data_4573 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1HN,15N,13CO,13Ca,13Cb chemical shifts of 7,8-dihydroneopterin aldolase (DHNA) from Staphylococcus aureus ; _BMRB_accession_number 4573 _BMRB_flat_file_name bmr4573.str _Entry_type original _Submission_date 2000-01-25 _Accession_date 2000-01-25 _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 Salzmann Michael . . 2 Pervushin Konstantin . . 3 Wider Gerhard . . 4 Senn Hans . . 5 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 302 "15N chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-05-15 original author . stop_ _Original_release_date 2004-05-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments ; _Citation_status published _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 Salzmann Michael . . 2 Pervushin Konstantin . . 3 Wider Gerhard . . 4 Senn Hans . . 5 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 122 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7543 _Page_last 7548 _Year 2000 _Details . loop_ _Keyword NMR TROSY DHNA Aldolase 'Large Protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; Wishart DS, Sykes BD. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR. 1994 Mar;4(2):171-80. ; _Citation_title 'The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8019132 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 4 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 171 _Page_last 180 _Year 1994 _Details ; A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements. ; save_ ################################## # Molecular system description # ################################## save_system_DHNA _Saveframe_category molecular_system _Mol_system_name '7,8-dihydroneopterin aldolase' _Abbreviation_common DHNA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label subunit-1 $DHNA subunit-2 $DHNA subunit-3 $DHNA subunit-4 $DHNA subunit-5 $DHNA subunit-6 $DHNA subunit-7 $DHNA subunit-8 $DHNA stop_ _System_molecular_weight 110000 _System_physical_state native _System_oligomer_state octamer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 subunit-1 1 subunit-2 1 subunit-3 1 subunit-4 1 subunit-5 1 subunit-6 1 subunit-7 1 subunit-8 stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DHNA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Aldolase _Abbreviation_common DHNA _Molecular_mass 15000 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 121 _Mol_residue_sequence ; MQDTIFLKGMRFYGYHGALS AENEIGQIFKVDVTLKVDLS EAGRTDNVIDTVHYGEVFEE VKSIMEGKAVNLLEHLAERI ANRINSQYNRVMETKVRITK ENPPIPGHYDGVGIEIVREN K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ASP 4 THR 5 ILE 6 PHE 7 LEU 8 LYS 9 GLY 10 MET 11 ARG 12 PHE 13 TYR 14 GLY 15 TYR 16 HIS 17 GLY 18 ALA 19 LEU 20 SER 21 ALA 22 GLU 23 ASN 24 GLU 25 ILE 26 GLY 27 GLN 28 ILE 29 PHE 30 LYS 31 VAL 32 ASP 33 VAL 34 THR 35 LEU 36 LYS 37 VAL 38 ASP 39 LEU 40 SER 41 GLU 42 ALA 43 GLY 44 ARG 45 THR 46 ASP 47 ASN 48 VAL 49 ILE 50 ASP 51 THR 52 VAL 53 