data_4012 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the Acid State of E. coli Ribonuclease HI ; _BMRB_accession_number 4012 _BMRB_flat_file_name bmr4012.str _Entry_type update _Submission_date 1996-06-21 _Accession_date 1996-06-21 _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 Dabora Jonathan M. . 2 Pelton Jeffrey G. . 3 Marqusee Susan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 276 "13C chemical shifts" 138 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-16 reformat BMRB 'Edit deposition to format 2.1 version' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the Acid State of E. coli Ribonuclease H1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8810899 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dabora Jonathan M. . 2 Pelton Jeffrey G. . 3 Marqusee Susan . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 35 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11951 _Page_last 11958 _Year 1996 _Details . loop_ _Keyword 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_system_RNase_H1 _Saveframe_category molecular_system _Mol_system_name 'Ribonuclease H1' _Abbreviation_common 'RNase H1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RNase H1' $RNase_H1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RNase_H1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ribonuclease H1' _Name_variant 'C13A C63A C133A' _Abbreviation_common 'RNase H1' _Molecular_mass 17502 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; MLKQVEIFTDGSALGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHAEVILSTDSQYVRQGITQ WIHNWKKRGWKTADKKPVKN VDLWQRLDAALGQHQIKWEW VKGHAGHPENERADELARAA 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 ALA 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 ALA 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 ALA 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 2015-07-14 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 98.06 98.06 1.99e-108 PDB 1F21 "Divalent Metal Cofactor Binding In The Kinetic Folding Trajectory Of E. Coli Ribonuclease Hi" 100.00 155 100.00 100.00 1.35e-109 PDB 1G15 "Co-Crystal Of E. Coli Rnase Hi With Two Mn2+ Ions Bound In The The Active Site" 100.00 155 99.35 99.35 8.22e-109 PDB 1GOA "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.65 156 97.44 97.44 1.28e-106 PDB 1GOB "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" 100.00 155 97.42 97.42 7.89e-108 PDB 1JL1 "D10a E. Coli Ribonuclease Hi" 100.00 155 99.35 99.35 1.77e-108 PDB 1JXB "I53a, A Point Mutant Of The Cysteine-Free Variant Of E. Coli Rnase Hi" 100.00 155 99.35 99.35 9.90e-109 PDB 1KVA "E. Coli Ribonuclease Hi D134a Mutant" 100.00 155 97.42 97.42 2.30e-107 PDB 1KVB "E. Coli Ribonuclease Hi D134h Mutant" 100.00 155 97.42 97.42 2.43e-107 PDB 1KVC "E. Coli Ribonuclease Hi D134n Mutant" 100.00 155 97.42 