data_4129 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Resonance Assignment of the Calcium-bound Form of the Nereis Diversicolor Sarcoplasmic Calcium(2+)-binding Protein. ; _BMRB_accession_number 4129 _BMRB_flat_file_name bmr4129.str _Entry_type original _Submission_date 1998-03-31 _Accession_date 1998-03-31 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; We report the proton and nitrogen-15 resonance assignments for the natural and recombinant Nereis diversicolor Sarcoplasmic Calcium-binding Protein (NSCP). It is a high-affinity calcium binding protein of 174 residues. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Craescu Constantin T. . 2 Precheur Benedicte . . 3 'van Riel' Annick . . 4 Sakamoto Hiroshi . . 5 Engelborghs Yves . . 6 Cox Jos A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 863 "15N chemical shifts" 179 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 update BMRB 'updating non-standard residue' 2008-03-24 update BMRB . 2000-04-03 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H and 15N Resonance Assignment of the Calcium-bound Form of the Nereis Diversicolor Sarcoplasmic Calcium(2+)-binding Protein. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99079125 _PubMed_ID 9862132 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Craescu Constantin T. . 2 Precheur Benedicte . . 3 'van Riel' Annick . . 4 Sakamoto Hiroshi . . 5 Engelborghs Yves . . 6 Cox Jos A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 12 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 565 _Page_last 566 _Year 1998 _Details . loop_ _Keyword 'calcium-bound form' 'NMR, nuclear magnetic resonance' 'NSCP, Nereis sarcoplasmic calcium-binding protein' protein 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_NSCP _Saveframe_category molecular_system _Mol_system_name 'Nereis diversicolor sarcoplasmic calcium-binding protein' _Abbreviation_common NSCP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NSCP $NSCP 'NSCP acetylated' $NSCP_acetylated Ca $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Calcium binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NSCP_acetylated _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'calcium-binding protein' _Name_variant 'Nereis diversicolor sarcoplasmic calcium-binding protein' _Abbreviation_common NSCP _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 174 _Mol_residue_sequence ; XDLWVQKMKTYFNRIDFDKD GAITRMDFESMAERFAKESE MKAEHAKVLMDSLTGVWDNF LTAVAGGKGIDETTFINSMK EMVKNPEAKSVVEGPLPLFF RAVDTNEDNNISRDEYGIFF GMLGLDKTMAPASFDAIDTN NDGLLSLEEFVIAGSDFFMN DGDSTNKVFWGPLV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 SAC 2 2 ASP 3 3 LEU 4 4 TRP 5 5 VAL 6 6 GLN 7 7 LYS 8 8 MET 9 9 LYS 10 10 THR 11 11 TYR 12 12 PHE 13 13 ASN 14 14 ARG 15 15 ILE 16 16 ASP 17 17 PHE 18 18 ASP 19 19 LYS 20 20 ASP 21 21 GLY 22 22 ALA 23 23 ILE 24 24 THR 25 25 ARG 26 26 MET 27 27 ASP 28 28 PHE 29 29 GLU 30 30 SER 31 31 MET 32 32 ALA 33 33 GLU 34 34 ARG 35 35 PHE 36 36 ALA 37 37 LYS 38 38 GLU 39 39 SER 40 40 GLU 41 41 MET 42 42 LYS 43 43 ALA 44 44 GLU 45 45 HIS 46 46 ALA 47 47 LYS 48 48 VAL 49 49 LEU 50 50 MET 51 51 ASP 52 52 SER 53 53 LEU 54 54 THR 55 55 GLY 56 56 VAL 57 57 TRP 58 58 ASP 59 59 ASN 60 60 PHE 61 61 LEU 62 62 THR 63 63 ALA 64 64 VAL 65 65 ALA 66 66 GLY 67 67 GLY 68 68 LYS 69 69 GLY 70 70 ILE 71 71 ASP 72 72 GLU 73 73 THR 74 74 THR 75 75 PHE 76 76 ILE 77 77 ASN 78 78 SER 79 79 MET 80 80 LYS 81 81 GLU 82 82 MET 83 83 VAL 84 84 LYS 85 85 ASN 86 86 PRO 87 87 GLU 88 88 ALA 89 89 LYS 90 90 SER 91 91 VAL 92 92 VAL 93 93 GLU 94 94 GLY 95 95 PRO 96 96 LEU 97 97 PRO 98 98 LEU 99 99 PHE 100 100 PHE 101 101 ARG 102 102 ALA 103 103 VAL 104 104 ASP 105 105 THR 106 106 ASN 107 107 GLU 108 108 ASP 109 109 ASN 110 110 ASN 111 111 ILE 112 112 SER 113 113 ARG 114 114 ASP 115 115 GLU 116 116 TYR 117 117 GLY 118 118 ILE 119 119 PHE 120 120 PHE 121 121 GLY 122 122 MET 123 123 LEU 124 124 GLY 125 125 LEU 126 126 ASP 127 127 LYS 128 128 THR 129 129 MET 130 130 ALA 131 131 PRO 132 132 ALA 133 133 SER 134 134 PHE 135 135 ASP 136 136 ALA 137 137 ILE 138 138 ASP 139 139 THR 140 140 ASN 141 141 ASN 142 142 ASP 143 143 GLY 144 144 LEU 145 145 LEU 146 146 SER 147 147 LEU 148 148 GLU 149 149 GLU 150 150 PHE 151 151 VAL 152 152 ILE 153 153 ALA 154 154 GLY 155 155 SER 156 156 ASP 157 157 PHE 158 158 PHE 159 159 MET 160 160 ASN 161 161 ASP 162 162 GLY 163 163 ASP 164 164 SER 165 165 THR 166 166 ASN 167 167 LYS 168 168 VAL 169 169 PHE 170 170 TRP 171 171 GLY 172 172 PRO 173 173 LEU 174 174 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1Q80 "Solution Structure And Dynamics Of Nereis Sarcoplasmic Calcium Binding Protein" 99.43 174 100.00 100.00 1.63e-120 PDB 2SCP "Structure Of A Sarcoplasmic Calcium-Binding Protein From Nereis Diversicolor Refined At 2.0 Angstroms Resolution" 99.43 174 100.00 100.00 1.63e-120 SP P04571 "RecName: Full=Sarcoplasmic calcium-binding protein; Short=SCP" 99.43 174 100.00 100.00 1.63e-120 stop_ save_ save_NSCP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'calcium-binding protein' _Name_variant 'Nereis diversicolor sarcoplasmic calcium-binding protein' _Abbreviation_common NSCP _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 174 _Mol_residue_sequence ; SDLWVQKMKTYFNRIDFDKD GAITRMDFESMAERFAKESE