data_4207 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; CRO Repressor Insertion Mutant K56-[DGEVK] ; _BMRB_accession_number 4207 _BMRB_flat_file_name bmr4207.str _Entry_type original _Submission_date 1998-10-11 _Accession_date 1998-10-11 _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 Mossing M. C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 358 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-10 original author 'Original release.' 2002-07-12 update BMRB 'Modify the saveframe name.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Mossing, M.C., "Solution Structure and Dynamics of a Designed Monomeric Variant of the Lambda CRO Repressor," Protein Sci. 7, 983-993 (1998). ; _Citation_title ; Solution Structure and Dynamics of a Designed Monomeric Variant of the Lambda CRO Repressor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98227860 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mossing M. C. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 983 _Page_last 993 _Year 1998 _Details . loop_ _Keyword 'gene regulating protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_CRO-K56-DGEVK _Saveframe_category molecular_system _Mol_system_name 'CRO Repressor Insertion Mutant K56-[DGEVK]' _Abbreviation_common CRO-K56-[DGEVK] _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CRO-K56-[DGEVK] $CRO-K56-DGEVK 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_CRO-K56-DGEVK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CRO Repressor Insertion Mutant K56-[DGEVK]' _Name_variant INS(K56-DGEVK) _Abbreviation_common CRO-K56-[DGEVK] _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; MEQRITLKDYAMRFGQTKTA KDLGVYQSAINKAIHAGRKI FLTINADGSVYAEEVKDGEV KPFPSNKKTTA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLN 4 ARG 5 ILE 6 THR 7 LEU 8 LYS 9 ASP 10 TYR 11 ALA 12 MET 13 ARG 14 PHE 15 GLY 16 GLN 17 THR 18 LYS 19 THR 20 ALA 21 LYS 22 ASP 23 LEU 24 GLY 25 VAL 26 TYR 27 GLN 28 SER 29 ALA 30 ILE 31 ASN 32 LYS 33 ALA 34 ILE 35 HIS 36 ALA 37 GLY 38 ARG 39 LYS 40 ILE 41 PHE 42 LEU 43 THR 44 ILE 45 ASN 46 ALA 47 ASP 48 GLY 49 SER 50 VAL 51 TYR 52 ALA 53 GLU 54 GLU 55 VAL 56 LYS 57 ASP 58 GLY 59 GLU 60 VAL 61 LYS 62 PRO 63 PHE 64 PRO 65 SER 66 ASN 67 LYS 