data_5008 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H,13C and 15N backbone resonances of p13suc1 proteins -- wild type ; _BMRB_accession_number 5008 _BMRB_flat_file_name bmr5008.str _Entry_type original _Submission_date 2001-05-09 _Accession_date 2001-05-09 _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 Odaert Benoit . . 2 Landrieu Isabelle . . 3 Dijkstra Klaas . . 4 Schuurman-wolters Gea . . 5 Casteels Peter . . 6 Wieruszeski Jean-Michel . . 7 Scheek Ruud M. . 8 Lippens Guy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 85 "13C chemical shifts" 266 "15N chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5009 'PA90 mutant' stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe ; _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 Odaert Benoit . . 2 Landrieu Isabelle . . 3 Dijkstra Klaas . . 4 Schuurman-Wolters Gea . . 5 Casteels Peter . . 6 Wieruszeski Jean-Michel . . 7 Scheek Ruud M. . 8 Lippens Guy . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 155 _Page_last 156 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_suc1 _Saveframe_category molecular_system _Mol_system_name p13suc1 _Abbreviation_common suc1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'p13 wild type' $P13WT 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_P13WT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common suc1 _Name_variant p13suc1 _Abbreviation_common suc1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; MSKSGVPRLLTASERERLEP FIDQIHYSPRYADDEYEYRH VMLPKAMLKAIPTDYFNPET GTLRILQEEEWRGLGITQSL GWEMYEVHVPEPHILLFKRE KDYQMKFSQQRGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LYS 4 SER 5 GLY 6 VAL 7 PRO 8 ARG 9 LEU 10 LEU 11 THR 12 ALA 13 SER 14 GLU 15 ARG 16 GLU 17 ARG 18 LEU 19 GLU 20 PRO 21 PHE 22 ILE 23 ASP 24 GLN 25 ILE 26 HIS 27 TYR 28 SER 29 PRO 30 ARG 31 TYR 32 ALA 33 ASP 34 ASP 35 GLU 36 TYR 37 GLU 38 TYR 39 ARG 40 HIS 41 VAL 42 MET 43 LEU 44 PRO 45 LYS 46 ALA 47 MET 48 LEU 49 LYS 50 ALA 51 ILE 52 PRO 53 THR 54 ASP 55 TYR 56 PHE 57 ASN 58 PRO 59 GLU 60 THR 61 GLY 62 THR 63 LEU 64 ARG 65 ILE 66 LEU 67 GLN 68 GLU 69 GLU 70 GLU 71 TRP 72 ARG 73 GLY 74 LEU 75 GLY 76 ILE 77 THR 78 GLN 79 SER 80 LEU 81 GLY 82 TRP 83 GLU 84 MET 85 TYR 86 GLU 87 VAL 88 HIS 89 VAL 90 PRO 91 GLU 92 PRO 93 HIS 94 ILE 95 LEU 96 LEU 97 PHE 98 LYS 99 ARG 100 GLU 101 LYS 102 ASP 103 TYR 104 GLN 105 MET 106 LYS 107 PHE 108 SER 109 GLN 110 GLN 111 ARG 112 GLY 113 