data_144 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Two-dimensional 1H Nuclear Magnetic Resonance Study of Pike pI 5.0 Parvalbumin (Esox lucius) Sequential Resonance Assignments and Folding of the Polypeptide Chain ; _BMRB_accession_number 144 _BMRB_flat_file_name bmr144.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Padilla Andre . . 2 Cave Adrien . . 3 Parello Joseph . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 555 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Padilla, Andre, Cave, Adrien, Parello, Joseph, "Two-dimensional 1H Nuclear Magnetic Resonance Study of Pike pI 5.0 Parvalbumin (Esox lucius) Sequential Resonance Assignments and Folding of the Polypeptide Chain," J. Mol. Biol. 204, 995-1017 (1988). ; _Citation_title ; Two-dimensional 1H Nuclear Magnetic Resonance Study of Pike pI 5.0 Parvalbumin (Esox lucius) Sequential Resonance Assignments and Folding of the Polypeptide Chain ; _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 Padilla Andre . . 2 Cave Adrien . . 3 Parello Joseph . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 204 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 995 _Page_last 1017 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_parvalbumin _Saveframe_category molecular_system _Mol_system_name parvalbumin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label parvalbumin $parvalbumin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_parvalbumin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common parvalbumin _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; XAKDLLKADDIKKALDAVKA EGSFNHKKFFALVGLKAMSA NDVKKVFKAIDADASGFIEE EELKFVLKSFAADGRDLTDA ETKAFLKAADKDGDGKIGID EFETLVHEA ; loop_ _Residue_seq_code _Residue_label 1 AYA 2 ALA 3 LYS 4 ASP 5 LEU 6 LEU 7 LYS 8 ALA 9 ASP 10 ASP 11 ILE 12 LYS 13 LYS 14 ALA 15 LEU 16 ASP 17 ALA 18 VAL 19 LYS 20 ALA 21 GLU 22 GLY 23 SER 24 PHE 25 ASN 26 HIS 27 LYS 28 LYS 29 PHE 30 PHE 31 ALA 32 LEU 33 VAL 34 GLY 35 LEU 36 LYS 37 ALA 38 MET 39 SER 40 ALA 41 ASN 42 ASP 43 VAL 44 LYS 45 LYS 46 VAL 47 PHE 48 LYS 49 ALA 50 ILE 51 ASP 52 ALA 53 ASP 54 ALA 55 SER 56 GLY 57 PHE 58 ILE 59 GLU 60 GLU 61 GLU 62 GLU 63 LEU 64 LYS 65 PHE 66 VAL 67 LEU 68 LYS 69 SER 70 PHE 71 ALA 72 ALA 73 ASP 74 GLY 75 ARG 76 ASP 77 LEU 78 THR 79 ASP 80 ALA 81 GLU 82 THR 83 LYS 84 ALA 85 PHE 86 LEU 87 LYS 88 ALA 89 ALA 90 ASP 91 LYS 92 ASP 93 GLY 94 ASP 95 GLY 96 LYS 97 ILE 98 