98.06 8.52e-108 PDB 1LAV "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 97.42 98.06 5.15e-108 PDB 1LAW "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" 100.00 155 97.42 98.06 3.05e-108 PDB 1RBR "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 97.42 97.42 5.52e-107 PDB 1RBS "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 97.42 97.42 2.74e-107 PDB 1RBT "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 97.42 97.42 1.79e-107 PDB 1RBU "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 97.42 97.42 8.81e-108 PDB 1RBV "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" 100.00 155 97.42 97.42 9.10e-108 PDB 1RCH "Solution Nmr Structure Of Ribonuclease Hi From Escherichia Coli, 8 Structures" 100.00 155 98.06 98.06 1.99e-108 PDB 1RDA "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 97.42 98.06 8.52e-108 PDB 1RDB "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 97.42 98.06 4.93e-108 PDB 1RDC "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" 100.00 155 97.42 98.06 8.52e-108 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 98.06 98.06 1.99e-108 PDB 2RN2 "Structural Details Of Ribonuclease H From Escherichia Coli As Refined To An Atomic Resolution" 100.00 155 98.06 98.06 1.99e-108 PDB 3AA2 "A52i E. Coli Rnase Hi" 100.00 155 97.42 97.42 1.03e-107 PDB 3AA3 "A52l E. Coli Rnase Hi" 100.00 155 97.42 97.42 1.12e-107 PDB 3AA4 "A52v E.Coli Rnase Hi" 100.00 155 97.42 97.42 7.23e-108 PDB 3AA5 "A52f E.Coli Rnase Hi" 100.00 155 97.42 97.42 1.28e-107 PDB 4Z0U "Rnase Hi/ssb-ct Complex" 100.00 155 98.06 98.06 1.99e-108 DBJ BAA77885 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K12 substr. W3110]" 100.00 155 98.06 98.06 1.99e-108 DBJ BAB33633 "RNase HI [Escherichia coli O157:H7 str. Sakai]" 100.00 155 98.06 98.06 1.99e-108 DBJ BAG75734 "ribonuclease H [Escherichia coli SE11]" 100.00 155 98.06 98.06 1.99e-108 DBJ BAI23570 "ribonuclease HI [Escherichia coli O26:H11 str. 11368]" 100.00 155 98.06 98.06 1.99e-108 DBJ BAI29084 "ribonuclease HI [Escherichia coli O103:H2 str. 12009]" 100.00 155 97.42 98.06 7.56e-108 EMBL CAA23620 "ribonuclease H [Escherichia coli]" 100.00 155 98.06 98.06 1.99e-108 EMBL CAA27660 "unnamed protein product [Escherichia coli]" 100.00 155 98.06 98.06 1.99e-108 EMBL CAP74778 "ribonuclease HI [Escherichia coli LF82]" 100.00 155 97.42 97.42 1.75e-107 EMBL CAQ30729 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli BL21(DE3)]" 100.00 155 98.06 98.06 1.99e-108 EMBL CAQ87812 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia fergusonii ATCC 35469]" 100.00 155 98.06 98.06 1.99e-108 GB AAA24565 "ribonuclease H [Escherichia coli]" 100.00 155 98.06 98.06 1.99e-108 GB AAB08636 "ribonuclease H [Escherichia coli]" 100.00 155 98.06 98.06 1.99e-108 GB AAC73319 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 98.06 98.06 1.99e-108 