data_4718 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of amide 1H, amide 15N, and Ca, CO, Cb 13C shifts for the replication terminator protein ; _BMRB_accession_number 4718 _BMRB_flat_file_name bmr4718.str _Entry_type original _Submission_date 2000-04-12 _Accession_date 2000-04-17 _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 Wilce Jackie W. . 2 Vivian Julian P. . 3 Hastings Adam F. . 4 Otting Gottfried . . 5 Folmer Rutger . . 6 Duggin I. G. . 7 Wake R. Gerry . 8 Wilce Matthew C. J. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 "13C chemical shifts" 333 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-01 original author . stop_ _Original_release_date 2001-05-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the RTP-DNA Complex and the Mechanism of Polar Replication Fork Arrest ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21127481 _PubMed_ID 11224562 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wilce Jackie A. . 2 Vivian Julian P. . 3 Hastings Adam F. . 4 Otting Gottfried . . 5 Folmer Rutger H. . 6 Duggin I. G. . 7 Wake R. Gerry . 8 Wilce Matthew C. J. stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 8 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 206 _Page_last 210 _Year 2001 _Details . loop_ _Keyword 'replication terminator protein' 'Bacillus subtilis' stop_ save_ ################################## # Molecular system description # ################################## save_system_RTP _Saveframe_category molecular_system _Mol_system_name 'replication terminator protein' _Abbreviation_common RTP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RTP subunit 1' $RTP 'RTP subunit 2' $RTP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'RTP subunit 1' 1 'RTP subunit 2' stop_ loop_ _Biological_function 'replication terminator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RTP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'replication termination protein' _Name_variant C110S _Abbreviation_common RTP _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MKEEKRSSTGFLVKQRAFLK LYMITMTEQERLYGLKLLEV LRSEFKEIGFKPNHTEVYRS LHELLDDGILKQIKVKKEGA KLQEVVLYQFKDYEAAKLYK KQLKVELDRSKKLIEKALSD NF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 GLU 4 GLU 5 LYS 6 ARG 7 SER 8 SER 9 THR 10 GLY 11 PHE 12 LEU 13 VAL 14 LYS 15 GLN 16 ARG 17 ALA 18 PHE 19 LEU 20 LYS 21 LEU 22 TYR 23 MET 24 ILE 25 THR 26 MET 27 THR 28 GLU 29 GLN 30 GLU 31 ARG 32 LEU 33 TYR 34 GLY 35 LEU 36 LYS 37 LEU 38 LEU 39 GLU 40 VAL 41 LEU 42 ARG 43 SER 44 GLU 45 PHE 46 LYS 47 GLU 48 ILE 49 GLY 50 PHE 51 LYS 52 PRO 53 ASN 54 HIS 55 THR 56 GLU 57 VAL 58 TYR 59 ARG 60 SER 61 LEU 62 HIS 63 GLU 64 LEU 65 LEU 66 ASP 67 ASP 68 GLY 69 ILE 70 LEU 71 LYS 72 GLN 73 ILE 74 LYS 75 VAL 76 LYS 77 LYS 78 GLU 79 GLY 80 ALA 81 LYS 82 LEU 83 GLN 84 GLU 85 VAL 86 VAL 87 LEU 88 TYR 89 GLN 90 PHE 91 LYS 92 ASP 93 TYR 94 GLU 95 ALA 96 ALA 97 LYS 98 LEU 99 TYR 100 LYS 101 LYS 102 GLN 103 LEU 104 LYS 105 VAL 106 GLU 107 LEU 108 ASP 109 ARG 110 SER 111 LYS 112 LYS 113 LEU 114 ILE 115 GLU 116 LYS 117 ALA 118 LEU 119 SER 120 ASP 121 ASN 