data_4283 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of the Angiogenesis Marker Oncofoetal Fibronectin ED-B Domain ; _BMRB_accession_number 4283 _BMRB_flat_file_name bmr4283.str _Entry_type original _Submission_date 1998-12-14 _Accession_date 1998-12-14 _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 Fattorusso Roberto . . 2 Pellecchia Maurizio . . 3 Viti Francesca . . 4 Neri Paolo . . 5 Neri Dario . . 6 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" 523 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-01 original author . stop_ _Original_release_date 1999-10-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Fattorusso, R., Pellecchia, M., Viti, F., Neri, P., Neri, D. and Wuthrich, K. "NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis," Structure 7, 381-390 (1999). ; _Citation_title 'NMR Structure of the Angiogenesis Marker Oncofoetal Fibronectin ED-B Domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99216534 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fattorusso Roberto . . 2 Pellecchia Maurizio . . 3 Viti Francesca . . 4 Neri Paolo . . 5 Neri Dario . . 6 Wuthrich Kurt . . stop_ _Journal_abbreviation Structure _Journal_volume 7 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 381 _Page_last 390 _Year 1999 _Details . loop_ _Keyword ED-B Fibronectin 'type-III domain' Angiogenesis stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'Markley et al, J. Biomol. NMR, 12 (1998), 1-23.' _Citation_title 'Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9729785 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Markley 'J L' L. . 2 Bax A . . 3 Arata Y . . 4 Hilbers 'C W' W. . 5 Kaptein R . . 6 Sykes 'B D' D. . 7 Wright 'P E' E. . 8 Wuthrich K . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 12 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1 _Page_last 23 _Year 1998 _Details ; The recommendations presented here are designed to support easier communication of NMR data and NMR structures of proteins and nucleic acids through unified nomenclature and reporting standards. Much of this document pertains to the reporting of data in journal articles; however, in the interest of the future development of structural biology, it is desirable that the bulk of the reported information be stored in computer-accessible form and be freely accessible to the scientific community in standardized formats for data exchange. These recommendations stem from an IUPAC-IUBMB-IUPAB inter-union venture with the direct involvement of ICSU and CODATA. The Task Group has reviewed previous formal recommendations and has extended them in the light of more recent developments in the field of biomolecular NMR spectroscopy. Drafts of the recommendations presented here have been examined critically by more than 50 specialists in the field and have