data_5269 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the 1H, 13C, and 15N signals of Synechocystis sp. PCC 6803 methemoglobin ; _BMRB_accession_number 5269 _BMRB_flat_file_name bmr5269.str _Entry_type original _Submission_date 2002-01-31 _Accession_date 2002-01-31 _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 Falzone Christopher J. . 2 Lecomte Juliette T.J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 659 "13C chemical shifts" 494 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-23 original BMRB . stop_ _Original_release_date 2002-01-31 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of the 1H, 13C, and 15N signals of Synechocystis sp. PCC 6803 methemoglobin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22056593 _PubMed_ID 12061721 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Falzone Christopher J. . 2 Lecomte Juliette T.J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 71 _Page_last 72 _Year 2002 _Details . loop_ _Keyword glbN globin 'truncated hemoglobin' stop_ save_ ################################## # Molecular system description # ################################## save_system_GlbN _Saveframe_category molecular_system _Mol_system_name trHb _Abbreviation_common GlbN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GlbN $GlbN Heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GlbN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cyanobacterial hemoglobin' _Abbreviation_common Hb _Molecular_mass 14353 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MSTLYEKLGGTTAVDLAVDK FYERVLQDDRIKHFFADVDM AKQRAHQKAFLTYAFGGTDK YDGRYMREAHKELVENHGLN GEHFDAVAEDLLATLKEMGV PEDLIAEVAAVAGAPAHKRD VLNQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 THR 4 LEU 5 TYR 6 GLU 7 LYS 8 LEU 9 GLY 10 GLY 11 THR 12 THR 13 ALA 14 VAL 15 ASP 16 LEU 17 ALA 18 VAL 19 ASP 20 LYS 21 PHE 22 TYR 23 GLU 24 ARG 25 VAL 26 LEU 27 GLN 28 ASP 29 ASP 30 ARG 31 ILE 32 LYS 33 HIS 34 PHE 35 PHE 36 ALA 37 ASP 38 VAL 39 ASP 40 MET 41 ALA 42 LYS 43 GLN 44 ARG 45 ALA 46 HIS 47 GLN 48 LYS 49 ALA 50 PHE 51 LEU 52 THR 53 TYR 54 ALA 55 PHE 56 GLY 57 GLY 58 THR 59 ASP 60 LYS 61 TYR 62 ASP 63 GLY 64 ARG 65 TYR 66 MET 67 ARG 68 GLU 69 ALA 70 HIS 71 LYS 72 GLU 73 LEU 74 VAL 75 GLU 76 ASN 77 HIS 78 GLY 79 LEU 80 ASN 81 GLY 82 GLU 83 HIS 84 PHE 85 ASP 86 ALA 87 VAL 88 ALA 89 GLU 90 ASP 91 LEU 92 LEU 93 ALA 94 THR 95 LEU 96 LYS 97 GLU 98 MET 99 GLY 100 VAL 101 PRO 102 GLU 103 ASP 104 LEU 105 ILE 106 ALA 107 GLU 108 VAL 109 ALA 110 ALA 111 VAL 112 ALA 113 GLY 114 ALA 115 PRO 116 ALA 117 HIS 118 LYS 119 ARG 120 ASP 121 VAL 122 LEU 123 ASN 124 GLN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1MWB 'Solution Structure Of The Recombinant Hemoglobin From The Cyanobacterium Synechocystis Sp. Pcc 6803 In Its Hemichrome State' 99.19 123 100.00 100.00 5.16e-65 PDB 1RTX 'Crystal Structure Of Synechocystis Hemoglobin With A Covalent Heme Linkage' 99.19 123 100.00 100.00 5.16e-65 PDB 1S69 'The X-Ray Structure Of The Cyanobacteria Synechocystis Hemoglobin "cyanoglobin" With Cyanide Ligand' 100.00 124 100.00 100.00 1.17e-65 PDB 1S6A 'The X-Ray Structure Of The Cyanobacteria Synechocystis Hemoglobin "cyanoglobin" With Azide Ligand' 100.00 124 100.00 100.00 1.17e-65 PDB 2HZ1 'The X-Ray Crystal Structure Of Ferrous Synechocystis Hemoglobin With A Covalent Linkage' 99.19 123 100.00 100.00 5.16e-65 PDB 2HZ2 'The X-Ray Crystal Structure Of Ferric Synechocystis Hemoglobin H117a Mutant With A Covalent Linkage' 99.19 123 99.19 99.19 5.62e-64 PDB 2HZ3 'The X-Ray Crystal Structure Of Ferrous Synechocystis Hemoglobin H117a Mutant With A Covalent Linkage' 99.19 123 99.19 99.19 5.62e-64 DBJ BAA17991 'cyanoglobin [Synechocystis sp. PCC 6803]' 100.00 124 100.00 100.00 1.17e-65 REF NP_441311 'cyanoglobin [Synechocystis sp. PCC 6803]' 100.00 124 100.00 100.00 1.17e-65 SWISS-PROT P73925 'Cyanoglobin (Hemoglobin) (Hb)' 100.00 124 100.00 100.00 1.17e-65 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (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 Thu Jun 9 09:34:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $GlbN 'Synechocystis sp. PCC 6803' 1148 Bacteria . . . glbN 'Pasteur Culture Collection of Cyanobacteria.' $HEM . . . . . . . 'Not applicable.' 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 _Details $GlbN 'recombinant technology' 'E. coli' . . BL21(DE3) . ; Purified apoprotein reconstituted with Fe(III) protoporphyrin IX (unlabeled, Sigma). N-terminal methionine cleaved by E. coli. ; $HEM . . . . . . 'The heme was not isotopically labeled.' 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 $GlbN . mM 1 1.5 '[U-13C; U-15N]' phosphate 20 mM . . . H2O 95 % . . . D2O 5 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GlbN . mM 1 1.5 [U-15N] phosphate 20 mM . . . H2O 95 % . . . D2O 5 % . . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GlbN . mM 1 2 . phosphate 20 mM . . . H2O 95 % . . . D2O 5 % . . . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GlbN . mM 1 2 . phosphate 20 mM . . . D2O 100 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'manual peak assignment' stop_ _Details . save_ save_Felix_97.0 _Saveframe_category software _Name 'Felix 97.0' _Version . loop_ _Task 'cross-peak volume determination' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2QF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_1H-15N-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-NOESY _Sample_label . save_ save_1H-15N-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-TOCSY _Sample_label . save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HCCH-COSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_CBCA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_12 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_1H-13C_HSQC-NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-NOESY' _Sample_label . save_ save_HCC(CO)NH_14 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _Sample_label . save_ save_1H-15N_HMQC_15 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC' _Sample_label . save_ save_1H-13C_HMQC_16 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HMQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 na temperature 298 0.5 K stop_ save_ save_ex-cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.5 0.1 na temperature 298 0.5 K stop_ save_ save_ex-cond_3 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.1 na temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio dioxane C 13 'methylene protons' ppm 67.8 internal direct cylindrical internal parallel 1.000000000 H2O H 1 protons ppm 4.76 internal direct cylindrical internal parallel 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 2QF-COSY TOCSY NOESY 1H-15N-NOESY 1H-15N-TOCSY HNCA HN(CA)CO HNCO HCCH-TOCSY HCCH-COSY CBCA(CO)NH CBCANH '1H-13C HSQC-NOESY' HCC(CO)NH '1H-15N HMQC' '1H-13C HMQC' stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name GlbN _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 SER HA H 4.00 0.03 1 2 . 2 SER HB2 H 3.82 0.03 2 3 . 2 SER CA C 55.4 0.50 1 4 . 2 SER CB C 63.4 0.50 1 5 . 3 THR H H 7.48 0.03 1 6 . 3 THR HA H 4.43 0.03 1 7 . 3 THR HB H 4.51 0.03 1 8 . 3 THR HG2 H 1.27 0.03 1 9 . 3 THR CA C 60.0 0.50 1 10 . 3 THR CB C 69.2 0.50 1 11 . 3 THR CG2 C 19.5 0.50 1 12 . 4 LEU H H 8.47 0.03 1 13 . 4 LEU HA H 3.74 0.03 1 14 . 4 LEU HB2 H 1.46 0.03 2 15 . 4 LEU HB3 H 1.35 0.03 2 16 . 4 LEU HG H 1.26 0.03 1 17 . 4 LEU HD1 H 0.48 0.03 2 18 . 4 LEU HD2 H 0.58 0.03 2 19 . 4 LEU C C 175.7 0.50 1 20 . 4 LEU CA C 56.5 0.50 1 21 . 4 LEU CB C 39.6 0.50 1 22 . 4 LEU CG C 23.9 0.50 1 23 . 4 LEU CD1 C 21.8 0.50 2 24 . 4 LEU CD2 C 23.1 0.50 2 25 . 4 LEU N N 121.4 0.30 1 26 . 5 TYR H H 7.50 0.03 1 27 . 5 TYR HA H 3.94 0.03 1 28 . 5 TYR HB2 H 2.91 0.03 1 29 . 5 TYR HB3 H 2.91 0.03 1 30 . 5 TYR HD1 H 6.97 0.03 3 31 . 5 TYR HE1 H 6.75 0.03 3 32 . 5 TYR C C 176.9 0.50 1 33 . 5 TYR CA C 59.1 0.50 1 34 . 5 TYR CB C 36.1 0.50 1 35 . 5 TYR CD1 C 131.2 0.50 3 36 . 5 TYR CE1 C 116.8 0.50 3 37 . 5 TYR N N 115.5 0.30 1 38 . 6 GLU H H 7.73 0.03 1 39 . 6 GLU HA H 3.97 0.03 1 40 . 6 GLU HB2 H 2.08 0.03 2 41 . 6 GLU HB3 H 2.00 0.03 2 42 . 6 GLU HG2 H 2.30 0.03 2 43 . 6 GLU C C 178.4 0.50 1 44 . 6 GLU CA C 57.2 0.50 1 45 . 6 GLU CB C 27.5 0.50 1 46 . 6 GLU N N 118.1 0.30 1 47 . 7 LYS H H 8.23 0.03 1 48 . 7 LYS HA H 4.00 0.03 1 49 . 7 LYS HB2 H 1.74 0.03 2 50 . 7 LYS HB3 H 1.78 0.03 2 51 . 7 LYS HG2 H 1.53 0.03 2 52 . 7 LYS HG3 H 1.40 0.03 2 53 . 7 LYS C C 176.7 0.50 1 54 . 7 LYS CA C 57.3 0.50 1 55 . 7 LYS CB C 30.9 0.50 1 56 . 7 LYS CG C 23.1 0.50 1 57 . 7 LYS N N 119.1 0.30 1 58 . 8 LEU H H 7.67 0.03 1 59 . 8 LEU HA H 4.06 0.03 1 60 . 8 LEU HB2 H 1.38 0.03 1 61 . 8 LEU HB3 H 1.25 0.03 1 62 . 8 LEU HG H 1.30 0.03 1 63 . 8 LEU HD1 H 0.53 0.03 1 64 . 8 LEU HD2 H 0.37 0.03 1 65 . 8 LEU C C 175.0 0.50 1 66 . 8 LEU CA C 53.9 0.50 1 67 . 8 LEU CB C 40.2 0.50 1 68 . 8 LEU CG C 24.9 0.50 1 69 . 8 LEU CD1 C 21.6 0.50 1 70 . 8 LEU CD2 C 22.6 0.50 1 71 . 8 LEU N N 115.3 0.30 1 72 . 9 GLY H H 7.33 0.03 1 73 . 9 GLY HA2 H 3.70 0.03 1 74 . 9 GLY HA3 H 4.26 0.03 1 75 . 9 GLY C C 173.5 0.50 1 76 . 9 GLY CA C 43.4 0.50 1 77 . 9 GLY N N 102.7 0.30 1 78 . 10 GLY H H 8.16 0.03 1 79 . 10 GLY HA2 H 4.28 0.03 1 80 . 10 GLY HA3 H 3.42 0.03 1 81 . 10 GLY C C 172.5 0.50 1 82 . 10 GLY CA C 42.5 0.50 1 83 . 10 GLY N N 108.7 0.30 1 84 . 11 THR H H 8.44 0.03 1 85 . 11 THR HA H 3.90 0.03 1 86 . 11 THR HB H 4.17 0.03 1 87 . 11 THR HG2 H 1.28 0.03 1 88 . 11 THR CA C 64.0 0.50 1 89 . 11 THR CB C 66.8 0.50 1 90 . 11 THR CG2 C 20.2 0.50 1 91 . 11 THR N N 113.8 0.30 1 92 . 12 THR H H 8.15 0.03 1 93 . 12 THR HA H 4.05 0.03 1 94 . 12 THR HB H 4.09 0.03 1 95 . 12 THR HG2 H 1.23 0.03 1 96 . 12 THR C C 174.4 0.50 1 97 . 12 THR CA C 64.0 0.50 1 98 . 12 THR CB C 66.7 0.50 1 99 . 12 THR CG2 C 18.9 0.50 1 100 . 12 THR N N 115.6 0.30 1 101 . 13 ALA H H 7.32 0.03 1 102 . 13 ALA HA H 4.14 0.03 1 103 . 13 ALA HB H 1.30 0.03 1 104 . 13 ALA C C 177.9 0.50 1 105 . 13 ALA CA C 52.9 0.50 1 106 . 13 ALA CB C 17.4 0.50 1 107 . 13 ALA N N 124.1 0.30 1 108 . 14 VAL H H 7.77 0.03 1 109 . 14 VAL HA H 3.35 0.03 1 110 . 14 VAL HB H 2.09 0.03 1 111 . 14 VAL HG1 H 0.80 0.03 1 112 . 14 VAL HG2 H 0.68 0.03 1 113 . 14 VAL C C 175.8 0.50 1 114 . 14 VAL CA C 65.2 0.50 1 115 . 14 VAL CB C 29.5 0.50 1 116 . 14 VAL CG1 C 19.9 0.50 1 117 . 14 VAL CG2 C 21.9 0.50 1 118 . 14 VAL N N 118.1 0.30 1 119 . 15 ASP H H 8.17 0.03 1 120 . 15 ASP HA H 4.41 0.03 1 121 . 15 ASP HB2 H 2.70 0.03 2 122 . 15 ASP C C 177.3 0.50 1 123 . 15 ASP CA C 56.0 0.50 1 124 . 15 ASP CB C 38.1 0.50 1 125 . 15 ASP N N 118.2 0.30 1 126 . 16 LEU H H 7.71 0.03 1 127 . 16 LEU HA H 4.34 0.03 1 128 . 16 LEU HB2 H 1.77 0.03 2 129 . 16 LEU HB3 H 1.66 0.03 2 130 . 16 LEU HG H 1.70 0.03 1 131 . 16 LEU HD1 H 0.98 0.03 2 132 . 16 LEU HD2 H 1.00 0.03 2 133 . 16 LEU C C 176.8 0.50 1 134 . 16 LEU CA C 56.0 0.50 1 135 . 16 LEU CB C 40.2 0.50 1 136 . 16 LEU CG C 24.5 0.50 1 137 . 16 LEU CD1 C 22.6 0.50 1 138 . 16 LEU CD2 C 22.6 0.50 1 139 . 16 LEU N N 120.1 0.30 1 140 . 17 ALA H H 8.16 0.03 1 141 . 17 ALA HA H 4.22 0.03 1 142 . 17 ALA HB H 1.35 0.03 1 143 . 17 ALA C C 178.2 0.50 1 144 . 17 ALA CA C 53.2 0.50 1 145 . 17 ALA CB C 16.2 0.50 1 146 . 17 ALA N N 121.1 0.30 1 147 . 18 VAL H H 8.65 0.03 1 148 . 18 VAL HA H 3.82 0.03 1 149 . 18 VAL HB H 2.49 0.03 1 150 . 18 VAL HG1 H 1.32 0.03 1 151 . 18 VAL HG2 H 1.35 0.03 1 152 . 18 VAL C C 176.0 0.50 1 153 . 18 VAL CA C 66.4 0.50 1 154 . 18 VAL CB C 29.4 0.50 1 155 . 18 VAL CG1 C 19.5 0.50 1 156 . 18 VAL CG2 C 21.9 0.50 1 157 . 18 VAL N N 116.8 0.30 1 158 . 19 ASP H H 8.30 0.03 1 159 . 19 ASP HA H 4.71 0.03 1 160 . 19 ASP HB2 H 3.00 0.03 2 161 . 19 ASP HB3 H 2.90 0.03 2 162 . 19 ASP C C 177.6 0.50 1 163 . 19 ASP CA C 56.9 0.50 1 164 . 