122 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1BM9 "Replication Terminator Protein From Bacillus Subtilis" 100.00 122 99.18 99.18 1.50e-77 PDB 1F4K "Crystal Structure Of The Replication Terminator ProteinB- Site Dna Complex" 100.00 122 100.00 100.00 3.21e-78 PDB 1J0R "Crystal Structure Of The Replication Termination Protein Mutant C110s" 100.00 122 100.00 100.00 3.21e-78 PDB 2DPD "Crystal Structure Of The Replication Termination Protein In Complex With A Pseudosymmetric B-Site" 100.00 122 100.00 100.00 3.21e-78 PDB 2DPU "Crystal Structure Of The Replication Termination Protein In Complex With A Pseudosymmetric 21mer B-Site Dna" 100.00 122 100.00 100.00 3.21e-78 PDB 2DQR "Crystal Structure Of The Replication Terminator Protein Mutant Rtp.E39k.R42q" 100.00 122 97.54 99.18 3.79e-76 PDB 2EFW "Crystal Structure Of The Rtp:nrb Complex From Bacillus Subtilis" 100.00 122 100.00 100.00 3.21e-78 DBJ BAM52503 "replication terminator protein [Bacillus subtilis BEST7613]" 100.00 122 99.18 99.18 1.50e-77 DBJ BAM58079 "replication terminator protein [Bacillus subtilis BEST7003]" 100.00 122 99.18 99.18 1.50e-77 DBJ BAO93415 "hypothetical protein BSNT_08440 [Bacillus subtilis subsp. natto BEST195]" 100.00 130 99.18 99.18 1.43e-77 DBJ GAK78159 "replication terminator protein [Bacillus subtilis Miyagi-4]" 100.00 123 99.18 99.18 1.30e-77 EMBL CAA29534 "unnamed protein product [Bacillus subtilis]" 100.00 122 99.18 99.18 1.50e-77 EMBL CAB13742 "replication terminator protein [Bacillus subtilis subsp. subtilis str. 168]" 100.00 122 99.18 99.18 1.50e-77 EMBL CCU58469 "replication terminator protein [Bacillus subtilis E1]" 100.00 123 99.18 99.18 1.30e-77 EMBL CEI57043 "hypothetical protein BS49_20480 [Bacillus subtilis]" 100.00 123 99.18 99.18 1.30e-77 EMBL CEJ77468 "hypothetical protein BS34A_20480 [Bacillus sp.]" 100.00 123 99.18 99.18 1.30e-77 GB AAA22721 "replication terminator protein (rtp; terC) [Bacillus subtilis]" 100.00 122 99.18 99.18 1.50e-77 GB AAC38659 "replication terminator protein [Bacillus vallismortis]" 100.00 122 99.18 99.18 1.50e-77 GB AAC38660 "replication terminator protein [Bacillus mojavensis]" 100.00 122 98.36 99.18 7.13e-77 GB AAC38662 "replication terminator protein [Bacillus amyloliquefaciens DSM 7]" 100.00 122 97.54 98.36 1.58e-76 GB ADM38012 "replication terminator protein [Bacillus subtilis subsp. spizizenii str. W23]" 100.00 122 99.18 99.18 1.50e-77 REF NP_389731 "replication termination protein [Bacillus subtilis subsp. subtilis str. 168]" 100.00 122 99.18 99.18 1.50e-77 REF WP_003220337 "MULTISPECIES: replication termination protein [Bacillales]" 100.00 122 99.18 99.18 1.50e-77 REF WP_010334473 "MULTISPECIES: replication terminator protein [Bacillaceae]" 100.00 122 98.36 99.18 7.13e-77 REF WP_024715459 "replication termination protein [Bacillus tequilensis]" 100.00 122 98.36 99.18 2.88e-77 REF WP_041849904 "MULTISPECIES: replication termination protein [Bacillus]" 100.00 122 98.36 99.18 2.61e-77 SP E0TY12 "RecName: Full=Replication termination protein; AltName: Full=Replication terminator protein" 100.00 122 99.18 99.18 1.50e-77 SP P0CI76 "RecName: Full=Replication termination protein; AltName: Full=Replication terminator protein" 100.00 122 99.18 99.18 1.50e-77 SP P68733 "RecName: Full=Replication termination protein; AltName: Full=Replication terminator protein" 100.00 122 99.18 99.18 1.50e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RTP 'Bacillus subtilis' 1423 Eubacteria . 