N 123.909 0.05 1 135 . 29 GLN H H 8.551 0.02 1 136 . 29 GLN HA H 4.441 0.02 1 137 . 29 GLN HB2 H 2.078 0.02 2 138 . 29 GLN HB3 H 2.180 0.02 2 139 . 29 GLN HG2 H 2.470 0.02 1 140 . 29 GLN HG3 H 2.470 0.02 1 141 . 30 SER N N 117.819 0.05 1 142 . 30 SER H H 8.440 0.02 1 143 . 30 SER HA H 4.567 0.02 1 144 . 30 SER HB2 H 3.986 0.02 1 145 . 30 SER HB3 H 3.986 0.02 1 146 . 31 LYS N N 122.055 0.05 1 147 . 31 LYS H H 8.231 0.02 1 148 . 31 LYS HA H 4.378 0.02 1 149 . 31 LYS HB2 H 1.738 0.02 1 150 . 31 LYS HB3 H 1.738 0.02 1 151 . 32 SER N N 116.747 0.05 1 152 . 32 SER H H 8.368 0.02 1 153 . 32 SER HA H 4.441 0.02 1 154 . 32 SER HB2 H 3.974 0.02 1 155 . 32 SER HB3 H 3.974 0.02 1 156 . 33 ARG N N 123.547 0.05 1 157 . 33 ARG H H 8.496 0.02 1 158 . 33 ARG HA H 4.492 0.02 1 159 . 33 ARG HB2 H 1.889 0.02 2 160 . 33 ARG HB3 H 1.991 0.02 2 161 . 33 ARG HG2 H 1.750 0.02 1 162 . 33 ARG HG3 H 1.750 0.02 1 163 . 34 THR N N 115.049 0.05 1 164 . 34 THR H H 8.189 0.02 1 165 . 34 THR HA H 4.360 0.02 4 166 . 34 THR HB H 4.346 0.02 4 167 . 34 THR HG2 H 1.321 0.02 2 168 . 35 ALA N N 125.788 0.05 1 169 . 35 ALA H H 8.334 0.02 1 170 . 35 ALA HA H 4.340 0.02 1 171 . 35 ALA HB H 1.510 0.02 1 172 . 36 GLU N N 119.801 0.05 1 173 . 36 GLU H H 8.348 0.02 1 174 . 36 GLU HA H 4.340 0.02 1 175 . 36 GLU HB2 H 2.117 0.02 1 176 . 36 GLU HB3 H 2.117 0.02 1 177 . 36 GLU HG2 H 2.445 0.02 1 178 . 36 GLU HG3 H 2.445 0.02 1 179 . 37 LEU N N 122.494 0.05 1 180 . 37 LEU H H 8.220 0.02 1 181 . 37 LEU HA H 4.327 0.02 1 182 . 37 LEU HB2 H 1.750 0.02 1 183 . 37 LEU HB3 H 1.750 0.02 1 184 . 37 LEU HD1 H 0.980 0.02 1 185 . 37 LEU HD2 H 0.980 0.02 1 186 . 38 GLN N N 120.681 0.05 1 187 . 38 GLN H H 8.342 0.02 1 188 . 38 GLN HA H 4.340 0.02 1 189 . 38 GLN HB2 H 2.142 0.02 1 190 . 38 GLN HB3 H 2.142 0.02 1 191 . 38 GLN HG2 H 2.458 0.02 1 192 . 38 GLN HG3 H 2.458 0.02 1 193 . 39 ALA N N 124.112 0.05 1 194 . 39 ALA H H 8.227 0.02 1 195 . 39 ALA HA H 4.315 0.02 1 196 . 39 ALA HB H 1.498 0.02 1 197 . 40 GLU N N 119.381 0.05 1 198 . 40 GLU H H 8.233 0.02 1 199 . 40 GLU HA H 4.365 0.02 1 200 . 40 GLU HB2 H 2.129 0.02 1 201 . 