data_5583 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of P41icf, a potent inhibitor of human cathepsin L ; _BMRB_accession_number 5583 _BMRB_flat_file_name bmr5583.str _Entry_type original _Submission_date 2002-11-06 _Accession_date 2002-11-06 _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 Chiva C. . . 2 Barthe P. . . 3 Codina A. . . 4 Giralt E. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 339 "coupling constants" 42 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-05-14 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Synthesis and NMR Structure of P41icf, a Potent Inhibitor of Human Cathepsin L' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22456786 _PubMed_ID 12568610 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chiva C. . . 2 Barthe P. . . 3 Codina A. . . 4 Gairi M. . . 5 Molina F. . . 6 Granier C. . . 7 Pugniere M. . . 8 Inui T. . . 9 Nishio H. . . 10 Nishiuchi Y. . . 11 Kimura T. . . 12 Sakakibara S. . . 13 Albericio F. . . 14 Giralt E. . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 125 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1508 _Page_last 1517 _Year 2003 _Details . loop_ _Keyword 'ALPHA HELIX' 'BETA SHEET' 'DISULFIDE BONDS' stop_ save_ ################################## # Molecular system description # ################################## save_system_P41icf _Saveframe_category molecular_system _Mol_system_name 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT (P41icf)' _Abbreviation_common 'p41 fragment, P41icf' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' $P41icf stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Human cathepsin L inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_P41icf _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT (P41icf)' _Abbreviation_common 'P41 fragment' _Molecular_mass 7246 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 65 _Mol_residue_sequence ; LTKCQEEVSHIPAVHPGSFR PKCDENGNYLPLQCYGSIGY CWCVFPNGTEVPNTRSRGHH NCSES ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 THR 3 LYS 4 CYS 5 GLN 6 GLU 7 GLU 8 VAL 9 SER 10 HIS 11 ILE 12 PRO 13 ALA 14 VAL 15 HIS 16 PRO 17 GLY 18 SER 19 PHE 20 ARG 21 PRO 22 LYS 23 CYS 24 ASP 25 GLU 26 ASN 27 GLY 28 ASN 29 TYR 30 LEU 31 PRO 32 LEU 33 GLN 34 CYS 35 TYR 36 GLY 37 SER 38 ILE 39 GLY 40 TYR 41 CYS 42 TRP 43 CYS 44 VAL 45 PHE 46 PRO 47 ASN 48 GLY 49 THR 50 GLU 51 VAL 52 PRO 53 ASN 54 THR 55 ARG 56 SER 57 ARG 58 GLY 59 HIS 60 HIS 61 ASN 62 CYS 63 SER 64 GLU 65 SER 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 1ICF "Crystal Structure Of Mhc Class Ii Associated P41 Ii Fragment In Complex With Cathepsin L" 100.00 65 100.00 100.00 4.05e-40 PDB 