data_5337 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete assignments of 1H, 13C and 15N Chemical Shifts for Oxidized Human Adrenodoxin (4-114) ; _BMRB_accession_number 5337 _BMRB_flat_file_name bmr5337.str _Entry_type original _Submission_date 2002-04-01 _Accession_date 2002-04-02 _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 Kostic Milka . . 2 Pochapsky Susan S. . 3 Obenauer John . . 4 Mo Huaping . . 5 Pagani Gina M. . 6 Pejchal Robert . . 7 Pochapsky Thomas C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 464 "13C chemical shifts" 374 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-08 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4566 'Chemical Shift of Bovine Adrenodoxin' 4073 'Chemical Shift of Oxidized Human Ferredoxin' stop_ _Original_release_date 2002-05-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Comparison of functional domains in vertebrate-type ferredoxins' _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kostic Milka . . 2 Pochapsky Susan S. . 3 Obenauer John . . 4 Mo Huaping . . 5 Pagani Gina M. . 6 Pejchal Robert . . 7 Pochapsky Thomas C. . stop_ _Journal_abbreviation Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword ferredoxin 'cytochrome P450' 'paramagnetic protein' NMR 'molecular model' 'protein dynamics' stop_ save_ ################################## # Molecular system description # ################################## save_system_Adx _Saveframe_category molecular_system _Mol_system_name 'human adrenodoxin' _Abbreviation_common Adx _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human Adx (4-114), chain A' $Adx 'human Adx (4-114), chain B' $Adx 'FES A' $FES 'FES B' $FES stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic yes _System_thiol_state 'other bound and free' loop_ _Biological_function 'electron-transfer protein' stop_ _Database_query_date . _Details ; 1AYF-structure of bovine Adx (4-114) 1CJE-structure of full-length bovine Adx ; save_ ######################## # Monomeric polymers # ######################## save_Adx _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human adrenodoxin' _Name_variant 4-114 _Abbreviation_common Adx _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; EDKITVHFINRDGETLTTKG KVGDSLLDVVVENNLDIDGF GACDGTLACSTCHLIFEDHI YEKLDAITDEENDMLDLAYG LTDRSRLGCQICLTKSMDNM TVRVPETVADA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 4 GLU 2 5 ASP 3 6 LYS 4 7 ILE 5 8 THR 6 9 VAL 7 10 HIS 8 11 PHE 9 12 ILE 10 13 ASN 11 14 ARG 12 15 ASP 13 16 GLY 14 17 GLU 15 18 THR 16 19 LEU 17 20 THR 18 21 THR 19 22 LYS 20 23 GLY 21 24 LYS 22 25 VAL 23 26 GLY 24 27 ASP 25 28 SER 26 29 LEU 27 30 LEU 28 31 ASP 29 32 VAL 30 33 VAL 31 34 VAL 32 35 GLU 33 36 ASN 34 37 ASN 35 38 LEU 36 39 ASP 37 40 ILE 38 41 ASP 39 42 GLY 40 43 PHE 41 44 GLY 42 45 ALA 43 46 CYS 44 47 ASP 45 48 GLY 46 49 THR 47 50 LEU 48 51 ALA 49 52 CYS 50 53 SER 51 54 THR 52 55 CYS 53 56 HIS 54 57 LEU 55 58 ILE 56 59 PHE 57 60 GLU 58 61 ASP 59 62 HIS 60 63 ILE 61 64 TYR 62 65 GLU 63 66 LYS 64 67 LEU 65 68 ASP 66 69 ALA 67 70 ILE 68 71 THR 69 72 ASP 70 73 GLU 71 74 GLU 72 75 ASN 73 76 ASP 74 77 MET 75 78 LEU 76 79 ASP 77 80 LEU 78 81 ALA 79 82 TYR 80 83 GLY 81 84 LEU 82 85 THR 83 86 ASP 84 87 ARG 85 88 SER 86 89 ARG 87 90 LEU 88 91 GLY 89 92 CYS 90 93 GLN 91 94 ILE 92 95 CYS 93 96 LEU 94 97 THR 95 98 LYS 96 99 SER 97 100 MET 98 101 ASP 99 102 ASN 100 103 MET 101 104 THR 102 105 VAL 103 106 ARG 104 107 VAL 105 108 PRO 106 109 GLU 107 110 THR 108 111 VAL 109 112 ALA 110 113 ASP 111 114 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4073 HuFd-ox 100.00 124 99.10 100.00 6.78e-73 BMRB 4074 HuFd-red 100.00 124 99.10 100.00 6.78e-73 BMRB 4439 HuFd 100.00 124 99.10 100.00 6.78e-73 BMRB 4440 HuFd 100.00 124 99.10 100.00 6.78e-73 BMRB 6026 Ferredoxin 100.00 124 99.10 100.00 6.78e-73 PDB 3N9Y "Crystal Structure Of Human Cyp11a1 In Complex With Cholesterol" 100.00 114 99.10 100.00 1.28e-72 PDB 3N9Z "Crystal Structure Of Human Cyp11a1 In Complex With 22- Hydroxycholesterol" 100.00 123 