data_4957 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Transcriptional Activation Domain of the Bacteriophage T4 Protein, MotA ; _BMRB_accession_number 4957 _BMRB_flat_file_name bmr4957.str _Entry_type original _Submission_date 2001-02-16 _Accession_date 2001-02-19 _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 Li Ning . . 2 Zhang Weixing . . 3 White Stephen W. . 4 Kriwacki Richard W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 541 "13C chemical shifts" 413 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-01 original author . stop_ _Original_release_date 2002-04-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the Transcriptional Activation Domain of the Bacteriophage T4 Protein, MotA ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21181601 _PubMed_ID 11284685 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li Ning . . 2 Zhang Weixing . . 3 White Stephen W. . 4 Kriwacki Richard W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 14 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4293 _Page_last 4302 _Year 2001 _Details . loop_ _Keyword MotNF 'transcription activator' stop_ save_ ################################## # Molecular system description # ################################## save_system_MotNF _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of MotA, MotNF' _Abbreviation_common MotNF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MotNF subunit 1' $MotNF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'activator of T4 phage middle-mode gene expression' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MotNF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of MotA' _Abbreviation_common MotNF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; MSKVTYIIKASNDVLNEKTA TILITIAKKDFITAAEVREV HPDLGNAVVNSNIGVLIKKG LVEKSGDGLIITGEAQDIIS NAATLYAQENAPELLK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LYS 4 VAL 5 THR 6 TYR 7 ILE 8 ILE 9 LYS 10 ALA 11 SER 12 ASN 13 ASP 14 VAL 15 LEU 16 ASN 17 GLU 18 LYS 19 THR 20 ALA 21 THR 22 ILE 23 LEU 24 ILE 25 THR 26 ILE 27 ALA 28 LYS 29 LYS 30 ASP 31 PHE 32 ILE 33 THR 34 ALA 35 ALA 36 GLU 37 VAL 38 ARG 39 GLU 40 VAL 41 HIS 42 PRO 43 ASP 44 LEU 45 GLY 46 ASN 47 ALA 48 VAL 49 VAL 50 ASN 51 SER 52 ASN 53 ILE 54 GLY 55 VAL 56 LEU 57 ILE 58 LYS 59 LYS 60 GLY 61 LEU 62 VAL 63 GLU 64 LYS 65 SER 66 GLY 67 ASP 68 GLY 69 LEU 70 ILE 71 ILE 72 THR 73 GLY 74 GLU 75 ALA 76 GLN 77 ASP 78 ILE 79 ILE 80 SER 81 ASN 82 ALA 83 ALA 84 THR 85 LEU 86 TYR 87 ALA 88 GLN 89 GLU 90 ASN 91 ALA 92 PRO 93 GLU 94 LEU 95 LEU 96 LYS 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 PDB 1BJA "Activation Domain Of The Phage T4 Transcription Factor Mota" 98.96 95 100.00 100.00 3.22e-58 PDB 1I1S "Solution Structure Of The Transcriptional Activation Domain Of The Bacteriophage T4 Protein Mota" 100.00 96 100.00 100.00 2.70e-59 DBJ BAI83277 "MotA activator of middle period transcription [Enterobacteria phage AR1]" 100.00 211 98.96 98.96 2.72e-57 EMBL CAA88453 "MotA [Enterobacteria phage T4]" 100.00 211 100.00 100.00 3.91e-58 EMBL CCI89155 "protein of unknown function [Yersinia phage phiD1]" 100.00 211 98.96 98.96 2.55e-57 GB AAD42607 "MotA activator of middle period transcription [Enterobacteria phage T4]" 100.00 211 100.00 100.00 3.91e-58 GB ABI95078 "activator middle promoter [Enterobacteria phage RB32]" 100.00 211 98.96 98.96 2.72e-57 GB ACP30901 "MotA [Enterobacteria phage RB14]" 100.00 211 98.96 98.96 2.72e-57 GB ACP31176 "MotA [Enterobacteria phage RB51]" 100.00 211 98.96 98.96 2.31e-57 GB ADJ39982 "activator of middle period transcription [Enterobacteria phage T4T]" 100.00 211 100.00 100.00 3.91e-58 REF NP_049873 "MotA activator of middle period transcription [Enterobacteria phage T4]" 100.00 211 100.00 100.00 3.91e-58 REF YP_002854213 "MotA [Enterobacteria phage RB51]" 100.00 211 98.96 98.96 2.31e-57 REF YP_002854593 "MotA [Enterobacteria phage RB14]" 100.00 211 98.96 98.96 2.72e-57 REF YP_004415151 "putative activator of middle period transcription [Shigella phage Shfl2]" 100.00 211 98.96 98.96 2.72e-57 REF YP_006986818 "activator of middle period transcription [Enterobacteria phage vB_EcoM_ACG-C40]" 100.00 211 98.96 98.96 2.72e-57 SP P22915 "RecName: Full=Middle transcription regulatory protein motA [Enterobacteria phage T4]" 100.00 211 100.00 100.00 3.91e-58 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $MotNF 'Coliphage T4' . virus . 