data_6441 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments for human Orexin-A ; _BMRB_accession_number 6441 _BMRB_flat_file_name bmr6441.str _Entry_type original _Submission_date 2004-12-22 _Accession_date 2004-12-22 _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 Ikegami Takahisa . . 2 Takai Tomoyo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 54 "15N chemical shifts" 31 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-11 update BMRB 'Updating non-standard residue' 2008-07-17 update BMRB 'Updating non-standard residue' 2007-11-09 update BMRB 'complete the entry citation' 2006-04-17 original author 'original release' stop_ _Original_release_date 2004-12-22 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Orexin-A is composed of a highly conserved C-terminal and a specific, hydrophilic N-terminal region, revealing the structural basis of specific recognition by the orexin-1 receptor. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16429482 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takai Tomoyo . . 2 Takaya Takao . . 3 Nakano Mutsuko . . 4 Akutsu Hideo . . 5 Nakagawa Atsushi . . 6 Aimoto Saburo . . 7 Nagai Katsuya . . 8 Ikegami Takahisa . . stop_ _Journal_abbreviation 'J. Pept. Sci.' _Journal_volume 12 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 443 _Page_last 454 _Year 2006 _Details . loop_ _Keyword GPCR Hypocretin Narcolepsy Orexin 'Orphan G-protein coupled receptor' neuropeptide stop_ save_ ################################## # Molecular system description # ################################## save_assembly_human-orexin-A _Saveframe_category molecular_system _Mol_system_name human-orexin-A _Abbreviation_common human-orexin-A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human Orexin-A' $human-orexin-A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_human-orexin-A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human Orexin-A' _Abbreviation_common 'human Orexin-A' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; XPLPDCCRQKTCSCRLYELL HGAGNHAAGILTX ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 PRO 3 LEU 4 PRO 5 ASP 6 CYS 7 CYS 8 ARG 9 GLN 10 LYS 11 THR 12 CYS 13 SER 14 CYS 15 ARG 16 LEU 17 TYR 18 GLU 19 LEU 20 LEU 21 HIS 22 GLY 23 ALA 24 GLY 25 ASN 26 HIS 27 ALA 28 ALA 29 GLY 30 ILE 31 LEU 32 THR 33 NLW stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-03-03 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 5994 'human orexin-A' 100.00 33 100 100 5e-12 PDB 1R02 'A Chain A, Solution Structure Of HumanOrexin-A:regulator Of Appetite And Wakefulness' 100.00 33 100 100 5e-12 PDB 1WSO 'A Chain A, The Solution Structures Of HumanOrexin-A' 100.00 33 100 100 5e-12 DBJ BAB91446.1 'prepro-orexin [Bos taurus]' 33.33 99 100 100 5e-12 EMBL CAM19469.1 'hypocretin [Mus musculus]' 31.13 106 100 100 5e-12 EMBL CAM19468.1 'hypocretin [Mus musculus]' 25.38 130 100 100 5e-12 GenBank AAL17613.1 'AF425237_1 orexin A and B