data_2281 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin ; _BMRB_accession_number 2281 _BMRB_flat_file_name bmr2281.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Baron Martin . . 2 Main Alison L. . 3 Driscoll Paul C. . 4 Mardon Helen J. . 5 Boyd Jonathan . . 6 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 480 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Baron, Martin, Main, Alison L., Driscoll, Paul C., Mardon, Helen J., Boyd, Jonathan, Campbell, Iain D., "1H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin," Biochemistry 31 (7), 2068-2073 (1992). ; _Citation_title ; 1H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin ; _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 Baron Martin . . 2 Main Alison L. . 3 Driscoll Paul C. . 4 Mardon Helen J. . 5 Boyd Jonathan . . 6 Campbell Iain D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 31 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2068 _Page_last 2073 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_fibronectin _Saveframe_category molecular_system _Mol_system_name fibronectin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label fibronectin $fibronectin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_fibronectin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common fibronectin _Name_variant 'cell adhesion type III module' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; VSDVPRDLEVVAATPTSLLI SWDAPAVTVRYYRITYGETG GNSPVQEFTVPGSKSTATIS GLKPGVDYTITVYAVTGRGD SPASSKPISINYRT ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 SER 3 ASP 4 VAL 5 PRO 6 ARG 7 ASP 8 LEU 9 GLU 10 VAL 11 VAL 12 ALA 13 ALA 14 THR 15 PRO 16 THR 17 SER 18 LEU 19 LEU 20 ILE 21 SER 22 TRP 23 ASP 24 ALA 25 PRO 26 ALA 27 VAL 28 THR 29 VAL 30 ARG 31 TYR 32 TYR 33 ARG 34 ILE 35 THR 36 TYR 37 GLY 38 GLU 39 THR 40 GLY 41 GLY 42 ASN 43 SER 44 PRO 45 VAL 46 GLN 47 GLU 48 PHE 49 THR 50 VAL 51 PRO 52 GLY 53 SER 54 LYS 55 SER 56 THR 57 ALA 58 THR 59 ILE 60 SER 61 GLY 62 LEU 63 LYS 64 PRO 65 GLY 66 VAL 67 ASP 68 TYR 69 THR 70 ILE 71 THR 72 VAL 73 TYR 74 ALA 75 VAL 76 THR 77 GLY 78 ARG 79 GLY 80 ASP 81 SER 82 PRO 83 ALA 84 SER 85 SER 86 LYS 87 PRO 88 ILE 89 SER 90 ILE 91 ASN 92 TYR 93 ARG 94 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1FNA "Crystal Structure Of The Tenth Type Iii Cell Adhesion Module Of