data_4224 #Corrected using PDB structure: 1MYO_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 11 K HA 3.68 4.47 # 32 L HA 4.62 3.90 # 37 K HA 3.88 4.87 # 39 L HA 3.73 4.62 # 46 G HA 3.16 4.56 # 47 Q HA 4.57 3.37 # 59 A HA 4.11 5.16 # 63 A HA 4.48 3.77 # 64 P HA 4.74 3.96 # 80 H HA 5.28 4.15 #102 L HA 4.88 3.57 #103 T HA 4.71 3.26 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 28 V CA 64.17 58.82 # 80 H CA 53.89 59.00 # 81 V CA 67.69 62.01 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 65 D CB 40.37 45.98 # 94 K CB 32.86 38.09 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 8 W N 117.64 128.74 # 36 R N 66.80 117.19 # 48 L N 127.92 114.03 # 58 G N 104.92 118.79 # 81 V N 126.30 107.96 # 94 K N 125.90 111.21 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 15 L H 7.84 10.05 # 77 Y H 9.18 6.41 # 90 K H 7.35 9.66 # 91 G H 7.54 9.74 #101 G H 8.27 10.31 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.07 0.04 0.28 N/A -0.34 -0.06 # #bmr4224.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4224.str file): #HA CA CB CO N HN #N/A +0.16 +0.16 N/A -0.34 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.19 +/-0.17 N/A +/-0.47 +/-0.09 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.373 0.940 0.991 N/A 0.364 -0.051 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.184 1.023 0.889 N/A 2.401 0.470 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Myotrophin ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yan Y. . . 2 Nanduri S. . . 3 Sen S. . . 4 Quin J. . . stop_ _BMRB_accession_number 4224 _BMRB_flat_file_name bmr4224.str _Entry_type new _Submission_date 1998-08-17 _Accession_date 1998-08-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 659 '13C chemical shifts' 385 '15N chemical shifts' 120 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Nuclear Magnetic Resonance Assignment and Secondary Structure of Ankyrin-like Repeat-bearing protein: Myotrophin ; _Citation_status 'published' _Citation_type journal _MEDLINE_UI_code 97337457 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yan Y. . . 2 Nanduri S. . . 3 Sen S. . . 4 Quin J. . . stop_ _Journal_abbreviation "Protein Sci." _Journal_name_full "Protein Science" _Journal_volume 6 _Page_first 1347 _Page_last 1351 _Year 1997 loop_ _Keyword myotrophin NM ANK-repeat stop_ save_ ################################## # Molecular system description # ################################## save_system_Myotrophin _Saveframe_category molecular_system _Mol_system_name Myotrophin _Abbreviation_common Myotrophin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Myotrophin $Myotrophin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1MYO "Solution Structure Of Myotrophin, Nmr, 44 Structures" . PDB 2MYO "Solution Structure Of Myotrophin, Nmr, Minimized Average Structure" . stop_ save_ ######################## # Monomeric polymers # ######################## save_Myotrophin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Myotrophin _Mol_thiol_state 'not reported' ############################## # Polymer residue sequence # ############################## _Residue_count 118 _Mol_residue_sequence ; MCDKEFMWALKNGDLDEVKD YVAKGEDVNRTLEGGRKPLH YAADCGQLEILEFLLLKGAD INAPDKHHITPLLSAVYEGH VSCVKLLLSKGADKTVKGPD GLTALEATDNQAIKALLQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . MET 2 . CYS 3 . ASP 4 . LYS 5 . GLU 6 . PHE 7 . MET 8 . TRP 9 . ALA 10 . LEU 11 . LYS 12 . ASN 13 . GLY 14 . ASP 15 . LEU 16 . ASP 17 . GLU 18 . VAL 19 . LYS 20 . ASP 21 . TYR 22 . VAL 23 . ALA 24 . LYS 25 . GLY 26 . GLU 27 . ASP 28 . VAL 29 . ASN 30 . ARG 31 . THR 32 . LEU 33 . GLU 34 . GLY 35 . GLY 36 . ARG 37 . LYS 38 . PRO 39 . LEU 40 . HIS 41 . TYR 42 . ALA 43 . ALA 44 . ASP 45 . CYS 46 . GLY 47 . GLN 48 . LEU 49 . GLU 50 . ILE 51 . LEU 52 . GLU 53 . PHE 54 . LEU 55 . LEU 56 . LEU 57 . LYS 58 . GLY 59 . ALA 60 . ASP 61 . ILE 62 . ASN 63 . ALA 64 . PRO 65 . ASP 66 . LYS 67 . HIS 68 . HIS 69 . ILE 70 . THR 71 . PRO 72 . LEU 73 . LEU 74 . SER 75 . ALA 76 . VAL 77 . TYR 78 . GLU 79 . GLY 80 . HIS 81 . VAL 82 . SER 83 . CYS 84 . VAL 85 . LYS 86 . LEU 87 . LEU 88 . LEU 89 . SER 90 . LYS 91 . GLY 92 . ALA 93 . ASP 94 . LYS 95 . THR 96 . VAL 97 . LYS 98 . GLY 99 . PRO 100 . ASP 101 . GLY 102 . LEU 103 . THR 104 . ALA 105 . LEU 106 . GLU 107 . ALA 108 . THR 109 . ASP 110 . ASN 111 . GLN 112 . ALA 113 . ILE 114 . LYS 115 . ALA 116 . LEU 117 . LEU 118 . GLN stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-28 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 1MYO "Solution Structure Of Myotrophin, Nmr, 