'Coliphage T4' 'coliphage T4' MotA stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $MotNF 'recombinant technology' . . . . . ; MotNF is comprised of the N-terminal domain of MotA, amino acids 1-96. ; 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 $MotNF 2.0 mM '[U-98% 15N]' 'potassium phosphate' 200 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MotNF 2.0 mM '[U-99% 13C; U-98% 15N]' 'potassium phosphate' 200 mM . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 97.0 loop_ _Vendor _Address _Electronic_address 'Molecular Simulations, Inc.' 'San Diego, CA' . stop_ loop_ _Task 'data processing' 'display and analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 301 1 K 'ionic strength' 300 . mM 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 TSP H 1 'methyl protons' ppm 0.0 . direct . external parallel 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'MotNF subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 3 LYS HA H 4.33 0.01 1 2 . 3 LYS HB2 H 1.87 0.01 2 3 . 3 LYS HB3 H 1.81 0.01 2 4 . 3 LYS HG2 H 1.38 0.01 2 5 . 3 LYS HG3 H 1.24 0.01 2 6 . 3 LYS HD2 H 1.56 0.01 1 7 . 3 LYS HD3 H 1.56 0.01 1 8 . 3 LYS C C 178.2 0.15 1 9 . 3 LYS CA C 58.5 0.15 1 10 . 3 LYS CB C 32.6 0.15 1 11 . 3 LYS CG C 25.2 0.15 1 12 . 3 LYS CD C 29.1 0.15 1 13 . 3 LYS CE C 41.9 0.15 1 14 . 4 VAL H H 8.09 0.01 1 15 . 4 VAL HA H 3.64 0.01 1 16 . 4 VAL HB H 2.08 0.01 1 17 . 4 VAL HG1 H 0.99 0.01 1 18 . 4 VAL HG2 H 0.91 0.01 1 19 . 4 VAL C C 176.9 0.15 1 20 . 4 VAL CA C 66.1 0.15 1 21 . 4 VAL CB C 32.0 0.15 1 22 . 4 VAL CG1 C 22.6 0.15 1 23 . 4 VAL CG2 C 21.5 0.15 1 24 . 4 VAL N N 118.7 0.20 1 25 . 5 THR H H 7.80 0.01 1 26 . 5 THR HA H 3.73 0.01 1 27 . 5 THR HB H 3.92 0.01 1 28 . 5 THR HG2 H 1.00 0.01 1 29 . 5 THR C C 176.6 0.15 1 30 . 5 THR CA C 66.3 0.15 1 31 . 5 THR CB C 68.5 0.15 1 32 . 5 THR CG2 C 21.9 0.15 1 33 . 5 THR N N 115.9 0.20 1 34 . 6 TYR H H 7.47 0.01 1 35 . 6 TYR HA H 4.10 0.01 1 36 . 6 TYR HB2 H 3.00 0.01 1 37 . 6 TYR HB3 H 3.28 0.01 1 38 . 6 TYR HD1 H 7.23 0.01 1 39 . 6 TYR HD2 H 7.23 0.01 1 40 . 6 TYR HE1 H 6.92 0.01 1 41 . 6 TYR HE2 H 6.92 0.01 1 42 . 6 TYR C C 177.4 0.15 1 43 . 6 TYR CA C 62.5 0.15 1 44 . 6 TYR CB C 38.2 0.15 1 45 . 6 TYR CD1 C 132.9 0.15 1 46 . 6 TYR CD2 C 132.9 0.15 1 47 . 6 TYR CE1 C 118.7 0.15 1 48 . 6 TYR CE2 C 118.7 0.15 1 49 . 6 TYR N N 120.8 0.20 1 50 . 7 ILE H H 7.75 0.01 1 51 . 7 ILE HA H 3.65 0.01 1 52 . 7 ILE HB H 2.05 0.01 1 53 . 7 ILE HG12 H 1.57 0.01 2 54 . 7 ILE HG13 H 1.13 0.01 2 55 . 7 ILE HG2 H 0.76 0.01 1 56 . 7 ILE HD1 H 0.76 0.01 1 57 . 7 ILE C C 177.4 0.15 1 58 . 7 ILE CA C 64.5 0.15 1 59 . 7 ILE CB C 36.9 0.15 1 60 . 7 ILE CG1 C 28.9 0.15 1 61 . 7 ILE CG2 C 18.2 0.15 1 62 . 7 ILE CD1 C 13.0 0.15 1 63 . 7 ILE N N 123.1 0.20 1 64 . 8 ILE H H 8.05 0.01 1 65 . 8 ILE HA H 3.31 0.01 1 66 . 8 ILE HB H 1.76 0.01 1 67 . 8 ILE HG12 H 1.52 0.01 2 68 . 8 ILE HG13 H 0.35 0.01 2 69 . 8 ILE HG2 H 0.63 0.01 1 70 . 8 ILE HD1 H 0.88 0.01 1 71 . 8 ILE C C 181.0 0.15 1 72 . 8 ILE CA C 66.5 0.15 1 73 . 8 ILE CB C 38.4 0.15 1 74 . 8 ILE CG1 C 29.2 0.15 1 75 . 8 ILE CG2 C 16.8 0.15 1 76 . 8 ILE CD1 C 14.0 0.15 1 77 . 8 ILE N N 120.9 0.02 1 78 . 9 LYS H H 8.04 0.01 1 79 . 9 LYS HA H 4.19 0.01 1 80 . 9 LYS HB2 H 1.87 0.01 1 81 . 9 LYS HB3 H 1.87 0.01 1 82 . 9 LYS HG2 H 1.54 0.01 2 83 . 9 LYS HG3 H 1.48 0.01 2 84 . 9 LYS HD2 H 1.47 0.01 1 85 . 9 LYS HD3 H 1.47 0.01 1 86 . 9 LYS HE2 H 2.79 0.01 1 87 . 9 LYS HE3 H 2.79 0.01 1 88 . 9 LYS C C 180.1 0.15 1 89 . 9 LYS CA C 59.7 0.15 1 90 . 9 LYS CB C 32.6 0.15 1 91 . 9 LYS CG C 24.9 0.15 1 92 . 9 LYS CD C 29.3 0.15 1 93 . 9 LYS CE C 41.9 0.15 1 94 . 9 LYS N N 123.2 0.20 1 95 . 10 ALA H H 8.63 0.01 1 96 . 10 ALA HA H 4.25 0.01 1 97 . 10 ALA HB H 1.58 0.01 1 98 . 10 ALA C C 177.8 0.15 1 99 . 10 ALA CA C 54.4 0.15 1 100 . 10 ALA CB C 19.3 0.15 1 101 . 10 ALA N N 123.7 0.20 1 102 . 11 SER H H 7.96 0.01 1 103 . 11 SER HA H 4.44 0.01 1 104 . 11 SER HB2 H 4.16 0.01 1 105 . 11 SER HB3 H 4.08 0.01 1 106 . 11 SER C C 174.8 0.15 1 107 . 11 SER CA C 58.7 0.15 1 108 . 11 SER CB C 64.8 0.15 1 109 . 11 SER N N 113.6 0.20 1 110 . 12 ASN H H 8.48 0.01 1 111 . 12 ASN HA H 4.46 0.01 1 112 . 12 ASN HB2 H 2.86 0.01 1 113 . 12 ASN HB3 H 3.15 0.01 1 114 . 12 ASN HD21 H 7.51 0.01 9 115 . 12 ASN HD22 H 6.82 0.01 9 116 . 12 ASN C C 174.3 0.15 1 117 . 12 ASN CA C 54.8 0.15 1 118 . 12 ASN CB C 37.0 0.15 1 119 . 12 ASN N N 123.0 0.20 1 120 . 13 ASP H H 7.79 0.01 1 121 . 13 ASP HA H 4.08 0.01 1 122 . 13 ASP HB2 H 2.86 0.01 1 123 . 13 ASP HB3 H 2.92 0.01 1 124 . 13 ASP C C 175.1 0.15 1 125 . 13 ASP CA C 56.5 0.15 1 126 . 13 ASP CB C 39.1 0.15 1 127 . 13 ASP N N 110.4 0.20 1 128 . 14 VAL H H 7.51 0.01 1 129 . 14 VAL HA H 3.89 0.01 1 130 . 14 VAL HB H 1.95 0.01 1 131 . 14 VAL HG1 H 0.97 0.01 1 132 . 14 VAL HG2 H 1.13 0.01 1 133 . 14 VAL C C 177.7 0.15 1 134 . 14 VAL CA C 65.0 0.15 1 135 . 