GB AAG54510 "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli O157:H7 str. EDL933]" 100.00 155 98.06 98.06 1.99e-108 GB AAN41862 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 98.06 98.06 8.83e-109 REF NP_308237 "ribonuclease H [Escherichia coli O157:H7 str. Sakai]" 100.00 155 98.06 98.06 1.99e-108 REF NP_414750 "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 98.06 98.06 1.99e-108 REF NP_706155 "RNase HI [Shigella flexneri 2a str. 301]" 100.00 192 98.06 98.06 8.83e-109 REF WP_000917867 "ribonuclease H [Escherichia coli]" 100.00 155 97.42 97.42 1.75e-107 REF WP_000917875 "hypothetical protein [Escherichia albertii]" 100.00 155 97.42 98.06 4.38e-108 SP A7ZHV1 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 98.06 98.06 1.99e-108 SP A7ZWF6 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 97.42 98.06 7.56e-108 SP B1IPU4 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 98.06 98.06 1.99e-108 SP B1LHM3 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 98.06 98.06 1.99e-108 SP B1XD78 "RecName: Full=Ribonuclease H; Short=RNase H" 100.00 155 98.06 98.06 1.99e-108 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RNase_H1 'E. coli' 562 Eubacteria . 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 _Variant _Vector_type _Vector_name _Details $RNase_H1 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pSM101 synthetic stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $RNase_H1 . mM 1 3 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_one loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $RNase_H1 99 % 'mass spectrometry' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 n/a temperature 298 1.0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details '1H referenced to H2O - 4.77 PPM 25C' 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 H2O H 1 . ppm 4.77 internal direct cylindrical 'in the sample' parallel TSP C 13 . ppm 0.0 external indirect cylindrical 'external to sample' parallel NH3 N 15 . ppm 0.0 external indirect cylindrical 'external to sample' parallel 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'RNase H1' _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 . 7 ILE H H 8.4 . 1 2 . 7 ILE N N 121.6 . 1 3 . 7 ILE HA H 5.3 . 1 4 . 7 ILE CA C 59.3 . 1 5 . 8 PHE H H 9.11 . 1 6 . 8 PHE N N 127.2 . 1 7 . 8 PHE HA H 5.77 . 1 8 . 8 PHE CA C 55.5 . 1 9 . 9 THR H H 8.24 . 1 10 . 9 THR N N 110.1 . 1 11 . 9 THR HA H 5.61 . 1 12 . 9 THR CA C 60.4 . 1 13 . 11 GLY H H 8.71 . 1 14 . 11 GLY N N 106.7 . 1 15 . 11 GLY CA C 44.7 . 1 16 . 12 SER H H 8.7 . 1 17 . 12 SER N N 112.6 . 1 18 . 12 SER HA H 3.7 . 1 19 . 12 SER CA C 57.7 . 1 20 . 13 ALA H H 8.36 . 1 21 . 13 ALA N N 121.9 . 1 22 . 13 ALA HA H 5.15 . 1 23 . 13 ALA CA C 51.4 . 1 24 . 14 LEU H H 9.09 . 1 25 . 14 LEU N N 120.4 . 1 26 . 14 LEU HA H 4.4 . 1 27 . 14 LEU CA C 54.2 . 