data_6524 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ApoE N-terminal domain ; _BMRB_accession_number 6524 _BMRB_flat_file_name bmr6524.str _Entry_type original _Submission_date 2005-02-24 _Accession_date 2005-02-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shift assignment of the apoE N-terminal domain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Chao . . 2 Sivashanmugam Arun . . 3 Hoyt David . . 4 Wang Jianjun . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 175 "13C chemical shifts" 348 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-26 original author . stop_ _Original_release_date 2005-07-26 save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A complete backbone assignment of the apolipoprotein E LDL receptor binding domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Chao . . 2 Sivashanmugam Arun . . 3 Hoyt David . . 4 Wang Jianjun . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 32 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 177 _Page_last 177 _Year 2005 _Details . loop_ _Keyword 'Apolipoprotein E' 'Chemical Shift' 'LDL Receptor' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'apoE N-terminal domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'apoE N-terminal domain' $apoEN stop_ _System_molecular_weight 21323 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_apoEN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human apolipoprotein E N-terminal domain' _Molecular_mass 21323 _Mol_thiol_state 'all free' loop_ _Biological_function 'LDL receptor binding, lipoprotein binding, amyloid peptide binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 183 _Mol_residue_sequence . loop_ _Residue_seq_code _Residue_label 1 LYS 2 VAL 3 GLU 4 GLN 5 ALA 6 VAL 7 GLU 8 THR 9 GLU 10 PRO 11 GLU 12 PRO 13 GLU 14 LEU 15 ARG 16 GLN 17 GLN 18 THR 19 GLU 20 TRP 21 GLN 22 SER 23 GLY 24 GLN 25 ARG 26 TRP 27 GLU 28 LEU 29 ALA 30 LEU 31 GLY 32 ARG 33 PHE 34 TRP 35 ASP 36 TYR 37 LEU 38 ARG 39 TRP 40 VAL 41 GLN 42 THR 43 LEU 44 SER 45 GLU 46 GLN 47 VAL 48 GLN 49 GLU 50 GLU 51 LEU 52 LEU 53 SER 54 SER 55 GLN 56 VAL 57 THR 58 GLN 59 GLU 60 LEU 61 ARG 62 ALA 63 LEU 64 MET 65 ASP 66 GLU 67 THR 68 MET 69 LYS 70 GLU 71 LEU 72 LYS 73 ALA 74 TYR 75 LYS 76 SER 77 GLU 78 LEU 79 GLU 80 GLU 81 GLN 82 LEU 83 THR 84 PRO 85 VAL 86 ALA 87 GLU 88 GLU 89 THR 90 ARG 91 ALA 92 ARG 93 LEU 94 SER 95 LYS 96 GLU 97 LEU 98 GLN 99 ALA 100 ALA 101 GLN 102 ALA 103 ARG 104 LEU 105 GLY 106 ALA 107 ASP 108 MET 109 GLU 110 ASP 111 VAL 112 CYS 113 GLY 114 ARG 115 LEU 116 VAL 117 GLN 118 TYR 119 ARG 120 GLY 121 GLU 122 VAL 123 GLN 124 ALA 125 MET 126 LEU 127 GLY 128 GLN 129 SER 130 THR 131 GLU 132 GLU 133 LEU 134 ARG 135 VAL 136 ARG 137 LEU 138 ALA 139 SER 140 HIS 141 LEU 142 ARG 143 LYS 144 LEU 145 ARG 146 LYS 147 ARG 148 LEU 149 LEU 150 ARG 151 ASP 152 ALA 153 ASP 154 ASP 155 LEU 156 GLN 157 LYS 158 ARG 159 LEU 160 ALA 161 VAL 162 TYR 163 GLN 164 ALA 165 GLY 166 ALA 167 ARG 168 GLU 169 GLY 170 ALA 171 GLU 172 ARG 173 GLY 174 LEU 175 SER 176 ALA 177 ILE 178 ARG 179 GLU 180 ARG 181 LEU 182 GLY 183 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15744 Apolipoprotein_E 100.00 308 100.00 100.00 2.55e-121 PDB 1B68 "Apolipoprotein E4 (Apoe4), 22k Fragment" 100.00 191 99.45 99.45 9.62e-120 PDB 1BZ4 "Apolipoprotein E3 (Apo-E3), Truncation Mutant 165" 78.69 144 100.00 100.00 4.01e-93 PDB 1EA8 "Apolipoprotein E3 22kd Fragment Lys146glu Mutant" 100.00 191 99.45 100.00 6.00e-121 PDB 1GS9 "Apolipoprotein E4, 22k Domain" 90.16 165 99.39 99.39 9.76e-107 PDB 1H7I "Apolipoprotein E3 22kd Fragment Lys146gln Mutant" 100.00 191 99.45 100.00 4.56e-121 PDB 1LE2 "Structural Basis