HIS 54 TYR 55 GLY 56 GLU 57 VAL 58 PHE 59 GLU 60 GLU 61 VAL 62 LYS 63 SER 64 ILE 65 MET 66 GLU 67 GLY 68 LYS 69 ALA 70 VAL 71 ASN 72 LEU 73 LEU 74 GLU 75 HIS 76 LEU 77 ALA 78 GLU 79 ARG 80 ILE 81 ALA 82 ASN 83 ARG 84 ILE 85 ASN 86 SER 87 GLN 88 TYR 89 ASN 90 ARG 91 VAL 92 MET 93 GLU 94 THR 95 LYS 96 VAL 97 ARG 98 ILE 99 THR 100 LYS 101 GLU 102 ASN 103 PRO 104 PRO 105 ILE 106 PRO 107 GLY 108 HIS 109 TYR 110 ASP 111 GLY 112 VAL 113 GLY 114 ILE 115 GLU 116 ILE 117 VAL 118 ARG 119 GLU 120 ASN 121 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1DHN "1.65 Angstrom Resolution Structure Of 7,8-dihydroneopterin Aldolase From Staphylococcus Aureus" 100.00 121 100.00 100.00 1.38e-81 PDB 1RRI "Dhna Complex With 3-(5-Amino-7-Hydroxy-[1,2,3] Triazolo [4,5- D]pyrimidin-2-Yl)-Benzoic Acid" 100.00 121 100.00 100.00 1.38e-81 PDB 1RRW "Dhna Complexed With 9-Methylguanine" 100.00 121 100.00 100.00 1.38e-81 PDB 1RRY "Dhna Complexed With 2-Amino-4-Hydroxy-5-Carboxyethylpyrimidine" 100.00 121 100.00 100.00 1.38e-81 PDB 1RS2 "Dhna Complex With 8-Amino-1,3-Dimethyl-3,7-Dihydropurine-2,6-Dione" 100.00 121 100.00 100.00 1.38e-81 PDB 1RS4 "Dhna, 7,8-Dihydroneopterin Aldolase Complexed With 3-(5-Amino-7- Hydroxy-[1,2,3]triazolo[4,5-D]pyrimidin-2-Yl)-N-(3,5-Dichlorob" 100.00 121 100.00 100.00 1.38e-81 PDB 1RSD "Dhna Complex With 3-(5-Amino-7-Hydroxy-[1,2,3]triazolo[4,5- D]pyrimidin-2-Yl)-N-[2-(2-Hydroxymethyl-Phenylsulfanyl)-Benzyl]- Be" 100.00 121 100.00 100.00 1.38e-81 PDB 1RSI "Dhna Complex With 2-amino-5-bromo-3-hydroxy-6-phenylpyrimidine" 100.00 121 100.00 100.00 1.38e-81 PDB 1U68 "Dhna 7,8 Dihydroneopterin Complex" 100.00 121 100.00 100.00 1.38e-81 PDB 2DHN "Complex Of 7,8-Dihydroneopterin Aldolase From Staphylococcus Aureus With 6-Hydroxymethyl-7,8-Dihydropterin At 2.2 A Resolution" 100.00 121 100.00 100.00 1.38e-81 PDB 2NM2 "Crystal Structure Of Dihydroneopterin Aldolase From S. Aureus In Complex With (1s,2r)-Neopterin At 1.50 Angstrom Resolution" 100.00 121 100.00 100.00 1.38e-81 PDB 2NM3 "Crystal Structure Of Dihydroneopterin Aldolase From S. Aureus In Complex With (1s,2s)-Monapterin At 1.68 Angstrom Resolution" 100.00 121 100.00 100.00 1.38e-81 DBJ BAB41703 "7,8-dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus N315]" 100.00 121 99.17 100.00 3.97e-81 DBJ BAB56677 "7,8-dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus Mu50]" 100.00 121 99.17 100.00 3.97e-81 DBJ BAB94335 "7,8-dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus MW2]" 100.00 121 99.17 100.00 3.97e-81 DBJ BAF66749 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus str. Newman]" 100.00 121 99.17 100.00 3.97e-81 DBJ BAF77395 "7,8-dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus Mu3]" 100.00 121 99.17 100.00 3.97e-81 EMBL CAG39538 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus MRSA252]" 100.00 121 100.00 100.00 1.38e-81 EMBL CAG42247 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 121 99.17 100.00 3.97e-81 EMBL