data_5122 ####################### # 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 5122 _BMRB_flat_file_name bmr5122.str _Entry_type original _Submission_date 2001-08-23 _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" 687 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-08 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4297 'DnaB(24-136) recorded at different conditions' 5121 'N-terminal domain of DnaB(24-136) helicase' stop_ _Original_release_date 2001-08-24 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_cz-DnaB-N(24-136) _Saveframe_category molecular_system _Mol_system_name 'cyclic N-terminal domain of DnaB helicase' _Abbreviation_common cz-DnaB-N(24-136) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cz-DnaB-N(24-136) $cz-DnaB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details 'cz-DnaB is cyclized DnaB(24-136) with extra 8 amino acid residues.' save_ ######################## # Monomeric polymers # ######################## save_cz-DnaB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal Domain of E. coli DnaB Helicase' _Name_variant 'cyclic DnaB Helicase' _Abbreviation_common cz-DnaB _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; KVPPHSIEAEQSVLGGLMLD NERWDDVAERVVADDFYTRP HRHIFTEMARLQESGSPIDL ITLAESLERQGQLDSVGGFA YLAELSKNTPSAANISAYAD IVRERAVVREMISTRESGSI EF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 LYS 2 25 VAL 3 26 PRO 4 27 PRO 5 28 HIS 6 29 SER 7 30 ILE 8 31 GLU 9 32 ALA 10 33 GLU 11 34 GLN 12 35 SER 13 36 VAL 14 37 LEU 15 38 GLY 16 39 GLY 17 40 LEU 18 41 MET 19 42 LEU 20 43 ASP 21 44 ASN 22 45 GLU 23 46 ARG 24 47 TRP 25 48 ASP 26 49 ASP 27 50 VAL 28 51 ALA 29 52 GLU 30 53 ARG 31 54 VAL 32 55 VAL 33 56 ALA 34 57 ASP 35 58 ASP 36 59 PHE 37 60 TYR 38 61 THR 39 62 ARG 40 63 PRO 41 64 HIS 42 65 ARG 43 66 HIS 44 67 ILE 45 68 PHE 46 69 THR 47 70 GLU 48 71 MET 49 72 ALA 50 73 ARG 51 74 LEU 52 75 GLN 53 76 GLU 54 77 SER 55 78 GLY 56 79 SER 57 80 PRO 58 81 ILE 59 82 ASP 60 83 LEU 61 84 ILE 62 85 THR 63 86 LEU 64 87 ALA 65 88 GLU 66 89 SER 67 90 LEU 68 91 GLU 69 92 ARG 70 93 GLN 71 94 GLY 72 95 GLN 73 96 LEU 74 97 ASP 75 98 SER 76 99 VAL 77 100 GLY 78 101 GLY 79 102 PHE 80 103 ALA 81 104 TYR 82 105 LEU 83 106 ALA 84 107 GLU 85 108 LEU 86 109 SER 87 110 LYS 88 111 ASN 89 112 THR 90 113 PRO 91 114 SER 92 115 ALA 93 116 ALA 94 117 ASN 95 118 ILE 96 119 SER 97 120 ALA 98 121 TYR 99 122 ALA 100 123 ASP 101 124 ILE 102 125 VAL 103 126 ARG 104 127 GLU 105 128 ARG 106 129 ALA 107 130 VAL 108 131 VAL 109 132 ARG 110 133 GLU 111 134 MET 112 135 ILE 113 136 SER 114 137 THR 115 138 ARG 116 139 GLU 117 140 SER 118 141 GLY 119 142 SER 120 143 ILE 121 144 GLU 122 145 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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' 93.44 142 99.12 99.12 7.65e-60 BMRB 4297 'DnaB helicase' 92.62 114 100.00 100.00 1.12e-59 BMRB 5121 'N-terminal Domain of E. coli DnaB Helicase' 92.62 114 100.00 100.00 1.12e-59 PDB 1B79 'N-Terminal Domain Of Dna Replication Protein Dnab' 86.07 119 100.00 100.00 3.36e-55 PDB 1JWE 'Nmr Structure Of The N-Terminal Domain Of E. Coli Dnab Helicase' 92.62 114 100.00 100.00 1.12e-59 DBJ BAB38457 'replicative DNA helicase DnaB [Escherichia coli O157:H7 str. Sakai]' 93.44 471 98.25 99.12 1.25e-59 DBJ BAE78054 'replicative DNA helicase [Escherichia coli W3110]' 93.44 471 99.12 99.12 5.00e-60 DBJ BAG66812 'replicative DNA helicase [Escherichia coli O111:H-]' 93.44 471 99.12 99.12 5.00e-60 GenBank AAA23689 'DnaB replication protein (dnaB)' 93.44 471 99.12 99.12 5.00e-60 GenBank AAA23690 helicase 93.44 157 99.12 99.12 9.59e-60 GenBank AAC43146 'ORF_o471 [Escherichia coli]' 93.44 471 99.12 99.12 5.00e-60 GenBank AAC77022 'replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]' 93.44 471 99.12 99.12 5.00e-60 GenBank AAG59250 'replicative DNA helicase; part of primosome [Escherichia coli O157:H7 EDL933]' 93.44 471 98.25 99.12 1.25e-59 REF AP_004553 'replicative DNA helicase [Escherichia coli