GLY 99 ILE 100 ASP 101 GLU 102 PHE 103 GLU 104 THR 105 LEU 106 VAL 107 HIS 108 GLU 109 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 3471 parvalbumin 99.08 108 100.00 100.00 2.53e-63 BMRB 3472 parvalbumin 99.08 109 100.00 100.00 2.61e-63 PDB 1PVA "Comparison Between The Crystal And The Solution Structures Of The Ef Hand Parvalbumin (alpha Component From Pike Muscle)" 99.08 110 100.00 100.00 3.01e-63 PDB 2PAS "Comparison Between The Crystal And The Solution Structures Of The Ef Hand Parvalbumin" 99.08 110 100.00 100.00 3.01e-63 PDB 3PAT "Comparison Between The Crystal And The Solution Structures Of The Ef Hand Parvalbumin" 99.08 110 100.00 100.00 3.01e-63 REF XP_010870996 "PREDICTED: parvalbumin alpha [Esox lucius]" 99.08 110 97.22 100.00 4.52e-61 SP P02628 "RecName: Full=Parvalbumin alpha; AltName: Full=Parvalbumin III; AltName: Full=Parvalbumin pI 5.0; AltName: Full=Parvalbumin-3" 99.08 108 100.00 100.00 2.53e-63 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_AYA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-ACETYLALANINE _BMRB_code AYA _PDB_code AYA _Standard_residue_derivative . _Molecular_mass 131.130 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CT CT C . 0 . ? OT OT O . 0 . ? CM CM C . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HM1 HM1 H . 0 . ? HM2 HM2 H . 0 . ? HM3 HM3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CT ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB CT OT ? ? SING CT CM ? ? SING CM HM1 ? ? SING CM HM2 ? ? SING CM HM3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $parvalbumin pike 8010 Eukaryota Metazoa Esox lucius generic 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 $parvalbumin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 . n/a temperature 335 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name parvalbumin _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 AYA HM1 H 1.95 . 1 2 . 1 AYA HM2 H 1.95 . 1 3 . 1 AYA HM3 H 1.95 . 1 4 . 1 AYA H H 8.16 . 1 5 . 1 AYA HA H 4.19 . 1 6 . 1 AYA HB1 H 1.39 . 1 7 . 1 AYA HB2 H 1.39 . 1 8 . 1 AYA HB3 H 1.39 . 1 9 . 2 ALA H H 8.45 . 1 10 . 2 ALA HA H 4.17 . 1 11 . 2 ALA HB H 1.02 . 1 12 . 3 LYS H H 7.61 . 1 13 . 3 LYS HA H 4.05 . 1 14 . 3 LYS HB2 H 1.94 . 1 15 . 3 LYS HB3 H 1.94 . 1 16 . 4 ASP H H 7.84 . 1 17 . 4 ASP HA H 4.65 . 1 18 . 4 ASP HB2 H 2.8 . 2 19 . 4 ASP HB3 H 2.61 . 2 20 . 5 LEU H H 7.61 . 1 21 . 5 LEU HA H 4.36 . 1 22 . 