44Structures" 100.00 118 100 100 1e-63 PDB 2MYO "Solution Structure Of Myotrophin, Nmr,Minimized Average Structure" 100.00 118 100 100 1e-63 DBJ BAA05167.1 "V-1 protein [Rattus norvegicus]" 100.00 118 100 100 1e-63 DBJ BAC25707.1 "unnamed protein product [Mus musculus]" 100.00 118 100 100 1e-63 DBJ BAC33734.1 "unnamed protein product [Mus musculus]" 100.00 118 100 100 1e-63 DBJ BAC39050.1 "unnamed protein product [Mus musculus]" 100.00 118 100 100 1e-63 DBJ BAB22235.1 "unnamed protein product [Mus musculus]" 100.00 118 99 100 4e-63 EMBL CAD38909.1 "hypothetical protein [Homo sapiens]" 100.00 118 99 99 4e-63 GenBank AAA86719.1 "V-1 protein" 100.00 118 100 100 1e-63 GenBank AAC52498.1 myotrophin 100.00 118 100 100 1e-63 GenBank AAH43084.1 "Myotrophin [Mus musculus]" 100.00 118 100 100 1e-63 GenBank AAH54811.1 "Myotrophin [Mus musculus]" 100.00 118 100 100 1e-63 GenBank AAH28093.1 "Myotrophin [Homo sapiens]" 100.00 118 99 99 4e-63 PIR A54412 "V-1 protein - rat" 100.00 118 100 100 1e-63 REF NP_032124.1 "myotrophin; granule celldifferentiation protein [Mus musculus]" 100.00 118 100 100 1e-63 REF NP_077350.1 "myotrophin; V-1 protein [Rattusnorvegicus]" 100.00 118 100 100 1e-63 REF NP_665807.1 "myotrophin; granule celldifferentiation protein [Homo sapiens]" 100.00 118 99 99 4e-63 SWISS-PROT P80144 "MTPN_MOUSE Myotrophin (V-1 protein) (Granulecell differentiation protein)" 100.00 118 100 100 1e-63 SWISS-PROT P58546 "MTPN_HUMAN Myotrophin (V-1 protein)" 100.00 118 99 99 4e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $Myotrophin human 9606 Eukaryota Metazoa Homo sapiens heart 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 $Myotrophin ? . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Myotrophin . mM . 'phosphate buffer' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D- and 4D-NOESY 3D-TOCSY HNCACB HNHA C(CO)NH H(CCO)NH HCCH-TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . n/a temperature 297 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference 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 . H 1 . ppm . . . . . . . . C 13 . ppm . . . . . . . . N 15 . ppm . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name Myotrophin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 ASP H H 8.34 . 1 2 3 ASP HA H 4.39 . 1 3 3 ASP HB2 H 2.84 . 1 4 3 ASP HB3 H 2.84 . 1 5 3 ASP CA C 57.51 . 1 6 3 ASP CB C 40.72 . 1 7 3 ASP N N 120.33 . 1 8 4 LYS H H 8.51 . 1 9 4 LYS HA H 3.93 . 1 10 4 LYS HB2 H 1.91 . 1 11 4 LYS HB3 H 1.78 . 1 12 4 LYS HG2 H 1.45 . 1 13 4 LYS HG3 H 1.31 . 1 14 4 LYS HD2 H 1.69 . 1 15 4 LYS HD3 H 1.69 . 1 16 4 LYS HE2 H 2.97 . 1 17 4 LYS HE3 H 2.97 . 1 18 4 LYS CA C 60.11 . 1 19 4 LYS CB C 32.00 . 1 20 4 LYS CG C 25.12 . 1 21 4 LYS CD C 29.29 . 1 22 4 LYS CE C 41.90 . 1 23 4 LYS N N 118.83 . 1 24 5 GLU H H 8.38 . 1 25 5 GLU HA H 4.13 . 1 26 5 GLU HB2 H 2.20 . 1 27 5 GLU HB3 H 2.20 . 1 28 5 GLU HG2 H 2.38 . 1 29 5 GLU HG3 H 2.38 . 1 30 5 GLU CA C 60.02 . 1 31 5 GLU CB C 28.81 . 1 32 5 GLU CG C 35.79 . 1 33 5 GLU N N 119.91 . 1 34 6 PHE H H 8.56 . 1 35 6 PHE HA H 4.26 . 1 36 6 PHE HB2 H 2.81 . 1 37 6 PHE HB3 H 2.51 . 1 38 6 PHE HD1 H 7.04 . 1 39 6 PHE HD2 H 7.04 . 1 40 6 PHE CA C 58.30 . 1 41 6 PHE CB C 38.57 . 1 42 6 PHE CD1 C 129.76 . 3 43 6 PHE CD2 C 129.86 . 3 44 6 PHE N N 122.40 . 1 45 7 MET H H 8.49 . 1 46 7 MET HA H 3.20 . 1 47 7 MET HB2 H 1.93 . 1 48 7 MET HB3 H 1.40 . 1 49 7 MET HG2 H 2.14 . 1 50 7 MET HG3 H 2.03 . 1 51 7 MET HE H 1.80 . 1 52 7 MET CA C 59.75 . 1 53 7 MET CB C 30.70 . 1 54 7 MET CG C 32.44 . 1 55 7 MET CE C 16.36 . 1 56 7 MET N N 116.33 . 1 57 8 TRP H H 8.06 . 1 58 8 TRP HA H 4.10 . 1 59 8 TRP HB2 H 3.33 . 1 60 8 TRP HB3 H 3.42 . 1 61 8 TRP HD1 H 7.25 . 1 62 8 TRP HE1 H 10.16 . 1 63 8 TRP HE3 H 7.24 . 1 64 8 TRP HZ2 H 7.45 . 1 65 8 TRP HZ3 H 7.12 . 1 67 8 TRP CB C 28.55 . 1 68 8 TRP CD1 C 126.79 . 1 69 8 TRP CE3 C 124.45 . 1 70 8 TRP CZ2 C 114.40 . 1 71 8 TRP CZ3 C 112.27 . 1 72 8 TRP N N 117.64 . 1 73 8 TRP NE1 N 71.67 . 1 74 9 ALA H H 8.15 . 1 75 9 ALA HA H 4.16 . 1 76 9 ALA HB H 1.83 . 1 77 9 ALA CA C 55.64 . 1 78 9 ALA CB C 18.41 . 1 79 9 ALA N N 122.16 . 1 80 10 LEU H H 7.82 . 1 81 10 LEU HA H 3.61 . 1 82 10 LEU HB2 H 1.92 . 1 83 10 LEU HB3 H 0.92 . 1 84 10 LEU HG H 1.32 . 1 85 10 LEU HD1 H 0.12 . 1 86 10 LEU HD2 H 0.75 . 1 87 10 LEU CB C 43.43 . 1 88 10 LEU CG C 25.80 . 1 89 10 LEU CD1 C 25.71 . 1 90 10 LEU CD2 C 25.68 . 1 91 10 LEU N N 116.80 . 1 92 11 LYS H H 7.68 . 1 93 11 LYS HA H 3.61 . 1 94 11 LYS HB2 H 1.53 . 1 95 11 LYS HB3 H 1.92 . 1 96 11 LYS HG2 H 1.56 . 1 97 11 LYS HG3 H 1.56 . 1 98 11 LYS CA C 59.35 . 