gone through two rounds of extensive modification to incorporate suggestions and criticisms. ; save_ ################################## # Molecular system description # ################################## save_system_EDB _Saveframe_category molecular_system _Mol_system_name EDB _Abbreviation_common EDB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EDB $EDB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'fibronectin module' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EDB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'fibronectin extra domain B' _Abbreviation_common EDB _Molecular_mass 10000 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; MRGSEVPQLTDLSFVDITDS SIGLRWTPLNSSTIIGYRIT VVAAGEGIPIFEDFVDSSVG YYTVTGLEPGIDYDISVITL INGGESAPTTLTQQT ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 GLU 6 VAL 7 PRO 8 GLN 9 LEU 10 THR 11 ASP 12 LEU 13 SER 14 PHE 15 VAL 16 ASP 17 ILE 18 THR 19 ASP 20 SER 21 SER 22 ILE 23 GLY 24 LEU 25 ARG 26 TRP 27 THR 28 PRO 29 LEU 30 ASN 31 SER 32 SER 33 THR 34 ILE 35 ILE 36 GLY 37 TYR 38 ARG 39 ILE 40 THR 41 VAL 42 VAL 43 ALA 44 ALA 45 GLY 46 GLU 47 GLY 48 ILE 49 PRO 50 ILE 51 PHE 52 GLU 53 ASP 54 PHE 55 VAL 56 ASP 57 SER 58 SER 59 VAL 60 GLY 61 TYR 62 TYR 63 THR 64 VAL 65 THR 66 GLY 67 LEU 68 GLU 69 PRO 70 GLY 71 ILE 72 ASP 73 TYR 74 ASP 75 ILE 76 SER 77 VAL 78 ILE 79 THR 80 LEU 81 ILE 82 ASN 83 GLY 84 GLY 85 GLU 86 SER 87 ALA 88 PRO 89 THR 90 THR 91 LEU 92 THR 93 GLN 94 GLN 95 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 BMRB 19906 EDB 97.89 93 100.00 100.00 2.23e-56 PDB 2FNB "Nmr Structure Of The Fibronectin Ed-B Domain, Nmr, 20 Structures" 100.00 95 100.00 100.00 1.89e-58 PDB 2MNU "Backbone And Side Chain 1h, 13c, And 15n Chemical Shift Assignments For Edb And Specific Binding Aptide" 97.89 93 100.00 100.00 2.23e-56 PDB 4GH7 "Crystal Structure Of Anticalin N7a In Complex With Oncofetal Fibronectin Fragment Fn7b8" 95.79 285 100.00 100.00 1.16e-53 EMBL CAB52437 "fibronectin [Homo sapiens]" 95.79 147 100.00 100.00 2.97e-54 GB AAA52461 "fibronectin, partial [Homo sapiens]" 95.79 109 100.00 100.00 1.03e-54 GB AAA67749 "fibronectin ED-B, partial [Canis lupus familiaris]" 94.74 90 100.00 100.00 3.30e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EDB human 9606 Eukaryota Metazoa homo sapiens 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 $EDB 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EDB 1.3 mM . NaCl 40 mM . phosphate_buffer 20 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EDB 1.3 mM . NaCl 40 mM . phosphate_buffer 20 mM . D2O 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . n/a stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 _Indirect_shift_ratio_citation_label DSS H 1 'methyl protons' ppm 0.00 internal direct . . . . . DSS N 15 'methyl protons' ppm 0.00 internal indirect . . . 