data_1657 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy ; _BMRB_accession_number 1657 _BMRB_flat_file_name bmr1657.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Yamazaki Toshio . . 2 Yoshida Mayumi . . 3 Kanaya Shigenori . . 4 Nakamura Haruki . . 5 Nagayama Kuniaki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 317 "13C chemical shifts" 122 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Yamazaki, Toshio, Yoshida, Mayumi, Kanaya, Shigenori, Nakamura, Haruki, Nagayama, Kuniaki, "Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy," Biochemistry 30, 6036-6047 (1991). ; _Citation_title ; Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yamazaki Toshio . . 2 Yoshida Mayumi . . 3 Kanaya Shigenori . . 4 Nakamura Haruki . . 5 Nagayama Kuniaki . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6036 _Page_last 6047 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_ribonuclease_H _Saveframe_category molecular_system _Mol_system_name 'ribonuclease H' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ribonuclease H' $ribonuclease_H stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ribonuclease_H _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribonuclease H' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; MLKQVEIFTDGSCLGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQ WIHNWKKRGWKTADKKPVKN VDLWQRLDAALGQHQIKWEW VKGHAGHPENERCDELARAA AMNPTLEDTGYQVEV ; 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 TRP 82 ILE 83 HIS 84 ASN 85 TRP 86 LYS 87 LYS 88 ARG 89 GLY 90 TRP 91 LYS 92 THR 93 ALA 94 ASP 95 LYS 96 LYS 97 PRO 98 VAL 99 LYS 100 ASN 101 VAL 102 ASP 103 LEU 104 TRP 105 GLN 106 ARG 107 LEU 108 ASP 109 ALA 110 ALA 111 LEU 112 GLY 113 GLN 114 HIS 115 GLN 116 ILE 117 LYS 118 TRP 119 GLU 120 TRP 121 VAL 122 LYS 123 GLY 124 HIS 125 ALA 126 GLY 127 HIS 128 PRO 129 GLU 130 ASN 131 GLU 132 ARG 133 CYS 134 ASP 135 GLU 136 LEU 137 ALA 138 ARG 139 ALA 140 ALA 141 ALA 142 MET 143 ASN 144 PRO 145 THR 146 LEU 147 GLU 148 ASP 149 THR 150 GLY 151 TYR 152 GLN 153 VAL 154 GLU 155 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 4012 "Ribonuclease H1" 100.00 155 98.06 98.06 2.35e-108 PDB 1F21 "Divalent Metal Cofactor Binding In The Kinetic Folding Trajectory Of E. Coli Ribonuclease Hi" 100.00 155 98.06 98.06 2.35e-108 PDB 1G15 "Co-Crystal Of E. Coli Rnase Hi With Two Mn2+ Ions Bound In The The Active Site" 100.00 155 97.42 97.42 9.22e-108 PDB 1GOA "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.65 156 99.36 99.36 1.97e-109 PDB 1GOB "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.00 155 99.35 99.35 1.10e-110 PDB 1GOC "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.65 156 98.72 98.72 9.82e-109 PDB 1JL1 "D10a E. Coli Ribonuclease Hi" 100.00 155 97.42 97.42 2.07e-107 PDB 1JXB "I53a, A Point Mutant Of The Cysteine-Free Variant Of E. Coli Rnase Hi" 100.00 155 97.42 97.42 1.01e-107 PDB 1KVA "E. Coli Ribonuclease Hi D134a Mutant" 100.00 155 99.35 99.35 2.63e-110 PDB 1KVB "E. Coli Ribonuclease Hi D134h Mutant" 100.00 155 99.35 99.35 3.74e-110 