data_4267 ####################### # 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. ; _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 2.1.1 _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_ _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_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 heteronucl_NOE 9 T1_relaxation 3 T2_relaxation 3 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 "order parameters" 152 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-08-15 . BMRB 'chemical shift for LYS 135 CE corrected' 2011-03-03 . BMRB 'sequence numbering corrected in several data loops' 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 _CAS_abstract_code . _MEDLINE_UI_code 99272561 _PubMed_ID ? 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 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 139 _Page_last 157 _Year 1999 _Details . loop_ _Keyword 'coupling constants' lipocalin NGAL NMR protein 'resonance assignment' 'secondary structure' 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 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HNGAL $HNGAL stop_ _System_molecular_weight 20660 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'reduced and oxidized present' loop_ _Biological_function 'chemotactic recognition' 'multimeric matrix-metalloproteinase component' 'small molecule transport' stop_ _Database_query_date . _Details . 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 _Mol_thiol_state . _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 . _Sequence_homology_query_revised_last_date 2015-08-25 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 1DFV "Crystal Structure Of Human Neutrophil Gelatinase Associated Lipocalin Monomer" 98.88 177 100.00 100.00 1.93e-127 PDB 1L6M "Neutrophil Gelatinase-Associated Lipocalin Is A Novel Bacteriostatic Agent That Interferes With Siderophore- Mediated Iron Acqu" 99.44 180 99.44 99.44 3.43e-127 PDB 1NGL "Human Neutrophil Gelatinase-Associated Lipocalin (Hngal), Regularised Average Nmr Structure" 100.00 179 100.00 100.00 1.90e-129 PDB 1QQS "Neutrophil Gelatinase Associated Lipocalin Homodimer" 97.21 174 97.70 97.70 4.05e-121 PDB 1X71 "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Trencam-3,2-Hopo, A Cepabactin Analogue" 99.44 178 99.44 99.44 3.00e-127 PDB 1X89 "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Carboxymycobactin S" 99.44 178 99.44 99.44 3.00e-127 PDB 1X8U "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Carboxymycobactin T" 99.44 178 99.44 99.44 3.00e-127 PDB 3BY0 "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) W79a-R81a Complexed With Ferric Enterobactin" 99.44 198 98.31 98.31 1.13e-124 PDB 3CBC "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Y106f Complexed With Ferric Enterobactin" 99.44 198 98.88 99.44 1.40e-126 PDB 3CMP "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K125a Mutant Complexed With Ferric Enterobactin" 99.44 198 98.88 98.88 1.52e-126 PDB 3FW4 "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Ferric Catechol" 99.44 178 99.44 99.44 3.00e-127 PDB 3FW5 "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Ferric 4-Methyl-Catechol" 99.44 178 99.44 99.44 3.00e-127 PDB 3HWD "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K125a-K Mutant Complexed With Ferric Enterobactin" 99.44 198 98.31 98.31 6.10e-126 PDB 3HWE "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Bishacam" 99.44 198 99.44 99.44 3.88e-127 PDB 3HWF "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Trencam2-Hopo" 99.44 198 99.44 99.44 3.88e-127 PDB 3HWG "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complex Fe-Trencam-Hopo2" 99.44 198 99.44 99.44 3.88e-127 PDB 3I0A "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) K134a M Complexed With Ferric Enterobactin" 99.44 198 98.88 98.88 1.52e-126 PDB 3K3L "Crystal Structure Of Siderocalin (Ngal, Lipocalin 2) Complexed With Apo Enterobactin" 99.44 178 99.44 99.44 3.00e-127 PDB 3PEC "Siderocalin Recognitin Of Carboxymycobactins: Interference By The Immune System In Intracellular Iron Acquisition By Mycobacter" 99.44 178 99.44 99.44 3.00e-127 PDB 3PED "Siderocalin Recognitin Of Carboxymycobactins: Interference By The Immune System In Intracellular Iron Acquisition By Mycobacter" 99.44 178 99.44 99.44 3.00e-127 PDB 3T1D "The Mutant Structure Of Human Siderocalin W79a, R81a, Y106f Bound To Enterobactin" 99.44 198 97.75 98.31 4.06e-124 PDB 3TF6 "Crystal Structure Of Neutrophil Gelatinase-associated Lipocalin (c87s Mutant) In Complex With Europium And The Siderophore Anal" 99.44 179 99.44 99.44 3.74e-127 PDB 3TZS "Crystal Structure Of Neutrophil Gelatinase-associated Lipocalin Ngal (c87s Mutant) In Complex With Fragment 1026, Phenylurea" 99.44 183 99.44 99.44 4.11e-127 PDB 3U03 "The Structure Of Human Siderocalin Bound To The Bacterial Siderophore Pyochelin" 99.44 198 99.44 99.44 3.88e-127 PDB 3U0D "The Structure Of Human Siderocalin Bound To The Bacterial Siderophore 2,3-dhba" 99.44 198 99.44 99.44 3.88e-127 PDB 4K19 "The Structure Of Human Siderocalin Bound To The Bacterial Siderophore Fluvibactin" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZFX "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZHC "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZHD "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZHF "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZHG "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 PDB 4ZHH "Siderocalin-mediated Recognition And Cellular Uptake Of Actinides" 99.44 180 99.44 99.44 3.43e-127 DBJ BAG63166 "unnamed protein product [Homo sapiens]" 99.44 198 97.19 97.19 4.59e-123 DBJ BAH14588 "unnamed protein product [Homo sapiens]" 99.44 198 97.19 97.19 4.80e-123 DBJ BAJ21166 "lipocalin 2 [synthetic construct]" 99.44 198 100.00 100.00 2.50e-128 EMBL CAA58127 "neutrophil gelatinase associated lipocalin [Homo sapiens]" 99.44 198 100.00 100.00 2.50e-128 EMBL CAA67574 "NGAL [Homo sapiens]" 99.44 198 99.44 99.44 2.77e-127 EMBL CAG46889 "LCN2 [Homo sapiens]" 99.44 198 100.00 100.00 1.92e-128 GB AAB26529 "neutrophil gelatinase-associated lipocalin, NGAL [human, neutrophils, Peptide, 178 aa]" 99.44 178 99.44 100.00 8.07e-128 GB AAD14168 "neutrophil lipocalin, partial [Homo sapiens]" 99.44 178 100.00 100.00 2.27e-128 GB AAH33089 "Lipocalin 2 [Homo sapiens]" 99.44 198 100.00 100.00 2.50e-128 GB AAV38204 "lipocalin 2 (oncogene 24p3) [synthetic construct]" 99.44 199 100.00 100.00 2.22e-128 GB AAX36313 "lipocalin 2 [synthetic construct]" 99.44 198 100.00 100.00 2.50e-128 REF NP_005555 "neutrophil gelatinase-associated lipocalin precursor [Homo sapiens]" 99.44 198 100.00 100.00 2.50e-128 REF XP_003822366 "PREDICTED: neutrophil gelatinase-associated lipocalin [Pan paniscus]" 99.44 198 99.44 99.44 8.91e-127 REF XP_004048725 "PREDICTED: neutrophil gelatinase-associated lipocalin [Gorilla gorilla gorilla]" 99.44 198 99.44 99.44 3.88e-127 REF XP_520287 "PREDICTED: neutrophil gelatinase-associated lipocalin [Pan troglodytes]" 99.44 198 98.88 99.44 2.78e-126 SP P80188 "RecName: Full=Neutrophil gelatinase-associated lipocalin; Short=NGAL; AltName: Full=25 kDa alpha-2-microglobulin-related subuni" 99.44 198 100.00 100.00 2.50e-128 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_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_all _Saveframe_category sample_conditions _Details . 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 _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TMS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.25144953 TMS H 1 'methyl protons' ppm 0.0 internal direct . . . . TMS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.10132912 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; 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 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HE H 2.14 . 1 2 . 1 MET CE C 16.6 . 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 178.11 . 1 9 . 2 GLN CA C 55.71 . 1 10 . 2 GLN CB C 29.53 . 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 176.41 . 1 16 . 3 ASP CA C 54.22 . 1 17 . 3 ASP CB C 41.19 . 1 18 . 3 ASP N N 122.81 . 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 175.11 . 1 24 . 4 SER CA C 58.42 . 1 25 . 4 SER CB C 63.58 . 1 26 . 4 SER N N 116.81 . 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 174.81 . 1 32 . 5 THR CA C 62.03 . 1 33 . 5 THR CB C 69.52 . 1 34 . 5 THR CG2 C 22.30 . 1 35 . 5 THR N N 115.32 . 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 174.17 . 1 41 . 6 SER CA C 58.34 . 1 42 . 6 SER CB C 63.73 . 1 43 . 6 SER N N 117.63 . 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 175.75 . 1 49 . 7 ASP CA C 54.19 . 1 50 . 7 ASP CB C 40.95 . 1 51 . 7 ASP N N 122.50 . 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 177.42 . 1 60 . 8 LEU CA C 54.05 . 1 61 . 8 LEU CB C 43.33 . 1 62 . 8 LEU CG C 27.3 . 1 63 . 8 LEU CD1 C 24.5 . 2 64 . 8 LEU CD2 C 23.8 . 2 65 . 8 LEU N N 122.64 . 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 59.64 . 1 74 . 9 ILE CB C 39.72 . 1 75 . 