data_4267 #Corrected using PDB structure: 1X8UC # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 25 D HA 4.15 4.96 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #116 Y CA 65.90 59.64 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 48 D CB 32.64 39.97 # 77 C CB 36.83 41.89 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #116 Y C 176.48 170.47 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 35 V N 106.65 119.15 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.03 0.10 0.24 0.09 -0.09 -0.01 # #bmr4267.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4267.str file): #HA CA CB CO N HN #N/A +0.17 +0.17 +0.09 -0.09 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.12 +/-0.12 +/-0.13 +/-0.27 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.901 0.960 0.994 0.724 0.860 0.760 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.152 0.764 0.750 0.783 1.691 0.299 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments, 3JHNHA coupling constants and secondary structure of HNGAL (Human Neutrophil Gelatinase-Associated Lipocalin) in its apo form. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Coles Murray . . 2 Diercks Tammo . . 3 Muehlenweg Bernd . . 4 Bartsch Stefan . . 5 Zoelzer Volker . . 6 Tschesche Harald . . 7 Kessler Horst . . stop_ _BMRB_accession_number 4267 _BMRB_flat_file_name bmr4267.str _Entry_type update _Submission_date 1998-11-11 _Accession_date 1998-11-11 _Entry_origination author _NMR_STAR_version 2.1 _Experimental_method NMR _Details ; The data presented are for apo-HNGAL (Human Neutrophil Gelatinase-Associated Lipocalin), a member of the lipocalin family of extracellular proteins which generally function as transporters of small, hydrophobic molecules. HNGAL binds bacterially-derived chemotactic formyl-peptides which induce leukocyte granule discharge. HNGAL aslo forms a protein-protein complex with the proenzyme of matrix metalloproteinase-9, pro-MMP-9 (or progelatinase B) which influences its subsequent complexations and metalloproteinase activity. This is the first lipocalin structure solved by NMR methods. ; loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 T1_relaxation 3 T2_relaxation 3 heteronuclear_NOE 9 S2_parameters 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 1080 '13C chemical shifts' 737 '15N chemical shifts' 188 'coupling constants' 125 'T1 relaxation values' 443 'T2 relaxation values' 445 'heteronuclear NOE values' 443 'S2 values' 152 'secondary structure features' 11 stop_ loop_ _Revision_date _Revision_type _Revision_author _Revision_detail 2000-08-15 update BMRB 'chemical shift for LYS 135 CE corrected' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zoelzer, V., Tschesche, H., and Kessler, H., "The Solution Structure and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin," J. Mol. Biol. 289, 139-157 (1999). ; _Citation_title ; The Solution Strucuture and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin. ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99272561 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Coles Murray . . 2 Diercks Tammo . . 3 Muehlenweg Bernd . . 4 Bartsch Stefan . . 5 Zoelzer Volker . . 6 Tschesche Harald . . 7 Kessler Horst . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 289 _Journal_issue 1 _Page_first 139 _Page_last 157 _Year 1999 loop_ _Keyword NMR protein 'resonance assignment' 'coupling constants' 'secondary structure' 'lipocalin' 'NGAL' stop_ save_ ################################## # Molecular system description # ################################## save_system_HNGAL _Saveframe_category molecular_system _Mol_system_name 'apo-HNGAL Human Neutrophil Gelatinase-Associated Lipocalin' _Abbreviation_common HNGAL loop_ _Mol_system_component_name _Mol_label HNGAL $HNGAL stop_ _System_molecular_weight 20660 _System_physical_state native _System_oligomer_state monomer _System_type 'monomeric protein' _System_paramagnetic no _System_thiol_state 'reduced and oxidized present' loop_ _Biological_function 'small molecule transport' 'chemotactic recognition' 'multimeric matrix-metalloproteinase component' stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1NGL "A Chain A, Human Neutrophil Gelatinase-Associated Lipocalin (Hngal), Regularised Average Nmr Structure" . PDB 1DFV "B Chain B, Crystal Structure Of Human Neutrophil Gelatinase Associated Lipocalin Monomer" . stop_ save_ ######################## # Monomeric polymers # ######################## save_HNGAL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'HNGAL Human Neutrophil Gelatinase-Associated Lipocalin' _Abbreviation_common HNGAL _Molecular_mass 20660 _Details ; Construct contains the mature protein sequence, without N-terminal signal sequence, preceded by a N-terminal methionine. Residue numbering refers to the mature sequence with the methionine designated M0. Disulphide bridge C76-C175. ; ############################## # Polymer residue sequence # ############################## _Residue_count 179 _Mol_residue_sequence ; MQDSTSDLIPAPPLSKVPLQ QNFQDNQFQGKWYVVGLAGN AILREDKDPQKMYATIYELK EDKSYNVTSVLFRKKKCDYW IRTFVPGCQPGEFTLGNIKS YPGLTSYLVRVVSTNYNQHA MVFFKKVSQNREYFKITLYG RTKELTSELKENFIRFSKSL GLPENHIVFPVPIDQCIDG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 GLN 3 2 ASP 4 3 SER 5 4 THR 6 5 SER 7 6 ASP 8 7 LEU 9 8 ILE 10 9 PRO 11 10 ALA 12 11 PRO 13 12 PRO 14 13 LEU 15 14 SER 16 15 LYS 17 16 VAL 18 17 PRO 19 18 LEU 20 19 GLN 21 20 GLN 22 21 ASN 23 22 PHE 24 23 GLN 25 24 ASP 26 25 ASN 27 26 GLN 28 27 PHE 29 28 GLN 30 29 GLY 31 30 LYS 32 31 TRP 33 32 TYR 34 33 VAL 35 34 VAL 36 35 GLY 37 36 LEU 38 37 ALA 39 38 GLY 40 39 ASN 41 40 ALA 42 41 ILE 43 42 LEU 44 43 ARG 45 44 GLU 46 45 ASP 47 46 LYS 48 47 ASP 49 48 PRO 50 49 GLN 51 50 LYS 52 51 MET 53 52 TYR 54 53 ALA 55 54 THR 56 55 ILE 57 56 TYR 58 57 GLU 59 58 LEU 60 59 LYS 61 60 GLU 62 61 ASP 63 62 LYS 64 63 SER 65 64 TYR 66 65 ASN 67 66 VAL 68 67 THR 69 68 SER 70 69 VAL 71 70 LEU 72 71 PHE 73 72 ARG 74 73 LYS 75 74 LYS 76 75 LYS 77 76 CYS 78 77 ASP 79 78 TYR 80 79 TRP 81 80 ILE 82 81 ARG 83 82 THR 84 83 PHE 85 84 VAL 86 85 PRO 87 86 GLY 88 87 CYS 89 88 GLN 90 89 PRO 91 90 GLY 92 91 GLU 93 92 PHE 94 93 THR 95 94 LEU 96 95 GLY 97 96 ASN 98 97 ILE 99 98 LYS 100 99 SER 101 100 TYR 102 101 PRO 103 102 GLY 104 103 LEU 105 104 THR 106 105 SER 107 106 TYR 108 107 LEU 109 108 VAL 110 109 ARG 111 110 VAL 112 111 VAL 113 112 SER 114 113 THR 115 114 ASN 116 115 TYR 117 116 ASN 118 117 GLN 119 118 HIS 120 119 ALA 121 120 MET 122 121 VAL 123 122 PHE 124 123 PHE 125 124 LYS 126 125 LYS 127 126 VAL 128 127 SER 129 128 GLN 130 129 ASN 131 130 ARG 132 131 GLU 133 132 TYR 134 133 PHE 135 134 LYS 136 135 ILE 137 136 THR 138 137 LEU 139 138 TYR 140 139 GLY 141 140 ARG 142 141 THR 143 142 LYS 144 143 GLU 145 144 LEU 146 145 THR 147 146 SER 148 147 GLU 149 148 LEU 150 149 LYS 151 150 GLU 152 151 ASN 153 152 PHE 154 153 ILE 155 154 ARG 156 155 PHE 157 156 SER 158 157 LYS 159 158 SER 160 159 LEU 161 160 GLY 162 161 LEU 163 162 PRO 164 163 GLU 165 164 ASN 166 165 HIS 167 166 ILE 168 167 VAL 169 168 PHE 170 169 PRO 171 170 VAL 172 171 PRO 173 172 ILE 174 173 ASP 175 174 GLN 176 175 CYS 177 176 ILE 178 177 ASP 179 178 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1QQS "A Chain A, Neutrophil Gelatinase AssociatedLipocalin Homodimer" 102.87 174 98 98 2e-95 PDB 1DFV "A Chain A, Crystal Structure Of HumanNeutrophil Gelatinase Associated Lipocalin Monomer" 101.13 177 100 100 1e-101 PDB 1NGL "A Chain A, Human NeutrophilGelatinase-Associated Lipocalin (Hngal), RegularisedAverage Nmr Structure" 100.00 179 100 100 1e-102 PDB 1L6M "A Chain A, Neutrophil Gelatinase-AssociatedLipocalin Is A Novel Bacteriostatic Agent ThatInterferes With Siderophore- Mediated Iron Acquisition" 99.44 180 99 99 10e-101 EMBL CAA58127.1 "neutrophil gelatinase associatedlipocalin [Homo sapiens]" 90.40 198 100 100 1e-101 EMBL CAG46889.1 "LCN2 [Homo sapiens]" 90.40 198 100 100 1e-101 EMBL CAA67574.1 "NGAL [Homo sapiens]" 90.40 198 99 99 1e-101 GenBank AAD14168.1 "neutrophil lipocalin [Homo sapiens]" 100.56 178 100 100 1e-101 GenBank AAB26529.1 "neutrophil gelatinase-associatedlipocalin, NGAL [human, neutrophils, Peptide, 178 aa]" 100.56 178 99 100 1e-101 GenBank AAH33089.1 "Lipocalin 2 (oncogene 24p3) [Homosapiens]" 90.40 198 100 100 1e-101 PIR JC2339 "neutrophil gelatinase-associated lipocalinprecursor - human" 90.86 197 100 100 1e-101 REF NP_005555.2 "lipocalin 2 (oncogene 24p3) [Homosapiens]" 90.40 198 100 100 1e-101 SWISS-PROT P80188 "NGAL_HUMAN Neutrophil gelatinase-associatedlipocalin precursor (NGAL) (P25) (25 kDaalpha-2-microglobulin-related subunit of MMP-9)(Lipocalin 2) (Oncogene 24p3)" 90.40 198 100 100 1e-101 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _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 HNGAL 76 CYS SG HNGAL 175 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 $HNGAL 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_type _Vector_name _Details $HNGAL 'recombinant technology' 'E. coli' 'Bl21[DE3]' Escherichia coli plasmid pET11a ; Expression controlled with the T7 lac promoter ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_HNGAL_sample_N15 _Saveframe_category sample _Sample_type solution _Details ; Uniformly 15N labelled sample, unliganded HNGAL. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HNGAL 1.43 mM '[U-15N]' 'sodium acetate' 50 mM . 'acetic acid' 50 mM . 'sodium chloride' 50 mM . 'sodium azide' 0.02 % . D2O 10.0 % . H2O 90.0 % . stop_ save_ save_HNGAL_sample_dl _Saveframe_category sample _Sample_type solution _Details ; Uniformly 15N,13C labelled sample, unliganded HNGAL. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HNGAL 1.15 mM '[U-15N; U-13C]' 'sodium acetate' 50 mM . 'acetic acid' 50 mM . 'sodium chloride' 50 mM . 'sodium azide' 0.02 % . D2O 10.0 % . H2O 90.0 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_label_750 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details ; four channel, three gradient, triple resonance ; save_ save_NMR_spectrometer_label_600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details ; four channel, three gradient, triple resonance ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_all _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Internal TMS referencing for proton, 15N and 13C by frequency ratio ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _Indirect_shift_ratio TMS H 1 'methyl protons' ppm 0.0 internal direct . TMS N 15 'methyl protons' ppm 0.0 . indirect 0.10132912 TMS C 13 'methyl protons' ppm 0.0 . indirect 0.25144953 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; Many methylene and valine/luecine methyl groups have been stereospecifically assigned. those not stereo-assigned are given ambiguity code 2 even where HB2,HB3 etc. are stated as having different shifts. Glycine HA pairs are steroassigned (exception G178). ; loop_ _Sample_label $HNGAL_sample_N15 stop_ _Sample_conditions_label $sample_conditions_all _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HNGAL loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET HE H 2.14 . 1 2 1 MET CE C 16.77 . 1 3 2 GLN HA H 4.41 . 1 4 2 GLN HB2 H 2.09 . 1 5 2 GLN HB3 H 2.09 . 1 6 2 GLN HG2 H 2.33 . 1 7 2 GLN HG3 H 2.33 . 1 8 2 GLN C C 178.20 . 1 9 2 GLN CA C 55.88 . 1 10 2 GLN CB C 29.70 . 1 11 3 ASP H H 8.58 . 1 12 3 ASP HA H 4.64 . 1 13 3 ASP HB2 H 2.72 . 2 14 3 ASP HB3 H 2.66 . 2 15 3 ASP C C 176.50 . 1 16 3 ASP CA C 54.39 . 1 17 3 ASP CB C 41.36 . 1 18 3 ASP N N 122.72 . 1 19 4 SER H H 8.51 . 1 20 4 SER HA H 4.55 . 1 21 4 SER HB2 H 3.94 . 1 22 4 SER HB3 H 3.94 . 1 23 4 SER C C 175.20 . 1 24 4 SER CA C 58.59 . 1 25 4 SER CB C 63.75 . 1 26 4 SER N N 116.72 . 1 27 5 THR H H 8.38 . 1 28 5 THR HA H 4.41 . 1 29 5 THR HB H 4.34 . 1 30 5 THR HG2 H 1.26 . 1 31 5 THR C C 174.90 . 1 32 5 THR CA C 62.20 . 1 33 5 THR CB C 69.69 . 1 34 5 THR CG2 C 22.47 . 1 35 5 THR N N 115.23 . 1 36 6 SER H H 8.26 . 1 37 6 SER HA H 4.50 . 1 38 6 SER HB2 H 3.92 . 1 39 6 SER HB3 H 3.92 . 1 40 6 SER C C 174.26 . 1 41 6 SER CA C 58.51 . 1 42 6 SER CB C 63.90 . 1 43 6 SER N N 117.54 . 1 44 7 ASP H H 8.32 . 1 45 7 ASP HA H 4.64 . 1 46 7 ASP HB2 H 2.65 . 2 47 7 ASP HB3 H 2.72 . 2 48 7 ASP C C 175.84 . 1 49 7 ASP CA C 54.36 . 1 50 7 ASP CB C 41.12 . 1 51 7 ASP N N 122.41 . 1 52 8 LEU H H 8.06 . 1 53 8 LEU HA H 4.55 . 1 54 8 LEU HB2 H 1.55 . 2 55 8 LEU HB3 H 1.54 . 2 56 8 LEU HG H 1.57 . 1 57 8 LEU HD1 H 0.71 . 2 58 8 LEU HD2 H 0.76 . 2 59 8 LEU C C 177.51 . 1 60 8 LEU CA C 54.22 . 1 61 8 LEU CB C 43.50 . 1 62 8 LEU CG C 27.47 . 1 63 8 LEU CD1 C 24.67 . 2 64 8 LEU CD2 C 23.97 . 2 65 8 LEU N N 122.55 . 1 66 9 ILE H H 8.85 . 1 67 9 ILE HA H 4.27 . 1 68 9 ILE HB H 1.66 . 1 69 9 ILE HG12 H 1.40 . 2 70 9 ILE HG13 H 1.19 . 2 71 9 ILE HG2 H 1.17 . 1 72 9 ILE HD1 H 0.74 . 1 73 9 ILE CA C 59.81 . 1 74 9 ILE CB C 39.89 . 1 75 9 ILE CG1 C 24.27 . 1 76 9 ILE CG2 C 16.17 . 1 77 9 ILE CD1 C 13.87 . 1 78 9 ILE N N 128.18 . 1 79 10 PRO HA H 4.48 . 1 80 10 PRO HB2 H 1.84 . 1 81 10 PRO HB3 H 2.28 . 1 82 10 PRO HG2 H 2.10 . 2 83 10 PRO HG3 H 2.03 . 2 84 10 PRO HD2 H 3.92 . 2 85 10 PRO HD3 H 3.75 . 2 86 10 PRO C C 175.94 . 1 87 10 PRO CA C 62.45 . 1 88 10 PRO CB C 32.32 . 1 89 10 PRO CG C 27.57 . 1 90 10 PRO CD C 51.27 . 1 91 11 ALA H H 8.50 . 1 92 11 ALA HA H 3.92 . 1 93 11 ALA HB H 1.06 . 1 94 11 ALA CA C 49.77 . 1 95 11 ALA CB C 16.45 . 1 96 11 ALA N N 121.66 . 1 97 12 PRO HA H 4.59 . 1 98 12 PRO HB2 H 1.97 . 2 99 12 PRO HB3 H 1.87 . 2 100 12 PRO HG2 H 1.52 . 1 101 12 PRO HG3 H 1.52 . 1 102 12 PRO HD2 H 2.48 . 2 103 12 PRO HD3 H 2.26 . 2 104 12 PRO CA C 60.07 . 1 105 12 PRO CG C 26.97 . 1 106 12 PRO CD C 48.17 . 1 107 13 PRO HA H 4.36 . 1 108 13 PRO HB2 H 2.24 . 2 109 13 PRO HB3 H 1.90 . 