data_16322 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Extracellular CD147 (EMMPRIN): Isoforms -2 ; _BMRB_accession_number 16322 _BMRB_flat_file_name bmr16322.str _Entry_type original _Submission_date 2009-05-28 _Accession_date 2009-05-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignments for the extracellular domains of CD147 isoforms -2 and -3. Residues 207-214 exist in both cis and trans conformations and the chemical shift assignments are provided here for each isomer for isoform-2.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schelgel Jennifer . . 2 Redzic Jasmina S. . 3 Porter Christopher . . 4 Yurchenko Vyacheslav . . 5 Bukrinsky Michael . . 6 Armstrong Geoffrey S. . 7 Zhang Fengli . . 8 Isern Nancy G. . 9 Degregori James . . 10 Hodges Robert . . 11 Eisenmesser Elan Z. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 182 "13C chemical shifts" 356 "15N chemical shifts" 182 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-01-21 update BMRB 'complete entry citation' 2009-06-23 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 7433 'Extracellular CD147 Isoform-3' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution characterization of the extracellular region of CD147 and its interaction with its enzyme ligand cyclophilin A.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19500591 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlegel Jennifer . . 2 Redzic Jasmina S. . 3 Porter Christopher C. . 4 Yurchenko Vyacheslav . . 5 Bukrinsky Michael . . 6 Labeikovsky Wladimir . . 7 Armstrong Geoffrey S. . 8 Zhang Fengli . . 9 Isern Nancy G. . 10 DeGregori James . . 11 Hodges Robert . . 12 Eisenmesser 'Elan Zohar' . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 391 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 518 _Page_last 535 _Year 2009 _Details . loop_ _Keyword CD147 cyclophilin EMMPRIN isomerization proline stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CD147 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Extracellular CD147 Iso-2, trans' $CD147_22-214 'Extracellular CD147 Iso-2, cis' $CD147_22-214 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CD147_22-214 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CD147_22-214 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Inducer of matrix metalloproteinases' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; GSHMMAAGTVFTTVEDLGSK ILLTCSLNDSATEVTGHRWL KGGVVLKEDALPGQKTEFKV DSDDQWGEYSCVFLPEPMGT ANIQLHGPPRVKAVKSSEHI NEGETAMLVCKSESVPPVTD WAWYKITDSEDKALMNGSES RFFVSSSQGRSELHIENLNM EADPGQYRCNGTSSKGSDQA IITLRVRSHLAALWPFLG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 17 GLY 2 18 SER 3 19 HIS 4 20 MET 5 21 MET 6 22 ALA 7 23 ALA 8 24 GLY 9 25 THR 10 26 VAL 11 27 PHE 12 28 THR 13 29 THR 14 30 VAL 15 31 GLU 16 32 ASP 17 33 LEU 18 34 GLY 19 35 SER 20 36 LYS 21 37 ILE 22 38 LEU 23 39 LEU 24 40 THR 25 41 CYS 26 42 SER 27 43 LEU 28 44 ASN 29 45 ASP 30 46 SER 31 47 ALA 32 48 THR 33 49 GLU 34 50 VAL 35 51 THR 36 52 GLY 37 53 HIS 38 54 ARG 39 55 TRP 40 56 LEU 41 57 LYS 42 58 GLY 43 59 GLY 44 60 VAL 45 61 VAL 46 62 LEU 47 63 LYS 48 64 GLU 49 65 ASP 50 66 ALA 51 67 LEU 52 68 PRO 53 69 GLY 54 70 GLN 55 71 LYS 56 72 THR 57 73 GLU 58 74 PHE 59 75 LYS 60 76 VAL 61 77 ASP 62 78 SER 63 79 ASP 64 80 ASP 65 81 GLN 66 82 TRP 67 83 GLY 68 84 GLU 69 85 TYR 70 86 SER 71 87 CYS 72 88 VAL 73 89 PHE 74 90 LEU 75 91 PRO 76 92 GLU 77 93 PRO 78 94 MET 79 95 GLY 80 96 THR 81 97 ALA 82 98 ASN 83 99 ILE 84 100 GLN 85 101 LEU 86 102 HIS 87 103 GLY 88 104 PRO 89 105 PRO 90 106 ARG 91 107 VAL 92 108 LYS 93 109 ALA 94 110 VAL 95 111 LYS 96 112 SER 97 113 SER 98 114 GLU 99 115 HIS 100 116 ILE 101 117 ASN 102 118 GLU 103 119 GLY 104 120 GLU 105 121 THR 106 122 ALA 107 123 MET 108 124 LEU 109 125 VAL 110 126 CYS 111 127 LYS 112 128 SER 113 129 GLU 114 130 SER 115 131 VAL 116 132 PRO 117 133 PRO 118 134 VAL 119 135 THR 120 136 ASP 121 137 TRP 122 138 ALA 123 139 