data_6447 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a two-repeat fragment of major vault protein ; _BMRB_accession_number 6447 _BMRB_flat_file_name bmr6447.str _Entry_type original _Submission_date 2004-12-28 _Accession_date 2004-12-28 _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 Kozlov G. . . 2 Vavelyuk O. . . 3 Minailiuc O. . . 4 Banville D. . . 5 Gehring K. . . 6 Ekiel I. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 508 "13C chemical shifts" 204 "15N chemical shifts" 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-29 original author . stop_ _Original_release_date 2007-01-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of a Two-repeat Fragment of Major Vault Protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16373071 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kozlov G. . . 2 Vavelyuk O. . . 3 Minailiuc O. . . 4 Banville D. . . 5 Gehring K. . . 6 Ekiel I. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 356 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 444 _Page_last 452 _Year 2006 _Details . loop_ _Keyword 'beta-sheet modules' 'structural repeats' stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name 'Major vault protein' _Abbreviation_common 'Major vault protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label mv_protein $mv_protein 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_mv_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Major vault protein' _Abbreviation_common 'Major vault protein' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; GSHMQVVLPNTALHLKALLD FEDKDGDKVVAGDEWLFEGP GTYIPRKEVEVVEIIQATII RQNQALRLRARKECWDRDGK ERVTGEEWLVTTVGAYLPAV FEEVLDLVDAVIL ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 GLN 6 VAL 7 VAL 8 LEU 9 PRO 10 ASN 11 THR 12 ALA 13 LEU 14 HIS 15 LEU 16 LYS 17 ALA 18 LEU 19 LEU 20 ASP 21 PHE 22 GLU 23 ASP 24 LYS 25 ASP 26 GLY 27 ASP 28 LYS 29 VAL 30 VAL 31 ALA 32 GLY 33 ASP 34 GLU 35 TRP 36 LEU 37 PHE 38 GLU 39 GLY 40 PRO 41 GLY 42 THR 43 TYR 44 ILE 45 PRO 46 ARG 47 LYS 48 GLU 49 VAL 50 GLU 51 VAL 52 VAL 53 GLU 54 ILE 55 ILE 56 GLN 57 ALA 58 THR 59 ILE 60 ILE 61 ARG 62 GLN 63 ASN 64 GLN 65 ALA 66 LEU 67 ARG 68 LEU 69 ARG 70 ALA 71 ARG 72 LYS 73 GLU 74 CYS 75 TRP 76 ASP 77 ARG 78 ASP 79 GLY 80 LYS 81 GLU 82 ARG 83 VAL 84 THR 85 GLY 86 GLU 87 GLU 88 TRP 89 LEU 90 VAL 91 THR 92 THR 93 VAL 94 GLY 95 ALA 96 TYR 97 LEU 98 PRO 99 ALA 100 VAL 101 PHE 102 GLU 103 GLU 104 VAL 105 LEU 106 ASP 107 LEU 108 VAL 109 ASP 110 ALA 111 VAL 112 ILE 113 LEU 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 PDB 1Y7X "Solution Structure Of A Two-Repeat Fragment Of Major Vault Protein" 100.00 113 100.00 100.00 2.42e-74 GB AHW56615 "major vault protein isoform G, partial [Homo sapiens]" 99.12 326 97.32 99.11 2.49e-68 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $mv_protein 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 $mv_protein '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 $mv_protein 1 mM [U-15N] bis-Tris 20 mM . NaCl 150 mM . CaCl2 2 mM . DTT 15 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.1 loop_ _Task collection processing stop_ _Details 'Bruker Biospin' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details Wuthrich save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0.6 loop_ _Task 'structure solution' stop_ _Details Guentert save_ save_Xplor-NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.9.2 loop_ _Task refinement stop_ _Details Clore save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . 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' 150 . mM pH 6.8 . pH pressure 1 . atm temperature 303 . 