0.101329118 $citation_one 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name EDB _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 MET HA H 3.95 . 1 2 . 1 MET HB2 H 2.06 . 1 3 . 1 MET HB3 H 2.06 . 1 4 . 1 MET HG2 H 2.53 . 1 5 . 1 MET HG3 H 2.53 . 1 6 . 2 ARG N N 113.2 . 1 7 . 2 ARG H H 8.15 . 1 8 . 2 ARG HA H 4.36 . 1 9 . 2 ARG HB2 H 1.85 . 2 10 . 2 ARG HB3 H 1.76 . 2 11 . 2 ARG HG2 H 1.63 . 1 12 . 2 ARG HG3 H 1.63 . 1 13 . 2 ARG HD2 H 3.17 . 1 14 . 2 ARG HD3 H 3.17 . 1 15 . 3 GLY N N 111.6 . 1 16 . 3 GLY H H 7.98 . 1 17 . 3 GLY HA2 H 3.84 . 2 18 . 3 GLY HA3 H 3.81 . 2 19 . 4 SER N N 111.3 . 1 20 . 4 SER H H 8.18 . 1 21 . 4 SER HA H 4.42 . 1 22 . 4 SER HB2 H 3.83 . 2 23 . 4 SER HB3 H 3.81 . 2 24 . 5 GLU N N 122.4 . 1 25 . 5 GLU H H 8.47 . 1 26 . 5 GLU HA H 4.25 . 1 27 . 5 GLU HB2 H 1.89 . 1 28 . 5 GLU HB3 H 1.99 . 1 29 . 5 GLU HG2 H 2.21 . 2 30 . 5 GLU HG3 H 2.17 . 2 31 . 6 VAL N N 124.9 . 1 32 . 6 VAL H H 8.20 . 1 33 . 6 VAL HA H 4.18 . 1 34 . 6 VAL HB H 1.57 . 1 35 . 6 VAL HG1 H 0.82 . 1 36 . 6 VAL HG2 H 0.75 . 1 37 . 7 PRO HA H 4.39 . 1 38 . 7 PRO HB2 H 2.23 . 1 39 . 7 PRO HB3 H 1.92 . 1 40 . 7 PRO HG2 H 2.00 . 1 41 . 7 PRO HG3 H 2.00 . 1 42 . 7 PRO HD2 H 3.77 . 2 43 . 7 PRO HD3 H 3.52 . 2 44 . 8 GLN N N 118.4 . 1 45 . 8 GLN H H 8.11 . 1 46 . 8 GLN HA H 4.41 . 1 47 . 8 GLN HB2 H 2.08 . 2 48 . 8 GLN HB3 H 1.98 . 2 49 . 8 GLN HG2 H 2.37 . 2 50 . 8 GLN HG3 H 2.30 . 2 51 . 8 GLN NE2 N 112.4 . 1 52 . 8 GLN HE21 H 7.12 . 1 53 . 8 GLN HE22 H 6.70 . 1 54 . 9 LEU N N 120.7 . 1 55 . 9 LEU H H 8.15 . 1 56 . 9 LEU HA H 4.32 . 1 57 . 9 LEU HB2 H 1.19 . 2 58 . 9 LEU HB3 H 1.54 . 2 59 . 9 LEU HG H 0.92 . 1 60 . 9 LEU HD1 H -0.20 . 1 61 . 9 LEU HD2 H 0.64 . 1 62 . 10 THR N N 110.1 . 1 63 . 10 THR H H 8.20 . 1 64 . 10 THR HA H 4.72 . 1 65 . 10 THR HB H 4.38 . 1 66 . 10 THR HG2 H 1.19 . 1 67 . 11 ASP N N 121.4 . 1 68 . 11 ASP H H 7.62 . 1 69 . 11 ASP HA H 4.75 . 1 70 . 11 ASP HB2 H 2.89 . 2 71 . 11 ASP HB3 H 2.44 . 2 72 . 12 LEU N N 121.4 . 1 73 . 12 LEU H H 7.47 . 1 74 . 12 LEU HA H 4.81 . 1 75 . 12 LEU HB2 H 1.63 . 2 76 . 12 LEU HB3 H 1.05 . 2 77 . 12 LEU HG H 1.29 . 1 78 . 12 LEU HD1 H 0.60 . 1 79 . 12 LEU HD2 H 0.87 . 1 80 . 13 SER N N 121.7 . 1 81 . 13 SER H H 9.27 . 1 82 . 13 SER HA H 4.56 . 1 83 . 13 SER HB2 H 3.73 . 1 84 . 13 SER HB3 H 3.73 . 1 85 . 14 PHE N N 118.8 . 1 86 . 14 PHE H H 8.28 . 1 87 . 14 PHE HA H 5.87 . 1 88 . 14 PHE HB2 H 3.01 . 1 89 . 14 PHE HB3 H 2.97 . 1 90 . 14 PHE HD1 H 7.27 . 1 91 . 14 PHE HD2 H 7.27 . 1 92 . 14 PHE HE1 H 7.14 . 1 93 . 14 PHE HE2 H 7.14 . 1 94 . 14 PHE HZ H 7.04 . 1 95 . 15 VAL N N 118.8 . 1 96 . 15 VAL H H 9.13 . 1 97 . 15 VAL HA H 4.46 . 1 98 . 15 VAL HB H 2.05 . 1 99 . 15 VAL HG1 H 0.83 . 1 100 . 15 VAL HG2 H 0.77 . 1 101 . 16 ASP N N 118.5 . 1 102 . 16 ASP H H 8.39 . 1 103 . 16 ASP HA H 4.32 . 1 104 . 16 ASP HB2 H 2.60 . 1 105 . 