data_5606 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H 13C and 15N chemical shift assignments for HI0719 ; _BMRB_accession_number 5606 _BMRB_flat_file_name bmr5606.str _Entry_type original _Submission_date 2002-12-02 _Accession_date 2002-12-02 _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 Parsons Lisa . . 2 Orban John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 622 "13C chemical shifts" 441 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-02 original author . stop_ _Original_release_date 2003-06-02 save_ ############################# # Citation for this entry # ############################# save_HI0719_paper _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Functional Ligand Screening of HI0719, a Highly Conserved Protein from Bacteria to Humans in the YjgF/YER057c/UK114 Family ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22403672 _PubMed_ID 12515541 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Parsons Lisa . . 2 Bonander Nicklas . . 3 Eisenstein Edward . . 4 Gilson Michael . . 5 Kairys Visvaldas . . 6 Orban John . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 42 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 80 _Page_last 89 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_HI0719_homotrimer _Saveframe_category molecular_system _Mol_system_name 'HI0719 homotrimer' _Abbreviation_common HI0719 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HI0719 homotrimer 1' $HI0719 'HI0719 homotrimer 2' $HI0719 'HI0719 homotrimer 3' $HI0719 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state trimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'HI0719 homotrimer 1' 2 'HI0719 homotrimer 2' 3 'HI0719 homotrimer 3' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HI0719 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HI0719 _Abbreviation_common HI0719 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MMTQIIHTEKAPAAIGPYVQ AVDLGNLVLTSGQIPVNPAT GEVPADIVAQARQSLENVKA IIEKAGLTAADIVKTTVFVK DLNDFAAVNAEYERFFKENN HPNFPARSCVEVARLPKDVG LEIEAIAVRK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 MET 3 3 THR 4 4 GLN 5 5 ILE 6 6 ILE 7 7 HIS 8 8 THR 9 9 GLU 10 10 LYS 11 11 ALA 12 12 PRO 13 13 ALA 14 14 ALA 15 15 ILE 16 16 GLY 17 17 PRO 18 18 TYR 19 19 VAL 20 20 GLN 21 21 ALA 22 22 VAL 23 23 ASP 24 24 LEU 25 25 GLY 26 26 ASN 27 27 LEU 28 28 VAL 29 29 LEU 30 30 THR 31 31 SER 32 32 GLY 33 33 GLN 34 34 ILE 35 35 PRO 36 36 VAL 37 37 ASN 38 38 PRO 39 39 ALA 40 40 THR 41 41 GLY 42 42 GLU 43 43 VAL 44 44 PRO 45 45 ALA 46 46 ASP 47 47 ILE 48 48 VAL 49 49 ALA 50 50 GLN 51 51 ALA 52 52 ARG 53 53 GLN 54 54 SER 55 55 LEU 56 56 GLU 57 57 ASN 58 58 VAL 59 59 LYS 60 60 ALA 61 61 ILE 62 62 ILE 63 63 GLU 64 64 LYS 65 65 ALA 66 66 GLY 67 67 LEU 68 68 THR 69 69 ALA 70 70 ALA 71 71 ASP 72 72 ILE 73 73 VAL 74 74 LYS 75 75 THR 76 76 THR 77 77 VAL 78 78 PHE 79 79 VAL 80 80 LYS 81 81 ASP 82 82 LEU 83 83 ASN 84 84 ASP 85 85 PHE 86 86 ALA 87 87 ALA 88 88 VAL 89 89 ASN 90 90 ALA 91 91 GLU 92 92 TYR 93 93 GLU 94 94 ARG 95 95 PHE 96 96 PHE 97 97 LYS 98 98 GLU 99 99 ASN 100 100 ASN 101 101 HIS 102 102 PRO 103 103 ASN 104 104 PHE 105 105 PRO 106 106 ALA 107 107 ARG 108 108 SER 109 109 CYS 110 110 VAL 111 111 GLU 112 112 VAL 113 113 ALA 114 114 ARG 115 115 LEU 116 116 PRO 117 117 LYS 118 118 ASP 119 119 VAL 120 120 GLY 121 121 LEU 122 122 GLU 123 123 ILE 124 124 GLU 125 125 ALA 126 126 ILE 127 127 ALA 128 128 VAL 129 129 ARG 130 130 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1J7H "Solution Structure Of Hi0719, A Hypothetical Protein From Haemophilus Influenzae" 100.00 130 100.00 100.00 1.54e-87 EMBL CBW29037 "ketoacid-binding protein [Haemophilus influenzae 10810]" 100.00 150 100.00 100.00 4.82e-88 EMBL CBY86245 "conserved hypothetical protein [Haemophilus influenzae F3047]" 100.00 130 100.00 100.00 1.54e-87 GB AAC22376 "conserved hypothetical protein [Haemophilus influenzae Rd KW20]" 100.00 130 100.00 100.00 1.54e-87 GB AAX87747 "putative translation initiation inhibitor, YjgF family [Haemophilus influenzae 86-028NP]" 100.00 130 100.00 100.00 1.54e-87 GB ABQ99007 "putative translation initiation inhibitor, YjgF family protein [Haemophilus influenzae PittEE]" 99.23 129 100.00 100.00 1.56e-86 GB ABR00257 "transcription antitermination protein NusG [Haemophilus influenzae PittGG]" 99.23 129 99.22 100.00 3.59e-86 GB ADO81666 "Conserved hypothetical protein [Haemophilus influenzae R2866]" 100.00 130 100.00 100.00 1.54e-87 REF NP_438877 "hypothetical protein HI0719 [Haemophilus influenzae Rd KW20]" 100.00 130 100.00 100.00 1.54e-87 REF WP_005629596 "endoribonuclease L-PSP [Haemophilus haemolyticus]" 99.23 129 99.22 100.00 3.59e-86 REF WP_005630808 "MULTISPECIES: endoribonuclease L-PSP [Haemophilus]" 99.23 129 100.00 100.00 1.56e-86 REF WP_005633088 "endoribonuclease L-PSP [Haemophilus influenzae]" 100.00 130 100.00 100.00 1.54e-87 REF WP_005641565 "endoribonuclease L-PSP [Haemophilus haemolyticus]" 100.00 130 98.46 98.46 2.85e-86 SP P44839 "RecName: Full=RutC family protein HI_0719 [Haemophilus influenzae Rd KW20]" 100.00 130 100.00 100.00 1.54e-87 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HI0719 'Haemophilus influenzae' 727 Bacteria . Haemophilus influenzae 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 $HI0719 'recombinant technology' . . . . . 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 _Isotopic_labeling $HI0719 1.5 mM '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HI0719 1.5 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HI0719 1.5 mM '[U-13C; U-15N]' $HI0719 1.