data_4405 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; C-TERMINAL KH DOMAIN OF HNRNP K (KH3) ; _BMRB_accession_number 4405 _BMRB_flat_file_name bmr4405.str _Entry_type original _Submission_date 1999-09-15 _Accession_date 1999-09-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 BABER J. . . 2 LIBUTTI D. . . 3 LEVENS D. . . 4 TJANDRA N. . . stop_ 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_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-11-29 original author . stop_ _Original_release_date 1999-11-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _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 _CAS_abstract_code . _MEDLINE_UI_code 99299390 _PubMed_ID ? 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_volume 289 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 949 _Page_last 962 _Year 1999 _Details . loop_ _Keyword C-MYC 'DIPOLAR COUPLING' DNA-BINDING 'HNRNP K' 'KH DOMAIN' NMR RNA-BINDING 'THREE-DIMENSIONAL STRUCTURE' stop_ save_ ################################## # Molecular system description # ################################## save_hnRNP_K _Saveframe_category molecular_system _Mol_system_name 'hnRNP K' _Abbreviation_common 'hnRNP K' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hnRNP K subunit 1' $KH3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . 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 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # 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 . _Sequence_homology_query_revised_last_date 2015-06-02 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 "C-Terminal Kh Domain Of Hnrnp K (Kh3)" 100.00 89 100.00 100.00 5.15e-55 PDB 1ZZI "Crystal Structure Analysis Of The Third Kh Domain Of Hnrnp K In Complex With Ssdna" 88.76 82 98.73 98.73 9.60e-46 PDB 1ZZJ "Structure Of The Third Kh Domain Of Hnrnp K In Complex With 15-Mer Ssdna" 88.76 82 98.73 98.73 9.60e-46 PDB 1ZZK "Crystal Structure Of The Third Kh Domain Of Hnrnp K At 0.95a Resolution" 88.76 82 98.73 98.73 9.60e-46 GB EGW07100 "Kinesin-like protein KIF27 [Cricetulus griseus]" 80.90 1648 98.61 98.61 1.96e-36 GB EMP30398 "Heterogeneous nuclear ribonucleoprotein K [Chelonia mydas]" 80.90 384 98.61 98.61 5.48e-37 GB ERE80796 "heterogeneous nuclear ribonucleoprotein K-like isoform 1 [Cricetulus griseus]" 87.64 459 97.44 98.72 1.58e-40 GB ERE80797 "heterogeneous nuclear ribonucleoprotein K-like isoform 2 [Cricetulus griseus]" 92.13 458 98.78 98.78 2.19e-44 REF XP_011972837 "PREDICTED: heterogeneous nuclear ribonucleoprotein K isoform X1 [Ovis aries]" 87.64 459 97.44 98.72 1.59e-40 REF XP_011972846 "PREDICTED: heterogeneous nuclear ribonucleoprotein K isoform X2 [Ovis aries]" 92.13 458 98.78 98.78 2.15e-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 _Vector_name $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 _Details . 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 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 5 . mM pH* 5.5 0.1 n/a pressure 1 . atm temperature 300 0.4 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.251449530 $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 1.000 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . 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' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 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 56.43 . 1 5 . 2 SER CB C 63.19 . 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 176.53 . 1 14 . 3 PRO CA C 63.67 . 1 15 . 3 PRO CB C 32.13 . 1 16 . 3 PRO CD C 50.99 . 1 17 . 3 PRO CG C 27.50 . 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 175.09 . 1 23 . 4 ASN CA C 53.42 . 1 24 . 4 ASN CB C 39.04 . 1 25 . 4 ASN N N 117.83 . 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 174.15 . 1 31 . 5 SER CA C 58.52 . 1 32 . 5 SER CB C 63.92 . 1 33 . 5 SER N N 115.52 . 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 176.31 . 1 39 . 6 TYR CA C 58.29 . 1 40 . 6 TYR CB C 38.75 . 1 41 . 6 TYR N N 121.28 . 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 173.78 . 1 46 . 7 GLY CA C 45.57 . 1 47 . 7 GLY N N 109.58 . 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 176.54 . 1 53 . 8 ASP CA C 54.67 . 1 54 . 8 ASP CB C 41.35 . 1 55 . 8 ASP N N 120.31 . 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 178.09 . 1 64 . 9 LEU CA C 55.70 . 1 65 . 9 LEU CB C 42.19 . 1 66 . 9 LEU CD1 C 25.27 . 1 67 . 9 LEU CD2 C 23.45 . 1 68 . 9 LEU CG C 27.24 . 1 69 . 9 LEU N N 121.99 . 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 73 . 10 GLY C C 174.33 . 1 74 . 10 GLY CA C 45.62 . 1 75 . 10 GLY N N 108.56 . 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 44.73 . 1 80 . 11 GLY N N 108.67 . 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 175.94 . 1 89 . 12 PRO CA C 63.04 . 1 90 . 12 PRO CB C 32.50 . 1 91 . 12 PRO CD C 49.98 . 1 92 . 12 PRO CG C 27.34 . 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 175.86 . 1 101 . 13 ILE CA C 60.42 . 1 102 . 13 ILE CB C 37.00 . 1 103 . 13 ILE CD1 C 11.51 . 1 104 . 13 ILE CG1 C 27.47 . 1 105 . 13 ILE CG2 C 18.36 . 1 106 . 13 ILE N N 120.56 . 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 173.63 . 1 115 . 14 ILE CA C 60.21 . 1 116 . 14 ILE CB C 41.68 . 1 117 . 14 ILE CD1 C 13.87 . 1 118 . 14 ILE CG1 C 26.98 . 1 119 . 14 ILE CG2 C 18.21 . 1 120 . 14 ILE N N 128.87 . 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 174.08 . 1 126 . 15 THR CA C 61.44 . 1 127 . 15 THR CB C 71.85 . 1 128 . 15 THR CG2 C 21.85 . 1 129 . 15 THR N N 116.10 . 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 181.39 . 1 135 . 16 THR CA C 60.55 . 1 136 . 16 THR CB C 71.33 . 1 137 . 16 THR CG2 C 20.57 . 1 138 . 16 THR N N 122.22 . 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 175.34 . 1 148 . 17 GLN CA C 54.48 . 1 149 . 17 GLN CB C 32.58 . 1 150 . 17 GLN CG C 34.62 . 1 151 . 17 GLN N N 121.74 . 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 173.96 . 1 159 . 18 VAL CA C 60.53 . 1 160 . 18 VAL CB C 35.68 . 1 161 . 18 VAL CG1 C 21.43 . 1 162 . 18 VAL CG2 C 20.73 . 1 163 . 18 VAL N N 120.81 . 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 . 1 168 . 19 THR C C 174.16 . 1 169 . 19 THR CA C 61.82 . 1 170 . 19 THR CB C 69.77 . 1 171 . 19 THR CG2 C 21.97 . 1 172 . 19 THR N N 119.93 . 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 56.99 . 