data_4075 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR Assignments and Secondary Structure of the N Terminal Domain of DnaB Helicase from E. coli ; _BMRB_accession_number 4075 _BMRB_flat_file_name bmr4075.str _Entry_type original _Submission_date 1997-11-25 _Accession_date 1997-11-28 _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 Weigelt Johan . . 2 Miles Caroline S. . 3 Dixon Nicholas E. . 4 Otting Gottfried . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 259 "13C chemical shifts" 253 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-10-12 original author . stop_ _Original_release_date 1998-10-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Weigelt, J., Miles, C. S., Dixon, N. E., and Otting, G., "Backbone NMR Assignments and Secondary Structure of the N Terminal Domain of DnaB Helicase from E. coli," J. Biomol. NMR 11, 233-234 (1998). ; _Citation_title ; Backbone NMR Assignments and Secondary Structure of the N Terminal Domain of DnaB Helicase from E. coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98344243 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weigelt Johan . . 2 Miles Caroline S. . 3 Dixon Nicholas E. . 4 Otting Gottfried . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 11 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 233 _Page_last 234 _Year 1998 _Details . loop_ _Keyword 'DnaB helicase' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, J. H., Oldfield, E., Markley, J. L., and Sykes, B. D., J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_DnaB-Nterm _Saveframe_category molecular_system _Mol_system_name 'DnaB helicase' _Abbreviation_common 'DnaB helicase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DnaB-Nterm $DnaB-Nterm stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'N-terminal domain, residues 1-142' save_ ######################## # Monomeric polymers # ######################## save_DnaB-Nterm _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DnaB helicase' _Name_variant DnaBDC(143-470) _Abbreviation_common DnaB _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; AGNKPFNKQQAEPRERDPQV AGLKVPPHSIEAEQSVLGGL MLDNERWDDVAERVVADDFY TRPHRHIFTEMARLQESGSP IDLITLAESLERQGQLDSVG GFAYLAELSKNTPSAANISA YADIVRERAVVREMISVANE IA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 GLY 3 3 ASN 4 4 LYS 5 5 PRO 6 6 PHE 7 7 ASN 8 8 LYS 9 9 GLN 10 10 GLN 11 11 ALA 12 12 GLU 13 13 PRO 14 14 ARG 15 15 GLU 16 16 ARG 17 17 ASP 18 18 PRO 19 19 GLN 20 20 VAL 21 21 ALA 22 22 GLY 23 23 LEU 24 24 LYS 25 25 VAL 26 26 PRO 27 27 PRO 28 28 HIS 29 29 SER 30 30 ILE 31 31 GLU 32 32 ALA 33 33 GLU 34 34 GLN 35 35 SER 36 36 VAL 37 37 LEU 38 38 GLY 39 39 GLY 40 40 LEU 41 41 MET 42 42 LEU 43 43 ASP 44 44 ASN 45 45 GLU 46 46 ARG 47 47 TRP 48 48 ASP 49 49 ASP 50 50 VAL 51 51 ALA 52 52 GLU 53 53 ARG 54 54 VAL 55 55 VAL 56 56 ALA 57 57 ASP 58 58 ASP 59 59 PHE 60 60 TYR 61 61 THR 62 62 ARG 63 63 PRO 64 64 HIS 65 65 ARG 66 66 HIS 67 67 ILE 68 68 PHE 69 69 THR 70 70 GLU 71 71 MET 72 72 ALA 73 73 ARG 74 74 LEU 75 75 GLN 76 76 GLU 77 77 SER 78 78 GLY 79 79 SER 80 80 PRO 81 81 ILE 82 82 ASP 83 83 LEU 84 84 ILE 85 85 THR 86 86 LEU 87 87 ALA 88 88 GLU 89 89 SER 90 90 LEU 91 91 GLU 92 92 ARG 93 93 GLN 94 94 GLY 95 95 GLN 96 96 LEU 97 97 ASP 98 98 SER 99 99 VAL 