data_7278 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone amide chemical shifts for iG80b E. coli RNase H ; _BMRB_accession_number 7278 _BMRB_flat_file_name bmr7278.str _Entry_type original _Submission_date 2006-08-28 _Accession_date 2006-08-29 _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 Butterwick Joel A. . 2 Palmer Arthur G. III stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-10-09 original author . stop_ _Original_release_date 2007-10-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'An inserted Gly residue fine tunes dynamics between mesophilc and thermophilic ribonucleases H' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17088323 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Butterwick Joel A. . 2 Palmer Arthur G. III stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 15 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2697 _Page_last 2707 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'iG80b ecRNH' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'iG80b ecRNH' $iG80b_ecRNH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_iG80b_ecRNH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'iG80b ecRNH' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; MLKQVEIFTDGSCLGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQ GWIHNWKKRGWKTADKKPVK NVDLWQRLDAALGQHQIKWE WVKGHAGHPENERCDELARA AAMNPTLEDTGYQVEV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 LYS 4 GLN 5 VAL 6 GLU 7 ILE 8 PHE 9 THR 10 ASP 11 GLY 12 SER 13 CYS 14 LEU 15 GLY 16 ASN 17 PRO 18 GLY 19 PRO 20 GLY 21 GLY 22 TYR 23 GLY 24 ALA 25 ILE 26 LEU 27 ARG 28 TYR 29 ARG 30 GLY 31 ARG 32 GLU 33 LYS 34 THR 35 PHE 36 SER 37 ALA 38 GLY 39 TYR 40 THR 41 ARG 42 THR 43 THR 44 ASN 45 ASN 46 ARG 47 MET 48 GLU 49 LEU 50 MET 51 ALA 52 ALA 53 ILE 54 VAL 55 ALA 56 LEU 57 GLU 58 ALA 59 LEU 60 LYS 61 GLU 62 HIS 63 CYS 64 GLU 65 VAL 66 ILE 67 LEU 68 SER 69 THR 70 ASP 71 SER 72 GLN 73 TYR 74 VAL 75 ARG 76 GLN 77 GLY 78 ILE 79 THR 80 GLN 81 GLY 82 TRP 83 ILE 84 HIS 85 ASN 86 TRP 87 LYS 88 LYS 89 ARG 90 GLY 91 TRP 92 LYS 93 THR 94 ALA 95 ASP 96 LYS 97 LYS 98 PRO 99 VAL 100 LYS 101 ASN 102 VAL 103 ASP 104 LEU 105 TRP 106 GLN 107 ARG 108 LEU 109 ASP 110 ALA 111 ALA 112 LEU 113 GLY 114 GLN 115 HIS 116 GLN 117 ILE 118 LYS 119 TRP 120 GLU 121 TRP 122 VAL 123 LYS 124 GLY 125 HIS 126 ALA 127 GLY 128 HIS 129 PRO 130 GLU 131 ASN 132 GLU 133 ARG 134 CYS 135 ASP 136 GLU 137 LEU 138 ALA 139 ARG 140 ALA 141 ALA 142 ALA 143 MET 144 ASN 145 PRO 146 THR 147 LEU 148 GLU 149 ASP 150 THR 151 GLY 152 TYR 153 GLN 154 VAL 155 GLU 156 VAL 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 1657 "ribonuclease H" 100.00 155 99.36 99.36 1.45e-109 BMRB 4012 RNase_H1 100.00 155 97.44 97.44 1.11e-106 PDB 1F21 "Divalent Metal Cofactor Binding In The Kinetic Folding Trajectory Of E. Coli Ribonuclease Hi" 100.00 155 97.44 97.44 1.11e-106 PDB 1GOA "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.00 156 100.00 100.00 4.06e-112 PDB 1GOB "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.00 155 98.72 98.72 6.85e-109 PDB 1GOC "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.00 156 99.36 99.36 2.18e-111 PDB 1KVA "E. Coli Ribonuclease Hi D134a Mutant" 100.00 155 98.72 98.72 1.57e-108 PDB 1KVB "E. Coli Ribonuclease Hi D134h Mutant" 100.00 155 98.72 98.72 2.11e-108 PDB 