data_15070 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase-G135A ; _BMRB_accession_number 15070 _BMRB_flat_file_name bmr15070.str _Entry_type original _Submission_date 2006-12-07 _Accession_date 2006-12-07 _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 Hom Kellie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 191 "13C chemical shifts" 571 "15N chemical shifts" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-31 update BMRB 'complete entry citation; add related entry' 2007-06-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15071 'apo Corynebacterium diptheriae heme oxygenase' 15073 'complex form, Corynebacterium diptheriae heme oxygenase' stop_ save_ ############################# # Citation for this entry # ############################# save_citation-1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheria' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636825 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hom Kellie . . 2 Furci Lena M. . 3 Deshmukh Rahul . . 4 Wilks Angela . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 55 _Page_last 56 _Year 2007 _Details . loop_ _Keyword 'Corynebacterium diptheriae' 'heme oxygenase' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'heme oxygenase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'heme oxygenase' $heme_oxygenase stop_ _System_molecular_weight 24152 _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_heme_oxygenase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common heme_oxygenase _Molecular_mass 24152 _Mol_thiol_state 'not present' loop_ _Biological_function 'heme degradation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 215 _Mol_residue_sequence ; MTTATAGLAVELKQSTAQAH EKAEHSTFMSDLLKGRLGVA EFTRLQEQAWLFYTALEQAV DAVRASGFAESLLDPALNRA EVLARDLDKLNGSSEWRSRI TASPAVIDYVNRLEEIRDNV DGPALVAHHYVRYLADLSGG QVIARMMQRHYGVDPEALGF YHFEGIAKLKVYKDEYREKL NNLELSDEQREHLLKEATDA FVFNHQVFADLGKGL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 THR 4 ALA 5 THR 6 ALA 7 GLY 8 LEU 9 ALA 10 VAL 11 GLU 12 LEU 13 LYS 14 GLN 15 SER 16 THR 17 ALA 18 GLN 19 ALA 20 HIS 21 GLU 22 LYS 23 ALA 24 GLU 25 HIS 26 SER 27 THR 28 PHE 29 MET 30 SER 31 ASP 32 LEU 33 LEU 34 LYS 35 GLY 36 ARG 37 LEU 38 GLY 39 VAL 40 ALA 41 GLU 42 PHE 43 THR 44 ARG 45 LEU 46 GLN 47 GLU 48 GLN 49 ALA 50 TRP 51 LEU 52 PHE 53 TYR 54 THR 55 ALA 56 LEU 57 GLU 58 GLN 59 ALA 60 VAL 61 ASP 62 ALA 63 VAL 64 ARG 65 ALA 66 SER 67 GLY 68 PHE 69 ALA 70 GLU 71 SER 72 LEU 73 LEU 74 ASP 75 PRO 76 ALA 77 LEU 78 ASN 79 ARG 80 ALA 81 GLU 82 VAL 83 LEU 84 ALA 85 ARG 86 ASP 87 LEU 88 ASP 89 LYS 90 LEU 91 ASN 92 GLY 93 SER 94 SER 95 GLU 96 TRP 97 ARG 98 SER 99 ARG 100 ILE 101 THR 102 ALA 103 SER 104 PRO 105 ALA 106 VAL 107 ILE 108 ASP 109 TYR 110 VAL 111 ASN 112 ARG 113 LEU 114 GLU 115 GLU 116 ILE 117 ARG 118 ASP 119 ASN 120 VAL 121 ASP 122 GLY 123 PRO 124 ALA 125 LEU 126 VAL 127 ALA 128 HIS 129 HIS 130 TYR 131 VAL 132 ARG 133 TYR 134 LEU 135 ALA 136 ASP 137 LEU 138 SER 139 GLY 140 GLY 141 GLN 142 VAL 143 ILE 144 ALA 145 ARG 146 MET 147 MET 148 GLN 149 ARG 150 HIS 151 TYR 152 GLY 153 VAL 154 ASP 155 PRO 156 GLU 157 ALA 158 LEU 159 GLY 160 PHE 161 TYR 162 HIS 163 PHE 164 GLU 165 GLY 166 ILE 167 ALA 168 LYS 169 LEU 170 LYS 171 VAL 172 TYR 173 LYS 174 ASP 175 GLU 176 TYR 177 ARG 178 GLU 179 LYS 180 LEU 181 ASN 182 ASN 183 LEU 184 GLU 185 LEU 186 SER 187 ASP 188 GLU 189 GLN 190 ARG 191 GLU 192 HIS 193 LEU 194 LEU 195 LYS 196 GLU 197 ALA 198 THR 199 ASP 200 ALA 201 PHE 202 VAL 203 PHE 204 ASN 205 HIS 206 GLN 207 VAL 208 PHE 209 ALA 210 ASP 211 LEU 212 GLY 213 LYS 214 GLY 215 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 15071 cdHO 100.00 215 99.53 99.53 9.57e-154 BMRB 15073 heme_oxygenase 100.00 215 99.53 99.53 9.57e-154 PDB 1IW0 "Crystal Structure Of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed With Heme In The Ferric State" 100.00 215 99.53 99.53 9.57e-154 PDB 1IW1 "Crystal Structure Of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed With Heme In The Ferrous State" 100.00 215 99.53 99.53 9.57e-154 PDB 1V8X "Crystal Structure Of The Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae" 100.00 215 99.53 99.53 9.57e-154 PDB 1WNV "D136a Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)" 100.00 215 99.07 99.07 1.43e-152 PDB 1WNW "D136n Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (hmuo)" 100.00 215 99.07 99.53 3.72e-153 PDB 1WNX "D136e Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)" 100.00 215 99.07 99.53 3.92e-153 PDB 1WZD "Crystal Structure Of An Artificial Metalloprotein: Fe(10-Ch2ch2cooh- Salophen)WILD TYPE HEME OXYGENASE" 100.00 215 99.53 99.53 9.57e-154 PDB 1WZF "Crystal Structure Of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)WILD TYPE HEME OXYGENASE" 100.00 215 99.53 99.53 9.57e-154 PDB 1WZG "Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)WILD Type Heme Oxygenase" 100.00 215 99.53 99.53 9.57e-154 PDB 2Z68 "Crystal Structure Of An Artificial Metalloprotein: Cr[n- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]WILD Type Heme Oxygen" 100.00 215 99.53 99.53 9.57e-154 PDB 3I8R "Crystal Structure Of The Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) In Complex With Heme Binding Ditiothreit" 100.00 215 99.53 99.53 9.57e-154 PDB 3MOO "Crystal Structure Of The Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, In Complex With Azide-Bound Verdoheme" 100.00 215 99.53 99.53 9.57e-154 PDB 4GOH "Structure Of The Substrate-free Hmuo, Ho From Corynebacterium Diphtheriae" 100.00 215 99.53 99.53 9.57e-154 PDB 4GPC "Structure Of The Biliverdin-hmuo, Heme Oxygenase From Corynebacterium Diphtheriae" 100.00 215 99.53 99.53 9.57e-154 PDB 4GPF "Structure Of The Fe3+-biliverdin-hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (data Set Iii)" 100.00 215 99.53 99.53 9.57e-154 PDB 4GPH "Structure Of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, In Complex With The Putative Reaction Intermediates Between" 100.00 215 99.53 99.53 9.57e-154 DBJ BAA76407 "Heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 99.53 99.53 9.57e-154 EMBL CAE50198 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.21 98.14 2.13e-149 EMBL CKH06070 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 99.53 99.53 9.57e-154 GB AAC44832 "HmuO [Corynebacterium diphtheriae]" 100.00 215 99.53 99.53 9.57e-154 GB AEX42338 "heme oxygenase [Corynebacterium diphtheriae 31A]" 100.00 215 98.14 98.14 5.39e-151 GB AEX44660 "heme oxygenase [Corynebacterium diphtheriae 241]" 100.00 215 97.67 98.60 1.72e-150 GB AEX46855 "heme oxygenase [Corynebacterium diphtheriae INCA 402]" 100.00 215 98.14 99.07 5.42e-152 GB AEX67845 "heme oxygenase [Corynebacterium diphtheriae C7 (beta)]" 100.00 215 99.53 99.53 9.57e-154 REF WP_003852259 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.67 98.60 2.21e-150 REF WP_010935240 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.21 98.14 2.13e-149 REF WP_014302152 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.67 98.60 1.72e-150 REF WP_014303664 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 98.14 99.07 5.42e-152 REF WP_014307115 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 98.60 98.60 9.57e-152 SP P71119 "RecName: Full=Heme oxygenase" 100.00 215 97.21 98.14 2.13e-149 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $heme_oxygenase 'Corynebacterium diphtheria' 1717 Bacteria . Corynebacterium diphtheriae 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 $heme_oxygenase 'recombinant technology' . Escherichia coli . pET21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $heme_oxygenase . mM 1 2 '[U-13C; U-15N; U-2H]' H2O 95 % . . 'natural abundance' D2O 5 % . . 'natural abundance' 'potassium phosphate' 50 mM . . 'natural abundance' 'potassium chloride' 100 mM . . 'natural abundance' DSS 0.5 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.11 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation-1 $citation-1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citation-1 $citation-1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation-1 $citation-1 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D 1H-15N NOESY' '3D HN(CO)CA' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'heme oxygenase' _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 4 4 ALA H H 8.535 0.02 1 2 4 4 ALA C C 176.6 0.2 1 3 4 4 ALA CA C 49.76 0.2 1 4 4 4 ALA CB C 16.29 0.2 1 5 4 4 ALA N N 127.2 0.2 1 6 5 5 THR H H 8.215 0.02 1 7 5 5 THR C C 172.9 0.2 1 8 5 5 THR CA C 58.75 0.2 1 9 5 5 THR CB C 66.82 0.2 1 10 5 5 THR N N 113.3 0.2 1 11 6 6 ALA H H 8.293 0.02 1 12 6 6 ALA C C 176.2 0.2 1 13 6 6 ALA CA C 49.23 0.2 1 14 6 6 ALA CB C 17.08 0.2 1 15 6 6 ALA N N 126.0 0.2 1 16 7 7 GLY H H 8.357 0.02 1 17 7 7 GLY C C 173.3 0.2 1 18 7 7 GLY CA C 41.78 0.2 1 19 7 7 GLY N N 107.9 0.2 1 20 8 8 LEU H H 8.583 0.02 1 21 8 8 LEU C C 176.7 0.2 1 22 8 8 LEU CA C 54.98 0.2 1 23 8 8 LEU CB C 38.73 0.2 1 24 8 8 LEU N N 124.3 0.2 1 25 9 9 ALA H H 9.069 0.02 1 26 9 9 ALA C C 179.5 0.2 1 27 9 9 ALA CA C 53.04 0.2 1 28 9 9 ALA CB C 15.28 0.2 1 29 9 9 ALA N N 117.4 0.2 1 30 10 10 VAL H H 7.640 0.02 1 31 10 10 VAL C C 176.9 0.2 1 32 10 10 VAL CA C 62.80 0.2 1 33 10 10 VAL CB C 28.73 0.2 1 34 10 10 VAL N N 118.9 0.2 1 35 11 11 GLU H H 8.045 0.02 1 36 11 11 GLU C C 178.9 0.2 1 37 11 11 GLU CA C 56.62 0.2 1 38 11 11 GLU CB C 26.62 0.2 1 39 11 11 GLU N N 121.4 0.2 1 40 12 12 LEU H H 8.946 0.02 1 41 12 12 LEU C C 177.9 0.2 1 42 12 12 LEU CA C 55.06 0.2 1 43 12 12 LEU CB C 38.88 0.2 1 44 12 12 LEU N N 120.6 0.2 1 45 13 13 LYS H H 7.490 0.02 1 46 13 13 LYS C C 177.5 0.2 1 47 13 13 LYS