1 100 11 LYS CG C 26.18 . 1 101 11 LYS CD C 29.72 . 1 102 11 LYS N N 113.37 . 1 103 12 ASN H H 8.06 . 1 104 12 ASN HA H 4.47 . 1 105 12 ASN HB2 H 2.46 . 1 106 12 ASN HB3 H 2.03 . 1 107 12 ASN HD22 H 6.38 . 1 108 12 ASN HD21 H 7.10 . 1 109 12 ASN CA C 53.11 . 1 110 12 ASN CB C 38.60 . 1 111 12 ASN N N 111.44 . 1 112 12 ASN ND2 N 65.31 . 1 113 13 GLY H H 7.36 . 1 114 13 GLY HA2 H 3.35 . 1 115 13 GLY HA3 H 3.95 . 1 116 13 GLY CA C 46.79 . 1 117 13 GLY N N 107.66 . 1 118 14 ASP H H 8.45 . 1 119 14 ASP HA H 4.77 . 1 120 14 ASP HB2 H 2.47 . 1 121 14 ASP HB3 H 3.12 . 1 122 14 ASP CA C 52.61 . 1 123 14 ASP CB C 39.45 . 1 124 14 ASP N N 121.80 . 1 125 15 LEU H H 7.90 . 1 126 15 LEU HA H 3.66 . 1 127 15 LEU HB2 H 1.81 . 1 128 15 LEU HB3 H 1.38 . 1 129 15 LEU HG H 1.28 . 1 130 15 LEU HD1 H 0.80 . 1 131 15 LEU HD2 H 0.54 . 1 132 15 LEU CA C 57.65 . 1 133 15 LEU CB C 41.20 . 1 134 15 LEU CG C 26.82 . 1 135 15 LEU CD1 C 25.79 . 1 136 15 LEU CD2 C 22.80 . 1 137 15 LEU N N 126.68 . 1 138 16 ASP H H 8.46 . 1 139 16 ASP HA H 4.21 . 1 140 16 ASP HB2 H 2.67 . 1 141 16 ASP HB3 H 2.60 . 1 142 16 ASP CA C 58.02 . 1 143 16 ASP CB C 39.64 . 1 144 16 ASP N N 117.88 . 1 145 17 GLU H H 7.74 . 1 146 17 GLU HA H 4.13 . 1 147 17 GLU HB2 H 2.15 . 1 148 17 GLU HB3 H 2.04 . 1 149 17 GLU HG2 H 2.38 . 1 150 17 GLU HG3 H 2.38 . 1 151 17 GLU CA C 59.10 . 1 152 17 GLU CB C 29.21 . 1 153 17 GLU CG C 35.57 . 1 154 17 GLU N N 120.46 . 1 155 18 VAL H H 8.14 . 1 156 18 VAL HA H 3.79 . 1 157 18 VAL HB H 2.22 . 1 158 18 VAL HG1 H 1.16 . 1 159 18 VAL HG2 H 1.07 . 1 160 18 VAL CA C 68.11 . 1 161 18 VAL CB C 31.54 . 1 162 18 VAL CG1 C 21.46 . 1 163 18 VAL CG2 C 24.20 . 1 164 18 VAL N N 119.85 . 1 165 19 LYS H H 8.73 . 1 166 19 LYS HA H 3.81 . 1 167 19 LYS HB2 H 1.68 . 1 168 19 LYS HB3 H 1.77 . 1 169 19 LYS HG2 H 0.95 . 1 170 19 LYS HG3 H 0.95 . 1 171 19 LYS HD2 H 1.41 . 1 172 19 LYS HD3 H 1.41 . 1 173 19 LYS HE2 H 2.68 . 1 174 19 LYS HE3 H 2.43 . 1 175 19 LYS CA C 60.16 . 1 176 19 LYS CB C 32.32 . 1 177 19 LYS CG C 25.30 . 1 178 19 LYS CD C 29.61 . 1 179 19 LYS CE C 41.63 . 1 180 19 LYS N N 117.78 . 1 181 20 ASP H H 7.73 . 1 182 20 ASP HA H 4.44 . 1 183 20 ASP HB2 H 2.69 . 1 184 20 ASP HB3 H 2.62 . 1 185 20 ASP CA C 57.53 . 1 186 20 ASP CB C 41.22 . 1 187 20 ASP N N 120.97 . 1 188 21 TYR H H 8.31 . 1 189 21 TYR HA H 3.97 . 1 190 21 TYR HB2 H 2.84 . 1 191 21 TYR HB3 H 2.32 . 1 192 21 TYR HD1 H 7.03 . 1 193 21 TYR HD2 H 7.03 . 1 194 21 TYR HE1 H 6.73 . 1 195 21 TYR HE2 H 6.73 . 1 196 21 TYR CA C 62.68 . 1 197 21 TYR CB C 37.79 . 1 198 21 TYR CD1 C 132.66 . 3 199 21 TYR CD2 C 132.72 . 3 200 21 TYR CE1 C 117.66 . 1 201 21 TYR CE2 C 117.66 . 1 202 21 TYR N N 117.88 . 1 203 22 VAL H H 8.24 . 1 204 22 VAL HA H 3.88 . 1 205 22 VAL HB H 2.39 . 1 206 22 VAL HG1 H 1.24 . 1 207 22 VAL HG2 H 1.13 . 1 208 22 VAL CA C 66.40 . 1 209 22 VAL CB C 31.73 . 1 210 22 VAL CG1 C 23.74 . 1 211 22 VAL CG2 C 21.38 . 1 212 22 VAL N N 118.80 . 1 213 23 ALA H H 8.76 . 1 214 23 ALA HA H 4.24 . 1 215 23 ALA HB H 1.63 . 1 216 23 ALA CA C 55.07 . 1 218 23 ALA N N 125.49 . 1 219 24 LYS H H 7.76 . 1 220 24 LYS HA H 4.22 . 1 221 24 LYS HB2 H 2.05 . 1 222 24 LYS HB3 H 1.74 . 1 223 24 LYS HG2 H 1.56 . 1 224 24 LYS HG3 H 1.44 . 1 225 24 LYS HD2 H 1.56 . 1 226 24 LYS HD3 H 1.44 . 1 227 24 LYS HE2 H 2.86 . 1 228 24 LYS HE3 H 2.86 . 1 229 24 LYS CA C 56.84 . 1 230 24 LYS CB C 32.60 . 1 231 24 LYS CG C 25.94 . 1 232 24 LYS CD C 29.02 . 1 233 24 LYS CE C 42.06 . 1 234 24 LYS N N 116.22 . 1 235 25 GLY HA2 H 3.72 . 1 236 25 GLY HA3 H 4.46 . 1 237 25 GLY CA C 45.21 . 1 238 25 GLY N N 105.90 . 1 239 26 GLU H H 7.88 . 1 240 26 GLU HA H 4.12 . 1 241 26 GLU HB2 H 1.37 . 1 242 26 GLU HB3 H 1.23 . 1 243 26 GLU HG2 H 1.70 . 1 244 26 GLU HG3 H 1.60 . 1 245 26 GLU CA C 56.46 . 1 246 26 GLU CB C 29.20 . 1 247 26 GLU CG C 35.30 . 1 248 26 GLU N N 121.10 . 1 249 27 ASP H H 8.75 . 1 250 27 ASP HA H 4.09 . 1 251 27 ASP HB2 H 2.82 . 1 252 27 ASP HB3 H 2.75 . 1 253 27 ASP CA C 52.80 . 1 254 27 ASP CB C 42.64 . 1 255 27 ASP N N 123.90 . 1 256 28 VAL H H 8.57 . 1 257 28 VAL HA H 4.06 . 1 258 28 VAL HB H 2.35 . 1 259 28 VAL HG1 H 1.09 . 1 260 28 VAL HG2 H 0.80 . 1 261 28 VAL CA C 64.29 . 1 262 28 VAL CB C 31.65 . 1 263 28 VAL CG1 C 23.11 . 1 264 28 VAL CG2 C 17.35 . 1 265 28 VAL N N 119.22 . 1 266 29 ASN H H 8.81 . 1 267 29 ASN HA H 4.96 . 1 268 29 ASN HB2 H 3.14 . 1 269 29 ASN HB3 H 2.73 . 1 270 29 ASN HD22 H 6.79 . 1 271 29 ASN HD21 H 8.25 . 1 272 29 ASN CA C 53.32 . 1 273 29 ASN CB C 40.62 . 1 274 29 ASN N N 116.11 . 1 275 29 ASN ND2 N 66.44 . 1 276 30 ARG H H 7.52 . 