data_979 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B ; _BMRB_accession_number 979 _BMRB_flat_file_name bmr979.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Vendrell Josep . . 2 Wider Gerhard . . 3 Aviles Francesc X. . 4 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 482 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 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 ; Vendrell, Josep, Wider, Gerhard, Aviles, Francesc X., Wuthrich, Kurt, "Sequence Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B," Biochemistry 29, 7515-7522 (1990). ; _Citation_title ; Sequence Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B ; _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 Vendrell Josep . . 2 Wider Gerhard . . 3 Aviles Francesc X. . 4 Wuthrich Kurt . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7515 _Page_last 7522 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_carboxypeptidase_B _Saveframe_category molecular_system _Mol_system_name 'carboxypeptidase B' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'carboxypeptidase B' $carboxypeptidase_B stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_carboxypeptidase_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'carboxypeptidase B' _Name_variant 'globular activation domain' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; HHSGEHFEGEKVFRVNVEDE NDISELHELASTRQIDFWLP DSVTQIKPHSTVDFRVKAED ILAVEDFLEQNELQYEVLIN N ; loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 SER 4 GLY 5 GLU 6 HIS 7 PHE 8 GLU 9 GLY 10 GLU 11 LYS 12 VAL 13 PHE 14 ARG 15 VAL 16 ASN 17 VAL 18 GLU 19 ASP 20 GLU 21 ASN 22 ASP 23 ILE 24 SER 25 GLU 26 LEU 27 HIS 28 GLU 29 LEU 30 ALA 31 SER 32 THR 33 ARG 34 GLN 35 ILE 36 ASP 37 PHE 38 TRP 39 LEU 40 PRO 41 ASP 42 SER 43 VAL 44 THR 45 GLN 46 ILE 47 LYS 48 PRO 49 HIS 50 SER 51 THR 52 VAL 53 ASP 54 PHE 55 ARG 56 VAL 57 LYS 58 ALA 59 GLU 60 ASP 61 ILE 62 LEU 63 ALA 64 VAL 65 GLU 66 ASP 67 PHE 68 LEU 69 GLU 70 GLN 71 ASN 72 GLU 73 LEU 74 GLN 75 TYR 76 GLU 77 VAL 78 LEU 79 ILE 80 ASN 81 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 PDB 1NSA "Three-Dimensional Structure Of Porcine Procarboxypeptidase B: A Structural Basis Of Its Inactivity" 92.59 395 98.67 98.67 1.05e-41 PDB 1PBA "The Nmr Structure Of The Activation Domain Isolated From Porcine