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-07-28 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 5009 P13PA90 100.00 113 99.12 99.12 4.42e-76 PDB 1PUC "P13suc1 In A Strand-Exchanged Dimer" 92.92 105 100.00 100.00 2.37e-70 PDB 1SCE "Crystal Structure Of The Cell Cycle Regulatory Protein Suc1 Reveals A Novel Beta-Hinge Conformational Switch" 100.00 112 99.12 99.12 3.68e-74 EMBL CAA21308 "cyclin-dependent protein kinase regulatory subunit Suc1 [Schizosaccharomyces pombe]" 100.00 113 100.00 100.00 5.87e-77 GB AAA35346 "cell division protein [Schizosaccharomyces pombe]" 100.00 113 100.00 100.00 5.87e-77 REF NP_595431 "cyclin-dependent protein kinase regulatory subunit Suc1 [Schizosaccharomyces pombe 972h-]" 100.00 113 100.00 100.00 5.87e-77 SP P08463 "RecName: Full=Cyclin-dependent kinases regulatory subunit; AltName: Full=P13 [Schizosaccharomyces pombe 972h-]" 100.00 113 100.00 100.00 5.87e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $P13WT 'fission yeast' 4896 Eukaryota Fungi Schizosaccharomyces pombe 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 $P13WT 'recombinat technology' 'E. coli' Escherichia coli BL21(DE3) pRK172 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $P13WT . mM 1.0 2.0 [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $P13WT . mM 1.0 2.0 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA/HNcaCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA/HNcaCO _Sample_label . save_ save_HNCO/HNcaCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO/HNcaCO _Sample_label . save_ save_CBCANH/CBCAcoNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH/CBCAcoNH _Sample_label . save_ save_15N_NOESY/TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY/TOCSY' _Sample_label . save_ save_15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA/HNcaCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO/HNcaCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH/CBCAcoNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY/TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 na temperature 293 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'p13 wild type' _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 . 3 LYS C C 176.700 . 1 2 . 3 LYS CA C 56.770 . 1 3 . 3 LYS CB C 33.110 . 1 4 . 4 SER H H 8.510 . 1 5 . 4 SER C C 174.900 . 1 6 . 4 SER CA C 58.560 . 1 7 . 4 SER CB C 63.920 . 1 8 . 4 SER N N 116.900 . 1 9 . 5 GLY H H 8.370 . 1 10 . 