CA C 56.62 0.2 1 48 13 13 LYS CB C 29.15 0.2 1 49 13 13 LYS N N 121.0 0.2 1 50 14 14 GLN H H 8.251 0.02 1 51 14 14 GLN C C 178.1 0.2 1 52 14 14 GLN CA C 55.45 0.2 1 53 14 14 GLN N N 116.9 0.2 1 54 15 15 SER H H 8.622 0.02 1 55 15 15 SER C C 175.3 0.2 1 56 15 15 SER CA C 58.82 0.2 1 57 15 15 SER CB C 60.46 0.2 1 58 15 15 SER N N 114.9 0.2 1 59 16 16 THR H H 7.541 0.02 1 60 16 16 THR C C 174.0 0.2 1 61 16 16 THR CA C 59.76 0.2 1 62 16 16 THR CB C 66.78 0.2 1 63 16 16 THR N N 109.1 0.2 1 64 17 17 ALA H H 7.407 0.02 1 65 17 17 ALA C C 178.9 0.2 1 66 17 17 ALA CA C 52.89 0.2 1 67 17 17 ALA CB C 15.59 0.2 1 68 17 17 ALA N N 124.9 0.2 1 69 18 18 GLN H H 8.375 0.02 1 70 18 18 GLN C C 177.1 0.2 1 71 18 18 GLN CA C 55.58 0.2 1 72 18 18 GLN CB C 25.10 0.2 1 73 18 18 GLN N N 116.9 0.2 1 74 19 19 ALA H H 8.021 0.02 1 75 19 19 ALA C C 178.5 0.2 1 76 19 19 ALA CA C 51.61 0.2 1 77 19 19 ALA CB C 16.00 0.2 1 78 19 19 ALA N N 122.7 0.2 1 79 20 20 HIS H H 8.364 0.02 1 80 20 20 HIS C C 176.9 0.2 1 81 20 20 HIS CA C 55.70 0.2 1 82 20 20 HIS CB C 26.35 0.2 1 83 20 20 HIS N N 118.1 0.2 1 84 21 21 GLU H H 7.664 0.02 1 85 21 21 GLU CA C 54.82 0.2 1 86 21 21 GLU CB C 29.40 0.2 1 87 21 21 GLU N N 117.5 0.2 1 88 22 22 LYS C C 176.9 0.2 1 89 22 22 LYS CA C 54.76 0.2 1 90 22 22 LYS CB C 29.60 0.2 1 91 23 23 ALA H H 7.663 0.02 1 92 23 23 ALA C C 177.3 0.2 1 93 23 23 ALA CA C 51.16 0.2 1 94 23 23 ALA CB C 16.16 0.2 1 95 23 23 ALA N N 121.0 0.2 1 96 24 24 GLU H H 8.305 0.02 1 97 24 24 GLU C C 175.7 0.2 1 98 24 24 GLU CA C 54.56 0.2 1 99 24 24 GLU CB C 26.89 0.2 1 100 24 24 GLU N N 118.5 0.2 1 101 25 25 HIS H H 8.053 0.02 1 102 25 25 HIS C C 173.5 0.2 1 103 25 25 HIS CA C 52.39 0.2 1 104 25 25 HIS CB C 26.39 0.2 1 105 25 25 HIS N N 117.6 0.2 1 106 26 26 SER H H 7.941 0.02 1 107 26 26 SER CA C 55.36 0.2 1 108 26 26 SER CB C 61.93 0.2 1 109 26 26 SER N N 116.9 0.2 1 110 27 27 THR C C 174.0 0.2 1 111 27 27 THR CA C 62.11 0.2 1 112 27 27 THR CB C 60.23 0.2 1 113 28 28 PHE H H 8.399 0.02 1 114 28 28 PHE C C 174.9 0.2 1 115 28 28 PHE CA C 59.02 0.2 1 116 28 28 PHE CB C 37.51 0.2 1 117 28 28 PHE N N 120.4 0.2 1 118 29 29 MET H H 7.570 0.02 1 119 29 29 MET C C 177.1 0.2 1 120 29 29 MET CA C 53.00 0.2 1 121 29 29 MET CB C 26.57 0.2 1 122 30 30 SER H H 8.051 0.02 1 123 30 30 SER C C 175.5 0.2 1 124 30 30 SER CA C 58.26 0.2 1 125 30 30 SER CB C 59.88 0.2 1 126 30 30 SER N N 114.2 0.2 1 127 31 31 ASP H H 8.587 0.02 1 128 31 31 ASP CA C 54.44 0.2 1 129 31 31 ASP CB C 36.14 0.2 1 130 31 31 ASP N N 120.0 0.2 1 131 32 32 LEU C C 176.6 0.2 1 132 32 32 LEU CA C 54.32 0.2 1 133 33 33 LEU H H 7.973 0.02 1 134 33 33 LEU C C 176.0 0.2 1 135 33 33 LEU CA C 54.57 0.2 1 136 33 33 LEU CB C 38.02 0.2 1 137 33 33 LEU N N 120.1 0.2 1 138 34 34 LYS H H 7.603 0.02 1 139 34 34 LYS C C 175.8 0.2 1 140 34 34 LYS CA C 52.86 0.2 1 141 34 34 LYS CB C 29.69 0.2 1 142 34 34 LYS N N 114.3 0.2 1 143 35 35 GLY H H 7.098 0.02 1 144 35 35 GLY C C 173.6 0.2 1 145 35 35 GLY CA C 42.63 0.2 1 146 35 35 GLY N N 106.2 0.2 1 147 36 36 ARG H H 7.963 0.02 1 148 36 36 ARG C C 174.9 0.2 1 149 36 36 ARG CA C 53.36 0.2 1 150 36 36 ARG CB C 27.86 0.2 1 151 36 36 ARG N N 115.9 0.2 1 152 37 37 LEU H H 7.413 0.02 1 153 37 37 LEU C C 172.3 0.2 1 154 37 37 LEU CA C 49.28 0.2 1 155 37 37 LEU CB C 37.06 0.2 1 156 37 37 LEU N N 118.7 0.2 1 157 38 38 GLY H H 6.975 0.02 1 158 38 38 GLY C C 170.8 0.2 1 159 38 38 GLY CA C 41.81 0.2 1 160 38 38 GLY N N 109.2 0.2 1 161 39 39 VAL H H 8.537 0.02 1 162 39 39 VAL C C 177.1 0.2 1 163 39 39 VAL CA C 62.43 0.2 1 164 39 39 VAL CB C 28.79 0.2 1 165 39 39 VAL N N 118.4 0.2 1 166 40 40 ALA H H 9.007 0.02 1 167 40 40 ALA C C 178.5 0.2 1 168 40 40 ALA CA C 52.72 0.2 1 169 40 40 ALA CB C 14.74 0.2 1 170 40 40 ALA N N 126.7 0.2 1 171 41 41 GLU H H 8.589 0.02 1 172 41 41 GLU C C 177.2 0.2 1 173 41 41 GLU CA C 56.72 0.2 1 174 41 41 GLU CB C 25.03 0.2 1 175 41 41 GLU N N 118.1 0.2 1 176 42 42 PHE H H 7.524 0.02 1 177 42 42 PHE C C 174.6 0.2 1 178 42 42 PHE CA C 57.56 0.2 1 179 42 42 PHE CB C 37.83 0.2 1 180 42 42 PHE N N 118.1 0.2 1 181 43 43 THR H H 8.558 0.02 1 182 43 43 THR CA C 64.31 0.2 1 183 43 43 THR CB C 68.41 0.2 1 184 43 43 THR N N 115.3 0.2 1 185 44 44 ARG C C 178.1 0.2 1 186 44 44 ARG CA C 56.10 0.2 1 187 45 45 LEU H H 7.682 0.02 1 188 45 45 LEU C C 175.8 0.2 1 189 45 45 LEU CA C 55.72 0.2 1 190 45 45 LEU CB C 37.49 0.2 1 191 45 45 LEU N N 120.0 0.2 1 192 46 46 GLN H H 7.676 0.02 1 193 46 46 GLN C C 177.4 0.2 1 194 46 46 GLN CA C 53.63 0.2 1 195 46 46 GLN CB C 25.20 0.2 1 196 46 46 GLN N N 116.6 0.2 1 197 47 47 GLU H H 8.301 0.02 1 198 47 47 GLU C C 177.2 0.2 1 199 47 47 GLU CA C 56.51 0.2 1 200 47 47 GLU CB C 26.81 0.2 1 201 47 47 GLU N N 120.2 0.2 1 202 48 48 GLN H H 7.499 0.02 1 203 48 48 GLN C C 177.1 0.2 1 204 48 48 GLN CA C 55.02 0.2 1 205 48 