W3110]' 93.44 471 99.12 99.12 5.00e-60 REF NP_290685 'replicative DNA helicase [Escherichia coli O157:H7 EDL933]' 93.44 471 98.25 99.12 1.25e-59 REF NP_313061 'replicative DNA helicase [Escherichia coli O157:H7 str. Sakai]' 93.44 471 98.25 99.12 1.25e-59 REF NP_418476 'replicative DNA helicase [Escherichia coli str. K-12 substr. MG1655]' 93.44 471 99.12 99.12 5.00e-60 REF NP_709868 'replicative DNA helicase [Shigella flexneri 2a str. 301]' 93.44 471 99.12 99.12 5.00e-60 SWISS-PROT P0ACB0 'Replicative DNA helicase' 93.44 471 99.12 99.12 5.00e-60 SWISS-PROT P0ACB1 'Replicative DNA helicase' 93.44 471 99.12 99.12 5.00e-60 SWISS-PROT Q8FB22 'Replicative DNA helicase' 92.62 471 100.00 100.00 5.26e-60 SWISS-PROT Q8X5V3 'Replicative DNA helicase' 93.44 471 98.25 99.12 1.25e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cz-DnaB '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 $cz-DnaB '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 $cz-DnaB 2.1 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cz-DnaB 2.1 mM '[U-95% 15N]' 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_1H-15N_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.02 M pH* 7.0 0.1 n/a temperature 304 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 DSS H 1 'methyl protons' ppm 0.0 internal direct cylindrical internal parallel 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N TOCSY' NOESY TOCSY COSY stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name cz-DnaB-N(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 1 LYS HA H 4.219 0.02 1 2 24 1 LYS HB2 H 1.701 0.02 2 3 24 1 LYS HB3 H 1.795 0.02 2 4 24 1 LYS HG2 H 1.402 0.02 2 5 24 1 LYS HG3 H 1.357 0.02 2 6 24 1 LYS HD2 H 1.619 0.02 1 7 24 1 LYS HD3 H 1.619 0.02 1 8 24 1 LYS HE2 H 2.931 0.02 1 9 24 1 LYS HE3 H 2.931 0.02 1 10 25 2 VAL N N 119.7 0.2 1 11 25 2 VAL H H 7.793 0.02 1 12 25 2 VAL HA H 4.364 0.02 1 13 25 2 VAL HB H 1.986 0.02 1 14 25 2 VAL HG1 H 0.980 0.02 1 15 25 2 VAL HG2 H 0.917 0.02 1 16 26 3 PRO HA H 4.470 0.02 1 17 26 3 PRO HB2 H 1.548 0.02 2 18 26 3 PRO HB3 H 2.215 0.02 2 19 26 3 PRO HG2 H 1.989 0.02 2 20 26 3 PRO HG3 H 2.107 0.02 2 21 26 3 PRO HD2 H 3.597 0.02 2 22 26 3 PRO HD3 H 3.919 0.02 2 23 27 4 PRO HA H 4.363 0.02 1 24 27 4 PRO HB2 H 1.943 0.02 2 25 27 4 PRO HB3 H 2.134 0.02 2 26 27 4 PRO HG2 H 1.904 0.02 2 27 27 4 PRO HG3 H 1.983 0.02 2 28 27 4 PRO HD2 H 3.240 0.02 2 29 27 4 PRO HD3 H 3.678 0.02 2 30 28 5 HIS N N 116.3 0.2 1 31 28 5 HIS H H 7.914 0.02 1 32 28 5 HIS HA H 4.144 0.02 1 33 28 5 HIS HB2 H 2.576 0.02 2 34 28 5 HIS HB3 H 2.799 0.02 2 35 28 5 HIS HD2 H 6.388 0.02 1 36 28 5 HIS HE1 H 7.424 0.02 1 37 29 6 SER N N 116.7 0.2 1 38 29 6 SER H H 10.31 0.02 1 39 29 6 SER HA H 4.708 0.02 1 40 29 6 SER HB2 H 3.551 0.02 2 41 29 6 SER HB3 H 3.679 0.02 2 42 30 7 ILE N N 130.5 0.2 1 43 30 7 ILE H H 9.170 0.02 1 44 30 7 ILE HA H 3.981 0.02 1 45 30 7 ILE HB H 2.053 0.02 1 46 30 7 ILE HG2 H 1.002 0.02 1 47 30 7 ILE HG12 H 1.642 0.02 2 48 30 7 ILE HG13 H 1.708 0.02 2 49 30 7 ILE HD1 H 0.981 0.02 1 50 31 8 GLU N N 119.9 0.2 1 51 31 8 GLU H H 8.927 0.02 1 52 31 8 GLU HA H 4.084 0.02 1 53 31 8 GLU HB2 H 1.945 0.02 2 54 31 8 GLU HB3 H 1.873 0.02 2 55 31 8 GLU HG2 H 2.234 0.02 1 56 31 8 GLU HG3 H 2.234 0.02 1 57 32 9 ALA N N 122.8 0.2 1 58 32 9 ALA H H 8.004 0.02 1 59 32 9 ALA HA H 3.780 0.02 1 60 32 9 ALA HB H 1.626 0.02 1 61 33 10 GLU N N 115.9 0.2 1 62 33 10 GLU H H 7.891 0.02 1 63 33 10 GLU HA H 3.760 0.02 1 64 33 10 GLU HB2 H 2.454 0.02 2 65 33 10 GLU HB3 H 2.273 0.02 2 66 33 10 GLU HG2 H 3.294 0.02 2 67 33 10 GLU HG3 H 2.246 0.02 2 68 34 11 GLN N N 115.2 0.2 1 69 34 11 GLN H H 8.677 0.02 1 70 34 11 GLN HA H 3.539 0.02 1 71 34 11 GLN HB2 H 2.277 0.02 1 72 34 11 GLN HB3 H 1.797 0.02 1 73 34 11 GLN HG2 H 2.229 0.02 1 74 34 11 GLN HG3 H 3.000 0.02 1 75 34 11 GLN NE2 N 111.3 0.2 1 76 34 11 GLN HE21 H 7.153 0.02 2 77 34 11 GLN HE22 H 7.800 0.02 2 78 35 12 SER N N 114.8 0.2 1 79 35 12 SER H H 7.847 0.02 1 80 35 12 SER HA H 4.119 0.02 1 81 35 