data_4297 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shifts (1H, 13C, 15N) and J-couplings (3JHNHA, 3JNHB, 3JHAHB) for the N-terminal Domain of E. coli DnaB Helicase, DnaB(24-136) ; _BMRB_accession_number 4297 _BMRB_flat_file_name bmr4297.str _Entry_type original _Submission_date 1999-01-20 _Accession_date 1999-01-20 _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 Brown Susan E. . 3 Miles Caroline S. . 4 Dixon Nicholas E. . 5 Otting Gottfried . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 631 "13C chemical shifts" 453 "15N chemical shifts" 112 "coupling constants" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-22 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4075 . stop_ _Original_release_date 1999-02-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Weigelt, J., Brown, S. E., Miles, C. S., Dixon, N. E., and Otting, G., "NMR Structure of the N-terminal Domain of E. coli DnaB Helicase: Implications for Structure Rearrangements in the Helicase Hexamer and its Biological Function," Structure Fold Des. 7(6) 681-690 (1999). ; _Citation_title ; NMR Structure of the N-terminal Domain of E. coli DnaB Helicase: Implications for Structure Rearrangements in the Helicase Hexamer and its Biological Function ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99332676 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weigelt Johan . . 2 Brown Susan E. . 3 Miles Caroline S. . 4 Dixon Nicholas E. . 5 Otting Gottfried . . stop_ _Journal_abbreviation 'Structure Fold Des.' _Journal_volume 7 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 681 _Page_last 690 _Year 1999 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR, 6, 135-40 (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(24-136) _Saveframe_category molecular_system _Mol_system_name 'DnaB helicase N-terminal domain' _Abbreviation_common DnaB(24-136) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DnaB(24-136) $DnaB(24-136) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DnaB(24-136) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DnaB helicase' _Name_variant DnaB(24-136) _Abbreviation_common DnaB(24-136) _Molecular_mass . _Mol_thiol_state . _Details ; N-terminal Met (residue 23) not cleaved off ; ############################## # Polymer residue sequence # ############################## _Residue_count 114 _Mol_residue_sequence ; MKVPPHSIEAEQSVLGGLML DNERWDDVAERVVADDFYTR PHRHIFTEMARLQESGSPID LITLAESLERQGQLDSVGGF AYLAELSKNTPSAANISAYA DIVRERAVVREMIS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 23 MET 2 24 LYS 3 25 VAL 4 26 PRO 5 27 PRO 6 28 HIS 7 29 SER 8 30 ILE 9 31 GLU 10 32 ALA 11 33 GLU 12 34 GLN 13 35 SER 14 36 VAL 15 37 LEU 16 38 GLY 17 39 GLY 18 40 LEU 19 41 MET 20 42 LEU 21 43 ASP 22 44 ASN 23 45 GLU 24 46 ARG 25 47 TRP 26 48 ASP 27 49 ASP 28 50 VAL 29 51 ALA 30 52 GLU 31 53 ARG 32 54 VAL 33 55 VAL 34 56 ALA 35 57 ASP 36 58 ASP 37 59 PHE 38 60 TYR 39 61 THR 40 62 ARG 41 63 PRO 42 64 HIS 43 65 ARG 44 66 HIS 45 67 ILE 46 68 PHE 47 69 THR 48 70 GLU 49 71 MET 50 72 ALA 51 73 ARG 52 74 LEU 53 75 GLN 54 76 GLU 55 77 SER 56 78 GLY 57 79 SER 58 80 PRO 59 81 ILE 60 82 ASP 61 83 LEU 62 84 ILE 63 85 THR 64 86 LEU 65 87 ALA 66 88 GLU 67 89 SER 68 90 LEU 69 91 GLU 70 92 ARG 71 93 GLN 72 94 GLY 73 95 GLN 74 96 LEU 75 97 ASP 76 98 SER 77 99 VAL 78 100 GLY 79 101 GLY 80 102 PHE 81 103 ALA 82 104 TYR 83 105 LEU 84 106 ALA 85 107 GLU 86 108 LEU 87 109 SER 88 110 LYS 89 111 ASN 90 112 THR 91 113 PRO 92 114 SER 93 115 ALA 94 116 ALA 95 117 ASN 96 118 ILE 97 119 SER 98 120 ALA 99 121 TYR 100 122 ALA 101 123 ASP 102 124 ILE 103 125 VAL 104 126 ARG 105 127 GLU 106 128 ARG 107 129 ALA 108 130 VAL 109 131 VAL 110 132 ARG 111 133 GLU 112 134 MET 113 135 ILE 114 136 SER 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 4075 "DnaB helicase" 100.00 142 99.12 100.00 7.97e-76 PDB 1B79 "N-Terminal Domain Of Dna Replication Protein Dnab" 92.98 119 99.06 100.00 3.29e-70 PDB 1JWE "Nmr Structure Of The N-Terminal Domain Of E. Coli Dnab Helicase" 100.00 114 100.00 100.00 1.67e-76 DBJ BAB38457 "replicative DNA helicase DnaB [Escherichia coli O157:H7 str. Sakai]" 100.00 471 98.25 100.00 1.67e-71 DBJ BAE78054 "replicative DNA helicase [Escherichia coli str. K12 substr. W3110]" 100.00 471 99.12 100.00 5.98e-72 DBJ BAG66812 "replicative DNA helicase [Escherichia coli O111:H-]" 100.00 471 99.12 100.00 5.98e-72 DBJ BAG79869 "replicative DNA helicase [Escherichia coli SE11]" 100.00 471 99.12 100.00 5.98e-72 DBJ BAH61192 "replicative DNA helicase [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 471 99.12 100.00 7.32e-72 EMBL CAP78509 "Replicative DNA helicase [Escherichia coli LF82]" 100.00 471 99.12 100.00 5.98e-72 EMBL CAQ34401 "dnaB, subunit of replicative DNA helicase and primosome [Escherichia coli BL21(DE3)]" 100.00 471 99.12 100.00 5.98e-72 EMBL CAQ91563 "replicative DNA helicase [Escherichia fergusonii ATCC 35469]" 100.00 471 98.25 99.12 2.56e-71 EMBL CAR01031 "replicative DNA helicase [Escherichia coli IAI1]" 100.00 471 99.12 100.00 5.98e-72 EMBL CAR05689 "replicative DNA helicase [Escherichia coli S88]" 100.00 471 99.12 100.00 6.17e-72 GB AAA23689 "DnaB replication protein (dnaB) [Escherichia coli]" 100.00 471 99.12 100.00 5.98e-72 GB AAA23690 "helicase, partial [Escherichia coli]" 100.00 157 99.12 100.00 1.51e-75 GB AAC43146 "ORF_o471 [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.98e-72 GB AAC77022 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.98e-72 GB AAG59250 "replicative DNA helicase; part of primosome [Escherichia coli O157:H7 str. EDL933]" 100.00 471 98.25 100.00 1.67e-71 REF NP_313061 "replicative DNA helicase [Escherichia coli O157:H7 str. Sakai]" 100.00 471 98.25 100.00 1.67e-71 REF NP_418476 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.98e-72 REF NP_709868 "replicative DNA helicase [Shigella flexneri 2a str. 301]" 100.00 471 99.12 100.00 5.98e-72 REF WP_000918354 "replicative DNA helicase [Shigella dysenteriae]" 100.00 471 99.12 100.00 6.17e-72 REF WP_000918355 "MULTISPECIES: replicative DNA helicase [Escherichia]" 100.00 471 99.12 100.00 6.44e-72 SP P0ACB0 "RecName: Full=Replicative DNA helicase" 100.00 471 99.12 100.00 5.98e-72 SP P0ACB1 "RecName: Full=Replicative DNA helicase" 100.00 471 99.12 100.00 5.98e-72 SP Q8FB22 "RecName: Full=Replicative DNA helicase" 100.00 471 99.12 100.00 6.17e-72 SP Q8X5V3 "RecName: Full=Replicative DNA helicase" 100.00 471 98.25 100.00 1.67e-71 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(24-136) '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_name $DnaB(24-136) '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 $DnaB(24-136) 2.2 mM '{U-98% 15N}' 'sodium phosphate' 20 mM . EDTA 1 mM . 