CAI80152 "dihydroneopterin aldolase [Staphylococcus aureus RF122]" 100.00 121 99.17 100.00 3.85e-81 EMBL CAQ49018 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus ST398]" 100.00 121 98.35 99.17 5.58e-80 EMBL CBI48462 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus TW20]" 100.00 121 99.17 100.00 3.97e-81 GB AAW37671 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus COL]" 100.00 121 99.17 100.00 3.97e-81 GB ABD20664 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 100.00 121 99.17 100.00 3.97e-81 GB ABD29643 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus NCTC 8325]" 100.00 121 99.17 100.00 3.97e-81 GB ABQ48341 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus JH9]" 100.00 121 99.17 100.00 3.97e-81 GB ABR51408 "dihydroneopterin aldolase [Staphylococcus aureus subsp. aureus JH1]" 100.00 121 99.17 100.00 3.97e-81 REF WP_001154300 "dihydroneopterin aldolase [Staphylococcus aureus]" 100.00 121 98.35 100.00 7.01e-81 REF WP_001154301 "dihydroneopterin aldolase [Staphylococcus aureus]" 100.00 121 98.35 99.17 5.58e-80 REF WP_001154302 "MULTISPECIES: dihydroneopterin aldolase [Bacteria]" 100.00 121 99.17 100.00 3.97e-81 REF WP_001154303 "dihydroneopterin aldolase [Staphylococcus aureus]" 100.00 121 100.00 100.00 1.38e-81 REF WP_001154304 "dihydroneopterin aldolase [Staphylococcus aureus]" 100.00 121 99.17 100.00 3.85e-81 SP P56740 "RecName: Full=Dihydroneopterin aldolase; Short=DHNA; AltName: Full=7,8-dihydroneopterin 2'-epimerase; AltName: Full=7,8-dihydro" 100.00 121 100.00 100.00 1.38e-81 SP P64145 "RecName: Full=Dihydroneopterin aldolase; Short=DHNA; AltName: Full=7,8-dihydroneopterin 2'-epimerase; AltName: Full=7,8-dihydro" 100.00 121 99.17 100.00 3.97e-81 SP P64146 "RecName: Full=Dihydroneopterin aldolase; Short=DHNA; AltName: Full=7,8-dihydroneopterin 2'-epimerase; AltName: Full=7,8-dihydro" 100.00 121 99.17 100.00 3.97e-81 SP P64147 "RecName: Full=Dihydroneopterin aldolase; Short=DHNA; AltName: Full=7,8-dihydroneopterin 2'-epimerase; AltName: Full=7,8-dihydro" 100.00 121 99.17 100.00 3.97e-81 SP Q5HIG0 "RecName: Full=Dihydroneopterin aldolase; Short=DHNA; AltName: Full=7,8-dihydroneopterin 2'-epimerase; AltName: Full=7,8-dihydro" 100.00 121 99.17 100.00 3.97e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $DHNA 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus ; Staphylococcus aureus 7,8-dihydroneopterin aldolase (DHNA) was overexpressed in E.coli M15(pRep4) harboring a pSaDHNA plasmid ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $DHNA 'recombinant technology' S.aureus . . . . ; Staphylococcus aureus 7,8-dihydroneopterin aldolase (DHNA) was overexpressed in E.coli M15(pRep4) harboring a pSaDHNA plasmid ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_label _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DHNA 0.5 mM '[U-95% 2H; U-98% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_label _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_label _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_label _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_label _Saveframe_category chemical_shift_reference _Details ; The 15N and 13C referencing was done using the indirect referencing according to the article Wishart and Sykes (1994), J.Biomol. NMR 4, 171-180. ; 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_citation_label TSP H 1 'methyl protons' ppm 0.00 . . . . . . TSP C 13 'methyl protons' ppm 0.00 . indirect . . . $ref1 TSP N 15 'methyl protons' ppm 0.00 . indirect . . . $ref1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_label _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_label stop_ _Sample_conditions_label $sample_conditions_label _Chem_shift_reference_set_label $chemical_shift_reference_label _Mol_system_component_name subunit-1 _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 . 3 ASP H H 7.54 . 1 2 . 3 ASP C C 174.1 . 1 3 . 3 ASP CA C 54.3 . 1 4 . 3 ASP CB C 40.5 . 1 5 . 3 ASP N N 125.0 . 1 6 . 4 THR H H 9.29 . 1 7 . 4 THR C C 175.9 . 1 8 . 4 THR CA C 58.8 . 1 9 . 4 THR N N 109.8 . 1 10 . 5 ILE H H 8.78 . 1 11 . 5 ILE C C 175.1 . 1 12 . 5 ILE CA C 59.2 . 1 13 . 5 ILE N N 118.7 . 1 14 . 6 PHE CA C 54.3 . 1 15 . 7 LEU H H 8.85 . 1 16 . 7 LEU C C 173.0 . 1 17 . 7 LEU CA C 56.3 . 1 18 . 7 LEU CB C 42.7 . 1 19 . 7 LEU N N 119.5 . 1 20 . 8 LYS H H 9.30 . 1 21 . 8 LYS C C 175.1 . 1 22 . 8 LYS CA C 53.9 . 1 23 . 8 LYS CB C 34.1 . 1 24 . 8 LYS N N 124.0 . 1 25 . 9 GLY H H 9.91 . 1 26 . 9 GLY C C 176.4 . 1 27 . 9 GLY CA C 46.3 . 1 28 . 9 GLY N N 115.6 . 1 29 . 10 MET H H 8.78 . 1 30 . 10 MET C C 175.1 . 1 31 . 10 MET CA C 55.4 . 1 32 . 10 MET CB C 34.4 . 1 33 . 10 MET N N 118.4 . 1 34 . 11 ARG H H 8.37 . 1 35 . 11 ARG C C 175.4 . 1 36 . 11 ARG CA C 53.9 . 1 37 . 11 ARG CB C 32.2 . 1 38 . 11 ARG N N 122.3 . 1 39 . 12 PHE H H 8.70 . 1 40 . 12 PHE C C 174.4 . 1 41 . 12 PHE CA C 54.9 . 1 42 . 12 PHE CB C 42.3 . 1 43 . 12 PHE N N 119.0 . 1 44 . 13 TYR H H 9.77 . 1 45 . 13 TYR C C 173.8 . 1 46 . 13 TYR CA C 57.7 . 1 47 . 13 TYR CB C 36.9 . 1 48 . 13 TYR N N 129.1 . 1 49 . 14 GLY H H 8.33 . 1 50 . 14 GLY C C 175.1 . 1 51 . 14 GLY CA C 43.2 . 1 52 . 14 GLY N N 114.4 . 1 53 . 15 TYR H H 7.57 . 1 54 . 15 TYR C C 172.1 . 1 55 . 15 TYR CA C 57.9 . 1 56 . 15 TYR N N 113.5 . 1 57 . 16 HIS H H 6.28 . 1 58 . 16 HIS C C 173.8 . 1 59 . 16 HIS CA C 54.4 . 1 60 . 16 HIS CB C 30.5 . 1 61 . 16 HIS N N 117.6 . 1 62 . 17 GLY H H 9.19 . 1 63 . 17 GLY C C 175.9 . 1 64 . 17 GLY CA C 44.7 . 1 65 . 17 GLY N N 110.5 . 1 66 . 18 ALA H H 8.02 . 1 67 . 18 ALA C C 172.9 . 1 68 . 18 ALA CA C 51.3 . 1 69 . 18 ALA CB C 18.3 . 1 70 . 18 ALA N N 122.1 . 1 71 . 19 LEU H H 7.64 . 1 72 . 19 LEU C C 177.7 . 1 73 . 19 LEU CA C 52.6 . 1 74 . 19 LEU CB C 41.4 . 1 75 . 19 LEU N N 118.8 . 1 76 . 20 SER H H 8.90 . 1 77 . 20 SER C C 177.6 . 1 78 . 20 SER CA C 60.7 . 1 79 . 20 SER N N 121.8 . 1 80 . 21 ALA H H 8.81 . 1 81 . 21 ALA C C 177.6 . 1 82 . 