40 GLU HB3 H 2.129 0.02 1 202 . 40 GLU HG2 H 2.496 0.02 1 203 . 40 GLU HG3 H 2.496 0.02 1 204 . 41 ILE N N 121.783 0.05 1 205 . 41 ILE H H 8.159 0.02 1 206 . 41 ILE HA H 4.176 0.02 1 207 . 41 ILE HB H 1.965 0.02 1 208 . 41 ILE HG2 H 1.258 0.02 1 209 . 41 ILE HG12 H 1.586 0.02 1 210 . 41 ILE HG13 H 1.586 0.02 1 211 . 41 ILE HD1 H 0.967 0.02 1 212 . 42 ASP N N 123.588 0.05 1 213 . 42 ASP H H 8.471 0.02 1 214 . 42 ASP HA H 4.719 0.02 1 215 . 42 ASP HB2 H 2.749 0.02 2 216 . 42 ASP HB3 H 2.887 0.02 2 217 . 43 ASP N N 118.939 0.05 1 218 . 43 ASP H H 8.343 0.02 1 219 . 43 ASP HA H 4.706 0.02 1 220 . 43 ASP HB2 H 2.862 0.02 1 221 . 43 ASP HB3 H 2.862 0.02 1 222 . 44 THR N N 114.119 0.05 1 223 . 44 THR H H 8.300 0.02 1 224 . 44 THR HA H 4.770 0.02 1 225 . 44 THR HG2 H 1.321 0.02 2 226 . 45 VAL N N 121.799 0.05 1 227 . 45 VAL H H 8.042 0.02 1 228 . 45 VAL HA H 4.163 0.02 1 229 . 45 VAL HB H 2.218 0.02 1 230 . 45 VAL HG1 H 1.056 0.02 1 231 . 45 VAL HG2 H 1.056 0.02 1 232 . 46 GLY N N 111.766 0.05 1 233 . 46 GLY H H 8.459 0.02 1 234 . 46 GLY HA2 H 4.024 0.02 1 235 . 46 GLY HA3 H 4.024 0.02 1 236 . 47 ILE N N 120.069 0.05 1 237 . 47 ILE H H 7.986 0.02 1 238 . 47 ILE HA H 4.226 0.02 1 239 . 47 ILE HB H 1.965 0.02 1 240 . 47 ILE HG2 H 1.258 0.02 1 241 . 47 ILE HG12 H 1.536 0.02 1 242 . 47 ILE HG13 H 1.536 0.02 1 243 . 47 ILE HD1 H 0.992 0.02 1 244 . 48 MET N N 123.951 0.05 1 245 . 48 MET H H 8.479 0.02 1 246 . 48 MET HA H 4.580 0.02 1 247 . 48 MET HB2 H 2.142 0.02 1 248 . 48 MET HB3 H 2.142 0.02 1 249 . 48 MET HG2 H 2.635 0.02 1 250 . 48 MET HG3 H 2.635 0.02 1 251 . 49 ARG N N 122.461 0.05 1 252 . 49 ARG H H 8.377 0.02 1 253 . 49 ARG HA H 4.378 0.02 1 254 . 49 ARG HB2 H 1.902 0.02 1 255 . 49 ARG HB3 H 1.902 0.02 1 256 . 49 ARG HG2 H 1.738 0.02 1 257 . 49 ARG HG3 H 1.738 0.02 1 258 . 50 ASP N N 120.551 0.05 1 259 . 50 ASP H H 8.403 0.02 1 260 . 50 ASP HA H 4.681 0.02 1 261 . 50 ASP HB2 H 2.786 0.02 1 262 . 50 ASP HB3 H 2.786 0.02 1 263 . 51 ASN N N 118.889 0.05 1 264 . 51 ASN H H 8.418 0.02 1 265 . 51 ASN HA H 4.770 0.02 1 266 . 51 ASN HB2 H 2.887 0.02 1 267 . 