'sodiumn azide' 0.02 '% w/v' . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DnaB(24-136) 2.2 mM '{U-98% 13C, U-98% 15N}' 'sodium phosphate' 20 mM . EDTA 1 mM . 'sodiumn azide' 0.02 '% w/v' . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DnaB(24-136) 2.2 mM '{U-10% 13C, U-98% 15N}' 'sodium phosphate' 20 mM . EDTA 1 mM . 'sodiumn azide' 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_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 na temperature 305 1 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 _Reference_correction_type _Correction_value _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $ref_1 temperature -0.083 $ref_1 H2O H 1 protons ppm 4.683 internal direct spherical internal parallel_to_Bo 100.0 $ref_1 temperature -0.083 $ref_1 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $ref_1 temperature -0.083 $ref_1 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 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DnaB(24-136) _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 . 2 LYS CA C 56.1 0.2 1 2 . 2 LYS HA H 4.34 0.02 1 3 . 2 LYS CB C 32.9 0.2 1 4 . 2 LYS HB2 H 1.72 0.02 2 5 . 2 LYS HB3 H 1.78 0.02 2 6 . 2 LYS CG C 24.7 0.2 1 7 . 2 LYS HG2 H 1.43 0.02 2 8 . 2 LYS HG3 H 1.37 0.02 2 9 . 2 LYS CD C 28.9 0.2 1 10 . 2 LYS HD2 H 1.66 0.02 1 11 . 2 LYS HD3 H 1.66 0.02 1 12 . 2 LYS CE C 41.8 0.2 1 13 . 2 LYS HE2 H 2.96 0.02 1 14 . 2 LYS HE3 H 2.96 0.02 1 15 . 3 VAL N N 123.4 0.1 1 16 . 3 VAL H H 8.18 0.02 1 17 . 3 VAL CA C 59.5 0.2 1 18 . 3 VAL HA H 4.41 0.02 1 19 . 3 VAL CB C 33.0 0.2 1 20 . 3 VAL HB H 2.03 0.02 1 21 . 3 VAL HG1 H 0.98 0.02 1 22 . 3 VAL HG2 H 0.94 0.02 1 23 . 3 VAL CG1 C 21.0 0.2 1 24 . 3 VAL CG2 C 20.4 0.2 1 25 . 4 PRO CD C 51.1 0.2 1 26 . 4 PRO CA C 61.2 0.2 1 27 . 4 PRO HA H 4.62 0.02 1 28 . 4 PRO CB C 31.5 0.2 1 29 . 4 PRO HB2 H 1.57 0.02 2 30 . 4 PRO HB3 H 2.28 0.02 2 31 . 4 PRO CG C 27.8 0.2 1 32 . 4 PRO HG2 H 2.00 0.02 2 33 . 4 PRO HG3 H 2.09 0.02 2 34 . 4 PRO HD2 H 3.62 0.02 2 35 . 4 PRO HD3 H 3.94 0.02 2 36 . 5 PRO CD C 50.7 0.2 1 37 . 5 PRO CA C 63.4 0.2 1 38 . 5 PRO HA H 4.39 0.02 1 39 . 5 PRO CB C 31.5 0.2 1 40 . 5 PRO HB2 H 1.97 0.02 2 41 . 5 PRO HB3 H 2.16 0.02 2 42 . 5 PRO CG C 27.6 0.2 1 43 . 5 PRO HG2 H 1.93 0.02 2 44 . 5 PRO HG3 H 2.01 0.02 2 45 . 5 PRO HD2 H 3.41 0.02 2 46 . 5 PRO HD3 H 3.89 0.02 2 47 . 6 HIS N N 116.4 0.1 1 48 . 6 HIS H H 7.83 0.02 1 49 . 6 HIS CA C 55.6 0.2 1 50 . 6 HIS HA H 4.21 0.02 1 51 . 6 HIS CB C 30.7 0.2 1 52 . 6 HIS HB2 H 2.86 0.02 2 53 . 6 HIS HB3 H 2.66 0.02 2 54 . 6 HIS HD2 H 6.42 0.02 1 55 . 6 HIS HE1 H 7.45 0.02 1 56 . 7 SER CA C 56.2 0.2 1 57 . 7 SER HA H 4.71 0.02 1 58 . 7 SER CB C 62.7 0.2 1 59 . 7 SER HB2 H 3.59 0.02 2 60 . 7 SER HB3 H 3.72 0.02 2 61 . 7 SER C C 174.6 0.2 1 62 . 8 ILE N N 129.9 0.1 1 63 . 8 ILE H H 9.12 0.02 1 64 . 8 ILE CA C 64.0 0.2 1 65 . 8 ILE HA H 4.02 0.02 1 66 . 8 ILE CB C 37.0 0.2 1 67 . 8 ILE HB H 2.06 0.02 1 68 . 8 ILE HG2 H 1.02 0.02 1 69 . 8 ILE CG2 C 17.6 0.2 1 70 . 8 ILE CG1 C 28.8 0.2 1 71 . 8 ILE HG12 H 1.60 0.02 2 72 . 8 ILE HG13 H 1.71 0.02 2 73 . 8 ILE HD1 H 0.99 0.02 1 74 . 8 ILE CD1 C 12.0 0.2 1 75 . 8 ILE C C 178.0 0.2 1 76 . 9 GLU N N 120.2 0.1 1 77 . 9 GLU H H 8.90 0.02 1 78 . 9 GLU CA C 59.9 0.2 1 79 . 9 GLU HA H 4.12 0.02 1 80 . 9 GLU CB C 28.9 0.2 1 81 . 9 GLU HB2 H 1.98 0.02 2 82 . 9 GLU HB3 H 1.90 0.02 2 83 . 9 GLU CG C 36.6 0.2 1 84 . 9 GLU HG2 H 2.26 0.02 1 85 . 9 GLU HG3 H 2.26 0.02 1 86 . 9 GLU C C 179.4 0.2 1 87 . 10 ALA N N 122.9 0.1 1 88 . 10 ALA H H 8.03 0.02 1 89 . 10 ALA CA C 55.5 0.2 1 90 . 10 ALA HA H 3.81 0.02 1 91 . 10 ALA HB H 1.65 0.02 1 92 . 10 ALA CB C 18.2 0.2 1 93 . 10 ALA C C 179.1 0.2 1 94 . 11 GLU N N 116.0 0.1 1 95 . 11 GLU H H 7.91 0.02 1 96 . 11 GLU CA C 60.9 0.2 1 97 . 11 GLU HA H 3.78 0.02 1 98 . 11 GLU CB C 30.8 0.2 1 99 . 11 GLU HB2 H 2.50 0.02 2 100 . 11 GLU HB3 H 2.29 0.02 2 101 . 11 GLU CG C 38.1 0.2 1 102 . 11 GLU HG2 H 3.29 0.02 2 103 . 11 GLU HG3 H 2.29 0.02 2 104 . 11 GLU C C 178.9 0.2 1 105 . 12 GLN N N 115.2 0.1 1 106 . 12 GLN H H 8.65 0.02 1 107 . 12 GLN CA C 59.5 0.2 1 108 . 12 GLN HA H 3.56 0.02 1 109 . 12 GLN CB C 28.2 0.2 1 110 . 12 GLN HB2 H 2.31 0.02 1 111 . 12 GLN HB3 H 1.80 0.02 1 112 . 12 GLN CG C 34.9 0.2 1 113 . 12 GLN HG2 H 2.26 0.02 1 114 . 12 GLN HG3 H 3.01 0.02 1 115 . 12 GLN NE2 N 111.2 0.1 1 116 . 12 GLN HE21 H 7.17 0.02 2 117 . 12 GLN HE22 H 7.82 0.02 2 118 . 12 GLN C C 178.6 0.2 1 119 . 13 SER N N 115.0 0.1 1 120 . 13 SER H H 7.88 0.02 1 121 . 13 SER CA C 62.5 0.2 1 122 . 13 SER HA H 4.15 0.02 1 123 . 13 SER CB C 62.9 0.2 1 124 . 13 SER HB2 H 3.27 0.02 1 125 . 13 SER HB3 H 3.13 0.02 1 126 . 13 SER C C 176.9 0.2 1 127 . 14 VAL N N 121.9 0.1 1 128 . 14 VAL H H 8.00 0.02 1 129 . 14 VAL CA C 66.9 0.2 1 130 . 14 VAL HA H 3.67 0.02 1 131 . 14 VAL CB C 31.8 0.2 1 132 . 14 VAL HB H 2.28 0.02 1 133 . 14 VAL HG1 H 1.06 0.02 1 134 . 14 VAL HG2 H 1.07 0.02 1 135 . 14 VAL CG1 C 23.1 0.2 1 136 . 14 VAL CG2 C 24.0 0.2 1 137 . 14 VAL C C 176.3 0.2 1 138 . 15 LEU N N 116.4 0.1 1 139 . 15 LEU H H 7.69 0.02 1 140 . 15 LEU CA C 58.3 0.2 1 141 . 15 LEU HA H 4.05 0.02 1 142 . 15 LEU CB C 42.1 0.2 1 143 . 15 LEU HB2 H 1.74 0.02 1 144 . 15 LEU HB3 H 1.08 0.02 1 145 . 15 LEU CG C 26.3 0.2 1 146 . 15 LEU HG H 2.00 0.02 1 147 . 15 LEU HD1 H 0.45 0.02 1 148 . 15 LEU HD2 H 0.80 0.02 1 149 . 15 LEU CD1 C 25.6 0.2 1 150 . 15 LEU CD2 C 22.7 0.2 1 151 . 15 LEU C C 179.0 0.2 1 152 . 16 GLY N N 104.7 0.1 1 153 . 16 GLY H H 8.82 0.02 1 154 . 16 GLY CA C 47.4 0.2 1 155 . 16 GLY HA2 H 3.50 0.02 1 156 . 16 GLY HA3 H 3.88 0.02 1 157 . 16 GLY C C 176.5 0.2 1 158 . 17 GLY N N 108.8 0.1 1 159 . 17 GLY H H 8.06 0.02 1 160 . 17 GLY CA C 47.5 0.2 1 161 . 17 GLY HA2 H 3.76 0.02 1 162 . 17 GLY HA3 H 3.76 0.02 1 163 . 17 GLY C C 175.8 0.2 1 164 . 18 LEU N N 122.2 0.1 1 165 . 18 LEU H H 7.93 0.02 1 166 . 18 LEU CA C 56.8 0.2 1 167 . 18 LEU HA H 4.15 0.02 1 168 . 18 LEU CB C 43.2 0.2 1 169 . 18 LEU HB2 H 2.15 0.02 1 170 . 18 LEU HB3 H 1.49 0.02 1 171 . 18 LEU CG C 27.2 0.2 1 172 . 18 LEU HG H 2.07 0.02 1 173 . 18 LEU HD1 H 1.20 0.02 1 174 . 18 LEU HD2 H 0.99 0.02 1 175 . 18 LEU CD1 C 27.2 0.2 1 176 . 18 LEU CD2 C 23.4 0.2 1 177 . 18 LEU C C 178.2 0.2 1 178 . 19 MET N N 115.6 0.1 1 179 . 19 MET H H 7.29 0.02 1 180 . 19 MET CA C 58.9 0.2 1 181 . 19 MET HA H 4.21 0.02 1 182 . 19 MET CB C 33.8 0.2 1 183 . 19 MET HB2 H 2.27 0.02 1 184 . 