1L3H "Nmr Structure Of P41icf, A Potent Inhibitor Of Human Cathepsin L" 98.46 65 100.00 100.00 2.26e-39 DBJ BAG60210 "unnamed protein product [Homo sapiens]" 100.00 296 100.00 100.00 3.47e-40 GB AAA35996 "protein 41, partial [Homo sapiens]" 100.00 71 100.00 100.00 3.77e-40 GB EAW61731 "CD74 antigen (invariant polypeptide of major histocompatibility complex, class II antigen-associated), isoform CRA_c [Homo sapi" 100.00 296 100.00 100.00 3.47e-40 REF NP_001020330 "HLA class II histocompatibility antigen gamma chain isoform a [Homo sapiens]" 100.00 296 100.00 100.00 3.47e-40 REF XP_003266686 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform 2 [Nomascus leucogenys]" 100.00 296 100.00 100.00 3.23e-40 REF XP_003829068 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform X1 [Pan paniscus]" 100.00 296 100.00 100.00 3.47e-40 REF XP_004042860 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform 2 [Gorilla gorilla gorilla]" 100.00 296 98.46 98.46 1.97e-39 REF XP_008986092 "PREDICTED: HLA class II histocompatibility antigen gamma chain isoform X1 [Callithrix jacchus]" 100.00 280 98.46 98.46 7.69e-41 SP P04233 "RecName: Full=HLA class II histocompatibility antigen gamma chain; AltName: Full=HLA-DR antigens-associated invariant chain; Al" 100.00 296 100.00 100.00 3.47e-40 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 4 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 23 CYS SG single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 34 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 41 CYS SG single disulfide 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 43 CYS SG 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' 62 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $P41icf 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 $P41icf 'chemical synthesis' . . . . . 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 $P41icf 1 mM . phosphate_buffer 20 mM . NaN3 0.01 mM . H20 85 % . D2O 15 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details Delaglio save_ save_NMRview _Saveframe_category software _Name NMRview _Version . loop_ _Task 'data analysis' stop_ _Details Johnson save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details Guntert save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task refinement stop_ _Details Case save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.7 0.2 n/a temperature 288 0.1 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' _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 LEU HA H 4.18 . 1 2 . 1 LEU HB2 H 1.76 . 1 3 . 1 LEU HD1 H 0.82 . 1 4 . 1 LEU HG H 1.67 . 1 5 . 2 THR H H 8.73 . 1 6 . 2 THR HA H 4.47 . 1 7 . 