PDB 1KVC "E. Coli Ribonuclease Hi D134n Mutant" 100.00 155 99.35 100.00 1.19e-110 PDB 1LAV "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 99.35 100.00 6.79e-111 PDB 1LAW "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 99.35 100.00 3.68e-111 PDB 1RBR "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 99.35 99.35 6.45e-110 PDB 1RBS "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 99.35 99.35 4.55e-110 PDB 1RBT "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 99.35 99.35 2.87e-110 PDB 1RBU "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 99.35 99.35 1.40e-110 PDB 1RBV "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 99.35 99.35 1.49e-110 PDB 1RCH "Solution Nmr Structure Of Ribonuclease Hi From Escherichia Coli, 8 Structures" 100.00 155 100.00 100.00 2.28e-111 PDB 1RDA "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 99.35 100.00 1.19e-110 PDB 1RDB "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 99.35 100.00 6.29e-111 PDB 1RDC "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 99.35 100.00 1.19e-110 PDB 1RDD "Crystal Structure Of Escherichia Coli Rnase Hi In Complex With Mg2+ At 2.8 Angstroms Resolution: Proof For A Single Mg2+ Site" 100.00 155 100.00 100.00 2.28e-111 PDB 1RNH "Structure Of Ribonuclease H Phased At 2 Angstroms Resolution By Mad Analysis Of The Selenomethionyl Protein" 99.35 155 98.05 98.05 3.20e-107 PDB 1WSE "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48a) With Mn2+" 100.00 155 98.71 98.71 1.02e-109 PDB 1WSF "Co-crystal Structure Of E.coli Rnase Hi Active Site Mutant (d134a*) With Mn2+" 100.00 155 98.71 98.71 1.93e-109 PDB 1WSG "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aD134N) WITH MN2+" 100.00 155 98.06 98.71 4.28e-109 PDB 1WSH "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87A)" 100.00 155 98.71 98.71 1.02e-109 PDB 1WSI "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87AD134N)" 100.00 155 98.06 98.71 4.28e-109 PDB 1WSJ "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (K87aH124A)" 100.00 155 98.71 98.71 2.82e-109 PDB 2RN2 "Structural Details Of Ribonuclease H From Escherichia Coli As Refined To An Atomic Resolution" 100.00 155 100.00 100.00 2.28e-111 PDB 3AA2 "A52i E. Coli Rnase Hi" 100.00 155 99.35 99.35 1.72e-110 PDB 3AA3 "A52l E. Coli Rnase Hi" 100.00 155 99.35 99.35 1.96e-110 PDB 3AA4 "A52v E.Coli Rnase Hi" 100.00 155 99.35 99.35 1.02e-110 PDB 3AA5 "A52f E.Coli Rnase Hi" 100.00 155 99.35 99.35 1.78e-110 PDB 4Z0U "Rnase Hi/ssb-ct Complex" 100.00 155 100.00 100.00 2.28e-111 DBJ BAA77885 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K12 substr. W3110]" 100.00 155 100.00 100.00 2.28e-111 DBJ BAB33633 "RNase HI [Escherichia coli O157:H7 str. Sakai]" 100.00 155 100.00 100.00 2.28e-111 DBJ BAG75734 "ribonuclease H [Escherichia coli SE11]" 100.00 155 100.00 100.00 2.28e-111 DBJ BAI23570 "ribonuclease HI [Escherichia coli O26:H11 str. 11368]" 100.00 155 100.00 100.00 2.28e-111 DBJ BAI29084 "ribonuclease HI [Escherichia coli O103:H2 str. 12009]" 100.00 155 99.35 100.00 