data_5121 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein ; _BMRB_accession_number 5121 _BMRB_flat_file_name bmr5121.str _Entry_type original _Submission_date 2001-08-24 _Accession_date 2001-08-24 _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 Williams Neal K. . 2 Prosselkov Pavel . . 3 Liepinsh Edvards . . 4 Line Inara . . 5 Sharipo Anatoly . . 6 Littler Dene R. . 7 Curmi Paul M.G. . 8 Otting Gottfried . . 9 Dixon Nicholas E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 638 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-08 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4297 'DnaB(24-136) recorded at different conditions' 5122 'cyclic N-terminal domain of DnaB helicase' stop_ _Original_release_date 2002-04-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21864163 _PubMed_ID 11742000 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Williams Neal K. . 2 Prosselkov Pavel . . 3 Liepinsh Edvards . . 4 Line Inara . . 5 Sharipo Anatoly . . 6 Littler Dene R. . 7 Curmi Paul M.G. . 8 Otting Gottfried . . 9 Dixon Nicholas E. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 277 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7790 _Page_last 7798 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_DnaB(24-136) _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of DnaB helicase' _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 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DnaB(24-136) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal Domain of E. coli DnaB Helicase' _Abbreviation_common DnaB(24-136) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # 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 2015-01-28 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-Nterm 100.00 142 99.12 100.00 6.88e-76 BMRB 4297 DnaB(24-136) 100.00 114 100.00 100.00 1.44e-76 BMRB 5122 cz-DnaB 99.12 122 100.00 100.00 1.04e-75 PDB 1B79 "N-Terminal Domain Of Dna Replication Protein Dnab" 92.98 119 99.06 100.00 2.84e-70 PDB 1JWE "Nmr Structure Of The N-Terminal Domain Of E. Coli Dnab Helicase" 100.00 114 100.00 100.00 1.44e-76 DBJ BAB38457 "replicative DNA helicase DnaB [Escherichia coli O157:H7 str. Sakai]" 100.00 471 98.25 100.00 1.44e-71 DBJ BAE78054 "replicative DNA helicase [Escherichia coli str. K-12 substr. W3110]" 100.00 471 99.12 100.00 5.16e-72 DBJ BAG66812 "replicative DNA helicase [Escherichia coli O111:H-]" 100.00 471 99.12 100.00 5.16e-72 DBJ BAG79869 "replicative DNA helicase [Escherichia coli SE11]" 100.00 471 99.12 100.00 5.16e-72 DBJ BAH61192 "replicative DNA helicase [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 471 99.12 100.00 6.32e-72 EMBL CAP78509 "Replicative DNA helicase [Escherichia coli LF82]" 100.00 471 99.12 100.00 5.16e-72 EMBL CAQ34401 "dnaB, subunit of replicative DNA helicase and primosome [Escherichia coli BL21(DE3)]" 100.00 471 99.12 100.00 5.16e-72 EMBL CAQ91563 "replicative DNA helicase [Escherichia fergusonii ATCC 35469]" 100.00 471 98.25 99.12 2.21e-71 EMBL CAR01031 "replicative DNA helicase [Escherichia coli IAI1]" 100.00 471 99.12 100.00 5.16e-72 EMBL CAR05689 "replicative DNA helicase [Escherichia coli S88]" 100.00 471 99.12 100.00 5.33e-72 GB AAA23689 "DnaB replication protein (dnaB) [Escherichia coli]" 100.00 