48 GLN CB C 24.50 0.2 1 206 48 48 GLN N N 114.4 0.2 1 207 49 49 ALA H H 8.554 0.02 1 208 49 49 ALA C C 177.9 0.2 1 209 49 49 ALA CA C 50.39 0.2 1 210 49 49 ALA CB C 13.43 0.2 1 211 49 49 ALA N N 119.6 0.2 1 212 50 50 TRP H H 8.669 0.02 1 213 50 50 TRP C C 178.1 0.2 1 214 50 50 TRP CA C 60.76 0.2 1 215 50 50 TRP CB C 24.51 0.2 1 216 50 50 TRP N N 121.5 0.2 1 217 51 51 LEU H H 7.514 0.02 1 218 51 51 LEU C C 179.3 0.2 1 219 51 51 LEU CA C 55.10 0.2 1 220 51 51 LEU CB C 38.55 0.2 1 221 51 51 LEU N N 119.0 0.2 1 222 52 52 PHE H H 7.846 0.02 1 223 52 52 PHE C C 176.8 0.2 1 224 52 52 PHE CA C 56.28 0.2 1 225 52 52 PHE CB C 35.68 0.2 1 226 52 52 PHE N N 114.7 0.2 1 227 53 53 TYR H H 9.892 0.02 1 228 53 53 TYR C C 177.5 0.2 1 229 53 53 TYR CA C 61.81 0.2 1 230 53 53 TYR CB C 33.26 0.2 1 231 53 53 TYR N N 124.2 0.2 1 232 54 54 THR H H 7.677 0.02 1 233 54 54 THR C C 175.3 0.2 1 234 54 54 THR CA C 64.83 0.2 1 235 54 54 THR N N 115.9 0.2 1 236 55 55 ALA H H 6.746 0.02 1 237 55 55 ALA C C 178.5 0.2 1 238 55 55 ALA CA C 51.91 0.2 1 239 55 55 ALA CB C 16.88 0.2 1 240 55 55 ALA N N 122.0 0.2 1 241 56 56 LEU H H 8.759 0.02 1 242 56 56 LEU C C 177.3 0.2 1 243 56 56 LEU CA C 55.08 0.2 1 244 56 56 LEU CB C 39.03 0.2 1 245 56 56 LEU N N 120.5 0.2 1 246 57 57 GLU H H 8.634 0.02 1 247 57 57 GLU C C 177.5 0.2 1 248 57 57 GLU CA C 57.25 0.2 1 249 57 57 GLU CB C 24.33 0.2 1 250 57 57 GLU N N 118.0 0.2 1 251 58 58 GLN CA C 56.00 0.2 1 252 58 58 GLN H H 7.607 0.02 1 253 58 58 GLN C C 179.0 0.2 1 254 58 58 GLN CB C 25.42 0.2 1 255 58 58 GLN N N 119.2 0.2 1 256 59 59 ALA H H 7.733 0.02 1 257 59 59 ALA C C 177.6 0.2 1 258 59 59 ALA CA C 53.04 0.2 1 259 59 59 ALA CB C 14.47 0.2 1 260 59 59 ALA N N 123.7 0.2 1 261 60 60 VAL H H 9.419 0.02 1 262 60 60 VAL C C 176.7 0.2 1 263 60 60 VAL CA C 63.55 0.2 1 264 60 60 VAL CB C 28.72 0.2 1 265 60 60 VAL N N 119.7 0.2 1 266 61 61 ASP H H 8.257 0.02 1 267 61 61 ASP C C 178.3 0.2 1 268 61 61 ASP CA C 54.27 0.2 1 269 61 61 ASP CB C 36.94 0.2 1 270 61 61 ASP N N 118.5 0.2 1 271 62 62 ALA H H 7.578 0.02 1 272 62 62 ALA C C 179.1 0.2 1 273 62 62 ALA CA C 52.05 0.2 1 274 62 62 ALA CB C 16.00 0.2 1 275 62 62 ALA N N 121.6 0.2 1 276 63 63 VAL H H 8.398 0.02 1 277 63 63 VAL C C 178.8 0.2 1 278 63 63 VAL CA C 63.44 0.2 1 279 63 63 VAL CB C 28.84 0.2 1 280 63 63 VAL N N 119.0 0.2 1 281 64 64 ARG H H 9.806 0.02 1 282 64 64 ARG C C 178.8 0.2 1 283 64 64 ARG CA C 57.41 0.2 1 284 64 64 ARG CB C 27.14 0.2 1 285 64 64 ARG N N 124.8 0.2 1 286 65 65 ALA H H 7.875 0.02 1 287 65 65 ALA C C 177.4 0.2 1 288 65 65 ALA CA C 51.67 0.2 1 289 65 65 ALA CB C 15.08 0.2 1 290 65 65 ALA N N 119.8 0.2 1 291 66 66 SER H H 7.650 0.02 1 292 66 66 SER C C 173.6 0.2 1 293 66 66 SER CA C 56.58 0.2 1 294 66 66 SER CB C 62.33 0.2 1 295 66 66 SER N N 113.2 0.2 1 296 67 67 GLY H H 8.094 0.02 1 297 67 67 GLY C C 172.1 0.2 1 298 67 67 GLY CA C 42.53 0.2 1 299 67 67 GLY N N 110.8 0.2 1 300 68 68 PHE H H 7.163 0.02 1 301 68 68 PHE C C 171.5 0.2 1 302 68 68 PHE CA C 54.86 0.2 1 303 68 68 PHE CB C 37.76 0.2 1 304 68 68 PHE N N 123.2 0.2 1 305 69 69 ALA H H 8.102 0.02 1 306 69 69 ALA C C 176.7 0.2 1 307 69 69 ALA CA C 48.88 0.2 1 308 69 69 ALA CB C 14.45 0.2 1 309 69 69 ALA N N 122.7 0.2 1 310 70 70 GLU H H 7.623 0.02 1 311 70 70 GLU C C 177.5 0.2 1 312 70 70 GLU CA C 58.28 0.2 1 313 70 70 GLU CB C 26.70 0.2 1 314 70 70 GLU N N 115.6 0.2 1 315 71 71 SER H H 8.264 0.02 1 316 71 71 SER C C 175.1 0.2 1 317 71 71 SER CA C 56.79 0.2 1 318 71 71 SER CB C 60.02 0.2 1 319 71 71 SER N N 110.2 0.2 1 320 72 72 LEU H H 7.455 0.02 1 321 72 72 LEU C C 177.6 0.2 1 322 72 72 LEU CA C 53.95 0.2 1 323 72 72 LEU CB C 39.95 0.2 1 324 72 72 LEU N N 121.7 0.2 1 325 73 73 LEU H H 7.129 0.02 1 326 73 73 LEU CA C 49.73 0.2 1 327 73 73 LEU CB C 34.04 0.2 1 328 73 73 LEU N N 120.3 0.2 1 329 74 74 ASP H H 7.754 0.02 1 330 74 74 ASP C C 175.5 0.2 1 331 74 74 ASP CA C 48.57 0.2 1 332 74 74 ASP CB C 39.72 0.2 1 333 74 74 ASP N N 123.5 0.2 1 334 75 75 PRO C C 176.8 0.2 1 335 75 75 PRO CA C 61.43 0.2 1 336 75 75 PRO CB C 28.70 0.2 1 337 76 76 ALA H H 8.378 0.02 1 338 76 76 ALA C C 177.8 0.2 1 339 76 76 ALA CA C 51.14 0.2 1 340 76 76 ALA CB C 15.30 0.2 1 341 76 76 ALA N N 121.8 0.2 1 342 77 77 LEU H H 7.483 0.02 1 343 77 77 LEU C C 175.7 0.2 1 344 77 77 LEU CA C 52.29 0.2 1 345 77 77 LEU CB C 37.57 0.2 1 346 77 77 LEU N N 114.2 0.2 1 347 78 78 ASN H H 7.287 0.02 1 348 78 78 ASN C C 177.1 0.2 1 349 78 78 ASN CA C 51.32 0.2 1 350 78 78 ASN CB C 35.06 0.2 1 351 78 78 ASN N N 115.6 0.2 1 352 79 79 ARG H H 12.48 0.02 1 353 79 79 ARG C C 176.7 0.2 1 354 79 79 ARG CA C 52.47 0.2 1 355 79 79 ARG N N 126.3 0.2 1 356 80 80 ALA H H 10.24 0.02 1 357 80 80 ALA C C 178.4 0.2 1 358 80 80 ALA CA C 55.18 0.2 1 359 80 80 ALA CB C 15.45 0.2 1 360 80 80 ALA N N 125.6 0.2 1 361 81 81 