data_6478 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The N-domain of the transcription factor AbrB ; _BMRB_accession_number 6478 _BMRB_flat_file_name bmr6478.str _Entry_type original _Submission_date 2005-02-02 _Accession_date 2005-02-08 _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 Coles Murray . . 2 Truffault Vincent . . 3 Lupas Andrei N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 326 "13C chemical shifts" 222 "15N chemical shifts" 55 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-06-12 original author . stop_ _Original_release_date 2005-06-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; AbrB-like Transcription Factors Assume a Swapped Hairpin Fold that Is Evolutionarily Related to Double-Psi beta Barrels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15939023 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Coles Murray . . 2 Djuranovic Sergej . . 3 Soding Johannes . . 4 Frickey Tancred . . 5 Koretke Kristin . . 6 Truffault Vincent . . 7 Martin Joerg . . 8 Lupas Andrei N. . stop_ _Journal_abbreviation 'Structure (Camb)' _Journal_volume 13 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 919 _Page_last 928 _Year 2005 _Details . loop_ _Keyword NMR Homodimer Bioinformatics stop_ save_ ################################## # Molecular system description # ################################## save_system_abrB _Saveframe_category molecular_system _Mol_system_name 'Transition state regulatory protein abrB' _Abbreviation_common 'Transition state regulatory protein abrB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Transition state regulatory protein abrB, chain A' $abrB 'Transition state regulatory protein abrB, chain B' $abrB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state homodimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Transition state regulatory protein abrB, chain A' 1 'Transition state regulatory protein abrB, chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_abrB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Transition state regulatory protein abrB' _Abbreviation_common 'Transition state regulatory protein abrB' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; MFMKSTGIVRKVDELGRVVI PIELRRTLGIAEKDALEIYV DDEKIILKKYKPN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PHE 3 MET 4 LYS 5 SER 6 THR 7 GLY 8 ILE 9 VAL 10 ARG 11 LYS 12 VAL 13 ASP 14 GLU 15 LEU 16 GLY 17 ARG 18 VAL 19 VAL 20 ILE 21 PRO 22 ILE 23 GLU 24 LEU 25 ARG 26 ARG 27 THR 28 LEU 29 GLY 30 ILE 31 ALA 32 GLU 33 LYS 34 ASP 35 ALA 36 LEU 37 GLU 38 ILE 39 TYR 40 VAL 41 ASP 42 ASP 43 GLU 44 LYS 45 ILE 46 ILE 47 LEU 48 LYS 49 LYS 50 TYR 51 LYS 52 PRO 53 ASN 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 17650 ba 96.23 94 100.00 100.00 1.22e-25 BMRB 4281 AbrBN 96.23 53 100.00 100.00 1.44e-25 PDB 1YFB "The Solution Structure Of The N-Domain Of The Transcription Factor Abrb" 98.11 59 100.00 100.00 3.09e-27 PDB 1YSF "The Solution Structure Of The N-Domain Of The Transcription Factor Abrb" 98.11 59 100.00 100.00 3.09e-27 PDB 1Z0R "Solution Structure Of The N-Terminal Dna Recognition Domain Of The Bacillus Subtilis Transcription-State Regulator Abrb" 96.23 53 100.00 100.00 