1.04e-110 EMBL CAA23620 "ribonuclease H [Escherichia coli]" 100.00 155 100.00 100.00 2.28e-111 EMBL CAA27660 "unnamed protein product [Escherichia coli]" 100.00 155 100.00 100.00 2.28e-111 EMBL CAP74778 "ribonuclease HI [Escherichia coli LF82]" 100.00 155 99.35 99.35 2.24e-110 EMBL CAQ30729 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli BL21(DE3)]" 100.00 155 100.00 100.00 2.28e-111 EMBL CAQ87812 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia fergusonii ATCC 35469]" 100.00 155 100.00 100.00 2.28e-111 GB AAA24565 "ribonuclease H [Escherichia coli]" 100.00 155 100.00 100.00 2.28e-111 GB AAB08636 "ribonuclease H [Escherichia coli]" 100.00 155 100.00 100.00 2.28e-111 GB AAC73319 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 100.00 100.00 2.28e-111 GB AAG54510 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli O157:H7 str. EDL933]" 100.00 155 100.00 100.00 2.28e-111 GB AAN41862 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 100.00 100.00 8.05e-112 REF NP_308237 "ribonuclease H [Escherichia coli O157:H7 str. Sakai]" 100.00 155 100.00 100.00 2.28e-111 REF NP_414750 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 100.00 100.00 2.28e-111 REF NP_706155 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 100.00 100.00 8.05e-112 REF WP_000917867 "ribonuclease H [Escherichia coli]" 100.00 155 99.35 99.35 2.24e-110 REF WP_000917875 "hypothetical protein [Escherichia albertii]" 100.00 155 99.35 100.00 6.15e-111 SP A7ZHV1 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 100.00 100.00 2.28e-111 SP A7ZWF6 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 99.35 100.00 1.04e-110 SP B1IPU4 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 100.00 100.00 2.28e-111 SP B1LHM3 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 100.00 100.00 2.28e-111 SP B1XD78 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 100.00 100.00 2.28e-111 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ribonuclease_H 'E. coli' 562 Bacteria . 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 $ribonuclease_H 'not available' . Escherichia coli N4839-1 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . na temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TMS C . . . 0 . . . . . $entry_citation $entry_citation TMS H . . . 0 . . . . . $entry_citation $entry_citation 'liquid ammonia' N . . . 0 . . . . . $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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'ribonuclease H' _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 CA C 53.1 . 1 2 . 1 MET HA H 4.17 . 1 3 . 2 LEU H H 8.71 . 1 4 . 2 LEU HA H 4.55 . 1 5 . 2 LEU N N 125.1 . 1 6 . 3 LYS H H 8.73 . 1 7 . 3 LYS CA C 55.1 . 1 8 . 3 LYS HA H 4.31 . 1 9 . 3 LYS N N 123.8 . 1 10 . 4 GLN H H 8.31 . 1 11 . 4 GLN CA C 53.3 . 1 12 . 4 GLN HA H 5.13 . 1 13 . 4 GLN N N 122.8 . 1 14 . 5 VAL H H 8.79 . 1 15 . 5 VAL HA H 4.82 . 1 16 . 5 VAL N N 121.8 . 1 17 . 6 GLU H H 8.64 . 1 18 . 6 GLU CA C 53.1 . 1 19 . 6 GLU HA H 4.83 . 1 20 . 6 GLU N N 124.1 . 1 21 . 7 ILE H H 8.6 . 