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_name $RTP '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 $RTP 0.25 mM '[U-100% 13C; U-100% 15N; U-70% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_TROSY-HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label . save_ save_TROSY-HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label . save_ save_TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label . save_ save_TROSY-HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label . save_ save_TROSY-HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _Sample_label . save_ save_3D_NOESY-15N-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-15N-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-15N-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 298 0.1 K 'ionic strength' 0.11 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label TROSY-HNCA TROSY-HNCO TROSY-HNCACB TROSY-HN(CO)CACB TROSY-HN(CA)CO '3D NOESY-15N-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RTP 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 . 2 LYS C C 175.9 0.1 1 2 . 2 LYS CA C 56.1 0.1 1 3 . 2 LYS CB C 32.2 0.1 1 4 . 3 GLU H H 8.60 0.02 1 5 . 3 GLU C C 175.9 0.1 1 6 . 3 GLU CA C 56.0 0.1 1 7 . 3 GLU CB C 29.5 0.1 1 8 . 3 GLU N N 123.3 0.2 1 9 . 4 GLU H H 8.57 0.02 1 10 . 4 GLU C C 176.4 0.1 1 11 . 4 GLU CA C 55.8 0.1 1 12 . 4 GLU CB C 29.5 0.1 1 13 . 4 GLU N N 123.4 0.2 1 14 . 5 LYS H H 8.48 0.02 1 15 . 5 LYS C C 176.6 0.1 1 16 . 5 LYS CA C 55.8 0.1 1 17 . 5 LYS CB C 32.0 0.1 1 18 . 5 LYS N N 123.0 0.2 1 19 . 6 ARG H H 8.42 0.02 1 20 . 6 ARG C C 176.2 0.1 1 21 . 6 ARG CA C 55.4 0.1 1 22 . 6 ARG CB C 30.0 0.1 1 23 . 6 ARG N N 122.0 0.2 1 24 . 7 SER H H 8.43 0.02 1 25 . 7 SER C C 174.7 0.1 1 26 . 7 SER CA C 57.7 0.1 1 27 . 7 SER N N 118.8 0.2 1 28 . 9 THR C C 175.2 0.1 1 29 . 9 THR CA C 61.5 0.1 1 30 . 9 THR CB C 70.0 0.1 1 31 . 10 GLY H H 8.42 0.02 1 32 . 10 GLY C C 173.3 0.1 1 33 . 10 GLY CA C 45.3 0.1 1 34 . 10 GLY N N 110.0 0.2 1 35 . 11 PHE H H 8.18 0.02 1 36 . 11 PHE C C 173.6 0.1 1 37 . 11 PHE CA C 54.5 0.1 1 38 . 11 PHE CB C 37.5 0.1 1 39 . 11 PHE N N 119.6 0.2 1 40 . 12 LEU H H 6.04 0.02 1 41 . 12 LEU C C 176.1 0.1 1 42 . 12 LEU CA C 52.6 0.1 1 43 . 12 LEU N N 121.1 0.2 1 44 . 13 VAL H H 6.93 0.02 1 45 . 13 VAL C C 172.9 0.1 1 46 . 13 VAL CA C 60.1 0.1 1 47 . 13 VAL CB C 32.2 0.1 1 48 . 13 VAL N N 118.0 0.2 1 49 . 14 LYS H H 8.52 0.02 1 50 . 14 LYS C C 177.9 0.1 1 51 . 14 LYS CA C 55.3 0.1 1 52 . 14 LYS CB C 32.3 0.1 1 53 . 14 LYS N N 125.4 0.2 1 54 . 15 GLN H H 8.94 0.02 1 55 . 15 GLN HE21 H 7.07 0.02 1 56 . 15 GLN HE22 H 6.69 0.02 1 57 . 15 GLN C C 177.7 0.1 1 58 . 15 GLN CA C 59.5 0.1 1 59 . 15 GLN CB C 27.2 0.1 1 60 . 