21 ALA CA C 54.6 . 1 83 . 21 ALA CB C 19.0 . 1 84 . 21 ALA N N 122.9 . 1 85 . 22 GLU H H 7.00 . 1 86 . 22 GLU C C 177.8 . 1 87 . 22 GLU CA C 58.5 . 1 88 . 22 GLU CB C 30.2 . 1 89 . 22 GLU N N 115.0 . 1 90 . 23 ASN H H 7.54 . 1 91 . 23 ASN C C 172.8 . 1 92 . 23 ASN CA C 54.0 . 1 93 . 23 ASN CB C 38.1 . 1 94 . 23 ASN N N 118.2 . 1 95 . 24 GLU H H 7.60 . 1 96 . 24 GLU C C 175.1 . 1 97 . 24 GLU CA C 57.6 . 1 98 . 24 GLU N N 117.0 . 1 99 . 25 ILE H H 8.17 . 1 100 . 25 ILE C C 176.4 . 1 101 . 25 ILE CA C 61.8 . 1 102 . 25 ILE N N 122.4 . 1 103 . 26 GLY H H 7.85 . 1 104 . 26 GLY C C 178.5 . 1 105 . 26 GLY CA C 45.4 . 1 106 . 26 GLY N N 111.9 . 1 107 . 27 GLN H H 7.63 . 1 108 . 27 GLN C C 171.3 . 1 109 . 27 GLN CA C 54.2 . 1 110 . 27 GLN CB C 30.3 . 1 111 . 27 GLN N N 111.8 . 1 112 . 28 ILE H H 8.34 . 1 113 . 28 ILE C C 172.1 . 1 114 . 28 ILE CA C 56.8 . 1 115 . 28 ILE CB C 34.8 . 1 116 . 28 ILE N N 117.9 . 1 117 . 29 PHE H H 9.26 . 1 118 . 29 PHE C C 176.3 . 1 119 . 29 PHE CA C 56.0 . 1 120 . 29 PHE CB C 42.1 . 1 121 . 29 PHE N N 126.9 . 1 122 . 30 LYS CA C 53.7 . 1 123 . 31 VAL H H 10.25 . 1 124 . 31 VAL C C 179.0 . 1 125 . 31 VAL CA C 59.8 . 1 126 . 31 VAL N N 127.6 . 1 127 . 32 ASP H H 9.41 . 1 128 . 32 ASP C C 173.7 . 1 129 . 32 ASP CA C 51.9 . 1 130 . 32 ASP CB C 43.3 . 1 131 . 32 ASP N N 126.4 . 1 132 . 33 VAL H H 9.06 . 1 133 . 33 VAL C C 176.0 . 1 134 . 33 VAL CA C 60.0 . 1 135 . 33 VAL CB C 34.5 . 1 136 . 33 VAL N N 122.7 . 1 137 . 34 THR H H 8.94 . 1 138 . 34 THR C C 174.1 . 1 139 . 34 THR CA C 61.5 . 1 140 . 34 THR CB C 69.3 . 1 141 . 34 THR N N 123.7 . 1 142 . 35 LEU H H 10.01 . 1 143 . 35 LEU C C 172.7 . 1 144 . 35 LEU CA C 51.9 . 1 145 . 35 LEU CB C 41.9 . 1 146 . 35 LEU N N 129.3 . 1 147 . 36 LYS H H 8.49 . 1 148 . 36 LYS C C 175.4 . 1 149 . 36 LYS CA C 55.4 . 1 150 . 36 LYS N N 125.1 . 1 151 . 37 VAL H H 7.74 . 1 152 . 37 VAL C C 175.0 . 1 153 . 37 VAL CA C 59.5 . 1 154 . 37 VAL CB C 36.0 . 1 155 . 37 VAL N N 127.8 . 1 156 . 38 ASP H H 8.79 . 1 157 . 38 ASP C C 172.0 . 1 158 . 38 ASP CA C 54.0 . 1 159 . 38 ASP CB C 39.4 . 1 160 . 38 ASP N N 122.8 . 1 161 . 39 LEU H H 8.93 . 1 162 . 39 LEU C C 177.6 . 1 163 . 39 LEU CA C 54.0 . 1 164 . 39 LEU CB C 39.1 . 1 165 . 39 LEU N N 131.6 . 1 166 . 40 SER H H 8.56 . 1 167 . 40 SER C C 177.5 . 1 168 . 40 SER CA C 61.1 . 1 169 . 40 SER CB C 66.8 . 1 170 . 40 SER N N 117.0 . 1 171 . 41 GLU H H 7.78 . 1 172 . 41 GLU C C 176.7 . 1 173 . 41 GLU CA C 59.0 . 1 174 . 41 GLU CB C 27.7 . 1 175 . 41 GLU N N 124.6 . 1 176 . 42 ALA H H 8.62 . 1 177 . 42 ALA C C 177.8 . 1 178 . 42 ALA CA C 53.2 . 1 179 . 42 ALA CB C 17.8 . 1 180 . 42 ALA N N 122.6 . 1 181 . 43 GLY H H 8.41 . 1 182 . 43 GLY C C 179.9 . 1 183 . 43 GLY CA C 45.6 . 1 184 . 43 GLY N N 103.4 . 1 185 . 44 ARG H H 7.76 . 1 186 . 44 ARG C C 176.1 . 1 187 . 44 ARG CA C 57.3 . 1 188 . 44 ARG N N 122.6 . 1 189 . 45 THR H H 8.85 . 1 190 . 45 THR C C 178.2 . 1 191 . 45 THR CA C 62.6 . 1 192 . 45 THR CB C 69.1 . 1 193 . 