14 VAL CB C 33.2 0.15 1 136 . 14 VAL CG1 C 20.9 0.15 1 137 . 14 VAL CG2 C 22.6 0.15 1 138 . 14 VAL N N 119.8 0.20 1 139 . 15 LEU H H 7.47 0.01 1 140 . 15 LEU HA H 4.39 0.01 1 141 . 15 LEU HB2 H 1.33 0.01 1 142 . 15 LEU HB3 H 1.49 0.01 1 143 . 15 LEU HG H 0.70 0.01 1 144 . 15 LEU HD1 H 0.66 0.01 1 145 . 15 LEU HD2 H 0.66 0.01 1 146 . 15 LEU C C 174.1 0.15 1 147 . 15 LEU CA C 53.2 0.15 1 148 . 15 LEU CB C 43.4 0.15 1 149 . 15 LEU CG C 27.3 0.15 1 150 . 15 LEU CD1 C 22.6 0.15 1 151 . 15 LEU CD2 C 22.6 0.15 1 152 . 15 LEU N N 117.8 0.20 1 153 . 16 ASN H H 7.62 0.01 1 154 . 16 ASN HA H 4.67 0.01 1 155 . 16 ASN HB2 H 2.81 0.01 1 156 . 16 ASN HB3 H 3.18 0.01 1 157 . 16 ASN HD21 H 7.17 0.01 9 158 . 16 ASN HD22 H 7.64 0.01 9 159 . 16 ASN C C 174.8 0.15 1 160 . 16 ASN CA C 51.0 0.15 1 161 . 16 ASN CB C 40.4 0.15 1 162 . 16 ASN N N 116.80 0.20 1 163 . 17 GLU H H 9.02 0.01 1 164 . 17 GLU HA H 3.73 0.01 1 165 . 17 GLU HB2 H 2.04 0.01 1 166 . 17 GLU HB3 H 2.04 0.01 1 167 . 17 GLU HG2 H 2.20 0.01 2 168 . 17 GLU HG3 H 2.24 0.01 2 169 . 17 GLU C C 178.5 0.15 1 170 . 17 GLU CA C 61.4 0.15 1 171 . 17 GLU CB C 29.3 0.15 1 172 . 17 GLU CG C 36.4 0.15 1 173 . 17 GLU N N 118.8 0.20 1 174 . 18 LYS H H 8.22 0.01 1 175 . 18 LYS HA H 4.01 0.01 1 176 . 18 LYS HB2 H 1.45 0.01 1 177 . 18 LYS HB3 H 2.03 0.01 1 178 . 18 LYS HG2 H 1.56 0.01 2 179 . 18 LYS HG3 H 1.37 0.01 2 180 . 18 LYS HD2 H 1.73 0.01 1 181 . 18 LYS HD3 H 1.73 0.01 1 182 . 18 LYS HE2 H 2.99 0.01 1 183 . 18 LYS HE3 H 2.99 0.01 1 184 . 18 LYS C C 178.1 0.15 1 185 . 18 LYS CA C 59.9 0.15 1 186 . 18 LYS CB C 32.7 0.15 1 187 . 18 LYS CG C 26.1 0.15 1 188 . 18 LYS CD C 29.3 0.15 1 189 . 18 LYS CE C 42.3 0.15 1 190 . 18 LYS N N 120.3 0.20 1 191 . 19 THR H H 8.38 0.01 1 192 . 19 THR HA H 3.69 0.01 1 193 . 19 THR HB H 4.14 0.01 1 194 . 19 THR HG2 H 1.41 0.01 1 195 . 19 THR C C 177.6 0.15 1 196 . 19 THR CA C 65.4 0.15 1 197 . 19 THR CB C 68.9 0.15 1 198 . 19 THR CG2 C 24.8 0.15 1 199 . 19 THR N N 111.07 0.20 1 200 . 20 ALA H H 9.03 0.01 1 201 . 20 ALA HA H 3.99 0.01 1 202 . 20 ALA HB H 1.31 0.01 1 203 . 20 ALA C C 178.0 0.15 1 204 . 20 ALA CA C 55.6 0.15 1 205 . 20 ALA CB C 20.0 0.15 1 206 . 20 ALA N N 122.1 0.20 1 207 . 21 THR H H 7.21 0.01 1 208 . 21 THR HA H 3.83 0.01 1 209 . 21 THR HB H 4.26 0.01 1 210 . 21 THR HG2 H 1.13 0.01 1 211 . 21 THR C C 176.0 0.15 1 212 . 21 THR CA C 67.1 0.15 1 213 . 21 THR CB C 69.0 0.15 1 214 . 21 THR CG2 C 21.4 0.15 1 215 . 21 THR N N 113.4 0.20 1 216 . 22 ILE H H 7.34 0.01 1 217 . 22 ILE HA H 3.53 0.01 1 218 . 22 ILE HB H 1.56 0.01 1 219 . 22 ILE HG12 H 1.25 0.01 2 220 . 22 ILE HG13 H 0.73 0.01 2 221 . 22 ILE HG2 H 0.70 0.01 1 222 . 22 ILE HD1 H 0.53 0.01 1 223 . 22 ILE C C 176.7 0.15 1 224 . 22 ILE CA C 64.2 0.15 1 225 . 22 ILE CB C 37.5 0.15 1 226 . 22 ILE CG1 C 28.8 0.15 1 227 . 22 ILE CG2 C 18.3 0.15 1 228 . 22 ILE CD1 C 13.8 0.15 1 229 . 22 ILE N N 121.8 0.20 1 230 . 23 LEU H H 8.13 0.01 1 231 . 23 LEU HA H 3.77 0.01 1 232 . 23 LEU HB2 H 1.58 0.01 2 233 . 23 LEU HB3 H 2.06 0.01 2 234 . 23 LEU HG H 0.76 0.01 1 235 . 23 LEU HD1 H 0.84 0.01 1 236 . 23 LEU HD2 H 0.84 0.01 1 237 . 23 LEU C C 177.8 0.15 1 238 . 23 LEU CA C 58.6 0.15 1 239 . 23 LEU CB C 41.8 0.15 1 240 . 23 LEU CG C 26.5 0.15 1 241 . 23 LEU CD1 C 24.9 0.15 1 242 . 23 LEU CD2 C 24.9 0.15 1 243 . 23 LEU N N 121.8 0.20 1 244 . 24 ILE H H 7.66 0.01 1 245 . 24 ILE HA H 3.59 0.01 1 246 . 24 ILE HB H 2.01 0.01 1 247 . 24 ILE HG12 H 1.70 0.01 2 248 . 24 ILE HG13 H 1.10 0.01 2 249 . 24 ILE HG2 H 0.93 0.01 1 250 . 24 ILE HD1 H 0.78 0.01 1 251 . 24 ILE C C 177.4 0.15 1 252 . 24 ILE CA C 64.8 0.15 1 253 . 24 ILE CB C 37.7 0.15 1 254 . 24 ILE CG1 C 29.0 0.15 1 255 . 24 ILE CG2 C 17.9 0.15 1 256 . 24 ILE CD1 C 13.6 0.15 1 257 . 24 ILE N N 117.9 0.20 1 258 . 25 THR H H 7.45 0.01 1 259 . 25 THR HA H 3.83 0.01 1 260 . 25 THR HB H 4.60 0.01 1 261 . 25 THR HG2 H 1.27 0.01 1 262 . 25 THR C C 176.0 0.15 1 263 . 25 THR CA C 67.1 0.15 1 264 . 25 THR CB C 67.6 0.15 1 265 . 25 THR CG2 C 23.9 0.15 1 266 . 25 THR N N 119.1 0.20 1 267 . 26 ILE H H 7.86 0.01 1 268 . 26 ILE HA H 3.77 0.01 1 269 . 26 ILE HB H 1.63 0.01 1 270 . 26 ILE HG12 H 1.83 0.01 2 271 . 26 ILE HG13 H 0.71 0.01 2 272 . 26 ILE HG2 H 0.71 0.01 1 273 . 26 ILE HD1 H 0.67 0.01 1 274 . 26 ILE C C 177.6 0.15 1 275 . 26 ILE CA C 64.8 0.15 1 276 . 26 ILE CB C 38.5 0.15 1 277 . 26 ILE CG1 C 29.4 0.15 1 278 . 26 ILE CG2 C 17.0 0.15 1 279 . 26 ILE CD1 C 16.1 0.15 1 280 . 26 ILE N N 122.0 0.20 1 281 . 27 ALA H H 8.66 0.01 1 282 . 27 ALA HA H 4.04 0.01 1 283 . 27 ALA HB H 1.43 0.01 1 284 . 27 ALA C C 178.8 0.15 1 285 . 27 ALA CA C 54.1 0.15 1 286 . 27 ALA CB C 19.3 0.15 1 287 . 