data_4405 #Corrected using PDB structure: 1J5KA # #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 # 64 T HA 5.71 4.61 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 16 T C 181.22 172.56 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.00 -0.39 0.02 -0.17 -0.20 -0.10 # #bmr4405.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4405.str file): #HA CA CB CO N HN #N/A -0.18 -0.18 -0.17 -0.20 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.16 +/-0.16 +/-0.13 +/-0.40 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.789 0.978 0.997 0.784 0.864 0.542 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.157 0.707 0.664 0.557 1.687 0.304 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; C-TERMINAL KH DOMAIN OF HNRNP K (KH3) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 BABER J. . . 2 LIBUTTI D. . . 3 LEVENS D. . . 4 TJANDRA N. . . stop_ _BMRB_accession_number 4405 _BMRB_flat_file_name bmr4405.str _Entry_type new _Submission_date 1999-09-15 _Accession_date 1999-09-15 _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' 506 '13C chemical shifts' 363 '15N chemical shifts' 92 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; HIGH PRECISION SOLUTION STRUCTURE OF THE C-TERMINAL KH DOMAIN OF HNRNP K, A C-MYC TRANSCRIPTION FACTOR ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99299390 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 BABER J. . . 2 LIBUTTI D. . . 3 LEVENS D. . . 4 TJANDRA N. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full . _Journal_volume 289 _Page_first 949 _Page_last 962 _Year 1999 loop_ _Keyword "HNRNP K" "KH DOMAIN" "THREE-DIMENSIONAL STRUCTURE" NMR C-MYC "DIPOLAR COUPLING" DNA-BINDING RNA-BINDING stop_ save_ ################################## # Molecular system description # ################################## save_hnRNP_K _Saveframe_category molecular_system _Mol_system_name "hnRNP K" _Abbreviation_common "hnRNP K" loop_ _Mol_system_component_name _Mol_label "hnRNP K subunit 1" $KH3 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1KHM "A Chain A, C-Terminal Kh Domain Of Hnrnp K (Kh3)" . stop_ save_ ######################## # Monomeric polymers # ######################## save_KH3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "hnRNP K" _Name_variant "G26R for fragment" _Abbreviation_common KH3 ############################## # Polymer residue sequence # ############################## _Residue_count 89 _Mol_residue_sequence ; GSPNSYGDLGGPIITTQVTI PKDLARSIIGKGGQRIKQIR HESGASIKIDEPLEGSEDRI ITITGTQDQIQNAQYLLQNS VKQYSGKFF ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 PRO 4 ASN 5 SER 6 TYR 7 GLY 8 ASP 9 LEU 10 GLY 11 GLY 12 PRO 13 ILE 14 ILE 15 THR 16 THR 17 GLN 18 VAL 19 THR 20 ILE 21 PRO 22 LYS 23 ASP 24 LEU 25 ALA 26 ARG 27 SER 28 ILE 29 ILE 30 GLY 31 LYS 32 GLY 33 GLY 34 GLN 35 ARG 36 ILE 37 LYS 38 GLN 39 ILE 40 ARG 41 HIS 42 GLU 43 SER 44 GLY 45 ALA 46 SER 47 ILE 48 LYS 49 ILE 50 ASP 51 GLU 52 PRO 53 LEU 54 GLU 55 GLY 56 SER 57 GLU 58 ASP 59 ARG 60 ILE 61 ILE 62 THR 63 ILE 64 THR 65 GLY 66 THR 67 GLN 68 ASP 69 GLN 70 ILE 71 GLN 72 ASN 73 ALA 74 GLN 75 TYR 76 LEU 77 LEU 78 GLN 79 ASN 80 SER 81 VAL 82 LYS 83 GLN 84 TYR 85 SER 86 GLY 87 LYS 88 PHE 89 PHE stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2003-09-25 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 1KHM "A Chain A, C-Terminal Kh Domain Of Hnrnp K(Kh3)" 100.00 89 100 100 2e-44 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $KH3 human 9606 Eukaryota Metazoa homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant $KH3 'recombinant technology' "Escherichia coli" Escherichia coli BL21 DE3 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 _Concentration_min_value _Isotopic_labeling $KH3 . mM 1 "[U-99% 13C; U-99% 15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 5.5 0.1 n/a temperature 300 0.4 K ionic_strength 5 . 