1 22 . 7 ILE HA H 5.33 . 1 23 . 7 ILE N N 121.8 . 1 24 . 8 PHE H H 9.13 . 1 25 . 8 PHE CA C 53.5 . 1 26 . 8 PHE HA H 5.67 . 1 27 . 8 PHE N N 128.2 . 1 28 . 9 THR H H 8.05 . 1 29 . 9 THR CA C 58.8 . 1 30 . 9 THR HA H 5.61 . 1 31 . 9 THR N N 109.5 . 1 32 . 10 ASP H H 9.06 . 1 33 . 10 ASP CA C 52.7 . 1 34 . 10 ASP HA H 5.16 . 1 35 . 10 ASP N N 120.2 . 1 36 . 11 GLY H H 8.7 . 1 37 . 11 GLY CA C 42.4 . 1 38 . 11 GLY HA2 H 3.39 . 2 39 . 11 GLY HA3 H 5.04 . 2 40 . 11 GLY N N 106.7 . 1 41 . 12 SER H H 8.8 . 1 42 . 12 SER CA C 55.8 . 1 43 . 12 SER HA H 4.78 . 1 44 . 12 SER N N 113.5 . 1 45 . 13 CYS H H 8.44 . 1 46 . 13 CYS CA C 56.6 . 1 47 . 13 CYS HA H 4.96 . 1 48 . 13 CYS N N 123.2 . 1 49 . 14 LEU H H 9.05 . 1 50 . 14 LEU HA H 4.49 . 1 51 . 14 LEU N N 128.3 . 1 52 . 15 GLY H H 7.82 . 1 53 . 15 GLY CA C 42.8 . 1 54 . 15 GLY HA2 H 3.83 . 2 55 . 15 GLY HA3 H 4.11 . 2 56 . 15 GLY N N 107.6 . 1 57 . 16 ASN H H 8.24 . 1 58 . 16 ASN CA C 49.2 . 1 59 . 16 ASN HA H 5.06 . 1 60 . 16 ASN N N 116.2 . 1 61 . 17 PRO CA C 61.3 . 1 62 . 17 PRO HA H 4.92 . 1 63 . 18 GLY H H 8.32 . 1 64 . 18 GLY CA C 43.8 . 1 65 . 18 GLY HA2 H 3.9 . 2 66 . 18 GLY HA3 H 4.3 . 2 67 . 18 GLY N N 105.3 . 1 68 . 19 PRO CA C 61.3 . 1 69 . 19 PRO HA H 4.92 . 1 70 . 20 GLY H H 8.96 . 1 71 . 20 GLY CA C 43.8 . 1 72 . 20 GLY HA2 H 3.76 . 2 73 . 20 GLY HA3 H 5.07 . 2 74 . 20 GLY N N 108.4 . 1 75 . 21 GLY H H 9.04 . 1 76 . 21 GLY CA C 44.6 . 1 77 . 21 GLY HA2 H 4.22 . 2 78 . 21 GLY HA3 H 5.36 . 2 79 . 21 GLY N N 106.5 . 1 80 . 22 TYR H H 7.87 . 1 81 . 22 TYR CA C 53.5 . 1 82 . 22 TYR HA H 5.74 . 1 83 . 22 TYR N N 113.3 . 1 84 . 23 GLY H H 8.99 . 1 85 . 23 GLY CA C 43.4 . 1 86 . 23 GLY HA2 H 3.9 . 2 87 . 23 GLY HA3 H 5.17 . 2 88 . 23 GLY N N 106.2 . 1 89 . 24 ALA H H 9.52 . 1 90 . 24 ALA CA C 49.2 . 1 91 . 24 ALA HA H 5.89 . 1 92 . 24 ALA N N 126 . 1 93 . 25 ILE H H 9.04 . 1 94 . 25 ILE HA H 4.88 . 1 95 . 25 ILE N N 120.7 . 1 96 . 26 LEU H H 9.21 . 1 97 . 26 LEU HA H 5.29 . 1 98 . 26 LEU N N 129.2 . 1 99 . 27 ARG H H 9.98 . 1 100 . 27 ARG CA C 53.1 . 1 101 . 27 ARG HA H 5.47 . 1 102 . 27 ARG N N 127.1 . 1 103 . 28 TYR H H 8.59 . 1 104 . 28 TYR CA C 54.7 . 1 105 . 28 TYR HA H 5.06 . 1 106 . 28 TYR N N 125.2 . 1 107 . 29 ARG H H 9.37 . 1 108 . 29 ARG CA C 55.1 . 1 109 . 29 ARG HA H 3.78 . 1 110 . 29 ARG N N 126.7 . 1 111 . 30 GLY H H 8.72 . 1 112 . 30 GLY CA C 43.6 . 1 113 . 30 GLY HA2 H 3.61 . 2 114 . 30 GLY HA3 H 4.14 . 2 115 . 30 GLY N N 104.9 . 1 116 . 31 ARG H H 7.95 . 1 117 . 31 ARG CA C 52.9 . 1 118 . 31 ARG HA H 4.69 . 1 119 . 31 ARG N N 121 . 1 120 . 32 GLU H H 8.76 . 1 121 . 32 GLU CA C 53.1 . 1 122 . 32 GLU HA H 5.43 . 1 123 . 32 GLU N N 122.7 . 1 124 . 33 LYS H H 9.21 . 1 125 . 33 LYS CA C 53.1 . 1 126 . 33 LYS HA H 4.67 . 1 127 . 33 LYS N N 125 . 1 128 . 34 THR H H 8.14 . 1 129 . 34 THR CA C 58.2 . 1 130 . 34 THR HA H 5.32 . 1 131 . 34 THR N N 114.5 . 1 132 . 35 PHE H H 9.31 . 1 133 . 35 PHE CA C 54.5 . 1 134 . 35 PHE HA H 4.99 . 1 135 . 35 PHE N N 120.6 . 1 136 . 36 SER H H 8.4 . 1 137 . 36 SER CA C 56.2 . 1 138 . 36 SER HA H 4.58 . 