For Altered Function In The Common Mutants Of Human Apolipoprotein-E" 78.69 144 99.31 99.31 7.46e-92 PDB 1LE4 "Structural Basis For Altered Function In The Common Mutants Of Human Apolipoprotein-E" 78.69 144 99.31 99.31 5.26e-91 PDB 1LPE "Three-Dimensional Structure Of The Ldl Receptor-Binding Domain Of Human Apolipoprotein E" 78.69 144 100.00 100.00 4.98e-93 PDB 1NFN "Apolipoprotein E3 (Apoe3)" 100.00 191 100.00 100.00 9.77e-122 PDB 1NFO "Apolipoprotein E2 (Apoe2, D154a Mutation)" 100.00 191 98.91 98.91 3.77e-119 PDB 1OR2 "Apolipoprotein E3 (Apoe3) Truncation Mutant 165" 90.16 165 97.58 97.58 1.84e-104 PDB 1OR3 "Apolipoprotein E3 (Apoe3), Trigonal Truncation Mutant 165" 90.16 165 100.00 100.00 7.08e-109 PDB 2KC3 "Nmr Solution Structure Of Complete Receptor Binding Domain Of Human Apolipoprotein E" 100.00 184 100.00 100.00 6.03e-122 PDB 2L7B "Nmr Structure Of Full Length Apoe3" 100.00 307 100.00 100.00 4.16e-121 DBJ BAG37412 "unnamed protein product [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 DBJ BAG72927 "apolipoprotein E [synthetic construct]" 100.00 317 100.00 100.00 3.02e-120 EMBL CAA25017 "unnamed protein product [Homo sapiens]" 75.41 176 100.00 100.00 3.81e-86 GB AAB59397 "apolipoprotein E [Homo sapiens]" 100.00 317 99.45 99.45 4.49e-118 GB AAB59518 "apolipoprotein E [Homo sapiens]" 100.00 317 98.91 98.91 9.77e-119 GB AAB59546 "preapolipoprotein E [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 GB AAD02505 "apolipoprotein E [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 GB AAG27089 "apolipoprotein-E [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 PRF 1506383A "apolipoprotein E mutant E3K" 100.00 317 99.45 100.00 1.24e-119 REF NP_000032 "apolipoprotein E isoform b precursor [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 REF NP_001289617 "apolipoprotein E isoform a precursor [Homo sapiens]" 100.00 343 100.00 100.00 2.22e-119 REF NP_001289618 "apolipoprotein E isoform b precursor [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 REF NP_001289619 "apolipoprotein E isoform b precursor [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 REF NP_001289620 "apolipoprotein E isoform b precursor [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 SP P02649 "RecName: Full=Apolipoprotein E; Short=Apo-E; Flags: Precursor [Homo sapiens]" 100.00 317 100.00 100.00 3.02e-120 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $apoEN 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 _Vector_name $apoEN 'recombinant technology' Bacteria . . . . 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 $apoEN 1 mM '[U-13C; U-15N; U-70% 2H]' $assembly 100 mM . $assembly 1 mM . $assembly 0.05 mM . $assembly 10 mM . $assembly 90 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apoEN 1 mM '[U-13C; U-15N; U-35% 2H]' $assembly 100 mM . $assembly 1 mM . $assembly 0.06 mM . $assembly 10 mM . $assembly 80 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . _Details . save_ save_NMRVIEW _Saveframe_category software _Name NMRView _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500_MHz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength '500 MHz' _Details 'Varian INOVA 500 MHz' save_ save_800_MHz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_3D_15N-edited_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _Sample_label $sample_2 save_ save_HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(COCA)CB _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_15N-edited_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . pH temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details 'DSS for proton 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $PIPP $NMRVIEW stop_ loop_ _Experiment_label HN(CO)CA HNCA HN(COCA)CB HNCACB 3D_15N-edited_NOESY stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'apoE N-terminal domain' _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 VAL CA C 62.030 0.5 1 2 . 