19 ASP CB C 38.4 0.50 1 165 . 19 ASP N N 120.1 0.30 1 166 . 20 LYS H H 8.54 0.03 1 167 . 20 LYS HA H 4.22 0.03 1 168 . 20 LYS HB2 H 1.94 0.03 2 169 . 20 LYS HG2 H 1.70 0.03 2 170 . 20 LYS HG3 H 1.60 0.03 2 171 . 20 LYS HD3 H 1.74 0.03 2 172 . 20 LYS HE2 H 3.10 0.03 2 173 . 20 LYS C C 178.0 0.50 1 174 . 20 LYS CA C 57.3 0.50 1 175 . 20 LYS CB C 31.2 0.50 1 176 . 20 LYS CG C 23.6 0.50 1 177 . 20 LYS CD C 26.7 0.50 1 178 . 20 LYS N N 118.5 0.30 1 179 . 21 PHE H H 9.02 0.03 1 180 . 21 PHE HA H 4.93 0.03 1 181 . 21 PHE HB2 H 3.59 0.03 2 182 . 21 PHE HB3 H 3.64 0.03 2 183 . 21 PHE HD1 H 7.29 0.03 3 184 . 21 PHE HE1 H 7.64 0.03 3 185 . 21 PHE HZ H 6.57 0.03 1 186 . 21 PHE C C 175.4 0.50 1 187 . 21 PHE CA C 56.1 0.50 1 188 . 21 PHE CB C 37.8 0.50 1 189 . 21 PHE N N 122.6 0.30 1 190 . 22 TYR H H 9.42 0.03 1 191 . 22 TYR HA H 4.36 0.03 1 192 . 22 TYR HB2 H 3.87 0.03 1 193 . 22 TYR HB3 H 3.54 0.03 1 194 . 22 TYR HD1 H 7.54 0.03 3 195 . 22 TYR HE1 H 7.10 0.03 3 196 . 22 TYR C C 175.6 0.50 1 197 . 22 TYR CA C 59.2 0.50 1 198 . 22 TYR CB C 36.1 0.50 1 199 . 22 TYR CD1 C 132.3 0.50 3 200 . 22 TYR CE1 C 117.0 0.50 3 201 . 22 TYR N N 119.7 0.30 1 202 . 23 GLU H H 8.01 0.03 1 203 . 23 GLU HA H 3.69 0.03 1 204 . 23 GLU HB2 H 2.09 0.03 2 205 . 23 GLU HG2 H 2.55 0.03 2 206 . 23 GLU HG3 H 2.27 0.03 2 207 . 23 GLU C C 176.9 0.50 1 208 . 23 GLU CA C 57.5 0.50 1 209 . 23 GLU CB C 27.7 0.50 1 210 . 23 GLU CG C 33.9 0.50 1 211 . 23 GLU N N 118.7 0.30 1 212 . 24 ARG H H 8.02 0.03 1 213 . 24 ARG HA H 3.92 0.03 1 214 . 24 ARG HB2 H 2.13 0.03 2 215 . 24 ARG HB3 H 1.88 0.03 2 216 . 24 ARG HG2 H 1.65 0.03 2 217 . 24 ARG HG3 H 1.41 0.03 2 218 . 24 ARG HD2 H 3.25 0.03 2 219 . 24 ARG C C 178.3 0.50 1 220 . 24 ARG CA C 57.5 0.50 1 221 . 24 ARG CB C 28.6 0.50 1 222 . 24 ARG CG C 26.5 0.50 1 223 . 24 ARG CD C 41.5 0.50 1 224 . 24 ARG N N 119.3 0.30 1 225 . 25 VAL H H 8.25 0.03 1 226 . 25 VAL HA H 3.46 0.03 1 227 . 25 VAL HB H 1.98 0.03 1 228 . 25 VAL HG1 H 0.46 0.03 1 229 . 25 VAL HG2 H 0.62 0.03 1 230 . 25 VAL C C 176.0 0.50 1 231 . 25 VAL CA C 65.0 0.50 1 232 . 25 VAL CB C 29.2 0.50 1 233 . 25 VAL CG1 C 19.4 0.50 1 234 . 25 VAL CG2 C 22.0 0.50 1 235 . 25 VAL N N 120.2 0.30 1 236 . 26 LEU H H 7.30 0.03 1 237 . 26 LEU HA H 4.02 0.03 1 238 . 26 LEU HB2 H 1.54 0.03 1 239 . 26 LEU HB3 H 1.54 0.03 1 240 . 26 LEU HG H 1.61 0.03 1 241 . 26 LEU HD1 H 0.91 0.03 2 242 . 26 LEU HD2 H 0.88 0.03 2 243 . 26 LEU C C 175.9 0.50 1 244 . 26 LEU CA C 54.7 0.50 1 245 . 26 LEU CB C 39.7 0.50 1 246 . 26 LEU CG C 24.7 0.50 1 247 . 26 LEU CD1 C 21.3 0.50 2 248 . 26 LEU CD2 C 22.2 0.50 2 249 . 26 LEU N N 116.3 0.30 1 250 . 27 GLN H H 7.08 0.03 1 251 . 27 GLN HA H 4.40 0.03 1 252 . 27 GLN HB2 H 2.20 0.03 2 253 . 27 GLN HB3 H 1.92 0.03 2 254 . 27 GLN HG2 H 2.38 0.03 2 255 . 27 GLN HG3 H 2.26 0.03 2 256 . 27 GLN HE21 H 6.80 0.03 2 257 . 27 GLN HE22 H 7.52 0.03 2 258 . 27 GLN C C 173.6 0.50 1 259 . 27 GLN CA C 52.5 0.50 1 260 . 27 GLN CB C 27.3 0.50 1 261 . 27 GLN CG C 31.7 0.50 1 262 . 27 GLN N N 112.7 0.30 1 263 . 27 GLN NE2 N 111.5 0.30 1 264 . 28 ASP H H 7.51 0.03 1 265 . 28 ASP HA H 4.57 0.03 1 266 . 28 ASP HB2 H 2.65 0.03 1 267 . 28 ASP HB3 H 3.31 0.03 1 268 . 28 ASP C C 174.6 0.50 1 269 . 28 ASP CA C 51.2 0.50 1 270 . 28 ASP CB C 37.9 0.50 1 271 . 28 ASP N N 120.7 0.30 1 272 . 29 ASP H H 8.94 0.03 1 273 . 29 ASP HA H 4.10 0.03 1 274 . 29 ASP HB2 H 2.77 0.03 2 275 . 29 ASP HB3 H 2.64 0.03 2 276 . 29 ASP C C 175.4 0.50 1 277 . 29 ASP CA C 55.3 0.50 1 278 . 29 ASP CB C 38.6 0.50 1 279 . 29 ASP N N 127.3 0.30 1 280 . 30 ARG H H 8.44 0.03 1 281 . 30 ARG HA H 4.10 0.03 1 282 . 30 ARG HB2 H 1.85 0.03 2 283 . 30 ARG HB3 H 1.71 0.03 2 284 . 30 ARG HG2 H 1.71 0.03 2 285 . 30 ARG HD2 H 2.88 0.03 2 286 . 30 ARG HD3 H 3.25 0.03 2 287 . 30 ARG HE H 8.24 0.03 1 288 . 30 ARG C C 176.5 0.50 1 289 . 30 ARG CA C 56.8 0.50 1 290 . 30 ARG CB C 29.3 0.50 1 291 . 30 ARG CG C 23.6 0.50 1 292 . 30 ARG CD C 41.5 0.50 1 293 . 30 ARG N N 116.6 0.30 1 294 . 30 ARG NE N 83.0 0.30 1 295 . 31 ILE H H 6.86 0.03 1 296 . 31 ILE HA H 4.40 0.03 1 297 . 31 ILE HB H 1.59 0.03 1 298 . 31 ILE HG12 H 0.66 0.03 1 299 . 31 ILE HG13 H 1.20 0.03 1 300 . 31 ILE HG2 H 0.57 0.03 1 301 . 31 ILE HD1 H 0.41 0.03 1 302 . 31 ILE C C 175.4 0.50 1 303 . 31 ILE CA C 58.6 0.50 1 304 . 31 ILE CB C 40.7 0.50 1 305 . 31 ILE CG1 C 23.3 0.50 1 306 . 31 ILE CG2 C 18.4 0.50 1 307 . 31 ILE CD1 C 13.7 0.50 1 308 . 31 ILE N N 101.9 0.30 1 309 . 32 LYS H H 8.45 0.03 1 310 . 32 LYS HA H 3.98 0.03 1 311 . 32 LYS HB2 H 1.94 0.03 2 312 . 32 LYS HG2 H 1.41 0.03 2 313 . 32 LYS HG3 H 1.15 0.03 2 314 . 32 LYS HD2 H 1.62 0.03 2 315 . 32 LYS HE2 H 2.90 0.03 2 316 . 32 LYS C C 176.4 0.50 1 317 . 32 LYS CA C 58.3 0.50 1 318 . 32 LYS CB C 29.0 0.50 1 319 . 32 LYS CG C 22.2 0.50 1 320 . 32 LYS CD C 26.7 0.50 1 321 . 32 LYS N N 121.9 0.30 1 322 . 33 HIS H H 8.33 0.03 1 323 . 33 HIS HA H 4.19 0.03 1 324 . 33 HIS HB2 H 2.68 0.03 2 325 . 33 HIS HB3 H 2.66 0.03 2 326 . 33 HIS HD2 H 6.06 0.03 1 327 . 33 HIS HE1 H 7.17 0.03 1 328 . 33 HIS C C 176.2 0.50 1 329 . 33 HIS CA C 56.5 0.50 1 330 . 33 HIS CB C 26.8 0.50 1 331 . 33 HIS CD2 C 115.8 0.50 1 332 . 33 HIS CE1 C 136.8 0.50 1 333 . 33 HIS N N 118.4 0.30 1 334 . 34 PHE H H 6.81 0.03 1 335 . 34 PHE HA H 3.35 0.03 1 336 . 34 PHE HB2 H 1.38 0.03 1 337 . 34 PHE HB3 H 1.12 0.03 1 338 . 34 PHE HD1 H 6.03 0.03 3 339 . 34 PHE HE1 H 5.93 0.03 3 340 . 34 PHE HZ H 6.17 0.03 1 341 . 34 PHE C C 173.0 0.50 1 342 . 34 PHE CA C 58.7 0.50 1 343 . 34 PHE CB C 35.5 0.50 1 344 . 34 PHE N N 117.5 0.30 1 345 . 35 PHE H H 7.15 0.03 1 346 . 35 PHE HA H 4.72 0.03 1 347 . 35 PHE HB2 H 2.65 0.03 1 348 . 35 PHE HB3 H 3.81 0.03 1 349 . 35 PHE HD1 H 7.65 0.03 3 350 . 35 PHE HE1 H 8.56 0.03 3 351 . 35 PHE HZ H 6.59 0.03 1 352 . 35 PHE C C 174.1 0.50 1 353 . 35 PHE CA C 56.1 0.50 1 354 . 35 PHE CB C 39.2 0.50 1 355 . 35 PHE CE1 C 130.1 0.50 3 356 . 35 PHE N N 112.0 0.30 1 357 . 