51 ASN HB3 H 2.887 0.02 1 268 . 52 ILE N N 120.605 0.05 1 269 . 52 ILE H H 8.108 0.02 1 270 . 52 ILE HA H 4.188 0.02 1 271 . 52 ILE HB H 2.003 0.02 1 272 . 52 ILE HG2 H 1.270 0.02 1 273 . 52 ILE HG12 H 1.536 0.02 1 274 . 52 ILE HG13 H 1.536 0.02 1 275 . 52 ILE HD1 H 0.980 0.02 1 276 . 53 ASN N N 121.581 0.05 1 277 . 53 ASN H H 8.497 0.02 1 278 . 53 ASN HA H 4.782 0.02 1 279 . 53 ASN HB2 H 2.875 0.02 1 280 . 53 ASN HB3 H 2.875 0.02 1 281 . 54 LYS N N 121.978 0.05 1 282 . 54 LYS H H 8.221 0.02 1 283 . 54 LYS HA H 4.365 0.02 1 284 . 54 LYS HB2 H 1.889 0.02 1 285 . 54 LYS HB3 H 1.889 0.02 1 286 . 54 LYS HG2 H 1.498 0.02 1 287 . 54 LYS HG3 H 1.498 0.02 1 288 . 55 VAL N N 121.264 0.05 1 289 . 55 VAL H H 8.147 0.02 1 290 . 55 VAL HA H 4.113 0.02 1 291 . 55 VAL HB H 2.167 0.02 1 292 . 55 VAL HG1 H 1.030 0.02 1 293 . 55 VAL HG2 H 1.030 0.02 1 294 . 56 ALA N N 127.228 0.05 1 295 . 56 ALA H H 8.370 0.02 1 296 . 56 ALA HA H 4.378 0.02 1 297 . 56 ALA HB H 1.472 0.02 1 298 . 57 GLU N N 120.205 0.05 1 299 . 57 GLU H H 8.368 0.02 1 300 . 57 GLU HA H 4.378 0.02 1 301 . 57 GLU HB2 H 2.053 0.02 2 302 . 57 GLU HB3 H 2.155 0.02 2 303 . 57 GLU HG2 H 2.420 0.02 1 304 . 57 GLU HG3 H 2.420 0.02 1 305 . 58 ARG N N 121.841 0.05 1 306 . 58 ARG H H 8.428 0.02 1 307 . 58 ARG HA H 4.365 0.02 1 308 . 58 ARG HB2 H 1.902 0.02 2 309 . 58 ARG HB3 H 1.990 0.02 2 310 . 58 ARG HG2 H 1.738 0.02 1 311 . 58 ARG HG3 H 1.738 0.02 1 312 . 59 GLY N N 109.769 0.05 1 313 . 59 GLY H H 8.476 0.02 1 314 . 59 GLY HA2 H 4.049 0.02 1 315 . 59 GLY HA3 H 4.049 0.02 1 316 . 60 GLU N N 120.605 0.05 1 317 . 60 GLU H H 8.318 0.02 1 318 . 60 GLU HA H 4.391 0.02 1 319 . 60 GLU HB2 H 2.079 0.02 1 320 . 60 GLU HB3 H 2.079 0.02 1 321 . 60 GLU HG2 H 2.407 0.02 1 322 . 60 GLU HG3 H 2.407 0.02 1 323 . 61 ARG N N 123.836 0.05 1 324 . 61 ARG H H 8.447 0.02 1 325 . 61 ARG HA H 4.252 0.02 1 326 . 61 ARG HB2 H 2.028 0.02 1 327 . 61 ARG HB3 H 2.028 0.02 1 328 . 62 LEU N N 123.756 0.05 1 329 . 62 LEU H H 8.436 0.02 1 330 . 62 LEU HA H 4.416 0.02 1 331 . 62 LEU HB2 H 1.738 0.02 1 332 . 62 LEU HB3 H 1.738 0.02 1 333 . 