1 277 30 ARG HA H 4.22 . 1 278 30 ARG HB2 H 1.84 . 1 279 30 ARG HB3 H 2.07 . 1 280 30 ARG HG2 H 1.58 . 1 281 30 ARG HG3 H 1.74 . 1 282 30 ARG HD2 H 3.48 . 1 283 30 ARG HD3 H 3.25 . 1 284 30 ARG CA C 56.89 . 1 285 30 ARG CB C 31.79 . 1 286 30 ARG CG C 27.28 . 1 287 30 ARG CD C 43.52 . 1 288 30 ARG N N 123.80 . 1 289 31 THR H H 8.68 . 1 290 31 THR HA H 3.93 . 1 291 31 THR HB H 4.03 . 1 292 31 THR HG2 H 1.18 . 1 293 31 THR CA C 63.78 . 1 294 31 THR CB C 68.59 . 1 295 31 THR CG2 C 22.67 . 1 297 32 LEU H H 8.73 . 1 298 32 LEU HA H 4.55 . 1 299 32 LEU HB2 H 2.08 . 1 300 32 LEU HB3 H 2.08 . 1 301 32 LEU HG H 1.98 . 9 302 32 LEU HD1 H 0.77 . 1 303 32 LEU HD2 H 0.96 . 1 304 32 LEU CA C 54.29 . 1 306 32 LEU CG C 28.10 . 1 307 32 LEU CD1 C 25.76 . 1 308 32 LEU CD2 C 22.96 . 1 309 32 LEU N N 129.15 . 1 310 33 GLU H H 7.76 . 1 311 33 GLU HA H 4.07 . 1 312 33 GLU HB2 H 2.15 . 1 313 33 GLU HB3 H 2.04 . 1 314 33 GLU HG2 H 2.35 . 1 315 33 GLU HG3 H 2.30 . 1 316 33 GLU CA C 59.08 . 1 318 33 GLU CG C 35.87 . 1 319 33 GLU N N -0.34 . 1 320 34 GLY H H 8.69 . 1 321 34 GLY HA2 H 4.04 . 1 322 34 GLY HA3 H 3.98 . 1 323 34 GLY CA C 45.56 . 1 324 34 GLY N N 107.89 . 1 325 35 GLY H H 8.57 . 1 326 35 GLY HA2 H 4.16 . 1 327 35 GLY HA3 H 3.59 . 1 328 35 GLY CA C 45.70 . 1 329 35 GLY N N 106.52 . 1 330 36 ARG H H 7.22 . 1 331 36 ARG HA H 4.59 . 1 332 36 ARG HB2 H 2.11 . 1 333 36 ARG HB3 H 2.11 . 1 334 36 ARG HG2 H 1.58 . 1 335 36 ARG HG3 H 1.58 . 1 336 36 ARG HD2 H 3.07 . 1 337 36 ARG HD3 H 3.07 . 1 338 36 ARG CA C 52.53 . 1 339 36 ARG CB C 31.49 . 1 340 36 ARG CG C 26.36 . 1 341 36 ARG CD C 46.12 . 1 343 37 LYS H H 9.60 . 1 344 37 LYS HA H 3.81 . 1 345 37 LYS HB2 H 1.65 . 1 346 37 LYS HB3 H 1.65 . 1 347 37 LYS HG2 H 0.52 . 1 348 37 LYS HG3 H 0.52 . 1 349 37 LYS HD2 H 1.41 . 1 350 37 LYS HD3 H 1.41 . 1 351 37 LYS HE2 H 2.94 . 1 352 37 LYS HE3 H 3.18 . 1 353 37 LYS CA C 53.82 . 1 354 37 LYS CB C 34.55 . 1 355 37 LYS CG C 25.11 . 1 356 37 LYS CD C 29.69 . 1 357 37 LYS CE C 42.73 . 1 358 37 LYS N N 121.53 . 1 359 38 PRO HA H 4.16 . 1 360 38 PRO HB2 H 1.80 . 1 361 38 PRO HB3 H 1.96 . 1 362 38 PRO HG2 H 2.35 . 1 363 38 PRO HG3 H 2.35 . 1 364 38 PRO CA C 67.16 . 1 365 38 PRO CB C 32.44 . 1 366 38 PRO CG C 28.60 . 1 367 39 LEU H H 9.34 . 1 368 39 LEU HA H 3.66 . 1 369 39 LEU HB2 H 1.36 . 1 370 39 LEU HG H 1.78 . 1 371 39 LEU HD1 H 0.69 . 1 372 39 LEU HD2 H 0.74 . 1 373 39 LEU CA C 57.65 . 1 374 39 LEU CB C 43.49 . 1 375 39 LEU CG C 27.49 . 1 376 39 LEU CD1 C 28.43 . 1 377 39 LEU CD2 C 26.37 . 1 378 39 LEU N N 113.86 . 1 379 40 HIS H H 7.65 . 1 380 40 HIS HA H 3.69 . 1 381 40 HIS HB2 H 2.95 . 1 382 40 HIS HB3 H 2.66 . 1 383 40 HIS CA C 63.02 . 1 384 40 HIS CB C 30.93 . 1 385 40 HIS N N 114.41 . 1 386 41 TYR H H 7.07 . 1 387 41 TYR HA H 4.20 . 1 388 41 TYR HB2 H 2.63 . 1 389 41 TYR HB3 H 2.76 . 1 390 41 TYR HD1 H 6.99 . 1 391 41 TYR HD2 H 6.99 . 1 392 41 TYR HE1 H 6.70 . 1 393 41 TYR HE2 H 6.70 . 1 394 41 TYR CA C 61.96 . 1 395 41 TYR CB C 38.47 . 1 396 41 TYR CD1 C 131.56 . 1 397 41 TYR CD2 C 131.56 . 1 398 41 TYR CE1 C 118.79 . 1 399 41 TYR CE2 C 118.79 . 1 400 41 TYR N N 114.66 . 1 401 42 ALA H H 7.56 . 1 402 42 ALA HA H 3.94 . 1 403 42 ALA HB H 1.32 . 1 404 42 ALA CA C 54.53 . 1 405 42 ALA CB C 18.37 . 1 406 42 ALA N N 117.73 . 1 407 43 ALA H H 8.38 . 1 408 43 ALA HA H 3.85 . 1 409 43 ALA HB H 1.44 . 1 410 43 ALA CA C 55.62 . 1 411 43 ALA CB C 19.14 . 1 412 43 ALA N N 120.53 . 1 413 44 ASP H H 8.34 . 1 414 44 ASP HA H 4.24 . 1 415 44 ASP HB2 H 2.86 . 1 416 44 ASP HB3 H 2.86 . 1 417 44 ASP CA C 57.39 . 1 419 44 ASP N N 116.77 . 1 420 45 CYS H H 6.90 . 1 421 45 CYS HA H 4.68 . 1 422 45 CYS HB2 H 2.88 . 1 423 45 CYS HB3 H 3.41 . 1 424 45 CYS CA C 59.31 . 1 425 45 CYS CB C 29.20 . 1 426 45 CYS N N 110.06 . 1 427 46 GLY H H 7.43 . 1 428 46 GLY HA2 H 3.56 . 1 429 46 GLY HA3 H 2.62 . 1 430 46 GLY CA C 46.29 . 1 431 46 GLY N N 111.52 . 1 432 47 GLN H H 8.10 . 1 433 47 GLN HA H 4.50 . 1 434 47 GLN HB2 H 2.74 . 1 435 47 GLN HB3 H 2.74 . 1 436 47 GLN HG2 H 2.04 . 1 437 47 GLN HG3 H 1.73 . 1 438 47 GLN HE22 H 6.88 . 1 439 47 GLN HE21 H 6.88 . 1 440 47 GLN CA C 53.10 . 1 441 47 GLN CB C 25.82 . 1 442 47 GLN CG C 30.13 . 1 443 47 GLN N N 118.05 . 1 444 47 GLN NE2 N 64.10 . 1 445 48 LEU H H 7.71 . 1 446 48 LEU HA H 3.79 . 1 447 48 LEU HB2 H 1.49 . 1 448 48 LEU HB3 H 1.73 . 1 449 48 LEU HG H 1.57 . 1 450 48 LEU HD1 H 0.86 . 1 451 48 LEU HD2 H 0.86 . 1 452 48 LEU CA C 59.25 . 1 453 48 LEU CB C 42.86 . 1 454 48 LEU CG C 26.89 . 1 455 48 LEU CD1 C 25.31 . 1 456 48 LEU CD2 C 25.31 . 1 457 48 LEU N N 127.92 . 1 458 49 GLU H H 8.82 . 