data_7184 #Corrected using PDB structure: 2GVSA # #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 # 12 N HA 4.55 5.69 # 42 G HA 3.96 3.09 # 48 V HA 4.88 3.98 #100 Y HA 3.99 4.76 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 38 C CB 46.11 39.56 # 57 C CB 34.69 42.22 # 97 S CB 69.23 63.02 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 6 T C 178.93 173.40 # 21 R C 173.39 178.71 # 22 L C 173.39 179.08 # 23 L C 173.10 178.44 # 25 K C 173.39 178.42 # 40 A C 173.37 179.08 # 41 D C 173.14 178.50 # 43 K C 173.50 178.92 # 46 K C 173.42 178.57 # 51 D C 172.69 177.75 # 52 A C 173.14 178.61 # 58 A C 172.36 179.99 # 62 E C 174.05 179.67 # 63 K C 172.07 179.23 # 64 Q C 173.28 178.30 # 66 E C 173.38 179.29 # 75 L C 174.51 179.52 # 84 A C 172.02 179.63 # 86 L C 173.42 179.02 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 48 V N 110.67 120.81 # 82 V N 19.35 118.16 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 96 Y H 9.39 6.94 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.05 2.36 2.33 1.76 -1.05 -0.23 # #bmr7184.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr7184.str file): #HA CA CB CO N HN #N/A +2.34 +2.34 +1.76 -1.05 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.21 +/-0.21 +/-0.45 +/-0.41 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.703 0.941 0.985 -0.704 0.229 0.342 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.161 1.075 1.003 1.697 2.078 0.376 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of CSPsg4 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomaselli S. . . 2 Crescenzi O. . . 3 Sanfelice D. . . 4 Ab E. . . 5 Tancredi T. . . 6 Picone D. . . stop_ _BMRB_accession_number 7184 _BMRB_flat_file_name bmr7184.str _Entry_type new _Submission_date 2006-06-21 _Accession_date 2006-07-14 _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' 604 '13C chemical shifts' 438 '15N chemical shifts' 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-10-17 update author "chemical shift data updated" 2006-10-11 original author "original release" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structure of a chemosensory protein from the desert locust Schistocerca gregaria ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 16939212 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomaselli S. . . 2 Crescenzi O. . . 3 Sanfelice D. . . 4 Ab E. . . 5 Wechselberger R. . . 6 Angeli S. . . 7 Scaloni A. . . 8 Boelens R. . . 9 Tancredi T. . . 10 Pelosi P. . . 11 Picone D. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 35 _Page_first 10606 _Page_last 10613 _Year 2006 loop_ _Keyword alpha-coil stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name "chemosensory protein CSP-sg4" _Abbreviation_common "chemosensory protein CSP-sg4" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "chemosensory protein CSP-sg4" $CSP-sg4 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all disulfide bound" loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 2GVS ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_CSP-sg4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "chemosensory protein CSP-sg4" _Name_variant . _Abbreviation_common "chemosensory protein CSP-sg4" _Mol_thiol_state "all disulfide bound" ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; EEKYTTKYDNVNLDEILAND RLLNKYVQCLLEDDESNCTA DGKELKSVIPDALSNECAKC NEKQKEGTKKVLKHLINHKP DVWAQLKAKYDPDGTYSKKY EDREKELHQ ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLU 3 LYS 4 TYR 5 THR 6 THR 7 LYS 8 TYR 9 ASP 10 ASN 11 VAL 12 ASN 13 LEU 14 ASP 15 GLU 16 ILE 17 LEU 18 ALA 19 ASN 20 ASP 21 ARG 22 LEU 23 LEU 24 ASN 25 LYS 26 TYR 27 VAL 28 GLN 29 CYS 30 LEU 31 LEU 32 GLU 33 ASP 34 ASP 35 GLU 36 SER 37 ASN 38 CYS 39 THR 40 ALA 41 ASP 42 GLY 43 LYS 44 GLU 45 LEU 46 LYS 47 SER 48 VAL 49 ILE 50 PRO 51 ASP 52 ALA 53 LEU 54 SER 55 ASN 56 GLU 57 CYS 58 ALA 59 LYS 60 CYS 61 ASN 62 GLU 63 LYS 64 GLN 65 LYS 66 GLU 67 GLY 68 THR 69 LYS 70 LYS 71 VAL 72 LEU 73 LYS 74 HIS 75 LEU 76 ILE 77 ASN 78 HIS 79 LYS 80 PRO 81 ASP 82 VAL 83 TRP 84 ALA 85 GLN 86 LEU 87 LYS 88 ALA 89 LYS 90 TYR 91 ASP 92 PRO 93 ASP 94 GLY 95 THR 96 TYR 97 SER 98 LYS 99 LYS 100 TYR 101 GLU 102 ASP 103 ARG 104 GLU 105 LYS 106 GLU 107 LEU 108 HIS 109 GLN stop_ _Sequence_homology_query_date 2006-10-26 _Sequence_homology_query_revised_last_date 2006-10-19 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 GenBank AAC25402.1 "chemosensory protein CSP-sg4[Schistocerca gregaria]" 100.00 109 100 100 10e-60 GenBank AAC25403.1 "chemosensory protein CSP-sg5[Schistocerca gregaria]" 100.00 109 98 98 2e-58 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "chemosensory protein CSP-sg4" 29 CYS SG "chemosensory protein CSP-sg4" 38 CYS SG single disulfide "chemosensory protein CSP-sg4" 57 CYS SG "chemosensory protein CSP-sg4" 60 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CSP-sg4 "desert locust" 7010 Eukaryota Metazoa Schistocerca gregaria 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 $CSP-sg4 "recombinant technology" . . . . . 