12 SER HB2 H 3.234 0.02 1 82 35 12 SER HB3 H 3.114 0.02 1 83 36 13 VAL N N 121.7 0.2 1 84 36 13 VAL H H 7.984 0.02 1 85 36 13 VAL HA H 3.647 0.02 1 86 36 13 VAL HB H 2.251 0.02 1 87 36 13 VAL HG1 H 1.033 0.02 1 88 36 13 VAL HG2 H 1.052 0.02 1 89 37 14 LEU N N 116.3 0.2 1 90 37 14 LEU H H 7.678 0.02 1 91 37 14 LEU HA H 4.027 0.02 1 92 37 14 LEU HB2 H 1.708 0.02 1 93 37 14 LEU HB3 H 1.036 0.02 1 94 37 14 LEU HG H 1.983 0.02 1 95 37 14 LEU HD1 H 0.425 0.02 1 96 37 14 LEU HD2 H 0.779 0.02 1 97 38 15 GLY N N 104.8 0.2 1 98 38 15 GLY H H 8.803 0.02 1 99 38 15 GLY HA2 H 3.479 0.02 1 100 38 15 GLY HA3 H 3.858 0.02 1 101 39 16 GLY N N 108.6 0.2 1 102 39 16 GLY H H 8.030 0.02 1 103 39 16 GLY HA2 H 3.739 0.02 1 104 39 16 GLY HA3 H 3.739 0.02 1 105 40 17 LEU N N 122.2 0.2 1 106 40 17 LEU H H 7.912 0.02 1 107 40 17 LEU HA H 4.126 0.02 1 108 40 17 LEU HB2 H 2.115 0.02 1 109 40 17 LEU HB3 H 1.467 0.02 1 110 40 17 LEU HG H 2.043 0.02 1 111 40 17 LEU HD1 H 1.170 0.02 1 112 40 17 LEU HD2 H 0.962 0.02 1 113 41 18 MET N N 115.6 0.2 1 114 41 18 MET H H 7.272 0.02 1 115 41 18 MET HA H 4.183 0.02 1 116 41 18 MET HB2 H 2.243 0.02 1 117 41 18 MET HB3 H 1.919 0.02 1 118 41 18 MET HG2 H 2.642 0.02 1 119 41 18 MET HG3 H 2.604 0.02 1 120 41 18 MET HE H 1.855 0.02 1 121 42 19 LEU N N 118.2 0.2 1 122 42 19 LEU H H 7.271 0.02 1 123 42 19 LEU HA H 4.208 0.02 1 124 42 19 LEU HB2 H 1.801 0.02 2 125 42 19 LEU HB3 H 1.687 0.02 2 126 42 19 LEU HG H 1.724 0.02 1 127 42 19 LEU HD1 H 0.916 0.02 1 128 42 19 LEU HD2 H 0.878 0.02 1 129 43 20 ASP N N 119.5 0.2 1 130 43 20 ASP H H 8.079 0.02 1 131 43 20 ASP HA H 4.897 0.02 1 132 43 20 ASP HB2 H 2.346 0.02 1 133 43 20 ASP HB3 H 2.863 0.02 1 134 44 21 ASN N N 120.8 0.2 1 135 44 21 ASN H H 9.080 0.02 1 136 44 21 ASN HA H 4.525 0.02 1 137 44 21 ASN HB2 H 2.885 0.02 1 138 44 21 ASN HB3 H 2.886 0.02 1 139 44 21 ASN ND2 N 115.3 0.2 1 140 44 21 ASN HD21 H 6.074 0.02 2 141 44 21 ASN HD22 H 8.094 0.02 2 142 45 22 GLU N N 116.7 0.2 1 143 45 22 GLU H H 8.313 0.02 1 144 45 22 GLU HA H 4.235 0.02 1 145 45 22 GLU HB2 H 2.239 0.02 1 146 45 22 GLU HB3 H 2.214 0.02 1 147 45 22 GLU HG2 H 2.348 0.02 2 148 45 22 GLU HG3 H 2.423 0.02 2 149 46 23 ARG N N 116.9 0.2 1 150 46 23 ARG H H 7.572 0.02 1 151 46 23 ARG HA H 4.484 0.02 1 152 46 23 ARG HB2 H 1.963 0.02 1 153 46 23 ARG HB3 H 2.194 0.02 1 154 46 23 ARG HG2 H 1.724 0.02 2 155 46 23 ARG HG3 H 1.764 0.02 2 156 46 23 ARG HD2 H 3.222 0.02 1 157 46 23 ARG HD3 H 3.222 0.02 1 158 46 23 ARG HE H 7.592 0.02 1 159 47 24 TRP N N 119.5 0.2 1 160 47 24 TRP H H 7.686 0.02 1 161 47 24 TRP HA H 3.960 0.02 1 162 47 24 TRP HB2 H 3.330 0.02 1 163 47 24 TRP HB3 H 3.104 0.02 1 164 47 24 TRP HD1 H 7.019 0.02 1 165 47 24 TRP NE1 N 128.9 0.2 1 166 47 24 TRP HE1 H 9.761 0.02 1 167 47 24 TRP HE3 H 7.206 0.02 1 168 47 24 TRP HZ2 H 7.134 0.02 1 169 47 24 TRP HZ3 H 6.379 0.02 1 170 47 24 TRP HH2 H 5.868 0.02 1 171 48 25 ASP N N 115.7 0.2 1 172 48 25 ASP H H 8.319 0.02 1 173 48 25 ASP HA H 4.032 0.02 1 174 48 25 ASP HB2 H 2.655 0.02 1 175 48 25 ASP HB3 H 2.599 0.02 1 176 49 26 ASP N N 117.8 0.2 1 177 49 26 ASP H H 7.762 0.02 1 178 49 26 ASP HA H 4.217 0.02 1 179 49 26 ASP HB2 H 2.703 0.02 2 180 49 26 ASP HB3 H 2.536 0.02 2 181 50 27 VAL N N 118.4 0.2 1 182 50 27 VAL H H 7.572 0.02 1 183 50 27 VAL HA H 3.329 0.02 1 184 50 27 VAL HB H 1.843 0.02 1 185 50 27 VAL HG1 H 0.758 0.02 1 186 50 27 VAL HG2 H 0.860 0.02 1 187 51 28 ALA N N 122.0 0.2 1 188 51 28 ALA H H 8.755 0.02 1 189 51 28 ALA HA H 4.018 0.02 1 190 51 28 ALA HB H 0.782 0.02 1 191 52 29 GLU N N 113.9 0.2 1 192 52 29 GLU H H 7.149 0.02 1 193 52 29 GLU HA H 4.183 0.02 1 194 52 29 GLU HB2 H 2.024 0.02 1 195 52 29 GLU HB3 H 2.024 0.02 1 196 52 29 GLU HG2 H 2.283 0.02 2 197 52 29 GLU HG3 H 2.336 0.02 2 198 53 30 ARG N N 118.4 0.2 1 199 53 30 ARG H H 7.807 0.02 1 200 53 30 ARG HA H 4.254 0.02 1 201 53 30 ARG HB2 H 1.625 0.02 2 202 53 30 ARG HB3 H 1.559 0.02 2 203 54 31 VAL N N 112.5 0.2 1 204 54 31 VAL H H 7.605 0.02 1 205 54 31 VAL HA H 4.767 