9 ILE CG1 C 24.1 . 1 76 . 9 ILE CG2 C 16.0 . 1 77 . 9 ILE CD1 C 13.7 . 1 78 . 9 ILE N N 128.27 . 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 175.85 . 1 87 . 10 PRO CA C 62.28 . 1 88 . 10 PRO CB C 32.15 . 1 89 . 10 PRO CG C 27.4 . 1 90 . 10 PRO CD C 51.1 . 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 49.60 . 1 95 . 11 ALA CB C 16.28 . 1 96 . 11 ALA N N 121.75 . 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 59.9 . 1 105 . 12 PRO CG C 26.8 . 1 106 . 12 PRO CD C 48.0 . 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 178.11 . 1 115 . 13 PRO CA C 61.93 . 1 116 . 13 PRO CB C 31.19 . 1 117 . 13 PRO CG C 30.1 . 1 118 . 13 PRO CD C 49.66 . 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 178.65 . 1 127 . 14 LEU CA C 56.88 . 1 128 . 14 LEU CB C 40.24 . 1 129 . 14 LEU CG C 26.7 . 1 130 . 14 LEU CD1 C 22.9 . 2 131 . 14 LEU CD2 C 24.8 . 2 132 . 14 LEU N N 122.64 . 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 176.04 . 1 138 . 15 SER CA C 59.61 . 1 139 . 15 SER CB C 61.66 . 1 140 . 15 SER N N 112.28 . 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 174.48 . 1 152 . 16 LYS CA C 55.79 . 1 153 . 16 LYS CB C 32.62 . 1 154 . 16 LYS CG C 24.1 . 1 155 . 16 LYS CE C 46.2 . 1 156 . 16 LYS N N 120.22 . 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 59.05 . 1 163 . 17 VAL CB C 31.22 . 1 164 . 17 VAL CG1 C 22.6 . 1 165 . 17 VAL CG2 C 19.0 . 1 166 . 17 VAL N N 120.27 . 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 171.63 . 1 175 . 18 PRO CA C 62.85 . 1 176 . 18 PRO CB C 32.02 . 1 177 . 18 PRO CG C 26.9 . 1 178 . 18 PRO CD C 51.26 . 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 177.27 . 1 187 . 19 LEU CA C 51.94 . 1 188 . 19 LEU CB C 46.05 . 1 189 . 19 LEU CG C 27.2 . 1 190 . 19 LEU CD1 C 25.8 . 2 191 . 19 LEU CD2 C 26.0 . 2 192 . 19 LEU N N 116.94 . 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 174.86 . 1 202 . 20 GLN CA C 55.38 . 1 203 . 20 GLN CB C 28.43 . 1 204 . 20 GLN N N 127.49 . 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 176.78 . 1 215 . 21 GLN CA C 56.16 . 1 216 . 21 GLN CB C 29.05 . 1 217 . 21 GLN CG C 33.59 . 1 218 . 21 GLN CD C 180.46 . 1 219 . 21 GLN N N 130.35 . 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 175.30 . 1 228 . 22 ASN CA C 53.48 . 1 229 . 22 ASN CB C 37.14 . 1 230 . 22 ASN CG C 178.23 . 1 231 . 22 ASN N N 120.60 . 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 175.55 . . 242 . 23 PHE CA C 59.75 . 1 243 . 23 PHE CB C 39.53 . 1 244 . 23 PHE N N 117.83 . 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 174.02 . 1 254 . 24 GLN CA C 52.72 . 1 255 . 24 GLN CB C 29.05 . 1 256 . 24 GLN CG C 32.2 . 1 257 . 24 GLN CD C 180.56 . 1 258 . 24 GLN N N 128.24 . 1 259 . 24 GLN NE2 N 114.3 . 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 180.67 . 1 265 . 25 ASP CA C 55.94 . 1 266 . 25 ASP CB C 38.57 . 1 267 . 25 ASP N N 126.45 . 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 177.13 . 1 275 . 26 ASN CA C 55.48 . 1 276 . 26 ASN CB C 37.14 . 1 277 . 26 ASN CG C 176.19 . 1 278 . 26 ASN N N 121.22 . 1 279 . 26 ASN ND2 N 114.2 . 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 176.24 . 1 289 . 27 GLN CA C 56.78 . 1 290 . 27 GLN CB C 28.81 . 1 291 . 27 GLN CG C 33.4 . 1 292 . 27 GLN CD C 178.95 . 1 293 . 27 GLN N N 117.56 . 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 173.04 . 1 304 . 28 PHE CA C 59.51 . 1 305 . 28 PHE CB C 41.43 . 1 306 . 28 PHE N N 119.51 . 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 174.66 . 1 316 . 29 GLN CA C 56.02 . 1 317 . 29 GLN CB C 31.91 . 1 318 . 29 GLN CD C 180.4 . 1 319 . 29 GLN N N 109.75 . 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 172.40 . 1 325 . 30 GLY CA C 43.31 . 1 326 . 30 GLY N N 109.71 . 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 175.40 . 1 332 . 31 LYS CA C 56.86 . 1 333 . 31 LYS CB C 32.38 . 1 334 . 31 LYS N N 120.60 . 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 174.52 . 1 345 . 32 TRP CA C 54.89 . 1 346 . 32 TRP CB C 31.93 . 1 347 . 32 TRP CD1 C 127.7 . 1 348 . 32 TRP CZ2 C 118.9 . 1 349 . 32 TRP CH2 C 122.0 . 1 350 . 32 TRP N N 130.53 . 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 176.53 . 1 361 . 33 TYR CA C 58.57 . 1 362 . 33 TYR CB C 39.05 . 1 363 . 33 TYR CD1 C 133.1 . 1 364 . 33 TYR CD2 C 133.1 . 1 365 . 33 TYR N N 120.80 . 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 173.24 . 1 372 . 34 VAL CA C 64.31 . 1 373 . 34 VAL CB C 30.24 . 1 374 . 34 VAL CG1 C 21.8 . 1 375 . 34 VAL CG2 C 21.8 . 1 376 . 34 VAL N N 123.12 . 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 176.68 . 1 383 . 35 VAL CA C 62.68 . 1 384 . 35 VAL CB C 33.10 . 1 385 . 35 VAL CG1 C 21.3 . 2 386 . 35 VAL CG2 C 21.5 . 2 387 . 35 VAL N N 106.74 . 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 170.19 . 1 392 . 36 GLY CA C 45.11 . 1 393 . 36 GLY N N 106.74 . 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 173.09 . 1 402 . 37 LEU CA C 54.47 . 1 403 . 37 LEU CB C 47.62 . 1 404 . 37 LEU CG C 26.7 . 1 405 . 37 LEU CD1 C 24.6 . 1 406 . 37 LEU CD2 C 25.0 . 1 407 . 37 LEU N N 125.14 . 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 176.54 . 1 412 . 38 ALA CA C 50.14 . 1 413 . 38 ALA CB C 24.77 . 1 414 . 38 ALA N N 125.45 . 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 173.29 . 1 419 . 39 GLY CA C 47.08 . 1 420 . 39 GLY N N 105.61 . 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 175.30 . 1 428 . 40 ASN CA C 54.72 . 1 429 . 40 ASN CB C 37.14 . 1 430 . 40 ASN N N 117.16 . 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 175.95 . 1 436 . 41 ALA CA C 50.95 . 1 437 . 41 ALA CB C 18.82 . 1 438 . 41 ALA N N 124.77 . 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 173.34 . 1 447 . 42 ILE CA C 59.52 . 1 448 . 42 ILE CB C 38.33 . 1 449 . 42 ILE CG2 C 17.3 . 1 450 . 42 ILE CD1 C 11.8 . 1 451 . 42 ILE N N 121.31 . 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 176.59 . 1 460 . 43 LEU CA C 52.83 . 1 461 . 43 LEU CB C 44.65 . 1 462 . 43 LEU CG C 27.1 . 1 463 . 43 LEU CD1 C 24.5 . 2 464 . 43 LEU CD2 C 23.9 . 2 465 . 43 LEU N N 124.79 . 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 56.96 . 1 475 . 44 ARG CB C 30.64 . 1 476 . 44 ARG N N 123.79 . 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 55.43 . 1 482 . 45 GLU CB C 30.42 . 1 483 . 45 GLU N N 126.5 . 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 177.08 . 1 489 . 46 ASP CA C 55.89 . 1 490 . 46 ASP CB C 40.95 . 1 491 . 46 ASP N N 123.68 . 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 176.34 . 1 503 . 47 LYS CA C 57.01 . 1 504 . 47 LYS CB C 32.30 . 1 505 . 47 LYS CG C 25.6 . 1 506 . 47 LYS CD C 25.2 . 1 507 . 47 LYS CE C 42.3 . 1 508 . 47 LYS N N 118.18 . 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 52.18 . 1 514 . 48 ASP CB C 32.40 . 1 515 . 48 ASP N N 118.69 . 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 27.0 . 1 523 . 49 PRO CD C 50.2 . 1 524 . 51 LYS H H 8.63 . 1 525 . 51 LYS HA H 4.68 . 1 526 . 51 LYS CA C 55.46 . 1 527 . 51 LYS CB C 33.82 . 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 58.43 . 1 536 . 52 MET CB C 34.31 . 1 537 . 52 MET CE C 17.25 . 1 538 . 52 MET N N 123.27 . 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 172.20 . 1 548 . 53 TYR CA C 54.44 . 1 549 . 53 TYR CB C 40.48 . 1 550 . 53 TYR N N 118.40 . 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 175.85 . 1 555 . 54 ALA CA C 49.96 . 1 556 . 54 ALA CB C 22.86 . 1 557 . 54 ALA N N 120.75 . 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 171.96 . 1 563 . 55 THR CA C 61.41 . 1 564 . 55 THR CB C 72.17 . 1 565 . 55 THR CG2 C 20.6 . 1 566 . 55 THR N N 116.71 . 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 175.40 . 1 575 . 56 ILE CA C 60.22 . 1 576 . 56 ILE CB C 40.00 . 1 577 . 56 ILE CG2 C 18.7 . 1 578 . 56 ILE CD1 C 14.4 . 1 579 . 56 ILE N N 127.71 . 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 176.14 . 1 589 . 57 TYR CA C 57.43 . 1 590 . 57 TYR CB C 39.91 . 1 591 . 57 TYR CD1 C 131.7 . 1 592 . 57 TYR CD2 C 131.7 . 1 593 . 57 TYR CE1 C 127.7 . 1 594 . 57 TYR CE2 C 127.7 . 1 595 . 57 TYR N N 127.91 . 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 174.66 . 1 603 . 58 GLU CA C 55.19 . 1 604 . 58 GLU CB C 32.38 . 1 605 . 58 GLU N N 125.98 . 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 176.29 . 1 614 . 59 LEU CA C 55.23 . 1 615 . 59 LEU CB C 43.52 . 1 616 . 59 LEU CG C 26.3 . 1 617 . 59 LEU CD1 C 22.6 . 1 618 . 59 LEU CD2 C 22.8 . 1 619 . 59 LEU N N 130.13 . 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 179.05 . 1 627 . 60 LYS CA C 54.27 . 1 628 . 60 LYS CB C 32.38 . 1 629 . 60 LYS N N 127.40 . 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 59.24 . 1 637 . 61 GLU CB C 28.88 . 1 638 . 61 GLU N N 121.95 . 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 176.59 . 1 644 . 62 ASP CA C 53.09 . 1 645 . 62 ASP CB C 39.29 . 1 646 . 62 ASP N N 116.45 . 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 174.27 . 1 658 . 63 LYS CA C 58.45 . 1 659 . 63 LYS CB C 28.34 . 1 660 . 63 LYS CG C 25.4 . 