data_19491 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N chemical shift assignments of full-length apo human Galectin-3 (2-250). ; _BMRB_accession_number 19491 _BMRB_flat_file_name bmr19491.str _Entry_type original _Submission_date 2013-09-11 _Accession_date 2013-09-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Backbone and side chain resonance assignments for apo human Galectin-3: full-length (2-250) with natural occurring P64H & T98P point mutations and containing an acetylated-Ala2 modification at the N-terminus. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ippel Hans . . 2 Andre Sabine . . 3 Suijlen Dennis . . 4 Hackeng Tilman . . 5 Weber Christian . . 6 Gabius Hans-Joachim . . 7 Mayo Kevin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 5 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1467 "13C chemical shifts" 1260 "15N chemical shifts" 336 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4909 'Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectin-3 with lactose bound' stop_ _Original_release_date 2014-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29kDa human chimera-type galectin-3.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24504927 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ippel Hans . . 2 Miller Michelle C. . 3 Berbis 'Manuel Alvaro' . . 4 Suylen Dennis . . 5 Andre Sabine . . 6 Hackeng Tilman M. . 7 Canada 'F. Javier' . . 8 Weber Christian . . 9 Gabius Hans-Joachim . . 10 Jimenez-Barbero Jesus . . 11 Mayo Kevin H. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2014 _Details . loop_ _Keyword apoptosis galectin glycan lectin 'NMR spectroscopy' proliferation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Galectin-3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Galectin-3, trans form, 1 (major form)' $Galectin-3 'Galectin-3, cis form, 1 (b)' $Galectin-3 'Galectin-3, cis form, 2 (c)' $Galectin-3 'Galectin-3, cis form, 3 (d)' $Galectin-3 'Galectin-3, cis form, 4 (e)' $Galectin-3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Galectin-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Galectin-3 _Molecular_mass 26150 _Mol_thiol_state 'all free' loop_ _Biological_function 'galactoside-binding lectin' 'Important in: cell adhesion, cell activation and chemoattraction, cell growth and differentiation, cell cycle, and apoptosis' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 250 _Mol_residue_sequence ; MADNFSLHDALSGSGNPNPQ GWPGAWGNQPAGAGGYPGAS YPGAYPGQAPPGAYPGQAPP GAYHGAPGAYPGAPAPGVYP GPPSGPGAYPSSGQPSAPGA YPATGPYGAPAGPLIVPYNL PLPGGVVPRMLITILGTVKP NANRIALDFQRGNDVAFHFN PRFNENNRRVIVCNTKLDNN WGREERQSVFPFESGKPFKI QVLVEPDHFKVAVNDAHLLQ YNHRVKKLNEISKLGISGDI DLTSASYTMI ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 ASN 5 PHE 6 SER 7 LEU 8 HIS 9 ASP 10 ALA 11 LEU 12 SER 13 GLY 14 SER 15 GLY 16 ASN 17 PRO 18 ASN 19 PRO 20 GLN 21 GLY 22 TRP 23 PRO 24 GLY 25 ALA 26 TRP 27 GLY 28 ASN 29 GLN 30 PRO 31 ALA 32 GLY 33 ALA 34 GLY 35 GLY 36 TYR 37 PRO 38 GLY 39 ALA 40 SER 41 TYR 42 PRO 43 GLY 44 ALA 45 TYR 46 PRO 47 GLY 48 GLN 49 ALA 50 PRO 51 PRO 52 GLY 53 ALA 54 TYR 55 PRO 56 GLY 57 GLN 58 ALA 59 PRO 60 PRO 61 GLY 62 ALA 63 TYR 64 HIS 65 GLY 66 ALA 67 PRO 68 GLY 69 ALA 70 TYR 71 PRO 72 GLY 73 ALA 74 PRO 75 ALA 76 PRO 77 GLY 78 VAL 79 TYR 80 PRO 81 GLY 82 PRO 83 PRO 84 SER 85 GLY 86 PRO 87 GLY 88 ALA 89 TYR 90 PRO 91 SER 92 SER 93 GLY 94 GLN 95 PRO 96 SER 97 ALA 98 PRO 99 GLY 100 ALA 101 TYR 102 PRO 103 ALA 104 THR 105 GLY 106 PRO 107 TYR 108 GLY 109 ALA 110 PRO 111 ALA 112 GLY 113 PRO 114 LEU 115 ILE 116 VAL 117 PRO 118 TYR 119 ASN 120 LEU 121 PRO 122 LEU 123 PRO 124 GLY 125 GLY 126 VAL 127 VAL 128 PRO 129 ARG 130 MET 131 LEU 132 ILE 133 THR 134 ILE 135 LEU 136 GLY 137 THR 138 VAL 139 LYS 140 PRO 141 ASN 142 ALA 143 ASN 144 ARG 145 ILE 146 ALA 147 LEU 148 ASP 149 PHE 150 GLN 151 ARG 152 GLY 153 ASN 154 ASP 155 VAL 156 ALA 157 PHE 158 HIS 159 PHE 160 ASN 161 PRO 162 ARG 163 PHE 164 ASN 165 GLU 166 ASN 167 ASN 168 ARG 169 ARG 170 VAL 171 ILE 172 VAL 173 CYS 174 ASN 175 THR 176 LYS 177 LEU 178 ASP 179 ASN 180 ASN 181 TRP 182 GLY 183 ARG 184 GLU 185 GLU 186 ARG 187 GLN 188 SER 189 VAL 190 PHE 191 PRO 192 PHE 193 GLU 194 SER 195 GLY 196 LYS 197 PRO 198 PHE 199 LYS 200 ILE 201 GLN 202 VAL 203 LEU 204 VAL 205 GLU 206 PRO 207 ASP 208 HIS 209 PHE 210 LYS 211 VAL 212 ALA 213 VAL 214 ASN 215 ASP 216 ALA 217 HIS 218 LEU 219 LEU 220 GLN 221 TYR 222 ASN 223 HIS 224 ARG 225 VAL 226 LYS 227 LYS 228 LEU 229 ASN 230 GLU 231 ILE 232 SER 233 LYS 234 LEU 235 GLY 236 ILE 237 SER 238 GLY 239 ASP 240 ILE 241 ASP 242 LEU 243 THR 244 SER 245 ALA 246 SER 247 TYR 248 THR 249 MET 250 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15705 Galectin-3-LBT 54.80 155 99.27 99.27 2.09e-93 PDB 1A3K "X-Ray Crystal Structure Of The Human Galectin-3 Carbohydrate Recognition Domain (Crd) At 2.1 Angstrom Resolution" 54.80 137 100.00 100.00 8.56e-95 PDB 1KJL "High Resolution X-Ray Structure Of Human Galectin-3 In Complex With Lacnac" 58.40 146 100.00 100.00 6.67e-101 PDB 1KJR "Crystal Structure Of The Human Galectin-3 Crd In Complex With A 3'- Derivative Of N-Acetyllactosamine" 58.40 146 100.00 100.00 6.67e-101 PDB 2NMN "Crystal Structure Of Human Galectin-3 Carbohydrate- Recognising Domain At 2.45 Angstrom Resolution" 55.20 138 100.00 100.00 1.90e-95 PDB 2NMO "Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain At 1.35 Angstrom Resolution" 55.20 138 100.00 100.00 1.90e-95 PDB 2NN8 "Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain With Lactose Bound, At 1.35 Angstrom Resolution" 55.20 138 100.00 100.00 1.90e-95 PDB 2XG3 "Human Galectin-3 In Complex With A Benzamido-N- Acetyllactoseamine Inhibitor" 54.80 138 100.00 100.00 6.74e-95 PDB 3AYA "Crystal Structure Of Galectin-3 Crd Domian Complexed With Thomsen- Friedenreich Antigen" 54.00 135 99.26 100.00 6.90e-93 PDB 3AYC "Crystal Structure Of Galectin-3 Crd Domian Complexed With Gm1 Pentasaccharide" 54.00 135 99.26 100.00 6.90e-93 PDB 3AYD "Crystal Structure Of Galectin-3 Crd Domian Complexed With Tfn" 54.00 135 99.26 100.00 6.90e-93 PDB 3AYE "Crystal Structure Of Galectin-3 Crd Domian Complexed With Lactose" 54.00 135 99.26 100.00 6.90e-93 PDB 3T1L "Crystal Structure Of Human Galectin-3 In Complex With Methyl 2-o- Acetyl-3-o-toluoyl-beta-d-talopyranoside" 57.20 143 100.00 100.00 1.35e-98 PDB 3T1M "Crystal Structure Of Human Galectin-3 Carbohydrate Recognition Domain In Complex With Methyl 3-deoxy-2-o-toluoyl-3-n-toluoyl-be" 57.20 143 100.00 100.00 1.35e-98 PDB 3ZSJ "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose At 0.86 Angstrom Resolution" 55.20 138 100.00 100.00 1.90e-95 PDB 3ZSK "Crystal Structure Of Human Galectin-3 Crd With Glycerol Bound At 0.90 Angstrom Resolution" 54.80 138 100.00 100.00 7.44e-95 PDB 3ZSL "Crystal Structure Of Apo Human Galectin-3 Crd At 1.08 Angstrom Resolution, At Cryogenic Temperature" 54.80 138 100.00 100.00 7.44e-95 PDB 3ZSM "Crystal Structure Of Apo Human Galectin-3 Crd At 1.25 Angstrom Resolution, At Room Temperature" 54.80 138 100.00 100.00 7.44e-95 PDB 4BLI "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 1" 54.80 138 100.00 100.00 7.44e-95 PDB 4BLJ "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 2" 54.80 138 100.00 100.00 7.44e-95 PDB 4BM8 "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 3" 54.80 138 100.00 100.00 6.74e-95 PDB 4JC1 "Galectin-3 Carbohydrate Recognition Domain In Complex With Thiodigalactoside" 57.20 143 100.00 100.00 1.35e-98 PDB 4JCK "Galectin-3 Carbohydrate Recognition Domain In Complex With Thioditaloside" 57.20 143 100.00 100.00 1.35e-98 PDB 4LBJ "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnt" 54.80 138 99.27 99.27 8.35e-94 PDB 4LBK "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnnt" 54.80 138 99.27 99.27 8.35e-94 PDB 4LBL "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With A-gm3" 54.80 138 99.27 99.27 8.35e-94 PDB 4LBM "Crystal Structure Of Human Galectin-3 Crd In Complex With Lnt" 55.60 139 100.00 100.00 3.97e-96 PDB 4LBN "Crystal Structure Of Human Galectin-3 Crd In Complex With Lnnt" 55.60 139 100.00 100.00 3.97e-96 PDB 4LBO "Crystal Structure Of Human Galectin-3 Crd In Complex With A-gm3" 55.20 138 100.00 100.00 1.90e-95 PDB 4R9A "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.0, Peg4000)" 56.00 144 100.00 100.00 8.38e-97 PDB 4R9B "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.0, Peg 6000)" 56.00 144 100.00 100.00 8.38e-97 PDB 4R9C "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.5, Peg6000)" 56.00 144 100.00 100.00 8.38e-97 PDB 4R9D "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.9, Peg6000)" 56.00 144 100.00 100.00 8.38e-97 PDB 4RL7 "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.5, Peg6000)" 56.00 144 100.00 100.00 8.38e-97 PDB 4XBN "Crystal Structure Of Human Galectin-3 Crd In Complex With Type 1 N- Acetyllactosamine" 55.20 158 100.00 100.00 2.04e-95 DBJ BAA22164 "galectin-3 [Homo sapiens]" 100.00 250 99.20 99.20 1.02e-173 DBJ BAD92628 "LGALS3 protein variant [Homo sapiens]" 100.00 258 97.20 98.00 6.20e-170 DBJ BAG37435 "unnamed protein product [Homo sapiens]" 100.00 250 100.00 100.00 4.25e-176 DBJ BAI46476 "lectin, galactoside-binding, soluble, 3 [synthetic construct]" 100.00 250 99.20 99.20 1.02e-173 EMBL CAG33178 "LGALS3 [Homo sapiens]" 100.00 250 99.20 99.20 1.02e-173 EMBL CAG46894 "LGALS3 [Homo sapiens]" 100.00 250 99.20 99.20 1.37e-173 GB AAA35607 "IgE-binding protein [Homo sapiens]" 100.00 250 100.00 100.00 4.25e-176 GB AAA36163 "laminin-binding protein [Homo sapiens]" 100.00 250 100.00 100.00 4.25e-176 GB AAA88086 "galactose-specific lectin [Homo sapiens]" 100.00 250 99.60 99.60 2.21e-174 GB AAB26229 "carbohydrate binding protein 35 [Homo sapiens]" 100.00 250 99.20 99.20 1.02e-173 GB AAB86584 "galectin 3 [Homo sapiens]" 100.00 250 99.20 99.20 1.02e-173 REF NP_001170859 "galectin-3 isoform 2 [Homo sapiens]" 69.60 200 98.28 98.28 8.78e-111 REF NP_002297 "galectin-3 isoform 1 [Homo sapiens]" 100.00 250 99.20 99.20 1.02e-173 REF XP_001148424 "PREDICTED: galectin-3 [Pan troglodytes]" 100.00 250 98.00 98.40 1.79e-171 REF XP_002824813 "PREDICTED: galectin-3 [Pongo abelii]" 100.00 250 98.40 98.40 1.65e-171 REF XP_003831735 "PREDICTED: galectin-3 [Pan paniscus]" 100.00 250 98.40 98.80 1.76e-172 SP P17931 "RecName: Full=Galectin-3; Short=Gal-3; AltName: Full=35 kDa lectin; AltName: Full=Carbohydrate-binding protein 35; Short=CBP 35" 100.00 250 99.20 99.20 1.02e-173 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $Galectin-3 Human 9606 Eukaryota Metazoa Homo sapiens 'Gal-3 protein with P64H and T98P mutations has been sequenced from human patients with progressive cancer.' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Galectin-3 'recombinant technology' . Escherichia coli . prCBP35s stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 0.4 mM [15N]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 0.4 mM '[U-98% 15N]' DSS 2 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 8 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 40 uM {15N]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 40 uM '[U-98% 15N]' DSS 1 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 8 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 20 uM [15N]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 20 uM '[U-98% 15N]' DSS 1 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 8 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 0.4 mM [13C,15N]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 0.4 mM '[U-98% 13C; U-98% 15N]' DSS 2 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 8 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ save_sample_5 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 40 uM [15N,13C]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 40 uM '[U-98% 13C; U-98% 15N]' DSS 1 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 8 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' stop_ save_ save_sample_6 _Saveframe_category sample _Sample_type solution _Details 'Gal-3 0.27 mM [13C,15N]' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Galectin-3 0.27 mM '[U-98% 13C; U-98% 15N]' DSS 2 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' DTT 11 mM 'natural abundance' EDTA 0.1 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.114 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details 'Analysis and averaging of deposited chemical shifts' save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details 'Data collection and processing' save_ save_PACES _Saveframe_category software _Name PACES _Version . loop_ _Vendor _Address _Electronic_address 'Coggins and Zhou' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details ; PACES: Protein sequential assignment by computer-assisted exhaustive search. Coggins and Zhou, J Biomol NMR. (2003), 26(2):93-111. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Avance_900 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details ; Bruker Avance 900 MHz with 13C,15N,1H cryoprobe ; save_ save_Avance_700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details ; Bruker Avance 700 MHz with 13C,15N,1H cryoprobe ; save_ save_Avance_HD_700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details ; Bruker Avance HD 700 MHz with 13C,15N,1H cryoprobe ; save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_3 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_4 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_5 save_ save_2D_1H-13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_6 save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_4 save_ save_3D_HNCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_4 save_ save_3D_CBCA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_4 save_ save_3D_CBCA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_5 save_ save_3D_HNCACB_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_4 save_ save_3D_CC(CO)NH_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CC(CO)NH' _Sample_label $sample_4 save_ save_3D_HN(CA)CO_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_4 save_ save_3D_HBHA(CO)NH_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_4 save_ save_3D_HNHA_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_4 save_ save_3D_HcCH_DIPSI_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HcCH DIPSI' _Sample_label $sample_4 save_ save_3D_HcCH_DIPSI_18 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HcCH DIPSI' _Sample_label $sample_6 save_ save_3D_hCCH_DIPSI_19 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCCH DIPSI' _Sample_label $sample_6 save_ save_3D_1H-15N_NOESY_20 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_21 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_22 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_2D_C_CON_23 _Saveframe_category NMR_applied_experiment _Experiment_name '2D C_CON' _Sample_label $sample_1 save_ save_2D_C_CACO_24 _Saveframe_category NMR_applied_experiment _Experiment_name '2D C_CACO' _Sample_label $sample_1 save_ save_2D_C_CAN_25 _Saveframe_category NMR_applied_experiment _Experiment_name '2D C_CAN' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'Standard sample conditions galectin-3' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.8 0.1 pH pressure 1 . atm temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; 1H chemical shift are referenced to internal DSS (present at trace concentrations of 1 to 2 uM). 