471 99.12 100.00 5.16e-72 GB AAA23690 "helicase, partial [Escherichia coli]" 100.00 157 99.12 100.00 1.30e-75 GB AAC43146 "ORF_o471 [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.16e-72 GB AAC77022 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.16e-72 GB AAG59250 "replicative DNA helicase; part of primosome [Escherichia coli O157:H7 str. EDL933]" 100.00 471 98.25 100.00 1.44e-71 REF NP_290685 "replicative DNA helicase [Escherichia coli O157:H7 str. EDL933]" 100.00 471 98.25 100.00 1.44e-71 REF NP_313061 "replicative DNA helicase [Escherichia coli O157:H7 str. Sakai]" 100.00 471 98.25 100.00 1.44e-71 REF NP_418476 "replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]" 100.00 471 99.12 100.00 5.16e-72 REF NP_709868 "replicative DNA helicase [Shigella flexneri 2a str. 301]" 100.00 471 99.12 100.00 5.16e-72 REF NP_756878 "replicative DNA helicase [Escherichia coli CFT073]" 100.00 483 99.12 100.00 6.85e-72 SP P0ACB0 "RecName: Full=Replicative DNA helicase [Escherichia coli K-12]" 100.00 471 99.12 100.00 5.16e-72 SP P0ACB1 "RecName: Full=Replicative DNA helicase [Shigella flexneri]" 100.00 471 99.12 100.00 5.16e-72 SP Q8FB22 "RecName: Full=Replicative DNA helicase [Escherichia coli CFT073]" 100.00 471 99.12 100.00 5.33e-72 SP Q8X5V3 "RecName: Full=Replicative DNA helicase [Escherichia coli O157:H7]" 100.00 471 98.25 100.00 1.44e-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) 0.6 mM . stop_ save_ ############################ # Computer software used # ############################ save_Prosa _Saveframe_category software _Name Prosa _Version 3.6 loop_ _Task 'spectra processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'peak analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.0 0.1 n/a temperature 304 1 K 'ionic strength' 0.1 0.02 M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct cylindrical internal parallel 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 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 24 2 LYS HA H 4.222 0.02 1 2 24 2 LYS HB2 H 1.698 0.02 2 3 24 2 LYS HB3 H 1.795 0.02 2 4 24 2 LYS HG2 H 1.407 0.02 2 5 24 2 LYS HG3 H 1.356 0.02 2 6 24 2 LYS HD2 H 1.640 0.02 1 7 24 2 LYS HD3 H 1.640 0.02 1 8 24 2 LYS HE2 H 2.940 0.02 1 9 24 2 LYS HE3 H 2.940 0.02 1 10 25 3 VAL H H 7.787 0.02 1 11 25 3 VAL HA H 4.391 0.02 1 12 25 3 VAL HB H 1.993 0.02 1 13 25 3 VAL HG1 H 0.976 0.02 1 14 25 3 VAL HG2 H 0.921 0.02 1 15 26 4 PRO HA H 4.601 0.02 1 16 26 4 PRO HB2 H 1.551 0.02 2 17 26 4 PRO HB3 H 2.260 0.02 2 18 26 4 PRO HG2 H 1.991 0.02 2 19 26 4 PRO HG3 H 2.104 0.02 2 20 26 4 PRO HD2 H 3.604 0.02 2 21 26 4 PRO HD3 H 3.920 0.02 2 22 27 5 PRO HA H 4.371 0.02 1 23 27 5 PRO HB2 H 1.951 0.02 2 24 27 5 PRO HB3 H 2.141 0.02 2 25 27 5 PRO HG2 H 1.910 0.02 2 26 27 5 PRO HG3 H 1.990 0.02 2 27 27 5 PRO HD2 H 3.396 0.02 2 28 27 5 PRO HD3 H 3.870 0.02 2 29 28 6 HIS H H 7.825 0.02 1 30 28 6 HIS HA H 4.200 0.02 1 31 28 6 HIS HB2 H 2.849 0.02 2 32 28 6 HIS HB3 H 2.667 0.02 2 33 28 6 HIS HD2 H 6.401 0.02 1 34 28 6 HIS HE1 H 7.431 0.02 1 35 29 7 SER H H 10.122 0.02 1 36 29 7 SER HA H 4.716 0.02 1 37 29 7 SER HB2 H 3.655 0.02 2 38 29 7 SER HB3 H 3.686 0.02 2 39 30 8 ILE H H 9.099 0.02 1 40 30 8 ILE HA H 4.005 0.02 1 41 30 8 ILE HB H 2.050 0.02 1 42 30 8 ILE HG2 H 1.014 0.02 