99.10 100.00 7.90e-73 PDB 3NA0 "Crystal Structure Of Human Cyp11a1 In Complex With 20,22- Dihydroxycholesterol" 61.26 68 98.53 100.00 2.21e-39 PDB 3NA1 "Crystal Structure Of Human Cyp11a1 In Complex With 20- Hydroxycholesterol" 100.00 123 99.10 100.00 7.90e-73 PDB 3P1M "Crystal Structure Of Human Ferredoxin-1 (Fdx1) In Complex With Iron- Sulfur Cluster" 100.00 132 99.10 100.00 4.75e-73 DBJ BAG73145 "ferredoxin 1 [synthetic construct]" 100.00 184 99.10 100.00 8.25e-74 GB AAA35829 "ferredoxin [Homo sapiens]" 100.00 184 99.10 100.00 8.25e-74 GB AAA35855 "ferredoxin, partial [Homo sapiens]" 63.06 80 98.57 100.00 5.27e-42 GB AAA35856 "ferredoxin, partial [Homo sapiens]" 63.06 80 98.57 100.00 5.27e-42 GB AAA50462 "adrenodoxin [Homo sapiens]" 100.00 184 99.10 100.00 8.25e-74 GB AAA76853 "ferredoxin [Homo sapiens]" 100.00 184 99.10 100.00 8.25e-74 REF NP_004100 "adrenodoxin, mitochondrial precursor [Homo sapiens]" 100.00 184 99.10 100.00 8.25e-74 REF XP_001105034 "PREDICTED: hypothetical protein LOC709110 [Macaca mulatta]" 100.00 335 99.10 100.00 1.90e-75 REF XP_003253520 "PREDICTED: adrenodoxin, mitochondrial [Nomascus leucogenys]" 100.00 184 99.10 100.00 8.80e-74 REF XP_003910717 "PREDICTED: adrenodoxin, mitochondrial [Papio anubis]" 100.00 184 99.10 100.00 7.64e-74 REF XP_003923949 "PREDICTED: adrenodoxin, mitochondrial, partial [Saimiri boliviensis boliviensis]" 100.00 163 98.20 100.00 1.02e-72 SP P10109 "RecName: Full=Adrenodoxin, mitochondrial; AltName: Full=Adrenal ferredoxin; AltName: Full=Ferredoxin-1; AltName: Full=Hepatored" 100.00 184 99.10 100.00 8.25e-74 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 Tue Jun 14 11:26:54 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 $Adx 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 $Adx '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 $Adx 1.5 mM '[U-90% 13C; U-90% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-13C_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Experimental_Conditions _Saveframe_category sample_conditions _Details 'The sample was equilibrated 0.5 hours before the spectra were collected.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 290 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Experimental_Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'human Adx (4-114), chain A' _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 GLU H H 8.42 . 1 2 . 1 GLU HA H 4.23 . 1 3 . 1 GLU HB2 H 2.03 . 2 4 . 1 GLU HB3 H 1.89 . 2 5 . 1 GLU HG2 H 2.40 . 2 6 . 1 GLU HG3 H 2.18 . 2 7 . 1 GLU C C 175.91 . 1 8 . 1 GLU CA C 56.57 . 1 9 . 1 GLU CB C 30.56 . 1 10 . 1 GLU CG C 35.87 . 1 11 . 1 GLU N N 122.42 . 1 12 . 2 ASP H H 8.30 . 1 13 . 2 ASP HA H 4.59 . 1 14 . 2 ASP HB2 H 3.03 . 2 15 . 2 ASP HB3 H 2.57 . 2 16 . 2 ASP C C 175.57 . 1 17 . 2 ASP CA C 54.35 . 1 18 . 2 ASP CB C 41.39 . 1 19 . 2 ASP N N 120.52 . 1 20 . 3 LYS H H 8.20 . 1 21 . 3 LYS HA H 4.87 . 1 22 . 3 LYS HB2 H 1.69 . 2 23 . 3 LYS HB3 H 1.49 . 2 24 . 3 LYS HG2 H 1.37 . 2 25 . 3 LYS HG3 H 1.29 . 2 26 . 3 LYS HD2 H 1.50 . 2 27 . 3 LYS HD3 H 1.02 . 2 28 . 3 LYS HE2 H 3.05 . 2 29 . 3 LYS HE3 H 2.95 . 2 30 . 3 LYS C C 176.19 . 1 31 . 3 LYS CA C 55.40 . 1 32 . 3 LYS CB C 35.83 . 1 33 . 3 LYS CG C 25.34 . 1 34 . 3 LYS CD C 28.78 . 1 35 . 3 LYS CE C 43.78 . 1 36 . 3 LYS N N 120.19 . 1 37 . 4 ILE H H 8.98 . 1 38 . 4 ILE HA H 4.43 . 1 39 . 4 ILE HB H 1.84 . 1 40 . 4 ILE HG12 H 0.84 . 2 41 . 4 ILE HG13 H 0.66 . 2 42 . 4 ILE HG2 H 1.06 . 1 43 . 4 ILE C C 175.57 . 1 44 . 4 ILE CA C 58.92 . 1 45 . 4 ILE CB C 40.84 . 1 46 . 4 ILE CG1 C 25.13 . 1 47 . 4 ILE CG2 C 17.70 . 1 48 . 4 ILE N N 118.38 . 1 49 . 5 THR H H 8.88 . 1 50 . 5 THR HA H 4.70 . 1 51 . 5 THR HB H 3.85 . 1 52 . 5 THR HG2 H 0.76 . 1 53 . 5 THR C C 174.01 . 1 54 . 5 THR CA C 63.49 . 1 55 . 5 THR CB C 69.87 . 1 56 . 5 THR CG2 C 20.44 . 1 57 . 5 THR N N 122.37 . 1 58 . 6 VAL H H 8.52 . 1 59 . 6 VAL HA H 4.21 . 1 60 . 6 VAL HB H 1.58 . 1 61 . 6 VAL HG1 H 0.69 . 2 62 . 6 VAL HG2 H 0.36 . 2 63 . 6 VAL C C 173.43 . 1 64 . 6 VAL CA C 60.79 . 