data_6026 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments for Oxidized Human Ferredoxin ; _BMRB_accession_number 6026 _BMRB_flat_file_name bmr6026.str _Entry_type original _Submission_date 2003-12-01 _Accession_date 2003-12-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; 1H and 13C Chemical Shift Assignments for Sidechains in the Diamagnetic Region; 1H, 13C, and 15N Assignments for the Paramagnetic Loops. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Machonkin Timothy E. . 2 Westler William M. . 3 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 449 "13C chemical shifts" 401 "15N chemical shifts" 16 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-30 original author . stop_ _Original_release_date 2004-07-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates by NMR Spectroscopy: Application to Oxidized Human [2Fe-2S] Ferredoxin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15113213 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Machonkin Timothy E. . 2 Westler William M. . 3 Markley John L. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 126 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5413 _Page_last 5426 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_Ferredoxin _Saveframe_category molecular_system _Mol_system_name 'Oxidized Human Ferredoxin' _Abbreviation_common Ferredoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ferredoxin $Ferredoxin '[2Fe-2S] cluster' $FES stop_ _System_molecular_weight 13000 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'free and other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ferredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Oxidized Human Ferredoxin' _Abbreviation_common Ferredoxin _Molecular_mass . _Mol_thiol_state 'free and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; SSSEDKITVHFINRDGETLT TKGKVGDSLLDVVVENNLDI DGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDL AYGLTDRSRLGCQICLTKSM DNMTVRVPETVADARQSIDV GKTS ; loop_ _Residue_seq_code _Residue_label 1 SER 2 SER 3 SER 4 GLU 5 ASP 6 LYS 7 ILE 8 THR 9 VAL 10 HIS 11 PHE 12 ILE 13 ASN 14 ARG 15 ASP 16 GLY 17 GLU 18 THR 19 LEU 20 THR 21 THR 22 LYS 23 GLY 24 LYS 25 VAL 26 GLY 27 ASP 28 SER 29 LEU 30 LEU 31 ASP 32 VAL 33 VAL 34 VAL 35 GLU 36 ASN 37 ASN 38 LEU 39 ASP 40 ILE 41 ASP 42 GLY 43 PHE 44 GLY 45 ALA 46 CYS 47 GLU 48 GLY 49 THR 50 LEU 51 ALA 52 CYS 53 SER 54 THR 55 CYS 56 HIS 57 LEU 58 ILE 59 PHE 60 GLU 61 ASP 62 HIS 63 ILE 64 TYR 65 GLU 66 LYS 67 LEU 68 ASP 69 ALA 70 ILE 71 THR 72 ASP 73 GLU 74 GLU 75 ASN 76 ASP 77 MET 78 LEU 79 ASP 80 LEU 81 ALA 82 TYR 83 GLY 84 LEU 85 THR 86 ASP 87 ARG 88 SER 89 ARG 90 LEU 91 GLY 92 CYS 93 GLN 94 ILE 95 CYS 96 LEU 97 THR 98 LYS 99 SER 100 MET 101 ASP 102 ASN 103 MET 104 THR 105 VAL 106 ARG 107 VAL 108 PRO 109 GLU 110 THR 111 VAL 112 ALA 113 ASP 114 ALA 115 ARG 116 GLN 117 SER 118 ILE 119 ASP 120 VAL 121 GLY 122 LYS 123 THR 124 SER 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 REF XP_508877 'PREDICT: similar to Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin) [Pan troglodytes]' 98.39 253 100.00 100.00 2.28e-66 SWISS-PROT P10109 'Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin)' 100.00 184 100.00 100.00 9.33e-67 REF NP_004100 'ferredoxin 1 precursor [Homo sapiens]' 100.00 184 100.00 100.00 9.33e-67 REF XP_001105034 'PREDICTED: similar to Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin) [Macaca mulatta]' 100.00 184 99.19 100.00 2.40e-66 GenBank AAA50462 adrenodoxin 100.00 184 100.00 100.00 9.33e-67 GenBank AAA76853 ferredoxin 100.00 184 100.00 100.00 9.33e-67 GenBank AAA35855 ferredoxin 64.52 80 100.00 100.00 7.45e-40 GenBank AAA35856 ferredoxin 64.52 80 100.00 100.00 7.45e-40 BMRB 5337 'human adrenodoxin' 89.52 111 99.10 100.00 1.76e-57 GenBank AAA35829 ferredoxin 100.00 184 100.00 100.00 9.33e-67 BMRB 4439 'Human Ferredoxin' 100.00 124 100.00 100.00 1.78e-65 BMRB 4440 'Human Ferredoxin' 100.00 124 100.00 100.00 1.78e-65 BMRB 4073 'human ferredoxin' 100.00 124 100.00 100.00 1.78e-65 BMRB 4074 'human ferredoxin' 100.00 124 100.00 100.00 1.78e-65 stop_ save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type non-polymer _Name_common "FES (FE2/S2 (INORGANIC) CLUSTER)" _BMRB_code . _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 12:23:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 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 FE1 S1 ? ? SING FE1 S2 ? ? SING FE2 S1 ? ? SING FE2 S2 ? ? 