data_4876 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,13C,15N assignment of Ca2+-bound state of Canine Milk Lysozyme at 30deg ; _BMRB_accession_number 4876 _BMRB_flat_file_name bmr4876.str _Entry_type original _Submission_date 2000-10-24 _Accession_date 2000-10-24 _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 Kobashigawa Yoshihiro . . 2 Nitta Katsutoshi . . 3 Tsuda Sakae . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 260 "13C chemical shifts" 244 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-04-30 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4883 'Ca2+-free state of Canine Milk Lysozyme at 20 deg' 4887 'Ca2+-bound state of Canine Milk Lysozyme at 20 deg' stop_ _Original_release_date 2000-10-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of 1H, 13C, and 15N Resonances of Canine Milk Lysozyme ; _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 Kobashigawa Yoshihiro . . 2 Miura Kazunori . . 3 Demura Makoto . . 4 Nemoto Nobuaki . . 5 Koshiba Takumi . . 6 Nitta Katsutoshi . . 7 Tsuda Sakae . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 387 _Page_last 388 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_canine_milk_lysozyme _Saveframe_category molecular_system _Mol_system_name 'Ca2+-bound state of canine milk lysozyme' _Abbreviation_common 'canine milk lysozyme' _Enzyme_commission_number 3.2.1.17. loop_ _Mol_system_component_name _Mol_label 'canine milk lysozyme' $CML Ca $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CML _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'canine milk lysozyme' _Abbreviation_common CML _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; SKIFSKCELARKLKSMGMDG FHGYSLANWVCMAEYESNFN TQAFNGRNSNGSSDYGIFQL NSKWWCKSNSHSSANACNIM CSKFLDDNIDDDIACAKRVV KDPNGMSAWVAWVKHCKGKD LSKYLASCNL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 SER 2 1 LYS 3 2 ILE 4 3 PHE 5 4 SER 6 5 LYS 7 6 CYS 8 7 GLU 9 8 LEU 10 9 ALA 11 10 ARG 12 11 LYS 13 12 LEU 14 13 LYS 15 14 SER 16 15 MET 17 16 GLY 18 17 MET 19 18 ASP 20 19 GLY 21 20 PHE 22 21 HIS 23 22 GLY 24 23 TYR 25 24 SER 26 25 LEU 27 26 ALA 28 27 ASN 29 28 TRP 30 29 VAL 31 30 CYS 32 31 MET 33 32 ALA 34 33 GLU 35 34 TYR 36 35 GLU 37 36 SER 38 37 ASN 39 38 PHE 40 39 ASN 41 40 THR 42 41 GLN 43 42 ALA 44 43 PHE 45 44 ASN 46 45 GLY 47 46 ARG 48 47 ASN 49 48 SER 50 49 ASN 51 50 GLY 52 51 SER 53 52 SER 54 53 ASP 55 54 TYR 56 55 GLY 57 56 ILE 58 57 PHE 59 58 GLN 60 59 LEU 61 60 ASN 62 61 SER 63 62 LYS 64 63 TRP 65 64 TRP 66 65 CYS 67 66 LYS 68 67 SER 69 68 ASN 70 69 SER 71 70 HIS 72 71 SER 73 72 SER 74 73 ALA 75 74 ASN 76 75 ALA 77 76 CYS 78 77 ASN 79 78 ILE 80 79 MET 81 80 CYS 82 81 SER 83 82 LYS 84 83 PHE 85 84 LEU 86 85 ASP 87 86 ASP 88 87 ASN 89 88 ILE 90 89 ASP 91 90 ASP 92 91 ASP 93 92 ILE 94 93 ALA 95 94 CYS 96 95 ALA 97 96 LYS 98 97 ARG 99 98 VAL 100 99 VAL 101 100 LYS 102 101 ASP 103 102 PRO 104 103 ASN 105 104 GLY 106 105 MET 107 106 SER 108 107 ALA 109 108 TRP 110 109 VAL 111 110 ALA 112 111 TRP 113 112 VAL 114 113 LYS 115 114 HIS 116 