Procarboxypeptidase B" 100.00 81 98.77 98.77 3.82e-49 PDB 3GLJ "A Polymorph Of Carboxypeptidase B Zymogen Structure" 100.00 401 97.53 97.53 4.11e-46 EMBL CAB46991 "procarboxypeptidase B [Sus scrofa]" 100.00 416 97.53 97.53 1.87e-46 REF NP_999334 "carboxypeptidase B precursor [Sus scrofa]" 100.00 416 97.53 97.53 1.87e-46 SP P09955 "RecName: Full=Carboxypeptidase B; Flags: Precursor [Sus scrofa]" 100.00 416 97.53 97.53 1.87e-46 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 _Tissue $carboxypeptidase_B pig 9823 Eukaryota Metazoa Sus scrofa generic pancreas 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 $carboxypeptidase_B '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 6.5 . na temperature 288 . 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 'carboxypeptidase B' _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 HIS HA H 4.27 . 1 2 . 1 HIS HB2 H 3.23 . 2 3 . 1 HIS HB3 H 3.13 . 2 4 . 1 HIS HD1 H 7.25 . 3 5 . 1 HIS HD2 H 7.11 . 3 6 . 1 HIS HE1 H 7.5 . 3 7 . 1 HIS HE2 H 7.25 . 3 8 . 2 HIS HA H 4.27 . 1 9 . 2 HIS HB2 H 3.23 . 2 10 . 2 HIS HB3 H 3.13 . 2 11 . 2 HIS HD1 H 7.25 . 3 12 . 2 HIS HD2 H 7.11 . 3 13 . 2 HIS HE1 H 7.5 . 3 14 . 2 HIS HE2 H 7.25 . 3 15 . 3 SER HA H 4.28 . 1 16 . 3 SER HB2 H 3.85 . 2 17 . 3 SER HB3 H 3.72 . 2 18 . 4 GLY H H 8.5 . 1 19 . 4 GLY HA2 H 3.89 . 1 20 . 4 GLY HA3 H 3.89 . 1 21 . 5 GLU H H 8.04 . 1 22 . 5 GLU HA H 4.2 . 1 23 . 5 GLU HB2 H 1.79 . 1 24 . 5 GLU HB3 H 1.79 . 1 25 . 5 GLU HG2 H 2.07 . 2 26 . 5 GLU HG3 H 1.95 . 2 27 . 6 HIS H H 8.58 . 1 28 . 6 HIS HA H 4.71 . 1 29 . 6 HIS HB2 H 3.1 . 2 30 . 6 HIS HB3 H 2.93 . 2 31 . 6 HIS HD2 H 7.17 . 1 32 . 6 HIS HE1 H 7.72 . 1 33 . 7 PHE H H 8.71 . 1 34 . 7 PHE HA H 4.82 . 1 35 . 7 PHE HB2 H 3.3 . 2 36 . 7 PHE HB3 H 2.95 . 2 37 . 7 PHE HD1 H 7.243 . 1 38 . 7 PHE HD2 H 7.243 . 1 39 . 7 PHE HE1 H 7.243 . 1 40 . 7 PHE HE2 H 7.243 . 1 41 . 7 PHE HZ H 7.243 . 1 42 . 8 GLU H H 9.11 . 1 43 . 8 GLU HA H 4.19 . 1 44 . 8 GLU HB2 H 2.05 . 1 45 . 8 GLU HB3 H 2.05 . 1 46 . 8 GLU HG2 H 2.34 . 1 47 . 8 GLU HG3 H 2.34 . 1 48 . 9 GLY H H 9.25 . 1 49 . 9 GLY HA2 H 3.85 . 2 50 . 9 GLY HA3 H 4.18 . 2 51 . 10 GLU H H 7.64 . 1 52 . 10 GLU HA H 4.71 . 1 53 . 10 GLU HB2 H 1.95 . 1 54 . 10 GLU HB3 H 1.95 . 1 55 . 10 GLU HG2 H 2.57 . 2 56 . 10 GLU HG3 H 2.41 . 2 57 . 11 LYS H H 8.83 . 1 58 . 