Human Fibronectin" 94.68 91 100.00 100.00 3.23e-54 PDB 1TTF "The Three-Dimensional Structure Of The Tenth Type Iii Module Of Fibronectin: An Insight Into Rgd-Mediated Interactions" 100.00 94 100.00 100.00 1.21e-57 PDB 1TTG "The Three-Dimensional Structure Of The Tenth Type Iii Module Of Fibronectin: An Insight Into Rgd-Mediated Interactions" 100.00 94 100.00 100.00 1.21e-57 PDB 4MMX "Integrin Alphavbeta3 Ectodomain Bound To The Tenth Domain Of Fibronectin" 98.94 98 100.00 100.00 4.02e-57 GB AAA58483 "fibronecton type III, partial [Homo sapiens]" 98.94 93 100.00 100.00 4.13e-57 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 $fibronectin human 9606 Eukaryota Metazoa Homo sapiens 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 $fibronectin 'not available' yeast Saccharomyces cerevisiae MD50/a,alpha/leu2,3 . 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 4 . na temperature 320 . 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 p-dioxane H . . ppm 3.75 . . . . . $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 fibronectin _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 VAL HA H 4.01 . 1 2 . 1 VAL HB H 2.35 . 1 3 . 1 VAL HG1 H 1.17 . 1 4 . 1 VAL HG2 H 1.17 . 1 5 . 2 SER HA H 4.79 . 1 6 . 2 SER HB2 H 4.08 . 1 7 . 2 SER HB3 H 4.08 . 1 8 . 3 ASP H H 8.66 . 1 9 . 3 ASP HA H 4.74 . 1 10 . 3 ASP HB2 H 3.07 . 2 11 . 3 ASP HB3 H 2.72 . 2 12 . 4 VAL H H 7.57 . 1 13 . 4 VAL HA H 4.79 . 1 14 . 4 VAL HB H 2.27 . 1 15 . 4 VAL HG1 H 1.23 . 2 16 . 4 VAL HG2 H 1.14 . 2 17 . 5 PRO HA H 4.77 . 1 18 . 5 PRO HB2 H 2.34 . 1 19 . 5 PRO HB3 H 2.34 . 1 20 . 5 PRO HG2 H 1.82 . 2 21 . 5 PRO HG3 H 1.94 . 2 22 . 5 PRO HD2 H 3.87 . 2 23 . 5 PRO HD3 H 4.06 . 2 24 . 6 ARG H H 8.31 . 1 25 . 6 ARG HA H 4.87 . 1 26 . 6 ARG HB2 H 1.84 . 1 27 . 6 ARG HB3 H 1.84 . 1 28 . 6 ARG HG2 H 1.8 . 1 29 . 6 ARG HG3 H 1.8 . 1 30 . 6 ARG HD2 H 3.38 . 1 31 . 6 ARG HD3 H 3.38 . 1 32 . 7 ASP H H 8.97 . 1 33 . 7 ASP HA H 4.44 . 1 34 . 7 ASP HB2 H 3.27 . 2 35 . 7 ASP HB3 H 2.68 . 2 36 . 8 LEU H H 7.45 . 1 37 . 8 LEU HA H 5.2 . 1 38 . 8 LEU HB2 H 1.8 . 2 39 . 8 LEU HB3 H 1.3 . 2 40 . 8 LEU HG H 1.57 . 1 41 . 8 LEU HD1 H 1.08 . 2 42 . 8 LEU HD2 H .84 . 2 43 . 9 GLU H H 9.34 . 1 44 . 9 GLU HA H 4.89 . 1 45 . 9 GLU HB2 H 2.14 . 2 46 . 9 GLU HB3 H 1.94 . 2 47 . 10 VAL H H 8.55 . 1 48 . 10 VAL HA H 4.43 . 1 49 . 10 VAL HB H 1.81 . 