5 LEU HB2 H 1.61 . 2 23 . 5 LEU HB3 H 1.75 . 2 24 . 5 LEU HG H 1.67 . 1 25 . 5 LEU HD1 H .86 . 2 26 . 5 LEU HD2 H .87 . 2 27 . 6 LEU H H 7.33 . 1 28 . 6 LEU HA H 4.7 . 1 29 . 6 LEU HB2 H 1.72 . 1 30 . 6 LEU HB3 H 1.72 . 1 31 . 6 LEU HG H 1.71 . 1 32 . 6 LEU HD1 H 1.01 . 2 33 . 6 LEU HD2 H 1.06 . 2 34 . 7 LYS H H 8.58 . 1 35 . 7 LYS HA H 4.44 . 1 36 . 7 LYS HB2 H 1.9 . 1 37 . 7 LYS HB3 H 1.9 . 1 38 . 8 ALA H H 8.97 . 1 39 . 8 ALA HA H 4.08 . 1 40 . 8 ALA HB H 1.57 . 1 41 . 9 ASP H H 8.85 . 1 42 . 9 ASP HA H 4.41 . 1 43 . 9 ASP HB2 H 2.55 . 2 44 . 9 ASP HB3 H 2.72 . 2 45 . 10 ASP H H 7.05 . 1 46 . 10 ASP HA H 4.51 . 1 47 . 10 ASP HB2 H 2.91 . 2 48 . 10 ASP HB3 H 3.03 . 2 49 . 11 ILE H H 7.84 . 1 50 . 11 ILE HA H 3.6 . 1 51 . 11 ILE HB H 2.03 . 1 52 . 11 ILE HG12 H .95 . 2 53 . 11 ILE HG13 H 1.91 . 2 54 . 11 ILE HG2 H 1.08 . 1 55 . 11 ILE HD1 H 1.15 . 1 56 . 12 LYS H H 7.83 . 1 57 . 12 LYS HA H 3.96 . 1 58 . 12 LYS HB2 H 1.97 . 1 59 . 12 LYS HB3 H 1.97 . 1 60 . 13 LYS H H 7.58 . 1 61 . 13 LYS HA H 4.09 . 1 62 . 13 LYS HB2 H 1.87 . 2 63 . 13 LYS HB3 H 2.02 . 2 64 . 14 ALA H H 8.23 . 1 65 . 14 ALA HA H 3.95 . 1 66 . 14 ALA HB H 1.08 . 1 67 . 15 LEU H H 8.58 . 1 68 . 15 LEU HA H 4.15 . 1 69 . 15 LEU HB2 H 2.01 . 1 70 . 15 LEU HB3 H 2.01 . 1 71 . 15 LEU HG H 2.01 . 1 72 . 15 LEU HD1 H .97 . 2 73 . 15 LEU HD2 H 1.02 . 2 74 . 16 ASP H H 8.27 . 1 75 . 16 ASP HA H 4.43 . 1 76 . 16 ASP HB2 H 2.64 . 2 77 . 16 ASP HB3 H 2.86 . 2 78 . 17 ALA H H 7.58 . 1 79 . 17 ALA HA H 4.24 . 1 80 . 17 ALA HB H 1.52 . 1 81 . 18 VAL H H 7.25 . 1 82 . 18 VAL HA H 5.03 . 1 83 . 18 VAL HB H 2.47 . 1 84 . 18 VAL HG1 H .91 . 2 85 . 18 VAL HG2 H 1.18 . 2 86 . 19 LYS H H 7.07 . 1 87 . 19 LYS HA H 4.02 . 1 88 . 19 LYS HB2 H 1.91 . 2 89 . 19 LYS HB3 H 2.07 . 2 90 . 20 ALA H H 7.95 . 1 91 . 20 ALA HA H 4.35 . 1 92 . 20 ALA HB H 1.36 . 1 93 . 21 GLU H H 9.03 . 1 94 . 21 GLU HA H 3.79 . 1 95 . 21 GLU HB2 H 1.98 . 2 96 . 21 GLU HB3 H 2.08 . 2 97 . 21 GLU HG2 H 2.42 . 1 98 . 21 GLU HG3 H 2.42 . 1 99 . 22 GLY H H 7.94 . 1 100 . 22 GLY HA2 H 3.71 . 2 101 . 22 GLY HA3 H 4.47 . 2 102 . 23 SER H H 7.98 . 1 103 . 23 SER HA H 4.51 . 1 104 . 23 SER HB2 H 3.75 . 2 105 . 23 SER HB3 H 4.15 . 2 106 . 24 PHE H H 9.13 . 1 107 . 24 PHE HA H 3.76 . 1 108 . 24 PHE HB2 H 2.83 . 2 109 . 24 PHE HB3 H 2.93 . 2 110 . 24 PHE HD1 H 7.01 . 1 111 . 24 PHE HD2 H 7.01 . 1 112 . 24 PHE HE1 H 6.3 . 1 113 . 24 PHE HE2 H 6.3 . 1 114 . 