1 661 . 63 LYS CE C 42.1 . 1 662 . 63 LYS N N 111.20 . 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 173.14 . 1 668 . 64 SER CA C 57.94 . 1 669 . 64 SER CB C 65.23 . 1 670 . 64 SER N N 111.75 . 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 177.42 . 1 680 . 65 TYR CA C 56.32 . 1 681 . 65 TYR CB C 42.14 . 1 682 . 65 TYR CD1 C 132.4 . 1 683 . 65 TYR CD2 C 132.4 . 1 684 . 65 TYR CE1 C 131.7 . 1 685 . 65 TYR CE2 C 131.7 . 1 686 . 65 TYR N N 113.30 . 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 174.71 . 1 694 . 66 ASN CA C 53.45 . 1 695 . 66 ASN CB C 39.76 . 1 696 . 66 ASN CG C 175.52 . 1 697 . 66 ASN N N 121.15 . 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 175.21 . 1 705 . 67 VAL CA C 61.32 . 1 706 . 67 VAL CB C 32.05 . 1 707 . 67 VAL CG1 C 20.0 . 1 708 . 67 VAL CG2 C 20.4 . 1 709 . 67 VAL N N 130.24 . 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 175.11 . 1 715 . 68 THR CA C 61.48 . 1 716 . 68 THR CB C 70.47 . 1 717 . 68 THR CG2 C 20.7 . 1 718 . 68 THR N N 125.19 . 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 171.66 . 1 724 . 69 SER CA C 57.82 . 1 725 . 69 SER CB C 64.52 . 1 726 . 69 SER N N 123.88 . 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 173.58 . 1 733 . 70 VAL CA C 60.62 . 1 734 . 70 VAL CB C 33.81 . 1 735 . 70 VAL CG1 C 20.8 . 1 736 . 70 VAL CG2 C 20.8 . 1 737 . 70 VAL N N 125.28 . 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 174.91 . 1 746 . 71 LEU CA C 53.47 . 1 747 . 71 LEU CB C 45.71 . 1 748 . 71 LEU CG C 27.4 . 1 749 . 71 LEU CD1 C 25.5 . 1 750 . 71 LEU CD2 C 25.7 . 1 751 . 71 LEU N N 123.88 . 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 174.97 . 1 761 . 72 PHE CA C 55.52 . 1 762 . 72 PHE CB C 40.10 . 1 763 . 72 PHE N N 123.01 . 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 174.71 . 1 773 . 73 ARG CA C 54.94 . 1 774 . 73 ARG CB C 32.40 . 1 775 . 73 ARG CG C 24.8 . 1 776 . 73 ARG CD C 43.9 . 1 777 . 73 ARG N N 127.60 . 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 177.07 . 1 783 . 74 LYS CA C 57.2 . 1 784 . 74 LYS CB C 30.0 . 1 785 . 74 LYS N N 123.36 . 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 174.91 . 1 797 . 75 LYS CA C 57.58 . 1 798 . 75 LYS CB C 30.24 . 1 799 . 75 LYS CD C 25.4 . 1 800 . 75 LYS CE C 42.2 . 1 801 . 75 LYS N N 109.33 . 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 173.83 . 1 813 . 76 LYS CA C 54.58 . 1 814 . 76 LYS CB C 35.48 . 1 815 . 76 LYS CE C 42.2 . 1 816 . 76 LYS N N 119.40 . 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 173.58 . 1 822 . 77 CYS CA C 52.87 . 1 823 . 77 CYS CB C 36.59 . 1 824 . 77 CYS N N 117.74 . 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 173.63 . 1 830 . 78 ASP CA C 52.39 . 1 831 . 78 ASP CB C 44.76 . 1 832 . 78 ASP N N 127.11 . 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 175.60 . 1 842 . 79 TYR CA C 56.38 . 1 843 . 79 TYR CB C 40.95 . 1 844 . 79 TYR CD1 C 133.1 . 1 845 . 79 TYR CD2 C 133.1 . 1 846 . 79 TYR N N 118.25 . 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 174.99 . 1 856 . 80 TRP CA C 54.91 . 1 857 . 80 TRP CB C 31.06 . 1 858 . 80 TRP CD1 C 125.6 . 1 859 . 80 TRP CZ2 C 113.8 . 1 860 . 80 TRP CH2 C 124.2 . 1 861 . 80 TRP N N 124.94 . 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 175.21 . 1 871 . 81 ILE CA C 60.73 . 1 872 . 81 ILE CB C 40.00 . 1 873 . 81 ILE CG1 C 28.2 . 1 874 . 81 ILE CG2 C 17.5 . 1 875 . 81 ILE CD1 C 13.7 . 1 876 . 81 ILE N N 130.09 . 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 173.14 . 1 882 . 82 ARG CA C 54.34 . 1 883 . 82 ARG CB C 33.73 . 1 884 . 82 ARG N N 126.67 . 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 174.42 . 1 890 . 83 THR CA C 60.87 . 1 891 . 83 THR CB C 71.04 . 1 892 . 83 THR CG2 C 21.7 . 1 893 . 83 THR N N 114.77 . 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 174.86 . 1 903 . 84 PHE CA C 52.01 . 1 904 . 84 PHE CB C 39.29 . 1 905 . 84 PHE CD1 C 128.6 . 1 906 . 84 PHE CD2 C 128.6 . 1 907 . 84 PHE CE1 C 129.1 . 1 908 . 84 PHE CE2 C 129.1 . 1 909 . 84 PHE N N 126.56 . 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 58.50 . 1 916 . 85 VAL CB C 32.40 . 1 917 . 85 VAL CG1 C 20.2 . 1 918 . 85 VAL CG2 C 21.3 . 1 919 . 85 VAL N N 121.44 . 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 177.37 . 1 926 . 86 PRO CA C 64.48 . 1 927 . 86 PRO CB C 32.62 . 1 928 . 86 PRO CD C 50.8 . 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 174.52 . 1 933 . 87 GLY CA C 43.05 . 1 934 . 87 GLY N N 111.57 . 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 174.37 . 1 940 . 88 CYS CA C 57.26 . 1 941 . 88 CYS CB C 40.24 . 1 942 . 88 CYS N N 119.88 . 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 52.36 . 1 952 . 89 GLN CB C 30.05 . 1 953 . 89 GLN CG C 32.95 . 1 954 . 89 GLN CD C 180.06 . 1 955 . 89 GLN N N 116.25 . 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 177.32 . 1 965 . 90 PRO CA C 63.23 . 1 966 . 90 PRO CB C 31.67 . 1 967 . 90 PRO CG C 28.0 . 1 968 . 90 PRO CD C 50.8 . 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 171.02 . 1 973 . 91 GLY CA C 44.17 . 1 974 . 91 GLY N N 112.73 . 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 176.78 . 1 982 . 92 GLU CA C 53.57 . 1 983 . 92 GLU CB C 33.57 . 1 984 . 92 GLU CG C 38.6 . 1 985 . 92 GLU N N 118.45 . 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 174.47 . 1 995 . 93 PHE CA C 56.08 . 1 996 . 93 PHE CB C 43.81 . 1 997 . 93 PHE CD1 C 131.2 . 1 998 . 93 PHE CD2 C 131.2 . 1 999 . 93 PHE N N 120.27 . 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 173.88 . 1 1005 . 94 THR CA C 59.34 . 1 1006 . 94 THR CB C 70.93 . 1 1007 . 94 THR CG2 C 20.1 . 1 1008 . 94 THR N N 112.81 . 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 177.52 . 1 1017 . 95 LEU CA C 54.30 . 1 1018 . 95 LEU CB C 43.81 . 1 1019 . 95 LEU CD1 C 23.7 . 1 1020 . 95 LEU CD2 C 25.7 . 1 1021 . 95 LEU N N 122.72 . 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 174.12 . 1 1026 . 96 GLY CA C 45.72 . 1 1027 . 96 GLY N N 113.66 . 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 176.78 . 1 1035 . 97 ASN CA C 53.36 . 1 1036 . 97 ASN CB C 36.91 . 1 1037 . 97 ASN CG C 178.66 . 1 1038 . 97 ASN N N 119.00 . 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 176.54 . 1 1048 . 98 ILE CA C 65.41 . 1 1049 . 98 ILE CB C 38.55 . 1 1050 . 98 ILE CG1 C 29.8 . 1 1051 . 98 ILE CG2 C 16.5 . 1 1052 . 98 ILE CD1 C 14.1 . 1 1053 . 98 ILE N N 119.75 . 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 177.67 . 1 1065 . 99 LYS CA C 57.73 . 1 1066 . 99 LYS CB C 31.19 . 1 1067 . 99 LYS CG C 25.3 . 1 1068 . 99 LYS CD C 29.0 . 1 1069 . 99 LYS CE C 42.1 . 1 1070 . 99 LYS N N 118.60 . 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 172.74 . 1 1076 . 100 SER CA C 59.41 . 1 1077 . 100 SER CB C 63.33 . 1 1078 . 100 SER N N 114.48 . 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 55.01 . 1 1088 . 101 TYR CB C 37.96 . 1 1089 . 101 TYR CD1 C 134.1 . 1 1090 . 101 TYR CD2 C 134.1 . 1 1091 . 101 TYR CE1 C 132.9 . 1 1092 . 101 TYR CE2 C 132.9 . 1 1093 . 101 TYR N N 123.52 . 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 178.69 . 1 1100 . 102 PRO CA C 63.80 . 1 1101 . 102 PRO CB C 31.67 . 1 1102 . 102 PRO CD C 50.6 . 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 173.78 . 1 1107 . 103 GLY CA C 45.69 . 1 1108 . 103 GLY N N 112.28 . 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 176.83 . 1 1117 . 104 LEU CA C 54.98 . 1 1118 . 104 LEU CB C 43.10 . 1 1119 . 104 LEU CD1 C 26.3 . 1 1120 . 104 LEU CD2 C 25.3 . 1 1121 . 104 LEU N N 123.61 . 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 175.01 . 1 1127 . 105 THR CA C 62.95 . 1 1128 . 105 THR CB C 69.53 . 1 1129 . 105 THR CG2 C 20.1 . 1 1130 . 105 THR N N 116.92 . 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 172.50 . 1 1136 . 106 SER CA C 57.88 . 1 1137 . 106 SER CB C 64.46 . 1 1138 . 106 SER N N 113.35 . 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 172.89 . 1 1148 . 107 TYR CA C 58.65 . 1 1149 . 107 TYR CB C 42.52 . 1 1150 . 107 TYR CD1 C 132.9 . 1 1151 . 107 TYR CD2 C 132.9 . 1 1152 . 107 TYR N N 124.72 . 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 173.09 . 1 1161 . 108 LEU CA C 54.16 . 1 1162 . 108 LEU CB C 46.32 . 1 1163 . 108 LEU CD1 C 26.0 . 2 1164 . 108 LEU CD2 C 24.1 . 2 1165 . 108 LEU N N 132.37 . 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 175.40 . 1 1172 . 109 VAL CA C 60.00 . 1 1173 . 109 VAL CB C 34.89 . 1 1174 . 109 VAL CG1 C 20.0 . 1 1175 . 109 VAL CG2 C 19.9 . 1 1176 . 109 VAL N N 124.90 . 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 174.33 . 1 1187 . 110 ARG CA C 54.97 . 1 1188 . 110 ARG CB C 35.15 . 1 1189 . 110 ARG CD C 42.0 . 1 1190 . 110 ARG N N 126.05 . 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 173.38 . 1 1198 . 111 VAL CA C 64.20 . 1 1199 . 111 VAL CB C 30.24 . 1 1200 . 111 VAL CG1 C 20.2 . 1 1201 . 111 VAL CG2 C 19.4 . 1 1202 . 111 VAL N N 127.45 . 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 175.65 . 1 1209 . 112 VAL CA C 63.23 . 1 1210 . 112 VAL CB C 32.86 . 1 1211 . 