62 LEU HD1 H 0.992 0.02 1 334 . 62 LEU HD2 H 0.992 0.02 1 335 . 63 THR N N 114.611 0.05 1 336 . 63 THR H H 8.206 0.02 1 337 . 63 THR HA H 4.504 0.02 1 338 . 63 THR HB H 4.340 0.02 1 339 . 63 THR HG2 H 1.296 0.02 2 340 . 64 SER N N 118.188 0.05 1 341 . 64 SER H H 8.394 0.02 1 342 . 64 SER HA H 4.605 0.02 1 343 . 64 SER HB2 H 3.986 0.02 1 344 . 64 SER HB3 H 3.986 0.02 1 345 . 65 ILE N N 122.400 0.05 1 346 . 65 ILE H H 8.248 0.02 1 347 . 65 ILE HA H 4.252 0.02 1 348 . 65 ILE HB H 1.990 0.02 1 349 . 65 ILE HG2 H 1.296 0.02 1 350 . 65 ILE HG12 H 1.561 0.02 1 351 . 65 ILE HG13 H 1.561 0.02 1 352 . 65 ILE HD1 H 1.005 0.02 1 353 . 66 GLU N N 123.911 0.05 1 354 . 66 GLU H H 8.457 0.02 1 355 . 66 GLU HA H 4.416 0.02 1 356 . 66 GLU HB2 H 2.104 0.02 1 357 . 66 GLU HB3 H 2.104 0.02 1 358 . 66 GLU HG2 H 2.420 0.02 1 359 . 66 GLU HG3 H 2.420 0.02 1 360 . 67 ASP N N 121.684 0.05 1 361 . 67 ASP H H 8.379 0.02 1 362 . 67 ASP HA H 4.694 0.02 1 363 . 67 ASP HB2 H 2.799 0.02 1 364 . 67 ASP HB3 H 2.799 0.02 1 365 . 68 LYS N N 122.013 0.05 1 366 . 68 LYS H H 8.272 0.02 1 367 . 68 LYS HA H 4.365 0.02 1 368 . 68 LYS HB2 H 1.851 0.02 2 369 . 68 LYS HB3 H 1.953 0.02 2 370 . 68 LYS HG2 H 1.523 0.02 1 371 . 68 LYS HG3 H 1.523 0.02 1 372 . 69 ALA N N 124.569 0.05 1 373 . 69 ALA H H 8.356 0.02 1 374 . 69 ALA HA H 4.353 0.02 1 375 . 69 ALA HB H 1.472 0.02 1 376 . 70 ASP N N 118.973 0.05 1 377 . 70 ASP H H 8.307 0.02 1 378 . 70 ASP HA H 4.353 0.02 1 379 . 70 ASP HB2 H 2.786 0.02 1 380 . 70 ASP HB3 H 2.786 0.02 1 381 . 73 ALA N N 124.222 0.05 1 382 . 73 ALA H H 8.203 0.02 1 383 . 73 ALA HA H 4.378 0.02 1 384 . 73 ALA HB H 1.485 0.02 1 385 . 74 VAL N N 118.530 0.05 1 386 . 74 VAL H H 8.041 0.02 1 387 . 74 VAL HA H 4.151 0.02 1 388 . 74 VAL HB H 2.167 0.02 1 389 . 74 VAL HG1 H 1.018 0.02 1 390 . 74 VAL HG2 H 1.018 0.02 1 391 . 75 SER N N 118.519 0.05 1 392 . 75 SER H H 8.316 0.02 1 393 . 75 SER HA H 4.517 0.02 1 394 . 75 SER HB2 H 3.948 0.02 1 395 . 75 SER HB3 H 3.948 0.02 1 396 . 76 ALA N N 126.059 0.05 1 397 . 76 ALA H H 8.392 0.02 1 398 . 76 ALA HA H 4.403 0.02 1 399 . 