data_4798 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Frq1 ; _BMRB_accession_number 4798 _BMRB_flat_file_name bmr4798.str _Entry_type original _Submission_date 2000-07-31 _Accession_date 2000-07-31 _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 Ames James B. . 2 Hendricks Kristin B. . 3 Strahl Thomas . . 4 Huttner Inken G. . 5 Hamasaki Nobuko . . 6 Thorner Jeremy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 381 "13C chemical shifts" 355 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-09-03 original author . stop_ _Original_release_date 2000-09-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Calcium-binding Properties of frq1, a Novel Calcium Sensor in the Yeast Saccharomyces cerevisiae ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20471909 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ames James B. . 2 Hendricks Kristin B. . 3 Strahl Thomas . . 4 Huttner Inken G. . 5 Hamasaki Nobuko . . 6 Thorner Jeremy . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 39 _Journal_issue 40 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12149 _Page_last 12161 _Year 2000 _Details . loop_ _Keyword '1H and 15N Assigned Chemical Shifts for Frq1' 'yeast frequenin' stop_ save_ ################################## # Molecular system description # ################################## save_system_Frq1 _Saveframe_category molecular_system _Mol_system_name 'yeast frequenin' _Abbreviation_common Frq1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Frq1 $Frq1 'Ca I' $CA 'Ca II' $CA 'Ca III' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'activator of phosphatidylinositol 4-kinase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Frq1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Yeast frequenin' _Abbreviation_common Frq1 _Molecular_mass 22000 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 190 _Mol_residue_sequence ; MGAKTSKLSKDDLTCLKQST YFDRREIQQWHKGFLRDCPS GQLAREDFVKIYKQFFPFGS PEDFANHLFTVFDKDNNGFI HFEEFITVLSTTSRGTLEEK LSWAFELYDLNHDGYITFDE MLTIVASVYKMMGSMVTLNE DEATPEMRVKKIFKLMDKNE DGYITLDEFREGSKVDPSII GALNLYDGLI ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 ALA 4 LYS 5 THR 6 SER 7 LYS 8 LEU 9 SER 10 LYS 11 ASP 12 ASP 13 LEU 14 THR 15 CYS 16 LEU 17 LYS 18 GLN 19 SER 20 THR 21 TYR 22 PHE 23 ASP 24 ARG 25 ARG 26 GLU 27 ILE 28 GLN 29 GLN 30 TRP 31 HIS 32 LYS 33 GLY 34 PHE 35 LEU 36 ARG 37 ASP 38 CYS 39 PRO 40 SER 41 GLY 42 GLN 43 LEU 44 ALA 45 ARG 46 GLU 47 ASP 48 PHE 49 VAL 50 LYS 51 ILE 52 TYR 53 LYS 54 GLN 55 PHE 56 PHE 57 PRO 58 PHE 59 GLY 60 SER 61 PRO 62 GLU 63 ASP 64 PHE 65 ALA 66 ASN 67 HIS 68 LEU 69 PHE 70 THR 71 VAL 72 PHE 73 ASP 74 LYS 75 ASP 76 ASN 77 ASN 78 GLY 79 PHE 80 ILE 81 HIS 82 PHE 83 GLU 84 GLU 85 PHE 86 ILE 87 THR 88 VAL 89 LEU 90 SER 91 THR 92 THR 93 SER 94 ARG 95 GLY 96 THR 97 LEU 98 GLU 99 GLU 100 LYS 101 LEU 102 SER 103 TRP 104 ALA 105 PHE 106 GLU 107 LEU 108 TYR 109 ASP 110 LEU 111 ASN 112 HIS 113 ASP 114 GLY 115 TYR 116 ILE 117 THR 118 PHE 119 ASP 120 GLU 121 MET 122 LEU 123 THR 124 ILE 125 VAL 126 ALA 127 SER 128 VAL 129 TYR 130 LYS 131 MET 132 MET 133 GLY 134 SER 135 MET 136 VAL 137 THR 138 LEU 139 ASN 140 GLU 141 ASP 142 GLU 143 ALA 144 THR 145 PRO 146 GLU 147 MET 148 ARG 149 VAL 150 LYS 151 LYS 152 ILE 153 PHE 154 LYS 155 LEU 156 MET 157 ASP 158 LYS 159 ASN 160 GLU 161 ASP 162 GLY 163 TYR 164 ILE 165 THR 166 LEU 167 ASP 168 GLU 169 PHE 170 ARG 171 GLU 172 GLY 173 SER 174 LYS 175 VAL 176 ASP 177 PRO 178 SER 179 ILE 180 ILE 181 GLY 182 ALA 183 LEU 184 ASN 185 LEU 186 TYR 187 ASP 188 GLY 189 LEU 190 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 1FPW "Structure Of Yeast Frequenin" 100.00 190 100.00 100.00 1.27e-137 PDB 2JU0 "Structure Of Yeast Frequenin Bound To Pdtins 4-Kinase" 100.00 190 100.00 100.00 1.27e-137 DBJ GAA22591 "K7_Frq1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 190 100.00 100.00 1.27e-137 EMBL CAY78874 "Frq1p [Saccharomyces cerevisiae EC1118]" 100.00 190 100.00 100.00 1.27e-137 GB AAB64809 "Ydr373wp [Saccharomyces