68 LYS 69 THR 70 THR 71 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 1D1M "Crystal Structure Of Cro K56-[dgevk]-F58w Mutant" 91.55 65 98.46 100.00 5.71e-39 PDB 1ORC "Cro Repressor Insertion Mutant K56-[dgevk]" 100.00 71 100.00 100.00 9.60e-44 PDB 2ORC "Cro Repressor Insertion Mutant K56-[dgevk], Nmr, 32 Structures" 100.00 71 100.00 100.00 9.60e-44 PDB 3ORC "Crystal Structure Of An Engineered Cro Monomer Bound Nonspecifically To Dna" 91.55 65 100.00 100.00 2.03e-39 GB EEW86110 "conserved hypothetical protein, partial [Brucella melitensis bv. 1 str. 16M]" 71.83 51 100.00 100.00 4.62e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CRO-K56-DGEVK 'bacteriophage lambda' 10710 . . 'Lambda phage group' 'bacteriophage lambda' 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_name $CRO-K56-DGEVK 'recombinant technology' E.coli Escherichia coli . X90 . 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 _Isotopic_labeling $CRO-K56-DGEVK . mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-plus _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-plus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_one save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_HSQC-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-NOESY _Sample_label $sample_one save_ save_HSQC-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-TOCSY _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . M pH 4.6 . n/a pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 . H 1 'methyl protons' ppm . . . . . . . N 15 'methyl protons' ppm . . . . . . 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 CRO-K56-[DGEVK] _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 HA H 4.18 . 1 2 . 1 MET HB2 H 2.25 . 2 3 . 2 GLU N N 124.2 . 1 4 . 2 GLU H H 8.97 . 1 5 . 2 GLU HA H 4.54 . 1 6 . 2 GLU HB2 H 2.04 . 2 7 . 2 GLU HB3 H 2.16 . 2 8 . 2 GLU HG2 H 2.37 . 2 9 . 3 GLN N N 122 . 1 10 . 3 GLN H H 8.6 . 1 11 . 3 GLN HA H 4.54 . 1 12 . 3 GLN HB2 H 2.19 . 2 13 . 3 GLN HB3 H 2.06 . 2 14 . 3 GLN HG2 H 2.44 . 2 15 . 3 GLN HG3 H 2.40 . 2 16 . 3 GLN NE2 N 112 . 1 17 . 3 GLN HE21 H 7.59 . 2 18 . 3 GLN HE22 H 6.93 . 2 19 . 4 ARG N N 122.9 . 1 20 . 4 ARG H H 8.38 . 1 21 . 4 ARG HA H 5.07 . 1 22 . 4 ARG HB2 H 1.82 . 