15 GLN N N 123.0 0.2 1 61 . 15 GLN NE2 N 106.9 0.2 1 62 . 16 ARG H H 8.82 0.02 1 63 . 16 ARG C C 177.9 0.1 1 64 . 16 ARG CA C 59.5 0.1 1 65 . 16 ARG CB C 29.0 0.1 1 66 . 16 ARG N N 116.8 0.2 1 67 . 17 ALA H H 6.63 0.02 1 68 . 17 ALA C C 179.0 0.1 1 69 . 17 ALA CA C 54.0 0.1 1 70 . 17 ALA CB C 18.0 0.1 1 71 . 17 ALA N N 120.2 0.2 1 72 . 18 PHE H H 8.12 0.02 1 73 . 18 PHE C C 176.7 0.1 1 74 . 18 PHE CA C 61.3 0.1 1 75 . 18 PHE CB C 40.5 0.1 1 76 . 18 PHE N N 119.3 0.2 1 77 . 19 LEU H H 8.62 0.02 1 78 . 19 LEU C C 179.5 0.1 1 79 . 19 LEU CA C 57.7 0.1 1 80 . 19 LEU CB C 40.5 0.1 1 81 . 19 LEU N N 116.8 0.2 1 82 . 20 LYS H H 8.65 0.02 1 83 . 20 LYS C C 178.3 0.1 1 84 . 20 LYS CA C 60.3 0.1 1 85 . 20 LYS N N 118.3 0.2 1 86 . 21 LEU H H 7.93 0.02 1 87 . 21 LEU C C 177.0 0.1 1 88 . 21 LEU CA C 58.0 0.1 1 89 . 21 LEU N N 118.0 0.2 1 90 . 22 TYR H H 7.16 0.02 1 91 . 22 TYR C C 177.7 0.1 1 92 . 22 TYR CA C 62.6 0.1 1 93 . 22 TYR CB C 41.2 0.1 1 94 . 22 TYR N N 114.6 0.2 1 95 . 23 MET H H 8.25 0.02 1 96 . 23 MET C C 174.5 0.1 1 97 . 23 MET CA C 57.9 0.1 1 98 . 23 MET N N 116.8 0.2 1 99 . 24 ILE H H 8.42 0.02 1 100 . 24 ILE C C 177.6 0.1 1 101 . 24 ILE CA C 66.4 0.1 1 102 . 24 ILE N N 122.3 0.2 1 103 . 25 THR H H 8.23 0.02 1 104 . 25 THR C C 178.5 0.1 1 105 . 25 THR CA C 65.6 0.1 1 106 . 25 THR N N 121.7 0.2 1 107 . 26 MET H H 9.03 0.02 1 108 . 26 MET C C 179.6 0.1 1 109 . 26 MET CA C 59.3 0.1 1 110 . 26 MET CB C 26.7 0.1 1 111 . 26 MET N N 118.3 0.2 1 112 . 27 THR H H 7.87 0.02 1 113 . 27 THR C C 179.5 0.1 1 114 . 27 THR CA C 59.5 0.1 1 115 . 27 THR N N 119.0 0.2 1 116 . 28 GLU H H 8.57 0.02 1 117 . 28 GLU C C 178.3 0.1 1 118 . 28 GLU CA C 59.7 0.1 1 119 . 28 GLU CB C 29.3 0.1 1 120 . 28 GLU N N 125.7 0.2 1 121 . 29 GLN H H 7.58 0.02 1 122 . 29 GLN HE21 H 7.39 0.02 1 123 . 29 GLN HE22 H 7.00 0.02 1 124 . 29 GLN C C 174.1 0.1 1 125 . 29 GLN CA C 54.5 0.1 1 126 . 29 GLN CB C 27.2 0.1 1 127 . 29 GLN N N 114.6 0.2 1 128 . 29 GLN NE2 N 111.2 0.2 1 129 . 30 GLU H H 7.96 0.02 1 130 . 30 GLU C C 176.0 0.1 1 131 . 30 GLU CA C 56.5 0.1 1 132 . 30 GLU CB C 26.0 0.1 1 133 . 30 GLU N N 115.6 0.2 1 134 . 31 ARG H H 8.55 0.02 1 135 . 31 ARG C C 174.7 0.1 1 136 . 31 ARG CA C 54.0 0.1 1 137 . 31 ARG CB C 30.0 0.1 1 138 . 31 ARG N N 112.8 0.2 1 139 . 32 LEU H H 8.17 0.02 1 140 . 32 LEU C C 173.8 0.1 1 141 . 32 LEU CA C 53.5 0.1 1 142 . 32 LEU CB C 39.0 0.1 1 143 . 32 LEU N N 125.1 0.2 1 144 . 33 TYR H H 7.67 0.02 1 145 . 33 TYR C C 176.9 0.1 1 146 . 33 TYR CA C 56.1 0.1 1 147 . 33 TYR CB C 39.5 0.1 1 148 . 33 TYR N N 124.8 0.2 1 149 . 34 GLY H H 8.57 0.02 1 150 . 34 GLY C C 175.0 0.1 1 151 . 34 GLY CA C 46.9 0.1 1 152 . 34 GLY N N 127.3 0.2 1 153 . 35 LEU H H 8.55 0.02 1 154 . 35 LEU CA C 56.2 0.1 1 155 . 35 LEU CB C 41.3 0.1 1 156 . 35 LEU N N 120.5 0.2 1 157 . 36 LYS H H 8.27 0.02 1 158 . 36 LYS C C 175.6 0.1 1 159 . 36 LYS CA C 55.3 0.1 1 160 . 36 LYS N N 118.0 0.2 1 161 . 37 LEU H H 7.19 0.02 1 162 . 37 LEU C C 177.7 0.1 1 163 . 37 LEU CA C 58.1 0.1 1 164 . 37 LEU CB C 41.3 0.1 1 165 . 37 LEU N N 120.2 0.2 1 166 . 38 LEU H H 8.22 0.02 1 167 . 38 LEU C C 178.0 0.1 1 168 . 