5 GLY C C 173.700 . 1 11 . 5 GLY CA C 45.060 . 1 12 . 5 GLY N N 110.600 . 1 13 . 6 VAL H H 8.080 . 1 14 . 6 VAL C C 174.800 . 1 15 . 6 VAL CA C 59.830 . 1 16 . 6 VAL CB C 32.400 . 1 17 . 6 VAL N N 120.400 . 1 18 . 7 PRO C C 174.700 . 1 19 . 7 PRO CA C 62.750 . 1 20 . 7 PRO CB C 32.760 . 1 21 . 8 ARG H H 9.860 . 1 22 . 8 ARG C C 175.300 . 1 23 . 8 ARG CA C 55.760 . 1 24 . 8 ARG CB C 29.990 . 1 25 . 8 ARG N N 127.400 . 1 26 . 9 LEU H H 8.600 . 1 27 . 9 LEU C C 177.800 . 1 28 . 9 LEU CA C 54.200 . 1 29 . 9 LEU CB C 41.710 . 1 30 . 9 LEU N N 126.700 . 1 31 . 10 LEU H H 8.670 . 1 32 . 10 LEU C C 179.500 . 1 33 . 10 LEU CA C 54.880 . 1 34 . 10 LEU CB C 42.500 . 1 35 . 10 LEU N N 122.100 . 1 36 . 11 THR H H 9.500 . 1 37 . 11 THR C C 175.600 . 1 38 . 11 THR CA C 60.850 . 1 39 . 11 THR CB C 70.700 . 1 40 . 11 THR N N 114.400 . 1 41 . 12 ALA H H 8.990 . 1 42 . 12 ALA C C 181.000 . 1 43 . 12 ALA CA C 55.990 . 1 44 . 12 ALA CB C 17.910 . 1 45 . 12 ALA N N 122.800 . 1 46 . 13 SER H H 8.510 . 1 47 . 13 SER C C 177.700 . 1 48 . 13 SER CA C 61.380 . 1 49 . 13 SER CB C 62.360 . 1 50 . 13 SER N N 112.500 . 1 51 . 14 GLU H H 7.610 . 1 52 . 14 GLU C C 18. . 1 53 . 14 GLU CA C 58.990 . 1 54 . 14 GLU CB C 30.770 . 1 55 . 14 GLU N N 122.200 . 1 56 . 15 ARG H H 8.610 . 1 57 . 15 ARG C C 179.600 . 1 58 . 15 ARG CA C 59.610 . 1 59 . 15 ARG CB C 29.720 . 1 60 . 15 ARG N N 118.800 . 1 61 . 16 GLU H H 8.190 . 1 62 . 16 GLU C C 179.300 . 1 63 . 16 GLU CA C 59.510 . 1 64 . 16 GLU CB C 29.660 . 1 65 . 16 GLU N N 119.700 . 1 66 . 17 ARG H H 7.290 . 1 67 . 17 ARG C C 177.000 . 1 68 . 17 ARG CA C 58.220 . 1 69 . 17 ARG CB C 30.740 . 1 70 . 17 ARG N N 115.600 . 1 71 . 18 LEU H H 7.430 . 1 72 . 18 LEU C C 177.800 . 1 73 . 18 LEU CA C 55.320 . 1 74 . 18 LEU CB C 42.740 . 1 75 . 18 LEU N N 114.500 . 1 76 . 19 GLU H H 7.580 . 1 77 . 19 GLU C C 175.000 . 1 78 . 19 GLU CA C 60.900 . 1 79 . 19 GLU CB C 27.930 . 1 80 . 19 GLU N N 120.100 . 1 81 . 20 PRO C C 177.000 . 1 82 . 20 PRO CA C 65.210 . 1 83 . 20 PRO CB C 31.360 . 1 84 . 21 PHE H H 7.730 . 1 85 . 21 PHE C C 177.500 . 1 86 . 21 PHE CA C 58.570 . 1 87 . 21 PHE CB C 41.350 . 1 88 . 21 PHE N N 111.700 . 1 89 . 22 ILE H H 7.340 . 1 90 . 22 ILE C C 178.500 . 1 91 . 22 ILE CA C 65.990 . 1 92 . 22 ILE CB C 37.990 . 1 93 . 22 ILE N N 117.500 . 1 94 . 23 ASP H H 8.720 . 1 95 . 23 ASP C C 176.700 . 1 96 . 23 ASP CA C 55.590 . 1 97 . 23 ASP CB C 40.140 . 1 98 . 23 ASP N N 117.600 . 1 99 . 