0.02 1 206 54 31 VAL HB H 1.828 0.02 1 207 54 31 VAL HG1 H 0.547 0.02 1 208 54 31 VAL HG2 H 0.530 0.02 1 209 55 32 VAL N N 113.3 0.2 1 210 55 32 VAL H H 8.279 0.02 1 211 55 32 VAL HA H 4.634 0.02 1 212 55 32 VAL HB H 2.413 0.02 1 213 55 32 VAL HG1 H 0.924 0.02 1 214 55 32 VAL HG2 H 0.724 0.02 1 215 56 33 ALA N N 123.8 0.2 1 216 56 33 ALA H H 8.975 0.02 1 217 56 33 ALA HA H 3.915 0.02 1 218 56 33 ALA HB H 1.591 0.02 1 219 57 34 ASP N N 110.8 0.2 1 220 57 34 ASP H H 8.028 0.02 1 221 57 34 ASP HA H 4.314 0.02 1 222 57 34 ASP HB2 H 2.346 0.02 1 223 57 34 ASP HB3 H 2.688 0.02 1 224 58 35 ASP N N 117.4 0.2 1 225 58 35 ASP H H 7.917 0.02 1 226 58 35 ASP HA H 4.242 0.02 1 227 58 35 ASP HB2 H 2.540 0.02 1 228 58 35 ASP HB3 H 2.158 0.02 1 229 59 36 PHE N N 121.3 0.2 1 230 59 36 PHE H H 7.848 0.02 1 231 59 36 PHE HA H 3.980 0.02 1 232 59 36 PHE HB2 H 3.167 0.02 1 233 59 36 PHE HB3 H 2.872 0.02 1 234 59 36 PHE HD1 H 7.396 0.02 1 235 59 36 PHE HD2 H 7.396 0.02 1 236 59 36 PHE HE1 H 6.382 0.02 1 237 59 36 PHE HE2 H 6.382 0.02 1 238 59 36 PHE HZ H 6.574 0.02 1 239 60 37 TYR N N 127.9 0.2 1 240 60 37 TYR H H 11.958 0.02 1 241 60 37 TYR HA H 4.176 0.02 1 242 60 37 TYR HB2 H 3.022 0.02 1 243 60 37 TYR HB3 H 2.970 0.02 1 244 60 37 TYR HD1 H 6.496 0.02 1 245 60 37 TYR HD2 H 6.496 0.02 1 246 60 37 TYR HE1 H 6.374 0.02 1 247 60 37 TYR HE2 H 6.374 0.02 1 248 61 38 THR N N 108.5 0.2 1 249 61 38 THR H H 7.511 0.02 1 250 61 38 THR HA H 4.230 0.02 1 251 61 38 THR HB H 4.071 0.02 1 252 61 38 THR HG2 H 0.957 0.02 1 253 62 39 ARG N N 124.8 0.2 1 254 62 39 ARG H H 8.942 0.02 1 255 62 39 ARG HA H 3.874 0.02 1 256 62 39 ARG HB2 H 1.449 0.02 2 257 62 39 ARG HB3 H 1.809 0.02 2 258 62 39 ARG HD2 H 3.106 0.02 2 259 62 39 ARG HD3 H 3.142 0.02 2 260 63 40 PRO HA H 4.437 0.02 1 261 63 40 PRO HB2 H 1.526 0.02 1 262 63 40 PRO HB3 H 2.293 0.02 1 263 63 40 PRO HG2 H 1.805 0.02 2 264 63 40 PRO HG3 H 1.785 0.02 2 265 63 40 PRO HD2 H 3.597 0.02 2 266 63 40 PRO HD3 H 3.555 0.02 2 267 64 41 HIS N N 114.1 0.2 1 268 64 41 HIS H H 7.179 0.02 1 269 64 41 HIS HA H 4.307 0.02 1 270 64 41 HIS HB2 H 3.545 0.02 1 271 64 41 HIS HB3 H 3.013 0.02 1 272 64 41 HIS HD2 H 6.484 0.02 1 273 64 41 HIS HE1 H 7.654 0.02 1 274 64 41 HIS HD1 H 14.913 0.02 1 275 65 42 ARG N N 119.1 0.2 1 276 65 42 ARG H H 8.006 0.02 1 277 65 42 ARG HA H 3.860 0.02 1 278 65 42 ARG HB2 H 1.923 0.02 2 279 65 42 ARG HB3 H 1.776 0.02 2 280 65 42 ARG HG2 H 2.042 0.02 2 281 65 42 ARG HG3 H 1.774 0.02 2 282 65 42 ARG HD2 H 3.020 0.02 2 283 65 42 ARG HD3 H 3.233 0.02 2 284 66 43 HIS N N 119.6 0.2 1 285 66 43 HIS H H 8.184 0.02 1 286 66 43 HIS HA H 4.254 0.02 1 287 66 43 HIS HB2 H 3.044 0.02 2 288 66 43 HIS HB3 H 3.127 0.02 2 289 67 44 ILE N N 120.4 0.2 1 290 67 44 ILE H H 8.636 0.02 1 291 67 44 ILE HA H 3.433 0.02 1 292 67 44 ILE HB H 1.852 0.02 1 293 67 44 ILE HG2 H 0.931 0.02 1 294 67 44 ILE HG12 H 0.672 0.02 1 295 67 44 ILE HG13 H 2.217 0.02 1 296 67 44 ILE HD1 H 0.933 0.02 1 297 68 45 PHE N N 120.1 0.2 1 298 68 45 PHE H H 8.392 0.02 1 299 68 45 PHE HA H 3.985 0.02 1 300 68 45 PHE HB2 H 2.401 0.02 1 301 68 45 PHE HB3 H 2.647 0.02 1 302 68 45 PHE HD1 H 6.866 0.02 1 303 68 45 PHE HD2 H 6.866 0.02 1 304 68 45 PHE HE1 H 7.039 0.02 1 305 68 45 PHE HE2 H 7.039 0.02 1 306 68 45 PHE HZ H 6.693 0.02 1 307 69 46 THR N N 113.5 0.2 1 308 69 46 THR H H 8.185 0.02 1 309 69 46 THR HA H 3.908 0.02 1 310 69 46 THR HB H 4.294 0.02 1 311 69 46 THR HG2 H 1.215 0.02 1 312 69 46 THR HG1 H 5.122 0.02 1 313 70 47 GLU N N 123.4 0.2 1 314 70 47 GLU H H 7.900 0.02 1 315 70 47 GLU HA H 4.314 0.02 1 316 70 47 GLU HB2 H 1.864 0.02 1 317 70 47 GLU HB3 H 1.766 0.02 1 318 70 47 GLU HG2 H 2.047 0.02 2 319 70 47 GLU HG3 H 2.037 0.02 2 320 71 48 MET N N 119.6 0.2 1 321 71 48 MET H H 8.459 0.02 1 322 71 48 MET HA H 3.550 0.02 1 323 71 48 MET HB2 H 2.027 0.02 1 324 71 48 MET HB3 H 1.619 0.02 1 325 71 48 MET HG2 H 3.029 0.02 2 326 71 48 MET HG3 H 1.981 0.02 2 327 71 48 MET HE H 2.110 0.02 1 328 72 49 ALA N N 119.8 0.2 1 329 72 49 