38 LEU CA C 57.9 0.1 1 169 . 38 LEU CB C 41.0 0.1 1 170 . 38 LEU N N 116.5 0.2 1 171 . 39 GLU H H 8.23 0.02 1 172 . 39 GLU C C 179.7 0.1 1 173 . 39 GLU CA C 59.4 0.1 1 174 . 39 GLU CB C 28.0 0.1 1 175 . 39 GLU N N 118.6 0.2 1 176 . 40 VAL H H 8.57 0.02 1 177 . 40 VAL C C 176.7 0.1 1 178 . 40 VAL CA C 66.0 0.1 1 179 . 40 VAL CB C 30.8 0.1 1 180 . 40 VAL N N 121.1 0.2 1 181 . 41 LEU H H 8.18 0.02 1 182 . 41 LEU C C 176.7 0.1 1 183 . 41 LEU CA C 57.0 0.1 1 184 . 41 LEU CB C 40.8 0.1 1 185 . 41 LEU N N 120.5 0.2 1 186 . 42 ARG H H 8.61 0.02 1 187 . 42 ARG C C 180.0 0.1 1 188 . 42 ARG CA C 59.7 0.1 1 189 . 42 ARG CB C 28.6 0.1 1 190 . 42 ARG N N 116.5 0.2 1 191 . 43 SER H H 8.22 0.02 1 192 . 43 SER C C 176.3 0.1 1 193 . 43 SER CA C 61.3 0.1 1 194 . 43 SER CB C 62.5 0.1 1 195 . 43 SER N N 114.6 0.2 1 196 . 44 GLU H H 7.58 0.02 1 197 . 44 GLU C C 177.6 0.1 1 198 . 44 GLU CA C 57.5 0.1 1 199 . 44 GLU CB C 28.2 0.1 1 200 . 44 GLU N N 121.1 0.2 1 201 . 45 PHE H H 6.93 0.02 1 202 . 45 PHE C C 176.1 0.1 1 203 . 45 PHE CA C 56.1 0.1 1 204 . 45 PHE CB C 40.2 0.1 1 205 . 45 PHE N N 111.8 0.2 1 206 . 46 LYS H H 7.36 0.02 1 207 . 46 LYS C C 178.5 0.1 1 208 . 46 LYS CA C 59.6 0.1 1 209 . 46 LYS CB C 31.5 0.1 1 210 . 46 LYS N N 121.4 0.2 1 211 . 47 GLU H H 8.81 0.02 1 212 . 47 GLU C C 178.0 0.1 1 213 . 47 GLU CA C 58.5 0.1 1 214 . 47 GLU CB C 28.1 0.1 1 215 . 47 GLU N N 118.6 0.2 1 216 . 48 ILE H H 7.86 0.02 1 217 . 48 ILE C C 176.4 0.1 1 218 . 48 ILE CA C 61.5 0.1 1 219 . 48 ILE CB C 38.9 0.1 1 220 . 48 ILE N N 117.4 0.2 1 221 . 49 GLY H H 8.01 0.02 1 222 . 49 GLY C C 173.8 0.1 1 223 . 49 GLY CA C 44.9 0.1 1 224 . 49 GLY N N 125.7 0.2 1 225 . 50 PHE H H 6.81 0.02 1 226 . 50 PHE C C 173.1 0.1 1 227 . 50 PHE CA C 54.1 0.1 1 228 . 50 PHE CB C 40.0 0.1 1 229 . 50 PHE N N 120.5 0.2 1 230 . 51 LYS H H 8.79 0.02 1 231 . 51 LYS C C 171.5 0.1 1 232 . 51 LYS CA C 51.7 0.1 1 233 . 51 LYS CB C 32.3 0.1 1 234 . 51 LYS N N 110.9 0.2 1 235 . 52 PRO C C 175.1 0.1 1 236 . 52 PRO CA C 61.0 0.1 1 237 . 52 PRO CB C 30.3 0.1 1 238 . 53 ASN H H 8.92 0.02 1 239 . 53 ASN HD21 H 7.74 0.02 1 240 . 53 ASN HD22 H 7.12 0.02 1 241 . 53 ASN C C 175.2 0.1 1 242 . 53 ASN CA C 51.5 0.1 1 243 . 53 ASN CB C 39.8 0.1 1 244 . 53 ASN N N 120.8 0.2 1 245 . 53 ASN ND2 N 113.4 0.2 1 246 . 54 HIS C C 176.6 0.1 1 247 . 54 HIS CA C 60.2 0.1 1 248 . 55 THR H H 7.88 0.02 1 249 . 55 THR C C 176.7 0.1 1 250 . 55 THR CA C 65.9 0.1 1 251 . 55 THR CB C 67.9 0.1 1 252 . 55 THR N N 114.3 0.2 1 253 . 56 GLU H H 7.93 0.02 1 254 . 56 GLU C C 172.0 0.1 1 255 . 56 GLU CA C 58.2 0.1 1 256 . 56 GLU CB C 28.2 0.1 1 257 . 56 GLU N N 119.9 0.2 1 258 . 57 VAL H H 7.92 0.02 1 259 . 57 VAL C C 176.7 0.1 1 260 . 57 VAL CA C 67.0 0.1 1 261 . 57 VAL N N 120.8 0.2 1 262 . 58 TYR H H 8.31 0.02 1 263 . 58 TYR C C 178.7 0.1 1 264 . 58 TYR CA C 62.2 0.1 1 265 . 58 TYR CB C 37.1 0.1 1 266 . 58 TYR N N 117.4 0.2 1 267 . 59 ARG H H 8.60 0.02 1 268 . 59 ARG C C 178.8 0.1 1 269 . 59 ARG CA C 58.9 0.1 1 270 . 59 ARG CB C 29.0 0.1 1 271 . 59 ARG N N 119.6 0.2 1 272 . 60 SER H H 7.83 0.02 1 273 . 60 SER C C 174.5 0.1 1 274 . 