19 MET HB3 H 1.94 0.02 1 185 . 19 MET CG C 32.6 0.2 1 186 . 19 MET HG2 H 2.66 0.02 1 187 . 19 MET HG3 H 2.66 0.02 1 188 . 19 MET HE H 1.88 0.02 1 189 . 19 MET CE C 18.0 0.2 1 190 . 19 MET C C 178.5 0.2 1 191 . 20 LEU N N 118.2 0.1 1 192 . 20 LEU H H 7.29 0.02 1 193 . 20 LEU CA C 56.4 0.2 1 194 . 20 LEU HA H 4.23 0.02 1 195 . 20 LEU CB C 42.8 0.2 1 196 . 20 LEU HB2 H 1.82 0.02 2 197 . 20 LEU HB3 H 1.73 0.02 2 198 . 20 LEU CG C 26.9 0.2 1 199 . 20 LEU HG H 1.75 0.02 1 200 . 20 LEU HD1 H 0.94 0.02 1 201 . 20 LEU HD2 H 0.90 0.02 1 202 . 20 LEU CD1 C 24.5 0.2 1 203 . 20 LEU CD2 C 24.1 0.2 1 204 . 20 LEU C C 177.1 0.2 1 205 . 21 ASP N N 119.5 0.1 1 206 . 21 ASP H H 8.11 0.02 1 207 . 21 ASP CA C 52.5 0.2 1 208 . 21 ASP HA H 4.92 0.02 1 209 . 21 ASP CB C 40.9 0.2 1 210 . 21 ASP HB2 H 2.36 0.02 1 211 . 21 ASP HB3 H 2.87 0.02 1 212 . 21 ASP C C 175.3 0.2 1 213 . 22 ASN N N 120.8 0.1 1 214 . 22 ASN H H 9.10 0.02 1 215 . 22 ASN CA C 55.1 0.2 1 216 . 22 ASN HA H 4.55 0.02 1 217 . 22 ASN CB C 38.9 0.2 1 218 . 22 ASN HB2 H 2.91 0.02 1 219 . 22 ASN HB3 H 2.91 0.02 1 220 . 22 ASN ND2 N 115.5 0.1 1 221 . 22 ASN HD21 H 6.08 0.02 2 222 . 22 ASN HD22 H 8.11 0.02 2 223 . 22 ASN C C 177.3 0.2 1 224 . 23 GLU N N 116.8 0.1 1 225 . 23 GLU H H 8.34 0.02 1 226 . 23 GLU CA C 58.1 0.2 1 227 . 23 GLU HA H 4.26 0.02 1 228 . 23 GLU CB C 29.1 0.2 1 229 . 23 GLU HB2 H 2.24 0.02 1 230 . 23 GLU HB3 H 2.24 0.02 1 231 . 23 GLU CG C 37.1 0.2 1 232 . 23 GLU HG2 H 2.37 0.02 2 233 . 23 GLU HG3 H 2.44 0.02 2 234 . 23 GLU C C 177.5 0.2 1 235 . 24 ARG N N 116.9 0.1 1 236 . 24 ARG H H 7.59 0.02 1 237 . 24 ARG CA C 55.2 0.2 1 238 . 24 ARG HA H 4.51 0.02 1 239 . 24 ARG HB2 H 1.99 0.02 1 240 . 24 ARG HB3 H 2.22 0.02 1 241 . 24 ARG CG C 25.9 0.2 1 242 . 24 ARG HG2 H 1.75 0.02 2 243 . 24 ARG HG3 H 1.79 0.02 2 244 . 24 ARG CD C 42.7 0.2 1 245 . 24 ARG HD2 H 3.24 0.02 1 246 . 24 ARG HD3 H 3.24 0.02 1 247 . 24 ARG NE N 83.6 0.1 1 248 . 24 ARG HE H 7.61 0.02 1 249 . 24 ARG C C 175.3 0.2 1 250 . 25 TRP N N 119.5 0.1 1 251 . 25 TRP H H 7.71 0.02 1 252 . 25 TRP CA C 61.5 0.2 1 253 . 25 TRP HA H 3.99 0.02 1 254 . 25 TRP CB C 29.2 0.2 1 255 . 25 TRP HB2 H 3.35 0.02 1 256 . 25 TRP HB3 H 3.12 0.02 1 257 . 25 TRP CD1 C 126.9 0.2 1 258 . 25 TRP CE3 C 119.4 0.2 1 259 . 25 TRP NE1 N 128.8 0.1 1 260 . 25 TRP HD1 H 7.04 0.02 1 261 . 25 TRP HE3 H 7.23 0.02 1 262 . 25 TRP CZ3 C 122.3 0.2 1 263 . 25 TRP CZ2 C 113.2 0.2 1 264 . 25 TRP HE1 H 9.78 0.02 1 265 . 25 TRP HZ3 H 6.41 0.02 1 266 . 25 TRP CH2 C 124.4 0.2 1 267 . 25 TRP HZ2 H 7.15 0.02 1 268 . 25 TRP HH2 H 5.89 0.02 1 269 . 25 TRP C C 176.2 0.2 1 270 . 26 ASP N N 115.7 0.1 1 271 . 26 ASP H H 8.33 0.02 1 272 . 26 ASP CA C 58.0 0.2 1 273 . 26 ASP HA H 4.05 0.02 1 274 . 26 ASP CB C 40.0 0.2 1 275 . 26 ASP HB2 H 2.67 0.02 1 276 . 26 ASP HB3 H 2.62 0.02 1 277 . 26 ASP C C 178.3 0.2 1 278 . 27 ASP N N 117.9 0.1 1 279 . 27 ASP H H 7.77 0.02 1 280 . 27 ASP CA C 56.8 0.2 1 281 . 27 ASP HA H 4.25 0.02 1 282 . 27 ASP CB C 41.4 0.2 1 283 . 27 ASP HB2 H 2.73 0.02 2 284 . 27 ASP HB3 H 2.56 0.02 2 285 . 27 ASP C C 178.2 0.2 1 286 . 28 VAL N N 118.5 0.1 1 287 . 28 VAL H H 7.59 0.02 1 288 . 28 VAL CA C 66.6 0.2 1 289 . 28 VAL HA H 3.36 0.02 1 290 . 28 VAL CB C 31.7 0.2 1 291 . 28 VAL HB H 1.87 0.02 1 292 . 28 VAL HG1 H 0.78 0.02 1 293 . 28 VAL HG2 H 0.89 0.02 1 294 . 28 VAL CG1 C 22.6 0.2 1 295 . 28 VAL CG2 C 24.0 0.2 1 296 . 28 VAL C C 177.6 0.2 1 297 . 29 ALA N N 122.0 0.1 1 298 . 29 ALA H H 8.78 0.02 1 299 . 29 ALA CA C 53.9 0.2 1 300 . 29 ALA HA H 4.04 0.02 1 301 . 29 ALA HB H 0.81 0.02 1 302 . 29 ALA CB C 17.0 0.2 1 303 . 29 ALA C C 178.8 0.2 1 304 . 30 GLU N N 114.0 0.1 1 305 . 30 GLU H H 7.18 0.02 1 306 . 30 GLU CA C 57.0 0.2 1 307 . 30 GLU HA H 4.21 0.02 1 308 . 30 GLU HB2 H 2.05 0.02 1 309 . 30 GLU HB3 H 2.05 0.02 1 310 . 30 GLU CG C 36.3 0.2 1 311 . 30 GLU HG2 H 2.31 0.02 2 312 . 30 GLU HG3 H 2.35 0.02 2 313 . 30 GLU C C 176.9 0.2 1 314 . 31 ARG N N 118.4 0.1 1 315 . 31 ARG H H 7.82 0.02 1 316 . 31 ARG CA C 57.1 0.2 1 317 . 31 ARG HA H 4.28 0.02 1 318 . 31 ARG HB2 H 1.66 0.02 2 319 . 31 ARG HB3 H 1.58 0.02 2 320 . 31 ARG C C 175.2 0.2 1 321 . 32 VAL N N 112.6 0.1 1 322 . 32 VAL H H 7.63 0.02 1 323 . 32 VAL CA C 58.9 0.2 1 324 . 32 VAL HA H 4.79 0.02 1 325 . 32 VAL CB C 36.0 0.2 1 326 . 32 VAL HB H 1.85 0.02 1 327 . 32 VAL HG1 H 0.57 0.02 1 328 . 32 VAL HG2 H 0.56 0.02 1 329 . 32 VAL CG1 C 23.2 0.2 1 330 . 32 VAL CG2 C 21.2 0.2 1 331 . 32 VAL C C 173.5 0.2 1 332 . 33 VAL N N 113.3 0.1 1 333 . 33 VAL H H 8.32 0.02 1 334 . 33 VAL CA C 58.8 0.2 1 335 . 33 VAL HA H 4.66 0.02 1 336 . 33 VAL CB C 35.0 0.2 1 337 . 33 VAL HB H 2.43 0.02 1 338 . 33 VAL HG1 H 0.95 0.02 1 339 . 33 VAL HG2 H 0.75 0.02 1 340 . 33 VAL CG1 C 21.6 0.2 1 341 . 33 VAL CG2 C 19.0 0.2 1 342 . 33 VAL C C 177.5 0.2 1 343 . 34 ALA N N 123.7 0.1 1 344 . 34 ALA H H 8.99 0.02 1 345 . 34 ALA CA C 56.4 0.2 1 346 . 34 ALA HA H 3.93 0.02 1 347 . 34 ALA HB H 1.62 0.02 1 348 . 34 ALA CB C 18.7 0.2 1 349 . 34 ALA C C 179.2 0.2 1 350 . 35 ASP N N 110.9 0.1 1 351 . 35 ASP H H 8.03 0.02 1 352 . 35 ASP CA C 56.0 0.2 1 353 . 35 ASP HA H 4.33 0.02 1 354 . 35 ASP CB C 40.6 0.2 1 355 . 35 ASP HB2 H 2.36 0.02 1 356 . 35 ASP HB3 H 2.71 0.02 1 357 . 35 ASP C C 176.1 0.2 1 358 . 36 ASP N N 117.6 0.1 1 359 . 36 ASP H H 7.94 0.02 1 360 . 36 ASP CA C 56.4 0.2 1 361 . 36 ASP HA H 4.27 0.02 1 362 . 36 ASP CB C 41.5 0.2 1 363 . 36 ASP HB2 H 2.55 0.02 1 364 . 36 ASP HB3 H 2.18 0.02 1 365 . 36 ASP C C 178.4 0.2 1 366 . 37 PHE N N 120.9 0.1 1 367 . 37 PHE H H 7.84 0.02 1 368 . 37 PHE CA C 59.5 0.2 1 369 . 37 PHE HA H 4.01 0.02 1 370 . 37 PHE CB C 38.1 0.2 1 371 . 37 PHE HB2 H 3.19 0.02 1 372 . 37 PHE HB3 H 2.90 0.02 1 373 . 37 PHE HD1 H 7.42 0.02 1 374 . 37 PHE HD2 H 7.42 0.02 1 375 . 37 PHE HE1 H 6.41 0.02 1 376 . 37 PHE HE2 H 6.41 0.02 1 377 . 37 PHE CD1 C 131.7 0.2 1 378 . 37 PHE CE1 C 130.3 0.2 1 379 . 37 PHE CZ C 128.3 0.2 1 380 . 37 PHE HZ H 6.59 0.02 1 381 . 38 TYR N N 128.9 0.1 1 382 . 38 TYR H H 11.92 0.02 1 383 . 38 TYR CA C 60.4 0.2 1 384 . 38 TYR HA H 4.21 0.02 1 385 . 38 TYR CB C 40.8 0.2 1 386 . 38 TYR HB2 H 3.06 0.02 1 387 . 38 TYR HB3 H 3.00 0.02 1 388 . 38 TYR HD1 H 6.57 0.02 1 389 . 38 TYR HD2 H 6.57 0.02 1 390 . 38 TYR HE1 H 6.44 0.02 1 391 . 38 TYR HE2 H 6.44 0.02 1 392 . 38 TYR CD1 C 132.3 0.2 1 393 . 38 TYR CE1 C 117.5 0.2 1 394 . 38 TYR C C 177.1 0.2 1 395 . 39 THR N N 108.6 0.1 1 396 . 39 THR H H 7.54 0.02 1 397 . 39 THR CA C 59.7 0.2 1 398 . 39 THR HA H 4.24 0.02 1 399 . 39 THR CB C 69.1 0.2 1 400 . 39 THR HB H 4.07 0.02 1 401 . 39 THR HG2 H 0.97 0.02 1 402 . 