1 43 30 8 ILE HG12 H 1.581 0.02 2 44 30 8 ILE HG13 H 1.656 0.02 2 45 30 8 ILE HD1 H 0.978 0.02 1 46 31 9 GLU H H 8.879 0.02 1 47 31 9 GLU HA H 4.102 0.02 1 48 31 9 GLU HB2 H 1.961 0.02 2 49 31 9 GLU HB3 H 1.880 0.02 2 50 31 9 GLU HG2 H 2.240 0.02 1 51 31 9 GLU HG3 H 2.240 0.02 1 52 32 10 ALA H H 8.010 0.02 1 53 32 10 ALA HA H 3.787 0.02 1 54 32 10 ALA HB H 1.633 0.02 1 55 33 11 GLU H H 7.891 0.02 1 56 33 11 GLU HA H 3.761 0.02 1 57 33 11 GLU HB2 H 2.477 0.02 2 58 33 11 GLU HB3 H 2.280 0.02 2 59 33 11 GLU HG2 H 3.273 0.02 2 60 33 11 GLU HG3 H 2.255 0.02 2 61 34 12 GLN H H 8.627 0.02 1 62 34 12 GLN HA H 3.543 0.02 1 63 34 12 GLN HB2 H 2.290 0.02 1 64 34 12 GLN HB3 H 1.798 0.02 1 65 34 12 GLN HG2 H 2.239 0.02 1 66 34 12 GLN HG3 H 3.001 0.02 1 67 34 12 GLN HE21 H 7.154 0.02 2 68 34 12 GLN HE22 H 7.804 0.02 2 69 35 13 SER H H 7.864 0.02 1 70 35 13 SER HA H 4.121 0.02 1 71 35 13 SER HB2 H 3.235 0.02 1 72 35 13 SER HB3 H 3.122 0.02 1 73 36 14 VAL H H 7.985 0.02 1 74 36 14 VAL HA H 3.654 0.02 1 75 36 14 VAL HB H 2.260 0.02 1 76 36 14 VAL HG1 H 1.028 0.02 1 77 36 14 VAL HG2 H 1.051 0.02 1 78 37 15 LEU H H 7.674 0.02 1 79 37 15 LEU HA H 4.024 0.02 1 80 37 15 LEU HB2 H 1.715 0.02 1 81 37 15 LEU HB3 H 1.051 0.02 1 82 37 15 LEU HG H 1.980 0.02 1 83 37 15 LEU HD1 H 0.428 0.02 1 84 37 15 LEU HD2 H 0.778 0.02 1 85 38 16 GLY H H 8.800 0.02 1 86 38 16 GLY HA2 H 3.481 0.02 1 87 38 16 GLY HA3 H 3.859 0.02 1 88 39 17 GLY H H 8.046 0.02 1 89 39 17 GLY HA2 H 3.738 0.02 1 90 39 17 GLY HA3 H 3.738 0.02 1 91 40 18 LEU H H 7.915 0.02 1 92 40 18 LEU HA H 4.132 0.02 1 93 40 18 LEU HB2 H 2.118 0.02 1 94 40 18 LEU HB3 H 1.471 0.02 1 95 40 18 LEU HG H 2.051 0.02 1 96 40 18 LEU HD1 H 1.177 0.02 1 97 40 18 LEU HD2 H 0.966 0.02 1 98 41 19 MET H H 7.280 0.02 1 99 41 19 MET HA H 4.191 0.02 1 100 41 19 MET HB2 H 2.250 0.02 1 101 41 19 MET HB3 H 1.926 0.02 1 102 41 19 MET HG2 H 2.640 0.02 1 103 41 19 MET HG3 H 2.640 0.02 1 104 42 20 LEU H H 7.280 0.02 1 105 42 20 LEU HA H 4.215 0.02 1 106 42 20 LEU HB2 H 1.799 0.02 2 107 42 20 LEU HB3 H 1.700 0.02 2 108 42 20 LEU HG H 1.730 0.02 1 109 42 20 LEU HD1 H 0.923 0.02 1 110 42 20 LEU HD2 H 0.881 0.02 1 111 43 21 ASP H H 8.090 0.02 1 112 43 21 ASP HA H 4.901 0.02 1 113 43 21 ASP HB2 H 2.348 0.02 1 114 43 21 ASP HB3 H 2.856 0.02 1 115 44 22 ASN H H 9.088 0.02 1 116 44 22 ASN HA H 4.530 0.02 1 117 44 22 ASN HB2 H 2.891 0.02 1 118 44 22 ASN HB3 H 2.891 0.02 1 119 44 22 ASN HD21 H 6.085 0.02 2 120 44 22 ASN HD22 H 8.099 0.02 2 121 45 23 GLU H H 8.323 0.02 1 122 45 23 GLU HA H 4.239 0.02 1 123 45 23 GLU HB2 H 2.221 0.02 1 124 45 23 GLU HB3 H 2.221 0.02 1 125 45 23 GLU HG2 H 2.338 0.02 2 126 45 23 GLU HG3 H 2.358 0.02 2 127 46 24 ARG H H 7.570 0.02 1 128 46 24 ARG HA H 4.490 0.02 1 129 46 24 ARG HB2 H 1.971 0.02 1 130 46 24 ARG HB3 H 2.201 0.02 1 131 46 24 ARG HG2 H 1.730 0.02 2 132 46 24 ARG HG3 H 1.771 0.02 2 133 46 24 ARG HD2 H 3.221 0.02 1 134 46 24 ARG HD3 H 3.221 0.02 1 135 46 24 ARG HE H 7.591 0.02 1 136 47 25 TRP H H 7.694 0.02 1 137 47 25 TRP HA H 3.967 0.02 1 138 47 25 TRP HB2 H 3.337 0.02 1 139 47 25 TRP HB3 H 3.113 0.02 1 140 47 25 TRP HD1 H 7.032 0.02 1 141 47 25 TRP HE1 H 9.769 0.02 1 142 47 25 TRP HE3 H 7.215 0.02 1 143 47 25 TRP HZ2 H 7.141 0.02 1 144 47 25 TRP HZ3 H 6.395 0.02 1 145 47 25 