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 $CSP-sg4 1.2 mM "[U-13C; U-15N]" "phosphate buffer" 50 mM . D2O 5 % . H2O 95 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task collection stop_ save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version linux loop_ _Task processing stop_ _Details "Delaglio et al." save_ save_nmrview _Saveframe_category software _Name nmrview _Version 5.0.4 loop_ _Task "data analysis" stop_ _Details "Johnson et al." save_ save_cyana _Saveframe_category software _Name cyana _Version 2.0 loop_ _Task "structure solution" stop_ save_ save_amber _Saveframe_category software _Name amber _Version 99 loop_ _Task refinement stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D 13C-separated NOESY 3D 15N-separated NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . pH temperature 300 . K 'ionic strength' 50 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H2O H 1 protons ppm 4.81616 internal direct . . . 1.0 H2O N 15 protons ppm . internal indirect . . . 0.251449530 H2O C 13 protons ppm . internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_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 _Mol_system_component_name "chemosensory protein CSP-sg4" 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 1 GLU HA H 4.37 . 1 2 1 GLU N N 114.17 . 1 3 2 GLU H H 8.64 . 1 4 2 GLU HA H 4.27 . 1 5 2 GLU HB2 H 1.94 . 2 6 2 GLU HB3 H 2.00 . 2 7 2 GLU HG2 H 2.32 . 2 8 2 GLU HG3 H 2.24 . 2 9 2 GLU C C 176.27 . 1 10 2 GLU CA C 56.34 . 1 11 2 GLU CB C 30.04 . 1 12 2 GLU CG C 35.94 . 1 13 2 GLU N N 123.07 . 1 14 3 LYS H H 8.37 . 1 15 3 LYS HA H 4.30 . 1 16 3 LYS HB2 H 1.73 . 2 17 3 LYS HG2 H 1.66 . 2 18 3 LYS HD2 H 1.32 . 2 19 3 LYS HE2 H 2.98 . 2 20 3 LYS CA C 56.14 . 1 21 3 LYS CB C 32.84 . 1 22 3 LYS CG C 28.81 . 1 23 3 LYS CD C 24.42 . 1 24 3 LYS CE C 41.76 . 1 25 3 LYS N N 121.88 . 1 26 4 TYR H H 8.28 . 1 27 4 TYR HA H 4.66 . 1 28 4 TYR HB2 H 3.00 . 2 29 4 TYR HB3 H 3.12 . 2 30 4 TYR HD1 H 7.13 . 3 31 4 TYR HE1 H 6.84 . 3 32 4 TYR CA C 57.44 . 1 33 4 TYR CB C 38.54 . 1 34 4 TYR N N 121.09 . 1 35 5 THR H H 8.00 . 1 36 5 THR HA H 4.39 . 1 37 5 THR HB H 4.12 . 1 38 5 THR HG2 H 1.17 . 1 39 5 THR C C 173.71 . 1 40 5 THR N N 116.82 . 1 41 6 THR H H 8.38 . 1 42 6 THR HA H 4.23 . 1 43 6 THR HB H 4.08 . 1 44 6 THR HG2 H 1.16 . 1 45 6 THR C C 178.93 . 1 46 6 THR CA C 62.51 . 1 47 6 THR CB C 68.84 . 1 48 6 THR CG2 C 22.44 . 1 49 6 THR N N 119.25 . 1 50 7 LYS H H 8.36 . 1 51 7 LYS HA H 4.70 . 1 52 7 LYS HB2 H 1.37 . 2 53 7 LYS HB3 H 1.65 . 2 54 7 LYS HG2 H 1.12 . 2 55 7 LYS HG3 H 1.39 . 2 56 7 LYS HD2 H 1.46 . 2 57 7 LYS HD3 H 1.56 . 2 58 7 LYS HE2 H 2.92 . 2 59 7 LYS C C 177.23 . 1 60 7 LYS CA C 55.34 . 1 61 7 LYS CB C 34.74 . 1 62 7 LYS CG C 24.84 . 1 63 7 LYS CD C 29.24 . 1 64 7 LYS CE C 41.94 . 1 65 7 LYS N N 124.70 . 1 66 8 TYR H H 8.66 . 1 67 8 TYR HA H 4.84 . 1 68 8 TYR HB2 H 2.73 . 2 69 8 TYR HB3 H 2.81 . 2 70 8 TYR HD1 H 6.63 . 3 71 8 TYR HE1 H 6.83 . 3 72 8 TYR CA C 56.74 . 1 73 8 TYR CB C 39.04 . 1 74 8 TYR N N 121.15 . 1 75 10 ASN H H 8.67 . 1 76 10 ASN HA H 4.29 . 1 77 10 ASN HB2 H 2.94 . 2 78 10 ASN HB3 H 3.14 . 2 79 10 ASN HD21 H 6.93 . 2 80 10 ASN HD22 H 7.59 . 2 81 10 ASN C C 176.01 . 1 82 10 ASN CA C 54.34 . 1 83 10 ASN CB C 38.27 . 1 84 10 ASN N N 109.39 . 1 85 10 ASN ND2 N 113.54 . 1 86 11 VAL H H 8.20 . 1 87 11 VAL HA H 4.32 . 1 88 11 VAL HB H 2.14 . 1 89 11 VAL HG1 H 1.07 . 1 90 11 VAL HG2 H 1.00 . 1 91 11 VAL C C 177.65 . 1 92 11 VAL CA C 60.80 . 1 93 11 VAL CB C 33.64 . 1 94 11 VAL CG1 C 20.74 . 1 95 11 VAL CG2 C 21.54 . 1 96 11 VAL N N 120.97 . 1 97 12 ASN H H 8.79 . 1 98 12 ASN HA H 4.60 . 1 99 12 ASN HB2 H 2.85 . 2 100 12 ASN HB3 H 2.92 . 2 101 12 ASN HD21 H 7.78 . 2 102 12 ASN HD22 H 7.11 . 2 103 12 ASN C C 175.64 . 1 104 12 ASN CA C 53.57 . 1 105 12 ASN CB C 38.24 . 1 106 12 ASN N N 124.16 . 1 107 12 ASN ND2 N 113.60 . 1 108 13 LEU H H 8.79 . 1 109 13 LEU HA H 3.93 . 1 110 13 LEU HB2 H 1.37 . 2 111 13 LEU HB3 H 1.62 . 2 112 13 LEU HG H 1.43 . 1 113 13 LEU HD1 H 0.70 . 2 114 13 LEU HD2 H 0.52 . 2 115 13 LEU C C 175.06 . 1 116 13 LEU CA C 57.55 . 