24 GLN H H 7.860 . 1 100 . 24 GLN C C 176.000 . 1 101 . 24 GLN CA C 55.310 . 1 102 . 24 GLN CB C 30.210 . 1 103 . 24 GLN N N 115.800 . 1 104 . 25 ILE H H 7.320 . 1 105 . 25 ILE C C 175.100 . 1 106 . 25 ILE CA C 64.000 . 1 107 . 25 ILE CB C 38.490 . 1 108 . 25 ILE N N 121.900 . 1 109 . 26 HIS H H 8.360 . 1 110 . 26 HIS C C 172.700 . 1 111 . 26 HIS CA C 54.580 . 1 112 . 26 HIS CB C 32.720 . 1 113 . 26 HIS N N 125.400 . 1 114 . 27 TYR H H 8.660 . 1 115 . 27 TYR C C 175.600 . 1 116 . 27 TYR CA C 56.960 . 1 117 . 27 TYR CB C 40.030 . 1 118 . 27 TYR N N 122.900 . 1 119 . 28 SER H H 8.820 . 1 120 . 28 SER CA C 58.260 . 1 121 . 28 SER N N 121.100 . 1 122 . 29 PRO C C 177.300 . 1 123 . 29 PRO CA C 62.970 . 1 124 . 29 PRO CB C 32.140 . 1 125 . 30 ARG H H 8.750 . 1 126 . 30 ARG C C 176.500 . 1 127 . 30 ARG CA C 55.990 . 1 128 . 30 ARG N N 122.600 . 1 129 . 31 TYR H H 8.910 . 1 130 . 31 TYR C C 173.300 . 1 131 . 31 TYR CA C 56.520 . 1 132 . 31 TYR CB C 40.030 . 1 133 . 31 TYR N N 120.600 . 1 134 . 32 ALA H H 8.760 . 1 135 . 32 ALA C C 178.000 . 1 136 . 32 ALA CA C 52.270 . 1 137 . 32 ALA CB C 23.570 . 1 138 . 32 ALA N N 121.200 . 1 139 . 33 ASP H H 8.980 . 1 140 . 33 ASP C C 176.000 . 1 141 . 33 ASP CA C 52.940 . 1 142 . 33 ASP CB C 41.930 . 1 143 . 33 ASP N N 122.400 . 1 144 . 34 ASP H H 8.430 . 1 145 . 34 ASP C C 176.500 . 1 146 . 34 ASP CA C 57.000 . 1 147 . 34 ASP CB C 40.820 . 1 148 . 34 ASP N N 115.600 . 1 149 . 35 GLU H H 8.640 . 1 150 . 35 GLU C C 175.600 . 1 151 . 35 GLU CA C 57.670 . 1 152 . 35 GLU CB C 33.980 . 1 153 . 35 GLU N N 117.700 . 1 154 . 36 TYR H H 9.150 . 1 155 . 36 TYR C C 174.300 . 1 156 . 36 TYR CA C 57.730 . 1 157 . 36 TYR CB C 42.000 . 1 158 . 36 TYR N N 119.600 . 1 159 . 37 GLU H H 8.650 . 1 160 . 37 GLU C C 174.400 . 1 161 . 37 GLU CA C 54.120 . 1 162 . 37 GLU CB C 33.650 . 1 163 . 37 GLU N N 114.900 . 1 164 . 38 TYR H H 9.090 . 1 165 . 38 TYR C C 175.300 . 1 166 . 38 TYR CA C 57.150 . 1 167 . 38 TYR CB C 43.000 . 1 168 . 38 TYR N N 116.700 . 1 169 . 40 HIS C C 174.200 . 1 170 . 40 HIS CA C 53.980 . 1 171 . 40 HIS CB C 32.740 . 1 172 . 41 VAL H H 9.340 . 1 173 . 41 VAL C C 173.900 . 1 174 . 41 VAL CA C 61.270 . 1 175 . 41 VAL N N 123.100 . 1 176 . 42 MET H H 9.140 . 1 177 . 42 MET C C 175.800 . 1 178 . 42 MET CA C 54.490 . 1 179 . 42 MET CB C 34.860 . 1 180 . 42 MET N N 125.900 . 1 181 . 43 LEU H H 9.360 . 1 182 . 43 LEU C C 174.900 . 1 183 . 43 LEU CA C 52.440 . 1 184 . 