MKAEHAKVLMDSLTGVWDNF LTAVAGGKGIDETTFINSMK EMVKNPEAKSVVEGPLPLFF RAVDTNEDNNISRDEYGIFF GMLGLDKTMAPASFDAIDTN NDGLLSLEEFVIAGSDFFMN DGDSTNKVFWGPLV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 SER 2 2 ASP 3 3 LEU 4 4 TRP 5 5 VAL 6 6 GLN 7 7 LYS 8 8 MET 9 9 LYS 10 10 THR 11 11 TYR 12 12 PHE 13 13 ASN 14 14 ARG 15 15 ILE 16 16 ASP 17 17 PHE 18 18 ASP 19 19 LYS 20 20 ASP 21 21 GLY 22 22 ALA 23 23 ILE 24 24 THR 25 25 ARG 26 26 MET 27 27 ASP 28 28 PHE 29 29 GLU 30 30 SER 31 31 MET 32 32 ALA 33 33 GLU 34 34 ARG 35 35 PHE 36 36 ALA 37 37 LYS 38 38 GLU 39 39 SER 40 40 GLU 41 41 MET 42 42 LYS 43 43 ALA 44 44 GLU 45 45 HIS 46 46 ALA 47 47 LYS 48 48 VAL 49 49 LEU 50 50 MET 51 51 ASP 52 52 SER 53 53 LEU 54 54 THR 55 55 GLY 56 56 VAL 57 57 TRP 58 58 ASP 59 59 ASN 60 60 PHE 61 61 LEU 62 62 THR 63 63 ALA 64 64 VAL 65 65 ALA 66 66 GLY 67 67 GLY 68 68 LYS 69 69 GLY 70 70 ILE 71 71 ASP 72 72 GLU 73 73 THR 74 74 THR 75 75 PHE 76 76 ILE 77 77 ASN 78 78 SER 79 79 MET 80 80 LYS 81 81 GLU 82 82 MET 83 83 VAL 84 84 LYS 85 85 ASN 86 86 PRO 87 87 GLU 88 88 ALA 89 89 LYS 90 90 SER 91 91 VAL 92 92 VAL 93 93 GLU 94 94 GLY 95 95 PRO 96 96 LEU 97 97 PRO 98 98 LEU 99 99 PHE 100 100 PHE 101 101 ARG 102 102 ALA 103 103 VAL 104 104 ASP 105 105 THR 106 106 ASN 107 107 GLU 108 108 ASP 109 109 ASN 110 110 ASN 111 111 ILE 112 112 SER 113 113 ARG 114 114 ASP 115 115 GLU 116 116 TYR 117 117 GLY 118 118 ILE 119 119 PHE 120 120 PHE 121 121 GLY 122 122 MET 123 123 LEU 124 124 GLY 125 125 LEU 126 126 ASP 127 127 LYS 128 128 THR 129 129 MET 130 130 ALA 131 131 PRO 132 132 ALA 133 133 SER 134 134 PHE 135 135 ASP 136 136 ALA 137 137 ILE 138 138 ASP 139 139 THR 140 140 ASN 141 141 ASN 142 142 ASP 143 143 GLY 144 144 LEU 145 145 LEU 146 146 SER 147 147 LEU 148 148 GLU 149 149 GLU 150 150 PHE 151 151 VAL 152 152 ILE 153 153 ALA 154 154 GLY 155 155 SER 156 156 ASP 157 157 PHE 158 158 PHE 159 159 MET 160 160 ASN 161 161 ASP 162 162 GLY 163 163 ASP 164 164 SER 165 165 THR 166 166 ASN 167 167 LYS 168 168 VAL 169 169 PHE 170 170 TRP 171 171 GLY 172 172 PRO 173 173 LEU 174 174 VAL stop_ _Sequence_homology_query_date 2007-10-08 _Sequence_homology_query_revised_last_date 2007-05-31 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 2SCP 'A Chain A, Sarcoplasmic Calcium-Binding Protein' 100.00 174 100 100 2e-96 SWISS-PROT P04571 'SCP_NERDI Sarcoplasmic calcium-binding protein(SCP)' 100.00 174 100 100 2e-96 BMRB 4129 'calcium-binding protein' 100.00 174 100 100 5e-96 PDB 1Q80 'A Chain A, Solution Structure And Dynamics OfNereis Sarcoplasmic Calcium Binding Protein' 100.00 174 100 100 2e-96 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SAC _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-ACETYL-SERINE _BMRB_code . _PDB_code SAC _Standard_residue_derivative . _Molecular_mass 147.129 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 13:12:29 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1A C1A C . 0 . ? C2A C2A C . 0 . ? OAC OAC O . 0 . ? N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? OG OG O . 0 . ? H2A1 H2A1 H . 0 . ? H2A2 H2A2 H . 0 . ? H2A3 H2A3 H . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG HG H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1A C2A ? ? DOUB C1A OAC ? ? SING C1A N ? ? SING C2A H2A1 ? ? SING C2A H2A2 ? ? SING C2A H2A3 ? ? SING N CA ? ? SING N H ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG HG ? ? 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 $NSCP sandworm 6352 Eukaryota Metazoa Neanthes diversicolor 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 $NSCP 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)/pDIA17/pHSP234 pET22b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details 'recombinant sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NSCP 1.0 mM [U-15N] H2O 93 % . D2O 7 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details 'natural protein sample where it is acetylated' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NSCP_acetylated 1.2 mM . H2O 93 % . D2O 7 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.68 internal direct . . . $entry_citation $entry_citation 'liquid ammonia' N 15 nitrogen ppm 0.0 external direct . . . $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_one _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame corresponds to the recombinant protein. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name NSCP _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 ASP H H 8.77 0.01 1 2 . 2 ASP HA H 4.42 0.01 1 3 . 2 ASP HB2 H 2.73 0.01 2 4 . 2 ASP HB3 H 2.67 0.01 2 5 . 2 ASP N N 118.9 0.1 1 6 . 3 LEU H H 8.29 0.01 1 7 . 3 LEU HA H 4.30 0.01 1 8 . 3 LEU HB2 H 1.61 0.01 2 9 . 3 LEU HG H 1.73 0.01 1 10 . 3 LEU HD1 H 0.93 0.01 2 11 . 3 LEU HD2 H 0.85 0.01 2 12 . 3 LEU N N 120.3 0.1 1 13 . 4 TRP H H 8.45 0.01 1 14 . 4 TRP HA H 3.72 0.01 1 15 . 4 TRP HB2 H 3.79 0.01 1 16 . 4 TRP HB3 H 3.31 0.01 1 17 . 4 TRP HD1 H 7.03 0.01 1 18 . 4 TRP HE1 H 10.52 0.01 1 19 . 4 TRP HE3 H 7.54 0.01 1 20 . 4 TRP HZ2 H 7.30 0.01 1 21 . 4 TRP HZ3 H 6.86 0.01 1 22 . 4 TRP HH2 H 7.18 0.01 1 23 . 4 TRP N N 120.5 0.1 1 24 . 4 TRP NE1 N 128.5 0.1 1 25 . 5 VAL H H 8.39 0.01 1 26 . 5 VAL HA H 3.18 0.01 1 27 . 5 VAL HB H 2.32 0.01 1 28 . 5 VAL HG1 H 1.01 0.01 1 29 . 5 VAL HG2 H 1.35 0.01 1 30 . 