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 . pH temperature 308 0.1 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 H2O H 1 protons ppm 4.75 . . . . . 1.0 $HI0719_paper $HI0719_paper H2O N 15 protons ppm . . . . . . . $HI0719_paper $HI0719_paper H2O C 13 protons ppm . . . . . . . $HI0719_paper $HI0719_paper 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_cs_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'HI0719 homotrimer 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 . 1 MET N N 121.86 0.015 1 2 . 1 MET H H 8.49 0.015 1 3 . 1 MET CA C 55.45 0.015 1 4 . 1 MET HA H 4.69 0.015 1 5 . 1 MET CB C 33.54 0.015 1 6 . 1 MET HB2 H 2.09 0.015 1 7 . 1 MET HB3 H 2.09 0.015 1 8 . 1 MET C C 176.5 0.015 1 9 . 2 MET N N 120.36 0.015 1 10 . 2 MET H H 8.23 0.015 1 11 . 2 MET CA C 54.94 0.015 1 12 . 2 MET HA H 4.7 0.015 1 13 . 2 MET CB C 34.56 0.015 1 14 . 2 MET HB2 H 2.02 0.015 1 15 . 2 MET HB3 H 2.15 0.015 1 16 . 2 MET HG2 H 2.54 0.015 1 17 . 2 MET HG3 H 2.54 0.015 1 18 . 2 MET C C 176.15 0.015 1 19 . 3 THR N N 115.36 0.015 1 20 . 3 THR H H 8.31 0.015 1 21 . 3 THR CA C 62.58 0.015 1 22 . 3 THR HA H 4.62 0.015 1 23 . 3 THR CB C 70.22 0.015 1 24 . 3 THR HB H 4.15 0.015 1 25 . 3 THR CG2 C 22.7 0.015 1 26 . 3 THR HG2 H 1.19 0.015 1 27 . 3 THR C C 175.7 0.015 1 28 . 4 GLN N N 123.86 0.015 1 29 . 4 GLN H H 8.67 0.015 1 30 . 4 GLN CA C 54.94 0.015 1 31 . 4 GLN HA H 4.69 0.015 1 32 . 4 GLN CB C 32.02 0.015 1 33 . 4 GLN HB2 H 2.29 0.015 1 34 . 4 GLN HB3 H 2.1 0.015 1 35 . 4 GLN HG2 H 2.43 0.015 1 36 . 4 GLN HG3 H 2.43 0.015 1 37 . 5 ILE N N 120.8 0.015 1 38 . 5 ILE H H 8.73 0.015 1 39 . 5 ILE CA C 59.96 0.015 1 40 . 5 ILE HA H 4.82 0.015 1 41 . 5 ILE CB C 39.07 0.015 1 42 . 5 ILE HB H 1.77 0.015 1 43 . 5 ILE HG12 H 1.53 0.015 1 44 . 5 ILE HG13 H 1.16 0.015 1 45 . 5 ILE HG2 H 1.07 0.015 1 46 . 5 ILE CD1 C 13.49 0.015 1 47 . 5 ILE HD1 H 1 0.015 1 48 . 5 ILE C C 176.2 0.015 1 49 . 6 ILE N N 125.36 0.015 1 50 . 6 ILE H H 8.01 0.015 1 51 . 6 ILE CA C 59.01 0.015 1 52 . 6 ILE HA H 4.49 0.015 1 53 . 6 ILE CB C 38.64 0.015 1 54 . 6 ILE HB H 1.75 0.015 1 55 . 6 ILE CG1 C 29.43 0.015 1 56 . 6 ILE HG12 H 1.39 0.015 1 57 . 6 ILE HG13 H 1.26 0.015 1 58 . 6 ILE CG2 C 18.49 0.015 1 59 . 6 ILE HG2 H 1 0.015 1 60 . 6 ILE CD1 C 12.55 0.015 1 61 . 6 ILE HD1 H 0.81 0.015 1 62 . 6 ILE C C 176.1 0.015 1 63 . 7 HIS N N 125.36 0.015 1 64 . 7 HIS H H 8.45 0.015 1 65 . 7 HIS CA C 56.47 0.015 1 66 . 7 HIS HA H 5.29 0.015 1 67 . 7 HIS CB C 33.54 0.015 1 68 . 7 HIS HB2 H 3.02 0.015 1 69 . 7 HIS HB3 H 3.02 0.015 1 70 . 7 HIS C C 175.35 0.015 1 71 . 8 THR N N 121.86 0.015 1 72 . 8 THR H H 9.79 0.015 1 73 . 8 THR CA C 58.5 0.015 1 74 . 8 THR HA H 4.75 0.015 1 75 . 8 THR CB C 69.71 0.015 1 76 . 8 THR HB H 3.95 0.015 1 77 . 8 THR CG2 C 20.37 0.015 1 78 . 8 THR HG2 H 1.08 0.015 1 79 . 9 GLU N N 128.35 0.015 1 80 . 9 GLU H H 9.28 0.015 1 81 . 9 GLU CA C 57.6 0.015 1 82 . 9 GLU HA H 4.75 0.015 1 83 . 9 GLU CB C 28.9 0.015 1 84 . 10 LYS N N 119.26 0.015 1 85 . 10 LYS H H 8.48 0.015 1 86 . 10 LYS CA C 56.98 0.015 1 87 . 10 LYS HA H 4.19 0.015 1 88 . 10 LYS CB C 32.45 0.015 1 89 . 10 LYS HB2 H 1.69 0.015 1 90 . 10 LYS HB3 H 2.22 0.015 1 91 . 10 LYS C C 174.8 0.015 1 92 . 11 ALA N N 119.8 0.015 1 93 . 11 ALA H H 7.55 0.015 1 94 . 11 ALA CA C 49.84 0.015 1 95 . 11 ALA HA H 4.72 0.015 1 96 . 11 ALA CB C 20.3 0.015 1 97 . 11 ALA HB H 1.37 0.015 1 98 . 12 PRO CA C 63.6 0.015 1 99 . 12 PRO HA H 4.35 0.015 1 100 . 12 PRO CB C 31.51 0.015 1 101 . 12 PRO HB2 H 1.97 0.015 1 102 . 12 PRO HB3 H 2.3 0.015 1 103 . 12 PRO CD C 50.37 0.015 1 104 . 12 PRO HD2 H 3.7 0.015 1 105 . 12 PRO HD3 H 3.7 0.015 1 106 . 12 PRO C C 177.7 0.015 1 107 . 13 ALA N N 128.85 0.015 1 108 . 13 ALA H H 8.76 0.015 1 109 . 13 ALA CA C 52.9 0.015 1 110 . 13 ALA HA H 4.22 0.015 1 111 . 13 ALA CB C 18.77 0.015 1 112 . 13 ALA HB H 1.49 0.015 1 113 . 13 ALA C C 178.2 0.015 1 114 . 14 ALA N N 125.86 0.015 1 115 . 14 ALA H H 8.87 0.015 1 116 . 14 ALA CA C 52.39 0.015 1 117 . 14 ALA HA H 4.15 0.015 1 118 . 14 ALA CB C 18.26 0.015 1 119 . 14 ALA HB H 0.75 0.015 1 120 . 14 ALA C C 177.1 0.015 1 121 . 15 ILE N N 122.86 0.015 1 122 . 15 ILE H H 7.43 0.015 1 123 . 15 ILE CA C 60.54 0.015 1 124 . 15 ILE HA H 4.35 0.015 1 125 . 15 ILE CB C 37.62 0.015 1 126 . 15 ILE HB H 2.09 0.015 1 127 . 15 ILE HG12 H 1.52 0.015 1 128 . 15 ILE HG13 H 1.25 0.015 1 129 . 15 ILE CG2 C 17.87 0.015 1 130 . 15 ILE HG2 H 0.97 0.015 1 131 . 15 ILE CD1 C 13.18 0.015 1 132 . 15 ILE HD1 H 0.92 0.015 1 133 . 15 ILE C C 176.25 0.015 1 134 . 16 GLY N N 112.86 0.015 1 135 . 16 GLY H H 7.65 0.015 1 136 . 16 GLY CA C 43.73 0.015 1 137 . 17 PRO CA C 61.36 0.015 1 138 . 17 PRO HA H 4.35 0.015 1 139 . 17 PRO CB C 28.76 0.015 1 140 . 17 PRO HB2 H 1.88 0.015 1 141 . 17 PRO HB3 H 1.88 0.015 1 142 . 17 PRO CD C 48.8 0.015 1 143 . 17 PRO HD2 H 3.5 0.015 1 144 . 17 PRO HD3 H 3.37 0.015 1 145 . 17 PRO C C 174.75 0.015 1 146 . 18 TYR N N 120.3 0.015 1 147 . 18 TYR H H 8.35 0.015 1 148 . 18 TYR CA C 56.98 0.015 1 149 . 18 TYR HA H 4.75 0.015 1 150 . 18 TYR CB C 40.17 0.015 1 151 . 18 TYR HB2 H 2.95 0.015 1 152 . 18 TYR HB3 H 2.95 0.015 1 153 . 18 TYR HD1 H 6.9 0.015 1 154 . 18 TYR HD2 H 6.9 0.015 1 155 . 18 TYR HE1 H 6.71 0.015 1 156 . 18 TYR HE2 H 6.71 0.015 1 157 . 18 TYR C C 173.6 0.015 1 158 . 19 VAL N N 107.37 0.015 1 159 . 19 VAL H H 6.57 0.015 1 160 . 19 VAL CA C 59.01 0.015 1 161 . 