cerevisiae]" 100.00 190 100.00 100.00 1.27e-137 GB AHY75328 "Frq1p [Saccharomyces cerevisiae YJM993]" 100.00 190 100.00 100.00 1.27e-137 GB EDN60701 "frequenin-like protein [Saccharomyces cerevisiae YJM789]" 100.00 190 100.00 100.00 1.27e-137 GB EDV07959 "calcium-binding protein NCS-1 [Saccharomyces cerevisiae RM11-1a]" 100.00 190 100.00 100.00 1.27e-137 GB EDZ72897 "YDR373Wp-like protein [Saccharomyces cerevisiae AWRI1631]" 100.00 190 100.00 100.00 1.27e-137 REF NP_010661 "Frq1p [Saccharomyces cerevisiae S288c]" 100.00 190 100.00 100.00 1.27e-137 REF XP_011104984 "frq1p [Saccharomyces arboricola H-6]" 100.00 190 97.37 98.42 2.94e-133 SP Q06389 "RecName: Full=Calcium-binding protein NCS-1 [Saccharomyces cerevisiae S288c]" 100.00 190 100.00 100.00 1.27e-137 TPG DAA12214 "TPA: Frq1p [Saccharomyces cerevisiae S288c]" 100.00 190 100.00 100.00 1.27e-137 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 15:31:50 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Frq1 'budding 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 $Frq1 '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 $Frq1 0.8 mM '[U-95% 13C; U-90% 15N]' 'octyl glucoside' 20 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_1 save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance probe with triple axis pulsed-field gradients' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance probe with triple axis pulsed-field gradients' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance probe with triple axis pulsed-field gradients' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance probe with triple axis pulsed-field gradients' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance probe with triple axis pulsed-field gradients' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.1 n/a temperature 318 1 K 'ionic strength' 0.05 0.01 M 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 . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Frq1 _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 . 13 LEU HA H 4.37 0.04 1 2 . 13 LEU HB2 H 1.70 0.04 2 3 . 13 LEU C C 178.10 0.3 1 4 . 13 LEU CA C 55.76 0.3 1 5 . 13 LEU CB C 42.10 0.3 1 6 . 14 THR H H 8.09 0.04 1 7 . 14 THR HA H 4.57 0.04 1 8 . 14 THR HB H 4.20 0.04 1 9 . 14 THR CA C 62.41 0.3 1 10 . 14 THR CB C 69.85 0.3 1 11 . 14 THR N N 113.76 0.3 1 12 . 39 PRO HA H 4.49 0.04 1 13 . 39 PRO C C 177.39 0.3 1 14 . 39 PRO CA C 64.39 0.3 1 15 . 39 PRO CB C 32.15 0.3 1 16 . 40 SER H H 8.18 0.04 1 17 . 40 SER N N 113.39 0.3 1 18 . 41 GLY H H 8.33 0.04 1 19 . 41 GLY HA2 H 3.80 0.03 2 20 . 41 GLY C C 172.37 0.3 1 21 . 41 GLY CA C 45.75 0.3 1 22 . 41 GLY N N 110.11 0.3 1 23 . 42 GLN H H 7.68 0.3 1 24 . 42 GLN HA H 5.08 0.04 1 25 . 42 GLN C C 173.71 0.3 1 26 . 42 GLN CA C 54.34 0.3 1 27 . 42 GLN CB C 32.00 0.3 1 28 . 42 GLN N N 116.24 0.3 1 29 . 43 LEU H H 8.83 0.04 1 30 . 43 LEU HA H 4.96 0.04 1 31 . 43 LEU HB2 H 1.98 0.04 2 32 . 43 LEU HB3 H 1.72 0.04 2 33 . 43 LEU C C 175.81 0.3 1 34 . 43 LEU CA C 54.18 0.3 1 35 . 43 LEU CB C 45.52 0.3 1 36 . 43 LEU N N 123.31 0.3 1 37 . 44 ALA H H 9.53 0.04 1 38 . 44 ALA HA H 4.76 0.04 1 39 . 44 ALA HB H 1.58 0.04 1 40 . 44 ALA C C 178.49 0.3 1 41 . 44 ALA CA C 51.26 0.3 1 42 . 44 ALA CB C 20.51 0.3 1 43 . 44 ALA N N 129.76 0.3 1 44 . 45 ARG H H 7.69 0.04 1 45 . 45 ARG HA H 2.78 0.04 1 46 . 45 ARG HB2 H 1.29 0.04 2 47 . 45 ARG HB3 H 0.88 0.04 2 48 . 45 ARG C C 177.80 0.3 1 49 . 45 ARG CA C 60.86 0.3 1 50 . 45 ARG CB C 30.53 0.3 1 51 . 45 ARG N N 123.29 0.3 1 52 . 46 GLU H H 9.00 0.04 1 53 . 46 GLU HA H 3.89 0.04 1 54 . 46 GLU HB2 H 1.94 0.04 2 55 . 46 GLU C C 178.83 0.3 1 56 . 46 GLU CA C 59.87 0.3 1 57 . 46 GLU CB C 29.14 0.3 1 58 . 46 GLU N N 115.41 0.3 1 59 . 47 ASP H H 6.93 0.04 1 60 . 47 ASP HA H 4.35 0.04 1 61 . 47 ASP HB2 H 1.84 0.04 2 62 . 47 ASP HB3 H 2.91 0.04 2 63 . 47 ASP C C 177.61 0.3 1 64 . 47 ASP CA C 57.15 0.3 1 65 . 47 ASP CB C 42.05 0.3 1 66 . 47 ASP N N 117.93 0.3 1 67 . 48 PHE H H 8.24 0.04 1 68 . 48 PHE HA H 4.21 0.04 1 69 . 48 PHE HB2 H 3.14 0.04 2 70 . 