1.44e-25 PDB 2K1N "Dna Bound Structure Of The N-Terminal Domain Of Abrb" 96.23 55 100.00 100.00 1.11e-25 PDB 2RO4 "Rdc-Refined Solution Structure Of The N-Terminal Dna Recognition Domain Of The Bacillus Subtilis Transition-State Regulator Abr" 96.23 53 100.00 100.00 1.44e-25 DBJ BAA05272 "transition state regulatory protein [Bacillus subtilis]" 100.00 96 100.00 100.00 7.34e-28 DBJ BAI83483 "transcriptional regulator [Bacillus subtilis subsp. natto BEST195]" 100.00 96 100.00 100.00 7.34e-28 DBJ BAL15827 "transition state transcriptional regulatory protein AbrB [Bacillus cereus NC7401]" 96.23 94 100.00 100.00 9.72e-26 DBJ BAM48968 "transcriptional regulator [Bacillus subtilis BEST7613]" 96.23 94 100.00 100.00 6.31e-26 DBJ BAM56238 "transcriptional regulator [Bacillus subtilis BEST7003]" 96.23 94 100.00 100.00 6.31e-26 EMBL CAA31307 "unnamed protein product [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 7.34e-28 EMBL CAA43955 "abrB [Bacillus subtilis]" 96.23 94 100.00 100.00 6.31e-26 EMBL CAB11813 "transcriptional regulator for transition state genes [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 7.34e-28 EMBL CBI41163 "transcriptional regulator for transition state genes [Bacillus amyloliquefaciens DSM 7]" 96.23 94 100.00 100.00 5.91e-26 EMBL CCF03572 "Transition state regulatory protein abrB [Bacillus amyloliquefaciens subsp. plantarum CAU B946]" 96.23 94 100.00 100.00 5.91e-26 GB AAA22195 "abrB protein [Bacillus subtilis]" 96.23 94 100.00 100.00 6.31e-26 GB AAP07140 "Transcription state regulatory protein abrB [Bacillus cereus ATCC 14579]" 96.23 94 100.00 100.00 9.72e-26 GB AAP24090 "transition state transcriptional regulatory protein AbrB [Bacillus anthracis str. Ames]" 96.23 94 100.00 100.00 1.22e-25 GB AAS38971 "transition state transcriptional regulatory protein AbrB [Bacillus cereus ATCC 10987]" 96.23 94 100.00 100.00 9.72e-26 GB AAT29114 "transition state transcriptional regulatory protein AbrB [Bacillus anthracis str. 'Ames Ancestor']" 96.23 94 100.00 100.00 1.22e-25 PRF 1715209A "transcription regulator AbrB" 96.23 94 100.00 100.00 6.31e-26 REF NP_387918 "transition state regulatory protein AbrB [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 7.34e-28 REF NP_829939 "transcription state transcriptional regulator AbrB [Bacillus cereus ATCC 14579]" 96.23 94 100.00 100.00 9.72e-26 REF NP_842604 "transition state transcriptional regulatory protein AbrB [Bacillus anthracis str. Ames]" 96.23 94 100.00 100.00 1.22e-25 REF NP_976363 "transition state transcriptional regulatory protein AbrB [Bacillus cereus ATCC 10987]" 96.23 94 100.00 100.00 9.72e-26 REF WP_000843034 "transition state regulator Abh [Bacillus anthracis]" 96.23 94 100.00 100.00 1.23e-25 SP P08874 "RecName: Full=Transition state regulatory protein AbrB [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 7.34e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $abrB 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $abrB 'recombinant technology' . Esherichia coli . plasmid pet30b 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 $abrB 0.5 mM [U-15N] KPO4 20.0 mM . KCl 50.0 mM . NaN3 0.02 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $abrB 