ALA H H 7.925 0.02 1 330 72 49 ALA HA H 3.315 0.02 1 331 72 49 ALA HB H 1.466 0.02 1 332 73 50 ARG N N 120.3 0.2 1 333 73 50 ARG H H 7.684 0.02 1 334 73 50 ARG HA H 3.852 0.02 1 335 73 50 ARG HB2 H 1.803 0.02 1 336 73 50 ARG HB3 H 1.781 0.02 1 337 73 50 ARG HG2 H 1.447 0.02 2 338 73 50 ARG HG3 H 1.644 0.02 2 339 73 50 ARG HD2 H 3.003 0.02 2 340 73 50 ARG HD3 H 3.201 0.02 2 341 74 51 LEU N N 122.3 0.2 1 342 74 51 LEU H H 8.367 0.02 1 343 74 51 LEU HA H 3.725 0.02 1 344 74 51 LEU HB2 H 1.684 0.02 1 345 74 51 LEU HB3 H 1.004 0.02 1 346 74 51 LEU HG H 1.713 0.02 1 347 74 51 LEU HD1 H 0.819 0.02 1 348 74 51 LEU HD2 H 0.722 0.02 1 349 75 52 GLN N N 120.5 0.2 1 350 75 52 GLN H H 8.358 0.02 1 351 75 52 GLN HA H 3.703 0.02 1 352 75 52 GLN HB2 H 1.307 0.02 2 353 75 52 GLN HB3 H 1.211 0.02 2 354 75 52 GLN HG2 H 1.269 0.02 1 355 75 52 GLN HG3 H 0.989 0.02 1 356 75 52 GLN NE2 N 109.5 0.2 1 357 75 52 GLN HE21 H 6.502 0.02 2 358 75 52 GLN HE22 H 6.595 0.02 2 359 76 53 GLU N N 120.8 0.2 1 360 76 53 GLU H H 7.865 0.02 1 361 76 53 GLU HA H 3.891 0.02 1 362 76 53 GLU HB2 H 2.103 0.02 1 363 76 53 GLU HB3 H 2.024 0.02 1 364 76 53 GLU HG2 H 2.285 0.02 2 365 76 53 GLU HG3 H 2.293 0.02 2 366 77 54 SER N N 112.0 0.2 1 367 77 54 SER H H 7.389 0.02 1 368 77 54 SER HA H 4.470 0.02 1 369 77 54 SER HB2 H 4.025 0.02 2 370 77 54 SER HB3 H 3.892 0.02 2 371 78 55 GLY N N 110.1 0.2 1 372 78 55 GLY H H 7.748 0.02 1 373 78 55 GLY HA2 H 3.745 0.02 1 374 78 55 GLY HA3 H 4.075 0.02 1 375 79 56 SER N N 117.2 0.2 1 376 79 56 SER H H 7.816 0.02 1 377 79 56 SER HA H 4.798 0.02 1 378 79 56 SER HB2 H 3.479 0.02 1 379 79 56 SER HB3 H 3.646 0.02 1 380 80 57 PRO HA H 4.410 0.02 1 381 80 57 PRO HB2 H 2.172 0.02 1 382 80 57 PRO HB3 H 2.387 0.02 1 383 80 57 PRO HG2 H 1.959 0.02 2 384 80 57 PRO HG3 H 2.073 0.02 2 385 80 57 PRO HD2 H 3.774 0.02 2 386 80 57 PRO HD3 H 3.688 0.02 2 387 81 58 ILE N N 109.0 0.2 1 388 81 58 ILE H H 7.051 0.02 1 389 81 58 ILE HA H 4.296 0.02 1 390 81 58 ILE HB H 2.030 0.02 1 391 81 58 ILE HG2 H 0.646 0.02 1 392 81 58 ILE HG12 H 1.440 0.02 2 393 81 58 ILE HG13 H 0.622 0.02 2 394 81 58 ILE HD1 H 0.845 0.02 1 395 82 59 ASP N N 114.1 0.2 1 396 82 59 ASP H H 7.374 0.02 1 397 82 59 ASP HA H 4.786 0.02 1 398 82 59 ASP HB2 H 2.987 0.02 2 399 82 59 ASP HB3 H 2.805 0.02 2 400 83 60 LEU N N 118.4 0.2 1 401 83 60 LEU H H 8.338 0.02 1 402 83 60 LEU HA H 3.920 0.02 1 403 83 60 LEU HB2 H 1.594 0.02 1 404 83 60 LEU HB3 H 1.710 0.02 1 405 83 60 LEU HG H 1.395 0.02 1 406 83 60 LEU HD1 H 0.806 0.02 1 407 83 60 LEU HD2 H 0.486 0.02 1 408 84 61 ILE N N 115.4 0.2 1 409 84 61 ILE H H 7.565 0.02 1 410 84 61 ILE HA H 3.777 0.02 1 411 84 61 ILE HB H 2.003 0.02 1 412 84 61 ILE HG2 H 0.883 0.02 1 413 84 61 ILE HG12 H 1.613 0.02 2 414 84 61 ILE HG13 H 1.396 0.02 2 415 84 61 ILE HD1 H 0.893 0.02 1 416 85 62 THR N N 119.3 0.2 1 417 85 62 THR H H 7.932 0.02 1 418 85 62 THR HA H 3.729 0.02 1 419 85 62 THR HB H 3.680 0.02 1 420 85 62 THR HG2 H 1.132 0.02 1 421 86 63 LEU N N 122.2 0.2 1 422 86 63 LEU H H 8.555 0.02 1 423 86 63 LEU HA H 3.838 0.02 1 424 86 63 LEU HB2 H 1.254 0.02 1 425 86 63 LEU HB3 H 1.693 0.02 1 426 86 63 LEU HG H 1.381 0.02 1 427 86 63 LEU HD1 H 0.757 0.02 1 428 86 63 LEU HD2 H 0.811 0.02 1 429 87 64 ALA N N 120.4 0.2 1 430 87 64 ALA H H 8.573 0.02 1 431 87 64 ALA HA H 3.775 0.02 1 432 87 64 ALA HB H 1.497 0.02 1 433 88 65 GLU N N 116.9 0.2 1 434 88 65 GLU H H 8.413 0.02 1 435 88 65 GLU HA H 3.977 0.02 1 436 88 65 GLU HB2 H 2.151 0.02 1 437 88 65 GLU HB3 H 2.033 0.02 1 438 88 65 GLU HG2 H 2.154 0.02 2 439 88 65 GLU HG3 H 2.516 0.02 2 440 89 66 SER N N 114.4 0.2 1 441 89 66 SER H H 7.998 0.02 1 442 89 66 SER HA H 4.101 0.02 1 443 89 66 SER HB2 H 3.913 0.02 1 444 89 66 SER HB3 H 4.053 0.02 1 445 90 67 LEU N N 118.6 0.2 1 446 90 67 LEU H H 8.385 0.02 1 447 90 67 LEU HA H 3.861 0.02 1 448 90 67 LEU HB2 H 1.950 0.02 1 449 90 67 LEU HB3 H 0.775 0.02 1 450 90 67 LEU HG H 1.733 0.02 1 451 90 67 LEU HD1 H 0.763 0.02 1 452 90 67 LEU HD2 H 0.677 0.02 