2 VAL CB C 32.110 0.5 1 3 . 3 GLU H H 8.574 0.06 1 4 . 3 GLU CA C 55.987 0.5 1 5 . 3 GLU CB C 29.815 0.5 1 6 . 3 GLU N N 125.443 0.6 1 7 . 4 GLN H H 8.369 0.06 1 8 . 4 GLN CA C 55.252 0.5 1 9 . 4 GLN CB C 29.253 0.5 1 10 . 4 GLN N N 121.688 0.6 1 11 . 5 ALA H H 8.378 0.06 1 12 . 5 ALA CA C 52.110 0.5 1 13 . 5 ALA CB C 18.840 0.5 1 14 . 5 ALA N N 125.936 0.6 1 15 . 6 VAL H H 8.099 0.06 1 16 . 6 VAL CA C 61.720 0.5 1 17 . 6 VAL CB C 32.443 0.5 1 18 . 6 VAL N N 119.165 0.6 1 19 . 7 GLU H H 8.489 0.06 1 20 . 7 GLU CA C 56.113 0.5 1 21 . 7 GLU CB C 29.867 0.5 1 22 . 7 GLU N N 124.492 0.6 1 23 . 8 THR H H 8.130 0.06 1 24 . 8 THR CA C 61.287 0.5 1 25 . 8 THR CB C 69.600 0.5 1 26 . 8 THR N N 115.454 0.6 1 27 . 9 GLU H H 8.386 0.06 1 28 . 9 GLU CA C 53.940 0.5 1 29 . 9 GLU CB C 29.480 0.5 1 30 . 9 GLU N N 124.651 0.6 1 31 . 10 PRO CA C 62.525 0.5 1 32 . 10 PRO CB C 31.640 0.5 1 33 . 11 GLU H H 8.471 0.06 1 34 . 11 GLU CA C 54.140 0.5 1 35 . 11 GLU CB C 29.260 0.5 1 36 . 11 GLU N N 122.193 0.6 1 37 . 12 PRO CA C 63.120 0.5 1 38 . 12 PRO CB C 31.540 0.5 1 39 . 13 GLU H H 8.526 0.06 1 40 . 13 GLU CA C 56.343 0.5 1 41 . 13 GLU CB C 29.797 0.5 1 42 . 13 GLU N N 120.182 0.6 1 43 . 14 LEU H H 8.065 0.06 1 44 . 14 LEU CA C 54.950 0.5 1 45 . 14 LEU CB C 41.410 0.5 1 46 . 14 LEU N N 122.787 0.6 1 47 . 15 ARG H H 8.207 0.06 1 48 . 15 ARG CA C 56.015 0.5 1 49 . 15 ARG CB C 30.040 0.5 1 50 . 15 ARG N N 121.656 0.6 1 51 . 16 GLN H H 8.348 0.06 1 52 . 16 GLN CA C 56.630 0.5 1 53 . 16 GLN CB C 30.065 0.5 1 54 . 16 GLN N N 122.232 0.6 1 55 . 17 GLN H H 8.285 0.06 1 56 . 17 GLN CA C 55.820 0.5 1 57 . 17 GLN CB C 28.720 0.5 1 58 . 17 GLN N N 120.828 0.6 1 59 . 18 THR H H 8.046 0.06 1 60 . 18 THR CA C 61.967 0.5 1 61 . 18 THR CB C 69.180 0.5 1 62 . 18 THR N N 114.434 0.6 1 63 . 19 GLU H H 8.338 0.06 1 64 . 19 GLU CA C 56.595 0.5 1 65 . 19 GLU CB C 29.220 0.5 1 66 . 19 GLU N N 122.238 0.6 1 67 . 20 TRP H H 7.939 0.06 1 68 . 20 TRP CA C 56.840 0.5 1 69 . 20 TRP CB C 29.075 0.5 1 70 . 20 TRP N N 120.917 0.6 1 71 . 21 GLN H H 7.990 0.06 1 72 . 21 GLN CA C 55.830 0.5 1 73 . 21 GLN CB C 28.715 0.5 1 74 . 21 GLN N N 120.168 0.6 1 75 . 22 SER H H 8.419 0.06 1 76 . 22 SER CA C 58.187 0.5 1 77 . 22 SER CB C 63.760 0.5 1 78 . 22 SER N N 116.453 0.6 1 79 . 23 GLY H H 8.115 0.06 1 80 . 23 GLY CA C 44.793 0.5 1 81 . 23 GLY N N 110.201 0.6 1 82 . 24 GLN H H 8.101 0.06 1 83 . 24 GLN CA C 54.620 0.5 1 84 . 24 GLN CB C 28.435 0.5 1 85 . 24 GLN N N 118.091 0.6 1 86 . 25 ARG H H 8.539 0.06 1 87 . 25 ARG CA C 60.255 0.5 1 88 . 25 ARG CB C 29.505 0.5 1 89 . 25 ARG N N 121.173 0.6 1 90 . 26 TRP H H 9.293 0.06 1 91 . 26 TRP CA C 59.435 0.5 1 92 . 26 TRP CB C 26.385 0.5 1 93 . 26 TRP N N 119.230 0.6 1 94 . 27 GLU H H 6.025 0.06 1 95 . 27 GLU CA C 58.120 0.5 1 96 . 27 GLU CB C 28.215 0.5 1 97 . 27 GLU N N 122.215 0.6 1 98 . 28 LEU H H 7.611 0.06 1 99 . 28 LEU CA C 57.015 0.5 1 100 . 28 LEU CB C 40.575 0.5 1 101 . 28 LEU N N 120.518 0.6 1 102 . 29 ALA H H 7.648 0.06 1 103 . 29 ALA CA C 55.320 0.5 1 104 . 29 ALA CB C 17.105 0.5 1 105 . 29 ALA N N 123.179 0.6 1 106 . 30 LEU H H 8.325 0.06 1 107 . 30 LEU CA C 57.240 0.5 1 108 . 30 LEU CB C 39.925 0.5 1 109 . 30 LEU N N 121.727 0.6 1 110 . 31 GLY H H 8.431 0.06 1 111 . 31 GLY CA C 46.858 0.5 1 112 . 31 GLY N N 106.945 0.6 1 113 . 32 ARG H H 7.870 0.06 1 114 . 32 ARG CA C 59.620 0.5 1 115 . 32 ARG CB C 30.105 0.5 1 116 . 