TRP 124 140 TYR 125 141 LYS 126 142 ILE 127 143 THR 128 144 ASP 129 145 SER 130 146 GLU 131 147 ASP 132 148 LYS 133 149 ALA 134 150 LEU 135 151 MET 136 152 ASN 137 153 GLY 138 154 SER 139 155 GLU 140 156 SER 141 157 ARG 142 158 PHE 143 159 PHE 144 160 VAL 145 161 SER 146 162 SER 147 163 SER 148 164 GLN 149 165 GLY 150 166 ARG 151 167 SER 152 168 GLU 153 169 LEU 154 170 HIS 155 171 ILE 156 172 GLU 157 173 ASN 158 174 LEU 159 175 ASN 160 176 MET 161 177 GLU 162 178 ALA 163 179 ASP 164 180 PRO 165 181 GLY 166 182 GLN 167 183 TYR 168 184 ARG 169 185 CYS 170 186 ASN 171 187 GLY 172 188 THR 173 189 SER 174 190 SER 175 191 LYS 176 192 GLY 177 193 SER 178 194 ASP 179 195 GLN 180 196 ALA 181 197 ILE 182 198 ILE 183 199 THR 184 200 LEU 185 201 ARG 186 202 VAL 187 203 ARG 188 204 SER 189 205 HIS 190 206 LEU 191 207 ALA 192 208 ALA 193 209 LEU 194 210 TRP 195 211 PRO 196 212 PHE 197 213 LEU 198 214 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 3B5H "Crystal Structure Of The Extracellular Portion Of Hab18gCD147" 92.93 184 100.00 100.00 6.35e-133 PDB 4U0Q "Plasmodium Falciparum Reticulocyte-binding Protein Homologue 5 (pfrh5) Bound To Basigin" 97.47 269 100.00 100.00 6.60e-140 DBJ BAA08109 "basigin [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 DBJ BAB88938 "EMMPRIN [Homo sapiens]" 97.47 269 98.96 98.96 4.07e-137 DBJ BAC67167 "EMMPRIN [Bos taurus]" 92.93 205 100.00 100.00 5.53e-133 DBJ BAC67168 "cervical EMMPRIN [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 DBJ BAC76828 "CD147 [Homo sapiens]" 97.47 269 99.48 99.48 4.05e-139 EMBL CAA45716 "M6 antigen [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 EMBL CAH92402 "hypothetical protein [Pongo abelii]" 97.47 269 100.00 100.00 6.60e-140 GB AAA68936 "collagenase stimulatory factor [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 GB AAA91084 "amino acid feature: intracellular domain, aa 707 .. 829; amino acid feature: transmembrane domain, aa 638 .. 706; amino acid fe" 97.47 269 100.00 100.00 6.60e-140 GB AAB41120 "extracellular matrix metalloproteinase inducer [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 GB AAC33279 "basigin [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 GB AAD10704 "EMMPRIN [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 REF NP_001128860 "basigin (Ok blood group) precursor [Pongo abelii]" 97.47 269 100.00 100.00 6.60e-140 REF NP_001719 "basigin isoform 1 precursor [Homo sapiens]" 98.48 385 97.95 98.97 3.95e-136 REF NP_940991 "basigin isoform 2 [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 REF NP_940992 "basigin isoform 3 [Homo sapiens]" 61.11 176 100.00 100.00 6.24e-83 REF XP_005259676 "PREDICTED: basigin isoform X1 [Homo sapiens]" 97.47 269 100.00 100.00 6.60e-140 SP P35613 "RecName: Full=Basigin; AltName: Full=5F7; AltName: Full=Collagenase stimulatory factor; AltName: Full=Extracellular matrix meta" 98.48 385 97.95 98.97 3.95e-136 SP Q865R3 "RecName: Full=Basigin; AltName: Full=EMMPRIN; AltName: CD_antigen=CD147; Flags: Precursor" 92.93 205 100.00 100.00 5.53e-133 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CD147_22-214 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 $CD147_22-214 'recombinant technology' . Escherichia coli DE3 pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' imidazole 50 mM 'natural abundance' $CD147_22-214 0.5 mM '[U-99% 13C; U-99% 15N]' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 720 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.232 . M pH 6.5 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 water C 13 protons ppm 4.77 internal indirect . . . 0.25144953 water H 1 protons ppm 4.77 internal direct . . . 1.00000000 water N 15 protons ppm 4.77 internal indirect . . . 