1 117 13 LEU CB C 41.44 . 1 118 13 LEU CG C 26.13 . 1 119 13 LEU CD1 C 25.42 . 1 120 13 LEU CD2 C 22.14 . 1 121 13 LEU N N 125.88 . 1 122 14 ASP H H 8.40 . 1 123 14 ASP HA H 4.21 . 1 124 14 ASP HB2 H 2.58 . 2 125 14 ASP HB3 H 2.61 . 2 126 14 ASP C C 173.64 . 1 127 14 ASP CA C 57.20 . 1 128 14 ASP CB C 39.33 . 1 129 14 ASP N N 115.52 . 1 130 15 GLU H H 7.43 . 1 131 15 GLU HA H 4.07 . 1 132 15 GLU HB2 H 2.37 . 2 133 15 GLU HG2 H 2.24 . 2 134 15 GLU HG3 H 2.31 . 2 135 15 GLU C C 173.81 . 1 136 15 GLU CA C 58.31 . 1 137 15 GLU CB C 29.24 . 1 138 15 GLU CG C 36.04 . 1 139 15 GLU N N 118.91 . 1 140 16 ILE H H 7.43 . 1 141 16 ILE HA H 3.67 . 1 142 16 ILE HB H 1.92 . 1 143 16 ILE HG12 H 0.96 . 2 144 16 ILE HG13 H 1.73 . 2 145 16 ILE HD1 H 0.54 . 1 146 16 ILE C C 175.95 . 1 147 16 ILE CA C 64.69 . 1 148 16 ILE CB C 37.39 . 1 149 16 ILE CG1 C 28.64 . 2 150 16 ILE CD1 C 16.64 . 1 151 16 ILE N N 120.10 . 1 152 17 LEU H H 7.65 . 1 153 17 LEU HA H 3.59 . 1 154 17 LEU HB2 H 1.51 . 2 155 17 LEU HG H 1.67 . 1 156 17 LEU HD1 H 0.53 . 2 157 17 LEU HD2 H 0.70 . 2 158 17 LEU C C 175.52 . 1 159 17 LEU CA C 56.19 . 1 160 17 LEU CB C 40.14 . 1 161 17 LEU CG C 25.64 . 1 162 17 LEU CD1 C 22.24 . 1 163 17 LEU CD2 C 21.72 . 1 164 17 LEU N N 112.16 . 1 165 18 ALA H H 6.91 . 1 166 18 ALA HA H 4.30 . 1 167 18 ALA HB H 1.46 . 1 168 18 ALA C C 175.92 . 1 169 18 ALA CA C 51.48 . 1 170 18 ALA CB C 19.24 . 1 171 18 ALA N N 115.47 . 1 172 19 ASN H H 7.49 . 1 173 19 ASN HA H 5.02 . 1 174 19 ASN HB2 H 2.81 . 2 175 19 ASN HB3 H 3.06 . 2 176 19 ASN HD21 H 7.01 . 2 177 19 ASN HD22 H 8.01 . 2 178 19 ASN C C 178.35 . 1 179 19 ASN CA C 51.21 . 1 180 19 ASN CB C 39.84 . 1 181 19 ASN N N 117.84 . 1 182 19 ASN ND2 N 113.74 . 1 183 20 ASP H H 9.04 . 1 184 20 ASP HA H 4.43 . 1 185 20 ASP HB2 H 2.73 . 2 186 20 ASP C C 175.12 . 1 187 20 ASP CA C 57.91 . 1 188 20 ASP CB C 40.41 . 1 189 20 ASP N N 125.68 . 1 190 21 ARG H H 8.21 . 1 191 21 ARG HA H 4.16 . 1 192 21 ARG HB2 H 1.95 . 2 193 21 ARG HB3 H 1.98 . 2 194 21 ARG HG2 H 1.69 . 2 195 21 ARG HG3 H 1.80 . 2 196 21 ARG HD2 H 3.31 . 2 197 21 ARG C C 173.39 . 1 198 21 ARG CA C 58.98 . 1 199 21 ARG CB C 29.35 . 1 200 21 ARG CG C 27.20 . 1 201 21 ARG CD C 42.63 . 1 202 21 ARG N N 116.79 . 1 203 22 LEU H H 7.65 . 1 204 22 LEU HA H 4.39 . 1 205 22 LEU HB2 H 1.65 . 2 206 22 LEU HB3 H 2.28 . 2 207 22 LEU HG H 1.73 . 1 208 22 LEU HD1 H 1.06 . 2 209 22 LEU HD2 H 0.98 . 2 210 22 LEU C C 173.39 . 1 211 22 LEU CA C 56.50 . 1 212 22 LEU CB C 42.24 . 1 213 22 LEU CG C 26.94 . 1 214 22 LEU CD1 C 24.64 . 1 215 22 LEU CD2 C 22.35 . 2 216 22 LEU N N 118.68 . 1 217 23 LEU H H 8.82 . 1 218 23 LEU HA H 4.04 . 1 219 23 LEU HB2 H 1.93 . 2 220 23 LEU HB3 H 2.07 . 2 221 23 LEU HG H 1.72 . 1 222 23 LEU HD1 H 0.90 . 2 223 23 LEU HD2 H 1.06 . 2 224 23 LEU C C 173.10 . 1 225 23 LEU CA C 58.27 . 1 226 23 LEU CB C 39.76 . 1 227 23 LEU CG C 26.85 . 1 228 23 LEU CD1 C 24.34 . 1 229 23 LEU CD2 C 22.44 . 1 230 23 LEU N N 121.28 . 1 231 24 ASN H H 8.65 . 1 232 24 ASN HA H 4.50 . 1 233 24 ASN HB2 H 2.85 . 2 234 24 ASN HB3 H 3.02 . 2 235 24 ASN HD21 H 6.89 . 2 236 24 ASN HD22 H 7.55 . 2 237 24 ASN C C 173.48 . 1 238 24 ASN CA C 55.78 . 1 239 24 ASN CB C 37.54 . 1 240 24 ASN N N 115.25 . 1 241 24 ASN ND2 N 111.90 . 1 242 25 LYS H H 7.53 . 1 243 25 LYS HA H 4.24 . 1 244 25 LYS HB2 H 1.93 . 2 245 25 LYS HB3 H 1.98 . 2 246 25 LYS HG2 H 1.52 . 2 247 25 LYS HG3 H 1.59 . 2 248 25 LYS HD2 H 1.74 . 2 249 25 LYS HE2 H 2.99 . 2 250 25 LYS C C 173.39 . 1 251 25 LYS CA C 58.62 . 1 252 25 LYS CB C 31.49 . 1 253 25 LYS CG C 24.35 . 1 254 25 LYS CD C 28.99 . 1 255 25 LYS CE C 41.49 . 1 256 25 LYS N N 118.66 . 1 257 26 TYR H H 7.69 . 1 258 26 TYR HA H 4.14 . 1 259 26 TYR HB2 H 2.80 . 2 260 26 TYR HB3 H 3.14 . 2 261 26 TYR HD1 H 7.14 . 3 262 26 TYR HE1 H 6.64 . 3 263 26 TYR C C 174.47 . 1 264 26 TYR CA C 61.68 . 1 265 26 TYR CB C 37.20 . 1 266 26 TYR N N 119.55 . 1 267 27 VAL H H 8.56 . 1 268 27 VAL HA H 3.44 . 1 269 27 VAL HB H 2.30 . 1 270 27 VAL HG1 H 1.06 . 1 271 27 VAL HG2 H 1.14 . 1 272 27 VAL C C 175.67 . 1 273 27 VAL CA C 67.34 . 1 274 27 VAL CB C 31.13 . 1 275 27 VAL CG1 C 23.04 . 1 276 27 VAL CG2 C 22.64 . 1 277 27 VAL N N 119.34 . 1 278 28 GLN H H 8.21 . 1 279 28 GLN HA H 3.98 . 1 280 28 GLN HB2 H 2.12 . 2 281 28 GLN HB3 H 2.17 . 2 282 28 GLN HG2 H 2.29 . 2 283 28 GLN HG3 H 2.50 . 2 284 28 GLN HE21 H 7.78 . 2 285 28 GLN HE22 H 6.75 . 2 286 28 GLN C C 175.46 . 1 287 28 GLN CA C 59.34 . 1 288 28 GLN CB C 27.20 . 1 289 28 GLN CG C 33.24 . 1 290 28 GLN N N 118.20 . 1 291 28 GLN NE2 N 111.78 . 