1 65 . 6 VAL CB C 35.77 . 1 66 . 6 VAL CG1 C 21.90 . 1 67 . 6 VAL CG2 C 22.84 . 1 68 . 6 VAL N N 124.64 . 1 69 . 7 HIS H H 8.61 . 1 70 . 7 HIS HA H 5.49 . 1 71 . 7 HIS HB2 H 3.40 . 2 72 . 7 HIS HB3 H 2.68 . 2 73 . 7 HIS HD2 H 7.78 . 1 74 . 7 HIS HE1 H 6.67 . 1 75 . 7 HIS C C 174.41 . 1 76 . 7 HIS CA C 53.64 . 1 77 . 7 HIS CB C 31.65 . 1 78 . 7 HIS CD2 C 117.74 . 1 79 . 7 HIS CE1 C 137.45 . 1 80 . 7 HIS N N 125.25 . 1 81 . 8 PHE H H 9.65 . 1 82 . 8 PHE HA H 5.18 . 1 83 . 8 PHE HB2 H 3.03 . 2 84 . 8 PHE HB3 H 2.26 . 2 85 . 8 PHE HD1 H 7.23 . 1 86 . 8 PHE HD2 H 7.23 . 1 87 . 8 PHE HE1 H 6.74 . 1 88 . 8 PHE HE2 H 6.74 . 1 89 . 8 PHE HZ H 7.53 . 1 90 . 8 PHE C C 175.57 . 1 91 . 8 PHE CA C 55.64 . 1 92 . 8 PHE CB C 42.45 . 1 93 . 8 PHE CD1 C 124.79 . 1 94 . 8 PHE CD2 C 124.79 . 1 95 . 8 PHE CE1 C 125.03 . 1 96 . 8 PHE CE2 C 125.03 . 1 97 . 8 PHE CZ C 124.60 . 1 98 . 8 PHE N N 122.65 . 1 99 . 9 ILE H H 9.05 . 1 100 . 9 ILE HA H 4.69 . 1 101 . 9 ILE HB H 1.73 . 1 102 . 9 ILE HG12 H 1.23 . 2 103 . 9 ILE HG13 H 0.96 . 2 104 . 9 ILE HG2 H 0.85 . 1 105 . 9 ILE HD1 H 0.66 . 1 106 . 9 ILE C C 176.19 . 1 107 . 9 ILE CA C 60.44 . 1 108 . 9 ILE CB C 37.28 . 1 109 . 9 ILE CG1 C 26.69 . 1 110 . 9 ILE CG2 C 16.82 . 1 111 . 9 ILE CD1 C 12.52 . 1 112 . 9 ILE N N 123.13 . 1 113 . 10 ASN H H 8.93 . 1 114 . 10 ASN HA H 4.65 . 1 115 . 10 ASN HB2 H 3.47 . 2 116 . 10 ASN HB3 H 2.95 . 2 117 . 10 ASN C C 177.90 . 1 118 . 10 ASN CA C 51.18 . 1 119 . 10 ASN CB C 38.31 . 1 120 . 10 ASN N N 125.09 . 1 121 . 11 ARG H H 8.61 . 1 122 . 11 ARG HA H 4.04 . 2 123 . 11 ARG HB2 H 2.07 . 2 124 . 11 ARG HB3 H 2.02 . 2 125 . 11 ARG HG2 H 1.56 . 2 126 . 11 ARG C C 176.19 . 1 127 . 11 ARG CA C 59.27 . 1 128 . 11 ARG CB C 29.73 . 1 129 . 11 ARG CG C 28.78 . 1 130 . 11 ARG CD C 43.97 . 1 131 . 11 ARG N N 119.22 . 1 132 . 12 ASP H H 7.69 . 1 133 . 12 ASP HA H 4.67 . 1 134 . 12 ASP HB2 H 2.78 . 2 135 . 12 ASP HB3 H 2.61 . 2 136 . 12 ASP C C 176.97 . 1 137 . 12 ASP CA C 53.41 . 1 138 . 12 ASP CB C 40.93 . 1 139 . 12 ASP N N 116.04 . 1 140 . 13 GLY H H 8.17 . 1 141 . 13 GLY HA2 H 4.21 . 2 142 . 13 GLY HA3 H 3.50 . 2 143 . 13 GLY C C 174.32 . 1 144 . 13 GLY CA C 45.21 . 1 145 . 13 GLY N N 108.39 . 1 146 . 14 GLU H H 7.96 . 1 147 . 14 GLU HA H 4.26 . 1 148 . 14 GLU HB2 H 2.12 . 2 149 . 14 GLU HB3 H 1.75 . 2 150 . 14 GLU HG2 H 2.37 . 2 151 . 14 GLU C C 175.57 . 1 152 . 14 GLU CA C 56.10 . 1 153 . 14 GLU CB C 30.72 . 1 154 . 14 GLU CG C 35.97 . 1 155 . 14 GLU N N 122.33 . 1 156 . 15 THR H H 8.70 . 1 157 . 15 THR HA H 4.89 . 1 158 . 15 THR HB H 4.03 . 1 159 . 15 THR HG2 H 1.07 . 1 160 . 15 THR C C 174.32 . 1 161 . 15 THR CA C 62.90 . 1 162 . 15 THR CB C 69.32 . 1 163 . 15 THR CG2 C 21.28 . 1 164 . 15 THR N N 119.21 . 1 165 . 16 LEU H H 10.05 . 1 166 . 16 LEU HA H 4.79 . 1 167 . 16 LEU HB2 H 1.91 . 2 168 . 16 LEU HB3 H 1.48 . 2 169 . 16 LEU HG H 1.71 . 1 170 . 16 LEU HD1 H 0.87 . 2 171 . 16 LEU HD2 H 0.77 . 2 172 . 16 LEU C C 175.72 . 1 173 . 16 LEU CA C 53.41 . 1 174 . 16 LEU CB C 42.0 . 1 175 . 16 LEU N N 131.44 . 1 176 . 17 THR H H 8.94 . 1 177 . 17 THR HA H 4.98 . 1 178 . 17 THR HB H 3.95 . 1 179 . 17 THR HG2 H 1.17 . 1 180 . 17 THR C C 174.01 . 1 181 . 17 THR CA C 63.37 . 1 182 . 17 THR CB C 70.28 . 1 183 . 17 THR CG2 C 22.22 . 1 184 . 17 THR N N 122.83 . 1 185 . 18 THR H H 8.86 . 1 186 . 18 THR HA H 4.72 . 1 187 . 18 THR HB H 3.82 . 1 188 . 18 THR HG2 H 0.93 . 1 189 . 18 THR C C 171.84 . 1 190 . 18 THR CA C 60.09 . 1 191 . 18 THR CB C 70.49 . 1 192 . 18 THR CG2 C 20.03 . 1 193 . 18 THR N N 122.63 . 1 194 . 19 LYS H H 8.02 . 1 195 . 19 LYS HA H 5.61 . 1 196 . 19 LYS HB2 H 1.74 . 2 197 . 19 LYS HB3 H 1.50 . 2 198 . 19 LYS HG2 H 1.37 . 2 199 . 19 LYS HG3 H 1.23 . 2 200 . 19 LYS HD2 H 1.46 . 2 201 . 19 LYS HD3 H 1.31 . 2 202 . 19 LYS HE2 H 2.81 . 2 203 . 19 LYS HE3 H 2.21 . 2 204 . 19 LYS C C 176.40 . 1 205 . 19 LYS CA C 53.99 . 1 206 . 19 LYS CB C 36.32 . 1 207 . 19 LYS CG C 25.03 . 1 208 . 19 LYS CD C 29.72 . 1 209 . 19 LYS CE C 41.63 . 1 210 . 19 LYS N N 118.47 . 1 211 . 20 GLY H H 8.87 . 1 212 . 