2 23 . 4 ARG HB3 H 1.71 . 2 24 . 4 ARG HG2 H 1.59 . 2 25 . 4 ARG HD2 H 2.99 . 2 26 . 4 ARG NE N 84.6 . 1 27 . 4 ARG HE H 6.96 . 1 28 . 5 ILE N N 124.3 . 1 29 . 5 ILE H H 9.27 . 1 30 . 5 ILE HA H 4.83 . 1 31 . 5 ILE HB H 2.08 . 1 32 . 5 ILE HG12 H 1.47 . 2 33 . 5 ILE HG13 H 1.91 . 2 34 . 5 ILE HG2 H 1.34 . 1 35 . 5 ILE HD1 H 1.1 . 1 36 . 6 THR N N 117.9 . 1 37 . 6 THR H H 9.3 . 1 38 . 6 THR HA H 4.43 . 1 39 . 6 THR HB H 4.63 . 1 40 . 6 THR HG2 H 1.48 . 1 41 . 7 LEU N N 121.5 . 1 42 . 7 LEU H H 7.76 . 1 43 . 7 LEU HA H 3.99 . 1 44 . 7 LEU HB2 H 1.75 . 2 45 . 7 LEU HG H 1.48 . 1 46 . 7 LEU HD1 H 0.085 . 1 47 . 7 LEU HD2 H 0.069 . 1 48 . 8 LYS N N 116.7 . 1 49 . 8 LYS H H 8.6 . 1 50 . 8 LYS HA H 3.86 . 1 51 . 8 LYS HB2 H 1.75 . 2 52 . 8 LYS HG2 H 1.48 . 1 53 . 8 LYS HG3 H 1.43 . 1 54 . 8 LYS HD2 H 1.8 . 2 55 . 8 LYS HE2 H 3.04 . 2 56 . 9 ASP N N 119.7 . 1 57 . 9 ASP H H 8 . 1 58 . 9 ASP HA H 4.48 . 1 59 . 9 ASP HB2 H 2.98 . 1 60 . 9 ASP HB3 H 2.68 . 1 61 . 10 TYR N N 124.3 . 1 62 . 10 TYR H H 8.95 . 1 63 . 10 TYR HA H 4 . 1 64 . 10 TYR HB2 H 3.26 . 1 65 . 10 TYR HB3 H 2.98 . 1 66 . 10 TYR HD1 H 7.31 . 3 67 . 10 TYR HE1 H 6.6 . 3 68 . 11 ALA N N 119.7 . 1 69 . 11 ALA H H 8.94 . 1 70 . 11 ALA HA H 4.2 . 1 71 . 11 ALA HB H 1.42 . 1 72 . 12 MET N N 119 . 1 73 . 12 MET H H 8.15 . 1 74 . 12 MET HA H 4.24 . 1 75 . 12 MET HB2 H 2.28 . 2 76 . 12 MET HB3 H 2.21 . 2 77 . 12 MET HG2 H 2.80 . 2 78 . 12 MET HG3 H 2.67 . 2 79 . 13 ARG N N 118.8 . 1 80 . 13 ARG H H 7.69 . 1 81 . 13 ARG HA H 3.89 . 1 82 . 13 ARG HB2 H 1.48 . 1 83 . 13 ARG HB3 H 1.14 . 1 84 . 13 ARG HG2 H 0.55 . 2 85 . 13 ARG HD2 H 2.74 . 2 86 . 13 ARG HD3 H 2.69 . 2 87 . 13 ARG NE N 84.9 . 1 88 . 13 ARG HE H 6.97 . 1 89 . 14 PHE N N 113.8 . 1 90 . 14 PHE H H 8.44 . 1 91 . 14 PHE HA H 4.73 . 1 92 . 14 PHE HB2 H 3.03 . 2 93 . 14 PHE HB3 H 2.46 . 2 94 . 14 PHE HD1 H 6.56 . 3 95 . 14 PHE HE1 H 7.04 . 3 96 . 14 PHE HZ H 7.19 . 1 97 . 15 GLY N N 110.2 . 1 98 . 15 GLY H H 7.98 . 1 99 . 15 GLY HA2 H 4.72 . 1 100 . 15 GLY HA3 H 4.13 . 1 101 . 16 GLN N N 123.4 . 1 102 . 16 GLN H H 9.39 . 1 103 . 16 GLN HA H 3.91 . 1 104 . 16 GLN HB2 H 2.19 . 2 105 . 16 GLN NE2 N 109.3 . 1 106 . 16 GLN HE21 H 7.57 . 2 107 . 16 GLN HE22 H 7.03 . 2 108 . 17 THR N N 117.3 . 