48 PHE C C 176.62 0.3 1 71 . 48 PHE CA C 62.20 0.3 1 72 . 48 PHE CB C 40.11 0.3 1 73 . 48 PHE N N 120.68 0.3 1 74 . 49 VAL H H 8.38 0.04 1 75 . 49 VAL HA H 3.40 0.04 1 76 . 49 VAL HB H 2.13 0.04 1 77 . 49 VAL C C 177.18 0.3 1 78 . 49 VAL CA C 67.24 0.3 1 79 . 49 VAL CB C 31.58 0.3 1 80 . 49 VAL N N 118.22 0.3 1 81 . 50 LYS H H 7.45 0.04 1 82 . 50 LYS HA H 3.93 0.04 1 83 . 50 LYS HB2 H 1.99 0.04 2 84 . 50 LYS C C 179.24 0.3 1 85 . 50 LYS CA C 60.38 0.3 1 86 . 50 LYS CB C 32.77 0.3 1 87 . 50 LYS N N 118.06 0.3 1 88 . 51 ILE H H 7.84 0.04 1 89 . 51 ILE HA H 3.73 0.04 1 90 . 51 ILE HB H 1.85 0.04 1 91 . 51 ILE C C 177.42 0.3 1 92 . 51 ILE CA C 64.71 0.3 1 93 . 51 ILE CB C 38.42 0.3 1 94 . 51 ILE N N 119.45 0.3 1 95 . 52 TYR H H 8.36 0.04 1 96 . 52 TYR HA H 3.87 0.04 1 97 . 52 TYR HB2 H 2.99 0.04 2 98 . 52 TYR HB3 H 2.60 0.04 2 99 . 52 TYR C C 177.71 0.3 1 100 . 52 TYR CA C 63.03 0.3 1 101 . 52 TYR CB C 39.03 0.3 1 102 . 52 TYR N N 121.14 0.3 1 103 . 53 LYS H H 8.21 0.04 1 104 . 53 LYS HA H 3.94 0.04 1 105 . 53 LYS HB2 H 1.89 0.04 2 106 . 53 LYS C C 177.54 0.3 1 107 . 53 LYS CA C 59.05 0.04 1 108 . 53 LYS CB C 32.37 0.04 1 109 . 53 LYS N N 115.92 0.3 1 110 . 54 GLN H H 7.42 0.04 1 111 . 54 GLN HA H 3.89 0.04 1 112 . 54 GLN HB2 H 1.98 0.04 2 113 . 54 GLN HB3 H 1.85 0.04 2 114 . 54 GLN C C 177.24 0.3 1 115 . 54 GLN CA C 57.92 0.3 1 116 . 54 GLN CB C 28.44 0.3 1 117 . 54 GLN N N 116.51 0.3 1 118 . 55 PHE H H 7.33 0.04 1 119 . 55 PHE HA H 4.24 0.04 1 120 . 55 PHE HB2 H 2.47 0.04 2 121 . 55 PHE CA C 59.35 0.3 1 122 . 55 PHE CB C 40.27 0.3 1 123 . 55 PHE N N 116.09 0.3 1 124 . 65 ALA HA H 3.58 0.04 1 125 . 65 ALA HB H 1.29 0.04 1 126 . 65 ALA C C 179.25 0.3 1 127 . 65 ALA CA C 55.50 0.3 1 128 . 65 ALA CB C 19.08 0.3 1 129 . 66 ASN H H 8.21 0.04 1 130 . 66 ASN HA H 4.31 0.04 1 131 . 66 ASN CA C 56.51 0.3 1 132 . 66 ASN CB C 38.46 0.3 1 133 . 66 ASN N N 115.26 0.3 1 134 . 73 ASP HA H 4.69 0.04 1 135 . 73 ASP HB2 H 1.74 0.04 2 136 . 73 ASP HB3 H 2.76 0.04 2 137 . 73 ASP C C 177.67 0.3 1 138 . 73 ASP CA C 52.54 0.3 1 139 . 73 ASP CB C 39.00 0.3 1 140 . 74 LYS H H 7.78 0.041 1 141 . 74 LYS HA H 3.99 0.04 1 142 . 74 LYS HB2 H 1.84 0.04 1 143 . 74 LYS C C 177.68 0.3 1 144 . 74 LYS CA C 58.53 0.3 1 145 . 74 LYS CB C 32.71 0.3 1 146 . 74 LYS N N 126.55 0.3 1 147 . 75 ASP H H 8.13 0.04 1 148 . 75 ASP HA H 4.61 0.04 1 149 . 75 ASP HB2 H 2.59 0.04 2 150 . 75 ASP HB3 H 3.09 0.04 2 151 . 75 ASP C C 176.15 0.3 1 152 . 75 ASP CA C 52.61 0.3 1 153 . 75 ASP CB C 39.47 0.3 1 154 . 75 ASP N N 114.66 0.3 1 155 . 76 ASN H H 7.97 0.04 1 156 . 76 ASN HA H 4.37 0.04 1 157 . 76 ASN HB2 H 2.62 0.04 2 158 . 76 ASN HB3 H 3.12 0.04 2 159 . 76 ASN C C 174.78 0.3 1 160 . 76 ASN CA C 54.38 0.3 1 161 . 76 ASN CB C 38.12 0.3 1 162 . 76 ASN N N 116.22 0.3 1 163 . 77 ASN H H 8.50 0.04 1 164 . 77 ASN HA H 4.90 0.04 1 165 . 77 ASN HB2 H 2.63 0.04 2 166 . 77 ASN HB3 H 3.44 0.04 2 167 . 77 ASN C C 176.77 0.3 1 168 . 77 ASN CA C 52.45 0.3 1 169 . 77 ASN CB C 38.87 0.3 1 170 . 77 ASN N N 117.37 0.3 1 171 . 78 GLY H H 10.53 0.04 1 172 . 78 GLY HA2 H 4.11 0.04 2 173 . 78 GLY HA3 H 3.53 0.04 2 174 . 78 GLY C C 173.15 0.3 1 175 . 78 GLY CA C 45.63 0.3 1 176 . 78 GLY N N 112.50 0.3 1 177 . 79 PHE H H 7.88 0.04 1 178 . 79 PHE HA H 5.60 0.04 1 179 . 79 PHE C C 175.35 0.3 1 180 . 79 PHE CA C 56.61 0.3 1 181 . 79 PHE CB C 44.43 0.3 1 182 . 79 PHE N N 116.93 0.3 1 183 . 80 ILE H H 9.64 0.04 1 184 . 80 ILE HA H 5.43 0.04 1 185 . 80 ILE C C 175.67 0.3 1 186 . 80 ILE N N 124.73 0.3 1 187 . 82 PHE H H 8.62 0.04 1 188 . 82 PHE HA H 3.50 0.04 1 189 . 82 PHE HB2 H 2.70 0.04 2 190 . 82 PHE C C 175.83 0.3 1 191 . 82 PHE CA C 61.70 0.3 1 192 . 82 PHE CB C 39.29 0.3 1 193 . 82 PHE N N 117.23 0.3 1 194 . 84 GLU H H 8.18 0.04 1 195 . 84 GLU HA H 3.91 0.04 1 196 . 84 GLU HB2 H 2.14 0.04 2 197 . 84 GLU C C 179.12 0.3 1 198 . 84 GLU CA C 58.48 0.3 1 199 . 84 GLU CB C 30.34 0.3 1 200 . 84 GLU N N 117.8 0.3 1 201 . 85 PHE H H 8.55 0.04 1 202 . 85 PHE HA H 3.91 0.04 1 203 . 85 PHE HB2 H 2.89 0.04 2 204 . 