precursor[Ovis aries]' 50.00 66 100 100 5e-12 GenBank AAC26827.1 'prepro-orexin [Sus scrofa]' 25.19 131 100 100 5e-12 GenBank ABJ15704.1 'prepro-orexin [Sus scrofa]' 25.19 131 100 100 5e-12 GenBank ABO15568.1 'prepro-orexin precursor [Sus scrofa]' 25.19 131 100 100 5e-12 GenBank EDM06064.1 'hypocretin, isoform CRA_a [Rattusnorvegicus]' 23.08 143 100 100 5e-12 REF XP_001166578.1 'PREDICTED: orexin [Pantroglodytes]' 25.38 130 100 100 5e-12 REF NP_001515.1 'orexin precursor [Homo sapiens]' 25.19 131 100 100 5e-12 REF NP_999321.1 'orexin [Sus scrofa]' 25.19 131 100 100 5e-12 REF XP_001108991.1 'PREDICTED: similar to orexinprecursor [Macaca mulatta]' 25.19 131 100 100 5e-12 REF XP_609741.2 'PREDICTED: similar to prepro-orexin;PPOX; neuropeptide [Bos taurus]' 25.19 131 100 100 5e-12 SWISS-PROT O55232 'OREX_RAT Orexin precursor (Hypocretin)(Hcrt) [Contains: Orexin-A (Hypocretin-1) (Hcrt1);Orexin-B (Hypocretin-2) (Hcrt2)]' 25.38 130 100 100 5e-12 SWISS-PROT O55241 'OREX_MOUSE Orexin precursor (Hypocretin)(Hcrt) [Contains: Orexin-A (Hypocretin-1) (Hcrt1);Orexin-B (Hypocretin-2) (Hcrt2' 25.38 130 100 100 5e-12 SWISS-PROT Q9GLF6 'OREX_CANFA Orexin precursor (Hypocretin)(Hcrt) [Contains: Orexin-A (Hypocretin-1) (Hcrt1);Orexin-B (Hypocretin-2) (Hcrt2' 25.38 130 100 100 5e-12 SWISS-PROT O43612 'OREX_HUMAN Orexin precursor (Hypocretin)(Hcrt) [Contains: Orexin-A (Hypocretin-1) (Hcrt1);Orexin-B (Hypocretin-2) (Hcrt2' 25.19 131 100 100 5e-12 SWISS-PROT O77668 'OREX_PIG Orexin precursor (Hypocretin)(Hcrt) [Contains: Orexin-A (Hypocretin-1) (Hcrt1);Orexin-B (Hypocretin-2) (Hcrt2)]' 25.19 131 100 100 5e-12 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code . _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 2 11:16:41 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT 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 N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_NLW _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common L-leucinamide _BMRB_code NLW _PDB_code NLW _Standard_residue_derivative . _Molecular_mass 130.188 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CD2 CD2 C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CB CB C . 0 . ? CA CA C . 0 . ? N N N . 0 . ? C C C . 0 . ? O O O . 0 . ? NH2 NH2 N . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H9 H9 H . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H14 H14 H . 0 . ? H15 H15 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 CD1 CG ? ? SING CG CD2 ? ? SING CG CB ? ? SING CB CA ? ? SING N CA ? ? SING CA C ? ? SING C NH2 ? ? DOUB C O ? ? SING CD2 H1 ? ? SING CD2 H2 ? ? SING CD2 H3 ? ? SING CG H4 ? ? SING CD1 H5 ? ? SING CD1 H6 ? ? SING CD1 H7 ? ? SING CB H8 ? ? SING CB H9 ? ? SING CA H10 ? ? SING N H11 ? ? SING N H12 ? ? SING NH2 H14 ? ? SING NH2 H15 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $human-orexin-A 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 $human-orexin-A 'chemical synthesis' . . . . . 