1 28 . 15 GLY H H 7.29 . 1 29 . 15 GLY N N 104.8 . 1 30 . 15 GLY HA2 H 4.00 . 1 31 . 15 GLY HA3 H 3.8 . 1 32 . 15 GLY CA C 43.9 . 1 33 . 16 ASN H H 8.46 . 1 34 . 16 ASN N N 116.2 . 1 35 . 16 ASN HA H 5.18 . 1 36 . 16 ASN CA C 50.3 . 1 37 . 18 GLY H H 8.62 . 1 38 . 18 GLY N N 105.5 . 1 39 . 18 GLY HA2 H 4.3 . 1 40 . 18 GLY HA3 H 3.77 . 1 41 . 18 GLY CA C 44.9 . 1 42 . 20 GLY H H 8.94 . 1 43 . 20 GLY N N 107.2 . 1 44 . 20 GLY HA2 H 4.98 . 1 45 . 20 GLY HA3 H 3.72 . 1 46 . 20 GLY CA C 45.00 . 1 47 . 21 GLY H H 9.17 . 1 48 . 21 GLY N N 106.4 . 1 49 . 21 GLY HA2 H 5.36 . 1 50 . 21 GLY HA3 H 4.22 . 1 51 . 21 GLY CA C 46.4 . 1 52 . 22 TYR H H 7.86 . 1 53 . 22 TYR N N 113.3 . 1 54 . 22 TYR HA H 5.72 . 1 55 . 22 TYR CA C 54.9 . 1 56 . 23 GLY H H 9.11 . 1 57 . 23 GLY N N 106.3 . 1 58 . 23 GLY HA2 H 5.1 . 1 59 . 23 GLY HA3 H 4.05 . 1 60 . 23 GLY CA C 44.9 . 1 61 . 24 ALA H H 9.4 . 1 62 . 24 ALA N N 124.5 . 1 63 . 24 ALA HA H 5.67 . 1 64 . 24 ALA CA C 50.7 . 1 65 . 25 ILE H H 9.1 . 1 66 . 25 ILE N N 121.3 . 1 67 . 25 ILE HA H 4.72 . 1 68 . 25 ILE CA C 60.1 . 1 69 . 26 LEU H H 9.25 . 1 70 . 26 LEU N N 129.5 . 1 71 . 26 LEU HA H 5.38 . 1 72 . 26 LEU CA C 54.4 . 1 73 . 27 ARG H H 9.99 . 1 74 . 27 ARG N N 126.8 . 1 75 . 27 ARG HA H 5.45 . 1 76 . 27 ARG CA C 54.8 . 1 77 . 28 TYR H H 8.52 . 1 78 . 28 TYR N N 123.6 . 1 79 . 28 TYR HA H 4.93 . 1 80 . 28 TYR CA C 56.8 . 1 81 . 29 ARG H H 9.43 . 1 82 . 29 ARG N N 125.9 . 1 83 . 29 ARG HA H 3.72 . 1 84 . 29 ARG CA C 56.9 . 1 85 . 30 GLY H H 8.82 . 1 86 . 30 GLY N N 104.5 . 1 87 . 30 GLY HA2 H 4.09 . 1 88 . 30 GLY HA3 H 3.56 . 1 89 . 30 GLY CA C 45.3 . 1 90 . 31 ARG H H 7.86 . 5 91 . 31 ARG N N 120.6 . 5 92 . 31 ARG HA H 4.66 . 1 93 . 31 ARG CA C 54.5 . 1 94 . 32 GLU H H 8.72 . 1 95 . 32 GLU N N 122.3 . 1 96 . 32 GLU HA H 5.45 . 1 97 . 32 GLU CA C 54.6 . 1 98 . 33 LYS H H 9.28 . 1 99 . 33 LYS N N 124.8 . 1 100 . 33 LYS HA H 4.61 . 1 101 . 33 LYS CA C 54.8 . 1 102 . 34 THR H H 8.07 . 1 103 . 34 THR N N 112.5 . 1 104 . 34 THR HA H 5.35 . 1 105 . 34 THR CA C 59.5 . 1 106 . 35 PHE H H 9.17 . 1 107 . 35 PHE N N 119.3 . 1 108 . 35 PHE HA H 4.98 . 1 109 . 35 PHE CA C 56.3 . 1 110 . 36 SER H H 8.38 . 1 111 . 36 SER N N 113.8 . 1 112 . 36 SER HA H 4.56 . 1 113 . 36 SER CA C 57.9 . 1 114 . 37 ALA H H 6.36 . 1 115 . 37 ALA N N 120.3 . 1 116 . 37 ALA HA H 4.19 . 1 117 . 37 ALA CA C 52.00 . 1 118 . 38 GLY H H 8.59 . 1 119 . 38 GLY N N 106.1 . 1 120 . 38 GLY HA2 H 5.35 . 1 121 . 38 GLY HA3 H 3.48 . 1 122 . 38 GLY CA C 44.1 . 1 123 . 39 TYR H H 9.69 . 1 124 . 39 TYR N N 122.8 . 1 125 . 39 TYR HA H 5.45 . 1 126 . 39 TYR CA C 55.7 . 1 127 . 40 THR H H 8.77 . 1 128 . 40 THR N N 112.7 . 1 129 . 40 THR HA H 3.7 . 1 130 . 40 THR CA C 65.2 . 1 131 . 41 ARG H H 7.77 . 1 132 . 41 ARG N N 120.00 . 1 133 . 41 ARG HA H 3.87 . 1 134 . 41 ARG CA C 56.7 . 1 135 . 42 THR H H 9.12 . 1 136 . 