1 453 91 68 GLU N N 122.5 0.2 1 454 91 68 GLU H H 8.811 0.02 1 455 91 68 GLU HA H 4.128 0.02 1 456 91 68 GLU HB2 H 1.853 0.02 2 457 91 68 GLU HB3 H 1.968 0.02 2 458 91 68 GLU HG2 H 2.213 0.02 1 459 91 68 GLU HG3 H 2.213 0.02 1 460 92 69 ARG N N 121.6 0.2 1 461 92 69 ARG H H 8.385 0.02 1 462 92 69 ARG HA H 4.103 0.02 1 463 92 69 ARG HB2 H 1.960 0.02 2 464 92 69 ARG HB3 H 2.058 0.02 2 465 92 69 ARG HG2 H 1.733 0.02 2 466 92 69 ARG HG3 H 1.808 0.02 2 467 92 69 ARG HD2 H 3.214 0.02 1 468 92 69 ARG HD3 H 3.214 0.02 1 469 93 70 GLN N N 114.3 0.2 1 470 93 70 GLN H H 7.316 0.02 1 471 93 70 GLN HA H 4.353 0.02 1 472 93 70 GLN HB2 H 1.804 0.02 1 473 93 70 GLN HB3 H 2.392 0.02 1 474 93 70 GLN HG2 H 2.234 0.02 2 475 93 70 GLN HG3 H 2.514 0.02 2 476 93 70 GLN NE2 N 111.6 0.2 1 477 93 70 GLN HE21 H 6.962 0.02 2 478 93 70 GLN HE22 H 6.782 0.02 2 479 94 71 GLY N N 109.5 0.2 1 480 94 71 GLY H H 8.134 0.02 1 481 94 71 GLY HA2 H 4.054 0.02 1 482 94 71 GLY HA3 H 4.054 0.02 1 483 95 72 GLN N N 115.4 0.2 1 484 95 72 GLN H H 8.157 0.02 1 485 95 72 GLN HA H 4.600 0.02 1 486 95 72 GLN HB2 H 1.508 0.02 1 487 95 72 GLN HB3 H 2.260 0.02 1 488 95 72 GLN HG2 H 2.243 0.02 2 489 95 72 GLN HG3 H 2.179 0.02 2 490 95 72 GLN NE2 N 109.8 0.2 1 491 95 72 GLN HE21 H 6.505 0.02 2 492 95 72 GLN HE22 H 7.120 0.02 2 493 96 73 LEU N N 122.9 0.2 1 494 96 73 LEU H H 7.685 0.02 1 495 96 73 LEU HA H 3.954 0.02 1 496 96 73 LEU HB2 H 1.166 0.02 1 497 96 73 LEU HB3 H 1.990 0.02 1 498 96 73 LEU HG H 1.569 0.02 1 499 96 73 LEU HD1 H 0.845 0.02 1 500 96 73 LEU HD2 H 1.016 0.02 1 501 97 74 ASP N N 118.9 0.2 1 502 97 74 ASP H H 8.521 0.02 1 503 97 74 ASP HA H 4.272 0.02 1 504 97 74 ASP HB2 H 2.589 0.02 1 505 97 74 ASP HB3 H 2.584 0.02 1 506 98 75 SER N N 115.4 0.2 1 507 98 75 SER H H 7.814 0.02 1 508 98 75 SER HA H 4.198 0.02 1 509 98 75 SER HB2 H 3.845 0.02 1 510 98 75 SER HB3 H 3.830 0.02 1 511 99 76 VAL N N 111.3 0.2 1 512 99 76 VAL H H 7.090 0.02 1 513 99 76 VAL HA H 4.434 0.02 1 514 99 76 VAL HB H 2.579 0.02 1 515 99 76 VAL HG1 H 0.857 0.02 1 516 99 76 VAL HG2 H 0.997 0.02 1 517 100 77 GLY N N 105.1 0.2 1 518 100 77 GLY H H 7.371 0.02 1 519 100 77 GLY HA2 H 4.332 0.02 2 520 100 77 GLY HA3 H 3.531 0.02 2 521 101 78 GLY N N 107.5 0.2 1 522 101 78 GLY H H 7.932 0.02 1 523 101 78 GLY HA2 H 4.404 0.02 2 524 101 78 GLY HA3 H 3.669 0.02 2 525 102 79 PHE HA H 3.722 0.02 1 526 102 79 PHE HB2 H 3.060 0.02 1 527 102 79 PHE HB3 H 2.892 0.02 1 528 102 79 PHE HD1 H 6.938 0.02 1 529 102 79 PHE HD2 H 6.938 0.02 1 530 102 79 PHE HE1 H 7.110 0.02 1 531 102 79 PHE HE2 H 7.110 0.02 1 532 102 79 PHE HZ H 7.094 0.02 1 533 103 80 ALA H H 8.983 0.02 1 534 103 80 ALA HA H 3.934 0.02 1 535 103 80 ALA HB H 1.479 0.02 1 536 104 81 TYR N N 117.4 0.2 1 537 104 81 TYR H H 7.123 0.02 1 538 104 81 TYR HA H 4.344 0.02 1 539 104 81 TYR HB2 H 3.148 0.02 1 540 104 81 TYR HB3 H 2.757 0.02 1 541 104 81 TYR HD1 H 7.179 0.02 1 542 104 81 TYR HD2 H 7.179 0.02 1 543 104 81 TYR HE1 H 6.681 0.02 1 544 104 81 TYR HE2 H 6.681 0.02 1 545 105 82 LEU N N 116.7 0.22 1 546 105 82 LEU H H 7.009 0.02 1 547 105 82 LEU HA H 3.537 0.02 1 548 105 82 LEU HB2 H 1.498 0.02 1 549 105 82 LEU HB3 H 1.042 0.02 1 550 105 82 LEU HG H 1.664 0.02 1 551 105 82 LEU HD1 H 0.656 0.02 1 552 105 82 LEU HD2 H 0.643 0.02 1 553 106 83 ALA N N 119.3 0.2 1 554 106 83 ALA H H 8.416 0.02 1 555 106 83 ALA HA H 3.650 0.02 1 556 106 83 ALA HB H 1.019 0.02 1 557 107 84 GLU N N 121.2 0.2 1 558 107 84 GLU H H 7.655 0.02 1 559 107 84 GLU HA H 3.789 0.02 1 560 107 84 GLU HB2 H 2.059 0.02 1 561 107 84 GLU HB3 H 1.983 0.02 1 562 107 84 GLU HG2 H 2.114 0.02 2 563 107 84 GLU HG3 H 2.174 0.02 2 564 108 85 LEU N N 118.6 0.2 1 565 108 85 LEU H H 7.752 0.02 1 566 108 85 LEU HA H 3.662 0.02 1 567 108 85 LEU HB2 H 1.866 0.02 1 568 108 85 LEU HB3 H 0.864 0.02 1 569 108 85 LEU HG H 1.307 0.02 1 570 108 85 LEU HD1 H 0.596 0.02 1 571 108 85 LEU HD2 H 0.660 0.02 1 572 109 86 SER N N 111.7 0.2 1 573 109 86 SER H H 7.518 0.02 1 574 109 86 SER HA H 4.166 