39 THR CG2 C 21.6 0.2 1 403 . 41 PRO CD C 49.6 0.2 1 404 . 41 PRO CA C 66.4 0.2 1 405 . 41 PRO HA H 4.24 0.02 1 406 . 41 PRO CB C 31.5 0.2 1 407 . 41 PRO HB2 H 1.55 0.02 1 408 . 41 PRO HB3 H 2.31 0.02 1 409 . 41 PRO CG C 28.2 0.2 1 410 . 41 PRO HG2 H 1.81 0.02 1 411 . 41 PRO HG3 H 1.81 0.02 1 412 . 41 PRO HD2 H 3.59 0.02 1 413 . 41 PRO HD3 H 3.59 0.02 1 414 . 41 PRO C C 178.1 0.2 1 415 . 42 HIS N N 114.1 0.1 1 416 . 42 HIS H H 7.19 0.02 1 417 . 42 HIS CA C 56.9 0.2 1 418 . 42 HIS HA H 4.33 0.02 1 419 . 42 HIS CB C 28.9 0.2 1 420 . 42 HIS HB2 H 3.57 0.02 1 421 . 42 HIS HB3 H 3.02 0.02 1 422 . 42 HIS CD2 C 123.2 0.2 1 423 . 42 HIS HD1 H 14.94 0.02 1 424 . 42 HIS CE1 C 136.5 0.2 1 425 . 42 HIS HD2 H 6.51 0.02 1 426 . 42 HIS HE1 H 7.68 0.02 1 427 . 42 HIS C C 176.7 0.2 1 428 . 43 ARG N N 119.2 0.1 1 429 . 43 ARG H H 8.02 0.02 1 430 . 43 ARG CA C 60.8 0.2 1 431 . 43 ARG HA H 3.89 0.02 1 432 . 43 ARG CB C 30.5 0.2 1 433 . 43 ARG HB2 H 1.95 0.02 2 434 . 43 ARG HB3 H 1.81 0.02 2 435 . 43 ARG CG C 27.7 0.2 1 436 . 43 ARG HG2 H 2.07 0.02 2 437 . 43 ARG HG3 H 1.80 0.02 2 438 . 43 ARG CD C 44.2 0.2 1 439 . 43 ARG HD2 H 3.02 0.02 2 440 . 43 ARG HD3 H 3.26 0.02 2 441 . 43 ARG C C 179.4 0.2 1 442 . 44 HIS N N 119.7 0.1 1 443 . 44 HIS H H 8.20 0.02 1 444 . 44 HIS CA C 59.0 0.2 1 445 . 44 HIS HA H 4.27 0.02 1 446 . 44 HIS CB C 31.2 0.2 1 447 . 44 HIS HB2 H 3.06 0.02 2 448 . 44 HIS HB3 H 3.14 0.02 2 449 . 44 HIS CD2 C 118.9 0.2 1 450 . 44 HIS HD2 H 6.70 0.02 1 451 . 44 HIS C C 178.9 0.2 1 452 . 45 ILE N N 120.2 0.1 1 453 . 45 ILE H H 8.65 0.02 1 454 . 45 ILE CA C 66.8 0.2 1 455 . 45 ILE HA H 3.46 0.02 1 456 . 45 ILE CB C 38.3 0.2 1 457 . 45 ILE HB H 1.88 0.02 1 458 . 45 ILE HG2 H 0.96 0.02 1 459 . 45 ILE CG2 C 18.6 0.2 1 460 . 45 ILE CG1 C 30.4 0.2 1 461 . 45 ILE HG12 H 0.70 0.02 1 462 . 45 ILE HG13 H 2.25 0.02 1 463 . 45 ILE HD1 H 0.96 0.02 1 464 . 45 ILE CD1 C 14.7 0.2 1 465 . 45 ILE C C 176.7 0.2 1 466 . 46 PHE N N 120.1 0.1 1 467 . 46 PHE H H 8.42 0.02 1 468 . 46 PHE CA C 62.7 0.2 1 469 . 46 PHE HA H 4.01 0.02 1 470 . 46 PHE CB C 39.4 0.2 1 471 . 46 PHE HB2 H 2.44 0.02 1 472 . 46 PHE HB3 H 2.68 0.02 1 473 . 46 PHE HD1 H 6.89 0.02 1 474 . 46 PHE HD2 H 6.89 0.02 1 475 . 46 PHE HE1 H 7.06 0.02 1 476 . 46 PHE HE2 H 7.06 0.02 1 477 . 46 PHE CD1 C 131.4 0.2 1 478 . 46 PHE CE1 C 130.8 0.2 1 479 . 46 PHE CZ C 130.7 0.2 1 480 . 46 PHE HZ H 6.73 0.02 1 481 . 46 PHE C C 177.0 0.2 1 482 . 47 THR N N 113.6 0.1 1 483 . 47 THR H H 8.21 0.02 1 484 . 47 THR CA C 67.1 0.2 1 485 . 47 THR HA H 3.93 0.02 1 486 . 47 THR CB C 68.8 0.2 1 487 . 47 THR HB H 4.32 0.02 1 488 . 47 THR HG2 H 1.24 0.02 1 489 . 47 THR CG2 C 21.0 0.2 1 490 . 47 THR C C 176.3 0.2 1 491 . 48 GLU N N 123.5 0.1 1 492 . 48 GLU H H 7.92 0.02 1 493 . 48 GLU CA C 58.1 0.2 1 494 . 48 GLU HA H 4.33 0.02 1 495 . 48 GLU CB C 28.3 0.2 1 496 . 48 GLU HB2 H 1.98 0.02 1 497 . 48 GLU HB3 H 1.81 0.02 1 498 . 48 GLU CG C 34.7 0.2 1 499 . 48 GLU HG2 H 2.07 0.02 1 500 . 48 GLU HG3 H 2.07 0.02 1 501 . 48 GLU C C 178.2 0.2 1 502 . 49 MET N N 119.6 0.1 1 503 . 49 MET H H 8.48 0.02 1 504 . 49 MET CA C 60.3 0.2 1 505 . 49 MET HA H 3.58 0.02 1 506 . 49 MET HB2 H 2.04 0.02 1 507 . 49 MET HB3 H 1.63 0.02 1 508 . 49 MET CG C 35.2 0.2 1 509 . 49 MET HG2 H 3.05 0.02 2 510 . 49 MET HG3 H 2.01 0.02 2 511 . 49 MET HE H 2.13 0.02 1 512 . 49 MET CE C 19.2 0.2 1 513 . 49 MET C C 176.7 0.2 1 514 . 50 ALA N N 119.9 0.1 1 515 . 50 ALA H H 7.95 0.02 1 516 . 50 ALA CA C 54.9 0.2 1 517 . 50 ALA HA H 3.34 0.02 1 518 . 50 ALA HB H 1.49 0.02 1 519 . 50 ALA CB C 17.6 0.2 1 520 . 50 ALA C C 180.2 0.2 1 521 . 51 ARG N N 120.4 0.1 1 522 . 51 ARG H H 7.71 0.02 1 523 . 51 ARG CA C 59.2 0.2 1 524 . 51 ARG HA H 3.88 0.02 1 525 . 51 ARG CB C 30.5 0.2 1 526 . 51 ARG HB2 H 1.83 0.02 1 527 . 51 ARG HB3 H 1.83 0.02 1 528 . 51 ARG CG C 27.2 0.2 1 529 . 51 ARG HG2 H 1.46 0.02 2 530 . 51 ARG HG3 H 1.67 0.02 2 531 . 51 ARG CD C 42.8 0.2 1 532 . 51 ARG HD2 H 3.02 0.02 2 533 . 51 ARG HD3 H 3.23 0.02 2 534 . 51 ARG C C 180.2 0.2 1 535 . 52 LEU N N 122.3 0.1 1 536 . 52 LEU H H 8.40 0.02 1 537 . 52 LEU CA C 57.9 0.2 1 538 . 52 LEU HA H 3.75 0.02 1 539 . 52 LEU CB C 40.9 0.2 1 540 . 52 LEU HB2 H 1.71 0.02 1 541 . 52 LEU HB3 H 1.03 0.02 1 542 . 52 LEU CG C 27.2 0.2 1 543 . 52 LEU HG H 1.74 0.02 1 544 . 52 LEU HD1 H 0.84 0.02 1 545 . 52 LEU HD2 H 0.74 0.02 1 546 . 52 LEU CD1 C 26.0 0.2 1 547 . 52 LEU CD2 C 21.9 0.2 1 548 . 52 LEU C C 179.7 0.2 1 549 . 53 GLN N N 120.5 0.1 1 550 . 53 GLN H H 8.38 0.02 1 551 . 53 GLN CA C 59.1 0.2 1 552 . 53 GLN HA H 3.73 0.02 1 553 . 53 GLN CB C 26.4 0.2 1 554 . 53 GLN HB2 H 1.33 0.02 2 555 . 53 GLN HB3 H 1.24 0.02 2 556 . 53 GLN CG C 32.3 0.2 1 557 . 53 GLN HG2 H 1.29 0.02 1 558 . 53 GLN HG3 H 1.01 0.02 1 559 . 53 GLN NE2 N 110.1 0.1 1 560 . 53 GLN HE21 H 6.51 0.02 2 561 . 53 GLN HE22 H 6.62 0.02 2 562 . 53 GLN C C 180.4 0.2 1 563 . 54 GLU N N 120.8 0.1 1 564 . 54 GLU H H 7.89 0.02 1 565 . 54 GLU CA C 58.9 0.2 1 566 . 54 GLU HA H 3.91 0.02 1 567 . 54 GLU CB C 29.2 0.2 1 568 . 54 GLU HB2 H 2.13 0.02 1 569 . 54 GLU HB3 H 2.05 0.02 1 570 . 54 GLU CG C 36.1 0.2 1 571 . 54 GLU HG2 H 2.32 0.02 1 572 . 54 GLU HG3 H 2.32 0.02 1 573 . 54 GLU C C 177.6 0.2 1 574 . 55 SER N N 112.0 0.1 1 575 . 55 SER H H 7.42 0.02 1 576 . 55 SER CA C 58.4 0.2 1 577 . 55 SER HA H 4.49 0.02 1 578 . 55 SER CB C 64.1 0.2 1 579 . 55 SER HB2 H 4.04 0.02 2 580 . 55 SER HB3 H 3.91 0.02 2 581 . 55 SER C C 174.5 0.2 1 582 . 56 GLY N N 110.1 0.1 1 583 . 56 GLY H H 7.77 0.02 1 584 . 56 GLY CA C 45.8 0.2 1 585 . 56 GLY HA2 H 3.77 0.02 1 586 . 56 GLY HA3 H 4.10 0.02 1 587 . 56 GLY C C 174.6 0.2 1 588 . 57 SER N N 117.2 0.1 1 589 . 57 SER H H 7.84 0.02 1 590 . 57 SER CA C 56.0 0.2 1 591 . 57 SER HA H 4.82 0.02 1 592 . 57 SER CB C 64.2 0.2 1 593 . 57 SER HB2 H 3.50 0.02 1 594 . 57 SER HB3 H 3.67 0.02 1 595 . 58 PRO CD C 50.8 0.2 1 596 . 58 PRO CA C 62.8 0.2 1 597 . 58 PRO HA H 4.43 0.02 1 598 . 58 PRO CB C 32.8 0.2 1 599 . 58 PRO HB2 H 2.20 0.02 1 600 . 58 PRO HB3 H 2.41 0.02 1 601 . 58 PRO CG C 27.2 0.2 1 602 . 58 PRO HG2 H 1.99 0.02 2 603 . 58 PRO HG3 H 2.09 0.02 2 604 . 58 PRO HD2 H 3.80 0.02 2 605 . 58 PRO HD3 H 3.70 0.02 2 606 . 58 PRO C C 174.5 0.2 1 607 . 59 ILE N N 109.0 0.1 1 608 . 59 ILE H H 7.06 0.02 1 609 . 59 ILE CA C 60.1 0.2 1 610 . 59 ILE HA H 4.33 0.02 1 611 . 59 ILE CB C 38.1 0.2 1 612 . 59 ILE HB H 2.06 0.02 1 613 . 59 ILE HG2 H 0.67 0.02 1 614 . 59 ILE CG2 C 19.3 0.2 1 615 . 59 ILE CG1 C 25.0 0.2 1 616 . 59 ILE HG12 H 1.47 0.02 2 617 . 59 ILE HG13 H 0.65 0.02 2 618 . 59 ILE HD1 H 0.88 0.02 1 619 . 