36 ALA H H 7.37 0.03 1 358 . 36 ALA HA H 4.18 0.03 1 359 . 36 ALA HB H 1.35 0.03 1 360 . 36 ALA C C 176.8 0.50 1 361 . 36 ALA CA C 53.7 0.50 1 362 . 36 ALA CB C 16.9 0.50 1 363 . 36 ALA N N 121.3 0.30 1 364 . 37 ASP H H 8.52 0.03 1 365 . 37 ASP HA H 4.80 0.03 1 366 . 37 ASP HB2 H 2.46 0.03 1 367 . 37 ASP HB3 H 2.71 0.03 1 368 . 37 ASP C C 173.9 0.50 1 369 . 37 ASP CA C 52.0 0.50 1 370 . 37 ASP CB C 38.6 0.50 1 371 . 37 ASP N N 114.4 0.30 1 372 . 38 VAL H H 7.70 0.03 1 373 . 38 VAL HA H 4.32 0.03 1 374 . 38 VAL HB H 2.74 0.03 1 375 . 38 VAL HG1 H 1.65 0.03 1 376 . 38 VAL HG2 H 1.26 0.03 1 377 . 38 VAL C C 174.6 0.50 1 378 . 38 VAL CA C 59.9 0.50 1 379 . 38 VAL CB C 31.2 0.50 1 380 . 38 VAL CG1 C 20.2 0.50 1 381 . 38 VAL CG2 C 20.0 0.50 1 382 . 38 VAL N N 121.3 0.30 1 383 . 39 ASP H H 8.93 0.03 1 384 . 39 ASP HA H 4.65 0.03 1 385 . 39 ASP HB2 H 3.06 0.03 1 386 . 39 ASP HB3 H 2.81 0.03 1 387 . 39 ASP C C 175.7 0.50 1 388 . 39 ASP CA C 53.4 0.50 1 389 . 39 ASP CB C 40.1 0.50 1 390 . 39 ASP N N 127.3 0.30 1 391 . 40 MET H H 9.03 0.03 1 392 . 40 MET HA H 4.48 0.03 1 393 . 40 MET HB2 H 2.44 0.03 2 394 . 40 MET HB3 H 2.37 0.03 2 395 . 40 MET HG2 H 2.91 0.03 2 396 . 40 MET HG3 H 2.75 0.03 2 397 . 40 MET HE H 2.28 0.03 1 398 . 40 MET C C 176.9 0.50 1 399 . 40 MET CA C 58.6 0.50 1 400 . 40 MET CB C 30.7 0.50 1 401 . 40 MET CG C 29.5 0.50 1 402 . 40 MET CE C 14.7 0.50 1 403 . 40 MET N N 122.4 0.30 1 404 . 41 ALA H H 8.76 0.03 1 405 . 41 ALA HA H 4.40 0.03 1 406 . 41 ALA HB H 1.65 0.03 1 407 . 41 ALA C C 180.5 0.50 1 408 . 41 ALA CA C 53.9 0.50 1 409 . 41 ALA CB C 16.2 0.50 1 410 . 41 ALA N N 121.1 0.30 1 411 . 42 LYS H H 8.33 0.03 1 412 . 42 LYS HA H 4.70 0.03 1 413 . 42 LYS HB2 H 2.41 0.03 1 414 . 42 LYS HB3 H 2.41 0.03 1 415 . 42 LYS HG2 H 1.87 0.03 2 416 . 42 LYS HG3 H 1.74 0.03 2 417 . 42 LYS HE2 H 2.91 0.03 2 418 . 42 LYS C C 179.8 0.50 1 419 . 42 LYS CA C 58.0 0.50 1 420 . 42 LYS CB C 30.8 0.50 1 421 . 42 LYS CG C 23.9 0.50 1 422 . 42 LYS N N 120.8 0.30 1 423 . 43 GLN H H 9.47 0.03 1 424 . 43 GLN HA H 5.82 0.03 1 425 . 43 GLN HB2 H 3.24 0.03 1 426 . 43 GLN HB3 H 3.24 0.03 1 427 . 43 GLN HG2 H 3.40 0.03 2 428 . 43 GLN HG3 H 3.02 0.03 2 429 . 43 GLN HE21 H 6.77 0.03 2 430 . 43 GLN HE22 H 7.94 0.03 2 431 . 43 GLN C C 178.4 0.50 1 432 . 43 GLN CA C 60.3 0.50 1 433 . 43 GLN CB C 29.5 0.50 1 434 . 43 GLN CG C 34.8 0.50 1 435 . 43 GLN N N 122.1 0.30 1 436 . 43 GLN NE2 N 111.0 0.30 1 437 . 44 ARG H H 9.09 0.03 1 438 . 44 ARG HA H 4.43 0.03 1 439 . 44 ARG HB2 H 1.95 0.03 1 440 . 44 ARG HB3 H 2.12 0.03 1 441 . 44 ARG HG2 H 1.56 0.03 2 442 . 44 ARG HG3 H 1.61 0.03 2 443 . 44 ARG HD2 H 3.26 0.03 2 444 . 44 ARG HD3 H 3.18 0.03 2 445 . 44 ARG C C 177.8 0.50 1 446 . 44 ARG CA C 59.9 0.50 1 447 . 44 ARG CB C 28.2 0.50 1 448 . 44 ARG CG C 27.2 0.50 1 449 . 44 ARG CD C 41.0 0.50 1 450 . 44 ARG N N 119.6 0.30 1 451 . 45 ALA H H 8.89 0.03 1 452 . 45 ALA HA H 4.79 0.03 1 453 . 45 ALA HB H 2.07 0.03 1 454 . 45 ALA C C 180.8 0.50 1 455 . 45 ALA CA C 53.9 0.50 1 456 . 45 ALA CB C 16.4 0.50 1 457 . 45 ALA N N 120.4 0.30 1 458 . 46 HIS H H 10.71 0.03 1 459 . 46 HIS HA H 7.70 0.03 1 460 . 46 HIS HB2 H 10.82 0.03 1 461 . 46 HIS HB3 H 9.20 0.03 1 462 . 46 HIS HD1 H 13.20 0.03 1 463 . 46 HIS HE1 H -11.60 0.03 1 464 . 46 HIS C C 178.6 0.50 1 465 . 46 HIS CA C 77.7 0.50 1 466 . 46 HIS CB C 24.3 0.50 1 467 . 46 HIS N N 123.0 0.30 1 468 . 46 HIS ND1 N 135.6 0.30 1 469 . 47 GLN H H 10.47 0.03 1 470 . 47 GLN HA H 6.76 0.03 1 471 . 47 GLN HB2 H 3.25 0.03 1 472 . 47 GLN HB3 H 2.77 0.03 1 473 . 47 GLN HG2 H 2.82 0.03 2 474 . 47 GLN HG3 H 1.88 0.03 2 475 . 47 GLN HE21 H 8.66 0.03 2 476 . 47 GLN HE22 H 6.08 0.03 2 477 . 47 GLN C C 178.5 0.50 1 478 . 47 GLN CA C 57.0 0.50 1 479 . 47 GLN CB C 27.5 0.50 1 480 . 47 GLN CG C 31.8 0.50 1 481 . 47 GLN N N 124.0 0.30 1 482 . 47 GLN NE2 N 111.0 0.30 1 483 . 48 LYS H H 9.74 0.03 1 484 . 48 LYS HA H 4.40 0.03 1 485 . 48 LYS HB2 H 2.30 0.03 1 486 . 48 LYS HB3 H 2.54 0.03 1 487 . 48 LYS HG2 H 1.60 0.03 2 488 . 48 LYS HG3 H 1.44 0.03 2 489 . 48 LYS HD2 H 1.81 0.03 2 490 . 48 LYS HE2 H 3.02 0.03 2 491 . 48 LYS C C 177.8 0.50 1 492 . 48 LYS CA C 59.0 0.50 1 493 . 48 LYS CB C 30.7 0.50 1 494 . 48 LYS CG C 23.4 0.50 1 495 . 48 LYS CD C 27.7 0.50 1 496 . 48 LYS CE C 39.9 0.50 1 497 . 48 LYS N N 121.6 0.30 1 498 . 49 ALA H H 9.18 0.03 1 499 . 49 ALA HA H 4.05 0.03 1 500 . 49 ALA HB H 0.96 0.03 1 501 . 49 ALA C C 177.9 0.50 1 502 . 49 ALA CA C 53.4 0.50 1 503 . 49 ALA CB C 15.0 0.50 1 504 . 49 ALA N N 125.9 0.30 1 505 . 50 PHE H H 9.47 0.03 1 506 . 50 PHE HA H 3.14 0.03 1 507 . 50 PHE HB2 H 2.73 0.03 1 508 . 50 PHE HB3 H 3.76 0.03 1 509 . 50 PHE HD1 H 5.14 0.03 3 510 . 50 PHE HE1 H 5.72 0.03 3 511 . 50 PHE HZ H 5.98 0.03 1 512 . 50 PHE C C 175.0 0.50 1 513 . 50 PHE CA C 60.6 0.50 1 514 . 50 PHE CB C 37.2 0.50 1 515 . 50 PHE CD1 C 130.0 0.50 3 516 . 50 PHE CE1 C 128.6 0.50 3 517 . 50 PHE N N 119.3 0.30 1 518 . 51 LEU H H 8.83 0.03 1 519 . 51 LEU HA H 3.73 0.03 1 520 . 51 LEU HB2 H 2.04 0.03 2 521 . 51 LEU HB3 H 1.93 0.03 2 522 . 51 LEU HG H 1.56 0.03 1 523 . 51 LEU HD1 H 0.88 0.03 1 524 . 51 LEU HD2 H 0.57 0.03 1 525 . 51 LEU C C 175.5 0.50 1 526 . 51 LEU CA C 58.1 0.50 1 527 . 51 LEU CB C 40.6 0.50 1 528 . 51 LEU CG C 25.7 0.50 1 529 . 51 LEU CD1 C 24.4 0.50 1 530 . 51 LEU CD2 C 24.0 0.50 1 531 . 51 LEU N N 119.9 0.30 1 532 . 52 THR H H 8.48 0.03 1 533 . 52 THR HA H 3.60 0.03 1 534 . 52 THR HB H 4.25 0.03 1 535 . 52 THR HG2 H 1.12 0.03 1 536 . 52 THR C C 175.1 0.50 1 537 . 52 THR CA C 64.9 0.50 1 538 . 52 THR CB C 65.9 0.50 1 539 . 52 THR CG2 C 19.0 0.50 1 540 . 52 THR N N 113.9 0.30 1 541 . 53 TYR H H 7.86 0.03 1 542 . 53 TYR HA H 3.78 0.03 1 543 . 53 TYR HB2 H 2.52 0.03 2 544 . 53 TYR HB3 H 2.48 0.03 2 545 . 53 TYR HD1 H 6.34 0.03 3 546 . 53 TYR HE1 H 6.27 0.03 3 547 . 53 TYR C C 175.3 0.50 1 548 . 53 TYR CA C 58.8 0.50 1 549 . 