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 TSP H 1 'methyl protons' ppm 0.00 external_to_the_sample indirect cylindrical external_to_the_sample parallel_to_Bo 1.000 DSS C 13 'methyl protons' ppm 0.00 external_to_the_sample indirect cylindrical external_to_the_sample parallel_to_Bo 0.251449530 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 _Mol_system_component_name "hnRNP K subunit 1" 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 2 SER HB2 H 3.88 . 1 2 2 SER HB3 H 3.88 . 1 3 2 SER HA H 4.85 . 1 4 2 SER CA C 56.25 . 1 5 2 SER CB C 63.01 . 1 6 3 PRO HA H 4.43 . 1 7 3 PRO HB3 H 2.28 . 1 8 3 PRO HB2 H 1.92 . 1 9 3 PRO HD3 H 3.82 . 1 10 3 PRO HD2 H 3.72 . 1 11 3 PRO HG2 H 2.00 . 1 12 3 PRO HG3 H 2.00 . 1 13 3 PRO C C 176.36 . 1 14 3 PRO CA C 63.49 . 1 15 3 PRO CB C 31.95 . 1 16 3 PRO CD C 50.81 . 1 17 3 PRO CG C 27.32 . 1 18 4 ASN HA H 4.65 . 1 19 4 ASN HB2 H 2.74 . 1 20 4 ASN HB3 H 2.74 . 1 21 4 ASN H H 8.41 . 1 22 4 ASN C C 174.92 . 1 23 4 ASN CA C 53.24 . 1 24 4 ASN CB C 38.86 . 1 25 4 ASN N N 117.63 . 1 26 5 SER HA H 4.39 . 1 27 5 SER HB2 H 3.77 . 1 28 5 SER HB3 H 3.77 . 1 29 5 SER H H 8.14 . 1 30 5 SER C C 173.98 . 1 31 5 SER CA C 58.34 . 1 32 5 SER CB C 63.74 . 1 33 5 SER N N 115.32 . 1 34 6 TYR HA H 4.58 . 1 35 6 TYR HB3 H 3.11 . 1 36 6 TYR HB2 H 2.94 . 1 37 6 TYR H H 8.19 . 1 38 6 TYR C C 176.14 . 1 39 6 TYR CA C 58.11 . 1 41 6 TYR N N 121.08 . 1 42 7 GLY HA2 H 3.90 . 1 43 7 GLY HA3 H 3.90 . 1 44 7 GLY H H 8.24 . 1 45 7 GLY C C 173.61 . 1 46 7 GLY CA C 45.39 . 1 47 7 GLY N N 109.38 . 1 48 8 ASP HA H 4.61 . 1 49 8 ASP HB3 H 2.67 . 1 50 8 ASP HB2 H 2.61 . 1 51 8 ASP H H 8.22 . 1 52 8 ASP C C 176.37 . 1 53 8 ASP CA C 54.49 . 1 54 8 ASP CB C 41.17 . 1 55 8 ASP N N 120.11 . 1 56 9 LEU HA H 4.34 . 1 57 9 LEU HB2 H 1.66 . 1 58 9 LEU HB3 H 1.66 . 1 59 9 LEU HD1 H 0.92 . 1 60 9 LEU HD2 H 0.86 . 1 61 9 LEU HG H 1.67 . 1 62 9 LEU H H 8.30 . 1 63 9 LEU C C 177.92 . 1 64 9 LEU CA C 55.52 . 1 66 9 LEU CD1 C 25.09 . 1 67 9 LEU CD2 C 23.27 . 1 68 9 LEU CG C 27.06 . 1 69 9 LEU N N 121.79 . 1 70 10 GLY HA3 H 4.34 . 1 71 10 GLY HA2 H 4.00 . 1 72 10 GLY H H 8.43 . 1 74 10 GLY CA C 45.44 . 1 75 10 GLY N N 108.36 . 1 76 11 GLY HA3 H 4.16 . 1 77 11 GLY HA2 H 4.01 . 1 78 11 GLY H H 8.01 . 1 79 11 GLY CA C 44.55 . 1 81 12 PRO HA H 4.39 . 1 82 12 PRO HB3 H 2.24 . 1 83 12 PRO HB2 H 1.83 . 1 84 12 PRO HD3 H 3.63 . 1 85 12 PRO HD2 H 3.57 . 1 86 12 PRO HG2 H 2.00 . 1 87 12 PRO HG3 H 2.00 . 1 88 12 PRO C C 175.77 . 1 89 12 PRO CA C 62.86 . 1 90 12 PRO CB C 32.32 . 1 91 12 PRO CD C 49.80 . 1 92 12 PRO CG C 27.16 . 1 93 13 ILE HA H 3.94 . 1 94 13 ILE HB H 1.77 . 1 95 13 ILE HD1 H 0.75 . 1 96 13 ILE HG13 H 1.47 . 1 97 13 ILE HG12 H 1.26 . 1 98 13 ILE HG2 H 0.74 . 1 99 13 ILE H H 8.12 . 1 100 13 ILE C C 175.69 . 1 101 13 ILE CA C 60.24 . 1 102 13 ILE CB C 36.82 . 1 103 13 ILE CD1 C 11.33 . 1 104 13 ILE CG1 C 27.29 . 1 105 13 ILE CG2 C 18.18 . 1 106 13 ILE N N 120.36 . 1 107 14 ILE HA H 4.50 . 1 108 14 ILE HB H 1.89 . 1 109 14 ILE HD1 H 0.82 . 1 110 14 ILE HG13 H 1.38 . 1 111 14 ILE HG12 H 1.13 . 1 112 14 ILE HG2 H 0.85 . 1 113 14 ILE H H 8.98 . 1 114 14 ILE C C 173.46 . 1 115 14 ILE CA C 60.03 . 1 116 14 ILE CB C 41.50 . 1 117 14 ILE CD1 C 13.69 . 1 118 14 ILE CG1 C 26.80 . 1 119 14 ILE CG2 C 18.03 . 1 120 14 ILE N N 128.67 . 