19 VAL HA H 4.75 0.015 1 162 . 19 VAL CB C 35.07 0.015 1 163 . 19 VAL HB H 2.49 0.015 1 164 . 19 VAL HG1 H 1.12 0.015 1 165 . 19 VAL CG2 C 17.55 0.015 1 166 . 19 VAL HG2 H 0.78 0.015 1 167 . 19 VAL C C 177.15 0.015 1 168 . 20 GLN N N 122.5 0.015 1 169 . 20 GLN H H 10.1 0.015 1 170 . 20 GLN CA C 60.7 0.015 1 171 . 20 GLN HA H 4.29 0.015 1 172 . 20 GLN CB C 28.1 0.015 1 173 . 20 GLN HB2 H 2.75 0.015 1 174 . 20 GLN HB3 H 2.75 0.015 1 175 . 20 GLN HE21 H 6.9 0.015 1 176 . 20 GLN HE22 H 7.62 0.015 1 177 . 20 GLN C C 177.85 0.015 1 178 . 21 ALA N N 110.86 0.015 1 179 . 21 ALA H H 7.45 0.015 1 180 . 21 ALA CA C 51.58 0.015 1 181 . 21 ALA HA H 4.95 0.015 1 182 . 21 ALA CB C 23.54 0.015 1 183 . 21 ALA HB H 1.35 0.015 1 184 . 21 ALA C C 175.7 0.015 1 185 . 22 VAL N N 113.36 0.015 1 186 . 22 VAL H H 8.52 0.015 1 187 . 22 VAL CA C 60.03 0.015 1 188 . 22 VAL HA H 5.02 0.015 1 189 . 22 VAL CB C 35.07 0.015 1 190 . 22 VAL HB H 2.02 0.015 1 191 . 22 VAL CG1 C 21.62 0.015 1 192 . 22 VAL HG1 H 0.87 0.015 1 193 . 22 VAL C C 175.15 0.015 1 194 . 23 ASP N N 125.36 0.015 1 195 . 23 ASP H H 9.31 0.015 1 196 . 23 ASP CA C 52.9 0.015 1 197 . 23 ASP HA H 5.09 0.015 1 198 . 23 ASP CB C 42.71 0.015 1 199 . 23 ASP HB2 H 2.29 0.015 1 200 . 23 ASP HB3 H 3.15 0.015 1 201 . 23 ASP C C 176.8 0.015 1 202 . 24 LEU N N 124.36 0.015 1 203 . 24 LEU H H 9.26 0.015 1 204 . 24 LEU CA C 54.43 0.015 1 205 . 24 LEU HA H 4.95 0.015 1 206 . 24 LEU CB C 42.2 0.015 1 207 . 24 LEU HB2 H 2.15 0.015 1 208 . 24 LEU HB3 H 2.04 0.015 1 209 . 24 LEU HG H 1.85 0.015 1 210 . 24 LEU HD1 H 1.15 0.015 1 211 . 24 LEU CD2 C 24.74 0.015 1 212 . 24 LEU HD2 H 0.98 0.015 1 213 . 24 LEU C C 178.3 0.015 1 214 . 25 GLY N N 112.86 0.015 1 215 . 25 GLY H H 9.17 0.015 1 216 . 25 GLY CA C 46.28 0.015 1 217 . 25 GLY HA2 H 4.8 0.015 1 218 . 25 GLY HA3 H 3.45 0.015 1 219 . 26 ASN CA C 54.5 0.015 1 220 . 26 ASN HA H 5.09 0.015 1 221 . 26 ASN CB C 39 0.015 1 222 . 26 ASN HB2 H 3.07 0.015 1 223 . 26 ASN HB3 H 3.4 0.015 1 224 . 26 ASN C C 175.7 0.015 1 225 . 27 LEU N N 117.86 0.015 1 226 . 27 LEU H H 7.21 0.015 1 227 . 27 LEU CA C 53.92 0.015 1 228 . 27 LEU HA H 5.29 0.015 1 229 . 27 LEU CB C 47.81 0.015 1 230 . 27 LEU HB2 H 1.62 0.015 1 231 . 27 LEU HB3 H 1.35 0.015 1 232 . 27 LEU C C 176.2 0.015 1 233 . 28 VAL N N 120.86 0.015 1 234 . 28 VAL H H 9.01 0.015 1 235 . 28 VAL CA C 61.56 0.015 1 236 . 28 VAL HA H 4.95 0.015 1 237 . 28 VAL CB C 35.07 0.015 1 238 . 28 VAL HB H 1.7 0.015 1 239 . 28 VAL CG1 C 21.2 0.015 1 240 . 28 VAL HG1 H 0.86 0.015 1 241 . 28 VAL CG2 C 20.99 0.015 1 242 . 28 VAL HG2 H 0.72 0.015 1 243 . 29 LEU N N 125.36 0.015 1 244 . 29 LEU H H 8.67 0.015 1 245 . 29 LEU CA C 54.43 0.015 1 246 . 29 LEU HA H 5.15 0.015 1 247 . 29 LEU CB C 42.71 0.015 1 248 . 29 LEU HB2 H 1.82 0.015 1 249 . 29 LEU HB3 H 1.57 0.015 1 250 . 29 LEU CD1 C 26.61 0.015 1 251 . 29 LEU HD1 H 0.83 0.015 1 252 . 29 LEU CD2 C 25.36 0.015 1 253 . 29 LEU HD2 H 0.85 0.015 1 254 . 29 LEU C C 179.9 0.015 1 255 . 30 THR N N 110.86 0.015 1 256 . 30 THR H H 8.6 0.015 1 257 . 30 THR CA C 61.05 0.015 1 258 . 30 THR HA H 5.15 0.015 1 259 . 30 THR CB C 71.75 0.015 1 260 . 30 THR HB H 4.95 0.015 1 261 . 30 THR CG2 C 21.5 0.015 1 262 . 30 THR HG2 H 1.28 0.015 1 263 . 30 THR C C 177.1 0.015 1 264 . 31 SER N N 117.36 0.015 1 265 . 31 SER H H 8.87 0.015 1 266 . 31 SER CA C 61.05 0.015 1 267 . 31 SER HA H 4.62 0.015 1 268 . 31 SER CB C 65.13 0.015 1 269 . 31 SER HB2 H 4.44 0.015 1 270 . 31 SER HB3 H 4.44 0.015 1 271 . 31 SER C C 177.8 0.015 1 272 . 32 GLY N N 116.75 0.015 1 273 . 32 GLY H H 8.77 0.015 1 274 . 32 GLY CA C 47.3 0.015 1 275 . 32 GLY HA2 H 3.88 0.015 1 276 . 32 GLY HA3 H 4.19 0.015 1 277 . 32 GLY C C 174.3 0.015 1 278 . 33 GLN N N 125.36 0.015 1 279 . 33 GLN H H 9.31 0.015 1 280 . 33 GLN CA C 54.18 0.015 1 281 . 33 GLN HA H 4.79 0.015 1 282 . 33 GLN CB C 30.71 0.015 1 283 . 33 GLN HB2 H 2.35 0.015 1 284 . 33 GLN HB3 H 1.82 0.015 1 285 . 33 GLN HE21 H 6.96 0.015 1 286 . 33 GLN HE22 H 7.43 0.015 1 287 . 33 GLN C C 177.35 0.015 1 288 . 34 ILE N N 120 0.015 1 289 . 34 ILE H H 8.98 0.015 1 290 . 34 ILE CA C 59.01 0.015 1 291 . 34 ILE HA H 4.07 0.015 1 292 . 34 ILE CB C 39.15 0.015 1 293 . 34 ILE HG12 H 1.44 0.015 1 294 . 34 ILE HG13 H 1.39 0.015 1 295 . 34 ILE CD1 C 15 0.015 1 296 . 34 ILE HD1 H 0.82 0.015 1 297 . 35 PRO CA C 63.6 0.015 1 298 . 35 PRO HA H 4.29 0.015 1 299 . 35 PRO CB C 29.47 0.015 1 300 . 35 PRO HB2 H 2.6 0.015 1 301 . 35 PRO HB3 H 2.6 0.015 1 302 . 35 PRO CD C 51.3 0.015 1 303 . 35 PRO HD2 H 3.74 0.015 1 304 . 35 PRO HD3 H 3.97 0.015 1 305 . 35 PRO C C 174.8 0.015 1 306 . 36 VAL N N 121 0.015 1 307 . 36 VAL H H 7.62 0.015 1 308 . 36 VAL CA C 61.05 0.015 1 309 . 36 VAL HA H 3.99 0.015 1 310 . 36 VAL CB C 34.56 0.015 1 311 . 36 VAL HB H 1.62 0.015 1 312 . 36 VAL CG1 C 20.99 0.015 1 313 . 36 VAL HG1 H 0.75 0.015 1 314 . 36 VAL CG2 C 22.24 0.015 1 315 . 36 VAL HG2 H 0.83 0.015 1 316 . 36 VAL C C 176.85 0.015 1 317 . 37 ASN N N 127.36 0.015 1 318 . 37 ASN H H 8.67 0.015 1 319 . 37 ASN CA C 50.86 0.015 1 320 . 37 ASN HA H 4.79 0.015 1 321 . 37 ASN CB C 39.66 0.015 1 322 . 37 ASN HB2 H 3.35 0.015 1 323 . 37 ASN HB3 H 2.7 0.015 1 324 . 37 ASN HD21 H 7.35 0.015 1 325 . 37 ASN HD22 H 7.75 0.015 1 326 . 37 ASN ND2 N 113.8 0.015 1 327 . 38 PRO CA C 64.7 0.015 1 328 . 38 PRO HA H 4.22 0.015 1 329 . 38 PRO CB C 31.9 0.015 1 330 . 38 PRO HB2 H 2.24 0.015 1 331 . 38 PRO HB3 H 1.91 0.015 1 332 . 38 PRO CD C 50 0.015 1 333 . 38 PRO HD2 H 3.64 0.015 1 334 . 