1 292 29 CYS H H 7.02 . 1 293 29 CYS HA H 4.45 . 1 294 29 CYS HB2 H 3.34 . 2 295 29 CYS HB3 H 3.37 . 2 296 29 CYS C C 175.46 . 1 297 29 CYS CA C 57.91 . 1 298 29 CYS CB C 40.08 . 1 299 29 CYS N N 113.46 . 1 300 30 LEU H H 7.81 . 1 301 30 LEU HA H 4.07 . 1 302 30 LEU HB2 H 1.45 . 2 303 30 LEU HG H 2.22 . 1 304 30 LEU HD1 H 0.79 . 2 305 30 LEU HD2 H 0.82 . 2 306 30 LEU C C 173.16 . 1 307 30 LEU CA C 57.55 . 1 308 30 LEU CB C 41.78 . 1 309 30 LEU CG C 26.14 . 1 310 30 LEU CD1 C 22.14 . 1 311 30 LEU CD2 C 23.64 . 1 312 30 LEU N N 113.81 . 1 313 31 LEU H H 8.34 . 1 314 31 LEU HA H 4.28 . 1 315 31 LEU HB2 H 1.59 . 2 316 31 LEU HB3 H 1.94 . 2 317 31 LEU HG H 1.88 . 1 318 31 LEU HD1 H 0.90 . 2 319 31 LEU HD2 H 0.81 . 2 320 31 LEU C C 174.32 . 1 321 31 LEU CA C 55.77 . 1 322 31 LEU CB C 42.37 . 1 323 31 LEU CG C 27.20 . 1 324 31 LEU CD1 C 25.42 . 1 325 31 LEU CD2 C 22.24 . 1 326 31 LEU N N 117.34 . 1 327 32 GLU H H 7.84 . 1 328 32 GLU HA H 4.32 . 1 329 32 GLU HB2 H 2.15 . 2 330 32 GLU HB3 H 2.23 . 2 331 32 GLU HG2 H 2.39 . 2 332 32 GLU HG3 H 2.93 . 2 333 32 GLU C C 174.86 . 1 334 32 GLU CA C 56.48 . 1 335 32 GLU CB C 30.43 . 1 336 32 GLU CG C 37.92 . 1 337 32 GLU N N 119.44 . 1 338 33 ASP H H 8.87 . 1 339 33 ASP HA H 4.55 . 1 340 33 ASP HB2 H 2.63 . 2 341 33 ASP HB3 H 2.88 . 2 342 33 ASP C C 176.90 . 1 343 33 ASP CA C 55.07 . 1 344 33 ASP CB C 40.41 . 1 345 33 ASP N N 120.02 . 1 346 34 ASP H H 7.53 . 1 347 34 ASP HA H 4.76 . 1 348 34 ASP HB2 H 2.71 . 2 349 34 ASP HB3 H 3.13 . 2 350 34 ASP C C 175.99 . 1 351 34 ASP CA C 52.20 . 1 352 34 ASP CB C 41.84 . 1 353 34 ASP N N 116.29 . 1 354 35 GLU H H 8.25 . 1 355 35 GLU HA H 4.74 . 1 356 35 GLU HB2 H 2.07 . 2 357 35 GLU HB3 H 2.23 . 2 358 35 GLU HG2 H 2.19 . 2 359 35 GLU HG3 H 2.46 . 2 360 35 GLU C C 174.55 . 1 361 35 GLU CA C 56.26 . 1 362 35 GLU CB C 28.99 . 1 363 35 GLU CG C 38.63 . 1 364 35 GLU N N 116.36 . 1 365 36 SER H H 8.69 . 1 366 36 SER HA H 4.05 . 1 367 36 SER HB2 H 3.90 . 2 368 36 SER C C 177.12 . 1 369 36 SER CA C 62.14 . 1 370 36 SER CB C 62.44 . 1 371 36 SER N N 119.44 . 1 372 37 ASN H H 9.53 . 1 373 37 ASN HA H 5.06 . 1 374 37 ASN HB2 H 2.46 . 2 375 37 ASN HB3 H 2.89 . 2 376 37 ASN HD21 H 9.43 . 2 377 37 ASN HD22 H 6.80 . 2 378 37 ASN C C 178.06 . 1 379 37 ASN CA C 52.55 . 1 380 37 ASN CB C 38.63 . 1 381 37 ASN N N 118.35 . 1 382 37 ASN ND2 N 121.25 . 1 383 38 CYS H H 7.45 . 1 384 38 CYS HA H 4.47 . 1 385 38 CYS HB2 H 3.11 . 2 386 38 CYS HB3 H 3.30 . 2 387 38 CYS C C 176.59 . 1 388 38 CYS CA C 54.47 . 1 389 38 CYS CB C 46.13 . 1 390 38 CYS N N 115.25 . 1 391 39 THR H H 8.46 . 1 392 39 THR HA H 4.50 . 1 393 39 THR HB H 4.79 . 1 394 39 THR HG2 H 1.23 . 1 395 39 THR C C 177.41 . 1 396 39 THR CA C 60.21 . 1 397 39 THR CB C 69.69 . 1 398 39 THR CG2 C 21.44 . 1 399 39 THR N N 114.21 . 1 400 40 ALA H H 9.05 . 1 401 40 ALA HA H 4.12 . 1 402 40 ALA HB H 1.57 . 1 403 40 ALA C C 173.37 . 1 404 40 ALA CA C 56.17 . 1 405 40 ALA CB C 17.64 . 1 406 40 ALA N N 123.81 . 1 407 41 ASP H H 9.22 . 1 408 41 ASP HA H 4.74 . 1 409 41 ASP HB2 H 2.53 . 2 410 41 ASP HB3 H 2.94 . 2 411 41 ASP C C 173.14 . 1 412 41 ASP CA C 56.34 . 1 413 41 ASP CB C 38.63 . 1 414 41 ASP N N 117.08 . 1 415 42 GLY H H 8.34 . 1 416 42 GLY HA2 H 3.88 . 2 417 42 GLY HA3 H 4.14 . 2 418 42 GLY C C 177.19 . 1 419 42 GLY CA C 47.20 . 1 420 42 GLY N N 111.23 . 1 421 43 LYS H H 8.66 . 1 422 43 LYS HA H 3.94 . 1 423 43 LYS HB2 H 1.99 . 2 424 43 LYS HG2 H 1.64 . 2 425 43 LYS HG3 H 1.74 . 2 426 43 LYS HD2 H 1.40 . 2 427 43 LYS HE2 H 2.98 . 2 428 43 LYS C C 173.50 . 1 429 43 LYS CA C 60.05 . 1 430 43 LYS CB C 32.20 . 1 431 43 LYS CG C 28.99 . 1 432 43 LYS CD C 24.64 . 1 433 43 LYS CE C 41.50 . 1 434 43 LYS N N 121.19 . 1 435 44 GLU H H 7.52 . 1 436 44 GLU HA H 4.12 . 1 437 44 GLU HB2 H 2.16 . 2 438 44 GLU HB3 H 2.24 . 2 439 44 GLU HG2 H 2.44 . 2 440 44 GLU C C 173.48 . 1 441 44 GLU CA C 58.84 . 1 442 44 GLU CB C 29.35 . 1 443 44 GLU CG C 36.49 . 1 444 44 GLU N N 119.47 . 1 445 45 LEU H H 7.98 . 1 446 45 LEU HA H 4.07 . 1 447 45 LEU HB2 H 1.83 . 2 448 45 LEU HB3 H 1.99 . 2 449 45 LEU HG H 1.67 . 1 450 45 LEU HD1 H 0.84 . 2 451 45 LEU HD2 H 0.87 . 2 452 45 LEU C C 174.96 . 1 453 45 LEU CA C 57.55 . 1 454 45 LEU CB C 41.49 . 1 455 45 LEU CG C 28.99 . 1 456 45 LEU CD1 C 24.64 . 1 457 45 LEU CD2 C 23.44 . 1 458 45 LEU N N 120.78 . 1 459 46 LYS H H 8.45 . 1 460 46 LYS HA H 3.67 . 1 461 46 LYS HB2 H 1.93 . 2 462 46 LYS HB3 H 2.07 . 2 463 46 LYS HG2 H 1.56 . 2 464 46 LYS HG3 H 1.54 . 2 465 46 LYS HD2 H 1.75 . 2 466 46 LYS HE2 H 3.02 . 2 467 46 LYS C C 173.42 . 