2 THR HB H 4.73 . 1 8 . 2 THR HG2 H 1.20 . 1 9 . 3 LYS H H 8.8 . 1 10 . 3 LYS HA H 4.02 . 1 11 . 3 LYS HB2 H 1.96 . 1 12 . 3 LYS HG2 H 1.67 . 1 13 . 3 LYS HG3 H 1.57 . 1 14 . 3 LYS HD2 H 1.81 . 1 15 . 3 LYS HE2 H 3.08 . 1 16 . 3 LYS HZ H 7.54 . 1 17 . 4 CYS H H 8.69 . 1 18 . 4 CYS HA H 3.49 . 1 19 . 4 CYS HB2 H 2.47 . 1 20 . 4 CYS HB3 H 1.16 . 1 21 . 5 GLN H H 7.41 . 1 22 . 5 GLN HA H 3.72 . 1 23 . 5 GLN HB2 H 2.22 . 1 24 . 5 GLN HG2 H 2.32 . 1 25 . 5 GLN HE21 H 7.59 . 1 26 . 5 GLN HE22 H 6.84 . 1 27 . 6 GLU H H 8.8 . 1 28 . 6 GLU HA H 3.92 . 1 29 . 6 GLU HB2 H 2.14 . 1 30 . 6 GLU HG2 H 2.44 . 1 31 . 6 GLU HG3 H 2.36 . 1 32 . 7 GLU H H 8.14 . 1 33 . 7 GLU HA H 4.05 . 1 34 . 7 GLU HB2 H 2.28 . 1 35 . 7 GLU HB3 H 2.07 . 1 36 . 7 GLU HG2 H 2.65 . 1 37 . 7 GLU HG3 H 2.39 . 1 38 . 8 VAL H H 7.95 . 1 39 . 8 VAL HA H 3.65 . 1 40 . 8 VAL HB H 2.05 . 1 41 . 8 VAL HG1 H 1.01 . 1 42 . 8 VAL HG2 H 0.86 . 1 43 . 9 SER H H 7.71 . 1 44 . 9 SER HA H 4.25 . 1 45 . 9 SER HB2 H 3.81 . 1 46 . 10 HIS H H 7.66 . 1 47 . 10 HIS HA H 4.75 . 1 48 . 10 HIS HB2 H 3.42 . 1 49 . 10 HIS HB3 H 3.17 . 1 50 . 10 HIS HD2 H 7.28 . 1 51 . 10 HIS HE1 H 8.56 . 1 52 . 11 ILE H H 7.8 . 1 53 . 11 ILE HA H 4.45 . 1 54 . 11 ILE HB H 1.75 . 1 55 . 11 ILE HG2 H 0.88 . 1 56 . 11 ILE HG12 H 1.15 . 1 57 . 11 ILE HD1 H 0.86 . 1 58 . 12 PRO HA H 4.35 . 1 59 . 12 PRO HB2 H 2.3 . 1 60 . 12 PRO HB3 H 1.98 . 1 61 . 12 PRO HG2 H 2.08 . 1 62 . 12 PRO HD2 H 3.86 . 1 63 . 13 ALA H H 8.26 . 1 64 . 13 ALA HA H 4.1 . 1 65 . 13 ALA HB H 1.37 . 1 66 . 14 VAL H H 7.81 . 1 67 . 14 VAL HA H 3.95 . 1 68 . 14 VAL HB H 1.98 . 1 69 . 14 VAL HG1 H 0.84 . 1 70 . 14 VAL HG2 H 0.77 . 1 71 . 15 HIS H H 8.43 . 1 72 . 15 HIS HA H 5.03 . 1 73 . 15 HIS HB2 H 3.21 . 1 74 . 15 HIS HB3 H 3.12 . 1 75 . 15 HIS HD2 H 7.36 . 1 76 . 15 HIS HE1 H 8.67 . 1 77 . 16 PRO HA H 4.37 . 1 78 . 16 PRO HB2 H 2.31 . 1 79 . 16 PRO HB3 H 1.97 . 1 80 . 16 PRO HG2 H 2.15 . 1 81 . 16 PRO HG3 H 2.04 . 1 82 . 16 PRO HD2 H 3.59 . 1 83 . 17 GLY H H 8.84 . 1 84 . 17 GLY HA2 H 4.1 . 1 85 . 17 GLY HA3 H 4.01 . 1 86 . 18 SER H H 7.99 . 1 87 . 18 SER HA H 4.66 . 1 88 . 18 SER HB2 H 3.88 . 1 89 . 19 PHE H H 8.55 . 1 90 . 19 PHE HA H 4.29 . 1 91 . 19 PHE HB2 H 2.54 . 1 92 . 19 PHE HB3 H 2.36 . 1 93 . 19 PHE HD1 H 7.11 . 1 94 . 19 PHE HE1 H 7.38 . 1 95 . 19 PHE HZ H 6.93 . 1 96 . 20 ARG H H 7.62 . 1 97 . 20 ARG HA H 4.35 . 1 98 . 20 ARG HB2 H 1.2 . 1 99 . 20 ARG HG2 H 1.57 . 1 100 . 20 ARG HG3 H 1.42 . 1 101 . 20 ARG HD2 H 3.14 . 1 102 . 20 ARG HD3 H 3.04 . 1 103 . 20 ARG HE H 7.15 . 1 104 . 21 PRO HA H 4.37 . 1 105 . 21 PRO HB2 H 2.31 . 1 106 . 21 PRO HB3 H 2.15 . 1 107 . 21 PRO HG2 H 1.95 . 1 108 . 21 PRO HD2 H 3.25 . 1 109 . 