38 PRO HD3 H 3.6 0.015 1 335 . 38 PRO C C 176.85 0.015 1 336 . 39 ALA N N 119.05 0.015 1 337 . 39 ALA H H 8.02 0.015 1 338 . 39 ALA CA C 54.43 0.015 1 339 . 39 ALA HA H 4.42 0.015 1 340 . 39 ALA CB C 19.5 0.015 1 341 . 39 ALA HB H 1.55 0.015 1 342 . 39 ALA C C 179.3 0.015 1 343 . 40 THR N N 103.87 0.015 1 344 . 40 THR H H 7.4 0.015 1 345 . 40 THR CA C 61.05 0.015 1 346 . 40 THR HA H 4.6 0.015 1 347 . 40 THR CB C 71.75 0.015 1 348 . 40 THR HB H 4.42 0.015 1 349 . 40 THR HG2 H 1.19 0.015 1 350 . 40 THR C C 177.2 0.015 1 351 . 41 GLY N N 111.36 0.015 1 352 . 41 GLY H H 8.77 0.015 1 353 . 41 GLY CA C 45.77 0.015 1 354 . 41 GLY HA2 H 3.62 0.015 1 355 . 41 GLY HA3 H 3.62 0.015 1 356 . 41 GLY C C 175.3 0.015 1 357 . 42 GLU N N 119.1 0.015 1 358 . 42 GLU H H 7.84 0.015 1 359 . 42 GLU CA C 55.96 0.015 1 360 . 42 GLU HA H 4.49 0.015 1 361 . 42 GLU CB C 32.02 0.015 1 362 . 42 GLU HB2 H 1.89 0.015 1 363 . 42 GLU HB3 H 2.02 0.015 1 364 . 42 GLU CG C 36.3 0.015 1 365 . 42 GLU HG2 H 2.26 0.015 1 366 . 42 GLU HG3 H 2.17 0.015 1 367 . 42 GLU C C 176.6 0.015 1 368 . 43 VAL N N 124.36 0.015 1 369 . 43 VAL H H 8.54 0.015 1 370 . 43 VAL CA C 59.01 0.015 1 371 . 43 VAL HA H 5.09 0.015 1 372 . 43 VAL CB C 34.56 0.015 1 373 . 43 VAL HB H 1.99 0.015 1 374 . 43 VAL CG1 C 20.37 0.015 1 375 . 43 VAL HG1 H 1.04 0.015 1 376 . 43 VAL HG2 H 1.12 0.015 1 377 . 44 PRO CA C 63.09 0.015 1 378 . 44 PRO HA H 4.57 0.015 1 379 . 44 PRO CB C 32.52 0.015 1 380 . 44 PRO HB2 H 2.02 0.015 1 381 . 44 PRO HB3 H 2.42 0.015 1 382 . 44 PRO CD C 51.3 0.015 1 383 . 44 PRO HD2 H 4 0.015 1 384 . 44 PRO HD3 H 4 0.015 1 385 . 44 PRO C C 177.3 0.015 1 386 . 45 ALA N N 122.2 0.015 1 387 . 45 ALA H H 8.35 0.015 1 388 . 45 ALA CA C 54.43 0.015 1 389 . 45 ALA HA H 4.22 0.015 1 390 . 45 ALA HB H 1.54 0.015 1 391 . 45 ALA C C 178.8 0.015 1 392 . 46 ASP N N 115.86 0.015 1 393 . 46 ASP H H 7.91 0.015 1 394 . 46 ASP CA C 53.92 0.015 1 395 . 46 ASP HA H 4.75 0.015 1 396 . 46 ASP CB C 43.73 0.015 1 397 . 46 ASP HB2 H 2.72 0.015 1 398 . 46 ASP HB3 H 2.85 0.015 1 399 . 46 ASP C C 178.1 0.015 1 400 . 47 ILE N N 125.86 0.015 1 401 . 47 ILE H H 8.92 0.015 1 402 . 47 ILE CA C 61.05 0.015 1 403 . 47 ILE HA H 4.09 0.015 1 404 . 47 ILE CB C 38.64 0.015 1 405 . 47 ILE HB H 2.02 0.015 1 406 . 47 ILE CG1 C 26.93 0.015 1 407 . 47 ILE HG12 H 1.52 0.015 1 408 . 47 ILE HG13 H 1.26 0.015 1 409 . 47 ILE HG2 H 0.97 0.015 1 410 . 47 ILE CD1 C 14.43 0.015 1 411 . 47 ILE HD1 H 0.93 0.015 1 412 . 47 ILE C C 176.9 0.015 1 413 . 48 VAL N N 125.36 0.015 1 414 . 48 VAL H H 8.04 0.015 1 415 . 48 VAL CA C 68.18 0.015 1 416 . 48 VAL HA H 3.44 0.015 1 417 . 48 VAL CB C 31 0.015 1 418 . 48 VAL HB H 2.29 0.015 1 419 . 48 VAL CG1 C 21.3 0.015 1 420 . 48 VAL HG1 H 0.95 0.015 1 421 . 48 VAL CG2 C 24.37 0.015 1 422 . 48 VAL HG2 H 1.09 0.015 1 423 . 48 VAL C C 178.2 0.015 1 424 . 49 ALA N N 122 0.015 1 425 . 49 ALA H H 7.62 0.015 1 426 . 49 ALA CA C 54.94 0.015 1 427 . 49 ALA HA H 4.22 0.015 1 428 . 49 ALA CB C 18.77 0.015 1 429 . 49 ALA HB H 1.62 0.015 1 430 . 49 ALA C C 181.4 0.015 1 431 . 50 GLN N N 119.2 0.015 1 432 . 50 GLN H H 8.71 0.015 1 433 . 50 GLN CA C 61.05 0.015 1 434 . 50 GLN HA H 4.02 0.015 1 435 . 50 GLN CB C 28.45 0.015 1 436 . 50 GLN HB2 H 2.15 0.015 1 437 . 50 GLN HB3 H 2.15 0.015 1 438 . 50 GLN C C 178.4 0.015 1 439 . 51 ALA N N 124.86 0.015 1 440 . 51 ALA H H 8.84 0.015 1 441 . 51 ALA CA C 56.47 0.015 1 442 . 51 ALA HA H 4.02 0.015 1 443 . 51 ALA CB C 17.75 0.015 1 444 . 51 ALA HB H 1.55 0.015 1 445 . 51 ALA C C 178.75 0.015 1 446 . 52 ARG N N 115.86 0.015 1 447 . 52 ARG H H 8.31 0.015 1 448 . 52 ARG CA C 58.18 0.015 1 449 . 52 ARG HA H 3.95 0.015 1 450 . 52 ARG CB C 28.96 0.015 1 451 . 52 ARG HB2 H 2.02 0.015 1 452 . 52 ARG HB3 H 2.35 0.015 1 453 . 52 ARG HG2 H 1.82 0.015 1 454 . 52 ARG HG3 H 1.82 0.015 1 455 . 52 ARG CD C 44.12 0.015 1 456 . 52 ARG HD2 H 3.12 0.015 1 457 . 52 ARG HD3 H 3.01 0.015 1 458 . 52 ARG C C 177.8 0.015 1 459 . 53 GLN N N 118.2 0.015 1 460 . 53 GLN H H 8.56 0.015 1 461 . 53 GLN CA C 58.5 0.015 1 462 . 53 GLN HA H 4.02 0.015 1 463 . 53 GLN CB C 29.47 0.015 1 464 . 53 GLN HB2 H 1.95 0.015 1 465 . 53 GLN HB3 H 2.35 0.015 1 466 . 53 GLN C C 178.9 0.015 1 467 . 54 SER N N 113.86 0.015 1 468 . 54 SER H H 8.62 0.015 1 469 . 54 SER CA C 64.11 0.015 1 470 . 54 SER HA H 4.1 0.015 1 471 . 54 SER CB C 63.6 0.015 1 472 . 54 SER HB2 H 3.76 0.015 1 473 . 54 SER HB3 H 3.7 0.015 1 474 . 54 SER C C 176.95 0.015 1 475 . 55 LEU N N 120.36 0.015 1 476 . 55 LEU H H 7.6 0.015 1 477 . 55 LEU CA C 58.5 0.015 1 478 . 55 LEU HA H 3.55 0.015 1 479 . 55 LEU CB C 39.15 0.015 1 480 . 55 LEU HB2 H 1.09 0.015 1 481 . 55 LEU HB3 H -0.87 0.015 1 482 . 55 LEU CD1 C 25.68 0.015 1 483 . 55 LEU HD1 H 0.44 0.015 1 484 . 55 LEU HD2 H 0.98 0.015 1 485 . 55 LEU C C 178.6 0.015 1 486 . 56 GLU N N 119.86 0.015 1 487 . 56 GLU H H 8.84 0.015 1 488 . 56 GLU CA C 59.01 0.015 1 489 . 56 GLU HA H 4.15 0.015 1 490 . 56 GLU CB C 28.45 0.015 1 491 . 56 GLU HB2 H 2.29 0.015 1 492 . 56 GLU HB3 H 2.29 0.015 1 493 . 56 GLU CG C 36.61 0.015 1 494 . 56 GLU HG2 H 2.48 0.015 1 495 . 56 GLU HG3 H 2.38 0.015 1 496 . 56 GLU C C 179.5 0.015 1 497 . 57 ASN N N 121.6 0.015 1 498 . 57 ASN H H 8.26 0.015 1 499 . 57 ASN CA C 56.47 0.015 1 500 . 57 ASN HA H 4.75 0.015 1 501 . 57 ASN CB C 37.62 0.015 1 502 . 57 ASN HB2 H 3.29 0.015 1 503 . 57 ASN HB3 H 3.41 0.015 1 504 . 57 ASN HD21 H 6.71 0.015 1 505 . 57 ASN HD22 H 7.29 0.015 1 506 . 57 ASN C C 177.6 0.015 1 507 . 58 VAL N N 118.86 0.015 1 508 . 