15N chemical shifts are referenced indirectly by the chemical shift ratio 0.101329118 (IUPAC) 13C chemical shifts are externally referenced to DSS 0 ppm from a natural abundance 13C-1H HSQC spectrum of DSS 20 mM recorded under similar conditions as the protein sample. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details ; Estimated error limits of chemical shifts are based upon the standard error in average chemical shift position of corresponding resonance lines across different NMR spectra. Typical standard errors of the average position of resonances taken over different spectra and sample preparations are 0.005 ppm for 1H, 0.06 ppm for 13C and 0.07 ppm for 15N. Number of equivalent peak positions per assigned resonance is considered as a Figure of Merit tohave an indicator of accurate shifts. Tbis number is given in column _Atom_chem_shift.Assign_fig_of_merit of the chemical shift table. No stereospecific assignments have been carried out for the protein and prochiral methylene and methyl groups are therefore listed as unambiguously assignments. Because of the highly repetative sequence parts PGAYP that are present in the first N-terminal region of the protein (1-109), the following residues must be considered interresidue ambiguous (index type 5) and the corresponding PGAYP resonances may well be interchangeable seen in terms of a five-amino stretch. P42 = P51 G43 = G52 A44 = A52 Y45 = Y53 P46 = P54 G47 = G55 Q48 = Q57 A49 = A58 P50 = P59 P67 = P98 G68 = G99 A69 = A100 Y70 = Y101 P71 = P102 ; loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D CC(CO)NH' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D HNHA' '3D HN(CO)CA' '3D HcCH DIPSI' '3D hCCH DIPSI' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D C_CON' '2D C_CACO' '2D C_CAN' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Galectin-3, trans form, 1 (major form)' _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 2 2 ALA H H 8.238 0.01 . 2 2 2 ALA HA H 4.241 0.01 . 3 2 2 ALA HB H 1.345 0.01 . 4 2 2 ALA C C 177.888 0.1 . 5 2 2 ALA CA C 52.716 0.1 . 6 2 2 ALA CB C 19.404 0.1 . 7 2 2 ALA N N 129.426 0.1 . 8 3 3 ASP H H 8.301 0.01 . 9 3 3 ASP HA H 4.517 0.01 . 10 3 3 ASP HB2 H 2.581 0.01 . 11 3 3 ASP HB3 H 2.581 0.01 . 12 3 3 ASP C C 176.051 0.1 . 13 3 3 ASP CA C 54.205 0.1 . 14 3 3 ASP CB C 41.149 0.1 . 15 3 3 ASP N N 118.321 0.1 . 16 4 4 ASN H H 8.176 0.01 . 17 4 4 ASN HA H 4.625 0.01 . 18 4 4 ASN HB2 H 2.721 0.01 . 19 4 4 ASN HB3 H 2.645 0.01 . 20 4 4 ASN HD21 H 7.470 0.01 . 21 4 4 ASN HD22 H 6.816 0.01 . 22 4 4 ASN C C 175.106 0.1 . 23 4 4 ASN CA C 53.360 0.1 . 24 4 4 ASN CB C 38.782 0.1 . 25 4 4 ASN CG C 177.137 0.1 . 26 4 4 ASN N N 118.384 0.1 . 27 4 4 ASN ND2 N 112.259 0.1 . 28 5 5 PHE H H 8.155 0.01 . 29 5 5 PHE HA H 4.583 0.01 . 30 5 5 PHE HB2 H 3.159 0.01 . 31 5 5 PHE HB3 H 3.037 0.01 . 32 5 5 PHE C C 175.870 0.1 . 33 5 5 PHE CA C 58.138 0.1 . 34 5 5 PHE CB C 39.386 0.1 . 35 5 5 PHE N N 120.324 0.1 . 36 6 6 SER H H 8.158 0.01 . 37 6 6 SER HA H 4.390 0.01 . 38 6 6 SER HB2 H 3.805 0.01 . 39 6 6 SER HB3 H 3.805 0.01 . 40 6 6 SER C C 174.462 0.1 . 41 6 6 SER CA C 58.398 0.1 . 42 6 6 SER CB C 63.927 0.1 . 43 6 6 SER N N 116.964 0.1 . 44 7 7 LEU H H 8.097 0.01 . 45 7 7 LEU HA H 4.252 0.01 . 46 7 7 LEU HB2 H 1.546 0.01 . 47 7 7 LEU HB3 H 1.509 0.01 . 48 7 7 LEU HG H 1.539 0.01 . 49 7 7 LEU HD1 H 0.896 0.01 . 50 7 7 LEU HD2 H 0.840 0.01 . 51 7 7 LEU C C 177.286 0.1 . 52 7 7 LEU CA C 55.637 0.1 . 53 7 7 LEU CB C 42.264 0.1 . 54 7 7 LEU CG C 27.040 0.1 . 55 7 7 LEU CD1 C 24.943 0.1 . 56 7 7 LEU CD2 C 23.710 0.1 . 57 7 7 LEU N N 123.605 0.1 . 58 8 8 HIS H H 8.115 0.01 . 59 8 8 HIS HA H 4.530 0.01 . 60 8 8 HIS HB2 H 3.116 0.01 . 61 8 8 HIS HB3 H 3.042 0.01 . 62 8 8 HIS C C 175.317 0.1 . 63 8 8 HIS CA C 56.647 0.1 . 64 8 8 HIS CB C 30.588 0.1 . 65 8 8 HIS N N 118.959 0.1 . 66 9 9 ASP H H 8.134 0.01 . 67 9 9 ASP HA H 4.528 0.01 . 68 9 9 ASP HB2 H 2.654 0.01 . 69 9 9 ASP HB3 H 2.599 0.01 . 70 9 9 ASP C C 176.413 0.1 . 71 9 9 ASP CA C 54.586 0.1 . 72 9 9 ASP CB C 41.267 0.1 . 73 9 9 ASP N N 121.228 0.1 . 74 10 10 ALA H H 8.229 0.01 . 75 10 10 ALA HA H 4.244 0.01 . 76 10 10 ALA HB H 1.401 0.01 . 77 10 10 ALA C C 178.269 0.1 . 78 10 10 ALA CA C 53.249 0.1 . 79 10 10 ALA CB C 19.103 0.1 . 80 10 10 ALA N N 124.125 0.1 . 81 11 11 LEU H H 8.149 0.01 . 82 11 11 LEU HA H 4.342 0.01 . 83 11 11 LEU HB2 H 1.698 0.01 . 84 11 11 LEU HB3 H 1.602 0.01 . 85 11 11 LEU HG H 1.620 0.01 . 86 11 11 LEU HD1 H 0.897 0.01 . 87 11 11 LEU HD2 H 0.847 0.01 . 88 11 11 LEU C C 177.948 0.1 . 89 11 11 LEU CA C 55.449 0.1 . 90 11 11 LEU CB C 42.144 0.1 . 91 11 11 LEU CG C 27.053 0.1 . 92 11 11 LEU CD1 C 24.952 0.1 . 93 11 11 LEU CD2 C 23.404 0.1 . 94 11 11 LEU N N 119.459 0.1 . 95 12 12 SER H H 8.066 0.01 . 96 12 12 SER HA H 4.397 0.01 . 97 12 12 SER HB2 H 3.878 0.01 . 98 12 12 SER HB3 H 3.878 0.01 . 99 12 12 SER C C 175.291 0.1 . 100 12 12 SER CA C 58.913 0.1 . 101 12 12 SER CB C 63.860 0.1 . 102 12 12 SER N N 115.475 0.1 . 103 13 13 GLY H H 8.305 0.01 . 104 13 13 GLY HA2 H 3.992 0.01 . 105 13 13 GLY HA3 H 3.992 0.01 . 106 13 13 GLY C C 174.449 0.1 . 107 13 13 GLY CA C 45.557 0.1 . 108 13 13 GLY N N 110.617 0.1 . 109 14 14 SER H H 8.181 0.01 . 110 14 14 SER HA H 4.444 0.01 . 111 14 14 SER HB2 H 3.893 0.01 . 112 14 14 SER HB3 H 3.859 0.01 . 113 14 14 SER C C 174.999 0.1 . 114 14 14 SER CA C 58.670 0.1 . 115 14 14 SER CB C 63.977 0.1 . 116 14 14 SER N N 115.370 0.1 . 117 15 15 GLY H H 8.380 0.01 . 118 15 15 GLY HA2 H 3.921 0.01 . 119 15 15 GLY HA3 H 3.921 0.01 . 120 15 15 GLY C C 173.448 0.1 . 121 15 15 GLY CA C 45.200 0.1 . 122 15 15 GLY N N 110.280 0.1 . 123 16 16 ASN H H 8.160 0.01 . 124 16 16 ASN HA H 4.924 0.01 . 125 16 16 ASN HB2 H 2.787 0.01 . 126 16 16 ASN HB3 H 2.625 0.01 . 127 16 16 ASN HD21 H 7.536 0.01 . 128 16 16 ASN HD22 H 6.879 0.01 . 129 16 16 ASN C C 173.424 0.1 . 130 16 16 ASN CA C 51.193 0.1 . 131 16 16 ASN CB C 38.930 0.1 . 132 16 16 ASN CG C 176.973 0.1 . 133 16 16 ASN N N 119.427 0.1 . 134 16 16 ASN ND2 N 112.496 0.1 . 135 17 17 PRO HA H 4.392 0.01 . 136 17 17 PRO HB2 H 2.196 0.01 . 137 17 17 PRO HB3 H 1.887 0.01 . 138 17 17 PRO C C 176.287 0.1 . 139 17 17 PRO CA C 63.340 0.1 . 140 17 17 PRO CB C 32.142 0.1 . 141 17 17 PRO CG C 26.970 0.1 . 142 17 17 PRO CD C 50.721 0.1 . 143 17 17 PRO N N 136.113 0.1 . 144 18 18 ASN H H 8.327 0.01 . 145 18 18 ASN HA H 4.900 0.01 . 146 18 18 ASN HB2 H 2.724 0.01 . 147 18 18 ASN HB3 H 2.620 0.01 . 148 18 18 ASN HD21 H 7.499 0.01 . 149 18 18 ASN HD22 H 6.892 0.01 . 150 18 18 ASN C C 173.343 0.1 . 151 18 18 ASN CA C 51.376 0.1 . 152 18 18 ASN CB C 38.857 0.1 . 153 18 18 ASN CG C 177.122 0.1 . 154 18 18 ASN N N 118.870 0.1 . 155 18 18 ASN ND2 N 112.621 0.1 . 156 19 19 PRO HA H 4.288 0.01 . 157 19 19 PRO HB2 H 2.179 0.01 . 158 19 19 PRO HB3 H 1.867 0.01 . 159 19 19 PRO C C 177.057 0.1 . 160 19 19 PRO CA C 63.715 0.1 . 161 19 19 PRO CB C 32.041 0.1 . 162 19 19 PRO CG C 27.189 0.1 . 163 19 19 PRO CD C 50.501 0.1 . 164 19 19 PRO N N 136.939 0.1 . 165 20 20 GLN H H 8.309 0.01 . 166 20 20 GLN HA H 4.238 0.01 . 167 20 20 GLN HB2 H 2.033 0.01 . 168 20 20 GLN HB3 H 1.893 0.01 . 169 20 20 GLN HG2 H 2.294 0.01 . 170 20 20 GLN HG3 H 2.294 0.01 . 171 20 20 GLN HE21 H 7.420 0.01 . 172 20 20 GLN HE22 H 6.802 0.01 . 173 20 20 GLN C C 176.387 0.1 . 174 20 20 GLN CA C 56.105 0.1 . 175 20 20 GLN CB C 29.226 0.1 . 176 20 20 GLN CG C 34.006 0.1 . 177 20 20 GLN CD C 180.393 0.1 . 178 20 20 GLN N N 118.856 0.1 . 179 20 20 GLN NE2 N 111.999 0.1 . 180 21 21 GLY H H 8.109 0.01 . 181 21 21 GLY HA2 H 3.858 0.01 . 182 21 21 GLY HA3 H 3.858 0.01 . 183 21 21 GLY C C 173.353 0.1 . 184 21 21 GLY CA C 45.246 0.1 . 185 21 21 GLY N N 108.956 0.1 . 186 22 22 TRP H H 7.952 0.01 . 187 22 22 TRP HA H 4.906 0.01 . 188 22 22 TRP HB2 H 3.241 0.01 . 189 22 22 TRP HB3 H 3.119 0.01 . 190 22 22 TRP HD1 H 7.174 0.01 . 191 22 22 TRP HE1 H 10.096 0.01 . 192 22 22 TRP C C 174.651 0.1 . 193 22 22 TRP CA C 54.963 0.1 . 194 22 22 TRP CB C 29.266 0.1 . 195 22 22 TRP N N 122.077 0.1 . 196 22 22 TRP NE1 N 129.490 0.1 . 197 23 23 PRO HA H 4.261 0.01 . 198 23 23 PRO HB2 H 2.095 0.01 . 199 23 23 PRO HB3 H 1.734 0.01 . 200 23 23 PRO C C 177.202 0.1 . 201 23 23 PRO CA C 63.596 0.1 . 202 23 23 PRO CB C 31.785 0.1 . 203 23 23 PRO CG C 27.216 0.1 . 204 23 23 PRO CD C 50.828 0.1 . 205 23 23 PRO N N 135.065 0.1 . 206 24 24 GLY H H 7.564 0.01 . 207 24 24 GLY HA2 H 3.670 0.01 . 208 24 24 GLY HA3 H 3.670 0.01 . 209 24 24 GLY C C 173.992 0.1 . 210 24 24 GLY CA C 45.302 0.1 . 211 24 24 GLY N N 108.033 0.1 . 212 25 25 ALA H H 7.867 0.01 . 213 25 25 ALA HA H 4.231 0.01 . 214 25 25 ALA HB H 1.198 0.01 . 215 25 25 ALA C C 177.514 0.1 . 216 25 25 ALA CA C 52.663 0.1 . 217 25 25 ALA CB C 19.165 0.1 . 218 25 25 ALA N N 122.654 0.1 . 219 26 26 TRP H H 7.983 0.01 . 220 26 26 TRP HA H 4.631 0.01 . 221 26 26 TRP HB2 H 3.286 0.01 . 222 26 26 TRP HB3 H 3.157 0.01 . 223 26 26 TRP HD1 H 7.132 0.01 . 224 26 26 TRP HE1 H 10.079 0.01 . 225 26 26 TRP C C 176.758 0.1 . 226 26 26 TRP CA C 57.267 0.1 . 227 26 26 TRP CB C 29.586 0.1 . 228 26 26 TRP N N 119.345 0.1 . 229 26 26 TRP NE1 N 129.105 0.1 . 230 27 27 GLY H H 8.073 0.01 . 231 27 27 GLY HA2 H 3.887 0.01 . 232 27 27 GLY HA3 H 3.806 0.01 . 233 27 27 GLY C C 173.765 0.1 . 234 27 27 GLY CA C 45.486 0.1 . 235 27 27 GLY N N 109.308 0.1 . 236 28 28 ASN H H 8.179 0.01 . 237 28 28 ASN HA H 4.664 0.01 . 238 28 28 ASN HB2 H 2.765 0.01 . 239 28 28 ASN HB3 H 2.680 0.01 . 240 28 28 ASN HD21 H 7.484 0.01 . 241 28 28 ASN HD22 H 6.856 0.01 . 242 28 28 ASN C C 174.825 0.1 . 243 28 28 ASN CA C 53.125 0.1 . 244 28 28 ASN CB C 38.924 0.1 . 245 28 28 ASN N N 118.268 0.1 . 246 28 28 ASN ND2 N 112.190 0.1 . 247 29 29 GLN H H 8.190 0.01 . 248 29 29 GLN HA H 4.500 0.01 . 249 29 29 GLN HB2 H 2.026 0.01 . 250 29 29 GLN HB3 H 1.855 0.01 . 251 29 29 GLN HG2 H 2.276 0.01 . 252 29 29 GLN HG3 H 2.276 0.01 . 253 29 29 GLN HE21 H 7.374 0.01 . 254 29 29 GLN HE22 H 6.747 0.01 . 255 29 29 GLN C C 173.836 0.1 . 256 29 29 GLN CA C 53.824 0.1 . 257 29 29 GLN CB C 28.947 0.1 . 258 29 29 GLN CG C 33.472 0.1 . 259 29 29 GLN CD C 180.338 0.1 . 260 29 29 GLN N N 120.933 0.1 . 261 29 29 GLN NE2 N 111.842 0.1 . 262 30 30 PRO HA H 4.346 0.01 . 263 30 30 PRO HB2 H 2.215 0.01 . 264 30 30 PRO HB3 H 1.855 0.01 . 265 30 30 PRO C C 176.635 0.1 . 266 30 30 PRO CA C 63.172 0.1 . 267 30 30 PRO CB C 32.079 0.1 . 268 30 30 PRO CG C 27.401 0.1 . 269 30 30 PRO CD C 50.618 0.1 . 270 30 30 PRO N N 137.023 0.1 . 271 31 31 ALA H H 8.337 0.01 . 272 31 31 ALA HA H 4.212 0.01 . 273 31 31 ALA HB H 1.324 0.01 . 274 31 31 ALA C C 178.333 0.1 . 275 31 31 ALA CA C 52.730 0.1 . 276 31 31 ALA CB C 19.184 0.1 . 277 31 31 ALA N N 123.948 0.1 . 278 32 32 GLY H H 8.232 0.01 . 279 32 32 GLY HA2 H 3.898 0.01 . 280 32 32 GLY HA3 H 3.898 0.01 . 281 32 32 GLY C C 174.041 0.1 . 282 32 32 GLY CA C 45.297 0.1 . 283 32 32 GLY N N 107.983 0.1 . 284 33 33 ALA H H 8.099 0.01 . 285 33 33 ALA HA H 4.293 0.01 . 286 33 33 ALA HB H 1.357 0.01 . 287 33 33 ALA C C 178.164 0.1 . 288 33 33 ALA CA C 52.703 0.1 . 289 33 33 ALA CB C 19.356 0.1 . 290 33 33 ALA N N 123.561 0.1 . 291 34 34 GLY H H 8.331 0.01 . 292 34 34 GLY HA2 H 3.892 0.01 . 293 34 34 GLY HA3 H 3.892 0.01 . 294 34 34 GLY C C 174.410 0.1 . 295 34 34 GLY CA C 45.348 0.1 . 296 34 34 GLY N N 107.625 0.1 . 297 35 35 GLY H H 8.039 0.01 . 298 35 35 GLY HA2 H 3.841 0.01 . 299 35 35 GLY HA3 H 3.841 0.01 . 300 35 35 GLY C C 173.208 0.1 . 301 35 35 GLY CA C 44.957 0.1 . 302 35 35 GLY N N 107.759 0.1 . 303 36 36 TYR H H 7.981 0.01 . 304 36 36 TYR HA H 4.719 0.01 . 305 36 36 TYR HB2 H 2.952 0.01 . 306 36 36 TYR HB3 H 2.822 0.01 . 307 36 36 TYR HD1 H 7.034 0.01 . 308 36 36 TYR HD2 H 7.034 0.01 . 309 36 36 TYR C C 174.311 0.1 . 310 36 36 TYR CA C 55.780 0.1 . 311 36 36 TYR CB C 38.538 0.1 . 312 36 36 TYR N N 120.985 0.1 . 313 37 37 PRO HA H 4.339 0.01 . 314 37 37 PRO HB2 H 2.150 0.01 . 315 37 37 PRO HB3 H 1.865 0.01 . 316 37 37 PRO C C 177.126 0.1 . 317 37 37 PRO CA C 63.676 0.1 . 318 37 37 PRO CB C 31.824 0.1 . 319 37 37 PRO CG C 27.394 0.1 . 320 37 37 PRO CD C 50.625 0.1 . 321 37 37 PRO N N 138.244 0.1 . 322 38 38 GLY H H 7.966 0.01 . 323 38 38 GLY HA2 H 3.871 0.01 . 324 38 38 GLY HA3 H 3.871 0.01 . 325 38 38 GLY C C 173.807 0.1 . 326 38 38 GLY CA C 45.253 0.1 . 327 38 38 GLY N N 108.852 0.1 . 328 39 39 ALA H H 7.948 0.01 . 329 39 39 ALA HA H 4.285 0.01 . 330 39 39 ALA HB H 1.287 0.01 . 331 39 39 ALA C C 177.337 0.1 . 332 39 39 ALA CA C 52.435 0.1 . 333 39 39 ALA CB C 19.598 0.1 . 334 39 39 ALA N N 123.003 0.1 . 335 40 40 SER H H 8.118 0.01 . 336 40 40 SER HA H 4.424 0.01 . 337 40 40 SER HB2 H 3.752 0.01 . 338 40 40 SER HB3 H 3.752 0.01 . 339 40 40 SER C C 173.395 0.1 . 340 40 40 SER CA C 58.023 0.1 . 341 40 40 SER CB C 64.071 0.1 . 342 40 40 SER N N 114.243 0.1 . 343 41 41 TYR H H 8.035 0.01 . 344 41 41 TYR HA H 4.740 0.01 . 345 41 41 TYR HB2 H 2.971 0.01 . 346 41 41 TYR HB3 H 2.820 0.01 . 347 41 41 TYR C C 174.018 0.1 . 348 41 41 TYR CA C 55.705 0.1 . 349 41 41 TYR CB C 38.560 0.1 . 350 41 41 TYR N N 122.518 0.1 . 351 42 42 PRO C C 177.072 0.1 . 352 42 42 PRO CA C 63.681 0.1 . 353 42 42 PRO CB C 31.815 0.1 . 354 42 42 PRO N N 137.090 0.1 . 355 43 43 GLY H H 7.967 0.01 . 