22 LYS H H 8.95 . 1 110 . 22 LYS HA H 4.54 . 1 111 . 22 LYS HB2 H 1.83 . 1 112 . 22 LYS HG2 H 1.56 . 1 113 . 22 LYS HG3 H 1.42 . 1 114 . 22 LYS HD2 H 1.70 . 1 115 . 22 LYS HE2 H 2.99 . 1 116 . 22 LYS HZ H 7.52 . 1 117 . 23 CYS H H 8.6 . 1 118 . 23 CYS HA H 5.26 . 1 119 . 23 CYS HB2 H 2.71 . 1 120 . 23 CYS HB3 H 2.49 . 1 121 . 24 ASP H H 9.08 . 1 122 . 24 ASP HA H 4.64 . 1 123 . 24 ASP HB2 H 3.33 . 1 124 . 24 ASP HB3 H 2.62 . 1 125 . 25 GLU H H 8.71 . 1 126 . 25 GLU HA H 4.09 . 1 127 . 25 GLU HB2 H 2.07 . 1 128 . 25 GLU HG2 H 2.44 . 1 129 . 26 ASN H H 8.04 . 1 130 . 26 ASN HA H 4.81 . 1 131 . 26 ASN HB2 H 2.91 . 1 132 . 26 ASN HB3 H 2.69 . 1 133 . 26 ASN HD21 H 7.82 . 1 134 . 26 ASN HD22 H 6.94 . 1 135 . 27 GLY H H 8.14 . 1 136 . 27 GLY HA2 H 4.2 . 1 137 . 27 GLY HA3 H 3.36 . 1 138 . 28 ASN H H 8.73 . 1 139 . 28 ASN HA H 4.85 . 1 140 . 28 ASN HB2 H 2.97 . 1 141 . 28 ASN HB3 H 2.75 . 1 142 . 28 ASN HD21 H 8.44 . 1 143 . 28 ASN HD22 H 7.27 . 1 144 . 29 TYR H H 8.79 . 1 145 . 29 TYR HA H 4.47 . 1 146 . 29 TYR HB2 H 2.8 . 1 147 . 29 TYR HB3 H 2.58 . 1 148 . 29 TYR HD1 H 7.15 . 1 149 . 29 TYR HE1 H 6.62 . 1 150 . 30 LEU H H 7.93 . 1 151 . 30 LEU HA H 4.46 . 1 152 . 30 LEU HB2 H 1.62 . 1 153 . 30 LEU HD1 H 0.92 . 1 154 . 30 LEU HD2 H 0.84 . 1 155 . 30 LEU HG H 1.47 . 1 156 . 31 PRO HA H 4.17 . 1 157 . 31 PRO HB2 H 2.32 . 1 158 . 31 PRO HB3 H 1.77 . 1 159 . 31 PRO HG2 H 2.01 . 1 160 . 31 PRO HD2 H 3.85 . 1 161 . 31 PRO HD3 H 3.69 . 1 162 . 32 LEU H H 6.81 . 1 163 . 32 LEU HA H 4.78 . 1 164 . 32 LEU HB2 H 1.63 . 1 165 . 32 LEU HD1 H 0.62 . 1 166 . 32 LEU HD2 H 0.27 . 1 167 . 32 LEU HG H 1.09 . 1 168 . 33 GLN H H 8.55 . 1 169 . 33 GLN HA H 4.17 . 1 170 . 33 GLN HB2 H 1.78 . 1 171 . 33 GLN HB3 H 0.33 . 1 172 . 33 GLN HG2 H 2.32 . 1 173 . 33 GLN HG3 H 2.16 . 1 174 . 33 GLN HE21 H 8.85 . 1 175 . 33 GLN HE22 H 8.18 . 1 176 . 34 CYS H H 8.47 . 1 177 . 34 CYS HA H 4.85 . 1 178 . 34 CYS HB2 H 2.92 . 1 179 . 34 CYS HB3 H 2.77 . 1 180 . 35 TYR H H 8.37 . 1 181 . 35 TYR HA H 5.15 . 1 182 . 35 TYR HB2 H 3.41 . 1 183 . 35 TYR HB3 H 3.27 . 1 184 . 35 TYR HD1 H 7.35 . 1 185 . 35 TYR HE1 H 6.90 . 1 186 . 36 GLY H H 8.64 . 1 187 . 36 GLY HA2 H 4.18 . 1 188 . 36 GLY HA3 H 3.71 . 1 189 . 37 SER H H 8.37 . 1 190 . 37 SER HA H 4.22 . 1 191 . 37 SER HB2 H 3.76 . 1 192 . 38 ILE H H 7.34 . 1 193 . 38 ILE HA H 4.36 . 1 194 . 38 ILE HB H 2.0 . 1 195 . 38 ILE HG2 H 0.87 . 1 196 . 38 ILE HG12 H 1.48 . 1 197 . 38 ILE HG13 H 1.09 . 1 198 . 38 ILE HD1 H 0.75 . 1 199 . 39 GLY H H 7.88 . 1 200 . 39 GLY HA2 H 4.08 . 1 201 . 39 GLY HA3 H 3.71 . 1 202 . 40 TYR H H 7.78 . 1 203 . 40 TYR HA H 4.83 . 1 204 . 40 TYR HB2 H 2.99 . 1 205 . 40 TYR HD1 H 6.96 . 1 206 . 