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 $Ferredoxin Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Ferredoxin 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 4.4 mM '[U-13C; U-15N]' $FES 4.4 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 6.1 mM '[13C; 15N]-Cys' $FES 6.1 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 1.0 mM [13Cb]-Cys $FES 1.0 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 2.2 mM [U-15N] $FES 2.2 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_5 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 5.5 mM [15N]-Ala $FES 5.5 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_6 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 5.4 mM [15N]-Leu $FES 5.4 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_7 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 4.4 mM [15N]-Gly $FES 4.4 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ save_sample_8 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ferredoxin 4.7 mM [15N]-Thr $FES 4.7 mM . 'Phosphate buffer' 50 mM . D2O 10 % . H2O 90 % . DSS 250 uM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1D_1H-SuperWEFT_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 1H-SuperWEFT' _Sample_label . save_ save_1D_13C-SuperWEFT_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 13C-SuperWEFT' _Sample_label . save_ save_1D_15N_1-pulse_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 15N 1-pulse' _Sample_label . save_ save_1D_15N-SuperWEFT_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 15N-SuperWEFT' _Sample_label . save_ save_1D_1H{13C}_Difference_Decoupling_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 1H{13C} Difference Decoupling' _Sample_label . save_ save_1D_13C{15N}_Difference_Decoupling_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 13C{15N} Difference Decoupling' _Sample_label . save_ save_2D_1H{13C}_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H{13C} HSQC' _Sample_label . save_ save_3D_1H{13C}_HC(C)H-COSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H{13C} HC(C)H-COSY' _Sample_label . save_ save_2D_13C{13C}_CT-COSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C{13C} CT-COSY' _Sample_label . save_ save_2D_1H{13C}_PRE-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H{13C} PRE-HSQC' _Sample_label . save_ save_3D_1H{13C}_(H)CCH-COSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H{13C} (H)CCH-COSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 1H-SuperWEFT' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 13C-SuperWEFT' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 15N 1-pulse' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 15N-SuperWEFT' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 1H{13C} Difference Decoupling' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 13C{15N} Difference Decoupling' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H{13C} HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H{13C} HC(C)H-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C{13C} CT-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H{13C} PRE-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H{13C} (H)CCH-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.35 0.05 n/a temperature 293 0.2 K pressure 1 0.01 atm 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Ferredoxin _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 SER HA H 4.596 . 5 2 . 1 SER HB2 H 3.958 . 5 3 . 1 SER HB3 H 3.913 . 5 4 . 1 SER CA C 58.45 . 5 5 . 1 SER CB C 61.13 . 5 6 . 2 SER HA H 4.458 . 1 7 . 2 SER HB2 H 3.870 . 1 8 . 2 SER HB3 H 3.870 . 1 9 . 2 SER CA C 58.42 . 1 10 . 2 SER CB C 63.76 . 1 11 . 3 SER HA H 4.454 . 1 12 . 3 SER HB2 H 3.912 . 1 13 . 