60 SER CA C 63.5 0.1 1 275 . 60 SER CB C 62.5 0.1 1 276 . 60 SER N N 116.5 0.2 1 277 . 61 LEU H H 7.44 0.02 1 278 . 61 LEU C C 178.1 0.1 1 279 . 61 LEU CA C 57.3 0.1 1 280 . 61 LEU CB C 41.0 0.1 1 281 . 61 LEU N N 120.8 0.2 1 282 . 62 HIS H H 8.27 0.02 1 283 . 62 HIS C C 177.3 0.1 1 284 . 62 HIS CA C 59.3 0.1 1 285 . 62 HIS CB C 27.6 0.1 1 286 . 62 HIS N N 114.6 0.2 1 287 . 63 GLU H H 8.39 0.02 1 288 . 63 GLU C C 178.3 0.1 1 289 . 63 GLU CA C 59.4 0.1 1 290 . 63 GLU N N 119.9 0.2 1 291 . 64 LEU H H 7.36 0.02 1 292 . 64 LEU C C 180.1 0.1 1 293 . 64 LEU CA C 57.5 0.1 1 294 . 64 LEU N N 117.1 0.2 1 295 . 65 LEU H H 7.74 0.02 1 296 . 65 LEU C C 180.5 0.1 1 297 . 65 LEU CA C 56.9 0.1 1 298 . 65 LEU N N 120.5 0.2 1 299 . 66 ASP H H 9.11 0.02 1 300 . 66 ASP C C 178.6 0.1 1 301 . 66 ASP CA C 57.0 0.1 1 302 . 66 ASP CB C 39.5 0.1 1 303 . 66 ASP N N 124.2 0.2 1 304 . 67 ASP H H 8.59 0.02 1 305 . 67 ASP C C 177.0 0.1 1 306 . 67 ASP CA C 54.5 0.1 1 307 . 67 ASP CB C 39.5 0.1 1 308 . 67 ASP N N 117.1 0.2 1 309 . 68 GLY H H 7.83 0.02 1 310 . 68 GLY C C 174.0 0.1 1 311 . 68 GLY CA C 45.2 0.1 1 312 . 68 GLY N N 126.4 0.2 1 313 . 69 ILE H H 7.99 0.02 1 314 . 69 ILE C C 177.8 0.1 1 315 . 69 ILE CA C 63.5 0.1 1 316 . 69 ILE N N 117.7 0.2 1 317 . 69 ILE CB C 37.2 0.1 1 318 . 70 LEU H H 7.09 0.02 1 319 . 70 LEU C C 174.6 0.1 1 320 . 70 LEU CA C 52.1 0.1 1 321 . 70 LEU CB C 45.7 0.1 1 322 . 70 LEU N N 117.7 0.2 1 323 . 71 LYS H H 9.10 0.02 1 324 . 71 LYS C C 173.0 0.1 1 325 . 71 LYS CA C 54.0 0.1 1 326 . 71 LYS CB C 35.2 0.1 1 327 . 71 LYS N N 115.6 0.2 1 328 . 72 GLN H H 8.74 0.02 1 329 . 72 GLN HE21 H 7.27 0.02 1 330 . 72 GLN HE22 H 7.03 0.02 1 331 . 72 GLN C C 174.6 0.1 1 332 . 72 GLN CA C 54.2 0.1 1 333 . 72 GLN CB C 30.8 0.1 1 334 . 72 GLN N N 121.7 0.2 1 335 . 72 GLN NE2 N 111.8 0.2 1 336 . 73 ILE H H 8.82 0.02 1 337 . 73 ILE C C 173.8 0.1 1 338 . 73 ILE CA C 58.8 0.1 1 339 . 73 ILE CB C 39.7 0.1 1 340 . 73 ILE N N 124.8 0.2 1 341 . 74 LYS H H 8.25 0.02 1 342 . 74 LYS C C 176.1 0.1 1 343 . 74 LYS CA C 54.5 0.1 1 344 . 74 LYS CB C 33.1 0.1 1 345 . 74 LYS N N 123.0 0.2 1 346 . 75 VAL H H 8.83 0.02 1 347 . 75 VAL C C 174.8 0.1 1 348 . 75 VAL CA C 60.0 0.1 1 349 . 75 VAL CB C 33.8 0.1 1 350 . 75 VAL N N 122.0 0.2 1 351 . 76 LYS H H 8.47 0.02 1 352 . 76 LYS C C 176.1 0.1 1 353 . 76 LYS CA C 55.3 0.1 1 354 . 76 LYS CB C 32.5 0.1 1 355 . 76 LYS N N 124.5 0.2 1 356 . 77 LYS H H 8.52 0.02 1 357 . 77 LYS C C 175.8 0.1 1 358 . 77 LYS CA C 54.9 0.1 1 359 . 77 LYS CB C 33.5 0.1 1 360 . 77 LYS N N 124.8 0.2 1 361 . 78 GLU H H 8.64 0.02 1 362 . 78 GLU C C 176.9 0.1 1 363 . 78 GLU CA C 56.5 0.1 1 364 . 78 GLU CB C 29.0 0.1 1 365 . 78 GLU N N 124.2 0.2 1 366 . 79 GLY H H 8.47 0.02 1 367 . 79 GLY C C 173.6 0.1 1 368 . 79 GLY CA C 44.5 0.1 1 369 . 79 GLY N N 111.2 0.2 1 370 . 80 ALA H H 8.14 0.02 1 371 . 80 ALA C C 177.8 0.1 1 372 . 80 ALA CA C 52.1 0.1 1 373 . 80 ALA CB C 18.9 0.1 1 374 . 80 ALA N N 123.9 0.2 1 375 . 81 LYS H H 8.18 0.02 1 376 . 81 LYS C C 176.3 0.1 1 377 . 81 LYS CA C 56.0 0.1 1 378 . 81 LYS CB C 32.0 0.1 1 379 . 81 LYS N N 118.0 0.2 1 380 . 