42 THR N N 124.1 . 1 137 . 42 THR HA H 4.09 . 1 138 . 42 THR CA C 60.00 . 1 139 . 44 ASN H H 9.4 . 1 140 . 44 ASN N N 121.2 . 1 141 . 44 ASN HA H 3.8 . 1 142 . 44 ASN CA C 57.5 . 1 143 . 45 ASN H H 8.53 . 1 144 . 45 ASN N N 115.8 . 1 145 . 45 ASN CA C 55.6 . 1 146 . 46 ARG H H 7.36 . 1 147 . 46 ARG N N 116.3 . 1 148 . 46 ARG CA C 60.7 . 1 149 . 47 MET H H 7.64 . 1 150 . 47 MET N N 117.7 . 1 151 . 47 MET HA H 4.4 . 1 152 . 47 MET CA C 57.2 . 1 153 . 48 GLU H H 8.45 . 1 154 . 48 GLU N N 119.8 . 1 155 . 48 GLU HA H 3.78 . 1 156 . 48 GLU CA C 59.7 . 1 157 . 49 LEU H H 7.21 . 5 158 . 49 LEU N N 116.2 . 5 159 . 49 LEU HA H 3.93 . 1 160 . 49 LEU CA C 57.1 . 1 161 . 50 MET H H 8.66 . 5 162 . 50 MET N N 118.6 . 5 163 . 50 MET CA C 57.3 . 1 164 . 51 ALA H H 7.78 . 1 165 . 51 ALA N N 116.9 . 1 166 . 51 ALA HA H 3.35 . 1 167 . 51 ALA CA C 55.2 . 1 168 . 52 ALA H H 6.46 . 1 169 . 52 ALA N N 113.7 . 1 170 . 52 ALA HA H 3.98 . 1 171 . 52 ALA CA C 54.7 . 1 172 . 53 ILE H H 7.86 . 5 173 . 53 ILE N N 116.1 . 5 174 . 53 ILE HA H 3.1 . 1 175 . 53 ILE CA C 66.00 . 1 176 . 54 VAL H H 8.25 . 1 177 . 54 VAL N N 116.5 . 1 178 . 54 VAL HA H 3.2 . 1 179 . 54 VAL CA C 65.9 . 1 180 . 55 ALA H H 6.86 . 1 181 . 55 ALA N N 119.00 . 1 182 . 55 ALA HA H 3.3 . 1 183 . 55 ALA CA C 54.4 . 1 184 . 56 LEU H H 7.45 . 1 185 . 56 LEU N N 112.5 . 1 186 . 56 LEU HA H 3.7 . 1 187 . 56 LEU CA C 57.00 . 1 188 . 57 GLU H H 8.71 . 1 189 . 57 GLU N N 118.1 . 1 190 . 57 GLU HA H 3.87 . 1 191 . 57 GLU CA C 58.2 . 1 192 . 58 ALA H H 7.07 . 1 193 . 58 ALA N N 119.3 . 1 194 . 58 ALA HA H 4.03 . 1 195 . 58 ALA CA C 52.8 . 1 196 . 59 LEU H H 7.06 . 1 197 . 59 LEU N N 118.5 . 1 198 . 59 LEU HA H 4.19 . 1 199 . 59 LEU CA C 54.3 . 1 200 . 60 LYS H H 8.55 . 1 201 . 60 LYS N N 121.8 . 1 202 . 60 LYS HA H 4.25 . 1 203 . 60 LYS CA C 55.9 . 1 204 . 61 GLU H H 7.57 . 1 205 . 61 GLU N N 116.7 . 1 206 . 61 GLU HA H 4.4 . 1 207 . 61 GLU CA C 54.2 . 1 208 . 62 HIS H H 8.24 . 1 209 . 62 HIS N N 118.3 . 1 210 . 62 HIS HA H 4.55 . 1 211 . 62 HIS CA C 56.4 . 1 212 . 64 GLU H H 8.27 . 1 213 . 64 GLU N N 121.1 . 1 214 . 64 GLU HA H 4.87 . 1 215 . 64 GLU CA C 55.4 . 1 216 . 65 VAL H H 8.62 . 1 217 . 65 VAL N N 123.9 . 1 218 . 65 VAL HA H 4.72 . 1 219 . 65 VAL CA C 59.7 . 1 220 . 66 ILE H H 8.46 . 1 221 . 66 ILE N N 127.2 . 1 222 . 66 ILE HA H 4.72 . 1 223 . 66 ILE CA C 59.8 . 1 224 . 67 LEU H H 8.54 . 1 225 . 67 LEU N N 134.00 . 1 226 . 67 LEU HA H 4.56 . 1 227 . 67 LEU CA C 54.7 . 1 228 . 68 SER H H 8.75 . 1 229 . 68 SER N N 120.6 . 1 230 . 68 SER HA H 5.72 . 1 231 . 68 SER CA C 55.7 . 1 232 . 69 THR H H 8.68 . 1 233 . 69 THR N N 119.2 . 1 234 . 69 THR CA C 60.3 . 1 235 . 70 ASP H H 8.8 . 1 236 . 70 ASP N N 127.2 . 1 237 . 70 ASP CA C 52.7 . 1 238 . 71 SER H H 8.29 . 5 239 . 71 SER N N 115.3 . 5 240 . 71 SER CA C 58.7 . 1 241 . 72 GLN H H 9.37 . 1 242 . 72 GLN N N 132.7 . 