11 LYS HA H 4.67 . 1 59 . 11 LYS HB2 H 1.53 . 2 60 . 11 LYS HB3 H 1.33 . 2 61 . 11 LYS HG2 H 1.13 . 1 62 . 11 LYS HG3 H 1.13 . 1 63 . 11 LYS HD2 H 1.7 . 2 64 . 11 LYS HD3 H 1.53 . 2 65 . 11 LYS HE2 H 2.8 . 1 66 . 11 LYS HE3 H 2.8 . 1 67 . 12 VAL H H 8.75 . 1 68 . 12 VAL HA H 4.47 . 1 69 . 12 VAL HB H 1.85 . 1 70 . 12 VAL HG1 H .6 . 1 71 . 12 VAL HG2 H .6 . 1 72 . 13 PHE H H 8.83 . 1 73 . 13 PHE HA H 4.74 . 1 74 . 13 PHE HB2 H 1.94 . 2 75 . 13 PHE HB3 H 1.61 . 2 76 . 13 PHE HD1 H 6.74 . 1 77 . 13 PHE HD2 H 6.74 . 1 78 . 13 PHE HE1 H 6.86 . 1 79 . 13 PHE HE2 H 6.86 . 1 80 . 13 PHE HZ H 7.22 . 1 81 . 14 ARG H H 8.89 . 1 82 . 14 ARG HA H 5.69 . 1 83 . 14 ARG HB2 H 1.69 . 2 84 . 14 ARG HB3 H 1.65 . 2 85 . 14 ARG HG2 H 1.59 . 2 86 . 14 ARG HG3 H 1.53 . 2 87 . 14 ARG HD2 H 3.19 . 2 88 . 14 ARG HD3 H 2.98 . 2 89 . 14 ARG HE H 9.78 . 1 90 . 14 ARG HH11 H 6.7 . 1 91 . 14 ARG HH12 H 6.7 . 1 92 . 14 ARG HH21 H 6.7 . 1 93 . 14 ARG HH22 H 6.7 . 1 94 . 15 VAL H H 9.88 . 1 95 . 15 VAL HA H 4.95 . 1 96 . 15 VAL HB H 2.08 . 1 97 . 15 VAL HG1 H 1.16 . 2 98 . 15 VAL HG2 H 1.07 . 2 99 . 16 ASN H H 8.72 . 1 100 . 16 ASN HA H 4.99 . 1 101 . 16 ASN HB2 H 2.88 . 2 102 . 16 ASN HB3 H 2.78 . 2 103 . 16 ASN HD21 H 7.54 . 2 104 . 16 ASN HD22 H 7.02 . 2 105 . 17 VAL H H 8.86 . 1 106 . 17 VAL HA H 4.32 . 1 107 . 17 VAL HB H 2.18 . 1 108 . 17 VAL HG1 H .88 . 2 109 . 17 VAL HG2 H .79 . 2 110 . 18 GLU H H 10.38 . 1 111 . 18 GLU HA H 4.57 . 1 112 . 18 GLU HB2 H 2.17 . 2 113 . 18 GLU HB3 H 2.05 . 2 114 . 18 GLU HG2 H 2.43 . 2 115 . 18 GLU HG3 H 2.27 . 2 116 . 19 ASP H H 7.51 . 1 117 . 19 ASP HA H 4.67 . 1 118 . 19 ASP HB2 H 3.1 . 2 119 . 19 ASP HB3 H 2.82 . 2 120 . 20 GLU H H 8.88 . 1 121 . 20 GLU HA H 3.92 . 1 122 . 20 GLU HB2 H 2.08 . 2 123 . 20 GLU HB3 H 2.01 . 2 124 . 20 GLU HG2 H 2.38 . 2 125 . 20 GLU HG3 H 2.34 . 2 126 . 21 ASN H H 8.38 . 1 127 . 21 ASN HA H 4.49 . 1 128 . 21 ASN HB2 H 2.99 . 2 129 . 21 ASN HB3 H 2.86 . 2 130 . 21 ASN HD21 H 8.18 . 2 131 . 21 ASN HD22 H 7.13 . 2 132 . 22 ASP H H 8.21 . 1 133 . 22 ASP HA H 4.5 . 1 134 . 22 ASP HB2 H 3.15 . 2 135 . 22 ASP HB3 H 2.63 . 2 136 . 23 ILE H H 7.42 . 1 137 . 23 ILE HA H 3.4 . 1 138 . 23 ILE HB H 1.97 . 1 139 . 23 ILE HG12 H 1.98 . 2 140 . 23 ILE HG13 H 1.74 . 2 141 . 23 ILE HG2 H .84 . 1 142 . 23 ILE HD1 H .59 . 1 143 . 24 SER H H 8.18 . 1 144 . 