20 GLY HA2 H 4.70 . 2 213 . 20 GLY HA3 H 3.34 . 2 214 . 20 GLY C C 171.06 . 1 215 . 20 GLY CA C 43.68 . 1 216 . 20 GLY N N 107.23 . 1 217 . 21 LYS H H 8.78 . 1 218 . 21 LYS HA H 4.67 . 1 219 . 21 LYS HB2 H 1.65 . 2 220 . 21 LYS HB3 H 1.45 . 2 221 . 21 LYS HG2 H 1.37 . 2 222 . 21 LYS HG3 H 1.44 . 2 223 . 21 LYS HD2 H 1.75 . 2 224 . 21 LYS C C 176.34 . 1 225 . 21 LYS CA C 55.17 . 1 226 . 21 LYS CB C 33.50 . 1 227 . 21 LYS CG C 24.09 . 1 228 . 21 LYS CD C 28.15 . 1 229 . 21 LYS N N 121.33 . 1 230 . 22 VAL H H 8.42 . 1 231 . 22 VAL HA H 3.22 . 1 232 . 22 VAL HB H 1.94 . 1 233 . 22 VAL HG1 H 0.98 . 2 234 . 22 VAL HG2 H 0.86 . 2 235 . 22 VAL C C 177.43 . 1 236 . 22 VAL CA C 65.71 . 1 237 . 22 VAL CB C 30.86 . 1 238 . 22 VAL CG1 C 21.59 . 2 239 . 22 VAL CG2 C 22.53 . 2 240 . 22 VAL N N 122.46 . 1 241 . 23 GLY H H 8.83 . 1 242 . 23 GLY HA2 H 4.54 . 1 243 . 23 GLY HA3 H 3.56 . 1 244 . 23 GLY C C 174.48 . 1 245 . 23 GLY CA C 45.09 . 1 246 . 23 GLY N N 116.85 . 1 247 . 24 ASP H H 8.18 . 1 248 . 24 ASP HA H 4.79 . 1 249 . 24 ASP HB2 H 2.83 . 2 250 . 24 ASP C C 178.99 . 1 251 . 24 ASP CA C 54.70 . 1 252 . 24 ASP CB C 41.56 . 1 253 . 24 ASP N N 123.07 . 1 254 . 25 SER H H 9.58 . 1 255 . 25 SER HA H 5.75 . 1 256 . 25 SER HB2 H 4.30 . 2 257 . 25 SER HB3 H 4.04 . 2 258 . 25 SER C C 176.65 . 1 259 . 25 SER CA C 57.04 . 1 260 . 25 SER CB C 66.28 . 1 261 . 25 SER N N 120.94 . 1 262 . 26 LEU H H 8.27 . 1 263 . 26 LEU HA H 4.58 . 1 264 . 26 LEU HB2 H 2.27 . 2 265 . 26 LEU HB3 H 1.41 . 2 266 . 26 LEU HG H 1.93 . 1 267 . 26 LEU HD1 H 0.99 . 2 268 . 26 LEU HD2 H 0.84 . 2 269 . 26 LEU C C 178.68 . 1 270 . 26 LEU CA C 57.98 . 1 271 . 26 LEU CB C 41.18 . 1 272 . 26 LEU CG C 26.01 . 1 273 . 26 LEU CD1 C 24.15 . 2 274 . 26 LEU CD2 C 23.27 . 2 275 . 26 LEU N N 119.04 . 1 276 . 27 LEU H H 7.24 . 1 277 . 27 LEU C C 175.57 . 1 278 . 27 LEU CA C 55.71 . 1 279 . 27 LEU CB C 42.75 . 1 280 . 27 LEU N N 116.56 . 1 281 . 28 ASP H H 7.88 . 1 282 . 28 ASP HA H 4.34 . 1 283 . 28 ASP HB2 H 2.72 . 2 284 . 28 ASP HB3 H 2.56 . 2 285 . 28 ASP C C 178.21 . 1 286 . 28 ASP CA C 57.98 . 1 287 . 28 ASP CB C 40.34 . 1 288 . 28 ASP N N 121.81 . 1 289 . 29 VAL H H 7.82 . 1 290 . 29 VAL HA H 3.79 . 1 291 . 29 VAL HB H 2.32 . 1 292 . 29 VAL HG1 H 1.18 . 2 293 . 29 VAL HG2 H 0.90 . 2 294 . 29 VAL C C 178.68 . 1 295 . 29 VAL CA C 66.18 . 1 296 . 29 VAL CB C 32.21 . 1 297 . 29 VAL CG1 C 22.59 . 2 298 . 29 VAL CG2 C 23.78 . 2 299 . 29 VAL N N 117.05 . 1 300 . 30 VAL H H 7.48 . 1 301 . 30 VAL HA H 3.04 . 1 302 . 30 VAL HB H 2.21 . 1 303 . 30 VAL HG1 H 0.63 . 2 304 . 30 VAL HG2 H 0.27 . 2 305 . 30 VAL C C 177.90 . 1 306 . 30 VAL CA C 67.12 . 1 307 . 30 VAL CB C 32.28 . 1 308 . 30 VAL CG1 C 20.65 . 2 309 . 30 VAL CG2 C 23.78 . 2 310 . 30 VAL N N 121.62 . 1 311 . 31 VAL H H 8.42 . 1 312 . 31 VAL HA H 3.77 . 1 313 . 31 VAL HB H 2.16 . 1 314 . 31 VAL HG1 H 0.90 . 2 315 . 31 VAL HG2 H 1.14 . 2 316 . 31 VAL C C 180.85 . 1 317 . 31 VAL CA C 66.42 . 1 318 . 31 VAL CB C 32.09 . 1 319 . 31 VAL CG1 C 21.15 . 2 320 . 31 VAL CG2 C 21.61 . 2 321 . 31 VAL N N 118.59 . 1 322 . 32 GLU H H 9.16 . 1 323 . 32 GLU HA H 4.09 . 1 324 . 32 GLU HB2 H 2.07 . 2 325 . 32 GLU HB3 H 2.12 . 2 326 . 32 GLU HG2 H 2.42 . 2 327 . 32 GLU HG3 H 2.34 . 2 328 . 32 GLU C C 177.74 . 1 329 . 32 GLU CA C 59.15 . 1 330 . 32 GLU CB C 29.56 . 1 331 . 32 GLU CG C 35.97 . 1 332 . 32 GLU N N 120.39 . 1 333 . 33 ASN H H 7.17 . 1 334 . 33 ASN HA H 4.72 . 1 335 . 33 ASN HB2 H 2.76 . 2 336 . 33 ASN HB3 H 2.61 . 2 337 . 33 ASN C C 173.08 . 1 338 . 33 ASN CA C 53.53 . 1 339 . 33 ASN CB C 39.85 . 1 340 . 33 ASN N N 111.49 . 1 341 . 34 ASN H H 7.86 . 1 342 . 34 ASN HA H 4.36 . 1 343 . 34 ASN HB2 H 2.96 . 2 344 . 34 ASN HB3 H 2.60 . 2 345 . 34 ASN C C 174.79 . 1 346 . 34 ASN CA C 53.99 . 1 347 . 34 ASN CB C 37.58 . 1 348 . 34 ASN N N 117.61 . 1 349 . 35 LEU H H 7.83 . 1 350 . 35 LEU HA H 4.06 . 1 351 . 35 LEU HB2 H 1.27 . 2 352 . 35 LEU HG H 1.68 . 1 353 . 35 LEU C C 178.09 . 1 354 . 35 LEU CA C 55.40 . 1 355 . 35 LEU CB C 42.23 . 1 356 . 35 LEU CG C 26.59 . 