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 DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.00000 DSS N 15 'methyl protons' ppm 0.00 external 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_chemical_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 mv_protein _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 . 3 HIS N N 125.0 0.25 1 2 . 3 HIS H H 8.10 0.01 1 3 . 3 HIS CA C 56.6 0.20 1 4 . 3 HIS CB C 31.3 0.20 1 5 . 4 MET N N 118.1 0.25 1 6 . 4 MET H H 7.96 0.01 1 7 . 4 MET CA C 56.7 0.20 1 8 . 4 MET HA H 4.47 0.01 1 9 . 4 MET CB C 34.8 0.20 1 10 . 4 MET HB2 H 1.80 0.01 2 11 . 4 MET HG2 H 2.29 0.01 2 12 . 5 GLN N N 121.6 0.25 1 13 . 5 GLN H H 8.86 0.01 1 14 . 5 GLN CA C 55.5 0.20 1 15 . 5 GLN HA H 4.63 0.01 1 16 . 5 GLN CB C 32.2 0.20 1 17 . 5 GLN HB2 H 1.96 0.01 2 18 . 5 GLN HB3 H 1.87 0.01 2 19 . 5 GLN HG2 H 2.16 0.01 2 20 . 5 GLN HE21 H 7.40 0.01 2 21 . 5 GLN HE22 H 6.33 0.01 2 22 . 6 VAL N N 126.6 0.25 1 23 . 6 VAL H H 8.75 0.01 1 24 . 6 VAL CA C 64.7 0.20 1 25 . 6 VAL HA H 4.06 0.01 1 26 . 6 VAL CB C 32.9 0.20 1 27 . 6 VAL HB H 1.92 0.01 1 28 . 6 VAL HG1 H 0.93 0.01 2 29 . 7 VAL N N 129.8 0.25 1 30 . 7 VAL H H 9.09 0.01 1 31 . 7 VAL CA C 62.4 0.20 1 32 . 7 VAL HA H 4.16 0.01 1 33 . 7 VAL CB C 33.2 0.20 1 34 . 7 VAL HB H 1.88 0.01 1 35 . 7 VAL HG1 H 0.87 0.01 2 36 . 7 VAL HG2 H 0.82 0.01 2 37 . 8 LEU N N 128.8 0.25 1 38 . 8 LEU H H 8.37 0.01 1 39 . 8 LEU HA H 4.38 0.01 1 40 . 8 LEU HB2 H 1.75 0.01 2 41 . 8 LEU HB3 H 1.55 0.01 2 42 . 8 LEU HG H 1.60 0.01 1 43 . 8 LEU HD1 H 0.92 0.01 2 44 . 8 LEU HD2 H 0.85 0.01 2 45 . 9 PRO CA C 64.0 0.20 1 46 . 9 PRO HA H 3.82 0.01 1 47 . 9 PRO CB C 32.5 0.20 1 48 . 9 PRO HB2 H 2.21 0.01 2 49 . 9 PRO HB3 H 1.99 0.01 2 50 . 9 PRO HG2 H 2.09 0.01 2 51 . 9 PRO HG3 H 1.76 0.01 2 52 . 10 ASN N N 113.3 0.25 1 53 . 10 ASN H H 9.21 0.01 1 54 . 10 ASN CA C 55.4 0.20 1 55 . 10 ASN HA H 4.07 0.01 1 56 . 10 ASN CB C 37.5 0.20 1 57 . 10 ASN HB2 H 3.02 0.01 2 58 . 10 ASN HB3 H 2.83 0.01 2 59 . 10 ASN HD21 H 6.71 0.01 2 60 . 10 ASN HD22 H 7.49 0.01 2 61 . 11 THR N N 105.4 0.25 1 62 . 11 THR H H 7.57 0.01 1 63 . 11 THR CA C 60.7 0.20 1 64 . 11 THR HA H 5.22 0.01 1 65 . 11 THR CB C 74.3 0.20 1 66 . 11 THR HB H 3.99 0.01 1 67 . 11 THR HG2 H 1.03 0.01 1 68 . 12 ALA N N 117.6 0.25 1 69 . 12 ALA H H 9.02 0.01 1 70 . 12 ALA CA C 51.1 0.20 1 71 . 12 ALA HA H 5.04 0.01 1 72 . 12 ALA HB H 1.12 0.01 1 73 . 12 ALA CB C 25.8 0.20 1 74 . 13 LEU N N 116.4 0.25 1 75 . 13 LEU H H 8.99 0.01 1 76 . 13 LEU CA C 54.2 0.20 1 77 . 13 LEU HA H 4.82 0.01 1 78 . 13 LEU CB C 43.0 0.20 1 79 . 13 LEU HB2 H 0.85 0.01 2 80 . 13 LEU HB3 H 0.59 0.01 2 81 . 13 LEU HD1 H 0.07 0.01 2 82 . 14 HIS N N 122.2 0.25 1 83 . 14 HIS H H 8.60 0.01 1 84 . 14 HIS CA C 53.3 0.20 1 85 . 14 HIS HA H 4.83 0.01 1 86 . 14 HIS CB C 31.0 0.20 1 87 . 14 HIS HB2 H 3.33 0.01 2 88 . 14 HIS HB3 H 2.62 0.01 2 89 . 14 HIS HD2 H 7.03 0.01 1 90 . 14 HIS HE1 H 8.48 0.01 1 91 . 15 LEU N N 129.3 0.25 1 92 . 15 LEU H H 8.95 0.01 1 93 . 15 LEU CA C 53.9 0.20 1 94 . 15 LEU HA H 4.82 0.01 1 95 . 15 LEU CB C 42.1 0.20 1 96 . 15 LEU HB2 H 0.99 0.01 1 97 . 15 LEU HG H 0.54 0.01 1 98 . 15 LEU HD1 H 0.22 0.01 2 99 . 15 LEU HD2 H -0.17 0.01 2 100 . 16 LYS N N 117.9 0.25 1 101 . 16 LYS H H 8.19 0.01 1 102 . 16 LYS CA C 55.0 0.20 1 103 . 16 LYS HA H 5.15 0.01 1 104 . 16 LYS CB C 38.2 0.20 1 105 . 16 LYS HB2 H 1.22 0.01 2 106 . 16 LYS HG2 H 1.47 0.01 2 107 . 17 ALA N N 127.4 0.25 1 108 . 17 ALA H H 9.18 0.01 1 109 . 17 ALA CA C 53.1 0.20 1 110 . 17 ALA HA H 5.00 0.01 1 111 . 17 ALA HB H 1.86 0.01 1 112 . 17 ALA CB C 20.2 0.20 1 113 . 