40 TYR HD2 H 6.78 . 1 207 . 41 CYS H H 8.89 . 1 208 . 41 CYS HA H 5.49 . 1 209 . 41 CYS HB2 H 2.83 . 1 210 . 41 CYS HB3 H 2.58 . 1 211 . 42 TRP H H 9.39 . 1 212 . 42 TRP HA H 5.32 . 1 213 . 42 TRP HB2 H 3.12 . 1 214 . 42 TRP HB3 H 3.06 . 1 215 . 42 TRP HD1 H 6.76 . 1 216 . 42 TRP HE1 H 9.86 . 1 217 . 42 TRP HE3 H 6.36 . 1 218 . 42 TRP HZ2 H 6.93 . 1 219 . 42 TRP HZ3 H 6.21 . 1 220 . 42 TRP HH2 H 6.75 . 1 221 . 43 CYS H H 8.4 . 1 222 . 43 CYS HA H 6.06 . 1 223 . 43 CYS HB2 H 3.3 . 1 224 . 43 CYS HB3 H 2.57 . 1 225 . 44 VAL H H 9.29 . 1 226 . 44 VAL HA H 5.24 . 1 227 . 44 VAL HB H 1.87 . 1 228 . 44 VAL HG1 H 0.78 . 1 229 . 45 PHE H H 8.79 . 1 230 . 45 PHE HA H 4.77 . 1 231 . 45 PHE HB2 H 3.39 . 1 232 . 45 PHE HB3 H 2.78 . 1 233 . 45 PHE HD1 H 7.30 . 1 234 . 45 PHE HE1 H 7.37 . 1 235 . 45 PHE HZ H 7.10 . 1 236 . 46 PRO HA H 4.63 . 1 237 . 46 PRO HB2 H 2.49 . 1 238 . 46 PRO HB3 H 1.97 . 1 239 . 46 PRO HG2 H 2.23 . 1 240 . 46 PRO HG3 H 2.11 . 1 241 . 46 PRO HD2 H 4.11 . 1 242 . 46 PRO HD3 H 3.98 . 1 243 . 47 ASN H H 7.52 . 1 244 . 47 ASN HA H 4.72 . 1 245 . 47 ASN HB2 H 3.29 . 1 246 . 47 ASN HB3 H 2.86 . 1 247 . 47 ASN HD21 H 7.64 . 1 248 . 47 ASN HD22 H 6.8 . 1 249 . 48 GLY H H 8.69 . 1 250 . 48 GLY HA2 H 3.22 . 1 251 . 48 GLY HA3 H 2.16 . 1 252 . 49 THR H H 7.68 . 1 253 . 49 THR HA H 4.18 . 1 254 . 49 THR HB H 4.3 . 1 255 . 49 THR HG2 H 1.23 . 1 256 . 50 GLU H H 8.6 . 1 257 . 50 GLU HA H 4.37 . 1 258 . 50 GLU HB2 H 1.8 . 1 259 . 50 GLU HB3 H 1.71 . 1 260 . 50 GLU HG2 H 2.22 . 1 261 . 50 GLU HG3 H 2.03 . 1 262 . 51 VAL H H 8.89 . 1 263 . 51 VAL HA H 3.9 . 1 264 . 51 VAL HB H 1.54 . 1 265 . 51 VAL HG1 H 0.74 . 1 266 . 51 VAL HG2 H -0.37 . 1 267 . 52 PRO HA H 4.25 . 1 268 . 52 PRO HB2 H 2.3 . 1 269 . 52 PRO HB3 H 1.86 . 1 270 . 52 PRO HG2 H 2.16 . 1 271 . 52 PRO HG3 H 2.03 . 1 272 . 52 PRO HD2 H 4.31 . 1 273 . 52 PRO HD3 H 3.77 . 1 274 . 53 ASN H H 8.89 . 1 275 . 53 ASN HA H 4.51 . 1 276 . 53 ASN HB2 H 3.05 . 1 277 . 53 ASN HB3 H 2.92 . 1 278 . 53 ASN HD21 H 7.66 . 1 279 . 53 ASN HD22 H 6.98 . 1 280 . 54 THR H H 7.92 . 1 281 . 54 THR HA H 4.65 . 1 282 . 54 THR HB H 4.61 . 1 283 . 54 THR HG2 H 1.03 . 1 284 . 55 ARG H H 8.11 . 1 285 . 55 ARG HA H 5.46 . 1 286 . 55 ARG HB2 H 1.85 . 1 287 . 55 ARG HG2 H 1.48 . 1 288 . 55 ARG HD2 H 2.83 . 1 289 . 55 ARG HD3 H 2.74 . 1 290 . 55 ARG HE H 7.05 . 1 291 . 56 SER H H 9.41 . 1 292 . 56 SER HA H 4.77 . 1 293 . 56 SER HB2 H 3.92 . 1 294 . 56 SER HB3 H 3.84 . 1 295 . 57 ARG H H 8.81 . 1 296 . 57 ARG HA H 4.29 . 1 297 . 57 ARG HB2 H 1.73 . 1 298 . 57 ARG HB3 H 1.51 . 1 299 . 57 ARG HG2 H 1.25 . 1 300 . 57 ARG HG3 H 1.02 . 1 301 . 57 ARG HD2 H 2.96 . 1 302 . 57 ARG HE H 6.97 . 1 303 . 58 GLY H H 8.18 . 