1 109 . 17 THR H H 8.51 . 1 110 . 17 THR HA H 3.99 . 1 111 . 17 THR HB H 4.2 . 1 112 . 17 THR HG2 H 1.36 . 1 113 . 18 LYS N N 124 . 1 114 . 18 LYS H H 8.93 . 1 115 . 18 LYS HA H 4.16 . 1 116 . 18 LYS HB2 H 1.87 . 2 117 . 18 LYS HG2 H 1.66 . 2 118 . 18 LYS HG3 H 1.97 . 2 119 . 19 THR N N 113.9 . 1 120 . 19 THR H H 7.57 . 1 121 . 19 THR HA H 3.92 . 1 122 . 19 THR HB H 4.29 . 1 123 . 19 THR HG2 H 1.23 . 1 124 . 20 ALA N N 121.7 . 1 125 . 20 ALA H H 8.1 . 1 126 . 20 ALA HA H 3.85 . 1 127 . 20 ALA HB H 1.61 . 1 128 . 21 LYS N N 119 . 1 129 . 21 LYS H H 7.83 . 1 130 . 21 LYS HA H 4.14 . 1 131 . 21 LYS HB2 H 2.03 . 2 132 . 21 LYS HB3 H 2.0 . 2 133 . 21 LYS HG2 H 1.59 . 2 134 . 21 LYS HG3 H 1.64 . 2 135 . 21 LYS HD2 H 1.78 . 2 136 . 21 LYS HE2 H 3.07 . 2 137 . 22 ASP N N 120.9 . 1 138 . 22 ASP H H 9.13 . 1 139 . 22 ASP HA H 4.36 . 1 140 . 22 ASP HB2 H 2.9 . 2 141 . 23 LEU N N 115.7 . 1 142 . 23 LEU H H 7.63 . 1 143 . 23 LEU HA H 4.5 . 1 144 . 23 LEU HB2 H 1.78 . 2 145 . 23 LEU HG H 1.58 . 1 146 . 23 LEU HD1 H 0.8 . 1 147 . 23 LEU HD2 H 1.8 . 1 148 . 24 GLY N N 110 . 1 149 . 24 GLY H H 8.04 . 1 150 . 24 GLY HA2 H 4.02 . 1 151 . 24 GLY HA3 H 3.96 . 1 152 . 25 VAL N N 111.9 . 1 153 . 25 VAL H H 7.94 . 1 154 . 25 VAL HA H 4.54 . 1 155 . 25 VAL HB H 2.2 . 1 156 . 25 VAL HG1 H 0.77 . 1 157 . 25 VAL HG2 H 0.70 . 1 158 . 26 TYR N N 118.8 . 1 159 . 26 TYR H H 8.02 . 1 160 . 26 TYR HA H 4.82 . 1 161 . 26 TYR HB2 H 3.47 . 1 162 . 26 TYR HB3 H 2.93 . 1 163 . 26 TYR HD1 H 7.34 . 2 164 . 26 TYR HE1 H 6.96 . 2 165 . 27 GLN N N 123.3 . 1 166 . 27 GLN H H 9.36 . 1 167 . 27 GLN HA H 3.87 . 1 168 . 27 GLN HB2 H 2.2 . 2 169 . 27 GLN HG2 H 2.43 . 2 170 . 27 GLN NE2 N 112.8 . 1 171 . 27 GLN HE21 H 7.01 . 2 172 . 27 GLN HE22 H 7.68 . 2 173 . 28 SER N N 113.6 . 1 174 . 28 SER H H 8.7 . 1 175 . 28 SER HA H 4.28 . 1 176 . 28 SER HB2 H 4.03 . 2 177 . 29 ALA N N 124 . 1 178 . 29 ALA H H 7.49 . 1 179 . 29 ALA HA H 4.34 . 1 180 . 29 ALA HB H 1.67 . 1 181 . 30 ILE N N 118 . 1 182 . 30 ILE H H 7.47 . 1 183 . 30 ILE HA H 3.79 . 1 184 . 30 ILE HB H 2.51 . 1 185 . 30 ILE HG12 H 1.46 . 2 186 . 30 ILE HG13 H 1.77 . 2 187 . 30 ILE HG2 H 0.97 . 1 188 . 30 ILE HD1 H 0.82 . 1 189 . 31 ASN N N 118.2 . 1 190 . 31 ASN H H 8.14 . 1 191 . 