data_15963 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the heme bound form of Full-Length HasAp. ; _BMRB_accession_number 15963 _BMRB_flat_file_name bmr15963.str _Entry_type original _Submission_date 2008-09-24 _Accession_date 2008-09-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Holo Full-Length HasAp assignments' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alontaga Aileen Y. . 2 Rivera Mario . . 3 Rodriguez Juan C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 "13C chemical shifts" 578 "15N chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-01-20 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 15962 'HasAp truncated polypeptide' stop_ _Original_release_date 2009-01-20 save_ ############################# # Citation for this entry # ############################# save_HasAp_Full_Length _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19072037 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alontaga Aileen Y. . 2 Rodriguez Juan C. . 3 Schonbrunn Ernst . . 4 Becker Andreas . . 5 Funke Todd . . 6 Yukl Erik T. . 7 Hayashi Takahiro . . 8 Stobaugh Jordan T. . 9 Moenne-Loccoz Pierre . . 10 Rivera Mario . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 48 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 96 _Page_last 109 _Year 2009 _Details . loop_ _Keyword HasAp Hemophore NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HasAp Full-Length polypeptide' _Enzyme_commission_number PA3407 loop_ _Mol_system_component_name _Mol_label monomer $HasAp_Full-length_polypeptide cofactor $HEM stop_ _System_molecular_weight 20902 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Full-Length HasAp bound to heme' save_ ######################## # Monomeric polymers # ######################## save_HasAp_Full-length_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HasAp_Full-length_polypeptide _Molecular_mass 21000 _Mol_thiol_state 'not present' loop_ _Biological_function 'heme acquisition protein' stop_ _Details n/a ############################## # Polymer residue sequence # ############################## _Residue_count 205 _Mol_residue_sequence ; MSISISYSTTYSGWTVADYL ADWSAYFGDVNHRPGQVVDG SNTGGFNPGPFDGSQYALKS TASDAAFIAGGDLHYTLFSN PSHTLWGKLDSIALGDTLTG GASSGGYALDSQEVSFSNLG LDSPIAQGRDGTVHKVVYGL MSGDSSALQGQIDALLKAVD PSLSINSTFDQLAAAGVAHA TPAAAAAEVGVVGVQELPHD LALAA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ILE 4 SER 5 ILE 6 SER 7 TYR 8 SER 9 THR 10 THR 11 TYR 12 SER 13 GLY 14 TRP 15 THR 16 VAL 17 ALA 18 ASP 19 TYR 20 LEU 21 ALA 22 ASP 23 TRP 24 SER 25 ALA 26 TYR 27 PHE 28 GLY 29 ASP 30 VAL 31 ASN 32 HIS 33 ARG 34 PRO 35 GLY 36 GLN 37 VAL 38 VAL 39 ASP 40 GLY 41 SER 42 ASN 43 THR 44 GLY 45 GLY 46 PHE 47 ASN 48 PRO 49 GLY 50 PRO 51 PHE 52 ASP 53 GLY 54 SER 55 GLN 56 TYR 57 ALA 58 LEU 59 LYS 60 SER 61 THR 62 ALA 63 SER 64 ASP 65 ALA 66 ALA 67 PHE 68 ILE 69 ALA 70 GLY 71 GLY 72 ASP 73 LEU 74 HIS 75 TYR 76 THR 77 LEU 78 PHE 79 SER 80 ASN 81 PRO 82 SER 83 HIS 84 THR 85 LEU 86 TRP 87 GLY 88 LYS 89 LEU 90 ASP 91 SER 92 ILE 93 ALA 94 LEU 95 GLY 96 ASP 97 THR 98 LEU 99 THR 100 GLY 101 GLY 102 ALA 103 SER 104 SER 105 GLY 106 GLY 107 TYR 108 ALA 109 LEU 110 ASP 111 SER 112 GLN 113 GLU 114 VAL 115 SER 116 PHE 117 SER 118 ASN 119 LEU 120 GLY 121 LEU 122 ASP 123 SER 124 PRO 125 ILE 126 ALA 127 GLN 128 GLY 129 ARG 130 ASP 131 GLY 132 THR 133 VAL 134 HIS 135 LYS 136 VAL 137 VAL 138 TYR 139 GLY 140 LEU 141 MET 142 SER 143 GLY 144 ASP 145 SER 146 SER 147 ALA 148 LEU 149 GLN 150 GLY 151 GLN 152 ILE 153 ASP 154 ALA 155 LEU 156 LEU 157 LYS 158 ALA 159 VAL 160 ASP 161 PRO 162 SER 163 LEU 164 SER 165 ILE 166 ASN 167 SER 168 THR 169 PHE 170 ASP 171 GLN 172 LEU 173 ALA 174 ALA 175 ALA 176 GLY 177 VAL 178 ALA 179 HIS 180 ALA 181 THR 182 PRO 183 ALA 184 ALA 185 ALA 186 ALA 187 ALA 188 GLU 189 VAL 190 GLY 191 VAL 192 VAL 193 GLY 194 VAL 195 GLN 196 GLU 197 LEU 198 PRO 199 HIS 200 ASP 201 LEU 202 ALA 203 LEU 204 ALA 205 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-29 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 15962 HasAp_truncated_polypeptide 89.76 184 100.00 100.00 1.70e-125 BMRB 19720 WT_apo-HasAp 89.76 184 100.00 100.00 1.70e-125 BMRB 19721 Y75A_apo-HasAp 89.76 184 99.46 99.46 3.05e-124 BMRB 19722 H83A_apo-HasAp 89.76 184 99.46 99.46 3.59e-124 PDB 3ELL "Structure Of The Hemophore From Pseudomonas Aeruginosa (Hasap)" 89.76 184 100.00 100.00 1.70e-125 PDB 3MOK "Structure Of Apo Hasap From Pseudomonas Aeruginosa To 1.55a Resolution" 89.76 184 100.00 100.00 1.70e-125 PDB 3MOL "Structure Of Dimeric Holo Hasap H32a Mutant From Pseudomonas Aeruginosa To 1.20a Resolution" 89.76 184 99.46 99.46 3.59e-124 PDB 3MOM "Structure Of Holo Hasap H32a Mutant Complexed With Imidazole From Pseudomonas Aeruginosa To 2.25a Resolution" 89.76 184 99.46 99.46 3.59e-124 PDB 3W8M "Crystal Structure Of Hasap With Iron Salophen" 89.76 186 100.00 100.00 1.50e-125 PDB 3W8O "Crystal Structure Of Hasap With Iron Phthalocyanine" 89.76 186 100.00 100.00 1.50e-125 PDB 3WAH "Crystal Structure Of Hasap With Iron Mesoporphyrinix" 89.76 186 100.00 100.00 1.50e-125 PDB 4O6Q "0.95a Resolution Structure Of The Hemophore Hasa From Pseudomonas Aeruginosa (y75a Mutant)" 89.76 184 99.46 99.46 3.05e-124 PDB 4O6S "1.32a Resolution Structure Of The Hemophore