58 VAL H H 7.87 0.015 1 509 . 58 VAL CA C 68.18 0.015 1 510 . 58 VAL HA H 3.49 0.015 1 511 . 58 VAL CB C 32.02 0.015 1 512 . 58 VAL HB H 2.35 0.015 1 513 . 58 VAL CG1 C 23.18 0.015 1 514 . 58 VAL HG1 H 1.09 0.015 1 515 . 58 VAL HG2 H 0.92 0.015 1 516 . 58 VAL C C 177.85 0.015 1 517 . 59 LYS N N 120 0.015 1 518 . 59 LYS H H 8.9 0.015 1 519 . 59 LYS CA C 60.37 0.015 1 520 . 59 LYS HA H 3.69 0.015 1 521 . 59 LYS CB C 33.54 0.015 1 522 . 59 LYS HB2 H 2.15 0.015 1 523 . 59 LYS HB3 H 2.29 0.015 1 524 . 59 LYS CD C 30.36 0.015 1 525 . 59 LYS HD2 H 1.82 0.015 1 526 . 59 LYS HD3 H 1.7 0.015 1 527 . 59 LYS HE2 H 3.13 0.015 1 528 . 59 LYS HE3 H 3.13 0.015 1 529 . 59 LYS C C 177.4 0.015 1 530 . 60 ALA N N 119.6 0.015 1 531 . 60 ALA H H 8.48 0.015 1 532 . 60 ALA CA C 54.94 0.015 1 533 . 60 ALA HA H 4.22 0.015 1 534 . 60 ALA CB C 18.77 0.015 1 535 . 60 ALA HB H 1.49 0.015 1 536 . 60 ALA C C 180.5 0.015 1 537 . 61 ILE N N 119.8 0.015 1 538 . 61 ILE H H 7.43 0.015 1 539 . 61 ILE CA C 65.64 0.015 1 540 . 61 ILE HA H 3.4 0.015 1 541 . 61 ILE CB C 39.15 0.015 1 542 . 61 ILE HB H 1.95 0.015 1 543 . 61 ILE CG2 C 19.74 0.015 1 544 . 61 ILE HG2 H 0.79 0.015 1 545 . 61 ILE CD1 C 15.3 0.015 1 546 . 61 ILE HD1 H 0.88 0.015 1 547 . 62 ILE N N 118.36 0.015 1 548 . 62 ILE H H 8.06 0.015 1 549 . 62 ILE CA C 63.6 0.015 1 550 . 62 ILE HA H 3.62 0.015 1 551 . 62 ILE CB C 36.6 0.015 1 552 . 62 ILE HB H 2.02 0.015 1 553 . 62 ILE CG1 C 29.11 0.015 1 554 . 62 ILE HG12 H 1.16 0.015 1 555 . 62 ILE HG13 H 1.66 0.015 1 556 . 62 ILE CG2 C 19.74 0.015 1 557 . 62 ILE HG2 H 0.67 0.015 1 558 . 62 ILE CD1 C 11.93 0.015 1 559 . 62 ILE HD1 H 0.59 0.015 1 560 . 62 ILE C C 178.7 0.015 1 561 . 63 GLU N N 120 0.015 1 562 . 63 GLU H H 8.95 0.015 1 563 . 63 GLU CA C 59.01 0.015 1 564 . 63 GLU HA H 4.79 0.015 1 565 . 63 GLU CB C 29.47 0.015 1 566 . 63 GLU HB2 H 2.02 0.015 1 567 . 63 GLU HB3 H 2.02 0.015 1 568 . 63 GLU C C 181.3 0.015 1 569 . 64 LYS N N 123.86 0.015 1 570 . 64 LYS H H 7.85 0.015 1 571 . 64 LYS CA C 56.98 0.015 1 572 . 64 LYS HA H 4.41 0.015 1 573 . 64 LYS CB C 30.49 0.015 1 574 . 64 LYS HB2 H 1.8 0.015 1 575 . 64 LYS HB3 H 2.22 0.015 1 576 . 64 LYS C C 178.1 0.015 1 577 . 65 ALA N N 119.5 0.015 1 578 . 65 ALA H H 7.38 0.015 1 579 . 65 ALA CA C 52.39 0.015 1 580 . 65 ALA HA H 4.42 0.015 1 581 . 65 ALA CB C 18.77 0.015 1 582 . 65 ALA HB H 1.49 0.015 1 583 . 65 ALA C C 177.2 0.015 1 584 . 66 GLY N N 105.87 0.015 1 585 . 66 GLY H H 8.07 0.015 1 586 . 66 GLY CA C 45.77 0.015 1 587 . 66 GLY HA2 H 3.89 0.015 1 588 . 66 GLY HA3 H 4.3 0.015 1 589 . 66 GLY C C 175.7 0.015 1 590 . 67 LEU N N 121.86 0.015 1 591 . 67 LEU H H 7.6 0.015 1 592 . 67 LEU CA C 52.39 0.015 1 593 . 67 LEU HA H 4.91 0.015 1 594 . 67 LEU CB C 44.24 0.015 1 595 . 67 LEU HB2 H 1.89 0.015 1 596 . 67 LEU HB3 H 1.89 0.015 1 597 . 67 LEU CD1 C 26.05 0.015 1 598 . 67 LEU HD1 H 0.69 0.015 1 599 . 67 LEU HD2 H 0.94 0.015 1 600 . 67 LEU C C 175.95 0.015 1 601 . 68 THR N N 109.36 0.015 1 602 . 68 THR H H 9.28 0.015 1 603 . 68 THR CA C 60.03 0.015 1 604 . 68 THR HA H 5 0.015 1 605 . 68 THR CB C 73.79 0.015 1 606 . 68 THR HB H 4.69 0.015 1 607 . 68 THR HG2 H 1.37 0.015 1 608 . 68 THR C C 177.1 0.015 1 609 . 69 ALA N N 122.45 0.015 1 610 . 69 ALA H H 9.9 0.015 1 611 . 69 ALA CA C 54.43 0.015 1 612 . 69 ALA HA H 4.15 0.015 1 613 . 69 ALA CB C 17.75 0.015 1 614 . 69 ALA HB H 1.29 0.015 1 615 . 69 ALA C C 178.5 0.015 1 616 . 70 ALA N N 117 0.015 1 617 . 70 ALA H H 7.79 0.015 1 618 . 70 ALA CA C 54.43 0.015 1 619 . 70 ALA HA H 4.02 0.015 1 620 . 70 ALA CB C 18.77 0.015 1 621 . 70 ALA HB H 1.29 0.015 1 622 . 70 ALA C C 177 0.015 1 623 . 71 ASP N N 115.36 0.015 1 624 . 71 ASP H H 8.02 0.015 1 625 . 71 ASP CA C 54.94 0.015 1 626 . 71 ASP HA H 4.69 0.015 1 627 . 71 ASP CB C 42.2 0.015 1 628 . 71 ASP HB2 H 2.89 0.015 1 629 . 71 ASP HB3 H 3.75 0.015 1 630 . 71 ASP C C 176.95 0.015 1 631 . 72 ILE N N 118.86 0.015 1 632 . 72 ILE H H 7.54 0.015 1 633 . 72 ILE CA C 63.6 0.015 1 634 . 72 ILE HA H 4.22 0.015 1 635 . 72 ILE CB C 38.13 0.015 1 636 . 72 ILE HB H 2.35 0.015 1 637 . 72 ILE CG2 C 18.49 0.015 1 638 . 72 ILE HG2 H 1.08 0.015 1 639 . 72 ILE CD1 C 13.8 0.015 1 640 . 72 ILE HD1 H 1.2 0.015 1 641 . 72 ILE C C 176.65 0.015 1 642 . 73 VAL N N 119.25 0.015 1 643 . 73 VAL H H 9.03 0.015 1 644 . 73 VAL CA C 61.05 0.015 1 645 . 73 VAL HA H 5.09 0.015 1 646 . 73 VAL CB C 33.03 0.015 1 647 . 73 VAL HB H 2.49 0.015 1 648 . 73 VAL CG1 C 21.9 0.015 1 649 . 73 VAL HG1 H 1.18 0.015 1 650 . 73 VAL CG2 C 18.49 0.015 1 651 . 73 VAL HG2 H 0.87 0.015 1 652 . 74 LYS N N 122.15 0.015 1 653 . 74 LYS H H 7.79 0.015 1 654 . 74 LYS CA C 55.05 0.015 1 655 . 74 LYS HA H 5.55 0.015 1 656 . 74 LYS CB C 35.58 0.015 1 657 . 74 LYS HB2 H 1.02 0.015 1 658 . 74 LYS HB3 H 1.89 0.015 1 659 . 74 LYS CD C 29.43 0.015 1 660 . 74 LYS HD2 H 1.3 0.015 1 661 . 74 LYS HD3 H 1.3 0.015 1 662 . 74 LYS HE2 H 2.91 0.015 1 663 . 74 LYS HE3 H 2.91 0.015 1 664 . 74 LYS C C 175.8 0.015 1 665 . 75 THR N N 115.7 0.015 1 666 . 75 THR H H 9.17 0.015 1 667 . 75 THR CA C 59.52 0.015 1 668 . 75 THR HA H 5.62 0.015 1 669 . 75 THR CB C 72.26 0.015 1 670 . 75 THR HB H 4.44 0.015 1 671 . 75 THR CG2 C 21.93 0.015 1 672 . 75 THR HG2 H 1.33 0.015 1 673 . 75 THR C C 176.5 0.015 1 674 . 76 THR N N 117.75 0.015 1 675 . 76 THR H H 8.29 0.015 1 676 . 76 THR CA C 63.6 0.015 1 677 . 76 THR HA H 4.62 0.015 1 678 . 76 THR CB C 69.71 0.015 1 679 . 76 THR HB H 3.66 0.015 1 680 . 76 THR CG2 C 21.78 0.015 1 681 . 