0.10132911 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_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Extracellular CD147 Iso-2, trans' _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 22 6 ALA H H 8.289 0.05 1 2 22 6 ALA CA C 51.768 0.3 1 3 22 6 ALA CB C 18.666 0.3 1 4 22 6 ALA N N 125.573 0.3 1 5 23 7 ALA H H 8.372 0.05 1 6 23 7 ALA CA C 52.061 0.3 1 7 23 7 ALA CB C 19.152 0.3 1 8 23 7 ALA N N 124.04 0.3 1 9 24 8 GLY H H 8.378 0.05 1 10 24 8 GLY CA C 44.727 0.3 1 11 24 8 GLY N N 108.958 0.3 1 12 25 9 THR H H 8.285 0.05 1 13 25 9 THR CA C 62.154 0.3 1 14 25 9 THR CB C 69.564 0.3 1 15 25 9 THR N N 115.606 0.3 1 16 26 10 VAL H H 8.218 0.05 1 17 26 10 VAL CA C 60.35 0.3 1 18 26 10 VAL CB C 33.419 0.3 1 19 26 10 VAL N N 124.502 0.3 1 20 27 11 PHE H H 9.176 0.05 1 21 27 11 PHE CA C 55.933 0.3 1 22 27 11 PHE CB C 40.292 0.3 1 23 27 11 PHE N N 127.756 0.3 1 24 28 12 THR H H 8.593 0.05 1 25 28 12 THR CA C 59.079 0.3 1 26 28 12 THR CB C 71.046 0.3 1 27 28 12 THR N N 117.181 0.3 1 28 29 13 THR H H 8.551 0.05 1 29 29 13 THR CA C 60.646 0.3 1 30 29 13 THR CB C 71.96 0.3 1 31 29 13 THR N N 112.116 0.3 1 32 30 14 VAL H H 8.087 0.05 1 33 30 14 VAL CA C 61.034 0.3 1 34 30 14 VAL CB C 33.838 0.3 1 35 30 14 VAL N N 120.342 0.3 1 36 31 15 GLU H H 9.021 0.05 1 37 31 15 GLU CA C 54.12 0.3 1 38 31 15 GLU CB C 32.367 0.3 1 39 31 15 GLU N N 126.945 0.3 1 40 32 16 ASP H H 8.857 0.05 1 41 32 16 ASP CA C 53.693 0.3 1 42 32 16 ASP CB C 40.489 0.3 1 43 32 16 ASP N N 124.832 0.3 1 44 33 17 LEU H H 8.447 0.05 1 45 33 17 LEU CA C 53.536 0.3 1 46 33 17 LEU CB C 41.029 0.3 1 47 33 17 LEU N N 127.482 0.3 1 48 34 18 GLY H H 8.93 0.05 1 49 34 18 GLY CA C 46.058 0.3 1 50 34 18 GLY N N 113.235 0.3 1 51 36 20 LYS H H 7.285 0.05 1 52 36 20 LYS CA C 53.72 0.3 1 53 36 20 LYS CB C 35.065 0.3 1 54 36 20 LYS N N 118.638 0.3 1 55 37 21 ILE H H 8.491 0.05 1 56 37 21 ILE CA C 59.136 0.3 1 57 37 21 ILE CB C 39.822 0.3 1 58 37 21 ILE N N 119.067 0.3 1 59 38 22 LEU H H 9.177 0.05 1 60 38 22 LEU CA C 53.288 0.3 1 61 38 22 LEU CB C 43.868 0.3 1 62 38 22 LEU N N 127.534 0.3 1 63 39 23 LEU H H 9.104 0.05 1 64 39 23 LEU CA C 52.813 0.3 1 65 39 23 LEU CB C 42.209 0.3 1 66 39 23 LEU N N 129.979 0.3 1 67 40 24 THR H H 8.796 0.05 1 68 40 24 THR CA C 60.862 0.3 1 69 40 24 THR CB C 70.902 0.3 1 70 40 24 THR N N 113.465 0.3 1 71 41 25 CYS H H 9.098 0.05 1 72 41 25 CYS CA C 54.052 0.3 1 73 41 25 CYS CB C 47.74 0.3 1 74 41 25 CYS N N 118.955 0.3 1 75 42 26 SER H H 9.119 0.05 1 76 42 26 SER CA C 56.551 0.3 1 77 42 26 SER CB C 65.049 0.3 1 78 42 26 SER N N 117.364 0.3 1 79 43 27 LEU H H 8.766 0.05 1 80 43 27 LEU CA C 53.718 0.3 1 81 43 27 LEU CB C 42.052 0.3 1 82 43 27 LEU N N 127.175 0.3 1 83 44 28 ASN H H 8.573 0.05 1 84 44 28 ASN CA C 53.41 0.3 1 85 44 28 ASN CB C 38.979 0.3 1 86 44 28 ASN N N 123.099 0.3 1 87 45 29 ASP H H 7.963 0.05 1 88 45 29 ASP CA C 53.992 0.3 1 89 45 29 ASP CB C 41.037 0.3 1 90 45 29 ASP N N 118.384 0.3 1 91 46 30 SER H H 8.31 0.05 1 92 46 30 SER CA C 57.977 0.3 1 93 46 30 SER CB C 63.5 0.3 1 94 46 30 SER N N 115.359 0.3 1 95 47 31 ALA H H 8.504 0.05 1 96 47 31 ALA CA C 52.302 0.3 1 97 47 31 ALA CB C 18.507 0.3 1 98 47 31 ALA N N 125.839 0.3 1 99 48 32 THR H H 7.684 0.05 1 100 48 32 THR CA C 61.561 0.3 1 101 48 32 THR CB C 69.412 0.3 1 102 48 32 THR N N 113.048 0.3 1 103 49 33 GLU H H 8.358 0.05 1 104 49 33 GLU CA C 56.132 0.3 1 105 49 33 GLU CB C 29.152 0.3 1 106 49 33 GLU N N 123.592 0.3 1 107 50 34 VAL H H 7.881 0.05 1 108 50 34 VAL CA C 62.078 0.3 1 109 50 34 VAL CB C 32.627 0.3 1 110 50 34 VAL N N 124.422 0.3 1 111 51 35 THR H H 9.302 0.05 1 112 51 35 THR CA C 60.393 0.3 1 113 51 35 THR CB C 68.465 0.3 1 114 51 35 THR N N 117.823 0.3 1 115 52 36 GLY H H 7.127 0.05 1 116 52 36 GLY CA C 45.338 0.3 1 117 52 36 GLY N N 109.048 0.3 1 118 53 37 HIS H H 7.948 0.05 1 119 53 37 HIS CA C 53.915 0.3 1 120 53 37 HIS CB C 31.78 0.3 1 121 53 37 HIS N N 113.49 0.3 1 122 54 38 ARG H H 9.1 0.05 1 123 54 38 ARG CA C 54.85 0.3 1 124 54 38 ARG CB C 35.081 0.3 1 125 54 38 ARG N N 120.849 0.3 1 126 55 39 TRP H H 8.957 0.05 1 127 55 39 TRP HE1 H 9.96 0.05 1 128 55 39 TRP CA C 56.019 0.3 1 129 55 39 