1 50 . 10 VAL HG1 H .59 . 2 51 . 10 VAL HG2 H .52 . 2 52 . 11 VAL H H 9 . 1 53 . 11 VAL HA H 4.2 . 1 54 . 11 VAL HB H 2.04 . 1 55 . 11 VAL HG1 H .99 . 2 56 . 11 VAL HG2 H .94 . 2 57 . 12 ALA H H 7.86 . 1 58 . 12 ALA HA H 4.67 . 1 59 . 12 ALA HB H 1.5 . 1 60 . 13 ALA H H 8.5 . 1 61 . 13 ALA HA H 5.12 . 1 62 . 13 ALA HB H 1.33 . 1 63 . 14 THR H H 9.03 . 1 64 . 14 THR HA H 5.02 . 1 65 . 14 THR HB H 4.83 . 1 66 . 14 THR HG2 H 1.28 . 1 67 . 15 PRO HA H 4.64 . 1 68 . 15 PRO HB2 H 2.08 . 2 69 . 15 PRO HB3 H 2.63 . 2 70 . 15 PRO HG2 H 2.33 . 1 71 . 15 PRO HG3 H 2.33 . 1 72 . 15 PRO HD2 H 3.92 . 2 73 . 15 PRO HD3 H 4.12 . 2 74 . 16 THR H H 7.36 . 1 75 . 16 THR HA H 4.72 . 1 76 . 16 THR HB H 4.76 . 1 77 . 16 THR HG2 H 1.27 . 1 78 . 17 SER H H 7.81 . 1 79 . 17 SER HA H 5.47 . 1 80 . 17 SER HB2 H 3.83 . 1 81 . 17 SER HB3 H 3.83 . 1 82 . 18 LEU H H 8.88 . 1 83 . 18 LEU HA H 5.02 . 1 84 . 18 LEU HB2 H 1.5 . 2 85 . 18 LEU HB3 H 1.36 . 2 86 . 18 LEU HG H 1.45 . 1 87 . 18 LEU HD1 H .78 . 2 88 . 18 LEU HD2 H .6 . 2 89 . 19 LEU H H 8.74 . 1 90 . 19 LEU HA H 5.24 . 1 91 . 19 LEU HB2 H 1.92 . 1 92 . 19 LEU HB3 H 1.92 . 1 93 . 19 LEU HG H 1.52 . 1 94 . 19 LEU HD1 H .92 . 2 95 . 19 LEU HD2 H .88 . 2 96 . 20 ILE H H 9.13 . 1 97 . 20 ILE HA H 5.6 . 1 98 . 20 ILE HB H 2.06 . 1 99 . 20 ILE HG12 H 1.88 . 2 100 . 20 ILE HG13 H 1.31 . 2 101 . 20 ILE HG2 H .89 . 1 102 . 20 ILE HD1 H .97 . 1 103 . 21 SER H H 9.01 . 1 104 . 21 SER HA H 5.13 . 1 105 . 21 SER HB2 H 3.56 . 2 106 . 21 SER HB3 H 3.77 . 2 107 . 22 TRP H H 7.8 . 1 108 . 22 TRP HA H 5.14 . 1 109 . 22 TRP HB2 H 3.03 . 2 110 . 22 TRP HB3 H 3.38 . 2 111 . 22 TRP HD1 H 6.64 . 1 112 . 22 TRP HE1 H 7.58 . 1 113 . 22 TRP HE3 H 6.94 . 1 114 . 22 TRP HZ2 H 6.29 . 1 115 . 22 TRP HZ3 H 6.56 . 1 116 . 22 TRP HH2 H 6.56 . 1 117 . 23 ASP H H 9.09 . 1 118 . 23 ASP HA H 5.2 . 1 119 . 23 ASP HB2 H 2.93 . 2 120 . 23 ASP HB3 H 2.76 . 2 121 . 24 ALA H H 8.83 . 1 122 . 24 ALA HA H 4.78 . 1 123 . 24 ALA HB H 1.71 . 1 124 . 25 PRO HA H 4.78 . 1 125 . 25 PRO HB2 H 2.02 . 1 126 . 25 PRO HB3 H 2.02 . 1 127 . 25 PRO HG2 H 1.93 . 1 128 . 25 PRO HG3 H 1.93 . 1 129 . 25 PRO HD2 H 3.71 . 2 130 . 25 PRO HD3 H 4.23 . 2 131 . 26 ALA H H 8.53 . 1 132 . 26 ALA HA H 4.53 . 1 133 . 26 ALA HB H 1.56 . 1 134 . 27 VAL H H 7.27 . 1 135 . 27 VAL HA H 4.52 . 1 136 . 27 VAL HB H 2.27 . 1 137 . 27 VAL HG1 H 1 . 