1 121 15 THR HA H 5.46 . 1 122 15 THR HB H 3.78 . 1 123 15 THR HG2 H 1.06 . 1 124 15 THR H H 8.06 . 1 125 15 THR C C 173.91 . 1 126 15 THR CA C 61.26 . 1 127 15 THR CB C 71.67 . 1 128 15 THR CG2 C 21.67 . 1 129 15 THR N N 115.90 . 1 130 16 THR HA H 4.70 . 1 131 16 THR HB H 3.88 . 1 132 16 THR HG2 H 1.05 . 1 133 16 THR H H 9.24 . 1 134 16 THR C C 181.22 . 1 135 16 THR CA C 60.37 . 1 136 16 THR CB C 71.15 . 1 137 16 THR CG2 C 20.39 . 1 138 16 THR N N 122.02 . 1 139 17 GLN HA H 5.63 . 1 140 17 GLN HB2 H 1.90 . 1 141 17 GLN HB3 H 1.79 . 1 142 17 GLN HG3 H 2.28 . 1 143 17 GLN HG2 H 2.23 . 1 144 17 GLN H H 8.15 . 1 145 17 GLN HE21 H 7.35 . 1 146 17 GLN HE22 H 6.78 . 1 147 17 GLN C C 175.17 . 1 148 17 GLN CA C 54.30 . 1 149 17 GLN CB C 32.40 . 1 150 17 GLN CG C 34.44 . 1 151 17 GLN N N 121.54 . 1 152 17 GLN NE2 N 112.32 . 1 153 18 VAL HA H 4.46 . 1 154 18 VAL HB H 1.95 . 1 155 18 VAL HG1 H 0.84 . 1 156 18 VAL HG2 H 0.80 . 1 157 18 VAL H H 9.07 . 1 158 18 VAL C C 173.79 . 1 159 18 VAL CA C 60.35 . 1 160 18 VAL CB C 35.50 . 1 161 18 VAL CG1 C 21.25 . 1 162 18 VAL CG2 C 20.55 . 1 163 18 VAL N N 120.61 . 1 164 19 THR HA H 4.97 . 1 165 19 THR HB H 3.93 . 1 166 19 THR HG2 H 1.03 . 1 167 19 THR H H 8.49 . 1 169 19 THR CA C 61.64 . 1 170 19 THR CB C 69.59 . 1 171 19 THR CG2 C 21.79 . 1 172 19 THR N N 119.73 . 1 173 20 ILE HA H 4.85 . 1 174 20 ILE HB H 1.73 . 1 175 20 ILE HD1 H 0.59 . 1 176 20 ILE HG13 H 1.39 . 1 177 20 ILE HG12 H 1.06 . 1 178 20 ILE HG2 H 0.77 . 1 179 20 ILE H H 9.06 . 1 180 20 ILE CA C 56.81 . 1 181 20 ILE CB C 40.30 . 1 182 20 ILE CD1 C 13.40 . 1 183 20 ILE CG1 C 26.03 . 1 184 20 ILE CG2 C 17.66 . 1 186 21 PRO HA H 4.79 . 1 187 21 PRO HB3 H 2.52 . 1 188 21 PRO HB2 H 1.99 . 1 189 21 PRO HD3 H 3.91 . 1 190 21 PRO HD2 H 3.43 . 1 191 21 PRO HG2 H 2.06 . 1 192 21 PRO HG3 H 2.06 . 1 193 21 PRO C C 178.32 . 1 194 21 PRO CA C 62.63 . 1 195 21 PRO CB C 32.85 . 1 196 21 PRO CD C 51.30 . 1 197 21 PRO CG C 27.90 . 1 198 22 LYS HA H 3.85 . 1 199 22 LYS HB3 H 1.72 . 1 200 22 LYS HB2 H 1.89 . 1 201 22 LYS HD2 H 1.67 . 1 202 22 LYS HD3 H 1.67 . 1 203 22 LYS HE2 H 2.98 . 1 204 22 LYS HE3 H 2.98 . 1 205 22 LYS HG2 H 1.39 . 1 206 22 LYS HG3 H 1.39 . 1 207 22 LYS H H 8.88 . 1 208 22 LYS C C 177.93 . 1 209 22 LYS CA C 60.26 . 1 210 22 LYS CB C 32.75 . 1 211 22 LYS CD C 29.65 . 1 212 22 LYS CE C 41.95 . 1 213 22 LYS CG C 24.24 . 1 214 22 LYS N N 121.79 . 1 215 23 ASP HA H 4.43 . 1 216 23 ASP HB3 H 2.63 . 1 217 23 ASP HB2 H 2.59 . 1 218 23 ASP H H 9.00 . 1 219 23 ASP C C 177.75 . 1 220 23 ASP CA C 57.10 . 1 221 23 ASP CB C 39.97 . 1 222 23 ASP N N 118.04 . 1 223 24 LEU HA H 4.25 . 1 224 24 LEU HB2 H 1.61 . 1 225 24 LEU HB3 H 1.61 . 1 226 24 LEU HD1 H 0.83 . 1 227 24 LEU HD2 H 0.78 . 1 228 24 LEU HG H 1.53 . 1 229 24 LEU H H 7.38 . 1 230 24 LEU C C 178.24 . 1 231 24 LEU CA C 56.29 . 1 232 24 LEU CB C 41.94 . 1 233 24 LEU CD1 C 24.42 . 1 234 24 LEU CD2 C 24.42 . 1 235 24 LEU CG C 27.55 . 1 236 24 LEU N N 119.70 . 1 237 25 ALA HA H 3.73 . 1 238 25 ALA HB H 1.33 . 1 239 25 ALA H H 8.02 . 1 240 25 ALA C C 178.13 . 1 241 25 ALA CA C 55.60 . 1 242 25 ALA CB C 17.84 . 1 243 25 ALA N N 120.57 . 1 244 26 ARG HA H 3.96 . 1 245 26 ARG HB2 H 1.91 . 1 246 26 ARG HB3 H 1.91 . 1 247 26 ARG HD2 H 3.21 . 1 248 26 ARG HD3 H 3.21 . 1 249 26 ARG HG3 H 1.76 . 1 250 26 ARG HG2 H 1.63 . 1 251 26 ARG H H 7.94 . 1 252 26 ARG C C 178.54 . 1 253 26 ARG CA C 59.49 . 1 254 26 ARG CB C 29.77 . 1 255 26 ARG CD C 43.35 . 1 256 26 ARG CG C 27.35 . 1 257 26 ARG N N 115.00 . 1 258 27 SER HA H 4.21 . 1 259 27 SER HB3 H 3.86 . 1 260 27 SER HB2 H 3.75 . 