32 ARG N N 121.685 0.6 1 117 . 33 PHE H H 8.174 0.06 1 118 . 33 PHE CA C 61.975 0.5 1 119 . 33 PHE CB C 38.550 0.5 1 120 . 33 PHE N N 122.766 0.6 1 121 . 34 TRP H H 9.536 0.06 1 122 . 34 TRP CA C 60.085 0.5 1 123 . 34 TRP CB C 29.560 0.5 1 124 . 34 TRP N N 119.871 0.6 1 125 . 35 ASP H H 9.042 0.06 1 126 . 35 ASP CA C 57.237 0.5 1 127 . 35 ASP CB C 40.160 0.5 1 128 . 35 ASP N N 120.511 0.6 1 129 . 36 TYR H H 8.140 0.06 1 130 . 36 TYR CA C 61.325 0.5 1 131 . 36 TYR CB C 38.255 0.5 1 132 . 36 TYR N N 123.896 0.6 1 133 . 37 LEU H H 8.366 0.06 1 134 . 37 LEU CA C 54.125 0.5 1 135 . 37 LEU CB C 40.793 0.5 1 136 . 37 LEU N N 119.008 0.6 1 137 . 38 ARG H H 8.053 0.06 1 138 . 38 ARG CA C 58.990 0.5 1 139 . 38 ARG CB C 32.400 0.5 1 140 . 38 ARG N N 119.611 0.6 1 141 . 39 TRP H H 7.464 0.06 1 142 . 39 TRP CA C 60.815 0.5 1 143 . 39 TRP CB C 30.120 0.5 1 144 . 39 TRP N N 120.798 0.6 1 145 . 40 VAL H H 8.383 0.06 1 146 . 40 VAL CA C 65.160 0.5 1 147 . 40 VAL CB C 30.600 0.5 1 148 . 40 VAL N N 121.246 0.6 1 149 . 41 GLN CA C 54.660 0.5 1 150 . 42 THR H H 7.524 0.06 1 151 . 42 THR CA C 58.830 0.5 1 152 . 42 THR CB C 69.745 0.5 1 153 . 42 THR N N 115.498 0.6 1 154 . 43 LEU H H 8.126 0.06 1 155 . 43 LEU CA C 56.385 0.5 1 156 . 43 LEU CB C 41.545 0.5 1 157 . 43 LEU N N 122.795 0.6 1 158 . 44 SER H H 8.215 0.06 1 159 . 44 SER CA C 58.060 0.5 1 160 . 44 SER CB C 63.700 0.5 1 161 . 44 SER N N 115.960 0.6 1 162 . 45 GLU H H 8.239 0.06 1 163 . 45 GLU CA C 55.620 0.5 1 164 . 45 GLU CB C 30.290 0.5 1 165 . 45 GLU N N 124.330 0.6 1 166 . 46 GLN H H 8.128 0.06 1 167 . 46 GLN CA C 57.260 0.5 1 168 . 46 GLN CB C 29.525 0.5 1 169 . 46 GLN N N 119.597 0.6 1 170 . 47 VAL H H 8.178 0.06 1 171 . 47 VAL CA C 62.130 0.5 1 172 . 47 VAL CB C 32.195 0.5 1 173 . 47 VAL N N 121.218 0.6 1 174 . 48 GLN H H 8.380 0.06 1 175 . 48 GLN CA C 56.950 0.5 1 176 . 48 GLN CB C 28.885 0.5 1 177 . 48 GLN N N 121.184 0.6 1 178 . 49 GLU H H 8.055 0.06 1 179 . 49 GLU CA C 56.775 0.5 1 180 . 49 GLU CB C 29.245 0.5 1 181 . 49 GLU N N 119.600 0.6 1 182 . 50 GLU H H 8.259 0.06 1 183 . 50 GLU CA C 56.325 0.5 1 184 . 50 GLU CB C 29.935 0.5 1 185 . 50 GLU N N 121.235 0.6 1 186 . 51 LEU H H 8.329 0.06 1 187 . 51 LEU CA C 56.190 0.5 1 188 . 51 LEU CB C 40.790 0.5 1 189 . 51 LEU N N 121.198 0.6 1 190 . 52 LEU H H 7.725 0.06 1 191 . 52 LEU CA C 55.855 0.5 1 192 . 52 LEU N N 118.577 0.6 1 193 . 53 SER H H 7.980 0.06 1 194 . 53 SER CA C 57.750 0.5 1 195 . 53 SER CB C 63.940 0.5 1 196 . 53 SER N N 114.908 0.6 1 197 . 54 SER H H 8.273 0.06 1 198 . 54 SER CA C 58.270 0.5 1 199 . 54 SER CB C 63.630 0.5 1 200 . 54 SER N N 115.930 0.6 1 201 . 55 GLN H H 8.420 0.06 1 202 . 55 GLN CA C 59.185 0.5 1 203 . 55 GLN CB C 28.170 0.5 1 204 . 55 GLN N N 122.686 0.6 1 205 . 56 VAL H H 7.708 0.06 1 206 . 56 VAL CA C 64.925 0.5 1 207 . 56 VAL CB C 31.760 0.5 1 208 . 56 VAL N N 117.092 0.6 1 209 . 57 THR H H 7.692 0.06 1 210 . 57 THR CA C 65.240 0.5 1 211 . 57 THR CB C 67.230 0.5 1 212 . 57 THR N N 108.715 0.6 1 213 . 58 GLN H H 8.028 0.06 1 214 . 58 GLN CA C 59.005 0.5 1 215 . 58 GLN CB C 28.285 0.5 1 216 . 58 GLN N N 122.009 0.6 1 217 . 59 GLU H H 8.325 0.06 1 218 . 59 GLU CA C 55.725 0.5 1 219 . 59 GLU CB C 29.845 0.5 1 220 . 59 GLU N N 121.158 0.6 1 221 . 60 LEU H H 8.210 0.06 1 222 . 60 LEU CA C 57.805 0.5 1 223 . 60 LEU CB C 41.600 0.5 1 224 . 60 LEU N N 121.628 0.6 1 225 . 61 ARG H H 8.227 0.06 1 226 . 61 ARG CA C 59.555 0.5 1 227 . 61 ARG CB C 28.900 0.5 1 228 . 61 ARG N N 118.612 0.6 1 229 . 62 ALA H H 7.885 0.06 1 230 . 62 ALA CA C 52.620 0.5 1 231 . 62 ALA CB C 17.410 0.5 1 232 . 62 ALA N N 121.692 0.6 1 233 . 63 LEU H H 8.282 0.06 1 234 . 63 LEU CA C 57.340 0.5 1 235 . 