1 459 49 GLU HA H 4.12 . 1 460 49 GLU HB2 H 2.10 . 1 461 49 GLU HB3 H 2.01 . 1 462 49 GLU HG2 H 2.45 . 1 463 49 GLU HG3 H 2.37 . 1 464 49 GLU CA C 59.94 . 1 465 49 GLU CB C 28.67 . 1 466 49 GLU CG C 37.10 . 1 467 49 GLU N N 116.12 . 1 468 50 ILE H H 7.34 . 1 469 50 ILE HA H 3.78 . 1 470 50 ILE HB H 2.19 . 1 471 50 ILE HG12 H 1.77 . 1 472 50 ILE HG13 H 1.67 . 1 473 50 ILE HG2 H 0.96 . 1 474 50 ILE HD1 H 0.66 . 1 475 50 ILE CA C 62.63 . 1 476 50 ILE CB C 35.40 . 1 477 50 ILE CG1 C 28.46 . 1 478 50 ILE CG2 C 19.91 . 1 479 50 ILE CD1 C 10.72 . 1 480 50 ILE N N 117.68 . 1 481 51 LEU H H 8.21 . 1 482 51 LEU HA H 3.71 . 1 483 51 LEU HB2 H 2.11 . 1 484 51 LEU HB3 H 1.30 . 1 485 51 LEU HG H 1.68 . 1 486 51 LEU HD1 H 0.83 . 1 487 51 LEU HD2 H 0.80 . 1 488 51 LEU CA C 58.90 . 1 489 51 LEU CB C 42.55 . 1 490 51 LEU CG C 26.11 . 1 491 51 LEU CD1 C 25.99 . 1 492 51 LEU CD2 C 26.70 . 1 493 51 LEU N N 119.89 . 1 494 52 GLU H H 8.26 . 1 495 52 GLU HA H 3.76 . 1 496 52 GLU HB2 H 2.14 . 1 497 52 GLU HB3 H 2.14 . 1 498 52 GLU HG2 H 2.36 . 1 499 52 GLU HG3 H 2.20 . 1 500 52 GLU CA C 60.32 . 1 501 52 GLU CB C 29.94 . 1 502 52 GLU CG C 36.86 . 1 503 52 GLU N N 115.82 . 1 504 53 PHE H H 7.64 . 1 505 53 PHE HA H 4.30 . 1 506 53 PHE HB2 H 3.36 . 1 507 53 PHE HB3 H 2.98 . 1 508 53 PHE HD1 H 7.18 . 1 509 53 PHE HD2 H 7.18 . 1 510 53 PHE HE1 H 7.26 . 1 511 53 PHE HE2 H 7.26 . 1 512 53 PHE CA C 61.46 . 1 513 53 PHE CB C 39.68 . 1 514 53 PHE CD1 C 131.52 . 1 515 53 PHE CD2 C 131.52 . 1 516 53 PHE N N 119.26 . 1 517 54 LEU H H 8.64 . 1 518 54 LEU HA H 3.59 . 1 519 54 LEU HB2 H 1.98 . 1 520 54 LEU HB3 H 1.02 . 1 521 54 LEU HG H 2.14 . 1 522 54 LEU HD1 H 0.71 . 1 523 54 LEU HD2 H 0.88 . 1 524 54 LEU CA C 57.71 . 1 525 54 LEU CB C 41.51 . 1 526 54 LEU CG C 26.69 . 1 527 54 LEU CD1 C 26.94 . 1 528 54 LEU CD2 C 21.67 . 1 529 54 LEU N N 117.11 . 1 530 55 LEU H H 8.18 . 1 531 55 LEU HA H 4.07 . 1 532 55 LEU HB2 H 1.95 . 1 533 55 LEU HB3 H 1.47 . 1 534 55 LEU HG H 1.83 . 1 535 55 LEU HD1 H 0.86 . 1 536 55 LEU HD2 H 0.72 . 1 537 55 LEU CA C 57.91 . 1 538 55 LEU CB C 40.73 . 1 539 55 LEU CG C 26.56 . 1 540 55 LEU CD1 C 22.83 . 1 541 55 LEU CD2 C 25.79 . 1 542 55 LEU N N 117.24 . 1 543 56 LEU H H 8.02 . 1 544 56 LEU HA H 4.11 . 1 545 56 LEU HB2 H 1.83 . 1 546 56 LEU HB3 H 1.83 . 1 547 56 LEU HG H 1.69 . 1 548 56 LEU HD2 H 0.94 . 1 549 56 LEU CA C 57.92 . 1 551 56 LEU CG C 26.87 . 1 552 56 LEU CD2 C 24.25 . 1 553 56 LEU N N 124.03 . 1 554 57 LYS H H 7.31 . 1 555 57 LYS HA H 4.21 . 1 556 57 LYS HB2 H 1.59 . 1 557 57 LYS HB3 H 2.00 . 1 558 57 LYS HG2 H 1.49 . 1 559 57 LYS HG3 H 1.49 . 1 560 57 LYS HD2 H 1.56 . 1 561 57 LYS HD3 H 1.56 . 1 562 57 LYS HE2 H 2.95 . 1 563 57 LYS HE3 H 2.95 . 1 564 57 LYS CA C 53.51 . 1 565 57 LYS CB C 31.12 . 1 566 57 LYS CG C 27.07 . 1 567 57 LYS CD C 26.97 . 1 568 57 LYS CE C 42.04 . 1 569 57 LYS N N 115.49 . 1 570 58 GLY H H 7.58 . 1 571 58 GLY HA2 H 4.22 . 1 572 58 GLY HA3 H 3.74 . 1 573 58 GLY CA C 45.44 . 1 574 58 GLY N N 104.92 . 1 575 59 ALA H H 8.01 . 1 576 59 ALA HA H 4.04 . 1 577 59 ALA HB H 1.02 . 1 578 59 ALA CA C 52.71 . 1 579 59 ALA CB C 19.44 . 1 580 59 ALA N N 123.66 . 1 581 60 ASP H H 8.92 . 1 582 60 ASP HA H 4.44 . 1 583 60 ASP HB2 H 2.68 . 1 584 60 ASP HB3 H 2.83 . 1 585 60 ASP CA C 53.83 . 1 586 60 ASP CB C 40.43 . 1 587 60 ASP N N 121.50 . 1 588 61 ILE H H 8.31 . 1 589 61 ILE HA H 3.64 . 1 590 61 ILE HB H 1.66 . 1 591 61 ILE HG12 H 1.19 . 1 592 61 ILE HG13 H 1.33 . 1 593 61 ILE HG2 H 0.76 . 1 594 61 ILE HD1 H 0.88 . 1 595 61 ILE CA C 63.44 . 1 596 61 ILE CB C 38.97 . 1 597 61 ILE CG1 C 30.77 . 1 598 61 ILE CG2 C 15.45 . 1 599 61 ILE CD1 C 16.83 . 1 600 61 ILE N N 128.75 . 1 601 62 ASN H H 8.01 . 1 602 62 ASN HA H 5.01 . 1 603 62 ASN HB2 H 2.67 . 1 604 62 ASN HB3 H 3.08 . 1 605 62 ASN HD22 H 7.09 . 1 606 62 ASN HD21 H 8.11 . 1 607 62 ASN CA C 52.36 . 1 608 62 ASN CB C 40.43 . 1 610 62 ASN ND2 N 67.16 . 1 611 63 ALA H H 6.77 . 1 612 63 ALA HA H 4.41 . 1 613 63 ALA HB H 1.36 . 1 614 63 ALA CA C 50.83 . 1 615 63 ALA CB C 19.24 . 1 616 63 ALA N N 123.09 . 1 617 64 PRO HA H 4.67 . 1 618 64 PRO HB2 H 1.89 . 1 619 64 PRO HB3 H 2.01 . 1 620 64 PRO HG2 H 2.03 . 1 621 64 PRO HG3 H 2.15 . 1 622 64 PRO HD2 H 3.75 . 1 623 64 PRO HD3 H 4.06 . 1 624 64 PRO CA C 61.70 . 1 625 64 PRO CB C 32.31 . 1 626 64 PRO CG C 27.00 . 1 627 64 PRO CD C 50.46 . 1 628 65 ASP H H 7.82 . 1 629 65 ASP HA H 4.49 . 1 630 65 ASP HB2 H 1.07 . 1 631 65 ASP HB3 H 3.09 . 1 632 65 ASP CA C 51.91 . 1 633 65 ASP CB C 40.25 . 1 634 65 ASP N N 119.85 . 1 635 66 LYS H H 7.72 . 1 636 66 LYS HA H 3.98 . 