53 TYR CB C 35.5 0.50 1 550 . 53 TYR CD1 C 131.3 0.50 3 551 . 53 TYR CE1 C 116.4 0.50 3 552 . 53 TYR N N 122.7 0.30 1 553 . 54 ALA H H 8.05 0.03 1 554 . 54 ALA HA H 3.21 0.03 1 555 . 54 ALA HB H 0.93 0.03 1 556 . 54 ALA C C 174.1 0.50 1 557 . 54 ALA CA C 52.5 0.50 1 558 . 54 ALA CB C 16.4 0.50 1 559 . 54 ALA N N 121.3 0.30 1 560 . 55 PHE H H 7.57 0.03 1 561 . 55 PHE HA H 4.23 0.03 1 562 . 55 PHE HB2 H 3.18 0.03 1 563 . 55 PHE HB3 H 2.96 0.03 1 564 . 55 PHE HD1 H 7.14 0.03 3 565 . 55 PHE HE1 H 6.90 0.03 3 566 . 55 PHE HZ H 6.82 0.03 1 567 . 55 PHE C C 174.5 0.50 1 568 . 55 PHE CA C 55.0 0.50 1 569 . 55 PHE CB C 36.8 0.50 1 570 . 55 PHE CD1 C 128.4 0.50 3 571 . 55 PHE CZ C 126.5 0.50 1 572 . 55 PHE N N 111.6 0.30 1 573 . 56 GLY H H 7.77 0.03 1 574 . 56 GLY HA2 H 3.70 0.03 2 575 . 56 GLY HA3 H 4.10 0.03 2 576 . 56 GLY C C 174.1 0.50 1 577 . 56 GLY CA C 44.0 0.50 1 578 . 56 GLY N N 106.2 0.30 1 579 . 57 GLY H H 8.36 0.03 1 580 . 57 GLY HA2 H 3.39 0.03 2 581 . 57 GLY HA3 H 3.98 0.03 2 582 . 57 GLY C C 173.1 0.50 1 583 . 57 GLY CA C 44.2 0.50 1 584 . 57 GLY N N 108.4 0.30 1 585 . 58 THR H H 7.78 0.03 1 586 . 58 THR HA H 4.02 0.03 1 587 . 58 THR HB H 4.09 0.03 1 588 . 58 THR HG2 H 0.80 0.03 1 589 . 58 THR C C 175.4 0.50 1 590 . 58 THR CA C 60.5 0.50 1 591 . 58 THR CB C 67.0 0.50 1 592 . 58 THR CG2 C 19.2 0.50 1 593 . 58 THR N N 112.4 0.30 1 594 . 59 ASP H H 8.33 0.03 1 595 . 59 ASP HA H 4.42 0.03 1 596 . 59 ASP HB2 H 2.54 0.03 2 597 . 59 ASP C C 174.9 0.50 1 598 . 59 ASP CA C 52.8 0.50 1 599 . 59 ASP CB C 38.6 0.50 1 600 . 59 ASP N N 121.6 0.30 1 601 . 60 LYS H H 7.66 0.03 1 602 . 60 LYS HA H 3.98 0.03 1 603 . 60 LYS HB2 H 1.32 0.03 2 604 . 60 LYS HG2 H 1.04 0.03 2 605 . 60 LYS HG3 H 1.00 0.03 2 606 . 60 LYS HD2 H 1.38 0.03 2 607 . 60 LYS HE2 H 2.75 0.03 2 608 . 60 LYS C C 174.0 0.50 1 609 . 60 LYS CA C 54.3 0.50 1 610 . 60 LYS CB C 30.3 0.50 1 611 . 60 LYS CG C 22.2 0.50 1 612 . 60 LYS CD C 26.4 0.50 1 613 . 60 LYS CE C 39.9 0.50 1 614 . 60 LYS N N 118.6 0.30 1 615 . 61 TYR H H 7.72 0.03 1 616 . 61 TYR HA H 4.21 0.03 1 617 . 61 TYR HB2 H 2.62 0.03 2 618 . 61 TYR HB3 H 2.52 0.03 2 619 . 61 TYR HD1 H 6.54 0.03 3 620 . 61 TYR HE1 H 6.31 0.03 3 621 . 61 TYR C C 172.5 0.50 1 622 . 61 TYR CA C 55.3 0.50 1 623 . 61 TYR CB C 36.2 0.50 1 624 . 61 TYR N N 121.3 0.30 1 625 . 62 ASP H H 7.97 0.03 1 626 . 62 ASP HA H 4.68 0.03 1 627 . 62 ASP HB2 H 2.77 0.03 2 628 . 62 ASP HB3 H 2.62 0.03 2 629 . 62 ASP C C 174.7 0.50 1 630 . 62 ASP CA C 51.2 0.50 1 631 . 62 ASP CB C 40.5 0.50 1 632 . 62 ASP N N 123.6 0.30 1 633 . 63 GLY H H 8.87 0.03 1 634 . 63 GLY HA2 H 3.93 0.03 2 635 . 63 GLY HA3 H 4.22 0.03 2 636 . 63 GLY C C 174.5 0.50 1 637 . 63 GLY CA C 46.6 0.50 1 638 . 63 GLY N N 111.6 0.30 1 639 . 64 ARG H H 8.24 0.03 1 640 . 64 ARG HA H 4.29 0.03 1 641 . 64 ARG HB2 H 2.07 0.03 2 642 . 64 ARG HG2 H 1.89 0.03 2 643 . 64 ARG HG3 H 1.75 0.03 2 644 . 64 ARG HD2 H 3.31 0.03 2 645 . 64 ARG C C 177.5 0.50 1 646 . 64 ARG CA C 58.0 0.50 1 647 . 64 ARG CB C 27.6 0.50 1 648 . 64 ARG CG C 24.9 0.50 1 649 . 64 ARG CD C 41.4 0.50 1 650 . 64 ARG N N 121.2 0.30 1 651 . 65 TYR H H 7.89 0.03 1 652 . 65 TYR HA H 4.60 0.03 1 653 . 65 TYR HB2 H 2.91 0.03 1 654 . 65 TYR HB3 H 3.09 0.03 1 655 . 65 TYR HD1 H 6.66 0.03 3 656 . 65 TYR HE1 H 5.66 0.03 3 657 . 65 TYR C C 176.5 0.50 1 658 . 65 TYR CA C 56.9 0.50 1 659 . 65 TYR CB C 36.0 0.50 1 660 . 65 TYR CD1 C 131.2 0.50 3 661 . 65 TYR CE1 C 115.2 0.50 3 662 . 65 TYR N N 120.1 0.30 1 663 . 66 MET H H 8.62 0.03 1 664 . 66 MET HA H 5.82 0.03 1 665 . 66 MET HB2 H 3.97 0.03 2 666 . 66 MET HB3 H 3.36 0.03 2 667 . 66 MET HG2 H 3.34 0.03 2 668 . 66 MET HG3 H 2.71 0.03 2 669 . 66 MET HE H 0.45 0.03 1 670 . 66 MET C C 179.9 0.50 1 671 . 66 MET CA C 57.7 0.50 1 672 . 66 MET CB C 34.6 0.50 1 673 . 66 MET CG C 31.7 0.50 1 674 . 66 MET CE C 17.5 0.50 1 675 . 66 MET N N 116.1 0.30 1 676 . 67 ARG H H 9.25 0.03 1 677 . 67 ARG HA H 6.18 0.03 1 678 . 67 ARG HB2 H 2.68 0.03 2 679 . 67 ARG HB3 H 2.74 0.03 2 680 . 67 ARG HG2 H 2.61 0.03 2 681 . 67 ARG HD2 H 3.76 0.03 2 682 . 67 ARG HD3 H 3.60 0.03 2 683 . 67 ARG HE H 7.96 0.03 1 684 . 67 ARG C C 179.3 0.50 1 685 . 67 ARG CA C 58.5 0.50 1 686 . 67 ARG CB C 30.1 0.50 1 687 . 67 ARG CG C 27.5 0.50 1 688 . 67 ARG CD C 41.9 0.50 1 689 . 67 ARG N N 122.7 0.30 1 690 . 67 ARG NE N 85.2 0.30 1 691 . 68 GLU H H 8.98 0.03 1 692 . 68 GLU HA H 4.47 0.03 1 693 . 68 GLU HB2 H 2.36 0.03 2 694 . 68 GLU HB3 H 2.25 0.03 2 695 . 68 GLU HG2 H 2.58 0.03 2 696 . 68 GLU HG3 H 2.50 0.03 2 697 . 68 GLU C C 178.5 0.50 1 698 . 68 GLU CA C 58.3 0.50 1 699 . 68 GLU CB C 27.7 0.50 1 700 . 68 GLU CG C 34.0 0.50 1 701 . 68 GLU N N 119.9 0.30 1 702 . 69 ALA H H 9.62 0.03 1 703 . 69 ALA HA H 3.46 0.03 1 704 . 69 ALA HB H -0.48 0.03 1 705 . 69 ALA C C 178.0 0.50 1 706 . 69 ALA CA C 52.5 0.50 1 707 . 69 ALA CB C 14.5 0.50 1 708 . 69 ALA N N 118.1 0.30 1 709 . 70 HIS H H 9.90 0.03 1 710 . 70 HIS HA H 6.75 0.03 1 711 . 70 HIS HB2 H 8.92 0.03 1 712 . 70 HIS HB3 H 9.62 0.03 1 713 . 70 HIS HD1 H 15.00 0.03 1 714 . 70 HIS C C 173.1 0.50 1 715 . 70 HIS CA C 69.1 0.50 1 716 . 70 HIS CB C 23.8 0.50 1 717 . 70 HIS N N 113.0 0.30 1 718 . 70 HIS ND1 N 133.8 0.30 1 719 . 71 LYS H H 8.57 0.03 1 720 . 71 LYS HA H 4.86 0.03 1 721 . 71 LYS HB2 H 2.79 0.03 2 722 . 71 LYS HB3 H 2.31 0.03 2 723 . 71 LYS HG2 H 1.79 0.03 2 724 . 71 LYS HG3 H 1.68 0.03 2 725 . 71 LYS HD2 H 2.00 0.03 2 726 . 71 LYS HD3 H 1.97 0.03 2 727 . 71 LYS HE2 H 2.66 0.03 2 728 . 71 LYS HE3 H 3.22 0.03 2 729 . 71 LYS C C 176.7 0.50 1 730 . 71 LYS CA C 60.1 0.50 1 731 . 71 LYS CB C 31.5 0.50 1 732 . 71 LYS CG C 22.9 0.50 1 733 . 71 LYS CD C 28.4 0.50 1 734 . 71 LYS CE C 40.2 0.50 1 735 . 71 LYS N N 125.2 0.30 1 736 . 72 GLU H H 8.92 0.03 1 737 . 72 GLU HA H 4.25 0.03 1 738 . 72 GLU HB2 H 2.03 0.03 2 739 . 72 GLU HB3 H 2.00 0.03 2 740 . 72 GLU HG2 H 2.26 0.03 2 741 . 72 GLU C C 178.3 0.50 1 742 . 