0.25 mM [U-15N] $abrB 0.25 mM [U-13C] KPO4 20.0 mM . KCl 50.0 mM . NaN3 0.02 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task collection processing stop_ _Details . save_ save_NMRview _Saveframe_category software _Name NMRview _Version . loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 2.9.7 loop_ _Task 'structure solution' refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 900 _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.2 pH temperature 305 0.1 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 external direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Transition state regulatory protein abrB, chain A' _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 . 1 MET HE H 1.85 0.02 1 2 . 1 MET CE C 16.76 0.05 1 3 . 2 PHE H H 8.47 0.02 1 4 . 2 PHE HA H 4.46 0.02 1 5 . 2 PHE HB2 H 3.09 0.02 2 6 . 2 PHE HB3 H 2.98 0.02 2 7 . 2 PHE HD1 H 7.20 0.02 1 8 . 2 PHE HD2 H 7.20 0.02 1 9 . 2 PHE HE1 H 7.28 0.02 1 10 . 2 PHE HE2 H 7.28 0.02 1 11 . 2 PHE C C 171.50 0.05 1 12 . 2 PHE CA C 54.89 0.05 1 13 . 2 PHE CB C 36.94 0.05 1 14 . 2 PHE N N 123.10 0.05 1 15 . 3 MET H H 8.39 0.02 1 16 . 3 MET HA H 4.60 0.02 1 17 . 3 MET HE H 2.04 0.02 1 18 . 3 MET CE C 16.76 0.05 1 19 . 3 MET N N 122.01 0.05 1 20 . 4 LYS H H 8.20 0.02 1 21 . 4 LYS HA H 4.49 0.02 1 22 . 4 LYS N N 122.13 0.05 1 23 . 5 SER H H 8.52 0.02 1 24 . 5 SER HA H 4.28 0.02 1 25 . 5 SER HB2 H 3.79 0.02 2 26 . 5 SER HB3 H 3.76 0.02 2 27 . 5 SER CA C 55.85 0.05 1 28 . 5 SER CB C 61.04 0.05 1 29 . 5 SER N N 117.73 0.05 1 30 . 6 THR H H 8.20 0.02 1 31 . 6 THR HA H 4.38 0.02 1 32 . 6 THR HB H 4.23 0.02 1 33 . 6 THR HG2 H 1.22 0.02 1 34 . 6 THR C C 172.91 0.05 1 35 . 6 THR CA C 59.63 0.05 1 36 . 6 THR CB C 67.64 0.05 1 37 . 6 THR CG2 C 19.08 0.05 1 38 . 6 THR N N 115.39 0.05 1 39 . 7 GLY H H 8.76 0.02 1 40 . 7 GLY HA2 H 4.00 0.02 2 41 . 7 GLY HA3 H 3.85 0.02 2 42 . 7 GLY CA C 42.61 0.05 1 43 . 7 GLY N N 111.39 0.05 1 44 . 8 ILE H H 8.40 0.02 1 45 . 8 ILE HA H 4.11 0.02 1 46 . 8 ILE HB H 1.87 0.02 1 47 . 8 ILE HG12 H 1.54 0.02 2 48 . 8 ILE HG13 H 1.08 0.02 2 49 . 8 ILE HG2 H 0.84 0.02 1 50 . 8 ILE HD1 H 0.84 0.02 1 51 . 8 ILE C C 171.89 0.05 1 52 . 8 ILE CA C 58.55 0.05 1 53 . 8 ILE CB C 36.31 0.05 1 54 . 8 ILE CG1 C 24.60 0.05 1 55 . 8 ILE CG2 C 15.70 0.05 1 56 . 8 ILE CD1 C 10.80 0.05 1 57 . 8 ILE N N 122.41 0.05 1 58 . 9 VAL H H 8.16 0.02 1 59 . 9 VAL HA H 4.98 0.02 1 60 . 9 VAL HB H 1.61 0.02 1 61 . 9 VAL HG1 H 0.44 0.02 1 62 . 9 VAL HG2 H 0.32 0.02 1 63 . 9 VAL C C 174.62 0.05 1 64 . 9 VAL CA C 58.21 0.05 1 65 . 9 VAL CB C 30.85 0.05 1 66 . 9 VAL CG1 C 18.86 0.05 1 67 . 9 VAL CG2 C 18.17 0.05 1 68 . 9 VAL N N 126.51 0.05 1 69 . 10 ARG H H 9.11 0.02 1 70 . 10 ARG HA H 4.81 0.02 1 71 . 10 ARG HB2 H 2.02 0.02 1 72 . 10 ARG HB3 H 1.54 0.02 1 73 . 10 ARG HG2 H 1.79 0.02 2 74 . 10 ARG HG3 H 1.38 0.02 2 75 . 10 ARG HD2 H 3.55 0.02 2 76 . 10 ARG HD3 H 3.24 0.02 2 77 . 10 ARG HE H 7.24 0.02 1 78 . 10 ARG C C 175.11 0.05 1 79 . 10 ARG CA C 50.34 0.05 1 80 . 10 ARG CB C 32.23 0.05 1 81 . 10 ARG CG C 24.11 0.05 1 82 . 10 ARG CD C 40.67 0.05 1 83 . 10 ARG N N 127.25 0.05 1 84 . 10 ARG NE N 109.82 0.05 1 85 . 11 LYS H H 8.50 0.02 1 86 . 11 LYS HA H 4.95 0.02 1 87 . 