24 SER HA H 4.2 . 1 145 . 24 SER HB2 H 4.09 . 1 146 . 24 SER HB3 H 4.09 . 1 147 . 25 GLU H H 8.27 . 1 148 . 25 GLU HA H 4.38 . 1 149 . 25 GLU HB2 H 2.44 . 1 150 . 25 GLU HB3 H 2.44 . 1 151 . 25 GLU HG2 H 1.98 . 1 152 . 25 GLU HG3 H 1.98 . 1 153 . 26 LEU H H 7.95 . 1 154 . 26 LEU HA H 4.09 . 1 155 . 26 LEU HB2 H 2.1 . 2 156 . 26 LEU HB3 H 2.02 . 2 157 . 26 LEU HG H 1.27 . 1 158 . 26 LEU HD1 H .95 . 2 159 . 26 LEU HD2 H .82 . 2 160 . 27 HIS H H 8.36 . 1 161 . 27 HIS HA H 4.13 . 1 162 . 27 HIS HB2 H 3.42 . 2 163 . 27 HIS HB3 H 3.26 . 2 164 . 27 HIS HD2 H 7.1 . 1 165 . 27 HIS HE1 H 8.03 . 1 166 . 28 GLU H H 8.27 . 1 167 . 28 GLU HA H 4.06 . 1 168 . 28 GLU HB2 H 2.37 . 2 169 . 28 GLU HB3 H 2.32 . 2 170 . 28 GLU HG2 H 2.38 . 2 171 . 28 GLU HG3 H 2.25 . 2 172 . 29 LEU H H 8.43 . 1 173 . 29 LEU HA H 3.32 . 1 174 . 29 LEU HB2 H 1.51 . 2 175 . 29 LEU HB3 H .71 . 2 176 . 29 LEU HG H .92 . 1 177 . 29 LEU HD1 H .35 . 2 178 . 29 LEU HD2 H .18 . 2 179 . 30 ALA H H 8.03 . 1 180 . 30 ALA HA H 4.19 . 1 181 . 30 ALA HB H 1.53 . 1 182 . 31 SER H H 7.65 . 1 183 . 31 SER HA H 4.44 . 1 184 . 31 SER HB2 H 4.05 . 2 185 . 31 SER HB3 H 3.98 . 2 186 . 32 THR H H 7.61 . 1 187 . 32 THR HA H 4.4 . 1 188 . 32 THR HB H 4.16 . 1 189 . 32 THR HG2 H 1.2 . 1 190 . 33 ARG H H 8 . 1 191 . 33 ARG HA H 4.57 . 1 192 . 33 ARG HB2 H 1.41 . 2 193 . 33 ARG HB3 H 1.3 . 2 194 . 33 ARG HG2 H 1.42 . 2 195 . 33 ARG HG3 H 1.3 . 2 196 . 33 ARG HD2 H 3.15 . 2 197 . 33 ARG HD3 H 2.81 . 2 198 . 33 ARG HE H 7.22 . 1 199 . 33 ARG HH11 H 6.53 . 1 200 . 33 ARG HH12 H 6.53 . 1 201 . 33 ARG HH21 H 6.53 . 1 202 . 33 ARG HH22 H 6.53 . 1 203 . 34 GLN H H 8.75 . 1 204 . 34 GLN HA H 4.31 . 1 205 . 34 GLN HB2 H 1.98 . 2 206 . 34 GLN HB3 H 1.86 . 2 207 . 35 ILE H H 8.26 . 1 208 . 35 ILE HA H 4.39 . 1 209 . 35 ILE HB H 1.3 . 1 210 . 35 ILE HG12 H .76 . 2 211 . 35 ILE HG13 H .65 . 2 212 . 35 ILE HG2 H .04 . 1 213 . 35 ILE HD1 H -.25 . 1 214 . 36 ASP H H 8 . 1 215 . 36 ASP HA H 5.13 . 1 216 . 36 ASP HB2 H 2.79 . 2 217 . 36 ASP HB3 H 2.53 . 2 218 . 37 PHE H H 8.93 . 1 219 . 37 PHE HA H 4.19 . 1 220 . 37 PHE HB2 H 3.56 . 2 221 . 37 PHE HB3 H 2.66 . 2 222 . 37 PHE HD1 H 7.27 . 1 223 . 37 PHE HD2 H 7.27 . 1 224 . 37 PHE HE1 H 6.98 . 1 225 . 37 PHE HE2 H 6.98 . 1 226 . 37 PHE HZ H 6.65 . 1 227 . 38 TRP H H 9.19 . 1 228 . 38 TRP HA H 5.13 . 1 229 . 