1KVC "E. Coli Ribonuclease Hi D134n Mutant" 100.00 155 98.72 99.36 6.70e-109 PDB 1LAV "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 98.72 99.36 3.96e-109 PDB 1LAW "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 98.72 99.36 2.15e-109 PDB 1RBR "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 98.72 98.72 4.44e-108 PDB 1RBS "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 98.72 98.72 2.57e-108 PDB 1RBT "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 98.72 98.72 1.93e-108 PDB 1RBU "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 98.72 98.72 9.61e-109 PDB 1RBV "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 98.72 98.72 9.71e-109 PDB 1RCH "Solution Nmr Structure Of Ribonuclease Hi From Escherichia Coli, 8 Structures" 100.00 155 99.36 99.36 1.45e-109 PDB 1RDA "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 98.72 99.36 6.70e-109 PDB 1RDB "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 98.72 99.36 3.79e-109 PDB 1RDC "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 98.72 99.36 6.70e-109 PDB 1RDD "Crystal Structure Of Escherichia Coli Rnase Hi In Complex With Mg2+ At 2.8 Angstroms Resolution: Proof For A Single Mg2+ Site" 100.00 155 99.36 99.36 1.45e-109 PDB 1RNH "Structure Of Ribonuclease H Phased At 2 Angstroms Resolution By Mad Analysis Of The Selenomethionyl Protein" 99.36 155 97.42 97.42 1.93e-105 PDB 1WSE "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48a) With Mn2+" 100.00 155 98.08 98.08 5.28e-108 PDB 1WSF "Co-crystal Structure Of E.coli Rnase Hi Active Site Mutant (d134a*) With Mn2+" 100.00 155 98.08 98.08 9.64e-108 PDB 1WSG "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aD134N) WITH MN2+" 100.00 155 97.44 98.08 2.39e-107 PDB 1WSH "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87A)" 100.00 155 98.08 98.08 5.28e-108 PDB 1WSI "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87AD134N)" 100.00 155 97.44 98.08 2.39e-107 PDB 1WSJ "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (K87aH124A)" 100.00 155 98.08 98.08 1.38e-107 PDB 2RN2 "Structural Details Of Ribonuclease H From Escherichia Coli As Refined To An Atomic Resolution" 100.00 155 99.36 99.36 1.45e-109 PDB 3AA2 "A52i E. Coli Rnase Hi" 100.00 155 98.72 98.72 8.33e-109 PDB 3AA3 "A52l E. Coli Rnase Hi" 100.00 155 98.72 98.72 8.52e-109 PDB 3AA4 "A52v E.Coli Rnase Hi" 100.00 155 98.72 98.72 5.87e-109 PDB 3AA5 "A52f E.Coli Rnase Hi" 100.00 155 98.72 98.72 9.50e-109 DBJ BAA77885 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. W3110]" 100.00 155 99.36 99.36 1.45e-109 DBJ BAB33633 "RNase HI [Escherichia coli O157:H7 str. Sakai]" 100.00 155 99.36 99.36 1.45e-109 DBJ BAG75734 "ribonuclease H [Escherichia coli SE11]" 100.00 155 99.36 99.36 1.45e-109 DBJ BAI23570 "ribonuclease HI [Escherichia coli O26:H11 str. 11368]" 100.00 155 99.36 99.36 1.45e-109 DBJ BAI29084 "ribonuclease HI [Escherichia coli O103:H2 str. 12009]" 100.00 155 98.72 99.36 6.70e-109 EMBL CAA23620 "ribonuclease H [Escherichia coli]" 100.00 155 99.36 99.36 1.45e-109 EMBL CAA27660 "unnamed protein product [Escherichia coli]" 100.00 155 99.36 99.36 1.45e-109 EMBL CAP74778 "ribonuclease HI [Escherichia coli LF82]" 100.00 155 98.72 98.72 1.39e-108 EMBL CAQ30729 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli BL21(DE3)]" 100.00 155 99.36 99.36 