5 VAL N N 117.5 0.1 1 31 . 6 GLN H H 8.16 0.01 1 32 . 6 GLN HA H 4.00 0.01 1 33 . 6 GLN HB2 H 2.46 0.01 2 34 . 6 GLN HB3 H 2.24 0.01 2 35 . 6 GLN HG2 H 2.61 0.01 2 36 . 6 GLN HE21 H 7.96 0.01 2 37 . 6 GLN HE22 H 6.48 0.01 2 38 . 6 GLN N N 118.6 0.1 1 39 . 6 GLN NE2 N 110.2 0.1 1 40 . 7 LYS H H 8.90 0.01 1 41 . 7 LYS HA H 3.91 0.01 1 42 . 7 LYS HB2 H 1.87 0.01 2 43 . 7 LYS HB3 H 1.78 0.01 2 44 . 7 LYS N N 121.4 0.1 1 45 . 8 MET H H 8.31 0.01 1 46 . 8 MET HA H 4.77 0.01 1 47 . 8 MET HB2 H 2.14 0.01 2 48 . 8 MET N N 119.2 0.1 1 49 . 9 LYS H H 8.83 0.01 1 50 . 9 LYS HA H 3.88 0.01 1 51 . 9 LYS HB2 H 1.81 0.01 2 52 . 9 LYS HG2 H 1.64 0.01 2 53 . 9 LYS N N 117.2 0.1 1 54 . 10 THR H H 8.20 0.01 1 55 . 10 THR HA H 5.22 0.01 1 56 . 10 THR HB H 4.88 0.01 1 57 . 10 THR HG2 H 1.33 0.01 1 58 . 10 THR N N 117.7 0.1 1 59 . 11 TYR H H 8.37 0.01 1 60 . 11 TYR HA H 3.62 0.01 1 61 . 11 TYR HB2 H 3.12 0.01 2 62 . 11 TYR HB3 H 3.07 0.01 2 63 . 11 TYR HD1 H 5.91 0.01 1 64 . 11 TYR HD2 H 5.91 0.01 1 65 . 11 TYR HE1 H 6.27 0.01 1 66 . 11 TYR HE2 H 6.27 0.01 1 67 . 11 TYR N N 119.9 0.1 1 68 . 12 PHE H H 8.46 0.01 1 69 . 12 PHE HA H 3.87 0.01 1 70 . 12 PHE HB2 H 3.14 0.01 1 71 . 12 PHE HB3 H 2.77 0.01 1 72 . 12 PHE HD1 H 6.72 0.01 1 73 . 12 PHE HD2 H 6.72 0.01 1 74 . 12 PHE HE1 H 7.10 0.01 1 75 . 12 PHE HE2 H 7.10 0.01 1 76 . 12 PHE HZ H 7.29 0.01 1 77 . 12 PHE N N 115.2 0.1 1 78 . 13 ASN H H 7.68 0.01 1 79 . 13 ASN HA H 4.18 0.01 1 80 . 13 ASN HB2 H 2.84 0.01 1 81 . 13 ASN HB3 H 2.98 0.01 1 82 . 13 ASN HD21 H 8.07 0.01 2 83 . 13 ASN HD22 H 7.09 0.01 2 84 . 13 ASN N N 111.5 0.1 1 85 . 13 ASN ND2 N 111.3 0.1 1 86 . 14 ARG H H 7.74 0.01 1 87 . 14 ARG HA H 3.99 0.01 1 88 . 14 ARG HB2 H 1.94 0.01 1 89 . 14 ARG HB3 H 1.83 0.01 1 90 . 14 ARG HG2 H 1.53 0.01 1 91 . 14 ARG HG3 H 1.53 0.01 1 92 . 14 ARG HD2 H 3.15 0.01 1 93 . 14 ARG HD3 H 3.15 0.01 1 94 . 14 ARG HE H 7.23 0.01 1 95 . 14 ARG N N 113.3 0.1 1 96 . 14 ARG NE N 115.5 0.1 1 97 . 15 ILE H H 7.16 0.01 1 98 . 15 ILE HA H 3.86 0.01 1 99 . 15 ILE HB H 1.50 0.01 1 100 . 15 ILE HG12 H 1.15 0.01 2 101 . 15 ILE HG13 H 0.81 0.01 2 102 . 15 ILE HG2 H 0.46 0.01 1 103 . 15 ILE HD1 H 0.40 0.01 1 104 . 15 ILE N N 108.5 0.1 1 105 . 16 ASP H H 7.16 0.01 1 106 . 16 ASP HA H 4.43 0.01 1 107 . 16 ASP HB2 H 2.41 0.01 2 108 . 16 ASP HB3 H 1.58 0.01 2 109 . 16 ASP N N 118.2 0.1 1 110 . 17 PHE H H 8.01 0.01 1 111 . 17 PHE HA H 3.91 0.01 1 112 . 17 PHE HB2 H 2.88 0.01 2 113 . 17 PHE HD1 H 7.14 0.01 1 114 . 17 PHE HD2 H 7.14 0.01 1 115 . 17 PHE HE1 H 7.34 0.01 1 116 . 17 PHE HE2 H 7.34 0.01 1 117 . 17 PHE N N 126.9 0.1 1 118 . 18 ASP H H 8.54 0.01 1 119 . 18 ASP HA H 4.27 0.01 1 120 . 18 ASP HB2 H 2.91 0.01 2 121 . 18 ASP HB3 H 2.47 0.01 2 122 . 18 ASP N N 112.7 0.1 1 123 . 19 LYS H H 7.58 0.01 1 124 . 19 LYS HA H 3.91 0.01 1 125 . 19 LYS HB2 H 1.97 0.01 2 126 . 19 LYS HB3 H 1.86 0.01 2 127 . 19 LYS HG2 H 1.53 0.01 2 128 . 19 LYS HD2 H 1.74 0.01 2 129 . 19 LYS N N 112.0 0.1 1 130 . 20 ASP H H 8.31 0.01 1 131 . 20 ASP HA H 4.46 0.01 1 132 . 20 ASP HB2 H 2.98 0.01 2 133 . 20 ASP HB3 H 2.38 0.01 2 134 . 20 ASP N N 117.4 0.1 1 135 . 21 GLY H H 10.27 0.01 1 136 . 21 GLY HA2 H 4.29 0.01 1 137 . 21 GLY HA3 H 3.68 0.01 1 138 . 21 GLY N N 111.5 0.1 1 139 . 22 ALA H H 8.21 0.01 1 140 . 22 ALA HA H 5.20 0.01 1 141 . 22 ALA HB H 1.05 0.01 1 142 . 22 ALA N N 121.4 0.1 1 143 . 23 ILE H H 9.60 0.01 1 144 . 23 ILE HA H 4.68 0.01 1 145 . 23 ILE HB H 2.04 0.01 1 146 . 23 ILE HG12 H 0.90 0.01 2 147 . 23 ILE HG13 H 0.70 0.01 2 148 . 23 ILE HG2 H 1.23 0.01 1 149 . 23 ILE HD1 H -0.02 0.01 1 150 . 23 ILE N N 124.7 0.1 1 151 . 24 THR H H 9.35 0.01 1 152 . 24 THR HA H 3.95 0.01 1 153 . 24 THR HB H 4.04 0.01 1 154 . 24 THR HG2 H 1.03 0.01 1 155 . 24 THR N N 116.9 0.1 1 156 . 25 ARG H H 7.23 0.01 1 157 . 25 ARG HA H 3.20 0.01 1 158 . 25 ARG HB2 H 1.18 0.01 1 159 . 25 ARG HB3 H 0.22 0.01 1 160 . 25 ARG HG2 H 2.05 0.01 2 161 . 25 ARG HD2 H 2.93 0.01 2 162 . 25 ARG HD3 H 3.22 0.01 2 163 . 25 ARG HE H 9.63 0.01 1 164 . 25 ARG NE N 115.8 0.01 1 165 . 25 ARG N N 118.2 0.1 1 166 . 26 MET H H 7.54 0.01 1 167 . 26 MET HA H 4.05 0.01 1 168 . 26 MET HB2 H 2.02 0.01 2 169 . 26 MET HB3 H 1.95 0.01 2 170 . 26 MET HG2 H 2.59 0.01 2 171 . 26 MET HG3 H 2.52 0.01 2 172 . 26 MET N N 112.4 0.1 1 173 . 27 ASP H H 7.46 0.01 1 174 . 27 ASP HA H 4.31 0.01 1 175 . 27 ASP HB2 H 2.82 0.01 2 176 . 27 ASP HB3 H 2.67 0.01 2 177 . 27 ASP N N 118.6 0.1 1 178 . 28 PHE H H 6.87 0.01 1 179 . 28 PHE HA H 4.07 0.01 1 180 . 28 PHE HB2 H 2.95 0.01 2 181 . 28 PHE HB3 H 2.81 0.01 2 182 . 28 PHE HD1 H 7.44 0.01 1 183 . 28 PHE HD2 H 7.44 0.01 1 184 . 28 PHE HE1 H 7.35 0.01 1 185 . 28 PHE HE2 H 7.35 0.01 1 186 . 28 PHE N N 114.9 0.1 1 187 . 29 GLU H H 8.20 0.01 1 188 . 29 GLU HA H 3.85 0.01 1 189 . 29 GLU HB2 H 2.16 0.01 2 190 . 29 GLU HB3 H 2.05 0.01 2 191 . 29 GLU HG2 H 2.35 0.01 1 192 . 29 GLU HG3 H 2.35 0.01 1 193 . 29 GLU N N 117.7 0.1 1 194 . 30 SER H H 8.45 0.01 1 195 . 30 SER HA H 4.20 0.01 1 196 . 30 SER HB2 H 3.99 0.01 2 197 . 30 SER HB3 H 3.91 0.01 2 198 . 30 SER N N 112.5 0.1 1 199 . 31 MET H H 7.75 0.01 1 200 . 31 MET HA H 2.87 0.01 1 201 . 31 MET HB2 H 1.78 0.01 2 202 . 31 MET HB3 H 2.08 0.01 2 203 . 31 MET N N 122.3 0.1 1 204 . 32 ALA H H 8.03 0.01 1 205 . 32 ALA HA H 3.92 0.01 1 206 . 32 ALA HB H 1.62 0.01 1 207 . 