1 261 27 SER H H 7.50 . 1 262 27 SER C C 175.20 . 1 263 27 SER CA C 61.12 . 1 264 27 SER CB C 63.20 . 1 265 27 SER N N 113.63 . 1 266 28 ILE HA H 3.86 . 1 267 28 ILE HB H 1.74 . 1 268 28 ILE HD1 H 0.68 . 1 269 28 ILE HG13 H 1.51 . 1 270 28 ILE HG12 H 1.11 . 1 271 28 ILE HG2 H 0.73 . 1 272 28 ILE H H 7.61 . 1 273 28 ILE C C 175.24 . 1 274 28 ILE CA C 63.66 . 1 275 28 ILE CB C 38.50 . 1 276 28 ILE CD1 C 13.99 . 1 277 28 ILE CG1 C 28.35 . 1 278 28 ILE CG2 C 17.75 . 1 279 28 ILE N N 118.43 . 1 280 29 ILE HA H 3.86 . 1 281 29 ILE HB H 1.90 . 1 282 29 ILE HD1 H 0.78 . 1 283 29 ILE HG13 H 1.59 . 1 284 29 ILE HG12 H 1.08 . 1 285 29 ILE HG2 H 1.01 . 1 286 29 ILE H H 7.83 . 1 287 29 ILE C C 177.84 . 1 288 29 ILE CA C 63.53 . 1 290 29 ILE CD1 C 13.46 . 1 291 29 ILE CG1 C 28.43 . 1 292 29 ILE CG2 C 17.88 . 1 293 29 ILE N N 115.58 . 1 294 30 GLY HA2 H 4.05 . 1 295 30 GLY HA3 H 4.05 . 1 296 30 GLY H H 7.56 . 1 298 30 GLY CA C 44.61 . 1 299 30 GLY N N 105.50 . 1 300 31 LYS HA H 4.14 . 1 301 31 LYS HB2 H 1.86 . 1 302 31 LYS HB3 H 1.86 . 1 303 31 LYS HD2 H 1.69 . 1 304 31 LYS HD3 H 1.69 . 1 305 31 LYS HE2 H 2.98 . 1 306 31 LYS HE3 H 2.98 . 1 307 31 LYS HG3 H 1.49 . 1 308 31 LYS HG2 H 1.39 . 1 309 31 LYS H H 8.86 . 1 310 31 LYS CA C 57.62 . 1 312 31 LYS CD C 29.16 . 1 313 31 LYS CE C 41.94 . 1 314 31 LYS CG C 24.93 . 1 315 31 LYS N N 121.71 . 1 316 32 GLY HA2 H 3.98 . 1 317 32 GLY HA3 H 3.98 . 1 318 32 GLY H H 9.02 . 1 319 32 GLY C C 175.22 . 1 320 32 GLY CA C 46.25 . 1 321 32 GLY N N 112.39 . 1 322 33 GLY HA3 H 4.03 . 1 323 33 GLY HA2 H 3.89 . 1 324 33 GLY H H 7.91 . 1 325 33 GLY C C 175.88 . 1 326 33 GLY CA C 46.16 . 1 327 33 GLY N N 106.77 . 1 328 34 GLN HA H 3.98 . 1 329 34 GLN HB3 H 2.16 . 1 330 34 GLN HB2 H 2.25 . 1 331 34 GLN HG2 H 2.46 . 1 332 34 GLN HG3 H 2.46 . 1 333 34 GLN H H 7.82 . 1 334 34 GLN C C 177.82 . 1 335 34 GLN CA C 59.24 . 1 336 34 GLN CB C 28.79 . 1 337 34 GLN CG C 33.65 . 1 338 34 GLN N N 118.01 . 1 339 35 ARG HA H 4.28 . 1 340 35 ARG HB2 H 1.89 . 1 341 35 ARG HB3 H 1.89 . 1 342 35 ARG H H 8.48 . 1 343 35 ARG HD3 H 3.38 . 1 344 35 ARG HD2 H 3.19 . 1 345 35 ARG HG3 H 1.78 . 1 346 35 ARG HG2 H 1.59 . 1 347 35 ARG C C 178.30 . 1 348 35 ARG CA C 58.37 . 1 349 35 ARG CB C 28.87 . 1 350 35 ARG CD C 42.73 . 1 351 35 ARG CG C 26.95 . 1 352 35 ARG N N 118.88 . 1 353 36 ILE HA H 3.90 . 1 354 36 ILE HB H 2.02 . 1 355 36 ILE HD1 H 0.73 . 1 356 36 ILE HG13 H 1.37 . 1 357 36 ILE HG12 H 1.28 . 1 358 36 ILE HG2 H 0.99 . 1 359 36 ILE H H 7.59 . 1 360 36 ILE C C 177.01 . 1 361 36 ILE CA C 63.01 . 1 362 36 ILE CB C 36.80 . 1 363 36 ILE CD1 C 12.58 . 1 364 36 ILE CG1 C 28.73 . 1 365 36 ILE CG2 C 17.80 . 1 366 36 ILE N N 118.49 . 1 367 37 LYS HA H 3.99 . 1 368 37 LYS HB2 H 1.93 . 1 369 37 LYS HB3 H 1.93 . 1 370 37 LYS HD2 H 1.68 . 1 371 37 LYS HD3 H 1.68 . 1 372 37 LYS HE2 H 2.98 . 1 373 37 LYS HE3 H 2.98 . 1 374 37 LYS HG3 H 1.59 . 1 375 37 LYS HG2 H 1.39 . 1 376 37 LYS H H 7.72 . 1 377 37 LYS C C 178.89 . 1 378 37 LYS CA C 60.37 . 1 379 37 LYS CB C 32.38 . 1 380 37 LYS CD C 29.64 . 1 381 37 LYS CE C 41.95 . 1 382 37 LYS CG C 25.46 . 1 383 37 LYS N N 121.19 . 1 384 38 GLN HA H 4.23 . 1 385 38 GLN HB2 H 2.31 . 1 386 38 GLN HB3 H 2.31 . 1 387 38 GLN HG3 H 2.58 . 1 388 38 GLN HG2 H 2.40 . 1 389 38 GLN H H 7.82 . 1 390 38 GLN HE21 H 7.82 . 1 391 38 GLN HE22 H 6.80 . 1 392 38 GLN C C 178.02 . 1 393 38 GLN CA C 58.98 . 1 394 38 GLN CB C 28.00 . 1 395 38 GLN CG C 33.12 . 1 396 38 GLN N N 119.90 . 1 397 38 GLN NE2 N 111.49 . 1 398 39 ILE HG13 H 2.00 . 1 399 39 ILE HG12 H 0.94 . 1 400 39 ILE HA H 3.70 . 