24 PHE HZ H 6.3 . 1 115 . 25 ASN H H 5.32 . 1 116 . 25 ASN HA H 4.5 . 1 117 . 25 ASN HB2 H 2.29 . 2 118 . 25 ASN HB3 H 2.54 . 2 119 . 26 HIS HA H 3.24 . 1 120 . 26 HIS HB2 H 2.02 . 2 121 . 26 HIS HB3 H 2.24 . 2 122 . 26 HIS HD2 H 6.69 . 1 123 . 26 HIS HE1 H 7.68 . 1 124 . 27 LYS H H 6.88 . 1 125 . 27 LYS HA H 3.75 . 1 126 . 27 LYS HB2 H 1.57 . 2 127 . 27 LYS HB3 H 1.65 . 2 128 . 27 LYS HG2 H .97 . 2 129 . 27 LYS HG3 H 1.15 . 2 130 . 28 LYS H H 7.11 . 1 131 . 28 LYS HA H 3.95 . 1 132 . 28 LYS HB2 H 1.54 . 2 133 . 28 LYS HB3 H 1.66 . 2 134 . 28 LYS HG2 H 1.25 . 1 135 . 28 LYS HG3 H 1.25 . 1 136 . 29 PHE H H 7.91 . 1 137 . 29 PHE HA H 3.78 . 1 138 . 29 PHE HB2 H 2.32 . 2 139 . 29 PHE HB3 H 2.53 . 2 140 . 29 PHE HD1 H 6.7 . 1 141 . 29 PHE HD2 H 6.7 . 1 142 . 29 PHE HE1 H 6.58 . 1 143 . 29 PHE HE2 H 6.58 . 1 144 . 29 PHE HZ H 6.12 . 1 145 . 30 PHE H H 8.48 . 1 146 . 30 PHE HA H 4.29 . 1 147 . 30 PHE HB2 H 3.35 . 2 148 . 30 PHE HB3 H 3.02 . 2 149 . 30 PHE HD1 H 7.38 . 1 150 . 30 PHE HD2 H 7.38 . 1 151 . 30 PHE HE1 H 7.31 . 1 152 . 30 PHE HE2 H 7.31 . 1 153 . 30 PHE HZ H 7.31 . 1 154 . 31 ALA H H 7.6 . 1 155 . 31 ALA HA H 4.16 . 1 156 . 31 ALA HB H 1.53 . 1 157 . 32 LEU H H 7.99 . 1 158 . 32 LEU HA H 4.02 . 1 159 . 32 LEU HB2 H 1.67 . 1 160 . 32 LEU HB3 H 1.67 . 1 161 . 32 LEU HG H 1.83 . 1 162 . 32 LEU HD1 H .78 . 2 163 . 32 LEU HD2 H .82 . 2 164 . 33 VAL H H 7.83 . 1 165 . 33 VAL HA H 3.71 . 1 166 . 33 VAL HB H 1.29 . 1 167 . 33 VAL HG1 H .65 . 2 168 . 33 VAL HG2 H .78 . 2 169 . 34 GLY H H 7.01 . 1 170 . 34 GLY HA2 H 3.87 . 2 171 . 34 GLY HA3 H 4.37 . 2 172 . 35 LEU H H 7.3 . 1 173 . 35 LEU HA H 4.16 . 1 174 . 35 LEU HB2 H 1.51 . 1 175 . 35 LEU HB3 H 1.51 . 1 176 . 35 LEU HG H 1.77 . 1 177 . 35 LEU HD1 H .94 . 2 178 . 35 LEU HD2 H .98 . 2 179 . 36 LYS H H 7.6 . 1 180 . 36 LYS HA H 3.91 . 1 181 . 36 LYS HB2 H 1.78 . 2 182 . 36 LYS HB3 H 1.85 . 2 183 . 37 ALA H H 7.1 . 1 184 . 37 ALA HA H 4.46 . 1 185 . 37 ALA HB H 1.43 . 1 186 . 38 MET H H 7.22 . 1 187 . 38 MET HA H 4.53 . 1 188 . 38 MET HB2 H 2.24 . 1 189 . 38 MET HB3 H 2.24 . 1 190 . 38 MET HG2 H 2.75 . 2 191 . 38 MET HG3 H 2.88 . 2 192 . 38 MET HE H 2.08 . 1 193 . 39 SER H H 8.62 . 1 194 . 39 SER HA H 4.47 . 1 195 . 39 SER HB2 H 4.12 . 2 196 . 39 SER HB3 H 4.35 . 2 197 . 40 ALA H H 8.98 . 1 198 . 40 ALA HA H 4.25 . 1 199 . 40 ALA HB H 1.51 . 1 200 . 41 ASN H H 8.64 . 1 201 . 41 ASN HA H 4.35 . 1 202 . 41 ASN HB2 H 2.56 . 2 203 . 