11 LYS HB2 H 1.66 0.02 2 88 . 11 LYS HB3 H 1.61 0.02 2 89 . 11 LYS HG2 H 1.26 0.02 1 90 . 11 LYS HG3 H 1.26 0.02 1 91 . 11 LYS HD2 H 1.74 0.02 1 92 . 11 LYS HD3 H 1.74 0.02 1 93 . 11 LYS HE2 H 2.98 0.02 1 94 . 11 LYS HE3 H 2.98 0.02 1 95 . 11 LYS C C 174.01 0.05 1 96 . 11 LYS CA C 52.58 0.05 1 97 . 11 LYS CB C 31.74 0.05 1 98 . 11 LYS CG C 22.93 0.05 1 99 . 11 LYS CD C 26.54 0.05 1 100 . 11 LYS CE C 39.5 0.05 1 101 . 11 LYS N N 119.71 0.05 1 102 . 12 VAL H H 8.30 0.02 1 103 . 12 VAL HA H 4.29 0.02 1 104 . 12 VAL HB H 1.91 0.02 1 105 . 12 VAL HG1 H 0.88 0.02 1 106 . 12 VAL HG2 H 0.79 0.02 1 107 . 12 VAL C C 174.24 0.05 1 108 . 12 VAL CA C 58.81 0.05 1 109 . 12 VAL CB C 29.83 0.05 1 110 . 12 VAL CG1 C 18.74 0.05 1 111 . 12 VAL CG2 C 18.92 0.05 1 112 . 12 VAL N N 121.71 0.05 1 113 . 13 ASP H H 8.55 0.02 1 114 . 13 ASP HA H 4.78 0.02 1 115 . 13 ASP HB2 H 3.38 0.02 1 116 . 13 ASP HB3 H 2.78 0.02 1 117 . 13 ASP C C 171.96 0.05 1 118 . 13 ASP CA C 50.12 0.05 1 119 . 13 ASP CB C 38.49 0.05 1 120 . 13 ASP N N 127.48 0.05 1 121 . 14 GLU H H 9.39 0.02 1 122 . 14 GLU HA H 4.07 0.02 1 123 . 14 GLU HB2 H 2.10 0.02 2 124 . 14 GLU HB3 H 2.05 0.02 2 125 . 14 GLU HG2 H 2.36 0.02 2 126 . 14 GLU HG3 H 2.27 0.02 2 127 . 14 GLU C C 174.44 0.05 1 128 . 14 GLU CA C 56.42 0.05 1 129 . 14 GLU CB C 25.92 0.05 1 130 . 14 GLU CG C 33.27 0.05 1 131 . 14 GLU N N 116.33 0.05 1 132 . 15 LEU H H 8.25 0.02 1 133 . 15 LEU HA H 4.50 0.02 1 134 . 15 LEU HB2 H 1.75 0.02 1 135 . 15 LEU HB3 H 1.53 0.02 1 136 . 15 LEU HG H 1.55 0.02 1 137 . 15 LEU HD1 H 0.81 0.02 2 138 . 15 LEU HD2 H 0.83 0.02 2 139 . 15 LEU C C 174.04 0.05 1 140 . 15 LEU CA C 51.48 0.05 1 141 . 15 LEU CB C 39.74 0.05 1 142 . 15 LEU CG C 24.64 0.05 1 143 . 15 LEU CD1 C 20.50 0.05 2 144 . 15 LEU CD2 C 22.13 0.05 2 145 . 15 LEU N N 121.97 0.05 1 146 . 16 GLY H H 8.11 0.02 1 147 . 16 GLY HA2 H 3.24 0.02 1 148 . 16 GLY HA3 H 4.12 0.02 1 149 . 16 GLY CA C 43.21 0.05 1 150 . 16 GLY N N 107.85 0.05 1 151 . 17 ARG H H 8.40 0.02 1 152 . 17 ARG HA H 5.20 0.02 1 153 . 17 ARG HB2 H 1.23 0.02 1 154 . 17 ARG HB3 H 2.16 0.02 1 155 . 17 ARG HG2 H 1.64 0.02 2 156 . 17 ARG HG3 H 1.38 0.02 2 157 . 17 ARG HD2 H 3.25 0.02 2 158 . 17 ARG HD3 H 2.65 0.02 2 159 . 17 ARG HE H 8.92 0.02 1 160 . 17 ARG C C 174.19 0.05 1 161 . 17 ARG CA C 52.10 0.05 1 162 . 17 ARG CB C 29.29 0.05 1 163 . 17 ARG CG C 24.17 0.05 1 164 . 17 ARG CD C 40.54 0.05 1 165 . 17 ARG N N 117.69 0.05 1 166 . 17 ARG NE N 109.76 0.05 1 167 . 18 VAL H H 8.31 0.02 1 168 . 18 VAL HA H 4.56 0.02 1 169 . 18 VAL HB H 1.64 0.02 1 170 . 18 VAL HG1 H 0.69 0.02 1 171 . 18 VAL HG2 H 0.76 0.02 1 172 . 18 VAL C C 170.53 0.05 1 173 . 18 VAL CA C 56.41 0.05 1 174 . 18 VAL CB C 33.41 0.05 1 175 . 18 VAL CG1 C 17.27 0.05 1 176 . 18 VAL CG2 C 18.60 0.05 1 177 . 18 VAL N N 118.28 0.05 1 178 . 19 VAL H H 8.11 0.02 1 179 . 19 VAL HA H 3.76 0.02 1 180 . 19 VAL HB H 1.84 0.02 1 181 . 19 VAL HG1 H 0.79 0.02 1 182 . 19 VAL HG2 H 0.92 0.02 1 183 . 19 VAL C C 172.30 0.05 1 184 . 19 VAL CA C 59.41 0.05 1 185 . 19 VAL CB C 30.32 0.05 1 186 . 19 VAL CG1 C 18.56 0.05 1 187 . 19 VAL CG2 C 19.11 0.05 1 188 . 19 VAL N N 125.81 0.05 1 189 . 20 ILE H H 8.51 0.02 1 190 . 20 ILE HA H 4.27 0.02 1 191 . 