45 THR N N 110.8 . 1 194 . 46 ASP H H 8.80 . 1 195 . 46 ASP C C 176.8 . 1 196 . 46 ASP CA C 55.5 . 1 197 . 46 ASP CB C 40.9 . 1 198 . 46 ASP N N 121.9 . 1 199 . 47 ASN H H 7.79 . 1 200 . 47 ASN C C 174.3 . 1 201 . 47 ASN CA C 50.8 . 1 202 . 47 ASN CB C 38.5 . 1 203 . 47 ASN N N 116.2 . 1 204 . 48 VAL H H 8.51 . 1 205 . 48 VAL C C 175.9 . 1 206 . 48 VAL CA C 63.4 . 1 207 . 48 VAL CB C 30.6 . 1 208 . 48 VAL N N 123.9 . 1 209 . 49 ILE H H 7.76 . 1 210 . 49 ILE C C 176.7 . 1 211 . 49 ILE CA C 61.9 . 1 212 . 49 ILE CB C 36.4 . 1 213 . 49 ILE N N 118.7 . 1 214 . 50 ASP H H 7.84 . 1 215 . 50 ASP C C 176.4 . 1 216 . 50 ASP CA C 54.2 . 1 217 . 50 ASP CB C 40.5 . 1 218 . 50 ASP N N 119.4 . 1 219 . 51 THR H H 7.11 . 1 220 . 51 THR C C 174.3 . 1 221 . 51 THR CA C 57.5 . 1 222 . 51 THR N N 114.8 . 1 223 . 52 VAL H H 7.95 . 1 224 . 52 VAL C C 172.6 . 1 225 . 52 VAL CA C 60.1 . 1 226 . 52 VAL CB C 32.1 . 1 227 . 52 VAL N N 122.7 . 1 228 . 53 HIS H H 8.49 . 1 229 . 53 HIS C C 174.1 . 1 230 . 53 HIS CA C 55.4 . 1 231 . 53 HIS CB C 29.7 . 1 232 . 53 HIS N N 126.6 . 1 233 . 54 TYR H H 6.74 . 1 234 . 54 TYR C C 176.5 . 1 235 . 54 TYR CA C 58.3 . 1 236 . 54 TYR N N 123.8 . 1 237 . 55 GLY H H 8.84 . 1 238 . 55 GLY C C 178.8 . 1 239 . 55 GLY CA C 46.3 . 1 240 . 55 GLY N N 107.1 . 1 241 . 56 GLU H H 7.71 . 1 242 . 56 GLU C C 176.1 . 1 243 . 56 GLU CA C 58.0 . 1 244 . 56 GLU N N 122.8 . 1 245 . 57 VAL H H 7.22 . 1 246 . 57 VAL C C 179.4 . 1 247 . 57 VAL CA C 65.9 . 1 248 . 57 VAL N N 119.3 . 1 249 . 58 PHE H H 8.33 . 1 250 . 58 PHE C C 177.5 . 1 251 . 58 PHE CA C 61.9 . 1 252 . 58 PHE CB C 37.9 . 1 253 . 58 PHE N N 119.6 . 1 254 . 59 GLU H H 7.78 . 1 255 . 59 GLU C C 176.3 . 1 256 . 59 GLU CA C 58.3 . 1 257 . 59 GLU CB C 28.0 . 1 258 . 59 GLU N N 117.0 . 1 259 . 60 GLU H H 7.65 . 1 260 . 60 GLU C C 179.6 . 1 261 . 60 GLU CA C 57.5 . 1 262 . 60 GLU CB C 27.7 . 1 263 . 60 GLU N N 118.8 . 1 264 . 61 VAL CA C 65.8 . 1 265 . 62 LYS H H 8.51 . 1 266 . 62 LYS C C 177.1 . 1 267 . 62 LYS CA C 58.6 . 1 268 . 62 LYS CB C 31.2 . 1 269 . 62 LYS N N 121.7 . 1 270 . 63 SER H H 7.70 . 1 271 . 63 SER C C 177.1 . 1 272 . 63 SER CA C 60.2 . 1 273 . 63 SER CB C 61.6 . 1 274 . 63 SER N N 111.1 . 1 275 . 64 ILE H H 6.66 . 1 276 . 64 ILE C C 176.8 . 1 277 . 64 ILE CA C 63.0 . 1 278 . 64 ILE CB C 37.5 . 1 279 . 64 ILE N N 119.8 . 1 280 . 65 MET H H 8.19 . 1 281 . 65 MET C C 178.5 . 1 282 . 65 MET CA C 54.5 . 1 283 . 65 MET N N 117.0 . 1 284 . 66 GLU H H 8.42 . 1 285 . 66 GLU C C 179.4 . 1 286 . 66 GLU CA C 55.3 . 1 287 . 66 GLU CB C 27.6 . 1 288 . 66 GLU N N 116.7 . 1 289 . 67 GLY H H 6.83 . 1 290 . 67 GLY C C 176.2 . 1 291 . 67 GLY CA C 43.3 . 1 292 . 67 GLY N N 108.5 . 1 293 . 68 LYS H H 7.94 . 1 294 . 68 LYS C C 171.8 . 1 295 . 68 LYS CA C 56.2 . 1 296 . 68 LYS CB C 31.3 . 1 297 . 68 LYS N N 120.1 . 1 298 . 69 ALA H H 8.05 . 1 299 . 69 ALA C C 176.2 . 1 300 . 69 ALA CA C 51.6 . 1 301 . 69 ALA CB C 18.0 . 1 302 . 69 ALA N N 126.0 . 1 303 . 70 VAL H H 10.16 . 