76 THR HG2 H 0.23 0.015 1 682 . 76 THR C C 174.3 0.015 1 683 . 77 VAL N N 126.36 0.015 1 684 . 77 VAL H H 8.59 0.015 1 685 . 77 VAL CA C 61.05 0.015 1 686 . 77 VAL HA H 4.42 0.015 1 687 . 77 VAL CB C 33.03 0.015 1 688 . 77 VAL HB H 2.09 0.015 1 689 . 77 VAL HG1 H 0.92 0.015 1 690 . 77 VAL CG2 C 21 0.015 1 691 . 77 VAL HG2 H 0.92 0.015 1 692 . 77 VAL C C 174.8 0.015 1 693 . 78 PHE N N 126.36 0.015 1 694 . 78 PHE H H 8.81 0.015 1 695 . 78 PHE CA C 55.45 0.015 1 696 . 78 PHE HA H 5.22 0.015 1 697 . 78 PHE CB C 40.68 0.015 1 698 . 78 PHE HB2 H 3.09 0.015 1 699 . 78 PHE HB3 H 2.82 0.015 1 700 . 78 PHE HD1 H 6.9 0.015 1 701 . 78 PHE HD2 H 6.9 0.015 1 702 . 78 PHE HE1 H 7 0.015 1 703 . 78 PHE HE2 H 7 0.015 1 704 . 78 PHE HZ H 7.32 0.015 1 705 . 78 PHE C C 176.8 0.015 1 706 . 79 VAL N N 113.86 0.015 1 707 . 79 VAL H H 8.84 0.015 1 708 . 79 VAL CA C 59.01 0.015 1 709 . 79 VAL HA H 5.29 0.015 1 710 . 79 VAL CB C 34.05 0.015 1 711 . 79 VAL HB H 2.6 0.015 1 712 . 79 VAL CG1 C 22.7 0.015 1 713 . 79 VAL HG1 H 0.9 0.015 1 714 . 79 VAL CG2 C 19.15 0.015 1 715 . 79 VAL HG2 H 0.62 0.015 1 716 . 79 VAL C C 175.9 0.015 1 717 . 80 LYS N N 122.2 0.015 1 718 . 80 LYS H H 7.99 0.015 1 719 . 80 LYS CA C 55.45 0.015 1 720 . 80 LYS HA H 4.55 0.015 1 721 . 80 LYS CB C 32.7 0.015 1 722 . 80 LYS HB2 H 1.89 0.015 1 723 . 80 LYS HB3 H 1.89 0.015 1 724 . 80 LYS C C 176.8 0.015 1 725 . 81 ASP N N 116.36 0.015 1 726 . 81 ASP H H 8.42 0.015 1 727 . 81 ASP CA C 52.9 0.015 1 728 . 81 ASP HA H 4.75 0.015 1 729 . 81 ASP CB C 43.22 0.015 1 730 . 81 ASP HB2 H 2.42 0.015 1 731 . 81 ASP HB3 H 3.15 0.015 1 732 . 81 ASP C C 178.3 0.015 1 733 . 82 LEU N N 129.35 0.015 1 734 . 82 LEU H H 10.4 0.015 1 735 . 82 LEU CA C 57.49 0.015 1 736 . 82 LEU HA H 4.02 0.015 1 737 . 82 LEU CB C 41.6 0.015 1 738 . 82 LEU HB2 H 1.75 0.015 1 739 . 82 LEU HB3 H 1.55 0.015 1 740 . 82 LEU HG H 1.69 0.015 1 741 . 82 LEU CD1 C 25.36 0.015 1 742 . 82 LEU HD1 H 0.41 0.015 1 743 . 82 LEU CD2 C 24.11 0.015 1 744 . 82 LEU HD2 H 0.47 0.015 1 745 . 82 LEU C C 179.5 0.015 1 746 . 83 ASN N N 120.86 0.015 1 747 . 83 ASN H H 9.43 0.015 1 748 . 83 ASN CA C 56.47 0.015 1 749 . 83 ASN HA H 4.69 0.015 1 750 . 83 ASN CB C 37.62 0.015 1 751 . 83 ASN HB2 H 3.02 0.015 1 752 . 83 ASN HB3 H 2.75 0.015 1 753 . 83 ASN HD21 H 7.21 0.015 1 754 . 83 ASN HD22 H 8.22 0.015 1 755 . 83 ASN ND2 N 116.1 0.015 1 756 . 84 ASP N N 119.36 0.015 1 757 . 84 ASP H H 8.04 0.015 1 758 . 84 ASP CA C 54.94 0.015 1 759 . 84 ASP HA H 5.11 0.015 1 760 . 84 ASP CB C 42.2 0.015 1 761 . 84 ASP HB2 H 2.89 0.015 1 762 . 84 ASP HB3 H 3.15 0.015 1 763 . 84 ASP C C 177.3 0.015 1 764 . 85 PHE N N 119.75 0.015 1 765 . 85 PHE H H 7.9 0.015 1 766 . 85 PHE CA C 61.56 0.015 1 767 . 85 PHE HA H 4.15 0.015 1 768 . 85 PHE CB C 40.17 0.015 1 769 . 85 PHE HB2 H 3.42 0.015 1 770 . 85 PHE HB3 H 3.09 0.015 1 771 . 85 PHE HD1 H 7.19 0.015 1 772 . 85 PHE HD2 H 7.19 0.015 1 773 . 85 PHE HE1 H 7.11 0.015 1 774 . 85 PHE HE2 H 7.11 0.015 1 775 . 85 PHE HZ H 6.91 0.015 1 776 . 85 PHE C C 177.2 0.015 1 777 . 86 ALA N N 121 0.015 1 778 . 86 ALA H H 8.82 0.015 1 779 . 86 ALA CA C 56.47 0.015 1 780 . 86 ALA HA H 4.09 0.015 1 781 . 86 ALA CB C 17.24 0.015 1 782 . 86 ALA HB H 1.49 0.015 1 783 . 86 ALA C C 180.3 0.015 1 784 . 87 ALA N N 121.36 0.015 1 785 . 87 ALA H H 7.85 0.015 1 786 . 87 ALA CA C 54.94 0.015 1 787 . 87 ALA HA H 4.22 0.015 1 788 . 87 ALA CB C 18.77 0.015 1 789 . 87 ALA HB H 1.49 0.015 1 790 . 87 ALA C C 180.2 0.015 1 791 . 88 VAL N N 118.36 0.015 1 792 . 88 VAL H H 7.65 0.015 1 793 . 88 VAL CA C 67.16 0.015 1 794 . 88 VAL HA H 3.29 0.015 1 795 . 88 VAL CB C 32.02 0.015 1 796 . 88 VAL HB H 1.95 0.015 1 797 . 88 VAL CG1 C 20.64 0.015 1 798 . 88 VAL HG1 H 0.72 0.015 1 799 . 88 VAL CG2 C 23.8 0.015 1 800 . 88 VAL HG2 H 1.01 0.015 1 801 . 88 VAL C C 177.9 0.015 1 802 . 89 ASN N N 117.86 0.015 1 803 . 89 ASN H H 9.06 0.015 1 804 . 89 ASN CA C 55.96 0.015 1 805 . 89 ASN HA H 3.95 0.015 1 806 . 89 ASN CB C 38.64 0.015 1 807 . 89 ASN HB2 H 2.16 0.015 1 808 . 89 ASN HB3 H 2.55 0.015 1 809 . 89 ASN C C 177.9 0.015 1 810 . 90 ALA N N 120.36 0.015 1 811 . 90 ALA H H 7.73 0.015 1 812 . 90 ALA CA C 54.94 0.015 1 813 . 90 ALA HA H 4.35 0.015 1 814 . 90 ALA CB C 18.26 0.015 1 815 . 90 ALA HB H 1.62 0.015 1 816 . 90 ALA C C 180.05 0.015 1 817 . 91 GLU N N 120.9 0.015 1 818 . 91 GLU H H 7.48 0.015 1 819 . 91 GLU CA C 58.5 0.015 1 820 . 91 GLU HA H 4.42 0.015 1 821 . 91 GLU CB C 29.47 0.015 1 822 . 91 GLU HB2 H 1.89 0.015 1 823 . 91 GLU HB3 H 2.22 0.015 1 824 . 91 GLU C C 177.9 0.015 1 825 . 92 TYR N N 121.7 0.015 1 826 . 92 TYR H H 8.96 0.015 1 827 . 92 TYR CA C 61.56 0.015 1 828 . 92 TYR HA H 4.1 0.015 1 829 . 92 TYR CB C 39.66 0.015 1 830 . 92 TYR HB2 H 2.84 0.015 1 831 . 92 TYR HB3 H 3.65 0.015 1 832 . 92 TYR HD1 H 7.03 0.015 1 833 . 92 TYR HD2 H 7.03 0.015 1 834 . 93 GLU N N 119.3 0.015 1 835 . 93 GLU H H 8.84 0.015 1 836 . 93 GLU CA C 61.05 0.015 1 837 . 93 GLU HA H 4.22 0.015 1 838 . 93 GLU CB C 30.49 0.015 1 839 . 93 GLU HB2 H 2.42 0.015 1 840 . 93 GLU HB3 H 2.42 0.015 1 841 . 93 GLU C C 178.1 0.015 1 842 . 94 ARG N N 118.36 0.015 1 843 . 94 ARG H H 7.96 0.015 1 844 . 94 ARG CA C 60.54 0.015 1 845 . 94 ARG HA H 4.09 0.015 1 846 . 94 ARG CB C 30.49 0.015 1 847 . 94 ARG HB2 H 2.02 0.015 1 848 . 94 ARG HB3 H 2.02 0.015 1 849 . 94 ARG HG2 H 1.66 0.015 1 850 . 94 ARG HG3 H 1.91 0.015 1 851 . 94 ARG CD C 43.49 0.015 1 852 . 94 ARG HD2 H 3.32 0.015 1 853 . 94 ARG HD3 H 3.32 0.015 1 854 . 94 ARG C C 178.5 0.015 1 855 . 