1 637 66 LYS HB2 H 1.73 . 1 638 66 LYS HB3 H 1.58 . 1 639 66 LYS HG2 H 1.17 . 1 640 66 LYS HG3 H 1.17 . 1 641 66 LYS HD2 H 0.94 . 1 642 66 LYS HD3 H 0.94 . 1 643 66 LYS HE2 H 2.85 . 1 644 66 LYS HE3 H 2.85 . 1 645 66 LYS CA C 58.42 . 1 646 66 LYS CB C 31.93 . 1 647 66 LYS CG C 24.17 . 1 648 66 LYS CD C 24.22 . 1 649 66 LYS CE C 41.79 . 1 650 66 LYS N N 115.66 . 1 651 67 HIS H H 8.14 . 1 652 67 HIS HA H 4.67 . 1 653 67 HIS HB2 H 3.49 . 1 654 67 HIS HB3 H 2.96 . 1 655 67 HIS CA C 54.66 . 1 656 67 HIS CB C 29.39 . 1 657 67 HIS N N 117.90 . 1 658 68 HIS H H 7.97 . 1 659 68 HIS HA H 3.90 . 1 660 68 HIS HB2 H 3.56 . 1 661 68 HIS HB3 H 3.47 . 1 662 68 HIS HE1 H 8.58 . 1 663 68 HIS CA C 57.61 . 1 664 68 HIS CB C 26.73 . 1 665 68 HIS CE1 C 120.86 . 1 666 68 HIS N N 110.95 . 1 667 69 ILE H H 8.59 . 1 668 69 ILE HA H 4.06 . 1 669 69 ILE HB H 2.14 . 1 670 69 ILE HG12 H 1.74 . 1 671 69 ILE HG13 H 1.74 . 1 672 69 ILE HG2 H 1.04 . 1 673 69 ILE HD1 H 1.04 . 1 674 69 ILE CA C 62.25 . 1 675 69 ILE CB C 38.31 . 1 676 69 ILE CG1 C 28.91 . 1 677 69 ILE CG2 C 18.69 . 1 678 69 ILE CD1 C 13.34 . 1 680 70 THR H H 6.59 . 1 681 70 THR HA H 4.91 . 1 682 70 THR HB H 4.76 . 1 683 70 THR HG2 H 1.22 . 1 684 70 THR CA C 59.26 . 1 685 70 THR CB C 68.47 . 1 686 70 THR CG2 C 22.89 . 1 687 70 THR N N 115.82 . 1 688 71 PRO HA H 3.76 . 1 689 71 PRO HB2 H 1.69 . 1 690 71 PRO HB3 H 1.69 . 1 691 71 PRO HG3 H 1.46 . 1 692 71 PRO HD2 H 3.76 . 1 693 71 PRO HD3 H 4.20 . 1 694 71 PRO CA C 67.00 . 1 695 71 PRO CB C 31.18 . 1 696 71 PRO CG C 28.92 . 1 697 71 PRO CD C 49.66 . 1 698 72 LEU H H 9.13 . 1 699 72 LEU HA H 3.79 . 1 700 72 LEU HB2 H 1.66 . 1 701 72 LEU HB3 H 1.39 . 1 702 72 LEU HG H 1.29 . 1 703 72 LEU HD1 H 0.72 . 1 704 72 LEU HD2 H 0.72 . 1 705 72 LEU CA C 58.33 . 1 706 72 LEU CB C 41.26 . 1 707 72 LEU CG C 27.34 . 1 708 72 LEU CD1 C 25.88 . 1 709 72 LEU CD2 C 21.68 . 1 710 72 LEU N N 115.23 . 1 711 73 LEU H H 7.18 . 1 712 73 LEU HA H 3.38 . 1 713 73 LEU HB2 H 0.98 . 1 714 73 LEU HB3 H 1.72 . 1 715 73 LEU HG H 1.45 . 1 716 73 LEU HD1 H 1.03 . 1 717 73 LEU HD2 H 0.70 . 1 718 73 LEU CA C 58.15 . 1 719 73 LEU CB C 41.72 . 1 720 73 LEU CG C 27.55 . 1 721 73 LEU CD1 C 25.19 . 1 722 73 LEU CD2 C 21.58 . 1 723 73 LEU N N 117.33 . 1 724 74 SER H H 7.94 . 1 725 74 SER HA H 4.06 . 1 726 74 SER HB2 H 3.97 . 1 727 74 SER HB3 H 3.97 . 1 728 74 SER CA C 62.66 . 1 729 74 SER CB C 63.36 . 1 730 74 SER N N 112.20 . 1 731 75 ALA H H 7.67 . 1 732 75 ALA HA H 4.20 . 1 733 75 ALA HB H 1.35 . 1 734 75 ALA CA C 54.76 . 1 735 75 ALA CB C 18.50 . 1 736 75 ALA N N 120.35 . 1 737 76 VAL H H 8.20 . 1 738 76 VAL HA H 3.36 . 1 739 76 VAL HB H 2.15 . 1 740 76 VAL HG1 H 0.98 . 1 741 76 VAL HG2 H 0.97 . 1 742 76 VAL CA C 66.91 . 1 743 76 VAL CB C 31.34 . 1 744 76 VAL CG1 C 24.32 . 1 745 76 VAL CG2 C 21.08 . 1 746 76 VAL N N 118.38 . 1 747 77 TYR H H 9.24 . 1 748 77 TYR HA H 4.61 . 1 749 77 TYR HB2 H 3.35 . 1 750 77 TYR HB3 H 3.19 . 1 751 77 TYR HD1 H 7.06 . 1 752 77 TYR HD2 H 7.06 . 1 753 77 TYR HE1 H 6.65 . 1 754 77 TYR HE2 H 6.65 . 1 755 77 TYR CA C 57.88 . 1 757 77 TYR CD1 C 130.90 . 1 758 77 TYR CD2 C 130.90 . 1 759 77 TYR CE1 C 117.45 . 1 760 77 TYR CE2 C 117.45 . 1 761 77 TYR N N 120.68 . 1 762 78 GLU H H 6.96 . 1 763 78 GLU HA H 4.45 . 1 764 78 GLU HB2 H 2.16 . 1 765 78 GLU HB3 H 1.62 . 1 766 78 GLU HG2 H 3.08 . 1 767 78 GLU HG3 H 2.54 . 1 768 78 GLU CA C 54.76 . 1 769 78 GLU CB C 30.26 . 1 770 78 GLU CG C 34.86 . 1 771 78 GLU N N 112.21 . 1 772 79 GLY H H 7.77 . 1 773 79 GLY HA2 H 3.46 . 1 774 79 GLY HA3 H 3.91 . 1 775 79 GLY CA C 46.59 . 1 776 79 GLY N N 107.19 . 1 777 80 HIS H H 7.98 . 1 778 80 HIS HA H 5.21 . 1 779 80 HIS HB2 H 3.41 . 1 780 80 HIS HB3 H 3.08 . 1 781 80 HIS HD1 H 7.40 . 9 782 80 HIS HE1 H 8.20 . 1 783 80 HIS CA C 54.01 . 1 784 80 HIS CB C 28.60 . 1 785 80 HIS CD2 C 116.68 . 9 786 80 HIS CE1 C 131.70 . 1 787 80 HIS N N 118.38 . 1 788 81 VAL H H 8.24 . 1 789 81 VAL HA H 3.13 . 1 790 81 VAL HB H 2.12 . 1 791 81 VAL HG1 H 1.06 . 1 792 81 VAL HG2 H 0.88 . 1 793 81 VAL CA C 67.81 . 1 794 81 VAL CB C 32.02 . 1 795 81 VAL CG1 C 21.96 . 1 796 81 VAL CG2 C 21.10 . 1 797 81 VAL N N 126.30 . 1 798 82 SER H H 9.00 . 1 799 82 SER HA H 4.17 . 1 800 82 SER HB2 H 4.02 . 1 801 82 SER HB3 H 4.02 . 1 802 82 SER CA C 61.56 . 1 803 82 SER CB C 61.61 . 1 804 82 SER N N 114.20 . 1 805 83 CYS H H 7.37 . 1 806 83 CYS HA H 4.08 . 1 807 83 CYS HB2 H 2.30 . 1 808 83 CYS HB3 H 3.26 . 1 809 83 CYS CA C 63.31 . 1 810 83 CYS CB C 26.78 . 1 811 83 CYS N N 120.28 . 1 812 84 VAL H H 8.11 . 1 813 84 VAL HA H 3.24 . 1 814 84 VAL HB H 2.34 . 