1 468 46 LYS CA C 60.05 . 1 469 46 LYS CB C 34.64 . 1 470 46 LYS CG C 25.42 . 1 471 46 LYS CD C 28.99 . 1 472 46 LYS CE C 41.49 . 1 473 46 LYS N N 117.89 . 1 474 47 SER H H 7.84 . 1 475 47 SER HA H 4.32 . 1 476 47 SER HB2 H 4.12 . 2 477 47 SER C C 173.71 . 1 478 47 SER CA C 60.77 . 1 479 47 SER CB C 63.01 . 1 480 47 SER N N 110.40 . 1 481 48 VAL H H 7.42 . 1 482 48 VAL HA H 4.94 . 1 483 48 VAL HB H 2.67 . 1 484 48 VAL HG1 H 0.94 . 1 485 48 VAL HG2 H 0.97 . 1 486 48 VAL C C 173.74 . 1 487 48 VAL CA C 60.77 . 1 488 48 VAL CB C 31.84 . 1 489 48 VAL CG1 C 21.34 . 1 490 48 VAL CG2 C 19.54 . 1 491 48 VAL N N 110.67 . 1 492 49 ILE H H 7.45 . 1 493 49 ILE HA H 3.82 . 1 494 49 ILE HB H 1.78 . 1 495 49 ILE HG12 H 1.71 . 2 496 49 ILE HG13 H 1.28 . 4 497 49 ILE HG2 H 0.25 . 1 498 49 ILE HD1 H 0.57 . 1 499 49 ILE CA C 63.98 . 1 500 49 ILE CB C 33.21 . 1 501 49 ILE CG1 C 27.20 . 2 502 49 ILE CG2 C 17.74 . 1 503 49 ILE CD1 C 16.24 . 1 504 49 ILE N N 122.59 . 1 505 50 PRO HA H 4.17 . 1 506 50 PRO HB2 H 2.03 . 2 507 50 PRO HB3 H 2.57 . 2 508 50 PRO HG2 H 2.15 . 2 509 50 PRO HG3 H 2.39 . 2 510 50 PRO HD2 H 3.64 . 2 511 50 PRO C C 173.14 . 1 512 50 PRO CA C 66.12 . 1 513 50 PRO CB C 30.50 . 1 514 50 PRO CG C 28.99 . 1 515 50 PRO CD C 49.70 . 1 516 51 ASP H H 7.36 . 1 517 51 ASP HA H 4.41 . 1 518 51 ASP HB2 H 2.71 . 2 519 51 ASP HB3 H 2.77 . 2 520 51 ASP C C 172.69 . 1 521 51 ASP CA C 56.29 . 1 522 51 ASP CB C 42.20 . 1 523 51 ASP N N 117.67 . 1 524 52 ALA H H 8.82 . 1 525 52 ALA HA H 4.03 . 1 526 52 ALA HB H 1.47 . 1 527 52 ALA C C 173.14 . 1 528 52 ALA CA C 55.41 . 1 529 52 ALA CB C 17.54 . 1 530 52 ALA N N 124.62 . 1 531 53 LEU H H 7.81 . 1 532 53 LEU HA H 4.06 . 1 533 53 LEU HB2 H 1.22 . 2 534 53 LEU HB3 H 1.86 . 2 535 53 LEU HG H 1.68 . 1 536 53 LEU HD1 H 0.58 . 2 537 53 LEU HD2 H 0.83 . 2 538 53 LEU C C 175.03 . 1 539 53 LEU CA C 56.48 . 1 540 53 LEU CB C 41.94 . 1 541 53 LEU CG C 25.78 . 1 542 53 LEU CD1 C 22.94 . 1 543 53 LEU CD2 C 22.14 . 1 544 53 LEU N N 113.81 . 1 545 54 SER H H 8.07 . 1 546 54 SER HA H 3.78 . 1 547 54 SER HB2 H 3.26 . 2 548 54 SER HB3 H 3.46 . 2 549 54 SER C C 176.32 . 1 550 54 SER CA C 59.34 . 1 551 54 SER CB C 63.62 . 1 552 54 SER N N 110.71 . 1 553 55 ASN H H 8.34 . 1 554 55 ASN HA H 5.14 . 1 555 55 ASN HB2 H 2.86 . 2 556 55 ASN HB3 H 2.98 . 2 557 55 ASN HD21 H 7.88 . 2 558 55 ASN HD22 H 7.17 . 2 559 55 ASN C C 176.21 . 1 560 55 ASN CA C 52.20 . 1 561 55 ASN CB C 38.74 . 1 562 55 ASN N N 118.76 . 1 563 55 ASN ND2 N 116.24 . 1 564 56 GLU H H 8.13 . 1 565 56 GLU HA H 4.17 . 1 566 56 GLU HB2 H 2.16 . 2 567 56 GLU HB3 H 2.33 . 2 568 56 GLU HG2 H 2.27 . 2 569 56 GLU C C 176.48 . 1 570 56 GLU CA C 57.19 . 1 571 56 GLU CB C 26.90 . 1 572 56 GLU CG C 36.84 . 1 573 56 GLU N N 115.13 . 1 574 57 CYS H H 8.77 . 1 575 57 CYS HA H 4.10 . 1 576 57 CYS HB2 H 2.62 . 2 577 57 CYS C C 175.73 . 1 578 57 CYS CA C 57.91 . 1 579 57 CYS CB C 34.70 . 1 580 57 CYS N N 119.49 . 1 581 58 ALA H H 7.80 . 1 582 58 ALA HA H 4.04 . 1 583 58 ALA HB H 1.51 . 1 584 58 ALA C C 172.36 . 1 585 58 ALA CA C 55.07 . 1 586 58 ALA CB C 18.24 . 1 587 58 ALA N N 121.14 . 1 588 59 LYS H H 9.35 . 1 589 59 LYS HA H 4.50 . 1 590 59 LYS HB2 H 1.68 . 2 591 59 LYS HB3 H 2.02 . 2 592 59 LYS HG2 H 1.41 . 2 593 59 LYS HD2 H 1.70 . 2 594 59 LYS HE2 H 3.00 . 2 595 59 LYS C C 176.26 . 1 596 59 LYS CA C 54.74 . 1 597 59 LYS CB C 31.14 . 1 598 59 LYS CG C 24.64 . 1 599 59 LYS CD C 28.67 . 1 600 59 LYS CE C 41.49 . 1 601 59 LYS N N 114.89 . 1 602 60 CYS H H 7.61 . 1 603 60 CYS HA H 4.37 . 1 604 60 CYS HB2 H 3.58 . 2 605 60 CYS HB3 H 3.30 . 2 606 60 CYS C C 178.37 . 1 607 60 CYS CA C 53.34 . 1 608 60 CYS CB C 40.04 . 1 609 60 CYS N N 118.96 . 1 610 61 ASN H H 8.54 . 1 611 61 ASN HA H 4.79 . 1 612 61 ASN HB2 H 2.97 . 2 613 61 ASN HB3 H 3.38 . 2 614 61 ASN HD21 H 7.48 . 2 615 61 ASN HD22 H 7.09 . 2 616 61 ASN C C 177.32 . 1 617 61 ASN CA C 51.54 . 1 618 61 ASN CB C 37.92 . 1 619 61 ASN N N 118.96 . 1 620 61 ASN ND2 N 112.23 . 1 621 62 GLU H H 8.68 . 1 622 62 GLU HA H 3.96 . 1 623 62 GLU HB2 H 2.06 . 2 624 62 GLU HG2 H 2.32 . 2 625 62 GLU HG3 H 2.39 . 2 626 62 GLU C C 174.05 . 1 627 62 GLU CA C 60.05 . 1 628 62 GLU CB C 29.04 . 1 629 62 GLU CG C 36.04 . 1 630 62 GLU N N 118.01 . 1 631 63 LYS H H 8.14 . 1 632 63 LYS HA H 4.12 . 1 633 63 LYS HB2 H 1.86 . 2 634 63 LYS HB3 H 1.96 . 2 635 63 LYS HG2 H 1.45 . 2 636 63 LYS HG3 H 1.26 . 2 637 63 LYS HD2 H 1.69 . 2 638 63 LYS HE2 H 2.71 . 2 639 63 LYS HE3 H 2.79 . 2 640 63 LYS C C 172.07 . 1 641 63 LYS CA C 59.34 . 1 642 63 LYS CB C 32.20 . 1 643 63 LYS CG C 24.74 . 