1 304 . 58 GLY HA2 H 4.03 . 1 305 . 58 GLY HA3 H 3.99 . 1 306 . 59 HIS H H 8.57 . 1 307 . 59 HIS HA H 4.22 . 1 308 . 59 HIS HB2 H 3.1 . 1 309 . 59 HIS HB3 H 3.07 . 1 310 . 59 HIS HD2 H 7.21 . 1 311 . 59 HIS HE1 H 8.53 . 1 312 . 60 HIS H H 7.35 . 1 313 . 60 HIS HA H 4.67 . 1 314 . 60 HIS HB2 H 3.35 . 1 315 . 60 HIS HB3 H 3.12 . 1 316 . 60 HIS HD2 H 7.27 . 1 317 . 60 HIS HE1 H 8.60 . 1 318 . 61 ASN H H 8.85 . 1 319 . 61 ASN HA H 4.75 . 1 320 . 61 ASN HB2 H 2.84 . 1 321 . 61 ASN HB3 H 2.73 . 1 322 . 61 ASN HD21 H 7.65 . 1 323 . 61 ASN HD22 H 7.01 . 1 324 . 62 CYS H H 8.71 . 1 325 . 62 CYS HA H 4.92 . 1 326 . 62 CYS HB2 H 3.25 . 1 327 . 62 CYS HB3 H 2.55 . 1 328 . 63 SER H H 8.55 . 1 329 . 63 SER HA H 4.45 . 1 330 . 63 SER HB2 H 3.87 . 1 331 . 64 GLU H H 8.47 . 1 332 . 64 GLU HA H 4.46 . 1 333 . 64 GLU HB2 H 2.2 . 1 334 . 64 GLU HB3 H 1.99 . 1 335 . 64 GLU HG2 H 2.46 . 1 336 . 65 SER H H 8.27 . 1 337 . 65 SER HA H 4.42 . 1 338 . 65 SER HB2 H 3.93 . 1 339 . 65 SER HB3 H 3.89 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 THR H 2 THR HA 8.3 . . . 2 3JHNHA 4 CYS H 4 CYS HA 4.9 . . . 3 3JHNHA 5 GLN H 5 GLN HA 6.4 . . . 4 3JHNHA 6 GLU H 6 GLU HA 5.0 . . . 5 3JHNHA 7 GLU H 7 GLU HA 3.8 . . . 6 3JHNHA 8 VAL H 8 VAL HA 6.0 . . . 7 3JHNHA 9 SER H 9 SER HA 3.8 . . . 8 3JHNHA 11 ILE H 11 ILE HA 7.9 . . . 9 3JHNHA 13 ALA H 13 ALA HA 5.4 . . . 10 3JHNHA 14 VAL H 14 VAL HA 4.9 . . . 11 3JHNHA 15 HIS H 15 HIS HA 8.0 . . . 12 3JHNHA 19 PHE H 19 PHE HA 6.8 . . . 13 3JHNHA 20 ARG H 20 ARG HA 8.2 . . . 14 3JHNHA 22 LYS H 22 LYS HA 9.8 . . . 15 3JHNHA 23 CYS H 23 CYS HA 10.2 . . . 16 3JHNHA 24 ASP H 24 ASP HA 6.8 . . . 17 3JHNHA 25 GLU H 25 GLU HA 4.3 . . . 18 3JHNHA 26 ASN H 26 ASN HA 9.6 . . . 19 3JHNHA 28 ASN H 28 ASN HA 3.8 . . . 20 3JHNHA 30 LEU H 30 LEU HA 6.8 . . . 21 3JHNHA 33 GLN H 33 GLN HA 9.1 . . . 22 3JHNHA 34 CYS H 34 CYS HA 8.1 . . . 23 3JHNHA 35 TYR H 35 TYR HA 9.7 . . . 24 3JHNHA 37 SER H 37 SER HA 5.8 . . . 25 3JHNHA 38 ILE H 38 ILE HA 6.9 . . . 26 3JHNHA 40 TYR H 40 TYR HA 9.5 . . . 27 3JHNHA 41 CYS H 41 CYS HA 10.8 . . . 28 3JHNHA 42 TRP H 42 TRP HA 11.9 . . . 29 3JHNHA 43 CYS H 43 CYS HA 9.8 . . . 30 3JHNHA 44 VAL H 44 VAL HA 12.2 . . . 31 3JHNHA 45 PHE H 45 PHE HA 7.7 . . . 32 3JHNHA 49 THR H 49 THR HA 5.0 . . . 33 3JHNHA 50 GLU H 50 GLU HA 4.4 . . . 34 3JHNHA 51 VAL H 51 VAL HA 8.6 . . . 35 3JHNHA 53 ASN H 53 ASN HA 6.8 . . . 36 3JHNHA 55 ARG H 55 ARG HA 7.9 . . . 37 3JHNHA 57 ARG H 57 ARG HA 6.2 . . . 38 3JHNHA 60 HIS H 60 HIS HA 15.6 . . . 39 3JHNHA 62 CYS H 62 CYS HA 8.3 . . . 40 3JHNHA 63 SER H 63 SER HA 7.7 . . . 41 3JHNHA 64 GLU H 64 GLU HA 7.3 . . . 42 3JHNHA 65 SER H 65 SER HA 6.5 . . . stop_ save_