41 ASN HB3 H 2.66 . 2 204 . 42 ASP H H 7.65 . 1 205 . 42 ASP HA H 4.76 . 1 206 . 42 ASP HB2 H 2.88 . 2 207 . 42 ASP HB3 H 2.98 . 2 208 . 43 VAL H H 8.41 . 1 209 . 43 VAL HA H 3.62 . 1 210 . 43 VAL HB H 2.35 . 1 211 . 43 VAL HG1 H 1.01 . 1 212 . 43 VAL HG2 H 1.01 . 1 213 . 44 LYS H H 7.87 . 1 214 . 44 LYS HA H 3.98 . 1 215 . 44 LYS HB2 H 2 . 1 216 . 44 LYS HB3 H 2 . 1 217 . 44 LYS HG2 H 1.7 . 1 218 . 44 LYS HG3 H 1.7 . 1 219 . 45 LYS H H 7.42 . 1 220 . 45 LYS HA H 4.01 . 1 221 . 45 LYS HB2 H 2.17 . 1 222 . 45 LYS HB3 H 2.17 . 1 223 . 45 LYS HG2 H 1.83 . 2 224 . 45 LYS HG3 H 1.89 . 2 225 . 46 VAL H H 7.72 . 1 226 . 46 VAL HA H 3.5 . 1 227 . 46 VAL HB H 2.5 . 1 228 . 46 VAL HG1 H 1.11 . 1 229 . 46 VAL HG2 H 1.11 . 1 230 . 47 PHE H H 8.12 . 1 231 . 47 PHE HA H 3.15 . 1 232 . 47 PHE HB2 H 2.61 . 2 233 . 47 PHE HB3 H 3.28 . 2 234 . 47 PHE HD1 H 6.56 . 1 235 . 47 PHE HD2 H 6.56 . 1 236 . 47 PHE HE1 H 6.87 . 1 237 . 47 PHE HE2 H 6.87 . 1 238 . 47 PHE HZ H 7.2 . 1 239 . 48 LYS H H 7.91 . 1 240 . 48 LYS HA H 3.89 . 1 241 . 48 LYS HB2 H 1.9 . 2 242 . 48 LYS HB3 H 1.92 . 2 243 . 48 LYS HG2 H 1.77 . 1 244 . 48 LYS HG3 H 1.77 . 1 245 . 49 ALA H H 7.28 . 1 246 . 49 ALA HA H 4.01 . 1 247 . 49 ALA HB H 1.4 . 1 248 . 50 ILE H H 7.18 . 1 249 . 50 ILE HA H 3.67 . 1 250 . 50 ILE HB H 1.3 . 1 251 . 50 ILE HG2 H .78 . 1 252 . 51 ASP H H 7.39 . 1 253 . 51 ASP HA H 4.55 . 1 254 . 51 ASP HB2 H 1.45 . 2 255 . 51 ASP HB3 H 2.44 . 2 256 . 52 ALA H H 7.71 . 1 257 . 52 ALA HA H 4.01 . 1 258 . 52 ALA HB H 1.49 . 1 259 . 53 ASP H H 8.17 . 1 260 . 53 ASP HA H 4.59 . 1 261 . 53 ASP HB2 H 2.66 . 2 262 . 53 ASP HB3 H 3.09 . 2 263 . 54 ALA H H 8.05 . 1 264 . 54 ALA HA H 4 . 1 265 . 54 ALA HB H 1.42 . 1 266 . 55 SER H H 8.83 . 1 267 . 55 SER HA H 4.31 . 1 268 . 55 SER HB2 H 4.31 . 1 269 . 55 SER HB3 H 4.31 . 1 270 . 56 GLY H H 10.33 . 1 271 . 56 GLY HA2 H 3.38 . 2 272 . 56 GLY HA3 H 4.16 . 2 273 . 57 PHE H H 7.97 . 1 274 . 57 PHE HA H 5.24 . 1 275 . 57 PHE HB2 H 2.49 . 2 276 . 57 PHE HB3 H 2.87 . 2 277 . 57 PHE HD1 H 7.02 . 1 278 . 57 PHE HD2 H 7.02 . 1 279 . 57 PHE HE1 H 7.44 . 1 280 . 57 PHE HE2 H 7.44 . 1 281 . 57 PHE HZ H 7.42 . 1 282 . 58 ILE H H 9.71 . 1 283 . 58 ILE HA H 4.75 . 1 284 . 58 ILE HB H 1.69 . 1 285 . 58 ILE HG12 H .17 . 2 286 . 58 ILE HG13 H .9 . 2 287 . 58 ILE HG2 H .73 . 1 288 . 58 ILE HD1 H .19 . 1 289 . 59 GLU H H 7.82 . 1 290 . 59 GLU HA H 4.55 . 1 291 . 59 GLU HB2 H 2.03 . 2 292 . 