356 43 43 GLY HA2 H 3.867 0.01 . 357 43 43 GLY HA3 H 3.867 0.01 . 358 43 43 GLY C C 173.477 0.1 . 359 43 43 GLY CA C 45.213 0.1 . 360 43 43 GLY N N 108.851 0.1 . 361 44 44 ALA H H 7.876 0.01 . 362 44 44 ALA HA H 4.248 0.01 . 363 44 44 ALA HB H 1.221 0.01 . 364 44 44 ALA C C 176.847 0.1 . 365 44 44 ALA CA C 52.284 0.1 . 366 44 44 ALA CB C 19.659 0.1 . 367 44 44 ALA N N 122.749 0.1 . 368 45 45 TYR H H 8.064 0.01 . 369 45 45 TYR HA H 4.753 0.01 . 370 45 45 TYR HB2 H 3.018 0.01 . 371 45 45 TYR HB3 H 2.816 0.01 . 372 45 45 TYR C C 174.120 0.1 . 373 45 45 TYR CA C 55.655 0.1 . 374 45 45 TYR CB C 38.455 0.1 . 375 45 45 TYR N N 120.020 0.1 . 376 46 46 PRO HA H 4.343 0.01 . 377 46 46 PRO HB2 H 2.174 0.01 . 378 46 46 PRO HB3 H 1.884 0.01 . 379 46 46 PRO CA C 63.670 0.1 . 380 46 46 PRO CB C 31.831 0.1 . 381 47 47 GLY H H 8.023 0.01 . 382 47 47 GLY C C 173.916 0.1 . 383 47 47 GLY CA C 45.354 0.1 . 384 47 47 GLY N N 108.908 0.1 . 385 48 48 GLN H H 8.009 0.01 . 386 48 48 GLN HA H 4.578 0.01 . 387 48 48 GLN HB2 H 2.054 0.01 . 388 48 48 GLN HB3 H 1.890 0.01 . 389 48 48 GLN HG2 H 2.301 0.01 . 390 48 48 GLN HG3 H 2.301 0.01 . 391 48 48 GLN HE21 H 7.498 0.01 . 392 48 48 GLN HE22 H 6.795 0.01 . 393 48 48 GLN C C 175.257 0.1 . 394 48 48 GLN CA C 55.681 0.1 . 395 48 48 GLN CB C 29.807 0.1 . 396 48 48 GLN CG C 33.896 0.1 . 397 48 48 GLN CD C 180.517 0.1 . 398 48 48 GLN N N 119.459 0.1 . 399 48 48 GLN NE2 N 111.972 0.1 . 400 49 49 ALA H H 8.306 0.01 . 401 49 49 ALA HA H 4.496 0.01 . 402 49 49 ALA HB H 1.280 0.01 . 403 49 49 ALA C C 174.773 0.1 . 404 49 49 ALA CA C 50.464 0.1 . 405 49 49 ALA CB C 18.260 0.1 . 406 49 49 ALA N N 126.768 0.1 . 407 50 50 PRO HA H 4.596 0.01 . 408 50 50 PRO HB2 H 2.250 0.01 . 409 50 50 PRO HB3 H 1.838 0.01 . 410 50 50 PRO HG2 H 1.943 0.01 . 411 50 50 PRO HG3 H 1.943 0.01 . 412 50 50 PRO HD2 H 3.696 0.01 . 413 50 50 PRO HD3 H 3.462 0.01 . 414 50 50 PRO C C 174.417 0.1 . 415 50 50 PRO CA C 61.432 0.1 . 416 50 50 PRO CB C 30.743 0.1 . 417 50 50 PRO CG C 27.430 0.1 . 418 50 50 PRO CD C 50.435 0.1 . 419 50 50 PRO N N 136.328 0.1 . 420 51 51 PRO C C 177.527 0.1 . 421 51 51 PRO CA C 63.464 0.1 . 422 52 52 GLY H H 8.367 0.01 . 423 52 52 GLY HA2 H 3.865 0.01 . 424 52 52 GLY HA3 H 3.865 0.01 . 425 52 52 GLY C C 173.509 0.1 . 426 52 52 GLY CA C 45.214 0.1 . 427 52 52 GLY N N 108.979 0.1 . 428 53 53 ALA H H 7.875 0.01 . 429 53 53 ALA HA H 4.242 0.01 . 430 53 53 ALA C C 176.843 0.1 . 431 53 53 ALA CA C 52.311 0.1 . 432 53 53 ALA CB C 19.673 0.1 . 433 53 53 ALA N N 122.763 0.1 . 434 54 54 TYR H H 8.066 0.01 . 435 54 54 TYR C C 174.116 0.1 . 436 54 54 TYR N N 120.035 0.1 . 437 55 55 PRO HA H 4.345 0.01 . 438 55 55 PRO HB2 H 2.164 0.01 . 439 55 55 PRO HB3 H 1.884 0.01 . 440 55 55 PRO C C 177.239 0.1 . 441 55 55 PRO CA C 63.645 0.1 . 442 55 55 PRO CB C 31.804 0.1 . 443 55 55 PRO CG C 27.326 0.1 . 444 55 55 PRO CD C 50.498 0.1 . 445 55 55 PRO N N 137.687 0.1 . 446 56 56 GLY H H 8.115 0.01 . 447 56 56 GLY HA2 H 3.965 0.01 . 448 56 56 GLY HA3 H 3.872 0.01 . 449 56 56 GLY C C 173.914 0.1 . 450 56 56 GLY CA C 45.315 0.1 . 451 56 56 GLY N N 109.184 0.1 . 452 57 57 GLN H H 8.008 0.01 . 453 57 57 GLN HA H 4.315 0.01 . 454 57 57 GLN HB2 H 2.063 0.01 . 455 57 57 GLN HB3 H 1.890 0.01 . 456 57 57 GLN HG2 H 2.304 0.01 . 457 57 57 GLN HG3 H 2.304 0.01 . 458 57 57 GLN HE21 H 7.497 0.01 . 459 57 57 GLN HE22 H 6.795 0.01 . 460 57 57 GLN C C 175.261 0.1 . 461 57 57 GLN CA C 55.589 0.1 . 462 57 57 GLN CB C 29.807 0.1 . 463 57 57 GLN CG C 33.833 0.1 . 464 57 57 GLN CD C 180.520 0.1 . 465 57 57 GLN N N 119.453 0.1 . 466 57 57 GLN NE2 N 111.977 0.1 . 467 58 58 ALA H H 8.306 0.01 . 468 58 58 ALA HA H 4.497 0.01 . 469 58 58 ALA HB H 1.277 0.01 . 470 58 58 ALA C C 174.772 0.1 . 471 58 58 ALA CA C 50.437 0.1 . 472 58 58 ALA CB C 18.285 0.1 . 473 58 58 ALA N N 126.762 0.1 . 474 59 59 PRO HA H 4.619 0.01 . 475 59 59 PRO HB2 H 2.265 0.01 . 476 59 59 PRO HB3 H 1.851 0.01 . 477 59 59 PRO HG2 H 1.954 0.01 . 478 59 59 PRO HG3 H 1.954 0.01 . 479 59 59 PRO HD2 H 3.711 0.01 . 480 59 59 PRO HD3 H 3.483 0.01 . 481 59 59 PRO C C 174.415 0.1 . 482 59 59 PRO CA C 61.475 0.1 . 483 59 59 PRO CB C 30.804 0.1 . 484 59 59 PRO CG C 27.364 0.1 . 485 59 59 PRO CD C 50.432 0.1 . 486 59 59 PRO N N 136.342 0.1 . 487 60 60 PRO HA H 4.380 0.01 . 488 60 60 PRO C C 177.533 0.1 . 489 60 60 PRO CA C 63.463 0.1 . 490 60 60 PRO CB C 31.952 0.1 . 491 60 60 PRO CG C 27.422 0.1 . 492 60 60 PRO CD C 50.406 0.1 . 493 61 61 GLY H H 8.365 0.01 . 494 61 61 GLY HA2 H 3.879 0.01 . 495 61 61 GLY HA3 H 3.879 0.01 . 496 61 61 GLY C C 173.801 0.1 . 497 61 61 GLY CA C 45.245 0.1 . 498 61 61 GLY N N 109.000 0.1 . 499 62 62 ALA H H 7.925 0.01 . 500 62 62 ALA HA H 4.249 0.01 . 501 62 62 ALA HB H 1.227 0.01 . 502 62 62 ALA C C 177.111 0.1 . 503 62 62 ALA CA C 52.435 0.1 . 504 62 62 ALA CB C 19.480 0.1 . 505 62 62 ALA N N 122.880 0.1 . 506 63 63 TYR H H 8.032 0.01 . 507 63 63 TYR HA H 4.492 0.01 . 508 63 63 TYR HB2 H 2.918 0.01 . 509 63 63 TYR HB3 H 2.880 0.01 . 510 63 63 TYR C C 175.448 0.1 . 511 63 63 TYR CA C 57.689 0.1 . 512 63 63 TYR CB C 38.870 0.1 . 513 63 63 TYR N N 118.841 0.1 . 514 64 64 HIS HA H 4.533 0.01 . 515 64 64 HIS HB2 H 3.082 0.01 . 516 64 64 HIS HB3 H 2.945 0.01 . 517 64 64 HIS C C 175.284 0.1 . 518 64 64 HIS CA C 56.222 0.1 . 519 64 64 HIS CB C 30.872 0.1 . 520 64 64 HIS N N 122.108 0.1 . 521 65 65 GLY H H 7.651 0.01 . 522 65 65 GLY HA2 H 3.834 0.01 . 523 65 65 GLY HA3 H 3.834 0.01 . 524 65 65 GLY C C 173.042 0.1 . 525 65 65 GLY CA C 45.014 0.1 . 526 65 65 GLY N N 109.200 0.1 . 527 66 66 ALA H H 8.057 0.01 . 528 66 66 ALA HA H 4.549 0.01 . 529 66 66 ALA HB H 1.312 0.01 . 530 66 66 ALA C C 175.576 0.1 . 531 66 66 ALA CA C 50.526 0.1 . 532 66 66 ALA CB C 18.356 0.1 . 533 66 66 ALA N N 124.418 0.1 . 534 67 67 PRO CA C 63.521 0.1 . 535 67 67 PRO N N 135.627 0.1 . 536 68 68 GLY HA2 H 3.879 0.01 . 537 68 68 GLY HA3 H 3.879 0.01 . 538 68 68 GLY C C 173.513 0.1 . 539 68 68 GLY CA C 45.212 0.1 . 540 69 69 ALA H H 7.898 0.01 . 541 69 69 ALA HA H 4.266 0.01 . 542 69 69 ALA C C 176.874 0.1 . 543 69 69 ALA CA C 52.261 0.1 . 544 69 69 ALA CB C 19.650 0.1 . 545 69 69 ALA N N 122.975 0.1 . 546 71 71 PRO HA H 4.343 0.01 . 547 71 71 PRO HB2 H 2.179 0.01 . 548 71 71 PRO HB3 H 1.894 0.01 . 549 71 71 PRO C C 177.098 0.1 . 550 71 71 PRO CA C 63.713 0.1 . 551 71 71 PRO CB C 31.803 0.1 . 552 71 71 PRO CG C 27.381 0.1 . 553 72 72 GLY H H 8.044 0.01 . 554 72 72 GLY HA2 H 3.948 0.01 . 555 72 72 GLY HA3 H 3.831 0.01 . 556 72 72 GLY C C 173.450 0.1 . 557 72 72 GLY CA C 45.042 0.1 . 558 72 72 GLY N N 109.300 0.1 . 559 73 73 ALA H H 7.884 0.01 . 560 73 73 ALA HA H 4.480 0.01 . 561 73 73 ALA HB H 1.218 0.01 . 562 73 73 ALA C C 175.377 0.1 . 563 73 73 ALA CA C 50.523 0.1 . 564 73 73 ALA CB C 18.256 0.1 . 565 73 73 ALA N N 124.381 0.1 . 566 74 74 PRO HA H 4.377 0.01 . 567 74 74 PRO HB2 H 2.199 0.01 . 568 74 74 PRO HB3 H 1.874 0.01 . 569 74 74 PRO C C 176.136 0.1 . 570 74 74 PRO CA C 62.845 0.1 . 571 74 74 PRO CB C 31.999 0.1 . 572 74 74 PRO CG C 27.392 0.1 . 573 74 74 PRO CD C 50.533 0.1 . 574 74 74 PRO N N 135.867 0.1 . 575 75 75 ALA H H 8.239 0.01 . 576 75 75 ALA HA H 4.527 0.01 . 577 75 75 ALA HB H 1.320 0.01 . 578 75 75 ALA C C 175.393 0.1 . 579 75 75 ALA CA C 50.359 0.1 . 580 75 75 ALA CB C 18.279 0.1 . 581 75 75 ALA N N 125.119 0.1 . 582 76 76 PRO HA H 4.374 0.01 . 583 76 76 PRO HB2 H 2.242 0.01 . 584 76 76 PRO HB3 H 1.897 0.01 . 585 76 76 PRO C C 177.558 0.1 . 586 76 76 PRO CA C 63.454 0.1 . 587 76 76 PRO CB C 31.960 0.1 . 588 76 76 PRO CG C 27.463 0.1 . 589 76 76 PRO CD C 50.392 0.1 . 590 76 76 PRO N N 135.056 0.1 . 591 77 77 GLY H H 8.344 0.01 . 592 77 77 GLY HA2 H 3.878 0.01 . 593 77 77 GLY HA3 H 3.878 0.01 . 594 77 77 GLY C C 173.567 0.1 . 595 77 77 GLY CA C 45.267 0.1 . 596 77 77 GLY N N 108.965 0.1 . 597 78 78 VAL H H 7.706 0.01 . 598 78 78 VAL HA H 4.054 0.01 . 599 78 78 VAL HB H 1.957 0.01 . 600 78 78 VAL HG1 H 0.811 0.01 . 601 78 78 VAL HG2 H 0.797 0.01 . 602 78 78 VAL C C 175.365 0.1 . 603 78 78 VAL CA C 62.154 0.1 . 604 78 78 VAL CB C 32.935 0.1 . 605 78 78 VAL CG1 C 20.743 0.1 . 606 78 78 VAL CG2 C 21.104 0.1 . 607 78 78 VAL N N 118.994 0.1 . 608 79 79 TYR H H 8.338 0.01 . 609 79 79 TYR HA H 4.832 0.01 . 610 79 79 TYR HB2 H 3.013 0.01 . 611 79 79 TYR HB3 H 2.853 0.01 . 612 79 79 TYR C C 174.268 0.1 . 613 79 79 TYR CA C 55.441 0.1 . 614 79 79 TYR CB C 38.751 0.1 . 615 79 79 TYR N N 125.285 0.1 . 616 80 80 PRO HA H 4.428 0.01 . 617 80 80 PRO HB2 H 2.160 0.01 . 618 80 80 PRO HB3 H 1.942 0.01 . 619 80 80 PRO C C 176.602 0.1 . 620 80 80 PRO CA C 63.282 0.1 . 621 80 80 PRO CB C 32.016 0.1 . 622 80 80 PRO CG C 27.189 0.1 . 623 80 80 PRO CD C 50.699 0.1 . 624 80 80 PRO N N 137.102 0.1 . 625 81 81 GLY H H 7.532 0.01 . 626 81 81 GLY HA2 H 4.042 0.01 . 627 81 81 GLY HA3 H 3.974 0.01 . 628 81 81 GLY C C 170.899 0.1 . 629 81 81 GLY CA C 44.368 0.1 . 630 81 81 GLY N N 108.163 0.1 . 631 82 82 PRO HA H 4.666 0.01 . 632 82 82 PRO HB2 H 2.283 0.01 . 633 82 82 PRO HB3 H 1.910 0.01 . 634 82 82 PRO HG2 H 1.986 0.01 . 635 82 82 PRO HG3 H 1.986 0.01 . 636 82 82 PRO HD2 H 3.565 0.01 . 637 82 82 PRO HD3 H 3.565 0.01 . 638 82 82 PRO C C 174.664 0.1 . 639 82 82 PRO CA C 61.526 0.1 . 640 82 82 PRO CB C 30.872 0.1 . 641 82 82 PRO CG C 27.278 0.1 . 642 82 82 PRO CD C 49.732 0.1 . 643 82 82 PRO N N 135.157 0.1 . 644 83 83 PRO HB2 H 2.240 0.01 . 645 83 83 PRO HB3 H 1.913 0.01 . 646 83 83 PRO C C 176.893 0.1 . 647 83 83 PRO CA C 63.292 0.1 . 648 83 83 PRO CB C 31.995 0.1 . 649 83 83 PRO CG C 27.394 0.1 . 650 83 83 PRO CD C 49.885 0.1 . 651 83 83 PRO N N 138.428 0.1 . 652 84 84 SER H H 8.235 0.01 . 653 84 84 SER HA H 4.453 0.01 . 654 84 84 SER HB2 H 3.853 0.01 . 655 84 84 SER HB3 H 3.823 0.01 . 656 84 84 SER C C 174.508 0.1 . 657 84 84 SER CA C 58.156 0.1 . 658 84 84 SER CB C 64.210 0.1 . 659 84 84 SER N N 115.115 0.1 . 660 85 85 GLY H H 8.160 0.01 . 661 85 85 GLY HA2 H 4.086 0.01 . 662 85 85 GLY HA3 H 4.086 0.01 . 663 85 85 GLY C C 171.841 0.1 . 664 85 85 GLY CA C 44.712 0.1 . 665 85 85 GLY N N 110.185 0.1 . 666 86 86 PRO HA H 4.382 0.01 . 667 86 86 PRO HB2 H 2.256 0.01 . 668 86 86 PRO HB3 H 1.910 0.01 . 669 86 86 PRO C C 177.570 0.1 . 670 86 86 PRO CA C 63.523 0.1 . 671 86 86 PRO CB C 31.994 0.1 . 672 86 86 PRO CG C 27.435 0.1 . 673 86 86 PRO CD C 49.871 0.1 . 674 86 86 PRO N N 134.029 0.1 . 675 87 87 GLY H H 8.379 0.01 . 676 87 87 GLY HA2 H 3.918 0.01 . 677 87 87 GLY HA3 H 3.918 0.01 . 678 87 87 GLY C C 173.507 0.1 . 679 87 87 GLY CA C 45.213 0.1 . 680 87 87 GLY N N 109.145 0.1 . 681 88 88 ALA H H 7.906 0.01 . 682 88 88 ALA HA H 4.288 0.01 . 683 88 88 ALA HB H 1.303 0.01 . 684 88 88 ALA C C 176.292 0.1 . 685 88 88 ALA CA C 52.263 0.1 . 686 88 88 ALA CB C 19.715 0.1 . 687 88 88 ALA N N 123.203 0.1 . 688 89 89 TYR H H 8.096 0.01 . 689 89 89 TYR HA H 4.524 0.01 . 690 89 89 TYR C C 174.342 0.1 . 691 89 89 TYR CA C 55.861 0.1 . 692 89 89 TYR CB C 40.439 0.1 . 693 89 89 TYR N N 120.636 0.1 . 694 90 90 PRO HA H 4.436 0.01 . 695 90 90 PRO HB2 H 2.234 0.01 . 696 90 90 PRO HB3 H 1.917 0.01 . 697 90 90 PRO C C 176.885 0.1 . 698 90 90 PRO CA C 63.340 0.1 . 699 90 90 PRO CB C 32.060 0.1 . 700 90 90 PRO CG C 27.353 0.1 . 701 90 90 PRO N N 138.608 0.1 . 702 91 91 SER H H 8.357 0.01 . 703 91 91 SER HA H 4.468 0.01 . 704 91 91 SER HB2 H 3.914 0.01 . 705 91 91 SER HB3 H 3.914 0.01 . 706 91 91 SER C C 174.834 0.1 . 707 91 91 SER CA C 58.527 0.1 . 708 91 91 SER CB C 63.932 0.1 . 709 91 91 SER N N 116.025 0.1 . 710 92 92 SER H H 8.313 0.01 . 711 92 92 SER HA H 4.457 0.01 . 712 92 92 SER HB2 H 3.880 0.01 . 713 92 92 SER HB3 H 3.880 0.01 . 714 92 92 SER C C 174.979 0.1 . 715 92 92 SER CA C 58.653 0.1 . 716 92 92 SER CB C 63.961 0.1 . 717 92 92 SER N N 117.065 0.1 . 718 93 93 GLY HA2 H 3.954 0.01 . 719 93 93 GLY HA3 H 3.954 0.01 . 720 93 93 GLY C C 173.676 0.1 . 721 93 93 GLY CA C 45.250 0.1 . 722 94 94 GLN H H 8.114 0.01 . 723 94 94 GLN HA H 4.612 0.01 . 724 94 94 GLN HB2 H 2.081 0.01 . 725 94 94 GLN HB3 H 1.911 0.01 . 726 94 94 GLN HG2 H 2.341 0.01 . 727 94 94 GLN HG3 H 2.341 0.01 . 728 94 94 GLN HE21 H 7.493 0.01 . 729 94 94 GLN HE22 H 6.832 0.01 . 730 94 94 GLN C C 174.069 0.1 . 731 94 94 GLN CA C 53.630 0.1 . 732 94 94 GLN CB C 28.998 0.1 . 733 94 94 GLN CG C 33.502 0.1 . 734 94 94 GLN CD C 180.509 0.1 . 735 94 94 GLN N N 120.407 0.1 . 736 94 94 GLN NE2 N 112.130 0.1 . 737 95 95 PRO HA H 4.432 0.01 . 738 95 95 PRO HB2 H 2.262 0.01 . 739 95 95 PRO HB3 H 1.911 0.01 . 740 95 95 PRO C C 176.829 0.1 . 741 95 95 PRO CA C 63.313 0.1 . 742 95 95 PRO CB C 32.161 0.1 . 743 95 95 PRO CG C 27.394 0.1 . 744 95 95 PRO CD C 50.652 0.1 . 745 95 95 PRO N N 137.219 0.1 . 746 96 96 SER H H 8.316 0.01 . 747 96 96 SER HA H 4.396 0.01 . 748 96 96 SER HB2 H 3.831 0.01 . 749 96 96 SER HB3 H 3.831 0.01 . 750 96 96 SER C C 173.743 0.1 . 751 96 96 SER CA C 58.224 0.1 . 752 96 96 SER CB C 64.012 0.1 . 753 96 96 SER N N 115.839 0.1 . 754 97 97 ALA H H 8.212 0.01 . 755 97 97 ALA HA H 4.593 0.01 . 756 97 97 ALA HB H 1.337 0.01 . 757 97 97 ALA C C 175.363 0.1 . 758 97 97 ALA CA C 50.510 0.1 . 759 97 97 ALA CB C 18.505 0.1 . 760 97 97 ALA N N 126.490 0.1 . 761 98 98 PRO HA H 4.386 0.01 . 762 98 98 PRO HB2 H 2.242 0.01 . 763 98 98 PRO HB3 H 1.937 0.01 . 764 98 98 PRO C C 177.666 0.1 . 765 98 98 PRO CA C 63.605 0.1 . 766 98 98 PRO CB C 32.035 0.1 . 767 98 98 PRO CG C 27.203 0.1 . 768 98 98 PRO N N 135.705 0.1 . 769 99 99 GLY H H 8.420 0.01 . 770 99 99 GLY HA2 H 3.866 0.01 . 771 99 99 GLY HA3 H 3.866 0.01 . 772 99 99 GLY C C 173.521 0.1 . 773 99 99 GLY CA C 45.221 0.1 . 774 99 99 GLY N N 109.121 0.1 . 775 100 100 ALA H H 7.939 0.01 . 776 100 100 ALA HA H 4.262 0.01 . 777 100 100 ALA HB H 1.278 0.01 . 778 100 100 ALA C C 176.705 0.1 . 779 100 100 ALA CA C 52.305 0.1 . 780 100 100 ALA CB C 19.595 0.1 . 781 100 100 ALA N N 122.846 0.1 . 782 101 101 TYR H H 7.923 0.01 . 783 101 101 TYR HA H 4.755 0.01 . 784 101 101 TYR HB2 H 2.982 0.01 . 785 101 101 TYR HB3 H 2.846 0.01 . 786 101 101 TYR C C 174.044 0.1 . 787 101 101 TYR CA C 55.508 0.1 . 788 101 101 TYR CB C 38.410 0.1 . 789 101 101 TYR N N 119.725 0.1 . 790 102 102 PRO HA H 4.413 0.01 . 791 102 102 PRO HB2 H 2.240 0.01 . 792 102 102 PRO HB3 H 1.925 0.01 . 793 102 102 PRO C C 176.458 0.1 . 794 102 102 PRO CA C 63.164 0.1 . 795 102 102 PRO CB C 32.078 0.1 . 796 102 102 PRO CG C 27.374 0.1 . 797 102 102 PRO CD C 50.604 0.1 . 