95 PHE N N 118.86 0.015 1 856 . 95 PHE H H 8.79 0.015 1 857 . 95 PHE CA C 62.07 0.015 1 858 . 95 PHE CB C 39.66 0.015 1 859 . 95 PHE HB2 H 2.8 0.015 1 860 . 95 PHE HB3 H 3.1 0.015 1 861 . 95 PHE HD1 H 6.27 0.015 1 862 . 95 PHE HD2 H 6.27 0.015 1 863 . 95 PHE HE1 H 6.59 0.015 1 864 . 95 PHE HE2 H 6.59 0.015 1 865 . 95 PHE HZ H 6.73 0.015 1 866 . 95 PHE C C 178.65 0.015 1 867 . 96 PHE N N 118.55 0.015 1 868 . 96 PHE H H 8.16 0.015 1 869 . 96 PHE CA C 65.64 0.015 1 870 . 96 PHE HA H 3.95 0.015 1 871 . 96 PHE CB C 38.64 0.015 1 872 . 96 PHE HB2 H 3.16 0.015 1 873 . 96 PHE HB3 H 3.16 0.015 1 874 . 96 PHE HD1 H 7.41 0.015 1 875 . 96 PHE HD2 H 7.41 0.015 1 876 . 96 PHE HE1 H 6.94 0.015 1 877 . 96 PHE HE2 H 6.94 0.015 1 878 . 96 PHE C C 177.9 0.015 1 879 . 97 LYS N N 120.1 0.015 1 880 . 97 LYS H H 8.56 0.015 1 881 . 97 LYS CA C 59.52 0.015 1 882 . 97 LYS HA H 4.35 0.015 1 883 . 97 LYS CB C 32.02 0.015 1 884 . 97 LYS HB2 H 1.95 0.015 1 885 . 97 LYS HB3 H 2.15 0.015 1 886 . 97 LYS C C 180.9 0.015 1 887 . 98 GLU N N 121.36 0.015 1 888 . 98 GLU H H 9.09 0.015 1 889 . 98 GLU CA C 58.5 0.015 1 890 . 98 GLU HA H 4.09 0.015 1 891 . 98 GLU CB C 29.47 0.015 1 892 . 98 GLU HB2 H 1.95 0.015 1 893 . 98 GLU HB3 H 2.15 0.015 1 894 . 98 GLU CG C 36.61 0.015 1 895 . 98 GLU HG2 H 2.37 0.015 1 896 . 98 GLU HG3 H 2.31 0.015 1 897 . 98 GLU C C 176.9 0.015 1 898 . 99 ASN N N 112.86 0.015 1 899 . 99 ASN H H 6.96 0.015 1 900 . 99 ASN CA C 54.43 0.015 1 901 . 99 ASN HA H 4.63 0.015 1 902 . 99 ASN CB C 39.15 0.015 1 903 . 99 ASN HB2 H 1.89 0.015 1 904 . 99 ASN HB3 H 2.69 0.015 1 905 . 99 ASN C C 174.6 0.015 1 906 . 100 ASN N N 112.86 0.015 1 907 . 100 ASN H H 7.88 0.015 1 908 . 100 ASN CA C 54.43 0.015 1 909 . 100 ASN HA H 4.35 0.015 1 910 . 100 ASN CB C 37.11 0.015 1 911 . 100 ASN HB2 H 2.75 0.015 1 912 . 100 ASN HB3 H 3.02 0.015 1 913 . 100 ASN C C 175.7 0.015 1 914 . 101 HIS N N 121 0.015 1 915 . 101 HIS H H 8.24 0.015 1 916 . 101 HIS CA C 56.98 0.015 1 917 . 101 HIS HA H 4.72 0.015 1 918 . 101 HIS CB C 32.02 0.015 1 919 . 101 HIS HB2 H 2.95 0.015 1 920 . 101 HIS HB3 H 2.95 0.015 1 921 . 102 PRO CA C 64.62 0.015 1 922 . 102 PRO HA H 4.29 0.015 1 923 . 102 PRO CB C 32.02 0.015 1 924 . 102 PRO HB2 H 2.29 0.015 1 925 . 102 PRO HB3 H 1.95 0.015 1 926 . 102 PRO CD C 50.68 0.015 1 927 . 102 PRO HD2 H 3.49 0.015 1 928 . 102 PRO HD3 H 3.11 0.015 1 929 . 102 PRO C C 178.2 0.015 1 930 . 103 ASN N N 121.5 0.015 1 931 . 103 ASN H H 10.75 0.015 1 932 . 103 ASN CA C 53.41 0.015 1 933 . 103 ASN HA H 4.22 0.015 1 934 . 103 ASN CB C 39.11 0.015 1 935 . 103 ASN HB2 H 2.55 0.015 1 936 . 103 ASN HB3 H 2.82 0.015 1 937 . 103 ASN HD21 H 6.92 0.015 1 938 . 103 ASN HD22 H 7.67 0.015 1 939 . 103 ASN ND2 N 114.6 0.015 1 940 . 103 ASN C C 173.5 0.015 1 941 . 104 PHE N N 117.2 0.015 1 942 . 104 PHE H H 7.87 0.015 1 943 . 104 PHE CA C 56.98 0.015 1 944 . 104 PHE CB C 44.24 0.015 1 945 . 104 PHE HD1 H 7.4 0.015 1 946 . 104 PHE HD2 H 7.4 0.015 1 947 . 105 PRO CA C 62.5 0.015 1 948 . 105 PRO HA H 4.55 0.015 1 949 . 105 PRO CB C 32 0.015 1 950 . 105 PRO HB2 H 1.82 0.015 1 951 . 105 PRO HB3 H 1.82 0.015 1 952 . 105 PRO C C 177.2 0.015 1 953 . 106 ALA N N 127.85 0.015 1 954 . 106 ALA H H 8.57 0.015 1 955 . 106 ALA CA C 54.43 0.015 1 956 . 106 ALA HA H 4.69 0.015 1 957 . 106 ALA CB C 18.77 0.015 1 958 . 106 ALA HB H 1.45 0.015 1 959 . 106 ALA C C 177.3 0.015 1 960 . 107 ARG N N 121.86 0.015 1 961 . 107 ARG H H 9.79 0.015 1 962 . 107 ARG CA C 56.47 0.015 1 963 . 107 ARG HA H 5.82 0.015 1 964 . 107 ARG C C 177 0.015 1 965 . 108 SER N N 120.36 0.015 1 966 . 108 SER H H 7.45 0.015 1 967 . 108 SER CA C 58.5 0.015 1 968 . 108 SER HA H 4.72 0.015 1 969 . 108 SER CB C 64.64 0.015 1 970 . 108 SER HB2 H 3.65 0.015 1 971 . 108 SER HB3 H 3.65 0.015 1 972 . 109 CYS CA C 56.8 0.015 1 973 . 109 CYS HA H 5.45 0.015 1 974 . 109 CYS CB C 29.2 0.015 1 975 . 109 CYS HB2 H 2.35 0.015 1 976 . 109 CYS HB3 H 2.35 0.015 1 977 . 109 CYS C C 175.1 0.015 1 978 . 110 VAL N N 117.75 0.015 1 979 . 110 VAL H H 7.85 0.015 1 980 . 110 VAL CA C 59.1 0.015 1 981 . 110 VAL HA H 4.35 0.015 1 982 . 110 VAL CB C 36.09 0.015 1 983 . 110 VAL HB H 1.69 0.015 1 984 . 110 VAL CG1 C 20.99 0.015 1 985 . 110 VAL HG1 H -0.12 0.015 1 986 . 110 VAL CG2 C 18.8 0.015 1 987 . 110 VAL HG2 H 0.42 0.015 1 988 . 110 VAL C C 174.7 0.015 1 989 . 111 GLU N N 122.5 0.015 1 990 . 111 GLU H H 8.07 0.015 1 991 . 111 GLU CA C 54.8 0.015 1 992 . 111 GLU HA H 5.42 0.015 1 993 . 111 GLU CB C 32 0.015 1 994 . 111 GLU HB2 H 2.07 0.015 1 995 . 111 GLU HB3 H 2.07 0.015 1 996 . 112 VAL N N 119.1 0.015 1 997 . 112 VAL H H 8.82 0.015 1 998 . 112 VAL CA C 59.6 0.015 1 999 . 112 VAL CB C 30.8 0.015 1 1000 . 112 VAL HB H 2.19 0.015 1 1001 . 112 VAL CG1 C 23.8 0.015 1 1002 . 112 VAL HG1 H 0.95 0.015 1 1003 . 112 VAL CG2 C 18.8 0.015 1 1004 . 112 VAL HG2 H 0.65 0.015 1 1005 . 113 ALA N N 120.1 0.015 1 1006 . 113 ALA H H 8.12 0.015 1 1007 . 113 ALA CA C 54.94 0.015 1 1008 . 113 ALA HA H 4.22 0.015 1 1009 . 113 ALA CB C 20.81 0.015 1 1010 . 113 ALA HB H 1.29 0.015 1 1011 . 113 ALA C C 177.8 0.015 1 1012 . 114 ARG N N 114 0.015 1 1013 . 114 ARG H H 7.52 0.015 1 1014 . 114 ARG CA C 56.98 0.015 1 1015 . 114 ARG HA H 4.13 0.015 1 1016 . 114 ARG CB C 32.52 0.015 1 1017 . 114 ARG HB2 H 1.95 0.015 1 1018 . 114 ARG HB3 H 1.95 0.015 1 1019 . 114 ARG C C 174.2 0.015 1 1020 . 115 LEU N N 125.86 0.015 1 1021 . 115 LEU H H 8.98 0.015 1 1022 . 115 LEU CA C 51.88 0.015 1 1023 . 115 LEU HA H 4.74 0.015 1 1024 . 