Hasa From Pseudomonas Aeruginosa (h83a Mutant, Zinc Bound)" 89.76 184 99.46 99.46 3.59e-124 PDB 4O6T "1.25a Resolution Structure Of The Hemophore Hasa From Pseudomonas Aeruginosa (h83a Mutant, Ph 5.4)" 89.76 184 99.46 99.46 3.59e-124 PDB 4O6U "0.89a Resolution Structure Of The Hemophore Hasa From Pseudomonas Aeruginosa (h83a Mutant)" 89.76 184 99.46 99.46 3.59e-124 DBJ BAK91367 "heme acquisition protein [Pseudomonas aeruginosa NCGM2.S1]" 100.00 205 99.51 100.00 8.89e-141 DBJ BAP21966 "heme acquisition protein [Pseudomonas aeruginosa]" 100.00 205 99.51 100.00 8.89e-141 DBJ BAP49596 "heme acquisition protein [Pseudomonas aeruginosa]" 100.00 205 99.51 100.00 8.89e-141 DBJ BAQ38483 "heme acquisition protein [Pseudomonas aeruginosa]" 100.00 205 99.51 100.00 8.89e-141 DBJ BAR66548 "hemophore HasA [Pseudomonas aeruginosa]" 100.00 205 99.51 100.00 8.89e-141 EMBL CAA76520 "HasAp [Pseudomonas aeruginosa PAO1]" 100.00 205 100.00 100.00 6.34e-141 EMBL CAW26382 "heme acquisition protein HasAp [Pseudomonas aeruginosa LESB58]" 100.00 205 99.51 100.00 8.89e-141 EMBL CCQ88896 "Hemophore HasA [Pseudomonas aeruginosa 18A]" 100.00 205 99.51 100.00 8.89e-141 EMBL CDH69922 "hypothetical protein P38_1623 [Pseudomonas aeruginosa MH38]" 100.00 205 99.51 100.00 8.89e-141 EMBL CDH76002 "hypothetical protein PAMH27_1585 [Pseudomonas aeruginosa MH27]" 100.00 205 99.51 100.00 8.89e-141 GB AAG06795 "heme acquisition protein HasAp [Pseudomonas aeruginosa PAO1]" 100.00 205 100.00 100.00 6.34e-141 GB AAT49927 "PA3407, partial [synthetic construct]" 100.00 206 100.00 100.00 5.57e-141 GB ABJ12662 "heme acquisition protein HasAp [Pseudomonas aeruginosa UCBPP-PA14]" 100.00 205 100.00 100.00 6.34e-141 GB ABR84528 "heme acquisition protein HasAp [Pseudomonas aeruginosa PA7]" 100.00 205 97.56 99.02 2.66e-137 GB AEO74046 "heme acquisition protein HasAp [Pseudomonas aeruginosa M18]" 100.00 205 99.51 100.00 8.89e-141 REF NP_252097 "heme acquisition protein HasA [Pseudomonas aeruginosa PAO1]" 100.00 205 100.00 100.00 6.34e-141 REF WP_003091842 "MULTISPECIES: heme acquisition protein HasA [Pseudomonas]" 100.00 205 99.51 100.00 8.89e-141 REF WP_003115011 "MULTISPECIES: heme acquisition protein HasA [Pseudomonas]" 100.00 205 100.00 100.00 6.34e-141 REF WP_003124283 "MULTISPECIES: heme acquisition protein HasAp [Pseudomonas]" 100.00 203 99.02 99.02 8.59e-138 REF WP_003153113 "heme acquisition protein HasAp [Pseudomonas aeruginosa]" 100.00 205 97.56 99.02 2.66e-137 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 19:17:10 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1A C1A C N 0 . ? C1B C1B C N 0 . ? C1C C1C C N 0 . ? C1D C1D C N 0 . ? C2A C2A C N 0 . ? C2B C2B C N 0 . ? C2C C2C C N 0 . ? C2D C2D C N 0 . ? C3A C3A C N 0 . ? C3B C3B C N 0 . ? C3C C3C C N 0 . ? C3D C3D C N 0 . ? C4A C4A C N 0 . ? C4B C4B C N 0 . ? C4C C4C C N 0 . ? C4D C4D C N 0 . ? CAA CAA C N 0 . ? CAB CAB C N 0 . ? CAC CAC C N 0 . ? CAD CAD C N 0 . ? CBA CBA C N 0 . ? CBB CBB C N 0 . ? CBC CBC C N 0 . ? CBD CBD C N 0 . ? CGA CGA C N 0 . ? CGD CGD C N 0 . ? CHA CHA C N 0 . ? CHB CHB C N 0 . ? CHC CHC C N 0 . ? CHD CHD C N 0 . ? CMA CMA C N 0 . ? CMB CMB C N 0 . ? CMC CMC C N 0 . ? CMD CMD C N 0 . ? FE FE FE N 0 . ? H2A H2A H N 0 . ? H2D H2D H N 0 . ? HAA1 HAA1 H N 0 . ? HAA2 HAA2 H N 0 . ? HAB HAB H N 0 . ? HAC HAC H N 0 . ? HAD1 HAD1 H N 0 . ? HAD2 HAD2 H N 0 . ? HBA1 HBA1 H N 0 . ? HBA2 HBA2 H N 0 . ? HBB1 HBB1 H N 0 . ? HBB2 HBB2 H N 0 . ? HBC1 HBC1 H N 0 . ? HBC2 HBC2 H N 0 . ? HBD1 HBD1 H N 0 . ? HBD2 HBD2 H N 0 . ? HHA HHA H N 0 . ? HHB HHB H N 0 . ? HHC HHC H N 0 . ? HHD HHD H N 0 . ? HMA1 HMA1 H N 0 . ? HMA2 HMA2 H N 0 . ? HMA3 HMA3 H N 0 . ? HMB1 HMB1 H N 0 . ? HMB2 HMB2 H N 0 . ? HMB3 HMB3 H N 0 . ? HMC1 HMC1 H N 0 . ? HMC2 HMC2 H N 0 . ? HMC3 HMC3 H N 0 . ? HMD1 HMD1 H N 0 . ? HMD2 HMD2 H N 0 . ? HMD3 HMD3 H N 0 . ? NA NA N N 0 . ? NB NB N N 0 . ? NC NC N N 0 . ? ND ND N N 0 . ? O1A O1A O N 0 . ? O1D O1D O N 0 . ? O2A O2A O N 0 . ? O2D O2D O N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? SING CHD C4C ? ? DOUB CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? DOUB NB C1B ? ? SING NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? DOUB C3C C4C ? ? SING C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING ND C1D ? ? DOUB ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HasAp_Full-length_polypeptide 'Pseudomonas aeruginosa' 287 Bacteria . Pseudomonas aeruginosa 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 $HasAp_Full-length_polypeptide 'recombinant technology' . Escherichia coli BL21(DE3)-Gold 'pET 11a' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The protein is in phosphate buffer (u=0.1).