TRP CB C 31.56 0.3 1 130 55 39 TRP N N 122.611 0.3 1 131 55 39 TRP NE1 N 130.562 0.3 1 132 56 40 LEU H H 9.404 0.05 1 133 56 40 LEU CA C 54.21 0.3 1 134 56 40 LEU CB C 45.963 0.3 1 135 56 40 LEU N N 122.219 0.3 1 136 57 41 LYS H H 8.416 0.05 1 137 57 41 LYS CA C 55.805 0.3 1 138 57 41 LYS CB C 35.642 0.3 1 139 57 41 LYS N N 118.76 0.3 1 140 58 42 GLY H H 9.315 0.05 1 141 58 42 GLY CA C 46.749 0.3 1 142 58 42 GLY N N 120.159 0.3 1 143 59 43 GLY H H 8.746 0.05 1 144 59 43 GLY CA C 44.619 0.3 1 145 59 43 GLY N N 106.244 0.3 1 146 60 44 VAL H H 7.709 0.05 1 147 60 44 VAL CA C 60.914 0.3 1 148 60 44 VAL CB C 32.752 0.3 1 149 60 44 VAL N N 122.586 0.3 1 150 61 45 VAL H H 8.662 0.05 1 151 61 45 VAL CA C 63.612 0.3 1 152 61 45 VAL CB C 30.702 0.3 1 153 61 45 VAL N N 126.086 0.3 1 154 62 46 LEU H H 9.363 0.05 1 155 62 46 LEU CA C 54.894 0.3 1 156 62 46 LEU CB C 42.855 0.3 1 157 62 46 LEU N N 129.653 0.3 1 158 63 47 LYS H H 7.616 0.05 1 159 63 47 LYS CA C 55.635 0.3 1 160 63 47 LYS CB C 35.489 0.3 1 161 63 47 LYS N N 117.599 0.3 1 162 64 48 GLU H H 8.761 0.05 1 163 64 48 GLU CA C 54.791 0.3 1 164 64 48 GLU CB C 32.322 0.3 1 165 64 48 GLU N N 124.974 0.3 1 166 65 49 ASP H H 9.281 0.05 1 167 65 49 ASP CA C 52.642 0.3 1 168 65 49 ASP CB C 44.575 0.3 1 169 65 49 ASP N N 120.958 0.3 1 170 66 50 ALA H H 8.966 0.05 1 171 66 50 ALA CA C 50.067 0.3 1 172 66 50 ALA CB C 17.904 0.3 1 173 66 50 ALA N N 126.637 0.3 1 174 67 51 LEU H H 8.49 0.05 1 175 67 51 LEU CA C 52.181 0.3 1 176 67 51 LEU CB C 41.832 0.3 1 177 67 51 LEU N N 123.075 0.3 1 178 68 52 PRO CA C 61.58 0.3 1 179 68 52 PRO CB C 31.747 0.3 1 180 69 53 GLY H H 7.827 0.05 1 181 69 53 GLY CA C 45.868 0.3 1 182 69 53 GLY N N 106.79 0.3 1 183 70 54 GLN H H 8.912 0.05 1 184 70 54 GLN CA C 57.341 0.3 1 185 70 54 GLN CB C 28.18 0.3 1 186 70 54 GLN N N 124.371 0.3 1 187 71 55 LYS H H 7.95 0.05 1 188 71 55 LYS CA C 54.031 0.3 1 189 71 55 LYS CB C 35.067 0.3 1 190 71 55 LYS N N 118.064 0.3 1 191 72 56 THR H H 8.961 0.05 1 192 72 56 THR CA C 59.693 0.3 1 193 72 56 THR CB C 68.476 0.3 1 194 72 56 THR N N 118.686 0.3 1 195 73 57 GLU H H 8.269 0.05 1 196 73 57 GLU CA C 54.021 0.3 1 197 73 57 GLU CB C 33.627 0.3 1 198 73 57 GLU N N 126.713 0.3 1 199 74 58 PHE H H 8.706 0.05 1 200 74 58 PHE CA C 57.379 0.3 1 201 74 58 PHE CB C 40.019 0.3 1 202 74 58 PHE N N 122.078 0.3 1 203 75 59 LYS H H 7.147 0.05 1 204 75 59 LYS CA C 54.576 0.3 1 205 75 59 LYS CB C 33.449 0.3 1 206 75 59 LYS N N 126.574 0.3 1 207 76 60 VAL H H 8.821 0.05 1 208 76 60 VAL CA C 60.226 0.3 1 209 76 60 VAL CB C 33.382 0.3 1 210 76 60 VAL N N 122.603 0.3 1 211 77 61 ASP H H 8.843 0.05 1 212 77 61 ASP CA C 54.728 0.3 1 213 77 61 ASP CB C 41.199 0.3 1 214 77 61 ASP N N 127.087 0.3 1 215 78 62 SER H H 8.285 0.05 1 216 78 62 SER CA C 60.869 0.3 1 217 78 62 SER CB C 63.163 0.3 1 218 78 62 SER N N 116.297 0.3 1 219 79 63 ASP H H 8.49 0.05 1 220 79 63 ASP CA C 55.113 0.3 1 221 79 63 ASP CB C 40.765 0.3 1 222 79 63 ASP N N 119.097 0.3 1 223 80 64 ASP H H 7.77 0.05 1 224 80 64 ASP CA C 53.706 0.3 1 225 80 64 ASP CB C 41.126 0.3 1 226 80 64 ASP N N 117.629 0.3 1 227 81 65 GLN H H 7.361 0.05 1 228 81 65 GLN CA C 55.359 0.3 1 229 81 65 GLN CB C 26.544 0.3 1 230 81 65 GLN N N 118.665 0.3 1 231 82 66 TRP H H 7.914 0.05 1 232 82 66 TRP CA C 55.953 0.3 1 233 82 66 TRP CB C 29.994 0.3 1 234 82 66 TRP N N 121.982 0.3 1 235 83 67 GLY H H 8.811 0.05 1 236 83 67 GLY CA C 44.81 0.3 1 237 83 67 GLY N N 108.52 0.3 1 238 84 68 GLU H H 8.145 0.05 1 239 84 68 GLU CA C 54.658 0.3 1 240 84 68 GLU CB C 31.383 0.3 1 241 84 68 GLU N N 119.959 0.3 1 242 85 69 TYR H H 9.236 0.05 1 243 85 69 TYR CA C 56.663 0.3 1 244 85 69 TYR CB C 42.019 0.3 1 245 85 69 TYR N N 126.445 0.3 1 246 86 70 SER H H 9.282 0.05 1 247 86 70 SER CA C 56.232 0.3 1 248 86 70 SER CB C 65.256 0.3 1 249 86 70 SER N N 115.19 0.3 1 250 87 71 CYS H H 8.586 0.05 1 251 87 71 CYS CA C 51.866 0.3 1 252 87 71 CYS CB C 42.466 0.3 1 253 87 71 