43 LEU CB C 39.930 . 1 185 . 43 LEU N N 126.700 . 1 186 . 44 PRO C C 178.900 . 1 187 . 44 PRO CA C 62.400 . 1 188 . 44 PRO CB C 31.180 . 1 189 . 45 LYS H H 8.670 . 1 190 . 45 LYS C C 179.900 . 1 191 . 45 LYS CA C 60.930 . 1 192 . 45 LYS CB C 31.870 . 1 193 . 45 LYS N N 125.800 . 1 194 . 46 ALA H H 8.840 . 1 195 . 46 ALA C C 178.900 . 1 196 . 46 ALA CA C 54.260 . 1 197 . 46 ALA CB C 18.860 . 1 198 . 46 ALA N N 118.700 . 1 199 . 47 MET H H 7.460 . 1 200 . 47 MET C C 177.900 . 1 201 . 47 MET CA C 57.820 . 1 202 . 47 MET CB C 33.230 . 1 203 . 47 MET N N 116.400 . 1 204 . 48 LEU H H 7.140 . 1 205 . 48 LEU C C 178.800 . 1 206 . 48 LEU CA C 58.360 . 1 207 . 48 LEU CB C 41.250 . 1 208 . 48 LEU N N 114.700 . 1 209 . 49 LYS H H 6.890 . 1 210 . 49 LYS C C 176.300 . 1 211 . 49 LYS CA C 57.170 . 1 212 . 49 LYS CB C 32.240 . 1 213 . 49 LYS N N 113.000 . 1 214 . 50 ALA H H 7.430 . 1 215 . 50 ALA C C 176.000 . 1 216 . 50 ALA CA C 51.400 . 1 217 . 50 ALA CB C 20.600 . 1 218 . 50 ALA N N 119.700 . 1 219 . 51 ILE H H 7.000 . 1 220 . 51 ILE C C 173.500 . 1 221 . 51 ILE CA C 60.210 . 1 222 . 51 ILE CB C 39.920 . 1 223 . 51 ILE N N 122.100 . 1 224 . 52 PRO C C 177.600 . 1 225 . 52 PRO CA C 63.500 . 1 226 . 52 PRO CB C 32.880 . 1 227 . 53 THR H H 8.590 . 1 228 . 53 THR C C 176.400 . 1 229 . 53 THR CA C 66.120 . 1 230 . 53 THR CB C 68.870 . 1 231 . 53 THR N N 114.800 . 1 232 . 54 ASP H H 8.800 . 1 233 . 54 ASP C C 176.500 . 1 234 . 54 ASP CA C 55.430 . 1 235 . 54 ASP CB C 39.280 . 1 236 . 54 ASP N N 117.100 . 1 237 . 55 TYR H H 8.190 . 1 238 . 55 TYR C C 173.700 . 1 239 . 55 TYR CA C 58.640 . 1 240 . 55 TYR CB C 36.750 . 1 241 . 55 TYR N N 119.700 . 1 242 . 56 PHE H H 7.900 . 1 243 . 56 PHE C C 175.500 . 1 244 . 56 PHE CA C 58.040 . 1 245 . 56 PHE CB C 40.560 . 1 246 . 56 PHE N N 116.500 . 1 247 . 57 ASN H H 9.330 . 1 248 . 57 ASN C C 175.300 . 1 249 . 57 ASN CA C 49.990 . 1 250 . 57 ASN CB C 39.420 . 1 251 . 57 ASN N N 121.300 . 1 252 . 58 PRO C C 178.300 . 1 253 . 58 PRO CA C 64.420 . 1 254 . 58 PRO CB C 32.190 . 1 255 . 59 GLU H H 8.230 . 1 256 . 59 GLU C C 178.000 . 1 257 . 59 GLU CA C 58.370 . 1 258 . 59 GLU CB C 30.210 . 1 259 . 59 GLU N N 115.500 . 1 260 . 60 THR H H 7.190 . 1 261 . 60 THR C C 176.700 . 1 262 . 60 THR CA C 61.480 . 1 263 . 60 THR CB C 70.110 . 1 264 . 60 THR N N 104.600 . 1 265 . 61 GLY H H 8.560 . 1 266 . 61 GLY C C 174.400 . 1 267 . 61 GLY CA C 46.040 . 1 268 . 61 GLY N N 11. . 1 269 . 