115 CYS 117 116 LYS 118 117 GLY 119 118 LYS 120 119 ASP 121 120 LEU 122 121 SER 123 122 LYS 124 123 TYR 125 124 LEU 126 125 ALA 127 126 SER 128 127 CYS 129 128 ASN 130 129 LEU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 4883 'canine milk lysozyme' 100.00 130 100.00 100.00 9.48e-70 BMRB 4887 'canine milk lysozyme' 100.00 130 100.00 100.00 9.48e-70 PDB 1EL1 'X-Ray Crystal Structure Analysis Of Canine Milk Lysozyme (Holo-Type)' 100.00 130 100.00 100.00 9.48e-70 PDB 1I56 'Solution Structure Of Ca2+-Bound State Of Canine Milk Lysozyme' 100.00 130 100.00 100.00 9.48e-70 PDB 1QQY 'X-Ray Crystal Structure Analysis Of Canine Milk Lysozyme (Apo-Type)' 99.23 130 100.00 100.00 2.47e-69 PDB 2CWI 'X-Ray Crystal Structure Analysis Of Recombinant Wild-Type Canine Milk Lysozyme (Apo-Type)' 99.23 129 100.00 100.00 2.54e-69 GenBank AAB31794 'type c lysozyme, alpha-lactalbumin, LZ {EC 3.2.1.17} [dogs, milk, Peptide, 129 aa]' 99.23 129 100.00 100.00 2.54e-69 REF XP_851313 'PREDICTED: similar to lysozyme [Canis familiaris]' 100.00 148 99.23 100.00 5.60e-70 SWISS-PROT P81708 'Lysozyme C, milk isozyme (1,4-beta-N-acetylmuramidase C)' 99.23 129 100.00 100.00 2.54e-69 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 15:31:50 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CML dog 9615 Eukaryota Metazoa Canis familiaris 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 $CML 'recombinant technology' 'E. coli' Escherichia coli . pet22(b) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CML 1.0 mM '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_experiment_1_1 _Saveframe_category NMR_applied_experiment _Experiment_name experiment_1 _Sample_label $sample1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 n/a temperature 303 1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_set1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label experiment_1 stop_ loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'canine milk lysozyme' _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 SER HA H 4.08 0.03 1 2 . 1 SER CA C 57.04 0.50 1 3 . 1 SER CB C 62.81 0.50 1 4 . 2 LYS H H 8.77 0.03 1 5 . 2 LYS HA H 4.37 0.03 1 6 . 2 LYS CA C 56.67 0.50 1 7 . 2 LYS CB C 33.17 0.50 1 8 . 2 LYS N N 123.51 0.25 1 9 . 3 ILE H H 8.78 0.03 1 10 . 3 ILE HA H 4.88 0.03 1 11 . 3 ILE CA C 60.04 0.50 1 12 . 3 ILE CB C 39.29 0.50 1 13 . 3 ILE N N 130.16 0.25 1 14 . 4 PHE H H 8.70 0.03 1 15 . 4 PHE HA H 4.39 0.03 1 16 . 4 PHE CA C 58.49 0.50 1 17 . 4 PHE CB C 41.58 0.50 1 18 . 4 PHE N N 126.42 0.25 1 19 . 5 SER H H 7.86 0.03 1 20 . 5 SER HA H 4.53 0.03 1 21 . 5 SER CA C 65.00 0.50 1 22 . 5 SER CB C 56.44 0.50 1 23 . 5 SER N N 112.60 0.25 1 24 . 6 LYS H H 8.60 0.03 1 25 . 6 LYS HA H 4.65 0.03 1 26 . 6 LYS CA C 60.25 0.50 1 27 . 6 LYS CB C 31.92 0.50 1 28 . 6 LYS N N 122.88 0.25 1 29 . 7 CYS H H 8.62 0.03 1 30 . 7 CYS HA H 4.51 0.03 1 31 . 7 CYS CA C 54.94 0.50 1 32 . 7 CYS CB C 34.36 0.50 1 33 . 7 CYS N N 113.20 0.25 1 34 . 8 GLU H H 7.72 0.03 1 35 . 8 GLU HA H 4.02 0.03 1 36 . 