1 304 . 70 VAL C C 178.6 . 1 305 . 70 VAL CA C 58.0 . 1 306 . 70 VAL CB C 31.3 . 1 307 . 70 VAL N N 122.3 . 1 308 . 71 ASN H H 11.21 . 1 309 . 71 ASN C C 175.1 . 1 310 . 71 ASN CA C 55.9 . 1 311 . 71 ASN N N 121.1 . 1 312 . 72 LEU H H 10.32 . 1 313 . 72 LEU C C 174.9 . 1 314 . 72 LEU CA C 53.3 . 1 315 . 72 LEU CB C 45.4 . 1 316 . 72 LEU N N 119.2 . 1 317 . 73 LEU H H 8.22 . 1 318 . 73 LEU C C 178.3 . 1 319 . 73 LEU CA C 56.8 . 1 320 . 73 LEU CB C 41.6 . 1 321 . 73 LEU N N 121.2 . 1 322 . 74 GLU H H 12.17 . 1 323 . 74 GLU C C 178.7 . 1 324 . 74 GLU CA C 60.1 . 1 325 . 74 GLU N N 120.5 . 1 326 . 75 HIS H H 6.82 . 1 327 . 75 HIS C C 172.2 . 1 328 . 75 HIS CA C 57.2 . 1 329 . 75 HIS N N 117.5 . 1 330 . 76 LEU H H 8.50 . 1 331 . 76 LEU C C 176.3 . 1 332 . 76 LEU CA C 55.5 . 1 333 . 76 LEU N N 123.9 . 1 334 . 77 ALA H H 8.54 . 1 335 . 77 ALA C C 168.9 . 1 336 . 77 ALA CA C 54.6 . 1 337 . 77 ALA N N 119.2 . 1 338 . 78 GLU H H 7.97 . 1 339 . 78 GLU C C 178.2 . 1 340 . 78 GLU CA C 58.0 . 1 341 . 78 GLU CB C 29.0 . 1 342 . 78 GLU N N 120.7 . 1 343 . 79 ARG H H 7.66 . 1 344 . 79 ARG C C 179.3 . 1 345 . 79 ARG CA C 58.1 . 1 346 . 79 ARG CB C 29.1 . 1 347 . 79 ARG N N 117.7 . 1 348 . 80 ILE CA C 59.2 . 1 349 . 80 ILE CB C 41.7 . 1 350 . 81 ALA H H 8.67 . 1 351 . 81 ALA C C 175.6 . 1 352 . 81 ALA CA C 54.4 . 1 353 . 81 ALA N N 122.4 . 1 354 . 82 ASN H H 8.29 . 1 355 . 82 ASN C C 178.2 . 1 356 . 82 ASN CA C 55.3 . 1 357 . 82 ASN CB C 37.9 . 1 358 . 82 ASN N N 114.0 . 1 359 . 83 ARG H H 7.98 . 1 360 . 83 ARG C C 178.2 . 1 361 . 83 ARG CA C 57.0 . 1 362 . 83 ARG CB C 29.5 . 1 363 . 83 ARG N N 121.4 . 1 364 . 84 ILE H H 8.06 . 1 365 . 84 ILE C C 177.4 . 1 366 . 84 ILE CA C 64.3 . 1 367 . 84 ILE N N 118.7 . 1 368 . 85 ASN H H 8.26 . 1 369 . 85 ASN C C 177.2 . 1 370 . 85 ASN CA C 54.3 . 1 371 . 85 ASN CB C 35.5 . 1 372 . 85 ASN N N 117.3 . 1 373 . 86 SER H H 7.75 . 1 374 . 86 SER C C 177.4 . 1 375 . 86 SER CA C 60.1 . 1 376 . 86 SER CB C 62.4 . 1 377 . 86 SER N N 111.1 . 1 378 . 87 GLN H H 7.43 . 1 379 . 87 GLN C C 175.5 . 1 380 . 87 GLN CA C 55.6 . 1 381 . 87 GLN CB C 29.7 . 1 382 . 87 GLN N N 119.3 . 1 383 . 88 TYR H H 7.60 . 1 384 . 88 TYR C C 176.0 . 1 385 . 88 TYR CA C 55.6 . 1 386 . 88 TYR CB C 37.8 . 1 387 . 88 TYR N N 118.8 . 1 388 . 89 ASN H H 8.37 . 1 389 . 89 ASN C C 174.9 . 1 390 . 89 ASN CA C 54.7 . 1 391 . 89 ASN CB C 37.0 . 1 392 . 89 ASN N N 122.1 . 1 393 . 90 ARG H H 8.16 . 1 394 . 90 ARG C C 176.7 . 1 395 . 90 ARG CA C 56.0 . 1 396 . 90 ARG CB C 29.4 . 1 397 . 90 ARG N N 115.6 . 1 398 . 91 VAL H H 7.54 . 1 399 . 91 VAL C C 176.7 . 1 400 . 91 VAL CA C 62.3 . 1 401 . 91 VAL CB C 30.1 . 1 402 . 91 VAL N N 120.6 . 1 403 . 92 MET H H 9.30 . 1 404 . 92 MET C C 175.6 . 1 405 . 92 MET CA C 56.2 . 1 406 . 92 MET CB C 32.6 . 1 407 . 92 MET N N 126.1 . 1 408 . 93 GLU H H 7.37 . 1 409 . 93 GLU C C 177.8 . 1 410 . 93 GLU CA C 55.2 . 1 411 . 93 GLU CB C 32.7 . 1 412 . 93 GLU N N 119.0 . 1 413 . 94 THR H H 8.41 . 