38 TRP HB2 H 3.21 . 2 230 . 38 TRP HB3 H 2.87 . 2 231 . 38 TRP HD1 H 6.93 . 1 232 . 38 TRP HE1 H 9.72 . 1 233 . 38 TRP HE3 H 7.47 . 1 234 . 38 TRP HZ2 H 7.25 . 1 235 . 38 TRP HZ3 H 7.1 . 1 236 . 38 TRP HH2 H 7.27 . 1 237 . 39 LEU H H 8.09 . 1 238 . 39 LEU HA H 4.58 . 1 239 . 39 LEU HB2 H 1.92 . 2 240 . 39 LEU HB3 H 1.87 . 2 241 . 40 PRO HA H 5.01 . 1 242 . 40 PRO HB2 H 2.49 . 2 243 . 40 PRO HB3 H 2.3 . 2 244 . 40 PRO HG2 H 1.76 . 2 245 . 40 PRO HG3 H 1.69 . 2 246 . 40 PRO HD2 H 3.79 . 2 247 . 40 PRO HD3 H 3.61 . 2 248 . 41 ASP H H 8.05 . 1 249 . 41 ASP HA H 4.42 . 1 250 . 41 ASP HB2 H 2.98 . 2 251 . 41 ASP HB3 H 2.64 . 2 252 . 42 SER H H 7.03 . 1 253 . 42 SER HA H 4.65 . 1 254 . 42 SER HB2 H 3.92 . 2 255 . 42 SER HB3 H 3.55 . 2 256 . 43 VAL H H 8.82 . 1 257 . 43 VAL HA H 3.05 . 1 258 . 43 VAL HB H 1.6 . 1 259 . 43 VAL HG1 H .63 . 2 260 . 43 VAL HG2 H .35 . 2 261 . 44 THR H H 7.42 . 1 262 . 44 THR HA H 4.12 . 1 263 . 44 THR HB H 4.31 . 1 264 . 44 THR HG2 H 1.25 . 1 265 . 45 GLN H H 7.3 . 1 266 . 45 GLN HA H 4.36 . 1 267 . 45 GLN HB2 H 1.87 . 1 268 . 45 GLN HB3 H 1.87 . 1 269 . 45 GLN HG2 H 2.39 . 2 270 . 45 GLN HG3 H 2.31 . 2 271 . 45 GLN HE21 H 7.57 . 2 272 . 45 GLN HE22 H 7.11 . 2 273 . 46 ILE H H 7 . 1 274 . 46 ILE HA H 3.93 . 1 275 . 46 ILE HB H 1.63 . 1 276 . 46 ILE HG12 H 1.67 . 1 277 . 46 ILE HG13 H 1.67 . 1 278 . 46 ILE HG2 H .8 . 1 279 . 46 ILE HD1 H .68 . 1 280 . 47 LYS H H 8.1 . 1 281 . 47 LYS HA H 4.83 . 1 282 . 47 LYS HB2 H 1.87 . 2 283 . 47 LYS HB3 H 1.61 . 2 284 . 48 PRO HA H 3.77 . 1 285 . 48 PRO HB2 H 1.97 . 2 286 . 48 PRO HB3 H 1.65 . 2 287 . 48 PRO HG2 H 2.11 . 2 288 . 48 PRO HG3 H 1.66 . 2 289 . 48 PRO HD2 H 3.71 . 2 290 . 48 PRO HD3 H 3.54 . 2 291 . 49 HIS H H 8.15 . 1 292 . 49 HIS HA H 4.58 . 1 293 . 49 HIS HB2 H 3.57 . 2 294 . 49 HIS HB3 H 3.35 . 2 295 . 49 HIS HD2 H 7.32 . 1 296 . 49 HIS HE1 H 8.69 . 1 297 . 50 SER H H 8.5 . 1 298 . 50 SER HA H 4.98 . 1 299 . 50 SER HB2 H 4.01 . 2 300 . 50 SER HB3 H 3.71 . 2 301 . 51 THR H H 8.3 . 1 302 . 51 THR HA H 5.46 . 1 303 . 51 THR HB H 3.98 . 1 304 . 51 THR HG2 H 1.2 . 1 305 . 52 VAL H H 9.15 . 1 306 . 52 VAL HA H 5.17 . 1 307 . 52 VAL HB H 2.3 . 1 308 . 52 VAL HG1 H 1.3 . 2 309 . 52 VAL HG2 H 1.16 . 2 310 . 53 ASP H H 9.43 . 1 311 . 53 ASP HA H 6.33 . 1 312 . 53 ASP HB2 H 2.74 . 2 313 . 53 ASP HB3 H 2.41 . 