8 GLU CA C 58.78 0.50 1 37 . 8 GLU CB C 30.48 0.50 1 38 . 8 GLU N N 123.27 0.25 1 39 . 9 LEU H H 8.62 0.03 1 40 . 9 LEU HA H 3.79 0.03 1 41 . 9 LEU CA C 57.18 0.50 1 42 . 9 LEU CB C 39.94 0.50 1 43 . 9 LEU N N 119.82 0.25 1 44 . 10 ALA H H 8.56 0.03 1 45 . 10 ALA HA H 4.53 0.03 1 46 . 10 ALA CA C 55.83 0.50 1 47 . 10 ALA CB C 19.43 0.50 1 48 . 10 ALA N N 121.17 0.25 1 49 . 11 ARG H H 8.09 0.03 1 50 . 11 ARG HA H 3.86 0.03 1 51 . 11 ARG CA C 60.06 0.50 1 52 . 11 ARG CB C 30.74 0.50 1 53 . 11 ARG N N 116.21 0.25 1 54 . 12 LYS H H 7.84 0.03 1 55 . 12 LYS HA H 4.25 0.03 1 56 . 12 LYS CA C 57.95 0.50 1 57 . 12 LYS CB C 31.03 0.50 1 58 . 12 LYS N N 121.40 0.25 1 59 . 13 LEU H H 9.05 0.03 1 60 . 13 LEU HA H 3.63 0.03 1 61 . 13 LEU CA C 57.76 0.50 1 62 . 13 LEU CB C 39.48 0.50 1 63 . 13 LEU N N 117.58 0.25 1 64 . 14 LYS H H 8.70 0.03 1 65 . 14 LYS HA H 3.96 0.03 1 66 . 14 LYS CA C 59.20 0.50 1 67 . 14 LYS CB C 32.51 0.50 1 68 . 14 LYS N N 121.91 0.25 1 69 . 15 SER H H 8.03 0.03 1 70 . 15 SER HA H 4.37 0.03 1 71 . 15 SER CA C 63.53 0.50 1 72 . 15 SER CB C 61.14 0.50 1 73 . 15 SER N N 115.93 0.25 1 74 . 16 MET H H 7.17 0.03 1 75 . 16 MET HA H 4.74 0.03 1 76 . 16 MET CA C 53.66 0.50 1 77 . 16 MET CB C 32.00 0.50 1 78 . 16 MET N N 118.12 0.25 1 79 . 17 GLY H H 7.62 0.03 1 80 . 17 GLY HA2 H 3.98 0.03 1 81 . 17 GLY HA3 H 3.98 0.03 1 82 . 17 GLY CA C 46.82 0.50 1 83 . 17 GLY N N 106.44 0.25 1 84 . 18 MET H H 7.31 0.03 1 85 . 18 MET HA H 4.10 0.03 1 86 . 18 MET CA C 55.24 0.50 1 87 . 18 MET CB C 31.58 0.50 1 88 . 18 MET N N 112.96 0.25 1 89 . 19 ASP H H 8.90 0.03 1 90 . 19 ASP HA H 4.43 0.03 1 91 . 19 ASP CA C 55.40 0.50 1 92 . 19 ASP CB C 40.90 0.50 1 93 . 19 ASP N N 118.10 0.25 1 94 . 20 GLY H H 8.67 0.03 1 95 . 20 GLY HA2 H 3.29 0.03 1 96 . 20 GLY HA3 H 4.35 0.03 1 97 . 20 GLY CA C 45.48 0.50 1 98 . 20 GLY N N 119.36 0.25 1 99 . 21 PHE H H 8.19 0.03 1 100 . 21 PHE HA H 4.20 0.03 1 101 . 21 PHE CA C 60.69 0.50 1 102 . 21 PHE CB C 39.19 0.50 1 103 . 21 PHE N N 125.89 0.25 1 104 . 22 HIS H H 9.22 0.03 1 105 . 22 HIS HA H 3.86 0.03 1 106 . 22 HIS CA C 56.10 0.50 1 107 . 22 HIS CB C 29.10 0.50 1 108 . 22 HIS N N 128.26 0.25 1 109 . 23 GLY H H 7.94 0.03 1 110 . 23 GLY HA2 H 3.47 0.03 1 111 . 23 GLY HA3 H 3.82 0.03 1 112 . 23 GLY CA C 44.80 0.50 1 113 . 23 GLY N N 102.18 0.25 1 114 . 24 TYR H H 7.49 0.03 1 115 . 24 TYR HA H 4.64 0.03 1 116 . 24 TYR CA C 57.77 0.50 1 117 . 24 TYR CB C 39.50 0.50 1 118 . 24 TYR N N 119.44 0.25 1 119 . 25 SER H H 9.04 0.03 1 120 . 25 SER HA H 4.49 0.03 1 121 . 25 SER CA C 57.18 0.50 1 122 . 25 SER CB C 65.01 0.50 1 123 . 25 SER N N 119.64 0.25 1 124 . 26 LEU H H 8.88 0.03 1 125 . 26 LEU HA H 4.25 0.03 1 126 . 26 LEU CA C 58.44 0.50 1 127 . 26 LEU CB C 42.53 0.50 1 128 . 26 LEU N N 121.67 0.25 1 129 . 27 ALA H H 9.15 0.03 1 130 . 27 ALA HA H 4.04 0.03 1 131 . 27 ALA CA C 56.04 0.50 1 132 . 27 ALA CB C 19.21 0.50 1 133 . 27 ALA N N 117.34 0.25 1 134 . 28 ASN H H 7.84 0.03 1 135 . 28 ASN HA H 4.18 0.03 1 136 . 28 ASN CA C 58.78 0.50 1 137 . 28 ASN CB C 39.75 0.50 1 138 . 