100 100 GLY 101 101 GLY 102 102 PHE 103 103 ALA 104 104 TYR 105 105 LEU 106 106 ALA 107 107 GLU 108 108 LEU 109 109 SER 110 110 LYS 111 111 ASN 112 112 THR 113 113 PRO 114 114 SER 115 115 ALA 116 116 ALA 117 117 ASN 118 118 ILE 119 119 SER 120 120 ALA 121 121 TYR 122 122 ALA 123 123 ASP 124 124 ILE 125 125 VAL 126 126 ARG 127 127 GLU 128 128 ARG 129 129 ALA 130 130 VAL 131 131 VAL 132 132 ARG 133 133 GLU 134 134 MET 135 135 ILE 136 136 SER 137 137 VAL 138 138 ALA 139 139 ASN 140 140 GLU 141 141 ILE 142 142 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4297 "DnaB helicase" 80.28 114 99.12 100.00 9.92e-76 PDB 1B79 "N-Terminal Domain Of Dna Replication Protein Dnab" 80.28 119 100.00 100.00 1.20e-76 PDB 1JWE "Nmr Structure Of The N-Terminal Domain Of E. Coli Dnab Helicase" 80.28 114 99.12 100.00 9.92e-76 DBJ BAB38457 "replicative DNA helicase DnaB [Escherichia coli O157:H7 str. Sakai]" 100.00 471 99.30 100.00 1.25e-93 DBJ BAE78054 "replicative DNA helicase [Escherichia coli str. K12 substr. W3110]" 100.00 471 100.00 100.00 4.48e-94 DBJ BAG66812 "replicative DNA helicase [Escherichia coli O111:H-]" 100.00 471 100.00 100.00 4.48e-94 DBJ BAG79869 "replicative DNA helicase [Escherichia coli SE11]" 100.00 471 100.00 100.00 4.48e-94 DBJ BAH61192 "replicative DNA helicase [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 471 97.18 97.89 1.02e-90 EMBL CAP78509 "Replicative DNA helicase [Escherichia coli LF82]" 100.00 471 100.00 100.00 4.48e-94 EMBL CAQ34401 "dnaB, subunit of replicative DNA helicase and primosome [Escherichia coli BL21(DE3)]" 100.00 471 100.00 100.00 4.48e-94 EMBL CAQ91563 "replicative DNA helicase [Escherichia fergusonii ATCC 35469]" 100.00 471 97.18 97.89 5.78e-91 EMBL CAR01031 "replicative DNA helicase [Escherichia coli IAI1]" 100.00 471 100.00 100.00 4.48e-94 EMBL CAR05689 "replicative DNA helicase [Escherichia coli S88]" 100.00 471 97.18 98.59 3.37e-91 GB AAA23689 "DnaB replication protein (dnaB) [Escherichia coli]" 100.00 471 100.00 100.00 4.48e-94 GB AAA23690 "helicase, partial [Escherichia coli]" 100.00 157 100.00 100.00 1.07e-97 GB AAC43146 "ORF_o471 [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 100.00 100.00 4.48e-94 GB AAC77022 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 100.00 100.00 4.48e-94 GB AAG59250 "replicative DNA helicase; part of primosome [Escherichia coli O157:H7 str. EDL933]" 100.00 471 99.30 100.00 1.25e-93 REF NP_313061 "replicative DNA helicase [Escherichia coli O157:H7 str. Sakai]" 100.00 471 99.30 100.00 1.25e-93 REF NP_418476 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 100.00 100.00 4.48e-94 REF NP_709868 "replicative DNA helicase [Shigella flexneri 2a str. 301]" 100.00 471 100.00 100.00 4.48e-94 REF WP_000918354 "replicative DNA helicase [Shigella dysenteriae]" 100.00 471 99.30 100.00 1.67e-93 REF WP_000918355 "MULTISPECIES: replicative DNA helicase [Escherichia]" 100.00 471 99.30 100.00 1.67e-93 SP P0ACB0 "RecName: Full=Replicative DNA helicase" 100.00 471 100.00 100.00 4.48e-94 SP P0ACB1 "RecName: Full=Replicative DNA helicase" 100.00 471 100.00 100.00 4.48e-94 SP Q8FB22 "RecName: Full=Replicative DNA helicase" 100.00 471 97.18 98.59 3.37e-91 SP Q8X5V3 "RecName: Full=Replicative DNA helicase" 100.00 471 99.30 100.00 1.25e-93 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DnaB-Nterm 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $DnaB-Nterm 'recombinant technology' 'E. coli' Escherichia coli BL21DE3 plasmid pCM865 'natural source' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DnaB-Nterm 1.8 mM [U-13C;U-15N] 'sodium phosphate' 20 mM . pefabloc 1 mM . EDTA 1 mM . NaN3 0.02 '% w/v' . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 305 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 _Reference_correction_type _Correction_value _Correction_value_citation_label DSS C 13 . ppm 0.0 . indirect . . . 0.251449530 $citation_one . . . H2O H 1 . ppm 4.766 internal direct . . . . . temperature -0.083 $citation_one DSS N 15 . ppm 0.0 . indirect . . . 0.101329118 $citation_one . . . 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_shift_assignment _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name DnaB-Nterm _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 ASN H H 8.41 0.01 1 2 . 3 ASN HA H 4.68 0.01 1 3 . 3 ASN C C 174.9 0.1 1 4 . 3 ASN CA C 53.1 0.1 1 5 . 3 ASN N N 118.5 0.1 1 6 . 4 LYS H H 8.23 0.01 1 7 . 4 LYS HA H 4.57 0.01 1 8 . 4 LYS CA C 54.2 0.1 1 9 . 4 LYS N N 122.4 0.1 1 10 . 5 PRO HA H 4.35 0.01 1 11 . 5 PRO C C 176.7 0.1 1 12 . 5 PRO CA C 63.2 0.1 1 13 . 6 PHE H H 8.2 0.01 1 14 . 6 PHE HA H 4.54 0.01 1 15 . 6 PHE CA C 57.7 0.1 1 16 . 6 PHE N N 120.1 0.1 1 17 . 7 ASN H H 8.19 0.01 1 18 . 7 ASN HA H 4.6 0.01 1 19 . 7 ASN C C 174.7 0.1 1 20 . 7 ASN CA C 52.9 0.1 1 21 . 7 ASN N N 120.9 0.1 1 22 . 8 LYS H H 8.14 0.01 1 23 . 8 LYS HA H 4.19 0.01 1 24 . 8 LYS CA C 56.7 0.1 1 25 . 8 LYS N N 121.9 0.1 1 26 . 9 GLN H H 8.29 0.01 1 27 . 9 GLN HA H 4.26 0.01 1 28 . 9 GLN CA C 56.1 0.1 1 29 . 9 GLN N N 120.9 0.1 1 30 . 10 GLN H H 8.21 0.01 1 31 . 10 GLN HA H 4.27 0.01 1 32 . 10 GLN C C 175.4 0.1 1 33 . 10 GLN CA C 55.7 0.1 1 34 . 10 GLN N N 121.1 0.1 1 35 . 11 ALA H H 8.22 0.01 1 36 . 11 ALA HA H 4.3 0.01 1 37 . 11 ALA C C 177.3 0.1 1 38 . 11 ALA CA C 52.3 0.1 1 39 . 11 ALA N N 125.1 0.1 1 40 . 12 GLU H H 8.28 0.01 1 41 . 12 GLU HA H 4.54 0.01 1 42 . 12 GLU CA C 54.4 0.1 1 43 . 12 GLU N N 121.5 0.1 1 44 . 13 PRO HA H 4.38 0.01 1 45 . 13 PRO C C 177.00 0.1 1 46 . 13 PRO CA C 63.3 0.1 1 47 . 14 ARG H H 8.35 0.01 1 48 . 14 ARG HA H 4.3 0.01 1 49 . 14 ARG C C 176.4 0.1 1 50 . 14 ARG CA C 56.2 0.1 1 51 . 14 ARG N N 120.9 0.1 1 52 . 15 GLU H H 8.36 0.01 1 53 . 15 GLU HA H 4.24 0.01 1 54 . 15 GLU C C 176.2 0.1 1 55 . 15 GLU CA C 56.6 0.1 1 56 . 15 GLU N N 121.3 0.1 1 57 . 16 ARG H H 8.23 0.01 1 58 . 16 ARG HA H 4.26 0.01 1 59 . 16 ARG C C 175.7 0.1 1 60 . 16 ARG CA C 55.9 0.1 1 61 . 16 ARG N N 121.3 0.1 1 62 . 17 ASP H H 8.28 0.01 1 63 . 17 ASP HA H 4.82 0.01 1 64 . 17 ASP CA C 52.4 0.1 1 65 . 17 ASP N N 122.8 0.1 1 66 . 18 PRO HA H 4.36 0.01 1 67 . 18 PRO C C 177.4 0.1 1 68 . 18 PRO CA C 63.7 0.1 1 69 . 19 GLN H H 8.47 0.01 1 70 . 19 GLN HA H 4.25 0.01 1 71 . 19 GLN C C 176.5 0.1 1 72 . 19 GLN CA C 56.4 0.1 1 73 . 19 GLN N N 119.00 0.1 1 74 . 20 VAL H H 7.86 0.01 1 75 . 20 VAL HA H 4.06 0.01 1 76 . 20 VAL C C 176.1 0.1 1 77 . 20 VAL CA C 62.5 0.1 1 78 . 20 VAL N N 119.7 0.1 1 79 . 21 ALA H H 8.2 0.01 1 80 . 21 ALA HA H 4.27 0.01 1 81 . 21 ALA C C 178.2 0.1 1 82 . 21 ALA CA C 52.9 0.1 1 83 . 21 ALA N N 126.4 0.1 1 84 . 