59 ILE CD1 C 15.5 0.2 1 620 . 59 ILE C C 173.3 0.2 1 621 . 60 ASP N N 114.1 0.1 1 622 . 60 ASP H H 7.41 0.02 1 623 . 60 ASP CA C 52.8 0.2 1 624 . 60 ASP HA H 4.81 0.02 1 625 . 60 ASP CB C 42.3 0.2 1 626 . 60 ASP HB2 H 3.01 0.02 2 627 . 60 ASP HB3 H 2.83 0.02 2 628 . 60 ASP C C 173.5 0.2 1 629 . 61 LEU N N 118.4 0.1 1 630 . 61 LEU H H 8.37 0.02 1 631 . 61 LEU CA C 59.2 0.2 1 632 . 61 LEU HA H 3.94 0.02 1 633 . 61 LEU CB C 42.8 0.2 1 634 . 61 LEU HB2 H 1.62 0.02 1 635 . 61 LEU HB3 H 1.73 0.02 1 636 . 61 LEU CG C 27.6 0.2 1 637 . 61 LEU HG H 1.41 0.02 1 638 . 61 LEU HD1 H 0.83 0.02 1 639 . 61 LEU HD2 H 0.52 0.02 1 640 . 61 LEU CD1 C 25.7 0.2 1 641 . 61 LEU CD2 C 24.1 0.2 1 642 . 61 LEU C C 176.9 0.2 1 643 . 62 ILE N N 115.4 0.1 1 644 . 62 ILE H H 7.59 0.02 1 645 . 62 ILE CA C 64.0 0.2 1 646 . 62 ILE HA H 3.79 0.02 1 647 . 62 ILE CB C 36.5 0.2 1 648 . 62 ILE HB H 2.03 0.02 1 649 . 62 ILE HG2 H 0.91 0.02 1 650 . 62 ILE CG2 C 17.3 0.2 1 651 . 62 ILE CG1 C 28.4 0.2 1 652 . 62 ILE HG12 H 1.64 0.02 2 653 . 62 ILE HG13 H 1.41 0.02 2 654 . 62 ILE HD1 H 0.92 0.02 1 655 . 62 ILE CD1 C 11.4 0.2 1 656 . 62 ILE C C 178.2 0.2 1 657 . 63 THR N N 119.2 0.1 1 658 . 63 THR H H 7.95 0.02 1 659 . 63 THR CA C 66.9 0.2 1 660 . 63 THR HA H 3.77 0.02 1 661 . 63 THR CB C 67.7 0.2 1 662 . 63 THR HB H 3.71 0.02 1 663 . 63 THR HG2 H 1.16 0.02 1 664 . 63 THR CG2 C 22.6 0.2 1 665 . 63 THR C C 177.8 0.2 1 666 . 64 LEU N N 122.2 0.1 1 667 . 64 LEU H H 8.58 0.02 1 668 . 64 LEU CA C 58.0 0.2 1 669 . 64 LEU HA H 3.86 0.02 1 670 . 64 LEU CB C 42.9 0.2 1 671 . 64 LEU HB2 H 1.28 0.02 1 672 . 64 LEU HB3 H 1.72 0.02 1 673 . 64 LEU HG H 1.40 0.02 1 674 . 64 LEU HD1 H 0.78 0.02 1 675 . 64 LEU HD2 H 0.84 0.02 1 676 . 64 LEU CD1 C 24.4 0.2 1 677 . 64 LEU CD2 C 27.3 0.2 1 678 . 64 LEU C C 177.9 0.2 1 679 . 65 ALA N N 120.3 0.1 1 680 . 65 ALA H H 8.59 0.02 1 681 . 65 ALA CA C 55.8 0.2 1 682 . 65 ALA HA H 3.79 0.02 1 683 . 65 ALA HB H 1.44 0.02 1 684 . 65 ALA CB C 18.7 0.2 1 685 . 65 ALA C C 179.6 0.2 1 686 . 66 GLU N N 116.9 0.1 1 687 . 66 GLU H H 8.43 0.02 1 688 . 66 GLU CA C 60.0 0.2 1 689 . 66 GLU HA H 3.99 0.02 1 690 . 66 GLU CB C 29.3 0.2 1 691 . 66 GLU HB2 H 2.18 0.02 1 692 . 66 GLU HB3 H 2.06 0.02 1 693 . 66 GLU CG C 36.9 0.2 1 694 . 66 GLU HG2 H 2.18 0.02 2 695 . 66 GLU HG3 H 2.52 0.02 2 696 . 66 GLU C C 178.9 0.2 1 697 . 67 SER N N 114.3 0.1 1 698 . 67 SER H H 8.02 0.02 1 699 . 67 SER CA C 61.3 0.2 1 700 . 67 SER HA H 4.12 0.02 1 701 . 67 SER CB C 63.2 0.2 1 702 . 67 SER HB2 H 3.94 0.02 1 703 . 67 SER HB3 H 4.08 0.02 1 704 . 67 SER C C 178.9 0.2 1 705 . 68 LEU N N 118.6 0.1 1 706 . 68 LEU H H 8.43 0.02 1 707 . 68 LEU CA C 58.0 0.2 1 708 . 68 LEU HA H 3.89 0.02 1 709 . 68 LEU CB C 42.1 0.2 1 710 . 68 LEU HB2 H 1.97 0.02 1 711 . 68 LEU HB3 H 0.82 0.02 1 712 . 68 LEU HG H 1.76 0.02 1 713 . 68 LEU HD1 H 0.79 0.02 1 714 . 68 LEU HD2 H 0.71 0.02 1 715 . 68 LEU CD1 C 27.4 0.2 1 716 . 68 LEU CD2 C 23.2 0.2 1 717 . 68 LEU C C 179.5 0.2 1 718 . 69 GLU N N 122.3 0.1 1 719 . 69 GLU H H 8.82 0.02 1 720 . 69 GLU CA C 59.8 0.2 1 721 . 69 GLU HA H 4.14 0.02 1 722 . 69 GLU CB C 28.9 0.2 1 723 . 69 GLU HB2 H 1.90 0.02 2 724 . 69 GLU HB3 H 1.97 0.02 2 725 . 69 GLU CG C 36.5 0.2 1 726 . 69 GLU HG2 H 2.24 0.02 1 727 . 69 GLU HG3 H 2.24 0.02 1 728 . 69 GLU C C 180.6 0.2 1 729 . 70 ARG N N 121.8 0.1 1 730 . 70 ARG H H 8.43 0.02 1 731 . 70 ARG CA C 59.5 0.2 1 732 . 70 ARG HA H 4.13 0.02 1 733 . 70 ARG CB C 29.9 0.2 1 734 . 70 ARG HB2 H 1.99 0.02 2 735 . 70 ARG HB3 H 2.08 0.02 2 736 . 70 ARG CG C 27.7 0.2 1 737 . 70 ARG HG2 H 1.76 0.02 2 738 . 70 ARG HG3 H 1.83 0.02 2 739 . 70 ARG CD C 43.3 0.2 1 740 . 70 ARG HD2 H 3.24 0.02 1 741 . 70 ARG HD3 H 3.24 0.02 1 742 . 70 ARG C C 178.2 0.2 1 743 . 71 GLN N N 114.3 0.1 1 744 . 71 GLN H H 7.35 0.02 1 745 . 71 GLN CA C 55.6 0.2 1 746 . 71 GLN HA H 4.37 0.02 1 747 . 71 GLN CB C 31.2 0.2 1 748 . 71 GLN HB2 H 1.83 0.02 1 749 . 71 GLN HB3 H 2.42 0.02 1 750 . 71 GLN CG C 34.9 0.2 1 751 . 71 GLN HG2 H 2.25 0.02 2 752 . 71 GLN HG3 H 2.54 0.02 2 753 . 71 GLN NE2 N 112.1 0.1 1 754 . 71 GLN HE21 H 6.99 0.02 2 755 . 71 GLN HE22 H 6.80 0.02 2 756 . 71 GLN C C 176.2 0.2 1 757 . 72 GLY N N 109.6 0.1 1 758 . 72 GLY H H 8.16 0.02 1 759 . 72 GLY CA C 46.5 0.2 1 760 . 72 GLY HA2 H 4.08 0.02 1 761 . 72 GLY HA3 H 4.08 0.02 1 762 . 72 GLY C C 176.1 0.2 1 763 . 73 GLN N N 115.4 0.1 1 764 . 73 GLN H H 8.18 0.02 1 765 . 73 GLN CA C 55.0 0.2 1 766 . 73 GLN HA H 4.62 0.02 1 767 . 73 GLN CB C 31.5 0.2 1 768 . 73 GLN HB2 H 1.54 0.02 1 769 . 73 GLN HB3 H 2.28 0.02 1 770 . 73 GLN CG C 32.7 0.2 1 771 . 73 GLN HG2 H 2.27 0.02 2 772 . 73 GLN HG3 H 2.20 0.02 2 773 . 73 GLN NE2 N 110.1 0.1 1 774 . 73 GLN HE21 H 6.52 0.02 2 775 . 73 GLN HE22 H 7.13 0.02 2 776 . 73 GLN C C 176.4 0.2 1 777 . 74 LEU N N 122.9 0.1 1 778 . 74 LEU H H 7.72 0.02 1 779 . 74 LEU CA C 58.1 0.2 1 780 . 74 LEU HA H 3.97 0.02 1 781 . 74 LEU CB C 41.0 0.2 1 782 . 74 LEU HB2 H 1.19 0.02 1 783 . 74 LEU HB3 H 2.00 0.02 1 784 . 74 LEU CG C 27.6 0.2 1 785 . 74 LEU HG H 1.59 0.02 1 786 . 74 LEU HD1 H 0.86 0.02 1 787 . 74 LEU HD2 H 1.02 0.02 1 788 . 74 LEU CD1 C 23.3 0.2 1 789 . 74 LEU CD2 C 25.9 0.2 1 790 . 74 LEU C C 178.9 0.2 1 791 . 75 ASP N N 118.8 0.1 1 792 . 75 ASP H H 8.54 0.02 1 793 . 75 ASP CA C 57.5 0.2 1 794 . 75 ASP HA H 4.29 0.02 1 795 . 75 ASP CB C 39.7 0.2 1 796 . 75 ASP HB2 H 2.61 0.02 1 797 . 75 ASP HB3 H 2.61 0.02 1 798 . 75 ASP C C 179.8 0.2 1 799 . 76 SER N N 115.3 0.1 1 800 . 76 SER H H 7.80 0.02 1 801 . 76 SER CA C 61.0 0.2 1 802 . 76 SER HA H 4.22 0.02 1 803 . 76 SER CB C 63.1 0.2 1 804 . 76 SER HB2 H 3.85 0.02 1 805 . 76 SER HB3 H 3.85 0.02 1 806 . 76 SER C C 175.7 0.2 1 807 . 77 VAL N N 111.2 0.1 1 808 . 77 VAL H H 7.11 0.02 1 809 . 77 VAL CA C 60.4 0.2 1 810 . 77 VAL HA H 4.46 0.02 1 811 . 77 VAL CB C 31.3 0.2 1 812 . 77 VAL HB H 2.60 0.02 1 813 . 77 VAL HG1 H 0.88 0.02 1 814 . 77 VAL HG2 H 1.02 0.02 1 815 . 77 VAL CG1 C 22.1 0.2 1 816 . 77 VAL CG2 C 19.1 0.2 1 817 . 77 VAL C C 173.5 0.2 1 818 . 78 GLY N N 105.1 0.1 1 819 . 78 GLY H H 7.39 0.02 1 820 . 78 GLY CA C 44.4 0.2 1 821 . 78 GLY HA2 H 4.35 0.02 2 822 . 78 GLY HA3 H 3.55 0.02 2 823 . 79 GLY N N 107.6 0.1 1 824 . 79 GLY H H 7.94 0.02 1 825 . 79 GLY CA C 44.3 0.2 1 826 . 79 GLY HA2 H 4.43 0.02 2 827 . 79 GLY HA3 H 3.68 0.02 2 828 . 80 PHE CA C 62.5 0.2 1 829 . 80 PHE HA H 3.73 0.02 1 830 . 80 PHE HB2 H 3.02 0.02 1 831 . 80 PHE HB3 H 2.87 0.02 1 832 . 80 PHE HE1 H 7.11 0.02 1 833 . 80 PHE HE2 H 7.11 0.02 1 834 . 80 PHE CE1 C 131.2 0.2 1 835 . 80 PHE CZ C 129.5 0.2 1 836 . 80 PHE HZ H 7.12 0.02 1 837 . 