798 102 102 PRO N N 137.857 0.1 . 799 103 103 ALA H H 8.358 0.01 . 800 103 103 ALA HA H 4.387 0.01 . 801 103 103 ALA HB H 1.428 0.01 . 802 103 103 ALA C C 177.893 0.1 . 803 103 103 ALA CA C 52.757 0.1 . 804 103 103 ALA CB C 19.355 0.1 . 805 103 103 ALA N N 124.259 0.1 . 806 104 104 THR H H 7.974 0.01 . 807 104 104 THR HA H 4.408 0.01 . 808 104 104 THR HB H 4.268 0.01 . 809 104 104 THR HG2 H 1.209 0.01 . 810 104 104 THR C C 174.771 0.1 . 811 104 104 THR CA C 61.453 0.1 . 812 104 104 THR CB C 70.049 0.1 . 813 104 104 THR CG2 C 21.612 0.1 . 814 104 104 THR N N 111.311 0.1 . 815 105 105 GLY H H 8.150 0.01 . 816 105 105 GLY HA2 H 4.083 0.01 . 817 105 105 GLY HA3 H 4.083 0.01 . 818 105 105 GLY C C 172.106 0.1 . 819 105 105 GLY CA C 44.759 0.1 . 820 105 105 GLY N N 110.556 0.1 . 821 106 106 PRO HA H 4.317 0.01 . 822 106 106 PRO HB2 H 2.069 0.01 . 823 106 106 PRO HB3 H 1.666 0.01 . 824 106 106 PRO C C 176.852 0.1 . 825 106 106 PRO CA C 63.450 0.1 . 826 106 106 PRO CB C 31.822 0.1 . 827 106 106 PRO CG C 27.062 0.1 . 828 106 106 PRO CD C 49.712 0.1 . 829 106 106 PRO N N 133.785 0.1 . 830 107 107 TYR H H 8.167 0.01 . 831 107 107 TYR HA H 4.553 0.01 . 832 107 107 TYR HB2 H 3.094 0.01 . 833 107 107 TYR HB3 H 2.900 0.01 . 834 107 107 TYR C C 176.254 0.1 . 835 107 107 TYR CA C 57.739 0.1 . 836 107 107 TYR CB C 38.430 0.1 . 837 107 107 TYR N N 119.430 0.1 . 838 108 108 GLY H H 8.027 0.01 . 839 108 108 GLY HA2 H 3.846 0.01 . 840 108 108 GLY HA3 H 3.846 0.01 . 841 108 108 GLY C C 173.113 0.1 . 842 108 108 GLY CA C 45.119 0.1 . 843 108 108 GLY N N 109.924 0.1 . 844 109 109 ALA H H 7.963 0.01 . 845 109 109 ALA HA H 4.594 0.01 . 846 109 109 ALA HB H 1.348 0.01 . 847 109 109 ALA C C 175.408 0.1 . 848 109 109 ALA CA C 50.476 0.1 . 849 109 109 ALA CB C 18.510 0.1 . 850 109 109 ALA N N 124.546 0.1 . 851 110 110 PRO HA H 4.416 0.01 . 852 110 110 PRO HB2 H 2.299 0.01 . 853 110 110 PRO HB3 H 1.950 0.01 . 854 110 110 PRO C C 176.660 0.1 . 855 110 110 PRO CA C 63.157 0.1 . 856 110 110 PRO CB C 32.097 0.1 . 857 110 110 PRO CG C 27.470 0.1 . 858 110 110 PRO CD C 50.495 0.1 . 859 110 110 PRO N N 135.611 0.1 . 860 111 111 ALA H H 8.395 0.01 . 861 111 111 ALA HA H 4.387 0.01 . 862 111 111 ALA HB H 1.421 0.01 . 863 111 111 ALA C C 177.722 0.1 . 864 111 111 ALA CA C 52.356 0.1 . 865 111 111 ALA CB C 19.636 0.1 . 866 111 111 ALA N N 124.399 0.1 . 867 112 112 GLY H H 8.079 0.01 . 868 112 112 GLY HA2 H 4.083 0.01 . 869 112 112 GLY HA3 H 4.083 0.01 . 870 112 112 GLY C C 171.356 0.1 . 871 112 112 GLY CA C 44.498 0.1 . 872 112 112 GLY N N 108.160 0.1 . 873 113 113 PRO HA H 4.426 0.01 . 874 113 113 PRO HB2 H 2.268 0.01 . 875 113 113 PRO HB3 H 1.934 0.01 . 876 113 113 PRO HD2 H 3.640 0.01 . 877 113 113 PRO HD3 H 3.640 0.01 . 878 113 113 PRO C C 176.798 0.1 . 879 113 113 PRO CA C 63.131 0.1 . 880 113 113 PRO CB C 32.384 0.1 . 881 113 113 PRO CG C 27.475 0.1 . 882 113 113 PRO CD C 50.708 0.1 . 883 113 113 PRO N N 133.586 0.1 . 884 114 114 LEU H H 8.307 0.01 . 885 114 114 LEU HA H 4.438 0.01 . 886 114 114 LEU HB2 H 1.391 0.01 . 887 114 114 LEU HB3 H 1.037 0.01 . 888 114 114 LEU HG H 1.485 0.01 . 889 114 114 LEU HD1 H 0.433 0.01 . 890 114 114 LEU HD2 H 0.608 0.01 . 891 114 114 LEU C C 176.041 0.1 . 892 114 114 LEU CA C 54.390 0.1 . 893 114 114 LEU CB C 41.607 0.1 . 894 114 114 LEU CG C 27.265 0.1 . 895 114 114 LEU CD1 C 24.722 0.1 . 896 114 114 LEU CD2 C 23.087 0.1 . 897 114 114 LEU N N 122.498 0.1 . 898 115 115 ILE H H 8.092 0.01 . 899 115 115 ILE HA H 4.199 0.01 . 900 115 115 ILE HB H 1.890 0.01 . 901 115 115 ILE HG12 H 1.581 0.01 . 902 115 115 ILE HG13 H 1.295 0.01 . 903 115 115 ILE HG2 H 0.966 0.01 . 904 115 115 ILE HD1 H 0.915 0.01 . 905 115 115 ILE C C 174.569 0.1 . 906 115 115 ILE CA C 60.754 0.1 . 907 115 115 ILE CB C 39.022 0.1 . 908 115 115 ILE CG1 C 27.825 0.1 . 909 115 115 ILE CG2 C 17.733 0.1 . 910 115 115 ILE CD1 C 12.615 0.1 . 911 115 115 ILE N N 123.256 0.1 . 912 116 116 VAL H H 7.926 0.01 . 913 116 116 VAL HA H 4.519 0.01 . 914 116 116 VAL HB H 2.240 0.01 . 915 116 116 VAL HG1 H 1.150 0.01 . 916 116 116 VAL HG2 H 1.131 0.01 . 917 116 116 VAL CA C 59.062 0.1 . 918 116 116 VAL CB C 34.158 0.1 . 919 116 116 VAL CG1 C 22.006 0.1 . 920 116 116 VAL CG2 C 21.676 0.1 . 921 116 116 VAL N N 121.529 0.1 . 922 117 117 PRO HA H 4.980 0.01 . 923 117 117 PRO HB2 H 2.370 0.01 . 924 117 117 PRO HB3 H 2.083 0.01 . 925 117 117 PRO HG2 H 2.062 0.01 . 926 117 117 PRO HG3 H 1.948 0.01 . 927 117 117 PRO HD2 H 3.726 0.01 . 928 117 117 PRO HD3 H 3.627 0.01 . 929 117 117 PRO C C 174.515 0.1 . 930 117 117 PRO CA C 63.157 0.1 . 931 117 117 PRO CB C 34.735 0.1 . 932 117 117 PRO CG C 25.660 0.1 . 933 117 117 PRO CD C 50.986 0.1 . 934 118 118 TYR H H 9.201 0.01 . 935 118 118 TYR HA H 4.833 0.01 . 936 118 118 TYR HB2 H 3.460 0.01 . 937 118 118 TYR HB3 H 2.572 0.01 . 938 118 118 TYR C C 173.858 0.1 . 939 118 118 TYR CA C 57.371 0.1 . 940 118 118 TYR CB C 42.987 0.1 . 941 118 118 TYR N N 126.260 0.1 . 942 119 119 ASN H H 7.871 0.01 . 943 119 119 ASN HA H 5.287 0.01 . 944 119 119 ASN HB2 H 2.408 0.01 . 945 119 119 ASN HB3 H 2.203 0.01 . 946 119 119 ASN HD21 H 7.353 0.01 . 947 119 119 ASN HD22 H 6.555 0.01 . 948 119 119 ASN C C 171.882 0.1 . 949 119 119 ASN CA C 51.906 0.1 . 950 119 119 ASN CB C 41.255 0.1 . 951 119 119 ASN CG C 177.012 0.1 . 952 119 119 ASN N N 126.290 0.1 . 953 119 119 ASN ND2 N 111.980 0.1 . 954 120 120 LEU H H 9.347 0.01 . 955 120 120 LEU HA H 4.923 0.01 . 956 120 120 LEU HB2 H 2.294 0.01 . 957 120 120 LEU HB3 H 1.250 0.01 . 958 120 120 LEU HG H 1.759 0.01 . 959 120 120 LEU HD1 H 1.215 0.01 . 960 120 120 LEU HD2 H 0.891 0.01 . 961 120 120 LEU CA C 51.020 0.1 . 962 120 120 LEU CB C 44.734 0.1 . 963 120 120 LEU CG C 26.780 0.1 . 964 120 120 LEU CD1 C 24.617 0.1 . 965 120 120 LEU CD2 C 26.734 0.1 . 966 120 120 LEU N N 128.124 0.1 . 967 121 121 PRO HA H 4.406 0.01 . 968 121 121 PRO HB2 H 2.422 0.01 . 969 121 121 PRO HB3 H 1.944 0.01 . 970 121 121 PRO HG2 H 2.205 0.01 . 971 121 121 PRO HG3 H 1.954 0.01 . 972 121 121 PRO HD2 H 4.251 0.01 . 973 121 121 PRO HD3 H 3.864 0.01 . 974 121 121 PRO C C 175.835 0.1 . 975 121 121 PRO CA C 63.169 0.1 . 976 121 121 PRO CB C 32.838 0.1 . 977 121 121 PRO CG C 27.717 0.1 . 978 121 121 PRO CD C 51.605 0.1 . 979 122 122 LEU H H 7.815 0.01 . 980 122 122 LEU HA H 4.801 0.01 . 981 122 122 LEU HB2 H 1.625 0.01 . 982 122 122 LEU HB3 H 0.891 0.01 . 983 122 122 LEU HG H 1.514 0.01 . 984 122 122 LEU HD1 H 0.549 0.01 . 985 122 122 LEU HD2 H 0.747 0.01 . 986 122 122 LEU CA C 51.068 0.1 . 987 122 122 LEU CB C 41.219 0.1 . 988 122 122 LEU CG C 25.897 0.1 . 989 122 122 LEU CD1 C 23.685 0.1 . 990 122 122 LEU CD2 C 26.593 0.1 . 991 122 122 LEU N N 122.285 0.1 . 992 123 123 PRO HA H 4.302 0.01 . 993 123 123 PRO HB2 H 2.309 0.01 . 994 123 123 PRO HB3 H 1.999 0.01 . 995 123 123 PRO HG2 H 2.172 0.01 . 996 123 123 PRO HG3 H 2.013 0.01 . 997 123 123 PRO HD2 H 3.543 0.01 . 998 123 123 PRO C C 178.538 0.1 . 999 123 123 PRO CA C 64.641 0.1 . 1000 123 123 PRO CB C 31.509 0.1 . 1001 123 123 PRO CG C 27.763 0.1 . 1002 123 123 PRO CD C 50.669 0.1 . 1003 124 124 GLY H H 8.748 0.01 . 1004 124 124 GLY C C 174.366 0.1 . 1005 124 124 GLY CA C 45.087 0.1 . 1006 124 124 GLY N N 111.980 0.1 . 1007 125 125 GLY H H 8.223 0.01 . 1008 125 125 GLY HA2 H 4.132 0.01 . 1009 125 125 GLY HA3 H 4.132 0.01 . 1010 125 125 GLY C C 173.546 0.1 . 1011 125 125 GLY CA C 44.099 0.1 . 1012 125 125 GLY N N 108.808 0.1 . 1013 126 126 VAL H H 7.183 0.01 . 1014 126 126 VAL HA H 4.393 0.01 . 1015 126 126 VAL HB H 2.263 0.01 . 1016 126 126 VAL HG1 H 1.012 0.01 . 1017 126 126 VAL HG2 H 1.044 0.01 . 1018 126 126 VAL C C 174.186 0.1 . 1019 126 126 VAL CA C 61.053 0.1 . 1020 126 126 VAL CB C 32.641 0.1 . 1021 126 126 VAL CG1 C 22.447 0.1 . 1022 126 126 VAL CG2 C 23.868 0.1 . 1023 126 126 VAL N N 113.350 0.1 . 1024 127 127 VAL H H 6.521 0.01 . 1025 127 127 VAL HA H 4.629 0.01 . 1026 127 127 VAL HB H 1.958 0.01 . 1027 127 127 VAL HG1 H 0.915 0.01 . 1028 127 127 VAL HG2 H 0.822 0.01 . 1029 127 127 VAL CA C 57.064 0.1 . 1030 127 127 VAL CB C 35.451 0.1 . 1031 127 127 VAL CG1 C 21.534 0.1 . 1032 127 127 VAL CG2 C 20.040 0.1 . 1033 127 127 VAL N N 116.723 0.1 . 1034 128 128 PRO HA H 3.928 0.01 . 1035 128 128 PRO HB2 H 1.846 0.01 . 1036 128 128 PRO HB3 H 1.846 0.01 . 1037 128 128 PRO HG2 H 2.174 0.01 . 1038 128 128 PRO HG3 H 1.345 0.01 . 1039 128 128 PRO C C 175.800 0.1 . 1040 128 128 PRO CA C 63.419 0.1 . 1041 128 128 PRO CB C 31.693 0.1 . 1042 128 128 PRO CG C 28.627 0.1 . 1043 128 128 PRO CD C 50.903 0.1 . 1044 129 129 ARG H H 8.764 0.01 . 1045 129 129 ARG HA H 3.582 0.01 . 1046 129 129 ARG HB2 H 2.539 0.01 . 1047 129 129 ARG HB3 H 2.452 0.01 . 1048 129 129 ARG HG2 H 1.590 0.01 . 1049 129 129 ARG HG3 H 1.502 0.01 . 1050 129 129 ARG HD2 H 3.327 0.01 . 1051 129 129 ARG HD3 H 3.082 0.01 . 1052 129 129 ARG HE H 7.897 0.01 . 1053 129 129 ARG C C 174.093 0.1 . 1054 129 129 ARG CA C 59.620 0.1 . 1055 129 129 ARG CB C 27.046 0.1 . 1056 129 129 ARG CG C 28.057 0.1 . 1057 129 129 ARG CD C 43.011 0.1 . 1058 129 129 ARG N N 112.576 0.1 . 1059 129 129 ARG NE N 85.379 0.1 . 1060 130 130 MET H H 7.891 0.01 . 1061 130 130 MET HA H 4.960 0.01 . 1062 130 130 MET HB2 H 2.283 0.01 . 1063 130 130 MET HB3 H 2.191 0.01 . 1064 130 130 MET HG2 H 2.453 0.01 . 1065 130 130 MET HG3 H 2.453 0.01 . 1066 130 130 MET HE H 1.749 0.01 . 1067 130 130 MET C C 173.741 0.1 . 1068 130 130 MET CA C 56.962 0.1 . 1069 130 130 MET CB C 36.541 0.1 . 1070 130 130 MET CG C 33.100 0.1 . 1071 130 130 MET CE C 17.753 0.1 . 1072 130 130 MET N N 119.228 0.1 . 1073 131 131 LEU H H 9.184 0.01 . 1074 131 131 LEU HA H 5.541 0.01 . 1075 131 131 LEU HB2 H 1.947 0.01 . 1076 131 131 LEU HB3 H 1.263 0.01 . 1077 131 131 LEU HG H 1.336 0.01 . 1078 131 131 LEU HD1 H 0.955 0.01 . 1079 131 131 LEU HD2 H 0.835 0.01 . 1080 131 131 LEU C C 176.804 0.1 . 1081 131 131 LEU CA C 53.344 0.1 . 1082 131 131 LEU CB C 45.611 0.1 . 1083 131 131 LEU CG C 27.704 0.1 . 1084 131 131 LEU CD1 C 24.840 0.1 . 1085 131 131 LEU CD2 C 26.641 0.1 . 1086 131 131 LEU N N 128.432 0.1 . 1087 132 132 ILE H H 9.973 0.01 . 1088 132 132 ILE HA H 4.980 0.01 . 1089 132 132 ILE HB H 1.997 0.01 . 1090 132 132 ILE HG12 H 1.819 0.01 . 1091 132 132 ILE HG13 H 1.245 0.01 . 1092 132 132 ILE HG2 H 0.945 0.01 . 1093 132 132 ILE HD1 H 1.202 0.01 . 1094 132 132 ILE C C 175.374 0.1 . 1095 132 132 ILE CA C 60.939 0.1 . 1096 132 132 ILE CB C 41.210 0.1 . 1097 132 132 ILE CG1 C 29.857 0.1 . 1098 132 132 ILE CG2 C 17.811 0.1 . 1099 132 132 ILE CD1 C 15.459 0.1 . 1100 132 132 ILE N N 132.364 0.1 . 1101 133 133 THR H H 9.122 0.01 . 1102 133 133 THR HA H 5.255 0.01 . 1103 133 133 THR HB H 3.830 0.01 . 1104 133 133 THR HG2 H 1.090 0.01 . 1105 133 133 THR C C 174.069 0.1 . 1106 133 133 THR CA C 63.088 0.1 . 1107 133 133 THR CB C 70.204 0.1 . 1108 133 133 THR CG2 C 21.541 0.1 . 1109 133 133 THR N N 123.699 0.1 . 1110 134 134 ILE H H 9.690 0.01 . 1111 134 134 ILE HA H 4.903 0.01 . 1112 134 134 ILE HB H 1.984 0.01 . 1113 134 134 ILE HG12 H 1.516 0.01 . 1114 134 134 ILE HG13 H 1.192 0.01 . 1115 134 134 ILE HG2 H 1.030 0.01 . 1116 134 134 ILE HD1 H 0.844 0.01 . 1117 134 134 ILE C C 173.741 0.1 . 1118 134 134 ILE CA C 59.924 0.1 . 1119 134 134 ILE CB C 41.476 0.1 . 1120 134 134 ILE CG1 C 27.927 0.1 . 1121 134 134 ILE CG2 C 18.813 0.1 . 1122 134 134 ILE CD1 C 14.883 0.1 . 1123 134 134 ILE N N 130.080 0.1 . 1124 135 135 LEU H H 8.893 0.01 . 1125 135 135 LEU HA H 5.064 0.01 . 1126 135 135 LEU HB2 H 1.620 0.01 . 1127 135 135 LEU HB3 H 1.482 0.01 . 1128 135 135 LEU HG H 1.480 0.01 . 1129 135 135 LEU HD1 H 0.876 0.01 . 1130 135 135 LEU HD2 H 0.798 0.01 . 1131 135 135 LEU C C 176.092 0.1 . 1132 135 135 LEU CA C 53.308 0.1 . 1133 135 135 LEU CB C 44.756 0.1 . 1134 135 135 LEU CG C 27.591 0.1 . 1135 135 135 LEU CD1 C 24.375 0.1 . 1136 135 135 LEU CD2 C 25.292 0.1 . 1137 135 135 LEU N N 126.875 0.1 . 1138 136 136 GLY H H 6.977 0.01 . 1139 136 136 GLY HA2 H 4.198 0.01 . 1140 136 136 GLY HA3 H 4.003 0.01 . 1141 136 136 GLY C C 171.183 0.1 . 1142 136 136 GLY CA C 46.337 0.1 . 1143 136 136 GLY N N 108.314 0.1 . 1144 137 137 THR H H 8.925 0.01 . 1145 137 137 THR HA H 4.772 0.01 . 1146 137 137 THR HB H 3.823 0.01 . 1147 137 137 THR HG2 H 0.993 0.01 . 1148 137 137 THR C C 174.022 0.1 . 1149 137 137 THR CA C 61.754 0.1 . 1150 137 137 THR CB C 71.599 0.1 . 1151 137 137 THR CG2 C 21.821 0.1 . 1152 137 137 THR N N 115.753 0.1 . 1153 138 138 VAL H H 8.447 0.01 . 1154 138 138 VAL HA H 4.090 0.01 . 1155 138 138 VAL HB H 2.631 0.01 . 1156 138 138 VAL HG1 H 1.082 0.01 . 1157 138 138 VAL HG2 H 1.290 0.01 . 1158 138 138 VAL C C 176.655 0.1 . 1159 138 138 VAL CA C 63.894 0.1 . 1160 138 138 VAL CB C 31.938 0.1 . 1161 138 138 VAL CG1 C 24.243 0.1 . 1162 138 138 VAL CG2 C 24.755 0.1 . 1163 138 138 VAL N N 128.072 0.1 . 1164 139 139 LYS H H 8.311 0.01 . 1165 139 139 LYS HA H 4.342 0.01 . 1166 139 139 LYS HG2 H 1.295 0.01 . 1167 139 139 LYS HG3 H 1.134 0.01 . 1168 139 139 LYS HD2 H 1.618 0.01 . 1169 139 139 LYS HD3 H 1.456 0.01 . 1170 139 139 LYS HE2 H 2.939 0.01 . 1171 139 139 LYS HE3 H 2.849 0.01 . 1172 139 139 LYS CA C 56.365 0.1 . 1173 139 139 LYS CB C 31.926 0.1 . 1174 139 139 LYS CG C 26.344 0.1 . 1175 139 139 LYS CD C 29.451 0.1 . 1176 139 139 LYS CE C 41.848 0.1 . 1177 139 139 LYS N N 128.685 0.1 . 1178 140 140 PRO HA H 4.136 0.01 . 1179 140 140 PRO HB2 H 2.247 0.01 . 1180 140 140 PRO HB3 H 1.744 0.01 . 1181 140 140 PRO HG2 H 2.061 0.01 . 1182 140 140 PRO HG3 H 1.938 0.01 . 1183 140 140 PRO HD2 H 3.831 0.01 . 1184 140 140 PRO HD3 H 3.519 0.01 . 1185 140 140 PRO C C 176.733 0.1 . 1186 140 140 PRO CA C 63.655 0.1 . 1187 140 140 PRO CB C 31.790 0.1 . 1188 140 140 PRO CG C 28.010 0.1 . 1189 140 140 PRO CD C 50.731 0.1 . 1190 141 141 ASN H H 8.428 0.01 . 1191 141 141 ASN HA H 4.381 0.01 . 1192 141 141 ASN HB2 H 2.776 0.01 . 1193 141 141 ASN HB3 H 2.696 0.01 . 1194 141 141 ASN HD21 H 7.500 0.01 . 1195 141 141 ASN HD22 H 6.823 0.01 . 1196 141 141 ASN C C 174.241 0.1 . 1197 141 141 ASN CA C 53.041 0.1 . 1198 141 141 ASN CB C 37.309 0.1 . 1199 141 141 ASN CG C 178.538 0.1 . 1200 141 141 ASN N N 115.743 0.1 . 1201 141 141 ASN ND2 N 113.167 0.1 . 1202 142 142 ALA H H 6.899 0.01 . 1203 142 142 ALA HA H 3.577 0.01 . 1204 142 142 ALA HB H 0.560 0.01 . 1205 142 142 ALA C C 175.713 0.1 . 1206 142 142 ALA CA C 53.329 0.1 . 1207 142 142 ALA CB C 20.223 0.1 . 