0.02 1 575 109 86 SER HB2 H 3.913 0.02 1 576 109 86 SER HB3 H 3.937 0.02 1 577 110 87 LYS N N 120.4 0.2 1 578 110 87 LYS H H 7.633 0.02 1 579 110 87 LYS HA H 4.081 0.02 1 580 110 87 LYS HB2 H 1.777 0.02 2 581 110 87 LYS HB3 H 1.763 0.02 2 582 110 87 LYS HG2 H 1.470 0.02 2 583 110 87 LYS HG3 H 1.394 0.02 2 584 110 87 LYS HD2 H 1.577 0.02 2 585 110 87 LYS HD3 H 1.564 0.02 2 586 110 87 LYS HE2 H 2.848 0.02 2 587 110 87 LYS HE3 H 2.828 0.02 2 588 111 88 ASN N N 116.7 0.2 1 589 111 88 ASN H H 7.739 0.02 1 590 111 88 ASN HA H 4.631 0.02 1 591 111 88 ASN HB2 H 2.728 0.02 1 592 111 88 ASN HB3 H 2.747 0.02 1 593 111 88 ASN ND2 N 113.5 0.2 1 594 111 88 ASN HD21 H 7.401 0.02 1 595 111 88 ASN HD22 H 6.970 0.02 1 596 112 89 THR N N 114.6 0.2 1 597 112 89 THR H H 7.471 0.02 1 598 112 89 THR HA H 4.529 0.02 1 599 112 89 THR HB H 4.045 0.02 1 600 112 89 THR HG2 H 1.095 0.02 1 601 113 90 PRO HA H 4.517 0.02 1 602 113 90 PRO HB2 H 1.988 0.02 2 603 113 90 PRO HB3 H 2.287 0.02 2 604 113 90 PRO HG2 H 1.941 0.02 2 605 113 90 PRO HG3 H 1.954 0.02 2 606 113 90 PRO HD2 H 3.675 0.02 1 607 113 90 PRO HD3 H 3.675 0.02 1 608 114 91 SER N N 113.3 0.2 1 609 114 91 SER H H 7.961 0.02 1 610 114 91 SER HA H 4.396 0.02 1 611 114 91 SER HB2 H 4.013 0.02 2 612 114 91 SER HB3 H 3.833 0.02 2 613 115 92 ALA N N 125.6 0.2 1 614 115 92 ALA H H 8.796 0.02 1 615 115 92 ALA HA H 4.366 0.02 1 616 115 92 ALA HB H 1.442 0.02 1 617 116 93 ALA N N 120.5 0.2 1 618 116 93 ALA H H 8.089 0.02 1 619 116 93 ALA HA H 4.094 0.02 1 620 116 93 ALA HB H 1.322 0.02 1 621 117 94 ASN N N 116.1 0.2 1 622 117 94 ASN H H 8.233 0.02 1 623 117 94 ASN HA H 4.771 0.02 1 624 117 94 ASN HB2 H 2.657 0.02 2 625 117 94 ASN HB3 H 2.720 0.02 2 626 117 94 ASN ND2 N 111.8 0.2 1 627 117 94 ASN HD21 H 7.343 0.02 2 628 117 94 ASN HD22 H 6.834 0.02 2 629 118 95 ILE N N 121.2 0.2 1 630 118 95 ILE H H 7.997 0.02 1 631 118 95 ILE HA H 3.887 0.02 1 632 118 95 ILE HB H 2.036 0.02 1 633 118 95 ILE HG2 H 0.964 0.02 1 634 118 95 ILE HG12 H 1.191 0.02 2 635 118 95 ILE HG13 H 1.661 0.02 2 636 118 95 ILE HD1 H 0.951 0.02 1 637 119 96 SER N N 117.3 0.2 1 638 119 96 SER H H 8.096 0.02 1 639 119 96 SER HA H 3.789 0.02 1 640 119 96 SER HB2 H 3.715 0.02 2 641 119 96 SER HB3 H 3.634 0.02 2 642 120 97 ALA N N 123.1 0.2 1 643 120 97 ALA H H 7.194 0.02 1 644 120 97 ALA HA H 4.089 0.02 1 645 120 97 ALA HB H 1.215 0.02 1 646 121 98 TYR N N 116.9 0.2 1 647 121 98 TYR H H 7.706 0.02 1 648 121 98 TYR HA H 4.382 0.02 1 649 121 98 TYR HB2 H 2.824 0.02 1 650 121 98 TYR HB3 H 3.245 0.02 1 651 121 98 TYR HD1 H 6.935 0.02 1 652 121 98 TYR HD2 H 6.935 0.02 1 653 121 98 TYR HE1 H 6.773 0.02 1 654 121 98 TYR HE2 H 6.773 0.02 1 655 122 99 ALA N N 122.9 0.2 1 656 122 99 ALA H H 8.282 0.02 1 657 122 99 ALA HA H 3.696 0.02 1 658 122 99 ALA HB H 1.418 0.02 1 659 123 100 ASP N N 117.2 0.2 1 660 123 100 ASP H H 7.998 0.02 1 661 123 100 ASP HA H 4.344 0.02 1 662 123 100 ASP HB2 H 2.838 0.02 1 663 123 100 ASP HB3 H 2.583 0.02 1 664 124 101 ILE N N 121.4 0.2 1 665 124 101 ILE H H 7.410 0.02 1 666 124 101 ILE HA H 3.740 0.02 1 667 124 101 ILE HB H 2.116 0.02 1 668 124 101 ILE HG2 H 0.842 0.02 1 669 124 101 ILE HG12 H 1.070 0.02 1 670 124 101 ILE HG13 H 1.778 0.02 1 671 124 101 ILE HD1 H 0.820 0.02 1 672 125 102 VAL N N 120.4 0.2 1 673 125 102 VAL H H 7.746 0.02 1 674 125 102 VAL HA H 3.369 0.02 1 675 125 102 VAL HB H 1.971 0.02 1 676 125 102 VAL HG1 H -0.001 0.02 1 677 125 102 VAL HG2 H 0.861 0.02 1 678 126 103 ARG N N 121.2 0.2 1 679 126 103 ARG H H 8.065 0.02 1 680 126 103 ARG HA H 3.793 0.02 1 681 126 103 ARG HB2 H 2.118 0.02 1 682 126 103 ARG HB3 H 1.923 0.02 1 683 126 103 ARG HG2 H 1.541 0.02 2 684 126 103 ARG HG3 H 1.655 0.02 2 685 126 103 ARG HD2 H 3.249 0.02 2 686 126 103 ARG HD3 H 3.335 0.02 2 687 127 104 GLU N N 119.9 0.2 1 688 127 104 GLU H H 8.544 0.02 1 689 127 104 GLU HA H 3.886 0.02 1 690 127 104 GLU HB2 H 2.075 0.02 1 691 127 104 GLU HB3 H 2.170 0.02 1 692 127 104 GLU HG2 H 2.194 0.02 2 693 127 104 GLU HG3 H 