2 110 13 PRO HG2 H 1.55 . 2 111 13 PRO HG3 H 1.94 . 2 112 13 PRO HD2 H 3.70 . 2 113 13 PRO HD3 H 3.34 . 2 114 13 PRO C C 178.20 . 1 115 13 PRO CA C 62.10 . 1 116 13 PRO CB C 31.36 . 1 117 13 PRO CG C 30.27 . 1 118 13 PRO CD C 49.83 . 1 119 14 LEU H H 8.52 . 1 120 14 LEU HA H 3.62 . 1 121 14 LEU HB2 H 1.38 . 1 122 14 LEU HB3 H 1.68 . 1 123 14 LEU HG H 1.74 . 1 124 14 LEU HD1 H 0.65 . 2 125 14 LEU HD2 H 0.86 . 2 126 14 LEU C C 178.74 . 1 127 14 LEU CA C 57.05 . 1 128 14 LEU CB C 40.41 . 1 129 14 LEU CG C 26.87 . 1 130 14 LEU CD1 C 23.07 . 2 131 14 LEU CD2 C 24.97 . 2 132 14 LEU N N 122.55 . 1 133 15 SER H H 7.87 . 1 134 15 SER HA H 4.04 . 1 135 15 SER HB2 H 3.92 . 2 136 15 SER HB3 H 3.83 . 2 137 15 SER C C 176.13 . 1 138 15 SER CA C 59.78 . 1 139 15 SER CB C 61.83 . 1 140 15 SER N N 112.19 . 1 141 16 LYS H H 7.60 . 1 142 16 LYS HA H 4.22 . 1 143 16 LYS HB2 H 1.57 . 1 144 16 LYS HB3 H 1.86 . 1 145 16 LYS HG2 H 1.33 . 1 146 16 LYS HG3 H 1.33 . 1 147 16 LYS HD2 H 1.91 . 1 148 16 LYS HD3 H 1.91 . 1 149 16 LYS HE2 H 3.77 . 1 150 16 LYS HE3 H 3.77 . 1 151 16 LYS C C 174.57 . 1 152 16 LYS CA C 55.96 . 1 153 16 LYS CB C 32.79 . 1 154 16 LYS CG C 24.27 . 1 155 16 LYS CE C 46.37 . 1 156 16 LYS N N 120.13 . 1 157 17 VAL H H 7.40 . 1 158 17 VAL HA H 4.27 . 1 159 17 VAL HB H 1.72 . 1 160 17 VAL HG1 H 0.40 . 1 161 17 VAL HG2 H -0.14 . 1 162 17 VAL CA C 59.22 . 1 163 17 VAL CB C 31.39 . 1 164 17 VAL CG1 C 22.77 . 1 165 17 VAL CG2 C 19.17 . 1 166 17 VAL N N 120.18 . 1 167 18 PRO HA H 4.21 . 1 168 18 PRO HB2 H 2.28 . 1 169 18 PRO HB3 H 1.76 . 1 170 18 PRO HG2 H 1.87 . 1 171 18 PRO HG3 H 1.87 . 1 172 18 PRO HD2 H 4.23 . 2 173 18 PRO HD3 H 3.46 . 2 174 18 PRO C C 171.72 . 1 175 18 PRO CA C 63.02 . 1 176 18 PRO CB C 32.19 . 1 177 18 PRO CG C 27.07 . 1 178 18 PRO CD C 51.43 . 1 179 19 LEU H H 7.40 . 1 180 19 LEU HA H 4.64 . 1 181 19 LEU HB2 H 1.50 . 1 182 19 LEU HB3 H 0.98 . 1 183 19 LEU HG H 1.52 . 1 184 19 LEU HD1 H 0.69 . 1 185 19 LEU HD2 H 0.69 . 1 186 19 LEU C C 177.36 . 1 187 19 LEU CA C 52.11 . 1 188 19 LEU CB C 46.22 . 1 189 19 LEU CG C 27.37 . 1 190 19 LEU CD1 C 25.97 . 2 191 19 LEU CD2 C 26.17 . 2 192 19 LEU N N 116.85 . 1 193 20 GLN H H 8.52 . 1 194 20 GLN HA H 3.94 . 1 195 20 GLN HB2 H 1.83 . 1 196 20 GLN HB3 H 1.58 . 1 197 20 GLN HG2 H 2.29 . 1 198 20 GLN HG3 H 2.29 . 1 199 20 GLN HE21 H 8.15 . 1 200 20 GLN HE22 H 7.03 . 1 201 20 GLN C C 174.95 . 1 202 20 GLN CA C 55.55 . 1 203 20 GLN CB C 28.60 . 1 204 20 GLN N N 127.40 . 1 205 20 GLN NE2 N 116.16 . 1 206 21 GLN H H 8.94 . 1 207 21 GLN HA H 4.13 . 1 208 21 GLN HB2 H 2.10 . 1 209 21 GLN HB3 H 2.10 . 1 210 21 GLN HG2 H 2.50 . 1 211 21 GLN HG3 H 2.50 . 1 212 21 GLN HE21 H 7.57 . 1 213 21 GLN HE22 H 6.95 . 1 214 21 GLN C C 176.87 . 1 215 21 GLN CA C 56.33 . 1 216 21 GLN CB C 29.22 . 1 217 21 GLN CG C 33.76 . 1 218 21 GLN CD C 180.63 . 1 219 21 GLN N N 130.26 . 1 220 21 GLN NE2 N 112.84 . 1 221 22 ASN H H 9.23 . 1 222 22 ASN HA H 4.48 . 1 223 22 ASN HB2 H 3.07 . 1 224 22 ASN HB3 H 2.74 . 1 225 22 ASN HD21 H 7.69 . 1 226 22 ASN HD22 H 6.96 . 1 227 22 ASN C C 175.39 . 1 228 22 ASN CA C 53.65 . 1 229 22 ASN CB C 37.31 . 1 230 22 ASN CG C 178.40 . 1 231 22 ASN N N 120.51 . 1 232 22 ASN ND2 N 112.72 . 1 233 23 PHE H H 8.00 . 1 234 23 PHE HA H 4.08 . 1 235 23 PHE HB2 H 2.54 . 1 236 23 PHE HB3 H 2.97 . 1 237 23 PHE HD1 H 7.13 . 1 238 23 PHE HD2 H 7.13 . 1 239 23 PHE HE1 H 7.59 . 1 240 23 PHE HE2 H 7.59 . 1 241 23 PHE C C 175.64 . . 242 23 PHE CA C 59.92 . 1 243 23 PHE CB C 39.70 . 1 244 23 PHE N N 117.74 . 1 245 24 GLN H H 7.56 . 1 246 24 GLN HA H 4.32 . 1 247 24 GLN HB2 H 1.26 . 1 248 24 GLN HB3 H 1.76 . 1 249 24 GLN HG2 H 2.47 . 2 250 24 GLN HG3 H 2.17 . 2 251 24 GLN HE21 H 7.02 . 1 252 24 GLN HE22 H 6.77 . 1 253 24 GLN C C 174.11 . 1 254 24 GLN CA C 52.89 . 1 255 24 GLN CB C 29.22 . 1 256 24 GLN CG C 32.37 . 1 257 24 GLN CD C 180.73 . 1 258 24 GLN N N 128.15 . 1 259 24 GLN NE2 N 114.30 . 1 260 25 ASP H H 8.70 . 1 261 25 ASP HA H 4.18 . 1 262 25 ASP HB2 H 2.87 . 1 263 25 ASP HB3 H 3.14 . 1 264 25 ASP C C 180.76 . 1 265 25 ASP CA C 56.11 . 1 266 25 ASP CB C 38.74 . 1 267 25 ASP N N 126.36 . 1 268 26 ASN H H 9.19 . 1 269 26 ASN HA H 4.39 . 1 270 26 ASN HB2 H 2.87 . 1 271 26 ASN HB3 H 2.74 . 1 272 26 ASN HD21 H 7.67 . 1 273 26 ASN HD22 H 7.00 . 1 274 26 ASN C C 177.22 . 1 275 26 ASN CA C 55.65 . 1 276 26 ASN CB C 37.31 . 1 277 26 ASN CG C 176.36 . 1 278 26 ASN N N 121.13 . 1 279 26 ASN ND2 N 114.20 . 1 280 27 GLN H H 7.03 . 1 281 27 GLN HA H 4.25 . 1 282 27 GLN HB2 H 1.77 . 2 283 27 GLN HB3 H 1.08 . 2 284 27 GLN HG2 H 2.11 . 1 285 27 GLN HG3 H 2.11 . 1 286 27 GLN HE21 H 7.17 . 1 287 27 GLN HE22 H 6.63 . 1 288 27 GLN C C 176.33 . 1 289 27 GLN CA C 56.95 . 1 290 27 GLN CB C 28.98 . 1 291 27 GLN CG C 33.57 . 1 292 27 GLN CD C 179.12 . 1 293 27 GLN N N 117.47 . 1 294 27 GLN NE2 N 110.89 . 1 295 28 PHE H H 7.52 . 1 296 28 PHE HA H 4.55 . 1 297 28 PHE HB2 H 3.42 . 2 298 28 PHE HB3 H 3.18 . 2 299 28 PHE HD1 H 6.87 . 1 300 28 PHE HD2 H 6.87 . 1 301 28 PHE HE1 H 7.10 . 1 302 28 PHE HE2 H 7.10 . 1 303 28 PHE C C 173.13 . 1 304 28 PHE CA C 59.68 . 1 305 28 PHE CB C 41.60 . 1 306 28 PHE N N 119.42 . 1 307 29 GLN H H 6.73 . 1 308 29 GLN HA H 4.41 . 1 309 29 GLN HB2 H 2.68 . 2 310 29 GLN HB3 H 2.38 . 2 311 29 GLN HG2 H 2.14 . 1 312 29 GLN HG3 H 2.14 . 1 313 29 GLN HE21 H 7.59 . 1 314 29 GLN HE22 H 6.75 . 1 315 29 GLN C C 174.75 . 1 316 29 GLN CA C 56.19 . 1 317 29 GLN CB C 32.08 . 1 318 29 GLN CD C 180.57 . 1 319 29 GLN N N 109.66 . 1 320 29 GLN NE2 N 112.60 . 1 321 30 GLY H H 9.58 . 1 322 30 GLY HA2 H 4.34 . 1 323 30 GLY HA3 H 3.76 . 1 324 30 GLY C C 172.49 . 1 325 30 GLY CA C 43.48 . 1 326 30 GLY N N 109.62 . 1 327 31 LYS H H 8.58 . 1 328 31 LYS HA H 4.36 . 1 329 31 LYS HB2 H 1.54 . 1 330 31 LYS HB3 H 1.54 . 1 331 31 LYS C C 175.49 . 1 332 31 LYS CA C 57.03 . 1 333 31 LYS CB C 32.55 . 1 334 31 LYS N N 120.51 . 1 335 32 TRP H H 8.99 . 1 336 32 TRP HA H 4.65 . 1 337 32 TRP HB2 H 2.37 . 2 338 32 TRP HB3 H 2.13 . 2 339 32 TRP HD1 H 6.50 . 1 340 32 TRP HE1 H 8.46 . 1 341 32 TRP HE3 H 6.42 . 1 342 32 TRP HZ2 H 6.72 . 1 343 32 TRP HH2 H 6.40 . 1 344 32 TRP C C 174.61 . 1 345 32 TRP CA C 55.06 . 1 346 32 TRP CB C 32.10 . 1 347 32 TRP CD1 C 127.87 . 1 348 32 TRP CZ2 C 119.07 . 1 349 32 TRP CH2 C 122.17 . 1 350 32 TRP N N 130.44 . 1 351 32 TRP NE1 N 126.66 . 1 352 33 TYR H H 9.95 . 1 353 33 TYR HA H 4.59 . 1 354 33 TYR HB2 H 3.16 . 2 355 33 TYR HB3 H 2.82 . 2 356 33 TYR HD1 H 6.74 . 1 357 33 TYR HD2 H 6.74 . 1 358 33 TYR HE1 H 7.00 . 1 359 33 TYR HE2 H 7.00 . 1 360 33 TYR C C 176.62 . 1 361 33 TYR CA C 58.74 . 1 362 33 TYR CB C 39.22 . 1 363 33 TYR CD1 C 133.27 . 1 364 33 TYR CD2 C 133.27 . 1 365 33 TYR N N 120.71 . 1 366 34 VAL H H 8.44 . 1 367 34 VAL HA H 4.17 . 1 368 34 VAL HB H 1.36 . 1 369 34 VAL HG1 H 0.73 . 1 370 34 VAL HG2 H 0.47 . 1 371 34 VAL C C 173.33 . 1 372 34 VAL CA C 64.48 . 1 373 34 VAL CB C 30.41 . 1 374 34 VAL CG1 C 21.97 . 1 375 34 VAL CG2 C 21.97 . 1 376 34 VAL N N 123.03 . 1 377 35 VAL H H 8.45 . 1 378 35 VAL HA H 4.18 . 1 379 35 VAL HB H 1.92 . 1 380 35 VAL HG1 H 1.01 . 1 381 35 VAL HG2 H 1.01 . 1 382 35 VAL C C 176.77 . 1 383 35 VAL CA C 62.85 . 1 384 35 VAL CB C 33.27 . 1 385 35 VAL CG1 C 21.47 . 2 386 35 VAL CG2 C 21.67 . 2 387 35 VAL N N 106.65 . 1 388 36 GLY H H 8.26 . 1 389 36 GLY HA2 H 4.80 . 1 390 36 GLY HA3 H 2.92 . 1 391 36 GLY C C 170.28 . 1 392 36 GLY CA C 45.28 . 1 393 36 GLY N N 106.65 . 1 394 37 LEU H H 9.28 . 1 395 37 LEU HA H 5.24 . 1 396 37 LEU HB2 H 1.52 . 2 397 37 LEU HB3 H 1.38 . 2 398 37 LEU HG H 1.43 . 1 399 37 LEU HD1 H 0.72 . 1 400 37 LEU HD2 H 0.93 . 1 401 37 LEU C C 173.18 . 1 402 37 LEU CA C 54.64 . 1 403 37 LEU CB C 47.79 . 1 404 37 LEU CG C 26.87 . 1 405 37 LEU CD1 C 24.77 . 1 406 37 LEU CD2 C 25.17 . 1 407 37 LEU N N 125.05 . 1 408 38 ALA H H 9.14 . 1 409 38 ALA HA H 5.69 . 1 410 38 ALA HB H 1.34 . 1 411 38 ALA C C 176.63 . 1 412 38 ALA CA C 50.31 . 1 413 38 ALA CB C 24.94 . 1 414 38 ALA N N 125.36 . 1 415 39 GLY H H 7.96 . 1 416 39 GLY HA2 H 3.73 . 1 417 39 GLY HA3 H 4.63 . 1 418 39 GLY C C 173.38 . 1 419 39 GLY CA C 47.25 . 1 420 39 GLY N N 105.52 . 1 421 40 ASN H H 7.71 . 1 422 40 ASN HA H 3.94 . 1 423 40 ASN HB2 H 3.28 . 1 424 40 ASN HB3 H 2.40 . 1 425 40 ASN HD21 H 8.49 . 1 426 40 ASN HD22 H 7.44 . 1 427 40 ASN C C 175.39 . 1 428 40 ASN CA C 54.89 . 1 429 40 ASN CB C 37.31 . 1 430 40 ASN N N 117.07 . 1 431 40 ASN ND2 N 110.10 . 1 432 41 ALA H H 9.49 . 1 433 41 ALA HA H 4.73 . 1 434 41 ALA HB H 1.43 . 1 435 41 ALA C C 176.04 . 1 436 41 ALA CA C 51.12 . 1 437 41 ALA CB C 18.99 . 1 438 41 ALA N N 124.68 . 1 439 42 ILE H H 6.76 . 1 440 42 ILE HA H 4.04 . 1 441 42 ILE HB H 1.82 . 1 442 42 ILE HG12 H 1.41 . 2 443 42 ILE HG13 H 1.22 . 2 444 42 ILE HG2 H 0.67 . 1 445 42 ILE HD1 H 0.65 . 1 446 42 ILE C C 173.43 . 1 447 42 ILE CA C 59.69 . 1 448 42 ILE CB C 38.50 . 1 449 42 ILE CG2 C 17.47 . 1 450 42 ILE CD1 C 11.97 . 1 451 42 ILE N N 121.22 . 1 452 43 LEU H H 7.96 . 1 453 43 LEU HA H 4.63 . 1 454 43 LEU HB2 H 1.36 . 1 455 43 LEU HB3 H 1.36 . 1 456 43 LEU HG H 1.29 . 1 457 43 LEU HD1 H 0.69 . 2 458 43 LEU HD2 H 0.60 . 2 459 43 LEU C C 176.68 . 1 460 43 LEU CA C 53.00 . 1 461 43 LEU CB C 44.82 . 1 462 43 LEU CG C 27.27 . 1 463 43 LEU CD1 C 24.67 . 2 464 43 LEU CD2 C 24.07 . 2 465 43 LEU N N 124.70 . 1 466 44 ARG H H 8.35 . 1 467 44 ARG HA H 3.99 . 1 468 44 ARG HB2 H 1.74 . 2 469 44 ARG HB3 H 1.81 . 2 470 44 ARG HG2 H 2.43 . 2 471 44 ARG HG3 H 2.28 . 2 472 44 ARG HD2 H 3.32 . 1 473 44 ARG HD3 H 3.32 . 1 474 44 ARG CA C 57.13 . 1 475 44 ARG CB C 30.81 . 1 476 44 ARG N N 123.70 . 1 477 45 GLU H H 8.49 . 1 478 45 GLU HA H 4.50 . 1 479 45 GLU HB2 H 2.10 . 2 480 45 GLU HB3 H 1.86 . 2 481 45 GLU CA C 55.60 . 1 482 45 GLU CB C 30.59 . 1 483 45 GLU N N 126.41 . 1 484 46 ASP H H 8.44 . 1 485 46 ASP HA H 4.46 . 1 486 46 ASP HB2 H 2.71 . 2 487 46 ASP HB3 H 2.64 . 2 488 46 ASP C C 177.17 . 1 489 46 ASP CA C 56.06 . 1 490 46 ASP CB C 41.12 . 1 491 46 ASP N N 123.59 . 1 492 47 LYS H H 8.47 . 1 493 47 LYS HA H 4.22 . 1 494 47 LYS HB2 H 1.86 . 1 495 47 LYS HB3 H 1.86 . 1 496 47 LYS HG2 H 1.68 . 1 497 47 LYS HG3 H 1.68 . 1 498 47 LYS HD2 H 1.33 . 1 499 47 LYS HD3 H 1.33 . 1 500 47 LYS HE2 H 2.99 . 1 501 47 LYS HE3 H 2.99 . 1 502 47 LYS C C 176.43 . 1 503 47 LYS CA C 57.18 . 1 504 47 LYS CB C 32.47 . 1 505 47 LYS CG C 25.77 . 1 506 47 LYS CD C 25.37 . 1 507 47 LYS CE C 42.47 . 1 508 47 LYS N N 118.09 . 1 509 48 ASP H H 7.91 . 1 510 48 ASP HA H 4.92 . 1 511 48 ASP HB2 H 2.43 . 1 512 48 ASP HB3 H 2.71 . 1 513 48 ASP CA C 52.35 . 1 514 48 ASP CB C 32.57 . 1 515 48 ASP N N 118.60 . 1 516 49 PRO HB2 H 2.36 . 1 517 49 PRO HB3 H 2.36 . 1 518 49 PRO HG2 H 2.06 . 1 519 49 PRO HG3 H 2.06 . 1 520 49 PRO HD2 H 3.69 . 2 521 49 PRO HD3 H 3.65 . 2 522 49 PRO CG C 27.17 . 1 523 49 PRO CD C 50.37 . 1 524 51 LYS H H 8.63 . 1 525 51 LYS HA H 4.68 . 1 526 51 LYS CA C 55.63 . 1 527 51 LYS CB C 33.99 . 1 528 52 MET H H 8.83 . 1 529 52 MET HA H 3.82 . 1 530 52 MET HB2 H 1.89 . 2 531 52 MET HB3 H 1.78 . 2 532 52 MET HG2 H 2.09 . 1 533 52 MET HG3 H 2.09 . 1 534 52 MET HE H 2.31 . 1 535 52 MET CA C 58.60 . 1 536 52 MET CB C 34.48 . 1 537 52 MET CE C 17.42 . 1 538 52 MET N N 123.18 . 1 539 53 TYR H H 6.85 . 1 540 53 TYR HA H 5.36 . 1 541 53 TYR HB2 H 3.24 . 1 542 53 TYR HB3 H 3.87 . 1 543 53 TYR HD1 H 7.09 . 1 544 53 TYR HD2 H 7.09 . 1 545 53 TYR HE1 H 6.78 . 1 546 53 TYR HE2 H 6.78 . 1 547 53 TYR C C 172.29 . 1 548 53 TYR CA C 54.61 . 1 549 53 TYR CB C 40.65 . 1 550 53 TYR N N 118.31 . 1 551 54 ALA H H 8.33 . 1 552 54 ALA HA H 5.38 . 1 553 54 ALA HB H 1.14 . 1 554 54 ALA C C 175.94 . 1 555 54 ALA CA C 50.13 . 1 556 54 ALA CB C 23.03 . 1 557 54 ALA N N 120.66 . 1 558 55 THR H H 9.34 . 1 559 55 THR HA H 5.20 . 1 560 55 THR HB H 3.61 . 1 561 55 THR HG2 H 0.86 . 1 562 55 THR C C 172.05 . 1 563 55 THR CA C 61.58 . 1 564 55 THR CB C 72.34 . 1 565 55 THR CG2 C 20.77 . 1 566 55 THR N N 116.62 . 1 567 56 ILE H H 9.51 . 1 568 56 ILE HA H 4.62 . 1 569 56 ILE HB H 1.75 . 1 570 56 ILE HG12 H 1.70 . 2 571 56 ILE HG13 H 1.38 . 2 572 56 ILE HG2 H 0.72 . 1 573 56 ILE HD1 H 0.86 . 1 574 56 ILE C C 175.49 . 1 575 56 ILE CA C 60.39 . 1 576 56 ILE CB C 40.17 . 1 577 56 ILE CG2 C 18.87 . 1 578 56 ILE CD1 C 14.57 . 1 579 56 ILE N N 127.62 . 1 580 57 TYR H H 8.88 . 1 581 57 TYR HA H 4.59 . 1 582 57 TYR HB2 H 3.04 . 1 583 57 TYR HB3 H 2.37 . 1 584 57 TYR HD1 H 6.36 . 1 585 57 TYR HD2 H 6.36 . 1 586 57 TYR HE1 H 6.50 . 1 587 57 TYR HE2 H 6.50 . 1 588 57 TYR C C 176.23 . 1 589 57 TYR CA C 57.60 . 1 590 57 TYR CB C 40.08 . 1 591 57 TYR CD1 C 131.87 . 1 592 57 TYR CD2 C 131.87 . 1 593 57 TYR CE1 C 127.87 . 1 594 57 TYR CE2 C 127.87 . 1 595 57 TYR N N 127.82 . 1 596 58 GLU H H 9.13 . 1 597 58 GLU HA H 4.96 . 1 598 58 GLU HB2 H 2.00 . 1 599 58 GLU HB3 H 2.24 . 1 600 58 GLU HG2 H 2.73 . 2 601 58 GLU HG3 H 2.26 . 2 602 58 GLU C C 174.75 . 1 603 58 GLU CA C 55.36 . 1 604 58 GLU CB C 32.55 . 1 605 58 GLU N N 125.89 . 1 606 59 LEU H H 8.93 . 1 607 59 LEU HA H 4.45 . 1 608 59 LEU HB2 H 1.84 . 2 609 59 LEU HB3 H 1.15 . 2 610 59 LEU HG H 1.55 . 1 611 59 LEU HD1 H 0.41 . 1 612 59 LEU HD2 H 0.64 . 1 613 59 LEU C C 176.38 . 1 614 59 LEU CA C 55.40 . 1 615 59 LEU CB C 43.69 . 1 616 59 LEU CG C 26.47 . 1 617 59 LEU CD1 C 22.77 . 1 618 59 LEU CD2 C 22.97 . 1 619 59 LEU N N 130.04 . 1 620 60 LYS H H 9.12 . 1 621 60 LYS HA H 4.64 . 1 622 60 LYS HB2 H 2.05 . 2 623 60 LYS HB3 H 1.98 . 2 624 60 LYS HG2 H 1.57 . 1 625 60 LYS HG3 H 1.57 . 1 626 60 LYS C C 179.14 . 1 627 60 LYS CA C 54.44 . 1 628 60 LYS CB C 32.55 . 1 629 60 LYS N N 127.31 . 1 630 61 GLU H H 9.11 . 1 631 61 GLU HA H 4.04 . 1 632 61 GLU HB2 H 1.91 . 1 633 61 GLU HB3 H 2.10 . 1 634 61 GLU HG2 H 2.37 . 1 635 61 GLU HG3 H 2.37 . 1 636 61 GLU CA C 59.41 . 1 637 61 GLU CB C 29.05 . 1 638 61 GLU N N 121.86 . 