72 GLU CA C 58.0 0.50 1 743 . 72 GLU CB C 27.2 0.50 1 744 . 72 GLU CG C 35.0 0.50 1 745 . 72 GLU N N 118.4 0.30 1 746 . 73 LEU H H 7.79 0.03 1 747 . 73 LEU HA H 3.98 0.03 1 748 . 73 LEU HB2 H 2.34 0.03 1 749 . 73 LEU HB3 H 0.84 0.03 1 750 . 73 LEU HG H 1.44 0.03 1 751 . 73 LEU HD1 H -1.14 0.03 1 752 . 73 LEU HD2 H -0.16 0.03 1 753 . 73 LEU C C 178.9 0.50 1 754 . 73 LEU CA C 55.6 0.50 1 755 . 73 LEU CB C 41.3 0.50 1 756 . 73 LEU CG C 23.5 0.50 1 757 . 73 LEU CD1 C 24.4 0.50 1 758 . 73 LEU CD2 C 21.1 0.50 1 759 . 73 LEU N N 118.4 0.30 1 760 . 74 VAL H H 8.50 0.03 1 761 . 74 VAL HA H 3.96 0.03 1 762 . 74 VAL HB H 2.80 0.03 1 763 . 74 VAL HG1 H 1.38 0.03 1 764 . 74 VAL HG2 H 1.90 0.03 1 765 . 74 VAL C C 177.0 0.50 1 766 . 74 VAL CA C 64.8 0.50 1 767 . 74 VAL CB C 31.1 0.50 1 768 . 74 VAL CG1 C 19.4 0.50 1 769 . 74 VAL CG2 C 22.3 0.50 1 770 . 74 VAL N N 120.6 0.30 1 771 . 75 GLU H H 8.88 0.03 1 772 . 75 GLU HA H 4.17 0.03 1 773 . 75 GLU HB2 H 2.08 0.03 2 774 . 75 GLU HB3 H 1.96 0.03 2 775 . 75 GLU HG2 H 2.63 0.03 2 776 . 75 GLU HG3 H 2.36 0.03 2 777 . 75 GLU C C 177.0 0.50 1 778 . 75 GLU CA C 57.9 0.50 1 779 . 75 GLU CB C 28.5 0.50 1 780 . 75 GLU CG C 34.5 0.50 1 781 . 75 GLU N N 116.7 0.30 1 782 . 76 ASN H H 8.42 0.03 1 783 . 76 ASN HA H 4.95 0.03 1 784 . 76 ASN HB2 H 2.53 0.03 1 785 . 76 ASN HB3 H 2.33 0.03 1 786 . 76 ASN HD21 H 7.00 0.03 2 787 . 76 ASN HD22 H 7.75 0.03 2 788 . 76 ASN C C 174.5 0.50 1 789 . 76 ASN CA C 51.7 0.50 1 790 . 76 ASN CB C 38.5 0.50 1 791 . 76 ASN N N 111.0 0.30 1 792 . 76 ASN ND2 N 113.3 0.30 1 793 . 77 HIS H H 7.21 0.03 1 794 . 77 HIS HA H 4.88 0.03 1 795 . 77 HIS HB2 H 3.04 0.03 1 796 . 77 HIS HB3 H 3.36 0.03 1 797 . 77 HIS HD2 H 6.94 0.03 1 798 . 77 HIS HE1 H 8.02 0.03 1 799 . 77 HIS C C 173.9 0.50 1 800 . 77 HIS CA C 53.6 0.50 1 801 . 77 HIS CB C 29.4 0.50 1 802 . 77 HIS N N 114.4 0.30 1 803 . 78 GLY H H 7.89 0.03 1 804 . 78 GLY HA2 H 3.91 0.03 2 805 . 78 GLY HA3 H 3.88 0.03 2 806 . 78 GLY C C 173.1 0.50 1 807 . 78 GLY CA C 45.3 0.50 1 808 . 78 GLY N N 107.3 0.30 1 809 . 79 LEU H H 7.35 0.03 1 810 . 79 LEU HA H 4.30 0.03 1 811 . 79 LEU HB2 H 0.36 0.03 1 812 . 79 LEU HB3 H 1.46 0.03 1 813 . 79 LEU HG H 1.09 0.03 1 814 . 79 LEU HD1 H -1.08 0.03 1 815 . 79 LEU HD2 H 0.66 0.03 1 816 . 79 LEU C C 175.2 0.50 1 817 . 79 LEU CA C 54.4 0.50 1 818 . 79 LEU CB C 39.5 0.50 1 819 . 79 LEU CG C 24.2 0.50 1 820 . 79 LEU CD1 C 23.5 0.50 1 821 . 79 LEU CD2 C 23.6 0.50 1 822 . 79 LEU N N 119.9 0.30 1 823 . 80 ASN H H 11.21 0.03 1 824 . 80 ASN HA H 4.98 0.03 1 825 . 80 ASN HB2 H 3.08 0.03 1 826 . 80 ASN HB3 H 2.79 0.03 1 827 . 80 ASN HD21 H 6.56 0.03 2 828 . 80 ASN HD22 H 7.28 0.03 2 829 . 80 ASN C C 174.7 0.50 1 830 . 80 ASN CA C 50.5 0.50 1 831 . 80 ASN CB C 38.6 0.50 1 832 . 80 ASN N N 130.4 0.30 1 833 . 80 ASN ND2 N 111.1 0.30 1 834 . 81 GLY H H 8.70 0.03 1 835 . 81 GLY HA2 H 3.87 0.03 2 836 . 81 GLY HA3 H 3.46 0.03 2 837 . 81 GLY C C 173.8 0.50 1 838 . 81 GLY CA C 46.1 0.50 1 839 . 81 GLY N N 104.7 0.30 1 840 . 82 GLU H H 8.07 0.03 1 841 . 82 GLU HA H 3.90 0.03 1 842 . 82 GLU HB2 H 1.76 0.03 2 843 . 82 GLU HB3 H 1.68 0.03 2 844 . 82 GLU HG2 H 1.95 0.03 2 845 . 82 GLU C C 178.6 0.50 1 846 . 82 GLU CA C 57.2 0.50 1 847 . 82 GLU CB C 26.7 0.50 1 848 . 82 GLU CG C 34.5 0.50 1 849 . 82 GLU N N 120.1 0.30 1 850 . 83 HIS H H 7.21 0.03 1 851 . 83 HIS HA H 3.59 0.03 1 852 . 83 HIS HB2 H 2.82 0.03 1 853 . 83 HIS HB3 H 1.92 0.03 1 854 . 83 HIS HD2 H 6.72 0.03 1 855 . 83 HIS HE1 H 7.78 0.03 1 856 . 83 HIS C C 175.5 0.50 1 857 . 83 HIS CA C 57.1 0.50 1 858 . 83 HIS CB C 29.8 0.50 1 859 . 83 HIS N N 120.6 0.30 1 860 . 84 PHE H H 7.02 0.03 1 861 . 84 PHE HA H 2.38 0.03 1 862 . 84 PHE HB2 H 3.17 0.03 1 863 . 84 PHE HB3 H 2.10 0.03 1 864 . 84 PHE HD1 H 6.74 0.03 3 865 . 84 PHE HE1 H 7.28 0.03 3 866 . 84 PHE HZ H 7.36 0.03 1 867 . 84 PHE C C 174.7 0.50 1 868 . 84 PHE CA C 58.8 0.50 1 869 . 84 PHE CB C 37.2 0.50 1 870 . 84 PHE N N 116.7 0.30 1 871 . 85 ASP H H 8.24 0.03 1 872 . 85 ASP HA H 4.02 0.03 1 873 . 85 ASP HB2 H 2.47 0.03 2 874 . 85 ASP C C 176.4 0.50 1 875 . 85 ASP CA C 55.1 0.50 1 876 . 85 ASP CB C 37.2 0.50 1 877 . 85 ASP N N 118.1 0.30 1 878 . 86 ALA H H 7.40 0.03 1 879 . 86 ALA HA H 3.70 0.03 1 880 . 86 ALA HB H 1.10 0.03 1 881 . 86 ALA C C 176.4 0.50 1 882 . 86 ALA CA C 53.9 0.50 1 883 . 86 ALA CB C 15.0 0.50 1 884 . 86 ALA N N 122.1 0.30 1 885 . 87 VAL H H 6.64 0.03 1 886 . 87 VAL HA H 2.71 0.03 1 887 . 87 VAL HB H 0.21 0.03 1 888 . 87 VAL HG1 H -1.33 0.03 1 889 . 87 VAL HG2 H -0.83 0.03 1 890 . 87 VAL C C 175.9 0.50 1 891 . 87 VAL CA C 64.5 0.50 1 892 . 87 VAL CB C 27.5 0.50 1 893 . 87 VAL CG1 C 17.2 0.50 1 894 . 87 VAL CG2 C 21.1 0.50 1 895 . 87 VAL N N 115.9 0.30 1 896 . 88 ALA H H 6.98 0.03 1 897 . 88 ALA HA H 3.47 0.03 1 898 . 88 ALA HB H 1.11 0.03 1 899 . 88 ALA C C 177.2 0.50 1 900 . 88 ALA CA C 53.6 0.50 1 901 . 88 ALA CB C 15.5 0.50 1 902 . 88 ALA N N 118.6 0.30 1 903 . 89 GLU H H 8.44 0.03 1 904 . 89 GLU HA H 3.64 0.03 1 905 . 89 GLU HB2 H 1.95 0.03 2 906 . 89 GLU HG2 H 2.25 0.03 2 907 . 89 GLU HG3 H 2.00 0.03 2 908 . 89 GLU C C 177.8 0.50 1 909 . 89 GLU CA C 57.4 0.50 1 910 . 89 GLU CB C 27.6 0.50 1 911 . 89 GLU CG C 33.8 0.50 1 912 . 89 GLU N N 118.9 0.30 1 913 . 90 ASP H H 8.21 0.03 1 914 . 90 ASP HA H 4.36 0.03 1 915 . 90 ASP HB2 H 3.12 0.03 1 916 . 90 ASP HB3 H 2.32 0.03 1 917 . 90 ASP C C 176.5 0.50 1 918 . 90 ASP CA C 53.9 0.50 1 919 . 90 ASP CB C 34.7 0.50 1 920 . 90 ASP N N 119.3 0.30 1 921 . 91 LEU H H 8.00 0.03 1 922 . 91 LEU HA H 3.40 0.03 1 923 . 91 LEU HB2 H 0.68 0.03 1 924 . 91 LEU HB3 H 1.82 0.03 1 925 . 91 LEU HG H 1.05 0.03 1 926 . 91 LEU HD1 H 0.35 0.03 1 927 . 91 LEU HD2 H 0.57 0.03 1 928 . 91 LEU C C 176.3 0.50 1 929 . 91 LEU CA C 56.4 0.50 1 930 . 91 LEU CB C 37.3 0.50 1 931 . 91 LEU CG C 25.5 0.50 1 932 . 91 LEU CD1 C 20.3 0.50 1 933 . 91 LEU CD2 C 24.5 0.50 1 934 . 91 LEU N N 124.9 0.30 1 935 . 