2.359 0.02 2 694 128 105 ARG N N 115.9 0.2 1 695 128 105 ARG H H 8.633 0.02 1 696 128 105 ARG HA H 3.934 0.02 1 697 128 105 ARG HB2 H 1.855 0.02 1 698 128 105 ARG HB3 H 1.466 0.02 1 699 128 105 ARG HG2 H 1.300 0.02 2 700 128 105 ARG HG3 H 2.051 0.02 2 701 128 105 ARG HD2 H 2.925 0.02 2 702 128 105 ARG HD3 H 2.844 0.02 2 703 129 106 ALA N N 121.9 0.2 1 704 129 106 ALA H H 7.567 0.02 1 705 129 106 ALA HA H 3.927 0.02 1 706 129 106 ALA HB H 1.710 0.02 1 707 130 107 VAL N N 120.7 0.2 1 708 130 107 VAL H H 8.105 0.02 1 709 130 107 VAL HA H 3.632 0.02 1 710 130 107 VAL HB H 2.231 0.02 1 711 130 107 VAL HG1 H 0.903 0.02 1 712 130 107 VAL HG2 H 1.010 0.02 1 713 131 108 VAL N N 119.7 0.2 1 714 131 108 VAL H H 7.571 0.02 1 715 131 108 VAL HA H 3.660 0.02 1 716 131 108 VAL HB H 2.039 0.02 1 717 131 108 VAL HG1 H 0.948 0.02 1 718 131 108 VAL HG2 H 1.014 0.02 1 719 132 109 ARG N N 119.2 0.2 1 720 132 109 ARG H H 8.330 0.02 1 721 132 109 ARG HA H 3.875 0.02 1 722 132 109 ARG HB2 H 1.935 0.02 2 723 132 109 ARG HB3 H 2.157 0.02 2 724 132 109 ARG HG2 H 1.355 0.02 2 725 132 109 ARG HG3 H 1.958 0.02 2 726 132 109 ARG HD2 H 3.344 0.02 2 727 132 109 ARG HD3 H 3.361 0.02 2 728 133 110 GLU N N 118.9 0.2 1 729 133 110 GLU H H 7.948 0.02 1 730 133 110 GLU HA H 4.134 0.02 1 731 133 110 GLU HB2 H 2.146 0.02 1 732 133 110 GLU HB3 H 2.092 0.02 1 733 133 110 GLU HG2 H 2.325 0.02 2 734 133 110 GLU HG3 H 2.270 0.02 2 735 134 111 MET N N 119.6 0.2 1 736 134 111 MET H H 7.917 0.02 1 737 134 111 MET HA H 4.219 0.02 1 738 134 111 MET HB2 H 2.537 0.02 2 739 134 111 MET HB3 H 2.231 0.02 2 740 134 111 MET HG2 H 2.196 0.02 2 741 134 111 MET HG3 H 2.735 0.02 2 742 134 111 MET HE H 1.712 0.02 1 743 135 112 ILE N N 118.2 0.2 1 744 135 112 ILE H H 8.111 0.02 1 745 135 112 ILE HA H 3.937 0.02 1 746 135 112 ILE HB H 1.940 0.02 1 747 135 112 ILE HG2 H 0.884 0.02 1 748 135 112 ILE HG12 H 1.558 0.02 2 749 135 112 ILE HG13 H 1.196 0.02 2 750 135 112 ILE HD1 H 0.730 0.02 1 751 136 113 SER N N 116.2 0.2 1 752 136 113 SER H H 7.940 0.02 1 753 136 113 SER HA H 4.372 0.02 1 754 136 113 SER HB2 H 3.995 0.02 2 755 136 113 SER HB3 H 3.975 0.02 2 756 137 114 THR N N 112.5 0.2 1 757 137 114 THR H H 7.761 0.02 1 758 137 114 THR HA H 4.358 0.02 1 759 137 114 THR HB H 4.352 0.02 1 760 137 114 THR HG2 H 1.236 0.02 1 761 138 115 ARG N N 121.6 0.2 1 762 138 115 ARG H H 7.846 0.02 1 763 138 115 ARG HA H 4.351 0.02 1 764 138 115 ARG HB2 H 1.837 0.02 2 765 138 115 ARG HB3 H 1.897 0.02 2 766 139 116 GLU N N 121.2 0.2 1 767 139 116 GLU H H 8.410 0.02 1 768 139 116 GLU HA H 4.275 0.02 1 769 139 116 GLU HB2 H 1.958 0.02 2 770 139 116 GLU HB3 H 2.071 0.02 2 771 140 117 SER N N 116.4 0.2 1 772 140 117 SER H H 8.246 0.02 1 773 140 117 SER HA H 4.341 0.02 1 774 140 117 SER HB2 H 3.839 0.02 2 775 140 117 SER HB3 H 3.906 0.02 2 776 141 118 GLY N N 111.0 0.2 1 777 141 118 GLY H H 8.416 0.02 1 778 141 118 GLY HA2 H 3.928 0.02 2 779 141 118 GLY HA3 H 3.986 0.02 2 780 142 119 SER N N 115.4 0.2 1 781 142 119 SER H H 8.080 0.02 1 782 142 119 SER HA H 4.442 0.02 1 783 142 119 SER HB2 H 3.823 0.02 2 784 142 119 SER HB3 H 3.884 0.02 2 785 143 120 ILE N N 121.9 0.2 1 786 143 120 ILE H H 7.980 0.02 1 787 143 120 ILE HA H 4.114 0.02 1 788 143 120 ILE HB H 1.827 0.02 1 789 143 120 ILE HG2 H 0.782 0.02 1 790 143 120 ILE HG12 H 1.123 0.02 2 791 143 120 ILE HG13 H 1.376 0.02 2 792 143 120 ILE HD1 H 0.813 0.02 1 793 144 121 GLU N N 123.4 0.2 1 794 144 121 GLU H H 8.235 0.02 1 795 144 121 GLU HA H 4.139 0.02 1 796 144 121 GLU HB2 H 1.759 0.02 2 797 144 121 GLU HB3 H 1.780 0.02 2 798 144 121 GLU HG2 H 1.946 0.02 2 799 144 121 GLU HG3 H 2.073 0.02 2 800 145 122 PHE N N 120.7 0.2 1 801 145 122 PHE H H 8.055 0.02 1 802 145 122 PHE HA H 4.571 0.02 1 803 145 122 PHE HB2 H 2.885 0.02 2 804 145 122 PHE HB3 H 3.082 0.02 2 805 145 122 PHE HD1 H 7.190 0.02 1 806 145 122 PHE HD2 H 7.190 0.02 1 807 145 122 PHE HE1 H 7.275 0.02 1 808 145 122 PHE HE2 H 7.275 0.02 1 809 145 122 PHE HZ H 7.235 0.02 1 stop_ save_