27 ALA N N 122.3 0.20 1 288 . 28 LYS H H 7.39 0.01 1 289 . 28 LYS HA H 4.10 0.01 1 290 . 28 LYS HB2 H 1.71 0.01 2 291 . 28 LYS HB3 H 1.93 0.01 2 292 . 28 LYS HG2 H 1.51 0.01 1 293 . 28 LYS HG3 H 1.51 0.01 1 294 . 28 LYS HD2 H 1.68 0.01 1 295 . 28 LYS HD3 H 1.68 0.01 1 296 . 28 LYS HE2 H 2.96 0.01 1 297 . 28 LYS HE3 H 2.96 0.01 1 298 . 28 LYS C C 176.3 0.15 1 299 . 28 LYS CA C 57.7 0.15 1 300 . 28 LYS CB C 33.5 0.15 1 301 . 28 LYS CG C 25.7 0.15 1 302 . 28 LYS CD C 29.5 0.15 1 303 . 28 LYS CE C 42.1 0.15 1 304 . 28 LYS N N 116.0 0.20 1 305 . 29 LYS H H 7.48 0.01 1 306 . 29 LYS HA H 4.43 0.01 1 307 . 29 LYS HB2 H 1.86 0.01 1 308 . 29 LYS HB3 H 1.58 0.01 1 309 . 29 LYS HG2 H 1.36 0.01 2 310 . 29 LYS HG3 H 1.24 0.01 2 311 . 29 LYS HD2 H 1.69 0.01 2 312 . 29 LYS HD3 H 1.58 0.01 2 313 . 29 LYS HE2 H 3.00 0.01 1 314 . 29 LYS HE3 H 3.00 0.01 1 315 . 29 LYS C C 172.3 0.15 1 316 . 29 LYS CA C 55.5 0.15 1 317 . 29 LYS CB C 34.8 0.15 1 318 . 29 LYS CG C 25.3 0.15 1 319 . 29 LYS CD C 29.6 0.15 1 320 . 29 LYS CE C 42.6 0.15 1 321 . 29 LYS N N 122.7 0.20 1 322 . 30 ASP H H 8.19 0.01 1 323 . 30 ASP HA H 4.39 0.01 1 324 . 30 ASP HB2 H 2.08 0.01 2 325 . 30 ASP HB3 H 2.42 0.01 2 326 . 30 ASP C C 177.3 0.15 1 327 . 30 ASP CA C 56.3 0.15 1 328 . 30 ASP CB C 40.8 0.15 1 329 . 30 ASP N N 125.6 0.20 1 330 . 31 PHE H H 8.10 0.01 1 331 . 31 PHE HA H 4.03 0.01 1 332 . 31 PHE HB2 H 3.37 0.01 2 333 . 31 PHE HB3 H 3.28 0.01 2 334 . 31 PHE HD1 H 7.08 0.01 1 335 . 31 PHE HD2 H 7.08 0.01 1 336 . 31 PHE HE1 H 7.39 0.01 1 337 . 31 PHE HE2 H 7.39 0.01 1 338 . 31 PHE HZ H 7.31 0.01 1 339 . 31 PHE C C 174.5 0.15 1 340 . 31 PHE CA C 60.3 0.15 1 341 . 31 PHE CB C 36.5 0.15 1 342 . 31 PHE CD1 C 131.4 0.15 1 343 . 31 PHE CD2 C 131.4 0.15 1 344 . 31 PHE CE1 C 131.8 0.15 1 345 . 31 PHE CE2 C 131.8 0.15 1 346 . 31 PHE CZ C 129.7 0.15 1 347 . 31 PHE N N 116.6 0.20 1 348 . 32 ILE H H 7.99 0.01 1 349 . 32 ILE HA H 4.25 0.01 1 350 . 32 ILE HB H 2.24 0.01 1 351 . 32 ILE HG12 H 1.72 0.01 1 352 . 32 ILE HG13 H 1.72 0.01 1 353 . 32 ILE HG2 H 0.95 0.01 1 354 . 32 ILE HD1 H 0.76 0.01 1 355 . 32 ILE C C 172.8 0.15 1 356 . 32 ILE CA C 61.9 0.15 1 357 . 32 ILE CB C 38.6 0.15 1 358 . 32 ILE CG1 C 29.9 0.15 1 359 . 32 ILE CG2 C 17.5 0.15 1 360 . 32 ILE CD1 C 14.4 0.15 1 361 . 32 ILE N N 124.4 0.20 1 362 . 33 THR H H 8.35 0.01 1 363 . 33 THR HA H 4.89 0.01 1 364 . 33 THR HB H 4.73 0.01 1 365 . 33 THR HG2 H 1.36 0.01 1 366 . 33 THR C C 176.2 0.15 1 367 . 33 THR CA C 60.6 0.15 1 368 . 33 THR CB C 72.0 0.15 1 369 . 33 THR CG2 C 22.0 0.15 1 370 . 33 THR N N 116.8 0.20 1 371 . 34 ALA H H 9.26 0.01 1 372 . 34 ALA HA H 3.80 0.01 1 373 . 34 ALA HB H 1.41 0.01 1 374 . 34 ALA C C 179.3 0.15 1 375 . 34 ALA CA C 56.0 0.15 1 376 . 34 ALA CB C 18.0 0.15 1 377 . 34 ALA N N 124.9 0.20 1 378 . 35 ALA H H 8.28 0.01 1 379 . 35 ALA HA H 3.94 0.01 1 380 . 35 ALA HB H 1.43 0.01 1 381 . 35 ALA C C 180.3 0.15 1 382 . 35 ALA CA C 55.6 0.15 1 383 . 35 ALA CB C 18.4 0.15 1 384 . 35 ALA N N 119.3 0.20 1 385 . 36 GLU H H 7.68 0.01 1 386 . 36 GLU HA H 4.02 0.01 1 387 . 36 GLU HB2 H 2.03 0.01 2 388 . 36 GLU HB3 H 2.37 0.01 2 389 . 36 GLU HG2 H 2.31 0.01 2 390 . 36 GLU HG3 H 2.23 0.01 2 391 . 36 GLU C C 179.0 0.15 1 392 . 36 GLU CA C 59.4 0.15 1 393 . 36 GLU CB C 29.9 0.15 1 394 . 36 GLU CG C 37.9 0.15 1 395 . 36 GLU N N 120.5 0.20 1 396 . 37 VAL H H 8.04 0.01 1 397 . 37 VAL HA H 3.50 0.01 1 398 . 37 VAL HB H 2.27 0.01 1 399 . 37 VAL HG1 H 0.98 0.01 1 400 . 37 VAL HG2 H 0.98 0.01 1 401 . 37 VAL C C 178.1 0.15 1 402 . 37 VAL CA C 67.1 0.15 1 403 . 37 VAL CB C 31.1 0.15 1 404 . 37 VAL CG1 C 23.7 0.15 1 405 . 37 VAL CG2 C 23.4 0.15 1 406 . 37 VAL N N 120.9 0.20 1 407 . 38 ARG H H 8.27 0.01 1 408 . 38 ARG HA H 3.86 0.01 1 409 . 38 ARG HB2 H 1.86 0.01 2 410 . 38 ARG HB3 H 2.01 0.01 2 411 . 38 ARG HG2 H 2.07 0.01 2 412 . 38 ARG HG3 H 1.30 0.01 2 413 . 38 ARG HD2 H 3.42 0.01 2 414 . 38 ARG HD3 H 3.05 0.01 2 415 . 38 ARG C C 179.1 0.15 1 416 . 38 ARG CA C 60.9 0.15 1 417 . 38 ARG CB C 30.6 0.15 1 418 . 38 ARG CG C 29.1 0.15 1 419 . 38 ARG CD C 43.8 0.15 1 420 . 38 ARG N N 117.7 0.20 1 421 . 39 GLU H H 7.61 0.01 1 422 . 39 GLU HA H 4.02 0.01 1 423 . 39 GLU HB2 H 2.17 0.01 1 424 . 39 GLU HB3 H 2.17 0.01 1 425 . 39 GLU HG2 H 2.43 0.01 2 426 . 39 GLU C C 178.2 0.15 1 427 . 39 GLU CA C 58.8 0.15 1 428 . 39 GLU CB C 29.8 0.15 1 429 . 39 GLU CG C 36.4 0.15 1 430 . 39 GLU N N 118.6 0.20 1 431 . 40 VAL H H 7.51 0.01 1 432 . 40 VAL HA H 3.94 0.01 1 433 . 40 VAL HB H 2.11 0.01 1 434 . 40 VAL HG1 H 0.97 0.01 2 435 . 40 VAL HG2 H 0.63 0.01 2 436 . 40 VAL C C 175.1 0.15 1 437 . 40 VAL CA C 63.4 0.15 1 438 . 40 VAL CB C 32.0 0.15 1 439 . 