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HasAp_Full-length_polypeptide 2.80 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 46.4 mM 'natural abundance' D2O 5 % '[U-99% 2H]' H2O 95 % 'natural abundance' $HEM 2.8 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 3.0 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 3.112 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 Bruker _Model Avance _Field_strength 800 _Details '5 mm TXI 1H-13C/15N/D xyz-gradient probe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'Triple resonance probe' 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_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_(HCA)CO(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label $sample_1 save_ save_3D_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Bruker 800 MHz instrument.' save_ save_3D_HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Bruker 800 MHz instrument.' save_ save_3D_CBCA(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Bruker 800 MHz instrument.' save_ save_3D_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Bruker 800 MHz instrument.' save_ save_2D_1H-15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Bruker 800 MHz instrument.' save_ save_3D_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Varian 600 MHz instrument.' save_ save_(HCA)CO(CA)NH _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _BMRB_pulse_sequence_accession_number . _Details 'Collected in a Varian 600 MHz instrument.' 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' .1 . M pH 7.0 . pH temperature 305 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HN(CO)CA' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' (HCA)CO(CA)NH 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 monomer _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 2 SER C C 171.20 0.2 1 2 2 2 SER CA C 57.69 0.2 1 3 2 2 SER CB C 64.63 0.2 1 4 3 3 ILE H H 8.57 0.02 1 5 3 3 ILE C C 171.89 0.2 1 6 3 3 ILE CA C 61.69 0.2 1 7 3 3 ILE CB C 38.84 0.2 1 8 3 3 ILE N N 122.25 0.1 1 9 4 4 SER H H 8.08 0.02 1 10 4 4 SER C C 174.15 0.2 1 11 4 4 SER CA C 56.63 0.2 1 12 4 4 SER CB C 65.23 0.2 1 13 4 4 SER N N 118.77 0.1 1 14 5 5 ILE H H 8.62 0.02 1 15 5 5 ILE C C 174.88 0.2 1 16 5 5 ILE CA C 60.14 0.2 1 17 5 5 ILE CB C 42.95 0.2 1 18 5 5 ILE N N 127.37 0.1 1 19 6 6 SER H H 8.82 0.02 1 20 6 6 SER C C 172.63 0.2 1 21 6 6 SER CA C 57.26 0.2 1 22 6 6 SER CB C 65.33 0.2 1 23 6 6 SER N N 124.37 0.1 1 24 7 7 TYR H H 7.98 0.02 1 25 7 7 TYR C C 172.54 0.2 1 26 7 7 TYR CA C 54.21 0.2 1 27 7 7 TYR CB C 41.47 0.2 1 28 7 7 TYR N N 120.17 0.1 1 29 8 8 SER H H 8.14 0.02 1 30 8 8 SER C C 177.45 0.2 1 31 8 8 SER CA C 57.20 0.2 1 32 8 8 SER CB C 63.87 0.2 1 33 8 8 SER N N 115.74 0.1 1 34 9 9 THR H H 8.47 0.02 1 35 9 9 THR C C 176.06 0.2 1 36 9 9 THR CA C 65.65 0.2 1 37 9 9 THR CB C 69.07 0.2 1 38 9 9 THR N N 118.75 0.1 1 39 10 10 THR H H 7.66 0.02 1 40 10 10 THR C C 174.64 0.2 1 41 10 10 THR CA C 65.87 0.2 1 42 10 10 THR CB C 69.07 0.2 1 43 10 10 THR N N 119.89 0.1 1 44 11 11 TYR H H 7.87 0.02 1 45 11 11 TYR C C 175.09 0.2 1 46 11 11 TYR CA C 58.77 0.2 1 47 11 11 TYR CB C 38.30 0.2 1 48 11 11 TYR N N 117.67 0.1 1 49 12 12 SER H H 7.66 0.02 1 50 12 12 SER C C 175.25 0.2 1 51 12 12 SER CB C 64.32 0.2 1 52 12 12 SER N N 115.81 0.1 1 53 13 13 GLY H H 8.04 0.02 1 54 13 13 GLY C C 175.00 0.2 1 55 13 13 GLY CA C 45.12 0.2 1 56 13 13 GLY N N 105.69 0.1 1 57 14 14 TRP H H 8.67 0.02 1 58 14 14 TRP C C 176.21 0.2 1 59 14 14 TRP CA C 57.55 0.2 1 60 14 14 TRP CB C 29.28 0.2 1 61 14 14 TRP N N 123.08 0.1 1 62 15 15 THR H H 8.83 0.02 1 63 15 15 THR C C 175.52 0.2 1 64 15 15 THR CA C 60.24 0.2 1 65 15 15 THR CB C 69.08 0.2 1 66 15 15 THR N N 109.41 0.1 1 67 16 16 VAL H H 7.33 0.02 1 68 16 16 VAL C C 178.40 0.2 1 69 16 16 VAL CA C 66.70 0.2 1 70 16 16 VAL CB C 30.90 0.2 1 71 16 16 VAL N N 120.78 0.1 1 72 17 17 ALA H H 8.50 0.02 1 73 17 17 ALA C C 179.51 0.2 1 74 17 17 ALA CA C 55.73 0.2 1 75 17 17 ALA CB C 19.13 0.2 1 76 17 17 ALA N N 119.93 0.1 1 77 18 18 ASP H H 8.22 0.02 1 78 18 18 ASP C C 179.97 0.2 1 79 18 18 ASP CA C 57.63 0.2 1 80 18 18 ASP CB C 39.80 0.2 1 81 18 18 ASP N N 118.39 0.1 1 82 19 19 TYR H H 8.85 0.02 1 83 19 19 TYR C C 176.85 0.2 1 84 19 19 TYR CA C 63.61 0.2 1 85 19 19 TYR CB C 39.08 0.2 1 86 19 19 TYR N N 121.47 0.1 1 87 20 20 LEU H H 8.78 0.02 1 88 20 20 LEU C C 179.45 0.2 1 89 20 20 LEU CA C 58.26 0.2 1 90 20 20 LEU CB C 41.87 0.2 1 91 20 20 LEU N N 118.73 0.1 1 92 21 21 ALA H H 8.44 0.02 1 93 21 21 ALA C C 180.32 0.2 1 94 21 21 ALA CA C 56.06 0.2 1 95 21 21 ALA CB C 18.76 0.2 1 96 21 21 ALA N N 122.51 0.1 1 97 22 22 ASP H H 7.92 0.02 1 98 22 22 ASP C C 178.33 0.2 1 99 22 22 ASP CA C 48.87 0.2 1 100 22 22 ASP CB C 42.90 0.2 1 101 22 22 ASP N N 120.85 0.1 1 102 23 23 TRP H H 9.12 0.02 1 103 23 23 TRP C C 178.56 0.2 1 104 23 23 TRP CA C 63.50 0.2 1 105 23 23 TRP CB C 28.82 0.2 1 106 23 23 TRP N N 122.14 0.1 1 107 24 24 SER H H 8.61 0.02 1 108 24 24 SER C C 176.88 0.2 1 109 24 24 SER CA C 63.15 0.2 1 110 24 24 SER CB C 63.81 0.2 1 111 24 24 SER N N 113.35 0.1 1 112 25 25 ALA H H 7.45 0.02 1 113 25 25 ALA C C 178.78 0.2 1 114 25 25 ALA CA C 54.65 0.2 1 115 25 25 ALA CB C 18.31 0.2 1 116 25 25 ALA N N 124.27 0.1 1 117 26 26 TYR H H 7.42 0.02 1 118 26 26 TYR C C 177.86 0.2 1 119 26 26 TYR CA C 58.51 0.2 1 120 26 26 TYR CB C 38.74 0.2 1 121 26 26 TYR N N 120.44 0.1 1 122 27 27 PHE H H 8.49 0.02 1 123 27 27 PHE C C 176.64 0.2 1 124 27 27 PHE CA C 61.54 0.2 1 125 27 27 PHE CB C 39.22 0.2 1 126 27 27 PHE N N 123.38 0.1 1 127 28 28 GLY H H 8.27 0.02 1 128 28 28 GLY C C 176.72 0.2 1 129 28 28 GLY CA C 45.02 0.2 1 130 28 28 GLY N N 108.27 0.1 1 131 29 29 ASP H H 7.28 0.02 1 132 29 29 ASP C C 177.96 0.2 1 133 29 29 ASP CA C 51.64 0.2 1 134 29 29 ASP CB C 42.97 0.2 1 135 29 29 ASP N N 116.34 0.1 1 136 30 30 VAL H H 