1 414 . 94 THR C C 172.9 . 1 415 . 94 THR CA C 62.5 . 1 416 . 94 THR CB C 68.7 . 1 417 . 94 THR N N 124.2 . 1 418 . 95 LYS H H 9.01 . 1 419 . 95 LYS C C 172.0 . 1 420 . 95 LYS CA C 53.4 . 1 421 . 95 LYS CB C 33.4 . 1 422 . 95 LYS N N 130.0 . 1 423 . 96 VAL H H 9.12 . 1 424 . 96 VAL C C 175.7 . 1 425 . 96 VAL CA C 60.0 . 1 426 . 96 VAL N N 125.4 . 1 427 . 97 ARG H H 9.19 . 1 428 . 97 ARG C C 172.7 . 1 429 . 97 ARG CA C 53.3 . 1 430 . 97 ARG N N 130.3 . 1 431 . 98 ILE H H 8.63 . 1 432 . 98 ILE C C 175.2 . 1 433 . 98 ILE CA C 59.9 . 1 434 . 98 ILE N N 126.1 . 1 435 . 99 THR H H 9.37 . 1 436 . 99 THR C C 173.5 . 1 437 . 99 THR CA C 60.9 . 1 438 . 99 THR CB C 69.9 . 1 439 . 99 THR N N 121.5 . 1 440 . 100 LYS H H 9.18 . 1 441 . 100 LYS C C 174.2 . 1 442 . 100 LYS CA C 54.6 . 1 443 . 100 LYS CB C 33.0 . 1 444 . 100 LYS N N 125.1 . 1 445 . 101 GLU H H 8.82 . 1 446 . 101 GLU C C 175.6 . 1 447 . 101 GLU CA C 56.7 . 1 448 . 101 GLU CB C 29.4 . 1 449 . 101 GLU N N 124.2 . 1 450 . 102 ASN H H 9.15 . 1 451 . 102 ASN C C 176.0 . 1 452 . 102 ASN CA C 50.9 . 1 453 . 102 ASN N N 118.2 . 1 454 . 104 PRO CA C 61.3 . 1 455 . 105 ILE H H 7.72 . 1 456 . 105 ILE C C 175.6 . 1 457 . 105 ILE CA C 56.9 . 1 458 . 105 ILE CB C 39.6 . 1 459 . 105 ILE N N 123.0 . 1 460 . 106 PRO CA C 60.0 . 1 461 . 106 PRO CB C 29.3 . 1 462 . 107 GLY H H 6.56 . 1 463 . 107 GLY C C 175.0 . 1 464 . 107 GLY CA C 43.6 . 1 465 . 107 GLY N N 113.7 . 1 466 . 108 HIS H H 8.62 . 1 467 . 108 HIS C C 168.8 . 1 468 . 108 HIS CA C 54.0 . 1 469 . 108 HIS CB C 29.9 . 1 470 . 108 HIS N N 119.6 . 1 471 . 109 TYR H H 7.49 . 1 472 . 109 TYR C C 173.1 . 1 473 . 109 TYR CA C 54.0 . 1 474 . 109 TYR CB C 36.9 . 1 475 . 109 TYR N N 120.1 . 1 476 . 110 ASP H H 8.38 . 1 477 . 110 ASP C C 174.3 . 1 478 . 110 ASP CA C 54.9 . 1 479 . 110 ASP CB C 40.4 . 1 480 . 110 ASP N N 118.8 . 1 481 . 111 GLY H H 7.54 . 1 482 . 111 GLY C C 177.2 . 1 483 . 111 GLY CA C 45.1 . 1 484 . 111 GLY N N 103.4 . 1 485 . 112 VAL H H 7.90 . 1 486 . 112 VAL C C 169.9 . 1 487 . 112 VAL CA C 57.1 . 1 488 . 112 VAL CB C 33.3 . 1 489 . 112 VAL N N 114.0 . 1 490 . 113 GLY H H 7.56 . 1 491 . 113 GLY C C 172.4 . 1 492 . 113 GLY CA C 45.6 . 1 493 . 113 GLY N N 108.6 . 1 494 . 116 ILE CA C 57.8 . 1 495 . 116 ILE CB C 40.5 . 1 496 . 117 VAL H H 7.07 . 1 497 . 117 VAL C C 174.6 . 1 498 . 117 VAL CA C 61.2 . 1 499 . 117 VAL CB C 32.9 . 1 500 . 117 VAL N N 119.3 . 1 501 . 118 ARG H H 8.90 . 1 502 . 118 ARG C C 176.3 . 1 503 . 118 ARG CA C 51.1 . 1 504 . 118 ARG CB C 29.6 . 1 505 . 118 ARG N N 127.9 . 1 506 . 119 GLU H H 9.28 . 1 507 . 119 GLU C C 175.8 . 1 508 . 119 GLU CA C 56.2 . 1 509 . 119 GLU CB C 29.6 . 1 510 . 119 GLU N N 128.6 . 1 511 . 120 ASN H H 8.04 . 1 512 . 120 ASN C C 174.9 . 1 513 . 120 ASN CA C 51.1 . 1 514 . 120 ASN CB C 36.6 . 1 515 . 120 ASN N N 123.8 . 1 516 . 121 LYS H H 7.69 . 1 517 . 121 LYS C C 173.8 . 1 518 . 121 LYS CA C 56.6 . 1 519 . 121 LYS CB C 32.6 . 1 520 . 121 LYS N N 128.6 . 1 stop_ save_