GLU H H 8.561 0.02 1 362 81 81 GLU C C 178.4 0.2 1 363 81 81 GLU CA C 56.30 0.2 1 364 81 81 GLU CB C 26.09 0.2 1 365 81 81 GLU N N 115.1 0.2 1 366 82 82 VAL H H 7.772 0.02 1 367 82 82 VAL C C 176.6 0.2 1 368 82 82 VAL CA C 62.81 0.2 1 369 82 82 VAL CB C 29.02 0.2 1 370 82 82 VAL N N 120.8 0.2 1 371 83 83 LEU H H 8.712 0.02 1 372 83 83 LEU C C 174.1 0.2 1 373 83 83 LEU CA C 55.08 0.2 1 374 83 83 LEU CB C 39.55 0.2 1 375 83 83 LEU N N 121.4 0.2 1 376 84 84 ALA H H 7.969 0.02 1 377 84 84 ALA C C 177.6 0.2 1 378 84 84 ALA CA C 52.08 0.2 1 379 84 84 ALA CB C 14.67 0.2 1 380 84 84 ALA N N 119.5 0.2 1 381 85 85 ARG H H 7.377 0.02 1 382 85 85 ARG C C 178.8 0.2 1 383 85 85 ARG CA C 56.80 0.2 1 384 85 85 ARG CB C 27.03 0.2 1 385 85 85 ARG N N 116.5 0.2 1 386 86 86 ASP H H 8.425 0.02 1 387 86 86 ASP C C 178.0 0.2 1 388 86 86 ASP CA C 55.25 0.2 1 389 86 86 ASP CB C 36.89 0.2 1 390 86 86 ASP N N 122.9 0.2 1 391 87 87 LEU H H 8.441 0.02 1 392 87 87 LEU C C 178.8 0.2 1 393 87 87 LEU CA C 54.89 0.2 1 394 87 87 LEU CB C 38.06 0.2 1 395 87 87 LEU N N 120.5 0.2 1 396 88 88 ASP H H 8.502 0.02 1 397 88 88 ASP C C 178.8 0.2 1 398 88 88 ASP CA C 54.07 0.2 1 399 88 88 ASP CB C 36.82 0.2 1 400 88 88 ASP N N 122.2 0.2 1 401 89 89 LYS H H 7.534 0.02 1 402 89 89 LYS C C 178.7 0.2 1 403 89 89 LYS CA C 55.26 0.2 1 404 89 89 LYS CB C 28.93 0.2 1 405 89 89 LYS N N 120.1 0.2 1 406 90 90 LEU H H 9.153 0.02 1 407 90 90 LEU C C 178.0 0.2 1 408 90 90 LEU CA C 54.99 0.2 1 409 90 90 LEU CB C 39.60 0.2 1 410 90 90 LEU N N 121.5 0.2 1 411 91 91 ASN H H 8.541 0.02 1 412 91 91 ASN C C 175.4 0.2 1 413 91 91 ASN CA C 51.78 0.2 1 414 91 91 ASN CB C 37.59 0.2 1 415 91 91 ASN N N 112.8 0.2 1 416 92 92 GLY H H 7.711 0.02 1 417 92 92 GLY C C 171.7 0.2 1 418 92 92 GLY CA C 43.37 0.2 1 419 92 92 GLY N N 109.8 0.2 1 420 93 93 SER H H 7.993 0.02 1 421 93 93 SER C C 171.7 0.2 1 422 93 93 SER CA C 54.25 0.2 1 423 93 93 SER CB C 61.40 0.2 1 424 93 93 SER N N 112.1 0.2 1 425 94 94 SER H H 8.486 0.02 1 426 94 94 SER C C 175.2 0.2 1 427 94 94 SER CA C 55.47 0.2 1 428 94 94 SER CB C 61.19 0.2 1 429 94 94 SER N N 113.0 0.2 1 430 95 95 GLU H H 8.292 0.02 1 431 95 95 GLU C C 175.3 0.2 1 432 95 95 GLU CA C 55.31 0.2 1 433 95 95 GLU CB C 26.01 0.2 1 434 95 95 GLU N N 121.6 0.2 1 435 96 96 TRP H H 7.259 0.02 1 436 96 96 TRP C C 176.0 0.2 1 437 96 96 TRP CA C 54.90 0.2 1 438 96 96 TRP CB C 25.70 0.2 1 439 96 96 TRP N N 118.9 0.2 1 440 97 97 ARG H H 5.991 0.02 1 441 97 97 ARG C C 176.5 0.2 1 442 97 97 ARG CA C 56.08 0.2 1 443 97 97 ARG CB C 26.42 0.2 1 444 97 97 ARG N N 120.3 0.2 1 445 98 98 SER H H 7.421 0.02 1 446 98 98 SER C C 173.2 0.2 1 447 98 98 SER CA C 55.90 0.2 1 448 98 98 SER CB C 60.96 0.2 1 449 98 98 SER N N 110.5 0.2 1 450 99 99 ARG H H 7.386 0.02 1 451 99 99 ARG C C 175.2 0.2 1 452 99 99 ARG CA C 52.91 0.2 1 453 99 99 ARG CB C 28.22 0.2 1 454 99 99 ARG N N 119.0 0.2 1 455 100 100 ILE H H 7.540 0.02 1 456 100 100 ILE C C 174.3 0.2 1 457 100 100 ILE CA C 59.07 0.2 1 458 100 100 ILE N N 118.9 0.2 1 459 101 101 THR H H 8.534 0.02 1 460 101 101 THR C C 172.4 0.2 1 461 101 101 THR CA C 57.38 0.2 1 462 101 101 THR CB C 68.26 0.2 1 463 101 101 THR N N 119.3 0.2 1 464 102 102 ALA H H 8.742 0.02 1 465 102 102 ALA C C 176.5 0.2 1 466 102 102 ALA CA C 48.94 0.2 1 467 102 102 ALA CB C 17.24 0.2 1 468 102 102 ALA N N 129.5 0.2 1 469 103 103 SER H H 8.873 0.02 1 470 103 103 SER CA C 55.07 0.2 1 471 103 103 SER CB C 59.11 0.2 1 472 103 103 SER N N 122.5 0.2 1 473 104 104 PRO C C 178.0 0.2 1 474 104 104 PRO CA C 63.70 0.2 1 475 105 105 ALA H H 9.546 0.02 1 476 105 105 ALA C C 179.7 0.2 1 477 105 105 ALA CA C 51.81 0.2 1 478 105 105 ALA CB C 16.37 0.2 1 479 105 105 ALA N N 118.9 0.2 1 480 106 106 VAL H H 7.584 0.02 1 481 106 106 VAL C C 176.0 0.2 1 482 106 106 VAL CA C 63.85 0.2 1 483 106 106 VAL CB C 29.14 0.2 1 484 106 106 VAL N N 120.2 0.2 1 485 107 107 ILE H H 8.427 0.02 1 486 107 107 ILE C C 177.5 0.2 1 487 107 107 ILE CA C 61.86 0.2 1 488 107 107 ILE CB C 34.37 0.2 1 489 107 107 ILE N N 121.6 0.2 1 490 108 108 ASP H H 7.253 0.02 1 491 108 108 ASP C C 177.0 0.2 1 492 108 108 ASP CA C 54.33 0.2 1 493 108 108 ASP CB C 37.61 0.2 1 494 108 108 ASP N N 117.9 0.2 1 495 109 109 TYR H H 7.955 0.02 1 496 109 109 TYR C C 176.3 0.2 1 497 109 109 TYR CA C 54.93 0.2 1 498 109 109 TYR CB C 36.35 0.2 1 499 109 109 TYR N N 123.6 0.2 1 500 110 110 VAL H H 9.174 0.02 1 501 110 110 VAL C C 176.4 0.2 1 502 110 110 VAL CA C 64.11 0.2 1 503 110 110 VAL CB C 27.73 0.2 1 504 110 110 VAL N N 118.7 0.2 1 505 111 111 ASN H H 8.279 0.02 1 506 111 111 ASN CA C 53.27 0.2 1 507 111 111 ASN N N 117.2 0.2 1 508 113 113 LEU C C 178.0 0.2 1 509 113 113 LEU CA C 54.73 0.2 1 510 114 114 GLU H H 8.726 0.02 1 511 114 114 GLU C C 176.9 0.2 1 512 114 114 GLU CA C 56.63 0.2 1 513 114 114 GLU CB C 