20 ILE HB H 1.89 0.02 1 192 . 20 ILE HG12 H 1.43 0.02 2 193 . 20 ILE HG13 H 1.21 0.02 2 194 . 20 ILE HG2 H 0.79 0.02 1 195 . 20 ILE HD1 H 0.58 0.02 1 196 . 20 ILE C C 171.66 0.05 1 197 . 20 ILE CA C 54.38 0.05 1 198 . 20 ILE CB C 34.32 0.05 1 199 . 20 ILE CG1 C 24.05 0.05 1 200 . 20 ILE CG2 C 15.67 0.05 1 201 . 20 ILE CD1 C 8.80 0.05 1 202 . 20 ILE N N 127.26 0.05 1 203 . 21 PRO HA H 4.48 0.02 1 204 . 21 PRO HB2 H 1.87 0.02 1 205 . 21 PRO HB3 H 2.68 0.02 1 206 . 21 PRO HG2 H 2.01 0.02 2 207 . 21 PRO HG3 H 1.94 0.02 2 208 . 21 PRO HD2 H 4.33 0.02 2 209 . 21 PRO HD3 H 3.39 0.02 2 210 . 21 PRO C C 175.51 0.05 1 211 . 21 PRO CA C 61.10 0.05 1 212 . 21 PRO CB C 30.41 0.05 1 213 . 21 PRO CG C 25.34 0.05 1 214 . 21 PRO CD C 48.34 0.05 1 215 . 22 ILE H H 8.94 0.02 1 216 . 22 ILE HA H 3.89 0.02 1 217 . 22 ILE HB H 1.90 0.02 1 218 . 22 ILE HG12 H 1.34 0.02 2 219 . 22 ILE HG13 H 1.31 0.02 2 220 . 22 ILE HG2 H 0.98 0.02 1 221 . 22 ILE HD1 H 0.93 0.02 1 222 . 22 ILE C C 173.22 0.05 1 223 . 22 ILE CA C 61.23 0.05 1 224 . 22 ILE CB C 35.85 0.05 1 225 . 22 ILE CG1 C 26.97 0.05 1 226 . 22 ILE CG2 C 14.90 0.05 1 227 . 22 ILE CD1 C 11.27 0.05 1 228 . 22 ILE N N 127.35 0.05 1 229 . 23 GLU H H 9.77 0.02 1 230 . 23 GLU HA H 4.01 0.02 1 231 . 23 GLU HB2 H 1.98 0.02 1 232 . 23 GLU HB3 H 1.98 0.02 1 233 . 23 GLU HG2 H 2.37 0.02 2 234 . 23 GLU HG3 H 2.28 0.02 2 235 . 23 GLU C C 176.57 0.05 1 236 . 23 GLU CA C 57.56 0.05 1 237 . 23 GLU CB C 25.53 0.05 1 238 . 23 GLU CG C 33.47 0.05 1 239 . 23 GLU N N 121.64 0.05 1 240 . 24 LEU H H 7.15 0.02 1 241 . 24 LEU HA H 4.20 0.02 1 242 . 24 LEU HB2 H 1.72 0.02 1 243 . 24 LEU HB3 H 1.35 0.02 1 244 . 24 LEU HG H 1.63 0.02 1 245 . 24 LEU HD1 H 0.83 0.02 2 246 . 24 LEU HD2 H 0.85 0.02 2 247 . 24 LEU C C 175.98 0.05 1 248 . 24 LEU CA C 54.38 0.05 1 249 . 24 LEU CB C 38.61 0.05 1 250 . 24 LEU CG C 25.06 0.05 1 251 . 24 LEU CD1 C 20.58 0.05 2 252 . 24 LEU CD2 C 23.04 0.05 2 253 . 24 LEU N N 117.35 0.05 1 254 . 25 ARG H H 7.56 0.02 1 255 . 25 ARG HA H 3.74 0.02 1 256 . 25 ARG HB2 H 2.21 0.02 1 257 . 25 ARG HB3 H 1.99 0.02 1 258 . 25 ARG HG2 H 1.62 0.02 2 259 . 25 ARG HG3 H 1.19 0.02 2 260 . 25 ARG HD2 H 3.25 0.02 2 261 . 25 ARG HD3 H 3.12 0.02 2 262 . 25 ARG HE H 6.99 0.02 1 263 . 25 ARG C C 176.08 0.05 1 264 . 25 ARG CA C 58.60 0.05 1 265 . 25 ARG CB C 26.63 0.05 1 266 . 25 ARG CG C 27.69 0.05 1 267 . 25 ARG CD C 41.04 0.05 1 268 . 25 ARG N N 117.66 0.05 1 269 . 25 ARG NE N 107.16 0.05 1 270 . 26 ARG H H 8.72 0.02 1 271 . 26 ARG HA H 4.13 0.02 1 272 . 26 ARG HB2 H 1.87 0.02 1 273 . 26 ARG HB3 H 1.87 0.02 1 274 . 26 ARG HG2 H 1.76 0.02 2 275 . 26 ARG HG3 H 1.65 0.02 2 276 . 26 ARG HD2 H 3.16 0.02 1 277 . 26 ARG HD3 H 3.16 0.02 1 278 . 26 ARG HE H 7.15 0.02 1 279 . 26 ARG C C 177.31 0.05 1 280 . 26 ARG CA C 56.60 0.05 1 281 . 26 ARG CB C 27.40 0.05 1 282 . 26 ARG CG C 24.95 0.05 1 283 . 26 ARG CD C 40.93 0.05 1 284 . 26 ARG N N 117.94 0.05 1 285 . 26 ARG NE N 109.79 0.05 1 286 . 27 THR H H 7.60 0.02 1 287 . 27 THR HA H 4.00 0.02 1 288 . 27 THR HB H 4.25 0.02 1 289 . 27 THR HG2 H 1.30 0.02 1 290 . 27 THR C C 172.80 0.05 1 291 . 27 THR CA C 63.74 0.05 1 292 . 27 THR CB C 66.43 0.05 1 293 . 27 THR CG2 C 19.01 0.05 1 294 . 