18 LEU N N 126.1 0.25 1 114 . 18 LEU H H 9.74 0.01 1 115 . 18 LEU CA C 53.8 0.20 1 116 . 18 LEU HA H 4.30 0.01 1 117 . 18 LEU CB C 46.7 0.20 1 118 . 18 LEU HB2 H 1.54 0.01 2 119 . 18 LEU HD1 H 0.82 0.01 2 120 . 18 LEU HD2 H 0.76 0.01 2 121 . 19 LEU N N 126.6 0.25 1 122 . 19 LEU H H 8.63 0.01 1 123 . 19 LEU CA C 53.8 0.20 1 124 . 19 LEU HA H 4.57 0.01 1 125 . 19 LEU CB C 48.2 0.20 1 126 . 19 LEU HB2 H 1.81 0.01 2 127 . 19 LEU HB3 H 1.18 0.01 2 128 . 19 LEU HG H 1.36 0.01 1 129 . 19 LEU HD1 H 0.92 0.01 2 130 . 20 ASP N N 117.8 0.25 1 131 . 20 ASP H H 8.08 0.01 1 132 . 20 ASP CA C 54.9 0.20 1 133 . 20 ASP HA H 4.92 0.01 1 134 . 20 ASP CB C 41.7 0.20 1 135 . 20 ASP HB2 H 2.72 0.01 2 136 . 20 ASP HB3 H 2.53 0.01 2 137 . 21 PHE N N 115.2 0.25 1 138 . 21 PHE H H 8.63 0.01 1 139 . 21 PHE CA C 58.0 0.20 1 140 . 21 PHE HA H 4.72 0.01 1 141 . 21 PHE CB C 40.9 0.20 1 142 . 21 PHE HB2 H 3.14 0.01 2 143 . 21 PHE HB3 H 2.83 0.01 2 144 . 21 PHE HD1 H 7.09 0.01 2 145 . 21 PHE HE1 H 7.18 0.01 2 146 . 22 GLU N N 118.3 0.25 1 147 . 22 GLU H H 8.27 0.01 1 148 . 22 GLU CA C 55.4 0.20 1 149 . 22 GLU HA H 4.73 0.01 1 150 . 22 GLU CB C 32.5 0.20 1 151 . 22 GLU HB2 H 1.79 0.01 2 152 . 23 ASP N N 125.4 0.25 1 153 . 23 ASP H H 8.80 0.01 1 154 . 23 ASP CA C 53.7 0.20 1 155 . 23 ASP HA H 4.69 0.01 1 156 . 23 ASP CB C 42.5 0.20 1 157 . 23 ASP HB2 H 2.87 0.01 2 158 . 23 ASP HB3 H 2.64 0.01 2 159 . 24 LYS N N 118.4 0.25 1 160 . 24 LYS H H 8.56 0.01 1 161 . 24 LYS CA C 59.1 0.20 1 162 . 24 LYS HA H 4.06 0.01 1 163 . 24 LYS CB C 32.9 0.20 1 164 . 24 LYS HB2 H 1.80 0.01 2 165 . 24 LYS HG2 H 1.38 0.01 2 166 . 25 ASP N N 117.1 0.25 1 167 . 25 ASP H H 8.09 0.01 1 168 . 25 ASP CA C 55.3 0.20 1 169 . 25 ASP HA H 4.65 0.01 1 170 . 25 ASP CB C 41.9 0.20 1 171 . 25 ASP HB2 H 2.73 0.01 2 172 . 25 ASP HB3 H 2.62 0.01 2 173 . 26 GLY N N 107.5 0.25 1 174 . 26 GLY H H 8.10 0.01 1 175 . 26 GLY CA C 45.8 0.20 1 176 . 26 GLY HA2 H 4.09 0.01 2 177 . 26 GLY HA3 H 3.64 0.01 2 178 . 27 ASP N N 120.9 0.25 1 179 . 27 ASP H H 8.02 0.01 1 180 . 27 ASP CA C 54.8 0.20 1 181 . 27 ASP HA H 4.48 0.01 1 182 . 27 ASP CB C 41.8 0.20 1 183 . 27 ASP HB2 H 2.48 0.01 2 184 . 27 ASP HB3 H 2.35 0.01 2 185 . 28 LYS N N 120.9 0.25 1 186 . 28 LYS H H 8.17 0.01 1 187 . 28 LYS CA C 57.2 0.20 1 188 . 28 LYS HA H 4.14 0.01 1 189 . 28 LYS CB C 33.3 0.20 1 190 . 28 LYS HB2 H 1.58 0.01 2 191 . 28 LYS HG2 H 1.26 0.01 2 192 . 28 LYS HG3 H 1.17 0.01 2 193 . 29 VAL N N 128.7 0.25 1 194 . 29 VAL H H 8.63 0.01 1 195 . 29 VAL HA H 3.60 0.01 1 196 . 29 VAL HB H 0.55 0.01 1 197 . 29 VAL HG1 H 0.38 0.01 2 198 . 29 VAL HG2 H 0.05 0.01 2 199 . 30 VAL N N 125.3 0.25 1 200 . 30 VAL H H 8.08 0.01 1 201 . 30 VAL CA C 60.8 0.20 1 202 . 30 VAL HA H 4.27 0.01 1 203 . 30 VAL CB C 34.3 0.20 1 204 . 30 VAL HB H 1.87 0.01 1 205 . 30 VAL HG1 H 0.89 0.01 2 206 . 30 VAL HG2 H 0.74 0.01 2 207 . 31 ALA N N 125.0 0.25 1 208 . 31 ALA H H 8.84 0.01 1 209 . 31 ALA CA C 54.8 0.20 1 210 . 31 ALA HA H 3.48 0.01 1 211 . 31 ALA HB H 1.19 0.01 1 212 . 31 ALA CB C 19.0 0.20 1 213 . 32 GLY N N 111.6 0.25 1 214 . 32 GLY H H 9.06 0.01 1 215 . 32 GLY CA C 45.6 0.20 1 216 . 32 GLY HA3 H 4.57 0.01 2 217 . 33 ASP N N 123.2 0.25 1 218 . 33 ASP H H 8.86 0.01 1 219 . 33 ASP CA C 56.9 0.20 1 220 . 33 ASP HA H 4.77 0.01 1 221 . 33 ASP CB C 41.8 0.20 1 222 . 33 ASP HB2 H 3.01 0.01 2 223 . 33 ASP HB3 H 2.74 0.01 2 224 . 34 GLU N N 116.2 0.25 1 225 . 34 GLU H H 8.40 0.01 1 226 . 34 GLU CA C 55.9 0.20 1 227 . 34 GLU HA H 5.70 0.01 1 228 . 34 GLU CB C 36.3 0.20 1 229 . 34 GLU HB2 H 1.98 0.01 2 230 . 34 GLU HG2 H 2.21 0.01 2 231 . 35 TRP N N 119.3 0.25 1 232 . 