1 139 . 36 SER N N 113.9 . 1 140 . 37 ALA H H 6.37 . 1 141 . 37 ALA CA C 50.2 . 1 142 . 37 ALA HA H 4.25 . 1 143 . 37 ALA N N 120.8 . 1 144 . 38 GLY H H 8.58 . 1 145 . 38 GLY CA C 42.2 . 1 146 . 38 GLY HA2 H 3.49 . 2 147 . 38 GLY HA3 H 5.36 . 2 148 . 38 GLY N N 106.2 . 1 149 . 39 TYR H H 9.69 . 1 150 . 39 TYR CA C 53.9 . 1 151 . 39 TYR HA H 5.47 . 1 152 . 39 TYR N N 122.8 . 1 153 . 40 THR H H 8.81 . 1 154 . 40 THR CA C 63.6 . 1 155 . 40 THR HA H 3.73 . 1 156 . 40 THR N N 113.5 . 1 157 . 41 ARG H H 7.77 . 1 158 . 41 ARG CA C 55.1 . 1 159 . 41 ARG HA H 3.88 . 1 160 . 41 ARG N N 119.9 . 1 161 . 42 THR H H 8.85 . 1 162 . 42 THR CA C 58 . 1 163 . 42 THR HA H 4.08 . 1 164 . 42 THR N N 125 . 1 165 . 43 THR H H 8.53 . 1 166 . 43 THR CA C 57 . 1 167 . 43 THR HA H 5.28 . 1 168 . 43 THR N N 106.5 . 1 169 . 44 ASN H H 9.19 . 1 170 . 44 ASN CA C 56 . 1 171 . 44 ASN HA H 3.92 . 1 172 . 44 ASN N N 120.6 . 1 173 . 45 ASN H H 8.56 . 1 174 . 45 ASN CA C 53.9 . 1 175 . 45 ASN HA H 4.03 . 1 176 . 45 ASN N N 116.3 . 1 177 . 46 ARG H H 7.38 . 1 178 . 46 ARG CA C 59 . 1 179 . 46 ARG HA H 3.58 . 1 180 . 46 ARG N N 116.5 . 1 181 . 47 MET H H 7.71 . 1 182 . 47 MET CA C 55.5 . 1 183 . 47 MET HA H 4.44 . 1 184 . 47 MET N N 118.2 . 1 185 . 48 GLU H H 8.44 . 1 186 . 48 GLU CA C 57.8 . 1 187 . 48 GLU HA H 3.86 . 1 188 . 48 GLU N N 119.3 . 1 189 . 49 LEU H H 7.24 . 1 190 . 49 LEU HA H 3.96 . 1 191 . 49 LEU N N 116.1 . 1 192 . 50 MET H H 8.69 . 1 193 . 50 MET CA C 55.5 . 1 194 . 50 MET HA H 3.93 . 1 195 . 50 MET N N 118.7 . 1 196 . 51 ALA H H 7.72 . 1 197 . 51 ALA CA C 53.3 . 1 198 . 51 ALA HA H 3.31 . 1 199 . 51 ALA N N 117 . 1 200 . 52 ALA H H 6.47 . 1 201 . 52 ALA CA C 52.7 . 1 202 . 52 ALA HA H 3.99 . 1 203 . 52 ALA N N 113.7 . 1 204 . 53 ILE H H 7.94 . 1 205 . 53 ILE HA H 3.13 . 1 206 . 53 ILE N N 116.5 . 1 207 . 54 VAL H H 8.25 . 1 208 . 54 VAL HA H 3.3 . 1 209 . 54 VAL N N 116.5 . 1 210 . 55 ALA H H 6.85 . 1 211 . 55 ALA CA C 52.7 . 1 212 . 55 ALA HA H 3.34 . 1 213 . 55 ALA N N 119.4 . 1 214 . 56 LEU H H 7.57 . 1 215 . 56 LEU HA H 3.76 . 1 216 . 56 LEU N N 112.8 . 1 217 . 57 GLU H H 8.75 . 1 218 . 57 GLU CA C 56.6 . 1 219 . 57 GLU HA H 3.94 . 1 220 . 57 GLU N N 118.4 . 1 221 . 58 ALA H H 7.1 . 1 222 . 58 ALA CA C 51.2 . 1 223 . 58 ALA HA H 4.11 . 1 224 . 58 ALA N N 119.6 . 1 225 . 59 LEU H H 7.15 . 1 226 . 59 LEU HA H 4.26 . 1 227 . 59 LEU N N 118.4 . 1 228 . 60 LYS H H 8.59 . 1 229 . 60 LYS CA C 53.9 . 1 230 . 60 LYS HA H 4.38 . 1 231 . 60 LYS N N 121.8 . 1 232 . 61 GLU H H 7.66 . 1 233 . 61 GLU CA C 52.2 . 1 234 . 61 GLU HA H 4.48 . 1 235 . 61 GLU N N 116.4 . 1 236 . 62 HIS H H 8.46 . 1 237 . 62 HIS HA H 4.77 . 1 238 . 62 HIS N N 119.2 . 1 239 . 63 CYS CA C 57 . 1 240 . 63 CYS HA H 5.12 . 1 241 . 64 GLU H H 8.75 . 1 242 . 64 GLU CA C 53.7 . 1 243 . 64 GLU HA H 5.02 . 1 244 . 64 GLU N N 122.6 . 1 245 . 65 VAL H H 8.82 . 1 246 . 65 VAL HA H 4.7 . 1 247 . 65 VAL N N 125.6 . 1 248 . 66 ILE H H 8.25 . 1 249 . 66 ILE HA H 4.75 . 1 250 . 66 ILE N N 127.4 . 1 251 . 67 LEU H H 8.57 . 1 252 . 67 LEU HA H 4.7 . 1 253 . 