1 401 39 ILE HB H 1.82 . 1 402 39 ILE HD1 H 0.71 . 1 403 39 ILE HG2 H 0.87 . 1 404 39 ILE H H 8.46 . 1 405 39 ILE C C 180.11 . 1 406 39 ILE CA C 65.93 . 1 407 39 ILE CB C 38.12 . 1 408 39 ILE CG2 C 17.19 . 1 409 39 ILE CD1 C 13.61 . 1 410 39 ILE CG1 C 29.05 . 1 411 39 ILE N N 119.66 . 1 412 40 ARG HA H 4.07 . 1 413 40 ARG HD2 H 3.24 . 1 414 40 ARG HD3 H 3.24 . 1 415 40 ARG H H 8.67 . 1 416 40 ARG HB2 H 2.02 . 1 417 40 ARG HB3 H 2.10 . 1 418 40 ARG HG3 H 1.89 . 1 419 40 ARG HG2 H 1.70 . 1 420 40 ARG C C 177.92 . 1 421 40 ARG CA C 60.26 . 1 422 40 ARG CB C 30.63 . 1 423 40 ARG CD C 44.25 . 1 424 40 ARG CG C 28.66 . 1 425 40 ARG N N 123.35 . 1 426 41 HIS HA H 4.33 . 1 427 41 HIS HB2 H 3.36 . 1 428 41 HIS HB3 H 3.36 . 1 429 41 HIS H H 8.01 . 1 430 41 HIS C C 176.93 . 1 431 41 HIS CA C 59.12 . 1 432 41 HIS CB C 29.22 . 1 433 41 HIS N N 117.09 . 1 434 42 GLU HA H 3.97 . 1 435 42 GLU HB2 H 2.02 . 1 436 42 GLU HB3 H 2.02 . 1 437 42 GLU HG3 H 2.51 . 1 438 42 GLU HG2 H 2.34 . 1 439 42 GLU H H 8.79 . 1 440 42 GLU C C 177.76 . 1 441 42 GLU CA C 58.85 . 1 442 42 GLU CB C 30.37 . 1 443 42 GLU CG C 36.71 . 1 444 42 GLU N N 116.55 . 1 445 43 SER HA H 4.40 . 1 446 43 SER HB3 H 4.22 . 1 447 43 SER HB2 H 3.71 . 1 448 43 SER H H 8.21 . 1 449 43 SER C C 175.19 . 1 450 43 SER CA C 60.09 . 1 452 43 SER N N 110.06 . 1 453 44 GLY HA3 H 4.30 . 1 454 44 GLY HA2 H 3.76 . 1 455 44 GLY H H 7.83 . 1 456 44 GLY C C 172.86 . 1 457 44 GLY CA C 45.47 . 1 458 44 GLY N N 110.16 . 1 459 45 ALA HA H 4.36 . 1 460 45 ALA HB H 1.04 . 1 461 45 ALA H H 7.94 . 1 462 45 ALA C C 176.90 . 1 463 45 ALA CA C 51.12 . 1 464 45 ALA CB C 19.65 . 1 465 45 ALA N N 120.62 . 1 466 46 SER HA H 4.65 . 1 467 46 SER HB2 H 3.84 . 1 468 46 SER HB3 H 3.84 . 1 469 46 SER H H 8.66 . 1 470 46 SER C C 174.34 . 1 471 46 SER CA C 57.71 . 1 472 46 SER CB C 63.31 . 1 473 46 SER N N 114.57 . 1 474 47 ILE HA H 4.98 . 1 475 47 ILE HB H 1.45 . 1 476 47 ILE HD1 H 0.69 . 1 477 47 ILE HG13 H 1.47 . 1 478 47 ILE HG12 H 0.85 . 1 479 47 ILE HG2 H 0.68 . 1 480 47 ILE H H 8.16 . 1 481 47 ILE C C 173.79 . 1 482 47 ILE CA C 60.34 . 1 483 47 ILE CB C 41.43 . 1 484 47 ILE CD1 C 14.43 . 1 485 47 ILE CG1 C 27.43 . 1 486 47 ILE CG2 C 17.83 . 1 487 47 ILE N N 124.17 . 1 488 48 LYS HA H 4.69 . 1 489 48 LYS HB3 H 1.72 . 1 490 48 LYS HB2 H 1.68 . 1 491 48 LYS HD2 H 1.63 . 1 492 48 LYS HD3 H 1.63 . 1 493 48 LYS HE2 H 2.92 . 1 494 48 LYS HE3 H 2.92 . 1 495 48 LYS HG3 H 1.37 . 1 496 48 LYS HG2 H 1.31 . 1 497 48 LYS H H 8.86 . 1 498 48 LYS C C 173.79 . 1 499 48 LYS CA C 54.59 . 1 500 48 LYS CB C 35.81 . 1 501 48 LYS CD C 29.29 . 1 502 48 LYS CE C 41.81 . 1 503 48 LYS CG C 24.60 . 1 504 48 LYS N N 128.23 . 1 505 49 ILE HA H 4.69 . 1 506 49 ILE HB H 1.69 . 1 507 49 ILE HD1 H 0.75 . 1 508 49 ILE HG13 H 1.47 . 1 509 49 ILE HG12 H 1.00 . 1 510 49 ILE HG2 H 0.83 . 1 511 49 ILE H H 8.75 . 1 512 49 ILE C C 174.87 . 1 513 49 ILE CA C 60.26 . 1 514 49 ILE CB C 39.35 . 1 515 49 ILE CD1 C 13.91 . 1 516 49 ILE CG1 C 27.82 . 1 517 49 ILE CG2 C 17.06 . 1 518 49 ILE N N 123.42 . 1 519 50 ASP HA H 4.77 . 1 520 50 ASP HB3 H 2.79 . 1 521 50 ASP HB2 H 2.70 . 1 522 50 ASP H H 8.44 . 1 524 50 ASP CA C 54.14 . 1 525 50 ASP CB C 42.34 . 1 526 50 ASP N N 128.11 . 1 527 51 GLU HA H 4.44 . 1 528 51 GLU HB2 H 1.81 . 1 529 51 GLU HB3 H 2.10 . 1 530 51 GLU HG3 H 2.37 . 1 531 51 GLU HG2 H 2.32 . 1 532 51 GLU H H 8.61 . 1 533 51 GLU CA C 54.54 . 1 534 51 GLU CB C 28.80 . 1 535 51 GLU CG C 35.97 . 1 537 52 PRO HA H 4.42 . 1 538 52 PRO HB3 H 2.14 . 1 539 52 PRO HB2 H 1.93 . 1 540 52 PRO HD3 H 3.72 . 1 541 52 PRO HD2 H 3.59 . 1 542 52 PRO HG3 H 2.09 . 