TRP HH2 H 5.873 0.02 1 146 48 26 ASP H H 8.320 0.02 1 147 48 26 ASP HA H 4.030 0.02 1 148 48 26 ASP HB2 H 2.662 0.02 1 149 48 26 ASP HB3 H 2.606 0.02 1 150 49 27 ASP H H 7.756 0.02 1 151 49 27 ASP HA H 4.224 0.02 1 152 49 27 ASP HB2 H 2.707 0.02 2 153 49 27 ASP HB3 H 2.542 0.02 2 154 50 28 VAL H H 7.575 0.02 1 155 50 28 VAL HA H 3.337 0.02 1 156 50 28 VAL HB H 1.850 0.02 1 157 50 28 VAL HG1 H 0.765 0.02 1 158 50 28 VAL HG2 H 0.867 0.02 1 159 51 29 ALA H H 8.760 0.02 1 160 51 29 ALA HA H 4.023 0.02 1 161 51 29 ALA HB H 0.794 0.02 1 162 52 30 GLU H H 7.162 0.02 1 163 52 30 GLU HA H 4.191 0.02 1 164 52 30 GLU HB2 H 2.030 0.02 1 165 52 30 GLU HB3 H 2.030 0.02 1 166 52 30 GLU HG2 H 2.291 0.02 2 167 52 30 GLU HG3 H 2.331 0.02 2 168 53 31 ARG H H 7.810 0.02 1 169 53 31 ARG HA H 4.259 0.02 1 170 53 31 ARG HB2 H 1.632 0.02 2 171 53 31 ARG HB3 H 1.566 0.02 2 172 54 32 VAL H H 7.614 0.02 1 173 54 32 VAL HA H 4.763 0.02 1 174 54 32 VAL HB H 1.830 0.02 1 175 54 32 VAL HG1 H 0.554 0.02 1 176 54 32 VAL HG2 H 0.537 0.02 1 177 55 33 VAL H H 8.298 0.02 1 178 55 33 VAL HA H 4.635 0.02 1 179 55 33 VAL HB H 2.411 0.02 1 180 55 33 VAL HG1 H 0.930 0.02 1 181 55 33 VAL HG2 H 0.731 0.02 1 182 56 34 ALA H H 8.976 0.02 1 183 56 34 ALA HA H 3.917 0.02 1 184 56 34 ALA HB H 1.604 0.02 1 185 57 35 ASP H H 8.019 0.02 1 186 57 35 ASP HA H 4.311 0.02 1 187 57 35 ASP HB2 H 2.348 0.02 1 188 57 35 ASP HB3 H 2.688 0.02 1 189 58 36 ASP H H 7.924 0.02 1 190 58 36 ASP HA H 4.249 0.02 1 191 58 36 ASP HB2 H 2.541 0.02 1 192 58 36 ASP HB3 H 2.168 0.02 1 193 59 37 PHE H H 7.820 0.02 1 194 59 37 PHE HA H 3.989 0.02 1 195 59 37 PHE HB2 H 3.166 0.02 1 196 59 37 PHE HB3 H 2.879 0.02 1 197 59 37 PHE HD1 H 7.410 0.02 1 198 59 37 PHE HD2 H 7.410 0.02 1 199 59 37 PHE HE1 H 6.386 0.02 1 200 59 37 PHE HE2 H 6.386 0.02 1 201 59 37 PHE HZ H 6.580 0.02 1 202 60 38 TYR H H 11.89 0.02 1 203 60 38 TYR HA H 4.193 0.02 1 204 60 38 TYR HB2 H 3.052 0.02 1 205 60 38 TYR HB3 H 2.983 0.02 1 206 60 38 TYR HD1 H 6.574 0.02 1 207 60 38 TYR HD2 H 6.574 0.02 1 208 60 38 TYR HE1 H 6.425 0.02 1 209 60 38 TYR HE2 H 6.425 0.02 1 210 61 39 THR H H 7.528 0.02 1 211 61 39 THR HA H 4.243 0.02 1 212 61 39 THR HB H 4.070 0.02 1 213 61 39 THR HG2 H 0.960 0.02 1 214 62 40 ARG H H 8.939 0.02 1 215 62 40 ARG HA H 3.885 0.02 1 216 62 40 ARG HB2 H 1.470 0.02 2 217 62 40 ARG HB3 H 1.818 0.02 2 218 62 40 ARG HD2 H 3.125 0.02 2 219 62 40 ARG HD3 H 3.153 0.02 2 220 63 41 PRO HA H 4.438 0.02 1 221 63 41 PRO HB2 H 1.539 0.02 2 222 63 41 PRO HB3 H 2.300 0.02 2 223 63 41 PRO HG2 H 1.810 0.02 2 224 63 41 PRO HG3 H 1.792 0.02 2 225 63 41 PRO HD2 H 3.600 0.02 2 226 63 41 PRO HD3 H 3.570 0.02 2 227 64 42 HIS H H 7.187 0.02 1 228 64 42 HIS HA H 4.306 0.02 1 229 64 42 HIS HB2 H 3.552 0.02 1 230 64 42 HIS HB3 H 3.009 0.02 1 231 64 42 HIS HD2 H 6.491 0.02 1 232 64 42 HIS HE1 H 7.660 0.02 1 233 64 42 HIS HD1 H 14.92 0.02 1 234 65 43 ARG H H 8.013 0.02 1 235 65 43 ARG HA H 3.867 0.02 1 236 65 43 ARG HB2 H 1.930 0.02 2 237 65 43 ARG HB3 H 1.791 0.02 2 238 65 43 ARG HG2 H 2.048 0.02 2 239 65 43 ARG HG3 H 1.781 0.02 2 240 65 43 ARG HD2 H 3.025 0.02 2 241 65 43 ARG HD3 H 3.241 0.02 2 242 66 44 HIS H H 8.173 0.02 1 243 66 44 HIS HA H 4.263 0.02 1 244 66 44 HIS HB2 H 3.051 0.02 2 245 66 44 HIS HB3 H 3.120 0.02 2 246 