1 243 . 72 GLN HA H 3.98 . 1 244 . 72 GLN CA C 57.9 . 1 245 . 73 TYR H H 8.69 . 1 246 . 73 TYR N N 123.4 . 1 247 . 73 TYR CA C 61.1 . 1 248 . 74 VAL H H 8.09 . 1 249 . 74 VAL N N 117.1 . 1 250 . 74 VAL HA H 3.75 . 1 251 . 74 VAL CA C 66.5 . 1 252 . 75 ARG H H 6.97 . 1 253 . 75 ARG N N 117.5 . 1 254 . 75 ARG HA H 2.35 . 1 255 . 75 ARG CA C 58.9 . 1 256 . 76 GLN H H 8.17 . 5 257 . 76 GLN N N 120.2 . 5 258 . 76 GLN HA H 3.1 . 1 259 . 76 GLN CA C 58.8 . 1 260 . 77 GLY H H 7.78 . 5 261 . 77 GLY N N 106.9 . 5 262 . 77 GLY HA2 H 3.77 . 1 263 . 77 GLY HA3 H 3.1 . 1 264 . 77 GLY CA C 47.9 . 1 265 . 78 ILE H H 8.35 . 1 266 . 78 ILE N N 119.7 . 1 267 . 78 ILE HA H 3.66 . 1 268 . 78 ILE CA C 60.9 . 1 269 . 79 THR H H 7.78 . 5 270 . 79 THR N N 106.9 . 5 271 . 79 THR HA H 4.09 . 1 272 . 79 THR CA C 63.8 . 1 273 . 80 GLN H H 7.51 . 5 274 . 80 GLN N N 117.1 . 5 275 . 80 GLN HA H 4.45 . 1 276 . 80 GLN CA C 56.8 . 1 277 . 81 TRP H H 7.1 . 1 278 . 81 TRP N N 118.00 . 1 279 . 81 TRP HA H 4.19 . 1 280 . 81 TRP CA C 57.5 . 1 281 . 82 ILE H H 8.46 . 1 282 . 82 ILE N N 117.7 . 1 283 . 82 ILE HA H 3.45 . 1 284 . 82 ILE CA C 66.1 . 1 285 . 83 HIS H H 7.94 . 1 286 . 83 HIS N N 118.1 . 1 287 . 83 HIS HA H 4.09 . 1 288 . 83 HIS CA C 58.8 . 1 289 . 84 ASN H H 7.41 . 1 290 . 84 ASN N N 117.5 . 1 291 . 84 ASN HA H 4.35 . 1 292 . 84 ASN CA C 55.2 . 1 293 . 85 TRP H H 8.17 . 5 294 . 85 TRP N N 120.2 . 5 295 . 85 TRP HA H 4.35 . 1 296 . 85 TRP CA C 57.5 . 1 297 . 86 LYS H H 8.09 . 1 298 . 86 LYS N N 118.9 . 1 299 . 86 LYS CA C 59.9 . 1 300 . 87 LYS H H 7.32 . 1 301 . 87 LYS N N 118.7 . 1 302 . 87 LYS HA H 4.03 . 1 303 . 87 LYS CA C 58.2 . 1 304 . 88 ARG H H 7.21 . 5 305 . 88 ARG N N 116.2 . 5 306 . 88 ARG HA H 4.45 . 1 307 . 88 ARG CA C 54.9 . 1 308 . 89 GLY H H 7.75 . 1 309 . 89 GLY N N 108.5 . 1 310 . 89 GLY HA2 H 3.9 . 1 311 . 89 GLY HA3 H 3.9 . 1 312 . 89 GLY CA C 47.2 . 1 313 . 90 TRP H H 8.51 . 1 314 . 90 TRP N N 112.6 . 1 315 . 90 TRP HA H 3.4 . 1 316 . 90 TRP CA C 58.1 . 1 317 . 91 LYS H H 6.78 . 1 318 . 91 LYS N N 116.4 . 1 319 . 91 LYS HA H 4.98 . 1 320 . 91 LYS CA C 53.8 . 1 321 . 92 THR H H 8.87 . 1 322 . 92 THR N N 109.4 . 1 323 . 92 THR HA H 4.35 . 1 324 . 92 THR CA C 60.7 . 1 325 . 93 ALA H H 9.08 . 1 326 . 93 ALA N N 123.5 . 1 327 . 93 ALA HA H 4.03 . 1 328 . 93 ALA CA C 54.8 . 1 329 . 94 ASP H H 7.97 . 1 330 . 94 ASP N N 113.8 . 1 331 . 94 ASP HA H 4.61 . 1 332 . 94 ASP CA C 52.9 . 1 333 . 95 LYS H H 8.03 . 1 334 . 95 LYS N N 122.2 . 1 335 . 95 LYS HA H 3.61 . 1 336 . 95 LYS CA C 57.7 . 1 337 . 96 LYS H H 7.59 . 1 338 . 96 LYS N N 119.7 . 1 339 . 96 LYS HA H 4.66 . 1 340 . 96 LYS CA C 53.4 . 1 341 . 98 VAL H H 7.57 . 1 342 . 98 VAL N N 120.5 . 1 343 . 98 VAL HA H 3.35 . 1 344 . 98 VAL CA C 61.6 . 1 345 . 99 LYS H H 8.27 . 1 346 . 99 LYS N N 127.7 . 1 347 . 99 LYS HA H 4.03 . 1 348 . 99 LYS CA C 57.2 . 