62 THR H H 7.820 . 1 270 . 62 THR C C 174.000 . 1 271 . 62 THR CA C 59.730 . 1 272 . 62 THR N N 109.100 . 1 273 . 63 LEU H H 9.180 . 1 274 . 63 LEU C C 177.500 . 1 275 . 63 LEU CA C 56.600 . 1 276 . 63 LEU N N 122.300 . 1 277 . 66 LEU C C 177.400 . 1 278 . 66 LEU CA C 53.840 . 1 279 . 67 GLN H H 9.410 . 1 280 . 67 GLN C C 177.600 . 1 281 . 67 GLN CA C 55.410 . 1 282 . 67 GLN CB C 30.500 . 1 283 . 67 GLN N N 120.800 . 1 284 . 68 GLU H H 9.380 . 1 285 . 68 GLU C C 177.200 . 1 286 . 68 GLU CA C 60.110 . 1 287 . 68 GLU CB C 28.800 . 1 288 . 68 GLU N N 125.200 . 1 289 . 69 GLU H H 9.500 . 1 290 . 69 GLU C C 180.100 . 1 291 . 69 GLU CA C 59.740 . 1 292 . 69 GLU CB C 29.720 . 1 293 . 69 GLU N N 114.400 . 1 294 . 70 GLU H H 7.340 . 1 295 . 70 GLU C C 178.900 . 1 296 . 70 GLU CA C 57.880 . 1 297 . 70 GLU CB C 30.510 . 1 298 . 70 GLU N N 114.200 . 1 299 . 71 TRP H H 8.360 . 1 300 . 71 TRP C C 180.100 . 1 301 . 71 TRP CA C 60.320 . 1 302 . 71 TRP CB C 28.310 . 1 303 . 71 TRP N N 115.700 . 1 304 . 72 ARG H H 8.420 . 1 305 . 72 ARG C C 181.700 . 1 306 . 72 ARG CA C 60.170 . 1 307 . 72 ARG CB C 29.450 . 1 308 . 72 ARG N N 122.600 . 1 309 . 73 GLY H H 7.380 . 1 310 . 73 GLY C C 174.300 . 1 311 . 73 GLY CA C 46.590 . 1 312 . 73 GLY N N 107.600 . 1 313 . 74 LEU H H 7.140 . 1 314 . 74 LEU C C 174.400 . 1 315 . 74 LEU CA C 55.080 . 1 316 . 74 LEU CB C 42.730 . 1 317 . 74 LEU N N 116.200 . 1 318 . 75 GLY H H 7.440 . 1 319 . 75 GLY C C 174.500 . 1 320 . 75 GLY CA C 44.200 . 1 321 . 75 GLY N N 98.600 . 1 322 . 76 ILE H H 7.140 . 1 323 . 76 ILE C C 175.400 . 1 324 . 76 ILE CA C 62.120 . 1 325 . 76 ILE CB C 38.190 . 1 326 . 76 ILE N N 120.500 . 1 327 . 77 THR H H 8.750 . 1 328 . 77 THR C C 172.900 . 1 329 . 77 THR CA C 61.040 . 1 330 . 77 THR CB C 7. . 1 331 . 77 THR N N 123.600 . 1 332 . 78 GLN H H 7.310 . 1 333 . 78 GLN C C 175.100 . 1 334 . 78 GLN CA C 53.710 . 1 335 . 78 GLN N N 118.800 . 1 336 . 79 SER H H 9.130 . 1 337 . 79 SER C C 173.500 . 1 338 . 79 SER CA C 59.260 . 1 339 . 79 SER CB C 64.000 . 1 340 . 79 SER N N 116.800 . 1 341 . 80 LEU H H 8.090 . 1 342 . 80 LEU C C 177.700 . 1 343 . 80 LEU CA C 56.530 . 1 344 . 80 LEU CB C 42.500 . 1 345 . 80 LEU N N 118.800 . 1 346 . 81 GLY H H 8.760 . 1 347 . 81 GLY C C 174.600 . 1 348 . 81 GLY CA C 45.000 . 1 349 . 81 GLY N N 109.700 . 1 350 . 82 TRP H H 7.060 . 1 351 . 82 TRP C C 176.600 . 1 352 . 82 TRP CA C 58.390 . 1 353 . 82 TRP N N 119.200 . 1 354 . 83 GLU H H 9.520 . 