22 GLY H H 8.19 0.01 1 85 . 22 GLY HA2 H 3.9 0.1 2 86 . 22 GLY C C 174.00 0.1 1 87 . 22 GLY CA C 45.3 0.1 1 88 . 22 GLY N N 107.3 0.1 1 89 . 23 LEU H H 7.87 0.01 1 90 . 23 LEU HA H 4.31 0.01 1 91 . 23 LEU C C 177.3 0.1 1 92 . 23 LEU CA C 55.2 0.1 1 93 . 23 LEU N N 121.2 0.1 1 94 . 24 LYS H H 8.29 0.01 1 95 . 24 LYS HA H 4.33 0.01 1 96 . 24 LYS C C 176.2 0.1 1 97 . 24 LYS CA C 56.1 0.1 1 98 . 24 LYS N N 122.3 0.1 1 99 . 25 VAL H H 7.95 0.01 1 100 . 25 VAL HA H 4.41 0.01 1 101 . 25 VAL C C 173.9 0.1 1 102 . 25 VAL CA C 59.5 0.1 1 103 . 25 VAL N N 122.00 0.1 1 104 . 29 SER HA H 4.7 0.01 1 105 . 29 SER C C 174.6 0.1 1 106 . 30 ILE H H 9.16 0.01 1 107 . 30 ILE HA H 4.01 0.01 1 108 . 30 ILE C C 178.00 0.1 1 109 . 30 ILE CA C 64.2 0.1 1 110 . 30 ILE N N 129.9 0.1 1 111 . 31 GLU H H 8.93 0.01 1 112 . 31 GLU HA H 4.12 0.01 1 113 . 31 GLU C C 179.4 0.1 1 114 . 31 GLU CA C 60.00 0.1 1 115 . 31 GLU N N 120.1 0.1 1 116 . 32 ALA H H 8.02 0.01 1 117 . 32 ALA HA H 3.81 0.01 1 118 . 32 ALA C C 179.2 0.1 1 119 . 32 ALA CA C 55.5 0.1 1 120 . 32 ALA N N 122.7 0.1 1 121 . 33 GLU H H 7.9 0.01 1 122 . 33 GLU HA H 3.79 0.01 1 123 . 33 GLU C C 178.9 0.1 1 124 . 33 GLU CA C 60.9 0.1 1 125 . 33 GLU N N 115.8 0.1 1 126 . 34 GLN H H 8.65 0.01 1 127 . 34 GLN HA H 3.56 0.01 1 128 . 34 GLN C C 178.7 0.1 1 129 . 34 GLN CA C 59.6 0.1 1 130 . 34 GLN N N 115.2 0.1 1 131 . 35 SER H H 7.87 0.01 1 132 . 35 SER HA H 4.15 0.01 1 133 . 35 SER C C 176.9 0.1 1 134 . 35 SER CA C 62.4 0.1 1 135 . 35 SER N N 114.8 0.1 1 136 . 36 VAL H H 7.99 0.01 1 137 . 36 VAL HA H 3.67 0.01 1 138 . 36 VAL C C 176.4 0.1 1 139 . 36 VAL CA C 66.9 0.1 1 140 . 36 VAL N N 121.7 0.1 1 141 . 37 LEU H H 7.7 0.01 1 142 . 37 LEU HA H 4.05 0.01 1 143 . 37 LEU C C 179.00 0.1 1 144 . 37 LEU CA C 58.2 0.1 1 145 . 37 LEU N N 116.2 0.1 1 146 . 38 GLY H H 8.81 0.01 1 147 . 38 GLY HA2 H 3.88 0.1 2 148 . 38 GLY HA3 H 3.5 0.1 2 149 . 38 GLY C C 176.6 0.1 1 150 . 38 GLY CA C 47.4 0.1 1 151 . 38 GLY N N 104.6 0.1 1 152 . 39 GLY H H 8.06 0.01 1 153 . 39 GLY HA2 H 3.75 0.1 2 154 . 39 GLY C C 175.8 0.1 1 155 . 39 GLY CA C 47.6 0.1 1 156 . 39 GLY N N 108.6 0.1 1 157 . 40 LEU H H 7.93 0.01 1 158 . 40 LEU HA H 4.14 0.01 1 159 . 40 LEU C C 178.3 0.1 1 160 . 40 LEU CA C 56.9 0.1 1 161 . 40 LEU N N 122.1 0.1 1 162 . 41 MET H H 7.29 0.01 1 163 . 41 MET HA H 4.2 0.01 1 164 . 41 MET C C 178.6 0.1 1 165 . 41 MET CA C 58.9 0.1 1 166 . 41 MET N N 115.5 0.1 1 167 . 42 LEU H H 7.29 0.01 1 168 . 42 LEU HA H 4.23 0.01 1 169 . 42 LEU C C 177.2 0.1 1 170 . 42 LEU CA C 56.5 0.1 1 171 . 42 LEU N N 118.1 0.1 1 172 . 43 ASP H H 8.1 0.01 1 173 . 43 ASP HA H 4.93 0.01 1 174 . 43 ASP C C 175.3 0.1 1 175 . 43 ASP CA C 52.5 0.1 1 176 . 43 ASP N N 119.4 0.1 1 177 . 44 ASN H H 9.1 0.01 1 178 . 44 ASN HA H 4.55 0.01 1 179 . 44 ASN C C 177.4 0.1 1 180 . 44 ASN CA C 55.1 0.1 1 181 . 44 ASN N N 120.6 0.1 1 182 . 45 GLU H H 8.35 0.01 1 183 . 45 GLU HA H 4.26 0.01 1 184 . 45 GLU C C 177.6 0.1 1 185 . 45 GLU CA C 58.1 0.1 1 186 . 45 GLU N N 116.6 0.1 1 187 . 46 ARG H H 7.59 0.01 1 188 . 46 ARG HA H 4.52 0.01 1 189 . 46 ARG C C 175.4 0.1 1 190 . 46 ARG CA C 55.2 0.1 1 191 . 46 ARG N N 116.8 0.1 1 192 . 47 TRP H H 7.71 0.01 1 193 . 47 TRP HA H 4.00 0.01 1 194 . 47 TRP C C 176.3 0.1 1 195 . 47 TRP CA C 61.5 0.1 1 196 . 47 TRP N N 119.4 0.1 1 197 . 