CYS N N 119.757 0.3 1 254 88 72 VAL H H 8.816 0.05 1 255 88 72 VAL CA C 60.811 0.3 1 256 88 72 VAL CB C 34.819 0.3 1 257 88 72 VAL N N 123.18 0.3 1 258 89 73 PHE H H 8.97 0.05 1 259 89 73 PHE CA C 57.879 0.3 1 260 89 73 PHE CB C 39.03 0.3 1 261 89 73 PHE N N 125.428 0.3 1 262 90 74 LEU H H 7.839 0.05 1 263 90 74 LEU CA C 50.948 0.3 1 264 90 74 LEU CB C 39.553 0.3 1 265 90 74 LEU N N 121.51 0.3 1 266 91 75 PRO CA C 60.508 0.3 1 267 91 75 PRO CB C 33.339 0.3 1 268 92 76 GLU H H 8.833 0.05 1 269 92 76 GLU CA C 55.173 0.3 1 270 92 76 GLU CB C 28.983 0.3 1 271 92 76 GLU N N 123.178 0.3 1 272 93 77 PRO CA C 62.625 0.3 1 273 93 77 PRO CB C 30.022 0.3 1 274 94 78 MET H H 8.886 0.05 1 275 94 78 MET CA C 58.606 0.3 1 276 94 78 MET CB C 32.369 0.3 1 277 94 78 MET N N 123.295 0.3 1 278 95 79 GLY H H 8.808 0.05 1 279 95 79 GLY CA C 47.09 0.3 1 280 95 79 GLY N N 105.451 0.3 1 281 96 80 THR H H 8.506 0.05 1 282 96 80 THR CA C 59.502 0.3 1 283 96 80 THR CB C 71.101 0.3 1 284 96 80 THR N N 122.541 0.3 1 285 97 81 ALA H H 8.427 0.05 1 286 97 81 ALA CA C 50.995 0.3 1 287 97 81 ALA CB C 22.598 0.3 1 288 97 81 ALA N N 125.968 0.3 1 289 98 82 ASN H H 8.43 0.05 1 290 98 82 ASN CA C 51.186 0.3 1 291 98 82 ASN CB C 40.912 0.3 1 292 98 82 ASN N N 116.575 0.3 1 293 99 83 ILE H H 9.621 0.05 1 294 99 83 ILE CA C 60.898 0.3 1 295 99 83 ILE CB C 41.593 0.3 1 296 99 83 ILE N N 123.841 0.3 1 297 100 84 GLN H H 8.693 0.05 1 298 100 84 GLN CA C 54.681 0.3 1 299 100 84 GLN CB C 28.733 0.3 1 300 100 84 GLN N N 126.279 0.3 1 301 101 85 LEU H H 8.852 0.05 1 302 101 85 LEU CA C 53.738 0.3 1 303 101 85 LEU CB C 40.974 0.3 1 304 101 85 LEU N N 126.245 0.3 1 305 102 86 HIS H H 8.465 0.05 1 306 102 86 HIS CA C 55.198 0.3 1 307 102 86 HIS CB C 31.628 0.3 1 308 102 86 HIS N N 121.918 0.3 1 309 103 87 GLY H H 8.479 0.05 1 310 103 87 GLY CA C 44.352 0.3 1 311 103 87 GLY N N 109.714 0.3 1 312 105 89 PRO CA C 62.197 0.3 1 313 105 89 PRO CB C 31.275 0.3 1 314 106 90 ARG H H 7.89 0.05 1 315 106 90 ARG CA C 53.343 0.3 1 316 106 90 ARG CB C 30.797 0.3 1 317 106 90 ARG N N 117.809 0.3 1 318 107 91 VAL H H 10.196 0.05 1 319 107 91 VAL CA C 60.392 0.3 1 320 107 91 VAL CB C 33.427 0.3 1 321 107 91 VAL N N 129.095 0.3 1 322 108 92 LYS H H 8.87 0.05 1 323 108 92 LYS CA C 53.68 0.3 1 324 108 92 LYS CB C 35.501 0.3 1 325 108 92 LYS N N 123.045 0.3 1 326 109 93 ALA H H 8.762 0.05 1 327 109 93 ALA CA C 50.914 0.3 1 328 109 93 ALA CB C 19.041 0.3 1 329 109 93 ALA N N 125.58 0.3 1 330 110 94 VAL H H 8.616 0.05 1 331 110 94 VAL CA C 65.891 0.3 1 332 110 94 VAL CB C 30.952 0.3 1 333 110 94 VAL N N 125.209 0.3 1 334 111 95 LYS H H 7.433 0.05 1 335 111 95 LYS CA C 55.317 0.3 1 336 111 95 LYS CB C 34.164 0.3 1 337 111 95 LYS N N 117.024 0.3 1 338 112 96 SER H H 8.862 0.05 1 339 112 96 SER CA C 60.231 0.3 1 340 112 96 SER CB C 63.299 0.3 1 341 112 96 SER N N 118.193 0.3 1 342 113 97 SER H H 7.686 0.05 1 343 113 97 SER CA C 56.56 0.3 1 344 113 97 SER CB C 64.28 0.3 1 345 113 97 SER N N 116.312 0.3 1 346 114 98 GLU H H 8.729 0.05 1 347 114 98 GLU CA C 54.17 0.3 1 348 114 98 GLU CB C 33.417 0.3 1 349 114 98 GLU N N 123.393 0.3 1 350 115 99 HIS H H 9.13 0.05 1 351 115 99 HIS CA C 53.558 0.3 1 352 115 99 HIS CB C 30.97 0.3 1 353 115 99 HIS N N 126.954 0.3 1 354 116 100 ILE H H 8.195 0.05 1 355 116 100 ILE CA C 58.308 0.3 1 356 116 100 ILE CB C 40.326 0.3 1 357 116 100 ILE N N 124.843 0.3 1 358 117 101 ASN H H 8.369 0.05 1 359 117 101 ASN CA C 53.411 0.3 1 360 117 101 ASN CB C 38.443 0.3 1 361 117 101 ASN N N 124.712 0.3 1 362 118 102 GLU H H 8.566 0.05 1 363 118 102 GLU CA C 56.681 0.3 1 364 118 102 GLU CB C 29.289 0.3 1 365 118 102 GLU N N 119.816 0.3 1 366 119 103 GLY H H 9.61 0.05 1 367 119 103 GLY CA C 44.631 0.3 1 368 119 103 GLY N N 113.714 0.3 1 369 120 104 GLU H H 7.52 0.05 1 370 120 104 GLU CA C 55.28 0.3 1 371 120 104 GLU CB C 29.238 0.3 1 372 120 104 GLU N N 120.399 0.3 1 373 121 105 THR H H 8.171 0.05 1 374 121 105 THR