81 ALA CA C 55.2 0.2 1 838 . 81 ALA HA H 3.92 0.02 1 839 . 81 ALA HB H 1.51 0.02 1 840 . 81 ALA CB C 18.4 0.2 1 841 . 81 ALA C C 180.1 0.2 1 842 . 82 TYR N N 117.4 0.1 1 843 . 82 TYR H H 7.14 0.02 1 844 . 82 TYR CA C 61.4 0.2 1 845 . 82 TYR HA H 4.37 0.02 1 846 . 82 TYR CB C 38.6 0.2 1 847 . 82 TYR HB2 H 3.17 0.02 1 848 . 82 TYR HB3 H 2.80 0.02 1 849 . 82 TYR HD1 H 7.20 0.02 1 850 . 82 TYR HD2 H 7.20 0.02 1 851 . 82 TYR HE1 H 6.70 0.02 1 852 . 82 TYR HE2 H 6.70 0.02 1 853 . 82 TYR CD1 C 133.5 0.2 1 854 . 82 TYR CE1 C 117.4 0.2 1 855 . 82 TYR C C 177.1 0.2 1 856 . 83 LEU N N 116.8 0.1 1 857 . 83 LEU H H 7.02 0.02 1 858 . 83 LEU CA C 57.9 0.2 1 859 . 83 LEU HA H 3.55 0.02 1 860 . 83 LEU CB C 41.1 0.2 1 861 . 83 LEU HB2 H 1.51 0.02 1 862 . 83 LEU HB3 H 1.05 0.02 1 863 . 83 LEU CG C 26.2 0.2 1 864 . 83 LEU HG H 1.69 0.02 1 865 . 83 LEU HD1 H 0.68 0.02 1 866 . 83 LEU HD2 H 0.67 0.02 1 867 . 83 LEU CD1 C 26.2 0.2 1 868 . 83 LEU CD2 C 22.7 0.2 1 869 . 83 LEU C C 178.5 0.2 1 870 . 84 ALA N N 119.2 0.1 1 871 . 84 ALA H H 8.42 0.02 1 872 . 84 ALA CA C 54.4 0.2 1 873 . 84 ALA HA H 3.65 0.02 1 874 . 84 ALA HB H 1.03 0.02 1 875 . 84 ALA CB C 17.2 0.2 1 876 . 84 ALA C C 180.5 0.2 1 877 . 85 GLU N N 121.3 0.1 1 878 . 85 GLU H H 7.68 0.02 1 879 . 85 GLU CA C 59.4 0.2 1 880 . 85 GLU HA H 3.80 0.02 1 881 . 85 GLU CB C 28.8 0.2 1 882 . 85 GLU HB2 H 2.08 0.02 1 883 . 85 GLU HB3 H 2.01 0.02 1 884 . 85 GLU CG C 35.8 0.2 1 885 . 85 GLU HG2 H 2.14 0.02 2 886 . 85 GLU HG3 H 2.20 0.02 2 887 . 85 GLU C C 179.0 0.2 1 888 . 86 LEU N N 118.6 0.1 1 889 . 86 LEU H H 7.77 0.02 1 890 . 86 LEU CA C 57.6 0.2 1 891 . 86 LEU HA H 3.68 0.02 1 892 . 86 LEU CB C 41.7 0.2 1 893 . 86 LEU HB2 H 1.88 0.02 1 894 . 86 LEU HB3 H 0.89 0.02 1 895 . 86 LEU CG C 25.7 0.2 1 896 . 86 LEU HG H 1.32 0.02 1 897 . 86 LEU HD1 H 0.62 0.02 1 898 . 86 LEU HD2 H 0.68 0.02 1 899 . 86 LEU CD1 C 26.2 0.2 1 900 . 86 LEU CD2 C 23.2 0.2 1 901 . 86 LEU C C 179.4 0.2 1 902 . 87 SER N N 111.8 0.1 1 903 . 87 SER H H 7.54 0.02 1 904 . 87 SER CA C 60.5 0.2 1 905 . 87 SER HA H 4.19 0.02 1 906 . 87 SER CB C 63.3 0.2 1 907 . 87 SER HB2 H 3.95 0.02 1 908 . 87 SER HB3 H 3.95 0.02 1 909 . 87 SER C C 175.5 0.2 1 910 . 88 LYS N N 120.3 0.1 1 911 . 88 LYS H H 7.68 0.02 1 912 . 88 LYS CA C 57.7 0.2 1 913 . 88 LYS HA H 4.10 0.02 1 914 . 88 LYS CB C 32.6 0.2 1 915 . 88 LYS HB2 H 1.79 0.02 1 916 . 88 LYS HB3 H 1.79 0.02 1 917 . 88 LYS CG C 24.9 0.2 1 918 . 88 LYS HG2 H 1.49 0.02 2 919 . 88 LYS HG3 H 1.41 0.02 2 920 . 88 LYS CD C 28.9 0.2 1 921 . 88 LYS HD2 H 1.59 0.02 1 922 . 88 LYS HD3 H 1.59 0.02 1 923 . 88 LYS CE C 41.7 0.2 1 924 . 88 LYS HE2 H 2.84 0.02 1 925 . 88 LYS HE3 H 2.84 0.02 1 926 . 88 LYS C C 177.6 0.2 1 927 . 89 ASN N N 116.7 0.1 1 928 . 89 ASN H H 7.75 0.02 1 929 . 89 ASN CA C 53.4 0.2 1 930 . 89 ASN HA H 4.65 0.02 1 931 . 89 ASN CB C 39.1 0.2 1 932 . 89 ASN HB2 H 2.75 0.02 1 933 . 89 ASN HB3 H 2.75 0.02 1 934 . 89 ASN ND2 N 113.3 0.1 1 935 . 89 ASN HD21 H 7.43 0.02 1 936 . 89 ASN HD22 H 6.98 0.02 1 937 . 89 ASN C C 174.1 0.2 1 938 . 90 THR N N 114.7 0.1 1 939 . 90 THR H H 7.48 0.02 1 940 . 90 THR CA C 59.5 0.2 1 941 . 90 THR HA H 4.55 0.02 1 942 . 90 THR CB C 69.5 0.2 1 943 . 90 THR HB H 4.06 0.02 1 944 . 90 THR HG2 H 1.12 0.02 1 945 . 90 THR CG2 C 20.9 0.2 1 946 . 91 PRO CD C 50.9 0.2 1 947 . 91 PRO CA C 63.2 0.2 1 948 . 91 PRO HA H 4.53 0.02 1 949 . 91 PRO CB C 32.2 0.2 1 950 . 91 PRO HB2 H 2.00 0.02 2 951 . 91 PRO HB3 H 2.30 0.02 2 952 . 91 PRO CG C 27.3 0.2 1 953 . 91 PRO HG2 H 1.98 0.02 1 954 . 91 PRO HG3 H 1.98 0.02 1 955 . 91 PRO HD2 H 3.70 0.02 1 956 . 91 PRO HD3 H 3.70 0.02 1 957 . 91 PRO C C 176.5 0.2 1 958 . 92 SER N N 113.3 0.1 1 959 . 92 SER H H 7.96 0.02 1 960 . 92 SER CA C 57.7 0.2 1 961 . 92 SER HA H 4.42 0.02 1 962 . 92 SER CB C 64.2 0.2 1 963 . 92 SER HB2 H 4.03 0.02 2 964 . 92 SER HB3 H 3.84 0.02 2 965 . 92 SER C C 174.3 0.2 1 966 . 93 ALA N N 125.6 0.1 1 967 . 93 ALA H H 8.81 0.02 1 968 . 93 ALA CA C 53.0 0.2 1 969 . 93 ALA HA H 4.40 0.02 1 970 . 93 ALA HB H 1.47 0.02 1 971 . 93 ALA CB C 18.7 0.2 1 972 . 93 ALA C C 177.9 0.2 1 973 . 94 ALA N N 120.5 0.1 1 974 . 94 ALA H H 8.10 0.02 1 975 . 94 ALA CA C 54.1 0.2 1 976 . 94 ALA HA H 4.11 0.02 1 977 . 94 ALA HB H 1.34 0.02 1 978 . 94 ALA CB C 18.7 0.2 1 979 . 94 ALA C C 178.8 0.2 1 980 . 95 ASN N N 116.2 0.1 1 981 . 95 ASN H H 8.28 0.02 1 982 . 95 ASN CA C 52.9 0.2 1 983 . 95 ASN HA H 4.80 0.02 1 984 . 95 ASN CB C 38.4 0.2 1 985 . 95 ASN HB2 H 2.67 0.02 2 986 . 95 ASN HB3 H 2.74 0.02 2 987 . 95 ASN ND2 N 111.9 0.1 1 988 . 95 ASN HD21 H 7.36 0.02 2 989 . 95 ASN HD22 H 6.85 0.02 2 990 . 95 ASN C C 176.1 0.2 1 991 . 96 ILE N N 121.0 0.1 1 992 . 96 ILE H H 7.99 0.02 1 993 . 96 ILE CA C 66.1 0.2 1 994 . 96 ILE HA H 3.91 0.02 1 995 . 96 ILE CB C 38.0 0.2 1 996 . 96 ILE HB H 2.06 0.02 1 997 . 96 ILE HG2 H 0.98 0.02 1 998 . 96 ILE CG2 C 17.3 0.2 1 999 . 96 ILE CG1 C 29.4 0.2 1 1000 . 96 ILE HG12 H 1.22 0.02 2 1001 . 96 ILE HG13 H 1.68 0.02 2 1002 . 96 ILE HD1 H 0.98 0.02 1 1003 . 96 ILE CD1 C 14.3 0.2 1 1004 . 96 ILE C C 176.8 0.2 1 1005 . 97 SER N N 117.4 0.1 1 1006 . 97 SER H H 8.14 0.02 1 1007 . 97 SER CA C 62.4 0.2 1 1008 . 97 SER HA H 3.81 0.02 1 1009 . 97 SER CB C 62.3 0.2 1 1010 . 97 SER HB2 H 3.73 0.02 2 1011 . 97 SER HB3 H 3.67 0.02 2 1012 . 97 SER C C 174.8 0.2 1 1013 . 98 ALA N N 123.2 0.1 1 1014 . 98 ALA H H 7.21 0.02 1 1015 . 98 ALA CA C 54.6 0.2 1 1016 . 98 ALA HA H 4.12 0.02 1 1017 . 98 ALA HB H 1.24 0.02 1 1018 . 98 ALA CB C 17.7 0.2 1 1019 . 98 ALA C C 181.4 0.2 1 1020 . 99 TYR N N 116.9 0.1 1 1021 . 99 TYR H H 7.70 0.02 1 1022 . 99 TYR CA C 60.8 0.2 1 1023 . 99 TYR HA H 4.39 0.02 1 1024 . 99 TYR CB C 37.6 0.2 1 1025 . 99 TYR HB2 H 2.85 0.02 1 1026 . 99 TYR HB3 H 3.26 0.02 1 1027 . 99 TYR HD1 H 6.96 0.02 1 1028 . 99 TYR HD2 H 6.96 0.02 1 1029 . 99 TYR HE1 H 6.80 0.02 1 1030 . 99 TYR HE2 H 6.80 0.02 1 1031 . 99 TYR CD1 C 132.2 0.2 1 1032 . 99 TYR CE1 C 118.4 0.2 1 1033 . 99 TYR C C 177.8 0.2 1 1034 . 100 ALA N N 122.9 0.1 1 1035 . 100 ALA H H 8.29 0.02 1 1036 . 100 ALA CA C 55.6 0.2 1 1037 . 100 ALA HA H 3.73 0.02 1 1038 . 100 ALA HB H 1.44 0.02 1 1039 . 100 ALA CB C 18.0 0.2 1 1040 . 100 ALA C C 177.9 0.2 1 1041 . 101 ASP N N 117.2 0.1 1 1042 . 101 ASP H H 8.00 0.02 1 1043 . 101 ASP CA C 57.5 0.2 1 1044 . 101 ASP HA H 4.37 0.02 1 1045 . 101 ASP CB C 39.9 0.2 1 1046 . 101 ASP HB2 H 2.86 0.02 1 1047 . 101 ASP HB3 H 2.60 0.02 1 1048 . 101 ASP C C 179.1 0.2 1 1049 . 102 ILE N N 121.2 0.1 1 1050 . 102 ILE H H 7.42 0.02 1 1051 . 102 ILE CA C 65.3 0.2 1 1052 . 102 ILE HA H 3.76 0.02 1 1053 . 