40 VAL CG1 C 21.7 0.15 1 440 . 40 VAL CG2 C 21.7 0.15 1 441 . 40 VAL N N 116.5 0.20 1 442 . 41 HIS H H 7.13 0.01 1 443 . 41 HIS HA H 3.90 0.01 1 444 . 41 HIS HB2 H 3.13 0.01 2 445 . 41 HIS HB3 H 2.80 0.01 2 446 . 41 HIS HD2 H 7.04 0.01 1 447 . 41 HIS HE1 H 7.66 0.01 1 448 . 41 HIS C C 180.8 0.15 1 449 . 41 HIS CA C 54.03 0.15 1 450 . 41 HIS CB C 29.80 0.15 1 451 . 41 HIS N N 118.7 0.20 1 452 . 42 PRO HA H 4.56 0.01 1 453 . 42 PRO HB2 H 1.99 0.01 2 454 . 42 PRO HB3 H 2.26 0.01 2 455 . 42 PRO HG2 H 2.06 0.01 2 456 . 42 PRO HG3 H 1.99 0.01 2 457 . 42 PRO HD2 H 3.62 0.01 2 458 . 42 PRO HD3 H 3.47 0.01 2 459 . 42 PRO C C 177.6 0.15 1 460 . 42 PRO CA C 65.2 0.15 1 461 . 42 PRO CB C 31.5 0.15 1 462 . 42 PRO CG C 27.1 0.15 1 463 . 42 PRO CD C 50.7 0.15 1 464 . 43 ASP H H 9.14 0.01 1 465 . 43 ASP HA H 4.34 0.01 1 466 . 43 ASP HB2 H 2.72 0.01 1 467 . 43 ASP HB3 H 2.63 0.01 1 468 . 43 ASP C C 177.1 0.01 1 469 . 43 ASP CA C 55.0 0.01 1 470 . 43 ASP CB C 39.3 0.01 1 471 . 43 ASP N N 117.8 0.20 1 472 . 44 LEU H H 7.34 0.01 1 473 . 44 LEU HA H 4.38 0.01 1 474 . 44 LEU HB2 H 1.28 0.01 1 475 . 44 LEU HB3 H 1.96 0.01 1 476 . 44 LEU HG H 1.77 0.01 1 477 . 44 LEU HD1 H 0.78 0.01 1 478 . 44 LEU HD2 H 0.70 0.01 1 479 . 44 LEU C C 178.1 0.15 1 480 . 44 LEU CA C 56.0 0.15 1 481 . 44 LEU CB C 42.9 0.15 1 482 . 44 LEU CG C 27.0 0.15 1 483 . 44 LEU CD1 C 22.9 0.15 1 484 . 44 LEU CD2 C 25.2 0.15 1 485 . 44 LEU N N 120.5 0.20 1 486 . 45 GLY H H 7.43 0.01 1 487 . 45 GLY HA2 H 4.41 0.01 2 488 . 45 GLY HA3 H 3.85 0.01 2 489 . 45 GLY C C 174.1 0.15 1 490 . 45 GLY CA C 44.6 0.15 1 491 . 45 GLY N N 107.2 0.20 1 492 . 46 ASN H H 8.66 0.01 1 493 . 46 ASN HA H 4.02 0.01 1 494 . 46 ASN HB2 H 2.71 0.01 1 495 . 46 ASN HB3 H 2.86 0.01 1 496 . 46 ASN HD21 H 7.04 0.01 9 497 . 46 ASN HD22 H 7.70 0.01 9 498 . 46 ASN C C 176.4 0.15 1 499 . 46 ASN CA C 57.2 0.15 1 500 . 46 ASN CB C 38.4 0.15 1 501 . 46 ASN N N 120.84 0.20 1 502 . 47 ALA H H 8.53 0.01 1 503 . 47 ALA HA H 4.17 0.01 1 504 . 47 ALA HB H 1.48 0.01 1 505 . 47 ALA C C 180.9 0.15 1 506 . 47 ALA CA C 55.5 0.15 1 507 . 47 ALA CB C 18.1 0.15 1 508 . 47 ALA N N 121.9 0.20 1 509 . 48 VAL H H 7.76 0.01 1 510 . 48 VAL HA H 3.71 0.01 1 511 . 48 VAL HB H 2.06 0.01 1 512 . 48 VAL HG1 H 1.07 0.01 1 513 . 48 VAL HG2 H 0.87 0.01 1 514 . 48 VAL C C 179.7 0.15 1 515 . 48 VAL CA C 65.7 0.15 1 516 . 48 VAL CB C 31.5 0.15 1 517 . 48 VAL CG1 C 23.0 0.15 1 518 . 48 VAL CG2 C 22.1 0.15 1 519 . 48 VAL N N 121.8 0.20 1 520 . 49 VAL H H 8.44 0.01 1 521 . 49 VAL HA H 3.42 0.01 1 522 . 49 VAL HB H 2.10 0.01 1 523 . 49 VAL HG1 H 1.13 0.01 1 524 . 49 VAL HG2 H 0.82 0.01 1 525 . 49 VAL C C 177.4 0.15 1 526 . 49 VAL CA C 68.1 0.15 1 527 . 49 VAL CB C 31.3 0.15 1 528 . 49 VAL CG1 C 25.1 0.15 1 529 . 49 VAL CG2 C 22.8 0.15 1 530 . 49 VAL N N 123.6 0.20 1 531 . 50 ASN H H 8.48 0.01 1 532 . 50 ASN HA H 4.37 0.01 1 533 . 50 ASN HB2 H 2.80 0.01 1 534 . 50 ASN HB3 H 2.87 0.01 1 535 . 50 ASN HD21 H 6.64 0.01 9 536 . 50 ASN HD22 H 7.51 0.01 9 537 . 50 ASN C C 179.3 0.15 1 538 . 50 ASN CA C 56.2 0.15 1 539 . 50 ASN CB C 37.4 0.15 1 540 . 50 ASN N N 118.8 0.20 1 541 . 51 SER H H 8.47 0.01 1 542 . 51 SER HA H 4.26 0.01 1 543 . 51 SER HB2 H 3.98 0.01 1 544 . 51 SER HB3 H 3.98 0.01 1 545 . 51 SER C C 177.3 0.15 1 546 . 51 SER CA C 61.8 0.15 1 547 . 51 SER CB C 62.8 0.15 1 548 . 51 SER N N 117.6 0.20 1 549 . 52 ASN H H 8.00 0.01 1 550 . 52 ASN HA H 4.48 0.01 1 551 . 52 ASN HB2 H 2.11 0.01 1 552 . 52 ASN HB3 H 2.72 0.01 1 553 . 52 ASN HD21 H 7.15 0.01 9 554 . 52 ASN HD22 H 7.26 0.01 9 555 . 52 ASN C C 177.6 0.15 1 556 . 52 ASN CA C 57.6 0.15 1 557 . 52 ASN CB C 40.1 0.15 1 558 . 52 ASN N N 121.6 0.20 1 559 . 53 ILE H H 8.71 0.01 1 560 . 53 ILE HA H 3.51 0.01 1 561 . 53 ILE HB H 1.95 0.01 1 562 . 53 ILE HG12 H 2.06 0.01 2 563 . 53 ILE HG13 H 0.64 0.01 2 564 . 53 ILE HG2 H 0.83 0.01 1 565 . 53 ILE HD1 H 0.83 0.01 1 566 . 53 ILE C C 177.5 0.15 1 567 . 53 ILE CA C 67.5 0.15 1 568 . 53 ILE CB C 38.2 0.15 1 569 . 53 ILE CG1 C 30.6 0.15 1 570 . 53 ILE CG2 C 17.9 0.15 1 571 . 53 ILE CD1 C 14.1 0.15 1 572 . 53 ILE N N 123.5 0.20 1 573 . 54 GLY H H 7.66 0.01 1 574 . 54 GLY HA2 H 3.76 0.01 2 575 . 54 GLY HA3 H 3.99 0.01 2 576 . 54 GLY C C 176.8 0.15 1 577 . 54 GLY CA C 47.7 0.15 1 578 . 54 GLY N N 106.2 0.20 1 579 . 55 VAL H H 7.83 0.01 1 580 . 55 VAL HA H 3.68 0.01 1 581 . 55 VAL HB H 2.23 0.01 1 582 . 55 VAL HG1 H 1.09 0.01 1 583 . 55 VAL HG2 H 0.95 0.01 1 584 . 55 VAL C C 177.4 0.15 1 585 . 55 VAL CA C 66.8 0.15 1 586 . 55 VAL CB C 31.8 0.15 1 587 . 55 VAL CG1 C 22.5 0.15 1 588 . 55 VAL CG2 C 21.9 0.15 1 589 . 55 VAL N N 124.3 0.20 1 590 . 56 LEU H H 7.69 0.01 1 591 . 