1 543 52 PRO HG2 H 1.81 . 1 544 52 PRO C C 176.48 . 1 545 52 PRO CA C 63.12 . 1 546 52 PRO CB C 31.93 . 1 547 52 PRO CD C 50.47 . 1 548 52 PRO CG C 27.57 . 1 549 53 LEU HA H 4.35 . 1 550 53 LEU HB2 H 1.57 . 1 551 53 LEU HB3 H 1.57 . 1 552 53 LEU HD1 H 0.90 . 1 553 53 LEU HD2 H 0.90 . 1 554 53 LEU HG H 1.71 . 1 555 53 LEU H H 8.47 . 1 556 53 LEU C C 177.26 . 1 557 53 LEU CA C 54.59 . 1 558 53 LEU CB C 42.83 . 1 559 53 LEU CD1 C 23.49 . 1 560 53 LEU CD2 C 25.01 . 1 561 53 LEU CG C 27.10 . 1 562 53 LEU N N 123.17 . 1 563 54 GLU HA H 4.09 . 1 564 54 GLU HB2 H 1.98 . 1 565 54 GLU HB3 H 1.98 . 1 566 54 GLU HG2 H 2.26 . 1 567 54 GLU HG3 H 2.26 . 1 568 54 GLU H H 8.55 . 1 569 54 GLU C C 177.38 . 1 570 54 GLU CA C 57.78 . 1 572 54 GLU CG C 35.95 . 1 573 54 GLU N N 121.88 . 1 574 55 GLY HA3 H 4.16 . 1 575 55 GLY HA2 H 3.75 . 1 576 55 GLY H H 8.75 . 1 577 55 GLY C C 173.91 . 1 578 55 GLY CA C 45.58 . 1 579 55 GLY N N 111.91 . 1 580 56 SER HA H 4.57 . 1 581 56 SER HB2 H 3.86 . 1 582 56 SER HB3 H 3.86 . 1 583 56 SER H H 7.93 . 1 584 56 SER C C 174.68 . 1 585 56 SER CA C 57.62 . 1 586 56 SER CB C 64.56 . 1 587 56 SER N N 114.30 . 1 588 57 GLU HA H 4.39 . 1 589 57 GLU HB2 H 1.93 . 1 590 57 GLU HB3 H 2.31 . 1 591 57 GLU HG3 H 2.32 . 1 592 57 GLU HG2 H 2.22 . 1 593 57 GLU H H 8.68 . 1 594 57 GLU C C 175.40 . 1 595 57 GLU CA C 56.52 . 1 596 57 GLU CB C 30.07 . 1 597 57 GLU CG C 36.37 . 1 598 57 GLU N N 121.56 . 1 599 58 ASP HA H 4.93 . 1 600 58 ASP HB2 H 2.35 . 1 601 58 ASP HB3 H 2.45 . 1 602 58 ASP H H 8.12 . 1 603 58 ASP C C 175.66 . 1 604 58 ASP CA C 54.13 . 1 605 58 ASP CB C 42.87 . 1 606 58 ASP N N 119.15 . 1 607 59 ARG HD2 H 3.12 . 1 608 59 ARG HD3 H 3.12 . 1 609 59 ARG HA H 4.67 . 1 610 59 ARG HB2 H 1.38 . 1 611 59 ARG HB3 H 1.69 . 1 612 59 ARG H H 8.86 . 1 613 59 ARG HG2 H 1.48 . 1 614 59 ARG HG3 H 1.48 . 1 615 59 ARG C C 173.90 . 1 616 59 ARG CA C 53.87 . 1 617 59 ARG CB C 32.97 . 1 618 59 ARG CD C 42.72 . 1 619 59 ARG CG C 27.76 . 1 620 59 ARG N N 117.30 . 1 621 60 ILE HA H 4.54 . 1 622 60 ILE HB H 1.69 . 1 623 60 ILE HD1 H 0.75 . 1 624 60 ILE HG13 H 1.43 . 1 625 60 ILE HG12 H 1.06 . 1 626 60 ILE HG2 H 0.70 . 1 627 60 ILE H H 8.36 . 1 628 60 ILE C C 175.48 . 1 629 60 ILE CA C 60.70 . 1 630 60 ILE CB C 39.03 . 1 631 60 ILE CD1 C 12.80 . 1 632 60 ILE CG1 C 27.98 . 1 633 60 ILE CG2 C 17.80 . 1 634 60 ILE N N 121.55 . 1 635 61 ILE HA H 4.92 . 1 636 61 ILE HB H 1.80 . 1 637 61 ILE HD1 H 0.67 . 1 638 61 ILE HG13 H 1.51 . 1 639 61 ILE HG12 H 0.99 . 1 640 61 ILE HG2 H 0.70 . 1 641 61 ILE H H 9.24 . 1 642 61 ILE C C 174.84 . 1 643 61 ILE CA C 59.30 . 1 644 61 ILE CB C 39.25 . 1 645 61 ILE CD1 C 13.83 . 1 646 61 ILE CG2 C 17.74 . 1 647 61 ILE CG1 C 27.80 . 1 648 61 ILE N N 127.67 . 1 649 62 THR HA H 4.90 . 1 650 62 THR HB H 3.89 . 1 651 62 THR HG2 H 1.10 . 1 652 62 THR H H 9.01 . 1 653 62 THR C C 173.82 . 1 654 62 THR CA C 62.47 . 1 655 62 THR CB C 69.53 . 1 656 62 THR CG2 C 21.78 . 1 657 62 THR N N 122.96 . 1 658 63 ILE HG13 H 1.57 . 1 659 63 ILE HG12 H 0.64 . 1 660 63 ILE HA H 4.92 . 1 661 63 ILE HB H 1.64 . 1 662 63 ILE HD1 H 0.64 . 1 663 63 ILE HG2 H 0.75 . 1 664 63 ILE H H 9.18 . 1 665 63 ILE C C 173.97 . 1 666 63 ILE CA C 60.37 . 1 667 63 ILE CB C 40.00 . 1 668 63 ILE CD1 C 14.21 . 1 669 63 ILE CG2 C 19.96 . 1 670 63 ILE CG1 C 27.88 . 1 671 63 ILE N N 128.59 . 1 672 64 THR HA H 5.71 . 1 673 64 THR HB H 3.78 . 1 674 64 THR HG2 H 1.12 . 1 675 64 THR H H 8.94 . 1 676 64 THR C C 173.81 . 1 677 64 THR CA C 60.59 . 1 679 64 THR CG2 C 21.73 . 1 680 64 THR N N 122.19 . 1 681 65 GLY HA2 H 4.28 . 1 682 65 GLY HA3 H 4.28 . 