102 ILE CB C 37.8 0.2 1 1054 . 102 ILE HB H 2.12 0.02 1 1055 . 102 ILE HG2 H 0.86 0.02 1 1056 . 102 ILE CG2 C 17.1 0.2 1 1057 . 102 ILE CG1 C 29.0 0.2 1 1058 . 102 ILE HG12 H 1.07 0.02 1 1059 . 102 ILE HG13 H 1.79 0.02 1 1060 . 102 ILE HD1 H 0.83 0.02 1 1061 . 102 ILE CD1 C 13.3 0.2 1 1062 . 102 ILE C C 177.4 0.2 1 1063 . 103 VAL N N 120.4 0.1 1 1064 . 103 VAL H H 7.75 0.02 1 1065 . 103 VAL CA C 67.0 0.2 1 1066 . 103 VAL HA H 3.39 0.02 1 1067 . 103 VAL CB C 31.3 0.2 1 1068 . 103 VAL HB H 1.99 0.02 1 1069 . 103 VAL HG1 H 0.03 0.02 1 1070 . 103 VAL HG2 H 0.88 0.02 1 1071 . 103 VAL CG1 C 20.4 0.2 1 1072 . 103 VAL CG2 C 23.2 0.2 1 1073 . 103 VAL C C 179.7 0.2 1 1074 . 104 ARG N N 120.9 0.1 1 1075 . 104 ARG H H 8.05 0.02 1 1076 . 104 ARG CA C 59.3 0.2 1 1077 . 104 ARG HA H 3.81 0.02 1 1078 . 104 ARG CB C 28.9 0.2 1 1079 . 104 ARG HB2 H 2.12 0.02 1 1080 . 104 ARG HB3 H 1.94 0.02 1 1081 . 104 ARG HG2 H 1.57 0.02 2 1082 . 104 ARG HG3 H 1.68 0.02 2 1083 . 104 ARG CD C 42.2 0.2 1 1084 . 104 ARG HD2 H 3.26 0.02 2 1085 . 104 ARG HD3 H 3.36 0.02 2 1086 . 104 ARG C C 177.3 0.2 1 1087 . 105 GLU N N 119.7 0.1 1 1088 . 105 GLU H H 8.52 0.02 1 1089 . 105 GLU CA C 59.8 0.2 1 1090 . 105 GLU HA H 3.92 0.02 1 1091 . 105 GLU CB C 29.1 0.2 1 1092 . 105 GLU HB2 H 2.11 0.02 1 1093 . 105 GLU HB3 H 2.17 0.02 1 1094 . 105 GLU CG C 36.1 0.2 1 1095 . 105 GLU HG2 H 2.22 0.02 2 1096 . 105 GLU HG3 H 2.38 0.02 2 1097 . 105 GLU C C 179.9 0.2 1 1098 . 106 ARG N N 116.1 0.1 1 1099 . 106 ARG H H 8.59 0.02 1 1100 . 106 ARG CA C 57.6 0.2 1 1101 . 106 ARG HA H 3.99 0.02 1 1102 . 106 ARG CB C 30.0 0.2 1 1103 . 106 ARG HB2 H 1.88 0.02 1 1104 . 106 ARG HB3 H 1.52 0.02 1 1105 . 106 ARG CG C 26.8 0.2 1 1106 . 106 ARG HG2 H 1.37 0.02 2 1107 . 106 ARG HG3 H 2.04 0.02 2 1108 . 106 ARG CD C 42.7 0.2 1 1109 . 106 ARG HD2 H 2.97 0.02 2 1110 . 106 ARG HD3 H 2.90 0.02 2 1111 . 106 ARG C C 177.4 0.2 1 1112 . 107 ALA N N 121.7 0.1 1 1113 . 107 ALA H H 7.58 0.02 1 1114 . 107 ALA CA C 55.3 0.2 1 1115 . 107 ALA HA H 3.98 0.02 1 1116 . 107 ALA HB H 1.71 0.02 1 1117 . 107 ALA CB C 18.7 0.2 1 1118 . 107 ALA C C 180.2 0.2 1 1119 . 108 VAL N N 119.6 0.1 1 1120 . 108 VAL H H 8.01 0.02 1 1121 . 108 VAL CA C 66.1 0.2 1 1122 . 108 VAL HA H 3.67 0.02 1 1123 . 108 VAL CB C 31.8 0.2 1 1124 . 108 VAL HB H 2.24 0.02 1 1125 . 108 VAL HG1 H 0.92 0.02 1 1126 . 108 VAL HG2 H 1.03 0.02 1 1127 . 108 VAL CG1 C 21.0 0.2 1 1128 . 108 VAL CG2 C 22.2 0.2 1 1129 . 108 VAL C C 178.9 0.2 1 1130 . 109 VAL N N 118.3 0.1 1 1131 . 109 VAL H H 7.50 0.02 1 1132 . 109 VAL CA C 65.5 0.2 1 1133 . 109 VAL HA H 3.79 0.02 1 1134 . 109 VAL CB C 31.5 0.2 1 1135 . 109 VAL HB H 2.12 0.02 1 1136 . 109 VAL HG1 H 0.95 0.02 1 1137 . 109 VAL HG2 H 1.05 0.02 1 1138 . 109 VAL CG1 C 21.6 0.2 1 1139 . 109 VAL CG2 C 22.1 0.2 1 1140 . 109 VAL C C 178.3 0.2 1 1141 . 110 ARG N N 120.1 0.1 1 1142 . 110 ARG H H 8.22 0.02 1 1143 . 110 ARG CA C 59.7 0.2 1 1144 . 110 ARG HA H 4.01 0.02 1 1145 . 110 ARG CB C 30.8 0.2 1 1146 . 110 ARG HB2 H 2.02 0.02 2 1147 . 110 ARG HB3 H 2.17 0.02 2 1148 . 110 ARG CG C 28.7 0.2 1 1149 . 110 ARG HG2 H 1.51 0.02 2 1150 . 110 ARG HG3 H 2.03 0.02 2 1151 . 110 ARG CD C 43.7 0.2 1 1152 . 110 ARG HD2 H 3.37 0.02 1 1153 . 110 ARG HD3 H 3.37 0.02 1 1154 . 110 ARG C C 177.9 0.2 1 1155 . 111 GLU N N 117.6 0.1 1 1156 . 111 GLU H H 7.83 0.02 1 1157 . 111 GLU CA C 57.3 0.2 1 1158 . 111 GLU HA H 4.21 0.02 1 1159 . 111 GLU CB C 30.0 0.2 1 1160 . 111 GLU HB2 H 2.17 0.02 1 1161 . 111 GLU HB3 H 2.04 0.02 1 1162 . 111 GLU HG2 H 2.40 0.02 2 1163 . 111 GLU HG3 H 2.32 0.02 2 1164 . 111 GLU C C 177.3 0.2 1 1165 . 112 MET N N 118.4 0.1 1 1166 . 112 MET H H 7.75 0.02 1 1167 . 112 MET CA C 56.6 0.2 1 1168 . 112 MET HA H 4.39 0.02 1 1169 . 112 MET CB C 32.9 0.2 1 1170 . 112 MET HB2 H 2.17 0.02 1 1171 . 112 MET HB3 H 2.17 0.02 1 1172 . 112 MET CG C 32.3 0.2 1 1173 . 112 MET HG2 H 2.61 0.02 2 1174 . 112 MET HG3 H 2.73 0.02 2 1175 . 112 MET C C 176.7 0.2 1 1176 . 113 ILE N N 119.4 0.1 1 1177 . 113 ILE H H 7.83 0.02 1 1178 . 113 ILE CA C 61.5 0.2 1 1179 . 113 ILE HA H 4.29 0.02 1 1180 . 113 ILE CB C 38.6 0.2 1 1181 . 113 ILE HB H 2.00 0.02 1 1182 . 113 ILE HG2 H 0.93 0.02 1 1183 . 113 ILE CG2 C 17.3 0.2 1 1184 . 113 ILE CG1 C 26.9 0.2 1 1185 . 113 ILE HG12 H 1.50 0.02 2 1186 . 113 ILE HG13 H 1.28 0.02 2 1187 . 113 ILE HD1 H 0.85 0.02 1 1188 . 113 ILE CD1 C 13.2 0.2 1 1189 . 113 ILE C C 175.5 0.2 1 1190 . 114 SER N N 125.0 0.1 1 1191 . 114 SER H H 7.76 0.02 1 1192 . 114 SER CA C 60.2 0.2 1 1193 . 114 SER HA H 4.27 0.02 1 1194 . 114 SER CB C 65.0 0.2 1 1195 . 114 SER HB2 H 3.85 0.02 1 1196 . 114 SER HB3 H 3.85 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values _Saveframe_category coupling_constants _Details ; J3HNHB and J3HAHB were only qualitatively measured and classified as big (HNHB <-3 Hz, HAHB >9 Hz) 9..11) or small (HNHB >-2.5Hz) ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name DnaB(24-136) _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 8 ILE H 8 ILE HA 2.8 . . 1.0 2 3JHNHA 9 GLU H 9 GLU HA 3.5 . . 1.0 3 3JHNHA 10 ALA H 10 ALA HA 4.6 . . 1.0 4 3JHNHA 11 GLU H 11 GLU HA 4.1 . . 1.0 5 3JHNHA 12 GLN H 12 GLN HA 4.4 . . 1.0 6 3JHNHA 13 SER H 13 SER HA 4.9 . . 1.0 7 3JHNHA 14 VAL H 14 VAL HA 5.3 . . 1.0 8 3JHNHA 15 LEU H 15 LEU HA 5.0 . . 1.0 9 3JHNHA 18 LEU H 18 LEU HA 4.9 . . 1.0 10 3JHNHA 19 MET H 19 MET HA 5.0 . . 1.0 11 3JHNHA 20 LEU H 20 LEU HA 6.8 . . 1.0 12 3JHNHA 21 ASP H 21 ASP HA 8.1 . . 1.0 13 3JHNHA 22 ASN H 22 ASN HA 4.7 . . 1.0 14 3JHNHA 23 GLU H 23 GLU HA 6.4 . . 1.0 15 3JHNHA 24 ARG H 24 ARG HA 8.0 . . 1.0 16 3JHNHA 25 TRP H 25 TRP HA 2.1 . . 1.0 17 3JHNHA 26 ASP H 26 ASP HA 3.4 . . 1.0 18 3JHNHA 27 ASP H 27 ASP HA 6.1 . . 1.0 19 3JHNHA 28 VAL H 28 VAL HA 6.5 . . 1.0 20 3JHNHA 29 ALA H 29 ALA HA 4.1 . . 1.0 21 3JHNHA 30 GLU H 30 GLU HA 7.2 . . 1.0 22 3JHNHA 31 ARG H 31 ARG HA 9.0 . . 1.0 23 3JHNHA 32 VAL H 32 VAL HA 8.9 . . 1.0 24 3JHNHA 33 VAL H 33 VAL HA 10.0 . . 1.0 25 3JHNHA 34 ALA H 34 ALA HA 1.9 . . 1.0 26 3JHNHA 35 ASP H 35 ASP HA 4.0 . . 1.0 27 3JHNHA 36 ASP H 36 ASP HA 6.1 . . 1.0 28 3JHNHA 37 PHE H 37 PHE HA 6.8 . . 1.0 29 3JHNHA 39 THR H 39 THR HA 8.5 . . 1.0 30 3JHNHA 42 HIS H 42 HIS HA 3.9 . . 1.0 31 3JHNHA 43 ARG H 43 ARG HA 4.3 . . 1.0 32 3JHNHA 44 HIS H 44 HIS HA 4.3 . . 1.0 33 3JHNHA 45 ILE H 45 ILE HA 4.4 . . 1.0 34 3JHNHA 46 PHE H 46 PHE HA 3.6 . . 1.0 35 3JHNHA 47 THR H 47 THR HA 4.0 . . 1.0 36 3JHNHA 48 GLU H 48 GLU HA 6.0 . . 1.0 37 3JHNHA 49 MET H 49 MET HA 3.8 . . 1.0 38 3JHNHA 50 ALA H 50 ALA HA 3.5 . . 1.0 39 3JHNHA 51 ARG H 51 ARG HA 4.5 . . 