2 138 . 27 VAL HG2 H .9 . 2 139 . 28 THR H H 8.15 . 1 140 . 28 THR HA H 4.11 . 1 141 . 28 THR HB H 4.09 . 1 142 . 28 THR HG2 H 1.27 . 1 143 . 29 VAL H H 8.59 . 1 144 . 29 VAL HA H 3.9 . 1 145 . 29 VAL HB H 2.01 . 1 146 . 29 VAL HG1 H 1 . 2 147 . 29 VAL HG2 H .11 . 2 148 . 30 ARG H H 8.92 . 1 149 . 30 ARG HA H 4.32 . 1 150 . 30 ARG HB2 H 1.7 . 2 151 . 30 ARG HB3 H 2.01 . 2 152 . 30 ARG HG2 H 1.75 . 2 153 . 30 ARG HG3 H 1.81 . 2 154 . 30 ARG HD2 H 3.3 . 2 155 . 30 ARG HD3 H 3.22 . 2 156 . 31 TYR H H 7.4 . 1 157 . 31 TYR HA H 4.81 . 1 158 . 31 TYR HB2 H 3.25 . 2 159 . 31 TYR HB3 H 3.57 . 2 160 . 31 TYR HD1 H 6.91 . 1 161 . 31 TYR HD2 H 6.91 . 1 162 . 31 TYR HE1 H 6.79 . 1 163 . 31 TYR HE2 H 6.79 . 1 164 . 32 TYR H H 9.6 . 1 165 . 32 TYR HA H 5.47 . 1 166 . 32 TYR HB2 H 2.62 . 2 167 . 32 TYR HB3 H 2.83 . 2 168 . 32 TYR HD1 H 7.09 . 1 169 . 32 TYR HD2 H 7.09 . 1 170 . 32 TYR HE1 H 7.1 . 1 171 . 32 TYR HE2 H 7.1 . 1 172 . 33 ARG H H 9.18 . 1 173 . 33 ARG HA H 5 . 1 174 . 33 ARG HB2 H 1.85 . 1 175 . 33 ARG HB3 H 1.85 . 1 176 . 33 ARG HG2 H 1.5 . 1 177 . 33 ARG HG3 H 1.5 . 1 178 . 33 ARG HD2 H 3.03 . 1 179 . 33 ARG HD3 H 3.03 . 1 180 . 34 ILE H H 9.05 . 1 181 . 34 ILE HA H 5.17 . 1 182 . 34 ILE HB H .75 . 1 183 . 34 ILE HG2 H .66 . 1 184 . 34 ILE HD1 H .57 . 1 185 . 35 THR H H 9.36 . 1 186 . 35 THR HA H 5.98 . 1 187 . 35 THR HB H 4.36 . 1 188 . 35 THR HG2 H 1.27 . 1 189 . 36 TYR H H 8.94 . 1 190 . 36 TYR HA H 6.11 . 1 191 . 36 TYR HB2 H 2.8 . 2 192 . 36 TYR HB3 H 3.31 . 2 193 . 36 TYR HD1 H 6.85 . 1 194 . 36 TYR HD2 H 6.85 . 1 195 . 36 TYR HE1 H 6.89 . 1 196 . 36 TYR HE2 H 6.89 . 1 197 . 37 GLY H H 8.38 . 1 198 . 37 GLY HA2 H 4.7 . 2 199 . 37 GLY HA3 H 4.32 . 2 200 . 38 GLU H H 9.01 . 1 201 . 38 GLU HA H 4.36 . 1 202 . 38 GLU HB2 H 2.11 . 2 203 . 38 GLU HB3 H 1.93 . 2 204 . 38 GLU HG2 H 2.49 . 2 205 . 38 GLU HG3 H 2.22 . 2 206 . 39 THR H H 9.01 . 1 207 . 39 THR HA H 4.08 . 1 208 . 39 THR HB H 3.91 . 1 209 . 39 THR HG2 H 1.23 . 1 210 . 40 GLY H H 8.93 . 1 211 . 40 GLY HA2 H 4.22 . 2 212 . 40 GLY HA3 H 3.96 . 2 213 . 41 GLY H H 8.05 . 1 214 . 41 GLY HA2 H 4.22 . 2 215 . 41 GLY HA3 H 4.03 . 2 216 . 42 ASN H H 8.49 . 1 217 . 42 ASN HA H 4.92 . 1 218 . 42 ASN HB2 H 3.02 . 2 219 . 42 ASN HB3 H 2.88 . 2 220 . 43 SER H H 7.85 . 1 221 . 43 SER HA H 4.97 . 1 222 . 43 SER HB2 H 4.02 . 1 223 . 43 SER HB3 H 4.02 . 1 224 . 