35 TRP H H 8.49 0.01 1 233 . 35 TRP CA C 58.1 0.20 1 234 . 35 TRP HA H 4.66 0.01 1 235 . 35 TRP CB C 31.5 0.20 1 236 . 35 TRP HB2 H 3.60 0.01 2 237 . 35 TRP HB3 H 3.22 0.01 2 238 . 35 TRP NE1 N 130.2 0.25 1 239 . 35 TRP HD1 H 7.10 0.01 1 240 . 35 TRP HE3 H 7.03 0.01 1 241 . 35 TRP HE1 H 10.26 0.01 1 242 . 35 TRP HZ3 H 6.86 0.01 1 243 . 35 TRP HZ2 H 7.56 0.01 1 244 . 35 TRP HH2 H 7.10 0.01 1 245 . 36 LEU N N 115.2 0.25 1 246 . 36 LEU H H 8.54 0.01 1 247 . 36 LEU CA C 53.5 0.20 1 248 . 36 LEU HA H 5.42 0.01 1 249 . 36 LEU CB C 45.4 0.20 1 250 . 36 LEU HB2 H 1.77 0.01 2 251 . 36 LEU HB3 H 1.49 0.01 2 252 . 36 LEU HD1 H 0.94 0.01 2 253 . 36 LEU HD2 H 0.61 0.01 2 254 . 37 PHE N N 122.0 0.25 1 255 . 37 PHE H H 8.75 0.01 1 256 . 37 PHE CA C 57.7 0.20 1 257 . 37 PHE HA H 4.81 0.01 1 258 . 37 PHE CB C 41.8 0.20 1 259 . 37 PHE HB2 H 2.85 0.01 2 260 . 37 PHE HZ H 7.22 0.01 1 261 . 37 PHE HD1 H 7.26 0.01 3 262 . 37 PHE HE1 H 7.14 0.01 3 263 . 38 GLU N N 127.4 0.25 1 264 . 38 GLU H H 8.70 0.01 1 265 . 38 GLU CA C 57.5 0.20 1 266 . 38 GLU HA H 4.14 0.01 1 267 . 38 GLU CB C 31.3 0.20 1 268 . 38 GLU HB2 H 2.05 0.01 2 269 . 38 GLU HB3 H 1.72 0.01 2 270 . 38 GLU HG2 H 1.87 0.01 2 271 . 39 GLY N N 107.7 0.25 1 272 . 39 GLY H H 8.44 0.01 1 273 . 39 GLY HA2 H 3.63 0.01 2 274 . 39 GLY HA3 H 3.48 0.01 2 275 . 40 PRO CA C 61.3 0.20 1 276 . 40 PRO HA H 4.77 0.01 1 277 . 40 PRO CB C 35.6 0.20 1 278 . 40 PRO HB2 H 1.96 0.01 2 279 . 40 PRO HB3 H 1.89 0.01 2 280 . 40 PRO HG2 H 2.19 0.01 2 281 . 41 GLY N N 107.7 0.25 1 282 . 41 GLY H H 8.40 0.01 1 283 . 41 GLY CA C 46.5 0.20 1 284 . 41 GLY HA2 H 4.29 0.01 2 285 . 41 GLY HA3 H 4.19 0.01 2 286 . 42 THR N N 115.7 0.25 1 287 . 42 THR H H 8.96 0.01 1 288 . 42 THR CA C 62.4 0.20 1 289 . 42 THR HA H 4.80 0.01 1 290 . 42 THR CB C 71.1 0.20 1 291 . 42 THR HB H 3.91 0.01 1 292 . 42 THR HG2 H 0.99 0.01 1 293 . 43 TYR N N 127.4 0.25 1 294 . 43 TYR H H 9.12 0.01 1 295 . 43 TYR CA C 57.9 0.20 1 296 . 43 TYR HA H 3.91 0.01 1 297 . 43 TYR CB C 41.3 0.20 1 298 . 43 TYR HB2 H 2.28 0.01 2 299 . 43 TYR HB3 H 1.94 0.01 2 300 . 43 TYR HE1 H 6.35 0.01 3 301 . 43 TYR HD1 H 6.18 0.01 3 302 . 44 ILE N N 128.0 0.25 1 303 . 44 ILE H H 7.22 0.01 1 304 . 44 ILE HA H 4.20 0.01 1 305 . 44 ILE HB H 1.53 0.01 1 306 . 44 ILE HG2 H 0.70 0.01 1 307 . 44 ILE HG12 H 1.30 0.01 2 308 . 44 ILE HG13 H 0.98 0.01 2 309 . 44 ILE HD1 H 0.70 0.01 1 310 . 45 PRO CA C 63.5 0.20 1 311 . 45 PRO HA H 3.94 0.01 1 312 . 45 PRO CB C 34.0 0.20 1 313 . 45 PRO HB2 H 2.20 0.01 2 314 . 45 PRO HG2 H 1.59 0.01 2 315 . 46 ARG N N 114.4 0.25 1 316 . 46 ARG H H 8.08 0.01 1 317 . 46 ARG CA C 55.5 0.20 1 318 . 46 ARG HA H 4.61 0.01 1 319 . 46 ARG CB C 34.3 0.20 1 320 . 46 ARG HB2 H 1.74 0.01 2 321 . 47 LYS N N 119.8 0.25 1 322 . 47 LYS H H 8.50 0.01 1 323 . 47 LYS CA C 59.5 0.20 1 324 . 47 LYS HA H 3.95 0.01 1 325 . 47 LYS CB C 33.0 0.20 1 326 . 47 LYS HB2 H 1.63 0.01 2 327 . 47 LYS HG2 H 1.34 0.01 2 328 . 48 GLU N N 114.2 0.25 1 329 . 48 GLU H H 9.11 0.01 1 330 . 48 GLU CA C 59.7 0.20 1 331 . 48 GLU HA H 3.90 0.01 1 332 . 48 GLU CB C 30.7 0.20 1 333 . 48 GLU HB2 H 1.74 0.01 2 334 . 48 GLU HB3 H 1.61 0.01 2 335 . 48 GLU HG2 H 2.31 0.01 2 336 . 49 VAL N N 117.2 0.25 1 337 . 49 VAL H H 7.64 0.01 1 338 . 49 VAL CA C 62.4 0.20 1 339 . 49 VAL HA H 4.59 0.01 1 340 . 49 VAL CB C 36.8 0.20 1 341 . 49 VAL HB H 1.76 0.01 1 342 . 49 VAL HG1 H 1.03 0.01 2 343 . 49 VAL HG2 H 0.81 0.01 2 344 . 50 GLU N N 128.2 0.25 1 345 . 50 GLU H H 9.25 0.01 1 346 . 50 GLU CA C 54.7 0.20 1 347 . 50 GLU HA H 4.99 0.01 1 348 . 50 GLU CB C 34.1 0.20 1 349 . 50 GLU HB2 H 1.80 0.01 2 350 . 