76 ALA HB H 1.510 0.02 1 400 . 77 GLN N N 118.557 0.05 1 401 . 77 GLN H H 8.287 0.02 1 402 . 77 GLN HA H 4.391 0.02 1 403 . 77 GLN HB2 H 2.053 0.02 2 404 . 77 GLN HB3 H 2.167 0.02 2 405 . 77 GLN HG2 H 2.458 0.02 1 406 . 77 GLN HG3 H 2.458 0.02 1 407 . 78 GLY N N 109.272 0.05 1 408 . 78 GLY H H 8.323 0.02 1 409 . 78 GLY HA2 H 3.974 0.02 1 410 . 78 GLY HA3 H 3.974 0.02 1 411 . 79 PHE N N 120.132 0.05 1 412 . 79 PHE H H 8.073 0.02 1 413 . 79 PHE HA H 4.681 0.02 1 414 . 79 PHE HB2 H 3.153 0.02 1 415 . 79 PHE HB3 H 3.153 0.02 1 416 . 80 LYS N N 123.429 0.05 1 417 . 80 LYS H H 8.297 0.02 1 418 . 80 LYS HA H 4.353 0.02 1 419 . 80 LYS HB2 H 1.814 0.02 1 420 . 80 LYS HB3 H 1.814 0.02 1 421 . 80 LYS HG2 H 1.460 0.02 1 422 . 80 LYS HG3 H 1.460 0.02 1 423 . 81 ARG N N 122.604 0.05 1 424 . 81 ARG H H 8.375 0.02 1 425 . 81 ARG HA H 4.567 0.02 1 426 . 81 ARG HB2 H 1.902 0.02 1 427 . 81 ARG HB3 H 1.902 0.02 1 428 . 81 ARG HG2 H 1.750 0.02 1 429 . 81 ARG HG3 H 1.750 0.02 1 430 . 82 GLY N N 110.647 0.05 1 431 . 82 GLY H H 8.532 0.02 1 432 . 82 GLY HA2 H 4.195 0.02 1 433 . 82 GLY HA3 H 4.195 0.02 1 434 . 83 ALA N N 123.868 0.05 1 435 . 83 ALA H H 8.245 0.02 1 436 . 83 ALA HA H 4.378 0.02 1 437 . 83 ALA HB H 1.460 0.02 1 438 . 84 ASN N N 117.719 0.05 1 439 . 84 ASN H H 8.494 0.02 1 440 . 84 ASN HA H 4.744 0.02 1 441 . 84 ASN HB2 H 2.875 0.02 1 442 . 84 ASN HB3 H 2.875 0.02 1 443 . 85 ARG N N 121.495 0.05 1 444 . 85 ARG H H 8.274 0.02 1 445 . 85 ARG HA H 4.403 0.02 1 446 . 85 ARG HB2 H 1.864 0.02 1 447 . 85 ARG HB3 H 1.864 0.02 1 448 . 85 ARG HG2 H 1.662 0.02 1 449 . 85 ARG HG3 H 1.662 0.02 1 450 . 86 VAL N N 121.452 0.05 1 451 . 86 VAL H H 8.173 0.02 1 452 . 86 VAL HA H 4.125 0.02 1 453 . 86 VAL HB H 2.155 0.02 1 454 . 86 VAL HG1 H 1.030 0.02 1 455 . 86 VAL HG2 H 1.030 0.02 1 456 . 87 ARG N N 125.294 0.05 1 457 . 87 ARG H H 8.423 0.02 1 458 . 87 ARG HA H 4.403 0.02 1 459 . 87 ARG HB2 H 1.839 0.02 1 460 . 87 ARG HB3 H 1.839 0.02 1 461 . 87 ARG HG2 H 1.662 0.02 1 462 . 87 ARG HG3 H 1.662 0.02 1 463 . 88 LYS N N 122.128 0.05 1 464 . 88 LYS H H 8.461 0.02 1 465 . 