1.45e-109 EMBL CAQ87812 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia fergusonii ATCC 35469]" 100.00 155 99.36 99.36 1.45e-109 GB AAA24565 "ribonuclease H [Escherichia coli]" 100.00 155 99.36 99.36 1.45e-109 GB AAB08636 "ribonuclease H [Escherichia coli]" 100.00 155 99.36 99.36 1.45e-109 GB AAC73319 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 99.36 99.36 1.45e-109 GB AAG54510 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli O157:H7 str. EDL933]" 100.00 155 99.36 99.36 1.45e-109 GB AAN41862 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 99.36 99.36 6.09e-110 REF NP_285902 "ribonuclease H [Escherichia coli O157:H7 str. EDL933]" 100.00 155 99.36 99.36 1.45e-109 REF NP_308237 "ribonuclease H [Escherichia coli O157:H7 str. Sakai]" 100.00 155 99.36 99.36 1.45e-109 REF NP_414750 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 99.36 99.36 1.45e-109 REF NP_706155 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 99.36 99.36 6.09e-110 REF NP_752197 "ribonuclease H [Escherichia coli CFT073]" 100.00 155 98.72 99.36 6.27e-109 SP A7ZHV1 "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli E24377A]" 100.00 155 99.36 99.36 1.45e-109 SP A7ZWF6 "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli HS]" 100.00 155 98.72 99.36 6.70e-109 SP B1IPU4 "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli ATCC 8739]" 100.00 155 99.36 99.36 1.45e-109 SP B1LHM3 "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli SMS-3-5]" 100.00 155 99.36 99.36 1.45e-109 SP B1XD78 "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli str. K-12 substr. DH10B]" 100.00 155 99.36 99.36 1.45e-109 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $iG80b_ecRNH 'E. coli' 562 Eubacteria Protista Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $iG80b_ecRNH 'recombinant technology' . Escherichia coli BL21(DE3) . 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 $iG80b_ecRNH 1.0 mM '[U-2H; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_700MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AV _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HMQC-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-NOESY-HSQC _Sample_label $sample_1 save_ save_1H-15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_HMQC-NOESY-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 1 mM pH 5.5 0.1 pH temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' HMQC-NOESY-HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'iG80b ecRNH' _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 2 LEU H H 8.698 0.01 1 2 2 2 LEU N N 125.722 0.1 1 3 3 3 LYS H H 8.720 0.01 1 4 3 3 LYS N N 124.362 0.1 1 5 4 4 GLN H H 8.300 0.01 1 6 4 4 GLN N N 123.183 0.1 1 7 5 5 VAL H H 8.763 0.01 1 8 5 5 VAL N N 122.661 0.1 1 9 6 6 GLU H H 8.627 0.01 1 10 6 6 GLU N N 124.813 0.1 1 11 7 7 ILE H H 8.549 0.01 1 12 7 7 ILE N N 122.330 0.1 1 13 8 8 PHE H H 9.190 0.01 1 14 8 8 PHE N N 128.929 0.1 1 15 9 9 THR H H 8.102 0.01 1 16 9 9 THR N N 110.369 0.1 1 17 10 10 ASP H H 9.072 0.01 1 18 10 10 ASP N N 121.772 0.1 1 19 11 11 GLY H H 8.684 0.01 1 20 11 11 GLY N N 107.621 0.1 1 21 12 12 SER H H 8.821 0.01 1 22 12 12 SER N N 114.518 0.1 1 23 13 13 CYS H H 8.467 0.01 1 24 13 13 CYS N N 123.754 0.1 1 25 14 14 LEU H H 9.047 0.01 1 26 14 14 LEU N N 128.999 0.1 1 27 15 15 GLY H H 7.830 