3 SER HB3 H 3.912 . 1 14 . 3 SER CA C 58.87 . 1 15 . 3 SER CB C 63.81 . 1 16 . 4 GLU HA H 4.316 . 1 17 . 4 GLU HB2 H 2.091 . 2 18 . 4 GLU HB3 H 1.925 . 2 19 . 4 GLU HG2 H 2.269 . 1 20 . 4 GLU HG3 H 2.269 . 1 21 . 4 GLU CA C 56.61 . 1 22 . 4 GLU CB C 30.29 . 1 23 . 4 GLU CG C 36.39 . 1 24 . 4 GLU CD C 184.0 . 1 25 . 5 ASP HA H 4.615 . 1 26 . 5 ASP HB2 H 2.686 . 2 27 . 5 ASP HB3 H 2.660 . 2 28 . 5 ASP CA C 54.44 . 1 29 . 5 ASP CB C 41.06 . 1 30 . 6 LYS HA H 4.909 . 1 31 . 6 LYS HB2 H 1.686 . 1 32 . 6 LYS HB3 H 1.686 . 1 33 . 6 LYS HG2 H 1.493 . 2 34 . 6 LYS HG3 H 1.199 . 2 35 . 6 LYS CA C 55.36 . 1 36 . 6 LYS CB C 35.48 . 1 37 . 6 LYS CG C 25.68 . 1 38 . 7 ILE HA H 4.476 . 1 39 . 7 ILE HB H 1.857 . 1 40 . 7 ILE HG12 H 1.094 . 2 41 . 7 ILE HG13 H 0.954 . 2 42 . 7 ILE HG2 H 0.797 . 1 43 . 7 ILE HD1 H 0.682 . 1 44 . 7 ILE CA C 58.92 . 1 45 . 7 ILE CB C 40.71 . 1 46 . 7 ILE CG1 C 25.77 . 1 47 . 7 ILE CG2 C 18.03 . 1 48 . 7 ILE CD1 C 13.81 . 1 49 . 8 THR HA H 4.728 . 1 50 . 8 THR HB H 3.871 . 1 51 . 8 THR HG2 H 0.812 . 1 52 . 8 THR CA C 63.40 . 1 53 . 8 THR CB C 69.14 . 1 54 . 8 THR CG2 C 21.91 . 1 55 . 9 VAL HA H 4.228 . 1 56 . 9 VAL HB H 1.601 . 1 57 . 9 VAL HG1 H 0.701 . 2 58 . 9 VAL HG2 H 0.372 . 2 59 . 9 VAL CA C 60.98 . 1 60 . 9 VAL CB C 35.53 . 1 61 . 9 VAL CG1 C 21.77 . 2 62 . 9 VAL CG2 C 22.93 . 2 63 . 10 HIS HA H 5.425 . 1 64 . 10 HIS HB2 H 3.307 . 2 65 . 10 HIS HB3 H 2.635 . 2 66 . 10 HIS HD2 H 6.690 . 1 67 . 10 HIS HE1 H 7.783 . 1 68 . 10 HIS CA C 54.13 . 1 69 . 10 HIS CB C 31.35 . 1 70 . 10 HIS CG C 135.5 . 1 71 . 10 HIS CD2 C 120.3 . 1 72 . 10 HIS CE1 C 138.9 . 1 73 . 11 PHE HA H 5.183 . 1 74 . 11 PHE HB2 H 3.121 . 2 75 . 11 PHE HB3 H 2.258 . 2 76 . 11 PHE HD1 H 7.120 . 1 77 . 11 PHE HD2 H 7.120 . 1 78 . 11 PHE CA C 55.61 . 1 79 . 11 PHE CB C 41.70 . 1 80 . 11 PHE CG C 139.3 . 1 81 . 11 PHE CD1 C 131.4 . 1 82 . 11 PHE CD2 C 131.4 . 1 83 . 12 ILE HA H 4.722 . 1 84 . 12 ILE HB H 1.769 . 1 85 . 12 ILE HG12 H 1.325 . 2 86 . 12 ILE HG13 H 1.105 . 2 87 . 12 ILE HG2 H 0.881 . 1 88 . 12 ILE HD1 H 0.699 . 1 89 . 12 ILE CA C 60.39 . 1 90 . 12 ILE CB C 37.04 . 1 91 . 12 ILE CG1 C 26.77 . 1 92 . 12 ILE CG2 C 16.88 . 1 93 . 12 ILE CD1 C 12.6 . 1 94 . 13 ASN HA H 4.687 . 1 95 . 13 ASN HB2 H 3.429 . 2 96 . 13 ASN HB3 H 2.958 . 2 97 . 13 ASN CA C 51.22 . 1 98 . 13 ASN CB C 38.85 . 1 99 . 13 ASN CG C 177.1 . 1 100 . 14 ARG HA H 4.049 . 1 101 . 14 ARG HB2 H 1.906 . 2 102 . 14 ARG HB3 H 1.807 . 2 103 . 14 ARG HG2 H 1.603 . 1 104 . 14 ARG HG3 H 1.603 . 1 105 . 14 ARG HD2 H 3.365 . 2 106 . 14 ARG HD3 H 3.335 . 2 107 . 14 ARG CA C 59.22 . 1 108 . 14 ARG CB C 29.55 . 1 109 . 14 ARG CG C 28.99 . 1 110 . 14 ARG CD C 43.95 . 1 111 . 15 ASP HA H 4.615 . 1 112 . 15 ASP HB2 H 2.892 . 1 113 . 15 ASP HB3 H 2.892 . 1 114 . 15 ASP CA C 53.47 . 1 115 . 15 ASP CB C 40.66 . 1 116 . 16 GLY HA2 H 4.247 . 2 117 . 16 GLY HA3 H 3.519 . 2 118 . 16 GLY C C 174.2 . 1 119 . 16 GLY CA C 45.23 . 1 120 . 17 GLU CB C 29.35 . 1 121 . 17 GLU CG C 36.60 . 1 122 . 18 THR HA H 4.933 . 1 123 . 18 THR HB H 4.029 . 1 124 . 18 THR HG2 H 1.101 . 1 125 . 18 THR CA C 62.99 . 1 126 . 18 THR CB C 69.17 . 1 127 . 18 THR CG2 C 21.65 . 1 128 . 19 LEU HA H 4.812 . 1 129 . 19 LEU HB2 H 1.944 . 2 130 . 19 LEU HB3 H 1.465 . 2 131 . 19 LEU HG H 1.721 . 1 132 . 19 LEU HD1 H 0.876 . 2 133 . 19 LEU HD2 H 0.797 . 2 134 . 19 LEU CA C 53.34 . 1 135 . 19 LEU CB C 42.68 . 1 136 . 19 LEU CG C 27.14 . 1 137 . 19 LEU CD1 C 23.25 . 2 138 . 19 LEU CD2 C 25.86 . 2 139 . 20 THR HA H 4.962 . 1 140 . 20 THR HB H 3.879 . 1 141 . 20 THR HG2 H 1.200 . 1 142 . 20 THR CA C 63.82 . 1 143 . 20 THR CB C 70.17 . 1 144 . 20 THR CG2 C 22.69 . 1 145 . 21 THR HA H 4.717 . 1 146 . 21 THR HB H 3.826 . 1 147 . 21 THR HG2 H 0.985 . 1 148 . 21 THR CA C 60.12 . 1 149 . 21 THR CB C 70.55 . 1 150 . 21 THR CG2 C 20.38 . 1 151 . 22 LYS HA H 5.600 . 1 152 . 22 LYS HB2 H 1.749 . 2 153 . 22 LYS HB3 H 1.526 . 2 154 . 22 LYS HG2 H 1.419 . 2 155 . 22 LYS HG3 H 1.366 . 2 156 . 22 LYS CA C 53.90 . 1 157 . 22 LYS CB C 35.91 . 1 158 . 22 LYS CG C 24.68 . 1 159 . 23 GLY HA2 H 4.725 . 2 160 . 23 GLY HA3 H 3.325 . 2 161 . 23 GLY C C 171.1 . 