85 PHE C C 175.50 0.3 1 205 . 85 PHE CA C 60.50 0.3 1 206 . 85 PHE CB C 38.64 0.3 1 207 . 85 PHE N N 120.41 0.3 1 208 . 87 THR HA H 3.89 0.04 1 209 . 87 THR HB H 4.36 0.04 1 210 . 87 THR C C 175.67 0.3 1 211 . 87 THR CA C 66.08 0.3 1 212 . 87 THR CB C 69.07 0.3 1 213 . 88 VAL H H 7.27 0.04 1 214 . 88 VAL HA H 3.53 0.04 1 215 . 88 VAL C C 178.58 0.3 1 216 . 88 VAL CA C 67.03 0.3 1 217 . 88 VAL CB C 31.58 0.3 1 218 . 88 VAL N N 119.34 0.3 1 219 . 89 LEU H H 7.81 0.04 1 220 . 89 LEU HA H 3.80 0.04 1 221 . 89 LEU HB2 H 1.31 0.04 2 222 . 89 LEU C C 178.9 0.3 1 223 . 89 LEU CA C 57.89 0.3 1 224 . 89 LEU CB C 41.49 0.3 1 225 . 89 LEU N N 120.13 0.3 1 226 . 90 SER H H 8.28 0.04 1 227 . 90 SER CA C 61.21 0.3 1 228 . 90 SER CB C 63.36 0.3 1 229 . 90 SER N N 113.89 0.3 1 230 . 95 GLY HA2 H 3.93 0.04 2 231 . 95 GLY HA3 H 4.27 0.04 2 232 . 95 GLY C C 174.20 0.3 1 233 . 95 GLY CA C 45.56 0.3 1 234 . 96 THR H H 8.53 0.04 1 235 . 96 THR HA H 4.16 0.04 1 236 . 96 THR HB H 4.29 0.04 1 237 . 96 THR C C 173.18 0.3 1 238 . 96 THR CA C 61.83 0.3 1 239 . 96 THR CB C 70.06 0.3 1 240 . 96 THR N N 111.77 0.3 1 241 . 97 LEU H H 7.63 0.04 1 242 . 97 LEU HA H 4.02 0.04 1 243 . 97 LEU HB2 H 1.73 0.04 2 244 . 97 LEU C C 178.48 0.3 1 245 . 97 LEU CA C 59.05 0.3 1 246 . 97 LEU CB C 41.39 0.3 1 247 . 97 LEU N N 126.82 0.3 1 248 . 98 GLU H H 8.39 0.04 1 249 . 98 GLU HA H 3.95 0.04 1 250 . 98 GLU HB2 H 1.99 0.04 2 251 . 98 GLU C C 179.49 0.3 1 252 . 98 GLU CA C 60.35 0.3 1 253 . 98 GLU CB C 29.14 0.3 1 254 . 98 GLU N N 116.36 0.3 1 255 . 99 GLU H H 7.65 0.04 1 256 . 99 GLU HA H 3.99 0.04 1 257 . 99 GLU CA C 59.34 0.3 1 258 . 99 GLU CB C 29.49 0.3 1 259 . 99 GLU N N 120.34 0.3 1 260 . 100 LYS HA H 3.96 0.04 1 261 . 100 LYS C C 178.77 0.3 1 262 . 100 LYS CA C 60.40 0.3 1 263 . 101 LEU H H 8.54 0.04 1 264 . 101 LEU HA H 4.24 0.04 1 265 . 101 LEU HB2 H 1.62 0.04 2 266 . 101 LEU HB3 H 2.04 0.04 2 267 . 101 LEU C C 178.69 0.3 1 268 . 101 LEU CA C 58.57 0.3 1 269 . 101 LEU CB C 42.47 0.3 1 270 . 101 LEU N N 119.07 0.3 1 271 . 102 SER H H 7.90 0.04 1 272 . 102 SER HA H 4.17 0.04 1 273 . 102 SER HB2 H 4.40 0.04 2 274 . 102 SER CA C 62.60 0.3 1 275 . 102 SER CB C 63.68 0.3 1 276 . 102 SER N N 114.49 0.3 1 277 . 104 ALA HA H 3.80 0.04 1 278 . 104 ALA HB H 1.79 0.04 1 279 . 104 ALA C C 177.94 0.3 1 280 . 104 ALA CA C 54.98 0.3 1 281 . 104 ALA CB C 18.60 0.3 1 282 . 105 PHE H H 8.22 0.04 1 283 . 105 PHE HA H 3.04 0.04 1 284 . 105 PHE C C 176.41 0.3 1 285 . 105 PHE CA C 62.29 0.3 1 286 . 105 PHE CB C 39.62 0.3 1 287 . 105 PHE N N 118.18 0.3 1 288 . 106 GLU H H 7.58 0.04 1 289 . 106 GLU HA H 3.94 0.04 1 290 . 106 GLU HB2 H 2.00 0.04 2 291 . 106 GLU C C 177.99 0.3 1 292 . 106 GLU CA C 58.56 0.3 1 293 . 106 GLU CB C 29.65 0.3 1 294 . 106 GLU N N 114.44 0.3 1 295 . 107 LEU H H 7.31 0.04 1 296 . 107 LEU HA H 3.69 0.04 1 297 . 107 LEU HB2 H 1.50 0.04 2 298 . 107 LEU C C 177.23 0.3 1 299 . 107 LEU CA C 57.36 0.3 1 300 . 107 LEU CB C 41.13 0.3 1 301 . 107 LEU N N 118.98 0.3 1 302 . 108 TYR H H 7.01 0.04 1 303 . 108 TYR HA H 4.17 0.04 1 304 . 108 TYR HB2 H 2.41 0.04 2 305 . 108 TYR HB3 H 2.70 0.04 2 306 . 108 TYR C C 175.29 0.3 1 307 . 108 TYR CA C 59.78 0.3 1 308 . 108 TYR CB C 40.12 0.32 1 309 . 108 TYR N N 113.42 0.3 1 310 . 109 ASP H H 7.23 0.04 1 311 . 109 ASP HA H 4.41 0.04 1 312 . 109 ASP HB2 H 1.63 0.04 2 313 . 109 ASP C C 177.45 0.3 1 314 . 109 ASP CA C 51.94 0.3 1 315 . 109 ASP CB C 38.37 0.3 1 316 . 109 ASP N N 114.63 0.3 1 317 . 110 LEU H H 7.30 0.04 1 318 . 110 LEU HA H 4.40 0.04 1 319 . 110 LEU HB2 H 1.66 0.04 2 320 . 110 LEU HB3 H 1.39 0.04 2 321 . 110 LEU C C 177.66 0.3 1 322 . 110 LEU CA C 57.91 0.3 1 323 . 110 LEU CB C 42.50 0.3 1 324 . 110 LEU N N 123.22 0.3 1 325 . 111 ASN H H 7.79 0.04 1 326 . 111 ASN HA H 4.64 0.04 1 327 . 111 ASN HB2 H 2.76 0.04 2 328 . 111 ASN HB3 H 3.30 0.04 2 329 . 111 ASN C C 175.49 0.3 1 330 . 111 ASN CA C 51.22 0.3 1 331 . 111 ASN CB C 37.51 0.3 1 332 . 111 ASN N N 111.47 0.3 1 333 . 112 HIS H H 7.81 0.041 1 334 . 112 HIS HA H 4.27 0.04 1 335 . 