27 THR N N 115.61 0.05 1 295 . 28 LEU H H 7.36 0.02 1 296 . 28 LEU HA H 4.42 0.02 1 297 . 28 LEU HB2 H 1.66 0.02 2 298 . 28 LEU HB3 H 1.57 0.02 2 299 . 28 LEU HG H 1.67 0.02 1 300 . 28 LEU HD1 H 0.75 0.02 2 301 . 28 LEU HD2 H 0.83 0.02 2 302 . 28 LEU C C 174.30 0.05 1 303 . 28 LEU CA C 52.15 0.05 1 304 . 28 LEU CB C 40.41 0.05 1 305 . 28 LEU CG C 25.21 0.05 1 306 . 28 LEU CD1 C 23.03 0.05 2 307 . 28 LEU CD2 C 20.56 0.05 2 308 . 28 LEU N N 118.48 0.05 1 309 . 29 GLY H H 7.71 0.02 1 310 . 29 GLY HA2 H 3.84 0.02 1 311 . 29 GLY HA3 H 3.91 0.02 1 312 . 29 GLY CA C 44.50 0.05 1 313 . 29 GLY N N 109.99 0.05 1 314 . 30 ILE H H 8.20 0.02 1 315 . 30 ILE HA H 4.22 0.02 1 316 . 30 ILE HB H 1.55 0.02 1 317 . 30 ILE HG12 H 1.55 0.02 2 318 . 30 ILE HG13 H 0.80 0.02 2 319 . 30 ILE HG2 H 0.82 0.02 1 320 . 30 ILE HD1 H 0.69 0.02 1 321 . 30 ILE C C 171.71 0.05 1 322 . 30 ILE CA C 58.08 0.05 1 323 . 30 ILE CB C 36.37 0.05 1 324 . 30 ILE CG1 C 24.49 0.05 1 325 . 30 ILE CG2 C 15.67 0.05 1 326 . 30 ILE CD1 C 11.47 0.05 1 327 . 30 ILE N N 119.89 0.05 1 328 . 31 ALA H H 9.48 0.02 1 329 . 31 ALA HA H 4.50 0.02 1 330 . 31 ALA HB H 1.40 0.02 1 331 . 31 ALA C C 174.42 0.05 1 332 . 31 ALA CA C 47.75 0.05 1 333 . 31 ALA CB C 18.72 0.05 1 334 . 31 ALA N N 109.56 0.05 1 335 . 32 GLU H H 8.59 0.02 1 336 . 32 GLU HA H 3.73 0.02 1 337 . 32 GLU HB2 H 1.99 0.02 1 338 . 32 GLU HB3 H 1.90 0.02 1 339 . 32 GLU HG2 H 2.36 0.02 2 340 . 32 GLU HG3 H 2.28 0.02 2 341 . 32 GLU C C 174.49 0.05 1 342 . 32 GLU CA C 56.59 0.05 1 343 . 32 GLU CB C 26.55 0.05 1 344 . 32 GLU CG C 33.45 0.05 1 345 . 32 GLU N N 119.66 0.05 1 346 . 33 LYS H H 8.26 0.02 1 347 . 33 LYS HA H 4.05 0.02 1 348 . 33 LYS HB2 H 2.17 0.02 1 349 . 33 LYS HB3 H 2.03 0.02 1 350 . 33 LYS HG2 H 1.36 0.02 1 351 . 33 LYS HG3 H 1.36 0.02 1 352 . 33 LYS HD2 H 1.64 0.02 1 353 . 33 LYS HD3 H 1.64 0.02 1 354 . 33 LYS HE2 H 2.98 0.02 1 355 . 33 LYS HE3 H 2.98 0.02 1 356 . 33 LYS C C 172.30 0.05 1 357 . 33 LYS CA C 55.69 0.05 1 358 . 33 LYS CB C 28.07 0.05 1 359 . 33 LYS CG C 23.14 0.05 1 360 . 33 LYS CD C 26.68 0.05 1 361 . 33 LYS CE C 39.5 0.05 1 362 . 33 LYS N N 115.98 0.05 1 363 . 34 ASP H H 7.81 0.02 1 364 . 34 ASP HA H 4.67 0.02 1 365 . 34 ASP HB2 H 2.99 0.02 1 366 . 34 ASP HB3 H 2.54 0.02 1 367 . 34 ASP C C 173.26 0.05 1 368 . 34 ASP CA C 52.83 0.05 1 369 . 34 ASP CB C 39.02 0.05 1 370 . 34 ASP N N 120.23 0.05 1 371 . 35 ALA H H 8.55 0.02 1 372 . 35 ALA HA H 4.67 0.02 1 373 . 35 ALA HB H 1.35 0.02 1 374 . 35 ALA C C 173.54 0.05 1 375 . 35 ALA CA C 48.56 0.05 1 376 . 35 ALA CB C 18.12 0.05 1 377 . 35 ALA N N 121.75 0.05 1 378 . 36 LEU H H 9.03 0.02 1 379 . 36 LEU HA H 5.07 0.02 1 380 . 36 LEU HB2 H 1.64 0.02 1 381 . 36 LEU HB3 H 1.20 0.02 1 382 . 36 LEU HG H 1.63 0.02 1 383 . 36 LEU HD1 H 0.67 0.02 2 384 . 36 LEU HD2 H 0.69 0.02 2 385 . 36 LEU CA C 50.48 0.05 1 386 . 36 LEU CB C 41.28 0.05 1 387 . 36 LEU CG C 24.24 0.05 1 388 . 36 LEU CD1 C 24.11 0.05 2 389 . 36 LEU CD2 C 20.62 0.05 2 390 . 36 LEU N N 121.69 0.05 1 391 . 37 GLU H H 9.45 0.02 1 392 . 37 GLU HA H 4.80 0.02 1 393 . 37 GLU HB2 H 1.89 0.02 1 394 . 37 GLU HB3 H 2.07 0.02 1 395 . 37 GLU HG2 H 2.07 0.02 1 396 . 37 GLU HG3 H 2.07 0.02 1 397 . 