112 VAL CG1 C 20.5 . 1 1212 . 112 VAL CG2 C 21.7 . 1 1213 . 112 VAL N N 132.71 . 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 174.12 . 1 1219 . 113 SER CA C 55.77 . 1 1220 . 113 SER CB C 64.52 . 1 1221 . 113 SER N N 106.63 . 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 170.09 . 1 1227 . 114 THR CA C 60.53 . 1 1228 . 114 THR CB C 68.95 . 1 1229 . 114 THR CG2 C 17.3 . 1 1230 . 114 THR N N 118.29 . 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 178.31 . 1 1238 . 115 ASN CA C 51.34 . 1 1239 . 115 ASN CB C 38.57 . 1 1240 . 115 ASN N N 121.46 . 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 176.39 . 1 1251 . 116 TYR CA C 65.80 . 1 1252 . 116 TYR CB C 36.43 . 1 1253 . 116 TYR CD1 C 122.1 . 1 1254 . 116 TYR CD2 C 122.1 . 1 1255 . 116 TYR N N 115.47 . 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 175.90 . 1 1263 . 117 ASN CA C 52.57 . 1 1264 . 117 ASN CB C 38.81 . 1 1265 . 117 ASN CG C 176.65 . 1 1266 . 117 ASN N N 118.30 . 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 174.52 . 1 1277 . 118 GLN CA C 58.69 . 1 1278 . 118 GLN CB C 32.24 . 1 1279 . 118 GLN CG C 33.3 . 1 1280 . 118 GLN CD C 180.58 . 1 1281 . 118 GLN N N 117.74 . 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 175.06 . 1 1288 . 119 HIS CA C 55.05 . 1 1289 . 119 HIS CB C 36.91 . 1 1290 . 119 HIS N N 116.41 . 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 174.86 . 1 1295 . 120 ALA CA C 51.32 . 1 1296 . 120 ALA CB C 22.86 . 1 1297 . 120 ALA N N 121.53 . 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 174.96 . 1 1306 . 121 MET CA C 55.11 . 1 1307 . 121 MET CB C 36.43 . 1 1308 . 121 MET CG C 32.2 . 1 1309 . 121 MET CE C 15.9 . 1 1310 . 121 MET N N 120.03 . 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 171.71 . 1 1317 . 122 VAL CA C 61.56 . 1 1318 . 122 VAL CB C 34.29 . 1 1319 . 122 VAL CG1 C 23.4 . 1 1320 . 122 VAL CG2 C 22.6 . 1 1321 . 122 VAL N N 124.41 . 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 171.96 . 1 1331 . 123 PHE CA C 56.30 . 1 1332 . 123 PHE CB C 43.17 . 1 1333 . 123 PHE CD1 C 131.5 . 1 1334 . 123 PHE CD2 C 131.5 . 1 1335 . 123 PHE CE1 C 130.1 . 1 1336 . 123 PHE CE2 C 130.1 . 1 1337 . 123 PHE N N 127.85 . 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 174.71 . 1 1347 . 124 PHE CA C 55.23 . 1 1348 . 124 PHE CB C 42.14 . 1 1349 . 124 PHE CD1 C 132.7 . 1 1350 . 124 PHE CD2 C 132.7 . 1 1351 . 124 PHE N N 124.94 . 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 173.88 . 1 1363 . 125 LYS CA C 54.86 . 1 1364 . 125 LYS CB C 36.19 . 1 1365 . 125 LYS N N 120.91 . 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 173.48 . 1 1373 . 126 LYS CA C 54.09 . 1 1374 . 126 LYS CB C 36.67 . 1 1375 . 126 LYS N N 127.67 . 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 175.45 . 1 1382 . 127 VAL CA C 61.39 . 1 1383 . 127 VAL CB C 32.38 . 1 1384 . 127 VAL CG1 C 21.1 . 1 1385 . 127 VAL CG2 C 20.8 . 1 1386 . 127 VAL N N 124.39 . 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 175.26 . 1 1392 . 128 SER CA C 55.82 . 1 1393 . 128 SER CB C 64.76 . 1 1394 . 128 SER N N 120.31 . 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 175.30 . 1 1404 . 129 GLN CA C 57.11 . 1 1405 . 129 GLN CB C 26.19 . 1 1406 . 129 GLN CG C 33.9 . 1 1407 . 129 GLN CD C 178.61 . 1 1408 . 129 GLN N N 126.12 . 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 173.93 . 1 1417 . 130 ASN CA C 54.62 . 1 1418 . 130 ASN CB C 37.86 . 1 1419 . 130 ASN CG C 178.61 . 1 1420 . 130 ASN N N 109.42 . 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 173.58 . 1 1431 . 131 ARG CA C 54.77 . 1 1432 . 131 ARG CB C 32.62 . 1 1433 . 131 ARG N N 119.93 . 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 174.96 . 1 1441 . 132 GLU CA C 54.91 . 1 1442 . 132 GLU CB C 31.23 . 1 1443 . 132 GLU N N 120.11 . 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 175.30 . 1 1453 . 133 TYR CA C 56.53 . 1 1454 . 133 TYR CB C 40.95 . 1 1455 . 133 TYR CD1 C 128.2 . 1 1456 . 133 TYR CD2 C 128.2 . 1 1457 . 133 TYR N N 124.41 . 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 173.09 . 1 1467 . 134 PHE CA C 55.61 . 1 1468 . 134 PHE CB C 42.25 . 1 1469 . 134 PHE CD1 C 131.7 . 1 1470 . 134 PHE CD2 C 131.7 . 1 1471 . 134 PHE CE1 C 132.9 . 1 1472 . 134 PHE CE2 C 132.9 . 1 1473 . 134 PHE N N 117.71 . 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 173.14 . 1 1485 . 135 LYS CA C 54.20 . 1 1486 . 135 LYS CB C 37.17 . 1 1487 . 135 LYS CG C 25.5 . 1 1488 . 135 LYS CD C 38.6 . 1 1489 . 135 LYS CE C 41.9 . 1 1490 . 135 LYS N N 122.84 . 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 175.85 . 1 1499 . 136 ILE CA C 59.50 . 1 1500 . 136 ILE CB C 41.33 . 1 1501 . 136 ILE CG1 C 29.9 . 1 1502 . 136 ILE CG2 C 21.1 . 1 1503 . 136 ILE CD1 C 17.2 . 1 1504 . 136 ILE N N 122.42 . 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 172.74 . 1 1510 . 137 THR CA C 59.60 . 1 1511 . 137 THR CB C 70.94 . 1 1512 . 137 THR CG2 C 22.3 . 1 1513 . 137 THR N N 117.47 . 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 174.71 . 1 1521 . 138 LEU CA C 52.80 . 1 1522 . 138 LEU CB C 40.95 . 1 1523 . 138 LEU CG C 26.86 . 1 1524 . 138 LEU CD2 C 25.90 . 2 1525 . 138 LEU N N 126.78 . 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 176.67 . 1 1535 . 139 TYR CA C 52.31 . 1 1536 . 139 TYR CB C 41.19 . 1 1537 . 139 TYR CD1 C 131.9 . 1 1538 . 139 TYR CD2 C 131.9 . 1 1539 . 139 TYR CE1 C 129.8 . 1 1540 . 139 TYR CE2 C 129.8 . 1 1541 . 139 TYR N N 127.07 . 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 175.45 . 1 1546 . 140 GLY CA C 44.02 . 1 1547 . 140 GLY N N 105.61 . 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 177.08 . 1 1562 . 141 ARG CA C 55.70 . 1 1563 . 141 ARG CB C 30.32 . 1 1564 . 141 ARG CG C 29.0 . 1 1565 . 141 ARG CD C 42.0 . 1 1566 . 141 ARG N N 120.91 . 1 1567 . 141 ARG NE N 85.0 . 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 172.40 . 1 1573 . 142 THR CA C 59.01 . 1 1574 . 142 THR CB C 70.71 . 1 1575 . 142 THR CG2 C 21.5 . 1 1576 . 142 THR N N 109.04 . 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 175.06 . 1 1588 . 143 LYS CA C 57.66 . 1 1589 . 143 LYS CB C 32.62 . 1 1590 . 143 LYS CG C 24.66 . 1 1591 . 143 LYS CE C 41.92 . 1 1592 . 143 LYS N N 114.28 . 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 175.60 . 1 1600 . 144 GLU CA C 54.78 . 1 1601 . 144 GLU CB C 32.15 . 1 1602 . 144 GLU CG C 36.0 . 1 1603 . 144 GLU N N 113.97 . 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 175.75 . 1 1612 . 145 LEU CA C 52.80 . 1 1613 . 145 LEU CB C 45.95 . 1 1614 . 145 LEU CG C 23.7 . 1 1615 . 145 LEU CD1 C 23.9 . 1 1616 . 145 LEU CD2 C 23.9 . 1 1617 . 145 LEU N N 122.13 . 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 175.40 . 1 1623 . 146 THR CA C 60.34 . 1 1624 . 146 THR CB C 70.47 . 1 1625 . 146 THR CG2 C 22.3 . 1 1626 . 146 THR N N 109.98 . 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 176.59 . 1 1632 . 147 SER CA C 61.60 . 1 1633 . 147 SER CB C 62.2 . 1 1634 . 147 SER N N 117.29 . 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 178.84 . 1 1642 . 148 GLU CA C 59.80 . 1 1643 . 148 GLU CB C 29.05 . 1 1644 . 148 GLU CG C 36.4 . 1 1645 . 148 GLU N N 121.15 . 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 180.03 . 1 1654 . 149 LEU CA C 57.11 . 1 1655 . 149 LEU CB C 42.01 . 1 1656 . 149 LEU CG C 27.2 . 1 1657 . 149 LEU CD1 C 22.4 . 1 1658 . 149 LEU CD2 C 25.6 . 1 1659 . 149 LEU N N 120.29 . 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 178.46 . 1 1671 . 150 LYS CA C 61.02 . 1 1672 . 150 LYS CB C 31.67 . 1 1673 . 150 LYS N N 119.89 . 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 179.64 . 1 1681 . 151 GLU CA C 59.28 . 1 1682 . 151 GLU CB C 28.81 . 1 1683 . 151 GLU CG C 36.3 . 1 1684 . 151 GLU N N 118.82 . 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 177.72 . 1 1692 . 152 ASN CA C 56.32 . 1 1693 . 152 ASN CB C 38.10 . 1 1694 . 152 ASN CG C 178.61 . 1 1695 . 152 ASN N N 119.20 . 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 178.21 . 1 1706 . 153 PHE CA C 60.64 . 1 1707 . 153 PHE CB C 40.00 . 1 1708 . 153 PHE CD1 C 130.0 . 1 1709 . 153 PHE CD2 C 130.0 . 1 1710 . 153 PHE N N 122.30 . 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 177.37 . 1 1719 . 154 ILE CA C 66.41 . 1 1720 . 154 ILE CB C 38.10 . 1 1721 . 154 ILE CG1 C 29.7 . 1 1722 . 154 ILE CG2 C 17.0 . 1 1723 . 154 ILE CD1 C 17.6 . 1 1724 . 154 ILE N N 124.99 . 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 179.88 . 1 1735 . 155 ARG CA C 60.00 . 1 1736 . 155 ARG CB C 30.00 . 1 1737 . 155 ARG CG C 27.9 . 1 1738 . 155 ARG CD C 43.5 . 1 1739 . 155 ARG N N 119.02 . 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 178.85 . 1 1750 . 156 PHE CA C 60.45 . 1 1751 . 156 PHE CB C 39.05 . 1 1752 . 156 PHE CD1 C 131.7 . 1 1753 . 156 PHE CD2 C 131.7 . 1 1754 . 156 PHE N N 120.84 . 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 176.54 . 1 1760 . 157 SER CA C 63.96 . 1 1761 . 157 SER CB C 62.14 . 1 1762 . 157 SER N N 118.38 . 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 181.36 . 1 1774 . 