59 GLU HB3 H 2.05 . 2 293 . 59 GLU HG2 H 2.55 . 1 294 . 59 GLU HG3 H 2.55 . 1 295 . 60 GLU H H 9.23 . 1 296 . 60 GLU HA H 3.54 . 1 297 . 60 GLU HB2 H 2 . 2 298 . 60 GLU HB3 H 2.09 . 2 299 . 60 GLU HG2 H 2.3 . 1 300 . 60 GLU HG3 H 2.3 . 1 301 . 61 GLU H H 8.8 . 1 302 . 61 GLU HA H 3.91 . 1 303 . 61 GLU HB2 H 2.02 . 1 304 . 61 GLU HB3 H 2.02 . 1 305 . 61 GLU HG2 H 2.31 . 1 306 . 61 GLU HG3 H 2.31 . 1 307 . 62 GLU H H 6.95 . 1 308 . 62 GLU HA H 4.16 . 1 309 . 62 GLU HB2 H 2.51 . 2 310 . 62 GLU HB3 H 2.55 . 2 311 . 62 GLU HG2 H 2.06 . 1 312 . 62 GLU HG3 H 2.06 . 1 313 . 63 LEU H H 7.75 . 1 314 . 63 LEU HA H 3.67 . 1 315 . 63 LEU HB2 H 1.47 . 2 316 . 63 LEU HB3 H 1.6 . 2 317 . 63 LEU HG H 1.4 . 1 318 . 63 LEU HD1 H .3 . 2 319 . 63 LEU HD2 H .33 . 2 320 . 64 LYS H H 7.17 . 1 321 . 64 LYS HA H 3.86 . 1 322 . 64 LYS HB2 H 1.24 . 2 323 . 64 LYS HB3 H 1.53 . 2 324 . 64 LYS HG2 H .83 . 1 325 . 64 LYS HG3 H .83 . 1 326 . 65 PHE H H 6.96 . 1 327 . 65 PHE HA H 5.13 . 1 328 . 65 PHE HB2 H 2.87 . 2 329 . 65 PHE HB3 H 3.65 . 2 330 . 65 PHE HD1 H 7.34 . 1 331 . 65 PHE HD2 H 7.34 . 1 332 . 65 PHE HE1 H 7.42 . 1 333 . 65 PHE HE2 H 7.42 . 1 334 . 65 PHE HZ H 7.3 . 1 335 . 66 VAL H H 7.71 . 1 336 . 66 VAL HA H 3.98 . 1 337 . 66 VAL HB H 2.51 . 1 338 . 66 VAL HG1 H .91 . 2 339 . 66 VAL HG2 H 1.27 . 2 340 . 67 LEU H H 9.49 . 1 341 . 67 LEU HA H 4.27 . 1 342 . 67 LEU HB2 H 2.04 . 1 343 . 67 LEU HB3 H 2.04 . 1 344 . 67 LEU HG H 1.52 . 1 345 . 67 LEU HD1 H .27 . 2 346 . 67 LEU HD2 H .76 . 2 347 . 68 LYS H H 7.8 . 1 348 . 68 LYS HA H 4.83 . 1 349 . 68 LYS HB2 H 2.05 . 1 350 . 68 LYS HB3 H 2.05 . 1 351 . 68 LYS HG2 H 1.53 . 1 352 . 68 LYS HG3 H 1.53 . 1 353 . 69 SER H H 7.7 . 1 354 . 69 SER HA H 4.35 . 1 355 . 69 SER HB2 H 3.36 . 2 356 . 69 SER HB3 H 3.71 . 2 357 . 70 PHE H H 7.74 . 1 358 . 70 PHE HA H 4.32 . 1 359 . 70 PHE HB2 H 3.19 . 2 360 . 70 PHE HB3 H 3.25 . 2 361 . 70 PHE HD1 H 7.46 . 1 362 . 70 PHE HD2 H 7.46 . 1 363 . 70 PHE HE1 H 7.28 . 1 364 . 70 PHE HE2 H 7.28 . 1 365 . 70 PHE HZ H 7.2 . 1 366 . 71 ALA H H 8.05 . 1 367 . 71 ALA HA H 4.51 . 1 368 . 71 ALA HB H 1.4 . 1 369 . 72 ALA H H 8.24 . 1 370 . 72 ALA HA H 4.24 . 1 371 . 72 ALA HB H 1.46 . 1 372 . 73 ASP H H 8.2 . 1 373 . 73 ASP HA H 4.63 . 1 374 . 73 ASP HB2 H 2.56 . 2 375 . 73 ASP HB3 H 2.83 . 2 376 . 74 GLY H H 7.85 . 1 377 . 74 GLY HA2 H 3.17 . 2 378 . 74 GLY HA3 H 3.97 . 2 379 . 75 ARG H H 8.04 . 1 380 . 75 ARG HA H 4.47 . 