67 LEU N N 134.5 . 1 254 . 68 SER H H 8.72 . 1 255 . 68 SER CA C 54.5 . 1 256 . 68 SER HA H 5.73 . 1 257 . 68 SER N N 120.8 . 1 258 . 69 THR H H 8.5 . 1 259 . 69 THR CA C 58.6 . 1 260 . 69 THR HA H 5.11 . 1 261 . 69 THR N N 119.7 . 1 262 . 70 ASP H H 8.94 . 1 263 . 70 ASP CA C 51.2 . 1 264 . 70 ASP HA H 5.45 . 1 265 . 70 ASP N N 127.7 . 1 266 . 71 SER H H 8.31 . 1 267 . 71 SER CA C 56.8 . 1 268 . 71 SER HA H 4.52 . 1 269 . 71 SER N N 115.5 . 1 270 . 72 GLN H H 9.37 . 1 271 . 72 GLN CA C 56.2 . 1 272 . 72 GLN HA H 3.98 . 1 273 . 72 GLN N N 132.8 . 1 274 . 73 TYR H H 8.72 . 1 275 . 73 TYR CA C 59.3 . 1 276 . 73 TYR HA H 4.48 . 1 277 . 73 TYR N N 123.6 . 1 278 . 74 VAL H H 8.06 . 1 279 . 74 VAL HA H 3.6 . 1 280 . 74 VAL N N 117.4 . 1 281 . 75 ARG H H 7.08 . 1 282 . 75 ARG CA C 57.4 . 1 283 . 75 ARG HA H 2.52 . 1 284 . 75 ARG N N 117.7 . 1 285 . 76 GLN H H 8.22 . 1 286 . 76 GLN CA C 57 . 1 287 . 76 GLN HA H 3.15 . 1 288 . 76 GLN N N 120.6 . 1 289 . 77 GLY H H 7.82 . 1 290 . 77 GLY CA C 46.1 . 1 291 . 77 GLY HA2 H 3.14 . 2 292 . 77 GLY HA3 H 3.75 . 2 293 . 77 GLY N N 107.1 . 1 294 . 78 ILE H H 8.4 . 1 295 . 78 ILE HA H 3.73 . 1 296 . 78 ILE N N 119.9 . 1 297 . 79 THR H H 7.8 . 1 298 . 79 THR CA C 62.1 . 1 299 . 79 THR HA H 4.11 . 1 300 . 79 THR N N 107.4 . 1 301 . 80 GLN H H 7.53 . 1 302 . 80 GLN CA C 55.1 . 1 303 . 80 GLN HA H 4.47 . 1 304 . 80 GLN N N 117.3 . 1 305 . 81 TRP H H 7.1 . 1 306 . 81 TRP CA C 55.8 . 1 307 . 81 TRP HA H 4.28 . 1 308 . 81 TRP N N 118.2 . 1 309 . 82 ILE H H 8.48 . 1 310 . 82 ILE HA H 3.49 . 1 311 . 82 ILE N N 117.9 . 1 312 . 83 HIS H H 7.93 . 1 313 . 83 HIS HA H 4.13 . 1 314 . 83 HIS N N 118.4 . 1 315 . 84 ASN H H 7.44 . 1 316 . 84 ASN CA C 53.5 . 1 317 . 84 ASN HA H 4.38 . 1 318 . 84 ASN N N 117.7 . 1 319 . 85 TRP H H 8.2 . 1 320 . 85 TRP CA C 55.8 . 1 321 . 85 TRP HA H 4.38 . 1 322 . 85 TRP N N 120.3 . 1 323 . 86 LYS H H 8.12 . 1 324 . 86 LYS CA C 58.2 . 1 325 . 86 LYS HA H 2.7 . 1 326 . 86 LYS N N 119 . 1 327 . 87 LYS H H 7.36 . 1 328 . 87 LYS CA C 56.6 . 1 329 . 87 LYS HA H 4.09 . 1 330 . 87 LYS N N 119 . 1 331 . 88 ARG H H 7.24 . 1 332 . 88 ARG CA C 53.1 . 1 333 . 88 ARG HA H 4.48 . 1 334 . 88 ARG N N 116.3 . 1 335 . 89 GLY H H 7.78 . 1 336 . 89 GLY CA C 45.3 . 1 337 . 89 GLY HA2 H 3.93 . 1 338 . 89 GLY HA3 H 3.93 . 1 339 . 89 GLY N N 108.7 . 1 340 . 90 TRP H H 8.56 . 1 341 . 90 TRP CA C 56.2 . 1 342 . 90 TRP HA H 3.42 . 1 343 . 90 TRP N N 112.8 . 1 344 . 91 LYS H H 6.82 . 1 345 . 91 LYS CA C 52 . 1 346 . 91 LYS HA H 5.05 . 1 347 . 91 LYS N N 116.7 . 1 348 . 92 THR H H 8.9 . 1 349 . 92 THR CA C 59 . 1 350 . 92 THR HA H 4.38 . 1 351 . 92 THR N N 109.6 . 1 352 . 93 ALA H H 9.1 . 1 353 . 93 ALA CA C 53.1 . 1 354 . 93 ALA HA H 4.07 . 1 355 . 93 ALA N N 123.6 . 1 356 . 94 ASP H H 8 . 1 357 . 94 ASP CA C 51.2 . 1 358 . 94 ASP HA H 4.64 . 1 359 . 94 ASP N N 114 . 1 360 . 95 LYS H H 8.06 . 1 361 . 95 LYS CA C 55.8 . 1 362 . 95 LYS HA H 3.67 . 1 363 . 95 LYS N N 112.5 . 1 364 . 96 LYS H H 7.62 . 1 365 . 96 LYS CA C 51.6 . 1 366 . 96 LYS HA H 4.72 . 1 367 . 96 LYS N N 119.8 . 