82 LEU H H 8.12 0.02 1 381 . 82 LEU C C 176.7 0.1 1 382 . 82 LEU CA C 54.6 0.1 1 383 . 82 LEU CB C 40.7 0.1 1 384 . 82 LEU N N 121.1 0.2 1 385 . 83 GLN H H 8.18 0.02 1 386 . 83 GLN HE21 H 7.53 0.02 1 387 . 83 GLN HE22 H 6.86 0.02 1 388 . 83 GLN C C 174.9 0.1 1 389 . 83 GLN CA C 55.1 0.1 1 390 . 83 GLN CB C 29.4 0.1 1 391 . 83 GLN N N 120.5 0.2 1 392 . 83 GLN NE2 N 112.2 0.2 1 393 . 84 GLU H H 8.37 0.02 1 394 . 84 GLU C C 175.6 0.1 1 395 . 84 GLU CA C 55.1 0.1 1 396 . 84 GLU CB C 31.0 0.1 1 397 . 84 GLU N N 121.4 0.2 1 398 . 85 VAL H H 8.79 0.02 1 399 . 85 VAL C C 174.3 0.1 1 400 . 85 VAL CA C 60.5 0.1 1 401 . 85 VAL CB C 33.5 0.1 1 402 . 85 VAL N N 121.7 0.2 1 403 . 86 VAL H H 8.19 0.02 1 404 . 86 VAL C C 175.0 0.1 1 405 . 86 VAL CA C 61.4 0.1 1 406 . 86 VAL CB C 32.0 0.1 1 407 . 86 VAL N N 123.6 0.2 1 408 . 87 LEU H H 8.94 0.02 1 409 . 87 LEU C C 173.5 0.1 1 410 . 87 LEU CA C 53.2 0.1 1 411 . 87 LEU CB C 43.9 0.1 1 412 . 87 LEU N N 110.3 0.2 1 413 . 88 TYR H H 7.58 0.02 1 414 . 88 TYR C C 174.3 0.1 1 415 . 88 TYR CA C 56.9 0.1 1 416 . 88 TYR CB C 39.7 0.1 1 417 . 88 TYR N N 118.3 0.2 1 418 . 89 GLN H H 8.43 0.02 1 419 . 89 GLN HE21 H 7.32 0.02 1 420 . 89 GLN HE22 H 6.87 0.02 1 421 . 89 GLN C C 175.0 0.1 1 422 . 89 GLN CA C 52.3 0.1 1 423 . 89 GLN CB C 33.3 0.1 1 424 . 89 GLN N N 118.3 0.2 1 425 . 89 GLN NE2 N 111.1 0.2 1 426 . 90 PHE H H 9.04 0.02 1 427 . 90 PHE C C 176.2 0.1 1 428 . 90 PHE CA C 60.4 0.1 1 429 . 90 PHE CB C 38.1 0.1 1 430 . 90 PHE N N 117.4 0.2 1 431 . 91 LYS H H 8.86 0.02 1 432 . 91 LYS C C 175.5 0.1 1 433 . 91 LYS CA C 56.6 0.1 1 434 . 91 LYS CB C 32.1 0.1 1 435 . 91 LYS N N 124.2 0.2 1 436 . 92 ASP H H 7.45 0.02 1 437 . 92 ASP C C 175.4 0.1 1 438 . 92 ASP CA C 52.2 0.1 1 439 . 92 ASP CB C 40.5 0.1 1 440 . 92 ASP N N 117.1 0.2 1 441 . 93 TYR H H 9.00 0.02 1 442 . 93 TYR C C 177.8 0.1 1 443 . 93 TYR CA C 58.5 0.1 1 444 . 93 TYR CB C 40.3 0.1 1 445 . 93 TYR N N 124.8 0.2 1 446 . 94 GLU H H 8.18 0.02 1 447 . 94 GLU C C 179.6 0.1 1 448 . 94 GLU CA C 58.9 0.1 1 449 . 94 GLU CB C 32.0 0.1 1 450 . 94 GLU N N 118.3 0.2 1 451 . 95 ALA H H 7.86 0.02 1 452 . 95 ALA C C 181.0 0.1 1 453 . 95 ALA CA C 53.9 0.1 1 454 . 95 ALA CB C 17.4 0.1 1 455 . 95 ALA N N 122.3 0.2 1 456 . 96 ALA H H 7.59 0.02 1 457 . 96 ALA C C 178.7 0.1 1 458 . 96 ALA CA C 54.8 0.1 1 459 . 96 ALA CB C 18.5 0.1 1 460 . 96 ALA N N 121.7 0.2 1 461 . 97 LYS H H 8.05 0.02 1 462 . 97 LYS C C 180.1 0.1 1 463 . 97 LYS CA C 59.4 0.1 1 464 . 97 LYS CB C 31.0 0.1 1 465 . 97 LYS N N 117.4 0.2 1 466 . 98 LEU H H 7.78 0.02 1 467 . 98 LEU C C 178.9 0.1 1 468 . 98 LEU CA C 57.3 0.1 1 469 . 98 LEU CB C 40.3 0.1 1 470 . 98 LEU N N 120.5 0.2 1 471 . 99 TYR H H 8.05 0.02 1 472 . 99 TYR C C 178.0 0.1 1 473 . 99 TYR CA C 60.9 0.1 1 474 . 99 TYR N N 121.4 0.2 1 475 . 100 LYS H H 8.38 0.02 1 476 . 100 LYS C C 177.9 0.1 1 477 . 100 LYS CA C 61.0 0.1 1 478 . 100 LYS CB C 31.6 0.1 1 479 . 100 LYS N N 117.1 0.2 1 480 . 101 LYS H H 7.76 0.02 1 481 . 101 LYS C C 179.5 0.1 1 482 . 101 LYS CA C 59.4 0.1 1 483 . 101 LYS CB C 31.2 0.1 1 484 . 101 LYS N N 117.4 0.2 1 485 . 102 GLN H H 7.87 0.02 1 486 . 