1 381 . 75 ARG HB2 H 1.96 . 1 382 . 75 ARG HB3 H 1.96 . 1 383 . 75 ARG HG2 H 1.28 . 1 384 . 75 ARG HG3 H 1.28 . 1 385 . 75 ARG HD2 H 3.17 . 2 386 . 75 ARG HD3 H 3.25 . 2 387 . 75 ARG HE H 6.9 . 1 388 . 76 ASP H H 8.27 . 1 389 . 76 ASP HA H 4.61 . 1 390 . 76 ASP HB2 H 2.45 . 2 391 . 76 ASP HB3 H 2.52 . 2 392 . 77 LEU H H 8.34 . 1 393 . 77 LEU HA H 4.44 . 1 394 . 77 LEU HB2 H 1.55 . 2 395 . 77 LEU HB3 H 1.82 . 2 396 . 77 LEU HG H 1.66 . 1 397 . 77 LEU HD1 H .12 . 2 398 . 77 LEU HD2 H .34 . 2 399 . 78 THR H H 9.58 . 1 400 . 78 THR HA H 4.46 . 1 401 . 78 THR HB H 4.8 . 1 402 . 78 THR HG2 H 1.37 . 1 403 . 79 ASP H H 9.17 . 1 404 . 79 ASP HA H 4.43 . 1 405 . 79 ASP HB2 H 2.69 . 1 406 . 79 ASP HB3 H 2.69 . 1 407 . 80 ALA H H 8.29 . 1 408 . 80 ALA HA H 4.16 . 1 409 . 80 ALA HB H 1.5 . 1 410 . 81 GLU H H 7.93 . 1 411 . 81 GLU HA H 4.18 . 1 412 . 81 GLU HB2 H 2.57 . 2 413 . 81 GLU HB3 H 2.59 . 2 414 . 81 GLU HG2 H 1.88 . 1 415 . 81 GLU HG3 H 1.88 . 1 416 . 82 THR H H 8.62 . 1 417 . 82 THR HA H 3.63 . 1 418 . 82 THR HB H 4.32 . 1 419 . 82 THR HG2 H 1.09 . 1 420 . 83 LYS H H 8.28 . 1 421 . 83 LYS HA H 3.94 . 1 422 . 83 LYS HB2 H 1.52 . 1 423 . 83 LYS HB3 H 1.52 . 1 424 . 84 ALA H H 7.83 . 1 425 . 84 ALA HA H 4.21 . 1 426 . 84 ALA HB H 1.66 . 1 427 . 85 PHE H H 7.95 . 1 428 . 85 PHE HA H 4.55 . 1 429 . 85 PHE HB2 H 3.52 . 2 430 . 85 PHE HB3 H 3.59 . 2 431 . 85 PHE HD1 H 7.21 . 1 432 . 85 PHE HD2 H 7.21 . 1 433 . 85 PHE HE1 H 7.17 . 1 434 . 85 PHE HE2 H 7.17 . 1 435 . 85 PHE HZ H 7.28 . 1 436 . 86 LEU H H 8.54 . 1 437 . 86 LEU HA H 3.7 . 1 438 . 86 LEU HB2 H 1.47 . 2 439 . 86 LEU HB3 H 1.86 . 2 440 . 86 LEU HG H 1.58 . 1 441 . 86 LEU HD1 H .71 . 2 442 . 86 LEU HD2 H .82 . 2 443 . 87 LYS H H 8.21 . 1 444 . 87 LYS HA H 4.05 . 1 445 . 87 LYS HB2 H 1.94 . 1 446 . 87 LYS HB3 H 1.94 . 1 447 . 88 ALA H H 7.47 . 1 448 . 88 ALA HA H 4.2 . 1 449 . 88 ALA HB H 1.51 . 1 450 . 89 ALA H H 7.79 . 1 451 . 89 ALA HA H 4.37 . 1 452 . 89 ALA HB H 1.38 . 1 453 . 90 ASP H H 8.33 . 1 454 . 90 ASP HA H 4.7 . 1 455 . 90 ASP HB2 H 2.33 . 2 456 . 90 ASP HB3 H 2.9 . 2 457 . 91 LYS H H 8.36 . 1 458 . 91 LYS HA H 4.23 . 1 459 . 91 LYS HB2 H 2 . 1 460 . 91 LYS HB3 H 2 . 1 461 . 91 LYS HG2 H 1.77 . 1 462 . 91 LYS HG3 H 1.77 . 1 463 . 92 ASP H H 8.5 . 1 464 . 92 ASP HA H 4.65 . 1 465 . 92 ASP HB2 H 2.6 . 2 466 . 92 ASP HB3 H 3.1 . 2 467 . 93 GLY H H 7.55 . 1 468 . 93 GLY HA2 H 3.83 . 2 469 . 93 GLY HA3 H 3.97 . 