1 683 65 GLY H H 9.07 . 1 684 65 GLY C C 172.03 . 1 685 65 GLY CA C 45.54 . 1 686 65 GLY N N 113.66 . 1 687 66 THR HA H 4.85 . 1 688 66 THR HB H 4.62 . 1 689 66 THR HG2 H 1.12 . 1 690 66 THR H H 8.68 . 1 691 66 THR C C 175.75 . 1 692 66 THR CA C 61.60 . 1 693 66 THR CB C 70.42 . 1 694 66 THR CG2 C 22.17 . 1 695 66 THR N N 110.42 . 1 696 67 GLN HA H 3.91 . 1 697 67 GLN HB3 H 2.12 . 1 698 67 GLN HB2 H 2.07 . 1 699 67 GLN HG2 H 2.36 . 1 700 67 GLN HG3 H 2.36 . 1 701 67 GLN H H 9.44 . 1 702 67 GLN HE21 H 6.80 . 1 703 67 GLN HE22 H 7.42 . 1 704 67 GLN C C 177.69 . 1 705 67 GLN CA C 59.90 . 1 706 67 GLN CB C 28.31 . 1 707 67 GLN CG C 33.45 . 1 708 67 GLN N N 120.08 . 1 709 67 GLN NE2 N 111.14 . 1 710 68 ASP HA H 4.35 . 1 711 68 ASP HB3 H 2.57 . 1 712 68 ASP HB2 H 2.52 . 1 713 68 ASP H H 8.49 . 1 714 68 ASP C C 178.32 . 1 715 68 ASP CA C 57.28 . 1 716 68 ASP CB C 40.73 . 1 717 68 ASP N N 115.82 . 1 718 69 GLN HA H 4.19 . 1 719 69 GLN HB3 H 2.38 . 1 720 69 GLN HB2 H 1.62 . 1 721 69 GLN H H 7.39 . 1 722 69 GLN HE21 H 7.59 . 1 723 69 GLN HE22 H 6.43 . 1 724 69 GLN HG3 H 2.81 . 1 725 69 GLN HG2 H 2.52 . 1 726 69 GLN C C 179.04 . 1 727 69 GLN CA C 58.90 . 1 728 69 GLN CB C 28.41 . 1 729 69 GLN CG C 33.53 . 1 730 69 GLN N N 119.14 . 1 731 69 GLN NE2 N 108.97 . 1 732 70 ILE HA H 3.46 . 1 733 70 ILE HB H 1.77 . 1 734 70 ILE HD1 H 0.68 . 1 735 70 ILE HG13 H 1.41 . 1 736 70 ILE HG12 H 0.87 . 1 737 70 ILE HG2 H 0.73 . 1 738 70 ILE H H 8.62 . 1 739 70 ILE C C 178.06 . 1 740 70 ILE CA C 65.25 . 1 741 70 ILE CB C 37.65 . 1 742 70 ILE CD1 C 14.06 . 1 743 70 ILE CG1 C 28.67 . 1 744 70 ILE CG2 C 17.89 . 1 745 70 ILE N N 117.41 . 1 746 71 GLN HA H 4.05 . 1 747 71 GLN HB3 H 2.15 . 1 748 71 GLN HB2 H 2.10 . 1 749 71 GLN HG3 H 2.47 . 1 750 71 GLN HG2 H 2.39 . 1 751 71 GLN H H 8.25 . 1 752 71 GLN HE21 H 7.34 . 1 753 71 GLN HE22 H 6.83 . 1 754 71 GLN C C 178.75 . 1 755 71 GLN CA C 59.03 . 1 756 71 GLN CB C 28.19 . 1 757 71 GLN CG C 34.24 . 1 758 71 GLN N N 119.35 . 1 759 71 GLN NE2 N 111.38 . 1 760 72 ASN HA H 4.62 . 1 761 72 ASN HB2 H 2.97 . 1 762 72 ASN HB3 H 2.75 . 1 763 72 ASN H H 8.00 . 1 764 72 ASN HD21 H 7.63 . 1 765 72 ASN HD22 H 6.85 . 1 766 72 ASN C C 177.15 . 1 767 72 ASN CA C 56.06 . 1 768 72 ASN CB C 38.48 . 1 769 72 ASN N N 117.98 . 1 770 72 ASN ND2 N 110.76 . 1 771 73 ALA HA H 3.88 . 1 772 73 ALA HB H 1.39 . 1 773 73 ALA H H 8.63 . 1 774 73 ALA C C 178.90 . 1 775 73 ALA CA C 55.99 . 1 776 73 ALA CB C 18.17 . 1 777 73 ALA N N 121.16 . 1 778 74 GLN HA H 3.81 . 1 779 74 GLN HB3 H 2.20 . 1 780 74 GLN HB2 H 2.03 . 1 781 74 GLN HG3 H 2.45 . 1 782 74 GLN HG2 H 2.00 . 1 783 74 GLN H H 8.68 . 1 784 74 GLN HE21 H 6.73 . 1 785 74 GLN HE22 H 6.65 . 1 786 74 GLN C C 177.95 . 1 787 74 GLN CA C 60.29 . 1 788 74 GLN CB C 28.75 . 1 789 74 GLN CG C 35.36 . 1 790 74 GLN N N 115.36 . 1 791 74 GLN NE2 N 108.54 . 1 792 75 TYR HD1 H 7.18 . 1 793 75 TYR HE1 H 7.18 . 1 794 75 TYR HE2 H 7.18 . 1 795 75 TYR HA H 4.27 . 1 796 75 TYR HB2 H 3.26 . 1 797 75 TYR HB3 H 3.26 . 1 798 75 TYR H H 8.02 . 1 799 75 TYR C C 178.00 . 1 800 75 TYR CA C 61.02 . 1 801 75 TYR CB C 37.94 . 1 802 75 TYR CD1 C 133.05 . 1 803 75 TYR CE1 C 133.05 . 1 804 75 TYR CE2 C 133.05 . 1 805 75 TYR N N 120.05 . 1 806 76 LEU HA H 3.89 . 1 807 76 LEU HB2 H 1.98 . 1 808 76 LEU HB3 H 1.33 . 1 809 76 LEU HD1 H 0.94 . 1 810 76 LEU HD2 H 0.94 . 1 811 76 LEU HG H 2.10 . 1 812 76 LEU H H 8.19 . 1 813 76 LEU C C 180.58 . 1 814 76 LEU CA C 57.72 . 1 815 76 LEU CB C 42.97 . 1 816 76 LEU CD1 C 27.00 . 1 817 76 LEU CD2 C 22.40 . 1 818 76 LEU CG C 27.22 . 1 819 76 LEU N N 118.93 . 