63 LEU CB C 42.530 0.5 1 236 . 63 LEU N N 119.479 0.6 1 237 . 64 MET H H 8.960 0.06 1 238 . 64 MET CA C 58.880 0.5 1 239 . 64 MET CB C 32.180 0.5 1 240 . 64 MET N N 125.677 0.6 1 241 . 65 ASP H H 8.872 0.06 1 242 . 65 ASP CA C 57.260 0.5 1 243 . 65 ASP CB C 39.600 0.5 1 244 . 65 ASP N N 121.250 0.6 1 245 . 66 GLU H H 8.236 0.06 1 246 . 66 GLU CA C 59.305 0.5 1 247 . 66 GLU CB C 29.435 0.5 1 248 . 66 GLU N N 120.260 0.6 1 249 . 67 THR H H 7.872 0.06 1 250 . 67 THR N N 116.070 0.6 1 251 . 68 MET H H 8.279 0.06 1 252 . 68 MET CA C 56.483 0.5 1 253 . 68 MET CB C 30.255 0.5 1 254 . 68 MET N N 117.458 0.6 1 255 . 69 LYS H H 8.521 0.06 1 256 . 69 LYS CA C 59.580 0.5 1 257 . 69 LYS CB C 31.850 0.5 1 258 . 69 LYS N N 122.177 0.6 1 259 . 70 GLU H H 8.443 0.06 1 260 . 70 GLU CA C 57.560 0.5 1 261 . 70 GLU CB C 28.183 0.5 1 262 . 70 GLU N N 118.577 0.6 1 263 . 71 LEU H H 8.736 0.06 1 264 . 71 LEU CA C 57.985 0.5 1 265 . 71 LEU CB C 41.035 0.5 1 266 . 71 LEU N N 124.901 0.6 1 267 . 72 LYS H H 8.105 0.06 1 268 . 72 LYS CA C 59.475 0.5 1 269 . 72 LYS CB C 31.680 0.5 1 270 . 72 LYS N N 119.109 0.6 1 271 . 73 ALA H H 7.842 0.06 1 272 . 73 ALA CA C 54.640 0.5 1 273 . 73 ALA CB C 17.680 0.5 1 274 . 73 ALA N N 121.271 0.6 1 275 . 74 TYR H H 8.290 0.06 1 276 . 74 TYR CA C 59.110 0.5 1 277 . 74 TYR CB C 38.455 0.5 1 278 . 74 TYR N N 120.710 0.6 1 279 . 75 LYS H H 8.468 0.06 1 280 . 75 LYS CA C 59.790 0.5 1 281 . 75 LYS CB C 31.485 0.5 1 282 . 75 LYS N N 118.252 0.6 1 283 . 76 SER H H 7.783 0.06 1 284 . 76 SER CA C 61.645 0.5 1 285 . 76 SER CB C 62.700 0.5 1 286 . 76 SER N N 112.700 0.6 1 287 . 77 GLU H H 7.830 0.06 1 288 . 77 GLU CA C 58.935 0.5 1 289 . 77 GLU CB C 28.930 0.5 1 290 . 77 GLU N N 122.791 0.6 1 291 . 78 LEU H H 8.095 0.06 1 292 . 78 LEU CA C 57.025 0.5 1 293 . 78 LEU CB C 41.145 0.5 1 294 . 78 LEU N N 119.143 0.6 1 295 . 79 GLU H H 8.134 0.06 1 296 . 79 GLU CA C 58.563 0.5 1 297 . 79 GLU CB C 28.965 0.5 1 298 . 79 GLU N N 117.525 0.6 1 299 . 80 GLU H H 7.618 0.06 1 300 . 80 GLU CA C 57.697 0.5 1 301 . 80 GLU CB C 29.255 0.5 1 302 . 80 GLU N N 117.576 0.6 1 303 . 81 GLN H H 7.559 0.06 1 304 . 81 GLN CA C 55.380 0.5 1 305 . 81 GLN CB C 28.840 0.5 1 306 . 81 GLN N N 116.097 0.6 1 307 . 82 LEU H H 7.579 0.06 1 308 . 82 LEU CA C 54.733 0.5 1 309 . 82 LEU CB C 41.560 0.5 1 310 . 82 LEU N N 120.314 0.6 1 311 . 83 THR H H 7.938 0.06 1 312 . 83 THR CA C 61.690 0.5 1 313 . 83 THR CB C 68.640 0.5 1 314 . 83 THR N N 117.534 0.6 1 315 . 84 PRO CA C 63.800 0.5 1 316 . 84 PRO CB C 30.970 0.5 1 317 . 85 VAL H H 7.737 0.06 1 318 . 85 VAL CA C 61.083 0.5 1 319 . 85 VAL CB C 33.037 0.5 1 320 . 85 VAL N N 118.606 0.6 1 321 . 86 ALA H H 8.305 0.06 1 322 . 86 ALA CA C 52.363 0.5 1 323 . 86 ALA CB C 18.437 0.5 1 324 . 86 ALA N N 125.929 0.6 1 325 . 87 GLU H H 8.754 0.06 1 326 . 87 GLU CA C 59.205 0.5 1 327 . 87 GLU CB C 29.055 0.5 1 328 . 87 GLU N N 123.187 0.6 1 329 . 88 GLU H H 9.157 0.06 1 330 . 88 GLU CA C 59.147 0.5 1 331 . 88 GLU CB C 28.620 0.5 1 332 . 88 GLU N N 118.120 0.6 1 333 . 89 THR H H 7.393 0.06 1 334 . 89 THR CA C 65.327 0.5 1 335 . 89 THR CB C 68.110 0.5 1 336 . 89 THR N N 116.512 0.6 1 337 . 90 ARG H H 8.193 0.06 1 338 . 90 ARG CA C 59.220 0.5 1 339 . 90 ARG CB C 29.275 0.5 1 340 . 90 ARG N N 121.776 0.6 1 341 . 91 ALA H H 8.426 0.06 1 342 . 91 ALA CA C 54.825 0.5 1 343 . 91 ALA CB C 17.695 0.5 1 344 . 91 ALA N N 121.191 0.6 1 345 . 92 ARG H H 7.647 0.06 1 346 . 92 ARG CA C 58.965 0.5 1 347 . 92 ARG CB C 29.280 0.5 1 348 . 92 ARG N N 119.377 0.6 1 349 . 93 LEU H H 8.327 0.06 1 350 . 93 LEU CA C 57.440 0.5 1 351 . 93 LEU CB C 40.970 0.5 1 352 . 93 LEU N N 118.669 0.6 1 353 . 