16 ASP HB3 H 2.60 . 1 106 . 17 ILE N N 119.9 . 1 107 . 17 ILE H H 8.20 . 1 108 . 17 ILE HA H 4.09 . 1 109 . 17 ILE HB H 1.73 . 1 110 . 17 ILE HG2 H 0.88 . 1 111 . 17 ILE HG12 H 1.50 . 2 112 . 17 ILE HG13 H 0.94 . 2 113 . 17 ILE HD1 H 0.77 . 1 114 . 18 THR N N 119.9 . 1 115 . 18 THR H H 8.75 . 1 116 . 18 THR HA H 4.51 . 1 117 . 18 THR HB H 4.50 . 1 118 . 18 THR HG2 H 1.10 . 1 119 . 19 ASP N N 116.3 . 1 120 . 19 ASP H H 8.44 . 1 121 . 19 ASP HA H 4.38 . 1 122 . 19 ASP HB2 H 2.67 . 1 123 . 19 ASP HB3 H 2.67 . 1 124 . 20 SER N N 108.8 . 1 125 . 20 SER H H 7.89 . 1 126 . 20 SER HA H 4.71 . 1 127 . 20 SER HB2 H 4.02 . 1 128 . 20 SER HB3 H 3.63 . 1 129 . 21 SER N N 117.2 . 1 130 . 21 SER H H 7.57 . 1 131 . 21 SER HA H 5.21 . 1 132 . 21 SER HB2 H 3.66 . 1 133 . 21 SER HB3 H 3.62 . 1 134 . 22 ILE N N 118.8 . 1 135 . 22 ILE H H 8.44 . 1 136 . 22 ILE HA H 4.37 . 1 137 . 22 ILE HB H 1.34 . 1 138 . 22 ILE HG2 H 0.63 . 1 139 . 22 ILE HG12 H 0.87 . 1 140 . 22 ILE HG13 H 0.87 . 1 141 . 22 ILE HD1 H 0.32 . 1 142 . 23 GLY N N 114.5 . 1 143 . 23 GLY H H 8.40 . 1 144 . 23 GLY HA2 H 4.76 . 1 145 . 23 GLY HA3 H 3.49 . 1 146 . 24 LEU N N 123.1 . 1 147 . 24 LEU H H 9.03 . 1 148 . 24 LEU HA H 5.33 . 1 149 . 24 LEU HB2 H 2.03 . 1 150 . 24 LEU HB3 H 1.61 . 1 151 . 24 LEU HG H 1.84 . 1 152 . 24 LEU HD1 H 0.82 . 1 153 . 24 LEU HD2 H 0.85 . 1 154 . 25 ARG N N 119.6 . 1 155 . 25 ARG H H 8.77 . 1 156 . 25 ARG HA H 5.05 . 1 157 . 25 ARG HB2 H 1.65 . 2 158 . 25 ARG HB3 H 1.60 . 2 159 . 25 ARG HG2 H 1.43 . 1 160 . 25 ARG HG3 H 1.43 . 1 161 . 25 ARG HD2 H 3.11 . 2 162 . 25 ARG HD3 H 3.04 . 2 163 . 25 ARG NE N 106.8 . 1 164 . 25 ARG HE H 7.01 . 1 165 . 26 TRP N N 121.7 . 1 166 . 26 TRP H H 8.38 . 1 167 . 26 TRP HA H 4.59 . 1 168 . 26 TRP HB2 H 2.72 . 2 169 . 26 TRP HB3 H 3.22 . 2 170 . 26 TRP NE1 N 126.0 . 1 171 . 26 TRP HD1 H 6.13 . 1 172 . 26 TRP HE3 H 6.70 . 1 173 . 26 TRP HE1 H 7.46 . 1 174 . 26 TRP HZ3 H 6.43 . 1 175 . 26 TRP HZ2 H 6.69 . 1 176 . 26 TRP HH2 H 6.43 . 1 177 . 27 THR N N 118.8 . 1 178 . 27 THR H H 9.59 . 1 179 . 27 THR HA H 4.48 . 1 180 . 27 THR HB H 4.12 . 1 181 . 27 THR HG2 H 1.18 . 1 182 . 28 PRO HA H 4.22 . 1 183 . 28 PRO HB2 H 2.62 . 2 184 . 28 PRO HB3 H 1.92 . 2 185 . 28 PRO HG2 H 1.82 . 2 186 . 28 PRO HG3 H 1.48 . 2 187 . 28 PRO HD2 H 4.12 . 2 188 . 28 PRO HD3 H 3.58 . 2 189 . 29 LEU N N 123.9 . 1 190 . 29 LEU H H 7.72 . 1 191 . 29 LEU HA H 4.27 . 1 192 . 29 LEU HB2 H 1.81 . 2 193 . 29 LEU HB3 H 1.46 . 2 194 . 29 LEU HG H 1.88 . 1 195 . 29 LEU HD1 H 0.64 . 1 196 . 29 LEU HD2 H 0.93 . 1 197 . 30 ASN N N 119.6 . 1 198 . 30 ASN H H 8.60 . 1 199 . 30 ASN HA H 4.72 . 1 200 . 30 ASN HB2 H 2.85 . 2 201 . 30 ASN HB3 H 2.72 . 2 202 . 30 ASN ND2 N 112.0 . 1 203 . 30 ASN HD21 H 7.55 . 1 204 . 30 ASN HD22 H 6.84 . 1 205 . 31 SER N N 114.9 . 1 206 . 31 SER H H 7.57 . 1 207 . 31 SER HA H 4.57 . 1 208 . 