26.12 0.2 1 514 114 114 GLU N N 119.9 0.2 1 515 115 115 GLU H H 7.706 0.02 1 516 115 115 GLU C C 178.1 0.2 1 517 115 115 GLU CA C 56.48 0.2 1 518 115 115 GLU CB C 26.80 0.2 1 519 115 115 GLU N N 121.1 0.2 1 520 116 116 ILE H H 8.185 0.02 1 521 116 116 ILE C C 176.9 0.2 1 522 116 116 ILE CA C 62.77 0.2 1 523 116 116 ILE CB C 34.40 0.2 1 524 116 116 ILE N N 120.8 0.2 1 525 117 117 ARG H H 8.144 0.02 1 526 117 117 ARG C C 177.2 0.2 1 527 117 117 ARG CA C 56.47 0.2 1 528 117 117 ARG CB C 27.09 0.2 1 529 117 117 ARG N N 119.5 0.2 1 530 118 118 ASP H H 8.697 0.02 1 531 118 118 ASP C C 176.6 0.2 1 532 118 118 ASP CA C 54.22 0.2 1 533 118 118 ASP CB C 36.89 0.2 1 534 118 118 ASP N N 119.8 0.2 1 535 119 119 ASN H H 8.362 0.02 1 536 119 119 ASN C C 172.8 0.2 1 537 119 119 ASN CA C 50.06 0.2 1 538 119 119 ASN CB C 35.74 0.2 1 539 119 119 ASN N N 115.6 0.2 1 540 120 120 VAL H H 7.867 0.02 1 541 120 120 VAL C C 173.1 0.2 1 542 120 120 VAL CA C 59.79 0.2 1 543 120 120 VAL CB C 26.16 0.2 1 544 120 120 VAL N N 123.1 0.2 1 545 121 121 ASP H H 7.683 0.02 1 546 121 121 ASP C C 174.2 0.2 1 547 121 121 ASP CA C 49.24 0.2 1 548 121 121 ASP CB C 37.27 0.2 1 549 121 121 ASP N N 118.2 0.2 1 550 122 122 GLY H H 7.956 0.02 1 551 122 122 GLY CA C 46.29 0.2 1 552 122 122 GLY N N 111.6 0.2 1 553 123 123 PRO C C 176.2 0.2 1 554 123 123 PRO CA C 63.02 0.2 1 555 123 123 PRO CB C 29.26 0.2 1 556 124 124 ALA H H 7.152 0.02 1 557 124 124 ALA C C 178.0 0.2 1 558 124 124 ALA CA C 51.73 0.2 1 559 124 124 ALA CB C 16.24 0.2 1 560 124 124 ALA N N 114.4 0.2 1 561 125 125 LEU H H 8.477 0.02 1 562 125 125 LEU C C 178.7 0.2 1 563 125 125 LEU CA C 53.39 0.2 1 564 125 125 LEU CB C 36.92 0.2 1 565 125 125 LEU N N 118.8 0.2 1 566 126 126 VAL H H 8.630 0.02 1 567 126 126 VAL C C 175.5 0.2 1 568 126 126 VAL CA C 64.41 0.2 1 569 126 126 VAL CB C 28.10 0.2 1 570 126 126 VAL N N 119.5 0.2 1 571 127 127 ALA H H 7.397 0.02 1 572 127 127 ALA C C 177.6 0.2 1 573 127 127 ALA CA C 53.02 0.2 1 574 127 127 ALA CB C 16.48 0.2 1 575 127 127 ALA N N 120.1 0.2 1 576 128 128 HIS H H 7.589 0.02 1 577 128 128 HIS C C 176.4 0.2 1 578 128 128 HIS CA C 58.43 0.2 1 579 128 128 HIS CB C 28.24 0.2 1 580 128 128 HIS N N 114.5 0.2 1 581 129 129 HIS H H 9.222 0.02 1 582 129 129 HIS C C 175.0 0.2 1 583 129 129 HIS CA C 58.65 0.2 1 584 129 129 HIS CB C 30.10 0.2 1 585 129 129 HIS N N 122.8 0.2 1 586 130 130 TYR H H 8.841 0.02 1 587 130 130 TYR C C 176.9 0.2 1 588 130 130 TYR CA C 58.45 0.2 1 589 130 130 TYR CB C 34.79 0.2 1 590 130 130 TYR N N 119.5 0.2 1 591 131 131 VAL H H 7.810 0.02 1 592 131 131 VAL CA C 63.54 0.2 1 593 131 131 VAL CB C 28.20 0.2 1 594 131 131 VAL N N 118.1 0.2 1 595 134 134 LEU C C 178.5 0.2 1 596 134 134 LEU CA C 52.87 0.2 1 597 135 135 ALA H H 7.547 0.02 1 598 135 135 ALA CB C 15.41 0.2 1 599 135 135 ALA N N 122.1 0.2 1 600 137 137 LEU C C 177.7 0.2 1 601 137 137 LEU CA C 54.71 0.2 1 602 138 138 SER H H 8.344 0.02 1 603 138 138 SER C C 174.8 0.2 1 604 138 138 SER CA C 57.81 0.2 1 605 138 138 SER CB C 60.31 0.2 1 606 138 138 SER N N 112.6 0.2 1 607 139 139 GLY H H 8.297 0.02 1 608 139 139 GLY C C 175.2 0.2 1 609 139 139 GLY CA C 43.11 0.2 1 610 139 139 GLY N N 109.7 0.2 1 611 140 140 GLY H H 8.255 0.02 1 612 140 140 GLY C C 173.9 0.2 1 613 140 140 GLY CA C 45.52 0.2 1 614 140 140 GLY N N 109.7 0.2 1 615 141 141 GLN H H 8.278 0.02 1 616 141 141 GLN C C 177.6 0.2 1 617 141 141 GLN CA C 55.47 0.2 1 618 141 141 GLN CB C 25.35 0.2 1 619 141 141 GLN N N 117.7 0.2 1 620 142 142 VAL H H 7.466 0.02 1 621 142 142 VAL C C 176.5 0.2 1 622 142 142 VAL CA C 62.96 0.2 1 623 142 142 VAL CB C 28.75 0.2 1 624 142 142 VAL N N 119.0 0.2 1 625 143 143 ILE H H 7.424 0.02 1 626 143 143 ILE C C 176.9 0.2 1 627 143 143 ILE CA C 62.87 0.2 1 628 143 143 ILE CB C 34.79 0.2 1 629 143 143 ILE N N 119.9 0.2 1 630 144 144 ALA H H 7.720 0.02 1 631 144 144 ALA C C 178.7 0.2 1 632 144 144 ALA CA C 52.43 0.2 1 633 144 144 ALA CB C 14.95 0.2 1 634 144 144 ALA N N 119.4 0.2 1 635 145 145 ARG H H 7.656 0.02 1 636 145 145 ARG CA C 56.31 0.2 1 637 145 145 ARG CB C 26.90 0.2 1 638 145 145 ARG N N 116.3 0.2 1 639 147 147 MET C C 179.0 0.2 1 640 147 147 MET CA C 53.94 0.2 1 641 148 148 GLN H H 7.525 0.02 1 642 148 148 GLN C C 176.9 0.2 1 643 148 148 GLN CA C 56.29 0.2 1 644 148 148 GLN CB C 31.61 0.2 1 645 148 148 GLN N N 118.4 0.2 1 646 149 149 ARG H H 8.079 0.02 1 647 149 149 ARG C C 177.0 0.2 1 648 149 149 ARG CA C 55.94 0.2 1 649 149 149 ARG CB C 27.58 0.2 1 650 149 149 ARG N N 118.5 0.2 1 651 150 150 HIS H H 8.370 0.02 1 652 150 150 HIS C C 176.4 0.2 1 653 150 150 HIS CA C 54.83 0.2 1 654 150 150 HIS CB C 27.70 0.2 1 655 150 150 HIS N N 113.0 0.2 1 656 151 151 TYR H H 6.732 0.02 1 657 151 151 TYR C C 175.2 0.2 1 658 151 151 TYR CA C 52.28 0.2 1 659 151 151 TYR CB C 36.94 0.2 1 660 