1 815 84 VAL HG1 H 0.84 . 1 816 84 VAL HG2 H 0.89 . 1 817 84 VAL CA C 67.50 . 1 818 84 VAL CB C 30.90 . 1 819 84 VAL CG1 C 21.40 . 1 820 84 VAL CG2 C 24.00 . 1 821 84 VAL N N 121.21 . 1 822 85 LYS H H 8.17 . 1 823 85 LYS HA H 3.76 . 1 824 85 LYS HB2 H 1.97 . 1 825 85 LYS HB3 H 1.80 . 1 826 85 LYS HG2 H 1.46 . 1 827 85 LYS HG3 H 1.46 . 1 828 85 LYS HD2 H 1.70 . 1 829 85 LYS HD3 H 1.70 . 1 830 85 LYS HE2 H 2.94 . 1 831 85 LYS HE3 H 2.94 . 1 832 85 LYS CA C 60.43 . 1 833 85 LYS CB C 32.54 . 1 834 85 LYS CG C 25.21 . 1 835 85 LYS CD C 29.95 . 1 836 85 LYS CE C 41.95 . 1 837 85 LYS N N 117.84 . 1 838 86 LEU H H 7.58 . 1 839 86 LEU HA H 4.13 . 1 840 86 LEU HB2 H 1.76 . 1 841 86 LEU HB3 H 1.76 . 1 842 86 LEU HG H 1.41 . 1 843 86 LEU HD1 H 0.82 . 1 844 86 LEU HD2 H 0.88 . 1 845 86 LEU CA C 57.86 . 1 846 86 LEU CB C 41.34 . 1 847 86 LEU CG C 27.51 . 1 848 86 LEU CD1 C 27.21 . 1 849 86 LEU CD2 C 26.90 . 1 850 86 LEU N N 119.24 . 1 851 87 LEU H H 8.37 . 1 852 87 LEU HA H 3.83 . 1 853 87 LEU HB2 H 1.09 . 1 854 87 LEU HB3 H 1.88 . 1 855 87 LEU HG H 1.87 . 1 856 87 LEU HD1 H 0.54 . 1 857 87 LEU HD2 H 0.78 . 1 858 87 LEU CA C 58.13 . 1 859 87 LEU CB C 40.86 . 1 860 87 LEU CG C 27.01 . 1 861 87 LEU CD1 C 25.71 . 1 862 87 LEU CD2 C 22.91 . 1 863 87 LEU N N 118.35 . 1 864 88 LEU H H 8.60 . 1 865 88 LEU HA H 4.08 . 1 866 88 LEU HB2 H 1.58 . 1 867 88 LEU HB3 H 1.88 . 1 868 88 LEU HG H 1.83 . 1 869 88 LEU HD1 H 0.78 . 1 870 88 LEU HD2 H 0.85 . 1 871 88 LEU CA C 58.08 . 1 872 88 LEU CB C 41.53 . 1 873 88 LEU CG C 26.35 . 1 874 88 LEU CD1 C 27.43 . 1 875 88 LEU CD2 C 22.79 . 1 876 88 LEU N N 118.28 . 1 877 89 SER H H 8.14 . 1 878 89 SER HA H 4.37 . 1 879 89 SER HB2 H 4.11 . 1 880 89 SER HB3 H 4.11 . 1 881 89 SER CA C 61.66 . 1 883 89 SER N N 116.66 . 1 884 90 LYS H H 7.41 . 1 885 90 LYS HA H 4.55 . 1 886 90 LYS HB2 H 2.15 . 1 887 90 LYS HB3 H 1.67 . 1 888 90 LYS HG2 H 1.54 . 1 889 90 LYS HG3 H 1.32 . 1 890 90 LYS HD2 H 1.57 . 1 891 90 LYS HD3 H 1.68 . 1 892 90 LYS HE2 H 2.95 . 1 893 90 LYS HE3 H 2.86 . 1 894 90 LYS CA C 54.29 . 1 895 90 LYS CB C 32.11 . 1 896 90 LYS CG C 24.50 . 1 897 90 LYS CD C 28.12 . 1 898 90 LYS CE C 42.36 . 1 899 90 LYS N N 119.04 . 1 900 91 GLY H H 7.60 . 1 901 91 GLY HA2 H 4.33 . 1 902 91 GLY HA3 H 3.80 . 1 903 91 GLY CA C 45.53 . 1 904 91 GLY N N 104.75 . 1 905 92 ALA H H 8.04 . 1 906 92 ALA HA H 4.02 . 1 907 92 ALA HB H 1.14 . 1 908 92 ALA CA C 52.91 . 1 909 92 ALA CB C 19.65 . 1 910 92 ALA N N 122.83 . 1 911 93 ASP H H 8.88 . 1 912 93 ASP HA H 4.62 . 1 913 93 ASP HB2 H 2.75 . 1 914 93 ASP HB3 H 2.66 . 1 915 93 ASP CA C 53.33 . 1 916 93 ASP CB C 40.16 . 1 917 93 ASP N N 120.36 . 1 918 94 LYS H H 8.94 . 1 919 94 LYS HA H 4.24 . 1 920 94 LYS HB2 H 2.14 . 1 921 94 LYS HB3 H 1.54 . 1 922 94 LYS HG2 H 1.56 . 1 923 94 LYS HG3 H 1.29 . 1 924 94 LYS HD2 H 1.74 . 1 925 94 LYS HD3 H 1.74 . 1 926 94 LYS HE2 H 3.03 . 1 927 94 LYS HE3 H 3.03 . 1 928 94 LYS CA C 56.88 . 1 929 94 LYS CB C 32.74 . 1 930 94 LYS CG C 23.77 . 1 931 94 LYS CD C 27.32 . 1 932 94 LYS CE C 42.06 . 1 933 94 LYS N N 125.90 . 1 934 95 THR H H 9.20 . 1 935 95 THR HA H 4.39 . 1 936 95 THR HB H 4.39 . 1 937 95 THR HG2 H 1.28 . 1 938 95 THR CA C 62.97 . 1 939 95 THR CB C 69.92 . 1 940 95 THR CG2 C 21.50 . 1 941 95 THR N N 116.13 . 1 942 96 VAL H H 6.25 . 1 943 96 VAL HA H 3.74 . 1 944 96 VAL HB H 2.05 . 1 945 96 VAL HG1 H 0.95 . 1 946 96 VAL HG2 H 0.95 . 1 947 96 VAL CA C 63.24 . 1 949 96 VAL CG1 C 21.25 . 1 950 96 VAL CG2 C 21.25 . 1 951 96 VAL N N 118.89 . 1 952 97 LYS H H 8.65 . 1 953 97 LYS HA H 4.13 . 1 954 97 LYS HB2 H 1.52 . 1 955 97 LYS HB3 H 1.75 . 1 956 97 LYS HG2 H 1.27 . 1 957 97 LYS HG3 H 1.27 . 1 958 97 LYS HE2 H 3.06 . 1 959 97 LYS HE3 H 3.06 . 1 960 97 LYS CA C 55.96 . 1 961 97 LYS CB C 34.00 . 1 962 97 LYS CG C 25.96 . 1 963 97 LYS CE C 42.25 . 1 965 98 GLY H H 8.26 . 1 966 98 GLY HA2 H 4.46 . 1 967 98 GLY HA3 H 4.18 . 1 968 98 GLY CA C 44.41 . 1 969 98 GLY N N 107.12 . 1 970 99 PRO HA H 4.41 . 1 971 99 PRO HB2 H 2.08 . 1 972 99 PRO HB3 H 2.59 . 1 973 99 PRO HG2 H 2.06 . 1 974 99 PRO HG3 H 2.26 . 1 975 99 PRO HD2 H 3.62 . 1 976 99 PRO HD3 H 3.92 . 1 977 99 PRO CA C 64.64 . 1 979 99 PRO CG C 27.08 . 1 980 99 PRO CD C 49.67 . 1 981 100 ASP H H 7.99 . 1 982 100 ASP HA H 4.49 . 1 983 100 ASP HB2 H 2.58 . 1 984 100 ASP HB3 H 2.99 . 1 985 100 ASP CA C 52.51 . 1 986 100 ASP CB C 39.91 . 1 987 100 ASP N N 115.90 . 1 988 101 GLY H H 8.33 . 1 989 101 GLY HA2 H 4.24 . 1 990 101 GLY HA3 H 3.65 . 1 991 101 GLY CA C 45.30 . 1 992 101 GLY N N 107.26 . 1 993 102 LEU H H 7.62 . 1 994 102 LEU HA H 4.81 . 1 995 102 LEU HB2 H 1.38 . 