115 LEU CB C 43.22 0.015 1 1025 . 115 LEU HB2 H 1.6 0.015 1 1026 . 115 LEU HB3 H 1.6 0.015 1 1027 . 115 LEU CD1 C 25.68 0.015 1 1028 . 115 LEU HD1 H 0.63 0.015 1 1029 . 115 LEU CD2 C 26.6 0.015 1 1030 . 115 LEU HD2 H 0.87 0.015 1 1031 . 116 PRO CA C 64 0.015 1 1032 . 116 PRO HA H 4.02 0.015 1 1033 . 116 PRO CB C 32.1 0.015 1 1034 . 116 PRO HB2 H 2.15 0.015 1 1035 . 116 PRO HB3 H 2.15 0.015 1 1036 . 116 PRO CD C 51 0.015 1 1037 . 116 PRO HD2 H 3.35 0.015 1 1038 . 116 PRO HD3 H 3.66 0.015 1 1039 . 116 PRO C C 176.2 0.015 1 1040 . 117 LYS N N 114.36 0.015 1 1041 . 117 LYS H H 8.49 0.015 1 1042 . 117 LYS CA C 57.99 0.015 1 1043 . 117 LYS HA H 3.75 0.015 1 1044 . 117 LYS CB C 29.98 0.015 1 1045 . 117 LYS HB2 H 1.89 0.015 1 1046 . 117 LYS HB3 H 2.02 0.015 1 1047 . 117 LYS CG C 25.68 0.015 1 1048 . 117 LYS HG2 H 1.38 0.015 1 1049 . 117 LYS HG3 H 1.38 0.015 1 1050 . 117 LYS CD C 29.43 0.015 1 1051 . 117 LYS HD2 H 1.6 0.015 1 1052 . 117 LYS HD3 H 1.53 0.015 1 1053 . 117 LYS CE C 41.62 0.015 1 1054 . 117 LYS HE2 H 3 0.015 1 1055 . 117 LYS HE3 H 3 0.015 1 1056 . 117 LYS C C 176.2 0.015 1 1057 . 118 ASP N N 112.36 0.015 1 1058 . 118 ASP H H 8.64 0.015 1 1059 . 118 ASP CA C 56.98 0.015 1 1060 . 118 ASP HA H 4.69 0.015 1 1061 . 118 ASP CB C 39.15 0.015 1 1062 . 118 ASP HB2 H 2.69 0.015 1 1063 . 118 ASP HB3 H 2.95 0.015 1 1064 . 118 ASP C C 177.1 0.015 1 1065 . 119 VAL N N 108.15 0.015 1 1066 . 119 VAL H H 6.76 0.015 1 1067 . 119 VAL CA C 62.07 0.015 1 1068 . 119 VAL HA H 4.29 0.015 1 1069 . 119 VAL CB C 33.03 0.015 1 1070 . 119 VAL HB H 2.29 0.015 1 1071 . 119 VAL CG1 C 22.24 0.015 1 1072 . 119 VAL HG1 H 1.1 0.015 1 1073 . 119 VAL HG2 H 0.94 0.015 1 1074 . 119 VAL C C 176.6 0.015 1 1075 . 120 GLY N N 104.87 0.015 1 1076 . 120 GLY H H 9.23 0.015 1 1077 . 120 GLY CA C 45.77 0.015 1 1078 . 120 GLY HA2 H 3.62 0.015 1 1079 . 120 GLY HA3 H 4.19 0.015 1 1080 . 120 GLY C C 176.15 0.015 1 1081 . 121 LEU N N 115.86 0.015 1 1082 . 121 LEU H H 7.23 0.015 1 1083 . 121 LEU CA C 55.45 0.015 1 1084 . 121 LEU HA H 5.3 0.015 1 1085 . 121 LEU CB C 43.73 0.015 1 1086 . 121 LEU HB2 H 1.62 0.015 1 1087 . 121 LEU HB3 H 2.09 0.015 1 1088 . 121 LEU HG H 1.16 0.015 1 1089 . 121 LEU CD1 C 26.61 0.015 1 1090 . 121 LEU HD1 H 0.88 0.015 1 1091 . 121 LEU C C 174.4 0.015 1 1092 . 122 GLU N N 117.25 0.015 1 1093 . 122 GLU H H 8.82 0.015 1 1094 . 122 GLU CA C 54.9 0.015 1 1095 . 122 GLU HA H 5 0.015 1 1096 . 122 GLU CB C 33.4 0.015 1 1097 . 122 GLU HB2 H 2.02 0.015 1 1098 . 122 GLU HB3 H 2.35 0.015 1 1099 . 122 GLU HG2 H 2.16 0.015 1 1100 . 122 GLU HG3 H 2.16 0.015 1 1101 . 122 GLU C C 175.7 0.015 1 1102 . 123 ILE N N 123.4 0.015 1 1103 . 123 ILE H H 8.37 0.015 1 1104 . 123 ILE CA C 61.05 0.015 1 1105 . 123 ILE HA H 5.49 0.015 1 1106 . 123 ILE CB C 42.2 0.015 1 1107 . 123 ILE HB H 1.69 0.015 1 1108 . 123 ILE CG2 C 16.3 0.015 1 1109 . 123 ILE HG2 H 0.96 0.015 1 1110 . 123 ILE C C 176.1 0.015 1 1111 . 124 GLU N N 125.36 0.015 1 1112 . 124 GLU H H 8.68 0.015 1 1113 . 124 GLU CA C 54.43 0.015 1 1114 . 124 GLU HA H 4.89 0.015 1 1115 . 124 GLU CB C 32.52 0.015 1 1116 . 124 GLU HB2 H 2.09 0.015 1 1117 . 124 GLU HB3 H 2.09 0.015 1 1118 . 124 GLU CG C 35.68 0.015 1 1119 . 124 GLU HG2 H 2.26 0.015 1 1120 . 124 GLU HG3 H 2.26 0.015 1 1121 . 124 GLU C C 176.43 0.015 1 1122 . 125 ALA N N 121.86 0.015 1 1123 . 125 ALA H H 8.04 0.015 1 1124 . 125 ALA CA C 50.86 0.015 1 1125 . 125 ALA HA H 5.65 0.015 1 1126 . 125 ALA CB C 24.88 0.015 1 1127 . 125 ALA HB H 1.42 0.015 1 1128 . 125 ALA C C 176.65 0.015 1 1129 . 126 ILE N N 120.9 0.015 1 1130 . 126 ILE H H 8.9 0.015 1 1131 . 126 ILE CA C 61.05 0.015 1 1132 . 126 ILE HA H 5.15 0.015 1 1133 . 126 ILE CB C 41.18 0.015 1 1134 . 126 ILE HB H 1.69 0.015 1 1135 . 126 ILE CG1 C 27.55 0.015 1 1136 . 126 ILE HG12 H 1.1 0.015 1 1137 . 126 ILE HG13 H 1.7 0.015 1 1138 . 126 ILE CG2 C 17.24 0.015 1 1139 . 126 ILE HG2 H 0.83 0.015 1 1140 . 126 ILE CD1 C 13.49 0.015 1 1141 . 126 ILE HD1 H 0.78 0.015 1 1142 . 126 ILE C C 176.2 0.015 1 1143 . 127 ALA N N 130.35 0.015 1 1144 . 127 ALA H H 9.48 0.015 1 1145 . 127 ALA CA C 49.84 0.015 1 1146 . 127 ALA HA H 5.65 0.015 1 1147 . 127 ALA CB C 23.87 0.015 1 1148 . 127 ALA HB H 1.22 0.015 1 1149 . 127 ALA C C 175.8 0.015 1 1150 . 128 VAL N N 117.86 0.015 1 1151 . 128 VAL H H 8.21 0.015 1 1152 . 128 VAL CA C 59.52 0.015 1 1153 . 128 VAL HA H 5.09 0.015 1 1154 . 128 VAL CB C 36.09 0.015 1 1155 . 128 VAL HB H 1.95 0.015 1 1156 . 128 VAL CG1 C 21.93 0.015 1 1157 . 128 VAL HG1 H 1.03 0.015 1 1158 . 128 VAL CG2 C 23.4 0.015 1 1159 . 128 VAL HG2 H 1.12 0.015 1 1160 . 128 VAL C C 174.2 0.015 1 1161 . 129 ARG N N 127 0.015 1 1162 . 129 ARG H H 8.01 0.015 1 1163 . 129 ARG CA C 55 0.015 1 1164 . 129 ARG HA H 4.51 0.015 1 1165 . 129 ARG CB C 32.52 0.015 1 1166 . 129 ARG HB2 H 1.55 0.015 1 1167 . 129 ARG HB3 H 2.09 0.015 1 1168 . 129 ARG HG2 H 2.58 0.015 1 1169 . 129 ARG HG3 H 2.58 0.015 1 1170 . 129 ARG C C 176.2 0.015 1 1171 . 130 LYS N N 131.85 0.015 1 1172 . 130 LYS H H 8.32 0.015 1 1173 . 130 LYS CA C 58.6 0.015 1 1174 . 130 LYS HA H 4.22 0.015 1 1175 . 130 LYS CB C 33.6 0.015 1 1176 . 130 LYS HB2 H 1.51 0.015 1 1177 . 130 LYS HB3 H 1.8 0.015 1 1178 . 130 LYS HG2 H 1.48 0.015 1 1179 . 130 LYS HG3 H 1.86 0.015 1 1180 . 130 LYS CD C 29.43 0.015 1 1181 . 130 LYS HD2 H 1.77 0.015 1 1182 . 130 LYS HD3 H 1.77 0.015 1 1183 . 130 LYS CE C 42.24 0.015 1 1184 . 130 LYS HE2 H 3.07 0.015 1 1185 . 130 LYS HE3 H 3.07 0.015 1 1186 . 130 LYS C C 175 0.015 1 stop_ save_