1 357 . 35 LEU N N 115.40 . 1 358 . 36 ASP H H 8.58 . 1 359 . 36 ASP HA H 4.59 . 1 360 . 36 ASP HB2 H 2.69 . 2 361 . 36 ASP HB3 H 2.60 . 2 362 . 36 ASP C C 174.63 . 1 363 . 36 ASP CA C 53.39 . 1 364 . 36 ASP CB C 39.78 . 1 365 . 36 ASP N N 122.81 . 1 366 . 37 ILE H H 7.61 . 1 367 . 37 ILE HA H 4.17 . 1 368 . 37 ILE HB H 1.31 . 1 369 . 37 ILE HG12 H 0.92 . 2 370 . 37 ILE HG13 H 0.63 . 2 371 . 37 ILE HG2 H 0.96 . 1 372 . 37 ILE HD1 H 0.05 . 1 373 . 37 ILE C C 175.88 . 1 374 . 37 ILE CA C 60.09 . 1 375 . 37 ILE CB C 38.71 . 1 376 . 37 ILE CG1 C 25.65 . 2 377 . 37 ILE CG2 C 18.78 . 2 378 . 37 ILE CD1 C 12.53 . 1 379 . 37 ILE N N 123.91 . 1 380 . 38 ASP H H 8.56 . 1 381 . 38 ASP HA H 4.37 . 1 382 . 38 ASP HB2 H 2.70 . 2 383 . 38 ASP HB3 H 2.56 . 2 384 . 38 ASP C C 178.21 . 1 385 . 38 ASP CA C 56.81 . 1 386 . 38 ASP CB C 41.90 . 1 387 . 38 ASP N N 127.48 . 1 388 . 39 GLY H H 9.04 . 1 389 . 39 GLY HA2 H 4.09 . 2 390 . 39 GLY HA3 H 3.75 . 2 391 . 39 GLY C C 174.01 . 1 392 . 39 GLY CA C 46.03 . 1 393 . 39 GLY N N 113.74 . 1 394 . 40 PHE H H 7.67 . 1 395 . 40 PHE HA H 4.68 . 1 396 . 40 PHE HB2 H 3.14 . 2 397 . 40 PHE HD1 H 6.86 . 3 398 . 40 PHE HE1 H 7.05 . 3 399 . 40 PHE HZ H 7.46 . 1 400 . 40 PHE CA C 60.32 . 1 401 . 40 PHE CB C 41.12 . 1 402 . 40 PHE CD1 C 138.12 . 3 403 . 40 PHE N N 120.86 . 1 404 . 54 LEU H H 9.41 . 1 405 . 54 LEU HA H 4.85 . 1 406 . 54 LEU HB2 H 1.70 . 2 407 . 54 LEU HB3 H 0.94 . 2 408 . 54 LEU HG H 1.02 . 1 409 . 54 LEU HD1 H 0.64 . 2 410 . 54 LEU C C 173.55 . 1 411 . 54 LEU CA C 53.89 . 1 412 . 54 LEU CB C 49.63 . 1 413 . 54 LEU CG C 28.15 . 1 414 . 54 LEU CD1 C 25.13 . 2 415 . 54 LEU N N 128.30 . 1 416 . 55 ILE H H 8.53 . 1 417 . 55 ILE HA H 4.53 . 1 418 . 55 ILE HB H 1.41 . 1 419 . 55 ILE HG12 H 1.28 . 2 420 . 55 ILE HG13 H 0.96 . 2 421 . 55 ILE HG2 H 0.87 . 1 422 . 55 ILE C C 177.12 . 1 423 . 55 ILE CA C 61.26 . 1 424 . 55 ILE CB C 40.39 . 1 425 . 55 ILE CG1 C 28.06 . 2 426 . 55 ILE CG2 C 17.41 . 2 427 . 55 ILE N N 119.75 . 1 428 . 56 PHE H H 8.76 . 1 429 . 56 PHE HA H 4.53 . 1 430 . 56 PHE HB2 H 3.21 . 2 431 . 56 PHE HB3 H 2.91 . 2 432 . 56 PHE C C 175.47 . 1 433 . 56 PHE CA C 58.47 . 1 434 . 56 PHE CB C 43.53 . 1 435 . 56 PHE N N 127.56 . 1 436 . 57 GLU H H 9.05 . 1 437 . 57 GLU HA H 4.34 . 1 438 . 57 GLU HB2 H 2.05 . 2 439 . 57 GLU HB3 H 1.93 . 2 440 . 57 GLU HG2 H 2.36 . 2 441 . 57 GLU HG3 H 2.27 . 2 442 . 57 GLU C C 178.83 . 1 443 . 57 GLU CA C 56.81 . 1 444 . 57 GLU CB C 32.80 . 1 445 . 57 GLU CG C 36.59 . 1 446 . 57 GLU N N 118.84 . 1 447 . 58 ASP H H 9.31 . 1 448 . 58 ASP HA H 4.15 . 1 449 . 58 ASP HB2 H 2.83 . 2 450 . 58 ASP HB3 H 2.64 . 2 451 . 58 ASP C C 177.48 . 1 452 . 58 ASP CA C 59.15 . 1 453 . 58 ASP CB C 41.65 . 1 454 . 58 ASP N N 123.73 . 1 455 . 59 HIS H H 8.53 . 1 456 . 59 HIS HA H 4.52 . 1 457 . 59 HIS HB2 H 3.22 . 2 458 . 59 HIS HB3 H 3.11 . 2 459 . 59 HIS HD2 H 7.85 . 2 460 . 59 HIS HE1 H 6.77 . 2 461 . 59 HIS C C 176.86 . 1 462 . 59 HIS CA C 58.45 . 1 463 . 59 HIS CB C 28.78 . 1 464 . 59 HIS CD2 C 117.11 . 1 465 . 59 HIS CE1 C 138.38 . 1 466 . 59 HIS N N 114.01 . 1 467 . 60 ILE H H 6.33 . 1 468 . 60 ILE HA H 3.84 . 1 469 . 60 ILE HB H 2.17 . 1 470 . 60 ILE HG12 H 1.07 . 2 471 . 60 ILE HG13 H 1.12 . 2 472 . 60 ILE HG2 H 0.81 . 1 473 . 60 ILE HD1 H 0.68 . 1 474 . 60 ILE C C 177.90 . 1 475 . 60 ILE CA C 59.85 . 1 476 . 60 ILE CB C 36.65 . 1 477 . 60 ILE CG1 C 25.03 . 1 478 . 60 ILE CG2 C 17.22 . 1 479 . 60 ILE CD1 C 9.11 . 1 480 . 60 ILE N N 119.51 . 1 481 . 61 TYR H H 8.70 . 1 482 . 61 TYR HA H 3.59 . 1 483 . 61 TYR HB2 H 3.05 . 2 484 . 61 TYR HB3 H 2.87 . 2 485 . 61 TYR HD1 H 6.75 . 3 486 . 61 TYR HE1 H 6.60 . 3 487 . 61 TYR C C 177.59 . 1 488 . 61 TYR CA C 61.73 . 1 489 . 61 TYR CB C 39.78 . 1 490 . 61 TYR CD1 C 138.38 . 3 491 . 61 TYR CE1 C 137.35 . 3 492 . 61 TYR N N 119.86 . 1 493 . 62 GLU H H 7.85 . 1 494 . 62 GLU HA H 4.06 . 1 495 . 62 GLU HB2 H 2.07 . 2 496 . 62 GLU HB3 H 1.88 . 2 497 . 62 GLU HG2 H 2.46 . 2 498 . 62 GLU C C 176.50 . 1 499 . 62 GLU CA C 57.98 . 1 500 . 62 GLU CB C 30.15 . 