28 ASN N N 115.83 0.25 1 139 . 29 TRP H H 7.45 0.03 1 140 . 29 TRP HA H 3.86 0.03 1 141 . 29 TRP CA C 60.85 0.50 1 142 . 29 TRP CB C 29.81 0.50 1 143 . 29 TRP N N 118.70 0.25 1 144 . 30 VAL H H 8.33 0.03 1 145 . 30 VAL HA H 3.65 0.03 1 146 . 30 VAL CA C 66.67 0.50 1 147 . 30 VAL CB C 31.92 0.50 1 148 . 30 VAL N N 116.75 0.25 1 149 . 31 CYS H H 8.70 0.03 1 150 . 31 CYS HA H 4.78 0.03 1 151 . 31 CYS CA C 60.55 0.50 1 152 . 31 CYS CB C 42.19 0.50 1 153 . 31 CYS N N 120.53 0.25 1 154 . 32 MET H H 8.28 0.03 1 155 . 32 MET HA H 3.79 0.03 1 156 . 32 MET CA C 60.86 0.50 1 157 . 32 MET CB C 30.15 0.50 1 158 . 32 MET N N 119.31 0.25 1 159 . 33 ALA H H 7.64 0.03 1 160 . 33 ALA HA H 4.04 0.03 1 161 . 33 ALA CA C 55.08 0.50 1 162 . 33 ALA CB C 19.12 0.50 1 163 . 33 ALA N N 122.17 0.25 1 164 . 34 GLU H H 8.82 0.03 1 165 . 34 GLU HA H 4.63 0.03 1 166 . 34 GLU CA C 59.77 0.50 1 167 . 34 GLU CB C 27.57 0.50 1 168 . 34 GLU N N 120.09 0.25 1 169 . 35 TYR H H 7.73 0.03 1 170 . 35 TYR HA H 4.06 0.03 1 171 . 35 TYR CA C 60.93 0.50 1 172 . 35 TYR CB C 38.17 0.50 1 173 . 35 TYR N N 113.15 0.25 1 174 . 36 GLU H H 8.78 0.03 1 175 . 36 GLU HA H 4.25 0.03 1 176 . 36 GLU CA C 58.45 0.50 1 177 . 36 GLU CB C 28.04 0.50 1 178 . 36 GLU N N 119.19 0.25 1 179 . 37 SER H H 8.06 0.03 1 180 . 37 SER HA H 4.57 0.03 1 181 . 37 SER CA C 57.74 0.50 1 182 . 37 SER CB C 67.11 0.50 1 183 . 37 SER N N 108.35 0.25 1 184 . 38 ASN H H 8.09 0.03 1 185 . 38 ASN HA H 4.29 0.03 1 186 . 38 ASN CA C 54.65 0.50 1 187 . 38 ASN CB C 37.81 0.50 1 188 . 38 ASN N N 125.25 0.25 1 189 . 39 PHE H H 7.26 0.03 1 190 . 39 PHE HA H 3.75 0.03 1 191 . 39 PHE CA C 58.36 0.50 1 192 . 39 PHE CB C 37.98 0.50 1 193 . 39 PHE N N 104.93 0.25 1 194 . 40 ASN H H 7.36 0.03 1 195 . 40 ASN HA H 4.98 0.03 1 196 . 40 ASN CA C 53.06 0.50 1 197 . 40 ASN CB C 39.08 0.50 1 198 . 40 ASN N N 118.29 0.25 1 199 . 41 THR H H 8.30 0.03 1 200 . 41 THR HA H 4.08 0.03 1 201 . 41 THR CA C 64.26 0.50 1 202 . 41 THR CB C 68.75 0.50 1 203 . 41 THR N N 116.00 0.25 1 204 . 42 GLN H H 7.71 0.03 1 205 . 42 GLN HA H 4.63 0.03 1 206 . 42 GLN CA C 55.16 0.50 1 207 . 42 GLN CB C 29.05 0.50 1 208 . 42 GLN N N 114.86 0.25 1 209 . 43 ALA H H 7.09 0.03 1 210 . 43 ALA HA H 4.04 0.03 1 211 . 43 ALA CA C 53.59 0.50 1 212 . 43 ALA CB C 19.46 0.50 1 213 . 43 ALA N N 123.06 0.25 1 214 . 44 PHE H H 8.30 0.03 1 215 . 44 PHE HA H 5.10 0.03 1 216 . 44 PHE CA C 57.01 0.50 1 217 . 44 PHE CB C 42.50 0.50 1 218 . 44 PHE N N 120.72 0.25 1 219 . 45 ASN H H 7.95 0.03 1 220 . 45 ASN HA H 4.78 0.03 1 221 . 45 ASN CA C 51.62 0.50 1 222 . 45 ASN CB C 40.71 0.50 1 223 . 45 ASN N N 125.07 0.25 1 224 . 46 GLY H H 8.56 0.03 1 225 . 46 GLY HA2 H 3.51 0.03 1 226 . 46 GLY HA3 H 4.14 0.03 1 227 . 46 GLY CA C 45.42 0.50 1 228 . 46 GLY N N 112.56 0.25 1 229 . 47 ARG H H 7.81 0.03 1 230 . 47 ARG HA H 4.47 0.03 1 231 . 47 ARG CA C 55.38 0.50 1 232 . 47 ARG CB C 30.24 0.50 1 233 . 47 ARG N N 120.62 0.25 1 234 . 48 ASN H H 8.01 0.03 1 235 . 48 ASN HA H 4.80 0.03 1 236 . 48 ASN CA C 53.05 0.50 1 237 . 48 ASN CB C 40.10 0.50 1 238 . 