32 ALA N N 118.2 0.1 1 208 . 33 GLU H H 8.00 0.01 1 209 . 33 GLU HA H 3.99 0.01 1 210 . 33 GLU HB2 H 2.13 0.01 1 211 . 33 GLU HB3 H 2.13 0.01 1 212 . 33 GLU HG2 H 2.22 0.01 1 213 . 33 GLU HG3 H 2.22 0.01 1 214 . 33 GLU N N 116.6 0.1 1 215 . 34 ARG H H 8.11 0.01 1 216 . 34 ARG HA H 4.13 0.01 1 217 . 34 ARG HB2 H 2.05 0.01 2 218 . 34 ARG N N 117.6 0.1 1 219 . 35 PHE H H 8.59 0.01 1 220 . 35 PHE HA H 4.41 0.01 1 221 . 35 PHE HB2 H 3.42 0.01 2 222 . 35 PHE HB3 H 3.28 0.01 2 223 . 35 PHE HD1 H 7.34 0.01 1 224 . 35 PHE HD2 H 7.34 0.01 1 225 . 35 PHE HE1 H 7.23 0.01 1 226 . 35 PHE HE2 H 7.23 0.01 1 227 . 35 PHE N N 119.2 0.1 1 228 . 36 ALA H H 8.07 0.01 1 229 . 36 ALA HA H 4.17 0.01 1 230 . 36 ALA HB H 1.55 0.01 1 231 . 36 ALA N N 116.8 0.1 1 232 . 37 LYS H H 7.64 0.01 1 233 . 37 LYS HA H 4.32 0.01 1 234 . 37 LYS HB2 H 2.02 0.01 1 235 . 37 LYS HB3 H 2.02 0.01 1 236 . 37 LYS HG2 H 1.55 0.01 1 237 . 37 LYS HG3 H 1.55 0.01 1 238 . 37 LYS HD2 H 1.70 0.01 2 239 . 37 LYS N N 114.2 0.1 1 240 . 38 GLU H H 8.03 0.01 1 241 . 38 GLU HA H 4.32 0.01 1 242 . 38 GLU HB2 H 2.00 0.01 1 243 . 38 GLU HB3 H 2.24 0.01 1 244 . 38 GLU HG2 H 2.38 0.01 1 245 . 38 GLU HG3 H 2.38 0.01 1 246 . 38 GLU N N 116.2 0.1 1 247 . 39 SER H H 7.74 0.01 1 248 . 39 SER HA H 4.54 0.01 1 249 . 39 SER HB2 H 3.85 0.01 2 250 . 39 SER HB3 H 3.78 0.01 2 251 . 39 SER N N 111.2 0.1 1 252 . 40 GLU H H 8.25 0.01 1 253 . 40 GLU HA H 4.29 0.01 1 254 . 40 GLU HB2 H 2.00 0.01 2 255 . 40 GLU HB3 H 2.24 0.01 2 256 . 40 GLU N N 120.1 0.1 1 257 . 41 MET H H 8.32 0.01 1 258 . 41 MET HA H 4.49 0.01 1 259 . 41 MET HG2 H 2.47 0.01 2 260 . 41 MET HE H 2.02 0.01 1 261 . 41 MET N N 116.9 0.1 1 262 . 42 LYS H H 8.46 0.01 1 263 . 42 LYS HA H 4.35 0.01 1 264 . 42 LYS N N 120.7 0.1 1 265 . 43 ALA H H 8.83 0.01 1 266 . 43 ALA HA H 4.10 0.01 1 267 . 43 ALA HB H 1.50 0.01 1 268 . 43 ALA N N 125.5 0.1 1 269 . 44 GLU H H 9.46 0.01 1 270 . 44 GLU HA H 4.16 0.01 1 271 . 44 GLU HB2 H 2.14 0.01 2 272 . 44 GLU HB3 H 2.08 0.01 2 273 . 44 GLU HG2 H 2.45 0.01 2 274 . 44 GLU HG3 H 2.35 0.01 2 275 . 44 GLU N N 115.2 0.1 1 276 . 45 HIS H H 8.06 0.01 1 277 . 45 HIS HA H 4.47 0.01 1 278 . 45 HIS HB2 H 3.35 0.01 2 279 . 45 HIS HB3 H 3.22 0.01 2 280 . 45 HIS HD2 H 7.23 0.01 1 281 . 45 HIS HE1 H 8.50 0.01 1 282 . 45 HIS N N 116.3 0.1 1 283 . 46 ALA H H 8.10 0.01 1 284 . 46 ALA HA H 3.98 0.01 1 285 . 46 ALA HB H 1.51 0.01 1 286 . 46 ALA N N 120.4 0.1 1 287 . 47 LYS H H 7.67 0.01 1 288 . 47 LYS HA H 4.07 0.01 1 289 . 47 LYS HB2 H 1.86 0.01 2 290 . 47 LYS HG2 H 1.48 0.01 2 291 . 47 LYS N N 116.7 0.1 1 292 . 48 VAL H H 6.86 0.01 1 293 . 48 VAL HA H 3.70 0.01 1 294 . 48 VAL HB H 1.69 0.01 1 295 . 48 VAL HG1 H 1.06 0.01 1 296 . 48 VAL HG2 H 0.70 0.01 1 297 . 48 VAL N N 117.9 0.1 1 298 . 49 LEU H H 8.33 0.01 1 299 . 49 LEU HA H 3.64 0.01 1 300 . 49 LEU HB2 H 1.61 0.01 2 301 . 49 LEU HG H 1.53 0.01 1 302 . 49 LEU HD1 H 0.75 0.01 1 303 . 49 LEU HD2 H 0.85 0.01 1 304 . 49 LEU N N 121.4 0.1 1 305 . 50 MET H H 7.79 0.01 1 306 . 50 MET HA H 4.19 0.01 1 307 . 50 MET HB2 H 2.23 0.01 2 308 . 50 MET HG2 H 2.73 0.01 2 309 . 50 MET N N 116.5 0.1 1 310 . 51 ASP H H 8.89 0.01 1 311 . 51 ASP HA H 4.15 0.01 1 312 . 51 ASP HB2 H 2.72 0.01 2 313 . 51 ASP HB3 H 2.58 0.01 2 314 . 51 ASP N N 120.1 0.1 1 315 . 52 SER H H 8.35 0.01 1 316 . 52 SER HA H 4.18 0.01 1 317 . 52 SER HB2 H 3.88 0.01 2 318 . 52 SER N N 114.5 0.1 1 319 . 53 LEU H H 8.01 0.01 1 320 . 53 LEU HA H 4.14 0.01 1 321 . 53 LEU HB2 H 2.05 0.01 2 322 . 53 LEU HB3 H 1.61 0.01 2 323 . 53 LEU HG H 1.89 0.01 1 324 . 53 LEU HD1 H 0.91 0.01 2 325 . 53 LEU HD2 H 0.77 0.01 2 326 . 53 LEU N N 115.4 0.1 1 327 . 54 THR H H 8.28 0.01 1 328 . 54 THR HA H 3.94 0.01 1 329 . 54 THR HB H 4.20 0.01 1 330 . 54 THR HG2 H 1.36 0.01 1 331 . 54 THR N N 104.6 0.1 1 332 . 55 GLY H H 7.64 0.01 1 333 . 55 GLY HA2 H 3.86 0.01 2 334 . 55 GLY HA3 H 3.81 0.01 2 335 . 55 GLY N N 109.6 0.1 1 336 . 56 VAL H H 7.38 0.01 1 337 . 56 VAL HA H 3.50 0.01 1 338 . 56 VAL HB H 1.67 0.01 1 339 . 56 VAL HG1 H 0.88 0.01 1 340 . 56 VAL HG2 H 0.76 0.01 1 341 . 56 VAL N N 121.6 0.1 1 342 . 57 TRP H H 6.47 0.01 1 343 . 57 TRP HA H 4.08 0.01 1 344 . 57 TRP HB2 H 3.42 0.01 2 345 . 57 TRP HB3 H 3.06 0.01 2 346 . 57 TRP HD1 H 7.82 0.01 1 347 . 57 TRP HE1 H 10.30 0.1 1 348 . 57 TRP HE3 H 7.36 0.01 1 349 . 57 TRP HZ2 H 7.34 0.01 1 350 . 57 TRP HZ3 H 6.92 0.01 1 351 . 57 TRP HH2 H 7.45 0.01 1 352 . 57 TRP N N 115.3 0.1 1 353 . 57 TRP NE1 N 129.2 0.1 1 354 . 58 ASP H H 8.96 0.01 1 355 . 58 ASP HA H 4.10 0.01 1 356 . 58 ASP HB2 H 2.71 0.01 1 357 . 58 ASP HB3 H 2.40 0.01 1 358 . 58 ASP N N 114.6 0.1 1 359 . 59 ASN H H 8.29 0.01 1 360 . 59 ASN HA H 4.46 0.01 1 361 . 59 ASN HB2 H 2.27 0.01 1 362 . 59 ASN HB3 H 1.75 0.01 1 363 . 59 ASN HD21 H 6.99 0.01 2 364 . 59 ASN HD22 H 6.64 0.01 2 365 . 59 ASN N N 109.7 0.1 1 366 . 59 ASN ND2 N 109.5 0.1 1 367 . 60 PHE H H 6.54 0.01 1 368 . 60 PHE HA H 4.82 0.01 1 369 . 60 PHE HB2 H 3.30 0.01 1 370 . 60 PHE HB3 H 3.30 0.01 1 371 . 60 PHE HD1 H 7.29 0.01 1 372 . 60 PHE HD2 H 7.29 0.01 1 373 . 60 PHE HE1 H 7.13 0.01 1 374 . 60 PHE HE2 H 7.13 0.01 1 375 . 60 PHE N N 112.0 0.1 1 376 . 61 LEU H H 8.19 0.01 1 377 . 61 LEU HA H 4.10 0.01 1 378 . 61 LEU HB2 H 1.81 0.01 2 379 . 61 LEU HD1 H 1.07 0.01 1 380 . 61 LEU HD2 H 1.07 0.01 1 381 . 61 LEU N N 118.6 0.1 1 382 . 