37 GLU CA C 52.73 0.05 1 398 . 37 GLU CB C 29.73 0.05 1 399 . 37 GLU CG C 33.82 0.05 1 400 . 37 GLU N N 123.47 0.05 1 401 . 38 ILE H H 8.41 0.02 1 402 . 38 ILE HA H 5.20 0.02 1 403 . 38 ILE HB H 1.63 0.02 1 404 . 38 ILE HG2 H 0.73 0.02 1 405 . 38 ILE HD1 H 0.61 0.02 1 406 . 38 ILE C C 173.05 0.05 1 407 . 38 ILE CA C 58.37 0.05 1 408 . 38 ILE CB C 36.57 0.05 1 409 . 38 ILE CG2 C 15.28 0.05 1 410 . 38 ILE CD1 C 11.22 0.05 1 411 . 38 ILE N N 123.15 0.05 1 412 . 39 TYR H H 9.40 0.02 1 413 . 39 TYR HA H 5.06 0.02 1 414 . 39 TYR HB2 H 3.02 0.02 2 415 . 39 TYR HB3 H 2.97 0.02 2 416 . 39 TYR HD1 H 6.83 0.02 1 417 . 39 TYR HD2 H 6.83 0.02 1 418 . 39 TYR HE1 H 6.60 0.02 1 419 . 39 TYR HE2 H 6.60 0.02 1 420 . 39 TYR C C 170.46 0.05 1 421 . 39 TYR CA C 53.66 0.05 1 422 . 39 TYR CB C 39.28 0.05 1 423 . 39 TYR N N 126.44 0.05 1 424 . 40 VAL H H 8.64 0.02 1 425 . 40 VAL HA H 5.12 0.02 1 426 . 40 VAL HB H 2.02 0.02 1 427 . 40 VAL HG1 H 0.94 0.02 2 428 . 40 VAL HG2 H 0.96 0.02 2 429 . 40 VAL C C 172.50 0.05 1 430 . 40 VAL CA C 57.56 0.05 1 431 . 40 VAL CB C 32.30 0.05 1 432 . 40 VAL CG1 C 18.99 0.05 2 433 . 40 VAL CG2 C 19.25 0.05 2 434 . 40 VAL N N 117.26 0.05 1 435 . 41 ASP H H 8.51 0.02 1 436 . 41 ASP HA H 4.83 0.02 1 437 . 41 ASP HB2 H 2.62 0.02 2 438 . 41 ASP HB3 H 2.57 0.02 2 439 . 41 ASP CA C 50.85 0.05 1 440 . 41 ASP CB C 40.71 0.05 1 441 . 41 ASP N N 125.79 0.05 1 442 . 42 ASP H H 8.81 0.02 1 443 . 42 ASP HA H 4.22 0.02 1 444 . 42 ASP HB2 H 2.89 0.02 1 445 . 42 ASP HB3 H 2.64 0.02 1 446 . 42 ASP C C 172.24 0.05 1 447 . 42 ASP CA C 53.66 0.05 1 448 . 42 ASP CB C 36.95 0.05 1 449 . 42 ASP N N 122.90 0.05 1 450 . 43 GLU H H 8.86 0.02 1 451 . 43 GLU HA H 4.27 0.02 1 452 . 43 GLU HB2 H 2.18 0.02 2 453 . 43 GLU HB3 H 2.11 0.02 2 454 . 43 GLU HG2 H 2.18 0.02 1 455 . 43 GLU HG3 H 2.18 0.02 1 456 . 43 GLU C C 171.66 0.05 1 457 . 43 GLU CA C 54.38 0.05 1 458 . 43 GLU CB C 26.97 0.05 1 459 . 43 GLU CG C 33.78 0.05 1 460 . 43 GLU N N 117.71 0.05 1 461 . 44 LYS H H 8.12 0.02 1 462 . 44 LYS HA H 4.76 0.02 1 463 . 44 LYS HB2 H 1.92 0.02 2 464 . 44 LYS HB3 H 1.53 0.02 2 465 . 44 LYS HG2 H 1.36 0.02 1 466 . 44 LYS HG3 H 1.36 0.02 1 467 . 44 LYS HD2 H 1.59 0.02 1 468 . 44 LYS HD3 H 1.59 0.02 1 469 . 44 LYS HE2 H 2.92 0.02 1 470 . 44 LYS HE3 H 2.92 0.02 1 471 . 44 LYS CA C 52.55 0.05 1 472 . 44 LYS CB C 31.95 0.05 1 473 . 44 LYS CG C 21.09 0.05 1 474 . 44 LYS CD C 26.60 0.05 1 475 . 44 LYS CE C 39.15 0.05 1 476 . 44 LYS N N 119.16 0.05 1 477 . 45 ILE H H 8.62 0.02 1 478 . 45 ILE HA H 4.42 0.02 1 479 . 45 ILE HB H 1.66 0.02 1 480 . 45 ILE HG12 H 1.63 0.02 2 481 . 45 ILE HG13 H 0.73 0.02 2 482 . 45 ILE HG2 H 0.74 0.02 1 483 . 45 ILE HD1 H 0.61 0.02 1 484 . 45 ILE C C 171.00 0.05 1 485 . 45 ILE CA C 58.01 0.05 1 486 . 45 ILE CB C 36.62 0.05 1 487 . 45 ILE CG1 C 25.66 0.05 1 488 . 45 ILE CG2 C 15.64 0.05 1 489 . 45 ILE CD1 C 11.25 0.05 1 490 . 45 ILE N N 120.05 0.05 1 491 . 46 ILE H H 8.98 0.02 1 492 . 46 ILE HA H 4.78 0.02 1 493 . 46 ILE HB H 0.99 0.02 1 494 . 46 ILE HG12 H 1.20 0.02 2 495 . 46 ILE HG13 H 1.01 0.02 2 496 . 46 ILE HG2 H 0.63 0.02 1 497 . 46 ILE HD1 H 0.69 0.02 1 498 . 46 ILE CA C 56.95 0.05 1 499 . 46 ILE CB C 36.87 0.05 1 500 . 46 ILE CG1 C 26.33 0.05 1 501 . 