1 162 . 23 GLY CA C 43.92 . 1 163 . 24 LYS HA H 4.725 . 1 164 . 24 LYS HB2 H 1.686 . 1 165 . 24 LYS HB3 H 1.686 . 1 166 . 24 LYS HG2 H 1.454 . 2 167 . 24 LYS HG3 H 1.389 . 2 168 . 24 LYS CA C 55.05 . 1 169 . 24 LYS CB C 33.39 . 1 170 . 24 LYS CG C 24.67 . 1 171 . 25 VAL HA H 3.237 . 1 172 . 25 VAL HB H 1.925 . 1 173 . 25 VAL HG1 H 0.978 . 2 174 . 25 VAL HG2 H 0.883 . 2 175 . 25 VAL CA C 65.62 . 1 176 . 25 VAL CB C 31.49 . 1 177 . 25 VAL CG1 C 21.30 . 2 178 . 25 VAL CG2 C 22.97 . 2 179 . 26 GLY HA2 H 4.558 . 2 180 . 26 GLY HA3 H 3.587 . 2 181 . 26 GLY C C 174.2 . 1 182 . 26 GLY CA C 45.14 . 1 183 . 27 ASP HA H 4.760 . 1 184 . 27 ASP HB2 H 2.975 . 2 185 . 27 ASP HB3 H 2.907 . 2 186 . 27 ASP CA C 54.67 . 1 187 . 27 ASP CB C 41.43 . 1 188 . 28 SER HA H 5.772 . 1 189 . 28 SER HB2 H 4.024 . 2 190 . 28 SER HB3 H 4.318 . 2 191 . 28 SER CA C 57.06 . 1 192 . 28 SER CB C 66.06 . 1 193 . 29 LEU HA H 4.247 . 1 194 . 29 LEU HB2 H 2.402 . 2 195 . 29 LEU HB3 H 1.526 . 2 196 . 29 LEU HG H 1.857 . 1 197 . 29 LEU HD1 H 1.093 . 2 198 . 29 LEU HD2 H 0.903 . 2 199 . 29 LEU CA C 57.87 . 1 200 . 29 LEU CB C 40.86 . 1 201 . 29 LEU CG C 28.53 . 1 202 . 29 LEU CD1 C 26.68 . 2 203 . 29 LEU CD2 C 24.40 . 2 204 . 30 LEU HA H 4.341 . 1 205 . 30 LEU HB2 H 1.652 . 2 206 . 30 LEU HB3 H 1.596 . 2 207 . 30 LEU HG H 1.627 . 1 208 . 30 LEU CA C 55.23 . 1 209 . 30 LEU CB C 42.42 . 1 210 . 32 VAL HA H 3.816 . 1 211 . 32 VAL HB H 2.370 . 1 212 . 32 VAL HG1 H 1.252 . 2 213 . 32 VAL HG2 H 0.925 . 2 214 . 32 VAL CA C 66.16 . 1 215 . 32 VAL CB C 32.15 . 1 216 . 32 VAL CG1 C 23.78 . 2 217 . 32 VAL CG2 C 23.17 . 2 218 . 33 VAL HA H 3.078 . 1 219 . 33 VAL HB H 2.212 . 1 220 . 33 VAL HG1 H 0.638 . 2 221 . 33 VAL HG2 H 0.283 . 2 222 . 33 VAL CA C 67.18 . 1 223 . 33 VAL CB C 32.13 . 1 224 . 33 VAL CG1 C 20.88 . 2 225 . 33 VAL CG2 C 23.83 . 2 226 . 34 VAL HA H 3.771 . 1 227 . 34 VAL HB H 2.165 . 1 228 . 34 VAL HG1 H 1.152 . 2 229 . 34 VAL HG2 H 0.963 . 2 230 . 34 VAL CA C 66.22 . 1 231 . 34 VAL CB C 32.57 . 1 232 . 34 VAL CG1 C 22.49 . 2 233 . 34 VAL CG2 C 21.14 . 2 234 . 35 GLU HA H 4.047 . 1 235 . 35 GLU HB2 H 2.159 . 2 236 . 35 GLU HB3 H 2.009 . 2 237 . 35 GLU HG2 H 2.537 . 1 238 . 35 GLU HG3 H 2.537 . 1 239 . 35 GLU CA C 59.21 . 1 240 . 35 GLU CB C 29.27 . 1 241 . 35 GLU CG C 33.99 . 1 242 . 35 GLU CD C 180.5 . 1 243 . 36 ASN HA H 4.726 . 1 244 . 36 ASN HB2 H 2.783 . 2 245 . 36 ASN HB3 H 2.541 . 2 246 . 36 ASN CA C 53.41 . 1 247 . 36 ASN CB C 39.53 . 1 248 . 36 ASN CG C 178.1 . 1 249 . 37 ASN HA H 4.403 . 1 250 . 37 ASN HB2 H 3.010 . 2 251 . 37 ASN HB3 H 2.647 . 2 252 . 37 ASN CA C 54.01 . 1 253 . 37 ASN CB C 37.33 . 1 254 . 37 ASN CG C 178.2 . 1 255 . 38 LEU HA H 4.025 . 1 256 . 38 LEU HB2 H 1.364 . 2 257 . 38 LEU HB3 H 0.916 . 2 258 . 38 LEU HG H 1.417 . 1 259 . 38 LEU HD1 H 0.529 . 2 260 . 38 LEU HD2 H 0.156 . 2 261 . 38 LEU CA C 55.49 . 1 262 . 38 LEU CB C 41.97 . 1 263 . 38 LEU CG C 26.84 . 1 264 . 38 LEU CD1 C 22.38 . 2 265 . 38 LEU CD2 C 25.67 . 2 266 . 39 ASP HA H 4.557 . 1 267 . 39 ASP HB2 H 2.825 . 2 268 . 39 ASP HB3 H 2.505 . 2 269 . 39 ASP CA C 53.48 . 1 270 . 39 ASP CB C 39.50 . 1 271 . 39 ASP CG C 180.9 . 5 272 . 40 ILE HA H 4.192 . 1 273 . 40 ILE HB H 1.349 . 1 274 . 40 ILE HG12 H 0.946 . 2 275 . 40 ILE HG13 H 0.653 . 2 276 . 40 ILE HG2 H 0.929 . 1 277 . 40 ILE HD1 H 0.079 . 1 278 . 40 ILE CA C 60.04 . 1 279 . 40 ILE CB C 38.45 . 1 280 . 40 ILE CG1 C 25.97 . 1 281 . 40 ILE CG2 C 19.13 . 1 282 . 40 ILE CD1 C 13.26 . 1 283 . 41 ASP HA H 4.379 . 1 284 . 41 ASP HB2 H 2.684 . 2 285 . 41 ASP HB3 H 2.587 . 2 286 . 41 ASP CA C 56.80 . 1 287 . 41 ASP CB C 41.56 . 1 288 . 42 GLY HA2 H 4.103 . 2 289 . 42 GLY HA3 H 3.794 . 2 290 . 42 GLY C C 174.0 . 1 291 . 42 GLY CA C 46.17 . 1 292 . 43 PHE HD1 H 7.13 . 1 293 . 43 PHE HD2 H 7.13 . 1 294 . 43 PHE HE1 H 6.70 . 1 295 . 43 PHE HE2 H 6.70 . 1 296 . 43 PHE CB C 40.90 . 1 297 . 43 PHE CG C 139.0 . 1 298 . 43 PHE CD1 C 133.3 . 1 299 . 43 PHE CD2 C 133.3 . 1 300 . 43 PHE CE1 C 130.6 . 1 301 . 43 PHE CE2 C 130.6 . 1 302 . 44 GLY C C 177.5 . 1 303 . 44 GLY CA C 45.4 . 1 304 . 44 GLY N N 125.8 . 5 305 . 