1 501 . 62 GLU CG C 35.34 . 1 502 . 62 GLU N N 113.22 . 1 503 . 63 LYS H H 7.23 . 1 504 . 63 LYS HA H 4.42 . 1 505 . 63 LYS HB2 H 2.07 . 2 506 . 63 LYS HB3 H 1.75 . 2 507 . 63 LYS HG2 H 1.66 . 2 508 . 63 LYS HG3 H 1.40 . 2 509 . 63 LYS HD2 H 1.64 . 2 510 . 63 LYS HE2 H 3.05 . 2 511 . 63 LYS C C 176.65 . 1 512 . 63 LYS CA C 54.72 . 1 513 . 63 LYS CB C 33.42 . 1 514 . 63 LYS CG C 24.15 . 1 515 . 63 LYS CD C 28.64 . 1 516 . 63 LYS CE C 41.73 . 1 517 . 63 LYS N N 115.99 . 1 518 . 64 LEU H H 6.83 . 1 519 . 64 LEU HA H 4.06 . 1 520 . 64 LEU HB2 H 1.31 . 2 521 . 64 LEU HB3 H 0.92 . 2 522 . 64 LEU HG H 1.83 . 1 523 . 64 LEU HD1 H 0.52 . 2 524 . 64 LEU HD2 H -0.02 . 2 525 . 64 LEU C C 177.12 . 1 526 . 64 LEU CA C 54.46 . 1 527 . 64 LEU CB C 41.58 . 1 528 . 64 LEU CG C 26.98 . 1 529 . 64 LEU CD1 C 22.84 . 2 530 . 64 LEU CD2 C 25.34 . 2 531 . 64 LEU N N 119.80 . 1 532 . 65 ASP H H 9.12 . 1 533 . 65 ASP HA H 4.32 . 1 534 . 65 ASP HB2 H 2.68 . 2 535 . 65 ASP HB3 H 2.60 . 2 536 . 65 ASP C C 175.41 . 1 537 . 65 ASP CA C 54.70 . 1 538 . 65 ASP CB C 41.03 . 1 539 . 65 ASP N N 122.52 . 1 540 . 66 ALA H H 8.20 . 1 541 . 66 ALA HA H 4.00 . 1 542 . 66 ALA HB H 1.36 . 1 543 . 66 ALA C C 178.21 . 1 544 . 66 ALA CA C 52.59 . 1 545 . 66 ALA CB C 19.02 . 1 546 . 66 ALA N N 122.31 . 1 547 . 67 ILE H H 8.40 . 1 548 . 67 ILE HA H 4.61 . 1 549 . 67 ILE HB H 1.52 . 1 550 . 67 ILE HG12 H 1.44 . 2 551 . 67 ILE HG13 H 1.28 . 2 552 . 67 ILE HG2 H 0.90 . 1 553 . 67 ILE HD1 H 0.81 . 1 554 . 67 ILE C C 176.65 . 1 555 . 67 ILE CA C 63.14 . 1 556 . 67 ILE CB C 39.33 . 1 557 . 67 ILE CG1 C 28.06 . 2 558 . 67 ILE N N 124.26 . 1 559 . 68 THR H H 8.14 . 1 560 . 68 THR HA H 4.57 . 1 561 . 68 THR HB H 4.68 . 1 562 . 68 THR HG2 H 1.23 . 1 563 . 68 THR C C 175.72 . 1 564 . 68 THR CA C 61.03 . 1 565 . 68 THR CB C 72.28 . 1 566 . 68 THR CG2 C 21.59 . 1 567 . 68 THR N N 119.12 . 1 568 . 69 ASP H H 9.06 . 1 569 . 69 ASP HA H 4.28 . 1 570 . 69 ASP HB2 H 2.67 . 2 571 . 69 ASP HB3 H 2.56 . 2 572 . 69 ASP C C 177.74 . 1 573 . 69 ASP CA C 57.74 . 1 574 . 69 ASP CB C 41.31 . 1 575 . 69 ASP N N 123.64 . 1 576 . 70 GLU H H 8.97 . 1 577 . 70 GLU HA H 4.03 . 1 578 . 70 GLU HB2 H 1.82 . 2 579 . 70 GLU HG2 H 2.37 . 2 580 . 70 GLU HG3 H 2.20 . 2 581 . 70 GLU C C 179.45 . 1 582 . 70 GLU CA C 60.56 . 1 583 . 70 GLU CB C 28.54 . 1 584 . 70 GLU CG C 36.65 . 1 585 . 70 GLU N N 117.27 . 1 586 . 71 GLU H H 7.53 . 1 587 . 71 GLU HA H 4.09 . 1 588 . 71 GLU HB2 H 2.23 . 2 589 . 71 GLU HB3 H 2.08 . 2 590 . 71 GLU HG2 H 2.84 . 2 591 . 71 GLU C C 178.05 . 1 592 . 71 GLU CA C 59.39 . 1 593 . 71 GLU CB C 29.31 . 1 594 . 71 GLU N N 119.54 . 1 595 . 72 ASN H H 8.60 . 1 596 . 72 ASN HA H 4.36 . 1 597 . 72 ASN HB2 H 2.99 . 2 598 . 72 ASN HB3 H 2.57 . 2 599 . 72 ASN C C 177.12 . 1 600 . 72 ASN CA C 57.04 . 1 601 . 72 ASN CB C 39.81 . 1 602 . 72 ASN N N 119.83 . 1 603 . 73 ASP H H 8.32 . 1 604 . 73 ASP HA H 4.32 . 1 605 . 73 ASP HB2 H 2.69 . 2 606 . 73 ASP HB3 H 2.59 . 2 607 . 73 ASP C C 178.68 . 1 608 . 73 ASP CA C 57.28 . 1 609 . 73 ASP CB C 41.18 . 1 610 . 73 ASP N N 117.14 . 1 611 . 74 MET H H 7.03 . 1 612 . 74 MET HA H 4.52 . 1 613 . 74 MET HB2 H 2.26 . 2 614 . 74 MET HG2 H 2.57 . 2 615 . 74 MET HG3 H 2.50 . 2 616 . 74 MET HE H 1.64 . 1 617 . 74 MET C C 179.92 . 1 618 . 74 MET CA C 55.64 . 1 619 . 74 MET CB C 34.78 . 1 620 . 74 MET CG C 32.22 . 1 621 . 74 MET CE C 19.27 . 1 622 . 74 MET N N 116.01 . 1 623 . 75 LEU H H 8.86 . 1 624 . 75 LEU HA H 3.76 . 1 625 . 75 LEU HB2 H 1.75 . 2 626 . 75 LEU HB3 H 1.60 . 2 627 . 75 LEU HG H 1.74 . 1 628 . 75 LEU HD1 H 0.93 . 2 629 . 75 LEU HD2 H 0.87 . 2 630 . 75 LEU C C 178.52 . 1 631 . 75 LEU CA C 57.74 . 1 632 . 75 LEU CB C 41.93 . 1 633 . 75 LEU CG C 26.59 . 1 634 . 75 LEU CD1 C 24.09 . 2 635 . 75 LEU CD2 C 23.27 . 2 636 . 75 LEU N N 123.93 . 1 637 . 76 ASP H H 7.96 . 1 638 . 76 ASP HA H 4.36 . 1 639 . 76 ASP HB2 H 2.64 . 2 640 . 76 ASP HB3 H 2.56 . 2 641 . 76 ASP C C 177.59 . 1 642 . 76 ASP CA C 56.81 . 1 643 . 76 ASP CB C 41.71 . 1 644 . 76 ASP N N 115.57 . 1 645 . 