151 151 TYR N N 112.2 0.2 1 661 152 152 GLY H H 7.581 0.02 1 662 152 152 GLY C C 173.2 0.2 1 663 152 152 GLY CA C 43.77 0.2 1 664 152 152 GLY N N 108.7 0.2 1 665 153 153 VAL H H 7.007 0.02 1 666 153 153 VAL C C 173.5 0.2 1 667 153 153 VAL CA C 60.45 0.2 1 668 153 153 VAL CB C 29.24 0.2 1 669 153 153 VAL N N 119.3 0.2 1 670 154 154 ASP H H 8.485 0.02 1 671 154 154 ASP CA C 49.44 0.2 1 672 154 154 ASP CB C 39.67 0.2 1 673 154 154 ASP N N 128.3 0.2 1 674 155 155 PRO C C 178.0 0.2 1 675 155 155 PRO CA C 62.17 0.2 1 676 155 155 PRO CB C 28.79 0.2 1 677 156 156 GLU H H 9.147 0.02 1 678 156 156 GLU C C 174.6 0.2 1 679 156 156 GLU CA C 55.08 0.2 1 680 156 156 GLU CB C 25.96 0.2 1 681 156 156 GLU N N 117.4 0.2 1 682 157 157 ALA H H 8.260 0.02 1 683 157 157 ALA C C 173.3 0.2 1 684 157 157 ALA CA C 48.29 0.2 1 685 157 157 ALA CB C 16.03 0.2 1 686 157 157 ALA N N 121.6 0.2 1 687 158 158 LEU H H 6.911 0.02 1 688 158 158 LEU C C 177.9 0.2 1 689 158 158 LEU CA C 50.58 0.2 1 690 158 158 LEU CB C 39.37 0.2 1 691 158 158 LEU N N 117.1 0.2 1 692 159 159 GLY H H 10.13 0.02 1 693 159 159 GLY C C 176.1 0.2 1 694 159 159 GLY CA C 45.21 0.2 1 695 159 159 GLY N N 118.4 0.2 1 696 160 160 PHE H H 11.14 0.02 1 697 160 160 PHE C C 174.4 0.2 1 698 160 160 PHE CA C 57.82 0.2 1 699 160 160 PHE CB C 37.25 0.2 1 700 160 160 PHE N N 124.4 0.2 1 701 161 161 TYR H H 7.247 0.02 1 702 161 161 TYR C C 172.5 0.2 1 703 161 161 TYR CA C 55.94 0.2 1 704 161 161 TYR CB C 35.92 0.2 1 705 161 161 TYR N N 113.6 0.2 1 706 162 162 HIS H H 7.946 0.02 1 707 162 162 HIS C C 171.7 0.2 1 708 162 162 HIS CA C 51.66 0.2 1 709 162 162 HIS CB C 29.13 0.2 1 710 162 162 HIS N N 120.1 0.2 1 711 163 163 PHE H H 8.892 0.02 1 712 163 163 PHE C C 174.4 0.2 1 713 163 163 PHE CA C 53.32 0.2 1 714 163 163 PHE CB C 36.01 0.2 1 715 163 163 PHE N N 126.3 0.2 1 716 164 164 GLU H H 8.959 0.02 1 717 164 164 GLU C C 176.5 0.2 1 718 164 164 GLU CA C 55.25 0.2 1 719 164 164 GLU CB C 26.47 0.2 1 720 164 164 GLU N N 125.6 0.2 1 721 165 165 GLY H H 8.847 0.02 1 722 165 165 GLY C C 172.5 0.2 1 723 165 165 GLY CA C 41.96 0.2 1 724 165 165 GLY N N 106.6 0.2 1 725 166 166 ILE H H 7.128 0.02 1 726 166 166 ILE C C 173.2 0.2 1 727 166 166 ILE CA C 57.51 0.2 1 728 166 166 ILE CB C 35.80 0.2 1 729 166 166 ILE N N 119.7 0.2 1 730 167 167 ALA H H 8.450 0.02 1 731 167 167 ALA C C 177.3 0.2 1 732 167 167 ALA CA C 51.45 0.2 1 733 167 167 ALA CB C 16.44 0.2 1 734 167 167 ALA N N 128.5 0.2 1 735 168 168 LYS H H 8.033 0.02 1 736 168 168 LYS CB C 30.21 0.2 1 737 168 168 LYS N N 116.8 0.2 1 738 169 169 LEU C C 177.3 0.2 1 739 169 169 LEU CA C 55.88 0.2 1 740 169 169 LEU CB C 38.77 0.2 1 741 170 170 LYS H H 8.695 0.02 1 742 170 170 LYS C C 177.6 0.2 1 743 170 170 LYS CA C 57.23 0.2 1 744 170 170 LYS CB C 29.18 0.2 1 745 170 170 LYS N N 118.2 0.2 1 746 171 171 VAL H H 6.739 0.02 1 747 171 171 VAL C C 176.5 0.2 1 748 171 171 VAL CA C 62.06 0.2 1 749 171 171 VAL CB C 29.19 0.2 1 750 171 171 VAL N N 117.5 0.2 1 751 172 172 TYR H H 8.086 0.02 1 752 172 172 TYR C C 177.2 0.2 1 753 172 172 TYR CA C 58.41 0.2 1 754 172 172 TYR CB C 36.55 0.2 1 755 172 172 TYR N N 121.1 0.2 1 756 173 173 LYS H H 7.886 0.02 1 757 173 173 LYS CA C 54.64 0.2 1 758 173 173 LYS N N 120.3 0.2 1 759 174 174 ASP C C 178.2 0.2 1 760 174 174 ASP CA C 54.76 0.2 1 761 174 174 ASP CB C 36.89 0.2 1 762 175 175 GLU H H 8.455 0.02 1 763 175 175 GLU C C 177.7 0.2 1 764 175 175 GLU CA C 56.27 0.2 1 765 175 175 GLU CB C 26.03 0.2 1 766 175 175 GLU N N 121.5 0.2 1 767 176 176 TYR H H 8.624 0.02 1 768 176 176 TYR C C 176.1 0.2 1 769 176 176 TYR CA C 58.87 0.2 1 770 176 176 TYR CB C 35.77 0.2 1 771 176 176 TYR N N 123.5 0.2 1 772 177 177 ARG H H 8.110 0.02 1 773 177 177 ARG C C 176.5 0.2 1 774 177 177 ARG CA C 57.43 0.2 1 775 177 177 ARG CB C 26.42 0.2 1 776 177 177 ARG N N 117.5 0.2 1 777 178 178 GLU H H 7.607 0.02 1 778 178 178 GLU C C 177.8 0.2 1 779 178 178 GLU CA C 56.13 0.2 1 780 178 178 GLU N N 117.6 0.2 1 781 179 179 LYS H H 7.993 0.02 1 782 179 179 LYS C C 179.6 0.2 1 783 179 179 LYS CA C 56.71 0.2 1 784 179 179 LYS CB C 26.32 0.2 1 785 179 179 LYS N N 118.8 0.2 1 786 180 180 LEU H H 8.303 0.02 1 787 180 180 LEU C C 177.5 0.2 1 788 180 180 LEU CA C 54.80 0.2 1 789 180 180 LEU CB C 38.81 0.2 1 790 180 180 LEU N N 120.5 0.2 1 791 181 181 ASN H H 7.984 0.02 1 792 181 181 ASN C C 175.3 0.2 1 793 181 181 ASN CA C 51.66 0.2 1 794 181 181 ASN CB C 34.91 0.2 1 795 181 181 ASN N N 116.2 0.2 1 796 182 182 ASN H H 7.550 0.02 1 797 182 182 ASN C C 173.9 0.2 1 798 182 182 ASN CA C 50.06 0.2 1 799 182 182 ASN CB C 36.90 0.2 1 800 182 182 ASN N N 116.0 0.2 1 801 183 183 LEU H H 7.202 0.02 1 802 183 183 LEU C C 175.3 0.2 1 803 183 183 LEU CA C 52.65 0.2 1 804 183 183 LEU CB C 39.03 0.2 1 805 183 183 LEU N N 122.4 0.2 1 806 184 184 GLU H H 8.727 