158 LYS CA C 59.21 . 1 1775 . 158 LYS CB C 32.01 . 1 1776 . 158 LYS CD C 29.9 . 1 1777 . 158 LYS CE C 41.9 . 1 1778 . 158 LYS N N 121.39 . 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 174.81 . 1 1784 . 159 SER CA C 61.14 . 1 1785 . 159 SER CB C 62.14 . 1 1786 . 159 SER N N 119.27 . 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 175.70 . 1 1795 . 160 LEU CA C 53.91 . 1 1796 . 160 LEU CB C 40.24 . 1 1797 . 160 LEU CG C 25.5 . 1 1798 . 160 LEU CD1 C 26.3 . 1 1799 . 160 LEU CD2 C 21.5 . 1 1800 . 160 LEU N N 120.35 . 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 174.12 . 1 1805 . 161 GLY CA C 44.44 . 1 1806 . 161 GLY N N 104.68 . 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 51.76 . 1 1815 . 162 LEU CB C 41.48 . 1 1816 . 162 LEU CG C 26.1 . 1 1817 . 162 LEU CD1 C 25.8 . 1 1818 . 162 LEU CD2 C 22.3 . 1 1819 . 162 LEU N N 118.60 . 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 177.37 . 1 1828 . 163 PRO CA C 60.89 . 1 1829 . 163 PRO CB C 32.38 . 1 1830 . 163 PRO CG C 27.2 . 1 1831 . 163 PRO CD C 50.5 . 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 176.84 . 1 1839 . 164 GLU CA C 59.94 . 1 1840 . 164 GLU CB C 29.29 . 1 1841 . 164 GLU CG C 37.15 . 1 1842 . 164 GLU N N 117.72 . 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 174.55 . 1 1850 . 165 ASN CA C 54.13 . 1 1851 . 165 ASN CB C 35.95 . 1 1852 . 165 ASN CG C 178.61 . 1 1853 . 165 ASN N N 112.63 . 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 171.61 . 1 1860 . 166 HIS CA C 55.41 . 1 1861 . 166 HIS CB C 28.58 . 1 1862 . 166 HIS N N 118.13 . 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 174.62 . 1 1871 . 167 ILE CA C 61.31 . 1 1872 . 167 ILE CB C 39.76 . 1 1873 . 167 ILE CG1 C 30.3 . 1 1874 . 167 ILE CG2 C 18.1 . 1 1875 . 167 ILE CD1 C 15.9 . 1 1876 . 167 ILE N N 118.18 . 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 173.34 . 1 1883 . 168 VAL CA C 59.50 . 1 1884 . 168 VAL CB C 36.07 . 1 1885 . 168 VAL CG1 C 20.8 . 1 1886 . 168 VAL CG2 C 20.8 . 1 1887 . 168 VAL N N 123.97 . 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 55.06 . 1 1897 . 169 PHE CB C 38.95 . 1 1898 . 169 PHE CD1 C 132.9 . 1 1899 . 169 PHE CD2 C 132.9 . 1 1900 . 169 PHE CE1 C 130.1 . 1 1901 . 169 PHE CE2 C 130.1 . 1 1902 . 169 PHE N N 123.86 . 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 175.26 . 1 1911 . 170 PRO CA C 62.54 . 1 1912 . 170 PRO CB C 32.86 . 1 1913 . 170 PRO CD C 51.2 . 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 60.05 . 1 1920 . 171 VAL CB C 32.69 . 1 1921 . 171 VAL CG1 C 20.8 . 1 1922 . 171 VAL CG2 C 20.8 . 1 1923 . 171 VAL N N 122.19 . 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 174.52 . 1 1932 . 172 PRO CA C 63.86 . 1 1933 . 172 PRO CB C 31.91 . 1 1934 . 172 PRO CG C 27.9 . 1 1935 . 172 PRO CD C 51.2 . 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 174.54 . 1 1944 . 173 ILE CA C 59.31 . 1 1945 . 173 ILE CB C 42.86 . 1 1946 . 173 ILE CG1 C 29.8 . 1 1947 . 173 ILE CG2 C 18.4 . 1 1948 . 173 ILE CD1 C 14.1 . 1 1949 . 173 ILE N N 113.50 . 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 175.85 . 1 1955 . 174 ASP CA C 53.38 . 1 1956 . 174 ASP CB C 41.18 . 1 1957 . 174 ASP N N 118.05 . 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 56.30 . 1 1967 . 175 GLN CB C 29.17 . 1 1968 . 175 GLN N N 118.71 . 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 176.83 . 1 1975 . 176 CYS CA C 59.88 . 1 1976 . 176 CYS CB C 36.5 . 1 1977 . 176 CYS N N 114.61 . 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 174.91 . 1 1986 . 177 ILE CA C 63.70 . 1 1987 . 177 ILE CB C 38.68 . 1 1988 . 177 ILE CG1 C 27.3 . 1 1989 . 177 ILE CG2 C 18.3 . 1 1990 . 177 ILE CD1 C 16.2 . 1 1991 . 177 ILE N N 116.8 . 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 175.50 . 1 1997 . 178 ASP CA C 54.06 . 1 1998 . 178 ASP CB C 40.95 . 1 1999 . 178 ASP N N 121.73 . 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 177.08 . 1 2004 . 179 GLY CA C 46.06 . 1 2005 . 179 GLY N N 114.48 . 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 _Spectrometer_frequency_1H . _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 9 ILE H 9 ILE HA 4.3 . . . 2 3JHNHA 11 ALA H 11 ALA HA 4.5 . . . 3 3JHNHA 16 LYS H 16 LYS HA 9.1 . . . 4 3JHNHA 17 VAL H 17 VAL HA 8.0 . . . 5 3JHNHA 19 LEU H 19 LEU HA 9.2 . . . 6 3JHNHA 20 GLN H 20 GLN HA 3.8 . . . 7 3JHNHA 21 GLN H 21 GLN HA 3.8 . . . 8 3JHNHA 23 PHE H 23 PHE HA 1.5 . . . 9 3JHNHA 24 GLN H 24 GLN HA 11.0 . . . 10 3JHNHA 25 ASP H 25 ASP HA 2.6 . . . 11 3JHNHA 26 ASN H 26 ASN HA 4.2 . . . 12 3JHNHA 27 GLN H 27 GLN HA 8.0 . . . 13 3JHNHA 29 GLN H 29 GLN HA 3.3 . . . 14 3JHNHA 30 GLY H 30 GLY HA2 8.5 . . . 15 3JHNHA 30 GLY H 30 GLY HA3 2.0 . . . 16 3JHNHA 31 LYS H 31 LYS HA 8.5 . . . 17 3JHNHA 32 TRP H 32 TRP HA 9.0 . . . 18 3JHNHA 33 TYR H 33 TYR HA 8.5 . . . 19 3JHNHA 34 VAL H 34 VAL HA 4.0 . . . 20 3JHNHA 36 GLY H 36 GLY HA2 3.7 . . . 21 3JHNHA 36 GLY H 36 GLY HA3 3.7 . . . 22 3JHNHA 37 LEU H 37 LEU HA 8.2 . . . 23 3JHNHA 38 ALA H 38 ALA HA 8.6 . . . 24 3JHNHA 39 GLY H 39 GLY HA2 2.7 . . . 25 3JHNHA 39 GLY H 39 GLY HA3 2.7 . . . 26 3JHNHA 41 ALA H 41 ALA HA 9.8 . . . 27 3JHNHA 42 ILE H 42 ILE HA 9.1 . . . 28 3JHNHA 43 LEU H 43 LEU HA 9.4 . . . 29 3JHNHA 48 ASP H 48 ASP HA 9.5 . . . 30 3JHNHA 54 ALA H 54 ALA HA 8.5 . . . 31 3JHNHA 55 THR H 55 THR HA 8.1 . . . 32 3JHNHA 57 TYR H 57 TYR HA 8.0 . . . 33 3JHNHA 58 GLU H 58 GLU HA 9.0 . . . 34 3JHNHA 60 LYS H 60 LYS HA 9.4 . . . 35 3JHNHA 61 GLU H 61 GLU HA 3.3 . . . 36 3JHNHA 62 ASP H 62 ASP HA 8.9 . . . 37 3JHNHA 64 SER H 64 SER HA 8.0 . . . 38 3JHNHA 65 TYR H 65 TYR HA 9.1 . . . 39 3JHNHA 66 ASN H 66 ASN HA 9.4 . . . 40 3JHNHA 67 VAL H 67 VAL HA 8.8 . . . 41 3JHNHA 68 THR H 68 THR HA 8.5 . . . 42 3JHNHA 71 LEU H 71 LEU HA 9.0 . . . 43 3JHNHA 73 ARG H 73 ARG HA 9.0 . . . 44 3JHNHA 74 LYS H 74 LYS HA 5.0 . . . 45 3JHNHA 75 LYS H 75 LYS HA 8.5 . . . 46 3JHNHA 76 LYS H 76 LYS HA 8.9 . . . 47 3JHNHA 77 CYS H 77 CYS HA 8.0 . . . 48 3JHNHA 78 ASP H 78 ASP HA 9.5 . . . 49 3JHNHA 79 TYR H 79 TYR HA 8.5 . . . 50 3JHNHA 80 TRP H 80 TRP HA 11.0 . . . 51 3JHNHA 82 ARG H 82 ARG HA 8.0 . . . 52 3JHNHA 83 THR H 83 THR HA 9.5 . . . 53 3JHNHA 84 PHE H 84 PHE HA 9.5 . . . 54 3JHNHA 85 VAL H 85 VAL HA 9.4 . . . 55 3JHNHA 87 GLY H 87 GLY HA2 2.5 . . . 56 3JHNHA 87 GLY H 87 GLY HA3 8.5 . . . 57 3JHNHA 89 GLN H 89 GLN HA 8.3 . . . 58 3JHNHA 91 GLY H 91 GLY HA2 8.5 . . . 59 3JHNHA 91 GLY H 91 GLY HA3 3.5 . . . 60 3JHNHA 92 GLU H 92 GLU HA 9.0 . . . 61 3JHNHA 93 PHE H 93 PHE HA 8.0 . . . 62 3JHNHA 94 THR H 94 THR HA 9.0 . . . 63 3JHNHA 96 GLY H 96 GLY HA2 5.6 . . . 64 3JHNHA 96 GLY H 96 GLY HA3 4.3 . . . 65 3JHNHA 98 ILE H 98 ILE HA 3.8 . . . 66 3JHNHA 99 LYS H 99 LYS HA 5.1 . . . 67 3JHNHA 100 SER H 100 SER HA 8.0 . . . 68 3JHNHA 101 TYR H 101 TYR HA 9.4 . . . 69 3JHNHA 103 GLY H 103 GLY HA2 6.7 . . . 70 3JHNHA 103 GLY H 103 GLY HA3 5.6 . . . 71 3JHNHA 104 LEU H 104 LEU HA 8.5 . . . 72 3JHNHA 105 THR H 105 THR HA 8.0 . . . 73 3JHNHA 106 SER H 106 SER HA 8.0 . . . 74 3JHNHA 107 TYR H 107 TYR HA 8.5 . . . 75 3JHNHA 108 LEU H 108 LEU HA 9.2 . . . 76 3JHNHA 109 VAL H 109 VAL HA 9.6 . . . 77 3JHNHA 110 ARG H 110 ARG HA 8.2 . . . 78 3JHNHA 114 THR H 114 THR HA 9.0 . . . 79 3JHNHA 115 ASN H 115 ASN HA 11.0 . . . 80 3JHNHA 116 TYR H 116 TYR HA 3.7 . . . 81 3JHNHA 117 ASN H 117 ASN HA 9.0 . . . 82 3JHNHA 118 GLN H 118 GLN HA 11.1 . . . 83 3JHNHA 119 HIS H 119 HIS HA 8.8 . . . 84 3JHNHA 120 ALA H 120 ALA HA 8.0 . . . 85 3JHNHA 121 MET H 121 MET HA 8.0 . . . 86 3JHNHA 122 VAL H 122 VAL HA 10.8 . . . 87 3JHNHA 123 PHE H 123 PHE HA 9.2 . . . 88 3JHNHA 124 PHE H 124 PHE HA 9.5 . . . 89 3JHNHA 126 LYS H 125 LYS HA 8.8 . . . 90 3JHNHA 127 VAL H 127 VAL HA 9.7 . . . 91 3JHNHA 128 SER H 128 SER HA 9.3 . . . 92 3JHNHA 130 ASN H 130 ASN HA 9.7 . . . 93 3JHNHA 131 ARG H 131 ARG HA 9.6 . . . 94 3JHNHA 132 GLU H 132 GLU HA 8.4 . . . 95 3JHNHA 133 TYR H 133 TYR HA 9.3 . . . 96 3JHNHA 136 ILE H 136 ILE HA 9.2 . . . 97 3JHNHA 137 THR H 137 THR HA 10.5 . . . 98 3JHNHA 138 LEU H 138 LEU HA 9.6 . . . 99 3JHNHA 139 TYR H 139 TYR HA 8.8 . . . 100 3JHNHA 140 GLY H 140 GLY HA2 1.5 . . . 101 3JHNHA 140 GLY H 140 GLY HA3 1.5 . . . 102 3JHNHA 142 THR H 142 THR HA 9.4 . . . 103 3JHNHA 143 LYS H 143 LYS HA 5.8 . . . 104 3JHNHA 144 GLU H 144 GLU HA 9.2 . . . 105 3JHNHA 147 SER H 147 SER HA 2.6 . . . 106 3JHNHA 148 GLU H 148 GLU HA 3.7 . . . 107 3JHNHA 150 LYS H 150 LYS HA 1.5 . . . 108 3JHNHA 151 GLU H 151 GLU HA 4.4 . . . 109 3JHNHA 152 ASN H 152 ASN HA 4.0 . . . 110 3JHNHA 154 ILE H 154 ILE HA 3.9 . . . 111 3JHNHA 155 ARG H 155 ARG HA 4.1 . . . 112 3JHNHA 156 PHE H 156 PHE HA 3.7 . . . 113 3JHNHA 158 LYS H 158 LYS HA 4.6 . . . 114 3JHNHA 159 SER H 159 SER HA 4.2 . . . 115 3JHNHA 160 LEU H 160 LEU HA 8.6 . . . 116 3JHNHA 161 GLY H 161 GLY HA2 8.4 . . . 117 3JHNHA 161 GLY H 161 GLY HA3 5.7 . . . 118 3JHNHA 164 GLU H 164 GLU HA 5.0 . . . 119 3JHNHA 165 ASN H 165 ASN HA 8.5 . . . 120 3JHNHA 166 HIS H 166 HIS HA 8.0 . . . 121 3JHNHA 167 ILE H 167 ILE HA 9.2 . . . 122 3JHNHA 168 VAL H 168 VAL HA 9.7 . . . 