31 SER HB2 H 3.52 . 2 209 . 31 SER HB3 H 3.96 . 2 210 . 32 SER N N 115.2 . 1 211 . 32 SER H H 8.17 . 1 212 . 32 SER HA H 4.35 . 1 213 . 32 SER HB2 H 4.02 . 2 214 . 32 SER HB3 H 3.94 . 2 215 . 33 THR N N 111.1 . 1 216 . 33 THR H H 7.83 . 1 217 . 33 THR HA H 4.76 . 1 218 . 33 THR HB H 4.20 . 1 219 . 33 THR HG2 H 1.20 . 1 220 . 34 ILE N N 120.6 . 1 221 . 34 ILE H H 7.10 . 1 222 . 34 ILE HA H 4.22 . 1 223 . 34 ILE HB H 1.89 . 1 224 . 34 ILE HG2 H 0.79 . 1 225 . 34 ILE HG12 H 1.47 . 2 226 . 34 ILE HG13 H 1.00 . 2 227 . 34 ILE HD1 H 0.77 . 1 228 . 35 ILE N N 121.5 . 1 229 . 35 ILE H H 8.63 . 1 230 . 35 ILE HA H 4.51 . 1 231 . 35 ILE HB H 1.94 . 1 232 . 35 ILE HG2 H 0.87 . 1 233 . 35 ILE HG12 H 1.10 . 1 234 . 35 ILE HG13 H 1.10 . 1 235 . 35 ILE HD1 H 0.69 . 1 236 . 36 GLY N N 108.8 . 1 237 . 36 GLY H H 7.24 . 1 238 . 36 GLY HA2 H 3.11 . 1 239 . 36 GLY HA3 H 4.54 . 1 240 . 37 TYR N N 115.6 . 1 241 . 37 TYR H H 8.53 . 1 242 . 37 TYR HA H 5.28 . 1 243 . 37 TYR HB2 H 2.40 . 2 244 . 37 TYR HB3 H 2.28 . 2 245 . 37 TYR HD1 H 6.86 . 1 246 . 37 TYR HD2 H 6.86 . 1 247 . 37 TYR HE1 H 7.02 . 1 248 . 37 TYR HE2 H 7.02 . 1 249 . 37 TYR HH H 10.26 . 1 250 . 38 ARG N N 122.4 . 1 251 . 38 ARG H H 9.16 . 1 252 . 38 ARG HA H 5.02 . 1 253 . 38 ARG HB2 H 1.61 . 1 254 . 38 ARG HB3 H 1.61 . 1 255 . 38 ARG HG2 H 1.28 . 2 256 . 38 ARG HG3 H 1.18 . 2 257 . 38 ARG HD2 H 3.03 . 1 258 . 38 ARG HD3 H 3.03 . 1 259 . 38 ARG NE N 106.6 . 1 260 . 38 ARG HE H 6.87 . 1 261 . 39 ILE N N 128.9 . 1 262 . 39 ILE H H 8.73 . 1 263 . 39 ILE HA H 4.83 . 1 264 . 39 ILE HB H 1.06 . 1 265 . 39 ILE HG2 H 0.47 . 1 266 . 39 ILE HG12 H 0.85 . 2 267 . 39 ILE HG13 H 0.59 . 2 268 . 39 ILE HD1 H 0.19 . 1 269 . 40 THR N N 117.8 . 1 270 . 40 THR H H 8.83 . 1 271 . 40 THR HA H 5.05 . 1 272 . 40 THR HB H 3.88 . 1 273 . 40 THR HG2 H 1.07 . 1 274 . 41 VAL N N 122.4 . 1 275 . 41 VAL H H 8.41 . 1 276 . 41 VAL HA H 4.71 . 1 277 . 41 VAL HB H 2.00 . 1 278 . 41 VAL HG1 H 0.72 . 1 279 . 41 VAL HG2 H 0.88 . 1 280 . 42 VAL N N 127.2 . 1 281 . 42 VAL H H 8.87 . 1 282 . 42 VAL HA H 4.62 . 1 283 . 42 VAL HB H 1.99 . 1 284 . 42 VAL HG1 H 0.85 . 1 285 . 42 VAL HG2 H 0.82 . 1 286 . 43 ALA N N 130.7 . 1 287 . 43 ALA H H 9.26 . 1 288 . 43 ALA HA H 4.39 . 1 289 . 43 ALA HB H 1.26 . 1 290 . 44 ALA N N 126.1 . 1 291 . 44 ALA H H 8.24 . 1 292 . 44 ALA HA H 3.97 . 1 293 . 44 ALA HB H 1.22 . 1 294 . 45 GLY N N 111.3 . 1 295 . 45 GLY H H 8.66 . 1 296 . 45 GLY HA2 H 4.06 . 2 297 . 45 GLY HA3 H 3.66 . 2 298 . 46 GLU N N 119.7 . 1 299 . 46 GLU H H 8.10 . 1 300 . 46 GLU HA H 4.41 . 1 301 . 46 GLU HB2 H 2.12 . 2 302 . 46 GLU HB3 H 2.05 . 2 303 . 46 GLU HG2 H 2.24 . 1 304 . 46 GLU HG3 H 2.24 . 1 305 . 47 GLY N N 107.0 . 1 306 . 47 GLY H H 8.34 . 1 307 . 47 GLY HA2 H 3.87 . 1 308 . 47 GLY HA3 H 3.87 . 1 309 . 48 ILE N N 119.9 . 1 310 . 48 ILE H H 7.31 . 1 311 . 48 ILE HA H 4.57 . 