7.96 0.02 1 137 30 30 VAL C C 176.31 0.2 1 138 30 30 VAL CA C 61.50 0.2 1 139 30 30 VAL CB C 31.17 0.2 1 140 30 30 VAL N N 118.54 0.1 1 141 31 31 ASN H H 8.93 0.02 1 142 31 31 ASN C C 172.58 0.2 1 143 31 31 ASN CA C 53.18 0.2 1 144 31 31 ASN CB C 36.04 0.2 1 145 31 31 ASN N N 123.87 0.1 1 146 34 34 PRO C C 177.42 0.2 1 147 34 34 PRO CA C 65.92 0.2 1 148 34 34 PRO CB C 32.55 0.2 1 149 35 35 GLY H H 9.60 0.02 1 150 35 35 GLY C C 174.95 0.2 1 151 35 35 GLY CA C 46.12 0.2 1 152 35 35 GLY N N 113.93 0.1 1 153 36 36 GLN H H 8.23 0.02 1 154 36 36 GLN C C 175.08 0.2 1 155 36 36 GLN CA C 54.22 0.2 1 156 36 36 GLN CB C 30.98 0.2 1 157 36 36 GLN N N 116.74 0.1 1 158 37 37 VAL H H 7.81 0.02 1 159 37 37 VAL C C 173.92 0.2 1 160 37 37 VAL CA C 62.89 0.2 1 161 37 37 VAL CB C 29.49 0.2 1 162 37 37 VAL N N 122.28 0.1 1 163 38 38 VAL H H 8.59 0.02 1 164 38 38 VAL C C 176.61 0.2 1 165 38 38 VAL CA C 64.21 0.2 1 166 38 38 VAL CB C 30.72 0.2 1 167 38 38 VAL N N 131.25 0.1 1 168 39 39 ASP H H 7.79 0.02 1 169 39 39 ASP C C 177.20 0.2 1 170 39 39 ASP CA C 49.46 0.2 1 171 39 39 ASP CB C 42.44 0.2 1 172 39 39 ASP N N 118.28 0.1 1 173 40 40 GLY H H 8.11 0.02 1 174 40 40 GLY C C 173.86 0.2 1 175 40 40 GLY CA C 45.84 0.2 1 176 40 40 GLY N N 112.48 0.1 1 177 41 41 SER H H 8.06 0.02 1 178 41 41 SER C C 174.11 0.2 1 179 41 41 SER CA C 59.09 0.2 1 180 41 41 SER CB C 63.37 0.2 1 181 41 41 SER N N 115.03 0.1 1 182 42 42 ASN H H 7.49 0.02 1 183 42 42 ASN C C 176.28 0.2 1 184 42 42 ASN CA C 51.10 0.2 1 185 42 42 ASN CB C 36.35 0.2 1 186 42 42 ASN N N 114.78 0.1 1 187 43 43 THR H H 6.90 0.02 1 188 43 43 THR C C 175.65 0.2 1 189 43 43 THR CA C 59.32 0.2 1 190 43 43 THR CB C 70.88 0.2 1 191 43 43 THR N N 105.67 0.1 1 192 44 44 GLY H H 8.42 0.02 1 193 44 44 GLY C C 173.75 0.2 1 194 44 44 GLY CA C 46.02 0.2 1 195 44 44 GLY N N 111.93 0.1 1 196 45 45 GLY H H 8.17 0.02 1 197 45 45 GLY C C 170.42 0.2 1 198 45 45 GLY CA C 46.10 0.2 1 199 45 45 GLY N N 107.37 0.1 1 200 46 46 PHE H H 9.46 0.02 1 201 46 46 PHE C C 176.12 0.2 1 202 46 46 PHE CA C 57.40 0.2 1 203 46 46 PHE CB C 44.35 0.2 1 204 46 46 PHE N N 117.55 0.1 1 205 47 47 ASN H H 8.96 0.02 1 206 47 47 ASN C C 175.20 0.2 1 207 47 47 ASN CA C 49.31 0.2 1 208 47 47 ASN CB C 43.00 0.2 1 209 47 47 ASN N N 116.32 0.1 1 210 48 48 PRO C C 179.70 0.2 1 211 48 48 PRO CA C 65.74 0.2 1 212 48 48 PRO CB C 34.68 0.2 1 213 49 49 GLY H H 8.03 0.02 1 214 49 49 GLY C C 176.28 0.2 1 215 49 49 GLY CA C 46.55 0.2 1 216 49 49 GLY N N 105.75 0.1 1 217 50 50 PRO C C 177.66 0.2 1 218 50 50 PRO CA C 64.73 0.2 1 219 50 50 PRO CB C 34.46 0.2 1 220 51 51 PHE H H 8.89 0.02 1 221 51 51 PHE C C 170.85 0.2 1 222 51 51 PHE CA C 55.87 0.2 1 223 51 51 PHE CB C 40.81 0.2 1 224 51 51 PHE N N 117.21 0.1 1 225 52 52 ASP H H 6.64 0.02 1 226 52 52 ASP C C 174.82 0.2 1 227 52 52 ASP CA C 52.10 0.2 1 228 52 52 ASP CB C 46.08 0.2 1 229 52 52 ASP N N 113.57 0.1 1 230 53 53 GLY H H 8.67 0.02 1 231 53 53 GLY C C 171.28 0.2 1 232 53 53 GLY CA C 47.52 0.2 1 233 53 53 GLY N N 106.85 0.1 1 234 54 54 SER H H 8.90 0.02 1 235 54 54 SER C C 176.77 0.2 1 236 54 54 SER CA C 58.32 0.2 1 237 54 54 SER CB C 64.10 0.2 1 238 54 54 SER N N 114.09 0.1 1 239 55 55 GLN H H 8.11 0.02 1 240 55 55 GLN C C 175.22 0.2 1 241 55 55 GLN CA C 54.79 0.2 1 242 55 55 GLN CB C 37.42 0.2 1 243 55 55 GLN N N 117.15 0.1 1 244 56 56 TYR H H 9.46 0.02 1 245 56 56 TYR C C 172.15 0.2 1 246 56 56 TYR CA C 57.59 0.2 1 247 56 56 TYR CB C 42.62 0.2 1 248 56 56 TYR N N 122.82 0.1 1 249 57 57 ALA H H 8.18 0.02 1 250 57 57 ALA C C 174.32 0.2 1 251 57 57 ALA CA C 49.63 0.2 1 252 57 57 ALA CB C 24.15 0.2 1 253 57 57 ALA N N 129.10 0.1 1 254 58 58 LEU H H 7.09 0.02 1 255 58 58 LEU C C 174.39 0.2 1 256 58 58 LEU CA C 54.17 0.2 1 257 58 58 LEU CB C 45.31 0.2 1 258 58 58 LEU N N 121.02 0.1 1 259 59 59 LYS H H 7.82 0.02 1 260 59 59 LYS C C 174.31 0.2 1 261 59 59 LYS CA C 54.05 0.2 1 262 59 59 LYS CB C 34.92 0.2 1 263 59 59 LYS N N 124.96 0.1 1 264 60 60 SER H H 8.22 0.02 1 265 60 60 SER C C 174.77 0.2 1 266 60 60 SER CA C 57.87 0.2 1 267 60 60 SER CB C 63.42 0.2 1 268 60 60 SER N N 117.57 0.1 1 269 61 61 THR H H 7.61 0.02 1 270 61 61 THR C C 174.75 0.2 1 271 61 61 THR CA C 62.34 0.2 1 272 61 61 THR CB C 68.62 0.2 1 273 61 61 THR N N 114.48 0.1 1 274 62 62 ALA H H 8.40 0.02 1 275 62 62 ALA C C 176.53 0.2 1 276 62 62 ALA CA C 52.54 0.2 1 277 62 62 ALA CB C 21.25 0.2 1 278 62 62 ALA N N 125.96 0.1 1 279 63 63 SER H H 7.80 0.02 1 280 63 63 SER C C 172.39 0.2 1 281 63 63 SER CA C 55.10 0.2 1 282 63 63 SER CB C 66.45 0.2 1 283 63 63 SER N N 116.01 0.1 1 284 64 64 ASP H H 8.01 0.02 1 285 64 64 ASP C C 175.78 0.2 1 286 64 64 ASP CA C 54.79 0.2 1 287 64 64 ASP CB C 41.44 0.2 1 288 64 64 ASP N N 114.95 0.1 1 289 65 65 ALA H H 7.63 0.02 1 290 65 65 ALA C C 175.26 0.2 1 291 65 65 ALA CA C 52.93 0.2 1 292 65 65 ALA CB C 20.05 0.2 1 293 65 65 ALA N N 124.15 0.1 1 294 66 66 ALA H H 9.26 0.02 1 295 66 66 ALA C C 174.16 0.2 1 296 66 66 ALA CA C 52.67 0.2 1 297 66 66 ALA CB C 21.09 0.2 1 298 66 66 ALA N N 120.57 0.1 1 299 67 67 PHE H H 8.22 0.02 1 300 67 67 PHE C C 172.88 0.2 1 301 67 67 PHE CA C 55.38 0.2 1 302 67 67 PHE CB C 44.36 0.2 1 303 67 67 PHE N N 112.86 0.1 1 304 68 68 ILE H H 8.68 0.02 1 305 68 68 ILE C C 176.28 0.2 1 306 68 68 ILE CA C 60.81 0.2 1 