44 PRO HA H 4.64 . 1 225 . 44 PRO HB2 H 2.47 . 1 226 . 44 PRO HB3 H 2.47 . 1 227 . 44 PRO HG2 H 1.99 . 2 228 . 44 PRO HG3 H 2.16 . 2 229 . 44 PRO HD2 H 3.84 . 2 230 . 44 PRO HD3 H 4.01 . 2 231 . 45 VAL H H 8.38 . 1 232 . 45 VAL HA H 4.39 . 1 233 . 45 VAL HB H 2.13 . 1 234 . 45 VAL HG1 H 1.04 . 1 235 . 45 VAL HG2 H 1.04 . 1 236 . 46 GLN H H 8.27 . 1 237 . 46 GLN HA H 4.62 . 1 238 . 46 GLN HB2 H 2.35 . 2 239 . 46 GLN HB3 H 2.4 . 2 240 . 46 GLN HG2 H 1.93 . 1 241 . 46 GLN HG3 H 1.93 . 1 242 . 47 GLU H H 8.49 . 1 243 . 47 GLU HA H 6 . 1 244 . 47 GLU HB2 H 2.13 . 2 245 . 47 GLU HB3 H 2.07 . 2 246 . 47 GLU HG2 H 2.41 . 1 247 . 47 GLU HG3 H 2.41 . 1 248 . 48 PHE H H 9.21 . 1 249 . 48 PHE HA H 5.19 . 1 250 . 48 PHE HB2 H 3.55 . 2 251 . 48 PHE HB3 H 3.65 . 2 252 . 48 PHE HD1 H 7.46 . 1 253 . 48 PHE HD2 H 7.46 . 1 254 . 48 PHE HE1 H 7.37 . 1 255 . 48 PHE HE2 H 7.37 . 1 256 . 48 PHE HZ H 7.14 . 1 257 . 49 THR H H 8.53 . 1 258 . 49 THR HA H 5.89 . 1 259 . 49 THR HB H 4.3 . 1 260 . 49 THR HG2 H 1.22 . 1 261 . 50 VAL H H 9.07 . 1 262 . 50 VAL HA H 5.22 . 1 263 . 50 VAL HB H 2.51 . 1 264 . 50 VAL HG1 H 1.62 . 2 265 . 50 VAL HG2 H 1.43 . 2 266 . 51 PRO HA H 4.88 . 1 267 . 51 PRO HB2 H 2.27 . 2 268 . 51 PRO HB3 H 2.85 . 2 269 . 51 PRO HG2 H 2.33 . 1 270 . 51 PRO HG3 H 2.33 . 1 271 . 51 PRO HD2 H 3.99 . 2 272 . 51 PRO HD3 H 4.25 . 2 273 . 52 GLY H H 7.95 . 1 274 . 52 GLY HA2 H 4.02 . 1 275 . 52 GLY HA3 H 4.02 . 1 276 . 53 SER H H 7.62 . 1 277 . 53 SER HA H 4.71 . 1 278 . 53 SER HB2 H 4.07 . 2 279 . 53 SER HB3 H 4.32 . 2 280 . 54 LYS H H 8.28 . 1 281 . 54 LYS HA H 4.67 . 1 282 . 54 LYS HB2 H 2.13 . 2 283 . 54 LYS HB3 H 2.28 . 2 284 . 54 LYS HG2 H 2.19 . 1 285 . 54 LYS HG3 H 2.19 . 1 286 . 55 SER H H 8.17 . 1 287 . 55 SER HA H 3.77 . 1 288 . 55 SER HB2 H 3.36 . 2 289 . 55 SER HB3 H 3.59 . 2 290 . 56 THR H H 6.62 . 1 291 . 56 THR HA H 4.82 . 1 292 . 56 THR HB H 4.12 . 1 293 . 56 THR HG2 H 1.06 . 1 294 . 57 ALA H H 8.63 . 1 295 . 57 ALA HA H 4.87 . 1 296 . 57 ALA HB H 1.76 . 1 297 . 58 THR H H 8.47 . 1 298 . 58 THR HA H 5.25 . 1 299 . 58 THR HB H 3.99 . 1 300 . 58 THR HG2 H 1.14 . 1 301 . 59 ILE H H 9.14 . 1 302 . 59 ILE HA H 4.12 . 1 303 . 59 ILE HB H 1.45 . 1 304 . 59 ILE HG12 H .95 . 2 305 . 59 ILE HG13 H 1.54 . 2 306 . 59 ILE HG2 H .08 . 1 307 . 59 ILE HD1 H .66 . 1 308 . 60 SER H H 8.44 . 1 309 . 60 SER HA H 5.11 . 