77 LEU H H 7.06 . 1 646 . 77 LEU HA H 4.36 . 1 647 . 77 LEU HB2 H 1.66 . 2 648 . 77 LEU HB3 H 1.44 . 2 649 . 77 LEU HG H 1.52 . 1 650 . 77 LEU HD1 H 0.88 . 2 651 . 77 LEU HD2 H 0.47 . 2 652 . 77 LEU C C 177.28 . 1 653 . 77 LEU CA C 53.99 . 1 654 . 77 LEU CB C 42.59 . 1 655 . 77 LEU CG C 26.49 . 1 656 . 77 LEU CD1 C 25.03 . 2 657 . 77 LEU CD2 C 22.10 . 2 658 . 77 LEU N N 116.73 . 1 659 . 78 ALA H H 7.87 . 1 660 . 78 ALA HA H 4.22 . 1 661 . 78 ALA HB H 1.32 . 1 662 . 78 ALA C C 177.12 . 1 663 . 78 ALA CA C 52.35 . 1 664 . 78 ALA CB C 19.41 . 1 665 . 78 ALA N N 124.31 . 1 666 . 79 TYR H H 8.33 . 1 667 . 79 TYR HA H 4.47 . 1 668 . 79 TYR HB2 H 2.89 . 2 669 . 79 TYR HB3 H 3.14 . 2 670 . 79 TYR HD1 H 7.07 . 3 671 . 79 TYR HE1 H 6.74 . 3 672 . 79 TYR C C 176.97 . 1 673 . 79 TYR CA C 58.45 . 1 674 . 79 TYR CB C 38.98 . 1 675 . 79 TYR CD1 C 125.56 . 3 676 . 79 TYR CE1 C 125.06 . 3 677 . 79 TYR N N 123.06 . 1 678 . 80 GLY H H 8.42 . 1 679 . 80 GLY HA2 H 4.56 . 2 680 . 80 GLY HA3 H 3.58 . 2 681 . 80 GLY C C 174.63 . 1 682 . 80 GLY CA C 46.26 . 1 683 . 80 GLY N N 112.95 . 1 684 . 81 LEU H H 7.24 . 1 685 . 81 LEU HA H 3.87 . 1 686 . 81 LEU HB2 H 1.53 . 2 687 . 81 LEU HB3 H 1.66 . 2 688 . 81 LEU HG H 1.48 . 2 689 . 81 LEU HD1 H 0.87 . 2 690 . 81 LEU HD2 H 0.81 . 2 691 . 81 LEU C C 176.65 . 1 692 . 81 LEU CA C 56.81 . 1 693 . 81 LEU CB C 42.91 . 1 694 . 81 LEU CG C 26.59 . 1 695 . 81 LEU CD1 C 25.03 . 2 696 . 81 LEU CD2 C 23.47 . 2 697 . 81 LEU N N 118.40 . 1 698 . 82 THR H H 8.87 . 1 699 . 82 THR HA H 4.94 . 1 700 . 82 THR HB H 4.40 . 1 701 . 82 THR HG2 H 1.28 . 1 702 . 82 THR C C 174.79 . 1 703 . 82 THR CA C 60.09 . 1 704 . 82 THR CB C 74.62 . 1 705 . 82 THR CG2 C 21.28 . 1 706 . 82 THR N N 117.74 . 1 707 . 83 ASP H H 8.51 . 1 708 . 83 ASP HA H 4.52 . 1 709 . 83 ASP HB2 H 2.77 . 2 710 . 83 ASP HB3 H 2.69 . 2 711 . 83 ASP C C 176.06 . 1 712 . 83 ASP CA C 54.23 . 1 713 . 83 ASP CB C 39.78 . 1 714 . 83 ASP N N 117.86 . 1 715 . 84 ARG H H 8.33 . 1 716 . 84 ARG HA H 4.27 . 1 717 . 84 ARG HB2 H 2.07 . 2 718 . 84 ARG HB3 H 1.94 . 2 719 . 84 ARG HG2 H 1.65 . 2 720 . 84 ARG HG3 H 1.58 . 2 721 . 84 ARG HD2 H 3.08 . 2 722 . 84 ARG C C 175.57 . 1 723 . 84 ARG CA C 53.76 . 1 724 . 84 ARG CB C 30.33 . 1 725 . 84 ARG CG C 26.90 . 1 726 . 84 ARG CD C 42.84 . 1 727 . 84 ARG N N 119.76 . 1 728 . 85 SER H H 7.04 . 1 729 . 85 SER HA H 5.46 . 1 730 . 85 SER HB2 H 4.02 . 2 731 . 85 SER HB3 H 3.93 . 2 732 . 85 SER HG H 11.36 . 1 733 . 85 SER C C 174.48 . 1 734 . 85 SER CA C 60.56 . 1 735 . 85 SER CB C 65.48 . 1 736 . 85 SER N N 120.06 . 1 737 . 86 ARG H H 9.39 . 1 738 . 86 ARG HA H 3.95 . 1 739 . 86 ARG CA C 52.81 . 1 740 . 86 ARG CB C 34.17 . 1 741 . 86 ARG N N 118.24 . 1 742 . 91 ILE HA H 4.25 . 1 743 . 91 ILE C C 174.01 . 1 744 . 91 ILE CA C 57.98 . 1 745 . 91 ILE CB C 37.08 . 1 746 . 92 CYS H H 8.12 . 1 747 . 92 CYS HA H 4.98 . 1 748 . 92 CYS HB2 H 2.69 . 2 749 . 92 CYS HB3 H 2.38 . 2 750 . 92 CYS C C 174.95 . 1 751 . 92 CYS CA C 57.28 . 1 752 . 92 CYS CB C 29.12 . 1 753 . 92 CYS N N 123.53 . 1 754 . 93 LEU H H 8.98 . 1 755 . 93 LEU HA H 4.72 . 1 756 . 93 LEU HB2 H 2.05 . 2 757 . 93 LEU HB3 H 1.11 . 2 758 . 93 LEU HG H 1.75 . 1 759 . 93 LEU HD1 H 0.76 . 2 760 . 93 LEU HD2 H 0.68 . 2 761 . 93 LEU C C 178.83 . 1 762 . 93 LEU CA C 55.40 . 1 763 . 93 LEU CB C 42.90 . 1 764 . 93 LEU CG C 28.78 . 1 765 . 93 LEU CD1 C 25.03 . 2 766 . 93 LEU N N 120.67 . 1 767 . 94 THR H H 7.81 . 1 768 . 94 THR HA H 4.68 . 1 769 . 94 THR HB H 4.60 . 1 770 . 94 THR HG2 H 1.22 . 1 771 . 94 THR C C 175.26 . 1 772 . 94 THR CA C 59.39 . 1 773 . 94 THR CB C 71.65 . 1 774 . 94 THR CG2 C 21.59 . 1 775 . 94 THR N N 113.86 . 1 776 . 95 LYS H H 9.19 . 1 777 . 95 LYS HA H 3.87 . 1 778 . 95 LYS HB2 H 1.85 . 2 779 . 95 LYS HB3 H 1.56 . 2 780 . 95 LYS HG2 H 1.48 . 2 781 . 95 LYS HE2 H 3.02 . 2 782 . 95 LYS HE3 H 2.74 . 2 783 . 95 LYS C C 178.99 . 1 784 . 95 LYS CA C 59.39 . 1 785 . 95 LYS CB C 32.28 . 1 786 . 95 LYS CG C 25.42 . 1 787 . 95 LYS CE C 40.66 . 1 788 . 95 LYS N N 121.13 . 1 789 . 96 SER H H 8.10 . 1 790 . 