0.01 1 28 15 15 GLY N N 108.403 0.1 1 29 18 18 GLY H H 8.308 0.01 1 30 18 18 GLY N N 105.967 0.1 1 31 20 20 GLY H H 8.948 0.01 1 32 20 20 GLY N N 108.908 0.1 1 33 21 21 GLY H H 9.051 0.01 1 34 21 21 GLY N N 107.236 0.1 1 35 22 22 TYR H H 7.870 0.01 1 36 22 22 TYR N N 113.783 0.1 1 37 23 23 GLY H H 9.034 0.01 1 38 23 23 GLY N N 106.776 0.1 1 39 24 24 ALA H H 9.515 0.01 1 40 24 24 ALA N N 126.729 0.1 1 41 25 25 ILE H H 9.120 0.01 1 42 25 25 ILE N N 121.551 0.1 1 43 26 26 LEU H H 9.204 0.01 1 44 26 26 LEU N N 129.527 0.1 1 45 27 27 ARG H H 9.894 0.01 1 46 27 27 ARG N N 126.463 0.1 1 47 28 28 TYR H H 8.627 0.01 1 48 28 28 TYR N N 125.627 0.1 1 49 29 29 ARG H H 9.334 0.01 1 50 29 29 ARG N N 127.755 0.1 1 51 30 30 GLY H H 8.705 0.01 1 52 30 30 GLY N N 105.675 0.1 1 53 31 31 ARG H H 7.995 0.01 1 54 31 31 ARG N N 122.064 0.1 1 55 32 32 GLU H H 8.747 0.01 1 56 32 32 GLU N N 123.276 0.1 1 57 33 33 LYS H H 9.217 0.01 1 58 33 33 LYS N N 125.729 0.1 1 59 34 34 THR H H 8.128 0.01 1 60 34 34 THR N N 115.580 0.1 1 61 35 35 PHE H H 9.347 0.01 1 62 35 35 PHE N N 121.343 0.1 1 63 36 36 SER H H 8.397 0.01 1 64 36 36 SER N N 114.521 0.1 1 65 37 37 ALA H H 6.370 0.01 1 66 37 37 ALA N N 121.663 0.1 1 67 38 38 GLY H H 8.525 0.01 1 68 38 38 GLY N N 106.773 0.1 1 69 39 39 TYR H H 9.695 0.01 1 70 39 39 TYR N N 123.573 0.1 1 71 40 40 THR H H 8.822 0.01 1 72 40 40 THR N N 114.178 0.1 1 73 41 41 ARG H H 7.754 0.01 1 74 41 41 ARG N N 120.504 0.1 1 75 42 42 THR H H 8.853 0.01 1 76 42 42 THR N N 125.720 0.1 1 77 43 43 THR H H 8.528 0.01 1 78 43 43 THR N N 107.286 0.1 1 79 44 44 ASN H H 9.137 0.01 1 80 44 44 ASN N N 121.199 0.1 1 81 45 45 ASN H H 8.584 0.01 1 82 45 45 ASN N N 117.084 0.1 1 83 46 46 ARG H H 7.356 0.01 1 84 46 46 ARG N N 116.820 0.1 1 85 47 47 MET H H 7.738 0.01 1 86 47 47 MET N N 118.636 0.1 1 87 51 51 ALA H H 7.700 0.01 1 88 51 51 ALA N N 117.626 0.1 1 89 52 52 ALA H H 6.443 0.01 1 90 52 52 ALA N N 114.189 0.1 1 91 55 55 ALA H H 6.841 0.01 1 92 55 55 ALA N N 119.995 0.1 1 93 58 58 ALA H H 7.083 0.01 1 94 58 58 ALA N N 120.276 0.1 1 95 59 59 LEU H H 7.122 0.01 1 96 59 59 LEU N N 118.611 0.1 1 97 60 60 LYS H H 8.548 0.01 1 98 60 60 LYS N N 122.767 0.1 1 99 61 61 GLU H H 7.664 0.01 1 100 61 61 GLU N N 117.382 0.1 1 101 62 62 HIS H H 8.417 0.01 1 102 62 62 HIS N N 119.596 0.1 1 103 63 63 CYS H H 10.997 0.01 1 104 63 63 CYS N N 126.965 0.1 1 105 64 64 GLU H H 8.692 0.01 1 106 64 64 GLU N N 123.039 0.1 1 107 65 65 VAL H H 8.833 0.01 1 108 65 65 VAL N N 126.072 0.1 1 109 67 67 LEU H H 8.624 0.01 1 110 67 67 LEU N N 135.444 0.1 1 111 68 68 SER H H 8.775 0.01 1 112 68 68 SER N N 121.622 0.1 1 113 69 69 THR H H 8.599 0.01 1 114 69 69 THR N N 120.144 0.1 1 115 70 70 ASP H H 8.989 0.01 1 116 70 70 ASP N N 129.384 0.1 1 117 71 71 SER H H 8.705 0.01 1 118 71 71 SER N N 117.902 0.1 1 119 72 72 GLN H H 9.541 0.01 1 120 72 72 GLN N N 131.938 0.1 1 121 73 73 TYR H H 9.004 0.01 1 122 73 73 TYR N N 124.882 0.1 1 123 74 74 VAL H H 7.555 0.01 1 124 74 74 VAL N N 116.743 0.1 1 125 75 75 ARG H H 6.905 0.01 1 126 75 75 ARG N N 117.469 0.1 1 127 76 76 GLN H H 8.126 0.01 1 128 76 76 GLN N N 121.449 0.1 1 129 77 77 GLY H H 7.181 0.01 1 130 77 77 GLY N N 104.605 0.1 1 131 78 78 ILE H H 8.126 0.01 1 132 78 78 ILE N N 120.774 0.1 1 133 79 79 THR H H 8.120 0.01 1 134 79 79 THR N N 112.829 0.1 1 stop_ save_