48 ASN N N 120.56 0.25 1 239 . 49 SER H H 8.99 0.03 1 240 . 49 SER HA H 4.67 0.03 1 241 . 49 SER CA C 60.80 0.50 1 242 . 49 SER CB C 62.48 0.50 1 243 . 49 SER N N 118.32 0.25 1 244 . 50 ASN H H 8.15 0.03 1 245 . 50 ASN HA H 4.78 0.03 1 246 . 50 ASN CA C 52.13 0.50 1 247 . 50 ASN CB C 38.06 0.50 1 248 . 50 ASN N N 117.31 0.25 1 249 . 51 GLY H H 8.08 0.03 1 250 . 51 GLY HA2 H 3.79 0.03 1 251 . 51 GLY HA3 H 4.14 0.03 1 252 . 51 GLY CA C 45.55 0.50 1 253 . 51 GLY N N 107.34 0.25 1 254 . 52 SER H H 7.83 0.03 1 255 . 52 SER HA H 4.45 0.03 1 256 . 52 SER CA C 57.60 0.50 1 257 . 52 SER CB C 64.67 0.50 1 258 . 52 SER N N 115.92 0.25 1 259 . 53 SER H H 8.49 0.03 1 260 . 53 SER HA H 4.94 0.03 1 261 . 53 SER N N 114.30 0.25 1 262 . 54 ASP CA C 53.14 0.50 1 263 . 54 ASP CB C 44.21 0.50 1 264 . 55 TYR H H 9.09 0.03 1 265 . 55 TYR HA H 4.78 0.03 1 266 . 55 TYR CA C 59.34 0.50 1 267 . 55 TYR CB C 43.73 0.50 1 268 . 55 TYR N N 118.61 0.25 1 269 . 56 GLY H H 9.09 0.03 1 270 . 56 GLY HA2 H 4.33 0.03 1 271 . 56 GLY HA3 H 5.08 0.03 1 272 . 56 GLY CA C 47.29 0.50 1 273 . 56 GLY N N 113.62 0.25 1 274 . 57 ILE H H 9.72 0.03 1 275 . 57 ILE HA H 4.69 0.03 1 276 . 57 ILE CA C 61.81 0.50 1 277 . 57 ILE CB C 38.91 0.50 1 278 . 57 ILE N N 124.68 0.25 1 279 . 58 PHE H H 8.97 0.03 1 280 . 58 PHE HA H 5.04 0.03 1 281 . 58 PHE CA C 53.10 0.50 1 282 . 58 PHE CB C 38.06 0.50 1 283 . 58 PHE N N 117.41 0.25 1 284 . 59 GLN H H 8.29 0.03 1 285 . 59 GLN HA H 3.45 0.03 1 286 . 59 GLN CA C 54.82 0.50 1 287 . 59 GLN CB C 27.88 0.50 1 288 . 59 GLN N N 116.28 0.25 1 289 . 60 LEU H H 7.84 0.03 1 290 . 60 LEU HA H 4.51 0.03 1 291 . 60 LEU CA C 55.16 0.50 1 292 . 60 LEU CB C 43.26 0.50 1 293 . 60 LEU N N 119.74 0.25 1 294 . 61 ASN H H 9.42 0.03 1 295 . 61 ASN HA H 4.96 0.03 1 296 . 61 ASN N N 118.47 0.25 1 297 . 62 SER HA H 3.41 0.03 1 298 . 62 SER CA C 60.09 0.50 1 299 . 63 LYS H H 8.59 0.03 1 300 . 63 LYS HA H 4.37 0.03 1 301 . 63 LYS CA C 58.22 0.50 1 302 . 63 LYS CB C 32.64 0.50 1 303 . 63 LYS N N 123.35 0.25 1 304 . 64 TRP H H 7.25 0.03 1 305 . 64 TRP HA H 4.71 0.03 1 306 . 64 TRP CA C 56.43 0.50 1 307 . 64 TRP CB C 30.62 0.50 1 308 . 64 TRP N N 114.40 0.25 1 309 . 65 TRP H H 7.50 0.03 1 310 . 65 TRP HA H 5.02 0.03 1 311 . 65 TRP CA C 59.16 0.50 1 312 . 65 TRP CB C 31.95 0.50 1 313 . 65 TRP N N 115.39 0.25 1 314 . 66 CYS H H 7.59 0.03 1 315 . 66 CYS HA H 5.71 0.03 1 316 . 66 CYS CA C 52.68 0.50 1 317 . 66 CYS CB C 46.59 0.50 1 318 . 66 CYS N N 110.99 0.25 1 319 . 67 LYS H H 8.64 0.03 1 320 . 67 LYS HA H 4.57 0.03 1 321 . 67 LYS CA C 55.24 0.50 1 322 . 67 LYS CB C 34.70 0.50 1 323 . 67 LYS N N 121.98 0.25 1 324 . 68 SER H H 9.25 0.03 1 325 . 68 SER HA H 4.67 0.03 1 326 . 68 SER CA C 56.92 0.50 1 327 . 68 SER CB C 65.38 0.50 1 328 . 68 SER N N 124.94 0.25 1 329 . 69 ASN H H 8.60 0.03 1 330 . 69 ASN HA H 4.71 0.03 1 331 . 69 ASN CA C 54.12 0.50 1 332 . 69 ASN CB C 38.32 0.50 1 333 . 69 ASN N N 119.30 0.25 1 334 . 70 SER H H 8.25 0.03 1 335 . 70 SER CA C 58.85 0.50 1 336 . 70 SER CB C 63.03 0.50 1 337 . 