307 68 68 ILE CB C 42.44 0.2 1 308 68 68 ILE N N 115.01 0.1 1 309 69 69 ALA H H 10.43 0.02 1 310 69 69 ALA C C 175.13 0.2 1 311 69 69 ALA CA C 50.55 0.2 1 312 69 69 ALA CB C 21.02 0.2 1 313 69 69 ALA N N 135.58 0.1 1 314 70 70 GLY H H 9.49 0.02 1 315 70 70 GLY C C 173.75 0.2 1 316 70 70 GLY CA C 43.75 0.2 1 317 70 70 GLY N N 110.92 0.1 1 318 71 71 GLY H H 8.67 0.02 1 319 71 71 GLY C C 171.60 0.2 1 320 71 71 GLY CA C 46.75 0.2 1 321 71 71 GLY N N 111.21 0.1 1 322 72 72 ASP H H 9.59 0.02 1 323 72 72 ASP C C 173.68 0.2 1 324 72 72 ASP CA C 54.65 0.2 1 325 72 72 ASP CB C 41.90 0.2 1 326 72 72 ASP N N 129.60 0.1 1 327 73 73 LEU H H 8.50 0.02 1 328 73 73 LEU C C 176.09 0.2 1 329 73 73 LEU CA C 54.48 0.2 1 330 73 73 LEU CB C 47.18 0.2 1 331 73 73 LEU N N 123.36 0.1 1 332 74 74 HIS H H 8.17 0.02 1 333 74 74 HIS C C 173.66 0.2 1 334 74 74 HIS CA C 55.15 0.2 1 335 74 74 HIS CB C 31.69 0.2 1 336 74 74 HIS N N 118.45 0.1 1 337 75 75 TYR H H 8.39 0.02 1 338 75 75 TYR C C 173.65 0.2 1 339 75 75 TYR CA C 52.69 0.2 1 340 75 75 TYR CB C 30.11 0.2 1 341 75 75 TYR N N 125.19 0.1 1 342 76 76 THR C C 176.31 0.2 1 343 77 77 LEU C C 179.14 0.2 1 344 77 77 LEU CA C 58.58 0.2 1 345 77 77 LEU CB C 41.63 0.2 1 346 78 78 PHE H H 6.47 0.02 1 347 78 78 PHE C C 175.30 0.2 1 348 78 78 PHE CA C 56.62 0.2 1 349 78 78 PHE CB C 38.51 0.2 1 350 78 78 PHE N N 120.56 0.1 1 351 79 79 SER H H 7.03 0.02 1 352 79 79 SER C C 170.58 0.2 1 353 79 79 SER CA C 57.86 0.2 1 354 79 79 SER CB C 63.10 0.2 1 355 79 79 SER N N 118.61 0.1 1 356 80 80 ASN H H 7.70 0.02 1 357 80 80 ASN C C 173.73 0.2 1 358 80 80 ASN CA C 51.68 0.2 1 359 80 80 ASN CB C 39.35 0.2 1 360 80 80 ASN N N 117.99 0.1 1 361 81 81 PRO C C 176.40 0.2 1 362 81 81 PRO CA C 61.57 0.2 1 363 81 81 PRO CB C 32.85 0.2 1 364 82 82 SER H H 8.17 0.02 1 365 82 82 SER C C 174.83 0.2 1 366 82 82 SER CA C 58.42 0.2 1 367 82 82 SER CB C 63.49 0.2 1 368 82 82 SER N N 124.72 0.1 1 369 83 83 HIS C C 174.83 0.2 1 370 83 83 HIS CA C 57.87 0.2 1 371 83 83 HIS CB C 30.50 0.2 1 372 84 84 THR H H 7.53 0.02 1 373 84 84 THR C C 176.29 0.2 1 374 84 84 THR CA C 62.18 0.2 1 375 84 84 THR CB C 68.56 0.2 1 376 84 84 THR N N 114.42 0.1 1 377 85 85 LEU C C 174.29 0.2 1 378 85 85 LEU CA C 54.48 0.2 1 379 85 85 LEU CB C 46.18 0.2 1 380 86 86 TRP H H 9.57 0.02 1 381 86 86 TRP C C 172.17 0.2 1 382 86 86 TRP CA C 55.50 0.2 1 383 86 86 TRP CB C 30.52 0.2 1 384 86 86 TRP N N 125.83 0.1 1 385 87 87 GLY H H 8.57 0.02 1 386 87 87 GLY C C 172.16 0.2 1 387 87 87 GLY CA C 43.30 0.2 1 388 87 87 GLY N N 106.23 0.1 1 389 88 88 LYS H H 8.47 0.02 1 390 88 88 LYS C C 175.12 0.2 1 391 88 88 LYS CA C 54.81 0.2 1 392 88 88 LYS CB C 34.82 0.2 1 393 88 88 LYS N N 120.83 0.1 1 394 89 89 LEU H H 8.79 0.02 1 395 89 89 LEU C C 172.91 0.2 1 396 89 89 LEU CA C 54.01 0.2 1 397 89 89 LEU CB C 46.25 0.2 1 398 89 89 LEU N N 126.63 0.1 1 399 90 90 ASP H H 9.52 0.02 1 400 90 90 ASP C C 176.71 0.2 1 401 90 90 ASP CA C 55.05 0.2 1 402 90 90 ASP CB C 45.02 0.2 1 403 90 90 ASP N N 125.07 0.1 1 404 91 91 SER H H 8.67 0.02 1 405 91 91 SER C C 173.55 0.2 1 406 91 91 SER CA C 56.92 0.2 1 407 91 91 SER CB C 66.79 0.2 1 408 91 91 SER N N 111.81 0.1 1 409 92 92 ILE H H 9.02 0.02 1 410 92 92 ILE C C 172.69 0.2 1 411 92 92 ILE CA C 59.76 0.2 1 412 92 92 ILE CB C 42.44 0.2 1 413 92 92 ILE N N 120.15 0.1 1 414 93 93 ALA H H 8.96 0.02 1 415 93 93 ALA C C 174.70 0.2 1 416 93 93 ALA CA C 50.99 0.2 1 417 93 93 ALA CB C 21.70 0.2 1 418 93 93 ALA N N 131.11 0.1 1 419 94 94 LEU H H 8.76 0.02 1 420 94 94 LEU C C 176.77 0.2 1 421 94 94 LEU CA C 53.70 0.2 1 422 94 94 LEU CB C 43.32 0.2 1 423 94 94 LEU N N 120.53 0.1 1 424 95 95 GLY H H 8.14 0.02 1 425 95 95 GLY C C 171.14 0.2 1 426 95 95 GLY CA C 47.15 0.2 1 427 95 95 GLY N N 109.13 0.1 1 428 96 96 ASP H H 8.90 0.02 1 429 96 96 ASP C C 174.06 0.2 1 430 96 96 ASP CA C 53.80 0.2 1 431 96 96 ASP CB C 45.47 0.2 1 432 96 96 ASP N N 123.19 0.1 1 433 97 97 THR H H 8.28 0.02 1 434 97 97 THR C C 172.64 0.2 1 435 97 97 THR CA C 64.70 0.2 1 436 97 97 THR CB C 65.33 0.2 1 437 97 97 THR N N 111.05 0.1 1 438 98 98 LEU H H 8.48 0.02 1 439 98 98 LEU C C 176.48 0.2 1 440 98 98 LEU CA C 55.30 0.2 1 441 98 98 LEU CB C 43.23 0.2 1 442 98 98 LEU N N 128.38 0.1 1 443 99 99 THR H H 9.34 0.02 1 444 99 99 THR C C 173.64 0.2 1 445 99 99 THR CA C 60.22 0.2 1 446 99 99 THR CB C 72.16 0.2 1 447 99 99 THR N N 120.89 0.1 1 448 100 100 GLY H H 8.35 0.02 1 449 100 100 GLY C C 173.40 0.2 1 450 100 100 GLY CA C 45.26 0.2 1 451 100 100 GLY N N 106.25 0.1 1 452 101 101 GLY H H 6.75 0.02 1 453 101 101 GLY C C 173.78 0.2 1 454 101 101 GLY CA C 43.77 0.2 1 455 101 101 GLY N N 106.29 0.1 1 456 102 102 ALA H H 8.72 0.02 1 457 102 102 ALA C C 174.43 0.2 1 458 102 102 ALA CA C 55.47 0.2 1 459 102 102 ALA CB C 19.33 0.2 1 460 102 102 ALA N N 123.55 0.1 1 461 103 103 SER C C 175.01 0.2 1 462 103 103 SER CA C 59.90 0.2 1 463 103 103 SER CB C 63.19 0.2 1 464 104 104 SER H H 7.41 0.02 1 465 104 104 SER C C 174.48 0.2 1 466 104 104 SER CA C 57.84 0.2 1 467 104 104 SER CB C 63.91 0.2 1 468 104 104 SER N N 114.79 0.1 1 469 105 105 GLY H H 7.93 0.02 1 470 105 105 GLY C C 174.16 0.2 1 471 105 105 GLY CA C 45.64 0.2 1 472 105 105 GLY N N 109.01 0.1 1 473 106 106 GLY H H 7.67 0.02 1 474 106 106 GLY C C 174.38 0.2 1 475 106 106 GLY