112 HIS HB2 H 3.31 0.04 2 336 . 112 HIS HB3 H 3.37 0.04 2 337 . 112 HIS C C 174.26 0.3 1 338 . 112 HIS CA C 56.72 0.3 1 339 . 112 HIS CB C 26.66 0.3 1 340 . 112 HIS N N 116.12 0.3 1 341 . 113 ASP H H 8.30 0.04 1 342 . 113 ASP HA H 4.65 0.04 1 343 . 113 ASP HB2 H 2.41 0.04 2 344 . 113 ASP HB3 H 3.12 0.04 2 345 . 113 ASP C C 177.23 0.3 1 346 . 113 ASP CA C 52.97 0.3 1 347 . 113 ASP CB C 41.18 0.3 1 348 . 113 ASP N N 118.49 0.3 1 349 . 114 GLY H H 10.53 0.04 1 350 . 114 GLY HA2 H 4.08 0.04 2 351 . 114 GLY HA3 H 3.47 0.04 2 352 . 114 GLY C C 172.56 0.3 1 353 . 114 GLY CA C 45.12 0.3 1 354 . 114 GLY N N 112.67 0.3 1 355 . 115 TYR H H 8.07 0.04 1 356 . 115 TYR HA H 5.25 0.04 1 357 . 115 TYR HB2 H 2.63 0.04 2 358 . 115 TYR C C 175.49 0.3 1 359 . 115 TYR CA C 55.31 0.3 1 360 . 115 TYR CB C 41.97 0.3 1 361 . 115 TYR N N 117.59 0.3 1 362 . 116 ILE H H 9.64 0.04 1 363 . 116 ILE HA H 4.96 0.04 1 364 . 116 ILE HB H 1.69 0.04 1 365 . 116 ILE C C 177.37 0.3 1 366 . 116 ILE CA C 61.50 0.3 1 367 . 116 ILE CB C 40.06 0.3 1 368 . 116 ILE N N 126.17 0.3 1 369 . 117 THR H H 8.87 0.04 1 370 . 117 THR HA H 5.22 0.04 1 371 . 117 THR HB H 4.82 0.04 1 372 . 117 THR C C 175.98 0.3 1 373 . 117 THR CA C 60.28 0.3 1 374 . 117 THR CB C 71.47 0.3 1 375 . 117 THR N N 117.83 0.3 1 376 . 118 PHE H H 9.17 0.04 1 377 . 118 PHE HA H 3.49 0.04 1 378 . 118 PHE HB2 H 2.28 0.04 2 379 . 118 PHE HB3 H 2.78 0.04 2 380 . 118 PHE C C 176.58 0.3 1 381 . 118 PHE CA C 62.30 0.3 1 382 . 118 PHE CB C 39.29 0.3 1 383 . 118 PHE N N 123.85 0.3 1 384 . 119 ASP H H 8.43 0.04 1 385 . 119 ASP HA H 4.27 0.04 1 386 . 119 ASP HB2 H 2.61 0.04 2 387 . 119 ASP C C 179.42 0.3 1 388 . 119 ASP CA C 57.27 0.3 1 389 . 119 ASP CB C 40.72 0.3 1 390 . 119 ASP N N 114.89 0.3 1 391 . 120 GLU H H 7.62 0.04 1 392 . 120 GLU HA H 3.96 0.04 1 393 . 120 GLU C C 177.46 0.3 1 394 . 120 GLU CA C 59.91 0.3 1 395 . 120 GLU CB C 29.22 0.3 1 396 . 120 GLU N N 121.90 0.3 1 397 . 121 MET H H 7.94 0.04 1 398 . 121 MET HA H 4.15 0.04 1 399 . 121 MET C C 178.35 0.3 1 400 . 121 MET CA C 59.63 0.3 1 401 . 121 MET CB C 32.85 0.3 1 402 . 121 MET N N 116.72 0.3 1 403 . 122 LEU H H 8.89 0.04 1 404 . 122 LEU HA H 3.81 0.04 1 405 . 122 LEU HB2 H 1.79 0.04 2 406 . 122 LEU HB3 H 1.06 0.04 2 407 . 122 LEU C C 177.47 0.3 1 408 . 122 LEU CA C 58.13 0.3 1 409 . 122 LEU CB C 41.49 0.3 1 410 . 122 LEU N N 118.86 0.3 1 411 . 123 THR H H 7.81 0.04 1 412 . 123 THR HA H 3.83 0.04 1 413 . 123 THR HB H 4.43 0.04 1 414 . 123 THR C C 176.81 0.3 1 415 . 123 THR CA C 67.80 0.3 1 416 . 123 THR CB C 68.85 0.3 1 417 . 123 THR N N 115.48 0.3 1 418 . 124 ILE H H 7.37 0.04 1 419 . 124 ILE HA H 3.86 0.04 1 420 . 124 ILE HB H 2.30 0.04 1 421 . 124 ILE C C 178.01 0.3 1 422 . 124 ILE CA C 63.47 0.3 1 423 . 124 ILE CB C 36.23 0.3 1 424 . 124 ILE N N 120.39 0.3 1 425 . 125 VAL H H 8.84 0.04 1 426 . 125 VAL HA H 3.58 0.04 1 427 . 125 VAL HB H 1.86 0.04 1 428 . 125 VAL C C 178.06 0.3 1 429 . 125 VAL CA C 67.87 0.3 1 430 . 125 VAL CB C 31.65 0.3 1 431 . 125 VAL N N 120.53 0.3 1 432 . 126 ALA H H 9.42 0.04 1 433 . 126 ALA HA H 3.95 0.04 1 434 . 126 ALA HB H 1.49 0.04 1 435 . 126 ALA C C 180.52 0.3 1 436 . 126 ALA CA C 55.92 0.3 1 437 . 126 ALA CB C 17.88 0.3 1 438 . 126 ALA N N 120.70 0.3 1 439 . 127 SER H H 7.52 0.04 1 440 . 127 SER HB2 H 4.43 0.04 2 441 . 127 SER C C 175.57 0.3 1 442 . 127 SER CB C 63.06 0.3 1 443 . 127 SER N N 114.69 0.3 1 444 . 128 VAL H H 8.25 0.04 1 445 . 128 VAL HA H 3.68 0.04 1 446 . 128 VAL HB H 2.36 0.04 1 447 . 128 VAL C C 178.03 0.3 1 448 . 128 VAL CA C 66.79 0.3 1 449 . 128 VAL CB C 31.60 0.3 1 450 . 128 VAL N N 117.91 0.3 1 451 . 129 TYR H H 8.78 0.04 1 452 . 129 TYR HA H 4.17 0.04 1 453 . 129 TYR HB2 H 3.05 0.04 2 454 . 129 TYR C C 176.14 0.3 1 455 . 129 TYR CA C 62.11 0.3 1 456 . 129 TYR CB C 37.71 0.3 1 457 . 129 TYR N N 121.50 0.3 1 458 . 130 LYS H H 7.90 0.04 1 459 . 130 LYS HA H 3.94 0.04 1 460 . 130 LYS HB2 H 2.06 0.04 2 461 . 130 LYS C C 178.78 0.3 1 462 . 130 LYS CA C 59.17 0.3 1 463 . 130 LYS CB C 32.77 0.3 1 464 . 