56 LEU HA H 3.84 0.01 1 592 . 56 LEU HB2 H 1.21 0.01 1 593 . 56 LEU HB3 H 2.17 0.01 1 594 . 56 LEU HG H 1.95 0.01 1 595 . 56 LEU HD1 H 0.85 0.01 1 596 . 56 LEU HD2 H 0.85 0.01 1 597 . 56 LEU C C 179.4 0.15 1 598 . 56 LEU CA C 58.6 0.15 1 599 . 56 LEU CB C 42.5 0.15 1 600 . 56 LEU CG C 27.0 0.15 1 601 . 56 LEU CD1 C 25.9 0.15 1 602 . 56 LEU CD2 C 24.8 0.15 1 603 . 56 LEU N N 120.3 0.20 1 604 . 57 ILE H H 8.17 0.01 1 605 . 57 ILE HA H 4.47 0.01 1 606 . 57 ILE HB H 1.90 0.01 1 607 . 57 ILE HG12 H 1.67 0.01 2 608 . 57 ILE HG13 H 0.74 0.01 2 609 . 57 ILE HG2 H 1.00 0.01 1 610 . 57 ILE HD1 H 0.74 0.01 1 611 . 57 ILE C C 180.9 0.15 1 612 . 57 ILE CA C 64.3 0.15 1 613 . 57 ILE CB C 38.6 0.15 1 614 . 57 ILE CG1 C 29.0 0.15 1 615 . 57 ILE CG2 C 16.8 0.15 1 616 . 57 ILE CD1 C 14.2 0.15 1 617 . 57 ILE N N 121.5 0.20 1 618 . 58 LYS H H 8.44 0.01 1 619 . 58 LYS HA H 4.12 0.01 1 620 . 58 LYS HB2 H 2.04 0.01 1 621 . 58 LYS HB3 H 2.04 0.01 1 622 . 58 LYS HG2 H 1.56 0.01 1 623 . 58 LYS HG3 H 1.56 0.01 1 624 . 58 LYS HD2 H 1.72 0.01 1 625 . 58 LYS HD3 H 1.72 0.01 1 626 . 58 LYS HE2 H 3.00 0.01 1 627 . 58 LYS HE3 H 3.00 0.01 1 628 . 58 LYS C C 179.1 0.15 1 629 . 58 LYS CA C 59.7 0.15 1 630 . 58 LYS CB C 32.3 0.15 1 631 . 58 LYS CG C 25.4 0.15 1 632 . 58 LYS CD C 29.3 0.15 1 633 . 58 LYS CE C 42.2 0.15 1 634 . 58 LYS N N 125.7 0.20 1 635 . 59 LYS H H 8.29 0.01 1 636 . 59 LYS HA H 4.32 0.01 1 637 . 59 LYS HB2 H 2.04 0.01 2 638 . 59 LYS HB3 H 1.74 0.01 2 639 . 59 LYS HG2 H 1.60 0.01 1 640 . 59 LYS HG3 H 1.60 0.01 1 641 . 59 LYS HD2 H 1.47 0.01 1 642 . 59 LYS HD3 H 1.47 0.01 1 643 . 59 LYS HE2 H 3.05 0.01 2 644 . 59 LYS HE3 H 2.88 0.01 2 645 . 59 LYS C C 176.4 0.15 1 646 . 59 LYS CA C 56.5 0.15 1 647 . 59 LYS CB C 33.1 0.15 1 648 . 59 LYS CG C 25.8 0.15 1 649 . 59 LYS CD C 29.0 0.15 1 650 . 59 LYS CE C 42.1 0.15 1 651 . 59 LYS N N 116.1 0.20 1 652 . 60 GLY H H 8.04 0.01 1 653 . 60 GLY HA2 H 4.05 0.01 2 654 . 60 GLY HA3 H 4.14 0.01 2 655 . 60 GLY C C 174.9 0.15 1 656 . 60 GLY CA C 46.1 0.15 1 657 . 60 GLY N N 108.3 0.20 1 658 . 61 LEU H H 8.15 0.01 1 659 . 61 LEU HA H 4.40 0.01 1 660 . 61 LEU HB2 H 1.51 0.01 2 661 . 61 LEU HB3 H 1.81 0.01 2 662 . 61 LEU HG H 1.51 0.01 1 663 . 61 LEU HD1 H 0.69 0.01 1 664 . 61 LEU HD2 H 0.82 0.01 1 665 . 61 LEU C C 174.6 0.15 1 666 . 61 LEU CA C 55.6 0.15 1 667 . 61 LEU CB C 43.4 0.15 1 668 . 61 LEU CG C 27.3 0.15 1 669 . 61 LEU CD1 C 22.8 0.15 1 670 . 61 LEU CD2 C 26.5 0.15 1 671 . 61 LEU N N 119.6 0.20 1 672 . 62 VAL H H 7.03 0.01 1 673 . 62 VAL HA H 4.76 0.01 1 674 . 62 VAL HB H 1.39 0.01 1 675 . 62 VAL HG1 H 0.78 0.01 1 676 . 62 VAL HG2 H 0.82 0.01 1 677 . 62 VAL C C 173.1 0.15 1 678 . 62 VAL CA C 59.3 0.15 1 679 . 62 VAL CB C 37.3 0.15 1 680 . 62 VAL CG1 C 24.9 0.15 1 681 . 62 VAL CG2 C 23.4 0.15 1 682 . 62 VAL N N 118.6 0.20 1 683 . 63 GLU H H 9.31 0.01 1 684 . 63 GLU HA H 4.70 0.01 1 685 . 63 GLU HB2 H 1.82 0.01 1 686 . 63 GLU HB3 H 1.82 0.01 1 687 . 63 GLU HG2 H 2.03 0.01 1 688 . 63 GLU HG3 H 2.03 0.01 1 689 . 63 GLU C C 174.0 0.15 1 690 . 63 GLU CA C 54.2 0.15 1 691 . 63 GLU CB C 33.9 0.15 1 692 . 63 GLU CG C 36.2 0.15 1 693 . 63 GLU N N 125.8 0.20 1 694 . 64 LYS H H 8.58 0.01 1 695 . 64 LYS HA H 4.89 0.01 1 696 . 64 LYS HB2 H 1.53 0.01 2 697 . 64 LYS HB3 H 1.88 0.01 2 698 . 64 LYS HG2 H 1.36 0.01 1 699 . 64 LYS HG3 H 1.36 0.01 1 700 . 64 LYS HD2 H 1.68 0.01 1 701 . 64 LYS HD3 H 1.68 0.01 1 702 . 64 LYS HE2 H 2.96 0.01 1 703 . 64 LYS HE3 H 2.96 0.01 1 704 . 64 LYS C C 176.7 0.15 1 705 . 64 LYS CA C 55.9 0.15 1 706 . 64 LYS CB C 33.7 0.15 1 707 . 64 LYS CG C 25.3 0.15 1 708 . 64 LYS CD C 29.5 0.15 1 709 . 64 LYS CE C 42.0 0.15 1 710 . 64 LYS N N 122.6 0.20 1 711 . 65 SER H H 8.56 0.01 1 712 . 65 SER HA H 4.61 0.01 1 713 . 65 SER HB2 H 3.65 0.01 1 714 . 65 SER HB3 H 3.70 0.01 1 715 . 65 SER C C 174.8 0.15 1 716 . 65 SER CA C 56.9 0.15 1 717 . 65 SER CB C 63.8 0.15 1 718 . 65 SER N N 121.4 0.20 1 719 . 66 GLY H H 9.05 0.01 1 720 . 66 GLY HA2 H 3.70 0.01 2 721 . 66 GLY HA3 H 4.02 0.01 2 722 . 66 GLY C C 174.9 0.15 1 723 . 66 GLY CA C 47.23 0.15 1 724 . 66 GLY N N 119.42 0.20 1 725 . 67 ASP H H 8.91 0.01 1 726 . 67 ASP HA H 4.78 0.01 1 727 . 67 ASP HB2 H 2.63 0.01 2 728 . 67 ASP HB3 H 2.87 0.01 2 729 . 67 ASP C C 175.8 0.15 1 730 . 67 ASP CA C 54.7 0.15 1 731 . 67 ASP CB C 41.4 0.15 1 732 . 67 ASP N N 127.5 0.20 1 733 . 68 GLY H H 8.24 0.01 1 734 . 68 GLY HA2 H 3.51 0.01 2 735 . 68 GLY HA3 H 4.45 0.01 2 736 . 68 GLY C C 172.3 0.15 1 737 . 68 GLY CA C 45.3 0.15 1 738 . 68 GLY N N 109.3 0.20 1 739 . 69 LEU H H 8.67 0.01 1 740 . 69 LEU HA H 5.14 0.01 1 741 . 69 LEU HB2 H 1.01 0.01 1 742 . 69 LEU HB3 H 1.79 0.01 1 743 . 69 LEU HG H 1.69 0.01 1 744 . 