45 ALA HA H 5.07 . 5 306 . 45 ALA HB H 1.45 . 5 307 . 45 ALA C C 178.0 . 5 308 . 45 ALA CA C 50.9 . 5 309 . 45 ALA CB C 21.7 . 5 310 . 45 ALA N N 126.8 . 1 311 . 46 CYS N N 132.5 . 5 312 . 47 GLU HB2 H 2.43 . 2 313 . 47 GLU HB3 H 2.27 . 2 314 . 47 GLU HG2 H 2.22 . 1 315 . 47 GLU HG3 H 2.22 . 1 316 . 47 GLU C C 178.0 . 1 317 . 47 GLU CA C 57.3 . 1 318 . 47 GLU CB C 27.1 . 1 319 . 47 GLU CG C 36.8 . 1 320 . 47 GLU CD C 185.0 . 1 321 . 48 GLY CA C 95.1 . 1 322 . 48 GLY N N 181.1 . 1 323 . 49 THR HB H 4.57 . 1 324 . 49 THR HG2 H 1.12 . 1 325 . 49 THR C C 173.1 . 1 326 . 49 THR CA C 60.8 . 1 327 . 49 THR CB C 69.0 . 1 328 . 49 THR CG2 C 21.7 . 1 329 . 49 THR N N 139.0 . 1 330 . 50 LEU C C 174.9 . 1 331 . 50 LEU CA C 85.6 . 1 332 . 50 LEU CB C 38.8 . 1 333 . 50 LEU N N 140.8 . 1 334 . 51 ALA HA H 4.24 . 5 335 . 51 ALA HB H 1.59 . 5 336 . 51 ALA C C 180.0 . 5 337 . 51 ALA CA C 56.1 . 5 338 . 51 ALA CB C 22.7 . 5 339 . 51 ALA N N 148.4 . 1 340 . 52 CYS N N 106.4 . 5 341 . 53 SER HB2 H 3.71 . 1 342 . 53 SER HB3 H 3.71 . 1 343 . 53 SER C C 180.1 . 1 344 . 53 SER CA C 56.8 . 1 345 . 53 SER CB C 63.9 . 1 346 . 54 THR HA H 4.70 . 1 347 . 54 THR HB H 5.88 . 1 348 . 54 THR HG2 H 1.79 . 1 349 . 54 THR C C 176.1 . 1 350 . 54 THR CA C 64.4 . 1 351 . 54 THR CB C 69.7 . 1 352 . 54 THR CG2 C 24.5 . 1 353 . 54 THR N N 164.0 . 1 354 . 55 CYS N N 129.4 . 1 355 . 56 HIS HA H 4.95 . 1 356 . 56 HIS HB2 H 3.23 . 1 357 . 56 HIS HB3 H 3.23 . 1 358 . 56 HIS HD1 H 11.90 . 1 359 . 56 HIS HD2 H 7.07 . 1 360 . 56 HIS HE1 H 7.51 . 1 361 . 56 HIS C C 173.6 . 1 362 . 56 HIS CA C 54.9 . 1 363 . 56 HIS CB C 30.5 . 1 364 . 56 HIS CG C 127.1 . 1 365 . 56 HIS CD2 C 127.2 . 1 366 . 56 HIS CE1 C 137.8 . 1 367 . 56 HIS ND1 N 169.6 . 1 368 . 56 HIS NE2 N 238.2 . 1 369 . 57 LEU HA H 4.93 . 1 370 . 57 LEU HB2 H 1.73 . 2 371 . 57 LEU HB3 H 0.96 . 2 372 . 57 LEU HG H 2.38 . 1 373 . 57 LEU HD1 H 1.01 . 2 374 . 57 LEU HD2 H 1.04 . 2 375 . 57 LEU C C 175.2 . 9 376 . 57 LEU CA C 53.6 . 1 377 . 57 LEU CB C 49.6 . 1 378 . 57 LEU CG C 26.1 . 1 379 . 57 LEU CD1 C 28.7 . 2 380 . 57 LEU CD2 C 24.2 . 2 381 . 58 ILE HA H 3.760 . 1 382 . 58 ILE HB H 1.557 . 1 383 . 58 ILE HG12 H 1.618 . 1 384 . 58 ILE HG13 H 1.024 . 1 385 . 58 ILE HG2 H 0.908 . 1 386 . 58 ILE HD1 H 0.913 . 1 387 . 58 ILE CA C 63.07 . 1 388 . 58 ILE CB C 39.29 . 1 389 . 58 ILE CG1 C 28.74 . 1 390 . 58 ILE CG2 C 16.87 . 1 391 . 58 ILE CD1 C 14.58 . 1 392 . 59 PHE CB C 43.35 . 1 393 . 59 PHE CG C 140.4 . 1 394 . 59 PHE CD1 C 131.8 . 1 395 . 59 PHE CD2 C 131.8 . 1 396 . 60 GLU HA H 4.364 . 1 397 . 60 GLU HB2 H 2.364 . 2 398 . 60 GLU HB3 H 1.883 . 2 399 . 60 GLU HG2 H 2.887 . 2 400 . 60 GLU HG3 H 2.335 . 2 401 . 60 GLU CB C 32.26 . 1 402 . 60 GLU CG C 38.25 . 1 403 . 60 GLU CD C 184.4 . 1 404 . 61 ASP HA H 4.122 . 1 405 . 61 ASP HB2 H 2.893 . 1 406 . 61 ASP HB3 H 2.893 . 1 407 . 61 ASP CA C 59.04 . 1 408 . 61 ASP CB C 40.93 . 1 409 . 62 HIS HA H 4.532 . 1 410 . 62 HIS HB2 H 3.224 . 2 411 . 62 HIS HB3 H 3.118 . 2 412 . 62 HIS HD2 H 7.050 . 1 413 . 62 HIS HE1 H 7.894 . 1 414 . 62 HIS CA C 58.50 . 1 415 . 62 HIS CB C 29.38 . 1 416 . 62 HIS CG C 136.3 . 1 417 . 62 HIS CD2 C 118.2 . 1 418 . 62 HIS CE1 C 139.6 . 1 419 . 63 ILE HA H 3.903 . 1 420 . 63 ILE HB H 2.195 . 1 421 . 63 ILE HG12 H 1.481 . 2 422 . 63 ILE HG13 H 0.764 . 2 423 . 63 ILE HG2 H 1.100 . 1 424 . 63 ILE HD1 H 0.700 . 1 425 . 63 ILE CA C 59.91 . 1 426 . 63 ILE CB C 36.51 . 1 427 . 63 ILE CG1 C 25.70 . 1 428 . 63 ILE CG2 C 17.75 . 1 429 . 63 ILE CD1 C 9.137 . 1 430 . 64 TYR HA H 3.592 . 1 431 . 64 TYR HB2 H 3.056 . 2 432 . 64 TYR HB3 H 2.899 . 2 433 . 64 TYR HD1 H 6.820 . 1 434 . 64 TYR HD2 H 6.820 . 1 435 . 64 TYR HE1 H 6.660 . 1 436 . 64 TYR HE2 H 6.660 . 1 437 . 64 TYR CA C 61.72 . 1 438 . 64 TYR CB C 39.60 . 1 439 . 64 TYR CG C 128.4 . 1 440 . 64 TYR CD1 C 132.9 . 1 441 . 64 TYR CD2 C 132.9 . 1 442 . 64 TYR CE1 C 119.4 . 1 443 . 64 TYR CE2 C 119.4 . 1 444 . 64 TYR CZ C 159.3 . 1 445 . 65 GLU HA H 4.135 . 1 446 . 65 GLU HB2 H 2.178 . 2 447 . 65 GLU HB3 H 2.138 . 2 448 . 65 GLU HG2 H 2.423 . 1 449 . 65 GLU HG3 H 2.423 . 1 450 . 65 GLU CA C 58.12 . 