31 ASN HA H 4.38 . 1 192 . 31 ASN HB2 H 3.08 . 2 193 . 31 ASN HB3 H 2.85 . 2 194 . 31 ASN ND2 N 113.4 . 1 195 . 31 ASN HD21 H 7.06 . 2 196 . 31 ASN HD22 H 7.72 . 2 197 . 32 LYS N N 118.4 . 1 198 . 32 LYS H H 8.25 . 1 199 . 32 LYS HA H 4.13 . 1 200 . 32 LYS HB2 H 1.97 . 2 201 . 32 LYS HG2 H 1.57 . 2 202 . 32 LYS HG3 H 1.79 . 2 203 . 32 LYS HD2 H 3.06 . 2 204 . 33 ALA N N 121.9 . 1 205 . 33 ALA H H 7.73 . 1 206 . 33 ALA HA H 4.17 . 1 207 . 33 ALA HB H 1.31 . 1 208 . 34 ILE N N 118.2 . 1 209 . 34 ILE H H 8.19 . 1 210 . 34 ILE HA H 3.84 . 1 211 . 34 ILE HB H 1.88 . 1 212 . 34 ILE HG12 H 1.48 . 2 213 . 34 ILE HG13 H 0.69 . 2 214 . 34 ILE HG2 H 0.87 . 1 215 . 34 ILE HD1 H 0.85 . 1 216 . 35 HIS N N 119.5 . 1 217 . 35 HIS H H 8.4 . 1 218 . 35 HIS HA H 4.41 . 1 219 . 35 HIS HB2 H 3.35 . 2 220 . 35 HIS HD1 H 7.25 . 2 221 . 35 HIS HE1 H 8.11 . 2 222 . 36 ALA N N 118.7 . 1 223 . 36 ALA H H 8.09 . 1 224 . 36 ALA HA H 4.41 . 1 225 . 36 ALA HB H 1.56 . 1 226 . 37 GLY N N 106.9 . 1 227 . 37 GLY H H 7.84 . 1 228 . 37 GLY HA2 H 4.02 . 1 229 . 37 GLY HA3 H 3.94 . 1 230 . 38 ARG N N 117.9 . 1 231 . 38 ARG H H 7.21 . 1 232 . 38 ARG HA H 4.1 . 1 233 . 38 ARG HB2 H 1.31 . 2 234 . 38 ARG HG2 H 1.89 . 2 235 . 38 ARG HG3 H 1.79 . 2 236 . 38 ARG HD2 H 2.96 . 2 237 . 38 ARG NE N 83 . 1 238 . 38 ARG HE H 8.125 . 1 239 . 39 LYS N N 126.3 . 1 240 . 39 LYS H H 9.18 . 1 241 . 39 LYS HA H 4.34 . 1 242 . 39 LYS HB2 H 2.39 . 1 243 . 39 LYS HB3 H 1.68 . 1 244 . 39 LYS HG2 H 1.85 . 2 245 . 39 LYS HG3 H 1.92 . 2 246 . 39 LYS HD2 H 3.18 . 2 247 . 40 ILE N N 123.7 . 1 248 . 40 ILE H H 7.01 . 1 249 . 40 ILE HA H 4.9 . 1 250 . 40 ILE HB H 1.08 . 1 251 . 40 ILE HG12 H 0.34 . 2 252 . 40 ILE HG13 H 1.02 . 2 253 . 40 ILE HG2 H 0.38 . 1 254 . 40 ILE HD1 H -0.19 . 1 255 . 41 PHE N N 126.6 . 1 256 . 41 PHE H H 9.25 . 1 257 . 41 PHE HA H 5.06 . 1 258 . 41 PHE HB2 H 2.70 . 2 259 . 41 PHE HB3 H 2.83 . 2 260 . 42 LEU N N 127.3 . 1 261 . 42 LEU H H 9.99 . 1 262 . 42 LEU HA H 5.18 . 1 263 . 42 LEU HB2 H 1.4 . 2 264 . 42 LEU HG H 1.39 . 1 265 . 42 LEU HD1 H 0.60 . 1 266 . 42 LEU HD2 H 0.10 . 1 267 . 43 THR N N 118 . 1 268 . 43 THR H H 8.79 . 1 269 . 43 THR HA H 4.73 . 1 270 . 43 THR HB H 3.3 . 1 271 . 43 THR HG2 H 1.13 . 1 272 . 44 ILE N N 125.7 . 