96 SER HA H 4.34 . 1 791 . 96 SER HB2 H 3.93 . 2 792 . 96 SER HB3 H 3.72 . 2 793 . 96 SER C C 174.63 . 1 794 . 96 SER CA C 60.32 . 1 795 . 96 SER CB C 62.62 . 1 796 . 96 SER N N 112.57 . 1 797 . 97 MET H H 7.68 . 1 798 . 97 MET HA H 4.11 . 1 799 . 97 MET HB2 H 2.54 . 2 800 . 97 MET HB3 H 2.07 . 2 801 . 97 MET HG2 H 2.64 . 2 802 . 97 MET HG3 H 2.51 . 2 803 . 97 MET HE H 2.11 . 1 804 . 97 MET C C 174.01 . 1 805 . 97 MET CA C 56.67 . 1 806 . 97 MET CB C 32.43 . 1 807 . 97 MET CG C 33.92 . 1 808 . 97 MET CE C 16.90 . 1 809 . 97 MET N N 120.43 . 1 810 . 98 ASP H H 7.23 . 1 811 . 98 ASP HA H 4.41 . 1 812 . 98 ASP HB2 H 2.69 . 2 813 . 98 ASP HB3 H 2.56 . 2 814 . 98 ASP C C 177.59 . 1 815 . 98 ASP CA C 56.89 . 1 816 . 98 ASP CB C 41.20 . 1 817 . 98 ASP N N 117.90 . 1 818 . 99 ASN H H 9.98 . 1 819 . 99 ASN HA H 3.84 . 1 820 . 99 ASN HB2 H 3.21 . 2 821 . 99 ASN HB3 H 3.01 . 2 822 . 99 ASN C C 174.32 . 1 823 . 99 ASN CA C 55.75 . 1 824 . 99 ASN CB C 38.53 . 1 825 . 99 ASN N N 122.46 . 1 826 . 100 MET H H 8.43 . 1 827 . 100 MET HA H 4.64 . 1 828 . 100 MET HB2 H 2.24 . 2 829 . 100 MET HB3 H 2.04 . 2 830 . 100 MET HG2 H 2.26 . 2 831 . 100 MET HG3 H 1.69 . 2 832 . 100 MET HE H 1.25 . 1 833 . 100 MET C C 173.08 . 1 834 . 100 MET CA C 56.57 . 1 835 . 100 MET CB C 31.03 . 1 836 . 100 MET CG C 33.47 . 1 837 . 100 MET CE C 21.59 . 1 838 . 100 MET N N 118.84 . 1 839 . 101 THR H H 8.69 . 1 840 . 101 THR HA H 5.41 . 1 841 . 101 THR HB H 3.76 . 1 842 . 101 THR HG2 H 0.96 . 1 843 . 101 THR C C 176.19 . 1 844 . 101 THR CA C 61.73 . 1 845 . 101 THR CB C 70.85 . 1 846 . 101 THR CG2 C 21.59 . 1 847 . 101 THR N N 117.40 . 1 848 . 102 VAL H H 9.13 . 1 849 . 102 VAL HA H 4.60 . 1 850 . 102 VAL HB H 1.36 . 1 851 . 102 VAL HG1 H 0.13 . 1 852 . 102 VAL HG2 H 0.02 . 1 853 . 102 VAL C C 173.39 . 1 854 . 102 VAL CA C 58.21 . 1 855 . 102 VAL CB C 34.54 . 1 856 . 102 VAL CG1 C 23.47 . 1 857 . 102 VAL CG2 C 19.72 . 1 858 . 102 VAL N N 123.36 . 1 859 . 103 ARG H H 8.41 . 1 860 . 103 ARG HA H 4.33 . 1 861 . 103 ARG HB2 H 1.63 . 2 862 . 103 ARG HB3 H 1.39 . 2 863 . 103 ARG HG2 H 1.72 . 2 864 . 103 ARG HD2 H 3.00 . 2 865 . 103 ARG CA C 54.46 . 1 866 . 103 ARG CB C 33.97 . 1 867 . 103 ARG N N 120.75 . 1 868 . 104 VAL H H 8.44 . 1 869 . 104 VAL HA H 4.47 . 1 870 . 104 VAL HB H 1.86 . 1 871 . 104 VAL HG1 H 0.98 . 2 872 . 104 VAL HG2 H 0.79 . 2 873 . 104 VAL C C 176.34 . 1 874 . 104 VAL CA C 59.62 . 1 875 . 104 VAL CB C 32.75 . 1 876 . 104 VAL N N 124.07 . 1 877 . 105 PRO HA H 4.28 . 1 878 . 105 PRO C C 176.19 . 1 879 . 105 PRO CA C 62.90 . 1 880 . 105 PRO CB C 32.26 . 1 881 . 106 GLU H H 8.63 . 1 882 . 106 GLU HA H 4.22 . 1 883 . 106 GLU HB3 H 2.05 . 2 884 . 106 GLU HG2 H 2.29 . 2 885 . 106 GLU C C 176.34 . 1 886 . 106 GLU CA C 57.28 . 1 887 . 106 GLU CB C 30.87 . 1 888 . 106 GLU CG C 36.59 . 1 889 . 106 GLU N N 120.92 . 1 890 . 107 THR H H 8.34 . 1 891 . 107 THR HA H 4.34 . 1 892 . 107 THR HB H 4.08 . 1 893 . 107 THR HG2 H 1.12 . 1 894 . 107 THR C C 174.01 . 1 895 . 107 THR CA C 61.26 . 1 896 . 107 THR CB C 70.25 . 1 897 . 107 THR CG2 C 21.28 . 1 898 . 107 THR N N 114.31 . 1 899 . 108 VAL H H 7.78 . 1 900 . 108 VAL HA H 3.92 . 1 901 . 108 VAL HB H 1.86 . 1 902 . 108 VAL HG1 H 1.08 . 2 903 . 108 VAL HG2 H 0.79 . 2 904 . 108 VAL C C 175.27 . 1 905 . 108 VAL CA C 61.73 . 1 906 . 108 VAL CB C 33.25 . 1 907 . 108 VAL CG1 C 17.53 . 1 908 . 108 VAL CG2 C 20.97 . 1 909 . 108 VAL N N 122.11 . 1 910 . 109 ALA H H 8.25 . 1 911 . 109 ALA HA H 4.21 . 1 912 . 109 ALA HB H 1.33 . 1 913 . 109 ALA C C 177.12 . 1 914 . 109 ALA CA C 52.71 . 1 915 . 109 ALA CB C 19.04 . 1 916 . 109 ALA N N 128.20 . 1 917 . 110 ASP H H 8.21 . 1 918 . 110 ASP HA H 4.50 . 1 919 . 110 ASP HB2 H 2.64 . 2 920 . 110 ASP HB3 H 2.56 . 2 921 . 110 ASP C C 174.95 . 1 922 . 110 ASP CA C 54.35 . 1 923 . 110 ASP CB C 41.37 . 1 924 . 110 ASP N N 121.38 . 1 925 . 111 ALA H H 7.82 . 1 926 . 111 ALA HA H 4.07 . 1 927 . 111 ALA HB H 1.29 . 1 928 . 111 ALA CA C 53.88 . 1 929 . 111 ALA CB C 20.55 . 1 930 . 111 ALA N N 129.40 . 1 stop_ save_