1 312 . 48 ILE HB H 1.81 . 1 313 . 48 ILE HG2 H 0.94 . 1 314 . 48 ILE HG12 H 1.11 . 1 315 . 48 ILE HG13 H 1.46 . 1 316 . 48 ILE HD1 H 0.82 . 1 317 . 49 PRO HA H 4.55 . 1 318 . 49 PRO HB2 H 2.21 . 2 319 . 49 PRO HB3 H 1.84 . 2 320 . 49 PRO HG2 H 2.08 . 1 321 . 49 PRO HG3 H 2.08 . 1 322 . 49 PRO HD2 H 4.01 . 1 323 . 49 PRO HD3 H 3.69 . 1 324 . 50 ILE N N 121.7 . 1 325 . 50 ILE H H 8.80 . 1 326 . 50 ILE HA H 4.30 . 1 327 . 50 ILE HB H 1.89 . 1 328 . 50 ILE HG2 H 0.99 . 1 329 . 50 ILE HG12 H 1.55 . 2 330 . 50 ILE HG13 H 1.34 . 2 331 . 50 ILE HD1 H 0.94 . 1 332 . 51 PHE N N 122.4 . 1 333 . 51 PHE H H 8.12 . 1 334 . 51 PHE HA H 4.77 . 1 335 . 51 PHE HB2 H 3.17 . 2 336 . 51 PHE HB3 H 2.73 . 2 337 . 51 PHE HD1 H 7.10 . 1 338 . 51 PHE HD2 H 7.10 . 1 339 . 51 PHE HE1 H 7.41 . 1 340 . 51 PHE HE2 H 7.41 . 1 341 . 51 PHE HZ H 7.54 . 1 342 . 52 GLU N N 124.2 . 1 343 . 52 GLU H H 7.57 . 1 344 . 52 GLU HA H 5.32 . 1 345 . 52 GLU HB2 H 1.77 . 1 346 . 52 GLU HB3 H 1.77 . 1 347 . 52 GLU HG2 H 1.98 . 1 348 . 52 GLU HG3 H 1.98 . 1 349 . 53 ASP N N 120.6 . 1 350 . 53 ASP H H 8.79 . 1 351 . 53 ASP HA H 4.89 . 1 352 . 53 ASP HB2 H 2.68 . 2 353 . 53 ASP HB3 H 2.28 . 2 354 . 54 PHE N N 121.0 . 1 355 . 54 PHE H H 8.81 . 1 356 . 54 PHE HA H 5.43 . 1 357 . 54 PHE HB2 H 2.95 . 2 358 . 54 PHE HB3 H 2.90 . 2 359 . 54 PHE HD1 H 7.06 . 1 360 . 54 PHE HD2 H 7.06 . 1 361 . 54 PHE HE1 H 7.13 . 1 362 . 54 PHE HE2 H 7.13 . 1 363 . 54 PHE HZ H 7.17 . 1 364 . 55 VAL N N 117.4 . 1 365 . 55 VAL H H 8.55 . 1 366 . 55 VAL HA H 4.72 . 1 367 . 55 VAL HB H 2.31 . 1 368 . 55 VAL HG1 H 1.07 . 1 369 . 55 VAL HG2 H 1.12 . 1 370 . 56 ASP N N 119.2 . 1 371 . 56 ASP H H 8.23 . 1 372 . 56 ASP HA H 4.68 . 1 373 . 56 ASP HB2 H 3.12 . 2 374 . 56 ASP HB3 H 2.74 . 2 375 . 57 SER N N 111.3 . 1 376 . 57 SER H H 7.71 . 1 377 . 57 SER HA H 4.02 . 1 378 . 57 SER HB2 H 3.42 . 1 379 . 57 SER HB3 H 3.42 . 1 380 . 58 SER N N 117.4 . 1 381 . 58 SER H H 8.72 . 1 382 . 58 SER HA H 4.51 . 1 383 . 58 SER HB2 H 4.04 . 1 384 . 58 SER HB3 H 3.87 . 1 385 . 59 VAL N N 127.1 . 1 386 . 59 VAL H H 7.73 . 1 387 . 59 VAL HA H 3.64 . 1 388 . 59 VAL HB H 2.34 . 1 389 . 59 VAL HG1 H 1.03 . 1 390 . 59 VAL HG2 H 1.08 . 1 391 . 60 GLY N N 109.1 . 1 392 . 60 GLY H H 7.43 . 1 393 . 60 GLY HA2 H 2.39 . 1 394 . 60 GLY HA3 H 2.74 . 1 395 . 61 TYR N N 117.8 . 1 396 . 61 TYR H H 6.34 . 1 397 . 61 TYR HA H 5.04 . 1 398 . 61 TYR HB2 H 2.71 . 2 399 . 61 TYR HB3 H 2.59 . 2 400 . 61 TYR HD1 H 6.81 . 1 401 . 61 TYR HD2 H 6.81 . 1 402 . 61 TYR HE1 H 6.61 . 1 403 . 61 TYR HE2 H 6.61 . 1 404 . 62 TYR N N 125.3 . 1 405 . 62 TYR H H 8.31 . 1 406 . 62 TYR HA H 4.31 . 1 407 . 62 TYR HB2 H 3.13 . 2 408 . 62 TYR HB3 H 2.65 . 2 409 . 62 TYR HD1 H 6.92 . 1 410 . 62 TYR HD2 H 6.92 . 1 411 . 62 TYR HE1 H 6.75 . 1 412 . 62 TYR HE2 H 6.75 . 1 413 . 63 THR N N 122.8 . 1 414 . 63 THR H H 7.45 . 