1 273 . 44 ILE H H 8.65 . 1 274 . 44 ILE HA H 4.52 . 1 275 . 44 ILE HB H 1.87 . 1 276 . 44 ILE HG12 H 1.69 . 2 277 . 44 ILE HG13 H 1.24 . 2 278 . 44 ILE HG2 H 1.02 . 1 279 . 44 ILE HD1 H 1.1 . 1 280 . 45 ASN N N 126.1 . 1 281 . 45 ASN H H 9.1 . 1 282 . 45 ASN HA H 4.9 . 1 283 . 45 ASN HB2 H 3.02 . 1 284 . 45 ASN HB3 H 2.95 . 1 285 . 45 ASN ND2 N 112.6 . 1 286 . 45 ASN HD21 H 6.37 . 2 287 . 45 ASN HD22 H 7.31 . 2 288 . 46 ALA N N 124.4 . 1 289 . 46 ALA H H 9.02 . 1 290 . 46 ALA HA H 4.19 . 1 291 . 46 ALA HB H 1.53 . 1 292 . 47 ASP N N 114 . 1 293 . 47 ASP H H 7.95 . 1 294 . 47 ASP HA H 4.56 . 1 295 . 47 ASP HB2 H 3.13 . 1 296 . 47 ASP HB3 H 2.67 . 1 297 . 48 GLY N N 109.2 . 1 298 . 48 GLY H H 8.22 . 1 299 . 48 GLY HA2 H 4.37 . 1 300 . 48 GLY HA3 H 3.57 . 1 301 . 49 SER N N 117.6 . 1 302 . 49 SER H H 8.29 . 1 303 . 49 SER HA H 4.4 . 1 304 . 49 SER HB2 H 4 . 2 305 . 50 VAL N N 117.8 . 1 306 . 50 VAL H H 8.37 . 1 307 . 50 VAL HA H 5.25 . 1 308 . 50 VAL HB H 1.73 . 1 309 . 50 VAL HG1 H 0.87 . 1 310 . 50 VAL HG2 H 0.72 . 1 311 . 51 TYR N N 122.9 . 1 312 . 51 TYR H H 8.5 . 1 313 . 51 TYR HA H 4.9 . 1 314 . 51 TYR HB2 H 3.14 . 2 315 . 51 TYR HB3 H 3.04 . 2 316 . 51 TYR HE1 H 7.1 . 2 317 . 51 TYR HE2 H 6.86 . 2 318 . 52 ALA N N 124.5 . 1 319 . 52 ALA H H 8.97 . 1 320 . 52 ALA HA H 5.67 . 1 321 . 52 ALA HB H 1.58 . 1 322 . 53 GLU N N 118.5 . 1 323 . 53 GLU H H 8.93 . 1 324 . 53 GLU HA H 5.03 . 1 325 . 53 GLU HB2 H 1.92 . 2 326 . 53 GLU HG2 H 2.32 . 2 327 . 53 GLU HG3 H 2.23 . 2 328 . 54 GLU N N 123.6 . 1 329 . 54 GLU H H 9.86 . 1 330 . 54 GLU HA H 5.35 . 1 331 . 54 GLU HB2 H 2 . 2 332 . 54 GLU HG2 H 2.13 . 2 333 . 54 GLU HG3 H 1.64 . 2 334 . 55 VAL N N 126.5 . 1 335 . 55 VAL H H 8.73 . 1 336 . 55 VAL HA H 4.86 . 1 337 . 55 VAL HB H 2.19 . 1 338 . 55 VAL HG1 H 1.07 . 2 339 . 55 VAL HG2 H 0.96 . 2 340 . 56 LYS N N 129.6 . 1 341 . 56 LYS H H 9 . 1 342 . 56 LYS HA H 4.67 . 1 343 . 56 LYS HB2 H 1.86 . 2 344 . 56 LYS HB3 H 1.64 . 2 345 . 56 LYS HG2 H 1.43 . 2 346 . 56 LYS HD2 H 2.62 . 2 347 . 56 LYS HE2 H 3.05 . 2 348 . 57 ASP N N 127.3 . 1 349 . 57 ASP H H 9.44 . 1 350 . 57 ASP HA H 4.39 . 1 351 . 57 ASP HB2 H 2.99 . 2 352 . 57 ASP HB3 H 2.79 . 2 353 . 58 GLY N N 104.6 . 1 354 . 58 GLY H H 8.48 . 