1 639 62 ASP H H 7.71 . 1 640 62 ASP HA H 4.50 . 1 641 62 ASP HB2 H 3.15 . 1 642 62 ASP HB3 H 2.59 . 1 643 62 ASP C C 176.68 . 1 644 62 ASP CA C 53.26 . 1 645 62 ASP CB C 39.46 . 1 646 62 ASP N N 116.36 . 1 647 63 LYS H H 8.02 . 1 648 63 LYS HA H 3.67 . 1 649 63 LYS HB2 H 2.23 . 1 650 63 LYS HB3 H 2.45 . 1 651 63 LYS HG2 H 1.72 . 2 652 63 LYS HG3 H 1.46 . 2 653 63 LYS HD2 H 2.07 . 1 654 63 LYS HD3 H 2.07 . 1 655 63 LYS HE2 H 3.08 . 1 656 63 LYS HE3 H 3.08 . 1 657 63 LYS C C 174.36 . 1 658 63 LYS CA C 58.62 . 1 659 63 LYS CB C 28.51 . 1 660 63 LYS CG C 25.57 . 1 661 63 LYS CE C 42.27 . 1 662 63 LYS N N 111.11 . 1 663 64 SER H H 7.94 . 1 664 64 SER HA H 4.92 . 1 665 64 SER HB2 H 4.12 . 2 666 64 SER HB3 H 4.06 . 2 667 64 SER C C 173.23 . 1 668 64 SER CA C 58.11 . 1 669 64 SER CB C 65.40 . 1 670 64 SER N N 111.66 . 1 671 65 TYR H H 9.15 . 1 672 65 TYR HA H 5.76 . 1 673 65 TYR HB2 H 2.43 . 1 674 65 TYR HB3 H 2.74 . 1 675 65 TYR HD1 H 6.66 . 1 676 65 TYR HD2 H 6.66 . 1 677 65 TYR HE1 H 6.34 . 1 678 65 TYR HE2 H 6.34 . 1 679 65 TYR C C 177.51 . 1 680 65 TYR CA C 56.49 . 1 681 65 TYR CB C 42.31 . 1 682 65 TYR CD1 C 132.57 . 1 683 65 TYR CD2 C 132.57 . 1 684 65 TYR CE1 C 131.87 . 1 685 65 TYR CE2 C 131.87 . 1 686 65 TYR N N 113.21 . 1 687 66 ASN H H 9.37 . 1 688 66 ASN HA H 4.96 . 1 689 66 ASN HB2 H 2.61 . 1 690 66 ASN HB3 H 2.85 . 1 691 66 ASN HD21 H 7.48 . 1 692 66 ASN HD22 H 6.51 . 1 693 66 ASN C C 174.80 . 1 694 66 ASN CA C 53.62 . 1 695 66 ASN CB C 39.93 . 1 696 66 ASN CG C 175.69 . 1 697 66 ASN N N 121.06 . 1 698 66 ASN ND2 N 111.87 . 1 699 67 VAL H H 9.04 . 1 700 67 VAL HA H 4.41 . 1 701 67 VAL HB H 0.97 . 1 702 67 VAL HG1 H -0.29 . 1 703 67 VAL HG2 H -0.41 . 1 704 67 VAL C C 175.30 . 1 705 67 VAL CA C 61.49 . 1 706 67 VAL CB C 32.22 . 1 707 67 VAL CG1 C 20.17 . 1 708 67 VAL CG2 C 20.57 . 1 709 67 VAL N N 130.15 . 1 710 68 THR H H 8.80 . 1 711 68 THR HA H 5.00 . 1 712 68 THR HB H 3.96 . 1 713 68 THR HG2 H 1.14 . 1 714 68 THR C C 175.20 . 1 715 68 THR CA C 61.65 . 1 716 68 THR CB C 70.64 . 1 717 68 THR CG2 C 20.87 . 1 718 68 THR N N 125.10 . 1 719 69 SER H H 9.43 . 1 720 69 SER HA H 5.87 . 1 721 69 SER HB2 H 3.89 . 1 722 69 SER HB3 H 3.89 . 1 723 69 SER C C 171.75 . 1 724 69 SER CA C 57.99 . 1 725 69 SER CB C 64.69 . 1 726 69 SER N N 123.79 . 1 727 70 VAL H H 9.16 . 1 728 70 VAL HA H 4.59 . 1 729 70 VAL HB H 1.88 . 1 730 70 VAL HG1 H 0.76 . 1 731 70 VAL HG2 H 0.76 . 1 732 70 VAL C C 173.67 . 1 733 70 VAL CA C 60.79 . 1 734 70 VAL CB C 33.98 . 1 735 70 VAL CG1 C 20.97 . 1 736 70 VAL CG2 C 20.97 . 1 737 70 VAL N N 125.19 . 1 738 71 LEU H H 8.54 . 1 739 71 LEU HA H 4.92 . 1 740 71 LEU HB2 H 1.30 . 2 741 71 LEU HB3 H 1.43 . 2 742 71 LEU HG H 1.33 . 1 743 71 LEU HD1 H 0.32 . 1 744 71 LEU HD2 H 0.48 . 1 745 71 LEU C C 175.00 . 1 746 71 LEU CA C 53.64 . 1 747 71 LEU CB C 45.88 . 1 748 71 LEU CG C 27.57 . 1 749 71 LEU CD1 C 25.67 . 1 750 71 LEU CD2 C 25.87 . 1 751 71 LEU N N 123.79 . 1 752 72 PHE H H 9.27 . 1 753 72 PHE HA H 5.35 . 1 754 72 PHE HB2 H 2.65 . 1 755 72 PHE HB3 H 3.08 . 1 756 72 PHE HD1 H 7.12 . 1 757 72 PHE HD2 H 7.12 . 1 758 72 PHE HE1 H 6.77 . 1 759 72 PHE HE2 H 6.77 . 1 760 72 PHE C C 175.06 . 1 761 72 PHE CA C 55.69 . 1 762 72 PHE CB C 40.27 . 1 763 72 PHE N N 122.92 . 1 764 73 ARG H H 8.61 . 1 765 73 ARG HA H 4.32 . 1 766 73 ARG HB2 H 1.55 . 2 767 73 ARG HB3 H 1.68 . 2 768 73 ARG HG2 H 1.49 . 2 769 73 ARG HG3 H 1.42 . 2 770 73 ARG HD2 H 3.07 . 1 771 73 ARG HD3 H 3.07 . 1 772 73 ARG C C 174.80 . 1 773 73 ARG CA C 55.11 . 1 774 73 ARG CB C 32.57 . 1 775 73 ARG CG C 24.97 . 1 776 73 ARG CD C 44.07 . 1 777 73 ARG N N 127.51 . 1 778 74 LYS H H 8.93 . 1 779 74 LYS HA H 3.67 . 1 780 74 LYS HB2 H 1.32 . 2 781 74 LYS HB3 H 1.81 . 2 782 74 LYS C C 177.16 . 1 783 74 LYS CA C 57.37 . 1 784 74 LYS CB C 30.17 . 1 785 74 LYS N N 123.27 . 1 786 75 LYS H H 7.99 . 1 787 75 LYS HA H 3.43 . 1 788 75 LYS HB2 H 2.02 . 1 789 75 LYS HB3 H 2.02 . 1 790 75 LYS HG2 H 1.31 . 1 791 75 LYS HG3 H 1.31 . 1 792 75 LYS HD2 H 1.67 . 1 793 75 LYS HD3 H 1.67 . 1 794 75 LYS HE2 H 3.01 . 1 795 75 LYS HE3 H 3.01 . 1 796 75 LYS C C 175.00 . 1 797 75 LYS CA C 57.75 . 1 798 75 LYS CB C 30.41 . 1 799 75 LYS CD C 25.57 . 1 800 75 LYS CE C 42.37 . 1 801 75 LYS N N 109.24 . 1 802 76 LYS H H 7.59 . 1 803 76 LYS HA H 4.78 . 1 804 76 LYS HB2 H 1.87 . 2 805 76 LYS HB3 H 1.79 . 2 806 76 LYS HG2 H 1.70 . 1 807 76 LYS HG3 H 1.70 . 1 808 76 LYS HD2 H 1.43 . 2 809 76 LYS HD3 H 1.30 . 2 810 76 LYS HE2 H 3.02 . 1 811 76 LYS HE3 H 3.02 . 1 812 76 LYS C C 173.92 . 1 813 76 LYS CA C 54.75 . 1 814 76 LYS CB C 35.65 . 1 815 76 LYS CE C 42.37 . 1 816 76 LYS N N 119.31 . 1 817 77 CYS H H 8.51 . 1 818 77 CYS HA H 5.47 . 1 819 77 CYS HB2 H 2.86 . 1 820 77 CYS HB3 H 2.86 . 1 821 77 CYS C C 173.67 . 1 822 77 CYS CA C 53.04 . 1 823 77 CYS CB C 36.76 . 1 824 77 CYS N N 117.65 . 1 825 78 ASP H H 9.34 . 1 826 78 ASP HA H 4.96 . 1 827 78 ASP HB2 H 2.47 . 2 828 78 ASP HB3 H 2.37 . 2 829 78 ASP C C 173.72 . 1 830 78 ASP CA C 52.56 . 1 831 78 ASP CB C 44.93 . 1 832 78 ASP N N 127.02 . 1 833 79 TYR H H 8.24 . 1 834 79 TYR HA H 5.47 . 1 835 79 TYR HB2 H 2.85 . 2 836 79 TYR HB3 H 2.73 . 2 837 79 TYR HD1 H 7.01 . 1 838 79 TYR HD2 H 7.01 . 1 839 79 TYR HE1 H 6.75 . 1 840 79 TYR HE2 H 6.75 . 1 841 79 TYR C C 175.69 . 1 842 79 TYR CA C 56.55 . 1 843 79 TYR CB C 41.12 . 1 844 79 TYR CD1 C 133.27 . 1 845 79 TYR CD2 C 133.27 . 1 846 79 TYR N N 118.16 . 1 847 80 TRP H H 9.04 . 1 848 80 TRP HA H 5.20 . 1 849 80 TRP HB2 H 2.94 . 1 850 80 TRP HB3 H 3.14 . 1 851 80 TRP HD1 H 7.14 . 1 852 80 TRP HE1 H 10.03 . 1 853 80 TRP HZ2 H 7.29 . 1 854 80 TRP HH2 H 6.98 . 1 855 80 TRP C C 175.08 . 1 856 80 TRP CA C 55.08 . 1 857 80 TRP CB C 31.23 . 1 858 80 TRP CD1 C 125.77 . 1 859 80 TRP CZ2 C 113.97 . 1 860 80 TRP CH2 C 124.37 . 1 861 80 TRP N N 124.85 . 1 862 80 TRP NE1 N 129.06 . 1 863 81 ILE H H 9.04 . 1 864 81 ILE HA H 5.01 . 1 865 81 ILE HB H 1.66 . 1 866 81 ILE HG12 H 1.52 . 2 867 81 ILE HG13 H 1.24 . 2 868 81 ILE HG2 H 0.80 . 1 869 81 ILE HD1 H 0.87 . 1 870 81 ILE C C 175.30 . 1 871 81 ILE CA C 60.90 . 1 872 81 ILE CB C 40.17 . 1 873 81 ILE CG1 C 28.37 . 1 874 81 ILE CG2 C 17.67 . 1 875 81 ILE CD1 C 13.87 . 1 876 81 ILE N N 130.00 . 1 877 82 ARG H H 8.88 . 1 878 82 ARG HA H 4.55 . 1 879 82 ARG HB2 H 1.72 . 2 880 82 ARG HB3 H 1.56 . 2 881 82 ARG C C 173.23 . 1 882 82 ARG CA C 54.51 . 1 883 82 ARG CB C 33.90 . 1 884 82 ARG N N 126.58 . 1 885 83 THR H H 8.36 . 1 886 83 THR HA H 5.38 . 1 887 83 THR HB H 3.96 . 1 888 83 THR HG2 H 1.28 . 1 889 83 THR C C 174.51 . 1 890 83 THR CA C 61.04 . 1 891 83 THR CB C 71.21 . 1 892 83 THR CG2 C 21.87 . 1 893 83 THR N N 114.68 . 1 894 84 PHE H H 9.32 . 1 895 84 PHE HA H 6.08 . 1 896 84 PHE HB2 H 3.08 . 1 897 84 PHE HB3 H 3.27 . 1 898 84 PHE HD1 H 6.97 . 1 899 84 PHE HD2 H 6.97 . 1 900 84 PHE HE1 H 7.42 . 1 901 84 PHE HE2 H 7.42 . 1 902 84 PHE C C 174.95 . 1 903 84 PHE CA C 52.18 . 1 904 84 PHE CB C 39.46 . 1 905 84 PHE CD1 C 128.77 . 1 906 84 PHE CD2 C 128.77 . 1 907 84 PHE CE1 C 129.27 . 1 908 84 PHE CE2 C 129.27 . 1 909 84 PHE N N 126.47 . 1 910 85 VAL H H 9.37 . 1 911 85 VAL HA H 4.92 . 1 912 85 VAL HB H 2.23 . 1 913 85 VAL HG1 H 0.95 . 1 914 85 VAL HG2 H 1.09 . 1 915 85 VAL CA C 58.67 . 1 916 85 VAL CB C 32.57 . 1 917 85 VAL CG1 C 20.37 . 1 918 85 VAL CG2 C 21.47 . 1 919 85 VAL N N 121.35 . 1 920 86 PRO HA H 4.28 . 1 921 86 PRO HB2 H 2.45 . 1 922 86 PRO HB3 H 2.03 . 1 923 86 PRO HD2 H 3.91 . 1 924 86 PRO HD3 H 3.91 . 1 925 86 PRO C C 177.46 . 1 926 86 PRO CA C 64.65 . 1 927 86 PRO CB C 32.79 . 1 928 86 PRO CD C 50.97 . 1 929 87 GLY H H 8.25 . 1 930 87 GLY HA2 H 3.46 . 1 931 87 GLY HA3 H 4.45 . 1 932 87 GLY C C 174.61 . 1 933 87 GLY CA C 43.22 . 1 934 87 GLY N N 111.48 . 1 935 88 CYS H H 9.23 . 1 936 88 CYS HA H 4.41 . 1 937 88 CYS HB2 H 3.11 . 1 938 88 CYS HB3 H 3.25 . 1 939 88 CYS C C 174.46 . 1 940 88 CYS CA C 57.43 . 1 941 88 CYS CB C 40.41 . 1 942 88 CYS N N 119.79 . 1 943 89 GLN H H 7.52 . 1 944 89 GLN HA H 4.82 . 1 945 89 GLN HB2 H 1.93 . 1 946 89 GLN HB3 H 1.65 . 1 947 89 GLN HG2 H 2.14 . 2 948 89 GLN HG3 H 1.95 . 2 949 89 GLN HE21 H 7.21 . 1 950 89 GLN HE22 H 6.67 . 1 951 89 GLN CA C 52.53 . 1 952 89 GLN CB C 30.22 . 1 953 89 GLN CG C 33.12 . 1 954 89 GLN CD C 180.23 . 1 955 89 GLN N N 116.16 . 1 956 89 GLN NE2 N 111.82 . 1 957 90 PRO HA H 4.48 . 1 958 90 PRO HB2 H 2.11 . 2 959 90 PRO HB3 H 2.62 . 2 960 90 PRO HG2 H 2.10 . 2 961 90 PRO HG3 H 1.95 . 2 962 90 PRO HD2 H 3.96 . 2 963 90 PRO HD3 H 3.64 . 2 964 90 PRO C C 177.41 . 1 965 90 PRO CA C 63.40 . 1 966 90 PRO CB C 31.84 . 1 967 90 PRO CG C 28.17 . 1 968 90 PRO CD C 50.97 . 1 969 91 GLY H H 8.33 . 1 970 91 GLY HA2 H 1.89 . 1 971 91 GLY HA3 H 3.78 . 1 972 91 GLY C C 171.11 . 1 973 91 GLY CA C 44.34 . 1 974 91 GLY N N 112.64 . 1 975 92 GLU H H 7.59 . 1 976 92 GLU HA H 5.43 . 1 977 92 GLU HB2 H 1.96 . 2 978 92 GLU HB3 H 1.92 . 2 979 92 GLU HG2 H 2.24 . 2 980 92 GLU HG3 H 2.06 . 2 981 92 GLU C C 176.87 . 1 982 92 GLU CA C 53.74 . 1 983 92 GLU CB C 33.74 . 1 984 92 GLU CG C 38.77 . 1 985 92 GLU N N 118.36 . 1 986 93 PHE H H 9.24 . 1 987 93 PHE HA H 5.33 . 1 988 93 PHE HB2 H 2.30 . 1 989 93 PHE HB3 H 3.32 . 1 990 93 PHE HD1 H 6.82 . 1 991 93 PHE HD2 H 6.82 . 1 992 93 PHE HE1 H 7.06 . 1 993 93 PHE HE2 H 7.06 . 1 994 93 PHE C C 174.56 . 1 995 93 PHE CA C 56.25 . 1 996 93 PHE CB C 43.98 . 1 997 93 PHE CD1 C 131.37 . 1 998 93 PHE CD2 C 131.37 . 1 999 93 PHE N N 120.18 . 1 1000 94 THR H H 9.30 . 1 1001 94 THR HA H 5.15 . 1 1002 94 THR HB H 4.53 . 1 1003 94 THR HG2 H 1.27 . 1 1004 94 THR C C 173.97 . 1 1005 94 THR CA C 59.51 . 1 1006 94 THR CB C 71.10 . 1 1007 94 THR CG2 C 20.27 . 1 1008 94 THR N N 112.72 . 1 1009 95 LEU H H 7.79 . 1 1010 95 LEU HA H 4.92 . 1 1011 95 LEU HB2 H 1.13 . 1 1012 95 LEU HB3 H 1.68 . 1 1013 95 LEU HG H 1.56 . 1 1014 95 LEU HD1 H 0.54 . 1 1015 95 LEU HD2 H 0.15 . 1 1016 95 LEU C C 177.61 . 1 1017 95 LEU CA C 54.47 . 1 1018 95 LEU CB C 43.98 . 1 1019 95 LEU CD1 C 23.87 . 1 1020 95 LEU CD2 C 25.87 . 1 1021 95 LEU N N 122.63 . 1 1022 96 GLY H H 9.30 . 1 1023 96 GLY HA2 H 3.63 . 1 1024 96 GLY HA3 H 4.15 . 1 1025 96 GLY C C 174.21 . 1 1026 96 GLY CA C 45.89 . 1 1027 96 GLY N N 113.57 . 1 1028 97 ASN H H 8.92 . 1 1029 97 ASN HA H 4.64 . 1 1030 97 ASN HB2 H 3.16 . 2 1031 97 ASN HB3 H 2.84 . 2 1032 97 ASN HD21 H 7.63 . 1 1033 97 ASN HD22 H 6.93 . 1 1034 97 ASN C C 176.87 . 1 1035 97 ASN CA C 53.53 . 1 1036 97 ASN CB C 37.08 . 1 1037 97 ASN CG C 178.83 . 1 1038 97 ASN N N 118.91 . 1 1039 97 ASN ND2 N 112.11 . 1 1040 98 ILE H H 7.80 . 1 1041 98 ILE HA H 3.99 . 1 1042 98 ILE HB H 2.07 . 1 1043 98 ILE HG12 H 1.63 . 2 1044 98 ILE HG13 H 1.46 . 2 1045 98 ILE HG2 H 1.08 . 1 1046 98 ILE HD1 H 0.96 . 1 1047 98 ILE C C 176.63 . 1 1048 98 ILE CA C 65.58 . 1 1049 98 ILE CB C 38.72 . 1 1050 98 ILE CG1 C 29.97 . 1 1051 98 ILE CG2 C 16.67 . 1 1052 98 ILE CD1 C 14.27 . 1 1053 98 ILE N N 119.66 . 1 1054 99 LYS H H 8.36 . 1 1055 99 LYS HA H 4.32 . 1 1056 99 LYS HB2 H 1.91 . 1 1057 99 LYS HB3 H 1.91 . 1 1058 99 LYS HG2 H 1.57 . 1 1059 99 LYS HG3 H 1.57 . 1 1060 99 LYS HD2 H 1.76 . 1 1061 99 LYS HD3 H 1.76 . 1 1062 99 LYS HE2 H 3.07 . 1 1063 99 LYS HE3 H 3.07 . 1 1064 99 LYS C C 177.76 . 1 1065 99 LYS CA C 57.90 . 1 1066 99 LYS CB C 31.36 . 1 1067 99 LYS CG C 25.47 . 1 1068 99 LYS CD C 29.17 . 1 1069 99 LYS CE C 42.27 . 1 1070 99 LYS N N 118.51 . 1 1071 100 SER H H 8.19 . 1 1072 100 SER HA H 4.27 . 1 1073 100 SER HB2 H 3.77 . 2 1074 100 SER HB3 H 3.82 . 2 1075 100 SER C C 172.83 . 1 1076 100 SER CA C 59.58 . 1 1077 100 SER CB C 63.50 . 1 1078 100 SER N N 114.39 . 1 1079 101 TYR H H 7.88 . 1 1080 101 TYR HA H 4.87 . 1 1081 101 TYR HB2 H 3.23 . 1 1082 101 TYR HB3 H 2.93 . 1 1083 101 TYR HD1 H 7.24 . 1 1084 101 TYR HD2 H 7.24 . 1 1085 101 TYR HE1 H 6.85 . 1 1086 101 TYR HE2 H 6.85 . 1 1087 101 TYR CA C 55.18 . 1 1088 101 TYR CB C 38.13 . 1 1089 101 TYR CD1 C 134.27 . 1 1090 101 TYR CD2 C 134.27 . 1 1091 101 TYR CE1 C 133.07 . 1 1092 101 TYR CE2 C 133.07 . 1 1093 101 TYR N N 123.43 . 1 1094 102 PRO HA H 4.37 . 1 1095 102 PRO HB2 H 2.33 . 1 1096 102 PRO HB3 H 1.97 . 1 1097 102 PRO HD2 H 3.91 . 2 1098 102 PRO HD3 H 3.88 . 2 1099 102 PRO C C 178.78 . 1 1100 102 PRO CA C 63.97 . 1 1101 102 PRO CB C 31.84 . 1 1102 102 PRO CD C 50.77 . 1 1103 103 GLY H H 8.96 . 1 1104 103 GLY HA2 H 4.22 . 1 1105 103 GLY HA3 H 3.87 . 1 1106 103 GLY C C 173.87 . 1 1107 103 GLY CA C 45.86 . 1 1108 103 GLY N N 112.19 . 1 1109 104 LEU H H 7.92 . 1 1110 104 LEU HA H 4.96 . 1 1111 104 LEU HB2 H 1.73 . 1 1112 104 LEU HB3 H 2.08 . 1 1113 104 LEU HG H 1.69 . 1 1114 104 LEU HD1 H 0.93 . 1 1115 104 LEU HD2 H 1.09 . 1 1116 104 LEU C C 176.92 . 1 1117 104 LEU CA C 55.15 . 1 1118 104 LEU CB C 43.27 . 1 1119 104 LEU CD1 C 26.47 . 1 1120 104 LEU CD2 C 25.47 . 1 1121 104 LEU N N 123.52 . 1 1122 105 THR H H 8.96 . 1 1123 105 THR HA H 4.55 . 1 1124 105 THR HB H 4.19 . 1 1125 105 THR HG2 H 1.27 . 1 1126 105 THR C C 175.10 . 1 1127 105 THR CA C 63.12 . 1 1128 105 THR CB C 69.70 . 1 1129 105 THR CG2 C 20.27 . 1 1130 105 THR N N 116.83 . 1 1131 106 SER H H 7.75 . 1 1132 106 SER HA H 4.68 . 1 1133 106 SER HB2 H 3.94 . 2 1134 106 SER HB3 H 3.80 . 2 1135 106 SER C C 172.59 . 1 1136 106 SER CA C 58.05 . 1 1137 106 SER CB C 64.63 . 1 1138 106 SER N N 113.26 . 1 1139 107 TYR H H 8.85 . 1 1140 107 TYR HA H 5.15 . 1 1141 107 TYR HB2 H 2.83 . 1 1142 107 TYR HB3 H 3.10 . 1 1143 107 TYR HD1 H 6.83 . 1 1144 107 TYR HD2 H 6.83 . 1 1145 107 TYR HE1 H 6.68 . 1 1146 107 TYR HE2 H 6.68 . 1 1147 107 TYR C C 172.98 . 1 1148 107 TYR CA C 58.82 . 1 1149 107 TYR CB C 42.69 . 1 1150 107 TYR CD1 C 133.07 . 1 1151 107 TYR CD2 C 133.07 . 1 1152 107 TYR N N 124.63 . 1 1153 108 LEU H H 9.08 . 1 1154 108 LEU HA H 5.10 . 1 1155 108 LEU HB2 H 1.66 . 2 1156 108 LEU HB3 H 1.68 . 2 1157 108 LEU HG H 1.60 . 