1 181 . 20 ILE CB C 40.48 . 1 182 . 20 ILE CD1 C 13.58 . 1 183 . 20 ILE CG1 C 26.21 . 1 184 . 20 ILE CG2 C 17.84 . 1 185 . 20 ILE N N 122.46 . 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 178.49 . 1 194 . 21 PRO CA C 62.81 . 1 195 . 21 PRO CB C 33.03 . 1 196 . 21 PRO CD C 51.48 . 1 197 . 21 PRO CG C 28.08 . 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 178.10 . 1 209 . 22 LYS CA C 60.44 . 1 210 . 22 LYS CB C 32.93 . 1 211 . 22 LYS CD C 29.83 . 1 212 . 22 LYS CE C 42.13 . 1 213 . 22 LYS CG C 24.42 . 1 214 . 22 LYS N N 121.99 . 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 177.92 . 1 220 . 23 ASP CA C 57.28 . 1 221 . 23 ASP CB C 40.15 . 1 222 . 23 ASP N N 118.24 . 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 178.41 . 1 231 . 24 LEU CA C 56.47 . 1 232 . 24 LEU CB C 42.12 . 1 233 . 24 LEU CD1 C 24.60 . 1 234 . 24 LEU CD2 C 24.60 . 1 235 . 24 LEU CG C 27.73 . 1 236 . 24 LEU N N 119.90 . 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 178.30 . 1 241 . 25 ALA CA C 55.78 . 1 242 . 25 ALA CB C 18.02 . 1 243 . 25 ALA N N 120.77 . 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 178.71 . 1 253 . 26 ARG CA C 59.67 . 1 254 . 26 ARG CB C 29.95 . 1 255 . 26 ARG CD C 43.53 . 1 256 . 26 ARG CG C 27.53 . 1 257 . 26 ARG N N 115.20 . 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 175.37 . 1 263 . 27 SER CA C 61.30 . 1 264 . 27 SER CB C 63.38 . 1 265 . 27 SER N N 113.83 . 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 175.41 . 1 274 . 28 ILE CA C 63.84 . 1 275 . 28 ILE CB C 38.68 . 1 276 . 28 ILE CD1 C 14.17 . 1 277 . 28 ILE CG1 C 28.53 . 1 278 . 28 ILE CG2 C 17.93 . 1 279 . 28 ILE N N 118.63 . 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 178.01 . 1 288 . 29 ILE CA C 63.71 . 1 289 . 29 ILE CB C 38.99 . 1 290 . 29 ILE CD1 C 13.64 . 1 291 . 29 ILE CG1 C 28.61 . 1 292 . 29 ILE CG2 C 18.06 . 1 293 . 29 ILE N N 115.78 . 1 294 . 30 GLY HA2 H 4.05 . 1 295 . 30 GLY HA3 H 4.05 . 1 296 . 30 GLY H H 7.56 . 1 297 . 30 GLY C C 174.24 . 1 298 . 30 GLY CA C 44.79 . 1 299 . 30 GLY N N 105.70 . 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 57.80 . 1 311 . 31 LYS CB C 31.62 . 1 312 . 31 LYS CD C 29.34 . 1 313 . 31 LYS CE C 42.12 . 1 314 . 31 LYS CG C 25.11 . 1 315 . 31 LYS N N 121.91 . 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 175.39 . 1 320 . 32 GLY CA C 46.43 . 1 321 . 32 GLY N N 112.59 . 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 176.05 . 1 326 . 33 GLY CA C 46.34 . 1 327 . 33 GLY N N 106.97 . 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 177.99 . 1 335 . 34 GLN CA C 59.42 . 1 336 . 34 GLN CB C 28.97 . 1 337 . 34 GLN CG C 33.83 . 1 338 . 34 GLN N N 118.21 . 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 178.47 . 1 348 . 35 ARG CA C 58.55 . 1 349 . 35 ARG CB C 29.05 . 1 350 . 35 ARG CD C 42.91 . 1 351 . 35 ARG CG C 27.13 . 1 352 . 35 ARG N N 119.08 . 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 177.18 . 1 361 . 36 ILE CA C 63.19 . 1 362 . 36 ILE CB C 36.98 . 1 363 . 36 ILE CD1 C 12.76 . 1 364 . 36 ILE CG1 C 28.91 . 1 365 . 36 ILE CG2 C 17.98 . 1 366 . 36 ILE N N 118.69 . 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 179.06 . 