2 314 . 54 PHE H H 8.97 . 1 315 . 54 PHE HA H 5.05 . 1 316 . 54 PHE HB2 H 2.33 . 2 317 . 54 PHE HB3 H 2.08 . 2 318 . 54 PHE HD1 H 6.62 . 1 319 . 54 PHE HD2 H 6.62 . 1 320 . 54 PHE HE1 H 6.67 . 1 321 . 54 PHE HE2 H 6.67 . 1 322 . 54 PHE HZ H 6.53 . 1 323 . 55 ARG H H 8.65 . 1 324 . 55 ARG HA H 4.61 . 1 325 . 55 ARG HB2 H 1.26 . 1 326 . 55 ARG HB3 H 1.26 . 1 327 . 56 VAL H H 9.21 . 1 328 . 56 VAL HA H 4.4 . 1 329 . 56 VAL HB H 2 . 1 330 . 56 VAL HG1 H .99 . 2 331 . 56 VAL HG2 H .86 . 2 332 . 57 LYS H H 9.37 . 1 333 . 57 LYS HA H 4.21 . 1 334 . 57 LYS HB2 H 1.63 . 2 335 . 57 LYS HB3 H 1.54 . 2 336 . 57 LYS HE2 H 2.58 . 1 337 . 57 LYS HE3 H 2.58 . 1 338 . 58 ALA H H 9.63 . 1 339 . 58 ALA HA H 4 . 1 340 . 58 ALA HB H 1.46 . 1 341 . 59 GLU H H 9.59 . 1 342 . 59 GLU HA H 4.16 . 1 343 . 59 GLU HB2 H 2.06 . 2 344 . 59 GLU HB3 H 2.01 . 2 345 . 59 GLU HG2 H 2.28 . 2 346 . 59 GLU HG3 H 2.2 . 2 347 . 60 ASP H H 8.14 . 1 348 . 60 ASP HA H 5.01 . 1 349 . 60 ASP HB2 H 2.6 . 1 350 . 60 ASP HB3 H 2.6 . 1 351 . 61 ILE H H 7.2 . 1 352 . 61 ILE HA H 3.36 . 1 353 . 61 ILE HB H 1.82 . 1 354 . 61 ILE HG12 H 2.02 . 1 355 . 61 ILE HG13 H 2.02 . 1 356 . 61 ILE HG2 H .98 . 1 357 . 61 ILE HD1 H 1.03 . 1 358 . 62 LEU H H 8.27 . 1 359 . 62 LEU HA H 4.12 . 1 360 . 62 LEU HB2 H 1.71 . 2 361 . 62 LEU HB3 H 1.59 . 2 362 . 62 LEU HG H 1.72 . 1 363 . 62 LEU HD1 H .98 . 2 364 . 62 LEU HD2 H .92 . 2 365 . 63 ALA H H 8.27 . 1 366 . 63 ALA HA H 4.16 . 1 367 . 63 ALA HB H 1.39 . 1 368 . 64 VAL H H 8.3 . 1 369 . 64 VAL HA H 3.4 . 1 370 . 64 VAL HB H 1.93 . 1 371 . 64 VAL HG1 H .77 . 2 372 . 64 VAL HG2 H .32 . 2 373 . 65 GLU H H 8.82 . 1 374 . 65 GLU HA H 3.54 . 1 375 . 65 GLU HB2 H 2.29 . 2 376 . 65 GLU HB3 H 2.24 . 2 377 . 65 GLU HG2 H 2.83 . 1 378 . 65 GLU HG3 H 2.83 . 1 379 . 66 ASP H H 8.32 . 1 380 . 66 ASP HA H 4.46 . 1 381 . 66 ASP HB2 H 2.85 . 2 382 . 66 ASP HB3 H 2.65 . 2 383 . 67 PHE H H 7.9 . 1 384 . 67 PHE HA H 4.04 . 1 385 . 67 PHE HB2 H 3.22 . 2 386 . 67 PHE HB3 H 3.13 . 2 387 . 67 PHE HD1 H 7.05 . 1 388 . 67 PHE HD2 H 7.05 . 1 389 . 67 PHE HE1 H 7.12 . 1 390 . 67 PHE HE2 H 7.12 . 1 391 . 67 PHE HZ H 7.38 . 1 392 . 68 LEU H H 8.79 . 1 393 . 68 LEU HA H 3.97 . 1 394 . 68 LEU HB2 H 1.75 . 2 395 . 68 LEU HB3 H 1.67 . 2 396 . 68 LEU HG H 2.01 . 1 397 . 68 LEU HD1 H .86 . 2 398 . 68 LEU HD2 H .03 . 