1 996 102 LEU HB3 H 1.95 . 1 997 102 LEU HG H 1.35 . 1 998 102 LEU HD1 H 0.76 . 1 999 102 LEU HD2 H 0.72 . 1 1000 102 LEU CA C 54.00 . 1 1001 102 LEU CB C 41.97 . 1 1002 102 LEU CG C 26.69 . 1 1003 102 LEU CD1 C 25.05 . 1 1004 102 LEU CD2 C 22.21 . 1 1005 102 LEU N N 119.26 . 1 1006 103 THR H H 8.92 . 1 1007 103 THR HA H 4.64 . 1 1008 103 THR HB H 4.66 . 1 1009 103 THR HG2 H 1.26 . 1 1010 103 THR CA C 61.04 . 1 1011 103 THR CB C 71.97 . 1 1012 103 THR CG2 C 22.30 . 1 1013 103 THR N N 115.79 . 1 1014 104 ALA H H 9.13 . 1 1015 104 ALA HA H 3.73 . 1 1016 104 ALA HB H 1.34 . 1 1017 104 ALA CA C 55.73 . 1 1018 104 ALA CB C 18.56 . 1 1019 104 ALA N N 121.44 . 1 1020 105 LEU H H 8.26 . 1 1021 105 LEU HA H 3.80 . 1 1022 105 LEU HB2 H 1.52 . 1 1023 105 LEU HB3 H 1.62 . 1 1024 105 LEU HG H 1.32 . 1 1025 105 LEU HD1 H 0.92 . 1 1026 105 LEU HD2 H 0.71 . 1 1027 105 LEU CA C 57.77 . 1 1028 105 LEU CB C 42.08 . 1 1029 105 LEU CG C 27.93 . 1 1030 105 LEU CD1 C 25.75 . 1 1031 105 LEU CD2 C 27.19 . 1 1032 105 LEU N N 114.45 . 1 1033 106 GLU H H 7.03 . 1 1034 106 GLU HA H 4.00 . 1 1035 106 GLU HB2 H 2.10 . 1 1036 106 GLU HB3 H 2.23 . 1 1037 106 GLU HG2 H 2.24 . 1 1038 106 GLU HG3 H 2.24 . 1 1039 106 GLU CA C 57.03 . 1 1040 106 GLU CB C 31.93 . 1 1041 106 GLU CG C 37.22 . 1 1042 106 GLU N N 114.11 . 1 1043 107 ALA H H 8.14 . 1 1044 107 ALA HA H 4.22 . 1 1045 107 ALA HB H 1.57 . 1 1046 107 ALA CA C 52.85 . 1 1047 107 ALA CB C 19.98 . 1 1048 107 ALA N N 119.67 . 1 1049 108 THR H H 7.10 . 1 1050 108 THR HA H 4.63 . 1 1051 108 THR HB H 3.94 . 1 1052 108 THR HG2 H 1.16 . 1 1053 108 THR CA C 60.45 . 1 1054 108 THR CB C 69.79 . 1 1055 108 THR CG2 C 19.25 . 1 1056 108 THR N N 110.56 . 1 1057 109 ASP H H 8.10 . 1 1058 109 ASP HA H 4.85 . 1 1059 109 ASP HB2 H 2.79 . 1 1060 109 ASP HB3 H 2.68 . 1 1061 109 ASP CA C 52.76 . 1 1062 109 ASP CB C 41.21 . 1 1063 109 ASP N N 124.17 . 1 1064 110 ASN H H 8.74 . 1 1065 110 ASN HA H 4.68 . 1 1066 110 ASN HB2 H 2.98 . 1 1067 110 ASN HB3 H 2.75 . 1 1068 110 ASN HD22 H 6.97 . 1 1069 110 ASN HD21 H 7.95 . 1 1070 110 ASN CA C 53.29 . 1 1071 110 ASN CB C 39.40 . 1 1072 110 ASN N N 122.64 . 1 1073 110 ASN ND2 N 65.13 . 1 1074 111 GLN H H 9.29 . 1 1075 111 GLN HA H 3.82 . 1 1076 111 GLN HB2 H 2.15 . 1 1077 111 GLN HB3 H 2.15 . 1 1078 111 GLN HG2 H 2.50 . 1 1079 111 GLN HG3 H 2.55 . 1 1080 111 GLN HE21 H 7.50 . 1 1081 111 GLN HE22 H 6.91 . 1 1082 111 GLN CA C 59.09 . 1 1083 111 GLN CB C 28.17 . 1 1084 111 GLN CG C 33.55 . 1 1085 111 GLN N N 127.97 . 1 1086 111 GLN NE2 N 65.00 . 1 1087 112 ALA H H 8.13 . 1 1088 112 ALA HA H 4.21 . 1 1089 112 ALA HB H 1.52 . 1 1090 112 ALA CA C 54.75 . 1 1091 112 ALA CB C 18.23 . 1 1092 112 ALA N N 121.95 . 1 1093 113 ILE H H 7.76 . 1 1094 113 ILE HA H 3.67 . 1 1095 113 ILE HB H 2.08 . 1 1096 113 ILE HG12 H 0.72 . 1 1097 113 ILE HG13 H 1.80 . 1 1098 113 ILE HG2 H 0.99 . 1 1099 113 ILE HD1 H 0.88 . 1 1100 113 ILE CA C 65.03 . 1 1101 113 ILE CB C 37.25 . 1 1102 113 ILE CG1 C 31.19 . 1 1103 113 ILE CG2 C 19.62 . 1 1104 113 ILE CD1 C 13.14 . 1 1105 113 ILE N N 117.76 . 1 1106 114 LYS H H 8.59 . 1 1107 114 LYS HA H 3.66 . 1 1108 114 LYS HB2 H 1.75 . 1 1109 114 LYS HB3 H 1.75 . 1 1110 114 LYS HG2 H 1.28 . 1 1111 114 LYS HG3 H 1.58 . 1 1112 114 LYS HD2 H 1.57 . 1 1113 114 LYS HD3 H 1.57 . 1 1114 114 LYS HE2 H 2.86 . 1 1115 114 LYS HE3 H 3.01 . 1 1116 114 LYS CA C 60.99 . 1 1117 114 LYS CB C 32.23 . 1 1118 114 LYS CG C 26.24 . 1 1119 114 LYS CD C 29.32 . 1 1120 114 LYS CE C 42.01 . 1 1121 114 LYS N N 119.78 . 1 1122 115 ALA H H 7.69 . 1 1123 115 ALA HA H 4.09 . 1 1124 115 ALA HB H 1.47 . 1 1125 115 ALA CA C 54.58 . 1 1126 115 ALA CB C 17.97 . 1 1127 115 ALA N N 117.03 . 1 1128 116 LEU H H 7.25 . 1 1129 116 LEU HA H 4.15 . 1 1130 116 LEU HB2 H 2.00 . 1 1131 116 LEU HB3 H 1.30 . 1 1132 116 LEU HG H 2.00 . 1 1133 116 LEU HD1 H 0.82 . 1 1134 116 LEU HD2 H 0.88 . 1 1135 116 LEU CA C 56.23 . 1 1136 116 LEU CB C 42.58 . 1 1137 116 LEU CG C 26.09 . 1 1138 116 LEU CD1 C 27.36 . 1 1139 116 LEU CD2 C 22.56 . 1 1140 116 LEU N N 115.61 . 1 1141 117 LEU H H 7.38 . 1 1142 117 LEU HA H 4.13 . 1 1143 117 LEU HB2 H 1.78 . 1 1144 117 LEU HB3 H 1.63 . 1 1145 117 LEU HD1 H 0.91 . 1 1146 117 LEU HD2 H 0.68 . 1 1149 117 LEU CD1 C 24.47 . 1 1150 117 LEU CD2 C 27.34 . 1 1152 118 GLN H H 7.39 . 1 1153 118 GLN HA H 3.93 . 1 1154 118 GLN HB2 H 2.06 . 1 1155 118 GLN HB3 H 2.01 . 1 1156 118 GLN HG2 H 2.45 . 1 1157 118 GLN HG3 H 2.42 . 1 1158 118 GLN HE22 H 6.79 . 1 1159 118 GLN HE21 H 7.32 . 1 1162 118 GLN CG C 34.31 . 1 1164 118 GLN NE2 N 64.50 . 1 stop_ save_