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 $human-orexin-A 0.76 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name Sparky _Version . loop_ _Task 'chemical shift assignment' stop_ _Details 'Chemical shift assignments' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details 'cryogenic probe' save_ save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_15N-1H-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-1H-HSQC _Sample_label $sample_1 save_ save_13C-1H-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-1H-HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 18 0.1 mM pH 6.0 0.1 pH temperature 293 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Reference_correction_type DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'human Orexin-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 PCA H H 7.85 0.02 1 2 . 1 PCA HA H 4.68 0.02 1 3 . 1 PCA HB2 H 2.6 0.02 2 4 . 1 PCA HB3 H 2.06 0.02 2 5 . 1 PCA HG2 H 2.4 0.02 2 6 . 1 PCA HG3 H 2.4 0.02 2 7 . 1 PCA CA C 58.188 0.08 1 8 . 1 PCA CB C 26.815 0.08 1 9 . 1 PCA N N 126.56 0.05 1 10 . 2 PRO HA H 4.46 0.02 1 11 . 2 PRO HB2 H 2.25 0.02 2 12 . 2 PRO HB3 H 1.87 0.02 2 13 . 2 PRO HG2 H 1.99 0.02 1 14 . 2 PRO HG3 H 1.99 0.02 1 15 . 2 PRO HD2 H 3.71 0.02 2 16 . 2 PRO HD3 H 3.58 0.02 2 17 . 2 PRO CA C 62.788 0.08 1 18 . 2 PRO CB C 31.88 0.08 1 19 . 3 LEU H H 8.39 0.02 1 20 . 3 LEU HA H 4.49 0.02 1 21 . 3 LEU HB2 H 1.53 0.02 2 22 . 3 LEU HB3 H 1.47 0.02 2 23 . 3 LEU HG H 1.66 0.02 1 24 . 3 LEU HD1 H 0.9 0.02 1 25 . 3 LEU HD2 H 0.9 0.02 1 26 . 3 LEU CA C 52.98 0.08 1 27 . 3 LEU CB C 42.045 0.08 1 28 . 3 LEU N N 123.68 0.05 1 29 . 4 PRO HA H 4.41 0.02 1 30 . 4 PRO HB2 H 2.31 0.02 2 31 . 4 PRO HB3 H 1.96 0.02 2 32 . 4 PRO HG2 H 1.94 0.02 1 33 . 4 PRO HG3 H 1.94 0.02 1 34 . 4 PRO HD2 H 3.78 0.02 2 35 . 4 PRO HD3 H 3.46 0.02 2 36 . 4 PRO CA C 62.957 0.08 1 37 . 4 PRO CB C 32.387 0.08 1 38 . 5 ASP H H 8.72 0.02 1 39 . 5 ASP HA H 4.39 0.02 1 40 . 5 ASP HB2 H 2.62 0.02 1 41 . 5 ASP HB3 H 2.62 0.02 1 42 . 5 ASP CA C 56.44 0.08 1 43 . 5 ASP CB C 41.002 0.08 1 44 . 5 ASP N N 123.32 0.05 1 45 . 6 CYS H H 8.64 0.02 1 46 . 6 CYS HA H 4.35 0.02 1 47 . 6 CYS HB2 H 3.37 0.02 2 48 . 6 CYS HB3 H 2.94 0.02 2 49 . 6 CYS CA C 59.51 0.08 1 50 . 6 CYS CB C 39.478 0.08 1 51 . 6 CYS N N 116.59 0.05 1 52 . 7 CYS H H 7.78 0.02 1 53 . 7 CYS HA H 4.5 0.02 1 54 . 7 CYS HB2 H 3.12 0.02 2 55 . 7 CYS HB3 H 3.05 0.02 2 56 . 7 CYS CA C 58.31 0.08 1 57 . 7 CYS CB C 38.793 0.08 1 58 . 7 CYS N N 122.18 0.05 1 59 . 8 ARG H H 7.8 0.02 1 60 . 8 ARG HA H 4.08 0.02 1 61 . 8 ARG HB2 H 1.95 0.02 2 62 . 8 ARG HB3 H 1.91 0.02 2 63 . 8 ARG HG2 H 1.67 0.02 2 64 . 8 ARG HG3 H 1.61 0.02 2 65 . 8 ARG HD2 H 3.25 0.02 2 66 . 8 ARG HD3 H 3.21 0.02 2 67 . 8 ARG HE H 7.47 0.02 1 68 . 8 ARG CA C 59.01 0.08 1 69 . 8 ARG CB C 29.913 0.08 1 70 . 8 ARG N N 122.6 0.05 1 71 . 9 GLN H H 7.89 0.02 1 72 . 9 GLN HA H 4.22 0.02 1 73 . 9 GLN HB2 H 2.29 0.02 2 74 . 