1 820 77 LEU HA H 3.85 . 1 821 77 LEU HB2 H 1.86 . 1 822 77 LEU HB3 H 1.26 . 1 823 77 LEU HD1 H 0.70 . 1 824 77 LEU HD2 H 0.70 . 1 825 77 LEU HG H 1.74 . 1 826 77 LEU H H 8.71 . 1 827 77 LEU C C 178.27 . 1 828 77 LEU CA C 58.26 . 1 829 77 LEU CB C 42.01 . 1 830 77 LEU CD1 C 25.70 . 1 831 77 LEU CD2 C 24.55 . 1 832 77 LEU CG C 27.03 . 1 833 77 LEU N N 121.10 . 1 834 78 GLN HA H 4.04 . 1 835 78 GLN HB2 H 2.09 . 1 836 78 GLN HB3 H 2.09 . 1 837 78 GLN HG3 H 2.41 . 1 838 78 GLN HG2 H 2.35 . 1 839 78 GLN H H 8.14 . 1 840 78 GLN HE21 H 7.29 . 1 841 78 GLN HE22 H 6.79 . 1 842 78 GLN C C 177.79 . 1 843 78 GLN CA C 58.27 . 1 844 78 GLN CB C 28.30 . 1 845 78 GLN CG C 33.78 . 1 846 78 GLN N N 117.00 . 1 847 78 GLN NE2 N 110.41 . 1 848 79 ASN HA H 4.51 . 1 849 79 ASN HB2 H 2.50 . 1 850 79 ASN HB3 H 2.64 . 1 851 79 ASN H H 7.94 . 1 852 79 ASN HD21 H 7.20 . 1 853 79 ASN HD22 H 6.40 . 1 854 79 ASN C C 176.37 . 1 855 79 ASN CA C 55.04 . 1 856 79 ASN CB C 38.46 . 1 857 79 ASN N N 116.43 . 1 858 79 ASN ND2 N 111.83 . 1 859 80 SER HA H 4.34 . 1 860 80 SER HB2 H 4.02 . 1 861 80 SER HB3 H 3.89 . 1 862 80 SER H H 7.78 . 1 863 80 SER C C 174.48 . 1 864 80 SER CA C 61.31 . 1 865 80 SER CB C 63.52 . 1 866 80 SER N N 114.94 . 1 867 81 VAL HA H 4.03 . 1 868 81 VAL HB H 2.26 . 1 869 81 VAL HG1 H 0.97 . 1 870 81 VAL HG2 H 0.93 . 1 871 81 VAL H H 7.76 . 1 872 81 VAL C C 176.84 . 1 873 81 VAL CA C 63.67 . 1 874 81 VAL CB C 32.17 . 1 875 81 VAL CG1 C 21.18 . 1 876 81 VAL CG2 C 21.72 . 1 877 81 VAL N N 118.41 . 1 878 82 LYS HA H 4.09 . 1 879 82 LYS HB2 H 1.80 . 1 880 82 LYS HB3 H 1.80 . 1 881 82 LYS HD2 H 1.60 . 1 882 82 LYS HD3 H 1.60 . 1 883 82 LYS HE2 H 2.91 . 1 884 82 LYS HE3 H 2.91 . 1 885 82 LYS HG2 H 1.39 . 1 886 82 LYS HG3 H 1.39 . 1 887 82 LYS H H 8.01 . 1 888 82 LYS C C 177.16 . 1 889 82 LYS CA C 57.87 . 1 890 82 LYS CB C 32.51 . 1 891 82 LYS CD C 29.06 . 1 892 82 LYS CE C 41.91 . 1 893 82 LYS CG C 24.94 . 1 894 82 LYS N N 121.46 . 1 895 83 GLN HA H 4.15 . 1 896 83 GLN HB2 H 1.92 . 1 897 83 GLN HB3 H 1.92 . 1 898 83 GLN HG3 H 2.20 . 1 899 83 GLN HG2 H 2.07 . 1 900 83 GLN H H 8.15 . 1 901 83 GLN HE21 H 7.34 . 1 902 83 GLN HE22 H 6.77 . 1 903 83 GLN C C 176.02 . 1 904 83 GLN CA C 56.86 . 1 905 83 GLN CB C 28.82 . 1 906 83 GLN CG C 33.51 . 1 907 83 GLN N N 118.29 . 1 908 83 GLN NE2 N 111.25 . 1 909 84 TYR HD1 H 7.18 . 1 910 84 TYR HE1 H 7.18 . 1 911 84 TYR HE2 H 7.18 . 1 912 84 TYR HA H 4.58 . 1 913 84 TYR HB2 H 2.92 . 1 914 84 TYR HB3 H 3.15 . 1 915 84 TYR H H 8.00 . 1 916 84 TYR C C 175.70 . 1 917 84 TYR CA C 58.40 . 1 918 84 TYR CB C 38.92 . 1 919 84 TYR CD1 C 133.13 . 1 920 84 TYR CE1 C 133.13 . 1 921 84 TYR CE2 C 133.13 . 1 922 84 TYR N N 118.92 . 1 923 85 SER HA H 4.41 . 1 924 85 SER HB2 H 3.89 . 1 925 85 SER HB3 H 3.89 . 1 926 85 SER H H 8.17 . 1 927 85 SER C C 174.53 . 1 928 85 SER CA C 58.67 . 1 930 85 SER N N 116.24 . 1 931 86 GLY HA2 H 3.86 . 1 932 86 GLY HA3 H 3.86 . 1 933 86 GLY H H 7.87 . 1 934 86 GLY C C 173.03 . 1 935 86 GLY CA C 45.23 . 1 936 86 GLY N N 109.79 . 1 937 87 LYS HA H 4.27 . 1 938 87 LYS HB2 H 1.62 . 1 939 87 LYS HB3 H 1.62 . 1 940 87 LYS HE2 H 2.90 . 1 941 87 LYS HE3 H 2.90 . 1 942 87 LYS HG2 H 1.22 . 1 943 87 LYS HG3 H 1.22 . 1 944 87 LYS HD2 H 1.57 . 1 945 87 LYS HD3 H 1.57 . 1 946 87 LYS H H 7.87 . 1 947 87 LYS C C 175.41 . 1 948 87 LYS CA C 55.80 . 1 949 87 LYS CB C 33.32 . 1 950 87 LYS CE C 41.94 . 1 951 87 LYS CD C 28.93 . 1 952 87 LYS CG C 24.59 . 1 953 87 LYS N N 119.46 . 1 954 88 PHE HA H 4.58 . 1 955 88 PHE HB3 H 3.04 . 1 956 88 PHE HB2 H 2.81 . 1 957 88 PHE H H 8.19 . 1 stop_ save_