92 LEU H H 8.23 0.03 1 936 . 92 LEU HA H 3.67 0.03 1 937 . 92 LEU HB2 H 1.80 0.03 1 938 . 92 LEU HB3 H 1.32 0.03 1 939 . 92 LEU HG H 1.76 0.03 1 940 . 92 LEU HD1 H 0.74 0.03 2 941 . 92 LEU HD2 H 0.60 0.03 2 942 . 92 LEU C C 177.8 0.50 1 943 . 92 LEU CA C 56.8 0.50 1 944 . 92 LEU CB C 38.1 0.50 1 945 . 92 LEU CG C 24.3 0.50 1 946 . 92 LEU CD1 C 22.7 0.50 2 947 . 92 LEU CD2 C 22.2 0.50 2 948 . 92 LEU N N 120.1 0.30 1 949 . 93 ALA H H 8.60 0.03 1 950 . 93 ALA HA H 4.03 0.03 1 951 . 93 ALA HB H 1.43 0.03 1 952 . 93 ALA C C 179.2 0.50 1 953 . 93 ALA CA C 53.2 0.50 1 954 . 93 ALA CB C 16.2 0.50 1 955 . 93 ALA N N 120.4 0.30 1 956 . 94 THR H H 7.51 0.03 1 957 . 94 THR HA H 3.92 0.03 1 958 . 94 THR HB H 4.56 0.03 1 959 . 94 THR HG2 H 1.35 0.03 1 960 . 94 THR C C 174.4 0.50 1 961 . 94 THR CA C 65.6 0.50 1 962 . 94 THR CB C 67.0 0.50 1 963 . 94 THR CG2 C 18.8 0.50 1 964 . 94 THR N N 116.4 0.30 1 965 . 95 LEU H H 8.01 0.03 1 966 . 95 LEU HA H 4.00 0.03 1 967 . 95 LEU HB2 H 1.90 0.03 1 968 . 95 LEU HB3 H 1.13 0.03 1 969 . 95 LEU HG H 2.02 0.03 1 970 . 95 LEU HD1 H 0.79 0.03 1 971 . 95 LEU HD2 H 0.88 0.03 1 972 . 95 LEU C C 177.3 0.50 1 973 . 95 LEU CA C 55.9 0.50 1 974 . 95 LEU CB C 38.6 0.50 1 975 . 95 LEU CG C 23.9 0.50 1 976 . 95 LEU CD1 C 25.0 0.50 1 977 . 95 LEU CD2 C 19.3 0.50 1 978 . 95 LEU N N 119.1 0.30 1 979 . 96 LYS H H 8.17 0.03 1 980 . 96 LYS HA H 3.97 0.03 1 981 . 96 LYS HB2 H 1.88 0.03 2 982 . 96 LYS HB3 H 1.80 0.03 2 983 . 96 LYS HG2 H 1.47 0.03 2 984 . 96 LYS HG3 H 1.39 0.03 2 985 . 96 LYS HD2 H 1.62 0.03 2 986 . 96 LYS HE2 H 2.89 0.03 2 987 . 96 LYS C C 179.2 0.50 1 988 . 96 LYS CA C 57.8 0.50 1 989 . 96 LYS CB C 30.2 0.50 1 990 . 96 LYS CG C 22.6 0.50 1 991 . 96 LYS CE C 39.5 0.50 1 992 . 96 LYS N N 119.3 0.30 1 993 . 97 GLU H H 7.95 0.03 1 994 . 97 GLU HA H 4.04 0.03 1 995 . 97 GLU HB2 H 2.20 0.03 2 996 . 97 GLU HG2 H 2.30 0.03 2 997 . 97 GLU C C 176.8 0.50 1 998 . 97 GLU CA C 57.3 0.50 1 999 . 97 GLU CB C 27.4 0.50 1 1000 . 97 GLU CG C 34.9 0.50 1 1001 . 97 GLU N N 121.4 0.30 1 1002 . 98 MET H H 7.74 0.03 1 1003 . 98 MET HA H 4.27 0.03 1 1004 . 98 MET HB2 H 2.14 0.03 1 1005 . 98 MET HB3 H 2.40 0.03 1 1006 . 98 MET HG2 H 2.68 0.03 2 1007 . 98 MET HG3 H 2.60 0.03 2 1008 . 98 MET HE H 2.10 0.03 1 1009 . 98 MET C C 175.0 0.50 1 1010 . 98 MET CA C 54.9 0.50 1 1011 . 98 MET CB C 32.5 0.50 1 1012 . 98 MET CG C 30.2 0.50 1 1013 . 98 MET CE C 14.3 0.50 1 1014 . 98 MET N N 115.8 0.30 1 1015 . 99 GLY H H 7.86 0.03 1 1016 . 99 GLY HA2 H 3.79 0.03 2 1017 . 99 GLY HA3 H 3.98 0.03 2 1018 . 99 GLY C C 173.3 0.50 1 1019 . 99 GLY CA C 44.0 0.50 1 1020 . 99 GLY N N 107.3 0.30 1 1021 . 100 VAL H H 7.45 0.03 1 1022 . 100 VAL HA H 4.12 0.03 1 1023 . 100 VAL HB H 1.77 0.03 1 1024 . 100 VAL HG1 H 1.01 0.03 1 1025 . 100 VAL HG2 H 1.01 0.03 1 1026 . 100 VAL C C 171.7 0.50 1 1027 . 100 VAL CA C 59.2 0.50 1 1028 . 100 VAL CB C 29.2 0.50 1 1029 . 100 VAL CG1 C 19.5 0.50 2 1030 . 100 VAL CG2 C 20.2 0.50 2 1031 . 100 VAL N N 121.3 0.30 1 1032 . 101 PRO HA H 4.36 0.03 1 1033 . 101 PRO HB2 H 2.03 0.03 1 1034 . 101 PRO HB3 H 2.45 0.03 1 1035 . 101 PRO HG2 H 2.09 0.03 2 1036 . 101 PRO HD2 H 3.59 0.03 1 1037 . 101 PRO HD3 H 3.96 0.03 1 1038 . 101 PRO C C 176.4 0.50 1 1039 . 101 PRO CA C 61.6 0.50 1 1040 . 101 PRO CB C 31.0 0.50 1 1041 . 101 PRO CG C 25.6 0.50 1 1042 . 101 PRO CD C 48.9 0.50 1 1043 . 102 GLU H H 8.81 0.03 1 1044 . 102 GLU HA H 3.73 0.03 1 1045 . 102 GLU HB2 H 2.02 0.03 2 1046 . 102 GLU HG2 H 2.28 0.03 2 1047 . 102 GLU C C 176.7 0.50 1 1048 . 102 GLU CA C 58.1 0.50 1 1049 . 102 GLU CB C 27.7 0.50 1 1050 . 102 GLU CG C 34.7 0.50 1 1051 . 102 GLU N N 121.8 0.30 1 1052 . 103 ASP H H 8.92 0.03 1 1053 . 103 ASP HA H 4.25 0.03 1 1054 . 103 ASP HB2 H 2.58 0.03 2 1055 . 103 ASP HB3 H 2.47 0.03 2 1056 . 103 ASP C C 176.8 0.50 1 1057 . 103 ASP CA C 54.6 0.50 1 1058 . 103 ASP CB C 36.6 0.50 1 1059 . 103 ASP N N 117.4 0.30 1 1060 . 104 LEU H H 7.22 0.03 1 1061 . 104 LEU HA H 4.18 0.03 1 1062 . 104 LEU HB2 H 1.60 0.03 2 1063 . 104 LEU HB3 H 1.54 0.03 2 1064 . 104 LEU HG H 1.51 0.03 1 1065 . 104 LEU HD1 H 0.85 0.03 1 1066 . 104 LEU HD2 H 0.79 0.03 1 1067 . 104 LEU C C 177.1 0.50 1 1068 . 104 LEU CA C 55.3 0.50 1 1069 . 104 LEU CB C 39.1 0.50 1 1070 . 104 LEU CG C 25.2 0.50 1 1071 . 104 LEU CD1 C 22.9 0.50 1 1072 . 104 LEU CD2 C 22.5 0.50 1 1073 . 104 LEU N N 122.1 0.30 1 1074 . 105 ILE H H 7.72 0.03 1 1075 . 105 ILE HA H 3.15 0.03 1 1076 . 105 ILE HB H 1.82 0.03 1 1077 . 105 ILE HG12 H 0.59 0.03 1 1078 . 105 ILE HG13 H 1.62 0.03 1 1079 . 105 ILE HG2 H 0.82 0.03 1 1080 . 105 ILE HD1 H 0.66 0.03 1 1081 . 105 ILE C C 175.7 0.50 1 1082 . 105 ILE CA C 64.5 0.50 1 1083 . 105 ILE CB C 34.7 0.50 1 1084 . 105 ILE CG1 C 26.9 0.50 1 1085 . 105 ILE CG2 C 16.0 0.50 1 1086 . 105 ILE CD1 C 11.6 0.50 1 1087 . 105 ILE N N 119.1 0.30 1 1088 . 106 ALA H H 7.85 0.03 1 1089 . 106 ALA HA H 3.98 0.03 1 1090 . 106 ALA HB H 1.35 0.03 1 1091 . 106 ALA C C 179.3 0.50 1 1092 . 106 ALA CA C 53.2 0.50 1 1093 . 106 ALA CB C 15.6 0.50 1 1094 . 106 ALA N N 118.6 0.30 1 1095 . 107 GLU H H 7.31 0.03 1 1096 . 107 GLU HA H 3.96 0.03 1 1097 . 107 GLU HB2 H 2.03 0.03 2 1098 . 107 GLU HG2 H 2.38 0.03 2 1099 . 107 GLU HG3 H 2.10 0.03 2 1100 . 107 GLU C C 177.7 0.50 1 1101 . 107 GLU CA C 57.8 0.50 1 1102 . 107 GLU CB C 27.5 0.50 1 1103 . 107 GLU CG C 34.0 0.50 1 1104 . 107 GLU N N 119.0 0.30 1 1105 . 108 VAL H H 7.85 0.03 1 1106 . 108 VAL HA H 3.50 0.03 1 1107 . 108 VAL HB H 1.79 0.03 1 1108 . 108 VAL HG1 H 0.44 0.03 1 1109 . 108 VAL HG2 H 0.24 0.03 1 1110 . 108 VAL C C 176.7 0.50 1 1111 . 108 VAL CA C 63.4 0.50 1 1112 . 108 VAL CB C 28.9 0.50 1 1113 . 108 VAL CG1 C 19.3 0.50 1 1114 . 108 VAL CG2 C 19.8 0.50 1 1115 . 108 VAL N N 120.7 0.30 1 1116 . 109 ALA H H 8.75 0.03 1 1117 . 109 ALA HA H 3.72 0.03 1 1118 . 109 ALA HB H 1.36 0.03 1 1119 . 109 ALA C C 179.0 0.50 1 1120 . 109 ALA CA C 53.4 0.50 1 1121 . 