1 349 . 100 ASN H H 9.44 . 1 350 . 100 ASN N N 115.8 . 1 351 . 100 ASN HA H 4.25 . 1 352 . 100 ASN CA C 54.8 . 1 353 . 101 VAL H H 7.61 . 1 354 . 101 VAL N N 118.8 . 1 355 . 101 VAL HA H 3.56 . 1 356 . 101 VAL CA C 65.4 . 1 357 . 102 ASP H H 8.56 . 1 358 . 102 ASP N N 119.3 . 1 359 . 102 ASP HA H 4.03 . 1 360 . 102 ASP CA C 56.00 . 1 361 . 103 LEU H H 7.24 . 1 362 . 103 LEU N N 118.3 . 1 363 . 103 LEU HA H 4.14 . 1 364 . 103 LEU CA C 55.8 . 1 365 . 104 TRP H H 8.49 . 1 366 . 104 TRP N N 120.8 . 1 367 . 104 TRP HA H 4.51 . 1 368 . 104 TRP CA C 61.3 . 1 369 . 105 GLN H H 8.39 . 1 370 . 105 GLN N N 115.6 . 1 371 . 105 GLN HA H 3.61 . 1 372 . 105 GLN CA C 59.2 . 1 373 . 106 ARG H H 7.00 . 1 374 . 106 ARG N N 120.8 . 1 375 . 106 ARG HA H 4.14 . 1 376 . 106 ARG CA C 59.2 . 1 377 . 107 LEU H H 8.71 . 1 378 . 107 LEU N N 121.4 . 1 379 . 107 LEU HA H 4.09 . 1 380 . 107 LEU CA C 58.2 . 1 381 . 108 ASP H H 8.74 . 1 382 . 108 ASP N N 118.2 . 1 383 . 108 ASP HA H 4.51 . 1 384 . 108 ASP CA C 58.2 . 1 385 . 109 ALA H H 7.87 . 1 386 . 109 ALA N N 118.9 . 1 387 . 109 ALA HA H 4.14 . 1 388 . 109 ALA CA C 54.8 . 1 389 . 110 ALA H H 7.65 . 1 390 . 110 ALA N N 120.9 . 1 391 . 110 ALA HA H 4.3 . 1 392 . 110 ALA CA C 54.6 . 1 393 . 111 LEU H H 8.65 . 5 394 . 111 LEU N N 117.3 . 5 395 . 111 LEU HA H 4.09 . 1 396 . 111 LEU CA C 57.5 . 1 397 . 112 GLY H H 7.52 . 1 398 . 112 GLY N N 101.5 . 1 399 . 112 GLY HA2 H 4.09 . 1 400 . 112 GLY HA3 H 3.91 . 1 401 . 112 GLY CA C 46.2 . 1 402 . 113 GLN H H 7.51 . 5 403 . 113 GLN N N 117.1 . 5 404 . 113 GLN CA C 55.3 . 1 405 . 114 HIS H H 7.43 . 5 406 . 114 HIS N N 116.7 . 5 407 . 114 HIS HA H 5.03 . 5 408 . 114 HIS CA C 55.5 . 1 409 . 115 GLN H H 8.6 . 1 410 . 115 GLN N N 121.4 . 1 411 . 115 GLN HA H 4.66 . 1 412 . 115 GLN CA C 54.7 . 1 413 . 116 ILE H H 8.52 . 1 414 . 116 ILE N N 125.9 . 1 415 . 116 ILE HA H 4.45 . 1 416 . 116 ILE CA C 59.9 . 1 417 . 117 LYS H H 8.68 . 1 418 . 117 LYS N N 129.5 . 1 419 . 117 LYS HA H 4.45 . 1 420 . 117 LYS CA C 54.6 . 1 421 . 118 TRP H H 8.26 . 1 422 . 118 TRP N N 25.8 . 1 423 . 118 TRP HA H 4.45 . 1 424 . 118 TRP CA C 55.8 . 1 425 . 119 GLU H H 8.91 . 1 426 . 119 GLU N N 126.7 . 1 427 . 119 GLU HA H 4.3 . 1 428 . 119 GLU CA C 54.3 . 1 429 . 120 TRP H H 8.00 . 1 430 . 120 TRP N N 126.1 . 1 431 . 120 TRP HA H 5.7 . 1 432 . 120 TRP CA C 53.4 . 1 433 . 121 VAL H H 7.99 . 5 434 . 121 VAL N N 122.7 . 5 435 . 121 VAL HA H 4.3 . 1 436 . 121 VAL CA C 61.1 . 1 437 . 122 LYS H H 8.41 . 1 438 . 122 LYS N N 123.8 . 1 439 . 122 LYS HA H 4.48 . 1 440 . 122 LYS CA C 55.5 . 1 441 . 123 GLY H H 8.53 . 1 442 . 123 GLY N N 111.3 . 1 443 . 123 GLY HA2 H 3.9 . 1 444 . 123 GLY HA3 H 3.9 . 1 445 . 123 GLY CA C 45.7 . 1 446 . 124 HIS H H 8.65 . 5 447 . 124 HIS N N 116.6 . 5 448 . 124 HIS CA C 55.9 . 1 449 . 125 ALA H H 8.07 . 5 450 . 125 ALA N N 123.2 . 5 451 . 