1 1158 108 LEU HD1 H 0.93 . 2 1159 108 LEU HD2 H 0.99 . 2 1160 108 LEU C C 173.18 . 1 1161 108 LEU CA C 54.33 . 1 1162 108 LEU CB C 46.49 . 1 1163 108 LEU CD1 C 26.17 . 2 1164 108 LEU CD2 C 24.27 . 2 1165 108 LEU N N 132.28 . 1 1166 109 VAL H H 8.69 . 1 1167 109 VAL HA H 4.59 . 1 1168 109 VAL HB H 1.62 . 1 1169 109 VAL HG1 H 0.32 . 1 1170 109 VAL HG2 H 0.28 . 1 1171 109 VAL C C 175.49 . 1 1172 109 VAL CA C 60.17 . 1 1173 109 VAL CB C 35.06 . 1 1174 109 VAL CG1 C 20.17 . 1 1175 109 VAL CG2 C 20.07 . 1 1176 109 VAL N N 124.81 . 1 1177 110 ARG H H 9.50 . 1 1178 110 ARG HA H 4.92 . 1 1179 110 ARG HB2 H 1.68 . 1 1180 110 ARG HB3 H 1.58 . 1 1181 110 ARG HG2 H 1.57 . 1 1182 110 ARG HG3 H 1.57 . 1 1183 110 ARG HD2 H 2.89 . 1 1184 110 ARG HD3 H 2.89 . 1 1185 110 ARG HE H 7.51 . 1 1186 110 ARG C C 174.42 . 1 1187 110 ARG CA C 55.14 . 1 1188 110 ARG CB C 35.32 . 1 1189 110 ARG CD C 42.17 . 1 1190 110 ARG N N 125.96 . 1 1191 110 ARG NE N 127.06 . 1 1192 111 VAL H H 8.62 . 1 1193 111 VAL HA H 3.67 . 1 1194 111 VAL HB H 1.55 . 1 1195 111 VAL HG1 H 0.54 . 1 1196 111 VAL HG2 H 0.24 . 1 1197 111 VAL C C 173.47 . 1 1198 111 VAL CA C 64.37 . 1 1199 111 VAL CB C 30.41 . 1 1200 111 VAL CG1 C 20.37 . 1 1201 111 VAL CG2 C 19.57 . 1 1202 111 VAL N N 127.36 . 1 1203 112 VAL H H 8.21 . 1 1204 112 VAL HA H 4.15 . 1 1205 112 VAL HB H 1.57 . 1 1206 112 VAL HG1 H 0.44 . 1 1207 112 VAL HG2 H 1.01 . 1 1208 112 VAL C C 175.74 . 1 1209 112 VAL CA C 63.40 . 1 1210 112 VAL CB C 33.03 . 1 1211 112 VAL CG1 C 20.67 . 1 1212 112 VAL CG2 C 21.87 . 1 1213 112 VAL N N 132.62 . 1 1214 113 SER H H 7.18 . 1 1215 113 SER HA H 5.10 . 1 1216 113 SER HB2 H 3.76 . 1 1217 113 SER HB3 H 3.45 . 1 1218 113 SER C C 174.21 . 1 1219 113 SER CA C 55.94 . 1 1220 113 SER CB C 64.69 . 1 1221 113 SER N N 106.54 . 1 1222 114 THR H H 8.47 . 1 1223 114 THR HA H 4.73 . 1 1224 114 THR HB H 4.37 . 1 1225 114 THR HG2 H 0.44 . 1 1226 114 THR C C 170.18 . 1 1227 114 THR CA C 60.70 . 1 1228 114 THR CB C 69.12 . 1 1229 114 THR CG2 C 17.47 . 1 1230 114 THR N N 118.20 . 1 1231 115 ASN H H 7.07 . 1 1232 115 ASN HA H 4.82 . 1 1233 115 ASN HB2 H 2.78 . 2 1234 115 ASN HB3 H 3.52 . 2 1235 115 ASN HD21 H 7.81 . 1 1236 115 ASN HD22 H 6.97 . 1 1237 115 ASN C C 178.40 . 1 1238 115 ASN CA C 51.51 . 1 1239 115 ASN CB C 38.74 . 1 1240 115 ASN N N 121.37 . 1 1241 115 ASN ND2 N 110.24 . 1 1242 116 TYR H H 9.11 . 1 1243 116 TYR HA H 3.94 . 1 1244 116 TYR HB2 H 3.65 . 2 1245 116 TYR HB3 H 3.07 . 2 1246 116 TYR HD1 H 6.40 . 1 1247 116 TYR HD2 H 6.40 . 1 1248 116 TYR HE1 H 6.71 . 1 1249 116 TYR HE2 H 6.71 . 1 1250 116 TYR C C 176.48 . 1 1251 116 TYR CA C 65.97 . 1 1252 116 TYR CB C 36.60 . 1 1253 116 TYR CD1 C 122.27 . 1 1254 116 TYR CD2 C 122.27 . 1 1255 116 TYR N N 115.38 . 1 1256 117 ASN H H 9.47 . 1 1257 117 ASN HA H 4.78 . 1 1258 117 ASN HB2 H 3.05 . 1 1259 117 ASN HB3 H 2.88 . 1 1260 117 ASN HD21 H 7.64 . 1 1261 117 ASN HD22 H 6.74 . 1 1262 117 ASN C C 175.99 . 1 1263 117 ASN CA C 52.74 . 1 1264 117 ASN CB C 38.98 . 1 1265 117 ASN CG C 176.82 . 1 1266 117 ASN N N 118.21 . 1 1267 117 ASN ND2 N 110.64 . 1 1268 118 GLN H H 7.76 . 1 1269 118 GLN HA H 4.73 . 1 1270 118 GLN HB2 H 2.57 . 1 1271 118 GLN HB3 H 2.25 . 1 1272 118 GLN HG2 H 2.65 . 1 1273 118 GLN HG3 H 2.65 . 1 1274 118 GLN HE21 H 7.85 . 1 1275 118 GLN HE22 H 7.06 . 1 1276 118 GLN C C 174.61 . 1 1277 118 GLN CA C 58.86 . 1 1278 118 GLN CB C 32.41 . 1 1279 118 GLN CG C 33.47 . 1 1280 118 GLN CD C 180.75 . 1 1281 118 GLN N N 117.65 . 1 1282 118 GLN NE2 N 112.37 . 1 1283 119 HIS H H 8.76 . 1 1284 119 HIS HA H 6.40 . 1 1285 119 HIS HB2 H 3.26 . 1 1286 119 HIS HB3 H 3.07 . 1 1287 119 HIS C C 175.15 . 1 1288 119 HIS CA C 55.22 . 1 1289 119 HIS CB C 37.08 . 1 1290 119 HIS N N 116.32 . 1 1291 120 ALA H H 8.94 . 1 1292 120 ALA HA H 5.09 . 1 1293 120 ALA HB H 0.92 . 1 1294 120 ALA C C 174.95 . 1 1295 120 ALA CA C 51.49 . 1 1296 120 ALA CB C 23.03 . 1 1297 120 ALA N N 121.44 . 1 1298 121 MET H H 9.17 . 1 1299 121 MET HA H 5.71 . 1 1300 121 MET HB2 H 1.99 . 1 1301 121 MET HB3 H 1.81 . 1 1302 121 MET HG2 H 2.67 . 2 1303 121 MET HG3 H 2.36 . 2 1304 121 MET HE H 1.70 . 1 1305 121 MET C C 175.05 . 1 1306 121 MET CA C 55.28 . 1 1307 121 MET CB C 36.60 . 1 1308 121 MET CG C 32.37 . 1 1309 121 MET CE C 16.07 . 1 1310 121 MET N N 119.94 . 1 1311 122 VAL H H 8.60 . 1 1312 122 VAL HA H 4.41 . 1 1313 122 VAL HB H 1.80 . 1 1314 122 VAL HG1 H 0.26 . 1 1315 122 VAL HG2 H 0.63 . 1 1316 122 VAL C C 171.80 . 1 1317 122 VAL CA C 61.73 . 1 1318 122 VAL CB C 34.46 . 1 1319 122 VAL CG1 C 23.57 . 1 1320 122 VAL CG2 C 22.77 . 1 1321 122 VAL N N 124.32 . 1 1322 123 PHE H H 9.09 . 1 1323 123 PHE HA H 5.43 . 1 1324 123 PHE HB2 H 2.82 . 1 1325 123 PHE HB3 H 3.02 . 1 1326 123 PHE HD1 H 7.01 . 1 1327 123 PHE HD2 H 7.01 . 1 1328 123 PHE HE1 H 6.14 . 1 1329 123 PHE HE2 H 6.14 . 1 1330 123 PHE C C 172.05 . 1 1331 123 PHE CA C 56.47 . 1 1332 123 PHE CB C 43.34 . 1 1333 123 PHE CD1 C 131.67 . 1 1334 123 PHE CD2 C 131.67 . 1 1335 123 PHE CE1 C 130.27 . 1 1336 123 PHE CE2 C 130.27 . 1 1337 123 PHE N N 127.76 . 1 1338 124 PHE H H 9.00 . 1 1339 124 PHE HA H 5.24 . 1 1340 124 PHE HB2 H 2.74 . 1 1341 124 PHE HB3 H 2.57 . 1 1342 124 PHE HD1 H 7.16 . 1 1343 124 PHE HD2 H 7.16 . 1 1344 124 PHE HE1 H 7.10 . 1 1345 124 PHE HE2 H 7.10 . 1 1346 124 PHE C C 174.80 . 1 1347 124 PHE CA C 55.40 . 1 1348 124 PHE CB C 42.31 . 1 1349 124 PHE CD1 C 132.87 . 1 1350 124 PHE CD2 C 132.87 . 1 1351 124 PHE N N 124.85 . 1 1352 125 LYS H H 8.98 . 1 1353 125 LYS HA H 5.10 . 1 1354 125 LYS HB2 H 1.68 . 1 1355 125 LYS HB3 H 1.68 . 1 1356 125 LYS HG2 H 1.59 . 1 1357 125 LYS HG3 H 1.59 . 1 1358 125 LYS HD2 H 1.41 . 1 1359 125 LYS HD3 H 1.41 . 1 1360 125 LYS HE2 H 2.67 . 1 1361 125 LYS HE3 H 2.67 . 1 1362 125 LYS C C 173.97 . 1 1363 125 LYS CA C 55.03 . 1 1364 125 LYS CB C 36.36 . 1 1365 125 LYS N N 120.82 . 1 1366 126 LYS H H 9.38 . 1 1367 126 LYS HA H 5.14 . 1 1368 126 LYS HB2 H 1.99 . 2 1369 126 LYS HB3 H 1.71 . 2 1370 126 LYS HG2 H 1.47 . 1 1371 126 LYS HG3 H 1.47 . 1 1372 126 LYS C C 173.57 . 1 1373 126 LYS CA C 54.26 . 1 1374 126 LYS CB C 36.84 . 1 1375 126 LYS N N 127.58 . 1 1376 127 VAL H H 8.31 . 1 1377 127 VAL HA H 5.15 . 1 1378 127 VAL HB H 2.08 . 1 1379 127 VAL HG1 H 0.90 . 1 1380 127 VAL HG2 H 0.85 . 1 1381 127 VAL C C 175.54 . 1 1382 127 VAL CA C 61.56 . 1 1383 127 VAL CB C 32.55 . 1 1384 127 VAL CG1 C 21.27 . 1 1385 127 VAL CG2 C 20.97 . 1 1386 127 VAL N N 124.30 . 1 1387 128 SER H H 8.93 . 1 1388 128 SER HA H 5.38 . 1 1389 128 SER HB2 H 3.86 . 2 1390 128 SER HB3 H 3.75 . 2 1391 128 SER C C 175.35 . 1 1392 128 SER CA C 55.99 . 1 1393 128 SER CB C 64.93 . 1 1394 128 SER N N 120.22 . 1 1395 129 GLN H H 9.36 . 1 1396 129 GLN HA H 4.04 . 1 1397 129 GLN HB2 H 2.28 . 1 1398 129 GLN HB3 H 2.28 . 1 1399 129 GLN HG2 H 2.41 . 1 1400 129 GLN HG3 H 2.41 . 1 1401 129 GLN HE21 H 7.96 . 1 1402 129 GLN HE22 H 6.69 . 1 1403 129 GLN C C 175.39 . 1 1404 129 GLN CA C 57.28 . 1 1405 129 GLN CB C 26.36 . 1 1406 129 GLN CG C 34.07 . 1 1407 129 GLN CD C 178.78 . 1 1408 129 GLN N N 126.03 . 1 1409 129 GLN NE2 N 112.30 . 1 1410 130 ASN H H 8.85 . 1 1411 130 ASN HA H 4.13 . 1 1412 130 ASN HB2 H 3.09 . 1 1413 130 ASN HB3 H 2.97 . 1 1414 130 ASN HD21 H 7.56 . 1 1415 130 ASN HD22 H 6.90 . 1 1416 130 ASN C C 174.02 . 1 1417 130 ASN CA C 54.79 . 1 1418 130 ASN CB C 38.03 . 1 1419 130 ASN CG C 178.78 . 1 1420 130 ASN N N 109.33 . 1 1421 130 ASN ND2 N 113.07 . 1 1422 131 ARG H H 7.92 . 1 1423 131 ARG HA H 4.55 . 1 1424 131 ARG HB2 H 1.86 . 2 1425 131 ARG HB3 H 1.32 . 2 1426 131 ARG HG2 H 1.89 . 2 1427 131 ARG HG3 H 1.54 . 2 1428 131 ARG HD2 H 3.19 . 1 1429 131 ARG HD3 H 3.19 . 1 1430 131 ARG C C 173.67 . 1 1431 131 ARG CA C 54.94 . 1 1432 131 ARG CB C 32.79 . 1 1433 131 ARG N N 119.84 . 1 1434 132 GLU H H 8.19 . 1 1435 132 GLU HA H 4.92 . 1 1436 132 GLU HB2 H 2.01 . 2 1437 132 GLU HB3 H 1.82 . 2 1438 132 GLU HG2 H 2.02 . 1 1439 132 GLU HG3 H 2.02 . 1 1440 132 GLU C C 175.05 . 1 1441 132 GLU CA C 55.08 . 1 1442 132 GLU CB C 31.40 . 1 1443 132 GLU N N 120.02 . 1 1444 133 TYR H H 9.35 . 1 1445 133 TYR HA H 5.29 . 1 1446 133 TYR HB2 H 3.10 . 1 1447 133 TYR HB3 H 2.78 . 1 1448 133 TYR HD1 H 7.02 . 1 1449 133 TYR HD2 H 7.02 . 1 1450 133 TYR HE1 H 6.77 . 1 1451 133 TYR HE2 H 6.77 . 1 1452 133 TYR C C 175.39 . 1 1453 133 TYR CA C 56.70 . 1 1454 133 TYR CB C 41.12 . 1 1455 133 TYR CD1 C 128.37 . 1 1456 133 TYR CD2 C 128.37 . 1 1457 133 TYR N N 124.32 . 1 1458 134 PHE H H 8.90 . 1 1459 134 PHE HA H 5.80 . 1 1460 134 PHE HB2 H 3.07 . 1 1461 134 PHE HB3 H 2.78 . 1 1462 134 PHE HD1 H 7.42 . 1 1463 134 PHE HD2 H 7.42 . 1 1464 134 PHE HE1 H 7.01 . 1 1465 134 PHE HE2 H 7.01 . 1 1466 134 PHE C C 173.18 . 1 1467 134 PHE CA C 55.78 . 1 1468 134 PHE CB C 42.42 . 1 1469 134 PHE CD1 C 131.87 . 1 1470 134 PHE CD2 C 131.87 . 1 1471 134 PHE CE1 C 133.07 . 1 1472 134 PHE CE2 C 133.07 . 1 1473 134 PHE N N 117.62 . 1 1474 135 LYS H H 9.27 . 1 1475 135 LYS HA H 5.43 . 1 1476 135 LYS HB2 H 1.73 . 2 1477 135 LYS HB3 H 1.67 . 2 1478 135 LYS HG2 H 1.42 . 2 1479 135 LYS HG3 H 1.30 . 2 1480 135 LYS HD2 H 2.23 . 2 1481 135 LYS HD3 H 2.05 . 2 1482 135 LYS HE2 H 3.03 . 1 1483 135 LYS HE3 H 3.03 . 1 1484 135 LYS C C 173.23 . 1 1485 135 LYS CA C 54.37 . 1 1486 135 LYS CB C 37.34 . 1 1487 135 LYS CG C 25.67 . 1 1488 135 LYS CD C 38.77 . 1 1489 135 LYS CE C 42.07 . 1 1490 135 LYS N N 122.75 . 1 1491 136 ILE H H 9.88 . 1 1492 136 ILE HA H 5.66 . 1 1493 136 ILE HB H 2.07 . 1 1494 136 ILE HG12 H 1.88 . 2 1495 136 ILE HG13 H 1.46 . 2 1496 136 ILE HG2 H 1.35 . 1 1497 136 ILE HD1 H 1.12 . 1 1498 136 ILE C C 175.94 . 1 1499 136 ILE CA C 59.67 . 1 1500 136 ILE CB C 41.50 . 1 1501 136 ILE CG1 C 30.07 . 1 1502 136 ILE CG2 C 21.27 . 1 1503 136 ILE CD1 C 17.37 . 1 1504 136 ILE N N 122.33 . 1 1505 137 THR H H 9.61 . 1 1506 137 THR HA H 5.01 . 1 1507 137 THR HB H 3.82 . 1 1508 137 THR HG2 H 1.06 . 1 1509 137 THR C C 172.83 . 1 1510 137 THR CA C 59.77 . 1 1511 137 THR CB C 71.11 . 1 1512 137 THR CG2 C 22.47 . 1 1513 137 THR N N 117.38 . 1 1514 138 LEU H H 8.50 . 1 1515 138 LEU HA H 4.82 . 1 1516 138 LEU HB2 H 0.93 . 1 1517 138 LEU HB3 H -0.03 . 1 1518 138 LEU HG H 1.21 . 1 1519 138 LEU HD2 H 0.59 . 2 1520 138 LEU C C 174.80 . 1 1521 138 LEU CA C 52.97 . 1 1522 138 LEU CB C 41.12 . 1 1523 138 LEU CG C 27.03 . 1 1524 138 LEU CD2 C 26.07 . 2 1525 138 LEU N N 126.69 . 1 1526 139 TYR H H 9.61 . 1 1527 139 TYR HA H 6.12 . 1 1528 139 TYR HB2 H 3.29 . 1 1529 139 TYR HB3 H 2.39 . 1 1530 139 TYR HD1 H 6.29 . 1 1531 139 TYR HD2 H 6.29 . 1 1532 139 TYR HE1 H 6.13 . 1 1533 139 TYR HE2 H 6.13 . 1 1534 139 TYR C C 176.76 . 1 1535 139 TYR CA C 52.48 . 1 1536 139 TYR CB C 41.36 . 1 1537 139 TYR CD1 C 132.07 . 1 1538 139 TYR CD2 C 132.07 . 1 1539 139 TYR CE1 C 129.97 . 1 1540 139 TYR CE2 C 129.97 . 1 1541 139 TYR N N 126.98 . 1 1542 140 GLY H H 9.95 . 1 1543 140 GLY HA2 H 6.13 . 1 1544 140 GLY HA3 H 4.21 . 1 1545 140 GLY C C 175.54 . 1 1546 140 GLY CA C 44.19 . 1 1547 140 GLY N N 105.52 . 1 1548 141 ARG H H 8.92 . 1 1549 141 ARG HA H 4.27 . 1 1550 141 ARG HB2 H 2.00 . 1 1551 141 ARG HB3 H 2.00 . 1 1552 141 ARG HG2 H 1.55 . 1 1553 141 ARG HG3 H 1.55 . 1 1554 141 ARG HD2 H 2.91 . 1 1555 141 ARG HD3 H 2.91 . 1 1556 141 ARG HE H 5.31 . 1 1557 141 ARG HH11 H 5.82 . 1 1558 141 ARG HH12 H 5.82 . 1 1559 141 ARG HH21 H 4.59 . 1 1560 141 ARG HH22 H 4.59 . 1 1561 141 ARG C C 177.17 . 1 1562 141 ARG CA C 55.87 . 1 1563 141 ARG CB C 30.49 . 1 1564 141 ARG CG C 29.17 . 1 1565 141 ARG CD C 42.17 . 1 1566 141 ARG N N 120.82 . 1 1567 141 ARG NE N 85.00 . 1 1568 142 THR H H 7.98 . 1 1569 142 THR HA H 4.59 . 1 1570 142 THR HB H 4.61 . 1 1571 142 THR HG2 H 1.27 . 1 1572 142 THR C C 172.49 . 1 1573 142 THR CA C 59.18 . 1 1574 142 THR CB C 70.88 . 1 1575 142 THR CG2 C 21.67 . 1 1576 142 THR N N 108.95 . 1 1577 143 LYS H H 7.82 . 1 1578 143 LYS HA H 3.53 . 1 1579 143 LYS HB2 H 1.52 . 1 1580 143 LYS HB3 H 1.40 . 1 1581 143 LYS HG2 H 0.44 . 1 1582 143 LYS HG3 H 0.44 . 1 1583 143 LYS HD2 H 0.93 . 1 1584 143 LYS HD3 H 0.93 . 1 1585 143 LYS HE2 H 2.73 . 2 1586 143 LYS HE3 H 2.69 . 2 1587 143 LYS C C 175.15 . 1 1588 143 LYS CA C 57.83 . 1 1589 143 LYS CB C 32.79 . 1 1590 143 LYS CG C 24.83 . 1 1591 143 LYS CE C 42.09 . 1 1592 143 LYS N N 114.19 . 1 1593 144 GLU H H 7.36 . 1 1594 144 GLU HA H 4.50 . 1 1595 144 GLU HB2 H 1.93 . 2 1596 144 GLU HB3 H 1.83 . 2 1597 144 GLU HG2 H 2.11 . 1 1598 144 GLU HG3 H 2.11 . 1 1599 144 GLU C C 175.69 . 1 1600 144 GLU CA C 54.95 . 1 1601 144 GLU CB C 32.32 . 1 1602 144 GLU CG C 36.17 . 1 1603 144 GLU N N 113.88 . 1 1604 145 LEU H H 8.47 . 1 1605 145 LEU HA H 4.87 . 1 1606 145 LEU HB2 H 1.47 . 2 1607 145 LEU HB3 H 1.64 . 2 1608 145 LEU HG H 1.18 . 1 1609 145 LEU HD1 H 0.92 . 2 1610 145 LEU HD2 H 0.97 . 2 1611 145 LEU C C 175.84 . 1 1612 145 LEU CA C 52.97 . 1 1613 145 LEU CB C 46.12 . 1 1614 145 LEU CG C 23.87 . 1 1615 145 LEU CD1 C 24.07 . 1 1616 145 LEU CD2 C 24.07 . 1 1617 145 LEU N N 122.04 . 1 1618 146 THR H H 7.08 . 1 1619 146 THR HA H 4.41 . 1 1620 146 THR HB H 4.73 . 1 1621 146 THR HG2 H 1.36 . 1 1622 146 THR C C 175.49 . 1 1623 146 THR CA C 60.51 . 1 1624 146 THR CB C 70.64 . 1 1625 146 THR CG2 C 22.47 . 1 1626 146 THR N N 109.89 . 1 1627 147 SER H H 9.00 . 1 1628 147 SER HA H 3.99 . 1 1629 147 SER HB2 H 3.93 . 1 1630 147 SER HB3 H 3.93 . 1 1631 147 SER C C 176.68 . 1 1632 147 SER CA C 61.77 . 1 1633 147 SER CB C 62.37 . 1 1634 147 SER N N 117.20 . 1 1635 148 GLU H H 8.80 . 1 1636 148 GLU HA H 4.04 . 1 1637 148 GLU HB2 H 2.10 . 2 1638 148 GLU HB3 H 1.91 . 2 1639 148 GLU HG2 H 2.29 . 1 1640 148 GLU HG3 H 2.29 . 1 1641 148 GLU C C 178.93 . 1 1642 148 GLU CA C 59.97 . 1 1643 148 GLU CB C 29.22 . 1 1644 148 GLU CG C 36.57 . 1 1645 148 GLU N N 121.06 . 1 1646 149 LEU H H 7.40 . 1 1647 149 LEU HA H 4.04 . 1 1648 149 LEU HB2 H 1.24 . 