1208 142 142 ALA N N 119.472 0.1 . 1209 143 143 ASN H H 9.596 0.01 . 1210 143 143 ASN HA H 4.920 0.01 . 1211 143 143 ASN HB2 H 2.777 0.01 . 1212 143 143 ASN HB3 H 2.777 0.01 . 1213 143 143 ASN HD21 H 7.800 0.01 . 1214 143 143 ASN HD22 H 7.011 0.01 . 1215 143 143 ASN C C 176.690 0.1 . 1216 143 143 ASN CA C 55.173 0.1 . 1217 143 143 ASN CB C 42.109 0.1 . 1218 143 143 ASN CG C 176.484 0.1 . 1219 143 143 ASN N N 116.518 0.1 . 1220 143 143 ASN ND2 N 114.601 0.1 . 1221 144 144 ARG H H 8.570 0.01 . 1222 144 144 ARG HA H 5.503 0.01 . 1223 144 144 ARG HB2 H 1.972 0.01 . 1224 144 144 ARG HB3 H 1.565 0.01 . 1225 144 144 ARG HG2 H 1.552 0.01 . 1226 144 144 ARG HG3 H 1.303 0.01 . 1227 144 144 ARG HD2 H 3.277 0.01 . 1228 144 144 ARG HD3 H 3.072 0.01 . 1229 144 144 ARG C C 173.108 0.1 . 1230 144 144 ARG CA C 55.324 0.1 . 1231 144 144 ARG CB C 33.968 0.1 . 1232 144 144 ARG CG C 25.812 0.1 . 1233 144 144 ARG CD C 43.549 0.1 . 1234 144 144 ARG N N 117.767 0.1 . 1235 145 145 ILE H H 8.156 0.01 . 1236 145 145 ILE HA H 4.190 0.01 . 1237 145 145 ILE HB H 0.743 0.01 . 1238 145 145 ILE HG12 H 1.420 0.01 . 1239 145 145 ILE HG13 H 0.728 0.01 . 1240 145 145 ILE HG2 H 0.517 0.01 . 1241 145 145 ILE HD1 H -0.169 0.01 . 1242 145 145 ILE C C 173.046 0.1 . 1243 145 145 ILE CA C 60.901 0.1 . 1244 145 145 ILE CB C 42.813 0.1 . 1245 145 145 ILE CG1 C 27.785 0.1 . 1246 145 145 ILE CG2 C 15.459 0.1 . 1247 145 145 ILE CD1 C 13.554 0.1 . 1248 145 145 ILE N N 119.826 0.1 . 1249 146 146 ALA H H 8.700 0.01 . 1250 146 146 ALA HA H 5.191 0.01 . 1251 146 146 ALA HB H 1.138 0.01 . 1252 146 146 ALA C C 174.936 0.1 . 1253 146 146 ALA CA C 52.502 0.1 . 1254 146 146 ALA CB C 21.618 0.1 . 1255 146 146 ALA N N 127.138 0.1 . 1256 147 147 LEU H H 8.537 0.01 . 1257 147 147 LEU HA H 5.097 0.01 . 1258 147 147 LEU HB2 H 1.623 0.01 . 1259 147 147 LEU HB3 H 1.300 0.01 . 1260 147 147 LEU HG H 1.664 0.01 . 1261 147 147 LEU HD1 H 0.711 0.01 . 1262 147 147 LEU HD2 H 0.783 0.01 . 1263 147 147 LEU C C 174.687 0.1 . 1264 147 147 LEU CA C 53.689 0.1 . 1265 147 147 LEU CB C 44.123 0.1 . 1266 147 147 LEU CG C 28.830 0.1 . 1267 147 147 LEU CD1 C 24.244 0.1 . 1268 147 147 LEU CD2 C 25.447 0.1 . 1269 147 147 LEU N N 122.087 0.1 . 1270 148 148 ASP H H 9.082 0.01 . 1271 148 148 ASP HA H 5.500 0.01 . 1272 148 148 ASP HB2 H 2.490 0.01 . 1273 148 148 ASP HB3 H 2.338 0.01 . 1274 148 148 ASP C C 175.522 0.1 . 1275 148 148 ASP CA C 53.629 0.1 . 1276 148 148 ASP CB C 44.446 0.1 . 1277 148 148 ASP N N 121.025 0.1 . 1278 149 149 PHE H H 9.332 0.01 . 1279 149 149 PHE HA H 4.816 0.01 . 1280 149 149 PHE HB2 H 3.360 0.01 . 1281 149 149 PHE HB3 H 2.989 0.01 . 1282 149 149 PHE C C 175.671 0.1 . 1283 149 149 PHE CA C 58.645 0.1 . 1284 149 149 PHE CB C 38.542 0.1 . 1285 149 149 PHE N N 125.385 0.1 . 1286 150 150 GLN H H 9.148 0.01 . 1287 150 150 GLN HA H 4.720 0.01 . 1288 150 150 GLN HB2 H 2.018 0.01 . 1289 150 150 GLN HG2 H 2.281 0.01 . 1290 150 150 GLN HG3 H 2.281 0.01 . 1291 150 150 GLN HE21 H 6.900 0.01 . 1292 150 150 GLN HE22 H 6.859 0.01 . 1293 150 150 GLN C C 173.460 0.1 . 1294 150 150 GLN CA C 57.044 0.1 . 1295 150 150 GLN CB C 31.669 0.1 . 1296 150 150 GLN CG C 34.421 0.1 . 1297 150 150 GLN CD C 179.060 0.1 . 1298 150 150 GLN N N 127.233 0.1 . 1299 150 150 GLN NE2 N 108.745 0.1 . 1300 151 151 ARG H H 8.167 0.01 . 1301 151 151 ARG HA H 4.979 0.01 . 1302 151 151 ARG HB2 H 1.820 0.01 . 1303 151 151 ARG HB3 H 1.412 0.01 . 1304 151 151 ARG HG2 H 1.636 0.01 . 1305 151 151 ARG HG3 H 1.535 0.01 . 1306 151 151 ARG HD2 H 3.498 0.01 . 1307 151 151 ARG HD3 H 2.940 0.01 . 1308 151 151 ARG HE H 7.292 0.01 . 1309 151 151 ARG CA C 54.230 0.1 . 1310 151 151 ARG CB C 31.610 0.1 . 1311 151 151 ARG CG C 27.430 0.1 . 1312 151 151 ARG CD C 42.776 0.1 . 1313 151 151 ARG N N 125.570 0.1 . 1314 151 151 ARG NE N 82.629 0.1 . 1315 152 152 GLY HA2 H 4.029 0.01 . 1316 152 152 GLY HA3 H 3.659 0.01 . 1317 152 152 GLY CA C 47.259 0.1 . 1318 153 153 ASN HA H 4.692 0.01 . 1319 153 153 ASN HB2 H 2.893 0.01 . 1320 153 153 ASN HB3 H 2.620 0.01 . 1321 153 153 ASN HD21 H 7.647 0.01 . 1322 153 153 ASN HD22 H 6.936 0.01 . 1323 153 153 ASN C C 175.561 0.1 . 1324 153 153 ASN CA C 53.841 0.1 . 1325 153 153 ASN CB C 39.165 0.1 . 1326 153 153 ASN CG C 177.383 0.1 . 1327 153 153 ASN ND2 N 113.856 0.1 . 1328 154 154 ASP H H 8.475 0.01 . 1329 154 154 ASP HA H 4.682 0.01 . 1330 154 154 ASP HB2 H 3.113 0.01 . 1331 154 154 ASP HB3 H 3.113 0.01 . 1332 154 154 ASP C C 176.495 0.1 . 1333 154 154 ASP CA C 53.984 0.1 . 1334 154 154 ASP CB C 42.385 0.1 . 1335 154 154 ASP N N 119.954 0.1 . 1336 155 155 VAL H H 9.213 0.01 . 1337 155 155 VAL HA H 4.428 0.01 . 1338 155 155 VAL HB H 1.804 0.01 . 1339 155 155 VAL HG1 H 0.817 0.01 . 1340 155 155 VAL HG2 H 1.197 0.01 . 1341 155 155 VAL C C 176.132 0.1 . 1342 155 155 VAL CA C 61.860 0.1 . 1343 155 155 VAL CB C 32.654 0.1 . 1344 155 155 VAL CG1 C 20.264 0.1 . 1345 155 155 VAL CG2 C 22.867 0.1 . 1346 155 155 VAL N N 121.297 0.1 . 1347 156 156 ALA H H 8.876 0.01 . 1348 156 156 ALA HA H 4.187 0.01 . 1349 156 156 ALA HB H 1.548 0.01 . 1350 156 156 ALA C C 179.147 0.1 . 1351 156 156 ALA CA C 55.353 0.1 . 1352 156 156 ALA CB C 19.494 0.1 . 1353 156 156 ALA N N 127.830 0.1 . 1354 157 157 PHE H H 7.658 0.01 . 1355 157 157 PHE HA H 5.133 0.01 . 1356 157 157 PHE HB2 H 3.188 0.01 . 1357 157 157 PHE HB3 H 2.279 0.01 . 1358 157 157 PHE C C 170.186 0.1 . 1359 157 157 PHE CA C 56.126 0.1 . 1360 157 157 PHE CB C 40.447 0.1 . 1361 157 157 PHE N N 118.506 0.1 . 1362 158 158 HIS H H 9.429 0.01 . 1363 158 158 HIS HA H 5.475 0.01 . 1364 158 158 HIS HB2 H 3.274 0.01 . 1365 158 158 HIS HB3 H 3.042 0.01 . 1366 158 158 HIS C C 171.401 0.1 . 1367 158 158 HIS CA C 54.143 0.1 . 1368 158 158 HIS CB C 31.706 0.1 . 1369 158 158 HIS N N 133.456 0.1 . 1370 159 159 PHE H H 8.470 0.01 . 1371 159 159 PHE HA H 4.651 0.01 . 1372 159 159 PHE HB2 H 2.532 0.01 . 1373 159 159 PHE HB3 H 2.104 0.01 . 1374 159 159 PHE C C 173.765 0.1 . 1375 159 159 PHE CA C 55.932 0.1 . 1376 159 159 PHE CB C 40.583 0.1 . 1377 159 159 PHE N N 126.889 0.1 . 1378 160 160 ASN H H 8.412 0.01 . 1379 160 160 ASN HA H 5.267 0.01 . 1380 160 160 ASN HB2 H 2.676 0.01 . 1381 160 160 ASN HB3 H 1.681 0.01 . 1382 160 160 ASN HD21 H 7.444 0.01 . 1383 160 160 ASN HD22 H 6.091 0.01 . 1384 160 160 ASN CA C 50.214 0.1 . 1385 160 160 ASN CB C 41.574 0.1 . 1386 160 160 ASN N N 123.342 0.1 . 1387 160 160 ASN ND2 N 106.406 0.1 . 1388 161 161 PRO HA H 4.262 0.01 . 1389 161 161 PRO HG2 H 0.743 0.01 . 1390 161 161 PRO HG3 H 0.743 0.01 . 1391 161 161 PRO HD2 H 3.251 0.01 . 1392 161 161 PRO HD3 H 2.260 0.01 . 1393 161 161 PRO C C 173.632 0.1 . 1394 161 161 PRO CA C 63.940 0.1 . 1395 161 161 PRO CB C 31.421 0.1 . 1396 161 161 PRO CG C 29.332 0.1 . 1397 161 161 PRO CD C 48.337 0.1 . 1398 162 162 ARG H H 9.301 0.01 . 1399 162 162 ARG HA H 4.762 0.01 . 1400 162 162 ARG HB2 H 1.880 0.01 . 1401 162 162 ARG HB3 H 1.880 0.01 . 1402 162 162 ARG HD2 H 3.108 0.01 . 1403 162 162 ARG HD3 H 2.606 0.01 . 1404 162 162 ARG HE H 7.132 0.01 . 1405 162 162 ARG C C 174.332 0.1 . 1406 162 162 ARG CA C 55.903 0.1 . 1407 162 162 ARG CB C 31.643 0.1 . 1408 162 162 ARG CG C 26.809 0.1 . 1409 162 162 ARG CD C 44.075 0.1 . 1410 162 162 ARG N N 126.311 0.1 . 1411 162 162 ARG NE N 85.157 0.1 . 1412 163 163 PHE H H 8.129 0.01 . 1413 163 163 PHE HA H 3.692 0.01 . 1414 163 163 PHE HB2 H 2.965 0.01 . 1415 163 163 PHE HB3 H 2.965 0.01 . 1416 163 163 PHE C C 175.319 0.1 . 1417 163 163 PHE CA C 59.653 0.1 . 1418 163 163 PHE CB C 39.739 0.1 . 1419 163 163 PHE N N 118.770 0.1 . 1420 164 164 ASN H H 8.695 0.01 . 1421 164 164 ASN HA H 4.493 0.01 . 1422 164 164 ASN HB2 H 2.878 0.01 . 1423 164 164 ASN HB3 H 2.647 0.01 . 1424 164 164 ASN HD21 H 7.450 0.01 . 1425 164 164 ASN HD22 H 6.702 0.01 . 1426 164 164 ASN C C 173.655 0.1 . 1427 164 164 ASN CA C 52.898 0.1 . 1428 164 164 ASN CB C 38.401 0.1 . 1429 164 164 ASN CG C 177.884 0.1 . 1430 164 164 ASN N N 117.497 0.1 . 1431 164 164 ASN ND2 N 110.409 0.1 . 1432 165 165 GLU H H 8.931 0.01 . 1433 165 165 GLU HA H 4.526 0.01 . 1434 165 165 GLU HB2 H 1.941 0.01 . 1435 165 165 GLU HB3 H 1.598 0.01 . 1436 165 165 GLU HG2 H 2.059 0.01 . 1437 165 165 GLU HG3 H 1.884 0.01 . 1438 165 165 GLU CA C 55.147 0.1 . 1439 165 165 GLU CB C 30.385 0.1 . 1440 165 165 GLU CG C 36.870 0.1 . 1441 165 165 GLU N N 125.571 0.1 . 1442 166 166 ASN HA H 4.266 0.01 . 1443 166 166 ASN HB2 H 2.987 0.01 . 1444 166 166 ASN HB3 H 2.677 0.01 . 1445 166 166 ASN HD21 H 7.510 0.01 . 1446 166 166 ASN HD22 H 6.868 0.01 . 1447 166 166 ASN C C 174.484 0.1 . 1448 166 166 ASN CA C 54.732 0.1 . 1449 166 166 ASN CB C 37.473 0.1 . 1450 166 166 ASN CG C 178.211 0.1 . 1451 166 166 ASN ND2 N 112.670 0.1 . 1452 167 167 ASN H H 8.076 0.01 . 1453 167 167 ASN HA H 4.323 0.01 . 1454 167 167 ASN HB2 H 3.049 0.01 . 1455 167 167 ASN HB3 H 2.967 0.01 . 1456 167 167 ASN HD21 H 7.452 0.01 . 1457 167 167 ASN HD22 H 6.851 0.01 . 1458 167 167 ASN C C 174.000 0.1 . 1459 167 167 ASN CA C 55.046 0.1 . 1460 167 167 ASN CB C 37.581 0.1 . 1461 167 167 ASN CG C 178.775 0.1 . 1462 167 167 ASN N N 108.167 0.1 . 1463 167 167 ASN ND2 N 112.941 0.1 . 1464 168 168 ARG H H 7.412 0.01 . 1465 168 168 ARG HA H 4.542 0.01 . 1466 168 168 ARG HB2 H 1.736 0.01 . 1467 168 168 ARG HB3 H 1.680 0.01 . 1468 168 168 ARG HG2 H 1.595 0.01 . 1469 168 168 ARG HG3 H 1.595 0.01 . 1470 168 168 ARG HD2 H 3.169 0.01 . 1471 168 168 ARG HD3 H 3.169 0.01 . 1472 168 168 ARG C C 173.942 0.1 . 1473 168 168 ARG CA C 54.410 0.1 . 1474 168 168 ARG CB C 33.175 0.1 . 1475 168 168 ARG CG C 27.083 0.1 . 1476 168 168 ARG CD C 43.384 0.1 . 1477 168 168 ARG N N 117.371 0.1 . 1478 169 169 ARG H H 7.880 0.01 . 1479 169 169 ARG HA H 4.469 0.01 . 1480 169 169 ARG HB2 H 0.879 0.01 . 1481 169 169 ARG HB3 H -0.513 0.01 . 1482 169 169 ARG HG2 H 1.276 0.01 . 1483 169 169 ARG HG3 H 1.191 0.01 . 1484 169 169 ARG HD2 H 2.891 0.01 . 1485 169 169 ARG HD3 H 2.731 0.01 . 1486 169 169 ARG C C 176.030 0.1 . 1487 169 169 ARG CA C 54.383 0.1 . 1488 169 169 ARG CB C 28.610 0.1 . 1489 169 169 ARG CG C 26.553 0.1 . 1490 169 169 ARG CD C 44.082 0.1 . 1491 169 169 ARG N N 119.067 0.1 . 1492 170 170 VAL H H 8.576 0.01 . 1493 170 170 VAL HA H 4.612 0.01 . 1494 170 170 VAL HB H 1.945 0.01 . 1495 170 170 VAL HG1 H 0.737 0.01 . 1496 170 170 VAL HG2 H 0.862 0.01 . 1497 170 170 VAL C C 172.030 0.1 . 1498 170 170 VAL CA C 60.416 0.1 . 1499 170 170 VAL CB C 35.847 0.1 . 1500 170 170 VAL CG1 C 19.453 0.1 . 1501 170 170 VAL CG2 C 21.143 0.1 . 1502 170 170 VAL N N 121.577 0.1 . 1503 171 171 ILE H H 8.745 0.01 . 1504 171 171 ILE HA H 4.227 0.01 . 1505 171 171 ILE HB H 1.816 0.01 . 1506 171 171 ILE HG12 H 1.807 0.01 . 1507 171 171 ILE HG13 H 0.673 0.01 . 1508 171 171 ILE HG2 H 0.165 0.01 . 1509 171 171 ILE HD1 H 0.824 0.01 . 1510 171 171 ILE C C 174.335 0.1 . 1511 171 171 ILE CA C 60.622 0.1 . 1512 171 171 ILE CB C 38.970 0.1 . 1513 171 171 ILE CG1 C 28.386 0.1 . 1514 171 171 ILE CG2 C 17.863 0.1 . 1515 171 171 ILE CD1 C 15.108 0.1 . 1516 171 171 ILE N N 124.678 0.1 . 1517 172 172 VAL H H 7.359 0.01 . 1518 172 172 VAL HA H 4.357 0.01 . 1519 172 172 VAL HB H 1.919 0.01 . 1520 172 172 VAL HG1 H 0.821 0.01 . 1521 172 172 VAL HG2 H 0.736 0.01 . 1522 172 172 VAL C C 174.569 0.1 . 1523 172 172 VAL CA C 62.069 0.1 . 1524 172 172 VAL CB C 34.020 0.1 . 1525 172 172 VAL CG1 C 21.877 0.1 . 1526 172 172 VAL CG2 C 21.603 0.1 . 1527 172 172 VAL N N 128.147 0.1 . 1528 173 173 CYS H H 8.791 0.01 . 1529 173 173 CYS HA H 6.070 0.01 . 1530 173 173 CYS HB2 H 3.224 0.01 . 1531 173 173 CYS HB3 H 3.016 0.01 . 1532 173 173 CYS C C 174.218 0.1 . 1533 173 173 CYS CA C 55.737 0.1 . 1534 173 173 CYS CB C 32.411 0.1 . 1535 173 173 CYS N N 123.600 0.1 . 1536 174 174 ASN H H 8.992 0.01 . 1537 174 174 ASN HA H 5.567 0.01 . 1538 174 174 ASN HB2 H 3.018 0.01 . 1539 174 174 ASN HB3 H 2.906 0.01 . 1540 174 174 ASN C C 173.940 0.1 . 1541 174 174 ASN CA C 52.413 0.1 . 1542 174 174 ASN CB C 42.679 0.1 . 1543 174 174 ASN N N 119.559 0.1 . 1544 175 175 THR H H 10.055 0.01 . 1545 175 175 THR HA H 4.762 0.01 . 1546 175 175 THR HB H 4.208 0.01 . 1547 175 175 THR HG2 H 1.472 0.01 . 1548 175 175 THR C C 171.608 0.1 . 1549 175 175 THR CA C 62.448 0.1 . 1550 175 175 THR CB C 75.515 0.1 . 1551 175 175 THR CG2 C 21.648 0.1 . 1552 175 175 THR N N 118.317 0.1 . 1553 176 176 LYS H H 9.057 0.01 . 1554 176 176 LYS HA H 4.307 0.01 . 1555 176 176 LYS HG2 H 0.484 0.01 . 1556 176 176 LYS HG3 H -0.426 0.01 . 1557 176 176 LYS HD2 H 0.837 0.01 . 1558 176 176 LYS HD3 H 0.837 0.01 . 1559 176 176 LYS HE2 H 2.315 0.01 . 1560 176 176 LYS HE3 H 2.315 0.01 . 1561 176 176 LYS C C 173.835 0.1 . 1562 176 176 LYS CA C 54.551 0.1 . 1563 176 176 LYS CB C 33.480 0.1 . 1564 176 176 LYS CG C 24.234 0.1 . 1565 176 176 LYS CD C 29.010 0.1 . 1566 176 176 LYS CE C 41.453 0.1 . 1567 176 176 LYS N N 130.427 0.1 . 1568 177 177 LEU H H 7.946 0.01 . 1569 177 177 LEU HA H 4.624 0.01 . 1570 177 177 LEU HB2 H 1.524 0.01 . 1571 177 177 LEU HB3 H 1.372 0.01 . 1572 177 177 LEU HG H 1.428 0.01 . 1573 177 177 LEU HD1 H 0.743 0.01 . 1574 177 177 LEU HD2 H 0.826 0.01 . 1575 177 177 LEU C C 177.132 0.1 . 1576 177 177 LEU CA C 52.934 0.1 . 1577 177 177 LEU CB C 44.765 0.1 . 1578 177 177 LEU CG C 26.435 0.1 . 1579 177 177 LEU CD1 C 23.638 0.1 . 1580 177 177 LEU CD2 C 25.062 0.1 . 1581 177 177 LEU N N 126.369 0.1 . 1582 178 178 ASP H H 9.040 0.01 . 1583 178 178 ASP HA H 4.177 0.01 . 1584 178 178 ASP HB2 H 2.822 0.01 . 1585 178 178 ASP HB3 H 2.538 0.01 . 1586 178 178 ASP C C 175.202 0.1 . 1587 178 178 ASP CA C 55.635 0.1 . 1588 178 178 ASP CB C 39.336 0.1 . 1589 178 178 ASP N N 126.154 0.1 . 1590 179 179 ASN H H 9.157 0.01 . 1591 179 179 ASN HA H 3.807 0.01 . 1592 179 179 ASN HB2 H 3.006 0.01 . 1593 179 179 ASN HB3 H 2.872 0.01 . 1594 179 179 ASN HD21 H 7.495 0.01 . 1595 179 179 ASN HD22 H 6.845 0.01 . 1596 179 179 ASN C C 173.687 0.1 . 1597 179 179 ASN CA C 54.695 0.1 . 1598 179 179 ASN CB C 38.518 0.1 . 1599 179 179 ASN CG C 178.585 0.1 . 1600 179 179 ASN N N 108.613 0.1 . 1601 179 179 ASN ND2 N 113.436 0.1 . 1602 180 180 ASN H H 7.798 0.01 . 1603 180 180 ASN HA H 5.055 0.01 . 1604 180 180 ASN HB2 H 2.716 0.01 . 1605 180 180 ASN HB3 H 2.657 0.01 . 1606 180 180 ASN HD21 H 7.441 0.01 . 1607 180 180 ASN HD22 H 6.892 0.01 . 1608 180 180 ASN C C 174.702 0.1 . 1609 180 180 ASN CA C 52.241 0.1 . 1610 180 180 ASN CB C 41.469 0.1 . 