67 45 ILE H H 8.635 0.02 1 247 67 45 ILE HA H 3.443 0.02 1 248 67 45 ILE HB H 1.859 0.02 1 249 67 45 ILE HG2 H 0.935 0.02 1 250 67 45 ILE HG12 H 0.690 0.02 1 251 67 45 ILE HG13 H 2.216 0.02 1 252 67 45 ILE HD1 H 0.940 0.02 1 253 68 46 PHE H H 8.403 0.02 1 254 68 46 PHE HA H 3.992 0.02 1 255 68 46 PHE HB2 H 2.407 0.02 1 256 68 46 PHE HB3 H 2.650 0.02 1 257 68 46 PHE HD1 H 6.877 0.02 1 258 68 46 PHE HD2 H 6.877 0.02 1 259 68 46 PHE HE1 H 7.046 0.02 1 260 68 46 PHE HE2 H 7.046 0.02 1 261 68 46 PHE HZ H 6.708 0.02 1 262 69 47 THR H H 8.192 0.02 1 263 69 47 THR HA H 3.915 0.02 1 264 69 47 THR HB H 4.301 0.02 1 265 69 47 THR HG2 H 1.222 0.02 1 266 70 48 GLU H H 7.918 0.02 1 267 70 48 GLU HA H 4.303 0.02 1 268 70 48 GLU HB2 H 1.961 0.02 1 269 70 48 GLU HB3 H 1.791 0.02 1 270 70 48 GLU HG2 H 2.051 0.02 1 271 70 48 GLU HG3 H 2.051 0.02 1 272 71 49 MET H H 8.469 0.02 1 273 71 49 MET HA H 3.551 0.02 1 274 71 49 MET HB2 H 2.020 0.02 1 275 71 49 MET HB3 H 1.610 0.02 1 276 71 49 MET HG2 H 3.031 0.02 2 277 71 49 MET HG3 H 1.990 0.02 2 278 72 50 ALA H H 7.917 0.02 1 279 72 50 ALA HA H 3.321 0.02 1 280 72 50 ALA HB H 1.471 0.02 1 281 73 51 ARG H H 7.689 0.02 1 282 73 51 ARG HA H 3.861 0.02 1 283 73 51 ARG HB2 H 1.811 0.02 1 284 73 51 ARG HB3 H 1.811 0.02 1 285 73 51 ARG HG2 H 1.464 0.02 2 286 73 51 ARG HG3 H 1.650 0.02 2 287 73 51 ARG HD2 H 3.011 0.02 2 288 73 51 ARG HD3 H 3.201 0.02 2 289 74 52 LEU H H 8.377 0.02 1 290 74 52 LEU HA H 3.732 0.02 1 291 74 52 LEU HB2 H 1.691 0.02 1 292 74 52 LEU HB3 H 1.011 0.02 1 293 74 52 LEU HG H 1.721 0.02 1 294 74 52 LEU HD1 H 0.826 0.02 1 295 74 52 LEU HD2 H 0.729 0.02 1 296 75 53 GLN H H 8.363 0.02 1 297 75 53 GLN HA H 3.709 0.02 1 298 75 53 GLN HB2 H 1.309 0.02 2 299 75 53 GLN HB3 H 1.225 0.02 2 300 75 53 GLN HG2 H 1.270 0.02 1 301 75 53 GLN HG3 H 0.990 0.02 1 302 75 53 GLN HE21 H 6.495 0.02 2 303 75 53 GLN HE22 H 6.600 0.02 2 304 76 54 GLU H H 7.872 0.02 1 305 76 54 GLU HA H 3.890 0.02 1 306 76 54 GLU HB2 H 2.111 0.02 1 307 76 54 GLU HB3 H 2.030 0.02 1 308 76 54 GLU HG2 H 2.300 0.02 1 309 76 54 GLU HG3 H 2.300 0.02 1 310 77 55 SER H H 7.399 0.02 1 311 77 55 SER HA H 4.470 0.02 1 312 77 55 SER HB2 H 4.021 0.02 2 313 77 55 SER HB3 H 3.891 0.02 2 314 78 56 GLY H H 7.756 0.02 1 315 78 56 GLY HA2 H 3.750 0.02 1 316 78 56 GLY HA3 H 4.080 0.02 1 317 79 57 SER H H 7.826 0.02 1 318 79 57 SER HA H 4.801 0.02 1 319 79 57 SER HB2 H 3.487 0.02 1 320 79 57 SER HB3 H 3.646 0.02 1 321 80 58 PRO HA H 4.406 0.02 1 322 80 58 PRO HB2 H 2.181 0.02 1 323 80 58 PRO HB3 H 2.391 0.02 1 324 80 58 PRO HG2 H 1.971 0.02 2 325 80 58 PRO HG3 H 2.070 0.02 2 326 80 58 PRO HD2 H 3.781 0.02 2 327 80 58 PRO HD3 H 3.685 0.02 2 328 81 59 ILE H H 7.063 0.02 1 329 81 59 ILE HA H 4.297 0.02 1 330 81 59 ILE HB H 2.037 0.02 1 331 81 59 ILE HG2 H 0.652 0.02 1 332 81 59 ILE HG12 H 1.450 0.02 2 333 81 59 ILE HG13 H 0.629 0.02 2 334 81 59 ILE HD1 H 0.863 0.02 1 335 82 60 ASP H H 7.378 0.02 1 336 82 60 ASP HA H 4.788 0.02 1 337 82 60 ASP HB2 H 2.988 0.02 2 338 82 60 ASP HB3 H 2.804 0.02 2 339 83 61 LEU H H 8.338 0.02 1 340 83 61 LEU HA H 3.924 0.02 1 341 83 61 LEU HB2 H 1.596 0.02 1 342 83 61 LEU HB3 H 1.700 0.02 1 343 83 61 LEU HG H 1.390 0.02 1 344 83 61 LEU HD1 H 0.813 0.02 1 345 83 61 LEU HD2 H 0.493 0.02 1 346 84 62 ILE H