94 SER H H 8.451 0.06 1 354 . 94 SER CA C 61.240 0.5 1 355 . 94 SER CB C 62.530 0.5 1 356 . 94 SER N N 114.163 0.6 1 357 . 95 LYS H H 7.933 0.06 1 358 . 95 LYS CA C 59.315 0.5 1 359 . 95 LYS CB C 31.685 0.5 1 360 . 95 LYS N N 122.241 0.6 1 361 . 96 GLU H H 8.313 0.06 1 362 . 96 GLU CA C 58.665 0.5 1 363 . 96 GLU CB C 29.100 0.5 1 364 . 96 GLU N N 119.255 0.6 1 365 . 97 LEU H H 8.244 0.06 1 366 . 97 LEU CA C 57.625 0.5 1 367 . 97 LEU CB C 40.850 0.5 1 368 . 97 LEU N N 121.700 0.6 1 369 . 98 GLN H H 8.319 0.06 1 370 . 98 GLN CA C 58.645 0.5 1 371 . 98 GLN CB C 27.597 0.5 1 372 . 98 GLN N N 119.596 0.6 1 373 . 99 ALA H H 7.876 0.06 1 374 . 99 ALA CA C 54.565 0.5 1 375 . 99 ALA CB C 17.475 0.5 1 376 . 99 ALA N N 121.262 0.6 1 377 . 100 ALA H H 7.801 0.06 1 378 . 100 ALA CA C 54.475 0.5 1 379 . 100 ALA CB C 17.983 0.5 1 380 . 100 ALA N N 121.238 0.6 1 381 . 101 GLN H H 8.582 0.06 1 382 . 101 GLN CA C 59.115 0.5 1 383 . 101 GLN CB C 27.965 0.5 1 384 . 101 GLN N N 120.961 0.6 1 385 . 102 ALA H H 8.171 0.06 1 386 . 102 ALA CA C 54.293 0.5 1 387 . 102 ALA CB C 17.340 0.5 1 388 . 102 ALA N N 121.146 0.6 1 389 . 103 ARG H H 7.890 0.06 1 390 . 103 ARG CA C 59.087 0.5 1 391 . 103 ARG CB C 29.977 0.5 1 392 . 103 ARG N N 119.377 0.6 1 393 . 104 LEU H H 7.318 0.06 1 394 . 104 LEU CA C 57.710 0.5 1 395 . 104 LEU CB C 41.430 0.5 1 396 . 104 LEU N N 118.647 0.6 1 397 . 105 GLY H H 8.312 0.06 1 398 . 105 GLY CA C 47.368 0.5 1 399 . 105 GLY N N 104.426 0.6 1 400 . 106 ALA H H 8.208 0.06 1 401 . 106 ALA CA C 54.520 0.5 1 402 . 106 ALA CB C 17.600 0.5 1 403 . 106 ALA N N 123.880 0.6 1 404 . 107 ASP H H 8.287 0.06 1 405 . 107 ASP CA C 56.455 0.5 1 406 . 107 ASP CB C 38.270 0.5 1 407 . 107 ASP N N 118.570 0.6 1 408 . 108 MET H H 8.111 0.06 1 409 . 108 MET CA C 60.480 0.5 1 410 . 108 MET CB C 33.010 0.5 1 411 . 108 MET N N 118.522 0.6 1 412 . 109 GLU H H 8.626 0.06 1 413 . 109 GLU CA C 59.320 0.5 1 414 . 109 GLU CB C 28.870 0.5 1 415 . 109 GLU N N 121.719 0.6 1 416 . 110 ASP H H 8.563 0.06 1 417 . 110 ASP CA C 56.735 0.5 1 418 . 110 ASP CB C 40.105 0.5 1 419 . 110 ASP N N 120.904 0.6 1 420 . 111 VAL H H 7.763 0.06 1 421 . 111 VAL CA C 66.785 0.5 1 422 . 111 VAL CB C 31.095 0.5 1 423 . 111 VAL N N 119.098 0.6 1 424 . 112 CYS H H 7.795 0.06 1 425 . 112 CYS CA C 64.323 0.5 1 426 . 112 CYS CB C 26.240 0.5 1 427 . 112 CYS N N 116.762 0.6 1 428 . 113 GLY H H 9.187 0.06 1 429 . 113 GLY CA C 46.710 0.5 1 430 . 113 GLY N N 106.483 0.6 1 431 . 114 ARG H H 8.409 0.06 1 432 . 114 ARG CA C 56.535 0.5 1 433 . 114 ARG CB C 28.185 0.5 1 434 . 114 ARG N N 122.579 0.6 1 435 . 115 LEU H H 7.733 0.06 1 436 . 115 LEU CA C 57.250 0.5 1 437 . 115 LEU CB C 40.400 0.5 1 438 . 115 LEU N N 120.704 0.6 1 439 . 116 VAL H H 8.153 0.06 1 440 . 116 VAL CA C 66.730 0.5 1 441 . 116 VAL CB C 31.340 0.5 1 442 . 116 VAL N N 122.820 0.6 1 443 . 117 GLN H H 8.306 0.06 1 444 . 117 GLN CA C 58.545 0.5 1 445 . 117 GLN CB C 28.120 0.5 1 446 . 117 GLN N N 121.153 0.6 1 447 . 118 TYR H H 8.038 0.06 1 448 . 118 TYR CA C 60.725 0.5 1 449 . 118 TYR CB C 38.155 0.5 1 450 . 118 TYR N N 120.123 0.6 1 451 . 119 ARG H H 7.778 0.06 1 452 . 119 ARG CA C 59.527 0.5 1 453 . 119 ARG CB C 29.023 0.5 1 454 . 119 ARG N N 118.106 0.6 1 455 . 120 GLY H H 7.748 0.06 1 456 . 120 GLY CA C 46.572 0.5 1 457 . 120 GLY N N 104.451 0.6 1 458 . 121 GLU H H 8.200 0.06 1 459 . 121 GLU CA C 59.170 0.5 1 460 . 121 GLU CB C 29.110 0.5 1 461 . 121 GLU N N 123.391 0.6 1 462 . 122 VAL H H 8.203 0.06 1 463 . 122 VAL CA C 65.683 0.5 1 464 . 122 VAL CB C 30.745 0.5 1 465 . 122 VAL N N 118.642 0.6 1 466 . 123 GLN H H 7.958 0.06 1 467 . 123 GLN CA C 58.415 0.5 1 468 . 123 GLN CB C 27.890 0.5 1 469 . 