1 451 . 65 GLU CB C 30.03 . 1 452 . 65 GLU CG C 35.97 . 1 453 . 65 GLU CD C 183.3 . 1 454 . 66 LYS HA H 4.464 . 1 455 . 66 LYS HB2 H 2.067 . 2 456 . 66 LYS HB3 H 1.781 . 2 457 . 66 LYS HG2 H 1.605 . 2 458 . 66 LYS HG3 H 1.425 . 2 459 . 66 LYS HD2 H 1.698 . 1 460 . 66 LYS HD3 H 1.698 . 1 461 . 66 LYS HE2 H 3.056 . 1 462 . 66 LYS HE3 H 3.056 . 1 463 . 66 LYS CA C 54.84 . 1 464 . 66 LYS CB C 33.27 . 1 465 . 66 LYS CG C 24.96 . 1 466 . 66 LYS CD C 28.79 . 1 467 . 66 LYS CE C 41.22 . 1 468 . 67 LEU HA H 4.071 . 1 469 . 67 LEU HB2 H 1.396 . 2 470 . 67 LEU HB3 H 1.314 . 2 471 . 67 LEU HG H 1.828 . 1 472 . 67 LEU HD1 H 0.520 . 2 473 . 67 LEU HD2 H -0.032 . 2 474 . 67 LEU CA C 54.58 . 1 475 . 67 LEU CB C 41.50 . 1 476 . 67 LEU CG C 25.06 . 1 477 . 67 LEU CD1 C 22.03 . 2 478 . 67 LEU CD2 C 25.19 . 2 479 . 68 ASP HA H 4.330 . 1 480 . 68 ASP HB2 H 2.691 . 2 481 . 68 ASP HB3 H 2.594 . 2 482 . 68 ASP CA C 54.64 . 1 483 . 68 ASP CB C 40.85 . 1 484 . 69 ALA HA H 3.999 . 1 485 . 69 ALA HB H 1.308 . 1 486 . 69 ALA CA C 52.57 . 1 487 . 69 ALA CB C 18.79 . 1 488 . 70 ILE HA H 4.633 . 1 489 . 70 ILE HB H 1.490 . 1 490 . 70 ILE HG12 H 1.319 . 2 491 . 70 ILE HG13 H 1.069 . 2 492 . 70 ILE HG2 H 0.877 . 1 493 . 70 ILE HD1 H 0.725 . 1 494 . 70 ILE CA C 61.28 . 1 495 . 70 ILE CB C 40.22 . 1 496 . 70 ILE CG1 C 28.24 . 1 497 . 70 ILE CG2 C 17.94 . 1 498 . 70 ILE CD1 C 14.53 . 1 499 . 71 THR HA H 4.515 . 1 500 . 71 THR HB H 4.714 . 1 501 . 71 THR HG2 H 1.421 . 1 502 . 71 THR CA C 61.06 . 1 503 . 71 THR CB C 72.17 . 1 504 . 71 THR CG2 C 21.76 . 1 505 . 72 ASP HA H 4.315 . 1 506 . 72 ASP HB2 H 2.800 . 2 507 . 72 ASP HB3 H 2.533 . 2 508 . 72 ASP CA C 57.81 . 1 509 . 72 ASP CB C 40.25 . 1 510 . 72 ASP CG C 180.2 . 5 511 . 73 GLU HA H 4.055 . 1 512 . 73 GLU HB2 H 2.058 . 2 513 . 73 GLU HB3 H 1.981 . 2 514 . 73 GLU HG2 H 2.556 . 2 515 . 73 GLU HG3 H 2.346 . 2 516 . 73 GLU CA C 60.60 . 1 517 . 73 GLU CB C 29.33 . 1 518 . 73 GLU CG C 37.61 . 1 519 . 73 GLU CD C 184.7 . 1 520 . 74 GLU CB C 28.86 . 1 521 . 74 GLU CG C 36.14 . 1 522 . 74 GLU CD C 180.8 . 1 523 . 75 ASN HA H 4.358 . 1 524 . 75 ASN HB2 H 2.994 . 2 525 . 75 ASN HB3 H 2.727 . 2 526 . 75 ASN CA C 57.07 . 1 527 . 75 ASN CB C 39.04 . 1 528 . 75 ASN CG C 176.0 . 1 529 . 76 ASP CB C 40.31 . 1 530 . 76 ASP CG C 179.1 . 5 531 . 77 MET HA H 4.554 . 1 532 . 77 MET HB2 H 2.137 . 2 533 . 77 MET HB3 H 2.031 . 2 534 . 77 MET CA C 55.78 . 1 535 . 77 MET CB C 34.49 . 1 536 . 77 MET CG C 33.17 . 1 537 . 78 LEU HA H 3.834 . 1 538 . 78 LEU HB2 H 1.856 . 2 539 . 78 LEU HB3 H 1.654 . 2 540 . 78 LEU CA C 57.81 . 1 541 . 78 LEU CB C 41.43 . 1 542 . 80 LEU HA H 4.394 . 1 543 . 80 LEU HB2 H 1.811 . 2 544 . 80 LEU HB3 H 1.693 . 2 545 . 80 LEU HG H 1.747 . 1 546 . 80 LEU HD1 H 0.941 . 2 547 . 80 LEU HD2 H 0.844 . 2 548 . 80 LEU CA C 53.94 . 1 549 . 80 LEU CB C 42.44 . 1 550 . 80 LEU CG C 26.64 . 1 551 . 80 LEU CD1 C 25.64 . 2 552 . 80 LEU CD2 C 22.40 . 2 553 . 81 ALA HA H 4.192 . 1 554 . 81 ALA HB H 1.320 . 1 555 . 81 ALA CA C 52.64 . 1 556 . 81 ALA CB C 19.18 . 1 557 . 82 TYR HA H 4.471 . 1 558 . 82 TYR HB2 H 3.100 . 2 559 . 82 TYR HB3 H 2.925 . 2 560 . 82 TYR HD1 H 7.120 . 1 561 . 82 TYR HD2 H 7.120 . 1 562 . 82 TYR HE1 H 6.800 . 1 563 . 82 TYR HE2 H 6.800 . 1 564 . 82 TYR CA C 58.40 . 1 565 . 82 TYR CB C 38.93 . 1 566 . 82 TYR CG C 130.3 . 1 567 . 82 TYR CD1 C 133.4 . 1 568 . 82 TYR CD2 C 133.4 . 1 569 . 82 TYR CE1 C 118.3 . 1 570 . 82 TYR CE2 C 118.3 . 1 571 . 82 TYR CZ C 157.5 . 1 572 . 83 GLY HA2 H 3.712 . 2 573 . 83 GLY HA3 H 3.554 . 2 574 . 83 GLY C C 174.7 . 1 575 . 83 GLY CA C 46.41 . 1 576 . 84 LEU HA H 3.879 . 1 577 . 84 LEU HB2 H 1.625 . 2 578 . 84 LEU HB3 H 1.518 . 2 579 . 84 LEU HG H 1.555 . 1 580 . 84 LEU HD1 H 0.902 . 2 581 . 84 LEU HD2 H 0.908 . 2 582 . 84 LEU CA C 56.86 . 1 583 . 84 LEU CB C 42.71 . 1 584 . 84 LEU CG C 26.64 . 1 585 . 84 LEU CD1 C 25.04 . 2 586 . 84 LEU CD2 C 23.85 . 2 587 . 85 THR HA H 4.974 . 1 588 . 85 THR HB H 4.440 . 1 589 . 85 THR HG2 H 1.288 . 1 590 . 85 THR CA C 60.06 . 1 591 . 85 THR CB C 74.54 . 1 592 . 85 THR CG2 C 21.89 . 1 593 . 86 ASP HA H 4.558 . 1 594 . 86 ASP HB2 H 2.851 . 