70 SER N N 112.64 0.25 1 338 . 71 HIS H H 7.92 0.03 1 339 . 71 HIS HA H 4.43 0.03 1 340 . 71 HIS CA C 55.36 0.50 1 341 . 71 HIS CB C 30.05 0.50 1 342 . 71 HIS N N 118.00 0.25 1 343 . 72 SER H H 8.57 0.03 1 344 . 72 SER HA H 3.88 0.03 1 345 . 72 SER CA C 58.66 0.50 1 346 . 72 SER CB C 62.93 0.50 1 347 . 72 SER N N 118.56 0.25 1 348 . 73 SER H H 8.26 0.03 1 349 . 73 SER HA H 4.74 0.03 1 350 . 73 SER CA C 56.38 0.50 1 351 . 73 SER CB C 64.83 0.50 1 352 . 73 SER N N 115.72 0.25 1 353 . 74 ALA H H 7.95 0.03 1 354 . 74 ALA HA H 4.12 0.03 1 355 . 74 ALA CA C 54.06 0.50 1 356 . 74 ALA CB C 18.19 0.50 1 357 . 74 ALA N N 127.37 0.25 1 358 . 75 ASN H H 8.56 0.03 1 359 . 75 ASN HA H 3.69 0.03 1 360 . 75 ASN CA C 51.88 0.50 1 361 . 75 ASN CB C 37.10 0.50 1 362 . 75 ASN N N 113.68 0.25 1 363 . 76 ALA H H 8.59 0.03 1 364 . 76 ALA HA H 4.12 0.03 1 365 . 76 ALA CA C 55.28 0.50 1 366 . 76 ALA CB C 19.31 0.50 1 367 . 76 ALA N N 120.08 0.25 1 368 . 77 CYS H H 9.04 0.03 1 369 . 77 CYS HA H 4.55 0.03 1 370 . 77 CYS CA C 55.32 0.50 1 371 . 77 CYS CB C 40.00 0.50 1 372 . 77 CYS N N 111.29 0.25 1 373 . 78 ASN H H 8.00 0.03 1 374 . 78 ASN HA H 4.16 0.03 1 375 . 78 ASN CA C 53.39 0.50 1 376 . 78 ASN CB C 36.64 0.50 1 377 . 78 ASN N N 120.21 0.25 1 378 . 79 ILE H H 9.28 0.03 1 379 . 79 ILE HA H 4.33 0.03 1 380 . 79 ILE CA C 60.21 0.50 1 381 . 79 ILE CB C 41.60 0.50 1 382 . 79 ILE N N 121.31 0.25 1 383 . 80 MET H H 7.77 0.03 1 384 . 80 MET HA H 4.90 0.03 1 385 . 80 MET CA C 54.09 0.50 1 386 . 80 MET CB C 31.68 0.50 1 387 . 80 MET N N 123.25 0.25 1 388 . 81 CYS H H 8.66 0.03 1 389 . 81 CYS HA H 4.55 0.03 1 390 . 81 CYS CA C 55.84 0.50 1 391 . 81 CYS CB C 37.54 0.50 1 392 . 81 CYS N N 121.83 0.25 1 393 . 82 SER H H 8.10 0.03 1 394 . 82 SER HA H 3.82 0.03 1 395 . 82 SER N N 112.28 0.25 1 396 . 83 LYS CA C 56.09 0.50 1 397 . 83 LYS CB C 29.73 0.50 1 398 . 84 PHE H H 8.33 0.03 1 399 . 84 PHE HA H 5.65 0.03 1 400 . 84 PHE CA C 53.64 0.50 1 401 . 84 PHE CB C 37.48 0.50 1 402 . 84 PHE N N 121.77 0.25 1 403 . 85 LEU H H 7.11 0.03 1 404 . 85 LEU HA H 5.71 0.03 1 405 . 85 LEU CA C 52.87 0.50 1 406 . 85 LEU CB C 43.53 0.50 1 407 . 85 LEU N N 113.86 0.25 1 408 . 86 ASP H H 7.50 0.03 1 409 . 86 ASP HA H 4.86 0.03 1 410 . 86 ASP CA C 52.15 0.50 1 411 . 86 ASP CB C 41.83 0.50 1 412 . 86 ASP N N 119.49 0.25 1 413 . 87 ASP H H 7.90 0.03 1 414 . 87 ASP HA H 4.47 0.03 1 415 . 87 ASP CA C 55.36 0.50 1 416 . 87 ASP CB C 40.59 0.50 1 417 . 87 ASP N N 114.47 0.25 1 418 . 88 ASN H H 7.21 0.03 1 419 . 88 ASN HA H 4.98 0.03 1 420 . 88 ASN CA C 51.62 0.50 1 421 . 88 ASN CB C 39.66 0.50 1 422 . 88 ASN N N 115.70 0.25 1 423 . 89 ILE H H 9.22 0.03 1 424 . 89 ILE HA H 5.10 0.03 1 425 . 89 ILE CA C 61.16 0.50 1 426 . 89 ILE CB C 38.70 0.50 1 427 . 89 ILE N N 121.32 0.25 1 428 . 90 ASP H H 8.46 0.03 1 429 . 90 ASP HA H 4.20 0.03 1 430 . 90 ASP CA C 58.80 0.50 1 431 . 90 ASP CB C 38.65 0.50 1 432 . 90 ASP N N 124.68 0.25 1 433 . 91 ASP H H 8.55 0.03 1 434 . 91 ASP HA H 5.35 0.03 1 435 . 91 ASP CA C 55.58 0.50 1 436 . 