130 LYS N N 118.43 0.3 1 465 . 131 MET H H 7.80 0.04 1 466 . 131 MET HA H 4.26 0.04 1 467 . 131 MET HB2 H 2.01 0.04 2 468 . 131 MET CA C 56.71 0.3 1 469 . 131 MET CB C 32.43 0.3 1 470 . 131 MET N N 118.60 0.3 1 471 . 132 MET HA H 4.36 0.04 1 472 . 132 MET HB2 H 2.03 0.04 2 473 . 132 MET C C 177.49 0.3 1 474 . 132 MET CA C 56.81 0.3 1 475 . 132 MET CB C 33.23 0.3 1 476 . 133 GLY H H 7.83 0.04 1 477 . 133 GLY HA2 H 4.06 0.04 2 478 . 133 GLY HA3 H 3.93 0.04 2 479 . 133 GLY CA C 46.58 0.3 1 480 . 133 GLY N N 106.63 0.3 1 481 . 134 SER HA H 3.96 0.04 1 482 . 134 SER HB2 H 4.46 0.04 2 483 . 134 SER C C 175.03 0.3 1 484 . 134 SER CA C 59.22 0.3 1 485 . 134 SER CB C 63.53 0.3 1 486 . 135 MET H H 8.15 0.04 1 487 . 135 MET HA H 4.45 0.04 1 488 . 135 MET HB2 H 2.11 0.04 2 489 . 135 MET C C 175.84 0.3 1 490 . 135 MET CA C 56.60 0.3 1 491 . 135 MET CB C 33.40 0.3 1 492 . 135 MET N N 120.15 0.3 1 493 . 136 VAL H H 7.44 0.04 1 494 . 136 VAL HA H 4.29 0.04 1 495 . 136 VAL HB H 2.00 0.04 1 496 . 136 VAL C C 175.13 0.3 1 497 . 136 VAL CA C 61.25 0.3 1 498 . 136 VAL CB C 33.64 0.3 1 499 . 136 VAL N N 115.77 0.3 1 500 . 137 THR H H 8.04 0.04 1 501 . 137 THR HA H 4.13 0.04 1 502 . 137 THR HB H 4.31 0.04 1 503 . 137 THR C C 174.00 0.3 1 504 . 137 THR CA C 62.02 0.3 1 505 . 137 THR CB C 69.57 0.3 1 506 . 137 THR N N 118.04 0.3 1 507 . 138 LEU H H 8.17 0.04 1 508 . 138 LEU HA H 4.42 0.04 1 509 . 138 LEU HB2 H 1.54 0.04 2 510 . 138 LEU HB3 H 1.62 0.04 2 511 . 138 LEU C C 177.00 0.3 1 512 . 138 LEU CA C 54.40 0.3 1 513 . 138 LEU CB C 43.09 0.3 1 514 . 138 LEU N N 126.01 0.3 1 515 . 139 ASN H H 8.55 0.04 1 516 . 139 ASN HA H 4.69 0.04 1 517 . 139 ASN HB2 H 2.70 0.04 2 518 . 139 ASN HB3 H 2.87 0.04 2 519 . 139 ASN C C 176.47 0.3 1 520 . 139 ASN CA C 53.09 0.3 1 521 . 139 ASN CB C 39.12 0.3 1 522 . 139 ASN N N 120.13 0.3 1 523 . 140 GLU H H 8.68 0.04 1 524 . 140 GLU HA H 4.10 0.04 1 525 . 140 GLU HB2 H 2.06 0.04 2 526 . 140 GLU C C 176.93 0.3 1 527 . 140 GLU CA C 59.11 0.3 1 528 . 140 GLU CB C 29.79 0.3 1 529 . 140 GLU N N 121.83 0.3 1 530 . 141 ASP H H 8.23 0.04 1 531 . 141 ASP HA H 4.58 0.04 1 532 . 141 ASP HB2 H 2.69 0.04 2 533 . 141 ASP HB3 H 2.85 0.04 2 534 . 141 ASP C C 175.77 0.3 1 535 . 141 ASP CA C 54.51 0.3 1 536 . 141 ASP CB C 40.14 0.3 1 537 . 141 ASP N N 116.99 0.3 1 538 . 142 GLU H H 7.84 0.04 1 539 . 142 GLU HA H 4.36 0.04 1 540 . 142 GLU HB2 H 1.93 0.04 2 541 . 142 GLU C C 176.37 0.3 1 542 . 142 GLU CA C 54.99 0.3 1 543 . 142 GLU CB C 30.35 0.3 1 544 . 142 GLU N N 117.56 0.3 1 545 . 143 ALA H H 7.56 0.04 1 546 . 143 ALA HA H 4.23 0.04 1 547 . 143 ALA HB H 1.54 0.04 1 548 . 143 ALA C C 177.08 0.3 1 549 . 143 ALA CA C 54.77 0.3 1 550 . 143 ALA CB C 19.77 0.3 1 551 . 143 ALA N N 123.12 0.3 1 552 . 144 THR H H 7.33 0.04 1 553 . 144 THR HA H 4.82 0.04 1 554 . 144 THR N N 106.54 0.3 1 555 . 145 PRO HA H 3.51 0.04 1 556 . 145 PRO HB2 H 1.77 0.04 2 557 . 145 PRO HB3 H 1.57 0.04 2 558 . 145 PRO C C 177.25 0.3 1 559 . 145 PRO CA C 65.30 0.3 1 560 . 145 PRO CB C 31.38 0.3 1 561 . 146 GLU H H 8.89 0.04 1 562 . 146 GLU HA H 3.77 0.04 1 563 . 146 GLU HB2 H 2.12 0.04 2 564 . 146 GLU HB3 H 2.00 0.04 2 565 . 146 GLU C C 178.36 0.3 1 566 . 146 GLU CA C 61.13 0.3 1 567 . 146 GLU CB C 29.12 0.3 1 568 . 146 GLU N N 116.89 0.3 1 569 . 147 MET H H 7.59 0.04 1 570 . 147 MET HA H 4.11 0.04 1 571 . 147 MET HB2 H 2.27 0.04 2 572 . 147 MET C C 179.13 0.3 1 573 . 147 MET CA C 59.08 0.3 1 574 . 147 MET CB C 33.16 0.3 1 575 . 147 MET N N 118.15 0.3 1 576 . 148 ARG H H 7.89 0.04 1 577 . 148 ARG HA H 4.06 0.04 1 578 . 148 ARG HB2 H 2.05 0.04 2 579 . 148 ARG C C 177.99 0.3 1 580 . 148 ARG CA C 58.95 0.3 1 581 . 148 ARG CB C 29.72 0.3 1 582 . 148 ARG N N 119.85 0.3 1 583 . 149 VAL H H 8.42 0.04 1 584 . 149 VAL HA H 3.59 0.04 1 585 . 149 VAL HB H 1.78 0.04 1 586 . 149 VAL C C 177.78 0.3 1 587 . 149 VAL CA C 67.31 0.3 1 588 . 149 VAL CB C 30.95 0.3 1 589 . 149 VAL N N 118.54 0.3 1 590 . 150 LYS H H 8.46 0.04 1 591 . 150 LYS HA H 4.01 0.04 1 592 . 150 LYS HB2 H 2.01 0.04 2 593 . 