1 355 . 83 GLU CA C 54.860 . 1 356 . 83 GLU CB C 33.250 . 1 357 . 83 GLU N N 120.400 . 1 358 . 97 PHE C C 175.100 . 1 359 . 97 PHE CA C 56.470 . 1 360 . 98 LYS H H 9.580 . 1 361 . 98 LYS C C 174.500 . 1 362 . 98 LYS CA C 54.560 . 1 363 . 98 LYS CB C 37.660 . 1 364 . 98 LYS N N 117.900 . 1 365 . 99 ARG H H 8.770 . 1 366 . 99 ARG C C 174.600 . 1 367 . 99 ARG CA C 55.010 . 1 368 . 99 ARG N N 119.900 . 1 369 . 100 GLU H H 9.100 . 1 370 . 100 GLU C C 177.000 . 1 371 . 100 GLU CA C 58.000 . 1 372 . 100 GLU CB C 30.060 . 1 373 . 100 GLU N N 125.600 . 1 374 . 101 LYS H H 7.970 . 1 375 . 101 LYS C C 176.700 . 1 376 . 101 LYS CA C 58.510 . 1 377 . 101 LYS CB C 32.390 . 1 378 . 101 LYS N N 122.900 . 1 379 . 102 ASP H H 8.500 . 1 380 . 102 ASP C C 176.200 . 1 381 . 102 ASP CA C 54.170 . 1 382 . 102 ASP CB C 39.840 . 1 383 . 102 ASP N N 118.300 . 1 384 . 103 TYR H H 7.550 . 1 385 . 103 TYR C C 176.700 . 1 386 . 103 TYR CA C 61.390 . 1 387 . 103 TYR CB C 38.710 . 1 388 . 103 TYR N N 119.300 . 1 389 . 104 GLN H H 8.450 . 1 390 . 104 GLN C C 177.200 . 1 391 . 104 GLN CA C 57.500 . 1 392 . 104 GLN CB C 28.610 . 1 393 . 104 GLN N N 118.200 . 1 394 . 105 MET H H 7.890 . 1 395 . 105 MET C C 177.300 . 1 396 . 105 MET CA C 56.670 . 1 397 . 105 MET CB C 32.390 . 1 398 . 105 MET N N 118.700 . 1 399 . 106 LYS H H 7.830 . 1 400 . 106 LYS C C 177.300 . 1 401 . 106 LYS CA C 57.660 . 1 402 . 106 LYS CB C 32.830 . 1 403 . 106 LYS N N 119.700 . 1 404 . 107 PHE H H 8.010 . 1 405 . 107 PHE C C 176.400 . 1 406 . 107 PHE CA C 58.210 . 1 407 . 107 PHE CB C 39.230 . 1 408 . 107 PHE N N 118.500 . 1 409 . 108 SER H H 7.990 . 1 410 . 108 SER C C 174.900 . 1 411 . 108 SER CA C 58.980 . 1 412 . 108 SER CB C 63.740 . 1 413 . 108 SER N N 115.500 . 1 414 . 109 GLN H H 8.290 . 1 415 . 109 GLN C C 176.200 . 1 416 . 109 GLN CA C 56.270 . 1 417 . 109 GLN CB C 29.250 . 1 418 . 109 GLN N N 121.200 . 1 419 . 110 GLN H H 8.280 . 1 420 . 110 GLN C C 176.000 . 1 421 . 110 GLN CA C 56.130 . 1 422 . 110 GLN CB C 29.210 . 1 423 . 110 GLN N N 120.300 . 1 424 . 111 ARG H H 8.370 . 1 425 . 111 ARG C C 176.800 . 1 426 . 111 ARG CA C 56.250 . 1 427 . 111 ARG CB C 30.830 . 1 428 . 111 ARG N N 121.900 . 1 429 . 112 GLY H H 8.440 . 1 430 . 112 GLY C C 173.800 . 1 431 . 112 GLY CA C 45.320 . 1 432 . 112 GLY N N 110.100 . 1 433 . 113 GLY H H 7.990 . 1 434 . 113 GLY C C 179.300 . 1 435 . 113 GLY CA C 46.030 . 1 436 . 113 GLY N N 114.800 . 1 stop_ save_