1 310 . 60 SER HB2 H 3.81 . 2 311 . 60 SER HB3 H 3.88 . 2 312 . 61 GLY H H 8.59 . 1 313 . 61 GLY HA2 H 4.13 . 2 314 . 61 GLY HA3 H 3.96 . 2 315 . 62 LEU H H 8.32 . 1 316 . 62 LEU HA H 4.39 . 1 317 . 62 LEU HB2 H 1.42 . 2 318 . 62 LEU HB3 H 1.28 . 2 319 . 62 LEU HG H 1.11 . 1 320 . 62 LEU HD1 H .24 . 2 321 . 62 LEU HD2 H .08 . 2 322 . 63 LYS H H 8.46 . 1 323 . 63 LYS HA H 4.11 . 1 324 . 63 LYS HB2 H 1.94 . 2 325 . 63 LYS HB3 H 2.02 . 2 326 . 63 LYS HD2 H 3.18 . 1 327 . 63 LYS HD3 H 3.18 . 1 328 . 64 PRO HA H 4.87 . 1 329 . 64 PRO HB2 H 2.42 . 1 330 . 64 PRO HB3 H 2.42 . 1 331 . 64 PRO HG2 H 2.08 . 2 332 . 64 PRO HG3 H 2.22 . 2 333 . 64 PRO HD2 H 3.83 . 2 334 . 64 PRO HD3 H 4 . 2 335 . 65 GLY H H 8.06 . 1 336 . 65 GLY HA2 H 4.13 . 2 337 . 65 GLY HA3 H 3.85 . 2 338 . 66 VAL H H 7.73 . 1 339 . 66 VAL HA H 4.25 . 1 340 . 66 VAL HB H 2.12 . 1 341 . 66 VAL HG1 H .86 . 2 342 . 66 VAL HG2 H .56 . 2 343 . 67 ASP H H 8.26 . 1 344 . 67 ASP HA H 5.13 . 1 345 . 67 ASP HB2 H 2.99 . 2 346 . 67 ASP HB3 H 2.69 . 2 347 . 68 TYR H H 9.44 . 1 348 . 68 TYR HA H 5.15 . 1 349 . 68 TYR HB2 H 2.93 . 2 350 . 68 TYR HB3 H 3.08 . 2 351 . 68 TYR HD1 H 7.25 . 1 352 . 68 TYR HD2 H 7.25 . 1 353 . 68 TYR HE1 H 7.25 . 1 354 . 68 TYR HE2 H 7.25 . 1 355 . 69 THR H H 9.13 . 1 356 . 69 THR HA H 5.22 . 1 357 . 69 THR HB H 4.04 . 1 358 . 69 THR HG2 H 1.26 . 1 359 . 70 ILE H H 9.38 . 1 360 . 70 ILE HA H 5.11 . 1 361 . 70 ILE HB H 1.82 . 1 362 . 70 ILE HG12 H 1.12 . 2 363 . 70 ILE HG13 H 1.62 . 2 364 . 70 ILE HG2 H .92 . 1 365 . 70 ILE HD1 H .83 . 1 366 . 71 THR H H 9.24 . 1 367 . 71 THR HA H 5.2 . 1 368 . 71 THR HB H 4.14 . 1 369 . 71 THR HG2 H .84 . 1 370 . 72 VAL H H 8.72 . 1 371 . 72 VAL HA H 4.73 . 1 372 . 72 VAL HB H 1.42 . 1 373 . 72 VAL HG1 H .37 . 2 374 . 72 VAL HG2 H .07 . 2 375 . 73 TYR H H 9.12 . 1 376 . 73 TYR HA H 4.75 . 1 377 . 73 TYR HB2 H 2.9 . 2 378 . 73 TYR HB3 H 3.02 . 2 379 . 73 TYR HD1 H 6.79 . 1 380 . 73 TYR HD2 H 6.79 . 1 381 . 73 TYR HE1 H 7.18 . 1 382 . 73 TYR HE2 H 7.18 . 1 383 . 74 ALA H H 9.07 . 1 384 . 74 ALA HA H 4.53 . 1 385 . 74 ALA HB H 1.42 . 1 386 . 75 VAL H H 8.31 . 1 387 . 75 VAL HA H 4.47 . 1 388 . 75 VAL HB H 1.18 . 1 389 . 75 VAL HG1 H .72 . 2 390 . 75 VAL HG2 H .65 . 2 391 . 76 THR H H 8.58 . 1 392 . 76 THR HA H 4.68 . 1 393 . 76 THR HB H 4.45 . 1 394 . 76 THR HG2 H 1.22 . 1 395 . 77 GLY H H 8.47 . 