1 1649 149 LEU HB3 H 1.84 . 1 1650 149 LEU HG H 1.53 . 1 1651 149 LEU HD1 H 0.38 . 1 1652 149 LEU HD2 H 0.79 . 1 1653 149 LEU C C 180.12 . 1 1654 149 LEU CA C 57.28 . 1 1655 149 LEU CB C 42.18 . 1 1656 149 LEU CG C 27.37 . 1 1657 149 LEU CD1 C 22.57 . 1 1658 149 LEU CD2 C 25.77 . 1 1659 149 LEU N N 120.20 . 1 1660 150 LYS H H 7.84 . 1 1661 150 LYS HA H 3.99 . 1 1662 150 LYS HB2 H 1.80 . 1 1663 150 LYS HB3 H 1.80 . 1 1664 150 LYS HG2 H 1.03 . 1 1665 150 LYS HG3 H 1.03 . 1 1666 150 LYS HD2 H 1.44 . 1 1667 150 LYS HD3 H 1.44 . 1 1668 150 LYS HE2 H 2.93 . 1 1669 150 LYS HE3 H 2.93 . 1 1670 150 LYS C C 178.55 . 1 1671 150 LYS CA C 61.19 . 1 1672 150 LYS CB C 31.84 . 1 1673 150 LYS N N 119.80 . 1 1674 151 GLU H H 8.74 . 1 1675 151 GLU HA H 4.13 . 1 1676 151 GLU HB2 H 2.11 . 1 1677 151 GLU HB3 H 2.11 . 1 1678 151 GLU HG2 H 2.39 . 1 1679 151 GLU HG3 H 2.39 . 1 1680 151 GLU C C 179.73 . 1 1681 151 GLU CA C 59.45 . 1 1682 151 GLU CB C 28.98 . 1 1683 151 GLU CG C 36.47 . 1 1684 151 GLU N N 118.73 . 1 1685 152 ASN H H 8.24 . 1 1686 152 ASN HA H 4.50 . 1 1687 152 ASN HB2 H 2.97 . 2 1688 152 ASN HB3 H 2.87 . 2 1689 152 ASN HD21 H 7.58 . 1 1690 152 ASN HD22 H 7.03 . 1 1691 152 ASN C C 177.81 . 1 1692 152 ASN CA C 56.49 . 1 1693 152 ASN CB C 38.27 . 1 1694 152 ASN CG C 178.78 . 1 1695 152 ASN N N 119.11 . 1 1696 152 ASN ND2 N 112.56 . 1 1697 153 PHE H H 8.10 . 1 1698 153 PHE HA H 4.73 . 1 1699 153 PHE HB2 H 3.57 . 2 1700 153 PHE HB3 H 3.47 . 2 1701 153 PHE HD1 H 7.36 . 1 1702 153 PHE HD2 H 7.36 . 1 1703 153 PHE HE1 H 6.83 . 1 1704 153 PHE HE2 H 6.83 . 1 1705 153 PHE C C 178.30 . 1 1706 153 PHE CA C 60.81 . 1 1707 153 PHE CB C 40.17 . 1 1708 153 PHE CD1 C 130.17 . 1 1709 153 PHE CD2 C 130.17 . 1 1710 153 PHE N N 122.21 . 1 1711 154 ILE H H 8.74 . 1 1712 154 ILE HA H 3.39 . 1 1713 154 ILE HB H 2.09 . 1 1714 154 ILE HG12 H 2.31 . 2 1715 154 ILE HG13 H 1.17 . 2 1716 154 ILE HG2 H 0.97 . 1 1717 154 ILE HD1 H 0.64 . 1 1718 154 ILE C C 177.46 . 1 1719 154 ILE CA C 66.58 . 1 1720 154 ILE CB C 38.27 . 1 1721 154 ILE CG1 C 29.87 . 1 1722 154 ILE CG2 C 17.17 . 1 1723 154 ILE CD1 C 17.77 . 1 1724 154 ILE N N 124.90 . 1 1725 155 ARG H H 8.47 . 1 1726 155 ARG HA H 3.90 . 1 1727 155 ARG HB2 H 2.05 . 2 1728 155 ARG HB3 H 2.00 . 2 1729 155 ARG HG2 H 1.92 . 2 1730 155 ARG HG3 H 1.66 . 2 1731 155 ARG HD2 H 3.34 . 2 1732 155 ARG HD3 H 3.30 . 2 1733 155 ARG HE H 7.51 . 1 1734 155 ARG C C 179.97 . 1 1735 155 ARG CA C 60.17 . 1 1736 155 ARG CB C 30.17 . 1 1737 155 ARG CG C 28.07 . 1 1738 155 ARG CD C 43.67 . 1 1739 155 ARG N N 118.93 . 1 1740 155 ARG NE N 83.99 . 1 1741 156 PHE H H 8.63 . 1 1742 156 PHE HA H 4.41 . 1 1743 156 PHE HB2 H 2.97 . 1 1744 156 PHE HB3 H 3.45 . 1 1745 156 PHE HD1 H 7.33 . 1 1746 156 PHE HD2 H 7.33 . 1 1747 156 PHE HE1 H 7.28 . 1 1748 156 PHE HE2 H 7.28 . 1 1749 156 PHE C C 178.94 . 1 1750 156 PHE CA C 60.62 . 1 1751 156 PHE CB C 39.22 . 1 1752 156 PHE CD1 C 131.87 . 1 1753 156 PHE CD2 C 131.87 . 1 1754 156 PHE N N 120.75 . 1 1755 157 SER H H 8.47 . 1 1756 157 SER HA H 3.59 . 1 1757 157 SER HB2 H 3.79 . 2 1758 157 SER HB3 H 3.23 . 2 1759 157 SER C C 176.63 . 1 1760 157 SER CA C 64.13 . 1 1761 157 SER CB C 62.31 . 1 1762 157 SER N N 118.29 . 1 1763 158 LYS H H 8.56 . 1 1764 158 LYS HA H 4.47 . 1 1765 158 LYS HB2 H 1.82 . 1 1766 158 LYS HB3 H 1.82 . 1 1767 158 LYS HG2 H 1.46 . 1 1768 158 LYS HG3 H 1.46 . 1 1769 158 LYS HD2 H 1.66 . 1 1770 158 LYS HD3 H 1.66 . 1 1771 158 LYS HE2 H 2.91 . 2 1772 158 LYS HE3 H 2.81 . 2 1773 158 LYS C C 181.45 . 1 1774 158 LYS CA C 59.38 . 1 1775 158 LYS CB C 32.18 . 1 1776 158 LYS CD C 30.07 . 1 1777 158 LYS CE C 42.07 . 1 1778 158 LYS N N 121.30 . 1 1779 159 SER H H 8.11 . 1 1780 159 SER HA H 4.32 . 1 1781 159 SER HB2 H 4.06 . 2 1782 159 SER HB3 H 4.00 . 2 1783 159 SER C C 174.90 . 1 1784 159 SER CA C 61.31 . 1 1785 159 SER CB C 62.31 . 1 1786 159 SER N N 119.18 . 1 1787 160 LEU H H 7.03 . 1 1788 160 LEU HA H 4.18 . 1 1789 160 LEU HB2 H 1.74 . 1 1790 160 LEU HB3 H 1.55 . 1 1791 160 LEU HG H 1.30 . 1 1792 160 LEU HD1 H 0.58 . 1 1793 160 LEU HD2 H 0.37 . 1 1794 160 LEU C C 175.79 . 1 1795 160 LEU CA C 54.08 . 1 1796 160 LEU CB C 40.41 . 1 1797 160 LEU CG C 25.67 . 1 1798 160 LEU CD1 C 26.47 . 1 1799 160 LEU CD2 C 21.67 . 1 1800 160 LEU N N 120.26 . 1 1801 161 GLY H H 7.76 . 1 1802 161 GLY HA2 H 4.23 . 1 1803 161 GLY HA3 H 3.65 . 1 1804 161 GLY C C 174.21 . 1 1805 161 GLY CA C 44.61 . 1 1806 161 GLY N N 104.59 . 1 1807 162 LEU H H 7.24 . 1 1808 162 LEU HA H 4.55 . 1 1809 162 LEU HB2 H 1.51 . 1 1810 162 LEU HB3 H 0.99 . 1 1811 162 LEU HG H 1.54 . 1 1812 162 LEU HD1 H 0.69 . 1 1813 162 LEU HD2 H 0.47 . 1 1814 162 LEU CA C 51.93 . 1 1815 162 LEU CB C 41.65 . 1 1816 162 LEU CG C 26.27 . 1 1817 162 LEU CD1 C 25.97 . 1 1818 162 LEU CD2 C 22.47 . 1 1819 162 LEU N N 118.51 . 1 1820 163 PRO HA H 4.71 . 1 1821 163 PRO HB2 H 2.28 . 2 1822 163 PRO HB3 H 2.44 . 2 1823 163 PRO HG2 H 2.06 . 1 1824 163 PRO HG3 H 2.06 . 1 1825 163 PRO HD2 H 4.07 . 2 1826 163 PRO HD3 H 3.10 . 2 1827 163 PRO C C 177.46 . 1 1828 163 PRO CA C 61.06 . 1 1829 163 PRO CB C 32.55 . 1 1830 163 PRO CG C 27.37 . 1 1831 163 PRO CD C 50.67 . 1 1832 164 GLU H H 8.91 . 1 1833 164 GLU HA H 3.85 . 1 1834 164 GLU HB2 H 2.13 . 1 1835 164 GLU HB3 H 2.13 . 1 1836 164 GLU HG2 H 2.38 . 1 1837 164 GLU HG3 H 2.38 . 1 1838 164 GLU C C 176.93 . 1 1839 164 GLU CA C 60.11 . 1 1840 164 GLU CB C 29.46 . 1 1841 164 GLU CG C 37.32 . 1 1842 164 GLU N N 117.63 . 1 1843 165 ASN H H 8.32 . 1 1844 165 ASN HA H 4.55 . 1 1845 165 ASN HB2 H 3.24 . 1 1846 165 ASN HB3 H 2.85 . 1 1847 165 ASN HD21 H 7.71 . 1 1848 165 ASN HD22 H 6.87 . 1 1849 165 ASN C C 174.64 . 1 1850 165 ASN CA C 54.30 . 1 1851 165 ASN CB C 36.12 . 1 1852 165 ASN CG C 178.78 . 1 1853 165 ASN N N 112.54 . 1 1854 165 ASN ND2 N 112.52 . 1 1855 166 HIS H H 8.23 . 1 1856 166 HIS HA H 5.20 . 1 1857 166 HIS HB2 H 1.72 . 2 1858 166 HIS HB3 H 1.63 . 2 1859 166 HIS C C 171.70 . 1 1860 166 HIS CA C 55.58 . 1 1861 166 HIS CB C 28.75 . 1 1862 166 HIS N N 118.04 . 1 1863 167 ILE H H 7.20 . 1 1864 167 ILE HA H 4.45 . 1 1865 167 ILE HB H 1.87 . 1 1866 167 ILE HG12 H 1.87 . 2 1867 167 ILE HG13 H 1.62 . 2 1868 167 ILE HG2 H 0.63 . 1 1869 167 ILE HD1 H 0.74 . 1 1870 167 ILE C C 174.71 . 1 1871 167 ILE CA C 61.48 . 1 1872 167 ILE CB C 39.93 . 1 1873 167 ILE CG1 C 30.47 . 1 1874 167 ILE CG2 C 18.27 . 1 1875 167 ILE CD1 C 16.07 . 1 1876 167 ILE N N 118.09 . 1 1877 168 VAL H H 9.36 . 1 1878 168 VAL HA H 4.55 . 1 1879 168 VAL HB H 1.95 . 1 1880 168 VAL HG1 H 0.76 . 2 1881 168 VAL HG2 H 0.80 . 2 1882 168 VAL C C 173.43 . 1 1883 168 VAL CA C 59.67 . 1 1884 168 VAL CB C 36.24 . 1 1885 168 VAL CG1 C 20.97 . 1 1886 168 VAL CG2 C 20.97 . 1 1887 168 VAL N N 123.88 . 1 1888 169 PHE H H 8.93 . 1 1889 169 PHE HA H 5.38 . 1 1890 169 PHE HB2 H 3.33 . 1 1891 169 PHE HB3 H 2.97 . 1 1892 169 PHE HD1 H 7.65 . 1 1893 169 PHE HD2 H 7.65 . 1 1894 169 PHE HE1 H 7.27 . 1 1895 169 PHE HE2 H 7.27 . 1 1896 169 PHE CA C 55.23 . 1 1897 169 PHE CB C 39.12 . 1 1898 169 PHE CD1 C 133.07 . 1 1899 169 PHE CD2 C 133.07 . 1 1900 169 PHE CE1 C 130.27 . 1 1901 169 PHE CE2 C 130.27 . 1 1902 169 PHE N N 123.77 . 1 1903 170 PRO HA H 4.29 . 1 1904 170 PRO HB2 H 2.00 . 2 1905 170 PRO HB3 H 1.78 . 2 1906 170 PRO HG2 H 1.92 . 2 1907 170 PRO HG3 H 1.51 . 2 1908 170 PRO HD2 H 3.83 . 2 1909 170 PRO HD3 H 3.53 . 2 1910 170 PRO C C 175.35 . 1 1911 170 PRO CA C 62.71 . 1 1912 170 PRO CB C 33.03 . 1 1913 170 PRO CD C 51.37 . 1 1914 171 VAL H H 8.64 . 1 1915 171 VAL HA H 4.45 . 1 1916 171 VAL HB H 2.16 . 1 1917 171 VAL HG1 H 1.16 . 1 1918 171 VAL HG2 H 1.16 . 1 1919 171 VAL CA C 60.22 . 1 1920 171 VAL CB C 32.86 . 1 1921 171 VAL CG1 C 20.97 . 1 1922 171 VAL CG2 C 20.97 . 1 1923 171 VAL N N 122.10 . 1 1924 172 PRO HA H 4.60 . 1 1925 172 PRO HB2 H 2.06 . 2 1926 172 PRO HB3 H 1.91 . 2 1927 172 PRO HG2 H 2.16 . 2 1928 172 PRO HG3 H 2.06 . 2 1929 172 PRO HD2 H 4.14 . 2 1930 172 PRO HD3 H 3.83 . 2 1931 172 PRO C C 174.61 . 1 1932 172 PRO CA C 64.03 . 1 1933 172 PRO CB C 32.08 . 1 1934 172 PRO CG C 28.07 . 1 1935 172 PRO CD C 51.37 . 1 1936 173 ILE H H 6.56 . 1 1937 173 ILE HA H 4.73 . 1 1938 173 ILE HB H 2.08 . 1 1939 173 ILE HG12 H 1.89 . 2 1940 173 ILE HG13 H 1.45 . 2 1941 173 ILE HG2 H 1.15 . 1 1942 173 ILE HD1 H 0.94 . 1 1943 173 ILE C C 174.63 . 1 1944 173 ILE CA C 59.48 . 1 1945 173 ILE CB C 43.03 . 1 1946 173 ILE CG1 C 29.97 . 1 1947 173 ILE CG2 C 18.57 . 1 1948 173 ILE CD1 C 14.27 . 1 1949 173 ILE N N 113.41 . 1 1950 174 ASP H H 8.25 . 1 1951 174 ASP HA H 4.68 . 1 1952 174 ASP HB2 H 2.63 . 1 1953 174 ASP HB3 H 2.63 . 1 1954 174 ASP C C 175.94 . 1 1955 174 ASP CA C 53.55 . 1 1956 174 ASP CB C 41.35 . 1 1957 174 ASP N N 117.96 . 1 1958 175 GLN H H 7.11 . 1 1959 175 GLN HA H 4.14 . 1 1960 175 GLN HB2 H 1.49 . 1 1961 175 GLN HB3 H 2.00 . 1 1962 175 GLN HG2 H 2.72 . 2 1963 175 GLN HG3 H 2.58 . 2 1964 175 GLN HE21 H 7.75 . 1 1965 175 GLN HE22 H 7.33 . 1 1966 175 GLN CA C 56.47 . 1 1967 175 GLN CB C 29.34 . 1 1968 175 GLN N N 118.62 . 1 1969 175 GLN NE2 N 113.01 . 1 1970 176 CYS H H 8.90 . 1 1971 176 CYS HA H 4.09 . 1 1972 176 CYS HB2 H 2.69 . 1 1973 176 CYS HB3 H 3.37 . 1 1974 176 CYS C C 176.92 . 1 1975 176 CYS CA C 60.05 . 1 1976 176 CYS CB C 36.67 . 1 1977 176 CYS N N 114.52 . 1 1978 177 ILE H H 9.00 . 1 1979 177 ILE HA H 3.97 . 1 1980 177 ILE HB H 2.14 . 1 1981 177 ILE HG12 H 1.71 . 2 1982 177 ILE HG13 H 1.45 . 2 1983 177 ILE HG2 H 0.95 . 1 1984 177 ILE HD1 H 0.95 . 1 1985 177 ILE C C 175.00 . 1 1986 177 ILE CA C 63.87 . 1 1987 177 ILE CB C 38.85 . 1 1988 177 ILE CG1 C 27.47 . 1 1989 177 ILE CG2 C 18.47 . 1 1990 177 ILE CD1 C 16.37 . 1 1991 177 ILE N N 116.71 . 1 1992 178 ASP H H 8.21 . 1 1993 178 ASP HA H 4.82 . 1 1994 178 ASP HB2 H 2.66 . 1 1995 178 ASP HB3 H 2.88 . 1 1996 178 ASP C C 175.59 . 1 1997 178 ASP CA C 54.23 . 1 1998 178 ASP CB C 41.12 . 1 1999 178 ASP N N 121.64 . 1 2000 179 GLY H H 7.66 . 1 2001 179 GLY HA2 H 3.74 . 2 2002 179 GLY HA3 H 3.77 . 2 2003 179 GLY C C 177.17 . 1 2004 179 GLY CA C 46.23 . 1 2005 179 GLY N N 114.39 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details ; 3JHNHA couplings measured from ratio of cross to diagonal peaks in an HNHA experiment. ; loop_ _Sample_label $HNGAL_sample_N15 stop_ _Sample_conditions_label $sample_conditions_all _Mol_system_component_name HNGAL loop_ _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 3JHNHA 9 ILE H 9 ILE HA 4.3 3JHNHA 11 ALA H 11 ALA HA 4.5 3JHNHA 16 LYS H 16 LYS HA 9.1 3JHNHA 17 VAL H 17 VAL HA 8.0 3JHNHA 19 LEU H 19 LEU HA 9.2 3JHNHA 20 GLN H 20 GLN HA 3.8 3JHNHA 21 GLN H 21 GLN HA 3.8 3JHNHA 23 PHE H 23 PHE HA 1.5 3JHNHA 24 GLN H 24 GLN HA 11.0 3JHNHA 25 ASP H 25 ASP HA 2.6 3JHNHA 26 ASN H 26 ASN HA 4.2 3JHNHA 27 GLN H 27 GLN HA 8.0 3JHNHA 29 GLN H 29 GLN HA 3.3 3JHNHA 30 GLY H 30 GLY HA2 8.5 3JHNHA 30 GLY H 30 GLY HA3 2.0 3JHNHA 31 LYS H 31 LYS HA 8.5 3JHNHA 32 TRP H 32 TRP HA 9.0 3JHNHA 33 TYR H 33 TYR HA 8.5 3JHNHA 34 VAL H 34 VAL HA 4.0 3JHNHA 36 GLY H 36 GLY HA2 3.7 3JHNHA 36 GLY H 36 GLY HA3 3.7 3JHNHA 37 LEU H 37 LEU HA 8.2 3JHNHA 38 ALA H 38 ALA HA 8.6 3JHNHA 39 GLY H 39 GLY HA2 2.7 3JHNHA 39 GLY H 39 GLY HA3 2.7 3JHNHA 41 ALA H 41 ALA HA 9.8 3JHNHA 42 ILE H 42 ILE HA 9.1 3JHNHA 43 LEU H 43 LEU HA 9.4 3JHNHA 48 ASP H 48 ASP HA 9.5 3JHNHA 54 ALA H 54 ALA HA 8.5 3JHNHA 55 THR H 55 THR HA 8.1 3JHNHA 57 TYR H 57 TYR HA 8.0 3JHNHA 58 GLU H 58 GLU HA 9.0 3JHNHA 60 LYS H 60 LYS HA 9.4 3JHNHA 61 GLU H 61 GLU HA 3.3 3JHNHA 62 ASP H 62 ASP HA 8.9 3JHNHA 64 SER H 64 SER HA 8.0 3JHNHA 65 TYR H 65 TYR HA 9.1 3JHNHA 66 ASN H 66 ASN HA 9.4 3JHNHA 67 VAL H 67 VAL HA 8.8 3JHNHA 68 THR H 68 THR HA 8.5 3JHNHA 71 LEU H 71 LEU HA 9.0 3JHNHA 73 ARG H 73 ARG HA 9.0 3JHNHA 74 LYS H 74 LYS HA 5.0 3JHNHA 75 LYS H 75 LYS HA 8.5 3JHNHA 76 LYS H 76 LYS HA 8.9 3JHNHA 77 CYS H 77 CYS HA 8.0 3JHNHA 78 ASP H 78 ASP HA 9.5 3JHNHA 79 TYR H 79 TYR HA 8.5 3JHNHA 80 TRP H 80 TRP HA 11.0 3JHNHA 82 ARG H 82 ARG HA 8.0 3JHNHA 83 THR H 83 THR HA 9.5 3JHNHA 84 PHE H 84 PHE HA 9.5 3JHNHA 85 VAL H 85 VAL HA 9.4 3JHNHA 87 GLY H 87 GLY HA2 2.5 3JHNHA 87 GLY H 87 GLY HA3 8.5 3JHNHA 89 GLN H 89 GLN HA 8.3 3JHNHA 91 GLY H 91 GLY HA2 8.5 3JHNHA 91 GLY H 91 GLY HA3 3.5 3JHNHA 92 GLU H 92 GLU HA 9.0 3JHNHA 93 PHE H 93 PHE HA 8.0 3JHNHA 94 THR H 94 THR HA 9.0 3JHNHA 96 GLY H 96 GLY HA2 5.6 3JHNHA 96 GLY H 96 GLY HA3 4.3 3JHNHA 98 ILE H 98 ILE HA 3.8 3JHNHA 99 LYS H 99 LYS HA 5.1 3JHNHA 100 SER H 100 SER HA 8.0 3JHNHA 101 TYR H 101 TYR HA 9.4 3JHNHA 103 GLY H 103 GLY HA2 6.7 3JHNHA 103 GLY H 103 GLY HA3 5.6 3JHNHA 104 LEU H 104 LEU HA 8.5 3JHNHA 105 THR H 105 THR HA 8.0 3JHNHA 106 SER H 106 SER HA 8.0 3JHNHA 107 TYR H 107 TYR HA 8.5 3JHNHA 108 LEU H 108 LEU HA 9.2 3JHNHA 109 VAL H 109 VAL HA 9.6 3JHNHA 110 ARG H 110 ARG HA 8.2 3JHNHA 114 THR H 114 THR HA 9.0 3JHNHA 115 ASN H 115 ASN HA 11.0 3JHNHA 116 TYR H 116 TYR HA 3.7 3JHNHA 117 ASN H 117 ASN HA 9.0 3JHNHA 118 GLN H 118 GLN HA 11.1 3JHNHA 119 HIS H 119 HIS HA 8.8 3JHNHA 120 ALA H 120 ALA HA 8.0 3JHNHA 121 MET H 121 MET HA 8.0 3JHNHA 122 VAL H 122 VAL HA 10.8 3JHNHA 123 PHE H 123 PHE HA 9.2 3JHNHA 124 PHE H 124 PHE HA 9.5 3JHNHA 126 LYS H 125 LYS HA 8.8 3JHNHA 127 VAL H 127 VAL HA 9.7 3JHNHA 128 SER H 128 SER HA 9.3 3JHNHA 130 ASN H 130 ASN HA 9.7 3JHNHA 131 ARG H 131 ARG HA 9.6 3JHNHA 132 GLU H 132 GLU HA 8.4 3JHNHA 133 TYR H 133 TYR HA 9.3 3JHNHA 136 ILE H 136 ILE HA 9.2 3JHNHA 137 THR H 137 THR HA 10.5 3JHNHA 138 LEU H 138 LEU HA 9.6 3JHNHA 139 TYR H 139 TYR HA 8.8 3JHNHA 140 GLY H 140 GLY HA2 1.5 3JHNHA 140 GLY H 140 GLY HA3 1.5 3JHNHA 142 THR H 142 THR HA 9.4 3JHNHA 143 LYS H 143 LYS HA 5.8 3JHNHA 144 GLU H 144 GLU HA 9.2 3JHNHA 147 SER H 147 SER HA 2.6 3JHNHA 148 GLU H 148 GLU HA 3.7 3JHNHA 150 LYS H 150 LYS HA 1.5 3JHNHA 151 GLU H 151 GLU HA 4.4 3JHNHA 152 ASN H 152 ASN HA 4.0 3JHNHA 154 ILE H 154 ILE HA 3.9 3JHNHA 155 ARG H 155 ARG HA 4.1 3JHNHA 156 PHE H 156 PHE HA 3.7 3JHNHA 158 LYS H 158 LYS HA 4.6 3JHNHA 159 SER H 159 SER HA 4.2 3JHNHA 160 LEU H 160 LEU HA 8.6 3JHNHA 161 GLY H 161 GLY HA2 8.4 3JHNHA 161 GLY H 161 GLY HA3 5.7 3JHNHA 164 GLU H 164 GLU HA 5.0 3JHNHA 165 ASN H 165 ASN HA 8.5 3JHNHA 166 HIS H 166 HIS HA 8.0 3JHNHA 167 ILE H 167 ILE HA 9.2 3JHNHA 168 VAL H 168 VAL HA 9.7 3JHNHA 169 PHE H 169 PHE HA 10.1 3JHNHA 175 GLN H 175 GLN HA 5.0 3JHNHA 178 ASP H 178 ASP HA 9.5 stop_ save_ save_T1_relaxation_750 _Saveframe_category T1_relaxation _Details ; N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 750 MHz. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 3 ASP N 1.030 0.031 4 SER N 1.064 0.032 5 THR N 0.960 0.029 6 SER N 0.910 0.027 7 ASP N 0.487 0.013 8 LEU N 1.019 0.031 9 ILE N 1.225 0.055 11 ALA N 1.431 0.063 14 LEU N 1.337 0.040 15 SER N 1.348 0.040 16 LYS N 1.395 0.043 17 VAL N 1.508 0.045 19 LEU N 1.490 0.046 20 GLN N 1.390 0.044 21 GLN N 1.455 0.044 22 ASN N 1.514 0.045 23 PHE N 1.568 0.060 24 GLN N 1.765 0.063 25 ASP N 1.577 0.047 26 ASN N 1.386 0.046 27 GLN N 1.456 0.044 28 PHE N 1.520 0.046 29 GLN N 1.528 0.046 30 GLY N 1.504 0.057 31 LYS N 1.525 0.052 32 TRP N 1.598 0.087 33 TYR N 1.552 0.075 34 VAL N 1.694 0.051 35 VAL N 1.565 0.094 36 GLY N 1.458 0.063 37 LEU N 1.433 0.043 38 ALA N 1.467 0.056 39 GLY N 1.550 0.053 40 ASN N 1.586 0.048 41 ALA N 1.431 0.043 42 ILE N 1.458 0.067 43 LEU N 1.423 0.058 46 ASP N 1.160 0.051 48 ASP N 1.248 0.075 52 MET N 1.650 0.077 53 TYR N 1.700 0.102 54 ALA N 1.500 0.090 55 THR N 1.646 0.051 56 ILE N 1.700 0.102 57 TYR N 1.640 0.050 58 GLU N 1.658 0.056 60 LYS N 1.513 0.045 61 GLU N 1.435 0.043 62 ASP N 1.504 0.045 63 LYS N 1.495 0.054 64 SER N 1.450 0.044 65 TYR N 1.473 0.044 66 ASN N 1.560 0.053 67 VAL N 1.638 0.066 68 THR N 1.655 0.099 69 SER N 1.790 0.106 71 LEU N 1.570 0.047 73 ARG N 1.515 0.065 74 LYS N 1.450 0.075 75 LYS N 1.327 0.040 76 LYS N 1.317 0.040 77 CYS N 1.408 0.042 78 ASP N 1.484 0.067 79 TYR N 1.534 0.049 80 TRP N 1.677 0.083 82 ARG N 1.713 0.077 83 THR N 1.630 0.051 84 PHE N 1.593 0.049 87 GLY N 1.500 0.076 88 CYS N 1.400 0.050 89 GLN N 1.310 0.039 92 GLU N 1.350 0.041 93 PHE N 1.418 0.043 94 THR N 1.575 0.062 95 LEU N 1.650 0.058 96 GLY N 1.393 0.067 97 ASN N 1.480 0.044 98 ILE N 1.487 0.045 99 LYS N 1.300 0.039 100 SER N 1.474 0.047 101 TYR N 1.463 0.044 104 LEU N 1.490 0.045 105 THR N 1.440 0.086 106 SER N 1.515 0.053 107 TYR N 1.480 0.044 108 LEU N 1.385 0.050 109 VAL N 1.545 0.077 110 ARG N 1.487 0.060 112 VAL N 1.290 0.077 113 SER N 1.535 0.046 114 THR N 1.485 0.045 115 ASN N 1.566 0.050 116 TYR N 1.540 0.092 117 ASN N 1.547 0.049 118 GLN N 1.583 0.055 119 HIS N 1.465 0.056 120 ALA N 1.536 0.046 122 VAL N 1.540 0.092 123 PHE N 1.535 0.074 124 PHE N 1.540 0.062 125 LYS N 1.605 0.077 127 VAL N 1.617 0.090 128 SER N 1.446 0.061 129 GLN N 1.363 0.041 130 ASN N 1.405 0.042 131 ARG N 1.495 0.045 132 GLU N 1.557 0.055 133 TYR N 1.560 0.060 134 PHE N 1.478 0.044 135 LYS N 1.556 0.051 136 ILE N 1.560 0.068 137 THR N 1.490 0.076 138 LEU N 1.725 0.104 139 TYR N 1.550 0.078 140 GLY N 1.570 0.094 141 ARG N 1.525 0.086 142 THR N 1.490 0.058 143 LYS N 1.660 0.075 144 GLU N 1.640 0.049 145 LEU N 1.560 0.080 146 THR N 1.725 0.052 147 SER N 1.880 0.057 148 GLU N 1.395 0.042 150 LYS N 1.410 0.047 151 GLU N 1.478 0.044 152 ASN N 1.388 0.042 153 PHE N 1.350 0.041 154 ILE N 1.357 0.047 155 ARG N 1.470 0.044 156 PHE N 1.420 0.043 157 SER N 1.395 0.042 158 LYS N 1.430 0.055 159 SER N 1.540 0.047 160 LEU N 1.423 0.043 161 GLY N 1.470 0.044 162 LEU N 1.490 0.057 165 ASN N 1.288 0.039 167 ILE N 1.533 0.046 168 VAL N 1.496 0.046 169 PHE N 1.590 0.100 171 VAL N 1.366 0.049 173 ILE N 1.600 0.100 175 GLN N 1.747 0.099 176 CYS N 1.555 0.063 178 ASP N 1.532 0.048 179 GLY N 1.127 0.034 32 TRP NE1 1.950 0.059 80 TRP NE1 1.378 0.041 110 ARG NE 1.700 0.102 141 ARG NE 1.245 0.075 155 ARG NE 1.830 0.110 stop_ save_ save_T1_relaxation_600 _Saveframe_category T1_relaxation _Details ; N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 600 MHz. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 3 ASP N 0.792 0.020 4 SER N 0.770 0.026 5 THR N 0.705 0.026 6 SER N 0.686 0.019 7 ASP N 0.670 0.013 8 LEU N 0.833 0.017 9 ILE N 0.990 0.047 11 ALA N 1.030 0.021 14 LEU N 1.019 0.020 15 SER N 0.942 0.033 16 LYS N 0.991 0.028 17 VAL N 1.034 0.021 19 LEU N 1.084 0.022 20 GLN N 0.996 0.033 21 GLN N 1.042 0.021 22 ASN N 0.948 0.022 23 PHE N 1.062 0.021 24 GLN N 1.106 0.055 25 ASP N 1.097 0.039 26 ASN N 0.992 0.020 27 GLN N 1.074 0.023 28 PHE N 1.049 0.033 29 GLN N 1.055 0.032 30 GLY N 1.008 0.037 31 LYS N 1.074 0.021 32 TRP N 0.992 0.035 33 TYR N 1.047 0.028 34 VAL N 1.093 0.055 35 VAL N 1.096 0.055 36 GLY N 1.091 0.034 37 LEU N 1.026 0.033 38 ALA N 1.094 0.032 39 GLY N 1.060 0.045 40 ASN N 1.020 0.046 41 ALA N 1.002 0.042 42 ILE N 1.060 0.039 43 LEU N 1.024 0.044 46 ASP N 0.890 0.045 48 ASP N 0.854 0.021 52 MET N 1.040 0.052 53 TYR N 1.040 0.052 54 ALA N 1.008 0.027 55 THR N 1.052 0.039 56 ILE N 1.030 0.052 57 TYR N 1.133 0.043 58 GLU N 1.060 0.052 60 LYS N 0.934 0.032 61 GLU N 0.965 0.019 62 ASP N 1.102 0.022 63 LYS N 0.999 0.044 64 SER N 0.999 0.044 65 TYR N 1.080 0.039 66 ASN N 1.055 0.038 67 VAL N 1.011 0.029 68 THR N 1.033 0.035 69 SER N 1.039 0.038 71 LEU N 1.030 0.039 73 ARG N 1.002 0.029 74 LYS N 0.980 0.043 75 LYS N 0.900 0.030 76 LYS N 0.983 0.020 77 CYS N 1.142 0.027 78 ASP N 1.099 0.039 79 TYR N 1.100 0.032 80 TRP N 1.100 0.055 82 ARG N 1.050 0.051 83 THR N 1.133 0.038 84 PHE N 1.105 0.037 87 GLY N 1.029 0.038 88 CYS N 1.033 0.031 89 GLN N 1.004 0.020 92 GLU N 0.994 0.020 93 PHE N 0.973 0.022 94 THR N 1.051 0.032 95 LEU N 1.020 0.036 96 GLY N 1.003 0.048 97 ASN N 0.915 0.023 98 ILE N 1.057 0.032 99 LYS N 0.993 0.020 100 SER N 1.018 0.027 101 TYR N 1.047 0.023 102 GLY N 1.016 0.051 103 LEU N 1.013 0.020 105 THR N 1.103 0.032 106 SER N 1.043 0.025 107 TYR N 1.059 0.031 108 LEU N 1.066 0.035 109 VAL N 1.059 0.021 110 ARG N 1.018 0.026 112 VAL N 1.001 0.035 113 SER N 1.068 0.025 115 ASN N 1.060 0.045 116 TYR N 1.000 0.050 117 ASN N 1.106 0.035 118 GLN N 0.955 0.028 119 HIS N 1.056 0.043 120 ALA N 1.047 0.033 122 VAL N 1.122 0.043 123 PHE N 1.064 0.038 124 PHE N 1.054 0.029 125 LYS N 1.047 0.030 127 VAL N 1.041 0.030 128 SER N 1.034 0.034 129 GLN N 1.000 0.034 130 ASN N 1.026 0.024 131 ARG N 1.034 0.029 132 GLU N 1.079 0.022 133 TYR N 1.087 0.041 134 PHE N 1.036 0.021 135 LYS N 1.070 0.028 136 ILE N 1.099 0.031 137 THR N 1.043 0.049 138 LEU N 1.071 0.047 139 TYR N 1.024 0.045 140 GLY N 1.090 0.036 141 ARG N 1.059 0.021 142 THR N 1.040 0.030 143 LYS N 1.056 0.034 144 GLU N 1.167 0.050 145 LEU N 1.112 0.040 146 THR N 1.227 0.042 147 SER N 0.985 0.041 148 GLU N 0.949 0.024 150 LYS N 1.041 0.021 151 GLU N 1.034 0.021 152 ASN N 1.007 0.020 153 PHE N 0.986 0.025 154 ILE N 0.986 0.020 155 ARG N 1.003 0.020 156 PHE N 0.999 0.028 157 SER N 1.033 0.021 158 LYS N 1.000 0.020 159 SER N 1.048 0.034 160 LEU N 1.009 0.020 161 GLY N 1.029 0.022 162 LEU N 1.069 0.021 165 ASN N 0.969 0.019 167 ILE N 1.060 0.029 168 VAL N 1.040 0.025 169 PHE N 1.088 0.040 171 VAL N 1.031 0.030 173 ILE N 1.142 0.057 175 GLN N 1.152 0.030 176 CYS N 1.022 0.051 178 ASP N 1.025 0.032 179 GLY N 0.984 0.021 32 TRP NE1 1.223 0.048 80 TRP NE1 0.918 0.037 110 ARG NE 1.470 0.074 141 ARG NE 1.129 0.056 155 ARG NE 1.745 0.087 stop_ save_ save_T1_relaxation_500 _Saveframe_category T1_relaxation _Details ; N15 T1 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 500 MHz. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 4 SER N 0.940 0.362 5 THR N 0.893 0.114 6 SER N 0.837 0.099 7 ASP N 0.704 0.052 8 LEU N 0.710 0.021 9 ILE N 0.790 0.033 11 ALA N 0.799 0.024 14 LEU N 0.785 0.024 15 SER N 0.798 0.052 16 LYS N 0.792 0.034 17 VAL N 0.844 0.025 19 LEU N 0.841 0.025 20 GLN N 0.799 0.031 21 GLN N 0.799 0.024 23 PHE N 0.872 0.032 24 GLN N 0.914 0.049 25 ASP N 0.904 0.033 26 ASN N 0.846 0.042 27 GLN N 0.854 0.026 28 PHE N 0.862 0.034 29 GLN N 0.831 0.027 30 GLY N 0.786 0.033 31 LYS N 0.832 0.028 32 TRP N 0.750 0.034 33 TYR N 0.832 0.042 34 VAL N 0.867 0.040 35 VAL N 0.839 0.045 36 GLY N 0.795 0.034 37 LEU N 0.769 0.023 38 ALA N 0.771 0.033 39 GLY N 0.859 0.044 40 ASN N 0.921 0.054 41 ALA N 0.823 0.077 43 LEU N 0.732 0.047 46 ASP N 0.771 0.166 48 ASP N 0.803 0.038 52 MET N 0.818 0.066 53 TYR N 0.874 0.204 54 ALA N 0.883 0.040 55 THR N 0.871 0.042 56 ILE N 0.855 0.056 57 TYR N 0.829 0.039 58 GLU N 0.855 0.029 60 LYS N 0.793 0.025 61 GLU N 0.899 0.108 62 ASP N 0.854 0.032 63 LYS N 0.805 0.024 64 SER N 0.834 0.025 65 TYR N 0.820 0.034 66 ASN N 0.777 0.025 67 VAL N 0.854 0.041 68 THR N 0.840 0.040 69 SER N 0.905 0.070 71 LEU N 0.901 0.038 73 ARG N 0.818 0.026 76 LYS N 0.796 0.029 77 CYS N 0.832 0.039 78 ASP N 0.850 0.042 79 TYR N 0.923 0.031 80 TRP N 0.823 0.034 82 ARG N 0.913 0.062 83 THR N 0.878 0.029 84 PHE N 0.806 0.056 87 GLY N 0.865 0.061 88 CYS N 0.812 0.029 89 GLN N 0.815 0.027 92 GLU N 0.781 0.023 93 PHE N 0.834 0.040 94 THR N 0.809 0.027 95 LEU N 0.868 0.026 96 GLY N 0.816 0.056 97 ASN N 0.827 0.134 98 ILE N 0.840 0.027 99 LYS N 0.786 0.024 100 SER N 0.816 0.029 101 TYR N 0.856 0.028 104 LEU N 0.841 0.027 105 THR N 0.879 0.061 106 SER N 0.851 0.029 107 TYR N 0.828 0.025 108 LEU N 0.790 0.024 109 VAL N 0.859 0.026 110 ARG N 0.809 0.035 112 VAL N 0.759 0.036 113 SER N 0.808 0.024 115 ASN N 0.789 0.047 116 TYR N 0.766 0.024 117 ASN N 0.817 0.028 118 GLN N 0.813 0.028 119 HIS N 0.849 0.037 120 ALA N 0.842 0.032 122 VAL N 0.823 0.056 123 PHE N 0.816 0.026 124 PHE N 0.821 0.025 125 LYS N 0.804 0.024 127 VAL N 0.810 0.026 128 SER N 0.863 0.040 129 GLN N 0.774 0.066 130 ASN N 0.813 0.043 131 ARG N 0.868 0.026 132 GLU N 0.829 0.025 133 TYR N 0.818 0.033 134 PHE N 0.776 0.023 135 LYS N 0.806 0.024 136 ILE N 0.769 0.023 137 THR N 0.859 0.043 138 LEU N 0.823 0.025 139 TYR N 0.810 0.040 140 GLY N 0.761 0.037 141 ARG N 0.855 0.041 142 THR N 0.821 0.030 143 LYS N 0.900 0.060 144 GLU N 0.899 0.027 146 THR N 0.969 0.042 148 GLU N 0.799 0.050 150 LYS N 0.787 0.024 151 GLU N 0.799 0.024 152 ASN N 0.773 0.023 153 PHE N 0.765 0.057 154 ILE N 0.777 0.023 155 ARG N 0.776 0.023 156 PHE N 0.796 0.024 157 SER N 0.799 0.024 158 LYS N 0.776 0.026 159 SER N 0.865 0.038 160 LEU N 0.820 0.028 161 GLY N 0.787 0.024 162 LEU N 0.806 0.024 165 ASN N 0.742 0.032 167 ILE N 0.831 0.034 168 VAL N 0.821 0.025 169 PHE N 0.921 0.033 171 VAL N 0.808 0.028 173 ILE N 0.832 0.149 175 GLN N 1.052 0.061 176 CYS N 0.949 0.122 178 ASP N 0.871 0.044 179 GLY N 0.910 0.032 32 TRP NE1 0.924 0.028 80 TRP NE1 0.694 0.035 110 ARG NE 1.078 0.081 stop_ save_ save_T2_relaxation_750 _Saveframe_category T2_relaxation _Details ; N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 750 MHz. CPMG echo delay delta=0.45 ms. Rex contributions also given where appropriate. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 3 ASP N 0.2828 0.0077 . . 4 SER N 0.2600 0.0055 . . 5 THR N 0.2160 0.0043 . . 6 SER N 0.1721 0.0034 . . 7 ASP N 0.1593 0.0032 . . 8 LEU N 0.1007 0.0020 . . 9 ILE N 0.0599 0.0021 . . 11 ALA N 0.0546 0.0011 . . 14 LEU N 0.0645 0.0018 . . 15 SER N 0.0510 0.0020 . . 16 LYS N 0.0536 0.0015 . . 17 VAL N 0.0531 0.0011 . . 19 LEU N 0.0606 0.0012 . . 20 GLN N 0.0530 0.0015 . . 21 GLN N 0.0541 0.0015 . . 22 ASN N 0.0549 0.0011 . . 23 PHE N 0.0540 0.0011 . . 24 GLN N 0.0573 0.0012 . . 25 ASP N 0.0586 0.0012 . . 26 ASN N 0.0521 0.0010 . . 27 GLN N 0.0577 0.0012 . . 28 PHE N 0.0509 0.0010 1.23 0.55 29 GLN N 0.0552 0.0011 . . 30 GLY N 0.0537 0.0011 . . 31 LYS N 0.0508 0.0010 . . 32 TRP N 0.0541 0.0011 . . 33 TYR N 0.0535 0.0011 . . 34 VAL N 0.0524 0.0011 2.10 0.80 35 VAL N 0.0451 0.0015 4.13 1.34 36 GLY N 0.0594 0.0019 . . 37 LEU N 0.0497 0.0010 . . 38 ALA N 0.0506 0.0010 . . 39 GLY N 0.0539 0.0011 . . 40 ASN N 0.0481 0.0010 2.99 0.77 41 ALA N 0.0541 0.0013 . . 42 ILE N 0.0326 0.0013 8.73 1.14 43 LEU N 0.0353 0.0011 8.71 1.30 46 ASP N 0.0509 0.0043 1.27 1.15 48 ASP N 0.0534 0.0011 . . 52 MET N 0.0366 0.0037 8.84 2.19 53 TYR N 0.0380 0.0026 9.14 2.48 54 ALA N 0.0490 0.0013 . . 55 THR N 0.0541 0.0011 . . 56 ILE N 0.0539 0.0025 . . 57 TYR N 0.0594 0.0017 . . 58 GLU N 0.0578 0.0012 . . 60 LYS N 0.0549 0.0011 . . 61 GLU N 0.0565 0.0011 . . 62 ASP N 0.0568 0.0011 . . 63 LYS N 0.0509 0.0016 . . 64 SER N 0.0557 0.0011 . . 65 TYR N 0.0559 0.0011 . . 66 ASN N 0.0546 0.0011 . . 67 VAL N 0.0547 0.0011 . . 68 THR N 0.0520 0.0014 . . 69 SER N 0.0533 0.0018 . . 71 LEU N 0.0621 0.0029 . . 73 ARG N 0.0565 0.0011 . . 74 LYS N 0.0550 0.0024 . . 75 LYS N 0.0530 0.0014 . . 76 LYS N 0.0556 0.0011 . . 77 CYS N 0.0383 0.0010 7.67 0.74 78 ASP N 0.0513 0.0012 1.53 0.84 79 TYR N 0.0493 0.0010 2.97 0.67 80 TRP N 0.0472 0.0013 3.06 0.82 82 ARG N 0.0524 0.0017 . . 83 THR N 0.0566 0.0011 . . 84 PHE N 0.0545 0.0011 . . 87 GLY N 0.0614 0.0038 . . 88 CYS N 0.0520 0.0010 2.43 0.80 89 GLN N 0.0650 0.0013 . . 92 GLU N 0.0494 0.0010 . . 93 PHE N 0.0559 0.0011 . . 94 THR N 0.0532 0.0011 . . 95 LEU N 0.0576 0.0012 . . 96 GLY N 0.0529 0.0019 . . 97 ASN N 0.0558 0.0011 . . 98 ILE N 0.0525 0.0011 . . 99 LYS N 0.0516 0.0010 . . 100 SER N 0.0567 0.0011 . . 101 TYR N 0.0545 0.0011 . . 103 GLY N 0.0651 0.0013 . . 104 LEU N 0.0542 0.0011 . . 105 THR N 0.0515 0.0013 . . 106 SER N 0.0561 0.0011 . . 107 TYR N 0.0553 0.0011 . . 108 LEU N 0.0521 0.0010 . . 109 VAL N 0.0537 0.0011 . . 110 ARG N 0.0538 0.0011 . . 112 VAL N 0.0517 0.0010 . . 113 SER N 0.0530 0.0011 . . 114 THR N 0.0495 0.0010 . . 115 ASN N 0.0487 0.0010 2.31 0.66 116 TYR N 0.0539 0.0014 . . 117 ASN N 0.0517 0.0010 1.14 0.77 118 GLN N 0.0509 0.0010 . . 119 HIS N 0.0488 0.0010 1.56 0.69 120 ALA N 0.0494 0.0010 . . 122 VAL N 0.0539 0.0011 . . 