50 GLU HB3 H 1.77 0.01 2 351 . 50 GLU HG2 H 1.85 0.01 2 352 . 51 VAL N N 124.2 0.25 1 353 . 51 VAL H H 8.60 0.01 1 354 . 51 VAL CA C 62.4 0.20 1 355 . 51 VAL HA H 3.90 0.01 1 356 . 51 VAL CB C 31.4 0.20 1 357 . 51 VAL HB H 1.93 0.01 1 358 . 51 VAL HG1 H 0.62 0.01 2 359 . 52 VAL N N 128.7 0.25 1 360 . 52 VAL H H 8.95 0.01 1 361 . 52 VAL CA C 65.7 0.20 1 362 . 52 VAL HA H 3.44 0.01 1 363 . 52 VAL CB C 33.7 0.20 1 364 . 52 VAL HB H 0.99 0.01 1 365 . 52 VAL HG1 H 0.46 0.01 2 366 . 52 VAL HG2 H 0.33 0.01 2 367 . 53 GLU N N 108.8 0.25 1 368 . 53 GLU H H 7.15 0.01 1 369 . 53 GLU CA C 55.3 0.20 1 370 . 53 GLU HA H 4.50 0.01 1 371 . 53 GLU CB C 33.9 0.20 1 372 . 53 GLU HB2 H 1.96 0.01 2 373 . 53 GLU HB3 H 1.93 0.01 2 374 . 53 GLU HG2 H 2.25 0.01 2 375 . 54 ILE N N 120.9 0.25 1 376 . 54 ILE H H 8.63 0.01 1 377 . 54 ILE CA C 61.9 0.20 1 378 . 54 ILE HA H 4.52 0.01 1 379 . 54 ILE CB C 39.8 0.20 1 380 . 54 ILE HB H 1.65 0.01 1 381 . 54 ILE HG13 H 0.75 0.01 2 382 . 54 ILE HG12 H 1.44 0.01 2 383 . 54 ILE HD1 H 0.55 0.01 1 384 . 55 ILE N N 127.5 0.25 1 385 . 55 ILE H H 9.30 0.01 1 386 . 55 ILE CA C 60.6 0.20 1 387 . 55 ILE HA H 4.24 0.01 1 388 . 55 ILE CB C 40.6 0.20 1 389 . 55 ILE HB H 1.59 0.01 1 390 . 55 ILE HG13 H 0.74 0.01 2 391 . 55 ILE HG12 H 1.29 0.01 2 392 . 55 ILE HD1 H 0.62 0.01 1 393 . 56 GLN N N 122.9 0.25 1 394 . 56 GLN H H 8.64 0.01 1 395 . 56 GLN CA C 54.6 0.20 1 396 . 56 GLN HA H 4.62 0.01 1 397 . 56 GLN CB C 31.9 0.20 1 398 . 56 GLN HB2 H 2.09 0.01 2 399 . 56 GLN HB3 H 1.88 0.01 2 400 . 56 GLN HG2 H 2.26 0.01 2 401 . 56 GLN HE21 H 6.72 0.01 1 402 . 56 GLN HE22 H 7.46 0.01 1 403 . 57 ALA N N 122.1 0.25 1 404 . 57 ALA H H 7.94 0.01 1 405 . 57 ALA CA C 53.4 0.20 1 406 . 57 ALA HA H 4.29 0.01 1 407 . 57 ALA HB H 0.99 0.01 1 408 . 57 ALA CB C 20.1 0.20 1 409 . 58 THR N N 119.4 0.25 1 410 . 58 THR H H 8.77 0.01 1 411 . 58 THR CA C 64.4 0.20 1 412 . 58 THR HA H 4.26 0.01 1 413 . 58 THR CB C 71.6 0.20 1 414 . 58 THR HB H 3.88 0.01 1 415 . 58 THR HG2 H 1.11 0.01 1 416 . 59 ILE N N 127.0 0.25 1 417 . 59 ILE H H 8.64 0.01 1 418 . 59 ILE CA C 61.6 0.20 1 419 . 59 ILE HA H 3.98 0.01 1 420 . 59 ILE CB C 37.3 0.20 1 421 . 59 ILE HB H 1.82 0.01 1 422 . 59 ILE HG2 H 0.58 0.01 1 423 . 59 ILE HD1 H 0.65 0.01 1 424 . 60 ILE N N 129.0 0.25 1 425 . 60 ILE H H 8.31 0.01 1 426 . 60 ILE CA C 62.9 0.20 1 427 . 60 ILE HA H 3.85 0.01 1 428 . 60 ILE CB C 39.2 0.20 1 429 . 60 ILE HB H 2.08 0.01 1 430 . 60 ILE HG2 H 0.59 0.01 1 431 . 60 ILE HD1 H 0.65 0.01 1 432 . 61 ARG N N 126.3 0.25 1 433 . 61 ARG H H 8.30 0.01 1 434 . 61 ARG CA C 57.7 0.20 1 435 . 61 ARG HA H 4.43 0.01 1 436 . 61 ARG CB C 32.1 0.20 1 437 . 61 ARG HB2 H 1.46 0.01 2 438 . 61 ARG HG2 H 1.84 0.01 2 439 . 62 GLN N N 115.9 0.25 1 440 . 62 GLN H H 8.09 0.01 1 441 . 62 GLN CA C 58.5 0.20 1 442 . 62 GLN HA H 3.85 0.01 1 443 . 62 GLN CB C 29.3 0.20 1 444 . 62 GLN HB2 H 1.94 0.01 2 445 . 62 GLN HB3 H 1.87 0.01 2 446 . 62 GLN HG2 H 2.34 0.01 1 447 . 62 GLN HE21 H 6.81 0.01 2 448 . 62 GLN HE22 H 7.45 0.01 2 449 . 63 ASN N N 115.1 0.25 1 450 . 63 ASN H H 8.89 0.01 1 451 . 63 ASN CA C 55.9 0.20 1 452 . 63 ASN HA H 4.25 0.01 1 453 . 63 ASN CB C 38.0 0.20 1 454 . 63 ASN HB2 H 3.11 0.01 2 455 . 63 ASN HB3 H 3.02 0.01 2 456 . 63 ASN HD21 H 6.91 0.01 2 457 . 63 ASN HD22 H 7.59 0.01 2 458 . 64 GLN N N 115.9 0.25 1 459 . 64 GLN H H 7.91 0.01 1 460 . 64 GLN CA C 55.6 0.20 1 461 . 64 GLN HA H 5.12 0.01 1 462 . 64 GLN CB C 33.6 0.20 1 463 . 64 GLN HB2 H 2.29 0.01 2 464 . 64 GLN HB3 H 2.06 0.01 2 465 . 64 GLN HG2 H 2.17 0.01 2 466 . 64 GLN HG3 H 1.74 0.01 2 467 . 64 GLN HE21 H 7.59 0.01 2 468 . 64 GLN HE22 H 6.38 0.01 2 469 . 