123 3JHNHA 169 PHE H 169 PHE HA 10.1 . . . 124 3JHNHA 175 GLN H 175 GLN HA 5.0 . . . 125 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 3 ASP N 1.030 0.031 2 4 SER N 1.064 0.032 3 5 THR N 0.960 0.029 4 6 SER N 0.910 0.027 5 7 ASP N 0.487 0.013 6 8 LEU N 1.019 0.031 7 9 ILE N 1.225 0.055 8 11 ALA N 1.431 0.063 9 14 LEU N 1.337 0.040 10 15 SER N 1.348 0.040 11 16 LYS N 1.395 0.043 12 17 VAL N 1.508 0.045 13 19 LEU N 1.490 0.046 14 20 GLN N 1.390 0.044 15 21 GLN N 1.455 0.044 16 22 ASN N 1.514 0.045 17 23 PHE N 1.568 0.060 18 24 GLN N 1.765 0.063 19 25 ASP N 1.577 0.047 20 26 ASN N 1.386 0.046 21 27 GLN N 1.456 0.044 22 28 PHE N 1.520 0.046 23 29 GLN N 1.528 0.046 24 30 GLY N 1.504 0.057 25 31 LYS N 1.525 0.052 26 32 TRP N 1.598 0.087 27 33 TYR N 1.552 0.075 28 34 VAL N 1.694 0.051 29 35 VAL N 1.565 0.094 30 36 GLY N 1.458 0.063 31 37 LEU N 1.433 0.043 32 38 ALA N 1.467 0.056 33 39 GLY N 1.550 0.053 34 40 ASN N 1.586 0.048 35 41 ALA N 1.431 0.043 36 42 ILE N 1.458 0.067 37 43 LEU N 1.423 0.058 38 46 ASP N 1.160 0.051 39 48 ASP N 1.248 0.075 40 52 MET N 1.650 0.077 41 53 TYR N 1.700 0.102 42 54 ALA N 1.500 0.090 43 55 THR N 1.646 0.051 44 56 ILE N 1.700 0.102 45 57 TYR N 1.640 0.050 46 58 GLU N 1.658 0.056 47 60 LYS N 1.513 0.045 48 61 GLU N 1.435 0.043 49 62 ASP N 1.504 0.045 50 63 LYS N 1.495 0.054 51 64 SER N 1.450 0.044 52 65 TYR N 1.473 0.044 53 66 ASN N 1.560 0.053 54 67 VAL N 1.638 0.066 55 68 THR N 1.655 0.099 56 69 SER N 1.790 0.106 57 71 LEU N 1.570 0.047 58 73 ARG N 1.515 0.065 59 74 LYS N 1.450 0.075 60 75 LYS N 1.327 0.040 61 76 LYS N 1.317 0.040 62 77 CYS N 1.408 0.042 63 78 ASP N 1.484 0.067 64 79 TYR N 1.534 0.049 65 80 TRP N 1.677 0.083 66 82 ARG N 1.713 0.077 67 83 THR N 1.630 0.051 68 84 PHE N 1.593 0.049 69 87 GLY N 1.500 0.076 70 88 CYS N 1.400 0.050 71 89 GLN N 1.310 0.039 72 92 GLU N 1.350 0.041 73 93 PHE N 1.418 0.043 74 94 THR N 1.575 0.062 75 95 LEU N 1.650 0.058 76 96 GLY N 1.393 0.067 77 97 ASN N 1.480 0.044 78 98 ILE N 1.487 0.045 79 99 LYS N 1.300 0.039 80 100 SER N 1.474 0.047 81 101 TYR N 1.463 0.044 82 104 LEU N 1.490 0.045 83 105 THR N 1.440 0.086 84 106 SER N 1.515 0.053 85 107 TYR N 1.480 0.044 86 108 LEU N 1.385 0.050 87 109 VAL N 1.545 0.077 88 110 ARG N 1.487 0.060 89 112 VAL N 1.290 0.077 90 113 SER N 1.535 0.046 91 114 THR N 1.485 0.045 92 115 ASN N 1.566 0.050 93 116 TYR N 1.540 0.092 94 117 ASN N 1.547 0.049 95 118 GLN N 1.583 0.055 96 119 HIS N 1.465 0.056 97 120 ALA N 1.536 0.046 98 122 VAL N 1.540 0.092 99 123 PHE N 1.535 0.074 100 124 PHE N 1.540 0.062 101 125 LYS N 1.605 0.077 102 127 VAL N 1.617 0.090 103 128 SER N 1.446 0.061 104 129 GLN N 1.363 0.041 105 130 ASN N 1.405 0.042 106 131 ARG N 1.495 0.045 107 132 GLU N 1.557 0.055 108 133 TYR N 1.560 0.060 109 134 PHE N 1.478 0.044 110 135 LYS N 1.556 0.051 111 136 ILE N 1.560 0.068 112 137 THR N 1.490 0.076 113 138 LEU N 1.725 0.104 114 139 TYR N 1.550 0.078 115 140 GLY N 1.570 0.094 116 141 ARG N 1.525 0.086 117 142 THR N 1.490 0.058 118 143 LYS N 1.660 0.075 119 144 GLU N 1.640 0.049 120 145 LEU N 1.560 0.080 121 146 THR N 1.725 0.052 122 147 SER N 1.880 0.057 123 148 GLU N 1.395 0.042 124 150 LYS N 1.410 0.047 125 151 GLU N 1.478 0.044 126 152 ASN N 1.388 0.042 127 153 PHE N 1.350 0.041 128 154 ILE N 1.357 0.047 129 155 ARG N 1.470 0.044 130 156 PHE N 1.420 0.043 131 157 SER N 1.395 0.042 132 158 LYS N 1.430 0.055 133 159 SER N 1.540 0.047 134 160 LEU N 1.423 0.043 135 161 GLY N 1.470 0.044 136 162 LEU N 1.490 0.057 137 165 ASN N 1.288 0.039 138 167 ILE N 1.533 0.046 139 168 VAL N 1.496 0.046 140 169 PHE N 1.590 0.100 141 171 VAL N 1.366 0.049 142 173 ILE N 1.600 0.100 143 175 GLN N 1.747 0.099 144 176 CYS N 1.555 0.063 145 178 ASP N 1.532 0.048 146 179 GLY N 1.127 0.034 147 32 TRP NE1 1.950 0.059 148 80 TRP NE1 1.378 0.041 149 110 ARG NE 1.700 0.102 150 141 ARG NE 1.245 0.075 151 155 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 3 ASP N 0.792 0.020 2 4 SER N 0.770 0.026 3 5 THR N 0.705 0.026 4 6 SER N 0.686 0.019 5 7 ASP N 0.670 0.013 6 8 LEU N 0.833 0.017 7 9 ILE N 0.990 0.047 8 11 ALA N 1.030 0.021 9 14 LEU N 1.019 0.020 10 15 SER N 0.942 0.033 11 16 LYS N 0.991 0.028 12 17 VAL N 1.034 0.021 13 19 LEU N 1.084 0.022 14 20 GLN N 0.996 0.033 15 21 GLN N 1.042 0.021 16 22 ASN N 0.948 0.022 17 23 PHE N 1.062 0.021 18 24 GLN N 1.106 0.055 19 25 ASP N 1.097 0.039 20 26 ASN N 0.992 0.020 21 27 GLN N 1.074 0.023 22 28 PHE N 1.049 0.033 23 29 GLN N 1.055 0.032 24 30 GLY N 1.008 0.037 25 31 LYS N 1.074 0.021 26 32 TRP N 0.992 0.035 27 33 TYR N 1.047 0.028 28 34 VAL N 1.093 0.055 29 35 VAL N 1.096 0.055 30 36 GLY N 1.091 0.034 31 37 LEU N 1.026 0.033 32 38 ALA N 1.094 0.032 33 39 GLY N 1.060 0.045 34 40 ASN N 1.020 0.046 35 41 ALA N 1.002 0.042 36 42 ILE N 1.060 0.039 37 43 LEU N 1.024 0.044 38 46 ASP N 0.890 0.045 39 48 ASP N 0.854 0.021 40 52 MET N 1.040 0.052 41 53 TYR N 1.040 0.052 42 54 ALA N 1.008 0.027 43 55 THR N 1.052 0.039 44 56 ILE N 1.030 0.052 45 57 TYR N 1.133 0.043 46 58 GLU N 1.060 0.052 47 60 LYS N 0.934 0.032 48 61 GLU N 0.965 0.019 49 62 ASP N 1.102 0.022 50 63 LYS N 0.999 0.044 51 64 SER N 0.999 0.044 52 65 TYR N 1.080 0.039 53 66 ASN N 1.055 0.038 54 67 VAL N 1.011 0.029 55 68 THR N 1.033 0.035 56 69 SER N 1.039 0.038 57 71 LEU N 1.030 0.039 58 73 ARG N 1.002 0.029 59 74 LYS N 0.980 0.043 60 75 LYS N 0.900 0.030 61 76 LYS N 0.983 0.020 62 77 CYS N 1.142 0.027 63 78 ASP N 1.099 0.039 64 79 TYR N 1.100 0.032 65 80 TRP N 1.100 0.055 66 82 ARG N 1.050 0.051 67 83 THR N 1.133 0.038 68 84 PHE N 1.105 0.037 69 87 GLY N 1.029 0.038 70 88 CYS N 1.033 0.031 71 89 GLN N 1.004 0.020 72 92 GLU N 0.994 0.020 73 93 PHE N 0.973 0.022 74 94 THR N 1.051 0.032 75 95 LEU N 1.020 0.036 76 96 GLY N 1.003 0.048 77 97 ASN N 0.915 0.023 78 98 ILE N 1.057 0.032 79 99 LYS N 0.993 0.020 80 100 SER N 1.018 0.027 81 101 TYR N 1.047 0.023 82 103 GLY N 1.016 0.051 83 104 LEU N 1.013 0.020 84 105 THR N 1.103 0.032 85 106 SER N 1.043 0.025 86 107 TYR N 1.059 0.031 87 108 LEU N 1.066 0.035 88 109 VAL N 1.059 0.021 89 110 ARG N 1.018 0.026 90 112 VAL N 1.001 0.035 91 113 SER N 1.068 0.025 92 115 ASN N 1.060 0.045 93 116 TYR N 1.000 0.050 94 117 ASN N 1.106 0.035 95 118 GLN N 0.955 0.028 96 119 HIS N 1.056 0.043 97 120 ALA N 1.047 0.033 98 122 VAL N 1.122 0.043 99 123 PHE N 1.064 0.038 100 124 PHE N 1.054 0.029 101 125 LYS N 1.047 0.030 102 127 VAL N 1.041 0.030 103 128 SER N 1.034 0.034 104 129 GLN N 1.000 0.034 105 130 ASN N 1.026 0.024 106 131 ARG N 1.034 0.029 107 132 GLU N 1.079 0.022 108 133 TYR N 1.087 0.041 109 134 PHE N 1.036 0.021 110 135 LYS N 1.070 0.028 111 136 ILE N 1.099 0.031 112 137 THR N 1.043 0.049 113 138 LEU N 1.071 0.047 114 139 TYR N 1.024 0.045 115 140 GLY N 1.090 0.036 116 141 ARG N 1.059 0.021 117 142 THR N 1.040 0.030 118 143 LYS N 1.056 0.034 119 144 GLU N 1.167 0.050 120 145 LEU N 1.112 0.040 121 146 THR N 1.227 0.042 122 147 SER N 0.985 0.041 123 148 GLU N 0.949 0.024 124 150 LYS N 1.041 0.021 125 151 GLU N 1.034 0.021 126 152 ASN N 1.007 0.020 127 153 PHE N 0.986 0.025 128 154 ILE N 0.986 0.020 129 155 ARG N 1.003 0.020 130 156 PHE N 0.999 0.028 131 157 SER N 1.033 0.021 132 158 LYS N 1.000 0.020 133 159 SER N 1.048 0.034 134 160 LEU N 1.009 0.020 135 161 GLY N 1.029 0.022 136 162 LEU N 1.069 0.021 137 165 ASN N 0.969 0.019 138 167 ILE N 1.060 0.029 139 168 VAL N 1.040 0.025 140 169 PHE N 1.088 0.040 141 171 VAL N 1.031 0.030 142 173 ILE N 1.142 0.057 143 175 GLN N 1.152 0.030 144 176 CYS N 1.022 0.051 145 178 ASP N 1.025 0.032 146 179 GLY N 0.984 0.021 147 32 TRP NE1 1.223 0.048 148 80 TRP NE1 0.918 0.037 149 110 ARG NE 1.470 0.074 150 141 ARG NE 1.129 0.056 151 155 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 4 SER N 0.940 0.362 2 5 THR N 0.893 0.114 3 6 SER N 0.837 0.099 4 7 ASP N 0.704 0.052 5 8 LEU N 0.710 0.021 6 9 ILE N 0.790 0.033 7 11 ALA N 0.799 0.024 8 14 LEU N 0.785 0.024 9 15 SER N 0.798 0.052 10 16 LYS N 0.792 0.034 11 17 VAL N 0.844 0.025 12 19 LEU N 0.841 0.025 13 20 GLN N 0.799 0.031 14 21 GLN N 0.799 0.024 15 23 PHE N 0.872 0.032 16 24 GLN N 0.914 0.049 17 25 ASP N 0.904 0.033 18 26 ASN N 0.846 0.042 19 27 GLN N 0.854 0.026 20 28 PHE N 0.862 0.034 21 29 GLN N 0.831 0.027 22 30 GLY N 0.786 0.033 23 31 LYS N 0.832 0.028 24 32 TRP N 0.750 0.034 25 33 TYR N 0.832 0.042 26 34 VAL N 0.867 0.040 27 35 VAL N 0.839 0.045 28 36 GLY N 0.795 0.034 29 37 LEU N 0.769 0.023 30 38 ALA N 0.771 0.033 31 39 GLY N 0.859 0.044 32 40 ASN N 0.921 0.054 33 41 ALA N 0.823 0.077 34 43 LEU N 0.732 0.047 35 46 ASP N 0.771 0.166 36 48 ASP N 0.803 0.038 37 52 MET N 0.818 0.066 38 53 TYR N 0.874 0.204 39 54 ALA N 0.883 0.040 40 55 THR N 0.871 0.042 41 56 ILE N 0.855 0.056 42 57 TYR N 0.829 0.039 43 58 GLU N 0.855 0.029 44 60 LYS N 0.793 0.025 45 61 GLU N 0.899 0.108 46 62 ASP N 0.854 0.032 47 63 LYS N 0.805 0.024 48 64 SER N 0.834 0.025 49 65 TYR N 0.820 0.034 50 66 ASN N 0.777 0.025 51 67 VAL N 0.854 0.041 52 68 THR N 0.840 0.040 53 69 SER N 0.905 0.070 54 71 LEU N 0.901 0.038 55 73 ARG N 0.818 0.026 56 76 LYS N 0.796 