123 GLN N N 118.984 0.6 1 470 . 124 ALA H H 7.611 0.06 1 471 . 124 ALA CA C 53.263 0.5 1 472 . 124 ALA CB C 18.050 0.5 1 473 . 124 ALA N N 120.384 0.6 1 474 . 125 MET H H 7.429 0.06 1 475 . 125 MET CA C 54.537 0.5 1 476 . 125 MET CB C 31.753 0.5 1 477 . 125 MET N N 117.041 0.6 1 478 . 126 LEU H H 7.683 0.06 1 479 . 126 LEU CA C 55.893 0.5 1 480 . 126 LEU CB C 39.697 0.5 1 481 . 126 LEU N N 119.092 0.6 1 482 . 127 GLY H H 8.570 0.06 1 483 . 127 GLY CA C 45.070 0.5 1 484 . 127 GLY N N 108.616 0.6 1 485 . 128 GLN H H 7.756 0.06 1 486 . 128 GLN CA C 54.243 0.5 1 487 . 128 GLN CB C 29.930 0.5 1 488 . 128 GLN N N 119.134 0.6 1 489 . 129 SER H H 8.370 0.06 1 490 . 129 SER CA C 57.550 0.5 1 491 . 129 SER CB C 63.250 0.5 1 492 . 129 SER N N 114.289 0.6 1 493 . 130 THR H H 8.194 0.06 1 494 . 130 THR CA C 60.820 0.5 1 495 . 130 THR CB C 69.435 0.5 1 496 . 130 THR N N 114.513 0.6 1 497 . 131 GLU H H 8.428 0.06 1 498 . 131 GLU CA C 59.830 0.5 1 499 . 131 GLU CB C 29.000 0.5 1 500 . 131 GLU N N 123.308 0.6 1 501 . 132 GLU H H 8.558 0.06 1 502 . 132 GLU CA C 59.340 0.5 1 503 . 132 GLU CB C 28.520 0.5 1 504 . 132 GLU N N 117.683 0.6 1 505 . 133 LEU H H 7.592 0.06 1 506 . 133 LEU CA C 57.435 0.5 1 507 . 133 LEU CB C 41.240 0.5 1 508 . 133 LEU N N 118.641 0.6 1 509 . 134 ARG H H 8.123 0.06 1 510 . 134 ARG CA C 60.120 0.5 1 511 . 134 ARG CB C 29.945 0.5 1 512 . 134 ARG N N 120.000 0.6 1 513 . 135 VAL H H 8.334 0.06 1 514 . 135 VAL CA C 65.977 0.5 1 515 . 135 VAL CB C 31.360 0.5 1 516 . 135 VAL N N 120.687 0.6 1 517 . 136 ARG H H 7.835 0.06 1 518 . 136 ARG CA C 58.960 0.5 1 519 . 136 ARG CB C 29.655 0.5 1 520 . 136 ARG N N 120.331 0.6 1 521 . 137 LEU H H 8.062 0.06 1 522 . 137 LEU CA C 57.800 0.5 1 523 . 137 LEU CB C 39.950 0.5 1 524 . 137 LEU N N 120.627 0.6 1 525 . 138 ALA H H 8.527 0.06 1 526 . 138 ALA CA C 55.183 0.5 1 527 . 138 ALA CB C 17.630 0.5 1 528 . 138 ALA N N 120.671 0.6 1 529 . 139 SER H H 7.864 0.06 1 530 . 139 SER CA C 60.980 0.5 1 531 . 139 SER CB C 62.500 0.5 1 532 . 139 SER N N 112.624 0.6 1 533 . 140 HIS H H 8.242 0.06 1 534 . 140 HIS CA C 58.750 0.5 1 535 . 140 HIS CB C 31.390 0.5 1 536 . 140 HIS N N 122.260 0.6 1 537 . 141 LEU H H 9.141 0.06 1 538 . 141 LEU CA C 57.750 0.5 1 539 . 141 LEU CB C 40.780 0.5 1 540 . 141 LEU N N 117.886 0.6 1 541 . 142 ARG H H 7.971 0.06 1 542 . 142 ARG CA C 60.265 0.5 1 543 . 142 ARG CB C 29.530 0.5 1 544 . 142 ARG N N 119.785 0.6 1 545 . 143 LYS H H 7.547 0.06 1 546 . 143 LYS CA C 59.325 0.5 1 547 . 143 LYS CB C 31.845 0.5 1 548 . 143 LYS N N 119.120 0.6 1 549 . 144 LEU H H 8.473 0.06 1 550 . 144 LEU CA C 57.457 0.5 1 551 . 144 LEU CB C 41.280 0.5 1 552 . 144 LEU N N 120.633 0.6 1 553 . 145 ARG H H 8.771 0.06 1 554 . 145 ARG CA C 60.130 0.5 1 555 . 145 ARG CB C 29.420 0.5 1 556 . 145 ARG N N 119.770 0.6 1 557 . 146 LYS H H 7.606 0.06 1 558 . 146 LYS CA C 59.605 0.5 1 559 . 146 LYS CB C 31.820 0.5 1 560 . 146 LYS N N 118.087 0.6 1 561 . 147 ARG H H 7.660 0.06 1 562 . 147 ARG CA C 59.285 0.5 1 563 . 147 ARG CB C 29.975 0.5 1 564 . 147 ARG N N 120.133 0.6 1 565 . 148 LEU H H 8.421 0.06 1 566 . 148 LEU CA C 57.985 0.5 1 567 . 148 LEU CB C 42.215 0.5 1 568 . 148 LEU N N 119.171 0.6 1 569 . 149 LEU H H 8.110 0.06 1 570 . 149 LEU CA C 57.995 0.5 1 571 . 149 LEU CB C 40.945 0.5 1 572 . 149 LEU N N 118.517 0.6 1 573 . 150 ARG H H 7.636 0.06 1 574 . 150 ARG CA C 58.840 0.5 1 575 . 150 ARG CB C 29.245 0.5 1 576 . 150 ARG N N 119.322 0.6 1 577 . 151 ASP H H 8.869 0.06 1 578 . 151 ASP CA C 56.210 0.5 1 579 . 151 ASP CB C 38.115 0.5 1 580 . 151 ASP N N 120.278 0.6 1 581 . 152 ALA H H 9.137 0.06 1 582 . 152 ALA CA C 55.495 0.5 1 583 . 152 ALA CB C 18.140 0.5 1 584 . 