CA C 60.614 0.3 1 375 121 105 THR CB C 69.945 0.3 1 376 121 105 THR N N 114.221 0.3 1 377 122 106 ALA H H 8.786 0.05 1 378 122 106 ALA CA C 49.913 0.3 1 379 122 106 ALA CB C 21.248 0.3 1 380 122 106 ALA N N 127.964 0.3 1 381 123 107 MET H H 8.498 0.05 1 382 123 107 MET CA C 54.151 0.3 1 383 123 107 MET CB C 33.442 0.3 1 384 123 107 MET N N 120.946 0.3 1 385 124 108 LEU H H 9.065 0.05 1 386 124 108 LEU CA C 53.457 0.3 1 387 124 108 LEU CB C 40.576 0.3 1 388 124 108 LEU N N 128.957 0.3 1 389 125 109 VAL H H 8.563 0.05 1 390 125 109 VAL CA C 60.814 0.3 1 391 125 109 VAL CB C 34.893 0.3 1 392 125 109 VAL N N 120.534 0.3 1 393 126 110 CYS H H 8.968 0.05 1 394 126 110 CYS CA C 53.447 0.3 1 395 126 110 CYS CB C 47.301 0.3 1 396 126 110 CYS N N 123.494 0.3 1 397 127 111 LYS H H 9.247 0.05 1 398 127 111 LYS CA C 54.092 0.3 1 399 127 111 LYS CB C 36.433 0.3 1 400 127 111 LYS N N 117.21 0.3 1 401 128 112 SER H H 8.719 0.05 1 402 128 112 SER CA C 57.166 0.3 1 403 128 112 SER CB C 65.611 0.3 1 404 128 112 SER N N 112.434 0.3 1 405 130 114 SER H H 8.198 0.05 1 406 130 114 SER CA C 59.59 0.3 1 407 130 114 SER CB C 63.928 0.3 1 408 130 114 SER N N 116.782 0.3 1 409 131 115 VAL H H 8.155 0.05 1 410 131 115 VAL CA C 59.347 0.3 1 411 131 115 VAL CB C 34.151 0.3 1 412 131 115 VAL N N 121.156 0.3 1 413 133 117 PRO CA C 61.843 0.3 1 414 133 117 PRO CB C 31.656 0.3 1 415 134 118 VAL H H 8.288 0.05 1 416 134 118 VAL CA C 63.047 0.3 1 417 134 118 VAL CB C 31.135 0.3 1 418 134 118 VAL N N 120.345 0.3 1 419 135 119 THR H H 7.995 0.05 1 420 135 119 THR CA C 61.031 0.3 1 421 135 119 THR CB C 69.496 0.3 1 422 135 119 THR N N 117.113 0.3 1 423 136 120 ASP H H 7.373 0.05 1 424 136 120 ASP CA C 53.468 0.3 1 425 136 120 ASP CB C 42.737 0.3 1 426 136 120 ASP N N 123.883 0.3 1 427 137 121 TRP H H 8.766 0.05 1 428 137 121 TRP HE1 H 10.091 0.05 1 429 137 121 TRP CA C 55.269 0.3 1 430 137 121 TRP CB C 33.325 0.3 1 431 137 121 TRP N N 124.042 0.3 1 432 137 121 TRP NE1 N 128.655 0.3 1 433 138 122 ALA H H 9.049 0.05 1 434 138 122 ALA CA C 51.37 0.3 1 435 138 122 ALA CB C 22.59 0.3 1 436 138 122 ALA N N 125.143 0.3 1 437 139 123 TRP H H 8.752 0.05 1 438 139 123 TRP CA C 56.055 0.3 1 439 139 123 TRP CB C 32.834 0.3 1 440 139 123 TRP N N 120.54 0.3 1 441 140 124 TYR H H 9.422 0.05 1 442 140 124 TYR CA C 55.655 0.3 1 443 140 124 TYR CB C 42.693 0.3 1 444 140 124 TYR N N 117.353 0.3 1 445 141 125 LYS H H 9.327 0.05 1 446 141 125 LYS CA C 54.421 0.3 1 447 141 125 LYS CB C 34.626 0.3 1 448 141 125 LYS N N 122.849 0.3 1 449 142 126 ILE H H 8.434 0.05 1 450 142 126 ILE CA C 60.996 0.3 1 451 142 126 ILE CB C 36.241 0.3 1 452 142 126 ILE N N 128.73 0.3 1 453 143 127 THR H H 8.604 0.05 1 454 143 127 THR CA C 59.702 0.3 1 455 143 127 THR CB C 70.896 0.3 1 456 143 127 THR N N 120.54 0.3 1 457 144 128 ASP H H 8.594 0.05 1 458 144 128 ASP CA C 55.826 0.3 1 459 144 128 ASP CB C 39.872 0.3 1 460 144 128 ASP N N 118.628 0.3 1 461 145 129 SER H H 8.256 0.05 1 462 145 129 SER CA C 57.819 0.3 1 463 145 129 SER CB C 63.397 0.3 1 464 145 129 SER N N 112.756 0.3 1 465 146 130 GLU H H 7.712 0.05 1 466 146 130 GLU CA C 55.387 0.3 1 467 146 130 GLU CB C 30.871 0.3 1 468 146 130 GLU N N 120.863 0.3 1 469 147 131 ASP H H 8.749 0.05 1 470 147 131 ASP CA C 53.708 0.3 1 471 147 131 ASP CB C 39.852 0.3 1 472 147 131 ASP N N 125.784 0.3 1 473 148 132 LYS H H 9.049 0.05 1 474 148 132 LYS CA C 54.835 0.3 1 475 148 132 LYS CB C 33.474 0.3 1 476 148 132 LYS N N 125.144 0.3 1 477 149 133 ALA H H 8.883 0.05 1 478 149 133 ALA CA C 52.62 0.3 1 479 149 133 ALA CB C 18.045 0.3 1 480 149 133 ALA N N 130.252 0.3 1 481 150 134 LEU H H 8.041 0.05 1 482 150 134 LEU CB C 40.256 0.3 1 483 150 134 LEU N N 124.795 0.3 1 484 161 145 SER H H 9.02 0.05 1 485 161 145 SER CA C 56.058 0.3 1 486 161 145 SER CB C 63.874 0.3 1 487 161 145 SER N N 122.691 0.3 1 488 162 146 SER H H 9.113 0.05 1 489 162 146 SER CA C 56.81 0.3 1 490 162 146 SER CB C 65.184 0.3 