69 LEU HD1 H 0.70 0.01 1 745 . 69 LEU HD2 H 0.70 0.01 1 746 . 69 LEU C C 175.1 0.15 1 747 . 69 LEU CA C 54.0 0.15 1 748 . 69 LEU CB C 44.9 0.15 1 749 . 69 LEU CG C 27.0 0.15 1 750 . 69 LEU CD1 C 26.1 0.15 1 751 . 69 LEU CD2 C 23.3 0.15 1 752 . 69 LEU N N 125.1 0.20 1 753 . 70 ILE H H 8.57 0.01 1 754 . 70 ILE HA H 4.90 0.01 1 755 . 70 ILE HB H 1.43 0.01 1 756 . 70 ILE HG12 H 1.29 0.01 2 757 . 70 ILE HG13 H 1.06 0.01 2 758 . 70 ILE HG2 H 0.66 0.01 1 759 . 70 ILE HD1 H 0.55 0.01 1 760 . 70 ILE C C 174.9 0.15 1 761 . 70 ILE CA C 58.9 0.15 1 762 . 70 ILE CB C 42.6 0.15 1 763 . 70 ILE CG1 C 26.9 0.15 1 764 . 70 ILE CG2 C 17.1 0.15 1 765 . 70 ILE CD1 C 14.1 0.15 1 766 . 70 ILE N N 117.8 0.20 1 767 . 71 ILE H H 8.36 0.01 1 768 . 71 ILE HA H 4.94 0.01 1 769 . 71 ILE HB H 2.15 0.01 1 770 . 71 ILE HG12 H 1.41 0.01 1 771 . 71 ILE HG13 H 1.41 0.01 1 772 . 71 ILE HG2 H 0.87 0.01 1 773 . 71 ILE HD1 H 0.78 0.01 1 774 . 71 ILE C C 176.4 0.15 1 775 . 71 ILE CA C 61.8 0.15 1 776 . 71 ILE CB C 39.0 0.15 1 777 . 71 ILE CG1 C 25.0 0.15 1 778 . 71 ILE CG2 C 19.0 0.15 1 779 . 71 ILE CD1 C 14.9 0.15 1 780 . 71 ILE N N 118.8 0.20 1 781 . 72 THR H H 7.52 0.01 1 782 . 72 THR HA H 4.61 0.01 1 783 . 72 THR HB H 4.76 0.01 1 784 . 72 THR HG2 H 0.94 0.01 1 785 . 72 THR C C 176.3 0.15 1 786 . 72 THR CA C 59.8 0.15 1 787 . 72 THR CB C 71.9 0.15 1 788 . 72 THR CG2 C 21.4 0.15 1 789 . 72 THR N N 112.3 0.20 1 790 . 73 GLY H H 8.96 0.01 1 791 . 73 GLY HA2 H 3.98 0.01 2 792 . 73 GLY HA3 H 3.86 0.01 2 793 . 73 GLY C C 176.2 0.15 1 794 . 73 GLY CA C 47.6 0.15 1 795 . 73 GLY N N 109.6 0.20 1 796 . 74 GLU H H 8.35 0.01 1 797 . 74 GLU HA H 4.15 0.01 1 798 . 74 GLU HB2 H 2.04 0.01 2 799 . 74 GLU HB3 H 1.81 0.01 2 800 . 74 GLU HG2 H 2.36 0.01 1 801 . 74 GLU HG3 H 2.36 0.01 1 802 . 74 GLU C C 179.5 0.15 1 803 . 74 GLU CA C 59.8 0.15 1 804 . 74 GLU CB C 29.6 0.15 1 805 . 74 GLU CG C 36.7 0.15 1 806 . 74 GLU N N 122.4 0.20 1 807 . 75 ALA H H 7.20 0.01 1 808 . 75 ALA HA H 4.03 0.01 1 809 . 75 ALA HB H 1.88 0.01 1 810 . 75 ALA C C 179.0 0.15 1 811 . 75 ALA CA C 55.0 0.15 1 812 . 75 ALA CB C 20.7 0.15 1 813 . 75 ALA N N 122.1 0.20 1 814 . 76 GLN H H 8.37 0.01 1 815 . 76 GLN HA H 3.90 0.01 1 816 . 76 GLN HB2 H 2.24 0.01 1 817 . 76 GLN HB3 H 2.24 0.01 1 818 . 76 GLN HG2 H 2.42 0.01 1 819 . 76 GLN HG3 H 2.42 0.01 1 820 . 76 GLN HE21 H 6.75 0.01 9 821 . 76 GLN HE22 H 7.25 0.01 9 822 . 76 GLN C C 178.6 0.15 1 823 . 76 GLN CA C 59.3 0.15 1 824 . 76 GLN CB C 28.0 0.15 1 825 . 76 GLN CG C 33.8 0.15 1 826 . 76 GLN N N 119.3 0.20 1 827 . 77 ASP H H 7.97 0.01 1 828 . 77 ASP HA H 4.44 0.01 1 829 . 77 ASP HB2 H 2.68 0.01 1 830 . 77 ASP HB3 H 2.81 0.01 1 831 . 77 ASP C C 178.2 0.15 1 832 . 77 ASP CA C 57.5 0.15 1 833 . 77 ASP CB C 40.4 0.15 1 834 . 77 ASP N N 121.2 0.20 1 835 . 78 ILE H H 7.38 0.01 1 836 . 78 ILE HA H 3.73 0.01 1 837 . 78 ILE HB H 1.98 0.01 1 838 . 78 ILE HG12 H 1.98 0.01 2 839 . 78 ILE HG13 H 0.80 0.01 2 840 . 78 ILE HG2 H 0.78 0.01 1 841 . 78 ILE HD1 H 0.80 0.01 1 842 . 78 ILE C C 177.5 0.15 1 843 . 78 ILE CA C 65.9 0.15 1 844 . 78 ILE CB C 38.6 0.15 1 845 . 78 ILE CG1 C 29.6 0.15 1 846 . 78 ILE CG2 C 18.0 0.15 1 847 . 78 ILE CD1 C 14.3 0.15 1 848 . 78 ILE N N 122.2 0.20 1 849 . 79 ILE H H 8.24 0.01 1 850 . 79 ILE HA H 3.46 0.01 1 851 . 79 ILE HB H 1.88 0.01 1 852 . 79 ILE HG12 H 1.68 0.01 2 853 . 79 ILE HG13 H 0.87 0.01 2 854 . 79 ILE HG2 H 0.87 0.01 1 855 . 79 ILE HD1 H 0.70 0.01 1 856 . 79 ILE C C 178.8 0.15 1 857 . 79 ILE CA C 65.9 0.15 1 858 . 79 ILE CB C 37.9 0.15 1 859 . 79 ILE CG1 C 29.8 0.15 1 860 . 79 ILE CG2 C 17.2 0.15 1 861 . 79 ILE CD1 C 13.3 0.15 1 862 . 79 ILE N N 121.3 0.20 1 863 . 80 SER H H 8.71 0.01 1 864 . 80 SER HA H 4.28 0.01 1 865 . 80 SER HB2 H 4.03 0.01 1 866 . 80 SER HB3 H 4.03 0.01 1 867 . 80 SER C C 177.4 0.15 1 868 . 80 SER CA C 61.9 0.15 1 869 . 80 SER CB C 62.8 0.15 1 870 . 80 SER N N 118.1 0.20 1 871 . 81 ASN H H 8.55 0.01 1 872 . 81 ASN HA H 4.58 0.01 1 873 . 81 ASN HB2 H 2.83 0.01 1 874 . 81 ASN HB3 H 3.05 0.01 1 875 . 81 ASN HD21 H 6.90 0.01 9 876 . 81 ASN HD22 H 7.69 0.01 9 877 . 81 ASN C C 178.0 0.15 1 878 . 81 ASN CA C 56.0 0.15 1 879 . 81 ASN CB C 38.0 0.15 1 880 . 81 ASN N N 123.1 0.20 1 881 . 82 ALA H H 8.76 0.01 1 882 . 82 ALA HA H 4.01 0.01 1 883 . 82 ALA HB H 1.47 0.01 1 884 . 82 ALA C C 179.0 0.15 1 885 . 82 ALA CA C 55.6 0.15 1 886 . 82 ALA CB C 19.2 0.15 1 887 . 82 ALA N N 124.7 0.20 1 888 . 83 ALA H H 7.86 0.01 1 889 . 83 ALA HA H 4.09 0.01 1 890 . 83 ALA HB H 1.60 0.01 1 891 . 83 ALA C C 180.7 0.15 1 892 . 83 ALA CA C 55.4 0.15 1 893 . 83 ALA CB C 18.0 0.15 1 894 . 83 ALA N N 122.2 0.20 1 895 . 84 THR H H 7.95 0.01 1 896 . 