48 ASP H H 8.34 0.01 1 198 . 48 ASP HA H 4.06 0.01 1 199 . 48 ASP C C 178.3 0.1 1 200 . 48 ASP CA C 58.00 0.1 1 201 . 48 ASP N N 115.6 0.1 1 202 . 49 ASP H H 7.77 0.01 1 203 . 49 ASP HA H 4.24 0.01 1 204 . 49 ASP C C 178.3 0.1 1 205 . 49 ASP CA C 56.9 0.1 1 206 . 49 ASP N N 117.7 0.1 1 207 . 50 VAL H H 7.58 0.01 1 208 . 50 VAL HA H 3.35 0.01 1 209 . 50 VAL C C 177.7 0.1 1 210 . 50 VAL CA C 66.7 0.1 1 211 . 50 VAL N N 118.3 0.1 1 212 . 51 ALA H H 8.79 0.01 1 213 . 51 ALA HA H 4.04 0.01 1 214 . 51 ALA C C 178.8 0.1 1 215 . 51 ALA CA C 53.9 0.1 1 216 . 51 ALA N N 121.9 0.1 1 217 . 52 GLU H H 7.18 0.01 1 218 . 52 GLU HA H 4.22 0.01 1 219 . 52 GLU C C 177.00 0.1 1 220 . 52 GLU CA C 57.00 0.1 1 221 . 52 GLU N N 113.7 0.1 1 222 . 53 ARG H H 7.82 0.01 1 223 . 53 ARG HA H 4.28 0.01 1 224 . 53 ARG C C 175.3 0.1 1 225 . 53 ARG CA C 57.1 0.1 1 226 . 53 ARG N N 118.3 0.1 1 227 . 54 VAL H H 7.63 0.01 1 228 . 54 VAL HA H 4.79 0.01 1 229 . 54 VAL C C 173.6 0.1 1 230 . 54 VAL CA C 59.00 0.1 1 231 . 54 VAL N N 112.5 0.1 1 232 . 55 VAL H H 8.29 0.01 1 233 . 55 VAL HA H 4.66 0.01 1 234 . 55 VAL C C 177.6 0.1 1 235 . 55 VAL CA C 58.8 0.1 1 236 . 55 VAL N N 113.1 0.1 1 237 . 56 ALA H H 8.99 0.01 1 238 . 56 ALA HA H 3.94 0.01 1 239 . 56 ALA C C 179.2 0.1 1 240 . 56 ALA CA C 56.5 0.1 1 241 . 56 ALA N N 123.6 0.1 1 242 . 57 ASP H H 8.04 0.01 1 243 . 57 ASP HA H 4.34 0.01 1 244 . 57 ASP C C 176.1 0.1 1 245 . 57 ASP CA C 56.00 0.1 1 246 . 57 ASP N N 110.7 0.1 1 247 . 58 ASP H H 7.94 0.01 1 248 . 58 ASP HA H 4.28 0.01 1 249 . 58 ASP CA C 56.3 0.1 1 250 . 58 ASP N N 117.4 0.1 1 251 . 63 PRO HA H 4.25 0.01 1 252 . 63 PRO C C 178.2 0.1 1 253 . 63 PRO CA C 66.4 0.1 1 254 . 64 HIS H H 7.2 0.01 1 255 . 64 HIS HA H 4.33 0.01 1 256 . 64 HIS C C 176.8 0.1 1 257 . 64 HIS CA C 57.1 0.1 1 258 . 64 HIS N N 114.00 0.1 1 259 . 65 ARG H H 8.03 0.01 1 260 . 65 ARG HA H 3.89 0.01 1 261 . 65 ARG CA C 60.7 0.1 1 262 . 65 ARG N N 119.00 0.1 1 263 . 66 HIS H H 8.18 0.01 1 264 . 66 HIS HA H 4.3 0.01 1 265 . 66 HIS C C 178.8 0.1 1 266 . 66 HIS CA C 58.9 0.1 1 267 . 66 HIS N N 119.3 0.1 1 268 . 67 ILE H H 8.66 0.01 1 269 . 67 ILE HA H 3.46 0.01 1 270 . 67 ILE C C 176.8 0.1 1 271 . 67 ILE CA C 66.9 0.1 1 272 . 67 ILE N N 120.2 0.1 1 273 . 68 PHE H H 8.41 0.01 1 274 . 68 PHE HA H 4.02 0.01 1 275 . 68 PHE C C 177.1 0.1 1 276 . 68 PHE CA C 62.7 0.1 1 277 . 68 PHE N N 120.00 0.1 1 278 . 69 THR H H 8.21 0.01 1 279 . 69 THR HA H 3.94 0.01 1 280 . 69 THR C C 176.4 0.1 1 281 . 69 THR CA C 67.1 0.1 1 282 . 69 THR N N 113.4 0.1 1 283 . 70 GLU H H 7.92 0.01 1 284 . 70 GLU HA H 4.31 0.01 1 285 . 70 GLU C C 178.3 0.1 1 286 . 70 GLU CA C 58.2 0.1 1 287 . 70 GLU N N 123.3 0.1 1 288 . 71 MET H H 8.47 0.01 1 289 . 71 MET HA H 3.57 0.01 1 290 . 71 MET C C 176.7 0.1 1 291 . 71 MET CA C 60.3 0.1 1 292 . 71 MET N N 119.4 0.1 1 293 . 72 ALA H H 7.94 0.01 1 294 . 72 ALA HA H 3.34 0.01 1 295 . 72 ALA C C 180.3 0.1 1 296 . 72 ALA CA C 54.9 0.1 1 297 . 72 ALA N N 119.8 0.1 1 298 . 73 ARG H H 7.71 0.01 1 299 . 73 ARG HA H 3.88 0.01 1 300 . 73 ARG C C 180.2 0.1 1 301 . 73 ARG CA C 59.1 0.1 1 302 . 73 ARG N N 120.2 0.1 1 303 . 74 LEU H H 8.38 0.01 1 304 . 74 LEU HA H 3.75 0.01 1 305 . 74 LEU C C 179.8 0.1 1 306 . 74 LEU CA C 58.00 0.1 1 307 . 74 LEU N N 122.2 0.1 1 308 . 