9 GLN HB3 H 1.94 0.02 2 75 . 9 GLN HG2 H 2.41 0.02 2 76 . 9 GLN HG3 H 2.36 0.02 2 77 . 9 GLN HE21 H 7.51 0.02 2 78 . 9 GLN HE22 H 6.84 0.02 2 79 . 9 GLN CA C 56.07 0.08 1 80 . 9 GLN CB C 29.349 0.08 1 81 . 9 GLN N N 114.75 0.05 1 82 . 10 LYS H H 7.71 0.02 1 83 . 10 LYS HA H 4.29 0.02 1 84 . 10 LYS HB2 H 2.2 0.02 2 85 . 10 LYS HB3 H 2.04 0.02 2 86 . 10 LYS HG2 H 1.4 0.02 1 87 . 10 LYS HG3 H 1.4 0.02 1 88 . 10 LYS HD2 H 1.78 0.02 2 89 . 10 LYS HD3 H 1.7 0.02 2 90 . 10 LYS CA C 57.502 0.08 1 91 . 10 LYS CB C 28.733 0.08 1 92 . 10 LYS N N 113.68 0.05 1 93 . 11 THR H H 8.69 0.02 1 94 . 11 THR HA H 4.52 0.02 1 95 . 11 THR HG2 H 1.12 0.02 1 96 . 11 THR CA C 61.39 0.08 1 97 . 11 THR CB C 68.89 0.08 1 98 . 12 CYS H H 7.66 0.02 1 99 . 12 CYS HA H 3.99 0.02 1 100 . 12 CYS HB2 H 2.79 0.02 1 101 . 12 CYS HB3 H 2.79 0.02 1 102 . 12 CYS CB C 48.634 0.08 1 103 . 12 CYS N N 117.27 0.05 1 104 . 13 SER H H 8.65 0.02 1 105 . 13 SER HA H 4.43 0.02 1 106 . 13 SER HB2 H 3.9 0.02 2 107 . 13 SER HB3 H 3.81 0.02 2 108 . 13 SER CA C 58.09 0.08 1 109 . 13 SER CB C 63.194 0.08 1 110 . 13 SER N N 114.76 0.05 1 111 . 14 CYS H H 9.08 0.02 1 112 . 14 CYS HA H 4.76 0.02 1 113 . 14 CYS HB2 H 3.31 0.02 2 114 . 14 CYS HB3 H 3.23 0.02 2 115 . 14 CYS CB C 44.204 0.08 1 116 . 14 CYS N N 125.78 0.05 1 117 . 15 ARG H H 8.44 0.02 1 118 . 15 ARG HA H 4.19 0.02 1 119 . 15 ARG HB2 H 1.76 0.02 1 120 . 15 ARG HB3 H 1.76 0.02 1 121 . 15 ARG HG2 H 1.6 0.02 2 122 . 15 ARG HG3 H 1.54 0.02 2 123 . 15 ARG HD2 H 3.21 0.02 2 124 . 15 ARG HD3 H 3.15 0.02 2 125 . 15 ARG HE H 7.35 0.02 1 126 . 15 ARG CA C 56.42 0.08 1 127 . 15 ARG CB C 30.216 0.08 1 128 . 15 ARG N N 122.16 0.05 1 129 . 16 LEU H H 8.16 0.02 1 130 . 16 LEU HA H 4.15 0.02 1 131 . 16 LEU HB2 H 1.6 0.02 2 132 . 16 LEU HB3 H 1.53 0.02 2 133 . 16 LEU HD1 H 0.9 0.02 2 134 . 16 LEU HD2 H 0.84 0.02 2 135 . 16 LEU CA C 56.78 0.08 1 136 . 16 LEU CB C 41.691 0.08 1 137 . 16 LEU N N 120.74 0.05 1 138 . 17 TYR H H 8 0.02 1 139 . 17 TYR HA H 4.28 0.02 1 140 . 17 TYR HB2 H 3.1 0.02 2 141 . 17 TYR HB3 H 3.03 0.02 2 142 . 17 TYR HD1 H 7.09 0.02 1 143 . 17 TYR HD2 H 7.09 0.02 1 144 . 17 TYR HE1 H 6.75 0.02 1 145 . 17 TYR HE2 H 6.75 0.02 1 146 . 17 TYR CA C 60.227 0.08 1 147 . 17 TYR N N 119.25 0.05 1 148 . 18 GLU H H 8.24 0.02 1 149 . 18 GLU HA H 4.13 0.02 1 150 . 18 GLU HB2 H 2.05 0.02 1 151 . 18 GLU HB3 H 2.05 0.02 1 152 . 18 GLU HG2 H 2.34 0.02 2 153 . 18 GLU HG3 H 2.28 0.02 2 154 . 18 GLU CA C 57.9 0.08 1 155 . 18 GLU CB C 26.82 0.08 1 156 . 18 GLU N N 120.01 0.05 1 157 . 19 LEU H H 7.98 0.02 1 158 . 19 LEU HA H 4.21 0.02 1 159 . 19 LEU HB2 H 1.72 0.02 2 160 . 19 LEU HB3 H 1.65 0.02 2 161 . 19 LEU HD1 H 0.9 0.02 2 162 . 19 LEU HD2 H 0.86 0.02 2 163 . 19 LEU CB C 42.199 0.08 1 164 . 19 LEU N N 121.38 0.05 1 165 . 20 LEU H H 7.95 0.02 1 166 . 20 LEU HA H 4.2 0.02 1 167 . 20 LEU HB2 H 1.56 0.02 2 168 . 20 LEU HB3 H 1.32 0.02 2 169 . 20 LEU HD1 H 0.84 0.02 2 170 . 20 LEU HD2 H 0.79 0.02 2 171 . 