1 396 . 77 GLY HA2 H 4.26 . 2 397 . 77 GLY HA3 H 4.12 . 2 398 . 78 ARG H H 8.35 . 1 399 . 78 ARG HA H 4.51 . 1 400 . 78 ARG HB2 H 1.87 . 2 401 . 78 ARG HB3 H 2.03 . 2 402 . 79 GLY H H 8.52 . 1 403 . 79 GLY HA2 H 4.15 . 2 404 . 79 GLY HA3 H 3.98 . 2 405 . 80 ASP H H 8.41 . 1 406 . 80 ASP HA H 4.78 . 1 407 . 80 ASP HB2 H 2.91 . 1 408 . 80 ASP HB3 H 2.91 . 1 409 . 81 SER H H 8.08 . 1 410 . 81 SER HA H 4.92 . 1 411 . 81 SER HB2 H 3.98 . 1 412 . 81 SER HB3 H 3.98 . 1 413 . 82 PRO HA H 4.58 . 1 414 . 82 PRO HB2 H 1.99 . 2 415 . 82 PRO HB3 H 2.21 . 2 416 . 82 PRO HG2 H 2.05 . 2 417 . 82 PRO HG3 H 2.18 . 2 418 . 82 PRO HD2 H 3.8 . 1 419 . 82 PRO HD3 H 3.8 . 1 420 . 83 ALA H H 8.32 . 1 421 . 83 ALA HA H 4.53 . 1 422 . 84 SER H H 8.25 . 1 423 . 84 SER HA H 4.97 . 1 424 . 84 SER HB2 H 3.94 . 1 425 . 84 SER HB3 H 3.94 . 1 426 . 85 SER H H 8.64 . 1 427 . 85 SER HA H 4.76 . 1 428 . 85 SER HB2 H 4.09 . 2 429 . 85 SER HB3 H 4.18 . 2 430 . 86 LYS H H 8.37 . 1 431 . 86 LYS HA H 4.78 . 1 432 . 86 LYS HB2 H 2.03 . 2 433 . 86 LYS HB3 H 1.93 . 2 434 . 86 LYS HG2 H 1.63 . 1 435 . 86 LYS HG3 H 1.63 . 1 436 . 86 LYS HE2 H 3.19 . 1 437 . 86 LYS HE3 H 3.19 . 1 438 . 87 PRO HA H 4.57 . 1 439 . 88 ILE H H 7.93 . 1 440 . 88 ILE HA H 4.66 . 1 441 . 88 ILE HB H 1.91 . 1 442 . 88 ILE HG12 H 1.22 . 2 443 . 88 ILE HG13 H 1.66 . 2 444 . 88 ILE HG2 H .95 . 1 445 . 88 ILE HD1 H .86 . 1 446 . 89 SER H H 8.24 . 1 447 . 89 SER HA H 5.95 . 1 448 . 89 SER HB2 H 3.63 . 2 449 . 89 SER HB3 H 3.72 . 2 450 . 90 ILE H H 9.08 . 1 451 . 90 ILE HA H 4.83 . 1 452 . 90 ILE HB H 2.05 . 1 453 . 90 ILE HG12 H 1.21 . 2 454 . 90 ILE HG13 H 1.61 . 2 455 . 90 ILE HG2 H 1.04 . 1 456 . 90 ILE HD1 H .98 . 1 457 . 91 ASN H H 8.36 . 1 458 . 91 ASN HA H 6.15 . 1 459 . 91 ASN HB2 H 2.8 . 1 460 . 91 ASN HB3 H 2.8 . 1 461 . 92 TYR H H 9.5 . 1 462 . 92 TYR HA H 4.6 . 1 463 . 92 TYR HB2 H 2.75 . 2 464 . 92 TYR HB3 H 2.86 . 2 465 . 92 TYR HD1 H 7.11 . 1 466 . 92 TYR HD2 H 7.11 . 1 467 . 92 TYR HE1 H 6.9 . 1 468 . 92 TYR HE2 H 6.9 . 1 469 . 93 ARG H H 7.5 . 1 470 . 93 ARG HA H 5.41 . 1 471 . 93 ARG HB2 H 1.69 . 1 472 . 93 ARG HB3 H 1.69 . 1 473 . 93 ARG HG2 H 1.41 . 1 474 . 93 ARG HG3 H 1.41 . 1 475 . 93 ARG HD2 H 3.18 . 1 476 . 93 ARG HD3 H 3.18 . 1 477 . 94 THR H H 8.94 . 1 478 . 94 THR HA H 4.4 . 1 479 . 94 THR HB H 5.03 . 1 480 . 94 THR HG2 H 1.51 . 1 stop_ save_