1 378 . 37 LYS CA C 60.55 . 1 379 . 37 LYS CB C 32.56 . 1 380 . 37 LYS CD C 29.82 . 1 381 . 37 LYS CE C 42.13 . 1 382 . 37 LYS CG C 25.64 . 1 383 . 37 LYS N N 121.39 . 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 178.19 . 1 393 . 38 GLN CA C 59.16 . 1 394 . 38 GLN CB C 28.18 . 1 395 . 38 GLN CG C 33.30 . 1 396 . 38 GLN N N 120.10 . 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 180.28 . 1 406 . 39 ILE CA C 66.11 . 1 407 . 39 ILE CB C 38.30 . 1 408 . 39 ILE CG2 C 17.37 . 1 409 . 39 ILE CD1 C 13.79 . 1 410 . 39 ILE CG1 C 29.23 . 1 411 . 39 ILE N N 119.86 . 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 178.09 . 1 421 . 40 ARG CA C 60.44 . 1 422 . 40 ARG CB C 30.81 . 1 423 . 40 ARG CD C 44.43 . 1 424 . 40 ARG CG C 28.84 . 1 425 . 40 ARG N N 123.55 . 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 177.10 . 1 431 . 41 HIS CA C 59.30 . 1 432 . 41 HIS CB C 29.40 . 1 433 . 41 HIS N N 117.29 . 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 177.93 . 1 441 . 42 GLU CA C 59.03 . 1 442 . 42 GLU CB C 30.55 . 1 443 . 42 GLU CG C 36.89 . 1 444 . 42 GLU N N 116.75 . 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 175.36 . 1 450 . 43 SER CA C 60.27 . 1 451 . 43 SER CB C 65.59 . 1 452 . 43 SER N N 110.26 . 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 173.03 . 1 457 . 44 GLY CA C 45.65 . 1 458 . 44 GLY N N 110.36 . 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 177.07 . 1 463 . 45 ALA CA C 51.30 . 1 464 . 45 ALA CB C 19.83 . 1 465 . 45 ALA N N 120.82 . 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 174.51 . 1 471 . 46 SER CA C 57.89 . 1 472 . 46 SER CB C 63.49 . 1 473 . 46 SER N N 114.77 . 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 173.96 . 1 482 . 47 ILE CA C 60.52 . 1 483 . 47 ILE CB C 41.61 . 1 484 . 47 ILE CD1 C 14.61 . 1 485 . 47 ILE CG1 C 27.61 . 1 486 . 47 ILE CG2 C 18.01 . 1 487 . 47 ILE N N 124.37 . 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 173.96 . 1 499 . 48 LYS CA C 54.77 . 1 500 . 48 LYS CB C 35.99 . 1 501 . 48 LYS CD C 29.47 . 1 502 . 48 LYS CE C 41.99 . 1 503 . 48 LYS CG C 24.78 . 1 504 . 48 LYS N N 128.43 . 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 175.04 . 1 513 . 49 ILE CA C 60.44 . 1 514 . 49 ILE CB C 39.53 . 1 515 . 49 ILE CD1 C 14.09 . 1 516 . 49 ILE CG1 C 28.00 . 1 517 . 49 ILE CG2 C 17.24 . 1 518 . 49 ILE N N 123.62 . 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 . 1 523 . 50 ASP C C 176.41 . 1 524 . 50 ASP CA C 54.32 . 1 525 . 50 ASP CB C 42.52 . 1 526 . 50 ASP N N 128.31 . 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 54.72 . 1 534 . 51 GLU CB C 28.98 . 1 535 . 51 GLU CG C 36.15 . 1 536 . 51 GLU N N 120.45 . 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 176.65 . 1 545 . 52 PRO CA C 63.30 . 1 546 . 52 PRO CB C 32.11 . 1 547 . 52 PRO CD C 50.65 . 1 548 . 52 PRO CG C 27.75 . 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 177.43 . 1 557 . 53 LEU CA C 54.77 . 1 558 . 53 LEU CB C 43.01 . 1 559 . 53 LEU CD1 C 23.67 . 1 560 . 53 LEU CD2 C 25.19 . 1 561 . 53 LEU CG C 27.28 . 1 562 . 53 LEU N N 123.37 . 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 177.55 . 