20 LEU CB C 42.38 0.08 1 172 . 20 LEU N N 119.87 0.05 1 173 . 21 HIS H H 8.21 0.02 1 174 . 21 HIS HA H 4.63 0.02 1 175 . 21 HIS HB2 H 3.23 0.02 2 176 . 21 HIS HB3 H 2.91 0.02 2 177 . 21 HIS HD2 H 7.02 0.02 2 178 . 21 HIS HE1 H 8.34 0.02 2 179 . 21 HIS CA C 55.82 0.08 1 180 . 21 HIS CB C 29.078 0.08 1 181 . 21 HIS N N 117.25 0.05 1 182 . 22 GLY H H 8.28 0.02 1 183 . 22 GLY HA2 H 3.98 0.02 1 184 . 22 GLY HA3 H 3.98 0.02 1 185 . 22 GLY CA C 48.619 0.08 1 186 . 22 GLY N N 109.79 0.05 1 187 . 23 ALA H H 8.31 0.02 1 188 . 23 ALA HA H 4.34 0.02 1 189 . 23 ALA HB H 1.41 0.02 1 190 . 23 ALA CB C 19.413 0.08 1 191 . 23 ALA N N 123.71 0.05 1 192 . 24 GLY H H 8.49 0.02 1 193 . 24 GLY HA2 H 3.92 0.02 1 194 . 24 GLY HA3 H 3.92 0.02 1 195 . 24 GLY CA C 45.355 0.08 1 196 . 24 GLY N N 107.88 0.05 1 197 . 25 ASN H H 8.28 0.02 1 198 . 25 ASN HA H 4.66 0.02 1 199 . 25 ASN HB2 H 2.77 0.02 2 200 . 25 ASN HB3 H 2.71 0.02 2 201 . 25 ASN HD21 H 7.6 0.02 2 202 . 25 ASN HD22 H 6.92 0.02 2 203 . 25 ASN CA C 53.25 0.08 1 204 . 25 ASN CB C 38.726 0.08 1 205 . 25 ASN N N 118.52 0.05 1 206 . 26 HIS H H 8.51 0.02 1 207 . 26 HIS HA H 4.66 0.02 1 208 . 26 HIS HB2 H 3.27 0.02 2 209 . 26 HIS HB3 H 3.15 0.02 2 210 . 26 HIS HD2 H 7.19 0.02 2 211 . 26 HIS CA C 55.64 0.08 1 212 . 26 HIS CB C 29.222 0.08 1 213 . 26 HIS N N 119.39 0.05 1 214 . 27 ALA H H 8.34 0.02 1 215 . 27 ALA HA H 4.28 0.02 1 216 . 27 ALA HB H 1.34 0.02 1 217 . 27 ALA CA C 52.74 0.08 1 218 . 27 ALA CB C 19.158 0.08 1 219 . 27 ALA N N 125 0.02 1 220 . 28 ALA H H 8.34 0.02 1 221 . 28 ALA HA H 4.3 0.02 1 222 . 28 ALA HB H 1.4 0.02 1 223 . 28 ALA CB C 19.281 0.08 1 224 . 28 ALA N N 123.32 0.05 1 225 . 29 GLY H H 8.35 0.02 1 226 . 29 GLY HA2 H 3.94 0.02 1 227 . 29 GLY HA3 H 3.94 0.02 1 228 . 29 GLY CA C 45.445 0.08 1 229 . 29 GLY N N 108.04 0.05 1 230 . 30 ILE H H 7.98 0.02 1 231 . 30 ILE HA H 4.16 0.02 1 232 . 30 ILE HB H 1.86 0.02 1 233 . 30 ILE HG12 H 1.43 0.02 2 234 . 30 ILE HG13 H 1.17 0.02 2 235 . 30 ILE HG2 H 0.89 0.02 1 236 . 30 ILE HD1 H 0.83 0.02 1 237 . 30 ILE CA C 61.29 0.08 1 238 . 30 ILE CB C 38.673 0.08 1 239 . 30 ILE N N 120.06 0.05 1 240 . 31 LEU H H 8.4 0.02 1 241 . 31 LEU HA H 4.42 0.02 1 242 . 31 LEU HB2 H 1.66 0.02 2 243 . 31 LEU HB3 H 1.6 0.02 2 244 . 31 LEU HG H 0.91 0.02 1 245 . 31 LEU HD1 H 0.9 0.02 2 246 . 31 LEU HD2 H 0.84 0.02 2 247 . 31 LEU CA C 55.31 0.08 1 248 . 31 LEU N N 126.09 0.05 1 249 . 32 THR H H 8.16 0.02 1 250 . 32 THR HA H 4.32 0.02 1 251 . 32 THR HB H 4.18 0.02 1 252 . 32 THR HG2 H 1.18 0.02 1 253 . 32 THR CA C 61.81 0.08 1 254 . 32 THR CB C 69.723 0.08 1 255 . 32 THR N N 115.98 0.05 1 256 . 33 NLW H H 8.26 0.02 1 257 . 33 NLW HA H 4.33 0.02 1 258 . 33 NLW HB2 H 1.67 0.02 2 259 . 33 NLW HB3 H 1.59 0.02 2 260 . 33 NLW HD1 H 0.92 0.02 2 261 . 33 NLW HD2 H 0.86 0.02 2 262 . 33 NLW CA C 54.97 0.08 1 263 . 33 NLW N N 125.43 0.05 1 264 . 33 NLW HT1 H 7.15 0.02 2 265 . 33 NLW HT2 H 7.61 0.02 2 266 . 33 NLW NT N 108.04 0.05 1 stop_ save_