1 415 . 63 THR HA H 4.78 . 1 416 . 63 THR HB H 3.62 . 1 417 . 63 THR HG2 H 0.90 . 1 418 . 64 VAL N N 105.2 . 1 419 . 64 VAL H H 9.09 . 1 420 . 64 VAL HA H 3.97 . 1 421 . 64 VAL HB H 2.01 . 1 422 . 64 VAL HG1 H 0.68 . 1 423 . 64 VAL HG2 H 0.95 . 1 424 . 65 THR N N 117.0 . 1 425 . 65 THR H H 7.92 . 1 426 . 65 THR HA H 4.69 . 1 427 . 65 THR HB H 4.13 . 1 428 . 65 THR HG2 H 0.95 . 1 429 . 66 GLY N N 106.3 . 1 430 . 66 GLY H H 8.35 . 1 431 . 66 GLY HA2 H 3.89 . 2 432 . 66 GLY HA3 H 3.68 . 2 433 . 67 LEU N N 119.5 . 1 434 . 67 LEU H H 7.99 . 1 435 . 67 LEU HA H 4.04 . 1 436 . 67 LEU HB2 H 1.12 . 1 437 . 67 LEU HB3 H 1.16 . 1 438 . 67 LEU HG H 0.96 . 1 439 . 67 LEU HD1 H 0.19 . 1 440 . 67 LEU HD2 H -0.21 . 1 441 . 68 GLU N N 122.8 . 1 442 . 68 GLU H H 8.38 . 1 443 . 68 GLU HA H 4.66 . 1 444 . 68 GLU HB2 H 1.92 . 1 445 . 68 GLU HB3 H 2.02 . 1 446 . 68 GLU HG2 H 2.29 . 2 447 . 68 GLU HG3 H 2.23 . 2 448 . 69 PRO HA H 4.63 . 1 449 . 69 PRO HB2 H 2.28 . 2 450 . 69 PRO HB3 H 1.89 . 2 451 . 69 PRO HG2 H 1.99 . 1 452 . 69 PRO HG3 H 1.99 . 1 453 . 69 PRO HD2 H 3.85 . 2 454 . 69 PRO HD3 H 3.69 . 2 455 . 70 GLY N N 109.1 . 1 456 . 70 GLY H H 8.55 . 1 457 . 70 GLY HA2 H 3.99 . 2 458 . 70 GLY HA3 H 3.65 . 2 459 . 71 ILE N N 121.4 . 1 460 . 71 ILE H H 7.41 . 1 461 . 71 ILE HA H 4.05 . 1 462 . 71 ILE HB H 1.61 . 1 463 . 71 ILE HG2 H 0.18 . 1 464 . 71 ILE HG12 H 1.16 . 2 465 . 71 ILE HG13 H 0.95 . 2 466 . 71 ILE HD1 H 0.63 . 1 467 . 72 ASP N N 124.6 . 1 468 . 72 ASP H H 7.98 . 1 469 . 72 ASP HA H 4.81 . 1 470 . 72 ASP HB2 H 2.31 . 1 471 . 72 ASP HB3 H 2.41 . 1 472 . 73 TYR N N 121.4 . 1 473 . 73 TYR H H 8.69 . 1 474 . 73 TYR HA H 5.07 . 1 475 . 73 TYR HB2 H 2.64 . 1 476 . 73 TYR HB3 H 2.64 . 1 477 . 73 TYR HD1 H 6.84 . 1 478 . 73 TYR HD2 H 6.84 . 1 479 . 73 TYR HE1 H 6.84 . 1 480 . 73 TYR HE2 H 6.84 . 1 481 . 74 ASP N N 122.6 . 1 482 . 74 ASP H H 9.24 . 1 483 . 74 ASP HA H 5.19 . 1 484 . 74 ASP HB2 H 2.54 . 1 485 . 74 ASP HB3 H 2.27 . 1 486 . 75 ILE N N 105.9 . 1 487 . 75 ILE H H 9.30 . 1 488 . 75 ILE HA H 4.94 . 1 489 . 75 ILE HB H 1.92 . 1 490 . 75 ILE HG2 H 0.87 . 1 491 . 75 ILE HG12 H 1.67 . 2 492 . 75 ILE HG13 H 1.08 . 2 493 . 75 ILE HD1 H 0.79 . 1 494 . 76 SER N N 120.6 . 1 495 . 76 SER H H 8.98 . 1 496 . 76 SER HA H 5.62 . 1 497 . 76 SER HB2 H 3.59 . 2 498 . 76 SER HB3 H 3.41 . 2 499 . 77 VAL N N 119.9 . 1 500 . 77 VAL H H 8.32 . 1 501 . 77 VAL HA H 4.80 . 1 502 . 77 VAL HB H 1.23 . 1 503 . 77 VAL HG1 H -0.21 . 1 504 . 77 VAL HG2 H 0.28 . 1 505 . 78 ILE N N 130.0 . 1 506 . 78 ILE H H 9.25 . 1 507 . 78 ILE HA H 3.98 . 1 508 . 78 ILE HB H 1.60 . 1 509 . 78 ILE HG2 H 0.90 . 1 510 . 78 ILE HG12 H 1.19 . 1 511 . 78 ILE HG13 H 1.19 . 1 512 . 78 ILE HD1 H 0.77 . 1 513 . 79 THR N N 124.6 . 1 514 . 79 THR H H 8.63 . 1 515 . 79 THR HA H 4.21 . 1 516 . 79 THR HB H 3.92 . 1 517 . 79 THR HG2 H 1.11 . 1 518 . 