1 595 . 86 ASP HB3 H 2.851 . 1 596 . 86 ASP CA C 54.25 . 1 597 . 86 ASP CB C 39.52 . 1 598 . 86 ASP CG C 179.8 . 5 599 . 88 SER HA H 5.480 . 1 600 . 88 SER HB2 H 4.036 . 2 601 . 88 SER HB3 H 3.946 . 2 602 . 88 SER CA C 60.61 . 1 603 . 88 SER CB C 65.40 . 1 604 . 89 ARG HA H 4.875 . 1 605 . 89 ARG HB2 H 2.028 . 2 606 . 89 ARG HB3 H 1.751 . 2 607 . 89 ARG CA C 52.83 . 1 608 . 89 ARG CB C 34.08 . 1 609 . 89 ARG CG C 32.32 . 1 610 . 90 LEU HA H 4.58 . 1 611 . 90 LEU C C 177.9 . 1 612 . 90 LEU CA C 58.21 . 1 613 . 90 LEU CB C 42.70 . 1 614 . 90 LEU N N 116.7 . 5 615 . 91 GLY HA2 H 4.53 . 2 616 . 91 GLY HA3 H 4.06 . 2 617 . 91 GLY C C 173.4 . 1 618 . 91 GLY CA C 47.9 . 1 619 . 91 GLY N N 116.4 . 5 620 . 92 CYS N N 136.2 . 1 621 . 93 GLN HA H 3.60 . 1 622 . 93 GLN HB2 H 2.41 . 2 623 . 93 GLN HB3 H 1.44 . 2 624 . 93 GLN HG2 H 1.23 . 1 625 . 93 GLN HG3 H 1.23 . 1 626 . 93 GLN C C 175.2 . 1 627 . 93 GLN CA C 53.7 . 1 628 . 93 GLN CB C 30.1 . 1 629 . 93 GLN CG C 38.6 . 1 630 . 93 GLN CD C 179.4 . 1 631 . 93 GLN NE2 N 155.0 . 1 632 . 94 ILE HA H 4.252 . 1 633 . 94 ILE HB H 2.346 . 1 634 . 94 ILE HG12 H 1.957 . 1 635 . 94 ILE HG13 H 0.963 . 1 636 . 94 ILE HG2 H 0.780 . 1 637 . 94 ILE HD1 H 0.559 . 1 638 . 94 ILE CA C 57.86 . 1 639 . 94 ILE CB C 36.96 . 1 640 . 94 ILE CG1 C 25.62 . 1 641 . 94 ILE CG2 C 18.04 . 1 642 . 94 ILE CD1 C 9.23 . 1 643 . 95 CYS HA H 4.995 . 1 644 . 95 CYS HB2 H 2.704 . 2 645 . 95 CYS HB3 H 2.395 . 2 646 . 95 CYS CA C 57.26 . 1 647 . 95 CYS CB C 29.23 . 1 648 . 96 LEU HA H 4.740 . 1 649 . 96 LEU HB2 H 2.063 . 2 650 . 96 LEU HB3 H 1.101 . 2 651 . 96 LEU HG H 1.870 . 1 652 . 96 LEU HD1 H 0.764 . 2 653 . 96 LEU HD2 H 0.705 . 2 654 . 96 LEU CA C 55.60 . 1 655 . 96 LEU CB C 42.34 . 1 656 . 96 LEU CG C 27.08 . 1 657 . 96 LEU CD1 C 24.82 . 2 658 . 96 LEU CD2 C 25.12 . 2 659 . 97 THR HA H 4.689 . 1 660 . 97 THR HB H 4.587 . 1 661 . 97 THR HG2 H 1.240 . 1 662 . 97 THR CA C 59.36 . 1 663 . 97 THR CB C 71.58 . 1 664 . 97 THR CG2 C 21.67 . 1 665 . 98 LYS HA H 3.923 . 1 666 . 98 LYS HB2 H 1.901 . 1 667 . 98 LYS HB3 H 1.901 . 1 668 . 98 LYS HG2 H 1.540 . 1 669 . 98 LYS HG3 H 1.540 . 1 670 . 98 LYS HD2 H 1.741 . 2 671 . 98 LYS HD3 H 1.682 . 2 672 . 98 LYS CA C 59.48 . 1 673 . 98 LYS CB C 31.99 . 1 674 . 98 LYS CG C 25.45 . 1 675 . 98 LYS CD C 29.30 . 1 676 . 99 SER HA H 4.317 . 1 677 . 99 SER HB2 H 3.930 . 1 678 . 99 SER HB3 H 3.930 . 1 679 . 99 SER CA C 60.26 . 1 680 . 99 SER CB C 62.58 . 1 681 . 100 MET HA H 4.163 . 1 682 . 100 MET HB2 H 2.583 . 2 683 . 100 MET HB3 H 2.036 . 2 684 . 100 MET HG2 H 2.614 . 2 685 . 100 MET HG3 H 2.531 . 2 686 . 100 MET CA C 56.76 . 1 687 . 100 MET CB C 32.35 . 1 688 . 100 MET CG C 32.13 . 1 689 . 101 ASP HA H 4.409 . 1 690 . 101 ASP HB2 H 2.734 . 1 691 . 101 ASP HB3 H 2.734 . 1 692 . 101 ASP CA C 56.83 . 1 693 . 101 ASP CB C 41.12 . 1 694 . 102 ASN HA H 3.897 . 1 695 . 102 ASN HB2 H 3.260 . 2 696 . 102 ASN HB3 H 3.055 . 2 697 . 102 ASN CA C 55.75 . 1 698 . 102 ASN CB C 38.01 . 1 699 . 102 ASN CG C 179.0 . 1 700 . 103 MET HA H 4.710 . 1 701 . 103 MET HB2 H 2.262 . 1 702 . 103 MET HB3 H 2.262 . 1 703 . 103 MET HG2 H 2.997 . 2 704 . 103 MET HG3 H 2.268 . 2 705 . 103 MET CA C 56.53 . 1 706 . 103 MET CB C 31.46 . 1 707 . 103 MET CG C 33.00 . 1 708 . 104 THR HA H 5.449 . 1 709 . 104 THR HB H 3.761 . 1 710 . 104 THR HG2 H 0.993 . 1 711 . 104 THR CA C 61.70 . 1 712 . 104 THR CB C 70.50 . 1 713 . 104 THR CG2 C 21.54 . 1 714 . 105 VAL HA H 4.607 . 1 715 . 105 VAL HB H 1.358 . 1 716 . 105 VAL HG1 H 0.145 . 2 717 . 105 VAL HG2 H 0.015 . 2 718 . 105 VAL CA C 58.28 . 1 719 . 105 VAL CB C 34.36 . 1 720 . 105 VAL CG1 C 23.35 . 2 721 . 105 VAL CG2 C 19.58 . 2 722 . 106 ARG HA H 4.878 . 1 723 . 106 ARG HB2 H 1.699 . 2 724 . 106 ARG HB3 H 1.482 . 2 725 . 106 ARG HG2 H 1.487 . 2 726 . 106 ARG HG3 H 1.316 . 2 727 . 106 ARG HD2 H 3.075 . 1 728 . 106 ARG HD3 H 3.075 . 1 729 . 106 ARG CA C 54.60 . 1 730 . 106 ARG CB C 33.63 . 1 731 . 106 ARG CG C 28.06 . 1 732 . 106 ARG CD C 43.52 . 1 733 . 107 VAL HA H 4.509 . 1 734 . 107 VAL HB H 2.273 . 1 735 . 107 VAL HG1 H 1.227 . 2 736 . 107 VAL HG2 H 0.996 . 