123 PHE N 0.0508 0.0024 1.14 0.99 124 PHE N 0.0535 0.0012 . . 125 LYS N 0.0514 0.0010 . . 127 VAL N 0.0503 0.0010 . . 128 SER N 0.0522 0.0011 . . 129 GLN N 0.0535 0.0011 . . 130 ASN N 0.0481 0.0010 3.10 1.35 131 ARG N 0.0579 0.0012 . . 132 GLU N 0.0553 0.0011 . . 133 TYR N 0.0565 0.0011 . . 134 PHE N 0.0545 0.0011 . . 135 LYS N 0.0496 0.0010 1.57 0.91 136 ILE N 0.0502 0.0010 1.21 0.87 137 THR N 0.0384 0.0009 7.37 0.95 138 LEU N 0.0529 0.0014 . . 139 TYR N 0.0547 0.0011 . . 140 GLY N 0.0548 0.0013 . . 141 ARG N 0.0530 0.0011 . . 142 THR N 0.0503 0.0010 . . 143 LYS N 0.0581 0.0012 . . 144 GLU N 0.0553 0.0011 1.84 0.81 145 LEU N 0.0314 0.0019 17.47 1.77 146 THR N 0.0628 0.0013 3.02 0.98 147 SER N 0.0564 0.0015 . . 148 GLU N 0.0508 0.0010 . . 150 LYS N 0.0532 0.0011 . . 151 GLU N 0.0518 0.0010 . . 152 ASN N 0.0517 0.0010 . . 153 PHE N 0.0528 0.0011 . . 154 ILE N 0.0508 0.0010 . . 155 ARG N 0.0508 0.0010 . . 156 PHE N 0.0499 0.0010 . . 157 SER N 0.0509 0.0010 . . 158 LYS N 0.0492 0.0010 . . 159 SER N 0.0508 0.0010 1.33 0.52 160 LEU N 0.0510 0.0010 . . 161 GLY N 0.0546 0.0011 . . 162 LEU N 0.0503 0.0010 1.36 0.70 165 ASN N 0.0575 0.0013 . . 167 ILE N 0.0514 0.0010 0.85 0.68 168 VAL N 0.0491 0.0010 1.69 0.61 169 PHE N 0.0529 0.0011 . . 171 VAL N 0.0486 0.0010 2.73 1.14 173 ILE N 0.0319 0.0038 20.67 2.70 175 GLN N 0.0625 0.0013 . . 176 CYS N 0.0320 0.0027 16.19 1.23 178 ASP N 0.0420 0.0008 5.29 0.75 179 GLY N 0.1281 0.0026 . . 32 TRP NE1 0.0624 0.0013 . . 80 TRP NE1 0.0889 0.0018 . . 110 ARG NE 0.1160 0.0271 . . 141 ARG NE 0.0825 0.0253 . . 155 ARG NE 0.3721 0.0347 . . stop_ save_ save_T2_relaxation_600 _Saveframe_category T2_relaxation _Details ; N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 600 MHz. CPMG echo delay delta=0.45 ms ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error 3 ASP N 0.3273 0.0085 4 SER N 0.2808 0.0067 5 THR N 0.2306 0.0071 6 SER N 0.1978 0.0040 7 ASP N 0.1748 0.0035 8 LEU N 0.1122 0.0022 9 ILE N 0.0705 0.0014 11 ALA N 0.0624 0.0013 14 LEU N 0.0634 0.0013 15 SER N 0.0566 0.0020 16 LYS N 0.0582 0.0012 17 VAL N 0.0590 0.0012 19 LEU N 0.0657 0.0013 20 GLN N 0.0596 0.0012 21 GLN N 0.0613 0.0014 22 ASN N 0.0611 0.0013 23 PHE N 0.0595 0.0012 24 GLN N 0.0622 0.0020 25 ASP N 0.0616 0.0013 26 ASN N 0.0578 0.0012 27 GLN N 0.0633 0.0013 28 PHE N 0.0576 0.0012 29 GLN N 0.0605 0.0012 30 GLY N 0.0606 0.0019 31 LYS N 0.0601 0.0012 32 TRP N 0.0597 0.0019 33 TYR N 0.0555 0.0011 34 VAL N 0.0589 0.0017 35 VAL N 0.0506 0.0041 36 GLY N 0.0856 0.0052 37 LEU N 0.0580 0.0012 38 ALA N 0.0544 0.0011 39 GLY N 0.0577 0.0018 40 ASN N 0.0548 0.0011 41 ALA N 0.0575 0.0012 42 ILE N 0.0470 0.0009 43 LEU N 0.0502 0.0012 46 ASP N 0.0740 0.0025 48 ASP N 0.0643 0.0019 52 MET N 0.0463 0.0037 53 TYR N 0.0451 0.0030 54 ALA N 0.0570 0.0011 55 THR N 0.0574 0.0029 56 ILE N 0.0554 0.0015 57 TYR N 0.0613 0.0012 58 GLU N 0.0611 0.0026 60 LYS N 0.0594 0.0020 61 GLU N 0.0613 0.0012 62 ASP N 0.0616 0.0012 63 LYS N 0.0587 0.0012 64 SER N 0.0621 0.0015 65 TYR N 0.0603 0.0018 66 ASN N 0.0586 0.0012 67 VAL N 0.0613 0.0014 68 THR N 0.0574 0.0012 69 SER N 0.0601 0.0031 71 LEU N 0.0617 0.0017 73 ARG N 0.0614 0.0016 74 LYS N 0.0628 0.0015 75 LYS N 0.0609 0.0026 76 LYS N 0.0618 0.0012 77 CYS N 0.0465 0.0012 78 ASP N 0.0554 0.0011 79 TYR N 0.0545 0.0011 80 TRP N 0.0563 0.0011 82 ARG N 0.0565 0.0020 83 THR N 0.0627 0.0013 84 PHE N 0.0620 0.0015 87 GLY N 0.0677 0.0019 88 CYS N 0.0597 0.0012 89 GLN N 0.0712 0.0014 92 GLU N 0.0560 0.0014 93 PHE N 0.0618 0.0012 94 THR N 0.0590 0.0012 95 LEU N 0.0579 0.0013 96 GLY N 0.0567 0.0011 97 ASN N 0.0610 0.0012 98 ILE N 0.0579 0.0013 99 LYS N 0.0577 0.0012 100 SER N 0.0632 0.0013 101 TYR N 0.0590 0.0012 103 GLY N 0.0717 0.0014 104 LEU N 0.0600 0.0012 105 THR N 0.0547 0.0012 106 SER N 0.0621 0.0012 107 TYR N 0.0620 0.0012 108 LEU N 0.0599 0.0012 109 VAL N 0.0605 0.0015 110 ARG N 0.0586 0.0012 112 VAL N 0.0594 0.0013 113 SER N 0.0590 0.0012 115 ASN N 0.0543 0.0018 116 TYR N 0.0581 0.0028 117 ASN N 0.0583 0.0012 118 GLN N 0.0592 0.0012 119 HIS N 0.0576 0.0012 120 ALA N 0.0576 0.0012 122 VAL N 0.0589 0.0012 123 PHE N 0.0570 0.0019 124 PHE N 0.0579 0.0012 125 LYS N 0.0552 0.0017 127 VAL N 0.0610 0.0017 128 SER N 0.0557 0.0011 129 GLN N 0.0588 0.0012 130 ASN N 0.0570 0.0016 131 ARG N 0.0648 0.0013 132 GLU N 0.0626 0.0013 133 TYR N 0.0583 0.0012 134 PHE N 0.0602 0.0012 135 LYS N 0.0566 0.0011 136 ILE N 0.0558 0.0011 137 THR N 0.0471 0.0012 138 LEU N 0.0558 0.0018 139 TYR N 0.0566 0.0013 140 GLY N 0.0590 0.0012 141 ARG N 0.0577 0.0012 142 THR N 0.0575 0.0018 143 LYS N 0.0617 0.0018 144 GLU N 0.0626 0.0014 145 LEU N 0.0367 0.0014 146 THR N 0.0708 0.0016 147 SER N 0.0600 0.0012 148 GLU N 0.0578 0.0012 150 LYS N 0.0603 0.0012 151 GLU N 0.0558 0.0011 152 ASN N 0.0560 0.0011 153 PHE N 0.0567 0.0011 154 ILE N 0.0580 0.0013 155 ARG N 0.0569 0.0011 156 PHE N 0.0559 0.0011 157 SER N 0.0563 0.0011 158 LYS N 0.0534 0.0011 159 SER N 0.0577 0.0012 160 LEU N 0.0557 0.0011 161 GLY N 0.0609 0.0012 162 LEU N 0.0550 0.0011 165 ASN N 0.0622 0.0012 167 ILE N 0.0591 0.0012 168 VAL N 0.0545 0.0011 169 PHE N 0.0573 0.0012 171 VAL N 0.0584 0.0012 173 ILE N 0.0333 0.0017 175 GLN N 0.0727 0.0018 176 CYS N 0.0371 0.0007 178 ASP N 0.0491 0.0010 179 GLY N 0.1337 0.0027 32 TRP NE1 0.0650 0.0014 80 TRP NE1 0.0935 0.0019 110 ARG NE 0.1128 0.0231 155 ARG NE 0.2909 0.0292 stop_ save_ save_T2_relaxation_500 _Saveframe_category T2_relaxation _Details ; N15 T2 relaxation data with decoupling of CSA/DD cross-relaxation, water flipback. Interleaved acquisition mode. 500 MHz. CPMG echo delay delta=0.45 ms ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL loop_ _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error 4 SER N 0.3173 0.0475 5 THR N 0.2437 0.0140 6 SER N 0.1868 0.0059 7 ASP N 0.1709 0.0039 8 LEU N 0.1166 0.0023 9 ILE N 0.0757 0.0015 11 ALA N 0.0677 0.0014 14 LEU N 0.0819 0.0022 15 SER N 0.0621 0.0020 16 LYS N 0.0658 0.0013 17 VAL N 0.0645 0.0013 19 LEU N 0.0719 0.0014 20 GLN N 0.0639 0.0015 21 GLN N 0.0667 0.0015 23 PHE N 0.0652 0.0013 24 GLN N 0.0679 0.0014 25 ASP N 0.0671 0.0013 26 ASN N 0.0625 0.0013 27 GLN N 0.0718 0.0014 28 PHE N 0.0630 0.0013 29 GLN N 0.0691 0.0014 30 GLY N 0.0658 0.0013 31 LYS N 0.0619 0.0012 32 TRP N 0.0653 0.0021 33 TYR N 0.0617 0.0015 34 VAL N 0.0612 0.0012 35 VAL N 0.0493 0.0018 36 GLY N 0.0641 0.0013 37 LEU N 0.0603 0.0012 38 ALA N 0.0597 0.0012 39 GLY N 0.0637 0.0014 40 ASN N 0.0567 0.0013 41 ALA N 0.0578 0.0016 42 ILE N 0.0530 0.0026 43 LEU N 0.0480 0.0016 46 ASP N 0.0627 0.0032 48 ASP N 0.0611 0.0013 52 MET N 0.0437 0.0018 53 TYR N 0.0481 0.0038 54 ALA N 0.0620 0.0012 55 THR N 0.0638 0.0013 56 ILE N 0.0600 0.0025 57 TYR N 0.0653 0.0016 58 GLU N 0.0683 0.0014 60 LYS N 0.0654 0.0013 61 GLU N 0.0688 0.0018 62 ASP N 0.0685 0.0014 63 LYS N 0.0669 0.0013 64 SER N 0.0734 0.0015 65 TYR N 0.0655 0.0013 66 ASN N 0.0616 0.0012 67 VAL N 0.0708 0.0018 68 THR N 0.0604 0.0012 69 SER N 0.0651 0.0025 71 LEU N 0.0627 0.0015 73 ARG N 0.0670 0.0013 76 LYS N 0.0693 0.0014 77 CYS N 0.0544 0.0013 78 ASP N 0.0612 0.0013 79 TYR N 0.0593 0.0012 80 TRP N 0.0610 0.0014 82 ARG N 0.0647 0.0020 83 THR N 0.0699 0.0014 84 PHE N 0.0612 0.0015 87 GLY N 0.0723 0.0020 88 CYS N 0.0670 0.0020 89 GLN N 0.0801 0.0016 92 GLU N 0.0605 0.0012 93 PHE N 0.0667 0.0013 94 THR N 0.0628 0.0013 95 LEU N 0.0685 0.0014 96 GLY N 0.0659 0.0028 97 ASN N 0.0682 0.0021 98 ILE N 0.0643 0.0015 99 LYS N 0.0636 0.0013 100 SER N 0.0675 0.0014 101 TYR N 0.0653 0.0013 103 GLY N 0.1128 0.0276 104 LEU N 0.0656 0.0013 105 THR N 0.0599 0.0012 106 SER N 0.0675 0.0014 107 TYR N 0.0636 0.0014 108 LEU N 0.0639 0.0013 109 VAL N 0.0647 0.0013 110 ARG N 0.0654 0.0013 112 VAL N 0.0624 0.0014 113 SER N 0.0641 0.0013 115 ASN N 0.0568 0.0011 116 TYR N 0.0609 0.0016 117 ASN N 0.0634 0.0013 118 GLN N 0.0606 0.0012 119 HIS N 0.0591 0.0012 120 ALA N 0.0595 0.0012 122 VAL N 0.0632 0.0014 123 PHE N 0.0623 0.0019 124 PHE N 0.0626 0.0013 125 LYS N 0.0616 0.0012 127 VAL N 0.0618 0.0018 128 SER N 0.0614 0.0012 129 GLN N 0.0625 0.0018 130 ASN N 0.0629 0.0013 131 ARG N 0.0706 0.0014 132 GLU N 0.0676 0.0014 133 TYR N 0.0653 0.0016 134 PHE N 0.0647 0.0013 135 LYS N 0.0617 0.0012 136 ILE N 0.0605 0.0017 137 THR N 0.0521 0.0015 138 LEU N 0.0619 0.0023 139 TYR N 0.0651 0.0014 140 GLY N 0.0610 0.0012 141 ARG N 0.0606 0.0013 142 THR N 0.0667 0.0016 143 LYS N 0.0671 0.0013 144 GLU N 0.0696 0.0014 146 THR N 0.0830 0.0017 148 GLU N 0.0605 0.0012 150 LYS N 0.0645 0.0013 151 GLU N 0.0609 0.0012 152 ASN N 0.0620 0.0012 153 PHE N 0.0663 0.0025 154 ILE N 0.0616 0.0012 155 ARG N 0.0618 0.0012 156 PHE N 0.0596 0.0012 157 SER N 0.0620 0.0012 158 LYS N 0.0708 0.0035 159 SER N 0.0634 0.0013 160 LEU N 0.0626 0.0013 161 GLY N 0.0663 0.0013 162 LEU N 0.0610 0.0012 165 ASN N 0.0712 0.0020 167 ILE N 0.0616 0.0012 168 VAL N 0.0596 0.0012 169 PHE N 0.0627 0.0013 171 VAL N 0.0616 0.0015 173 ILE N 0.0441 0.0046 175 GLN N 0.0783 0.0020 176 CYS N 0.0427 0.0039 178 ASP N 0.0558 0.0011 179 GLY N 0.1531 0.0031 32 TRP NE1 0.0708 0.0015 80 TRP NE1 0.0966 0.0019 110 ARG NE 0.0742 0.0015 stop_ save_ save_heteronuclear_NOE_750_TRP_NE1 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 750 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name NE1 _Atom_two_atom_name HE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 32 TRP 0.840 0.050 80 TRP 0.657 0.050 stop_ save_ save_heteronuclear_NOE_750_ARG_NE _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 750 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name NE _Atom_two_atom_name HE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 110 ARG 0.657 0.106 155 ARG -0.712 0.077 stop_ save_ save_heteronuclear_NOE_750_other _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 750 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 3 ASP -0.256 0.050 4 SER 0.024 0.050 5 THR 0.268 0.050 6 SER 0.290 0.050 7 ASP 0.410 0.050 8 LEU 0.437 0.050 9 ILE 0.719 0.050 11 ALA 0.788 0.050 14 LEU 0.778 0.050 15 SER 0.840 0.050 16 LYS 0.840 0.050 17 VAL 0.817 0.050 19 LEU 0.817 0.050 20 GLN 0.837 0.050 21 GLN 0.804 0.050 22 ASN 0.816 0.050 23 PHE 0.813 0.050 24 GLN 0.860 0.050 25 ASP 0.845 0.050 26 ASN 0.859 0.050 27 GLN 0.821 0.050 28 PHE 0.861 0.050 29 GLN 0.839 0.050 30 GLY 0.876 0.050 31 LYS 0.830 0.050 32 TRP 0.844 0.050 33 TYR 0.868 0.050 34 VAL 0.808 0.050 35 VAL 0.866 0.059 36 GLY 0.855 0.050 37 LEU 0.824 0.050 38 ALA 0.863 0.050 39 GLY 0.852 0.050 40 ASN 0.864 0.050 41 ALA 0.861 0.050 42 ILE 0.775 0.050 43 LEU 0.828 0.050 46 ASP 0.492 0.064 48 ASP 0.462 0.054 52 MET 0.849 0.086 53 TYR 0.845 0.087 54 ALA 0.809 0.050 55 THR 0.849 0.050 56 ILE 0.870 0.055 57 TYR 0.875 0.050 58 GLU 0.823 0.050 60 LYS 0.828 0.050 61 GLU 0.799 0.050 62 ASP 0.800 0.050 63 LYS 0.821 0.050 64 SER 0.812 0.050 65 TYR 0.843 0.050 66 ASN 0.844 0.050 67 VAL 0.814 0.050 68 THR 0.889 0.050 69 SER 0.783 0.052 71 LEU 0.811 0.050 74 LYS 0.762 0.060 75 LYS 0.707 0.050 76 LYS 0.702 0.050 77 CYS 0.692 0.050 78 ASP 0.777 0.050 79 TYR 0.815 0.050 80 TRP 0.822 0.050 82 ARG 0.807 0.050 83 THR 0.813 0.050 84 PHE 0.858 0.050 87 GLY 0.806 0.050 88 CYS 0.826 0.050 89 GLN 0.613 0.050 92 GLU 0.829 0.050 93 PHE 0.829 0.050 94 THR 0.824 0.050 95 LEU 0.773 0.050 96 GLY 0.823 0.050 97 ASN 0.813 0.050 98 ILE 0.833 0.050 99 LYS 0.799 0.050 100 SER 0.786 0.050 101 TYR 0.787 0.050 103 GLY 0.725 0.050 104 LEU 0.800 0.050 105 THR 0.751 0.050 106 SER 0.795 0.050 107 TYR 0.860 0.050 108 LEU 0.852 0.050 109 VAL 0.851 0.050 110 ARG 0.876 0.050 112 VAL 0.868 0.050 113 SER 0.858 0.050 114 THR 0.840 0.050 115 ASN 0.861 0.050 116 TYR 0.916 0.051 117 ASN 0.889 0.050 118 GLN 0.876 0.050 119 HIS 0.840 0.050 120 ALA 0.879 0.050 122 VAL 0.914 0.050 123 PHE 0.887 0.050 124 PHE 0.873 0.050 125 LYS 0.830 0.050 127 VAL 0.879 0.050 128 SER 0.812 0.050 129 GLN 0.749 0.050 130 ASN 0.756 0.050 131 ARG 0.755 0.050 132 GLU 0.759 0.050 133 TYR 0.781 0.050 134 PHE 0.806 0.050 135 LYS 0.846 0.050 136 ILE 0.840 0.050 137 THR 0.852 0.050 138 LEU 0.850 0.050 139 TYR 0.870 0.050 140 GLY 0.854 0.050 141 ARG 0.824 0.050 142 THR 0.847 0.050 143 LYS 0.865 0.050 144 GLU 0.726 0.050 145 LEU 0.665 0.050 146 THR 0.712 0.050 147 SER 0.832 0.050 148 GLU 0.829 0.050 150 LYS 0.756 0.050 151 GLU 0.843 0.050 152 ASN 0.872 0.050 153 PHE 0.822 0.050 154 ILE 0.830 0.050 155 ARG 0.861 0.050 156 PHE 0.874 0.050 157 SER 0.779 0.050 158 LYS 0.831 0.050 159 SER 0.890 0.050 160 LEU 0.837 0.050 161 GLY 0.828 0.050 162 LEU 0.842 0.050 165 ASN 0.801 0.050 167 ILE 0.844 0.050 168 VAL 0.805 0.050 169 PHE 0.836 0.050 171 VAL 0.829 0.050 173 ILE 0.847 0.155 175 GLN 0.558 0.050 176 CYS 0.830 0.060 178 ASP 0.707 0.050 179 GLY 0.234 0.050 stop_ save_ save_heteronuclear_NOE_600_TRP_NE1 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name NE1 _Atom_two_atom_name HE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 32 TRP 0.868 0.050 80 TRP 0.645 0.050 stop_ save_ save_heteronuclear_NOE_600_ARG_NE _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name NE _Atom_two_atom_name HE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 110 ARG 0.572 0.111 141 ARG 0.634 0.065 155 ARG -1.115 0.094 stop_ save_ save_heteronuclear_NOE_600 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 3 ASP -0.952 0.050 4 SER -0.086 0.050 5 THR 0.176 0.050 6 SER -0.115 0.050 7 ASP 0.062 0.050 8 LEU 0.493 0.050 9 ILE 0.706 0.050 11 ALA 0.839 0.050 14 LEU 0.777 0.050 15 SER 0.790 0.050 16 LYS 0.702 0.050 17 VAL 0.812 0.050 19 LEU 0.784 0.050 20 GLN 0.752 0.050 21 GLN 0.737 0.050 22 ASN 0.725 0.050 23 PHE 0.831 0.050 24 GLN 0.724 0.054 25 ASP 0.837 0.050 26 ASN 0.807 0.050 27 GLN 0.763 0.050 28 PHE 0.858 0.050 29 GLN 0.784 0.050 30 GLY 0.778 0.052 31 LYS 0.743 0.050 32 TRP 0.824 0.054 33 TYR 0.842 0.051 34 VAL 0.864 0.065 35 VAL 0.869 