2 399 . 69 GLU H H 8.44 . 1 400 . 69 GLU HA H 4.31 . 1 401 . 69 GLU HB2 H 2.32 . 2 402 . 69 GLU HB3 H 2.2 . 2 403 . 69 GLU HG2 H 2.72 . 2 404 . 69 GLU HG3 H 2.51 . 2 405 . 70 GLN H H 8.92 . 1 406 . 70 GLN HA H 4.03 . 1 407 . 70 GLN HB2 H 2.02 . 2 408 . 70 GLN HB3 H 1.99 . 2 409 . 70 GLN HG2 H 2.45 . 1 410 . 70 GLN HG3 H 2.45 . 1 411 . 70 GLN HE21 H 7.72 . 2 412 . 70 GLN HE22 H 6.8 . 2 413 . 71 ASN H H 7.29 . 1 414 . 71 ASN HA H 4.66 . 1 415 . 71 ASN HB2 H 2.75 . 2 416 . 71 ASN HB3 H 2.08 . 2 417 . 71 ASN HD21 H 6.55 . 2 418 . 71 ASN HD22 H 6.25 . 2 419 . 72 GLU H H 7.68 . 1 420 . 72 GLU HA H 3.93 . 1 421 . 72 GLU HB2 H 2.23 . 2 422 . 72 GLU HB3 H 2.18 . 2 423 . 73 LEU H H 8.35 . 1 424 . 73 LEU HA H 4.72 . 1 425 . 73 LEU HB2 H 1.81 . 2 426 . 73 LEU HB3 H 1.37 . 2 427 . 73 LEU HG H 1.62 . 1 428 . 73 LEU HD1 H 1 . 2 429 . 73 LEU HD2 H .87 . 2 430 . 74 GLN H H 9.32 . 1 431 . 74 GLN HA H 4.34 . 1 432 . 74 GLN HB2 H 2.13 . 1 433 . 74 GLN HB3 H 2.13 . 1 434 . 74 GLN HG2 H 2.49 . 2 435 . 74 GLN HG3 H 2.41 . 2 436 . 74 GLN HE21 H 7.58 . 2 437 . 74 GLN HE22 H 6.89 . 2 438 . 75 TYR H H 8.29 . 1 439 . 75 TYR HA H 5.88 . 1 440 . 75 TYR HB2 H 2.93 . 2 441 . 75 TYR HB3 H 2.86 . 2 442 . 75 TYR HD1 H 7.04 . 1 443 . 75 TYR HD2 H 7.04 . 1 444 . 75 TYR HE1 H 6.81 . 1 445 . 75 TYR HE2 H 6.81 . 1 446 . 76 GLU H H 9 . 1 447 . 76 GLU HA H 4.53 . 1 448 . 76 GLU HB2 H 1.92 . 1 449 . 76 GLU HB3 H 1.92 . 1 450 . 76 GLU HG2 H 2.1 . 1 451 . 76 GLU HG3 H 2.1 . 1 452 . 77 VAL H H 8.72 . 1 453 . 77 VAL HA H 4.18 . 1 454 . 77 VAL HB H 1.82 . 1 455 . 77 VAL HG1 H .66 . 2 456 . 77 VAL HG2 H .59 . 2 457 . 78 LEU H H 8.74 . 1 458 . 78 LEU HA H 4.36 . 1 459 . 78 LEU HB2 H 1.56 . 1 460 . 78 LEU HB3 H 1.56 . 1 461 . 78 LEU HG H 1.41 . 1 462 . 78 LEU HD1 H .79 . 2 463 . 78 LEU HD2 H .67 . 2 464 . 79 ILE H H 8.32 . 1 465 . 79 ILE HA H 4.21 . 1 466 . 79 ILE HB H 1.84 . 1 467 . 79 ILE HG12 H 1.45 . 2 468 . 79 ILE HG13 H 1.19 . 2 469 . 79 ILE HG2 H .9 . 1 470 . 79 ILE HD1 H .86 . 1 471 . 80 ASN H H 8.6 . 1 472 . 80 ASN HA H 4.78 . 1 473 . 80 ASN HB2 H 2.85 . 2 474 . 80 ASN HB3 H 2.7 . 2 475 . 80 ASN HD21 H 7.76 . 2 476 . 80 ASN HD22 H 6.95 . 2 477 . 81 ASN H H 8.13 . 1 478 . 81 ASN HA H 4.48 . 1 479 . 81 ASN HB2 H 2.71 . 2 480 . 81 ASN HB3 H 2.68 . 2 481 . 81 ASN HD21 H 7.56 . 2 482 . 81 ASN HD22 H 6.79 . 2 stop_ save_