CA C 44.33 0.2 1 476 106 106 GLY N N 107.40 0.1 1 477 107 107 TYR H H 9.31 0.02 1 478 107 107 TYR C C 175.73 0.2 1 479 107 107 TYR CA C 58.73 0.2 1 480 107 107 TYR CB C 41.26 0.2 1 481 107 107 TYR N N 121.49 0.1 1 482 108 108 ALA H H 8.79 0.02 1 483 108 108 ALA C C 174.62 0.2 1 484 108 108 ALA CA C 51.71 0.2 1 485 108 108 ALA CB C 22.50 0.2 1 486 108 108 ALA N N 123.97 0.1 1 487 109 109 LEU H H 8.30 0.02 1 488 109 109 LEU C C 176.99 0.2 1 489 109 109 LEU CA C 52.85 0.2 1 490 109 109 LEU CB C 43.38 0.2 1 491 109 109 LEU N N 119.69 0.1 1 492 110 110 ASP H H 9.31 0.02 1 493 110 110 ASP C C 177.49 0.2 1 494 110 110 ASP CA C 56.70 0.2 1 495 110 110 ASP CB C 41.76 0.2 1 496 110 110 ASP N N 124.74 0.1 1 497 111 111 SER H H 7.74 0.02 1 498 111 111 SER C C 173.14 0.2 1 499 111 111 SER CA C 55.88 0.2 1 500 111 111 SER CB C 63.20 0.2 1 501 111 111 SER N N 112.01 0.1 1 502 112 112 GLN H H 8.74 0.02 1 503 112 112 GLN C C 175.16 0.2 1 504 112 112 GLN CA C 56.65 0.2 1 505 112 112 GLN CB C 30.14 0.2 1 506 112 112 GLN N N 126.67 0.1 1 507 113 113 GLU H H 8.87 0.02 1 508 113 113 GLU C C 175.28 0.2 1 509 113 113 GLU CA C 58.64 0.2 1 510 113 113 GLU CB C 30.79 0.2 1 511 113 113 GLU N N 128.71 0.1 1 512 114 114 VAL H H 7.36 0.02 1 513 114 114 VAL C C 173.65 0.2 1 514 114 114 VAL CA C 60.39 0.2 1 515 114 114 VAL CB C 37.87 0.2 1 516 114 114 VAL N N 116.82 0.1 1 517 115 115 SER H H 8.61 0.02 1 518 115 115 SER C C 172.39 0.2 1 519 115 115 SER CA C 56.37 0.2 1 520 115 115 SER CB C 66.23 0.2 1 521 115 115 SER N N 117.50 0.1 1 522 116 116 PHE H H 9.17 0.02 1 523 116 116 PHE C C 174.15 0.2 1 524 116 116 PHE CA C 56.17 0.2 1 525 116 116 PHE CB C 42.09 0.2 1 526 116 116 PHE N N 122.63 0.1 1 527 117 117 SER H H 9.44 0.02 1 528 117 117 SER C C 172.83 0.2 1 529 117 117 SER CA C 57.78 0.2 1 530 117 117 SER CB C 65.71 0.2 1 531 117 117 SER N N 117.87 0.1 1 532 118 118 ASN H H 8.28 0.02 1 533 118 118 ASN C C 175.65 0.2 1 534 118 118 ASN CA C 53.85 0.2 1 535 118 118 ASN CB C 37.32 0.2 1 536 118 118 ASN N N 118.10 0.1 1 537 119 119 LEU H H 8.97 0.02 1 538 119 119 LEU C C 178.74 0.2 1 539 119 119 LEU CA C 57.26 0.2 1 540 119 119 LEU CB C 42.19 0.2 1 541 119 119 LEU N N 115.35 0.1 1 542 120 120 GLY H H 8.74 0.02 1 543 120 120 GLY C C 174.94 0.2 1 544 120 120 GLY CA C 47.41 0.2 1 545 120 120 GLY N N 102.57 0.1 1 546 121 121 LEU H H 7.39 0.02 1 547 121 121 LEU C C 176.22 0.2 1 548 121 121 LEU CA C 54.75 0.2 1 549 121 121 LEU CB C 42.88 0.2 1 550 121 121 LEU N N 118.53 0.1 1 551 122 122 ASP H H 8.54 0.02 1 552 122 122 ASP C C 175.93 0.2 1 553 122 122 ASP CA C 53.95 0.2 1 554 122 122 ASP CB C 43.71 0.2 1 555 122 122 ASP N N 124.91 0.1 1 556 123 123 SER H H 9.34 0.02 1 557 123 123 SER C C 172.36 0.2 1 558 123 123 SER CA C 56.21 0.2 1 559 123 123 SER CB C 66.86 0.2 1 560 123 123 SER N N 122.79 0.1 1 561 124 124 PRO C C 177.40 0.2 1 562 124 124 PRO CA C 61.93 0.2 1 563 124 124 PRO CB C 32.67 0.2 1 564 125 125 ILE H H 7.66 0.02 1 565 125 125 ILE C C 176.44 0.2 1 566 125 125 ILE CA C 64.83 0.2 1 567 125 125 ILE CB C 36.39 0.2 1 568 125 125 ILE N N 125.05 0.1 1 569 126 126 ALA H H 7.11 0.02 1 570 126 126 ALA C C 178.98 0.2 1 571 126 126 ALA CA C 53.95 0.2 1 572 126 126 ALA CB C 19.15 0.2 1 573 126 126 ALA N N 118.94 0.1 1 574 127 127 GLN H H 6.83 0.02 1 575 127 127 GLN C C 177.44 0.2 1 576 127 127 GLN CA C 56.70 0.2 1 577 127 127 GLN CB C 29.53 0.2 1 578 127 127 GLN N N 113.46 0.1 1 579 128 128 GLY H H 8.04 0.02 1 580 128 128 GLY C C 175.02 0.2 1 581 128 128 GLY CA C 46.48 0.2 1 582 128 128 GLY N N 107.47 0.1 1 583 129 129 ARG H H 8.64 0.02 1 584 129 129 ARG C C 174.77 0.2 1 585 129 129 ARG CA C 57.07 0.2 1 586 129 129 ARG CB C 29.66 0.2 1 587 129 129 ARG N N 122.97 0.1 1 588 130 130 ASP H H 7.57 0.02 1 589 130 130 ASP C C 177.01 0.2 1 590 130 130 ASP CA C 54.64 0.2 1 591 130 130 ASP CB C 41.97 0.2 1 592 130 130 ASP N N 114.81 0.1 1 593 131 131 GLY H H 7.76 0.02 1 594 131 131 GLY C C 173.13 0.2 1 595 131 131 GLY CA C 45.69 0.2 1 596 131 131 GLY N N 107.88 0.1 1 597 132 132 THR H H 8.62 0.02 1 598 132 132 THR C C 175.17 0.2 1 599 132 132 THR CA C 67.38 0.2 1 600 132 132 THR CB C 69.20 0.2 1 601 132 132 THR N N 119.98 0.1 1 602 133 133 VAL H H 8.75 0.02 1 603 133 133 VAL C C 176.47 0.2 1 604 133 133 VAL CA C 69.55 0.2 1 605 133 133 VAL CB C 31.68 0.2 1 606 133 133 VAL N N 122.38 0.1 1 607 134 134 HIS H H 8.48 0.02 1 608 134 134 HIS C C 178.35 0.2 1 609 134 134 HIS CA C 62.61 0.2 1 610 134 134 HIS CB C 31.38 0.2 1 611 134 134 HIS N N 119.87 0.1 1 612 135 135 LYS H H 8.57 0.02 1 613 135 135 LYS C C 181.44 0.2 1 614 135 135 LYS CA C 61.18 0.2 1 615 135 135 LYS CB C 33.23 0.2 1 616 135 135 LYS N N 116.19 0.1 1 617 136 136 VAL H H 9.02 0.02 1 618 136 136 VAL C C 178.22 0.2 1 619 136 136 VAL CA C 66.81 0.2 1 620 136 136 VAL CB C 31.78 0.2 1 621 136 136 VAL N N 118.58 0.1 1 622 137 137 VAL H H 8.17 0.02 1 623 137 137 VAL C C 176.86 0.2 1 624 137 137 VAL CA C 67.75 0.2 1 625 137 137 VAL CB C 32.34 0.2 1 626 137 137 VAL N N 119.11 0.1 1 627 138 138 TYR H H 10.08 0.02 1 628 138 138 TYR C C 179.69 0.2 1 629 138 138 TYR CA C 62.51 0.2 1 630 138 138 TYR CB C 40.18 0.2 1 631 138 138 TYR N N 122.79 0.1 1 632 139 139 GLY H H 8.04 0.02 1 633 139 139 GLY C C 176.33 0.2 1 634 139 139 GLY CA C 48.30 0.2 1 635 139 139 GLY