150 LYS HB3 H 2.05 0.04 2 594 . 150 LYS C C 179.17 0.3 1 595 . 150 LYS CA C 61.01 0.3 1 596 . 150 LYS CB C 32.70 0.3 1 597 . 150 LYS N N 120.45 0.3 1 598 . 151 LYS H H 7.71 0.04 1 599 . 151 LYS HA H 4.08 0.04 1 600 . 151 LYS HB2 H 2.08 0.04 2 601 . 151 LYS C C 178.82 0.3 1 602 . 151 LYS CA C 59.83 0.3 1 603 . 151 LYS CB C 32.65 0.3 1 604 . 151 LYS N N 119.69 0.3 1 605 . 152 ILE H H 8.10 0.04 1 606 . 152 ILE HA H 3.67 0.04 1 607 . 152 ILE HB H 2.08 0.04 1 608 . 152 ILE C C 178.05 0.3 1 609 . 152 ILE CA C 65.28 0.3 1 610 . 152 ILE CB C 37.75 0.3 1 611 . 152 ILE N N 120.35 0.3 1 612 . 153 PHE H H 9.11 0.04 1 613 . 153 PHE HA H 3.75 0.04 1 614 . 153 PHE HB2 H 3.18 0.04 2 615 . 153 PHE HB3 H 3.39 0.04 2 616 . 153 PHE C C 178.45 0.3 1 617 . 153 PHE CA C 63.49 0.3 1 618 . 153 PHE CB C 38.91 0.3 1 619 . 153 PHE N N 121.27 0.3 1 620 . 154 LYS H H 8.08 0.04 1 621 . 154 LYS HA H 4.15 0.04 1 622 . 154 LYS HB2 H 2.02 0.04 2 623 . 154 LYS C C 178.60 0.3 1 624 . 154 LYS CA C 58.74 0.3 1 625 . 154 LYS CB C 31.95 0.3 1 626 . 154 LYS N N 118.74 0.3 1 627 . 155 LEU H H 7.47 0.04 1 628 . 155 LEU HA H 4.20 0.04 1 629 . 155 LEU HB2 H 1.77 0.04 2 630 . 155 LEU C C 178.33 0.04 1 631 . 155 LEU CA C 57.34 0.04 1 632 . 155 LEU CB C 42.93 0.04 1 633 . 155 LEU N N 117.39 0.3 1 634 . 156 MET H H 8.26 0.04 1 635 . 156 MET HA H 4.35 0.04 1 636 . 156 MET HB2 H 1.77 0.04 2 637 . 156 MET C C 177.66 0.3 1 638 . 156 MET CA C 57.99 0.3 1 639 . 156 MET CB C 35.18 0.3 1 640 . 156 MET N N 113.08 0.3 1 641 . 157 ASP H H 8.57 0.04 1 642 . 157 ASP HA H 4.78 0.04 1 643 . 157 ASP HB2 H 2.16 0.04 2 644 . 157 ASP HB3 H 3.17 0.04 2 645 . 157 ASP C C 178.04 0.3 2 646 . 157 ASP CA C 53.19 0.3 1 647 . 157 ASP CB C 38.87 0.3 1 648 . 157 ASP N N 118.46 0.3 1 649 . 158 LYS H H 7.87 0.04 1 650 . 158 LYS HA H 4.07 0.04 1 651 . 158 LYS HB2 H 1.94 0.04 2 652 . 158 LYS C C 177.45 0.3 1 653 . 158 LYS CA C 58.75 0.3 1 654 . 158 LYS CB C 32.86 0.3 1 655 . 158 LYS N N 127.26 0.3 1 656 . 159 ASN H H 7.91 0.04 1 657 . 159 ASN HA H 4.84 0.04 1 658 . 159 ASN HB2 H 2.85 0.04 2 659 . 159 ASN HB3 H 3.31 0.04 2 660 . 159 ASN C C 174.27 0.3 1 661 . 159 ASN CA C 51.80 0.3 1 662 . 159 ASN CB C 36.89 0.3 1 663 . 159 ASN N N 112.99 0.3 1 664 . 160 GLU H H 7.72 0.04 1 665 . 160 GLU HA H 3.85 0.04 1 666 . 160 GLU HB2 H 2.07 0.04 2 667 . 160 GLU HB3 H 2.25 0.04 2 668 . 160 GLU C C 175.38 0.3 1 669 . 160 GLU CA C 57.93 0.3 1 670 . 160 GLU CB C 27.85 0.3 1 671 . 160 GLU N N 115.66 0.3 1 672 . 161 ASP H H 8.31 0.04 1 673 . 161 ASP HA H 4.64 0.04 1 674 . 161 ASP HB2 H 2.48 0.04 2 675 . 161 ASP HB3 H 3.11 0.04 2 676 . 161 ASP C C 177.26 0.04 1 677 . 161 ASP CA C 53.17 0.04 1 678 . 161 ASP CB C 40.99 0.04 1 679 . 161 ASP N N 117.38 0.3 1 680 . 162 GLY H H 10.33 0.04 1 681 . 162 GLY HA2 H 4.02 0.04 2 682 . 162 GLY HA3 H 3.50 0.04 2 683 . 162 GLY C C 172.70 0.3 1 684 . 162 GLY CA C 45.26 0.3 1 685 . 162 GLY N N 112.15 0.3 1 686 . 163 TYR H H 8.15 0.04 1 687 . 163 TYR HA H 5.41 0.04 1 688 . 163 TYR HB2 H 2.73 0.04 2 689 . 163 TYR HB3 H 2.87 0.04 2 690 . 163 TYR C C 175.87 0.3 1 691 . 163 TYR CA C 55.31 0.3 1 692 . 163 TYR CB C 41.97 0.3 1 693 . 163 TYR N N 117.94 0.3 1 694 . 164 ILE H H 9.64 0.04 1 695 . 164 ILE HA H 5.26 0.04 1 696 . 164 ILE HB H 1.79 0.04 1 697 . 164 ILE C C 177.15 0.3 1 698 . 164 ILE CA C 60.60 0.3 1 699 . 164 ILE CB C 39.58 0.3 1 700 . 164 ILE N N 125.77 0.3 1 701 . 165 THR H H 8.70 0.04 1 702 . 165 THR HA H 4.96 0.04 1 703 . 165 THR HB H 4.77 0.04 1 704 . 165 THR C C 175.97 0.3 1 705 . 165 THR CA C 60.42 0.3 1 706 . 165 THR CB C 71.46 0.3 1 707 . 165 THR N N 118.41 0.3 1 708 . 166 LEU H H 8.89 0.04 1 709 . 166 LEU HA H 3.45 0.04 1 710 . 166 LEU HB2 H 1.64 0.04 2 711 . 166 LEU HB3 H 1.40 0.04 2 712 . 166 LEU C C 178.34 0.3 1 713 . 166 LEU CA C 55.35 0.3 1 714 . 166 LEU CB C 42.64 0.3 1 715 . 166 LEU N N 124.13 0.3 1 716 . 167 ASP H H 8.22 0.04 1 717 . 167 ASP HA H 4.35 0.04 1 718 . 167 ASP HB2 H 2.57 0.04 2 719 . 167 ASP HB3 H 2.68 0.04 2 720 . 167 ASP C C 179.31 0.3 1 721 . 167 ASP CA C 57.82 0.3 1 722 . 