1 570 . 54 GLU CA C 57.96 . 1 571 . 54 GLU CB C 29.53 . 1 572 . 54 GLU CG C 36.13 . 1 573 . 54 GLU N N 122.08 . 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 174.08 . 1 578 . 55 GLY CA C 45.76 . 1 579 . 55 GLY N N 112.11 . 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 174.85 . 1 585 . 56 SER CA C 57.80 . 1 586 . 56 SER CB C 64.74 . 1 587 . 56 SER N N 114.50 . 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 175.57 . 1 595 . 57 GLU CA C 56.70 . 1 596 . 57 GLU CB C 30.25 . 1 597 . 57 GLU CG C 36.55 . 1 598 . 57 GLU N N 121.76 . 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 175.83 . 1 604 . 58 ASP CA C 54.31 . 1 605 . 58 ASP CB C 43.05 . 1 606 . 58 ASP N N 119.35 . 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 174.07 . 1 616 . 59 ARG CA C 54.05 . 1 617 . 59 ARG CB C 33.15 . 1 618 . 59 ARG CD C 42.90 . 1 619 . 59 ARG CG C 27.94 . 1 620 . 59 ARG N N 117.50 . 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 175.65 . 1 629 . 60 ILE CA C 60.88 . 1 630 . 60 ILE CB C 39.21 . 1 631 . 60 ILE CD1 C 12.98 . 1 632 . 60 ILE CG1 C 28.16 . 1 633 . 60 ILE CG2 C 17.98 . 1 634 . 60 ILE N N 121.75 . 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 175.01 . 1 643 . 61 ILE CA C 59.48 . 1 644 . 61 ILE CB C 39.43 . 1 645 . 61 ILE CD1 C 14.01 . 1 646 . 61 ILE CG2 C 17.92 . 1 647 . 61 ILE CG1 C 27.98 . 1 648 . 61 ILE N N 127.87 . 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 173.99 . 1 654 . 62 THR CA C 62.65 . 1 655 . 62 THR CB C 69.71 . 1 656 . 62 THR CG2 C 21.96 . 1 657 . 62 THR N N 123.16 . 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 174.14 . 1 666 . 63 ILE CA C 60.55 . 1 667 . 63 ILE CB C 40.18 . 1 668 . 63 ILE CD1 C 14.39 . 1 669 . 63 ILE CG2 C 20.14 . 1 670 . 63 ILE CG1 C 28.06 . 1 671 . 63 ILE N N 128.79 . 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 173.98 . 1 677 . 64 THR CA C 60.77 . 1 678 . 64 THR CB C 72.20 . 1 679 . 64 THR CG2 C 21.91 . 1 680 . 64 THR N N 122.39 . 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 172.20 . 1 685 . 65 GLY CA C 45.72 . 1 686 . 65 GLY N N 113.86 . 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 175.92 . 1 692 . 66 THR CA C 61.78 . 1 693 . 66 THR CB C 70.60 . 1 694 . 66 THR CG2 C 22.35 . 1 695 . 66 THR N N 110.62 . 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 177.86 . 1 705 . 67 GLN CA C 60.08 . 1 706 . 67 GLN CB C 28.49 . 1 707 . 67 GLN CG C 33.63 . 1 708 . 67 GLN N N 120.28 . 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 178.49 . 1 715 . 68 ASP CA C 57.46 . 1 716 . 68 ASP CB C 40.91 . 1 717 . 68 ASP N N 116.02 . 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 179.21 . 1 727 . 69 GLN CA C 59.08 . 1 728 . 69 GLN CB C 28.59 . 1 729 . 69 GLN CG C 33.71 . 1 730 . 69 GLN N N 119.34 . 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 178.23 . 1 740 . 70 ILE CA C 65.43 . 1 741 . 70 ILE CB C 37.83 . 1 742 . 70 ILE CD1 C 14.24 . 1 743 . 70 ILE CG1 C 28.85 . 1 744 . 70 ILE CG2 C 18.07 . 1 745 . 70 ILE N N 117.61 . 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 178.92 . 1 755 . 71 GLN CA C 59.21 . 1 756 . 71 GLN CB C 28.37 . 1 757 . 71 GLN CG C 34.42 . 1 758 . 71 GLN N N 119.55 . 