91 ASP CB C 37.73 0.50 1 437 . 91 ASP N N 120.88 0.25 1 438 . 92 ASP H H 10.19 0.03 1 439 . 92 ASP HA H 4.61 0.03 1 440 . 92 ASP CA C 57.60 0.50 1 441 . 92 ASP CB C 38.37 0.50 1 442 . 92 ASP N N 125.59 0.25 1 443 . 93 ILE H H 8.95 0.03 1 444 . 93 ILE HA H 3.33 0.03 1 445 . 93 ILE CA C 65.64 0.50 1 446 . 93 ILE CB C 38.06 0.50 1 447 . 93 ILE N N 117.92 0.25 1 448 . 94 ALA H H 7.74 0.03 1 449 . 94 ALA HA H 3.82 0.03 1 450 . 94 ALA CA C 55.28 0.50 1 451 . 94 ALA CB C 17.68 0.50 1 452 . 94 ALA N N 121.18 0.25 1 453 . 95 CYS H H 8.17 0.03 1 454 . 95 CYS HA H 4.97 0.03 1 455 . 95 CYS CA C 55.62 0.50 1 456 . 95 CYS CB C 35.20 0.50 1 457 . 95 CYS N N 115.67 0.25 1 458 . 96 ALA H H 8.76 0.03 1 459 . 96 ALA HA H 3.82 0.03 1 460 . 96 ALA CA C 55.76 0.50 1 461 . 96 ALA CB C 17.27 0.50 1 462 . 96 ALA N N 124.62 0.25 1 463 . 97 LYS H H 7.91 0.03 1 464 . 97 LYS HA H 3.57 0.03 1 465 . 97 LYS CA C 59.87 0.50 1 466 . 97 LYS CB C 33.35 0.50 1 467 . 97 LYS N N 113.34 0.25 1 468 . 98 ARG H H 7.21 0.03 1 469 . 98 ARG HA H 4.14 0.03 1 470 . 98 ARG CA C 57.77 0.50 1 471 . 98 ARG CB C 29.14 0.50 1 472 . 98 ARG N N 117.93 0.25 1 473 . 99 VAL H H 8.17 0.03 1 474 . 99 VAL HA H 2.59 0.03 1 475 . 99 VAL CA C 65.16 0.50 1 476 . 99 VAL N N 123.05 0.25 1 477 . 100 VAL H H 7.33 0.03 1 478 . 100 VAL HA H 3.57 0.03 1 479 . 100 VAL CA C 62.82 0.50 1 480 . 100 VAL CB C 32.51 0.50 1 481 . 100 VAL N N 113.08 0.25 1 482 . 101 LYS H H 7.06 0.03 1 483 . 101 LYS HA H 3.67 0.03 1 484 . 101 LYS CA C 57.01 0.50 1 485 . 101 LYS CB C 32.51 0.50 1 486 . 101 LYS N N 116.64 0.25 1 487 . 102 ASP H H 7.39 0.03 1 488 . 102 ASP HA H 4.82 0.03 1 489 . 102 ASP CA C 54.07 0.50 1 490 . 102 ASP CB C 40.25 0.50 1 491 . 102 ASP N N 121.36 0.25 1 492 . 103 PRO HA H 4.29 0.03 1 493 . 103 PRO CA C 65.67 0.50 1 494 . 103 PRO CB C 32.20 0.50 1 495 . 104 ASN H H 8.45 0.03 1 496 . 104 ASN HA H 4.61 0.03 1 497 . 104 ASN CA C 53.66 0.50 1 498 . 104 ASN CB C 37.86 0.50 1 499 . 104 ASN N N 112.78 0.25 1 500 . 105 GLY H H 8.36 0.03 1 501 . 105 GLY HA2 H 4.02 0.03 1 502 . 105 GLY HA3 H 4.29 0.03 1 503 . 105 GLY CA C 46.65 0.50 1 504 . 105 GLY N N 109.84 0.25 1 505 . 106 MET H H 7.41 0.03 1 506 . 106 MET HA H 3.69 0.03 1 507 . 106 MET CA C 57.60 0.50 1 508 . 106 MET CB C 30.57 0.50 1 509 . 106 MET N N 122.60 0.25 1 510 . 107 SER H H 7.90 0.03 1 511 . 107 SER HA H 4.37 0.03 1 512 . 107 SER CA C 60.82 0.50 1 513 . 107 SER CB C 62.10 0.50 1 514 . 107 SER N N 112.74 0.25 1 515 . 108 ALA H H 6.76 0.03 1 516 . 108 ALA HA H 3.82 0.03 1 517 . 108 ALA CA C 53.87 0.50 1 518 . 108 ALA CB C 18.95 0.50 1 519 . 108 ALA N N 121.17 0.25 1 520 . 109 TRP H H 8.05 0.03 1 521 . 109 TRP HA H 4.67 0.03 1 522 . 109 TRP CA C 59.96 0.50 1 523 . 109 TRP CB C 28.18 0.50 1 524 . 109 TRP N N 118.28 0.25 1 525 . 110 VAL H H 9.00 0.03 1 526 . 110 VAL HA H 3.84 0.03 1 527 . 110 VAL CA C 65.77 0.50 1 528 . 110 VAL CB C 31.33 0.50 1 529 . 110 VAL N N 127.25 0.25 1 530 . 111 ALA H H 8.24 0.03 1 531 . 111 ALA HA H 4.39 0.03 1 532 . 111 ALA CA C 54.91 0.50 1 533 . 111 ALA CB C 18.70 0.50 1 534 . 