102 GLN HE21 H 7.45 0.02 1 487 . 102 GLN HE22 H 6.83 0.02 1 488 . 102 GLN C C 179.1 0.1 1 489 . 102 GLN CA C 57.8 0.1 1 490 . 102 GLN CB C 27.0 0.1 1 491 . 102 GLN N N 119.0 0.2 1 492 . 102 GLN NE2 N 110.9 0.2 1 493 . 103 LEU H H 8.34 0.02 1 494 . 103 LEU C C 179.2 0.1 1 495 . 103 LEU CA C 54.6 0.1 1 496 . 103 LEU CB C 40.0 0.1 1 497 . 103 LEU N N 122.7 0.2 1 498 . 104 LYS H H 8.29 0.02 1 499 . 104 LYS C C 177.7 0.1 1 500 . 104 LYS CA C 59.0 0.1 1 501 . 104 LYS CB C 30.9 0.1 1 502 . 104 LYS N N 121.4 0.2 1 503 . 105 VAL H H 6.88 0.02 1 504 . 105 VAL C C 179.5 0.1 1 505 . 105 VAL CA C 65.4 0.1 1 506 . 105 VAL CB C 30.6 0.1 1 507 . 105 VAL N N 116.5 0.2 1 508 . 106 GLU H H 7.57 0.02 1 509 . 106 GLU C C 180.7 0.1 1 510 . 106 GLU CA C 58.6 0.1 1 511 . 106 GLU CB C 29.5 0.1 1 512 . 106 GLU N N 117.7 0.2 1 513 . 107 LEU H H 9.03 0.02 1 514 . 107 LEU C C 173.0 0.1 1 515 . 107 LEU CA C 57.8 0.1 1 516 . 107 LEU N N 123.3 0.2 1 517 . 108 ASP H H 8.74 0.02 1 518 . 108 ASP C C 179.5 0.1 1 519 . 108 ASP CA C 57.2 0.1 1 520 . 108 ASP N N 121.7 0.2 1 521 . 109 ARG H H 8.09 0.02 1 522 . 109 ARG C C 178.1 0.1 1 523 . 109 ARG CA C 59.1 0.1 1 524 . 109 ARG CB C 28.7 0.1 1 525 . 109 ARG N N 120.5 0.2 1 526 . 110 SER H H 7.16 0.02 1 527 . 110 SER HG H 4.90 0.02 1 528 . 110 SER C C 174.5 0.1 1 529 . 110 SER CA C 62.6 0.1 1 530 . 110 SER N N 114.6 0.2 1 531 . 111 LYS H H 8.60 0.02 1 532 . 111 LYS C C 177.6 0.1 1 533 . 111 LYS CA C 59.9 0.1 1 534 . 111 LYS N N 122.0 0.2 1 535 . 112 LYS H H 7.65 0.02 1 536 . 112 LYS C C 179.9 0.1 1 537 . 112 LYS CA C 59.0 0.1 1 538 . 112 LYS CB C 31.8 0.1 1 539 . 112 LYS N N 117.1 0.2 1 540 . 113 LEU H H 8.32 0.02 1 541 . 113 LEU C C 178.5 0.1 1 542 . 113 LEU CA C 57.9 0.1 1 543 . 113 LEU CB C 41.1 0.1 1 544 . 113 LEU N N 121.1 0.2 1 545 . 114 ILE H H 8.04 0.02 1 546 . 114 ILE C C 177.7 0.1 1 547 . 114 ILE CA C 63.5 0.1 1 548 . 114 ILE N N 118.6 0.2 1 549 . 115 GLU H H 8.69 0.02 1 550 . 115 GLU C C 179.6 0.1 1 551 . 115 GLU CA C 59.4 0.1 1 552 . 115 GLU CB C 28.3 0.1 1 553 . 115 GLU N N 118.0 0.2 1 554 . 116 LYS H H 8.42 0.02 1 555 . 116 LYS C C 177.5 0.1 1 556 . 116 LYS CA C 59.0 0.1 1 557 . 116 LYS N N 121.7 0.2 1 558 . 117 ALA H H 8.26 0.02 1 559 . 117 ALA C C 182.1 0.1 1 560 . 117 ALA CA C 54.0 0.1 1 561 . 117 ALA CB C 19.0 0.1 1 562 . 117 ALA N N 120.8 0.2 1 563 . 118 LEU H H 8.47 0.02 1 564 . 118 LEU C C 178.6 0.1 1 565 . 118 LEU CA C 57.7 0.1 1 566 . 118 LEU CB C 41.7 0.1 1 567 . 118 LEU N N 119.3 0.2 1 568 . 119 SER H H 8.10 0.02 1 569 . 119 SER C C 176.9 0.1 1 570 . 119 SER CA C 60.3 0.1 1 571 . 119 SER CB C 63.2 0.1 1 572 . 119 SER N N 114.3 0.2 1 573 . 120 ASP H H 8.92 0.02 1 574 . 120 ASP C C 178.4 0.1 1 575 . 120 ASP CA C 55.8 0.1 1 576 . 120 ASP CB C 40.8 0.1 1 577 . 120 ASP N N 116.8 0.2 1 578 . 121 ASN H H 6.99 0.02 1 579 . 121 ASN C C 171.5 0.1 1 580 . 121 ASN CA C 54.0 0.1 1 581 . 121 ASN CB C 41.2 0.1 1 582 . 121 ASN N N 111.2 0.2 1 583 . 122 PHE H H 7.02 0.02 1 584 . 122 PHE C C 179.7 0.1 1 585 . 122 PHE CA C 58.3 0.1 1 586 . 122 PHE CB C 40.8 0.1 1 587 . 122 PHE N N 120.5 0.2 1 stop_ save_