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 177.32 . 1 767 . 72 ASN CA C 56.24 . 1 768 . 72 ASN CB C 38.66 . 1 769 . 72 ASN N N 118.18 . 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 179.07 . 1 775 . 73 ALA CA C 56.17 . 1 776 . 73 ALA CB C 18.35 . 1 777 . 73 ALA N N 121.36 . 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 178.12 . 1 787 . 74 GLN CA C 60.47 . 1 788 . 74 GLN CB C 28.93 . 1 789 . 74 GLN CG C 35.54 . 1 790 . 74 GLN N N 115.56 . 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 178.17 . 1 800 . 75 TYR CA C 61.20 . 1 801 . 75 TYR CB C 38.12 . 1 802 . 75 TYR CD1 C 133.23 . 1 803 . 75 TYR CE1 C 133.23 . 1 804 . 75 TYR CE2 C 133.23 . 1 805 . 75 TYR N N 120.25 . 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 180.75 . 1 814 . 76 LEU CA C 57.90 . 1 815 . 76 LEU CB C 43.15 . 1 816 . 76 LEU CD1 C 27.18 . 1 817 . 76 LEU CD2 C 22.58 . 1 818 . 76 LEU CG C 27.40 . 1 819 . 76 LEU N N 119.13 . 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 178.44 . 1 828 . 77 LEU CA C 58.44 . 1 829 . 77 LEU CB C 42.19 . 1 830 . 77 LEU CD1 C 25.88 . 1 831 . 77 LEU CD2 C 24.73 . 1 832 . 77 LEU CG C 27.21 . 1 833 . 77 LEU N N 121.30 . 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 177.96 . 1 843 . 78 GLN CA C 58.45 . 1 844 . 78 GLN CB C 28.48 . 1 845 . 78 GLN CG C 33.96 . 1 846 . 78 GLN N N 117.20 . 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 176.54 . 1 855 . 79 ASN CA C 55.22 . 1 856 . 79 ASN CB C 38.64 . 1 857 . 79 ASN N N 116.63 . 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 174.65 . 1 864 . 80 SER CA C 61.49 . 1 865 . 80 SER CB C 63.70 . 1 866 . 80 SER N N 115.14 . 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 177.01 . 1 873 . 81 VAL CA C 63.85 . 1 874 . 81 VAL CB C 32.35 . 1 875 . 81 VAL CG1 C 21.36 . 1 876 . 81 VAL CG2 C 21.90 . 1 877 . 81 VAL N N 118.61 . 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 177.33 . 1 889 . 82 LYS CA C 58.05 . 1 890 . 82 LYS CB C 32.69 . 1 891 . 82 LYS CD C 29.24 . 1 892 . 82 LYS CE C 42.09 . 1 893 . 82 LYS CG C 25.12 . 1 894 . 82 LYS N N 121.66 . 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 176.19 . 1 904 . 83 GLN CA C 57.04 . 1 905 . 83 GLN CB C 29.00 . 1 906 . 83 GLN CG C 33.69 . 1 907 . 83 GLN N N 118.49 . 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 175.87 . 1 917 . 84 TYR CA C 58.58 . 1 918 . 84 TYR CB C 39.10 . 1 919 . 84 TYR CD1 C 133.31 . 1 920 . 84 TYR CE1 C 133.31 . 1 921 . 84 TYR CE2 C 133.31 . 1 922 . 84 TYR N N 119.12 . 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 174.70 . 1 928 . 85 SER CA C 58.85 . 1 929 . 85 SER CB C 64.13 . 1 930 . 85 SER N N 116.44 . 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 173.20 . 1 935 . 86 GLY CA C 45.41 . 1 936 . 86 GLY N N 109.99 . 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 175.58 . 1 948 . 87 LYS CA C 55.98 . 1 949 . 87 LYS CB C 33.50 . 1 950 . 87 LYS CE C 42.12 . 1 951 . 87 LYS CD C 29.11 . 1 952 . 87 LYS CG C 24.77 . 1 953 . 87 LYS N N 119.66 . 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 . 1 958 . 88 PHE C C 174.29 . 1 959 . 88 PHE CA C 57.85 . 1 960 . 88 PHE CB C 40.03 . 1 961 . 88 PHE N N 120.66 . 1 stop_ save_