75 GLN H H 8.38 0.01 1 309 . 75 GLN HA H 3.73 0.01 1 310 . 75 GLN C C 180.4 0.1 1 311 . 75 GLN CA C 59.2 0.1 1 312 . 75 GLN N N 120.4 0.1 1 313 . 76 GLU H H 7.89 0.01 1 314 . 76 GLU HA H 3.92 0.01 1 315 . 76 GLU C C 177.6 0.1 1 316 . 76 GLU CA C 58.9 0.1 1 317 . 76 GLU N N 120.6 0.1 1 318 . 77 SER H H 7.41 0.01 1 319 . 77 SER HA H 4.5 0.01 1 320 . 77 SER C C 174.6 0.1 1 321 . 77 SER CA C 58.4 0.1 1 322 . 77 SER N N 111.9 0.1 1 323 . 78 GLY H H 7.77 0.01 1 324 . 78 GLY HA2 H 4.1 0.1 2 325 . 78 GLY HA3 H 3.76 0.1 2 326 . 78 GLY C C 174.6 0.1 1 327 . 78 GLY CA C 45.7 0.1 1 328 . 78 GLY N N 109.9 0.1 1 329 . 79 SER H H 7.84 0.01 1 330 . 79 SER HA H 4.83 0.01 1 331 . 79 SER CA C 56.00 0.1 1 332 . 79 SER N N 117.1 0.1 1 333 . 80 PRO HA H 4.43 0.01 1 334 . 80 PRO C C 174.5 0.1 1 335 . 80 PRO CA C 62.8 0.1 1 336 . 81 ILE H H 7.06 0.01 1 337 . 81 ILE HA H 4.33 0.01 1 338 . 81 ILE C C 173.4 0.1 1 339 . 81 ILE CA C 60.1 0.1 1 340 . 81 ILE N N 108.8 0.1 1 341 . 82 ASP H H 7.4 0.01 1 342 . 82 ASP HA H 4.81 0.01 1 343 . 82 ASP C C 173.6 0.1 1 344 . 82 ASP CA C 52.8 0.1 1 345 . 82 ASP N N 113.9 0.1 1 346 . 83 LEU H H 8.37 0.01 1 347 . 83 LEU HA H 3.94 0.01 1 348 . 83 LEU C C 177.00 0.1 1 349 . 83 LEU CA C 59.2 0.1 1 350 . 83 LEU N N 118.3 0.1 1 351 . 84 ILE H H 7.59 0.01 1 352 . 84 ILE HA H 3.8 0.01 1 353 . 84 ILE C C 178.4 0.1 1 354 . 84 ILE CA C 64.2 0.1 1 355 . 84 ILE N N 115.3 0.1 1 356 . 85 THR H H 7.95 0.01 1 357 . 85 THR HA H 3.76 0.01 1 358 . 85 THR C C 177.9 0.1 1 359 . 85 THR CA C 66.8 0.1 1 360 . 85 THR N N 119.1 0.1 1 361 . 86 LEU H H 8.58 0.01 1 362 . 86 LEU HA H 3.86 0.01 1 363 . 86 LEU C C 178.00 0.1 1 364 . 86 LEU CA C 58.2 0.1 1 365 . 86 LEU N N 122.1 0.1 1 366 . 87 ALA H H 8.59 0.01 1 367 . 87 ALA HA H 3.81 0.01 1 368 . 87 ALA C C 179.8 0.1 1 369 . 87 ALA CA C 55.8 0.1 1 370 . 87 ALA N N 120.2 0.1 1 371 . 88 GLU H H 8.45 0.01 1 372 . 88 GLU HA H 4.01 0.01 1 373 . 88 GLU C C 179.1 0.1 1 374 . 88 GLU CA C 60.1 0.1 1 375 . 88 GLU N N 116.7 0.1 1 376 . 89 SER H H 8.02 0.01 1 377 . 89 SER HA H 4.12 0.01 1 378 . 89 SER C C 179.00 0.1 1 379 . 89 SER CA C 61.3 0.1 1 380 . 89 SER N N 114.2 0.1 1 381 . 90 LEU H H 8.4 0.01 1 382 . 90 LEU HA H 3.89 0.01 1 383 . 90 LEU C C 179.6 0.1 1 384 . 90 LEU CA C 58.1 0.1 1 385 . 90 LEU N N 118.4 0.1 1 386 . 91 GLU H H 8.84 0.01 1 387 . 91 GLU HA H 4.14 0.01 1 388 . 91 GLU C C 180.6 0.1 1 389 . 91 GLU CA C 59.9 0.1 1 390 . 91 GLU N N 122.2 0.1 1 391 . 92 ARG H H 8.42 0.01 1 392 . 92 ARG HA H 4.13 0.01 1 393 . 92 ARG C C 178.3 0.1 1 394 . 92 ARG CA C 59.4 0.1 1 395 . 92 ARG N N 121.5 0.1 1 396 . 93 GLN H H 7.33 0.01 1 397 . 93 GLN HA H 4.38 0.01 1 398 . 93 GLN C C 176.3 0.1 1 399 . 93 GLN CA C 55.7 0.1 1 400 . 93 GLN N N 114.2 0.1 1 401 . 94 GLY H H 8.16 0.01 1 402 . 94 GLY HA2 H 4.08 0.1 2 403 . 94 GLY C C 176.2 0.1 1 404 . 94 GLY CA C 46.5 0.1 1 405 . 94 GLY N N 109.5 0.1 1 406 . 95 GLN H H 8.18 0.01 1 407 . 95 GLN HA H 4.63 0.01 1 408 . 95 GLN C C 176.4 0.1 1 409 . 95 GLN CA C 55.00 0.1 1 410 . 95 GLN N N 115.2 0.1 1 411 . 96 LEU H H 7.74 0.01 1 412 . 96 LEU HA H 3.98 0.01 1 413 . 96 LEU C C 178.9 0.1 1 414 . 96 LEU CA C 58.2 0.1 1 415 . 96 LEU N N 122.9 0.1 1 416 . 97 ASP H H 8.54 0.01 1 417 . 97 ASP HA H 4.29 0.01 1 418 . 97 ASP C C 179.8 0.1 1 419 . 97 ASP CA C 57.6 0.1 1 420 . 