46 ILE CG2 C 16.64 0.05 1 502 . 46 ILE CD1 C 11.83 0.05 1 503 . 46 ILE N N 128.03 0.05 1 504 . 47 LEU H H 9.36 0.02 1 505 . 47 LEU HA H 5.44 0.02 1 506 . 47 LEU HB2 H 1.71 0.02 1 507 . 47 LEU HB3 H 1.32 0.02 1 508 . 47 LEU HG H 1.56 0.02 1 509 . 47 LEU HD1 H 0.66 0.02 2 510 . 47 LEU HD2 H 0.67 0.02 2 511 . 47 LEU C C 172.88 0.05 1 512 . 47 LEU CA C 50.73 0.05 1 513 . 47 LEU CB C 41.47 0.05 1 514 . 47 LEU CG C 24.09 0.05 1 515 . 47 LEU CD1 C 23.73 0.05 2 516 . 47 LEU CD2 C 23.57 0.05 2 517 . 47 LEU N N 124.41 0.05 1 518 . 48 LYS H H 8.66 0.02 1 519 . 48 LYS HA H 4.83 0.02 1 520 . 48 LYS HB2 H 1.93 0.02 2 521 . 48 LYS HB3 H 1.78 0.02 2 522 . 48 LYS HG2 H 1.56 0.02 2 523 . 48 LYS HG3 H 1.42 0.02 2 524 . 48 LYS HD2 H 1.65 0.02 1 525 . 48 LYS HD3 H 1.65 0.02 1 526 . 48 LYS HE2 H 2.98 0.02 1 527 . 48 LYS HE3 H 2.98 0.02 1 528 . 48 LYS C C 172.58 0.05 1 529 . 48 LYS CA C 51.56 0.05 1 530 . 48 LYS CB C 34.23 0.05 1 531 . 48 LYS CG C 21.71 0.05 1 532 . 48 LYS CD C 26.67 0.05 1 533 . 48 LYS CE C 39.4 0.05 1 534 . 48 LYS N N 119.16 0.05 1 535 . 49 LYS H H 9.25 0.02 1 536 . 49 LYS HA H 4.23 0.02 1 537 . 49 LYS HB2 H 1.88 0.02 1 538 . 49 LYS HB3 H 1.64 0.02 1 539 . 49 LYS HG2 H 1.52 0.02 2 540 . 49 LYS HG3 H 1.37 0.02 2 541 . 49 LYS HD2 H 1.72 0.02 1 542 . 49 LYS HD3 H 1.72 0.02 1 543 . 49 LYS HE2 H 2.91 0.02 1 544 . 49 LYS HE3 H 2.91 0.02 1 545 . 49 LYS C C 173.68 0.05 1 546 . 49 LYS CA C 56.36 0.05 1 547 . 49 LYS CB C 29.95 0.05 1 548 . 49 LYS CG C 23.39 0.05 1 549 . 49 LYS CD C 26.88 0.05 1 550 . 49 LYS CE C 39.7 0.05 1 551 . 49 LYS N N 124.15 0.05 1 552 . 50 TYR H H 8.59 0.02 1 553 . 50 TYR HA H 4.61 0.02 1 554 . 50 TYR HB2 H 2.79 0.02 1 555 . 50 TYR HB3 H 2.70 0.02 1 556 . 50 TYR HD1 H 7.03 0.02 1 557 . 50 TYR HD2 H 7.03 0.02 1 558 . 50 TYR HE1 H 6.75 0.02 1 559 . 50 TYR HE2 H 6.75 0.02 1 560 . 50 TYR C C 172.43 0.05 1 561 . 50 TYR CA C 55.24 0.05 1 562 . 50 TYR CB C 36.73 0.05 1 563 . 50 TYR N N 127.33 0.05 1 564 . 51 LYS H H 8.10 0.02 1 565 . 51 LYS HA H 4.50 0.02 1 566 . 51 LYS HB2 H 1.71 0.02 2 567 . 51 LYS HB3 H 1.54 0.02 2 568 . 51 LYS HG2 H 1.30 0.02 2 569 . 51 LYS HG3 H 1.27 0.02 2 570 . 51 LYS HD2 H 1.65 0.02 1 571 . 51 LYS HD3 H 1.65 0.02 1 572 . 51 LYS HE2 H 2.98 0.02 1 573 . 51 LYS HE3 H 2.98 0.02 1 574 . 51 LYS C C 170.07 0.05 1 575 . 51 LYS CA C 50.56 0.05 1 576 . 51 LYS CB C 30.81 0.05 1 577 . 51 LYS CG C 21.64 0.05 1 578 . 51 LYS CD C 26.18 0.05 1 579 . 51 LYS CE C 39.5 0.05 1 580 . 51 LYS N N 129.59 0.05 1 581 . 52 PRO HA H 4.17 0.02 1 582 . 52 PRO HB2 H 2.16 0.02 2 583 . 52 PRO HB3 H 1.96 0.02 2 584 . 52 PRO HG2 H 1.93 0.02 2 585 . 52 PRO HG3 H 1.88 0.02 2 586 . 52 PRO HD2 H 3.53 0.02 2 587 . 52 PRO HD3 H 3.06 0.02 2 588 . 52 PRO C C 173.17 0.05 1 589 . 52 PRO CA C 60.38 0.05 1 590 . 52 PRO CB C 29.21 0.05 1 591 . 52 PRO CG C 24.12 0.05 1 592 . 52 PRO CD C 47.84 0.05 1 593 . 53 ASN H H 7.81 0.02 1 594 . 53 ASN HA H 4.39 0.02 1 595 . 53 ASN HB2 H 2.73 0.02 2 596 . 53 ASN HB3 H 2.66 0.02 2 597 . 53 ASN HD21 H 6.78 0.02 2 598 . 53 ASN HD22 H 7.41 0.02 2 599 . 53 ASN C C 176.80 0.05 1 600 . 53 ASN CA C 52.08 0.05 1 601 . 53 ASN CB C 37.75 0.05 1 602 . 53 ASN N N 123.50 0.05 1 603 . 53 ASN ND2 N 112.74 0.05 1 stop_ save_