H 7.573 0.02 1 347 84 62 ILE HA H 3.779 0.02 1 348 84 62 ILE HB H 2.010 0.02 1 349 84 62 ILE HG2 H 0.890 0.02 1 350 84 62 ILE HG12 H 1.621 0.02 2 351 84 62 ILE HG13 H 1.407 0.02 2 352 84 62 ILE HD1 H 0.900 0.02 1 353 85 63 THR H H 7.937 0.02 1 354 85 63 THR HA H 3.733 0.02 1 355 85 63 THR HB H 3.687 0.02 1 356 85 63 THR HG2 H 1.140 0.02 1 357 86 64 LEU H H 8.564 0.02 1 358 86 64 LEU HA H 3.846 0.02 1 359 86 64 LEU HB2 H 1.260 0.02 1 360 86 64 LEU HB3 H 1.700 0.02 1 361 86 64 LEU HG H 1.376 0.02 1 362 86 64 LEU HD1 H 0.764 0.02 1 363 86 64 LEU HD2 H 0.817 0.02 1 364 87 65 ALA H H 8.583 0.02 1 365 87 65 ALA HA H 3.782 0.02 1 366 87 65 ALA HB H 1.519 0.02 1 367 88 66 GLU H H 8.418 0.02 1 368 88 66 GLU HA H 3.984 0.02 1 369 88 66 GLU HB2 H 2.161 0.02 1 370 88 66 GLU HB3 H 2.040 0.02 1 371 88 66 GLU HG2 H 2.161 0.02 2 372 88 66 GLU HG3 H 2.500 0.02 2 373 89 67 SER H H 8.005 0.02 1 374 89 67 SER HA H 4.100 0.02 1 375 89 67 SER HB2 H 3.921 0.02 1 376 89 67 SER HB3 H 4.060 0.02 1 377 90 68 LEU H H 8.394 0.02 1 378 90 68 LEU HA H 3.863 0.02 1 379 90 68 LEU HB2 H 1.971 0.02 1 380 90 68 LEU HB3 H 0.800 0.02 1 381 90 68 LEU HG H 1.740 0.02 1 382 90 68 LEU HD1 H 0.771 0.02 1 383 90 68 LEU HD2 H 0.685 0.02 1 384 91 69 GLU H H 8.832 0.02 1 385 91 69 GLU HA H 4.120 0.02 1 386 91 69 GLU HB2 H 1.881 0.02 2 387 91 69 GLU HB3 H 1.975 0.02 2 388 91 69 GLU HG2 H 2.220 0.02 1 389 91 69 GLU HG3 H 2.220 0.02 1 390 92 70 ARG H H 8.380 0.02 1 391 92 70 ARG HA H 4.111 0.02 1 392 92 70 ARG HB2 H 1.971 0.02 2 393 92 70 ARG HB3 H 2.060 0.02 2 394 92 70 ARG HG2 H 1.740 0.02 2 395 92 70 ARG HG3 H 1.810 0.02 2 396 92 70 ARG HD2 H 3.220 0.02 1 397 92 70 ARG HD3 H 3.220 0.02 1 398 93 71 GLN H H 7.324 0.02 1 399 93 71 GLN HA H 4.354 0.02 1 400 93 71 GLN HB2 H 1.811 0.02 1 401 93 71 GLN HB3 H 2.401 0.02 1 402 93 71 GLN HG2 H 2.237 0.02 2 403 93 71 GLN HG3 H 2.521 0.02 2 404 93 71 GLN HE21 H 6.972 0.02 2 405 93 71 GLN HE22 H 6.790 0.02 2 406 94 72 GLY H H 8.138 0.02 1 407 94 72 GLY HA2 H 4.061 0.02 1 408 94 72 GLY HA3 H 4.061 0.02 1 409 95 73 GLN H H 8.160 0.02 1 410 95 73 GLN HA H 4.600 0.02 1 411 95 73 GLN HB2 H 1.515 0.02 1 412 95 73 GLN HB3 H 2.260 0.02 1 413 95 73 GLN HG2 H 2.250 0.02 2 414 95 73 GLN HG3 H 2.181 0.02 2 415 95 73 GLN HE21 H 6.495 0.02 2 416 95 73 GLN HE22 H 7.120 0.02 2 417 96 74 LEU H H 7.679 0.02 1 418 96 74 LEU HA H 3.953 0.02 1 419 96 74 LEU HB2 H 1.177 0.02 1 420 96 74 LEU HB3 H 1.980 0.02 1 421 96 74 LEU HG H 1.570 0.02 1 422 96 74 LEU HD1 H 0.851 0.02 1 423 96 74 LEU HD2 H 1.005 0.02 1 424 97 75 ASP H H 8.527 0.02 1 425 97 75 ASP HA H 4.278 0.02 1 426 97 75 ASP HB2 H 2.587 0.02 1 427 97 75 ASP HB3 H 2.590 0.02 1 428 98 76 SER H H 7.812 0.02 1 429 98 76 SER HA H 4.204 0.02 1 430 98 76 SER HB2 H 3.847 0.02 1 431 98 76 SER HB3 H 3.837 0.02 1 432 99 77 VAL H H 7.102 0.02 1 433 99 77 VAL HA H 4.439 0.02 1 434 99 77 VAL HB H 2.580 0.02 1 435 99 77 VAL HG1 H 0.868 0.02 1 436 99 77 VAL HG2 H 1.003 0.02 1 437 100 78 GLY H H 7.376 0.02 1 438 100 78 GLY HA2 H 4.330 0.02 2 439 100 78 GLY HA3 H 3.531 0.02 2 440 101 79 GLY H H 7.947 0.02 1 441 101 79 GLY HA2 H 4.411 0.02 2 442 101 79 GLY HA3 H 3.676 0.02 2 443 102 80 PHE HA H 3.736 0.02 1 444 102 80 PHE HB2 H 3.079 0.02 1 445 102 80 PHE HB3 H 2.909 0.02 1 446 102 80 PHE HD1 H 