167 ASP CB C 40.30 0.3 1 723 . 167 ASP N N 116.71 0.3 1 724 . 168 GLU H H 7.57 0.04 1 725 . 168 GLU HA H 4.15 0.04 1 726 . 168 GLU HB2 H 2.48 0.04 2 727 . 168 GLU C C 179.79 0.3 1 728 . 168 GLU CA C 59.12 0.3 1 729 . 168 GLU CB C 30.20 0.3 1 730 . 168 GLU N N 120.39 0.3 1 731 . 169 PHE H H 9.06 0.04 1 732 . 169 PHE HA H 4.51 0.04 1 733 . 169 PHE HB2 H 3.31 0.04 2 734 . 169 PHE C C 178.06 0.3 1 735 . 169 PHE CA C 60.74 0.3 1 736 . 169 PHE CB C 40.78 0.3 1 737 . 169 PHE N N 124.09 0.3 1 738 . 170 ARG H H 9.05 0.04 1 739 . 170 ARG HA H 3.91 0.04 1 740 . 170 ARG C C 177.05 0.3 1 741 . 170 ARG CA C 60.24 0.3 1 742 . 170 ARG CB C 30.38 0.3 1 743 . 170 ARG N N 119.95 0.3 1 744 . 171 GLU H H 7.75 0.04 1 745 . 171 GLU HA H 4.08 0.04 1 746 . 171 GLU HB2 H 1.90 0.04 2 747 . 171 GLU HB3 H 2.09 0.04 2 748 . 171 GLU C C 179.76 0.3 1 749 . 171 GLU CA C 59.17 0.3 1 750 . 171 GLU CB C 29.64 0.3 1 751 . 171 GLU N N 117.48 0.3 1 752 . 172 GLY H H 8.44 0.04 1 753 . 172 GLY HA2 H 3.96 0.04 2 754 . 172 GLY HA3 H 3.68 0.04 2 755 . 172 GLY C C 175.32 0.3 1 756 . 172 GLY CA C 47.03 0.3 1 757 . 172 GLY N N 106.27 0.3 1 758 . 173 SER H H 7.89 0.04 1 759 . 173 SER HA H 3.94 0.04 1 760 . 173 SER HB2 H 4.40 0.04 2 761 . 173 SER C C 174.28 0.3 1 762 . 173 SER CA C 61.60 0.3 1 763 . 173 SER CB C 63.43 0.3 1 764 . 173 SER N N 116.70 0.3 1 765 . 174 LYS H H 7.08 0.04 1 766 . 174 LYS HA H 4.07 0.04 1 767 . 174 LYS HB2 H 1.89 0.04 2 768 . 174 LYS C C 177.70 0.3 1 769 . 174 LYS CA C 58.09 0.3 1 770 . 174 LYS CB C 32.78 0.3 1 771 . 174 LYS N N 118.10 0.3 1 772 . 175 VAL H H 7.18 0.04 1 773 . 175 VAL HA H 4.00 0.04 1 774 . 175 VAL HB H 2.20 0.04 1 775 . 175 VAL C C 176.04 0.3 1 776 . 175 VAL CA C 63.84 0.3 1 777 . 175 VAL CB C 32.30 0.3 1 778 . 175 VAL N N 116.43 0.3 1 779 . 176 ASP H H 7.55 0.04 1 780 . 176 ASP HA H 5.04 0.04 1 781 . 176 ASP HB2 H 2.39 0.04 2 782 . 176 ASP HB3 H 2.82 0.04 2 783 . 176 ASP CA C 51.11 0.3 1 784 . 176 ASP CB C 41.52 0.3 1 785 . 176 ASP N N 116.97 0.3 1 786 . 177 PRO HA H 4.57 0.04 1 787 . 177 PRO HB2 H 2.01 0.04 2 788 . 177 PRO HB3 H 2.37 0.04 2 789 . 177 PRO C C 178.39 0.3 1 790 . 177 PRO CA C 64.00 0.3 1 791 . 177 PRO CB C 32.14 0.3 1 792 . 178 SER H H 8.35 0.04 1 793 . 178 SER HA H 3.94 0.04 1 794 . 178 SER HB2 H 4.22 0.4 2 795 . 178 SER C C 176.46 0.3 1 796 . 178 SER CA C 61.63 0.3 1 797 . 178 SER CB C 63.35 0.3 1 798 . 178 SER N N 116.33 0.3 1 799 . 179 ILE H H 7.49 0.04 1 800 . 179 ILE HA H 4.00 0.04 1 801 . 179 ILE CA C 62.89 0.3 1 802 . 179 ILE CB C 37.89 0.3 1 803 . 179 ILE N N 121.41 0.3 1 804 . 180 ILE HA H 4.57 0.04 1 805 . 180 ILE HB H 2.68 0.04 1 806 . 180 ILE C C 177.03 0.3 1 807 . 180 ILE CA C 61.76 0.3 1 808 . 180 ILE CB C 37.89 0.3 1 809 . 181 GLY H H 7.96 0.04 1 810 . 181 GLY HA2 H 3.94 0.04 2 811 . 181 GLY C C 174.91 0.3 1 812 . 181 GLY CA C 46.95 0.3 1 813 . 181 GLY N N 108.44 0.3 1 814 . 182 ALA H H 7.81 0.04 1 815 . 182 ALA HA H 4.22 0.04 1 816 . 182 ALA HB H 1.43 0.04 1 817 . 182 ALA C C 177.32 0.3 1 818 . 182 ALA CA C 53.67 0.3 1 819 . 182 ALA CB C 18.89 0.3 1 820 . 182 ALA N N 121.99 0.3 1 821 . 183 LEU H H 7.66 0.04 1 822 . 183 LEU HA H 4.28 0.04 1 823 . 183 LEU C C 175.83 0.3 1 824 . 183 LEU CA C 56.42 0.3 1 825 . 183 LEU CB C 42.63 0.3 1 826 . 183 LEU N N 115.54 0.3 1 827 . 186 TYR HA H 4.51 0.04 1 828 . 186 TYR HB2 H 2.68 0.04 2 829 . 186 TYR C C 175.83 0.3 1 830 . 186 TYR CA C 58.66 0.3 1 831 . 186 TYR CB C 38.63 0.3 1 832 . 187 ASP H H 7.88 0.04 1 833 . 187 ASP HA H 4.50 0.04 1 834 . 187 ASP HB2 H 2.67 0.04 2 835 . 187 ASP C C 176.93 0.3 1 836 . 187 ASP CA C 55.46 0.3 1 837 . 187 ASP CB C 41.32 0.3 1 838 . 187 ASP N N 120.38 0.3 1 839 . 188 GLY H H 7.92 0.04 1 840 . 188 GLY HA2 H 3.91 0.04 2 841 . 188 GLY C C 174.32 0.3 1 842 . 188 GLY CA C 45.82 0.3 1 843 . 188 GLY N N 108.08 0.3 1 844 . 189 LEU H H 7.82 0.04 1 845 . 189 LEU HA H 4.34 0.04 1 846 . 189 LEU HB2 H 1.67 0.04 2 847 . 189 LEU C C 175.92 0.3 1 848 . 189 LEU CA C 55.31 0.3 1 849 . 189 LEU CB C 42.56 0.3 1 850 . 189 LEU N N 120.45 0.3 1 stop_ save_