62 THR H H 7.99 0.01 1 383 . 62 THR HA H 3.09 0.01 1 384 . 62 THR HB H 3.27 0.01 1 385 . 62 THR HG2 H 0.86 0.01 1 386 . 62 THR N N 113.2 0.1 1 387 . 63 ALA H H 7.06 0.01 1 388 . 63 ALA HA H 4.21 0.01 1 389 . 63 ALA HB H 1.39 0.01 1 390 . 63 ALA N N 117.9 0.1 1 391 . 64 VAL H H 7.43 0.01 1 392 . 64 VAL HA H 3.64 0.01 1 393 . 64 VAL HB H 2.16 0.01 1 394 . 64 VAL HG1 H 1.02 0.01 1 395 . 64 VAL HG2 H 1.08 0.01 1 396 . 64 VAL N N 116.7 0.1 1 397 . 65 ALA H H 7.83 0.01 1 398 . 65 ALA HA H 4.84 0.01 1 399 . 65 ALA HB H 1.35 0.01 1 400 . 65 ALA N N 118.3 0.01 1 401 . 66 GLY H H 7.59 0.01 1 402 . 66 GLY HA2 H 3.97 0.01 2 403 . 66 GLY HA3 H 3.86 0.01 2 404 . 66 GLY N N 107.8 0.01 1 405 . 67 GLY H H 8.67 0.01 1 406 . 67 GLY HA2 H 4.45 0.01 2 407 . 67 GLY HA3 H 3.97 0.01 2 408 . 67 GLY N N 106.6 0.1 1 409 . 68 LYS H H 7.35 0.01 1 410 . 68 LYS HA H 4.57 0.01 1 411 . 68 LYS HB2 H 2.08 0.01 4 412 . 68 LYS HG2 H 1.81 0.01 4 413 . 68 LYS HG3 H 1.61 0.01 4 414 . 68 LYS N N 118.8 0.1 1 415 . 69 GLY H H 8.29 0.01 1 416 . 69 GLY HA2 H 4.60 0.01 2 417 . 69 GLY HA3 H 3.58 0.01 2 418 . 69 GLY N N 103.1 0.1 1 419 . 70 ILE H H 9.26 0.01 1 420 . 70 ILE HA H 4.37 0.01 1 421 . 70 ILE HB H 2.19 0.01 1 422 . 70 ILE HG2 H 1.41 0.01 1 423 . 70 ILE N N 122.0 001 1 424 . 71 ASP H H 8.50 0.01 1 425 . 71 ASP HA H 5.32 0.01 1 426 . 71 ASP HB2 H 2.86 0.01 1 427 . 71 ASP HB3 H 3.24 0.01 1 428 . 71 ASP N N 124.3 0.1 1 429 . 72 GLU H H 8.54 0.01 1 430 . 72 GLU HA H 3.91 0.01 1 431 . 72 GLU HB2 H 3.02 0.01 2 432 . 72 GLU HB3 H 2.74 0.01 2 433 . 72 GLU N N 120.1 0.1 1 434 . 73 THR H H 8.04 0.01 1 435 . 73 THR HA H 3.83 0.01 1 436 . 73 THR HB H 4.13 0.01 1 437 . 73 THR HG2 H 1.23 0.01 1 438 . 73 THR N N 112.8 0.1 1 439 . 74 THR H H 8.37 0.01 1 440 . 74 THR HA H 3.91 0.01 1 441 . 74 THR HB H 4.27 0.01 1 442 . 74 THR HG2 H 1.27 0.01 1 443 . 74 THR N N 118.6 0.1 1 444 . 75 PHE H H 8.87 0.01 1 445 . 75 PHE HA H 3.97 0.01 1 446 . 75 PHE HB2 H 3.47 0.01 2 447 . 75 PHE HB3 H 3.37 0.01 2 448 . 75 PHE HD1 H 7.18 0.01 1 449 . 75 PHE HD2 H 7.18 0.01 1 450 . 75 PHE HE1 H 7.61 0.01 1 451 . 75 PHE HE2 H 7.61 0.01 1 452 . 75 PHE HZ H 7.58 0.01 1 453 . 75 PHE N N 121.6 0.1 1 454 . 76 ILE H H 8.65 0.01 1 455 . 76 ILE HA H 3.27 0.01 1 456 . 76 ILE HB H 1.98 0.01 1 457 . 76 ILE HG12 H 1.70 0.01 2 458 . 76 ILE HG2 H 0.88 0.01 1 459 . 76 ILE HD1 H 1.14 0.01 1 460 . 76 ILE N N 117.7 0.1 1 461 . 77 ASN H H 8.46 0.01 1 462 . 77 ASN HA H 4.49 0.01 1 463 . 77 ASN HB2 H 2.97 0.01 2 464 . 77 ASN HB3 H 2.86 0.01 2 465 . 77 ASN HD21 H 7.62 0.01 2 466 . 77 ASN HD22 H 6.92 0.01 2 467 . 77 ASN N N 115.9 0.1 1 468 . 77 ASN ND2 N 110.1 0.1 1 469 . 78 SER H H 8.39 0.01 1 470 . 78 SER HA H 4.35 0.01 1 471 . 78 SER HB2 H 3.97 0.01 1 472 . 78 SER HB3 H 3.97 0.01 1 473 . 78 SER N N 114.7 0.1 1 474 . 79 MET H H 8.34 0.01 1 475 . 79 MET HA H 4.51 0.01 1 476 . 79 MET HB2 H 2.16 0.01 1 477 . 79 MET HB3 H 2.00 0.01 1 478 . 79 MET N N 119.2 0.1 1 479 . 80 LYS H H 8.00 0.01 1 480 . 80 LYS HA H 3.72 0.01 1 481 . 80 LYS HB2 H 1.88 0.01 2 482 . 80 LYS HG2 H 1.54 0.01 2 483 . 80 LYS HD2 H 1.67 0.01 2 484 . 80 LYS N N 118.5 0.1 1 485 . 81 GLU H H 7.13 0.01 1 486 . 81 GLU HA H 4.08 0.01 1 487 . 81 GLU HB2 H 2.16 0.01 2 488 . 81 GLU HG2 H 2.41 0.01 2 489 . 81 GLU HG3 H 2.35 0.01 2 490 . 81 GLU N N 113.8 0.1 1 491 . 82 MET H H 8.00 0.01 1 492 . 82 MET HA H 4.10 0.01 1 493 . 82 MET HB2 H 2.22 0.01 2 494 . 82 MET HG2 H 2.79 0.01 2 495 . 82 MET N N 116.7 0.1 1 496 . 83 VAL H H 8.37 0.01 1 497 . 83 VAL HA H 3.90 0.01 1 498 . 83 VAL HB H 2.45 0.01 1 499 . 83 VAL HG1 H 1.28 0.01 1 500 . 83 VAL HG2 H 0.97 0.01 1 501 . 83 VAL N N 109.3 0.1 1 502 . 84 LYS H H 6.95 0.01 1 503 . 84 LYS HA H 4.29 0.01 1 504 . 84 LYS HB2 H 1.88 0.01 2 505 . 84 LYS HB3 H 1.78 0.01 2 506 . 84 LYS HG2 H 1.42 0.01 2 507 . 84 LYS N N 114.9 0.1 1 508 . 85 ASN H H 7.40 0.01 1 509 . 85 ASN HA H 5.16 0.01 1 510 . 85 ASN HB2 H 3.22 0.01 2 511 . 85 ASN HB3 H 2.83 0.01 2 512 . 85 ASN HD21 H 7.82 0.01 2 513 . 85 ASN HD22 H 7.14 0.01 2 514 . 85 ASN N N 117.7 0.1 1 515 . 85 ASN ND2 N 110.4 0.1 1 516 . 86 PRO HG2 H 2.13 0.01 2 517 . 86 PRO HG3 H 2.08 0.01 2 518 . 86 PRO HD2 H 4.13 0.01 2 519 . 86 PRO HD3 H 4.00 0.01 2 520 . 87 GLU H H 7.97 0.01 1 521 . 87 GLU HA H 4.27 0.01 1 522 . 87 GLU HB2 H 2.19 0.01 2 523 . 87 GLU HB3 H 1.96 0.01 2 524 . 87 GLU HG2 H 2.38 0.01 2 525 . 87 GLU HG3 H 2.29 0.01 2 526 . 87 GLU N N 113.4 0.1 1 527 . 88 ALA H H 8.00 0.01 1 528 . 88 ALA HA H 4.52 0.01 1 529 . 88 ALA HB H 1.65 0.01 1 530 . 88 ALA N N 119.8 0.1 1 531 . 89 LYS H H 7.36 0.01 1 532 . 89 LYS HA H 3.85 0.01 1 533 . 89 LYS HB2 H 1.91 0.01 2 534 . 89 LYS HB3 H 1.81 0.01 2 535 . 89 LYS HG2 H 1.37 0.01 2 536 . 89 LYS HD2 H 1.68 0.01 2 537 . 89 LYS N N 120.2 0.1 1 538 . 90 SER H H 8.32 0.01 1 539 . 90 SER HA H 4.18 0.01 1 540 . 90 SER HB2 H 3.92 0.01 2 541 . 90 SER HB3 H 3.90 0.01 2 542 . 90 SER N N 109.3 0.1 1 543 . 91 VAL H H 7.44 0.01 1 544 . 91 VAL HA H 3.94 0.01 1 545 . 91 VAL HB H 2.31 0.01 1 546 . 91 VAL HG1 H 1.06 0.01 1 547 . 91 VAL HG2 H 1.11 0.01 1 548 . 91 VAL N N 121.2 0.1 1 549 . 92 VAL H H 7.66 0.01 1 550 . 92 VAL HA H 3.32 0.01 1 551 . 92 VAL HB H 2.09 0.01 1 552 . 92 VAL HG1 H 0.74 0.01 1 553 . 92 VAL HG2 H 0.89 0.01 1 554 . 92 VAL N N 117.9 0.1 1 555 . 93 GLU H H 7.91 0.01 1 556 . 93 GLU HA H 3.97 0.01 1 557 . 