6.960 0.02 1 447 102 80 PHE HD2 H 6.960 0.02 1 448 102 80 PHE HE1 H 7.124 0.02 1 449 102 80 PHE HE2 H 7.124 0.02 1 450 102 80 PHE HZ H 7.101 0.02 1 451 103 81 ALA H H 8.912 0.02 1 452 103 81 ALA HA H 3.950 0.02 1 453 103 81 ALA HB H 1.491 0.02 1 454 104 82 TYR H H 7.136 0.02 1 455 104 82 TYR HA H 4.350 0.02 1 456 104 82 TYR HB2 H 3.155 0.02 1 457 104 82 TYR HB3 H 2.764 0.02 1 458 104 82 TYR HD1 H 7.187 0.02 1 459 104 82 TYR HD2 H 7.187 0.02 1 460 104 82 TYR HE1 H 6.690 0.02 1 461 104 82 TYR HE2 H 6.690 0.02 1 462 105 83 LEU H H 7.023 0.02 1 463 105 83 LEU HA H 3.540 0.02 1 464 105 83 LEU HB2 H 1.514 0.02 1 465 105 83 LEU HB3 H 1.042 0.02 1 466 105 83 LEU HG H 1.671 0.02 1 467 105 83 LEU HD1 H 0.661 0.02 1 468 105 83 LEU HD2 H 0.651 0.02 1 469 106 84 ALA H H 8.423 0.02 1 470 106 84 ALA HA H 3.657 0.02 1 471 106 84 ALA HB H 1.026 0.02 1 472 107 85 GLU H H 7.659 0.02 1 473 107 85 GLU HA H 3.805 0.02 1 474 107 85 GLU HB2 H 2.061 0.02 1 475 107 85 GLU HB3 H 1.990 0.02 1 476 107 85 GLU HG2 H 2.121 0.02 2 477 107 85 GLU HG3 H 2.181 0.02 2 478 108 86 LEU H H 7.757 0.02 1 479 108 86 LEU HA H 3.664 0.02 1 480 108 86 LEU HB2 H 1.860 0.02 1 481 108 86 LEU HB3 H 0.889 0.02 1 482 108 86 LEU HG H 1.313 0.02 1 483 108 86 LEU HD1 H 0.601 0.02 1 484 108 86 LEU HD2 H 0.669 0.02 1 485 109 87 SER H H 7.520 0.02 1 486 109 87 SER HA H 4.170 0.02 1 487 109 87 SER HB2 H 3.920 0.02 1 488 109 87 SER HB3 H 3.942 0.02 1 489 110 88 LYS H H 7.636 0.02 1 490 110 88 LYS HA H 4.088 0.02 1 491 110 88 LYS HB2 H 1.784 0.02 2 492 110 88 LYS HB3 H 1.771 0.02 2 493 110 88 LYS HG2 H 1.471 0.02 2 494 110 88 LYS HG3 H 1.401 0.02 2 495 110 88 LYS HD2 H 1.584 0.02 2 496 110 88 LYS HD3 H 1.570 0.02 2 497 110 88 LYS HE2 H 2.855 0.02 2 498 110 88 LYS HE3 H 2.835 0.02 2 499 111 89 ASN H H 7.744 0.02 1 500 111 89 ASN HA H 4.627 0.02 1 501 111 89 ASN HB2 H 2.735 0.02 1 502 111 89 ASN HB3 H 2.762 0.02 1 503 111 89 ASN HD21 H 7.410 0.02 1 504 111 89 ASN HD22 H 6.972 0.02 1 505 112 90 THR H H 7.483 0.02 1 506 112 90 THR HA H 4.532 0.02 1 507 112 90 THR HB H 4.049 0.02 1 508 112 90 THR HG2 H 1.103 0.02 1 509 113 91 PRO HA H 4.517 0.02 1 510 113 91 PRO HB2 H 1.980 0.02 2 511 113 91 PRO HB3 H 2.288 0.02 2 512 113 91 PRO HG2 H 1.961 0.02 1 513 113 91 PRO HG3 H 1.961 0.02 1 514 113 91 PRO HD2 H 3.682 0.02 1 515 113 91 PRO HD3 H 3.682 0.02 1 516 114 92 SER H H 7.966 0.02 1 517 114 92 SER HA H 4.396 0.02 1 518 114 92 SER HB2 H 4.020 0.02 2 519 114 92 SER HB3 H 3.840 0.02 2 520 115 93 ALA H H 8.794 0.02 1 521 115 93 ALA HA H 4.370 0.02 1 522 115 93 ALA HB H 1.448 0.02 1 523 116 94 ALA H H 8.090 0.02 1 524 116 94 ALA HA H 4.099 0.02 1 525 116 94 ALA HB H 1.325 0.02 1 526 117 95 ASN H H 8.216 0.02 1 527 117 95 ASN HA H 4.773 0.02 1 528 117 95 ASN HB2 H 2.657 0.02 2 529 117 95 ASN HB3 H 2.728 0.02 2 530 117 95 ASN HD21 H 7.347 0.02 2 531 117 95 ASN HD22 H 6.840 0.02 2 532 118 96 ILE H H 8.001 0.02 1 533 118 96 ILE HA H 3.897 0.02 1 534 118 96 ILE HB H 2.043 0.02 1 535 118 96 ILE HG2 H 0.971 0.02 1 536 118 96 ILE HG12 H 1.204 0.02 2 537 118 96 ILE HG13 H 1.660 0.02 2 538 118 96 ILE HD1 H 0.958 0.02 1 539 119 97 SER H H 8.109 0.02 1 540 119 97 SER HA H 3.794 0.02 1 541 119 97 SER HB2 H 3.713 0.02 2 542 119 97 SER HB3 H 3.649 0.02 2 543 120 98 ALA H H 7.202 0.02 1 544 120 