1 491 162 146 SER N N 124.128 0.3 1 492 163 147 SER H H 9.2 0.05 1 493 163 147 SER CA C 56.954 0.3 1 494 163 147 SER CB C 64.638 0.3 1 495 163 147 SER N N 119.33 0.3 1 496 164 148 GLN H H 8.836 0.05 1 497 164 148 GLN CA C 57.876 0.3 1 498 164 148 GLN CB C 27.31 0.3 1 499 164 148 GLN N N 120.488 0.3 1 500 165 149 GLY H H 9.189 0.05 1 501 165 149 GLY CA C 46.481 0.3 1 502 165 149 GLY N N 111.754 0.3 1 503 166 150 ARG H H 7.959 0.05 1 504 166 150 ARG CA C 55.214 0.3 1 505 166 150 ARG CB C 32.714 0.3 1 506 166 150 ARG N N 122.278 0.3 1 507 167 151 SER H H 8.123 0.05 1 508 167 151 SER CA C 56.652 0.3 1 509 167 151 SER CB C 62.483 0.3 1 510 167 151 SER N N 117.015 0.3 1 511 168 152 GLU H H 8.593 0.05 1 512 168 152 GLU CA C 52.457 0.3 1 513 168 152 GLU CB C 32.283 0.3 1 514 168 152 GLU N N 125.812 0.3 1 515 169 153 LEU H H 8.798 0.05 1 516 169 153 LEU CA C 52.595 0.3 1 517 169 153 LEU CB C 39.954 0.3 1 518 169 153 LEU N N 125.853 0.3 1 519 170 154 HIS H H 9.534 0.05 1 520 170 154 HIS CA C 52.6 0.3 1 521 170 154 HIS CB C 30.393 0.3 1 522 170 154 HIS N N 126.27 0.3 1 523 171 155 ILE H H 8.558 0.05 1 524 171 155 ILE CA C 59.824 0.3 1 525 171 155 ILE CB C 39.208 0.3 1 526 171 155 ILE N N 122.079 0.3 1 527 172 156 GLU H H 8.665 0.05 1 528 172 156 GLU CA C 55.204 0.3 1 529 172 156 GLU CB C 30.505 0.3 1 530 172 156 GLU N N 124.221 0.3 1 531 173 157 ASN H H 8.185 0.05 1 532 173 157 ASN CA C 52.417 0.3 1 533 173 157 ASN CB C 36.599 0.3 1 534 173 157 ASN N N 117.139 0.3 1 535 174 158 LEU H H 8.113 0.05 1 536 174 158 LEU CA C 55.549 0.3 1 537 174 158 LEU CB C 42.753 0.3 1 538 174 158 LEU N N 117.154 0.3 1 539 175 159 ASN H H 10.245 0.05 1 540 175 159 ASN CA C 51.424 0.3 1 541 175 159 ASN CB C 41.503 0.3 1 542 175 159 ASN N N 124.607 0.3 1 543 176 160 MET H H 9.059 0.05 1 544 176 160 MET CA C 56.611 0.3 1 545 176 160 MET CB C 32.25 0.3 1 546 176 160 MET N N 120.302 0.3 1 547 177 161 GLU H H 8.114 0.05 1 548 177 161 GLU CA C 57.654 0.3 1 549 177 161 GLU CB C 29.645 0.3 1 550 177 161 GLU N N 117.087 0.3 1 551 178 162 ALA H H 8.27 0.05 1 552 178 162 ALA CA C 53.302 0.3 1 553 178 162 ALA CB C 20.018 0.3 1 554 178 162 ALA N N 120.197 0.3 1 555 179 163 ASP H H 7.552 0.05 1 556 179 163 ASP CA C 57.006 0.3 1 557 179 163 ASP CB C 40.06 0.3 1 558 179 163 ASP N N 116.672 0.3 1 559 180 164 PRO CA C 65.14 0.3 1 560 180 164 PRO CB C 30.484 0.3 1 561 181 165 GLY H H 8.883 0.05 1 562 181 165 GLY CA C 43.86 0.3 1 563 181 165 GLY N N 109.675 0.3 1 564 182 166 GLN H H 8.79 0.05 1 565 182 166 GLN CA C 54.845 0.3 1 566 182 166 GLN CB C 31.204 0.3 1 567 182 166 GLN N N 119.67 0.3 1 568 183 167 TYR H H 9.61 0.05 1 569 183 167 TYR CA C 56.587 0.3 1 570 183 167 TYR CB C 41.381 0.3 1 571 183 167 TYR N N 122.332 0.3 1 572 184 168 ARG H H 9.682 0.05 1 573 184 168 ARG CA C 52.971 0.3 1 574 184 168 ARG CB C 35.076 0.3 1 575 184 168 ARG N N 122.751 0.3 1 576 185 169 CYS H H 8.831 0.05 1 577 185 169 CYS CA C 52.071 0.3 1 578 185 169 CYS CB C 42.171 0.3 1 579 185 169 CYS N N 121.638 0.3 1 580 186 170 ASN H H 9.447 0.05 1 581 186 170 ASN CA C 52.089 0.3 1 582 186 170 ASN CB C 41.539 0.3 1 583 186 170 ASN N N 122.493 0.3 1 584 187 171 GLY H H 8.877 0.05 1 585 187 171 GLY CA C 44.449 0.3 1 586 187 171 GLY N N 112.807 0.3 1 587 188 172 THR H H 8.448 0.05 1 588 188 172 THR CA C 61.298 0.3 1 589 188 172 THR CB C 70.925 0.3 1 590 188 172 THR N N 120.801 0.3 1 591 189 173 SER H H 9.439 0.05 1 592 189 173 SER CA C 54.807 0.3 1 593 189 173 SER CB C 69.062 0.3 1 594 189 173 SER N N 123.841 0.3 1 595 190 174 SER H H 8.86 0.05 1 596 190 174 SER CA C 59.853 0.3 1 597 190 174 SER CB C 62.024 0.3 1 598 190 174 SER N N 114.387 0.3 1 599 191 175 LYS H H 8.023 0.05 1 600 191 175 LYS CA C 53.877 0.3 1 601 191 175 LYS CB C 33.085 0.3 1 602 191 175 LYS N N 118.402 0.3 1 603 192 176 GLY H H 7.358 0.05 1 604 192 176 GLY CA C 44.675 0.3 1 605 192 176 GLY N N 107.423 0.3 1 606 193 177 SER H H 8.466 0.05 1 607 193 177 SER CA C 56.482 