1 644 63 LYS CD C 29.54 . 1 645 63 LYS CE C 41.61 . 1 646 63 LYS N N 120.43 . 1 647 64 GLN H H 8.70 . 1 648 64 GLN HA H 4.24 . 1 649 64 GLN HB2 H 2.14 . 2 650 64 GLN HB3 H 2.39 . 2 651 64 GLN HG2 H 2.49 . 2 652 64 GLN HG3 H 2.68 . 2 653 64 GLN HE21 H 7.96 . 2 654 64 GLN HE22 H 6.56 . 2 655 64 GLN C C 173.28 . 1 656 64 GLN CA C 57.45 . 1 657 64 GLN CB C 27.98 . 1 658 64 GLN CG C 32.92 . 1 659 64 GLN N N 119.03 . 1 660 64 GLN NE2 N 112.24 . 1 661 65 LYS H H 9.07 . 1 662 65 LYS HA H 3.93 . 1 663 65 LYS HB2 H 1.96 . 2 664 65 LYS HG2 H 1.49 . 2 665 65 LYS HG3 H 1.63 . 2 666 65 LYS HD2 H 1.73 . 2 667 65 LYS HD3 H 1.76 . 2 668 65 LYS HE2 H 3.08 . 2 669 65 LYS C C 174.28 . 1 670 65 LYS CA C 60.51 . 1 671 65 LYS CB C 32.92 . 1 672 65 LYS CG C 25.78 . 1 673 65 LYS CD C 28.99 . 1 674 65 LYS CE C 41.84 . 1 675 65 LYS N N 122.50 . 1 676 66 GLU H H 7.94 . 1 677 66 GLU HA H 4.14 . 1 678 66 GLU HB2 H 2.06 . 2 679 66 GLU HG2 H 2.29 . 2 680 66 GLU HG3 H 2.36 . 2 681 66 GLU C C 173.38 . 1 682 66 GLU CA C 58.27 . 1 683 66 GLU CB C 29.70 . 1 684 66 GLU CG C 35.42 . 1 685 66 GLU N N 116.67 . 1 686 67 GLY H H 8.55 . 1 687 67 GLY HA2 H 4.00 . 2 688 67 GLY HA3 H 3.63 . 2 689 67 GLY C C 173.11 . 1 690 67 GLY CA C 46.84 . 1 691 67 GLY N N 105.34 . 1 692 68 THR H H 8.34 . 1 693 68 THR HA H 3.65 . 1 694 68 THR HB H 3.75 . 1 695 68 THR HG2 H 1.32 . 1 696 68 THR C C 176.22 . 1 697 68 THR CA C 65.65 . 1 698 68 THR CB C 68.24 . 1 699 68 THR CG2 C 23.74 . 1 700 68 THR N N 110.43 . 1 701 69 LYS H H 7.37 . 1 702 69 LYS HA H 4.06 . 1 703 69 LYS HB2 H 2.05 . 2 704 69 LYS HG2 H 1.46 . 2 705 69 LYS HG3 H 1.57 . 2 706 69 LYS HD2 H 1.75 . 2 707 69 LYS HE2 H 2.97 . 2 708 69 LYS C C 174.77 . 1 709 69 LYS CA C 59.34 . 1 710 69 LYS CB C 31.49 . 1 711 69 LYS CG C 24.54 . 1 712 69 LYS CD C 32.56 . 1 713 69 LYS CE C 41.49 . 1 714 69 LYS N N 120.35 . 1 715 70 LYS H H 7.97 . 1 716 70 LYS HA H 4.01 . 1 717 70 LYS HB2 H 1.94 . 2 718 70 LYS HG2 H 1.44 . 2 719 70 LYS HG3 H 1.72 . 2 720 70 LYS HD2 H 1.65 . 2 721 70 LYS HE2 H 2.94 . 2 722 70 LYS C C 174.95 . 1 723 70 LYS CA C 60.05 . 1 724 70 LYS CB C 32.92 . 1 725 70 LYS CG C 25.78 . 1 726 70 LYS CD C 29.35 . 1 727 70 LYS CE C 41.49 . 1 728 70 LYS N N 116.12 . 1 729 71 VAL H H 8.48 . 1 730 71 VAL HA H 3.61 . 1 731 71 VAL HB H 2.06 . 1 732 71 VAL HG1 H 0.77 . 1 733 71 VAL HG2 H 0.90 . 1 734 71 VAL C C 175.13 . 1 735 71 VAL CA C 66.48 . 1 736 71 VAL CB C 31.49 . 1 737 71 VAL CG1 C 19.64 . 1 738 71 VAL CG2 C 22.94 . 1 739 71 VAL N N 118.09 . 1 740 72 LEU H H 8.46 . 1 741 72 LEU HA H 3.87 . 1 742 72 LEU HB2 H 1.05 . 2 743 72 LEU HB3 H 2.07 . 2 744 72 LEU HG H 1.88 . 1 745 72 LEU HD1 H 0.59 . 2 746 72 LEU HD2 H 0.70 . 2 747 72 LEU C C 174.27 . 1 748 72 LEU CA C 58.62 . 1 749 72 LEU CB C 38.99 . 1 750 72 LEU CG C 26.85 . 1 751 72 LEU CD1 C 23.04 . 1 752 72 LEU CD2 C 23.94 . 1 753 72 LEU N N 117.13 . 1 754 73 LYS H H 7.93 . 1 755 73 LYS HA H 3.68 . 1 756 73 LYS HB2 H 1.91 . 2 757 73 LYS HB3 H 1.93 . 2 758 73 LYS HG2 H 1.74 . 2 759 73 LYS HD2 H 1.47 . 2 760 73 LYS HE2 H 3.02 . 2 761 73 LYS C C 174.04 . 1 762 73 LYS CA C 59.77 . 1 763 73 LYS CB C 32.20 . 1 764 73 LYS CG C 29.34 . 1 765 73 LYS CD C 25.04 . 1 766 73 LYS CE C 41.94 . 1 767 73 LYS N N 116.67 . 1 768 74 HIS H H 7.75 . 1 769 74 HIS HA H 4.33 . 1 770 74 HIS HB2 H 3.33 . 2 771 74 HIS HB3 H 3.30 . 2 772 74 HIS HD2 H 7.50 . 3 773 74 HIS HE1 H 6.48 . 1 774 74 HIS C C 174.59 . 1 775 74 HIS CA C 60.41 . 1 776 74 HIS CB C 31.49 . 1 777 74 HIS N N 117.82 . 1 778 75 LEU H H 8.38 . 1 779 75 LEU HA H 3.94 . 1 780 75 LEU HB2 H 1.42 . 2 781 75 LEU HB3 H 1.62 . 2 782 75 LEU HG H 1.43 . 1 783 75 LEU HD1 H 0.70 . 2 784 75 LEU HD2 H 0.51 . 2 785 75 LEU C C 174.51 . 1 786 75 LEU CA C 57.88 . 1 787 75 LEU CB C 41.84 . 1 788 75 LEU CG C 26.86 . 1 789 75 LEU CD1 C 25.74 . 2 790 75 LEU CD2 C 22.74 . 1 791 75 LEU N N 116.75 . 1 792 76 ILE H H 8.14 . 1 793 76 ILE HA H 2.90 . 1 794 76 ILE HB H 1.23 . 1 795 76 ILE HG12 H -1.23 . 2 796 76 ILE HG13 H 0.47 . 2 797 76 ILE HG2 H 0.03 . 1 798 76 ILE HD1 H 0.48 . 1 799 76 ILE C C 175.79 . 1 800 76 ILE CA C 65.05 . 1 801 76 ILE CB C 37.92 . 1 802 76 ILE CG1 C 28.34 . 2 803 76 ILE CG2 C 16.24 . 1 804 76 ILE CD1 C 28.34 . 1 805 76 ILE N N 116.56 . 1 806 77 ASN H H 7.29 . 1 807 77 ASN HA H 4.40 . 1 808 77 ASN HB2 H 1.97 . 2 809 77 ASN HB3 H 2.36 . 2 810 77 ASN HD21 H 7.54 . 2 811 77 ASN HD22 H 7.39 . 2 812 77 ASN C C 176.34 . 1 813 77 ASN CA C 54.90 . 1 814 77 ASN CB C 39.34 . 1 815 77 ASN N N 110.51 . 1 816 77 ASN ND2 N 115.31 . 1 817 78 HIS H H 8.39 . 1 818 78 HIS HA H 4.89 . 1 819 78 HIS HB2 H 3.08 . 