0.093 36 GLY 0.807 0.055 37 LEU 0.791 0.050 38 ALA 0.916 0.050 39 GLY 0.769 0.050 40 ASN 0.832 0.050 41 ALA 0.849 0.054 42 ILE 0.808 0.052 43 LEU 0.649 0.050 46 ASP 0.537 0.070 48 ASP 0.407 0.057 52 MET 0.879 0.107 53 TYR 0.849 0.139 54 ALA 0.807 0.058 55 THR 0.803 0.050 56 ILE 0.788 0.076 57 TYR 0.901 0.058 58 GLU 0.861 0.050 60 LYS 0.839 0.050 61 GLU 0.822 0.050 62 ASP 0.775 0.050 63 LYS 0.778 0.050 64 SER 0.757 0.050 65 TYR 0.790 0.050 66 ASN 0.880 0.050 67 VAL 0.851 0.050 68 THR 0.951 0.066 69 SER 0.930 0.084 71 LEU 0.818 0.062 73 ARG 0.724 0.050 74 LYS 0.658 0.063 75 LYS 0.607 0.050 76 LYS 0.617 0.050 77 CYS 0.758 0.050 78 ASP 0.774 0.054 79 TYR 0.767 0.050 80 TRP 0.852 0.056 82 ARG 0.832 0.069 83 THR 0.762 0.050 84 PHE 0.805 0.054 87 GLY 0.740 0.066 88 CYS 0.772 0.050 89 GLN 0.635 0.050 92 GLU 0.759 0.050 93 PHE 0.676 0.050 94 THR 0.750 0.050 95 LEU 0.869 0.057 96 GLY 0.833 0.078 97 ASN 0.756 0.050 98 ILE 0.849 0.050 99 LYS 0.718 0.050 100 SER 0.773 0.050 101 TYR 0.699 0.050 103 GLY 0.588 0.050 104 LEU 0.661 0.050 105 THR 0.722 0.057 106 SER 0.867 0.050 107 TYR 0.787 0.050 108 LEU 0.806 0.053 109 VAL 0.793 0.052 110 ARG 0.858 0.050 112 VAL 0.822 0.064 113 SER 0.841 0.050 115 ASN 0.900 0.054 116 TYR 0.839 0.074 117 ASN 0.868 0.050 118 GLN 0.874 0.050 119 HIS 0.872 0.050 120 ALA 0.779 0.050 122 VAL 0.819 0.060 123 PHE 0.901 0.073 124 PHE 0.803 0.050 125 LYS 0.763 0.050 127 VAL 0.727 0.053 128 SER 0.709 0.050 129 GLN 0.759 0.050 130 ASN 0.732 0.050 131 ARG 0.631 0.050 132 GLU 0.798 0.050 133 TYR 0.811 0.058 134 PHE 0.726 0.050 135 LYS 0.716 0.050 136 ILE 0.725 0.051 137 THR 0.729 0.065 138 LEU 0.831 0.053 139 TYR 0.823 0.053 140 GLY 0.835 0.059 141 ARG 0.776 0.052 142 THR 0.758 0.050 143 LYS 0.861 0.055 144 GLU 0.688 0.050 145 LEU 0.600 0.100 146 THR 0.721 0.050 147 SER 0.791 0.050 148 GLU 0.939 0.050 150 LYS 0.786 0.050 151 GLU 0.881 0.050 152 ASN 0.782 0.050 153 PHE 0.881 0.050 154 ILE 0.867 0.050 155 ARG 0.910 0.050 156 PHE 0.764 0.050 157 SER 0.820 0.050 158 LYS 0.783 0.050 159 SER 0.893 0.050 160 LEU 0.821 0.050 161 GLY 0.904 0.050 162 LEU 0.833 0.050 165 ASN 0.776 0.050 167 ILE 0.846 0.050 168 VAL 0.747 0.050 169 PHE 0.702 0.050 171 VAL 0.737 0.050 173 ILE 0.992 0.221 175 GLN 0.617 0.061 176 CYS 0.871 0.084 178 ASP 0.682 0.050 179 GLY -0.145 0.050 stop_ save_ save_heteronuclear_NOE_500_TRP_NE1 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name NE1 _Atom_two_atom_name HE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 32 TRP 0.841 0.050 80 TRP 0.576 0.050 stop_ save_ save_heteronuclear_NOE_500_ARG_NE _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 600 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name NE _Atom_two_atom_name HE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 110 ARG 0.652 0.102 141 ARG 0.766 0.080 stop_ save_ save_heteronuclear_NOE_500 _Saveframe_category heteronuclear_NOE _Details ; N15{1H} Heteronuclear steady-state NOE using 3s 1H presat. time. water flipback. Reference experiment (i.e. no presat.) interleaved with acquisition. 500 MHz. Minimum error assumed to be 0.05. ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _Mol_system_component_name HNGAL _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 4 SER -0.651 0.183 5 THR -0.354 0.087 6 SER -0.052 0.052 7 ASP 0.112 0.050 8 LEU 0.310 0.050 9 ILE 0.627 0.064 11 ALA 0.740 0.050 14 LEU 0.722 0.050 15 SER 0.775 0.050 16 LYS 0.758 0.050 17 VAL 0.807 0.050 19 LEU 0.753 0.050 20 GLN 0.850 0.056 21 GLN 0.799 0.050 23 PHE 0.774 0.050 24 GLN 0.793 0.064 25 ASP 0.830 0.050 26 ASN 0.838 0.050 27 GLN 0.770 0.050 28 PHE 0.809 0.050 29 GLN 0.749 0.050 30 GLY 0.863 0.064 31 LYS 0.865 0.050 32 TRP 0.813 0.056 33 TYR 0.807 0.061 34 VAL 0.813 0.074 35 VAL 0.798 0.104 36 GLY 0.812 0.059 37 LEU 0.802 0.055 38 ALA 0.779 0.051 39 GLY 0.708 0.064 40 ASN 0.853 0.066 41 ALA 0.734 0.089 43 LEU 0.709 0.136 46 ASP 0.452 0.122 48 ASP 0.774 0.065 52 MET 0.716 0.130 53 TYR 0.637 0.140 54 ALA 0.842 0.067 55 THR 0.856 0.072 56 ILE 0.813 0.100 57 TYR 0.753 0.064 58 GLU 0.828 0.050 60 LYS 0.747 0.055 61 GLU 0.728 0.065 62 ASP 0.758 0.050 63 LYS 0.772 0.050 64 SER 0.739 0.050 65 TYR 0.776 0.054 66 ASN 0.883 0.061 67 VAL 0.829 0.055 68 THR 0.856 0.074 69 SER 0.901 0.114 71 LEU 0.732 0.067 73 ARG 0.765 0.050 76 LYS 0.677 0.050 77 CYS 0.696 0.053 78 ASP 0.781 0.070 79 TYR 0.733 0.050 80 TRP 0.878 0.062 82 ARG 0.718 0.074 83 THR 0.777 0.063 84 PHE 0.766 0.064 87 GLY 0.731 0.074 88 CYS 0.820 0.050 89 GLN 0.553 0.050 92 GLU 0.796 0.050 93 PHE 0.730 0.050 94 THR 0.782 0.062 95 LEU 0.865 0.065 96 GLY 0.712 0.080 97 ASN 0.862 0.106 98 ILE 0.770 0.050 99 LYS 0.726 0.050 100 SER 0.823 0.050 101 TYR 0.755 0.050 103 GLY 0.896 0.254 104 LEU 0.719 0.050 105 THR 0.764 0.060 106 SER 0.776 0.050 107 TYR 0.766 0.053 108 LEU 0.765 0.063 109 VAL 0.785 0.055 110 ARG 0.784 0.050 112 VAL 0.896 0.077 113 SER 0.818 0.050 115 ASN 0.778 0.059 116 TYR 0.797 0.080 117 ASN 0.829 0.050 118 GLN 0.845 0.051 119 HIS 0.881 0.068 120 ALA 0.851 0.050 122 VAL 0.886 0.074 123 PHE 0.815 0.077 124 PHE 0.840 0.050 125 LYS 0.819 0.050 127 VAL 0.854 0.073 128 SER 0.782 0.051 129 GLN 0.826 0.083 130 ASN 0.707 0.050 131 ARG 0.689 0.050 132 GLU 0.726 0.050 133 TYR 0.742 0.067 134 PHE 0.764 0.050 135 LYS 0.841 0.050 136 ILE 0.845 0.068 137 THR 0.799 0.080 138 LEU 0.903 0.073 139 TYR 0.795 0.059 140 GLY 0.763 0.063 141 ARG 0.861 0.062 142 THR 0.830 0.050 143 LYS 0.752 0.057 144 GLU 0.680 0.050 146 THR 0.622 0.050 148 GLU 0.831 0.050 150 LYS 0.761 0.050 151 GLU 0.785 0.050 152 ASN 0.827 0.050 154 ILE 0.799 0.050 155 ARG 0.790 0.050 156 PHE 0.819 0.050 157 SER 0.790 0.050 158 LYS 0.799 0.050 159 SER 0.826 0.050 160 LEU 0.808 0.050 161 GLY 0.846 0.050 162 LEU 0.818 0.050 165 ASN 0.788 0.055 167 ILE 0.825 0.058 168 VAL 0.787 0.054 169 PHE 0.773 0.051 171 VAL 0.718 0.053 173 ILE 0.721 0.189 175 GLN 0.534 0.063 176 CYS 0.703 0.145 178 ASP 0.708 0.050 79 GLY -0.224 0.050 stop_ save_ save_S2_parameters> _Saveframe_category S2_parameters _Details ; Order parameters are generalised, where applicable (i.e. S2=S2f*S2s), derived from model-free analysis using truncated Lipari-Szabo and the extended Clore model function (No residues fitted the full Lipari-Szabo model). ; _Sample_label $HNGAL_sample_N15 _Sample_conditions_label $sample_conditions_all _Mol_system_component_name HNGAL _Tau_s_value_units ns loop_ _Residue_seq_code _Residue_label _Atom_name _S2_value _S2_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error 3 ASP N 0.105 0.006 0.783 0.016 0.135 0.007 0.611 0.003 4 SER N 0.127 0.006 0.695 0.015 0.183 0.007 0.784 0.005 5 THR N 0.159 0.008 0.697 0.014 0.228 0.011 0.980 0.007 6 SER N 0.203 0.010 0.723 0.011 0.281 0.013 1.138 0.009 7 ASP N 0.219 0.008 0.769 0.011 0.285 0.009 1.327 0.009 8 LEU N 0.431 0.011 0.761 0.010 0.567 0.012 1.253 0.025 9 ILE N 0.744 0.022 0.849 0.018 0.876 0.017 1.355 0.125 11 ALA N 0.852 0.015 0.888 0.014 0.960 0.008 1.078 0.240 14 LEU N 0.692 0.054 0.786 0.011 0.881 0.067 2.894 0.683 15 SER N 0.927 0.014 0.948 0.010 0.978 0.010 1.401 0.750 16 LYS N 0.910 0.010 . . . . . . 17 VAL N 0.896 0.008 . . . . . . 19 LEU N 0.790 0.009 0.825 0.008 0.958 0.006 1.771 0.482 20 GLN N 0.909 0.010 . . . . . . 21 GLN N 0.889 0.010 . . . . . . 22 ASN N 0.907 0.014 . . . . . . 23 PHE N 0.882 0.012 . . . . . . 24 GLN N 0.837 0.012 . . . . . . 25 ASP N 0.840 0.014 . . . . . . 26 ASN N 0.927 0.011 . . . . . . 27 GLN N 0.816 0.014 0.845 0.011 0.965 0.011 1.376 0.395 28 PHE N 0.877 0.024 . . . . . . 29 GLN N 0.864 0.014 . . . . . . 30 GLY N 0.886 0.013 . . . . . . 31 LYS N 0.903 0.012 . . . . . . 32 TRP N 0.896 0.016 . . . . . . 33 TYR N 0.900 0.017 . . . . . . 34 VAL N 0.814 0.026 . . . . . . 35 VAL N 0.864 0.034 . . . . . . 36 GLY N 0.875 0.018 . . . . . . 37 LEU N 0.938 0.013 . . . . . . 38 ALA N 0.930 0.012 . . . . . . 39 GLY N 0.880 0.019 . . . . . . 40 ASN N 0.856 0.021 . . . . . . 41 ALA N 0.913 0.014 . . . . . . 42 ILE N 0.884 0.027 . . . . . . 43 LEU N 0.943 0.034 . . . . . . 46 ASP N 0.862 0.026 0.554 0.100 . . . . 48 ASP N 0.850 0.016 0.564 0.100 . . . . 52 MET N 0.862 0.032 . . . . . . 53 TYR N 0.871 0.042 . . . . . . 54 ALA N 0.931 0.013 . . . . . . 55 THR N 0.888 0.018 . . . . . . 56 ILE N 0.937 0.020 . . . . . . 57 TYR N 0.848 0.011 . . . . . . 58 GLU N 0.840 0.015 . . . . . . 60 LYS N 0.862 0.021 0.914 0.018 0.944 0.013 1.797 0.250 61 GLU N 0.838 0.015 0.902 0.012 0.929 0.011 1.643 0.179 62 ASP N 0.832 0.013 0.851 0.010 0.977 0.011 0.764 0.523 63 LYS N 0.912 0.014 . . . . . . 64 SER N 0.859 0.017 0.883 0.013 0.973 0.012 0.785 0.389 65 TYR N 0.871 0.012 . . . . . . 66 ASN N 0.901 0.012 . . . . . . 67 VAL N 0.885 0.015 . . . . . . 68 THR N 0.927 0.017 . . . . . . 69 SER N 0.891 0.016 . . . . . . 71 LEU N 0.860 0.019 . . . . . . 73 ARG N 0.848 0.015 0.882 0.012 0.962 0.011 0.984 0.528 74 LYS N 0.850 0.024 0.900 0.018 0.945 0.018 0.701 0.267 75 LYS N 0.892 0.023 0.961 0.019 0.928 0.015 0.620 0.183 76 LYS N 0.840 0.012 0.906 0.009 0.926 0.008 0.901 0.145 77 CYS N 0.872 0.017 . . . . . . 78 ASP N 0.885 0.028 . . . . . . 79 TYR N 0.856 0.019 . . . . . . 80 TRP N 0.852 0.030 . . . . . . 82 ARG N 0.889 0.022 . . . . . . 83 THR N 0.832 0.010 . . . . . . 84 PHE N 0.861 0.012 . . . . . . 87 GLY N 0.779 0.023 0.828 0.016 0.941 0.021 1.504 0.360 88 CYS N 0.787 0.026 0.837 0.020 0.940 0.022 3.900 2.200 89 GLN N 0.717 0.013 0.837 0.010 0.856 0.011 0.949 0.058 92 GLU N 0.954 0.012 . . . . . . 93 PHE N 0.852 0.017 0.877 0.015 0.971 0.011 0.989 0.361 94 THR N 0.898 0.013 . . . . . . 95 LEU N 0.839 0.015 . . . . . . 96 GLY N 0.932 0.019 . . . . . . 97 ASN N 0.842 0.019 0.923 0.015 0.913 0.015 1.967 0.191 98 ILE N 0.900 0.011 . . . . . . 99 LYS N 0.908 0.013 0.942 0.010 0.963 0.009 0.792 0.254 100 SER N 0.839 0.013 0.872 0.010 0.962 0.011 1.104 0.313 101 TYR N 0.887 0.012 . . . . . . 103 GLY N 0.721 0.028 0.835 0.022 0.864 0.025 1.085 0.136 104 LEU N 0.876 0.015 0.900 0.010 0.974 0.013 0.603 0.266 105 THR N 0.936 0.010 . . . . . . 106 SER N 0.863 0.015 . . . . . . 107 TYR N 0.877 0.013 . . . . . . 108 LEU N 0.904 0.014 . . . . . . 109 VAL N 0.883 0.012 . . . . . . 110 ARG N 0.897 0.012 . . . . . . 112 VAL N 0.922 0.017 . . . . . . 113 SER N 0.893 0.011 . . . . . . 114 THR N 0.935 0.016 . . . . . . 115 ASN N 0.874 0.030 . . . . . . 116 TYR N 0.923 0.016 . . . . . . 117 ASN N 0.869 0.021 . . . . . . 118 GLN N 0.943 0.014 . . . . . . 119 HIS N 0.897 0.019 . . . . . . 120 ALA N 0.944 0.012 . . . . . . 122 VAL N 0.891 0.014 . . . . . . 123 PHE N 0.888 0.026 . . . . . . 124 PHE N 0.902 0.012 . . . . . . 125 LYS N 0.921 0.013 . . . . . . 127 VAL N 0.922 0.019 . . . . . . 128 SER N 0.926 0.016 . . . . . . 129 GLN N 0.898 0.017 0.929 0.011 0.966 0.015 0.644 0.443 130 ASN N 0.828 0.050 0.876 0.047 0.946 0.027 0.969 0.501 131 ARG N 0.813 0.015 0.854 0.011 0.953 0.013 0.739 0.237 132 GLU N 0.852 0.013 0.870 0.010 0.979 0.010 0.386 0.186 133 TYR N 0.879 0.015 . . . . . . 134 PHE N 0.881 0.012 0.900 0.010 0.979 0.009 0.753 0.390 135 LYS N 0.885 0.019 . . . . . . 136 ILE N 0.902 0.021 . . . . . . 137 THR N 0.888 0.030 . . . . . . 138 LEU N 0.911 0.015 . . . . . . 139 TYR N 0.877 0.014 . . . . . . 140 GLY N 0.906 0.016 . . . . . . 141 ARG N 0.912 0.014 . . . . . . 142 THR N 0.923 0.010 . . . . . . 143 LYS N 0.844 0.014 0.854 0.017 0.968 0.018 . . 144 GLU N 0.775 0.019 0.804 0.019 0.964 0.007 0.310 0.082 145 LEU N 0.810 0.031 0.853 0.031 0.950 0.011 0.260 0.051 146 THR N 0.611 0.035 0.695 0.027 0.880 0.037 1.189 0.193 147 SER N 0.861 0.023 0.905 0.017 0.951 0.018 2.201 1.700 148 GLU N 0.945 0.012 . . . . . . 150 LYS N 0.886 0.013 0.908 0.010 0.976 0.009 0.648 0.448 151 GLU N 0.928 0.013 . . . . . . 152 ASN N 0.936 0.012 . . . . . . 153 PHE N 0.932 0.012 . . . . . . 154 ILE N 0.941 0.010 . . . . . . 155 ARG N 0.933 0.013 . . . . . . 156 PHE N 0.947 0.015 . . . . . . 157 SER N 0.930 0.011 . . . . . . 158 LYS N 0.967 0.013 . . . . . . 159 SER N 0.872 0.019 . . . . . . 160 LEU N 0.932 0.013 . . . . . . 161 GLY N 0.888 0.013 . . . . . . 162 LEU N 0.899 0.019 . . . . . . 165 ASN N 0.819 0.012 0.882 0.011 0.928 0.008 3.042 0.872 167 ILE N 0.885 0.017 . . . . . . 168 VAL N 0.904 0.014 . . . . . . 169 PHE N 0.907 0.011 . . . . . . 171 VAL N 0.833 0.049 0.877 0.043 0.950 0.031 1.245 0.484 173 ILE N 0.834 0.040 . . . . . . 175 GLN N 0.738 0.018 0.806 0.013 0.916 0.017 0.353 0.125 176 CYS N 0.878 0.032 . . . . . . 178 ASP N 0.889 0.022 . . . . . . 179 GLY N 0.342 0.009 0.705 0.011 0.485 0.010 0.784 0.011 32 TRP NE1 0.793 0.013 . . . . . . 80 TRP NE1 0.534 0.015 0.706 0.011 0.757 0.017 1.877 0.138 110 ARG NE 0.456 0.068 0.552 0.059 0.825 0.084 1.536 0.666 141 ARG NE 0.937 0.040 . . . . . . 155 ARG NE 0.134 0.016 0.464 0.022 0.288 0.031 0.444 0.018 stop_ save_ save_secondary_structure_features _Saveframe_category secondary_structure_features loop_ _Selection_method_data '3JHNHA coupling constants' 'chemical shifts' 'NOE patterns' stop_ loop_ _Mol_system_component_name _Beginning_residue_seq_code _Last_residue_seq_code _Secondary_structure_name _Secondary_structure_type _Selection_method _Details $HNGAL 25 28 '3-10 helix' '3-10 helix' author-determined . $HNGAL 30 39 'strand B1' beta-strand author-determined . $HNGAL 53 60 'strand B2' beta-strand author-determined . $HNGAL 64 73 'strand B3' beta-strand author-determined . $HNGAL 77 86 'strand B4' beta-strand author-determined . $HNGAL 92 95 'strand B5' beta-strand author-determined . $HNGAL 104 115 'strand B6' beta-strand author-determined . $HNGAL 119 128 'strand B7' beta-strand author-determined . $HNGAL 131 141 'strand B8' beta-strand author-determined . $HNGAL 149 159 'helix A1' alpha-helix author-determined . $HNGAL 166 169 'strand B9' beta-strand author-determined . stop_ save_