0.3 1 608 193 177 SER CB C 66.42 0.3 1 609 193 177 SER N N 113.848 0.3 1 610 194 178 ASP H H 8.73 0.05 1 611 194 178 ASP CA C 53.151 0.3 1 612 194 178 ASP CB C 44.459 0.3 1 613 194 178 ASP N N 119.674 0.3 1 614 195 179 GLN H H 7.932 0.05 1 615 195 179 GLN CA C 52.896 0.3 1 616 195 179 GLN CB C 31.836 0.3 1 617 195 179 GLN N N 115.874 0.3 1 618 196 180 ALA H H 8.226 0.05 1 619 196 180 ALA CA C 50.834 0.3 1 620 196 180 ALA CB C 22.345 0.3 1 621 196 180 ALA N N 120.355 0.3 1 622 197 181 ILE H H 7.939 0.05 1 623 197 181 ILE CA C 59.323 0.3 1 624 197 181 ILE CB C 39.208 0.3 1 625 197 181 ILE N N 117.773 0.3 1 626 198 182 ILE H H 9.686 0.05 1 627 198 182 ILE CA C 59.66 0.3 1 628 198 182 ILE CB C 42.227 0.3 1 629 198 182 ILE N N 129.591 0.3 1 630 199 183 THR H H 8.738 0.05 1 631 199 183 THR CA C 62.224 0.3 1 632 199 183 THR CB C 69.462 0.3 1 633 199 183 THR N N 123.36 0.3 1 634 200 184 LEU H H 9.572 0.05 1 635 200 184 LEU CA C 53.282 0.3 1 636 200 184 LEU CB C 44.493 0.3 1 637 200 184 LEU N N 129.23 0.3 1 638 201 185 ARG H H 8.894 0.05 1 639 201 185 ARG CA C 54.185 0.3 1 640 201 185 ARG CB C 31.831 0.3 1 641 201 185 ARG N N 128.059 0.3 1 642 202 186 VAL H H 8.242 0.05 1 643 202 186 VAL CA C 59.727 0.3 1 644 202 186 VAL CB C 33.07 0.3 1 645 202 186 VAL N N 121.93 0.3 1 646 203 187 ARG H H 8.59 0.05 1 647 203 187 ARG CA C 54.305 0.3 1 648 203 187 ARG CB C 30.939 0.3 1 649 203 187 ARG N N 128.461 0.3 1 650 204 188 SER H H 8.693 0.05 1 651 204 188 SER CA C 57.905 0.3 1 652 204 188 SER CB C 63.549 0.3 1 653 204 188 SER N N 120.345 0.3 1 654 205 189 HIS CA C 57.069 0.3 1 655 205 189 HIS CB C 28.779 0.3 1 656 206 190 LEU H H 8.065 0.05 1 657 206 190 LEU CA C 54.979 0.3 1 658 206 190 LEU CB C 40.939 0.3 1 659 206 190 LEU N N 121.434 0.3 1 660 207 191 ALA H H 7.876 0.05 1 661 207 191 ALA CA C 52.36 0.3 1 662 207 191 ALA CB C 18.136 0.3 1 663 207 191 ALA N N 123.645 0.3 1 664 208 192 ALA H H 7.883 0.05 1 665 208 192 ALA CA C 52.302 0.3 1 666 208 192 ALA CB C 18.208 0.3 1 667 208 192 ALA N N 121.415 0.3 1 668 209 193 LEU H H 7.931 0.05 1 669 209 193 LEU CA C 53.849 0.3 1 670 209 193 LEU CB C 41.904 0.3 1 671 209 193 LEU N N 119.988 0.3 1 672 210 194 TRP H H 7.883 0.05 1 673 210 194 TRP HE1 H 10.131 0.05 1 674 210 194 TRP CA C 54.556 0.3 1 675 210 194 TRP CB C 28.899 0.3 1 676 210 194 TRP N N 121.757 0.3 1 677 210 194 TRP NE1 N 129.233 0.3 1 678 211 195 PRO CA C 63.006 0.3 1 679 211 195 PRO CB C 30.99 0.3 1 680 212 196 PHE H H 7.988 0.05 1 681 212 196 PHE CA C 57.215 0.3 1 682 212 196 PHE CB C 38.66 0.3 1 683 212 196 PHE N N 119.502 0.3 1 684 213 197 LEU H H 8.128 0.05 1 685 213 197 LEU CA C 54.494 0.3 1 686 213 197 LEU CB C 41.47 0.3 1 687 213 197 LEU N N 125.338 0.3 1 688 214 198 GLY H H 7.179 0.05 1 689 214 198 GLY CA C 45.707 0.3 1 690 214 198 GLY N N 114.827 0.3 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Extracellular CD147 Iso-2, cis' _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 1 207 191 ALA H H 7.922 0.05 1 2 207 191 ALA CA C 52.338 0.3 1 3 207 191 ALA CB C 18.272 0.3 1 4 207 191 ALA N N 123.65 0.3 1 5 208 192 ALA H H 8.001 0.05 1 6 208 192 ALA CA C 52.3 0.3 1 7 208 192 ALA CB C 18.381 0.3 1 8 208 192 ALA N N 122.026 0.3 1 9 209 193 LEU H H 7.775 0.05 1 10 209 193 LEU CA C 54.746 0.3 1 11 209 193 LEU CB C 41.326 0.3 1 12 209 193 LEU N N 119.512 0.3 1 13 210 194 TRP H H 7.991 0.05 1 14 210 194 TRP HE1 H 10.21 0.05 1 15 210 194 TRP CA C 55.763 0.3 1 16 210 194 TRP CB C 29.944 0.3 1 17 210 194 TRP N N 123.049 0.3 1 18 210 194 TRP NE1 N 130.371 0.3 1 19 211 195 PRO CB C 32.031 0.3 1 20 212 196 PHE H H 8.354 0.05 1 21 212 196 PHE CA C 57.709 0.3 1 22 212 196 PHE CB C 37.812 0.3 1 23 212 196 PHE N N 123.123 0.3 1 24 213 197 LEU H H 8.072 0.05 1 25 213 197 LEU CA C 54.226 0.3 1 26 213 197 LEU CB C 41.536 0.3 1 27 213 197 LEU N N 124.068 0.3 1 28 214 198 GLY H H 7.277 0.05 1 29 214 198 GLY CA C 45.605 0.3 1 30 214 198 GLY N N 114.876 0.3 1 stop_ save_