65 ALA N N 118.0 0.25 1 470 . 65 ALA H H 8.53 0.01 1 471 . 65 ALA CA C 51.2 0.20 1 472 . 65 ALA HA H 4.72 0.01 1 473 . 65 ALA HB H 1.00 0.01 1 474 . 65 ALA CB C 24.4 0.20 1 475 . 66 LEU N N 122.6 0.25 1 476 . 66 LEU H H 8.76 0.01 1 477 . 66 LEU CA C 56.4 0.20 1 478 . 66 LEU CB C 44.4 0.20 1 479 . 66 LEU HB2 H 1.56 0.01 2 480 . 66 LEU HD1 H 0.66 0.01 2 481 . 66 LEU HD2 H 0.59 0.01 2 482 . 67 ARG N N 116.6 0.25 1 483 . 67 ARG H H 7.65 0.01 1 484 . 67 ARG CA C 56.5 0.20 1 485 . 67 ARG HA H 4.59 0.01 1 486 . 67 ARG CB C 32.6 0.20 1 487 . 67 ARG HB2 H 1.54 0.01 2 488 . 68 LEU N N 126.2 0.25 1 489 . 68 LEU H H 8.31 0.01 1 490 . 68 LEU CA C 53.0 0.20 1 491 . 68 LEU HA H 4.82 0.01 1 492 . 68 LEU CB C 46.0 0.20 1 493 . 68 LEU HB2 H 1.47 0.01 2 494 . 68 LEU HD1 H 0.10 0.01 2 495 . 68 LEU HD2 H -0.34 0.01 2 496 . 69 ARG N N 115.1 0.25 1 497 . 69 ARG H H 8.31 0.01 1 498 . 69 ARG CA C 53.9 0.20 1 499 . 69 ARG HA H 5.27 0.01 1 500 . 69 ARG CB C 36.4 0.20 1 501 . 69 ARG HB2 H 1.66 0.01 2 502 . 69 ARG HB3 H 1.37 0.01 2 503 . 70 ALA N N 127.1 0.25 1 504 . 70 ALA H H 8.63 0.01 1 505 . 70 ALA CA C 52.7 0.20 1 506 . 70 ALA HA H 4.95 0.01 1 507 . 70 ALA HB H 1.65 0.01 1 508 . 70 ALA CB C 19.4 0.20 1 509 . 71 ARG N N 124.1 0.25 1 510 . 71 ARG H H 9.61 0.01 1 511 . 71 ARG CA C 58.6 0.20 1 512 . 71 ARG HA H 4.19 0.01 1 513 . 71 ARG CB C 32.6 0.20 1 514 . 71 ARG HB2 H 1.68 0.01 2 515 . 71 ARG HG2 H 1.95 0.01 2 516 . 71 ARG HG3 H 1.60 0.01 2 517 . 71 ARG HD2 H 3.23 0.01 2 518 . 72 LYS N N 113.0 0.25 1 519 . 72 LYS H H 7.70 0.01 1 520 . 72 LYS CA C 54.8 0.20 1 521 . 72 LYS HA H 4.49 0.01 1 522 . 72 LYS CB C 35.9 0.20 1 523 . 72 LYS HB2 H 1.36 0.01 2 524 . 72 LYS HB3 H 1.15 0.01 2 525 . 72 LYS HG2 H 1.01 0.01 2 526 . 73 GLU N N 118.0 0.25 1 527 . 73 GLU H H 7.62 0.01 1 528 . 73 GLU CA C 58.6 0.20 1 529 . 73 GLU HA H 4.34 0.01 1 530 . 73 GLU CB C 29.4 0.20 1 531 . 73 GLU HB2 H 1.90 0.01 2 532 . 73 GLU HG2 H 2.22 0.01 2 533 . 74 CYS N N 115.8 0.25 1 534 . 74 CYS H H 8.28 0.01 1 535 . 74 CYS CA C 57.3 0.20 1 536 . 74 CYS HA H 4.66 0.01 1 537 . 74 CYS CB C 31.2 0.20 1 538 . 74 CYS HB2 H 3.06 0.01 2 539 . 75 TRP N N 118.1 0.25 1 540 . 75 TRP H H 8.17 0.01 1 541 . 75 TRP CA C 57.5 0.20 1 542 . 75 TRP HA H 4.96 0.01 1 543 . 75 TRP CB C 31.6 0.20 1 544 . 75 TRP HB2 H 3.06 0.01 2 545 . 75 TRP HB3 H 2.79 0.01 2 546 . 75 TRP NE1 N 128.8 0.25 1 547 . 75 TRP HD1 H 6.79 0.01 1 548 . 75 TRP HE3 H 6.94 0.01 1 549 . 75 TRP HE1 H 9.93 0.01 1 550 . 75 TRP HZ3 H 6.83 0.01 1 551 . 75 TRP HZ2 H 7.63 0.01 1 552 . 75 TRP HH2 H 6.68 0.01 1 553 . 76 ASP N N 122.6 0.25 1 554 . 76 ASP H H 8.84 0.01 1 555 . 76 ASP CA C 53.7 0.20 1 556 . 76 ASP HA H 4.59 0.01 1 557 . 76 ASP CB C 42.5 0.20 1 558 . 76 ASP HB2 H 1.90 0.01 2 559 . 77 ARG N N 117.2 0.25 1 560 . 77 ARG H H 8.79 0.01 1 561 . 77 ARG CA C 58.7 0.20 1 562 . 77 ARG HA H 4.13 0.01 1 563 . 77 ARG CB C 30.3 0.20 1 564 . 77 ARG HB2 H 1.89 0.01 2 565 . 77 ARG HG2 H 2.22 0.01 2 566 . 77 ARG HG3 H 2.06 0.01 2 567 . 78 ASP N N 117.4 0.25 1 568 . 78 ASP H H 8.34 0.01 1 569 . 78 ASP CA C 55.0 0.20 1 570 . 78 ASP HA H 4.82 0.01 1 571 . 78 ASP CB C 42.5 0.20 1 572 . 78 ASP HB2 H 2.81 0.01 2 573 . 78 ASP HB3 H 2.64 0.01 2 574 . 79 GLY N N 108.3 0.25 1 575 . 79 GLY H H 8.39 0.01 1 576 . 79 GLY CA C 46.5 0.20 1 577 . 79 GLY HA2 H 4.11 0.01 2 578 . 79 GLY HA3 H 3.62 0.01 2 579 . 80 LYS N N 122.2 0.25 1 580 . 80 LYS H H 8.44 0.01 1 581 . 80 LYS CA C 56.1 0.20 1 582 . 80 LYS HA H 4.29 0.01 1 583 . 80 LYS CB C 32.8 0.20 1 584 . 80 LYS HB2 H 1.70 0.01 2 585 . 80 LYS HB3 H 1.56 0.01 2 586 . 80 LYS HG2 H 1.22 0.01 2 587 . 81 GLU N N 124.1 0.25 1 588 . 