97 ASP N N 118.7 0.1 1 421 . 98 SER H H 7.82 0.01 1 422 . 98 SER HA H 4.23 0.01 1 423 . 98 SER C C 175.8 0.1 1 424 . 98 SER CA C 61.00 0.1 1 425 . 98 SER N N 115.2 0.1 1 426 . 99 VAL H H 7.11 0.01 1 427 . 99 VAL HA H 4.47 0.01 1 428 . 99 VAL C C 173.6 0.1 1 429 . 99 VAL CA C 60.4 0.1 1 430 . 99 VAL N N 111.2 0.1 1 431 . 100 GLY H H 7.39 0.01 1 432 . 100 GLY HA2 H 4.35 0.1 2 433 . 100 GLY HA3 H 3.55 0.1 2 434 . 100 GLY C C 175.4 0.1 1 435 . 100 GLY CA C 44.4 0.1 1 436 . 100 GLY N N 104.9 0.1 1 437 . 101 GLY H H 7.92 0.01 1 438 . 101 GLY HA2 H 3.68 0.01 2 439 . 101 GLY C C 172.9 0.1 1 440 . 101 GLY CA C 44.2 0.1 1 441 . 101 GLY N N 107.4 0.1 1 442 . 103 ALA HA H 3.94 0.01 1 443 . 103 ALA C C 180.2 0.1 1 444 . 103 ALA CA C 55.2 0.1 1 445 . 104 TYR H H 7.13 0.01 1 446 . 104 TYR HA H 4.36 0.01 1 447 . 104 TYR C C 177.2 0.1 1 448 . 104 TYR CA C 61.4 0.1 1 449 . 104 TYR N N 117.3 0.1 1 450 . 105 LEU H H 7.02 0.01 1 451 . 105 LEU HA H 3.56 0.01 1 452 . 105 LEU C C 178.6 0.1 1 453 . 105 LEU CA C 57.9 0.1 1 454 . 105 LEU N N 116.6 0.1 1 455 . 106 ALA H H 8.43 0.01 1 456 . 106 ALA HA H 3.67 0.01 1 457 . 106 ALA C C 180.7 0.1 1 458 . 106 ALA CA C 54.5 0.1 1 459 . 106 ALA N N 119.1 0.1 1 460 . 107 GLU H H 7.68 0.01 1 461 . 107 GLU HA H 3.82 0.01 1 462 . 107 GLU C C 179.1 0.1 1 463 . 107 GLU CA C 59.4 0.1 1 464 . 107 GLU N N 121.00 0.1 1 465 . 108 LEU H H 7.77 0.01 1 466 . 108 LEU HA H 3.69 0.01 1 467 . 108 LEU C C 179.4 0.1 1 468 . 108 LEU CA C 57.7 0.1 1 469 . 108 LEU N N 118.6 0.1 1 470 . 109 SER H H 7.53 0.01 1 471 . 109 SER HA H 4.18 0.01 1 472 . 109 SER C C 175.4 0.1 1 473 . 109 SER CA C 60.5 0.1 1 474 . 109 SER N N 111.7 0.1 1 475 . 110 LYS H H 7.66 0.01 1 476 . 110 LYS HA H 4.11 0.01 1 477 . 110 LYS C C 177.6 0.1 1 478 . 110 LYS CA C 57.9 0.1 1 479 . 110 LYS N N 120.2 0.1 1 480 . 111 ASN H H 7.75 0.01 1 481 . 111 ASN HA H 4.66 0.01 1 482 . 111 ASN C C 174.2 0.1 1 483 . 111 ASN CA C 53.4 0.1 1 484 . 111 ASN N N 116.5 0.1 1 485 . 112 THR H H 7.48 0.01 1 486 . 112 THR HA H 4.55 0.01 1 487 . 112 THR C C 172.8 0.1 1 488 . 112 THR CA C 59.5 0.1 1 489 . 112 THR N N 114.6 0.1 1 490 . 113 PRO HA H 4.53 0.01 1 491 . 113 PRO C C 176.6 0.1 1 492 . 113 PRO CA C 63.1 0.1 1 493 . 114 SER H H 7.97 0.01 1 494 . 114 SER HA H 4.42 0.01 1 495 . 114 SER C C 174.4 0.1 1 496 . 114 SER CA C 57.8 0.1 1 497 . 114 SER N N 113.2 0.1 1 498 . 115 ALA H H 8.81 0.01 1 499 . 115 ALA HA H 4.4 0.01 1 500 . 115 ALA C C 178.00 0.1 1 501 . 115 ALA CA C 53.00 0.1 1 502 . 115 ALA N N 125.4 0.1 1 503 . 116 ALA H H 8.1 0.01 1 504 . 116 ALA HA H 4.12 0.01 1 505 . 116 ALA C C 178.8 0.1 1 506 . 116 ALA CA C 54.2 0.1 1 507 . 116 ALA N N 120.4 0.1 1 508 . 117 ASN H H 8.26 0.01 1 509 . 117 ASN HA H 4.8 0.01 1 510 . 117 ASN C C 176.2 0.1 1 511 . 117 ASN CA C 52.9 0.1 1 512 . 117 ASN N N 116.1 0.1 1 513 . 118 ILE H H 8.00 0.01 1 514 . 118 ILE HA H 3.91 0.01 1 515 . 118 ILE C C 176.9 0.1 1 516 . 118 ILE CA C 66.1 0.1 1 517 . 118 ILE N N 121.00 0.1 1 518 . 119 SER H H 8.13 0.01 1 519 . 119 SER HA H 3.81 0.01 1 520 . 119 SER C C 174.9 0.1 1 521 . 119 SER CA C 62.5 0.1 1 522 . 119 SER N N 117.2 0.1 1 523 . 120 ALA H H 7.21 0.01 1 524 . 120 ALA HA H 4.12 0.01 1 525 . 120 ALA C C 181.5 0.1 1 526 . 120 ALA CA C 54.5 0.1 1 527 . 120 ALA N N 123.1 0.1 1 528 . 121 TYR H H 7.71 0.01 1 529 . 