80 LEU N N 125.3 . 1 519 . 80 LEU H H 8.46 . 1 520 . 80 LEU HA H 4.89 . 1 521 . 80 LEU HB2 H 1.46 . 2 522 . 80 LEU HB3 H 1.32 . 2 523 . 80 LEU HG H 1.58 . 1 524 . 80 LEU HD1 H 0.86 . 1 525 . 80 LEU HD2 H 0.83 . 1 526 . 81 ILE N N 115.6 . 1 527 . 81 ILE H H 8.00 . 1 528 . 81 ILE HA H 4.84 . 1 529 . 81 ILE HB H 1.82 . 1 530 . 81 ILE HG2 H 0.77 . 1 531 . 81 ILE HG12 H 1.10 . 2 532 . 81 ILE HG13 H 0.88 . 2 533 . 81 ILE HD1 H 0.67 . 1 534 . 82 ASN N N 119.9 . 1 535 . 82 ASN H H 8.88 . 1 536 . 82 ASN HA H 4.56 . 1 537 . 82 ASN HB2 H 2.76 . 2 538 . 82 ASN HB3 H 2.65 . 2 539 . 82 ASN ND2 N 112.7 . 1 540 . 82 ASN HD21 H 7.61 . 1 541 . 82 ASN HD22 H 6.91 . 1 542 . 83 GLY N N 115.2 . 1 543 . 83 GLY H H 8.87 . 1 544 . 83 GLY HA2 H 4.05 . 2 545 . 83 GLY HA3 H 3.78 . 2 546 . 84 GLY N N 107.3 . 1 547 . 84 GLY H H 7.62 . 1 548 . 84 GLY HA2 H 4.23 . 2 549 . 84 GLY HA3 H 3.77 . 2 550 . 85 GLU N N 116.0 . 1 551 . 85 GLU H H 8.23 . 1 552 . 85 GLU HA H 5.20 . 1 553 . 85 GLU HB2 H 1.88 . 1 554 . 85 GLU HB3 H 1.88 . 1 555 . 85 GLU HG2 H 2.15 . 1 556 . 85 GLU HG3 H 2.15 . 1 557 . 86 SER N N 116.7 . 1 558 . 86 SER H H 8.75 . 1 559 . 86 SER HA H 4.43 . 1 560 . 86 SER HB2 H 4.13 . 1 561 . 86 SER HB3 H 3.62 . 1 562 . 87 ALA N N 122.1 . 1 563 . 87 ALA H H 8.36 . 1 564 . 87 ALA HA H 4.52 . 1 565 . 87 ALA HB H 1.33 . 1 566 . 88 PRO HA H 4.26 . 1 567 . 88 PRO HB2 H 1.93 . 2 568 . 88 PRO HB3 H 1.71 . 2 569 . 88 PRO HG2 H 2.06 . 1 570 . 88 PRO HG3 H 2.06 . 1 571 . 88 PRO HD2 H 3.67 . 1 572 . 88 PRO HD3 H 3.67 . 1 573 . 89 THR N N 118.8 . 1 574 . 89 THR H H 7.86 . 1 575 . 89 THR HA H 4.40 . 1 576 . 89 THR HB H 4.03 . 1 577 . 89 THR HG2 H 1.16 . 1 578 . 90 THR N N 121.7 . 1 579 . 90 THR H H 8.29 . 1 580 . 90 THR HA H 5.02 . 1 581 . 90 THR HB H 3.68 . 1 582 . 90 THR HG2 H 0.98 . 1 583 . 91 LEU N N 127.5 . 1 584 . 91 LEU H H 8.96 . 1 585 . 91 LEU HA H 4.56 . 1 586 . 91 LEU HB2 H 1.31 . 1 587 . 91 LEU HB3 H 1.31 . 1 588 . 91 LEU HG H 1.28 . 1 589 . 91 LEU HD1 H 0.26 . 1 590 . 91 LEU HD2 H 0.68 . 1 591 . 92 THR N N 117.0 . 1 592 . 92 THR H H 8.35 . 1 593 . 92 THR HA H 5.38 . 1 594 . 92 THR HB H 3.87 . 1 595 . 92 THR HG2 H 1.13 . 1 596 . 93 GLN N N 126.4 . 1 597 . 93 GLN H H 9.06 . 1 598 . 93 GLN HA H 4.60 . 1 599 . 93 GLN HB2 H 1.97 . 1 600 . 93 GLN HB3 H 1.97 . 1 601 . 93 GLN HG2 H 2.11 . 1 602 . 93 GLN HG3 H 2.11 . 1 603 . 93 GLN NE2 N 111.0 . 1 604 . 93 GLN HE21 H 7.22 . 1 605 . 93 GLN HE22 H 6.57 . 1 606 . 94 GLN N N 124.6 . 1 607 . 94 GLN H H 8.27 . 1 608 . 94 GLN HA H 4.88 . 1 609 . 94 GLN HB2 H 1.99 . 1 610 . 94 GLN HB3 H 2.03 . 1 611 . 94 GLN HG2 H 2.31 . 2 612 . 94 GLN HG3 H 2.20 . 2 613 . 94 GLN NE2 N 112.5 . 1 614 . 94 GLN HE21 H 7.73 . 1 615 . 94 GLN HE22 H 6.66 . 1 616 . 95 THR N N 122.8 . 1 617 . 95 THR H H 8.59 . 1 618 . 95 THR HA H 4.40 . 1 619 . 95 THR HB H 4.41 . 1 620 . 95 THR HG2 H 1.09 . 1 stop_ save_