0.029 57 77 CYS N 0.832 0.039 58 78 ASP N 0.850 0.042 59 79 TYR N 0.923 0.031 60 80 TRP N 0.823 0.034 61 82 ARG N 0.913 0.062 62 83 THR N 0.878 0.029 63 84 PHE N 0.806 0.056 64 87 GLY N 0.865 0.061 65 88 CYS N 0.812 0.029 66 89 GLN N 0.815 0.027 67 92 GLU N 0.781 0.023 68 93 PHE N 0.834 0.040 69 94 THR N 0.809 0.027 70 95 LEU N 0.868 0.026 71 96 GLY N 0.816 0.056 72 97 ASN N 0.827 0.134 73 98 ILE N 0.840 0.027 74 99 LYS N 0.786 0.024 75 100 SER N 0.816 0.029 76 101 TYR N 0.856 0.028 77 104 LEU N 0.841 0.027 78 105 THR N 0.879 0.061 79 106 SER N 0.851 0.029 80 107 TYR N 0.828 0.025 81 108 LEU N 0.790 0.024 82 109 VAL N 0.859 0.026 83 110 ARG N 0.809 0.035 84 112 VAL N 0.759 0.036 85 113 SER N 0.808 0.024 86 115 ASN N 0.789 0.047 87 116 TYR N 0.766 0.024 88 117 ASN N 0.817 0.028 89 118 GLN N 0.813 0.028 90 119 HIS N 0.849 0.037 91 120 ALA N 0.842 0.032 92 122 VAL N 0.823 0.056 93 123 PHE N 0.816 0.026 94 124 PHE N 0.821 0.025 95 125 LYS N 0.804 0.024 96 127 VAL N 0.810 0.026 97 128 SER N 0.863 0.040 98 129 GLN N 0.774 0.066 99 130 ASN N 0.813 0.043 100 131 ARG N 0.868 0.026 101 132 GLU N 0.829 0.025 102 133 TYR N 0.818 0.033 103 134 PHE N 0.776 0.023 104 135 LYS N 0.806 0.024 105 136 ILE N 0.769 0.023 106 137 THR N 0.859 0.043 107 138 LEU N 0.823 0.025 108 139 TYR N 0.810 0.040 109 140 GLY N 0.761 0.037 110 141 ARG N 0.855 0.041 111 142 THR N 0.821 0.030 112 143 LYS N 0.900 0.060 113 144 GLU N 0.899 0.027 114 146 THR N 0.969 0.042 115 148 GLU N 0.799 0.050 116 150 LYS N 0.787 0.024 117 151 GLU N 0.799 0.024 118 152 ASN N 0.773 0.023 119 153 PHE N 0.765 0.057 120 154 ILE N 0.777 0.023 121 155 ARG N 0.776 0.023 122 156 PHE N 0.796 0.024 123 157 SER N 0.799 0.024 124 158 LYS N 0.776 0.026 125 159 SER N 0.865 0.038 126 160 LEU N 0.820 0.028 127 161 GLY N 0.787 0.024 128 162 LEU N 0.806 0.024 129 165 ASN N 0.742 0.032 130 167 ILE N 0.831 0.034 131 168 VAL N 0.821 0.025 132 169 PHE N 0.921 0.033 133 171 VAL N 0.808 0.028 134 173 ILE N 0.832 0.149 135 175 GLN N 1.052 0.061 136 176 CYS N 0.949 0.122 137 178 ASP N 0.871 0.044 138 179 GLY N 0.910 0.032 139 32 TRP NE1 0.924 0.028 140 80 TRP NE1 0.694 0.035 141 110 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. ; loop_ _Experiment_label $_1 stop_ _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 3 ASP N 0.2828 0.0077 . . 2 4 SER N 0.2600 0.0055 . . 3 5 THR N 0.2160 0.0043 . . 4 6 SER N 0.1721 0.0034 . . 5 7 ASP N 0.1593 0.0032 . . 6 8 LEU N 0.1007 0.0020 . . 7 9 ILE N 0.0599 0.0021 . . 8 11 ALA N 0.0546 0.0011 . . 9 14 LEU N 0.0645 0.0018 . . 10 15 SER N 0.0510 0.0020 . . 11 16 LYS N 0.0536 0.0015 . . 12 17 VAL N 0.0531 0.0011 . . 13 19 LEU N 0.0606 0.0012 . . 14 20 GLN N 0.0530 0.0015 . . 15 21 GLN N 0.0541 0.0015 . . 16 22 ASN N 0.0549 0.0011 . . 17 23 PHE N 0.0540 0.0011 . . 18 24 GLN N 0.0573 0.0012 . . 19 25 ASP N 0.0586 0.0012 . . 20 26 ASN N 0.0521 0.0010 . . 21 27 GLN N 0.0577 0.0012 . . 22 28 PHE N 0.0509 0.0010 1.23 0.55 23 29 GLN N 0.0552 0.0011 . . 24 30 GLY N 0.0537 0.0011 . . 25 31 LYS N 0.0508 0.0010 . . 26 32 TRP N 0.0541 0.0011 . . 27 33 TYR N 0.0535 0.0011 . . 28 34 VAL N 0.0524 0.0011 2.10 0.80 29 35 VAL N 0.0451 0.0015 4.13 1.34 30 36 GLY N 0.0594 0.0019 . . 31 37 LEU N 0.0497 0.0010 . . 32 38 ALA N 0.0506 0.0010 . . 33 39 GLY N 0.0539 0.0011 . . 34 40 ASN N 0.0481 0.0010 2.99 0.77 35 41 ALA N 0.0541 0.0013 . . 36 42 ILE N 0.0326 0.0013 8.73 1.14 37 43 LEU N 0.0353 0.0011 8.71 1.30 38 46 ASP N 0.0509 0.0043 1.27 1.15 39 48 ASP N 0.0534 0.0011 . . 40 52 MET N 0.0366 0.0037 8.84 2.19 41 53 TYR N 0.0380 0.0026 9.14 2.48 42 54 ALA N 0.0490 0.0013 . . 43 55 THR N 0.0541 0.0011 . . 44 56 ILE N 0.0539 0.0025 . . 45 57 TYR N 0.0594 0.0017 . . 46 58 GLU N 0.0578 0.0012 . . 47 60 LYS N 0.0549 0.0011 . . 48 61 GLU N 0.0565 0.0011 . . 49 62 ASP N 0.0568 0.0011 . . 50 63 LYS N 0.0509 0.0016 . . 51 64 SER N 0.0557 0.0011 . . 52 65 TYR N 0.0559 0.0011 . . 53 66 ASN N 0.0546 0.0011 . . 54 67 VAL N 0.0547 0.0011 . . 55 68 THR N 0.0520 0.0014 . . 56 69 SER N 0.0533 0.0018 . . 57 71 LEU N 0.0621 0.0029 . . 58 73 ARG N 0.0565 0.0011 . . 59 74 LYS N 0.0550 0.0024 . . 60 75 LYS N 0.0530 0.0014 . . 61 76 LYS N 0.0556 0.0011 . . 62 77 CYS N 0.0383 0.0010 7.67 0.74 63 78 ASP N 0.0513 0.0012 1.53 0.84 64 79 TYR N 0.0493 0.0010 2.97 0.67 65 80 TRP N 0.0472 0.0013 3.06 0.82 66 82 ARG N 0.0524 0.0017 . . 67 83 THR N 0.0566 0.0011 . . 68 84 PHE N 0.0545 0.0011 . . 69 87 GLY N 0.0614 0.0038 . . 70 88 CYS N 0.0520 0.0010 2.43 0.80 71 89 GLN N 0.0650 0.0013 . . 72 92 GLU N 0.0494 0.0010 . . 73 93 PHE N 0.0559 0.0011 . . 74 94 THR N 0.0532 0.0011 . . 75 95 LEU N 0.0576 0.0012 . . 76 96 GLY N 0.0529 0.0019 . . 77 97 ASN N 0.0558 0.0011 . . 78 98 ILE N 0.0525 0.0011 . . 79 99 LYS N 0.0516 0.0010 . . 80 100 SER N 0.0567 0.0011 . . 81 101 TYR N 0.0545 0.0011 . . 82 103 GLY N 0.0651 0.0013 . . 83 104 LEU N 0.0542 0.0011 . . 84 105 THR N 0.0515 0.0013 . . 85 106 SER N 0.0561 0.0011 . . 86 107 TYR N 0.0553 0.0011 . . 87 108 LEU N 0.0521 0.0010 . . 88 109 VAL N 0.0537 0.0011 . . 89 110 ARG N 0.0538 0.0011 . . 90 112 VAL N 0.0517 0.0010 . . 91 113 SER N 0.0530 0.0011 . . 92 114 THR N 0.0495 0.0010 . . 93 115 ASN N 0.0487 0.0010 2.31 0.66 94 116 TYR N 0.0539 0.0014 . . 95 117 ASN N 0.0517 0.0010 1.14 0.77 96 118 GLN N 0.0509 0.0010 . . 97 119 HIS N 0.0488 0.0010 1.56 0.69 98 120 ALA N 0.0494 0.0010 . . 99 122 VAL N 0.0539 0.0011 . . 100 123 PHE N 0.0508 0.0024 1.14 0.99 101 124 PHE N 0.0535 0.0012 . . 102 125 LYS N 0.0514 0.0010 . . 103 127 VAL N 0.0503 0.0010 . . 104 128 SER N 0.0522 0.0011 . . 105 129 GLN N 0.0535 0.0011 . . 106 130 ASN N 0.0481 0.0010 3.10 1.35 107 131 ARG N 0.0579 0.0012 . . 108 132 GLU N 0.0553 0.0011 . . 109 133 TYR N 0.0565 0.0011 . . 110 134 PHE N 0.0545 0.0011 . . 111 135 LYS N 0.0496 0.0010 1.57 0.91 112 136 ILE N 0.0502 0.0010 1.21 0.87 113 137 THR N 0.0384 0.0009 7.37 0.95 114 138 LEU N 0.0529 0.0014 . . 115 139 TYR N 0.0547 0.0011 . . 116 140 GLY N 0.0548 0.0013 . . 117 141 ARG N 0.0530 0.0011 . . 118 142 THR N 0.0503 0.0010 . . 119 143 LYS N 0.0581 0.0012 . . 120 144 GLU N 0.0553 0.0011 1.84 0.81 121 145 LEU N 0.0314 0.0019 17.47 1.77 122 146 THR N 0.0628 0.0013 3.02 0.98 123 147 SER N 0.0564 0.0015 . . 124 148 GLU N 0.0508 0.0010 . . 125 150 LYS N 0.0532 0.0011 . . 126 151 GLU N 0.0518 0.0010 . . 127 152 ASN N 0.0517 0.0010 . . 128 153 PHE N 0.0528 0.0011 . . 129 154 ILE N 0.0508 0.0010 . . 130 155 ARG N 0.0508 0.0010 . . 131 156 PHE N 0.0499 0.0010 . . 132 157 SER N 0.0509 0.0010 . . 133 158 LYS N 0.0492 0.0010 . . 134 159 SER N 0.0508 0.0010 1.33 0.52 135 160 LEU N 0.0510 0.0010 . . 136 161 GLY N 0.0546 0.0011 . . 137 162 LEU N 0.0503 0.0010 1.36 0.70 138 165 ASN N 0.0575 0.0013 . . 139 167 ILE N 0.0514 0.0010 0.85 0.68 140 168 VAL N 0.0491 0.0010 1.69 0.61 141 169 PHE N 0.0529 0.0011 . . 142 171 VAL N 0.0486 0.0010 2.73 1.14 143 173 ILE N 0.0319 0.0038 20.67 2.70 144 175 GLN N 0.0625 0.0013 . . 145 176 CYS N 0.0320 0.0027 16.19 1.23 146 178 ASP N 0.0420 0.0008 5.29 0.75 147 179 GLY N 0.1281 0.0026 . . 148 32 TRP NE1 0.0624 0.0013 . . 149 80 TRP NE1 0.0889 0.0018 . . 150 110 ARG NE 0.1160 0.0271 . . 151 141 ARG NE 0.0825 0.0253 . . 152 155 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 ; loop_ _Experiment_label $_1 stop_ _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 3 ASP N 0.3273 0.0085 . . 2 4 SER N 0.2808 0.0067 . . 3 5 THR N 0.2306 0.0071 . . 4 6 SER N 0.1978 0.0040 . . 5 7 ASP N 0.1748 0.0035 . . 6 8 LEU N 0.1122 0.0022 . . 7 9 ILE N 0.0705 0.0014 . . 8 11 ALA N 0.0624 0.0013 . . 9 14 LEU N 0.0634 0.0013 . . 10 15 SER N 0.0566 0.0020 . . 11 16 LYS N 0.0582 0.0012 . . 12 17 VAL N 0.0590 0.0012 . . 13 19 LEU N 0.0657 0.0013 . . 14 20 GLN N 0.0596 0.0012 . . 15 21 GLN N 0.0613 0.0014 . . 16 22 ASN N 0.0611 0.0013 . . 17 23 PHE N 0.0595 0.0012 . . 18 24 GLN N 0.0622 0.0020 . . 19 25 ASP N 0.0616 0.0013 . . 20 26 ASN N 0.0578 0.0012 . . 21 27 GLN N 0.0633 0.0013 . . 22 28 PHE N 0.0576 0.0012 . . 23 29 GLN N 0.0605 0.0012 . . 24 30 GLY N 0.0606 0.0019 . . 25 31 LYS N 0.0601 0.0012 . . 26 32 TRP N 0.0597 0.0019 . . 27 33 TYR N 0.0555 0.0011 . . 28 34 VAL N 0.0589 0.0017 . . 29 35 VAL N 0.0506 0.0041 . . 30 36 GLY N 0.0856 0.0052 . . 31 37 LEU N 0.0580 0.0012 . . 32 38 ALA N 0.0544 0.0011 . . 33 39 GLY N 0.0577 0.0018 . . 34 40 ASN N 0.0548 0.0011 . . 35 41 ALA N 0.0575 0.0012 . . 36 42 ILE N 0.0470 0.0009 . . 37 43 LEU N 0.0502 0.0012 . . 38 46 ASP N 0.0740 0.0025 . . 39 48 ASP N 0.0643 0.0019 . . 40 52 MET N 0.0463 0.0037 . . 41 53 TYR N 0.0451 0.0030 . . 42 54 ALA N 0.0570 0.0011 . . 43 55 THR N 0.0574 0.0029 . . 44 56 ILE N 0.0554 0.0015 . . 45 57 TYR N 0.0613 0.0012 . . 46 58 GLU N 0.0611 0.0026 . . 47 60 LYS N 0.0594 0.0020 . . 48 61 GLU N 0.0613 0.0012 . . 49 62 ASP N 0.0616 0.0012 . . 50 63 LYS N 0.0587 0.0012 . . 51 64 SER N 0.0621 0.0015 . . 52 65 TYR N 0.0603 0.0018 . . 53 66 ASN N 0.0586 0.0012 . . 54 67 VAL N 0.0613 0.0014 . . 55 68 THR N 0.0574 0.0012 . . 56 69 SER N 0.0601 0.0031 . . 57 71 LEU N 0.0617 0.0017 . . 58 73 ARG N 0.0614 0.0016 . . 