2 737 . 107 VAL CA C 59.61 . 1 738 . 107 VAL CB C 32.23 . 1 739 . 107 VAL CG1 C 21.56 . 2 740 . 107 VAL CG2 C 21.05 . 2 741 . 108 PRO HA H 4.335 . 1 742 . 108 PRO HB2 H 2.068 . 2 743 . 108 PRO HB3 H 1.993 . 2 744 . 108 PRO HG2 H 1.442 . 2 745 . 108 PRO HG3 H 0.932 . 2 746 . 108 PRO HD2 H 3.701 . 1 747 . 108 PRO HD3 H 3.701 . 1 748 . 108 PRO CA C 62.78 . 1 749 . 108 PRO CB C 32.35 . 1 750 . 108 PRO CG C 26.62 . 1 751 . 108 PRO CD C 51.27 . 1 752 . 109 GLU HA H 4.231 . 1 753 . 109 GLU HB2 H 2.173 . 2 754 . 109 GLU HB3 H 2.064 . 2 755 . 109 GLU HG2 H 2.408 . 1 756 . 109 GLU HG3 H 2.408 . 1 757 . 109 GLU CA C 57.16 . 1 758 . 109 GLU CB C 30.82 . 1 759 . 109 GLU CG C 36.66 . 1 760 . 109 GLU CD C 184.0 . 1 761 . 110 THR HA H 4.407 . 5 762 . 110 THR HB H 4.116 . 5 763 . 110 THR HG2 H 1.139 . 5 764 . 110 THR CA C 61.13 . 5 765 . 110 THR CB C 70.34 . 5 766 . 110 THR CG2 C 21.38 . 5 767 . 111 VAL HA H 3.885 . 1 768 . 111 VAL HB H 1.856 . 1 769 . 111 VAL HG1 H 0.809 . 2 770 . 111 VAL HG2 H 0.805 . 2 771 . 111 VAL CA C 61.85 . 1 772 . 111 VAL CB C 33.01 . 1 773 . 111 VAL CG1 C 20.83 . 2 774 . 111 VAL CG2 C 20.49 . 2 775 . 112 ALA HA H 4.281 . 1 776 . 112 ALA HB H 1.398 . 1 777 . 112 ALA CA C 52.90 . 1 778 . 112 ALA CB C 19.05 . 1 779 . 113 ASP HA H 4.524 . 1 780 . 113 ASP HB2 H 2.697 . 2 781 . 113 ASP HB3 H 2.652 . 2 782 . 113 ASP CA C 54.29 . 1 783 . 113 ASP CB C 41.35 . 1 784 . 114 ALA HA H 4.140 . 1 785 . 114 ALA HB H 1.389 . 1 786 . 114 ALA CA C 54.18 . 1 787 . 114 ALA CB C 20.04 . 1 788 . 115 ARG HA H 4.262 . 1 789 . 115 ARG HB2 H 1.877 . 2 790 . 115 ARG HB3 H 1.833 . 2 791 . 115 ARG HG2 H 1.662 . 1 792 . 115 ARG HG3 H 1.662 . 1 793 . 115 ARG HD2 H 3.206 . 1 794 . 115 ARG HD3 H 3.206 . 1 795 . 115 ARG HE H 4.565 . 1 796 . 115 ARG CA C 56.54 . 1 797 . 115 ARG CB C 30.54 . 1 798 . 115 ARG CG C 27.08 . 1 799 . 115 ARG CD C 43.38 . 1 800 . 116 GLN HA H 4.349 . 1 801 . 116 GLN HB2 H 2.143 . 2 802 . 116 GLN HB3 H 2.011 . 2 803 . 116 GLN HG2 H 2.389 . 1 804 . 116 GLN HG3 H 2.389 . 1 805 . 116 GLN CA C 55.94 . 1 806 . 116 GLN CB C 29.52 . 1 807 . 116 GLN CG C 33.87 . 1 808 . 116 GLN CD C 180.5 . 1 809 . 117 SER HA H 4.046 . 5 810 . 117 SER HB2 H 3.952 . 5 811 . 117 SER HB3 H 3.952 . 5 812 . 117 SER CA C 57.80 . 5 813 . 117 SER CB C 64.35 . 5 814 . 118 ILE HA H 4.198 . 1 815 . 118 ILE HB H 1.876 . 1 816 . 118 ILE HG12 H 1.452 . 2 817 . 118 ILE HG13 H 1.174 . 2 818 . 118 ILE HG2 H 0.902 . 1 819 . 118 ILE HD1 H 0.861 . 1 820 . 118 ILE CA C 61.26 . 1 821 . 118 ILE CB C 38.99 . 1 822 . 118 ILE CG1 C 27.24 . 1 823 . 118 ILE CG2 C 17.54 . 1 824 . 118 ILE CD1 C 13.15 . 1 825 . 119 ASP HA H 4.672 . 1 826 . 119 ASP HB2 H 2.735 . 2 827 . 119 ASP HB3 H 2.600 . 2 828 . 119 ASP CA C 54.19 . 1 829 . 119 ASP CB C 41.18 . 1 830 . 120 VAL HA H 4.118 . 1 831 . 120 VAL HB H 2.179 . 1 832 . 120 VAL HG1 H 0.962 . 1 833 . 120 VAL HG2 H 0.962 . 1 834 . 120 VAL CA C 62.70 . 1 835 . 120 VAL CB C 32.34 . 1 836 . 120 VAL CG1 C 21.14 . 2 837 . 120 VAL CG2 C 20.18 . 2 838 . 121 GLY HA2 H 3.960 . 1 839 . 121 GLY HA3 H 3.960 . 1 840 . 121 GLY C C 177.5 . 1 841 . 121 GLY CA C 45.43 . 1 842 . 122 LYS HA H 4.457 . 1 843 . 122 LYS HB2 H 1.905 . 2 844 . 122 LYS HB3 H 1.799 . 2 845 . 122 LYS HG2 H 1.456 . 2 846 . 122 LYS HG3 H 1.429 . 2 847 . 122 LYS HD2 H 1.697 . 1 848 . 122 LYS HD3 H 1.697 . 1 849 . 122 LYS HE2 H 3.006 . 1 850 . 122 LYS HE3 H 3.006 . 1 851 . 122 LYS CA C 56.27 . 1 852 . 122 LYS CB C 33.32 . 1 853 . 122 LYS CG C 24.73 . 1 854 . 122 LYS CD C 29.17 . 1 855 . 122 LYS CE C 42.14 . 1 856 . 123 THR HA H 4.441 . 5 857 . 123 THR HB H 4.331 . 5 858 . 123 THR HG2 H 1.221 . 5 859 . 123 THR CA C 61.71 . 5 860 . 123 THR CB C 69.99 . 5 861 . 123 THR CG2 C 21.55 . 5 862 . 124 SER HA H 4.287 . 1 863 . 124 SER HB2 H 3.872 . 1 864 . 124 SER HB3 H 3.872 . 1 865 . 124 SER CA C 60.04 . 1 866 . 124 SER CB C 64.79 . 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 809,1 811,810,3,2 812,4 813,5 598,271 530,510 334,305 335,335,335,306,306,306 336,307 337,308 338,309 856,761 857,762 858,858,858,763,763,763 859,764 860,765 861,766 614,619,304 340,311 stop_ save_