1611 180 180 ASN CG C 176.654 0.1 . 1612 180 180 ASN N N 117.756 0.1 . 1613 180 180 ASN ND2 N 114.557 0.1 . 1614 181 181 TRP H H 8.958 0.01 . 1615 181 181 TRP HA H 4.865 0.01 . 1616 181 181 TRP HB2 H 3.365 0.01 . 1617 181 181 TRP HB3 H 3.118 0.01 . 1618 181 181 TRP HD1 H 7.347 0.01 . 1619 181 181 TRP HE1 H 10.162 0.01 . 1620 181 181 TRP C C 177.476 0.1 . 1621 181 181 TRP CA C 57.800 0.1 . 1622 181 181 TRP CB C 30.422 0.1 . 1623 181 181 TRP N N 126.857 0.1 . 1624 181 181 TRP NE1 N 129.148 0.1 . 1625 182 182 GLY H H 8.250 0.01 . 1626 182 182 GLY HA2 H 4.582 0.01 . 1627 182 182 GLY HA3 H 3.907 0.01 . 1628 182 182 GLY C C 174.327 0.1 . 1629 182 182 GLY CA C 44.612 0.1 . 1630 182 182 GLY N N 110.388 0.1 . 1631 183 183 ARG H H 8.647 0.01 . 1632 183 183 ARG HA H 4.429 0.01 . 1633 183 183 ARG HB2 H 1.884 0.01 . 1634 183 183 ARG HB3 H 1.884 0.01 . 1635 183 183 ARG HG2 H 1.769 0.01 . 1636 183 183 ARG HG3 H 1.699 0.01 . 1637 183 183 ARG HD2 H 3.329 0.01 . 1638 183 183 ARG HD3 H 3.270 0.01 . 1639 183 183 ARG C C 176.108 0.1 . 1640 183 183 ARG CA C 56.220 0.1 . 1641 183 183 ARG CB C 30.402 0.1 . 1642 183 183 ARG CG C 27.186 0.1 . 1643 183 183 ARG CD C 43.529 0.1 . 1644 183 183 ARG N N 124.018 0.1 . 1645 184 184 GLU H H 8.820 0.01 . 1646 184 184 GLU HA H 4.446 0.01 . 1647 184 184 GLU HB2 H 2.105 0.01 . 1648 184 184 GLU HB3 H 1.875 0.01 . 1649 184 184 GLU HG2 H 2.439 0.01 . 1650 184 184 GLU HG3 H 2.161 0.01 . 1651 184 184 GLU C C 177.124 0.1 . 1652 184 184 GLU CA C 57.094 0.1 . 1653 184 184 GLU CB C 31.247 0.1 . 1654 184 184 GLU CG C 37.271 0.1 . 1655 184 184 GLU N N 125.903 0.1 . 1656 185 185 GLU H H 9.177 0.01 . 1657 185 185 GLU HA H 4.789 0.01 . 1658 185 185 GLU HB2 H 2.300 0.01 . 1659 185 185 GLU C C 176.327 0.1 . 1660 185 185 GLU CA C 55.723 0.1 . 1661 185 185 GLU CB C 30.815 0.1 . 1662 185 185 GLU CG C 36.748 0.1 . 1663 185 185 GLU N N 122.584 0.1 . 1664 186 186 ARG H H 8.898 0.01 . 1665 186 186 ARG HA H 5.445 0.01 . 1666 186 186 ARG HB2 H 1.705 0.01 . 1667 186 186 ARG HG2 H 1.673 0.01 . 1668 186 186 ARG HD2 H 3.240 0.01 . 1669 186 186 ARG C C 175.554 0.1 . 1670 186 186 ARG CA C 55.376 0.1 . 1671 186 186 ARG CB C 33.801 0.1 . 1672 186 186 ARG CG C 30.459 0.1 . 1673 186 186 ARG CD C 43.297 0.1 . 1674 186 186 ARG N N 124.126 0.1 . 1675 187 187 GLN H H 8.856 0.01 . 1676 187 187 GLN HA H 4.888 0.01 . 1677 187 187 GLN HB2 H 2.152 0.01 . 1678 187 187 GLN HB3 H 2.152 0.01 . 1679 187 187 GLN HG2 H 2.580 0.01 . 1680 187 187 GLN HG3 H 2.389 0.01 . 1681 187 187 GLN HE21 H 7.391 0.01 . 1682 187 187 GLN HE22 H 7.118 0.01 . 1683 187 187 GLN CA C 54.108 0.1 . 1684 187 187 GLN CB C 32.418 0.1 . 1685 187 187 GLN CG C 34.195 0.1 . 1686 187 187 GLN CD C 179.310 0.1 . 1687 187 187 GLN N N 121.715 0.1 . 1688 187 187 GLN NE2 N 111.739 0.1 . 1689 188 188 SER HA H 4.623 0.01 . 1690 188 188 SER HB2 H 4.001 0.01 . 1691 188 188 SER HB3 H 3.954 0.01 . 1692 188 188 SER C C 175.085 0.1 . 1693 188 188 SER CA C 59.573 0.1 . 1694 188 188 SER CB C 64.020 0.1 . 1695 189 189 VAL H H 7.892 0.01 . 1696 189 189 VAL HA H 3.815 0.01 . 1697 189 189 VAL HB H 1.892 0.01 . 1698 189 189 VAL HG1 H 0.811 0.01 . 1699 189 189 VAL HG2 H 1.016 0.01 . 1700 189 189 VAL C C 174.460 0.1 . 1701 189 189 VAL CA C 64.730 0.1 . 1702 189 189 VAL CB C 31.204 0.1 . 1703 189 189 VAL CG1 C 21.230 0.1 . 1704 189 189 VAL CG2 C 21.500 0.1 . 1705 189 189 VAL N N 125.289 0.1 . 1706 190 190 PHE H H 8.374 0.01 . 1707 190 190 PHE HA H 4.847 0.01 . 1708 190 190 PHE HB2 H 3.413 0.01 . 1709 190 190 PHE HB3 H 2.378 0.01 . 1710 190 190 PHE CA C 56.292 0.1 . 1711 190 190 PHE CB C 41.578 0.1 . 1712 190 190 PHE N N 125.713 0.1 . 1713 191 191 PRO HA H 4.567 0.01 . 1714 191 191 PRO HB2 H 1.995 0.01 . 1715 191 191 PRO HB3 H 1.519 0.01 . 1716 191 191 PRO HG2 H 1.596 0.01 . 1717 191 191 PRO HG3 H 0.820 0.01 . 1718 191 191 PRO HD2 H 3.435 0.01 . 1719 191 191 PRO HD3 H 2.846 0.01 . 1720 191 191 PRO C C 175.175 0.1 . 1721 191 191 PRO CA C 63.003 0.1 . 1722 191 191 PRO CB C 31.804 0.1 . 1723 191 191 PRO CG C 26.726 0.1 . 1724 191 191 PRO CD C 50.314 0.1 . 1725 192 192 PHE H H 5.782 0.01 . 1726 192 192 PHE HA H 4.403 0.01 . 1727 192 192 PHE HB2 H 2.918 0.01 . 1728 192 192 PHE HB3 H 2.278 0.01 . 1729 192 192 PHE C C 174.061 0.1 . 1730 192 192 PHE CA C 57.429 0.1 . 1731 192 192 PHE CB C 41.789 0.1 . 1732 192 192 PHE N N 113.393 0.1 . 1733 193 193 GLU H H 9.159 0.01 . 1734 193 193 GLU HA H 4.871 0.01 . 1735 193 193 GLU HB2 H 1.962 0.01 . 1736 193 193 GLU HB3 H 1.962 0.01 . 1737 193 193 GLU HG2 H 2.395 0.01 . 1738 193 193 GLU HG3 H 2.364 0.01 . 1739 193 193 GLU C C 175.452 0.1 . 1740 193 193 GLU CA C 55.341 0.1 . 1741 193 193 GLU CB C 33.859 0.1 . 1742 193 193 GLU CG C 36.452 0.1 . 1743 193 193 GLU N N 119.879 0.1 . 1744 194 194 SER H H 9.065 0.01 . 1745 194 194 SER HA H 3.881 0.01 . 1746 194 194 SER HB2 H 3.919 0.01 . 1747 194 194 SER HB3 H 3.919 0.01 . 1748 194 194 SER C C 174.882 0.1 . 1749 194 194 SER CA C 60.729 0.1 . 1750 194 194 SER CB C 63.139 0.1 . 1751 194 194 SER N N 120.525 0.1 . 1752 195 195 GLY H H 7.124 0.01 . 1753 195 195 GLY HA2 H 4.207 0.01 . 1754 195 195 GLY HA3 H 3.726 0.01 . 1755 195 195 GLY C C 174.077 0.1 . 1756 195 195 GLY CA C 45.708 0.1 . 1757 195 195 GLY N N 112.565 0.1 . 1758 196 196 LYS H H 7.736 0.01 . 1759 196 196 LYS HA H 5.122 0.01 . 1760 196 196 LYS HB2 H 2.096 0.01 . 1761 196 196 LYS HB3 H 1.995 0.01 . 1762 196 196 LYS HG2 H 1.529 0.01 . 1763 196 196 LYS HG3 H 1.349 0.01 . 1764 196 196 LYS HD2 H 1.744 0.01 . 1765 196 196 LYS HD3 H 1.657 0.01 . 1766 196 196 LYS HE2 H 3.015 0.01 . 1767 196 196 LYS HE3 H 3.015 0.01 . 1768 196 196 LYS CA C 53.325 0.1 . 1769 196 196 LYS CB C 33.090 0.1 . 1770 196 196 LYS CG C 25.031 0.1 . 1771 196 196 LYS CD C 28.497 0.1 . 1772 196 196 LYS CE C 42.329 0.1 . 1773 196 196 LYS N N 118.020 0.1 . 1774 197 197 PRO HA H 5.263 0.01 . 1775 197 197 PRO HB2 H 2.356 0.01 . 1776 197 197 PRO HB3 H 1.925 0.01 . 1777 197 197 PRO HG2 H 2.084 0.01 . 1778 197 197 PRO HD2 H 4.004 0.01 . 1779 197 197 PRO HD3 H 3.750 0.01 . 1780 197 197 PRO C C 175.850 0.1 . 1781 197 197 PRO CA C 62.659 0.1 . 1782 197 197 PRO CB C 33.149 0.1 . 1783 197 197 PRO CG C 27.404 0.1 . 1784 197 197 PRO CD C 51.621 0.1 . 1785 198 198 PHE H H 8.789 0.01 . 1786 198 198 PHE HA H 5.566 0.01 . 1787 198 198 PHE HB2 H 3.322 0.01 . 1788 198 198 PHE HB3 H 2.958 0.01 . 1789 198 198 PHE C C 172.823 0.1 . 1790 198 198 PHE CA C 56.181 0.1 . 1791 198 198 PHE CB C 43.378 0.1 . 1792 198 198 PHE N N 116.536 0.1 . 1793 199 199 LYS H H 8.184 0.01 . 1794 199 199 LYS HA H 5.188 0.01 . 1795 199 199 LYS HB2 H 1.700 0.01 . 1796 199 199 LYS HB3 H 1.700 0.01 . 1797 199 199 LYS HG2 H 1.234 0.01 . 1798 199 199 LYS HG3 H 1.110 0.01 . 1799 199 199 LYS HD2 H 1.613 0.01 . 1800 199 199 LYS HD3 H 1.538 0.01 . 1801 199 199 LYS HE2 H 2.736 0.01 . 1802 199 199 LYS HE3 H 2.682 0.01 . 1803 199 199 LYS C C 176.093 0.1 . 1804 199 199 LYS CA C 54.828 0.1 . 1805 199 199 LYS CB C 36.571 0.1 . 1806 199 199 LYS CG C 25.065 0.1 . 1807 199 199 LYS CD C 29.968 0.1 . 1808 199 199 LYS CE C 41.349 0.1 . 1809 199 199 LYS N N 121.597 0.1 . 1810 200 200 ILE H H 9.857 0.01 . 1811 200 200 ILE HA H 4.951 0.01 . 1812 200 200 ILE HB H 1.802 0.01 . 1813 200 200 ILE HG12 H 2.136 0.01 . 1814 200 200 ILE HG13 H 1.082 0.01 . 1815 200 200 ILE HG2 H 0.685 0.01 . 1816 200 200 ILE HD1 H 0.781 0.01 . 1817 200 200 ILE C C 175.077 0.1 . 1818 200 200 ILE CA C 60.656 0.1 . 1819 200 200 ILE CB C 41.938 0.1 . 1820 200 200 ILE CG1 C 28.229 0.1 . 1821 200 200 ILE CG2 C 17.476 0.1 . 1822 200 200 ILE CD1 C 14.399 0.1 . 1823 200 200 ILE N N 127.494 0.1 . 1824 201 201 GLN H H 9.368 0.01 . 1825 201 201 GLN HA H 5.841 0.01 . 1826 201 201 GLN HB2 H 1.991 0.01 . 1827 201 201 GLN HB3 H 1.917 0.01 . 1828 201 201 GLN HG2 H 2.588 0.01 . 1829 201 201 GLN HG3 H 2.063 0.01 . 1830 201 201 GLN HE21 H 7.695 0.01 . 1831 201 201 GLN HE22 H 7.085 0.01 . 1832 201 201 GLN C C 174.773 0.1 . 1833 201 201 GLN CA C 53.969 0.1 . 1834 201 201 GLN CB C 33.586 0.1 . 1835 201 201 GLN CG C 35.399 0.1 . 1836 201 201 GLN N N 125.211 0.1 . 1837 201 201 GLN NE2 N 113.832 0.1 . 1838 202 202 VAL H H 9.605 0.01 . 1839 202 202 VAL HA H 5.174 0.01 . 1840 202 202 VAL HB H 2.274 0.01 . 1841 202 202 VAL HG1 H 0.869 0.01 . 1842 202 202 VAL HG2 H 1.098 0.01 . 1843 202 202 VAL C C 173.882 0.1 . 1844 202 202 VAL CA C 60.747 0.1 . 1845 202 202 VAL CB C 34.490 0.1 . 1846 202 202 VAL CG1 C 20.051 0.1 . 1847 202 202 VAL CG2 C 21.998 0.1 . 1848 202 202 VAL N N 123.331 0.1 . 1849 203 203 LEU H H 9.523 0.01 . 1850 203 203 LEU HA H 5.427 0.01 . 1851 203 203 LEU HG H 1.264 0.01 . 1852 203 203 LEU HD1 H 0.817 0.01 . 1853 203 203 LEU HD2 H 0.633 0.01 . 1854 203 203 LEU C C 175.663 0.1 . 1855 203 203 LEU CA C 53.183 0.1 . 1856 203 203 LEU CB C 45.377 0.1 . 1857 203 203 LEU CG C 27.725 0.1 . 1858 203 203 LEU CD1 C 23.584 0.1 . 1859 203 203 LEU CD2 C 26.365 0.1 . 1860 203 203 LEU N N 130.215 0.1 . 1861 204 204 VAL H H 8.973 0.01 . 1862 204 204 VAL HA H 3.899 0.01 . 1863 204 204 VAL HB H 2.474 0.01 . 1864 204 204 VAL HG1 H 1.063 0.01 . 1865 204 204 VAL HG2 H 0.434 0.01 . 1866 204 204 VAL C C 174.741 0.1 . 1867 204 204 VAL CA C 63.486 0.1 . 1868 204 204 VAL CB C 30.976 0.1 . 1869 204 204 VAL CG1 C 20.529 0.1 . 1870 204 204 VAL CG2 C 21.496 0.1 . 1871 204 204 VAL N N 127.453 0.1 . 1872 205 205 GLU H H 8.325 0.01 . 1873 205 205 GLU HA H 5.062 0.01 . 1874 205 205 GLU HB2 H 1.984 0.01 . 1875 205 205 GLU HG2 H 1.940 0.01 . 1876 205 205 GLU HG3 H 1.940 0.01 . 1877 205 205 GLU CA C 54.406 0.1 . 1878 205 205 GLU CB C 28.819 0.1 . 1879 205 205 GLU CG C 36.071 0.1 . 1880 205 205 GLU N N 128.112 0.1 . 1881 206 206 PRO HA H 4.002 0.01 . 1882 206 206 PRO HB2 H 2.368 0.01 . 1883 206 206 PRO HB3 H 1.814 0.01 . 1884 206 206 PRO C C 176.847 0.1 . 1885 206 206 PRO CA C 66.221 0.1 . 1886 207 207 ASP H H 8.005 0.01 . 1887 207 207 ASP HA H 4.916 0.01 . 1888 207 207 ASP HB2 H 2.660 0.01 . 1889 207 207 ASP HB3 H 2.625 0.01 . 1890 207 207 ASP C C 176.327 0.1 . 1891 207 207 ASP CA C 53.679 0.1 . 1892 207 207 ASP CB C 41.970 0.1 . 1893 207 207 ASP N N 106.998 0.1 . 1894 208 208 HIS H H 6.500 0.01 . 1895 208 208 HIS HA H 3.996 0.01 . 1896 208 208 HIS HB2 H 3.286 0.01 . 1897 208 208 HIS HB3 H 2.463 0.01 . 1898 208 208 HIS C C 172.912 0.1 . 1899 208 208 HIS CA C 54.961 0.1 . 1900 208 208 HIS CB C 31.840 0.1 . 1901 208 208 HIS N N 116.267 0.1 . 1902 209 209 PHE H H 8.577 0.01 . 1903 209 209 PHE HA H 4.971 0.01 . 1904 209 209 PHE HB2 H 2.565 0.01 . 1905 209 209 PHE HB3 H 2.379 0.01 . 1906 209 209 PHE CA C 57.658 0.1 . 1907 209 209 PHE CB C 41.678 0.1 . 1908 209 209 PHE N N 114.701 0.1 . 1909 210 210 LYS H H 9.633 0.01 . 1910 210 210 LYS HA H 5.086 0.01 . 1911 210 210 LYS C C 175.163 0.1 . 1912 210 210 LYS CA C 56.662 0.1 . 1913 210 210 LYS CB C 35.817 0.1 . 1914 210 210 LYS CG C 27.450 0.1 . 1915 210 210 LYS CE C 41.483 0.1 . 1916 210 210 LYS N N 123.212 0.1 . 1917 211 211 VAL H H 9.037 0.01 . 1918 211 211 VAL HA H 5.047 0.01 . 1919 211 211 VAL HB H 1.840 0.01 . 1920 211 211 VAL HG1 H 0.464 0.01 . 1921 211 211 VAL HG2 H 0.829 0.01 . 1922 211 211 VAL C C 173.585 0.1 . 1923 211 211 VAL CA C 61.412 0.1 . 1924 211 211 VAL CB C 34.311 0.1 . 1925 211 211 VAL CG1 C 21.230 0.1 . 1926 211 211 VAL CG2 C 21.552 0.1 . 1927 211 211 VAL N N 122.218 0.1 . 1928 212 212 ALA H H 9.456 0.01 . 1929 212 212 ALA HA H 4.996 0.01 . 1930 212 212 ALA HB H 1.131 0.01 . 1931 212 212 ALA C C 177.022 0.1 . 1932 212 212 ALA CA C 50.928 0.1 . 1933 212 212 ALA CB C 22.585 0.1 . 1934 212 212 ALA N N 129.730 0.1 . 1935 213 213 VAL H H 8.380 0.01 . 1936 213 213 VAL HA H 5.107 0.01 . 1937 213 213 VAL HB H 1.614 0.01 . 1938 213 213 VAL HG1 H 0.260 0.01 . 1939 213 213 VAL HG2 H 0.760 0.01 . 1940 213 213 VAL C C 175.593 0.1 . 1941 213 213 VAL CA C 59.980 0.1 . 1942 213 213 VAL CB C 34.338 0.1 . 1943 213 213 VAL CG1 C 20.774 0.1 . 1944 213 213 VAL CG2 C 23.407 0.1 . 1945 213 213 VAL N N 120.514 0.1 . 1946 214 214 ASN H H 9.885 0.01 . 1947 214 214 ASN HA H 4.281 0.01 . 1948 214 214 ASN HB2 H 2.948 0.01 . 1949 214 214 ASN HB3 H 2.948 0.01 . 1950 214 214 ASN HD21 H 7.576 0.01 . 1951 214 214 ASN HD22 H 6.708 0.01 . 1952 214 214 ASN C C 173.983 0.1 . 1953 214 214 ASN CA C 54.448 0.1 . 1954 214 214 ASN CB C 35.779 0.1 . 1955 214 214 ASN N N 127.206 0.1 . 1956 214 214 ASN ND2 N 111.762 0.1 . 1957 215 215 ASP H H 8.899 0.01 . 1958 215 215 ASP HA H 4.042 0.01 . 1959 215 215 ASP HB2 H 3.014 0.01 . 1960 215 215 ASP HB3 H 2.864 0.01 . 1961 215 215 ASP C C 173.839 0.1 . 1962 215 215 ASP CA C 56.353 0.1 . 1963 215 215 ASP CB C 39.132 0.1 . 1964 215 215 ASP N N 107.612 0.1 . 1965 216 216 ALA H H 7.560 0.01 . 1966 216 216 ALA HA H 4.703 0.01 . 1967 216 216 ALA HB H 1.304 0.01 . 1968 216 216 ALA C C 176.538 0.1 . 1969 216 216 ALA CA C 50.912 0.1 . 1970 216 216 ALA CB C 21.069 0.1 . 1971 216 216 ALA N N 120.180 0.1 . 1972 217 217 HIS H H 8.882 0.01 . 1973 217 217 HIS HA H 4.135 0.01 . 1974 217 217 HIS HB2 H 3.059 0.01 . 1975 217 217 HIS HB3 H 2.935 0.01 . 1976 217 217 HIS C C 174.249 0.1 . 1977 217 217 HIS CA C 59.494 0.1 . 1978 217 217 HIS CB C 31.138 0.1 . 1979 217 217 HIS N N 124.086 0.1 . 1980 218 218 LEU H H 9.071 0.01 . 1981 218 218 LEU HA H 4.583 0.01 . 1982 218 218 LEU HB2 H 1.669 0.01 . 1983 218 218 LEU HB3 H 1.311 0.01 . 1984 218 218 LEU HG H 1.282 0.01 . 1985 218 218 LEU HD1 H 0.847 0.01 . 1986 218 218 LEU HD2 H 0.867 0.01 . 1987 218 218 LEU C C 174.780 0.1 . 1988 218 218 LEU CA C 55.640 0.1 . 1989 218 218 LEU CB C 45.281 0.1 . 1990 218 218 LEU CG C 27.474 0.1 . 1991 218 218 LEU CD1 C 22.529 0.1 . 1992 218 218 LEU CD2 C 26.907 0.1 . 1993 218 218 LEU N N 128.625 0.1 . 1994 219 219 LEU H H 7.713 0.01 . 1995 219 219 LEU HA H 4.691 0.01 . 1996 219 219 LEU HB2 H 2.040 0.01 . 1997 219 219 LEU HB3 H 1.771 0.01 . 1998 219 219 LEU HG H 1.579 0.01 . 1999 219 219 LEU HD1 H 0.973 0.01 . 2000 219 219 LEU HD2 H 1.007 0.01 . 2001 219 219 LEU C C 173.784 0.1 . 2002 219 219 LEU CA C 54.439 0.1 . 2003 219 219 LEU CB C 43.524 0.1 . 2004 219 219 LEU CG C 26.099 0.1 . 2005 219 219 LEU CD1 C 24.835 0.1 . 2006 219 219 LEU CD2 C 28.619 0.1 . 2007 219 219 LEU N N 110.515 0.1 . 2008 220 220 GLN H H 8.728 0.01 . 2009 220 220 GLN HA H 5.474 0.01 . 2010 220 220 GLN HB2 H 1.824 0.01 . 2011 220 220 GLN HB3 H 1.730 0.01 . 2012 220 220 GLN HG2 H 2.157 0.01 . 2013 220 220 GLN HG3 H 2.080 0.01 . 2014 220 220 GLN HE21 H 6.993 0.01 . 