2 820 78 HIS HB3 H 2.38 . 2 821 78 HIS HD2 H 6.75 . 3 822 78 HIS HE1 H 8.02 . 1 823 78 HIS C C 176.94 . 1 824 78 HIS CA C 56.12 . 1 825 78 HIS CB C 31.14 . 1 826 78 HIS N N 113.97 . 1 827 79 LYS H H 8.29 . 1 828 79 LYS HA H 5.20 . 1 829 79 LYS HB2 H 2.09 . 2 830 79 LYS HB3 H 2.01 . 2 831 79 LYS HG2 H 1.45 . 2 832 79 LYS HD2 H 1.96 . 2 833 79 LYS HD3 H 1.88 . 2 834 79 LYS HE2 H 1.65 . 2 835 79 LYS HE3 H 1.50 . 2 836 79 LYS CA C 52.20 . 1 837 79 LYS CB C 33.24 . 1 838 79 LYS CG C 24.84 . 1 839 79 LYS CD C 28.44 . 1 840 79 LYS CE C 42.20 . 1 841 79 LYS N N 118.45 . 1 842 80 PRO HA H 4.51 . 1 843 80 PRO HB2 H 2.22 . 2 844 80 PRO HB3 H 2.54 . 2 845 80 PRO HG2 H 2.13 . 2 846 80 PRO HG3 H 2.21 . 2 847 80 PRO HD2 H 3.26 . 3 848 80 PRO HD3 H 3.79 . 3 849 80 PRO C C 173.34 . 1 850 80 PRO CA C 65.24 . 1 851 80 PRO CB C 31.06 . 1 852 80 PRO CG C 27.20 . 1 853 80 PRO CD C 50.14 . 1 854 81 ASP H H 9.24 . 1 855 81 ASP HA H 4.34 . 1 856 81 ASP HB2 H 2.83 . 2 857 81 ASP HB3 H 2.71 . 2 858 81 ASP C C 173.77 . 1 859 81 ASP CA C 56.12 . 1 860 81 ASP CB C 38.71 . 1 861 81 ASP N N 118.18 . 1 862 82 VAL H H 7.78 . 1 863 82 VAL HA H 3.98 . 1 864 82 VAL HB H 2.47 . 1 865 82 VAL HG1 H 1.13 . 1 866 82 VAL HG2 H 1.17 . 1 867 82 VAL C C 173.74 . 1 868 82 VAL CA C 65.05 . 1 869 82 VAL CB C 31.14 . 1 870 82 VAL CG1 C 23.64 . 1 871 82 VAL CG2 C 67.78 . 1 872 82 VAL N N 19.35 . 1 873 83 TRP H H 8.39 . 1 874 83 TRP HA H 4.70 . 1 875 83 TRP HB2 H 3.41 . 2 876 83 TRP HB3 H 3.05 . 2 877 83 TRP HD1 H 7.37 . 1 878 83 TRP HE1 H 11.39 . 3 879 83 TRP HZ2 H 7.59 . 3 880 83 TRP HZ3 H 7.37 . 3 881 83 TRP HH2 H 6.75 . 1 882 83 TRP C C 176.01 . 1 883 83 TRP CA C 58.98 . 1 884 83 TRP CB C 29.35 . 1 885 83 TRP N N 120.22 . 1 886 83 TRP NE1 N 131.48 . 1 887 84 ALA H H 8.20 . 1 888 84 ALA HA H 3.70 . 1 889 84 ALA HB H 1.58 . 1 890 84 ALA C C 172.02 . 1 891 84 ALA CA C 55.05 . 1 892 84 ALA CB C 17.61 . 1 893 84 ALA N N 117.85 . 1 894 85 GLN H H 7.30 . 1 895 85 GLN HA H 4.08 . 1 896 85 GLN HB2 H 2.17 . 2 897 85 GLN HB3 H 2.35 . 2 898 85 GLN HG2 H 2.39 . 2 899 85 GLN HG3 H 2.67 . 2 900 85 GLN HE21 H 6.75 . 2 901 85 GLN HE22 H 7.26 . 2 902 85 GLN C C 176.31 . 1 903 85 GLN CA C 58.47 . 1 904 85 GLN CB C 29.34 . 1 905 85 GLN CG C 34.04 . 1 906 85 GLN N N 116.73 . 1 907 85 GLN NE2 N 111.21 . 1 908 86 LEU H H 8.43 . 1 909 86 LEU HA H 4.05 . 1 910 86 LEU HB2 H 1.68 . 2 911 86 LEU HB3 H 1.88 . 2 912 86 LEU HG H 1.73 . 1 913 86 LEU HD1 H 0.79 . 2 914 86 LEU HD2 H 1.07 . 2 915 86 LEU C C 173.42 . 1 916 86 LEU CA C 58.52 . 1 917 86 LEU CB C 41.94 . 1 918 86 LEU CG C 28.94 . 1 919 86 LEU CD1 C 26.85 . 1 920 86 LEU CD2 C 27.21 . 1 921 86 LEU N N 121.84 . 1 922 87 LYS H H 8.48 . 1 923 87 LYS HA H 3.34 . 1 924 87 LYS HB2 H 1.08 . 2 925 87 LYS HB3 H 1.40 . 2 926 87 LYS HG2 H 0.59 . 2 927 87 LYS HG3 H 0.82 . 2 928 87 LYS HD2 H 1.37 . 2 929 87 LYS HD3 H 1.41 . 2 930 87 LYS HE2 H 2.45 . 2 931 87 LYS HE3 H 2.83 . 2 932 87 LYS C C 175.20 . 1 933 87 LYS CA C 59.74 . 1 934 87 LYS CB C 30.49 . 1 935 87 LYS CG C 23.94 . 1 936 87 LYS CD C 29.04 . 1 937 87 LYS CE C 41.14 . 1 938 87 LYS N N 119.32 . 1 939 88 ALA H H 7.08 . 1 940 88 ALA HA H 3.95 . 1 941 88 ALA HB H 1.40 . 1 942 88 ALA CA C 53.99 . 1 943 88 ALA CB C 17.76 . 1 944 88 ALA N N 118.56 . 1 945 89 LYS H H 7.17 . 1 946 89 LYS HA H 4.06 . 1 947 89 LYS HB2 H 1.61 . 2 948 89 LYS HG2 H 0.04 . 2 949 89 LYS HD2 H 1.09 . 2 950 89 LYS C C 174.78 . 1 951 89 LYS CA C 57.91 . 1 952 89 LYS CB C 32.92 . 1 953 89 LYS CG C 70.05 . 1 954 89 LYS CD C 70.40 . 1 955 89 LYS N N 114.56 . 1 956 90 TYR H H 8.26 . 1 957 90 TYR HA H 4.45 . 1 958 90 TYR HB2 H 3.06 . 2 959 90 TYR HB3 H 2.42 . 2 960 90 TYR HD1 H 6.83 . 3 961 90 TYR HE1 H 7.36 . 3 962 90 TYR C C 177.21 . 1 963 90 TYR CA C 59.54 . 1 964 90 TYR CB C 39.40 . 1 965 90 TYR N N 112.42 . 1 966 91 ASP H H 8.61 . 1 967 91 ASP HA H 5.29 . 1 968 91 ASP HB2 H 2.42 . 2 969 91 ASP HB3 H 2.81 . 2 970 91 ASP CA C 52.19 . 1 971 91 ASP CB C 41.84 . 1 972 91 ASP N N 118.45 . 1 973 92 PRO HA H 4.20 . 1 974 92 PRO HB2 H 2.01 . 2 975 92 PRO HB3 H 2.46 . 2 976 92 PRO HG2 H 2.08 . 2 977 92 PRO HG3 H 2.01 . 2 978 92 PRO HD2 H 3.78 . 3 979 92 PRO HD3 H 3.30 . 3 980 92 PRO C C 174.36 . 1 981 92 PRO CA C 65.04 . 1 982 92 PRO CB C 31.14 . 1 983 92 PRO CG C 26.84 . 1 984 92 PRO CD C 49.84 . 1 985 93 ASP H H 8.43 . 1 986 93 ASP HA H 4.71 . 1 987 93 ASP HB2 H 2.76 . 2 988 93 ASP HB3 H 2.81 . 2 989 93 ASP C C 174.81 . 1 990 93 ASP CA C 54.45 . 1 991 93 ASP CB C 41.11 . 1 992 93 ASP N N 115.46 . 1 993 94 GLY H H 7.94 . 1 994 94 GLY HA2 H 3.98 . 2 995 94 GLY HA3 H 3.88 . 