93 GLU HB2 H 2.01 0.01 2 558 . 93 GLU HB3 H 1.97 0.01 2 559 . 93 GLU HG2 H 2.50 0.01 2 560 . 93 GLU N N 110.6 0.1 1 561 . 94 GLY H H 7.27 0.01 1 562 . 94 GLY HA2 H 3.67 0.01 1 563 . 94 GLY HA3 H 3.31 0.01 1 564 . 94 GLY N N 107.0 0.1 1 565 . 95 PRO HA H 4.31 0.01 1 566 . 95 PRO HG2 H 3.33 0.01 2 567 . 95 PRO HG3 H 3.10 0.01 2 568 . 96 LEU H H 8.15 0.01 1 569 . 96 LEU HA H 4.82 0.01 1 570 . 96 LEU HB2 H 2.00 0.01 2 571 . 96 LEU HG H 1.56 0.01 1 572 . 96 LEU HD1 H 1.15 0.01 2 573 . 96 LEU HD2 H 1.12 0.01 2 574 . 96 LEU N N 112.7 0.1 1 575 . 97 PRO HD2 H 3.75 0.01 2 576 . 98 LEU H H 6.87 0.01 1 577 . 98 LEU HA H 4.18 0.01 1 578 . 98 LEU HB2 H 1.98 0.01 2 579 . 98 LEU HG H 1.75 0.01 1 580 . 98 LEU HD1 H 1.14 0.01 1 581 . 98 LEU HD2 H 1.14 0.01 1 582 . 98 LEU N N 115.4 0.1 1 583 . 99 PHE H H 8.21 0.01 1 584 . 99 PHE HA H 4.21 0.01 1 585 . 99 PHE HB2 H 3.55 0.01 2 586 . 99 PHE HB3 H 3.21 0.01 2 587 . 99 PHE HD1 H 7.56 0.01 1 588 . 99 PHE HD2 H 7.56 0.01 1 589 . 99 PHE HE1 H 7.73 0.01 1 590 . 99 PHE HE2 H 7.73 0.01 1 591 . 99 PHE HZ H 7.70 0.01 1 592 . 99 PHE N N 114.9 0.1 1 593 . 100 PHE H H 8.24 0.01 1 594 . 100 PHE HA H 4.32 0.01 1 595 . 100 PHE HB2 H 3.11 0.01 2 596 . 100 PHE HB3 H 3.06 0.01 2 597 . 100 PHE HD1 H 6.47 0.01 1 598 . 100 PHE HD2 H 6.47 0.01 1 599 . 100 PHE HE1 H 6.88 0.01 1 600 . 100 PHE HE2 H 6.88 0.01 1 601 . 100 PHE HZ H 7.14 0.01 1 602 . 100 PHE N N 116.1 0.1 1 603 . 101 ARG H H 7.92 0.01 1 604 . 101 ARG HA H 4.02 0.01 1 605 . 101 ARG HB2 H 1.90 0.01 2 606 . 101 ARG HG2 H 1.78 0.01 2 607 . 101 ARG N N 114.0 0.1 1 608 . 102 ALA H H 7.67 0.01 1 609 . 102 ALA HA H 3.75 0.01 1 610 . 102 ALA HB H 1.49 0.01 1 611 . 102 ALA N N 116.4 0.1 1 612 . 103 VAL H H 7.55 0.01 1 613 . 103 VAL HA H 3.57 0.01 1 614 . 103 VAL HB H 1.59 0.01 1 615 . 103 VAL HG1 H 0.80 0.01 1 616 . 103 VAL HG2 H 0.38 0.01 1 617 . 103 VAL N N 114.0 0.1 1 618 . 104 ASP H H 7.34 0.01 1 619 . 104 ASP HA H 4.46 0.01 1 620 . 104 ASP HB2 H 2.57 0.01 2 621 . 104 ASP HB3 H 1.73 0.01 2 622 . 104 ASP N N 116.2 0.1 1 623 . 105 THR H H 8.07 0.01 1 624 . 105 THR HA H 4.48 0.01 1 625 . 105 THR HB H 4.32 0.01 1 626 . 105 THR HG2 H 1.30 0.01 1 627 . 105 THR N N 117.5 0.1 1 628 . 106 ASN H H 7.69 0.01 1 629 . 106 ASN HA H 4.81 0.01 1 630 . 106 ASN HB2 H 2.57 0.01 2 631 . 106 ASN N N 113.5 0.1 1 632 . 107 GLU H H 7.69 0.01 1 633 . 107 GLU HA H 3.88 0.01 1 634 . 107 GLU HB2 H 2.19 0.01 2 635 . 107 GLU HB3 H 2.04 0.01 2 636 . 107 GLU N N 114.4 0.1 1 637 . 108 ASP H H 8.33 0.01 1 638 . 108 ASP HA H 4.73 0.01 1 639 . 108 ASP N N 116.9 0.1 1 640 . 109 ASN H H 10.27 0.01 1 641 . 109 ASN HA H 4.32 0.01 1 642 . 109 ASN HB2 H 3.12 0.01 2 643 . 109 ASN N N 115.1 0.1 1 644 . 110 ASN H H 8.01 0.01 1 645 . 110 ASN HA H 5.61 0.01 1 646 . 110 ASN HB2 H 2.19 0.01 1 647 . 110 ASN HB3 H 2.50 0.01 1 648 . 110 ASN HD21 H 6.88 0.01 2 649 . 110 ASN HD22 H 6.65 0.01 2 650 . 110 ASN N N 112.6 0.1 1 651 . 110 ASN ND2 N 111.8 0.1 1 652 . 111 ILE H H 9.67 0.01 1 653 . 111 ILE HA H 4.98 0.01 1 654 . 111 ILE HB H 1.70 0.01 1 655 . 111 ILE HG12 H 0.64 0.01 2 656 . 111 ILE HG13 H 0.22 0.01 2 657 . 111 ILE HG2 H 1.18 0.01 1 658 . 111 ILE HD1 H -0.02 0.01 1 659 . 111 ILE N N 123.1 0.1 1 660 . 112 SER H H 9.12 0.01 1 661 . 112 SER HA H 4.99 0.01 1 662 . 112 SER HB2 H 4.49 0.01 2 663 . 112 SER HB3 H 3.91 0.01 2 664 . 112 SER N N 122.6 0.1 1 665 . 113 ARG H H 9.09 0.01 1 666 . 113 ARG HA H 3.31 0.01 1 667 . 113 ARG HB2 H 1.39 0.01 2 668 . 113 ARG HB3 H 1.04 0.01 2 669 . 113 ARG HG2 H -0.06 0.01 2 670 . 113 ARG HG3 H 2.82 0.01 2 671 . 113 ARG N N 119.3 0.1 1 672 . 114 ASP H H 8.43 0.01 1 673 . 114 ASP HA H 4.40 0.01 1 674 . 114 ASP HB2 H 2.63 0.01 2 675 . 114 ASP HB3 H 2.54 0.01 2 676 . 114 ASP N N 116.8 0.1 1 677 . 115 GLU H H 7.66 0.01 1 678 . 115 GLU HA H 4.08 0.01 1 679 . 115 GLU HB2 H 2.04 0.01 2 680 . 115 GLU HG2 H 2.49 0.01 2 681 . 115 GLU HG3 H 2.24 0.01 2 682 . 115 GLU N N 119.0 0.1 1 683 . 116 TYR H H 8.78 0.01 1 684 . 116 TYR HA H 4.10 0.01 1 685 . 116 TYR HB2 H 3.23 0.01 2 686 . 116 TYR HB3 H 3.04 0.01 2 687 . 116 TYR HD1 H 6.81 0.01 1 688 . 116 TYR HD2 H 6.81 0.01 1 689 . 116 TYR HE1 H 6.38 0.01 1 690 . 116 TYR HE2 H 6.38 0.01 1 691 . 116 TYR N N 120.5 0.1 1 692 . 117 GLY H H 8.30 0.01 1 693 . 117 GLY HA2 H 3.58 0.01 1 694 . 117 GLY HA3 H 4.05 0.01 1 695 . 117 GLY N N 103.2 0.1 1 696 . 118 ILE H H 7.66 0.01 1 697 . 118 ILE HA H 3.88 0.01 1 698 . 118 ILE HB H 2.05 0.01 1 699 . 118 ILE HG2 H 0.92 0.01 1 700 . 118 ILE HD1 H 1.42 0.01 1 701 . 118 ILE N N 119.8 0.1 1 702 . 119 PHE H H 7.60 0.01 1 703 . 119 PHE HA H 4.32 0.01 1 704 . 119 PHE HB2 H 3.47 0.01 2 705 . 119 PHE HB3 H 3.31 0.01 2 706 . 119 PHE HD1 H 6.84 0.01 1 707 . 119 PHE HD2 H 6.84 0.01 1 708 . 119 PHE HE1 H 7.14 0.01 1 709 . 119 PHE HE2 H 7.14 0.01 1 710 . 119 PHE HZ H 7.06 0.01 1 711 . 119 PHE N N 120.0 0.1 1 712 . 120 PHE H H 8.27 0.01 1 713 . 120 PHE HA H 3.66 0.01 1 714 . 120 PHE HB2 H 3.06 0.01 2 715 . 120 PHE HB3 H 2.58 0.01 2 716 . 120 PHE HD1 H 6.58 0.01 1 717 . 120 PHE HD2 H 6.58 0.01 1 718 . 120 PHE HE1 H 6.94 0.01 1 719 . 120 PHE HE2 H 6.94 0.01 1 720 . 120 PHE HZ H 7.05 0.01 1 721 . 120 PHE N N 118.2 0.1 1 722 . 121 GLY H H 8.11 0.01 1 723 . 121 GLY HA2 H 4.16 0.01 2 724 . 121 GLY HA3 H 3.91 0.01 2 725 . 121 GLY N N 103.7 0.1 1 726 . 122 MET H H 8.22 0.01 1 727 . 