2015 220 220 GLN HE22 H 6.399 0.01 . 2016 220 220 GLN C C 174.257 0.1 . 2017 220 220 GLN CA C 53.827 0.1 . 2018 220 220 GLN CB C 32.590 0.1 . 2019 220 220 GLN CG C 34.374 0.1 . 2020 220 220 GLN N N 118.908 0.1 . 2021 220 220 GLN NE2 N 110.654 0.1 . 2022 221 221 TYR H H 8.983 0.01 . 2023 221 221 TYR HA H 4.821 0.01 . 2024 221 221 TYR HB2 H 2.251 0.01 . 2025 221 221 TYR HB3 H 2.155 0.01 . 2026 221 221 TYR C C 174.499 0.1 . 2027 221 221 TYR CA C 56.705 0.1 . 2028 221 221 TYR CB C 42.027 0.1 . 2029 221 221 TYR N N 125.715 0.1 . 2030 222 222 ASN H H 9.246 0.01 . 2031 222 222 ASN HA H 4.512 0.01 . 2032 222 222 ASN HB2 H 2.668 0.01 . 2033 222 222 ASN HB3 H 2.588 0.01 . 2034 222 222 ASN HD21 H 7.335 0.01 . 2035 222 222 ASN HD22 H 6.787 0.01 . 2036 222 222 ASN C C 175.176 0.1 . 2037 222 222 ASN CA C 53.240 0.1 . 2038 222 222 ASN CB C 37.799 0.1 . 2039 222 222 ASN N N 129.653 0.1 . 2040 222 222 ASN ND2 N 110.721 0.1 . 2041 223 223 HIS H H 7.212 0.01 . 2042 223 223 HIS HA H 4.583 0.01 . 2043 223 223 HIS HB2 H 2.664 0.01 . 2044 223 223 HIS HB3 H 2.664 0.01 . 2045 223 223 HIS HE2 H 10.106 0.01 . 2046 223 223 HIS C C 177.257 0.1 . 2047 223 223 HIS CA C 57.595 0.1 . 2048 223 223 HIS CB C 31.094 0.1 . 2049 223 223 HIS N N 117.333 0.1 . 2050 223 223 HIS NE2 N 161.376 0.1 . 2051 224 224 ARG H H 9.478 0.01 . 2052 224 224 ARG HD2 H 3.273 0.01 . 2053 224 224 ARG HD3 H 3.273 0.01 . 2054 224 224 ARG HE H 7.498 0.01 . 2055 224 224 ARG C C 177.413 0.1 . 2056 224 224 ARG CA C 57.564 0.1 . 2057 224 224 ARG CB C 31.704 0.1 . 2058 224 224 ARG CG C 27.216 0.1 . 2059 224 224 ARG CD C 44.219 0.1 . 2060 224 224 ARG N N 125.249 0.1 . 2061 224 224 ARG NE N 84.750 0.1 . 2062 225 225 VAL H H 8.322 0.01 . 2063 225 225 VAL HA H 4.049 0.01 . 2064 225 225 VAL HB H 2.033 0.01 . 2065 225 225 VAL HG1 H 0.841 0.01 . 2066 225 225 VAL HG2 H 1.028 0.01 . 2067 225 225 VAL CA C 62.153 0.1 . 2068 225 225 VAL CB C 32.744 0.1 . 2069 225 225 VAL CG1 C 20.907 0.1 . 2070 225 225 VAL CG2 C 22.132 0.1 . 2071 225 225 VAL N N 120.290 0.1 . 2072 226 226 LYS HA H 4.029 0.01 . 2073 226 226 LYS HB2 H 1.942 0.01 . 2074 226 226 LYS HB3 H 1.638 0.01 . 2075 226 226 LYS HG2 H 1.390 0.01 . 2076 226 226 LYS HG3 H 1.288 0.01 . 2077 226 226 LYS HD2 H 1.597 0.01 . 2078 226 226 LYS HD3 H 1.597 0.01 . 2079 226 226 LYS HE2 H 3.011 0.01 . 2080 226 226 LYS HE3 H 3.011 0.01 . 2081 226 226 LYS C C 177.092 0.1 . 2082 226 226 LYS CA C 56.769 0.1 . 2083 226 226 LYS CB C 32.526 0.1 . 2084 226 226 LYS CG C 25.559 0.1 . 2085 226 226 LYS CD C 28.652 0.1 . 2086 226 226 LYS CE C 42.074 0.1 . 2087 227 227 LYS H H 7.082 0.01 . 2088 227 227 LYS HA H 4.472 0.01 . 2089 227 227 LYS HB2 H 1.751 0.01 . 2090 227 227 LYS HB3 H 1.526 0.01 . 2091 227 227 LYS HG2 H 1.385 0.01 . 2092 227 227 LYS HG3 H 1.336 0.01 . 2093 227 227 LYS HD2 H 1.654 0.01 . 2094 227 227 LYS HD3 H 1.616 0.01 . 2095 227 227 LYS HE2 H 2.965 0.01 . 2096 227 227 LYS HE3 H 2.965 0.01 . 2097 227 227 LYS C C 176.069 0.1 . 2098 227 227 LYS CA C 54.404 0.1 . 2099 227 227 LYS CB C 29.707 0.1 . 2100 227 227 LYS CG C 24.503 0.1 . 2101 227 227 LYS CD C 29.046 0.1 . 2102 227 227 LYS CE C 42.061 0.1 . 2103 227 227 LYS N N 120.647 0.1 . 2104 228 228 LEU H H 7.651 0.01 . 2105 228 228 LEU HA H 3.569 0.01 . 2106 228 228 LEU HB2 H 1.552 0.01 . 2107 228 228 LEU HB3 H 1.355 0.01 . 2108 228 228 LEU HG H 1.338 0.01 . 2109 228 228 LEU HD1 H 0.340 0.01 . 2110 228 228 LEU HD2 H -0.255 0.01 . 2111 228 228 LEU C C 178.315 0.1 . 2112 228 228 LEU CA C 57.857 0.1 . 2113 228 228 LEU CB C 40.438 0.1 . 2114 228 228 LEU CG C 26.567 0.1 . 2115 228 228 LEU CD1 C 24.382 0.1 . 2116 228 228 LEU CD2 C 20.044 0.1 . 2117 228 228 LEU N N 122.854 0.1 . 2118 229 229 ASN H H 8.421 0.01 . 2119 229 229 ASN HA H 4.602 0.01 . 2120 229 229 ASN HB2 H 2.888 0.01 . 2121 229 229 ASN HB3 H 2.730 0.01 . 2122 229 229 ASN HD21 H 7.546 0.01 . 2123 229 229 ASN HD22 H 7.019 0.01 . 2124 229 229 ASN C C 174.983 0.1 . 2125 229 229 ASN CA C 55.366 0.1 . 2126 229 229 ASN CB C 36.908 0.1 . 2127 229 229 ASN CG C 177.430 0.1 . 2128 229 229 ASN N N 112.968 0.1 . 2129 229 229 ASN ND2 N 113.799 0.1 . 2130 230 230 GLU H H 7.432 0.01 . 2131 230 230 GLU HA H 4.245 0.01 . 2132 230 230 GLU HB2 H 2.259 0.01 . 2133 230 230 GLU HB3 H 1.896 0.01 . 2134 230 230 GLU HG2 H 2.245 0.01 . 2135 230 230 GLU HG3 H 2.152 0.01 . 2136 230 230 GLU C C 176.589 0.1 . 2137 230 230 GLU CA C 56.011 0.1 . 2138 230 230 GLU CB C 30.416 0.1 . 2139 230 230 GLU CG C 36.758 0.1 . 2140 230 230 GLU N N 116.444 0.1 . 2141 231 231 ILE H H 7.651 0.01 . 2142 231 231 ILE HA H 4.456 0.01 . 2143 231 231 ILE HB H 2.320 0.01 . 2144 231 231 ILE HG12 H 1.894 0.01 . 2145 231 231 ILE HG13 H 0.621 0.01 . 2146 231 231 ILE HG2 H 1.125 0.01 . 2147 231 231 ILE HD1 H 0.931 0.01 . 2148 231 231 ILE C C 174.475 0.1 . 2149 231 231 ILE CA C 61.518 0.1 . 2150 231 231 ILE CB C 36.441 0.1 . 2151 231 231 ILE CG1 C 27.799 0.1 . 2152 231 231 ILE CG2 C 19.173 0.1 . 2153 231 231 ILE CD1 C 15.098 0.1 . 2154 231 231 ILE N N 122.140 0.1 . 2155 232 232 SER H H 7.714 0.01 . 2156 232 232 SER HA H 4.943 0.01 . 2157 232 232 SER HB2 H 4.188 0.01 . 2158 232 232 SER HB3 H 3.682 0.01 . 2159 232 232 SER C C 175.593 0.1 . 2160 232 232 SER CA C 58.566 0.1 . 2161 232 232 SER CB C 65.305 0.1 . 2162 232 232 SER N N 116.223 0.1 . 2163 233 233 LYS H H 7.880 0.01 . 2164 233 233 LYS HA H 4.837 0.01 . 2165 233 233 LYS HB2 H 1.877 0.01 . 2166 233 233 LYS HB3 H 1.663 0.01 . 2167 233 233 LYS HG2 H 1.268 0.01 . 2168 233 233 LYS HG3 H 1.241 0.01 . 2169 233 233 LYS HD2 H 1.523 0.01 . 2170 233 233 LYS HD3 H 1.523 0.01 . 2171 233 233 LYS HE2 H 2.816 0.01 . 2172 233 233 LYS HE3 H 2.816 0.01 . 2173 233 233 LYS C C 172.811 0.1 . 2174 233 233 LYS CA C 56.303 0.1 . 2175 233 233 LYS CB C 36.461 0.1 . 2176 233 233 LYS CG C 24.479 0.1 . 2177 233 233 LYS CD C 29.460 0.1 . 2178 233 233 LYS CE C 41.788 0.1 . 2179 233 233 LYS N N 120.904 0.1 . 2180 234 234 LEU H H 8.609 0.01 . 2181 234 234 LEU HA H 4.890 0.01 . 2182 234 234 LEU HB2 H 1.831 0.01 . 2183 234 234 LEU HB3 H 0.843 0.01 . 2184 234 234 LEU HG H 1.120 0.01 . 2185 234 234 LEU HD1 H -0.333 0.01 . 2186 234 234 LEU HD2 H 0.605 0.01 . 2187 234 234 LEU C C 174.241 0.1 . 2188 234 234 LEU CA C 52.714 0.1 . 2189 234 234 LEU CB C 44.016 0.1 . 2190 234 234 LEU CG C 26.790 0.1 . 2191 234 234 LEU CD1 C 22.040 0.1 . 2192 234 234 LEU CD2 C 26.694 0.1 . 2193 234 234 LEU N N 124.659 0.1 . 2194 235 235 GLY H H 9.314 0.01 . 2195 235 235 GLY HA2 H 5.100 0.01 . 2196 235 235 GLY HA3 H 3.516 0.01 . 2197 235 235 GLY C C 173.890 0.1 . 2198 235 235 GLY CA C 45.043 0.1 . 2199 235 235 GLY N N 114.530 0.1 . 2200 236 236 ILE H H 9.357 0.01 . 2201 236 236 ILE HA H 4.805 0.01 . 2202 236 236 ILE HB H 1.991 0.01 . 2203 236 236 ILE HG12 H 1.693 0.01 . 2204 236 236 ILE HG13 H 0.844 0.01 . 2205 236 236 ILE HG2 H 0.927 0.01 . 2206 236 236 ILE HD1 H 0.943 0.01 . 2207 236 236 ILE C C 174.249 0.1 . 2208 236 236 ILE CA C 61.327 0.1 . 2209 236 236 ILE CB C 40.572 0.1 . 2210 236 236 ILE CG1 C 27.873 0.1 . 2211 236 236 ILE CG2 C 18.591 0.1 . 2212 236 236 ILE CD1 C 15.939 0.1 . 2213 236 236 ILE N N 127.294 0.1 . 2214 237 237 SER H H 9.374 0.01 . 2215 237 237 SER HA H 4.803 0.01 . 2216 237 237 SER HB2 H 3.966 0.01 . 2217 237 237 SER HB3 H 3.903 0.01 . 2218 237 237 SER C C 171.932 0.1 . 2219 237 237 SER CA C 57.621 0.1 . 2220 237 237 SER CB C 66.406 0.1 . 2221 237 237 SER N N 120.328 0.1 . 2222 238 238 GLY H H 8.827 0.01 . 2223 238 238 GLY HA2 H 4.564 0.01 . 2224 238 238 GLY HA3 H 3.682 0.01 . 2225 238 238 GLY C C 175.015 0.1 . 2226 238 238 GLY CA C 43.432 0.1 . 2227 238 238 GLY N N 105.551 0.1 . 2228 239 239 ASP H H 8.590 0.01 . 2229 239 239 ASP HA H 4.756 0.01 . 2230 239 239 ASP HB2 H 2.661 0.01 . 2231 239 239 ASP HB3 H 2.486 0.01 . 2232 239 239 ASP C C 174.741 0.1 . 2233 239 239 ASP CA C 54.250 0.1 . 2234 239 239 ASP CB C 41.093 0.1 . 2235 239 239 ASP N N 121.821 0.1 . 2236 240 240 ILE H H 7.898 0.01 . 2237 240 240 ILE HA H 5.140 0.01 . 2238 240 240 ILE HB H 1.901 0.01 . 2239 240 240 ILE HG12 H 1.340 0.01 . 2240 240 240 ILE HG13 H 0.712 0.01 . 2241 240 240 ILE HG2 H 0.795 0.01 . 2242 240 240 ILE HD1 H 0.680 0.01 . 2243 240 240 ILE C C 173.952 0.1 . 2244 240 240 ILE CA C 58.778 0.1 . 2245 240 240 ILE CB C 42.577 0.1 . 2246 240 240 ILE CG1 C 25.138 0.1 . 2247 240 240 ILE CG2 C 19.959 0.1 . 2248 240 240 ILE CD1 C 14.153 0.1 . 2249 240 240 ILE N N 111.779 0.1 . 2250 241 241 ASP H H 8.903 0.01 . 2251 241 241 ASP HA H 4.952 0.01 . 2252 241 241 ASP HB2 H 2.591 0.01 . 2253 241 241 ASP HB3 H 2.411 0.01 . 2254 241 241 ASP C C 174.986 0.1 . 2255 241 241 ASP CA C 53.734 0.1 . 2256 241 241 ASP CB C 42.642 0.1 . 2257 241 241 ASP N N 120.726 0.1 . 2258 242 242 LEU H H 9.145 0.01 . 2259 242 242 LEU HA H 4.522 0.01 . 2260 242 242 LEU HB2 H 1.628 0.01 . 2261 242 242 LEU HB3 H 1.095 0.01 . 2262 242 242 LEU HG H 1.250 0.01 . 2263 242 242 LEU HD1 H 0.851 0.01 . 2264 242 242 LEU HD2 H 0.541 0.01 . 2265 242 242 LEU C C 174.897 0.1 . 2266 242 242 LEU CA C 54.438 0.1 . 2267 242 242 LEU CB C 45.131 0.1 . 2268 242 242 LEU CG C 27.004 0.1 . 2269 242 242 LEU CD1 C 24.684 0.1 . 2270 242 242 LEU CD2 C 27.002 0.1 . 2271 242 242 LEU N N 125.544 0.1 . 2272 243 243 THR H H 9.043 0.01 . 2273 243 243 THR HA H 4.359 0.01 . 2274 243 243 THR HB H 3.797 0.01 . 2275 243 243 THR HG2 H 1.066 0.01 . 2276 243 243 THR C C 174.772 0.1 . 2277 243 243 THR CA C 63.463 0.1 . 2278 243 243 THR CB C 69.329 0.1 . 2279 243 243 THR CG2 C 22.233 0.1 . 2280 243 243 THR N N 119.634 0.1 . 2281 244 244 SER H H 7.745 0.01 . 2282 244 244 SER HA H 4.407 0.01 . 2283 244 244 SER HB2 H 3.772 0.01 . 2284 244 244 SER HB3 H 3.531 0.01 . 2285 244 244 SER C C 172.179 0.1 . 2286 244 244 SER CA C 58.271 0.1 . 2287 244 244 SER CB C 64.455 0.1 . 2288 244 244 SER N N 112.326 0.1 . 2289 245 245 ALA H H 8.390 0.01 . 2290 245 245 ALA HA H 5.226 0.01 . 2291 245 245 ALA HB H 1.259 0.01 . 2292 245 245 ALA C C 174.003 0.1 . 2293 245 245 ALA CA C 51.913 0.1 . 2294 245 245 ALA CB C 21.623 0.1 . 2295 245 245 ALA N N 126.540 0.1 . 2296 246 246 SER H H 8.594 0.01 . 2297 246 246 SER HA H 4.857 0.01 . 2298 246 246 SER HB2 H 3.941 0.01 . 2299 246 246 SER HB3 H 3.941 0.01 . 2300 246 246 SER C C 171.538 0.1 . 2301 246 246 SER CA C 57.585 0.1 . 2302 246 246 SER CB C 65.754 0.1 . 2303 246 246 SER N N 115.297 0.1 . 2304 247 247 TYR H H 8.348 0.01 . 2305 247 247 TYR HA H 5.968 0.01 . 2306 247 247 TYR HB2 H 3.044 0.01 . 2307 247 247 TYR HB3 H 2.876 0.01 . 2308 247 247 TYR C C 173.194 0.1 . 2309 247 247 TYR CA C 55.655 0.1 . 2310 247 247 TYR CB C 43.516 0.1 . 2311 247 247 TYR N N 114.859 0.1 . 2312 248 248 THR H H 8.883 0.01 . 2313 248 248 THR HA H 4.631 0.01 . 2314 248 248 THR HB H 4.146 0.01 . 2315 248 248 THR HG2 H 1.167 0.01 . 2316 248 248 THR C C 171.929 0.1 . 2317 248 248 THR CA C 59.630 0.1 . 2318 248 248 THR CB C 70.597 0.1 . 2319 248 248 THR CG2 C 19.478 0.1 . 2320 248 248 THR N N 114.839 0.1 . 2321 249 249 MET H H 8.116 0.01 . 2322 249 249 MET HA H 5.528 0.01 . 2323 249 249 MET HB2 H 2.150 0.01 . 2324 249 249 MET HB3 H 1.990 0.01 . 2325 249 249 MET HG2 H 2.742 0.01 . 2326 249 249 MET HG3 H 2.559 0.01 . 2327 249 249 MET HE H 2.040 0.01 . 2328 249 249 MET C C 176.444 0.1 . 2329 249 249 MET CA C 53.281 0.1 . 2330 249 249 MET CB C 31.873 0.1 . 2331 249 249 MET CG C 31.799 0.1 . 2332 249 249 MET CE C 16.385 0.1 . 2333 249 249 MET N N 120.931 0.1 . 2334 250 250 ILE H H 8.585 0.01 . 2335 250 250 ILE HA H 4.428 0.01 . 2336 250 250 ILE HB H 2.097 0.01 . 2337 250 250 ILE HG12 H 1.341 0.01 . 2338 250 250 ILE HG13 H 1.222 0.01 . 2339 250 250 ILE HG2 H 0.891 0.01 . 2340 250 250 ILE HD1 H 0.871 0.01 . 2341 250 250 ILE CA C 62.240 0.1 . 2342 250 250 ILE CB C 40.203 0.1 . 2343 250 250 ILE CG1 C 26.659 0.1 . 2344 250 250 ILE CG2 C 19.692 0.1 . 2345 250 250 ILE CD1 C 15.199 0.1 . 2346 250 250 ILE N N 124.656 0.1 . stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details ; Estimated error limits of chemical shifts are based upon the standard error in average chemical shift position of corresponding resonance lines across different NMR spectra. Typical standard errors of the average position of resonances taken over different spectra and sample preparations are 0.005 ppm for 1H, 0.06 ppm for 13C and 0.07 ppm for 15N. Number of equivalent peak positions per assigned resonance is considered as a Figure of Merit tohave an indicator of accurate shifts. Tbis number is given in column _Atom_chem_shift.Assign_fig_of_merit of the chemical shift table. No stereospecific assignments have been carried out for the protein and prochiral methylene and methyl groups are therefore listed as unambiguously assignments. Because of the highly repetative sequence parts PGAYP that are present in the first N-terminal region of the protein (1-109), the following residues must be considered interresidue ambiguous (index type 5) and the corresponding PGAYP resonances may well be interchangeable seen in terms of a five-amino stretch. P42 = P51 G43 = G52 A44 = A52 Y45 = Y53 P46 = P54 G47 = G55 Q48 = Q57 A49 = A58 P50 = P59 P67 = P98 G68 = G99 A69 = A100 Y70 = Y101 P71 = P102 ; loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D CC(CO)NH' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D HNHA' '3D HN(CO)CA' '3D HcCH DIPSI' '3D hCCH DIPSI' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D C_CON' '2D C_CACO' '2D C_CAN' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Galectin-3, cis form, 1 (b)' _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 4 4 ASN HA H 4.635 0.01 . 2 4 4 ASN HB2 H 2.723 0.01 . 3 4 4 ASN HB3 H 2.654 0.01 . 4 4 4 ASN C C 174.963 0.1 . 5 4 4 ASN CA C 53.150 0.1 . 6 4 4 ASN CB C 38.808 0.1 . 7 5 5 PHE H H 8.236 0.01 . 8 5 5 PHE HA H 4.482 0.01 . 9 5 5 PHE HB2 H 3.155 0.01 . 10 5 5 PHE HB3 H 3.028 0.01 . 11 5 5 PHE C C 175.766 0.1 . 12 5 5 PHE CA C 58.006 0.1 . 13 5 5 PHE CB C 39.465 0.1 . 14 5 5 PHE N N 120.434 0.1 . 15 6 6 SER H H 8.208 0.01 . 16 6 6 SER HA H 4.401 0.01 . 17 6 6 SER HB2 H 3.804 0.01 . 18 6 6 SER HB3 H 3.804 0.01 . 19 6 6 SER C C 174.409 0.1 . 20 6 6 SER CA C 58.180 0.1 . 21 6 6 SER CB C 63.998 0.1 . 22 6 6 SER N N 117.229 0.1 . 23 7 7 LEU H H 8.157 0.01 . 24 7 7 LEU HA H 4.283 0.01 . 25 7 7 LEU HB2 H 1.543 0.01 . 26 7 7 LEU HB3 H 1.543 0.01 . 27 7 7 LEU HD1 H 0.902 0.01 . 28 7 7 LEU HD2 H 0.856 0.01 . 29 7 7 LEU C C 177.298 0.1 . 30 7 7 LEU CA C 55.477 0.1 . 31 7 7 LEU CB C 42.331 0.1 . 