88 LYS HA H 4.403 0.02 1 466 . 88 LYS HB2 H 1.889 0.02 1 467 . 88 LYS HB3 H 1.889 0.02 1 468 . 88 LYS HG2 H 1.725 0.02 1 469 . 88 LYS HG3 H 1.725 0.02 1 470 . 89 ALA N N 124.742 0.05 1 471 . 89 ALA H H 8.334 0.02 1 472 . 89 ALA HA H 4.277 0.02 1 473 . 89 ALA HB H 1.397 0.02 1 474 . 90 MET N N 118.798 0.05 1 475 . 90 MET H H 8.308 0.02 1 476 . 90 MET HA H 4.391 0.02 1 477 . 90 MET HB2 H 1.978 0.02 1 478 . 90 MET HB3 H 1.978 0.02 1 479 . 90 MET HG2 H 2.508 0.02 1 480 . 90 MET HG3 H 2.508 0.02 1 481 . 91 TRP N N 121.181 0.05 1 482 . 91 TRP H H 7.986 0.02 1 483 . 91 TRP HA H 4.681 0.02 1 484 . 91 TRP HB2 H 3.304 0.02 1 485 . 91 TRP HB3 H 3.304 0.02 1 486 . 91 TRP NE1 N 129.809 0.05 1 487 . 91 TRP HD1 H 7.271 0.02 1 488 . 91 TRP HE1 H 10.237 0.02 1 489 . 91 TRP HZ2 H 7.574 0.02 1 490 . 92 TYR N N 120.835 0.05 1 491 . 92 TYR H H 7.695 0.02 1 492 . 92 TYR HA H 4.428 0.02 1 493 . 92 TYR HB2 H 2.875 0.02 1 494 . 92 TYR HB3 H 2.875 0.02 1 495 . 92 TYR HD1 H 7.043 0.02 1 496 . 92 TYR HD2 H 7.043 0.02 1 497 . 93 LYS N N 122.327 0.05 1 498 . 93 LYS H H 7.892 0.02 1 499 . 93 LYS HA H 4.176 0.02 1 500 . 93 LYS HB2 H 1.788 0.02 1 501 . 93 LYS HB3 H 1.788 0.02 1 502 . 93 LYS HG2 H 1.384 0.02 1 503 . 93 LYS HG3 H 1.384 0.02 1 504 . 94 ASP N N 120.656 0.05 1 505 . 94 ASP H H 8.220 0.02 1 506 . 94 ASP HA H 4.668 0.02 1 507 . 94 ASP HB2 H 2.724 0.02 2 508 . 94 ASP HB3 H 2.862 0.02 2 509 . 95 LEU N N 122.870 0.05 1 510 . 95 LEU H H 8.093 0.02 1 511 . 95 LEU HA H 4.340 0.02 1 512 . 95 LEU HB2 H 1.700 0.02 1 513 . 95 LEU HB3 H 1.700 0.02 1 514 . 96 LYS N N 121.523 0.05 1 515 . 96 LYS H H 8.318 0.02 1 516 . 96 LYS HA H 4.340 0.02 1 517 . 96 LYS HB2 H 1.889 0.02 1 518 . 96 LYS HB3 H 1.889 0.02 1 519 . 96 LYS HG2 H 1.510 0.02 1 520 . 96 LYS HG3 H 1.510 0.02 1 521 . 97 MET N N 121.960 0.05 1 522 . 97 MET H H 8.306 0.02 1 523 . 97 MET HA H 4.542 0.02 1 524 . 97 MET HB2 H 2.079 0.02 1 525 . 97 MET HB3 H 2.079 0.02 1 526 . 98 LYS N N 127.389 0.05 1 527 . 98 LYS H H 7.979 0.02 1 528 . 98 LYS HA H 4.542 0.02 1 529 . 98 LYS HB2 H 1.814 0.02 1 530 . 98 LYS HB3 H 1.814 0.02 1 stop_ save_