1 368 . 97 PRO CA C 60.9 . 1 369 . 97 PRO HA H 4.61 . 1 370 . 98 VAL H H 7.57 . 1 371 . 98 VAL HA H 3.44 . 1 372 . 98 VAL N N 120.7 . 1 373 . 99 LYS H H 8.29 . 1 374 . 99 LYS CA C 55.5 . 1 375 . 99 LYS HA H 4.05 . 1 376 . 99 LYS N N 127.9 . 1 377 . 100 ASN H H 9.45 . 1 378 . 100 ASN CA C 53.1 . 1 379 . 100 ASN HA H 4.28 . 1 380 . 100 ASN N N 115.8 . 1 381 . 101 VAL H H 7.65 . 1 382 . 101 VAL HA H 3.6 . 1 383 . 101 VAL N N 119 . 1 384 . 102 ASP H H 8.59 . 1 385 . 102 ASP CA C 54.3 . 1 386 . 102 ASP HA H 4.09 . 1 387 . 102 ASP N N 119 . 1 388 . 103 LEU H H 7.28 . 1 389 . 103 LEU HA H 4.16 . 1 390 . 103 LEU N N 118.6 . 1 391 . 104 TRP H H 8.55 . 1 392 . 104 TRP CA C 59.3 . 1 393 . 104 TRP HA H 4.56 . 1 394 . 104 TRP N N 121 . 1 395 . 105 GLN H H 8.42 . 1 396 . 105 GLN CA C 57.4 . 1 397 . 105 GLN HA H 3.66 . 1 398 . 105 GLN N N 115.8 . 1 399 . 106 ARG H H 7.02 . 1 400 . 106 ARG CA C 57.4 . 1 401 . 106 ARG HA H 4.18 . 1 402 . 106 ARG N N 121 . 1 403 . 107 LEU H H 8.76 . 1 404 . 107 LEU HA H 4.12 . 1 405 . 107 LEU N N 121.6 . 1 406 . 108 ASP H H 8.76 . 1 407 . 108 ASP CA C 56.6 . 1 408 . 108 ASP HA H 4.56 . 1 409 . 108 ASP N N 118.4 . 1 410 . 109 ALA H H 7.88 . 1 411 . 109 ALA CA C 52.9 . 1 412 . 109 ALA HA H 4.2 . 1 413 . 109 ALA N N 119.1 . 1 414 . 110 ALA H H 7.67 . 1 415 . 110 ALA CA C 52.7 . 1 416 . 110 ALA HA H 4.3 . 1 417 . 110 ALA N N 121 . 1 418 . 111 LEU H H 8.68 . 1 419 . 111 LEU HA H 4.1 . 1 420 . 111 LEU N N 117.4 . 1 421 . 112 GLY H H 7.54 . 1 422 . 112 GLY CA C 44.4 . 1 423 . 112 GLY HA2 H 4.13 . 2 424 . 112 GLY HA3 H 3.95 . 2 425 . 112 GLY N N 101.5 . 1 426 . 113 GLN H H 7.52 . 1 427 . 113 GLN CA C 53.5 . 1 428 . 113 GLN HA H 4.27 . 1 429 . 113 GLN N N 117.2 . 1 430 . 114 HIS H H 7.37 . 1 431 . 114 HIS HA H 5.04 . 1 432 . 114 HIS N N 116.6 . 1 433 . 115 GLN H H 8.48 . 1 434 . 115 GLN CA C 52.7 . 1 435 . 115 GLN HA H 4.74 . 1 436 . 115 GLN N N 120.9 . 1 437 . 116 ILE H H 8.57 . 1 438 . 116 ILE HA H 4.54 . 1 439 . 116 ILE N N 125.9 . 1 440 . 117 LYS H H 8.81 . 1 441 . 117 LYS CA C 52.7 . 1 442 . 117 LYS HA H 4.48 . 1 443 . 117 LYS N N 129.8 . 1 444 . 118 TRP H H 8.26 . 1 445 . 118 TRP CA C 54.1 . 1 446 . 118 TRP HA H 4.46 . 1 447 . 118 TRP N N 125.9 . 1 448 . 119 GLU H H 8.94 . 1 449 . 119 GLU CA C 52.5 . 1 450 . 119 GLU HA H 4.34 . 1 451 . 119 GLU N N 126.5 . 1 452 . 120 TRP H H 7.93 . 1 453 . 120 TRP CA C 52 . 1 454 . 120 TRP HA H 5.62 . 1 455 . 120 TRP N N 125.8 . 1 456 . 121 VAL H H 8.03 . 1 457 . 121 VAL HA H 4.2 . 1 458 . 121 VAL N N 123.6 . 1 459 . 122 LYS H H 8.46 . 1 460 . 122 LYS CA C 53.9 . 1 461 . 122 LYS HA H 4.54 . 1 462 . 122 LYS N N 124.3 . 1 463 . 123 GLY H H 8.46 . 1 464 . 123 GLY CA C 43.4 . 1 465 . 123 GLY HA2 H 4.07 . 2 466 . 123 GLY HA3 H 3.91 . 2 467 . 123 GLY N N 111.3 . 1 468 . 124 HIS H H 8.57 . 1 469 . 124 HIS HA H 4.64 . 1 470 . 124 HIS N N 116.5 . 1 471 . 125 ALA H H 8.14 . 1 472 . 125 ALA CA C 50.8 . 1 473 . 125 ALA HA H 4.45 . 1 474 . 125 ALA N N 123.5 . 1 475 . 126 GLY H H 8.66 . 1 476 . 126 GLY CA C 43.4 . 1 477 . 126 GLY HA2 H 3.82 . 1 478 . 