2 996 94 GLY C C 177.31 . 1 997 94 GLY CA C 47.20 . 1 998 94 GLY N N 108.72 . 1 999 95 THR H H 8.29 . 1 1000 95 THR HA H 3.90 . 1 1001 95 THR HB H 3.77 . 1 1002 95 THR HG2 H 0.88 . 1 1003 95 THR C C 176.28 . 1 1004 95 THR CA C 64.69 . 1 1005 95 THR CB C 68.62 . 1 1006 95 THR CG2 C 21.02 . 1 1007 95 THR N N 116.74 . 1 1008 96 TYR H H 9.62 . 1 1009 96 TYR HA H 4.75 . 1 1010 96 TYR HB2 H 2.71 . 2 1011 96 TYR HB3 H 3.34 . 2 1012 96 TYR HD1 H 7.00 . 3 1013 96 TYR HE1 H 7.28 . 3 1014 96 TYR C C 173.34 . 1 1015 96 TYR CA C 59.34 . 1 1016 96 TYR CB C 39.33 . 1 1017 96 TYR N N 121.52 . 1 1018 97 SER H H 9.48 . 1 1019 97 SER HA H 4.20 . 1 1020 97 SER HB2 H 3.94 . 2 1021 97 SER HB3 H 4.07 . 2 1022 97 SER C C 176.68 . 1 1023 97 SER CA C 62.39 . 1 1024 97 SER CB C 69.24 . 1 1025 97 SER N N 117.00 . 1 1026 98 LYS H H 7.76 . 1 1027 98 LYS HA H 4.35 . 1 1028 98 LYS HB2 H 1.99 . 2 1029 98 LYS HG2 H 1.54 . 2 1030 98 LYS HG3 H 1.58 . 2 1031 98 LYS HD2 H 1.72 . 2 1032 98 LYS C C 174.04 . 1 1033 98 LYS CA C 58.62 . 1 1034 98 LYS CB C 31.82 . 1 1035 98 LYS CG C 24.63 . 1 1036 98 LYS CD C 28.54 . 1 1037 98 LYS N N 123.67 . 1 1038 99 LYS H H 7.79 . 1 1039 99 LYS HA H 4.20 . 1 1040 99 LYS HB2 H 1.96 . 2 1041 99 LYS HG2 H 1.55 . 2 1042 99 LYS HG3 H 1.58 . 2 1043 99 LYS HD2 H 1.83 . 2 1044 99 LYS HE2 H 3.32 . 2 1045 99 LYS HE3 H 3.10 . 2 1046 99 LYS C C 173.88 . 1 1047 99 LYS CA C 59.00 . 1 1048 99 LYS CB C 31.87 . 1 1049 99 LYS CG C 24.64 . 1 1050 99 LYS CD C 28.74 . 1 1051 99 LYS CE C 41.48 . 1 1052 99 LYS N N 117.33 . 1 1053 100 TYR H H 7.88 . 1 1054 100 TYR HA H 4.04 . 1 1055 100 TYR HB2 H 3.18 . 2 1056 100 TYR HB3 H 3.29 . 2 1057 100 TYR HD1 H 6.65 . 3 1058 100 TYR HE1 H 6.99 . 3 1059 100 TYR C C 174.95 . 1 1060 100 TYR CA C 61.11 . 1 1061 100 TYR CB C 39.28 . 1 1062 100 TYR N N 118.88 . 1 1063 101 GLU H H 8.47 . 1 1064 101 GLU HA H 3.95 . 1 1065 101 GLU HB2 H 2.35 . 2 1066 101 GLU HB3 H 2.42 . 2 1067 101 GLU HG2 H 2.53 . 2 1068 101 GLU HG3 H 2.60 . 2 1069 101 GLU C C 174.83 . 1 1070 101 GLU CA C 58.60 . 1 1071 101 GLU CB C 29.43 . 1 1072 101 GLU CG C 35.85 . 1 1073 101 GLU N N 118.44 . 1 1074 102 ASP H H 8.54 . 1 1075 102 ASP HA H 4.46 . 1 1076 102 ASP HB2 H 2.80 . 2 1077 102 ASP HB3 H 2.76 . 2 1078 102 ASP C C 174.31 . 1 1079 102 ASP CA C 56.29 . 1 1080 102 ASP CB C 40.29 . 1 1081 102 ASP N N 119.63 . 1 1082 103 ARG H H 7.76 . 1 1083 103 ARG HA H 4.20 . 1 1084 103 ARG HB2 H 1.87 . 2 1085 103 ARG HG2 H 1.57 . 2 1086 103 ARG HG3 H 1.73 . 2 1087 103 ARG HD2 H 3.16 . 2 1088 103 ARG C C 174.57 . 1 1089 103 ARG CA C 57.92 . 1 1090 103 ARG CB C 30.10 . 1 1091 103 ARG CG C 26.85 . 1 1092 103 ARG CD C 43.04 . 1 1093 103 ARG N N 118.76 . 1 1094 104 GLU H H 7.75 . 1 1095 104 GLU HA H 4.36 . 1 1096 104 GLU HB2 H 1.70 . 2 1097 104 GLU HG2 H 2.01 . 2 1098 104 GLU HG3 H 2.06 . 2 1099 104 GLU C C 174.85 . 1 1100 104 GLU CA C 56.23 . 1 1101 104 GLU CB C 29.63 . 1 1102 104 GLU CG C 34.83 . 1 1103 104 GLU N N 116.32 . 1 1104 105 LYS H H 7.96 . 1 1105 105 LYS HA H 4.20 . 1 1106 105 LYS HB2 H 1.82 . 2 1107 105 LYS HB3 H 1.93 . 2 1108 105 LYS HG2 H 1.46 . 2 1109 105 LYS HD2 H 1.72 . 2 1110 105 LYS HE2 H 3.01 . 2 1111 105 LYS C C 175.67 . 1 1112 105 LYS CA C 57.15 . 1 1113 105 LYS CB C 32.14 . 1 1114 105 LYS CG C 24.60 . 1 1115 105 LYS CD C 28.86 . 1 1116 105 LYS CE C 41.64 . 1 1117 105 LYS N N 120.12 . 1 1118 106 GLU H H 8.31 . 1 1119 106 GLU HA H 4.24 . 1 1120 106 GLU HB2 H 2.00 . 2 1121 106 GLU HB3 H 1.94 . 2 1122 106 GLU HG2 H 2.31 . 2 1123 106 GLU HG3 H 2.24 . 2 1124 106 GLU C C 176.22 . 1 1125 106 GLU CA C 56.11 . 1 1126 106 GLU CB C 30.22 . 1 1127 106 GLU CG C 35.84 . 1 1128 106 GLU N N 122.19 . 1 1129 107 LEU H H 8.11 . 1 1130 107 LEU HA H 4.34 . 1 1131 107 LEU HB2 H 1.50 . 2 1132 107 LEU HB3 H 1.62 . 2 1133 107 LEU HG H 1.62 . 1 1134 107 LEU C C 175.63 . 1 1135 107 LEU CA C 54.75 . 1 1136 107 LEU CB C 42.21 . 1 1137 107 LEU CG C 25.84 . 1 1138 107 LEU N N 121.74 . 1 1139 108 HIS H H 8.28 . 1 1140 108 HIS HA H 4.71 . 1 1141 108 HIS HB2 H 3.16 . 2 1142 108 HIS HB3 H 3.27 . 2 1143 108 HIS HD2 H 8.30 . 3 1144 108 HIS HE1 H 7.22 . 1 1145 108 HIS C C 178.48 . 1 1146 108 HIS CA C 55.43 . 1 1147 108 HIS CB C 34.41 . 1 1148 108 HIS N N 119.66 . 1 1149 109 GLN H H 8.04 . 1 1150 109 GLN HA H 4.22 . 1 1151 109 GLN HB2 H 1.96 . 2 1152 109 GLN HG2 H 2.16 . 2 1153 109 GLN HG3 H 2.32 . 2 1154 109 GLN HE21 H 7.56 . 2 1155 109 GLN HE22 H 6.85 . 2 1156 109 GLN CA C 57.33 . 1 1157 109 GLN CB C 30.04 . 1 1158 109 GLN CG C 34.04 . 1 1159 109 GLN N N 126.29 . 1 1160 109 GLN NE2 N 112.93 . 1 stop_ save_