0.02 1 807 184 184 GLU C C 173.9 0.2 1 808 184 184 GLU CA C 53.34 0.2 1 809 184 184 GLU CB C 26.12 0.2 1 810 184 184 GLU N N 127.5 0.2 1 811 185 185 LEU H H 8.153 0.02 1 812 185 185 LEU C C 176.3 0.2 1 813 185 185 LEU CA C 50.12 0.2 1 814 185 185 LEU CB C 42.72 0.2 1 815 185 185 LEU N N 125.1 0.2 1 816 186 186 SER H H 9.325 0.02 1 817 186 186 SER C C 173.7 0.2 1 818 186 186 SER CA C 54.01 0.2 1 819 186 186 SER CB C 62.25 0.2 1 820 186 186 SER N N 119.6 0.2 1 821 187 187 ASP H H 9.115 0.02 1 822 187 187 ASP C C 177.6 0.2 1 823 187 187 ASP CA C 55.26 0.2 1 824 187 187 ASP CB C 36.83 0.2 1 825 187 187 ASP N N 121.8 0.2 1 826 188 188 GLU H H 8.753 0.02 1 827 188 188 GLU C C 178.5 0.2 1 828 188 188 GLU CA C 56.60 0.2 1 829 188 188 GLU CB C 26.31 0.2 1 830 188 188 GLU N N 119.3 0.2 1 831 189 189 GLN H H 7.870 0.02 1 832 189 189 GLN C C 177.2 0.2 1 833 189 189 GLN CA C 55.53 0.2 1 834 189 189 GLN N N 119.6 0.2 1 835 190 190 ARG H H 8.790 0.02 1 836 190 190 ARG C C 176.3 0.2 1 837 190 190 ARG CA C 57.14 0.2 1 838 190 190 ARG CB C 27.34 0.2 1 839 190 190 ARG N N 120.4 0.2 1 840 191 191 GLU H H 8.142 0.02 1 841 191 191 GLU C C 177.8 0.2 1 842 191 191 GLU CA C 56.43 0.2 1 843 191 191 GLU CB C 26.30 0.2 1 844 191 191 GLU N N 117.6 0.2 1 845 193 193 LEU C C 177.6 0.2 1 846 193 193 LEU CA C 54.48 0.2 1 847 193 193 LEU CB C 36.41 0.2 1 848 194 194 LEU H H 8.499 0.02 1 849 194 194 LEU C C 179.1 0.2 1 850 194 194 LEU CA C 55.34 0.2 1 851 194 194 LEU CB C 38.27 0.2 1 852 194 194 LEU N N 121.4 0.2 1 853 195 195 LYS H H 8.164 0.02 1 854 195 195 LYS C C 177.8 0.2 1 855 195 195 LYS CA C 56.49 0.2 1 856 195 195 LYS CB C 29.14 0.2 1 857 195 195 LYS N N 121.1 0.2 1 858 196 196 GLU H H 8.231 0.02 1 859 196 196 GLU C C 176.7 0.2 1 860 196 196 GLU CA C 55.48 0.2 1 861 196 196 GLU CB C 24.43 0.2 1 862 196 196 GLU N N 120.4 0.2 1 863 197 197 ALA H H 8.350 0.02 1 864 197 197 ALA C C 177.7 0.2 1 865 197 197 ALA CA C 52.29 0.2 1 866 197 197 ALA CB C 14.96 0.2 1 867 197 197 ALA N N 119.9 0.2 1 868 198 198 THR H H 7.387 0.02 1 869 198 198 THR C C 174.8 0.2 1 870 198 198 THR CA C 65.26 0.2 1 871 198 198 THR N N 114.2 0.2 1 872 199 199 ASP H H 7.778 0.02 1 873 199 199 ASP C C 177.2 0.2 1 874 199 199 ASP CA C 54.43 0.2 1 875 199 199 ASP CB C 36.24 0.2 1 876 199 199 ASP N N 121.7 0.2 1 877 200 200 ALA H H 8.884 0.02 1 878 200 200 ALA C C 178.4 0.2 1 879 200 200 ALA CA C 52.52 0.2 1 880 200 200 ALA CB C 14.67 0.2 1 881 200 200 ALA N N 123.0 0.2 1 882 201 201 PHE H H 7.976 0.02 1 883 201 201 PHE C C 177.8 0.2 1 884 201 201 PHE CA C 59.75 0.2 1 885 201 201 PHE CB C 36.67 0.2 1 886 201 201 PHE N N 118.1 0.2 1 887 202 202 VAL H H 8.307 0.02 1 888 202 202 VAL CA C 64.17 0.2 1 889 202 202 VAL CB C 27.73 0.2 1 890 202 202 VAL N N 122.9 0.2 1 891 203 203 PHE H H 8.374 0.02 1 892 203 203 PHE C C 176.7 0.2 1 893 203 203 PHE CA C 57.69 0.2 1 894 203 203 PHE N N 119.1 0.2 1 895 204 204 ASN H H 7.445 0.02 1 896 204 204 ASN C C 174.7 0.2 1 897 204 204 ASN CA C 53.68 0.2 1 898 204 204 ASN CB C 35.77 0.2 1 899 204 204 ASN N N 115.7 0.2 1 900 205 205 HIS H H 7.825 0.02 1 901 205 205 HIS C C 177.1 0.2 1 902 205 205 HIS CA C 57.16 0.2 1 903 205 205 HIS CB C 27.43 0.2 1 904 205 205 HIS N N 116.2 0.2 1 905 206 206 GLN H H 8.358 0.02 1 906 206 206 GLN C C 177.1 0.2 1 907 206 206 GLN CA C 55.31 0.2 1 908 206 206 GLN CB C 25.45 0.2 1 909 206 206 GLN N N 119.4 0.2 1 910 207 207 VAL H H 8.088 0.02 1 911 207 207 VAL C C 176.9 0.2 1 912 207 207 VAL CA C 63.60 0.2 1 913 207 207 VAL CB C 28.05 0.2 1 914 207 207 VAL N N 120.7 0.2 1 915 208 208 PHE H H 7.340 0.02 1 916 208 208 PHE C C 177.5 0.2 1 917 208 208 PHE CA C 56.21 0.2 1 918 208 208 PHE CB C 34.53 0.2 1 919 208 208 PHE N N 117.5 0.2 1 920 209 209 ALA H H 8.218 0.02 1 921 209 209 ALA C C 179.4 0.2 1 922 209 209 ALA CA C 51.99 0.2 1 923 209 209 ALA CB C 14.83 0.2 1 924 209 209 ALA N N 123.8 0.2 1 925 210 210 ASP H H 8.172 0.02 1 926 210 210 ASP C C 178.5 0.2 1 927 210 210 ASP CA C 54.44 0.2 1 928 210 210 ASP CB C 37.50 0.2 1 929 210 210 ASP N N 120.2 0.2 1 930 211 211 LEU H H 7.932 0.02 1 931 211 211 LEU C C 178.9 0.2 1 932 211 211 LEU CA C 54.64 0.2 1 933 211 211 LEU CB C 36.82 0.2 1 934 211 211 LEU N N 120.6 0.2 1 935 212 212 GLY H H 8.146 0.02 1 936 212 212 GLY C C 173.6 0.2 1 937 212 212 GLY CA C 43.04 0.2 1 938 212 212 GLY N N 105.4 0.2 1 939 213 213 LYS H H 7.565 0.02 1 940 213 213 LYS C C 175.9 0.2 1 941 213 213 LYS CA C 54.28 0.2 1 942 213 213 LYS CB C 30.02 0.2 1 943 213 213 LYS N N 119.9 0.2 1 944 214 214 GLY H H 8.075 0.02 1 945 214 214 GLY C C 172.5 0.2 1 946 214 214 GLY CA C 42.67 0.2 1 947 214 214 GLY N N 108.5 0.2 1 948 215 215 LEU H H 7.726 0.02 1 949 215 215 LEU C C 180.9 0.2 1 950 215 215 LEU CA C 53.31 0.2 1 951 215 215 LEU CB C 39.57 0.2 1 952 215 215 LEU N N 126.4 0.2 1 stop_ save_