126 GLY HA3 H 3.82 . 1 479 . 126 GLY N N 109.8 . 1 480 . 127 HIS H H 8.4 . 1 481 . 127 HIS HA H 5.23 . 1 482 . 127 HIS N N 118.5 . 1 483 . 128 PRO CA C 63.6 . 1 484 . 128 PRO HA H 4.39 . 1 485 . 129 GLU H H 9.37 . 1 486 . 129 GLU CA C 59 . 1 487 . 129 GLU HA H 3.63 . 1 488 . 129 GLU N N 117.8 . 1 489 . 130 ASN H H 7.66 . 1 490 . 130 ASN CA C 56.6 . 1 491 . 130 ASN HA H 4.45 . 1 492 . 130 ASN N N 117.2 . 1 493 . 131 GLU H H 7.83 . 1 494 . 131 GLU CA C 57.8 . 1 495 . 131 GLU HA H 3.92 . 1 496 . 131 GLU N N 120.2 . 1 497 . 132 ARG H H 8.02 . 1 498 . 132 ARG CA C 57.4 . 1 499 . 132 ARG HA H 4.09 . 1 500 . 132 ARG N N 119.8 . 1 501 . 133 CYS H H 8.1 . 1 502 . 133 CYS CA C 63.2 . 1 503 . 133 CYS HA H 4.01 . 1 504 . 133 CYS N N 117.8 . 1 505 . 134 ASP H H 7.78 . 1 506 . 134 ASP CA C 55.3 . 1 507 . 134 ASP HA H 4.46 . 1 508 . 134 ASP N N 120.8 . 1 509 . 135 GLU H H 7.83 . 1 510 . 135 GLU CA C 57.8 . 1 511 . 135 GLU HA H 3.92 . 1 512 . 135 GLU N N 118.9 . 1 513 . 136 LEU H H 8.3 . 1 514 . 136 LEU HA H 4.02 . 1 515 . 136 LEU N N 120.1 . 1 516 . 137 ALA H H 8.35 . 1 517 . 137 ALA CA C 53.5 . 1 518 . 137 ALA HA H 3.62 . 1 519 . 137 ALA N N 122.7 . 1 520 . 138 ARG H H 8.24 . 1 521 . 138 ARG CA C 57.6 . 1 522 . 138 ARG HA H 3.8 . 1 523 . 138 ARG N N 116.5 . 1 524 . 139 ALA H H 7.89 . 1 525 . 139 ALA CA C 52.9 . 1 526 . 139 ALA HA H 4.04 . 1 527 . 139 ALA N N 120.4 . 1 528 . 140 ALA H H 7.88 . 1 529 . 140 ALA CA C 52.7 . 1 530 . 140 ALA HA H 3.98 . 1 531 . 140 ALA N N 121.8 . 1 532 . 141 ALA H H 7.79 . 1 533 . 141 ALA CA C 52.7 . 1 534 . 141 ALA HA H 3.75 . 1 535 . 141 ALA N N 119.2 . 1 536 . 142 MET H H 7.11 . 1 537 . 142 MET CA C 53.9 . 1 538 . 142 MET HA H 4.29 . 1 539 . 142 MET N N 111 . 1 540 . 143 ASN H H 7.42 . 1 541 . 143 ASN CA C 49.4 . 1 542 . 143 ASN HA H 5.04 . 1 543 . 143 ASN N N 117 . 1 544 . 144 PRO CA C 62.1 . 1 545 . 144 PRO HA H 4.1 . 1 546 . 145 THR H H 7.49 . 1 547 . 145 THR CA C 59.3 . 1 548 . 145 THR HA H 4.56 . 1 549 . 145 THR N N 108.4 . 1 550 . 146 LEU H H 8.08 . 1 551 . 146 LEU HA H 4.76 . 1 552 . 146 LEU N N 123.4 . 1 553 . 147 GLU H H 8.35 . 1 554 . 147 GLU CA C 52.5 . 1 555 . 147 GLU HA H 4.82 . 1 556 . 147 GLU N N 117.9 . 1 557 . 148 ASP H H 10.04 . 1 558 . 148 ASP CA C 50.4 . 1 559 . 148 ASP HA H 4.88 . 1 560 . 148 ASP N N 125.6 . 1 561 . 149 THR H H 7.88 . 1 562 . 149 THR CA C 62.5 . 1 563 . 149 THR HA H 4.14 . 1 564 . 149 THR N N 116.6 . 1 565 . 150 GLY H H 8.02 . 1 566 . 150 GLY CA C 43 . 1 567 . 150 GLY HA2 H 4.21 . 2 568 . 150 GLY HA3 H 3.73 . 2 569 . 150 GLY N N 106.7 . 1 570 . 151 TYR H H 7.27 . 1 571 . 151 TYR CA C 56.8 . 1 572 . 151 TYR HA H 4.24 . 1 573 . 151 TYR N N 121.4 . 1 574 . 152 GLN H H 7.6 . 1 575 . 152 GLN CA C 52.3 . 1 576 . 152 GLN HA H 4.15 . 1 577 . 152 GLN N N 126 . 1 578 . 153 VAL H H 7.86 . 1 579 . 153 VAL HA H 3.84 . 1 580 . 153 VAL N N 120.6 . 1 581 . 154 GLU H H 8.26 . 1 582 . 154 GLU CA C 54.5 . 1 583 . 154 GLU HA H 4.34 . 1 584 . 154 GLU N N 125.2 . 1 585 . 155 VAL H H 7.73 . 1 586 . 155 VAL HA H 4.04 . 1 587 . 155 VAL N N 125.4 . 1 stop_ save_