81 GLU H H 8.39 0.01 1 589 . 81 GLU CA C 57.6 0.20 1 590 . 81 GLU HA H 3.60 0.01 1 591 . 81 GLU CB C 30.4 0.20 1 592 . 81 GLU HB2 H 1.51 0.01 2 593 . 81 GLU HG2 H 1.29 0.01 2 594 . 82 ARG N N 122.7 0.25 1 595 . 82 ARG H H 8.55 0.01 1 596 . 82 ARG CA C 52.9 0.20 1 597 . 82 ARG HA H 4.59 0.01 1 598 . 82 ARG CB C 33.8 0.20 1 599 . 82 ARG HB2 H 1.66 0.01 2 600 . 83 VAL N N 114.8 0.25 1 601 . 83 VAL H H 8.25 0.01 1 602 . 83 VAL CA C 60.3 0.20 1 603 . 83 VAL HA H 4.42 0.01 1 604 . 83 VAL CB C 34.6 0.20 1 605 . 83 VAL HB H 2.22 0.01 1 606 . 83 VAL HG1 H 0.84 0.01 2 607 . 84 THR N N 115.2 0.25 1 608 . 84 THR H H 7.93 0.01 1 609 . 84 THR CA C 67.1 0.20 1 610 . 84 THR HA H 3.08 0.01 1 611 . 84 THR CB C 69.3 0.20 1 612 . 84 THR HB H 3.83 0.01 1 613 . 84 THR HG2 H 1.02 0.01 1 614 . 85 GLY N N 114.5 0.25 1 615 . 85 GLY H H 9.05 0.01 1 616 . 85 GLY CA C 46.1 0.20 1 617 . 85 GLY HA3 H 4.25 0.01 2 618 . 86 GLU N N 123.7 0.25 1 619 . 86 GLU H H 8.57 0.01 1 620 . 86 GLU CA C 58.5 0.20 1 621 . 86 GLU HA H 4.13 0.01 1 622 . 86 GLU CB C 31.5 0.20 1 623 . 86 GLU HB2 H 2.23 0.01 2 624 . 86 GLU HB3 H 2.11 0.01 2 625 . 86 GLU HG2 H 2.48 0.01 2 626 . 86 GLU HG3 H 2.36 0.01 2 627 . 87 GLU N N 121.0 0.25 1 628 . 87 GLU H H 8.29 0.01 1 629 . 87 GLU CA C 55.1 0.20 1 630 . 87 GLU HA H 5.90 0.01 1 631 . 87 GLU CB C 34.0 0.20 1 632 . 87 GLU HB2 H 1.79 0.01 2 633 . 88 TRP N N 121.4 0.25 1 634 . 88 TRP H H 8.63 0.01 1 635 . 88 TRP CA C 55.5 0.20 1 636 . 88 TRP HA H 4.85 0.01 1 637 . 88 TRP CB C 32.3 0.20 1 638 . 88 TRP HB2 H 3.38 0.01 2 639 . 88 TRP HB3 H 3.20 0.01 2 640 . 88 TRP NE1 N 128.2 0.25 1 641 . 88 TRP HD1 H 7.04 0.01 1 642 . 88 TRP HE3 H 7.42 0.01 1 643 . 88 TRP HE1 H 10.09 0.01 1 644 . 88 TRP HZ3 H 7.06 0.01 1 645 . 88 TRP HZ2 H 7.35 0.01 1 646 . 88 TRP HH2 H 7.10 0.01 1 647 . 89 LEU N N 115.4 0.25 1 648 . 89 LEU H H 8.06 0.01 1 649 . 89 LEU CA C 53.7 0.20 1 650 . 89 LEU HA H 5.27 0.01 1 651 . 89 LEU CB C 45.6 0.20 1 652 . 89 LEU HB2 H 1.61 0.01 2 653 . 89 LEU HB3 H 1.51 0.01 2 654 . 89 LEU HG H 0.97 0.01 1 655 . 89 LEU HD1 H 0.69 0.01 2 656 . 89 LEU HD2 H 0.56 0.01 2 657 . 90 VAL N N 122.2 0.25 1 658 . 90 VAL H H 9.12 0.01 1 659 . 90 VAL CA C 62.8 0.20 1 660 . 90 VAL HA H 4.25 0.01 1 661 . 90 VAL CB C 34.6 0.20 1 662 . 90 VAL HB H 1.54 0.01 1 663 . 90 VAL HG1 H 0.56 0.01 2 664 . 91 THR N N 113.0 0.25 1 665 . 91 THR H H 8.63 0.01 1 666 . 91 THR CA C 61.2 0.20 1 667 . 91 THR HA H 4.56 0.01 1 668 . 91 THR CB C 70.1 0.20 1 669 . 91 THR HG2 H 0.68 0.01 1 670 . 92 THR N N 118.1 0.25 1 671 . 92 THR H H 7.01 0.01 1 672 . 92 THR CA C 63.1 0.20 1 673 . 92 THR HA H 4.00 0.01 1 674 . 92 THR CB C 70.3 0.20 1 675 . 92 THR HB H 3.85 0.01 1 676 . 92 THR HG2 H 0.69 0.01 1 677 . 93 VAL N N 125.3 0.25 1 678 . 93 VAL H H 8.08 0.01 1 679 . 93 VAL CA C 64.1 0.20 1 680 . 93 VAL HA H 3.57 0.01 1 681 . 93 VAL CB C 32.9 0.20 1 682 . 93 VAL HB H 1.86 0.01 1 683 . 93 VAL HG1 H 0.89 0.01 2 684 . 93 VAL HG2 H 1.18 0.01 2 685 . 94 GLY N N 113.1 0.25 1 686 . 94 GLY H H 8.76 0.01 1 687 . 94 GLY CA C 44.2 0.20 1 688 . 94 GLY HA3 H 4.50 0.01 2 689 . 95 ALA N N 122.9 0.25 1 690 . 95 ALA H H 8.47 0.01 1 691 . 95 ALA CA C 53.1 0.20 1 692 . 95 ALA HA H 4.35 0.01 1 693 . 95 ALA HB H 1.03 0.01 1 694 . 95 ALA CB C 19.2 0.20 1 695 . 96 TYR N N 126.7 0.25 1 696 . 96 TYR H H 9.27 0.01 1 697 . 96 TYR CA C 59.4 0.20 1 698 . 96 TYR HA H 4.23 0.01 1 699 . 96 TYR CB C 40.9 0.20 1 700 . 96 TYR HB2 H 2.82 0.01 2 701 . 96 TYR HE1 H 6.55 0.01 3 702 . 96 TYR HD1 H 6.76 0.01 3 703 . 97 LEU N N 131.8 0.25 1 704 . 97 LEU HA H 4.57 0.01 1 705 . 97 LEU HB2 H 1.46 0.01 2 706 . 97 LEU HB3 H 1.01 0.01 2 707 . 