1.0 40 3JHNHA 52 LEU H 52 LEU HA 4.5 . . 1.0 41 3JHNHA 53 GLN H 53 GLN HA 3.5 . . 1.0 42 3JHNHA 54 GLU H 54 GLU HA 4.7 . . 1.0 43 3JHNHA 55 SER H 55 SER HA 8.9 . . 1.0 44 3JHNHA 57 SER H 57 SER HA 8.0 . . 1.0 45 3JHNHA 59 ILE H 59 ILE HA 10.0 . . 1.0 46 3JHNHA 60 ASP H 60 ASP HA 5.6 . . 1.0 47 3JHNHA 61 LEU H 61 LEU HA 2.1 . . 1.0 48 3JHNHA 62 ILE H 62 ILE HA 6.3 . . 1.0 49 3JHNHA 64 LEU H 64 LEU HA 3.9 . . 1.0 50 3JHNHA 65 ALA H 65 ALA HA 4.3 . . 1.0 51 3JHNHA 66 GLU H 66 GLU HA 3.9 . . 1.0 52 3JHNHA 67 SER H 67 SER HA 4.7 . . 1.0 53 3JHNHA 68 LEU H 68 LEU HA 4.6 . . 1.0 54 3JHNHA 69 GLU H 69 GLU HA 3.9 . . 1.0 55 3JHNHA 70 ARG H 70 ARG HA 4.5 . . 1.0 56 3JHNHA 71 GLN H 71 GLN HA 7.7 . . 1.0 57 3JHNHA 73 GLN H 73 GLN HA 9.7 . . 1.0 58 3JHNHA 74 LEU H 74 LEU HA 5.2 . . 1.0 59 3JHNHA 75 ASP H 75 ASP HA 4.8 . . 3.0 60 3JHNHA 77 VAL H 77 VAL HA 9.5 . . 1.0 61 3JHNHA 82 TYR H 82 TYR HA 6.5 . . 1.0 62 3JHNHA 83 LEU H 83 LEU HA 5.2 . . 1.0 63 3JHNHA 84 ALA H 84 ALA HA 4.1 . . 1.0 64 3JHNHA 85 GLU H 85 GLU HA 5.3 . . 1.0 65 3JHNHA 86 LEU H 86 LEU HA 4.2 . . 3.0 66 3JHNHA 87 SER H 87 SER HA 5.0 . . 1.0 67 3JHNHA 88 LYS H 88 LYS HA 6.1 . . 1.0 68 3JHNHA 89 ASN H 89 ASN HA 8.1 . . 1.0 69 3JHNHA 90 THR H 90 THR HA 8.4 . . 1.0 70 3JHNHA 97 SER H 97 SER HA 3.8 . . 1.0 71 3JHNHA 98 ALA H 98 ALA HA 5.4 . . 1.0 72 3JHNHA 99 TYR H 99 TYR HA 5.8 . . 1.0 73 3JHNHA 100 ALA H 100 ALA HA 4.4 . . 1.0 74 3JHNHA 101 ASP H 101 ASP HA 3.8 . . 1.0 75 3JHNHA 102 ILE H 102 ILE HA 5.1 . . 1.0 76 3JHNHA 103 VAL H 103 VAL HA 3.6 . . 1.0 77 3JHNHA 104 ARG H 104 ARG HA 3.7 . . 1.0 78 3JHNHA 105 GLU H 105 GLU HA 3.5 . . 1.0 79 3JHNHA 106 ARG H 106 ARG HA 4.8 . . 1.0 80 3JHNHA 107 ALA H 107 ALA HA 5.2 . . 1.0 81 3JHNHA 108 VAL H 108 VAL HA 4.0 . . 1.0 82 3JHNHA 109 VAL H 109 VAL HA 6.2 . . 1.0 83 3JHNHA 110 ARG H 110 ARG HA 3.3 . . 1.0 84 3JHNHA 111 GLU H 111 GLU HA 6.3 . . 1.0 85 3JHNHA 112 MET H 112 MET HA 7.4 . . 1.0 86 3JHNHA 113 ILE H 113 ILE HA 8.4 . . 1.0 87 3JHNHA 114 SER H 114 SER HA 8.2 . . 1.0 88 3JNHB 9 GLU N 9 GLU HB3 . -5.0 . 2.0 89 3JNHB 11 GLU N 11 GLU HB3 . -5.0 . 2.0 90 3JNHB 12 GLN N 12 GLN HB3 . -5.0 . 2.0 91 3JNHB 13 SER N 13 SER HB3 . -5.0 . 2.0 92 3JNHB 14 VAL N 14 VAL HB . . -0.5 2.0 93 3JNHB 15 LEU N 15 LEU HB3 . -5.0 . 2.0 94 3JNHB 18 LEU N 18 LEU HB3 . -5.0 . 2.0 95 3JNHB 19 MET N 19 MET HB3 . -5.0 . 2.0 96 3JNHB 20 LEU N 20 LEU HB3 . -5.0 . 2.0 97 3JNHB 21 ASP N 21 ASP HB2 . . -0.5 2.0 98 3JNHB 21 ASP N 21 ASP HB3 . . -0.5 2.0 99 3JNHB 24 ARG N 24 ARG HB3 . -5.0 . 2.0 100 3JNHB 25 TRP N 25 TRP HB2 . . -0.5 2.0 101 3JNHB 25 TRP N 25 TRP HB3 . . -0.5 2.0 102 3JNHB 26 ASP N 26 ASP HB3 . -5.0 . 2.0 103 3JNHB 27 ASP N 27 ASP HB3 . -5.0 . 2.0 104 3JNHB 28 VAL N 28 VAL HB . . -0.5 2.0 105 3JNHB 32 VAL N 32 VAL HB . -5.0 . 2.0 106 3JNHB 33 VAL N 33 VAL HB . -5.0 . 2.0 107 3JNHB 35 ASP N 35 ASP HB3 . -5.0 . 2.0 108 3JNHB 36 ASP N 36 ASP HB2 . -5.0 . 2.0 109 3JNHB 37 PHE N 37 PHE HB3 . -5.0 . 2.0 110 3JNHB 42 HIS N 42 HIS HB3 . -5.0 . 2.0 111 3JNHB 43 ARG N 43 ARG HB3 . -5.0 . 2.0 112 3JNHB 45 ILE N 45 ILE HB . . -0.5 2.0 113 3JNHB 46 PHE N 46 PHE HB2 . . -0.5 2.0 114 3JNHB 46 PHE N 46 PHE HB3 . . -0.5 2.0 115 3JNHB 47 THR N 47 THR HB . . -0.5 2.0 116 3JNHB 48 GLU N 48 GLU HB2 . . -0.5 2.0 117 3JNHB 48 GLU N 48 GLU HB3 . . -0.5 2.0 118 3JNHB 49 MET N 49 MET HB3 . -5.0 . 2.0 119 3JNHB 52 LEU N 52 LEU HB3 . -5.0 . 2.0 120 3JNHB 53 GLN N 53 GLN HB2 . . -0.5 2.0 121 3JNHB 53 GLN N 53 GLN HB3 . . -0.5 2.0 122 3JNHB 57 SER N 57 SER HB3 . -5.0 . 2.0 123 3JNHB 59 ILE N 59 ILE HB . -5.0 . 2.0 124 3JNHB 60 ASP N 60 ASP HB2 . -5.0 . 2.0 125 3JNHB 61 LEU N 61 LEU HB2 . . -0.5 2.0 126 3JNHB 61 LEU N 61 LEU HB3 . . -0.5 2.0 127 3JNHB 62 ILE N 62 ILE HB . . -0.5 2.0 128 3JNHB 63 THR N 63 THR HB . . -0.5 2.0 129 3JNHB 64 LEU N 64 LEU HB2 . . -0.5 2.0 130 3JNHB 64 LEU N 64 LEU HB3 . . -0.5 2.0 131 3JNHB 66 GLU N 66 GLU HB3 . -5.0 . 2.0 132 3JNHB 67 SER N 67 SER HB2 . . -0.5 2.0 133 3JNHB 67 SER N 67 SER HB3 . . -0.5 2.0 134 3JNHB 68 LEU N 68 LEU HB3 . -5.0 . 2.0 135 3JNHB 70 ARG N 70 ARG HB2 . -5.0 . 2.0 136 3JNHB 71 GLN N 71 GLN HB3 . -5.0 . 2.0 137 3JNHB 73 GLN N 73 GLN HB3 . -5.0 . 2.0 138 3JNHB 74 LEU N 74 LEU HB2 . . -0.5 2.0 139 3JNHB 74 LEU N 74 LEU HB3 . . -0.5 2.0 140 3JNHB 77 VAL N 77 VAL HB . -5.0 . 2.0 141 3JNHB 82 TYR N 82 TYR HB2 . . -0.5 2.0 142 3JNHB 82 TYR N 82 TYR HB3 . . -0.5 2.0 143 3JNHB 83 LEU N 83 LEU HB3 . -5.0 . 2.0 144 3JNHB 86 LEU N 86 LEU HB3 . -5.0 . 2.0 145 3JNHB 90 THR N 90 THR HB . . -0.5 2.0 146 3JNHB 96 ILE N 96 ILE HB . . -0.5 2.0 147 3JNHB 99 TYR N 99 TYR HB3 . -5.0 . 2.0 148 3JNHB 101 ASP N 101 ASP HB3 . -5.0 . 2.0 149 3JNHB 102 ILE N 102 ILE HB . . -0.5 2.0 150 3JNHB 103 VAL N 103 VAL HB . . -0.5 2.0 151 3JNHB 104 ARG N 104 ARG HB2 . . -0.5 2.0 152 3JNHB 104 ARG N 104 ARG HB3 . . -0.5 2.0 153 3JNHB 105 GLU N 105 GLU HB2 . . -0.5 2.0 154 3JNHB 105 GLU N 105 GLU HB3 . . -0.5 2.0 155 3JNHB 106 ARG N 106 ARG HB3 . -5.0 . 2.0 156 3JNHB 108 VAL N 108 VAL HB . . -0.5 2.0 157 3JNHB 109 VAL N 109 VAL HB . . -0.5 2.0 158 3JNHB 110 ARG N 110 ARG HB2 . . -0.5 2.0 159 3JNHB 110 ARG N 110 ARG HB3 . . -0.5 2.0 160 3JNHB 111 GLU N 111 GLU HB2 . -5.0 . 2.0 161 3JNHB 113 ILE N 113 ILE HB . -5.0 . 2.0 162 3JHAHB 13 SER HA 13 SER HB2 . 11.0 . 2.0 163 3JHAHB 15 LEU HA 15 LEU HB2 . 11.0 . 2.0 164 3JHAHB 19 MET HA 19 MET HB2 . 11.0 . 2.0 165 3JHAHB 21 ASP HA 21 ASP HB3 . 11.0 . 2.0 166 3JHAHB 24 ARG HA 24 ARG HB2 . 11.0 . 2.0 167 3JHAHB 25 TRP HA 25 TRP HB3 . 11.0 . 2.0 168 3JHAHB 26 ASP HA 26 ASP HB2 . 11.0 . 2.0 169 3JHAHB 35 ASP HA 35 ASP HB2 . 11.0 . 2.0 170 3JHAHB 36 ASP HA 36 ASP HB3 . 11.0 . 2.0 171 3JHAHB 37 PHE HA 37 PHE HB2 . 11.0 . 2.0 172 3JHAHB 42 HIS HA 42 HIS HB2 . 11.0 . 2.0 173 3JHAHB 46 PHE HA 46 PHE HB3 . 11.0 . 2.0 174 3JHAHB 48 GLU HA 48 GLU HB3 . 11.0 . 2.0 175 3JHAHB 49 MET HA 49 MET HB2 . 11.0 . 2.0 176 3JHAHB 52 LEU HA 52 LEU HB2 . 11.0 . 2.0 177 3JHAHB 57 SER HA 57 SER HB2 . 11.0 . 2.0 178 3JHAHB 61 LEU HA 61 LEU HB3 . 11.0 . 2.0 179 3JHAHB 64 LEU HA 64 LEU HB3 . 11.0 . 2.0 180 3JHAHB 68 LEU HA 68 LEU HB2 . 11.0 . 2.0 181 3JHAHB 71 GLN HA 71 GLN HB2 . 11.0 . 2.0 182 3JHAHB 73 GLN HA 73 GLN HB2 . 11.0 . 2.0 183 3JHAHB 74 LEU HA 74 LEU HB3 . 11.0 . 2.0 184 3JHAHB 80 PHE HA 80 PHE HB2 . 11.0 . 2.0 185 3JHAHB 82 TYR HA 82 TYR HB3 . 11.0 . 2.0 186 3JHAHB 83 LEU HA 83 LEU HB2 . 11.0 . 2.0 187 3JHAHB 86 LEU HA 86 LEU HB2 . 11.0 . 2.0 188 3JHAHB 99 TYR HA 99 TYR HB2 . 11.0 . 2.0 189 3JHAHB 101 ASP HA 101 ASP HB2 . 11.0 . 2.0 190 3JHAHB 106 ARG HA 106 ARG HB2 . 11.0 . 2.0 stop_ save_