98 ALA HA H 4.094 0.02 1 545 120 98 ALA HB H 1.222 0.02 1 546 121 99 TYR H H 7.697 0.02 1 547 121 99 TYR HA H 4.383 0.02 1 548 121 99 TYR HB2 H 2.830 0.02 2 549 121 99 TYR HB3 H 3.241 0.02 2 550 121 99 TYR HD1 H 6.950 0.02 1 551 121 99 TYR HD2 H 6.950 0.02 1 552 121 99 TYR HE1 H 6.778 0.02 1 553 121 99 TYR HE2 H 6.778 0.02 1 554 122 100 ALA H H 8.277 0.02 1 555 122 100 ALA HA H 3.703 0.02 1 556 122 100 ALA HB H 1.419 0.02 1 557 123 101 ASP H H 7.987 0.02 1 558 123 101 ASP HA H 4.350 0.02 1 559 123 101 ASP HB2 H 2.840 0.02 1 560 123 101 ASP HB3 H 2.580 0.02 1 561 124 102 ILE H H 7.402 0.02 1 562 124 102 ILE HA H 3.747 0.02 1 563 124 102 ILE HB H 2.123 0.02 1 564 124 102 ILE HG2 H 0.849 0.02 1 565 124 102 ILE HG12 H 1.066 0.02 1 566 124 102 ILE HG13 H 1.777 0.02 1 567 124 102 ILE HD1 H 0.827 0.02 1 568 125 103 VAL H H 7.729 0.02 1 569 125 103 VAL HA H 3.368 0.02 1 570 125 103 VAL HB H 1.975 0.02 1 571 125 103 VAL HG1 H 0.005 0.02 1 572 125 103 VAL HG2 H 0.849 0.02 1 573 126 104 ARG H H 8.029 0.02 1 574 126 104 ARG HA H 3.797 0.02 1 575 126 104 ARG HB2 H 2.101 0.02 1 576 126 104 ARG HB3 H 1.918 0.02 1 577 126 104 ARG HG2 H 1.553 0.02 2 578 126 104 ARG HG3 H 1.662 0.02 2 579 126 104 ARG HD2 H 3.258 0.02 2 580 126 104 ARG HD3 H 3.329 0.02 2 581 127 105 GLU H H 8.495 0.02 1 582 127 105 GLU HA H 3.904 0.02 1 583 127 105 GLU HB2 H 2.091 0.02 1 584 127 105 GLU HB3 H 2.151 0.02 1 585 127 105 GLU HG2 H 2.201 0.02 2 586 127 105 GLU HG3 H 2.367 0.02 2 587 128 106 ARG H H 8.566 0.02 1 588 128 106 ARG HA H 3.974 0.02 1 589 128 106 ARG HB2 H 1.862 0.02 1 590 128 106 ARG HB3 H 1.520 0.02 1 591 128 106 ARG HG2 H 1.307 0.02 2 592 128 106 ARG HG3 H 2.013 0.02 2 593 128 106 ARG HD2 H 2.932 0.02 2 594 128 106 ARG HD3 H 2.851 0.02 2 595 129 107 ALA H H 7.566 0.02 1 596 129 107 ALA HA H 3.966 0.02 1 597 129 107 ALA HB H 1.688 0.02 1 598 130 108 VAL H H 7.995 0.02 1 599 130 108 VAL HA H 3.649 0.02 1 600 130 108 VAL HB H 2.207 0.02 1 601 130 108 VAL HG1 H 0.901 0.02 1 602 130 108 VAL HG2 H 1.006 0.02 1 603 131 109 VAL H H 7.481 0.02 1 604 131 109 VAL HA H 3.789 0.02 1 605 131 109 VAL HB H 2.102 0.02 1 606 131 109 VAL HG1 H 0.972 0.02 1 607 131 109 VAL HG2 H 1.031 0.02 1 608 132 110 ARG H H 8.204 0.02 1 609 132 110 ARG HA H 3.991 0.02 1 610 132 110 ARG HB2 H 1.998 0.02 2 611 132 110 ARG HB3 H 2.145 0.02 2 612 132 110 ARG HG2 H 1.490 0.02 2 613 132 110 ARG HG3 H 2.010 0.02 2 614 132 110 ARG HD2 H 3.350 0.02 1 615 132 110 ARG HD3 H 3.350 0.02 1 616 133 111 GLU H H 7.822 0.02 1 617 133 111 GLU HA H 4.198 0.02 1 618 133 111 GLU HB2 H 2.151 0.02 1 619 133 111 GLU HB3 H 2.021 0.02 1 620 133 111 GLU HG2 H 2.381 0.02 2 621 133 111 GLU HG3 H 2.300 0.02 2 622 134 112 MET H H 7.763 0.02 1 623 134 112 MET HA H 4.379 0.02 1 624 134 112 MET HB2 H 2.151 0.02 1 625 134 112 MET HB3 H 2.151 0.02 1 626 134 112 MET HG2 H 2.591 0.02 2 627 134 112 MET HG3 H 2.714 0.02 2 628 135 113 ILE H H 7.917 0.02 1 629 135 113 ILE HA H 4.264 0.02 1 630 135 113 ILE HB H 1.814 0.02 1 631 135 113 ILE HG2 H 0.770 0.02 1 632 135 113 ILE HG12 H 1.383 0.02 2 633 135 113 ILE HG13 H 1.144 0.02 2 634 135 113 ILE HD1 H 0.823 0.02 1 635 136 114 SER H H 7.752 0.02 1 636 136 114 SER HA H 4.271 0.02 1 637 136 114 SER HB2 H 3.908 0.02 2 638 136 114 SER HB3 H 3.833 0.02 2 stop_ save_