84 THR HA H 3.98 0.01 1 897 . 84 THR HB H 4.38 0.01 1 898 . 84 THR HG2 H 1.26 0.01 1 899 . 84 THR C C 176.1 0.15 1 900 . 84 THR CA C 66.5 0.15 1 901 . 84 THR CB C 68.6 0.15 1 902 . 84 THR CG2 C 22.1 0.15 1 903 . 84 THR N N 118.5 0.20 1 904 . 85 LEU H H 8.09 0.01 1 905 . 85 LEU HA H 4.09 0.01 1 906 . 85 LEU HB2 H 1.99 0.01 1 907 . 85 LEU HB3 H 1.65 0.01 1 908 . 85 LEU HG H 1.90 0.01 1 909 . 85 LEU HD1 H 0.99 0.01 1 910 . 85 LEU HD2 H 0.91 0.01 1 911 . 85 LEU C C 178.9 0.15 1 912 . 85 LEU CA C 58.0 0.15 1 913 . 85 LEU CB C 42.5 0.15 1 914 . 85 LEU CG C 26.7 0.15 1 915 . 85 LEU CD1 C 25.1 0.15 1 916 . 85 LEU CD2 C 22.9 0.15 1 917 . 85 LEU N N 123.3 0.20 1 918 . 86 TYR H H 8.05 0.01 1 919 . 86 TYR HA H 3.27 0.01 1 920 . 86 TYR HB2 H 2.81 0.01 1 921 . 86 TYR HB3 H 2.38 0.01 1 922 . 86 TYR HD1 H 6.79 0.01 1 923 . 86 TYR HD2 H 6.79 0.01 1 924 . 86 TYR HE1 H 6.77 0.01 1 925 . 86 TYR HE2 H 6.77 0.01 1 926 . 86 TYR C C 177.5 0.15 1 927 . 86 TYR CA C 60.9 0.15 1 928 . 86 TYR CB C 38.1 0.15 1 929 . 86 TYR CD1 C 133.1 0.15 1 930 . 86 TYR CD2 C 133.1 0.15 1 931 . 86 TYR CE1 C 118.1 0.15 1 932 . 86 TYR CE2 C 118.1 0.15 1 933 . 86 TYR N N 120.3 0.20 1 934 . 87 ALA H H 7.88 0.01 1 935 . 87 ALA HA H 3.92 0.01 1 936 . 87 ALA HB H 1.52 0.01 1 937 . 87 ALA C C 179.3 0.15 1 938 . 87 ALA CA C 54.7 0.15 1 939 . 87 ALA CB C 18.5 0.15 1 940 . 87 ALA N N 122.6 0.20 1 941 . 88 GLN H H 7.92 0.01 1 942 . 88 GLN HA H 4.06 0.01 1 943 . 88 GLN HB2 H 2.19 0.01 2 944 . 88 GLN HB3 H 2.16 0.01 2 945 . 88 GLN HG2 H 2.59 0.01 2 946 . 88 GLN HG3 H 2.43 0.01 2 947 . 88 GLN HE21 H 6.76 0.01 9 948 . 88 GLN HE22 H 7.40 0.01 9 949 . 88 GLN C C 177.6 0.15 1 950 . 88 GLN CA C 58.0 0.15 1 951 . 88 GLN CB C 28.8 0.15 1 952 . 88 GLN CG C 34.3 0.15 1 953 . 88 GLN N N 117.1 0.20 1 954 . 89 GLU H H 7.56 0.01 1 955 . 89 GLU HA H 4.25 0.01 1 956 . 89 GLU HB2 H 1.92 0.01 2 957 . 89 GLU HB3 H 2.08 0.01 2 958 . 89 GLU HG2 H 2.50 0.01 2 959 . 89 GLU HG3 H 2.28 0.01 2 960 . 89 GLU C C 176.5 0.15 1 961 . 89 GLU CA C 57.6 0.15 1 962 . 89 GLU CB C 30.6 0.15 1 963 . 89 GLU CG C 36.7 0.15 1 964 . 89 GLU N N 118.1 0.20 1 965 . 90 ASN H H 7.66 0.01 1 966 . 90 ASN HA H 4.75 0.01 1 967 . 90 ASN HB2 H 2.08 0.01 2 968 . 90 ASN HB3 H 2.52 0.01 2 969 . 90 ASN HD21 H 6.57 0.01 9 970 . 90 ASN HD22 H 6.96 0.01 9 971 . 90 ASN C C 173.8 0.15 1 972 . 90 ASN CA C 53.2 0.15 1 973 . 90 ASN CB C 39.9 0.15 1 974 . 90 ASN N N 118.0 0.20 1 975 . 91 ALA H H 7.92 0.01 1 976 . 91 ALA HA H 4.54 0.01 1 977 . 91 ALA HB H 1.38 0.01 1 978 . 91 ALA C C 175.2 0.15 1 979 . 91 ALA CA C 52.0 0.15 1 980 . 91 ALA CB C 17.9 0.15 1 981 . 91 ALA N N 125.9 0.20 1 982 . 92 PRO HA H 4.31 0.01 1 983 . 92 PRO HB2 H 1.92 0.01 2 984 . 92 PRO HB3 H 2.29 0.01 2 985 . 92 PRO HG2 H 1.97 0.01 1 986 . 92 PRO HG3 H 1.97 0.01 1 987 . 92 PRO HD2 H 3.70 0.01 1 988 . 92 PRO HD3 H 3.70 0.01 1 989 . 92 PRO C C 177.5 0.15 1 990 . 92 PRO CA C 64.2 0.15 1 991 . 92 PRO CB C 31.8 0.15 1 992 . 92 PRO CG C 27.5 0.15 1 993 . 92 PRO CD C 50.4 0.15 1 994 . 93 GLU H H 8.60 0.01 1 995 . 93 GLU HA H 4.21 0.01 1 996 . 93 GLU HB2 H 2.04 0.01 2 997 . 93 GLU HB3 H 1.98 0.01 2 998 . 93 GLU HG2 H 2.31 0.01 2 999 . 93 GLU HG3 H 2.25 0.01 2 1000 . 93 GLU C C 176.7 0.15 1 1001 . 93 GLU CA C 57.4 0.15 1 1002 . 93 GLU CB C 29.8 0.15 1 1003 . 93 GLU CG C 36.2 0.15 1 1004 . 93 GLU N N 120.8 0.20 1 1005 . 94 LEU H H 8.09 0.01 1 1006 . 94 LEU HA H 4.34 0.01 1 1007 . 94 LEU HB2 H 1.62 0.01 1 1008 . 94 LEU HB3 H 1.62 0.01 1 1009 . 94 LEU HG H 1.62 0.01 1 1010 . 94 LEU HD1 H 0.89 0.01 2 1011 . 94 LEU HD2 H 0.85 0.01 2 1012 . 94 LEU C C 177.1 0.15 1 1013 . 94 LEU CA C 55.3 0.15 1 1014 . 94 LEU CB C 42.3 0.15 1 1015 . 94 LEU CG C 27.2 0.15 1 1016 . 94 LEU CD1 C 25.0 0.15 2 1017 . 94 LEU CD2 C 23.6 0.15 2 1018 . 94 LEU N N 123.4 0.20 1 1019 . 95 LEU H H 7.96 0.01 1 1020 . 95 LEU HA H 4.34 0.01 1 1021 . 95 LEU HB2 H 1.65 0.01 2 1022 . 95 LEU HB3 H 1.59 0.01 2 1023 . 95 LEU HG H 1.59 0.01 1 1024 . 95 LEU HD1 H 0.90 0.01 2 1025 . 95 LEU HD2 H 0.74 0.01 2 1026 . 95 LEU C C 176.0 0.15 1 1027 . 95 LEU CA C 55.2 0.15 1 1028 . 95 LEU CB C 42.1 0.15 1 1029 . 95 LEU CG C 27.1 0.15 1 1030 . 95 LEU CD1 C 25.1 0.15 2 1031 . 95 LEU CD2 C 23.8 0.15 2 1032 . 95 LEU N N 123.3 0.20 1 1033 . 96 LYS H H 7.63 0.01 1 1034 . 96 LYS HA H 4.09 0.01 1 1035 . 96 LYS HB2 H 1.67 0.01 2 1036 . 96 LYS HB3 H 1.79 0.01 2 1037 . 96 LYS HG2 H 1.36 0.01 1 1038 . 96 LYS HG3 H 1.36 0.01 1 1039 . 96 LYS HD2 H 1.63 0.01 1 1040 . 96 LYS HD3 H 1.63 0.01 1 1041 . 96 LYS HE2 H 3.00 0.01 1 1042 . 96 LYS HE3 H 3.00 0.01 1 1043 . 96 LYS CA C 57.8 0.15 1 1044 . 96 LYS CB C 33.9 0.15 1 1045 . 96 LYS N N 127.9 0.20 1 stop_ save_