97 LEU HD1 H 0.50 0.01 2 708 . 98 PRO CA C 63.5 0.20 1 709 . 98 PRO HA H 4.33 0.01 1 710 . 98 PRO CB C 32.5 0.20 1 711 . 98 PRO HB2 H 2.38 0.01 2 712 . 98 PRO HB3 H 2.34 0.01 2 713 . 98 PRO HG2 H 2.19 0.01 2 714 . 98 PRO HG3 H 2.04 0.01 2 715 . 99 ALA N N 120.4 0.25 1 716 . 99 ALA H H 7.78 0.01 1 717 . 99 ALA CA C 51.5 0.20 1 718 . 99 ALA HA H 4.11 0.01 1 719 . 99 ALA HB H 1.29 0.01 1 720 . 99 ALA CB C 21.0 0.20 1 721 . 100 VAL N N 116.3 0.25 1 722 . 100 VAL H H 8.22 0.01 1 723 . 100 VAL CA C 65.9 0.20 1 724 . 100 VAL HA H 3.28 0.01 1 725 . 100 VAL CB C 37.9 0.20 1 726 . 100 VAL HB H 1.50 0.01 1 727 . 100 VAL HG1 H 0.66 0.01 2 728 . 101 PHE N N 115.2 0.25 1 729 . 101 PHE H H 7.89 0.01 1 730 . 101 PHE CA C 57.1 0.20 1 731 . 101 PHE HA H 4.95 0.01 1 732 . 101 PHE CB C 38.6 0.20 1 733 . 101 PHE HB2 H 3.37 0.01 2 734 . 101 PHE HB3 H 3.17 0.01 2 735 . 101 PHE HZ H 7.45 0.01 1 736 . 101 PHE HD1 H 7.17 0.01 3 737 . 101 PHE HE1 H 7.39 0.01 3 738 . 102 GLU N N 118.8 0.25 1 739 . 102 GLU H H 7.57 0.01 1 740 . 102 GLU CA C 56.4 0.20 1 741 . 102 GLU HA H 4.56 0.01 1 742 . 102 GLU CB C 31.8 0.20 1 743 . 102 GLU HB2 H 2.35 0.01 2 744 . 102 GLU HG2 H 2.44 0.01 2 745 . 103 GLU N N 123.6 0.25 1 746 . 103 GLU H H 9.20 0.01 1 747 . 103 GLU CA C 55.3 0.20 1 748 . 103 GLU HA H 4.45 0.01 1 749 . 103 GLU CB C 32.8 0.20 1 750 . 103 GLU HB2 H 1.66 0.01 2 751 . 103 GLU HG2 H 1.98 0.01 2 752 . 104 VAL N N 124.9 0.25 1 753 . 104 VAL H H 8.61 0.01 1 754 . 104 VAL CA C 64.3 0.20 1 755 . 104 VAL HA H 3.75 0.01 1 756 . 104 VAL CB C 32.9 0.20 1 757 . 104 VAL HB H 1.94 0.01 1 758 . 104 VAL HG1 H 0.91 0.01 2 759 . 104 VAL HG2 H 0.78 0.01 2 760 . 105 LEU N N 128.1 0.25 1 761 . 105 LEU H H 8.76 0.01 1 762 . 105 LEU CA C 55.8 0.20 1 763 . 105 LEU HA H 4.43 0.01 1 764 . 105 LEU CB C 41.9 0.20 1 765 . 105 LEU HB2 H 1.40 0.01 2 766 . 105 LEU HB3 H 1.28 0.01 2 767 . 105 LEU HD1 H 0.52 0.01 2 768 . 106 ASP N N 113.9 0.25 1 769 . 106 ASP H H 7.61 0.01 1 770 . 106 ASP CA C 54.1 0.20 1 771 . 106 ASP HA H 4.51 0.01 1 772 . 106 ASP CB C 43.6 0.20 1 773 . 106 ASP HB2 H 2.47 0.01 2 774 . 106 ASP HB3 H 2.43 0.01 2 775 . 107 LEU N N 121.5 0.25 1 776 . 107 LEU H H 8.07 0.01 1 777 . 107 LEU CA C 55.1 0.20 1 778 . 107 LEU HA H 4.91 0.01 1 779 . 107 LEU CB C 44.6 0.20 1 780 . 107 LEU HB2 H 1.53 0.01 2 781 . 107 LEU HB3 H 1.31 0.01 2 782 . 107 LEU HD1 H 0.73 0.01 2 783 . 107 LEU HD2 H 0.67 0.01 2 784 . 108 VAL N N 121.1 0.25 1 785 . 108 VAL H H 9.13 0.01 1 786 . 108 VAL CA C 60.7 0.20 1 787 . 108 VAL HA H 4.39 0.01 1 788 . 108 VAL CB C 35.5 0.20 1 789 . 108 VAL HB H 2.04 0.01 1 790 . 108 VAL HG1 H 0.77 0.01 2 791 . 108 VAL HG2 H 0.68 0.01 2 792 . 109 ASP N N 121.5 0.25 1 793 . 109 ASP H H 8.24 0.01 1 794 . 109 ASP CA C 55.4 0.20 1 795 . 109 ASP HA H 4.71 0.01 1 796 . 109 ASP CB C 42.4 0.20 1 797 . 109 ASP HB2 H 2.61 0.01 2 798 . 109 ASP HB3 H 2.44 0.01 2 799 . 110 ALA N N 123.7 0.25 1 800 . 110 ALA H H 8.09 0.01 1 801 . 110 ALA CA C 53.0 0.20 1 802 . 110 ALA HA H 4.14 0.01 1 803 . 110 ALA HB H 1.08 0.01 1 804 . 110 ALA CB C 19.9 0.20 1 805 . 111 VAL N N 118.9 0.25 1 806 . 111 VAL CA C 63.1 0.20 1 807 . 111 VAL HA H 3.92 0.01 1 808 . 111 VAL CB C 33.4 0.20 1 809 . 111 VAL HB H 1.88 0.01 1 810 . 111 VAL HG1 H 0.80 0.01 2 811 . 112 ILE N N 124.5 0.25 1 812 . 112 ILE H H 8.10 0.01 1 813 . 112 ILE CA C 61.5 0.20 1 814 . 112 ILE HA H 4.09 0.01 1 815 . 112 ILE CB C 39.2 0.20 1 816 . 112 ILE HB H 1.78 0.01 1 817 . 112 ILE HG2 H 0.78 0.01 1 818 . 113 LEU N N 131.9 0.25 1 819 . 113 LEU H H 7.83 0.01 1 820 . 113 LEU HA H 4.12 0.01 1 821 . 113 LEU HB2 H 1.49 0.01 2 822 . 113 LEU HD1 H 0.82 0.01 2 stop_ save_