N N 105.75 0.1 1 636 140 140 LEU H H 7.18 0.02 1 637 140 140 LEU C C 179.13 0.2 1 638 140 140 LEU CA C 58.54 0.2 1 639 140 140 LEU CB C 41.54 0.2 1 640 140 140 LEU N N 122.72 0.1 1 641 141 141 MET H H 7.84 0.02 1 642 141 141 MET C C 174.96 0.2 1 643 141 141 MET CA C 59.89 0.2 1 644 141 141 MET CB C 33.71 0.2 1 645 141 141 MET N N 114.70 0.1 1 646 142 142 SER H H 7.15 0.02 1 647 142 142 SER C C 174.23 0.2 1 648 142 142 SER CA C 56.39 0.2 1 649 142 142 SER CB C 63.78 0.2 1 650 142 142 SER N N 109.48 0.1 1 651 143 143 GLY H H 7.71 0.02 1 652 143 143 GLY C C 173.67 0.2 1 653 143 143 GLY CA C 47.15 0.2 1 654 143 143 GLY N N 111.01 0.1 1 655 144 144 ASP H H 8.51 0.02 1 656 144 144 ASP C C 175.52 0.2 1 657 144 144 ASP CA C 52.53 0.2 1 658 144 144 ASP CB C 42.37 0.2 1 659 144 144 ASP N N 119.09 0.1 1 660 145 145 SER H H 9.01 0.02 1 661 145 145 SER C C 175.19 0.2 1 662 145 145 SER CA C 58.81 0.2 1 663 145 145 SER CB C 64.25 0.2 1 664 145 145 SER N N 119.69 0.1 1 665 146 146 SER H H 8.77 0.02 1 666 146 146 SER C C 177.11 0.2 1 667 146 146 SER CA C 63.59 0.2 1 668 146 146 SER CB C 62.40 0.2 1 669 146 146 SER N N 121.30 0.1 1 670 147 147 ALA H H 9.02 0.02 1 671 147 147 ALA C C 180.91 0.2 1 672 147 147 ALA CA C 55.77 0.2 1 673 147 147 ALA CB C 17.57 0.2 1 674 147 147 ALA N N 127.06 0.1 1 675 148 148 LEU H H 8.24 0.02 1 676 148 148 LEU C C 177.82 0.2 1 677 148 148 LEU CA C 58.43 0.2 1 678 148 148 LEU CB C 41.02 0.2 1 679 148 148 LEU N N 120.34 0.1 1 680 149 149 GLN H H 8.99 0.02 1 681 149 149 GLN C C 177.78 0.2 1 682 149 149 GLN CA C 61.01 0.2 1 683 149 149 GLN CB C 29.24 0.2 1 684 149 149 GLN N N 117.53 0.1 1 685 150 150 GLY H H 8.16 0.02 1 686 150 150 GLY C C 177.05 0.2 1 687 150 150 GLY CA C 47.46 0.2 1 688 150 150 GLY N N 104.11 0.1 1 689 151 151 GLN H H 7.59 0.02 1 690 151 151 GLN C C 178.05 0.2 1 691 151 151 GLN CA C 57.56 0.2 1 692 151 151 GLN CB C 27.72 0.2 1 693 151 151 GLN N N 119.40 0.1 1 694 152 152 ILE H H 8.41 0.02 1 695 152 152 ILE C C 177.24 0.2 1 696 152 152 ILE CA C 64.67 0.2 1 697 152 152 ILE CB C 36.71 0.2 1 698 152 152 ILE N N 118.80 0.1 1 699 153 153 ASP H H 8.46 0.02 1 700 153 153 ASP C C 177.18 0.2 1 701 153 153 ASP CA C 59.22 0.2 1 702 153 153 ASP CB C 42.89 0.2 1 703 153 153 ASP N N 118.72 0.1 1 704 154 154 ALA H H 7.22 0.02 1 705 154 154 ALA C C 181.17 0.2 1 706 154 154 ALA CA C 55.34 0.2 1 707 154 154 ALA CB C 18.41 0.2 1 708 154 154 ALA N N 117.28 0.1 1 709 155 155 LEU H H 7.94 0.02 1 710 155 155 LEU C C 180.16 0.2 1 711 155 155 LEU CA C 58.02 0.2 1 712 155 155 LEU CB C 42.89 0.2 1 713 155 155 LEU N N 119.52 0.1 1 714 156 156 LEU H H 8.56 0.02 1 715 156 156 LEU C C 178.48 0.2 1 716 156 156 LEU CA C 58.14 0.2 1 717 156 156 LEU CB C 41.58 0.2 1 718 156 156 LEU N N 120.61 0.1 1 719 157 157 LYS H H 7.99 0.02 1 720 157 157 LYS C C 178.30 0.2 1 721 157 157 LYS CA C 58.63 0.2 1 722 157 157 LYS CB C 32.93 0.2 1 723 157 157 LYS N N 118.59 0.1 1 724 158 158 ALA H H 7.28 0.02 1 725 158 158 ALA C C 179.37 0.2 1 726 158 158 ALA CA C 53.74 0.2 1 727 158 158 ALA CB C 18.56 0.2 1 728 158 158 ALA N N 118.42 0.1 1 729 159 159 VAL H H 7.50 0.02 1 730 159 159 VAL C C 176.62 0.2 1 731 159 159 VAL CA C 65.65 0.2 1 732 159 159 VAL CB C 31.97 0.2 1 733 159 159 VAL N N 120.04 0.1 1 734 160 160 ASP H H 7.79 0.02 1 735 160 160 ASP C C 173.93 0.2 1 736 160 160 ASP CA C 52.44 0.2 1 737 160 160 ASP CB C 44.17 0.2 1 738 160 160 ASP N N 118.84 0.1 1 739 161 161 PRO C C 176.80 0.2 1 740 161 161 PRO CA C 64.64 0.2 1 741 161 161 PRO CB C 32.17 0.2 1 742 162 162 SER H H 8.92 0.02 1 743 162 162 SER C C 174.53 0.2 1 744 162 162 SER CA C 59.97 0.2 1 745 162 162 SER CB C 64.09 0.2 1 746 162 162 SER N N 115.02 0.1 1 747 163 163 LEU H H 8.15 0.02 1 748 163 163 LEU C C 174.75 0.2 1 749 163 163 LEU CA C 53.96 0.2 1 750 163 163 LEU CB C 43.54 0.2 1 751 163 163 LEU N N 124.29 0.1 1 752 164 164 SER H H 8.24 0.02 1 753 164 164 SER C C 175.01 0.2 1 754 164 164 SER CA C 58.33 0.2 1 755 164 164 SER CB C 67.73 0.2 1 756 164 164 SER N N 109.82 0.1 1 757 165 165 ILE H H 9.09 0.02 1 758 165 165 ILE C C 174.10 0.2 1 759 165 165 ILE CA C 62.32 0.2 1 760 165 165 ILE CB C 39.23 0.2 1 761 165 165 ILE N N 114.84 0.1 1 762 166 166 ASN H H 8.41 0.02 1 763 166 166 ASN C C 174.79 0.2 1 764 166 166 ASN CA C 53.79 0.2 1 765 166 166 ASN CB C 39.21 0.2 1 766 166 166 ASN N N 116.64 0.1 1 767 167 167 SER H H 7.92 0.02 1 768 167 167 SER C C 173.17 0.2 1 769 167 167 SER CA C 60.36 0.2 1 770 167 167 SER CB C 64.47 0.2 1 771 167 167 SER N N 119.42 0.1 1 772 168 168 THR H H 8.40 0.02 1 773 168 168 THR C C 176.88 0.2 1 774 168 168 THR CA C 60.01 0.2 1 775 168 168 THR CB C 71.62 0.2 1 776 168 168 THR N N 111.25 0.1 1 777 169 169 PHE H H 8.01 0.02 1 778 169 169 PHE C C 177.70 0.2 1 779 169 169 PHE CA C 52.70 0.2 1 780 169 169 PHE CB C 36.10 0.2 1 781 169 169 PHE N N 118.95 0.1 1 782 170 170 ASP H H 8.50 0.02 1 783 170 170 ASP C C 180.09 0.2 1 784 170 170 ASP CA C 57.64 0.2 1 785 170 170 ASP CB C 41.17 0.2 1 786 170 170 ASP N N 116.72 0.1 1 787 171 171 GLN H H 8.09 0.02 1 788 171 171 GLN C C 180.18 0.2 1 789 171 171 GLN CA C 59.31 0.2 1 790 171 171 GLN CB C 28.25 0.2 1 791 171 171 GLN N N 121.59 0.1 1 792 172 172 LEU H H 8.32 0.02 1 793 172 172 LEU C C 179.40 0.2 1 794 172 172 LEU CA C 57.51 0.2 1 795 172 172 