2 470 . 94 ASP H H 8.37 . 1 471 . 94 ASP HA H 4.49 . 1 472 . 94 ASP HB2 H 2.48 . 2 473 . 94 ASP HB3 H 2.89 . 2 474 . 95 GLY H H 10.16 . 1 475 . 95 GLY HA2 H 3.45 . 2 476 . 95 GLY HA3 H 4.07 . 2 477 . 96 LYS H H 7.95 . 1 478 . 96 LYS HA H 4.79 . 1 479 . 96 LYS HB2 H 1.55 . 1 480 . 96 LYS HB3 H 1.55 . 1 481 . 96 LYS HG2 H 1.06 . 1 482 . 96 LYS HG3 H 1.06 . 1 483 . 97 ILE H H 8.92 . 1 484 . 97 ILE HA H 5.12 . 1 485 . 97 ILE HB H 2.15 . 1 486 . 97 ILE HG12 H .86 . 2 487 . 97 ILE HG13 H 1.48 . 2 488 . 97 ILE HG2 H 1.26 . 1 489 . 97 ILE HD1 H .66 . 1 490 . 98 GLY H H 9.77 . 1 491 . 98 GLY HA2 H 4.16 . 2 492 . 98 GLY HA3 H 4.85 . 2 493 . 99 ILE H H 8.45 . 1 494 . 99 ILE HA H 3.07 . 1 495 . 99 ILE HB H .87 . 1 496 . 99 ILE HG12 H .82 . 1 497 . 99 ILE HG13 H .82 . 1 498 . 99 ILE HG2 H .73 . 1 499 . 99 ILE HD1 H .57 . 1 500 . 100 ASP H H 8.24 . 1 501 . 100 ASP HA H 4.41 . 1 502 . 100 ASP HB2 H 2.63 . 2 503 . 100 ASP HB3 H 2.76 . 2 504 . 101 GLU H H 7.59 . 1 505 . 101 GLU HA H 4.1 . 1 506 . 101 GLU HB2 H 2.67 . 2 507 . 101 GLU HB3 H 2.7 . 2 508 . 101 GLU HG2 H 2.41 . 2 509 . 101 GLU HG3 H 2.51 . 2 510 . 102 PHE H H 8.75 . 1 511 . 102 PHE HA H 4.12 . 1 512 . 102 PHE HB2 H 3.23 . 2 513 . 102 PHE HB3 H 3.26 . 2 514 . 102 PHE HD1 H 7.08 . 1 515 . 102 PHE HD2 H 7.08 . 1 516 . 102 PHE HE1 H 7.22 . 1 517 . 102 PHE HE2 H 7.22 . 1 518 . 102 PHE HZ H 6.97 . 1 519 . 103 GLU H H 8.58 . 1 520 . 103 GLU HA H 3.66 . 1 521 . 103 GLU HB2 H 2.15 . 2 522 . 103 GLU HB3 H 2.18 . 2 523 . 103 GLU HG2 H 2.46 . 1 524 . 103 GLU HG3 H 2.46 . 1 525 . 104 THR H H 7.92 . 1 526 . 104 THR HA H 3.96 . 1 527 . 104 THR HB H 4.26 . 1 528 . 104 THR HG2 H 1.31 . 1 529 . 105 LEU H H 7.69 . 1 530 . 105 LEU HA H 4.15 . 1 531 . 105 LEU HB2 H 1.8 . 2 532 . 105 LEU HB3 H 1.87 . 2 533 . 105 LEU HG H 1.72 . 1 534 . 105 LEU HD1 H .8 . 2 535 . 105 LEU HD2 H .82 . 2 536 . 106 VAL H H 7.62 . 1 537 . 106 VAL HA H 3.33 . 1 538 . 106 VAL HB H 1.66 . 1 539 . 106 VAL HG1 H .08 . 2 540 . 106 VAL HG2 H .27 . 2 541 . 107 HIS H H 7.58 . 1 542 . 107 HIS HA H 4.69 . 1 543 . 107 HIS HB2 H 3.25 . 2 544 . 107 HIS HB3 H 3.46 . 2 545 . 107 HIS HD2 H 7.47 . 1 546 . 107 HIS HE1 H 8.43 . 1 547 . 108 GLU H H 7.81 . 1 548 . 108 GLU HA H 4.28 . 1 549 . 108 GLU HB2 H 2.17 . 2 550 . 108 GLU HB3 H 2.19 . 2 551 . 108 GLU HG2 H 2.52 . 1 552 . 108 GLU HG3 H 2.52 . 1 553 . 109 ALA H H 7.71 . 1 554 . 109 ALA HA H 4.09 . 1 555 . 109 ALA HB H 1.48 . 1 stop_ save_