152 ALA N N 125.906 0.6 1 585 . 153 ASP H H 8.162 0.06 1 586 . 153 ASP CA C 57.305 0.5 1 587 . 153 ASP CB C 41.545 0.5 1 588 . 153 ASP N N 119.330 0.6 1 589 . 154 ASP H H 8.114 0.06 1 590 . 154 ASP CA C 57.520 0.5 1 591 . 154 ASP CB C 41.540 0.5 1 592 . 154 ASP N N 118.025 0.6 1 593 . 155 LEU H H 7.919 0.06 1 594 . 155 LEU CA C 58.125 0.5 1 595 . 155 LEU CB C 41.610 0.5 1 596 . 155 LEU N N 118.599 0.6 1 597 . 156 GLN H H 8.761 0.06 1 598 . 156 GLN CA C 59.795 0.5 1 599 . 156 GLN CB C 28.233 0.5 1 600 . 156 GLN N N 118.524 0.6 1 601 . 157 LYS H H 8.214 0.06 1 602 . 157 LYS CA C 59.550 0.5 1 603 . 157 LYS CB C 31.875 0.5 1 604 . 157 LYS N N 119.663 0.6 1 605 . 158 ARG H H 8.216 0.06 1 606 . 158 ARG CA C 58.415 0.5 1 607 . 158 ARG CB C 29.345 0.5 1 608 . 158 ARG N N 118.622 0.6 1 609 . 159 LEU H H 8.720 0.06 1 610 . 159 LEU CA C 57.455 0.5 1 611 . 159 LEU CB C 41.375 0.5 1 612 . 159 LEU N N 120.673 0.6 1 613 . 160 ALA H H 7.942 0.06 1 614 . 160 ALA CA C 54.725 0.5 1 615 . 160 ALA CB C 17.810 0.5 1 616 . 160 ALA N N 121.263 0.6 1 617 . 161 VAL H H 7.596 0.06 1 618 . 161 VAL CA C 64.820 0.5 1 619 . 161 VAL CB C 31.430 0.5 1 620 . 161 VAL N N 116.950 0.6 1 621 . 162 TYR H H 7.686 0.06 1 622 . 162 TYR CA C 60.247 0.5 1 623 . 162 TYR CB C 38.847 0.5 1 624 . 162 TYR N N 120.937 0.6 1 625 . 163 GLN H H 8.231 0.06 1 626 . 163 GLN CA C 57.425 0.5 1 627 . 163 GLN CB C 28.685 0.5 1 628 . 163 GLN N N 116.971 0.6 1 629 . 164 ALA H H 7.910 0.06 1 630 . 164 ALA CA C 53.357 0.5 1 631 . 164 ALA CB C 18.330 0.5 1 632 . 164 ALA N N 121.375 0.6 1 633 . 165 GLY H H 8.064 0.06 1 634 . 165 GLY CA C 45.548 0.5 1 635 . 165 GLY N N 106.534 0.6 1 636 . 166 ALA H H 7.899 0.06 1 637 . 166 ALA CA C 52.465 0.5 1 638 . 166 ALA CB C 18.815 0.5 1 639 . 166 ALA N N 122.228 0.6 1 640 . 167 ARG H H 8.058 0.06 1 641 . 167 ARG CA C 56.290 0.5 1 642 . 167 ARG CB C 30.240 0.5 1 643 . 167 ARG N N 119.116 0.6 1 644 . 168 GLU CA C 56.920 0.5 1 645 . 168 GLU CB C 29.545 0.5 1 646 . 169 GLY H H 8.440 0.06 1 647 . 169 GLY CA C 45.303 0.5 1 648 . 169 GLY N N 109.704 0.6 1 649 . 170 ALA H H 8.076 0.06 1 650 . 170 ALA CA C 52.693 0.5 1 651 . 170 ALA CB C 18.857 0.5 1 652 . 170 ALA N N 123.339 0.6 1 653 . 171 GLU H H 8.486 0.06 1 654 . 171 GLU CA C 56.760 0.5 1 655 . 171 GLU CB C 29.315 0.5 1 656 . 171 GLU N N 119.127 0.6 1 657 . 172 ARG H H 8.205 0.06 1 658 . 172 ARG CA C 56.160 0.5 1 659 . 172 ARG CB C 30.107 0.5 1 660 . 172 ARG N N 121.162 0.6 1 661 . 173 GLY H H 8.331 0.06 1 662 . 173 GLY CA C 45.223 0.5 1 663 . 173 GLY N N 109.073 0.6 1 664 . 174 LEU H H 8.068 0.06 1 665 . 174 LEU CA C 55.183 0.5 1 666 . 174 LEU CB C 41.643 0.5 1 667 . 174 LEU N N 121.261 0.6 1 668 . 175 SER H H 8.274 0.06 1 669 . 175 SER CA C 58.413 0.5 1 670 . 175 SER CB C 63.330 0.5 1 671 . 175 SER N N 115.967 0.6 1 672 . 176 ALA H H 8.179 0.06 1 673 . 176 ALA CA C 52.407 0.5 1 674 . 176 ALA CB C 18.747 0.5 1 675 . 176 ALA N N 125.416 0.6 1 676 . 177 ILE H H 7.931 0.06 1 677 . 177 ILE CA C 61.340 0.5 1 678 . 177 ILE CB C 37.847 0.5 1 679 . 177 ILE N N 119.127 0.6 1 680 . 178 ARG H H 8.243 0.06 1 681 . 178 ARG CA C 56.305 0.5 1 682 . 178 ARG CB C 30.035 0.5 1 683 . 178 ARG N N 123.359 0.6 1 684 . 179 GLU H H 8.288 0.06 1 685 . 179 GLU CA C 56.625 0.5 1 686 . 179 GLU CB C 29.985 0.5 1 687 . 179 GLU N N 120.712 0.6 1 688 . 180 ARG H H 8.150 0.06 1 689 . 180 ARG CA C 56.440 0.5 1 690 . 180 ARG CB C 29.810 0.5 1 691 . 180 ARG N N 120.682 0.6 1 692 . 181 LEU H H 8.148 0.06 1 693 . 181 LEU CA C 54.733 0.5 1 694 . 181 LEU CB C 41.463 0.5 1 695 . 181 LEU N N 122.862 0.6 1 696 . 182 GLY H H 8.008 0.06 1 697 . 182 GLY CA C 44.110 0.5 1 698 . 182 GLY N N 109.209 0.6 1 stop_ save_