LEU CB C 41.39 0.2 1 796 172 172 LEU N N 120.35 0.1 1 797 173 173 ALA H H 8.92 0.02 1 798 173 173 ALA C C 182.15 0.2 1 799 173 173 ALA CA C 54.99 0.2 1 800 173 173 ALA CB C 18.86 0.2 1 801 173 173 ALA N N 126.61 0.1 1 802 174 174 ALA H H 8.07 0.02 1 803 174 174 ALA C C 178.93 0.2 1 804 174 174 ALA CA C 54.91 0.2 1 805 174 174 ALA CB C 17.66 0.2 1 806 174 174 ALA N N 123.97 0.1 1 807 175 175 ALA H H 7.35 0.02 1 808 175 175 ALA C C 177.61 0.2 1 809 175 175 ALA CA C 52.30 0.2 1 810 175 175 ALA CB C 20.57 0.2 1 811 175 175 ALA N N 117.17 0.1 1 812 176 176 GLY H H 7.86 0.02 1 813 176 176 GLY C C 174.47 0.2 1 814 176 176 GLY CA C 45.83 0.2 1 815 176 176 GLY N N 105.42 0.1 1 816 177 177 VAL H H 7.61 0.02 1 817 177 177 VAL C C 173.52 0.2 1 818 177 177 VAL CA C 62.21 0.2 1 819 177 177 VAL CB C 33.12 0.2 1 820 177 177 VAL N N 113.81 0.1 1 821 178 178 ALA H H 6.90 0.02 1 822 178 178 ALA C C 175.20 0.2 1 823 178 178 ALA CA C 49.03 0.2 1 824 178 178 ALA CB C 24.60 0.2 1 825 178 178 ALA N N 119.66 0.1 1 826 179 179 HIS H H 8.67 0.02 1 827 179 179 HIS C C 172.53 0.2 1 828 179 179 HIS CA C 55.40 0.2 1 829 179 179 HIS CB C 32.42 0.2 1 830 179 179 HIS N N 116.86 0.1 1 831 180 180 ALA H H 8.44 0.02 1 832 180 180 ALA C C 178.57 0.2 1 833 180 180 ALA CA C 50.79 0.2 1 834 180 180 ALA CB C 19.71 0.2 1 835 180 180 ALA N N 127.74 0.1 1 836 181 181 THR H H 8.56 0.02 1 837 181 181 THR C C 172.37 0.2 1 838 181 181 THR CA C 59.19 0.2 1 839 181 181 THR CB C 69.27 0.2 1 840 181 181 THR N N 117.70 0.1 1 841 182 182 PRO C C 176.70 0.2 1 842 182 182 PRO CA C 63.247 0.2 1 843 182 182 PRO CB C 32.31 0.2 1 844 183 183 ALA H H 8.26 0.02 1 845 183 183 ALA C C 174.60 0.2 1 846 183 183 ALA CA C 52.44 0.2 1 847 183 183 ALA CB C 19.75 0.2 1 848 183 183 ALA N N 125.72 0.1 1 849 184 184 ALA H H 7.81 0.02 1 850 184 184 ALA C C 176.25 0.2 1 851 184 184 ALA CA C 52.31 0.2 1 852 184 184 ALA CB C 20.54 0.2 1 853 184 184 ALA N N 129.35 0.1 1 854 185 185 ALA H H 8.29 0.02 1 855 185 185 ALA C C 177.24 0.2 1 856 185 185 ALA CA C 52.53 0.2 1 857 185 185 ALA CB C 19.60 0.2 1 858 185 185 ALA N N 123.98 0.1 1 859 186 186 ALA H H 8.24 0.02 1 860 186 186 ALA C C 177.27 0.2 1 861 186 186 ALA CA C 52.47 0.2 1 862 186 186 ALA CB C 19.38 0.2 1 863 186 186 ALA N N 123.59 0.1 1 864 187 187 ALA H H 8.20 0.02 1 865 187 187 ALA C C 177.61 0.2 1 866 187 187 ALA CA C 52.50 0.2 1 867 187 187 ALA CB C 19.51 0.2 1 868 187 187 ALA N N 123.31 0.1 1 869 188 188 GLU H H 8.23 0.02 1 870 188 188 GLU C C 176.34 0.2 1 871 188 188 GLU CA C 56.59 0.2 1 872 188 188 GLU CB C 33.04 0.2 1 873 188 188 GLU N N 124.37 0.1 1 874 189 189 VAL H H 8.14 0.02 1 875 189 189 VAL C C 176.56 0.2 1 876 189 189 VAL CA C 62.78 0.2 1 877 189 189 VAL CB C 33.00 0.2 1 878 189 189 VAL N N 121.17 0.1 1 879 190 190 GLY H H 8.42 0.02 1 880 190 190 GLY C C 173.69 0.2 1 881 190 190 GLY CA C 45.34 0.2 1 882 190 190 GLY N N 112.26 0.1 1 883 191 191 VAL H H 8.00 0.02 1 884 191 191 VAL C C 175.30 0.2 1 885 191 191 VAL CA C 59.65 0.2 1 886 191 191 VAL CB C 33.03 0.2 1 887 191 191 VAL N N 119.58 0.1 1 888 192 192 VAL H H 8.00 0.02 1 889 192 192 VAL C C 176.41 0.2 1 890 192 192 VAL CA C 62.64 0.2 1 891 192 192 VAL CB C 33.01 0.2 1 892 192 192 VAL N N 119.58 0.1 1 893 193 193 GLY H H 8.44 0.02 1 894 193 193 GLY C C 173.70 0.2 1 895 193 193 GLY CA C 45.39 0.2 1 896 193 193 GLY N N 112.85 0.1 1 897 194 194 VAL H H 7.98 0.02 1 898 194 194 VAL C C 176.07 0.2 1 899 194 194 VAL CA C 62.50 0.2 1 900 194 194 VAL CB C 32.90 0.2 1 901 194 194 VAL N N 119.90 0.1 1 902 195 195 GLN H H 8.46 0.02 1 903 195 195 GLN C C 175.43 0.2 1 904 195 195 GLN CA C 55.99 0.2 1 905 195 195 GLN CB C 29.96 0.2 1 906 195 195 GLN N N 124.20 0.1 1 907 196 196 GLU H H 8.40 0.02 1 908 196 196 GLU C C 175.82 0.2 1 909 196 196 GLU CA C 55.63 0.2 1 910 196 196 GLU CB C 30.69 0.2 1 911 196 196 GLU N N 122.98 0.1 1 912 197 197 LEU H H 8.21 0.02 1 913 197 197 LEU C C 176.54 0.2 1 914 197 197 LEU CA C 52.44 0.2 1 915 197 197 LEU CB C 42.60 0.2 1 916 197 197 LEU N N 124.12 0.1 1 917 198 198 PRO C C 178.20 0.2 1 918 198 198 PRO CA C 63.31 0.2 1 919 198 198 PRO CB C 32.32 0.2 1 920 199 199 HIS H H 8.32 0.02 1 921 199 199 HIS C C 174.82 0.2 1 922 199 199 HIS CA C 56.43 0.2 1 923 199 199 HIS CB C 30.64 0.2 1 924 199 199 HIS N N 119.63 0.1 1 925 200 200 ASP H H 8.28 0.02 1 926 200 200 ASP C C 175.87 0.2 1 927 200 200 ASP CA C 54.56 0.2 1 928 200 200 ASP CB C 41.25 0.2 1 929 200 200 ASP N N 120.74 0.1 1 930 201 201 LEU H H 8.13 0.02 1 931 201 201 LEU C C 176.11 0.2 1 932 201 201 LEU CA C 55.74 0.2 1 933 201 201 LEU CB C 42.58 0.2 1 934 201 201 LEU N N 122.80 0.1 1 935 202 202 ALA H H 8.21 0.02 1 936 202 202 ALA C C 177.47 0.2 1 937 202 202 ALA CA C 52.78 0.2 1 938 202 202 ALA CB C 19.18 0.2 1 939 202 202 ALA N N 123.68 0.1 1 940 203 203 LEU H H 7.95 0.02 1 941 203 203 LEU C C 176.80 0.2 1 942 203 203 LEU CA C 55.12 0.2 1 943 203 203 LEU CB C 42.66 0.2 1 944 203 203 LEU N N 120.84 0.1 1 945 204 204 ALA H H 8.10 0.02 1 946 204 204 ALA C C 175.90 0.2 1 947 204 204 ALA CA C 52.52 0.2 1 948 204 204 ALA CB C 19.54 0.2 1 949 204 204 ALA N N 125.39 0.1 1 950 205 205 ALA H H 8.34 0.02 1 951 205 205 ALA C C 175.12 0.2 1 952 205 205 ALA CA C 53.12 0.2 1 953 205 205 ALA CB C 21.32 0.2 1 954 205 205 ALA N N 125.15 0.1 1 stop_ save_