111 ALA N N 119.31 0.25 1 535 . 112 TRP H H 7.63 0.03 1 536 . 112 TRP HA H 3.86 0.03 1 537 . 112 TRP CA C 61.39 0.50 1 538 . 112 TRP CB C 28.21 0.50 1 539 . 112 TRP N N 116.56 0.25 1 540 . 113 VAL H H 7.97 0.03 1 541 . 113 VAL HA H 2.92 0.03 1 542 . 113 VAL CA C 66.53 0.50 1 543 . 113 VAL CB C 31.41 0.50 1 544 . 113 VAL N N 122.88 0.25 1 545 . 114 LYS H H 7.82 0.03 1 546 . 114 LYS HA H 3.75 0.03 1 547 . 114 LYS CA C 58.18 0.50 1 548 . 114 LYS CB C 33.52 0.50 1 549 . 114 LYS N N 113.93 0.25 1 550 . 115 HIS H H 7.39 0.03 1 551 . 115 HIS HA H 4.29 0.03 1 552 . 115 HIS CA C 55.70 0.50 1 553 . 115 HIS CB C 30.06 0.50 1 554 . 115 HIS N N 110.37 0.25 1 555 . 116 CYS H H 7.57 0.03 1 556 . 116 CYS HA H 4.33 0.03 1 557 . 116 CYS CA C 55.38 0.50 1 558 . 116 CYS CB C 45.67 0.50 1 559 . 116 CYS N N 115.20 0.25 1 560 . 117 LYS H H 6.79 0.03 1 561 . 117 LYS HA H 3.27 0.03 1 562 . 117 LYS CA C 57.77 0.50 1 563 . 117 LYS CB C 32.00 0.50 1 564 . 117 LYS N N 121.28 0.25 1 565 . 118 GLY H H 8.70 0.03 1 566 . 118 GLY HA2 H 3.71 0.03 1 567 . 118 GLY HA3 H 3.94 0.03 1 568 . 118 GLY CA C 45.56 0.50 1 569 . 118 GLY N N 114.30 0.25 1 570 . 119 LYS H H 7.29 0.03 1 571 . 119 LYS HA H 4.26 0.03 1 572 . 119 LYS CA C 54.01 0.50 1 573 . 119 LYS CB C 33.26 0.50 1 574 . 119 LYS N N 119.38 0.25 1 575 . 120 ASP H H 8.53 0.03 1 576 . 120 ASP HA H 4.61 0.03 1 577 . 120 ASP CA C 53.48 0.50 1 578 . 120 ASP CB C 39.58 0.50 1 579 . 120 ASP N N 119.08 0.25 1 580 . 121 LEU H H 8.80 0.03 1 581 . 121 LEU HA H 4.69 0.03 1 582 . 121 LEU CA C 53.44 0.50 1 583 . 121 LEU CB C 41.12 0.50 1 584 . 121 LEU N N 129.50 0.25 1 585 . 122 SER H H 8.77 0.03 1 586 . 122 SER HA H 4.12 0.03 1 587 . 122 SER CA C 62.32 0.50 1 588 . 122 SER CB C 60.70 0.50 1 589 . 122 SER N N 119.05 0.25 1 590 . 123 LYS H H 8.72 0.03 1 591 . 123 LYS HA H 4.74 0.03 1 592 . 123 LYS CA C 54.90 0.50 1 593 . 123 LYS CB C 32.17 0.50 1 594 . 123 LYS N N 119.24 0.25 1 595 . 124 TYR H H 7.68 0.03 1 596 . 124 TYR HA H 4.41 0.03 1 597 . 124 TYR CA C 60.88 0.50 1 598 . 124 TYR CB C 40.00 0.50 1 599 . 124 TYR N N 124.60 0.25 1 600 . 125 LEU H H 9.01 0.03 1 601 . 125 LEU HA H 4.51 0.03 1 602 . 125 LEU CA C 52.49 0.50 1 603 . 125 LEU CB C 40.85 0.50 1 604 . 125 LEU N N 114.63 0.25 1 605 . 126 ALA H H 7.40 0.03 1 606 . 126 ALA HA H 4.10 0.03 1 607 . 126 ALA CA C 55.59 0.50 1 608 . 126 ALA CB C 18.60 0.50 1 609 . 126 ALA N N 124.86 0.25 1 610 . 127 SER H H 8.57 0.03 1 611 . 127 SER HA H 4.34 0.03 1 612 . 127 SER CA C 59.41 0.50 1 613 . 127 SER CB C 62.48 0.50 1 614 . 127 SER N N 111.11 0.25 1 615 . 128 CYS H H 7.75 0.03 1 616 . 128 CYS HA H 4.71 0.03 1 617 . 128 CYS CA C 51.71 0.50 1 618 . 128 CYS CB C 34.70 0.50 1 619 . 128 CYS N N 117.31 0.25 1 620 . 129 ASN H H 8.32 0.03 1 621 . 129 ASN HA H 4.57 0.03 1 622 . 129 ASN CA C 53.98 0.50 1 623 . 129 ASN CB C 37.48 0.50 1 624 . 129 ASN N N 118.96 0.25 1 625 . 130 LEU H H 7.87 0.03 1 626 . 130 LEU HA H 4.14 0.03 1 627 . 130 LEU CA C 56.24 0.50 1 628 . 130 LEU CB C 44.40 0.50 1 629 . 130 LEU N N 126.03 0.25 1 stop_ save_