125 ALA HA H 4.45 . 1 452 . 125 ALA CA C 52.2 . 1 453 . 126 GLY H H 8.53 . 1 454 . 126 GLY N N 109.6 . 1 455 . 126 GLY HA2 H 3.82 . 1 456 . 126 GLY HA3 H 3.7 . 1 457 . 126 GLY CA C 45.00 . 1 458 . 127 HIS H H 8.66 . 5 459 . 127 HIS N N 118.8 . 5 460 . 127 HIS CA C 53.1 . 1 461 . 129 GLU H H 9.38 . 1 462 . 129 GLU N N 117.00 . 1 463 . 129 GLU HA H 3.6 . 1 464 . 129 GLU CA C 60.3 . 1 465 . 130 ASN H H 7.49 . 1 466 . 130 ASN N N 115.7 . 1 467 . 130 ASN HA H 4.4 . 1 468 . 130 ASN CA C 58.2 . 1 469 . 134 ASP H H 7.69 . 1 470 . 134 ASP N N 117.7 . 1 471 . 134 ASP CA C 56.8 . 1 472 . 135 GLU H H 8.05 . 1 473 . 135 GLU N N 118.9 . 1 474 . 135 GLU HA H 3.82 . 1 475 . 135 GLU CA C 59.5 . 1 476 . 136 LEU H H 8.23 . 1 477 . 136 LEU N N 119.8 . 1 478 . 136 LEU HA H 3.98 . 1 479 . 136 LEU CA C 57.6 . 1 480 . 137 ALA H H 7.99 . 5 481 . 137 ALA N N 122.7 . 5 482 . 137 ALA HA H 3.61 . 1 483 . 137 ALA CA C 55.5 . 1 484 . 138 ARG H H 8.25 . 5 485 . 138 ARG N N 115.9 . 5 486 . 138 ARG HA H 3.72 . 1 487 . 138 ARG CA C 59.2 . 1 488 . 139 ALA H H 7.94 . 1 489 . 139 ALA N N 120.3 . 1 490 . 139 ALA HA H 4.03 . 1 491 . 139 ALA CA C 54.5 . 1 492 . 140 ALA H H 7.83 . 1 493 . 140 ALA N N 121.7 . 1 494 . 140 ALA HA H 3.93 . 1 495 . 140 ALA CA C 54.6 . 1 496 . 141 ALA H H 7.67 . 1 497 . 141 ALA N N 118.6 . 1 498 . 141 ALA HA H 3.72 . 1 499 . 141 ALA CA C 54.3 . 1 500 . 142 MET H H 7.00 . 1 501 . 142 MET N N 110.3 . 1 502 . 142 MET HA H 4.29 . 1 503 . 142 MET CA C 55.4 . 1 504 . 143 ASN H H 7.43 . 5 505 . 143 ASN N N 116.7 . 5 506 . 143 ASN HA H 5.01 . 5 507 . 143 ASN CA C 51.2 . 1 508 . 145 THR H H 7.5 . 1 509 . 145 THR N N 108.6 . 1 510 . 145 THR HA H 4.51 . 1 511 . 145 THR CA C 61.2 . 1 512 . 146 LEU H H 8.07 . 5 513 . 146 LEU N N 123.2 . 5 514 . 146 LEU HA H 4.72 . 1 515 . 146 LEU CA C 53.8 . 1 516 . 147 GLU H H 8.33 . 1 517 . 147 GLU N N 117.7 . 1 518 . 147 GLU HA H 4.8 . 1 519 . 147 GLU CA C 54.3 . 1 520 . 148 ASP H H 10.00 . 1 521 . 148 ASP N N 125.5 . 1 522 . 148 ASP HA H 4.82 . 1 523 . 148 ASP CA C 51.9 . 1 524 . 149 THR H H 7.83 . 5 525 . 149 THR N N 116.2 . 5 526 . 149 THR HA H 4.09 . 1 527 . 149 THR CA C 64.2 . 1 528 . 150 GLY H H 8.00 . 1 529 . 150 GLY N N 106.5 . 1 530 . 150 GLY HA2 H 4.14 . 1 531 . 150 GLY HA3 H 3.72 . 1 532 . 150 GLY CA C 44.7 . 1 533 . 151 TYR H H 7.21 . 1 534 . 151 TYR N N 121.1 . 1 535 . 151 TYR HA H 4.19 . 1 536 . 151 TYR CA C 58.7 . 1 537 . 152 GLN H H 7.55 . 1 538 . 152 GLN N N 126.00 . 1 539 . 152 GLN HA H 4.14 . 1 540 . 152 GLN CA C 54.1 . 1 541 . 153 VAL H H 7.86 . 5 542 . 153 VAL N N 120.6 . 5 543 . 153 VAL HA H 3.82 . 1 544 . 153 VAL CA C 62.4 . 1 545 . 154 GLU H H 8.24 . 1 546 . 154 GLU N N 125.00 . 1 547 . 154 GLU HA H 4.3 . 1 548 . 154 GLU CA C 56.2 . 1 549 . 155 VAL H H 7.71 . 1 550 . 155 VAL N N 125.2 . 1 551 . 155 VAL HA H 4.03 . 1 552 . 155 VAL CA C 63.4 . 1 stop_ save_