122 MET HA H 4.24 0.01 1 728 . 122 MET HB2 H 2.08 0.01 2 729 . 122 MET HB3 H 1.99 0.01 2 730 . 122 MET HG2 H 2.30 0.01 2 731 . 122 MET N N 122.7 0.1 1 732 . 123 LEU H H 7.23 0.01 1 733 . 123 LEU HA H 4.26 0.01 1 734 . 123 LEU HB2 H 1.61 0.01 2 735 . 123 LEU HB3 H 1.32 0.01 2 736 . 123 LEU HG H 1.46 0.01 1 737 . 123 LEU HD1 H 0.20 0.01 1 738 . 123 LEU HD2 H 0.73 0.01 1 739 . 123 LEU N N 114.2 0.01 1 740 . 124 GLY H H 7.77 0.01 1 741 . 124 GLY HA2 H 4.10 0.01 2 742 . 124 GLY HA3 H 3.69 0.01 2 743 . 124 GLY N N 104.4 0.1 1 744 . 125 LEU H H 7.70 0.01 1 745 . 125 LEU HA H 4.43 0.01 1 746 . 125 LEU HB2 H 1.36 0.01 2 747 . 125 LEU HG H 1.16 0.01 1 748 . 125 LEU HD1 H 0.59 0.01 2 749 . 125 LEU HD2 H 0.06 0.01 2 750 . 125 LEU N N 118.9 0.1 1 751 . 126 ASP H H 8.03 0.01 1 752 . 126 ASP HA H 4.62 0.01 1 753 . 126 ASP HB2 H 2.74 0.01 2 754 . 126 ASP N N 118.9 0.1 1 755 . 127 LYS H H 8.76 0.01 1 756 . 127 LYS HA H 4.03 0.01 1 757 . 127 LYS HB2 H 1.89 0.01 1 758 . 127 LYS HG2 H 1.56 0.01 1 759 . 127 LYS N N 123.9 0.1 1 760 . 128 THR H H 8.76 0.01 1 761 . 128 THR HA H 4.16 0.01 1 762 . 128 THR HB H 4.02 0.01 1 763 . 128 THR HG2 H 1.34 0.01 1 764 . 128 THR N N 110.7 0.1 1 765 . 129 MET H H 8.08 0.01 1 766 . 129 MET HA H 4.16 0.01 1 767 . 129 MET HB2 H 2.32 0.01 2 768 . 129 MET HG2 H 2.77 0.01 2 769 . 129 MET HG3 H 2.60 0.01 2 770 . 129 MET N N 117.1 0.1 1 771 . 130 ALA H H 7.38 0.01 1 772 . 130 ALA HA H 3.68 0.01 1 773 . 130 ALA HB H 1.17 0.01 1 774 . 130 ALA N N 121.3 0.1 1 775 . 131 PRO HA H 4.20 0.01 1 776 . 131 PRO HB2 H 1.81 0.01 2 777 . 131 PRO HD2 H 3.52 0.01 2 778 . 131 PRO HD3 H 3.71 0.01 2 779 . 132 ALA H H 7.56 0.01 1 780 . 132 ALA HA H 4.16 0.01 1 781 . 132 ALA HB H 1.48 0.01 1 782 . 132 ALA N N 114.3 0.1 1 783 . 133 SER H H 7.14 0.01 1 784 . 133 SER HA H 4.18 0.01 1 785 . 133 SER HB2 H 3.97 0.01 1 786 . 133 SER HB3 H 3.97 0.01 1 787 . 133 SER N N 112.8 0.1 1 788 . 134 PHE H H 8.29 0.01 1 789 . 134 PHE HA H 4.60 0.01 1 790 . 134 PHE HB2 H 2.97 0.01 2 791 . 134 PHE HB3 H 2.51 0.01 2 792 . 134 PHE HD1 H 6.71 0.01 1 793 . 134 PHE HD2 H 6.71 0.01 1 794 . 134 PHE HE1 H 6.81 0.01 1 795 . 134 PHE HE2 H 6.81 0.01 1 796 . 134 PHE HZ H 7.02 0.01 1 797 . 134 PHE N N 121.2 0.1 1 798 . 135 ASP H H 8.83 0.01 1 799 . 135 ASP HA H 4.36 0.01 1 800 . 135 ASP HB2 H 2.64 0.01 2 801 . 135 ASP N N 114.8 0.01 1 802 . 136 ALA H H 6.98 0.01 1 803 . 136 ALA HA H 3.99 0.01 1 804 . 136 ALA HB H 1.37 0.01 1 805 . 136 ALA N N 117.9 0.1 1 806 . 137 ILE H H 7.10 0.01 1 807 . 137 ILE HA H 3.64 0.01 1 808 . 137 ILE HB H 1.52 0.01 1 809 . 137 ILE HG12 H 1.89 0.01 1 810 . 137 ILE HG13 H 0.72 0.01 1 811 . 137 ILE HG2 H 0.93 0.01 1 812 . 137 ILE HD1 H 0.38 0.01 1 813 . 137 ILE N N 115.8 0.1 1 814 . 138 ASP H H 7.56 0.01 1 815 . 138 ASP HA H 4.46 0.01 1 816 . 138 ASP HB2 H 2.73 0.01 1 817 . 138 ASP HB3 H 1.97 0.01 1 818 . 138 ASP N N 117.1 0.1 1 819 . 139 THR H H 8.30 0.01 1 820 . 139 THR HA H 4.05 0.01 1 821 . 139 THR HG2 H 1.29 0.01 1 822 . 139 THR N N 116.7 0.1 1 823 . 140 ASN H H 7.74 0.01 1 824 . 140 ASN HA H 4.86 0.01 1 825 . 140 ASN HB2 H 3.28 0.01 2 826 . 140 ASN HB3 H 2.85 0.01 2 827 . 140 ASN HD21 H 7.75 0.01 2 828 . 140 ASN HD22 H 6.62 0.01 2 829 . 140 ASN N N 114.2 0.1 1 830 . 140 ASN ND2 N 110.2 0.1 1 831 . 141 ASN H H 7.83 0.01 1 832 . 141 ASN HA H 4.38 0.01 1 833 . 141 ASN HB2 H 3.00 0.01 2 834 . 141 ASN HB3 H 2.72 0.01 2 835 . 141 ASN HD21 H 7.42 0.01 2 836 . 141 ASN HD22 H 6.64 0.01 2 837 . 141 ASN N N 113.0 0.1 1 838 . 141 ASN ND2 N 109.9 0.1 1 839 . 142 ASP H H 8.32 0.01 1 840 . 142 ASP HA H 4.38 0.01 1 841 . 142 ASP HB2 H 3.01 0.01 1 842 . 142 ASP HB3 H 3.01 0.01 1 843 . 142 ASP N N 115.9 0.1 1 844 . 143 GLY H H 10.46 0.01 1 845 . 143 GLY HA2 H 4.13 0.01 2 846 . 143 GLY HA3 H 3.60 0.01 2 847 . 143 GLY N N 111.4 0.1 1 848 . 144 LEU H H 7.92 0.01 1 849 . 144 LEU HA H 5.08 0.01 1 850 . 144 LEU HB2 H 1.61 0.01 2 851 . 144 LEU HB3 H 1.42 0.01 2 852 . 144 LEU HG H 1.03 0.01 1 853 . 144 LEU HD1 H 0.83 0.01 1 854 . 144 LEU HD2 H 0.74 0.01 1 855 . 144 LEU N N 117.1 0.1 1 856 . 145 LEU H H 9.64 0.01 1 857 . 145 LEU HA H 5.42 0.01 1 858 . 145 LEU HB2 H 2.04 0.01 2 859 . 145 LEU HG H 1.21 0.01 1 860 . 145 LEU HD1 H 0.32 0.01 1 861 . 145 LEU HD2 H -0.41 0.01 1 862 . 145 LEU N N 120.8 0.1 1 863 . 146 SER H H 9.00 0.01 1 864 . 146 SER HA H 4.94 0.01 1 865 . 146 SER HB2 H 4.44 0.01 1 866 . 146 SER HB3 H 4.05 0.01 1 867 . 146 SER N N 118.9 0.1 1 868 . 147 LEU H H 8.86 0.01 1 869 . 147 LEU HA H 3.01 0.01 1 870 . 147 LEU HB2 H 1.38 0.01 2 871 . 147 LEU HG H 1.23 0.01 1 872 . 147 LEU HD1 H 0.36 0.01 1 873 . 147 LEU HD2 H 0.70 0.01 1 874 . 147 LEU N N 122.5 0.1 1 875 . 148 GLU H H 8.29 0.01 1 876 . 148 GLU HA H 3.88 0.01 1 877 . 148 GLU HB2 H 2.00 0.01 2 878 . 148 GLU HB3 H 1.86 0.01 2 879 . 148 GLU HG2 H 2.22 0.01 2 880 . 148 GLU N N 114.8 0.1 1 881 . 149 GLU H H 7.85 0.01 1 882 . 149 GLU HA H 3.91 0.01 1 883 . 149 GLU HB2 H 2.46 0.01 2 884 . 149 GLU HB3 H 2.24 0.01 2 885 . 149 GLU HG2 H 2.49 0.01 2 886 . 149 GLU N N 115.7 0.1 1 887 . 150 PHE H H 8.59 0.01 1 888 . 150 PHE HA H 4.16 0.01 1 889 . 150 PHE HB2 H 3.47 0.01 2 890 . 150 PHE HB3 H 3.23 0.01 2 891 . 150 PHE HD1 H 7.15 0.01 1 892 . 150 PHE HD2 H 7.15 0.01 1 893 . 150 PHE HE1 H 7.42 0.01 1 894 . 150 PHE HE2 H 7.42 0.01 1 895 . 