121 TYR HA H 4.4 0.01 1 530 . 121 TYR C C 177.8 0.1 1 531 . 121 TYR CA C 60.8 0.1 1 532 . 121 TYR N N 116.8 0.1 1 533 . 122 ALA H H 8.3 0.01 1 534 . 122 ALA HA H 3.73 0.01 1 535 . 122 ALA C C 177.9 0.1 1 536 . 122 ALA CA C 55.7 0.1 1 537 . 122 ALA N N 122.9 0.1 1 538 . 123 ASP H H 8.01 0.01 1 539 . 123 ASP HA H 4.37 0.01 1 540 . 123 ASP C C 179.1 0.1 1 541 . 123 ASP CA C 57.5 0.1 1 542 . 123 ASP N N 117.2 0.1 1 543 . 124 ILE H H 7.42 0.01 1 544 . 124 ILE HA H 3.76 0.01 1 545 . 124 ILE C C 177.4 0.1 1 546 . 124 ILE CA C 65.3 0.1 1 547 . 124 ILE N N 121.1 0.1 1 548 . 125 VAL H H 7.75 0.01 1 549 . 125 VAL HA H 3.37 0.01 1 550 . 125 VAL C C 179.7 0.1 1 551 . 125 VAL CA C 67.00 0.1 1 552 . 125 VAL N N 120.3 0.1 1 553 . 126 ARG H H 8.06 0.01 1 554 . 126 ARG HA H 3.82 0.01 1 555 . 126 ARG C C 177.4 0.1 1 556 . 126 ARG CA C 59.4 0.1 1 557 . 126 ARG N N 120.9 0.1 1 558 . 127 GLU H H 8.53 0.01 1 559 . 127 GLU HA H 3.92 0.01 1 560 . 127 GLU C C 180.00 0.1 1 561 . 127 GLU CA C 59.8 0.1 1 562 . 127 GLU N N 119.6 0.1 1 563 . 128 ARG H H 8.62 0.01 1 564 . 128 ARG HA H 3.99 0.01 1 565 . 128 ARG C C 177.5 0.1 1 566 . 128 ARG CA C 57.7 0.1 1 567 . 128 ARG N N 115.9 0.1 1 568 . 129 ALA H H 7.6 0.01 1 569 . 129 ALA HA H 3.98 0.01 1 570 . 129 ALA C C 180.4 0.1 1 571 . 129 ALA CA C 55.4 0.1 1 572 . 129 ALA N N 121.8 0.1 1 573 . 130 VAL H H 8.08 0.01 1 574 . 130 VAL HA H 3.67 0.01 1 575 . 130 VAL C C 179.00 0.1 1 576 . 130 VAL CA C 66.3 0.1 1 577 . 130 VAL N N 120.2 0.1 1 578 . 131 VAL H H 7.57 0.01 1 579 . 131 VAL HA H 3.75 0.01 1 580 . 131 VAL C C 178.3 0.1 1 581 . 131 VAL CA C 66.1 0.1 1 582 . 131 VAL N N 119.1 0.1 1 583 . 132 ARG H H 8.29 0.01 1 584 . 132 ARG HA H 3.97 0.01 1 585 . 132 ARG C C 178.5 0.1 1 586 . 132 ARG CA C 60.3 0.1 1 587 . 132 ARG N N 119.5 0.1 1 588 . 133 GLU H H 7.97 0.01 1 589 . 133 GLU HA H 4.18 0.01 1 590 . 133 GLU C C 178.00 0.1 1 591 . 133 GLU CA C 58.3 0.1 1 592 . 133 GLU N N 118.5 0.1 1 593 . 134 MET H H 7.89 0.01 1 594 . 134 MET HA H 4.29 0.01 1 595 . 134 MET C C 177.9 0.1 1 596 . 134 MET CA C 57.7 0.1 1 597 . 134 MET N N 118.5 0.1 1 598 . 135 ILE H H 7.97 0.01 1 599 . 135 ILE HA H 4.12 0.01 1 600 . 135 ILE C C 176.9 0.1 1 601 . 135 ILE CA C 62.6 0.1 1 602 . 135 ILE N N 118.3 0.1 1 603 . 136 SER H H 7.97 0.01 1 604 . 136 SER HA H 4.41 0.01 1 605 . 136 SER C C 175.2 0.1 1 606 . 136 SER CA C 59.4 0.1 1 607 . 136 SER N N 117.6 0.1 1 608 . 137 VAL H H 7.94 0.01 1 609 . 137 VAL HA H 4.13 0.01 1 610 . 137 VAL C C 176.3 0.1 1 611 . 137 VAL CA C 62.7 0.1 1 612 . 137 VAL N N 120.3 0.1 1 613 . 138 ALA H H 8.07 0.01 1 614 . 138 ALA HA H 4.3 0.01 1 615 . 138 ALA C C 177.6 0.1 1 616 . 138 ALA CA C 52.8 0.1 1 617 . 138 ALA N N 125.8 0.1 1 618 . 139 ASN H H 8.18 0.01 1 619 . 139 ASN HA H 4.68 0.01 1 620 . 139 ASN C C 175.1 0.1 1 621 . 139 ASN CA C 53.4 0.1 1 622 . 139 ASN N N 117.2 0.1 1 623 . 140 GLU H H 8.15 0.01 1 624 . 140 GLU HA H 4.28 0.01 1 625 . 140 GLU C C 176.2 0.1 1 626 . 140 GLU CA C 56.7 0.1 1 627 . 140 GLU N N 120.7 0.1 1 628 . 141 ILE H H 8.05 0.01 1 629 . 141 ILE HA H 4.16 0.01 1 630 . 141 ILE C C 174.9 0.1 1 631 . 141 ILE CA C 61.1 0.1 1 632 . 141 ILE N N 121.5 0.1 1 633 . 142 ALA H H 7.84 0.01 1 634 . 142 ALA HA H 4.13 0.01 1 635 . 142 ALA CA C 53.8 0.1 1 636 . 142 ALA N N 133.6 0.1 1 stop_ save_