109 ALA CB C 16.4 0.50 1 1122 . 109 ALA N N 121.3 0.30 1 1123 . 110 ALA H H 7.35 0.03 1 1124 . 110 ALA HA H 4.04 0.03 1 1125 . 110 ALA HB H 1.44 0.03 1 1126 . 110 ALA C C 178.4 0.50 1 1127 . 110 ALA CA C 52.5 0.50 1 1128 . 110 ALA CB C 16.3 0.50 1 1129 . 110 ALA N N 118.4 0.30 1 1130 . 111 VAL H H 7.37 0.03 1 1131 . 111 VAL HA H 3.64 0.03 1 1132 . 111 VAL HB H 2.15 0.03 1 1133 . 111 VAL HG1 H 0.44 0.03 1 1134 . 111 VAL HG2 H 0.84 0.03 1 1135 . 111 VAL C C 176.8 0.50 1 1136 . 111 VAL CA C 63.9 0.50 1 1137 . 111 VAL CB C 29.6 0.50 1 1138 . 111 VAL CG1 C 19.8 0.50 1 1139 . 111 VAL CG2 C 20.1 0.50 1 1140 . 111 VAL N N 118.7 0.30 1 1141 . 112 ALA H H 8.77 0.03 1 1142 . 112 ALA HA H 3.74 0.03 1 1143 . 112 ALA HB H 1.10 0.03 1 1144 . 112 ALA C C 176.9 0.50 1 1145 . 112 ALA CA C 52.9 0.50 1 1146 . 112 ALA CB C 15.5 0.50 1 1147 . 112 ALA N N 119.3 0.30 1 1148 . 113 GLY H H 7.53 0.03 1 1149 . 113 GLY HA2 H 4.26 0.03 2 1150 . 113 GLY HA3 H 3.54 0.03 2 1151 . 113 GLY C C 172.4 0.50 1 1152 . 113 GLY CA C 42.7 0.50 1 1153 . 113 GLY N N 99.3 0.30 1 1154 . 114 ALA H H 7.18 0.03 1 1155 . 114 ALA HA H 4.40 0.03 1 1156 . 114 ALA HB H 1.36 0.03 1 1157 . 114 ALA C C 176.1 0.50 1 1158 . 114 ALA CA C 49.2 0.50 1 1159 . 114 ALA CB C 15.0 0.50 1 1160 . 114 ALA N N 125.3 0.30 1 1161 . 115 PRO HA H 4.08 0.03 1 1162 . 115 PRO HB2 H 1.93 0.03 1 1163 . 115 PRO HB3 H 2.34 0.03 1 1164 . 115 PRO HG2 H 2.09 0.03 2 1165 . 115 PRO HG3 H 2.03 0.03 2 1166 . 115 PRO HD2 H 3.78 0.03 2 1167 . 115 PRO HD3 H 3.97 0.03 2 1168 . 115 PRO CA C 63.9 0.50 1 1169 . 115 PRO CB C 30.2 0.50 1 1170 . 115 PRO CG C 25.1 0.50 1 1171 . 115 PRO CD C 49.2 0.50 1 1172 . 116 ALA H H 8.51 0.03 1 1173 . 116 ALA HA H 4.08 0.03 1 1174 . 116 ALA HB H 1.37 0.03 1 1175 . 116 ALA C C 177.8 0.50 1 1176 . 116 ALA CA C 53.8 0.50 1 1177 . 116 ALA CB C 16.2 0.50 1 1178 . 116 ALA N N 119.1 0.30 1 1179 . 117 HIS H H 7.38 0.03 1 1180 . 117 HIS HA H 5.04 0.03 1 1181 . 117 HIS HB2 H 3.40 0.03 2 1182 . 117 HIS HD2 H 6.79 0.03 1 1183 . 117 HIS HE1 H 7.78 0.03 1 1184 . 117 HIS C C 176.1 0.50 1 1185 . 117 HIS CA C 56.0 0.50 1 1186 . 117 HIS CB C 28.6 0.50 1 1187 . 117 HIS N N 115.4 0.30 1 1188 . 118 LYS H H 7.33 0.03 1 1189 . 118 LYS HA H 3.51 0.03 1 1190 . 118 LYS HB2 H 1.43 0.03 1 1191 . 118 LYS HB3 H 1.05 0.03 1 1192 . 118 LYS HG2 H 0.47 0.03 2 1193 . 118 LYS HG3 H 0.03 0.03 2 1194 . 118 LYS HD2 H 1.15 0.03 2 1195 . 118 LYS HD3 H 1.29 0.03 2 1196 . 118 LYS HE2 H 2.62 0.03 2 1197 . 118 LYS HE3 H 2.41 0.03 2 1198 . 118 LYS C C 175.9 0.50 1 1199 . 118 LYS CA C 57.3 0.50 1 1200 . 118 LYS CB C 30.8 0.50 1 1201 . 118 LYS CG C 22.5 0.50 1 1202 . 118 LYS CD C 27.9 0.50 1 1203 . 118 LYS CE C 39.9 0.50 1 1204 . 118 LYS N N 119.0 0.30 1 1205 . 119 ARG H H 7.76 0.03 1 1206 . 119 ARG HA H 4.10 0.03 1 1207 . 119 ARG HB2 H 2.02 0.03 2 1208 . 119 ARG HG2 H 1.89 0.03 2 1209 . 119 ARG HG3 H 1.66 0.03 2 1210 . 119 ARG HD2 H 3.20 0.03 2 1211 . 119 ARG C C 176.6 0.50 1 1212 . 119 ARG CA C 58.1 0.50 1 1213 . 119 ARG CB C 28.7 0.50 1 1214 . 119 ARG CG C 25.8 0.50 1 1215 . 119 ARG CD C 41.5 0.50 1 1216 . 119 ARG N N 115.5 0.30 1 1217 . 120 ASP H H 7.96 0.03 1 1218 . 120 ASP HA H 5.26 0.03 1 1219 . 120 ASP HB2 H 3.65 0.03 2 1220 . 120 ASP HB3 H 3.54 0.03 2 1221 . 120 ASP C C 178.2 0.50 1 1222 . 120 ASP CA C 56.6 0.50 1 1223 . 120 ASP CB C 39.5 0.50 1 1224 . 120 ASP N N 117.2 0.30 1 1225 . 121 VAL H H 9.07 0.03 1 1226 . 121 VAL HA H 6.95 0.03 1 1227 . 121 VAL HB H 3.39 0.03 1 1228 . 121 VAL HG1 H 3.46 0.03 2 1229 . 121 VAL HG2 H 3.64 0.03 2 1230 . 121 VAL C C 176.2 0.50 1 1231 . 121 VAL CA C 68.2 0.50 1 1232 . 121 VAL CB C 31.7 0.50 1 1233 . 121 VAL CG1 C 22.1 0.50 2 1234 . 121 VAL CG2 C 25.7 0.50 2 1235 . 121 VAL N N 121.4 0.30 1 1236 . 122 LEU H H 8.47 0.03 1 1237 . 122 LEU HA H 4.99 0.03 1 1238 . 122 LEU HB2 H 1.95 0.03 2 1239 . 122 LEU HB3 H 1.93 0.03 2 1240 . 122 LEU HG H 2.11 0.03 1 1241 . 122 LEU HD1 H 0.73 0.03 2 1242 . 122 LEU HD2 H 0.80 0.03 2 1243 . 122 LEU C C 175.1 0.50 1 1244 . 122 LEU CA C 53.2 0.50 1 1245 . 122 LEU CB C 38.6 0.50 1 1246 . 122 LEU CG C 24.4 0.50 1 1247 . 122 LEU CD1 C 23.6 0.50 2 1248 . 122 LEU CD2 C 19.7 0.50 2 1249 . 122 LEU N N 110.9 0.30 1 1250 . 123 ASN H H 9.26 0.03 1 1251 . 123 ASN HA H 4.76 0.03 1 1252 . 123 ASN HB2 H 3.70 0.03 2 1253 . 123 ASN HB3 H 3.60 0.03 2 1254 . 123 ASN HD21 H 8.02 0.03 2 1255 . 123 ASN HD22 H 8.65 0.03 2 1256 . 123 ASN C C 173.0 0.50 1 1257 . 123 ASN CA C 53.2 0.50 1 1258 . 123 ASN CB C 35.8 0.50 1 1259 . 123 ASN N N 117.8 0.30 1 1260 . 123 ASN ND2 N 110.4 0.30 1 1261 . 124 GLN H H 8.98 0.03 1 1262 . 124 GLN HA H 4.40 0.03 1 1263 . 124 GLN HB2 H 2.02 0.03 1 1264 . 124 GLN HB3 H 2.37 0.03 1 1265 . 124 GLN HG2 H 2.51 0.03 2 1266 . 124 GLN HE21 H 6.69 0.03 2 1267 . 124 GLN HE22 H 7.65 0.03 2 1268 . 124 GLN C C 179.9 0.50 1 1269 . 124 GLN CA C 55.3 0.50 1 1270 . 124 GLN CB C 28.6 0.50 1 1271 . 124 GLN CG C 32.7 0.50 1 1272 . 124 GLN N N 122.1 0.30 1 1273 . 124 GLN NE2 N 110.3 0.30 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts in this section were published in: Lecomte, J.T.J., Scott, N.L., Vu, B.C., and Falzone, C.J., "Binding of Ferric Heme by the Recombinant Globin From the Cyanobacterium Synechocystis sp. PCC 6803." Biochemistry 40, 6541-6552, (2001) ; loop_ _Experiment_label 2QF-COSY TOCSY NOESY 1H-15N-NOESY 1H-15N-TOCSY HNCA HN(CA)CO HNCO HCCH-TOCSY HCCH-COSY CBCA(CO)NH CBCANH '1H-13C HSQC-NOESY' HCC(CO)NH '1H-15N HMQC' '1H-13C HMQC' stop_ _Sample_conditions_label $ex-cond_3 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Heme _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 HEM HAB H 15.54 0.05 1 2 . 1 HEM HAC H 6.84 0.05 1 3 . 1 HEM HBB H -4.54 0.05 1 4 . 1 HEM HBBA H -5.15 0.05 1 5 . 1 HEM HBC H -1.67 0.05 1 6 . 1 HEM HBCA H -2.14 0.05 1 7 . 1 HEM HMA H 10.37 0.05 1 8 . 1 HEM HMB H 15.07 0.05 1 9 . 1 HEM HMC H 9.98 0.05 1 10 . 1 HEM HMD H 21.27 0.05 1 stop_ save_