150 PHE HZ H 6.89 0.01 1 896 . 150 PHE N N 120.2 0.1 1 897 . 151 VAL H H 9.05 0.01 1 898 . 151 VAL HA H 3.67 0.01 1 899 . 151 VAL HB H 2.13 0.01 1 900 . 151 VAL HG1 H 1.09 0.01 1 901 . 151 VAL HG2 H 0.93 0.01 1 902 . 151 VAL N N 116.2 0.1 1 903 . 152 ILE H H 8.53 0.01 1 904 . 152 ILE HA H 3.67 0.01 1 905 . 152 ILE HB H 1.84 0.01 1 906 . 152 ILE HG12 H 1.15 0.01 2 907 . 152 ILE HG2 H 0.93 0.01 1 908 . 152 ILE HD1 H 0.83 0.01 1 909 . 152 ILE N N 119.8 0.1 1 910 . 153 ALA H H 7.70 0.01 1 911 . 153 ALA HA H 4.08 0.01 1 912 . 153 ALA HB H 1.64 0.01 1 913 . 153 ALA N N 120.6 0.1 1 914 . 154 GLY H H 8.10 0.01 1 915 . 154 GLY HA2 H 2.53 0.01 2 916 . 154 GLY HA3 H 1.81 0.01 2 917 . 154 GLY N N 106.2 0.1 1 918 . 155 SER H H 8.70 0.01 1 919 . 155 SER HA H 4.08 0.01 1 920 . 155 SER HB2 H 3.91 0.01 2 921 . 155 SER N N 115.7 0.1 1 922 . 156 ASP H H 7.48 0.01 1 923 . 156 ASP HA H 4.43 0.01 1 924 . 156 ASP HB2 H 2.95 0.01 2 925 . 156 ASP HB3 H 2.84 0.01 2 926 . 156 ASP N N 118.3 0.1 1 927 . 157 PHE H H 8.01 0.01 1 928 . 157 PHE HA H 4.08 0.01 1 929 . 157 PHE HB2 H 3.07 0.01 1 930 . 157 PHE HB3 H 3.07 0.01 1 931 . 157 PHE HD1 H 7.34 0.01 1 932 . 157 PHE HD2 H 7.34 0.01 1 933 . 157 PHE HE1 H 7.15 0.01 1 934 . 157 PHE HE2 H 7.15 0.01 1 935 . 157 PHE HZ H 7.74 0.01 1 936 . 157 PHE N N 115.8 0.1 1 937 . 158 PHE H H 7.68 0.01 1 938 . 158 PHE HA H 4.20 0.01 1 939 . 158 PHE HB2 H 3.07 0.01 2 940 . 158 PHE HB3 H 2.94 0.01 2 941 . 158 PHE HD1 H 7.31 0.01 1 942 . 158 PHE HD2 H 7.31 0.01 1 943 . 158 PHE HE1 H 6.99 0.01 1 944 . 158 PHE HE2 H 6.99 0.01 1 945 . 158 PHE HZ H 6.32 0.01 1 946 . 158 PHE N N 113.4 0.1 1 947 . 159 MET H H 8.76 0.01 1 948 . 159 MET HA H 4.56 0.01 1 949 . 159 MET HB2 H 2.20 0.01 2 950 . 159 MET HB3 H 2.10 0.01 2 951 . 159 MET HG2 H 2.74 0.01 2 952 . 159 MET N N 110.9 0.1 1 953 . 160 ASN H H 8.29 0.01 1 954 . 160 ASN HA H 4.53 0.01 1 955 . 160 ASN HB2 H 2.74 0.01 2 956 . 160 ASN HB3 H 2.62 0.01 2 957 . 160 ASN N N 115.9 0.1 1 958 . 161 ASP H H 9.19 0.01 1 959 . 161 ASP HA H 4.81 0.01 1 960 . 161 ASP HB2 H 2.59 0.01 2 961 . 161 ASP HB3 H 2.48 0.01 2 962 . 161 ASP N N 127.3 0.1 1 963 . 162 GLY H H 8.69 0.01 1 964 . 162 GLY HA2 H 4.55 0.01 2 965 . 162 GLY HA3 H 3.64 0.01 2 966 . 162 GLY N N 106.0 0.1 1 967 . 166 ASN H H 7.13 0.01 1 968 . 166 ASN HA H 4.90 0.01 1 969 . 166 ASN HB2 H 2.91 0.01 1 970 . 166 ASN HB3 H 3.08 0.01 1 971 . 166 ASN HD21 H 6.77 0.01 1 972 . 166 ASN HD22 H 7.96 0.01 1 973 . 166 ASN N N 111.7 0.1 1 974 . 166 ASN ND2 N 111.5 0.1 1 975 . 167 LYS H H 7.80 0.01 1 976 . 167 LYS HA H 4.35 0.01 1 977 . 167 LYS HB2 H 1.84 0.01 2 978 . 167 LYS HG2 H 1.31 0.01 2 979 . 167 LYS HD2 H 1.63 0.01 2 980 . 167 LYS N N 117.3 0.1 1 981 . 168 VAL H H 6.53 0.01 1 982 . 168 VAL HA H 4.75 0.01 1 983 . 168 VAL HB H 2.08 0.01 1 984 . 168 VAL HG1 H 0.95 0.01 2 985 . 168 VAL HG2 H 0.93 0.01 2 986 . 168 VAL N N 103.5 0.1 1 987 . 169 PHE H H 7.76 0.01 1 988 . 169 PHE HA H 4.69 0.01 1 989 . 169 PHE HB2 H 3.81 0.01 2 990 . 169 PHE HB3 H 3.31 0.01 2 991 . 169 PHE HD1 H 5.65 0.01 1 992 . 169 PHE HD2 H 5.65 0.01 1 993 . 169 PHE HE1 H 6.25 0.01 1 994 . 169 PHE HE2 H 6.25 0.01 1 995 . 169 PHE HZ H 5.04 0.01 1 996 . 169 PHE N N 125.4 0.1 1 997 . 170 TRP H H 8.41 0.01 1 998 . 170 TRP HA H 4.49 0.01 1 999 . 170 TRP HB2 H 3.38 0.01 2 1000 . 170 TRP HB3 H 2.52 0.01 2 1001 . 170 TRP HD1 H 7.77 0.01 1 1002 . 170 TRP HE1 H 7.28 0.1 1 1003 . 170 TRP HE3 H 7.11 0.01 1 1004 . 170 TRP HZ2 H 6.97 0.01 1 1005 . 170 TRP HZ3 H 6.63 0.01 1 1006 . 170 TRP HH2 H 5.80 0.01 1 1007 . 170 TRP N N 111.0 0.1 1 1008 . 170 TRP NE1 N 122.3 0.1 1 1009 . 171 GLY H H 7.76 0.01 1 1010 . 171 GLY HA2 H 4.07 0.01 2 1011 . 171 GLY HA3 H 3.66 0.01 2 1012 . 171 GLY N N 104.3 0.1 1 1013 . 172 PRO HA H 4.26 0.01 1 1014 . 172 PRO HB2 H 2.34 0.01 2 1015 . 173 LEU H H 8.19 0.01 1 1016 . 173 LEU HA H 4.54 0.01 1 1017 . 173 LEU HB2 H 1.64 0.01 2 1018 . 173 LEU HG H 1.80 0.01 1 1019 . 173 LEU HD1 H 1.11 0.01 2 1020 . 173 LEU HD2 H 0.83 0.01 2 1021 . 173 LEU N N 120.5 0.1 1 1022 . 174 VAL H H 7.85 0.01 1 1023 . 174 VAL HA H 3.95 0.01 1 1024 . 174 VAL HB H 2.23 0.01 1 1025 . 174 VAL HG1 H 0.95 0.01 1 1026 . 174 VAL HG2 H 0.88 0.01 1 1027 . 174 VAL N N 121.2 0.01 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details ; Chemical shift assignments for residue Ser1 which was assigned only in the natural protein sample where it is acetylated. ; loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'NSCP acetylated' _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 . 1 SAC H3 H 1.84 0.01 1 2 . 1 SAC H H 9.54 0.01 1 3 . 1 SAC HA H 4.40 0.01 1 4 . 1 SAC HB2 H 4.33 0.01 2 stop_ save_ save_assigned_chemical_shifts_three _Saveframe_category assigned_chemical_shifts _Details ; The amide proton assignments in the natural sample (sample_two) which differ by more than 0.05 ppm from the values in the recombinant sample. ; loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'NSCP acetylated' _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 . 5 VAL H H 9.08 0.01 1 2 . 7 LYS H H 8.81 0.01 1 3 . 8 MET H H 8.24 0.01 1 4 . 9 LYS H H 8.95 0.01 1 5 . 80 LYS H H 8.73 0.01 1 6 . 84 LYS H H 6.88 0.01 1 7 . 114 ASP H H 8.34 0.01 1 8 . 159 MET H H 8.83 0.01 1 9 . 160 ASN H H 8.35 0.01 1 10 . 161 ASP H H 9.27 0.01 1 11 . 162 GLY H H 8.83 0.01 1 stop_ save_