59 74 LYS N 0.0628 0.0015 . . 60 75 LYS N 0.0609 0.0026 . . 61 76 LYS N 0.0618 0.0012 . . 62 77 CYS N 0.0465 0.0012 . . 63 78 ASP N 0.0554 0.0011 . . 64 79 TYR N 0.0545 0.0011 . . 65 80 TRP N 0.0563 0.0011 . . 66 82 ARG N 0.0565 0.0020 . . 67 83 THR N 0.0627 0.0013 . . 68 84 PHE N 0.0620 0.0015 . . 69 87 GLY N 0.0677 0.0019 . . 70 88 CYS N 0.0597 0.0012 . . 71 89 GLN N 0.0712 0.0014 . . 72 92 GLU N 0.0560 0.0014 . . 73 93 PHE N 0.0618 0.0012 . . 74 94 THR N 0.0590 0.0012 . . 75 95 LEU N 0.0579 0.0013 . . 76 96 GLY N 0.0567 0.0011 . . 77 97 ASN N 0.0610 0.0012 . . 78 98 ILE N 0.0579 0.0013 . . 79 99 LYS N 0.0577 0.0012 . . 80 100 SER N 0.0632 0.0013 . . 81 101 TYR N 0.0590 0.0012 . . 82 103 GLY N 0.0717 0.0014 . . 83 104 LEU N 0.0600 0.0012 . . 84 105 THR N 0.0547 0.0012 . . 85 106 SER N 0.0621 0.0012 . . 86 107 TYR N 0.0620 0.0012 . . 87 108 LEU N 0.0599 0.0012 . . 88 109 VAL N 0.0605 0.0015 . . 89 110 ARG N 0.0586 0.0012 . . 90 112 VAL N 0.0594 0.0013 . . 91 113 SER N 0.0590 0.0012 . . 92 115 ASN N 0.0543 0.0018 . . 93 116 TYR N 0.0581 0.0028 . . 94 117 ASN N 0.0583 0.0012 . . 95 118 GLN N 0.0592 0.0012 . . 96 119 HIS N 0.0576 0.0012 . . 97 120 ALA N 0.0576 0.0012 . . 98 122 VAL N 0.0589 0.0012 . . 99 123 PHE N 0.0570 0.0019 . . 100 124 PHE N 0.0579 0.0012 . . 101 125 LYS N 0.0552 0.0017 . . 102 127 VAL N 0.0610 0.0017 . . 103 128 SER N 0.0557 0.0011 . . 104 129 GLN N 0.0588 0.0012 . . 105 130 ASN N 0.0570 0.0016 . . 106 131 ARG N 0.0648 0.0013 . . 107 132 GLU N 0.0626 0.0013 . . 108 133 TYR N 0.0583 0.0012 . . 109 134 PHE N 0.0602 0.0012 . . 110 135 LYS N 0.0566 0.0011 . . 111 136 ILE N 0.0558 0.0011 . . 112 137 THR N 0.0471 0.0012 . . 113 138 LEU N 0.0558 0.0018 . . 114 139 TYR N 0.0566 0.0013 . . 115 140 GLY N 0.0590 0.0012 . . 116 141 ARG N 0.0577 0.0012 . . 117 142 THR N 0.0575 0.0018 . . 118 143 LYS N 0.0617 0.0018 . . 119 144 GLU N 0.0626 0.0014 . . 120 145 LEU N 0.0367 0.0014 . . 121 146 THR N 0.0708 0.0016 . . 122 147 SER N 0.0600 0.0012 . . 123 148 GLU N 0.0578 0.0012 . . 124 150 LYS N 0.0603 0.0012 . . 125 151 GLU N 0.0558 0.0011 . . 126 152 ASN N 0.0560 0.0011 . . 127 153 PHE N 0.0567 0.0011 . . 128 154 ILE N 0.0580 0.0013 . . 129 155 ARG N 0.0569 0.0011 . . 130 156 PHE N 0.0559 0.0011 . . 131 157 SER N 0.0563 0.0011 . . 132 158 LYS N 0.0534 0.0011 . . 133 159 SER N 0.0577 0.0012 . . 134 160 LEU N 0.0557 0.0011 . . 135 161 GLY N 0.0609 0.0012 . . 136 162 LEU N 0.0550 0.0011 . . 137 165 ASN N 0.0622 0.0012 . . 138 167 ILE N 0.0591 0.0012 . . 139 168 VAL N 0.0545 0.0011 . . 140 169 PHE N 0.0573 0.0012 . . 141 171 VAL N 0.0584 0.0012 . . 142 173 ILE N 0.0333 0.0017 . . 143 175 GLN N 0.0727 0.0018 . . 144 176 CYS N 0.0371 0.0007 . . 145 178 ASP N 0.0491 0.0010 . . 146 179 GLY N 0.1337 0.0027 . . 147 32 TRP NE1 0.0650 0.0014 . . 148 80 TRP NE1 0.0935 0.0019 . . 149 110 ARG NE 0.1128 0.0231 . . 150 155 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 ; loop_ _Experiment_label $_1 stop_ _Sample_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name HNGAL _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 4 SER N 0.3173 0.0475 . . 2 5 THR N 0.2437 0.0140 . . 3 6 SER N 0.1868 0.0059 . . 4 7 ASP N 0.1709 0.0039 . . 5 8 LEU N 0.1166 0.0023 . . 6 9 ILE N 0.0757 0.0015 . . 7 11 ALA N 0.0677 0.0014 . . 8 14 LEU N 0.0819 0.0022 . . 9 15 SER N 0.0621 0.0020 . . 10 16 LYS N 0.0658 0.0013 . . 11 17 VAL N 0.0645 0.0013 . . 12 19 LEU N 0.0719 0.0014 . . 13 20 GLN N 0.0639 0.0015 . . 14 21 GLN N 0.0667 0.0015 . . 15 23 PHE N 0.0652 0.0013 . . 16 24 GLN N 0.0679 0.0014 . . 17 25 ASP N 0.0671 0.0013 . . 18 26 ASN N 0.0625 0.0013 . . 19 27 GLN N 0.0718 0.0014 . . 20 28 PHE N 0.0630 0.0013 . . 21 29 GLN N 0.0691 0.0014 . . 22 30 GLY N 0.0658 0.0013 . . 23 31 LYS N 0.0619 0.0012 . . 24 32 TRP N 0.0653 0.0021 . . 25 33 TYR N 0.0617 0.0015 . . 26 34 VAL N 0.0612 0.0012 . . 27 35 VAL N 0.0493 0.0018 . . 28 36 GLY N 0.0641 0.0013 . . 29 37 LEU N 0.0603 0.0012 . . 30 38 ALA N 0.0597 0.0012 . . 31 39 GLY N 0.0637 0.0014 . . 32 40 ASN N 0.0567 0.0013 . . 33 41 ALA N 0.0578 0.0016 . . 34 42 ILE N 0.0530 0.0026 . . 35 43 LEU N 0.0480 0.0016 . . 36 46 ASP N 0.0627 0.0032 . . 37 48 ASP N 0.0611 0.0013 . . 38 52 MET N 0.0437 0.0018 . . 39 53 TYR N 0.0481 0.0038 . . 40 54 ALA N 0.0620 0.0012 . . 41 55 THR N 0.0638 0.0013 . . 42 56 ILE N 0.0600 0.0025 . . 43 57 TYR N 0.0653 0.0016 . . 44 58 GLU N 0.0683 0.0014 . . 45 60 LYS N 0.0654 0.0013 . . 46 61 GLU N 0.0688 0.0018 . . 47 62 ASP N 0.0685 0.0014 . . 48 63 LYS N 0.0669 0.0013 . . 49 64 SER N 0.0734 0.0015 . . 50 65 TYR N 0.0655 0.0013 . . 51 66 ASN N 0.0616 0.0012 . . 52 67 VAL N 0.0708 0.0018 . . 53 68 THR N 0.0604 0.0012 . . 54 69 SER N 0.0651 0.0025 . . 55 71 LEU N 0.0627 0.0015 . . 56 73 ARG N 0.0670 0.0013 . . 57 76 LYS N 0.0693 0.0014 . . 58 77 CYS N 0.0544 0.0013 . . 59 78 ASP N 0.0612 0.0013 . . 60 79 TYR N 0.0593 0.0012 . . 61 80 TRP N 0.0610 0.0014 . . 62 82 ARG N 0.0647 0.0020 . . 63 83 THR N 0.0699 0.0014 . . 64 84 PHE N 0.0612 0.0015 . . 65 87 GLY N 0.0723 0.0020 . . 66 88 CYS N 0.0670 0.0020 . . 67 89 GLN N 0.0801 0.0016 . . 68 92 GLU N 0.0605 0.0012 . . 69 93 PHE N 0.0667 0.0013 . . 70 94 THR N 0.0628 0.0013 . . 71 95 LEU N 0.0685 0.0014 . . 72 96 GLY N 0.0659 0.0028 . . 73 97 ASN N 0.0682 0.0021 . . 74 98 ILE N 0.0643 0.0015 . . 75 99 LYS N 0.0636 0.0013 . . 76 100 SER N 0.0675 0.0014 . . 77 101 TYR N 0.0653 0.0013 . . 78 103 GLY N 0.1128 0.0276 . . 79 104 LEU N 0.0656 0.0013 . . 80 105 THR N 0.0599 0.0012 . . 81 106 SER N 0.0675 0.0014 . . 82 107 TYR N 0.0636 0.0014 . . 83 108 LEU N 0.0639 0.0013 . . 84 109 VAL N 0.0647 0.0013 . . 85 110 ARG N 0.0654 0.0013 . . 86 112 VAL N 0.0624 0.0014 . . 87 113 SER N 0.0641 0.0013 . . 88 115 ASN N 0.0568 0.0011 . . 89 116 TYR N 0.0609 0.0016 . . 90 117 ASN N 0.0634 0.0013 . . 91 118 GLN N 0.0606 0.0012 . . 92 119 HIS N 0.0591 0.0012 . . 93 120 ALA N 0.0595 0.0012 . . 94 122 VAL N 0.0632 0.0014 . . 95 123 PHE N 0.0623 0.0019 . . 96 124 PHE N 0.0626 0.0013 . . 97 125 LYS N 0.0616 0.0012 . . 98 127 VAL N 0.0618 0.0018 . . 99 128 SER N 0.0614 0.0012 . . 100 129 GLN N 0.0625 0.0018 . . 101 130 ASN N 0.0629 0.0013 . . 102 131 ARG N 0.0706 0.0014 . . 103 132 GLU N 0.0676 0.0014 . . 104 133 TYR N 0.0653 0.0016 . . 105 134 PHE N 0.0647 0.0013 . . 106 135 LYS N 0.0617 0.0012 . . 107 136 ILE N 0.0605 0.0017 . . 108 137 THR N 0.0521 0.0015 . . 109 138 LEU N 0.0619 0.0023 . . 110 139 TYR N 0.0651 0.0014 . . 111 140 GLY N 0.0610 0.0012 . . 112 141 ARG N 0.0606 0.0013 . . 113 142 THR N 0.0667 0.0016 . . 114 143 LYS N 0.0671 0.0013 . . 115 144 GLU N 0.0696 0.0014 . . 116 146 THR N 0.0830 0.0017 . . 117 148 GLU N 0.0605 0.0012 . . 118 150 LYS N 0.0645 0.0013 . . 119 151 GLU N 0.0609 0.0012 . . 120 152 ASN N 0.0620 0.0012 . . 121 153 PHE N 0.0663 0.0025 . . 122 154 ILE N 0.0616 0.0012 . . 123 155 ARG N 0.0618 0.0012 . . 124 156 PHE N 0.0596 0.0012 . . 125 157 SER N 0.0620 0.0012 . . 126 158 LYS N 0.0708 0.0035 . . 127 159 SER N 0.0634 0.0013 . . 128 160 LEU N 0.0626 0.0013 . . 129 161 GLY N 0.0663 0.0013 . . 130 162 LEU N 0.0610 0.0012 . . 131 165 ASN N 0.0712 0.0020 . . 132 167 ILE N 0.0616 0.0012 . . 133 168 VAL N 0.0596 0.0012 . . 134 169 PHE N 0.0627 0.0013 . . 135 171 VAL N 0.0616 0.0015 . . 136 173 ILE N 0.0441 0.0046 . . 137 175 GLN N 0.0783 0.0020 . . 138 176 CYS N 0.0427 0.0039 . . 139 178 ASP N 0.0558 0.0011 . . 140 179 GLY N 0.1531 0.0031 . . 141 32 TRP NE1 0.0708 0.0015 . . 142 80 TRP NE1 0.0966 0.0019 . . 143 110 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name HE1 _Atom_two_atom_name NE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name HE _Atom_two_atom_name NE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 750 _Mol_system_component_name HNGAL _Atom_one_atom_name H _Atom_two_atom_name N _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name HE1 _Atom_two_atom_name NE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name HE _Atom_two_atom_name NE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name H _Atom_two_atom_name N _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name HE1 _Atom_two_atom_name NE1 _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 600 _Mol_system_component_name HNGAL _Atom_one_atom_name HE _Atom_two_atom_name NE _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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_conditions_label $sample_conditions_all _Spectrometer_frequency_1H 500 _Mol_system_component_name HNGAL _Atom_one_atom_name H _Atom_two_atom_name N _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1 _NOE_reference_description 'internal reference' _Text_data_format . _Text_data . 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 0.050 179 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). ; loop_ _Experiment_label $_1 stop_ _Sample_conditions_label $sample_conditions_all _Mol_system_component_name HNGAL _Tau_e_value_units . _Tau_s_value_units ns _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_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_