1 355 . 58 GLY HA2 H 4.19 . 2 356 . 58 GLY HA3 H 3.68 . 2 357 . 59 GLU N N 120.5 . 1 358 . 59 GLU H H 7.93 . 1 359 . 59 GLU HA H 4.75 . 1 360 . 59 GLU HB2 H 2.14 . 2 361 . 59 GLU HB3 H 2.04 . 2 362 . 59 GLU HG2 H 2.38 . 2 363 . 59 GLU HG3 H 2.31 . 2 364 . 60 VAL N N 122.3 . 1 365 . 60 VAL H H 8.47 . 1 366 . 60 VAL HA H 4.89 . 1 367 . 60 VAL HB H 1.95 . 1 368 . 60 VAL HG1 H 0.98 . 1 369 . 60 VAL HG2 H 0.90 . 1 370 . 61 LYS N N 127.4 . 1 371 . 61 LYS H H 9.26 . 1 372 . 61 LYS HA H 5.08 . 1 373 . 61 LYS HB2 H 1.83 . 2 374 . 61 LYS HG2 H 1.53 . 2 375 . 61 LYS HD2 H 2.00 . 2 376 . 61 LYS HD3 H 1.85 . 2 377 . 61 LYS HE2 H 3.04 . 2 378 . 62 PRO HA H 4.74 . 1 379 . 62 PRO HB2 H 2.58 . 1 380 . 62 PRO HB3 H 2.00 . 1 381 . 62 PRO HG2 H 2.2 . 2 382 . 62 PRO HD2 H 3.8 . 2 383 . 62 PRO HD3 H 4.0 . 2 384 . 63 PHE N N 121 . 1 385 . 63 PHE H H 7.7 . 1 386 . 63 PHE HA H 4.78 . 1 387 . 63 PHE HB2 H 2.56 . 1 388 . 63 PHE HB3 H 2.77 . 1 389 . 63 PHE HD1 H 7.19 . 2 390 . 63 PHE HE1 H 7.13 . 2 391 . 63 PHE HE2 H 6.98 . 2 392 . 64 PRO HA H 3.82 . 1 393 . 64 PRO HB2 H 2.55 . 2 394 . 64 PRO HG2 H 1.78 . 2 395 . 64 PRO HD2 H 3.9 . 2 396 . 64 PRO HD3 H 4.0 . 2 397 . 65 SER N N 114.2 . 1 398 . 65 SER H H 8.46 . 1 399 . 65 SER HA H 4.37 . 1 400 . 65 SER HB2 H 3.98 . 2 401 . 66 ASN N N 119.8 . 1 402 . 66 ASN H H 8.27 . 1 403 . 66 ASN HA H 4.75 . 1 404 . 66 ASN HB2 H 2.84 . 2 405 . 66 ASN ND2 N 112.8 . 1 406 . 66 ASN HD21 H 7.63 . 2 407 . 66 ASN HD22 H 6.93 . 2 408 . 67 LYS N N 121.8 . 1 409 . 67 LYS H H 8.24 . 1 410 . 67 LYS HA H 4.31 . 1 411 . 67 LYS HB2 H 1.87 . 2 412 . 67 LYS HB3 H 1.77 . 2 413 . 67 LYS HG2 H 1.46 . 2 414 . 68 LYS N N 123.3 . 1 415 . 68 LYS H H 8.48 . 1 416 . 68 LYS HA H 4.45 . 1 417 . 68 LYS HB2 H 1.91 . 2 418 . 68 LYS HB3 H 1.82 . 2 419 . 68 LYS HG2 H 1.47 . 2 420 . 68 LYS HD2 H 1.72 . 2 421 . 68 LYS HE2 H 3.07 . 2 422 . 69 THR N N 116.1 . 1 423 . 69 THR H H 8.12 . 1 424 . 69 THR HA H 4.42 . 1 425 . 69 THR HB H 4.35 . 1 426 . 69 THR HG2 H 1.27 . 1 427 . 70 THR N N 115.7 . 1 428 . 70 THR H H 8.12 . 1 429 . 70 THR HA H 4.48 . 1 430 . 70 THR HB H 4.35 . 1 431 . 70 THR HG2 H 1.27 . 1 432 . 71 ALA N N 131.6 . 1 433 . 71 ALA H H 8.05 . 1 434 . 71 ALA HA H 4.18 . 1 435 . 71 ALA HB H 1.38 . 1 stop_ save_