32 7 7 LEU CG C 26.988 0.1 . 33 7 7 LEU CD1 C 24.947 0.1 . 34 7 7 LEU CD2 C 23.591 0.1 . 35 7 7 LEU N N 123.853 0.1 . 36 11 11 LEU HA H 4.354 0.01 . 37 11 11 LEU HB2 H 1.703 0.01 . 38 11 11 LEU HB3 H 1.617 0.01 . 39 11 11 LEU HG H 1.615 0.01 . 40 11 11 LEU HD1 H 0.917 0.01 . 41 11 11 LEU HD2 H 0.863 0.01 . 42 11 11 LEU C C 177.816 0.1 . 43 11 11 LEU CA C 55.427 0.1 . 44 11 11 LEU CB C 42.205 0.1 . 45 11 11 LEU CG C 27.147 0.1 . 46 11 11 LEU CD1 C 24.952 0.1 . 47 11 11 LEU CD2 C 23.536 0.1 . 48 12 12 SER C C 175.222 0.1 . 49 12 12 SER CA C 58.715 0.1 . 50 17 17 PRO HA H 4.346 0.01 . 51 17 17 PRO HB2 H 2.133 0.01 . 52 17 17 PRO HB3 H 1.869 0.01 . 53 17 17 PRO C C 175.452 0.1 . 54 17 17 PRO CA C 63.329 0.1 . 55 17 17 PRO CB C 31.996 0.1 . 56 18 18 ASN H H 8.099 0.01 . 57 18 18 ASN HA H 4.747 0.01 . 58 18 18 ASN CA C 50.947 0.1 . 59 18 18 ASN CB C 40.379 0.1 . 60 18 18 ASN N N 118.585 0.1 . 61 19 19 PRO HA H 4.370 0.01 . 62 19 19 PRO HB2 H 2.230 0.01 . 63 19 19 PRO HB3 H 1.913 0.01 . 64 19 19 PRO C C 176.995 0.1 . 65 19 19 PRO CA C 63.605 0.1 . 66 19 19 PRO CB C 32.095 0.1 . 67 19 19 PRO CG C 27.271 0.1 . 68 20 20 GLN H H 8.380 0.01 . 69 20 20 GLN HA H 4.282 0.01 . 70 20 20 GLN HB2 H 2.095 0.01 . 71 20 20 GLN HB3 H 1.975 0.01 . 72 20 20 GLN HG2 H 2.350 0.01 . 73 20 20 GLN HG3 H 2.350 0.01 . 74 20 20 GLN C C 176.527 0.1 . 75 20 20 GLN CA C 56.301 0.1 . 76 20 20 GLN CB C 29.322 0.1 . 77 20 20 GLN CG C 34.052 0.1 . 78 20 20 GLN N N 119.336 0.1 . 79 21 21 GLY H H 8.260 0.01 . 80 21 21 GLY HA2 H 3.934 0.01 . 81 21 21 GLY HA3 H 3.889 0.01 . 82 21 21 GLY C C 172.910 0.1 . 83 21 21 GLY CA C 45.283 0.1 . 84 21 21 GLY N N 109.719 0.1 . 85 22 22 TRP H H 8.060 0.01 . 86 22 22 TRP HA H 4.587 0.01 . 87 22 22 TRP HB2 H 3.161 0.01 . 88 22 22 TRP HB3 H 3.161 0.01 . 89 22 22 TRP HE1 H 10.173 0.01 . 90 22 22 TRP C C 175.291 0.1 . 91 22 22 TRP CA C 55.705 0.1 . 92 22 22 TRP CB C 30.831 0.1 . 93 22 22 TRP N N 122.292 0.1 . 94 22 22 TRP NE1 N 130.070 0.1 . 95 23 23 PRO HA H 3.426 0.01 . 96 23 23 PRO HB2 H 1.583 0.01 . 97 23 23 PRO HB3 H 0.828 0.01 . 98 23 23 PRO HG2 H 1.462 0.01 . 99 23 23 PRO HG3 H 1.341 0.01 . 100 23 23 PRO HD2 H 3.380 0.01 . 101 23 23 PRO HD3 H 3.119 0.01 . 102 23 23 PRO C C 176.402 0.1 . 103 23 23 PRO CA C 63.225 0.1 . 104 23 23 PRO CB C 33.325 0.1 . 105 23 23 PRO CG C 24.267 0.1 . 106 23 23 PRO CD C 49.927 0.1 . 107 23 23 PRO N N 135.597 0.1 . 108 24 24 GLY H H 8.163 0.01 . 109 24 24 GLY HA2 H 3.752 0.01 . 110 24 24 GLY HA3 H 3.752 0.01 . 111 24 24 GLY C C 173.659 0.1 . 112 24 24 GLY CA C 45.703 0.1 . 113 24 24 GLY N N 111.592 0.1 . 114 26 26 TRP HA H 4.606 0.01 . 115 26 26 TRP HB2 H 3.297 0.01 . 116 26 26 TRP HB3 H 3.152 0.01 . 117 26 26 TRP HE1 H 10.119 0.01 . 118 26 26 TRP C C 176.723 0.1 . 119 26 26 TRP CA C 57.468 0.1 . 120 26 26 TRP CB C 29.704 0.1 . 121 26 26 TRP N N 129.130 0.1 . 122 27 27 GLY H H 8.063 0.01 . 123 27 27 GLY N N 109.167 0.1 . 124 28 28 ASN HA H 4.676 0.01 . 125 28 28 ASN HB2 H 2.771 0.01 . 126 28 28 ASN HB3 H 2.680 0.01 . 127 28 28 ASN C C 174.784 0.1 . 128 28 28 ASN CA C 53.186 0.1 . 129 28 28 ASN CB C 38.850 0.1 . 130 29 29 GLN H H 8.167 0.01 . 131 29 29 GLN HA H 4.549 0.01 . 132 29 29 GLN C C 173.999 0.1 . 133 29 29 GLN CA C 53.798 0.1 . 134 29 29 GLN CB C 28.980 0.1 . 135 29 29 GLN N N 120.813 0.1 . 136 31 31 ALA HA H 4.259 0.01 . 137 31 31 ALA HB H 1.375 0.01 . 138 31 31 ALA C C 178.339 0.1 . 139 31 31 ALA CA C 52.950 0.1 . 140 31 31 ALA CB C 19.288 0.1 . 141 32 32 GLY H H 8.307 0.01 . 142 32 32 GLY C C 174.038 0.1 . 143 32 32 GLY CA C 45.342 0.1 . 144 32 32 GLY N N 108.048 0.1 . 145 33 33 ALA HA H 4.324 0.01 . 146 33 33 ALA HB H 1.372 0.01 . 147 33 33 ALA C C 178.200 0.1 . 148 33 33 ALA CA C 52.716 0.1 . 149 33 33 ALA CB C 19.371 0.1 . 150 34 34 GLY H H 8.370 0.01 . 151 34 34 GLY HA2 H 3.931 0.01 . 152 34 34 GLY HA3 H 3.931 0.01 . 153 34 34 GLY C C 174.479 0.1 . 154 34 34 GLY CA C 45.447 0.1 . 155 34 34 GLY N N 107.761 0.1 . 156 35 35 GLY H H 8.087 0.01 . 157 35 35 GLY HA2 H 3.867 0.01 . 158 35 35 GLY HA3 H 3.867 0.01 . 159 35 35 GLY C C 172.792 0.1 . 160 35 35 GLY CA C 45.021 0.1 . 161 35 35 GLY N N 108.062 0.1 . 162 36 36 TYR H H 8.017 0.01 . 163 36 36 TYR HA H 4.509 0.01 . 164 36 36 TYR HB2 H 2.897 0.01 . 165 36 36 TYR HB3 H 2.822 0.01 . 166 36 36 TYR C C 174.627 0.1 . 167 36 36 TYR CA C 55.945 0.1 . 168 36 36 TYR CB C 40.203 0.1 . 169 36 36 TYR N N 121.280 0.1 . 170 37 37 PRO N N 137.750 0.1 . 171 40 40 SER HA H 4.446 0.01 . 172 40 40 SER HB2 H 3.797 0.01 . 173 40 40 SER HB3 H 3.797 0.01 . 174 40 40 SER C C 173.002 0.1 . 175 40 40 SER CA C 58.172 0.1 . 176 40 40 SER CB C 64.167 0.1 . 177 41 41 TYR H H 8.121 0.01 . 178 41 41 TYR HA H 4.514 0.01 . 179 41 41 TYR C C 174.361 0.1 . 180 41 41 TYR CA C 55.950 0.1 . 181 41 41 TYR CB C 40.329 0.1 . 182 41 41 TYR N N 123.006 0.1 . 183 46 46 PRO HA H 3.697 0.01 . 184 46 46 PRO HB2 H 1.851 0.01 . 185 46 46 PRO HB3 H 1.528 0.01 . 186 46 46 PRO C C 176.390 0.1 . 187 46 46 PRO CA C 63.357 0.1 . 188 46 46 PRO CB C 33.869 0.1 . 189 46 46 PRO CG C 24.436 0.1 . 190 47 47 GLY H H 8.365 0.01 . 191 47 47 GLY HA2 H 3.876 0.01 . 192 47 47 GLY HA3 H 3.876 0.01 . 193 47 47 GLY C C 173.448 0.1 . 194 47 47 GLY CA C 45.428 0.1 . 195 47 47 GLY N N 111.421 0.1 . 196 55 55 PRO HA H 4.356 0.01 . 197 55 55 PRO HB2 H 2.183 0.01 . 198 55 55 PRO HB3 H 1.892 0.01 . 199 55 55 PRO C C 177.249 0.1 . 200 55 55 PRO CA C 63.658 0.1 . 201 55 55 PRO CB C 31.818 0.1 . 202 55 55 PRO CG C 27.381 0.1 . 203 55 55 PRO CD C 50.433 0.1 . 204 56 56 GLY H H 8.138 0.01 . 205 56 56 GLY HA2 H 3.896 0.01 . 206 56 56 GLY HA3 H 3.896 0.01 . 207 56 56 GLY C C 173.913 0.1 . 208 56 56 GLY CA C 45.309 0.1 . 209 56 56 GLY N N 109.163 0.1 . 210 57 57 GLN HA H 4.321 0.01 . 211 57 57 GLN HB2 H 2.052 0.01 . 212 57 57 GLN HB3 H 1.890 0.01 . 213 57 57 GLN C C 175.218 0.1 . 214 57 57 GLN CA C 55.398 0.1 . 215 57 57 GLN CB C 29.928 0.1 . 216 57 57 GLN CG C 33.791 0.1 . 217 58 58 ALA H H 8.280 0.01 . 218 58 58 ALA HA H 4.502 0.01 . 219 58 58 ALA HB H 1.283 0.01 . 220 58 58 ALA C C 174.792 0.1 . 221 58 58 ALA CA C 50.421 0.1 . 222 58 58 ALA CB C 18.330 0.1 . 223 58 58 ALA N N 126.523 0.1 . 224 62 62 ALA HA H 4.231 0.01 . 225 62 62 ALA HB H 1.225 0.01 . 226 62 62 ALA C C 177.117 0.1 . 227 62 62 ALA CA C 52.502 0.1 . 228 62 62 ALA CB C 19.469 0.1 . 229 63 63 TYR H H 8.000 0.01 . 230 63 63 TYR HA H 4.486 0.01 . 231 63 63 TYR C C 175.431 0.1 . 232 63 63 TYR CA C 57.623 0.1 . 233 63 63 TYR CB C 38.891 0.1 . 234 63 63 TYR N N 118.585 0.1 . 235 65 65 GLY HA2 H 3.926 0.01 . 236 65 65 GLY HA3 H 3.926 0.01 . 237 65 65 GLY C C 173.018 0.1 . 238 65 65 GLY CA C 45.101 0.1 . 239 66 66 ALA H H 8.123 0.01 . 240 66 66 ALA HA H 4.596 0.01 . 241 66 66 ALA C C 175.546 0.1 . 242 66 66 ALA CA C 50.508 0.1 . 243 66 66 ALA CB C 18.465 0.1 . 244 66 66 ALA N N 124.627 0.1 . 245 74 74 PRO HA H 4.384 0.01 . 246 74 74 PRO HB2 H 2.201 0.01 . 247 74 74 PRO HB3 H 1.869 0.01 . 248 74 74 PRO C C 176.146 0.1 . 249 74 74 PRO CA C 62.688 0.1 . 250 74 74 PRO CB C 32.005 0.1 . 251 74 74 PRO CG C 27.319 0.1 . 252 74 74 PRO CD C 50.371 0.1 . 253 75 75 ALA H H 8.263 0.01 . 254 75 75 ALA HA H 4.531 0.01 . 255 75 75 ALA C C 175.413 0.1 . 256 75 75 ALA CA C 50.320 0.1 . 257 75 75 ALA CB C 18.322 0.1 . 258 75 75 ALA N N 125.161 0.1 . 259 77 77 GLY HA2 H 3.924 0.01 . 260 77 77 GLY HA3 H 3.926 0.01 . 261 77 77 GLY C C 173.775 0.1 . 262 77 77 GLY CA C 45.335 0.1 . 263 78 78 VAL H H 7.758 0.01 . 264 78 78 VAL HA H 4.091 0.01 . 265 78 78 VAL HB H 1.998 0.01 . 266 78 78 VAL HG1 H 0.861 0.01 . 267 78 78 VAL HG2 H 0.863 0.01 . 268 78 78 VAL C C 174.702 0.1 . 269 78 78 VAL CA C 62.266 0.1 . 270 78 78 VAL CB C 32.948 0.1 . 271 78 78 VAL CG1 C 20.778 0.1 . 272 78 78 VAL CG2 C 21.141 0.1 . 273 78 78 VAL N N 119.274 0.1 . 274 79 79 TYR H H 8.208 0.01 . 275 79 79 TYR HA H 4.562 0.01 . 276 79 79 TYR HB2 H 2.861 0.01 . 277 79 79 TYR HB3 H 2.861 0.01 . 278 79 79 TYR C C 174.366 0.1 . 279 79 79 TYR CA C 55.706 0.1 . 280 79 79 TYR CB C 40.643 0.1 . 281 79 79 TYR N N 124.608 0.1 . 282 80 80 PRO HA H 4.423 0.01 . 283 80 80 PRO HB2 H 2.144 0.01 . 284 80 80 PRO HB3 H 1.941 0.01 . 285 80 80 PRO C C 176.594 0.1 . 286 80 80 PRO CA C 63.321 0.1 . 287 80 80 PRO CB C 32.043 0.1 . 288 81 81 GLY H H 7.507 0.01 . 289 81 81 GLY HA2 H 3.996 0.01 . 290 81 81 GLY HA3 H 3.996 0.01 . 291 81 81 GLY CA C 44.347 0.1 . 292 81 81 GLY N N 108.122 0.1 . 293 84 84 SER HA H 4.470 0.01 . 294 84 84 SER HB2 H 3.877 0.01 . 295 84 84 SER HB3 H 3.877 0.01 . 296 84 84 SER C C 174.397 0.1 . 297 84 84 SER CA C 59.578 0.1 . 298 84 84 SER CB C 63.920 0.1 . 299 85 85 GLY H H 8.009 0.01 . 300 85 85 GLY C C 172.044 0.1 . 301 85 85 GLY CA C 44.514 0.1 . 302 85 85 GLY N N 110.301 0.1 . 303 88 88 ALA HA H 4.303 0.01 . 304 88 88 ALA HB H 1.301 0.01 . 305 88 88 ALA C C 176.315 0.1 . 306 88 88 ALA CA C 52.259 0.1 . 307 88 88 ALA CB C 19.663 0.1 . 308 89 89 TYR H H 8.097 0.01 . 309 89 89 TYR HA H 4.529 0.01 . 310 89 89 TYR C C 174.532 0.1 . 311 89 89 TYR CA C 55.816 0.1 . 312 89 89 TYR CB C 40.440 0.1 . 313 89 89 TYR N N 120.416 0.1 . 314 90 90 PRO N N 138.589 0.1 . 315 96 96 SER HA H 4.363 0.01 . 316 96 96 SER HB2 H 3.858 0.01 . 317 96 96 SER HB3 H 3.858 0.01 . 318 96 96 SER C C 173.775 0.1 . 319 96 96 SER CA C 58.401 0.1 . 320 96 96 SER CB C 64.128 0.1 . 321 97 97 ALA H H 8.282 0.01 . 322 97 97 ALA C C 175.382 0.1 . 323 97 97 ALA CA C 50.445 0.1 . 324 97 97 ALA N N 126.507 0.1 . 325 101 101 TYR C C 174.005 0.1 . 326 102 102 PRO N N 137.759 0.1 . 327 103 103 ALA HA H 4.354 0.01 . 328 103 103 ALA C C 177.816 0.1 . 329 103 103 ALA CA C 52.919 0.1 . 330 103 103 ALA CB C 19.222 0.1 . 331 104 104 THR H H 8.003 0.01 . 332 104 104 THR HA H 4.366 0.01 . 333 104 104 THR HB H 4.229 0.01 . 334 104 104 THR HG2 H 1.175 0.01 . 335 104 104 THR C C 174.771 0.1 . 336 104 104 THR CA C 61.408 0.1 . 337 104 104 THR CB C 70.058 0.1 . 338 104 104 THR CG2 C 21.565 0.1 . 339 104 104 THR N N 111.821 0.1 . 340 105 105 GLY H H 8.008 0.01 . 341 105 105 GLY HA2 H 3.604 0.01 . 342 105 105 GLY HA3 H 3.094 0.01 . 343 105 105 GLY C C 171.821 0.1 . 344 105 105 GLY CA C 43.930 0.1 . 345 105 105 GLY N N 110.307 0.1 . 346 108 108 GLY HA2 H 3.846 0.01 . 347 108 108 GLY HA3 H 3.846 0.01 . 348 108 108 GLY C C 173.069 0.1 . 349 108 108 GLY CA C 45.137 0.1 . 350 109 109 ALA H H 7.993 0.01 . 351 109 109 ALA HA H 4.603 0.01 . 352 109 109 ALA HB H 1.336 0.01 . 353 109 109 ALA C C 175.268 0.1 . 354 109 109 ALA CA C 50.423 0.1 . 355 109 109 ALA CB C 18.562 0.1 . 356 109 109 ALA N N 124.674 0.1 . 357 110 110 PRO HA H 4.417 0.01 . 358 110 110 PRO HB2 H 2.285 0.01 . 359 110 110 PRO HB3 H 1.955 0.01 . 360 110 110 PRO C C 176.436 0.1 . 361 110 110 PRO CA C 63.166 0.1 . 362 110 110 PRO CB C 32.051 0.1 . 363 111 111 ALA H H 8.323 0.01 . 364 111 111 ALA HA H 4.379 0.01 . 365 111 111 ALA HB H 1.407 0.01 . 366 111 111 ALA C C 177.564 0.1 . 367 111 111 ALA CA C 52.292 0.1 . 368 111 111 ALA CB C 19.774 0.1 . 369 111 111 ALA N N 124.189 0.1 . 370 112 112 GLY H H 8.112 0.01 . 371 112 112 GLY HA2 H 4.058 0.01 . 372 112 112 GLY HA3 H 3.722 0.01 . 373 112 112 GLY C C 171.929 0.1 . 374 112 112 GLY CA C 44.149 0.1 . 375 112 112 GLY N N 107.597 0.1 . 376 113 113 PRO HA H 4.653 0.01 . 377 113 113 PRO HB2 H 2.399 0.01 . 378 113 113 PRO HB3 H 2.143 0.01 . 379 113 113 PRO HG2 H 1.933 0.01 . 380 113 113 PRO HG3 H 1.860 0.01 . 381 113 113 PRO HD2 H 3.586 0.01 . 382 113 113 PRO HD3 H 3.586 0.01 . 383 113 113 PRO C C 176.163 0.1 . 384 113 113 PRO CA C 62.745 0.1 . 385 113 113 PRO CB C 34.990 0.1 . 386 113 113 PRO CG C 24.961 0.1 . 387 113 113 PRO CD C 50.678 0.1 . 388 114 114 LEU H H 8.478 0.01 . 389 114 114 LEU HA H 4.565 0.01 . 390 114 114 LEU HB2 H 1.362 0.01 . 391 114 114 LEU HG H 1.391 0.01 . 392 114 114 LEU HD1 H 0.338 0.01 . 393 114 114 LEU HD2 H 0.647 0.01 . 394 114 114 LEU C C 175.780 0.1 . 395 114 114 LEU CA C 53.953 0.1 . 396 114 114 LEU CB C 41.828 0.1 . 397 114 114 LEU CG C 27.063 0.1 . 398 114 114 LEU CD1 C 24.569 0.1 . 399 114 114 LEU CD2 C 22.520 0.1 . 400 114 114 LEU N N 122.407 0.1 . 401 115 115 ILE H H 8.173 0.01 . 402 115 115 ILE HA H 4.225 0.01 . 403 115 115 ILE HG2 H 0.934 0.01 . 404 115 115 ILE CA C 60.852 0.1 . 405 115 115 ILE CB C 38.946 0.1 . 406 115 115 ILE N N 123.152 0.1 . 407 118 118 TYR H H 9.196 0.01 . 408 118 118 TYR C C 173.843 0.1 . 409 118 118 TYR CA C 57.486 0.1 . 410 118 118 TYR N N 125.999 0.1 . 411 119 119 ASN H H 7.829 0.01 . 412 119 119 ASN HA H 5.289 0.01 . 413 119 119 ASN CA C 51.971 0.1 . 414 119 119 ASN N N 126.258 0.1 . 415 134 134 ILE C C 173.740 0.1 . 416 135 135 LEU H H 8.857 0.01 . 417 135 135 LEU N N 126.882 0.1 . 418 202 202 VAL HA H 5.264 0.01 . 419 202 202 VAL CA C 60.697 0.1 . 420 211 211 VAL HA H 5.119 0.01 . 421 211 211 VAL HG1 H 0.461 0.01 . 422 211 211 VAL HG2 H 0.837 0.01 . 423 211 211 VAL CA C 61.369 0.1 . 424 211 211 VAL CG1 C 21.268 0.1 . 425 211 211 VAL CG2 C 21.552 0.1 . 426 212 212 ALA HA H 5.003 0.01 . 427 212 212 ALA HB H 1.210 0.01 . 428 212 212 ALA CA C 50.901 0.1 . 429 212 212 ALA CB C 22.607 0.1 . 430 213 213 VAL HG2 H 0.533 0.01 . 431 213 213 VAL CG2 C 23.435 0.1 . 432 215 215 ASP HA H 3.987 0.01 . 433 215 215 ASP HB2 H 2.996 0.01 . 434 215 215 ASP HB3 H 2.851 0.01 . 435 215 215 ASP CA C 56.282 0.1 . 436 215 215 ASP CB C 39.160 0.1 . 437 216 216 ALA HA H 4.754 0.01 . 438 216 216 ALA HB H 1.346 0.01 . 439 216 216 ALA CA C 50.914 0.1 . 440 216 216 ALA CB C 21.043 0.1 . 441 219 219 LEU H H 7.688 0.01 . 442 219 219 LEU N N 110.446 0.1 . 443 242 242 LEU H H 9.153 0.01 . 444 242 242 LEU HD2 H 0.554 0.01 . 445 242 242 LEU CD2 C 27.205 0.1 . 446 242 242 LEU N N 125.750 0.1 . 447 243 243 THR H H 9.070 0.01 . 448 243 243 THR HA H 4.290 0.01 . 449 243 243 THR HB H 3.775 0.01 . 450 243 243 THR HG2 H 1.082 0.01 . 451 243 243 THR C C 174.304 0.1 . 452 243 243 THR CA C 63.916 0.1 . 453 243 243 THR CB C 69.259 0.1 . 454 243 243 THR CG2 C 22.270 0.1 . 455 243 243 THR N N 121.203 0.1 . 456 244 244 SER H H 7.712 0.01 . 457 244 244 SER C C 172.124 0.1 . 458 244 244 SER CA C 58.147 0.1 . 459 244 244 SER N N 111.348 0.1 . 460 245 245 ALA H H 8.278 0.01 . 461 245 245 ALA HA H 5.214 0.01 . 462 245 245 ALA N N 126.193 0.1 . 463 246 246 SER HA H 4.884 0.01 . 464 246 246 SER C C 171.510 0.1 . 465 246 246 SER CA C 57.460 0.1 . 466 246 246 SER CB C 65.823 0.1 . 467 247 247 TYR H H 8.320 0.01 . 468 247 247 TYR HA H 5.971 0.01 . 469 247 247 TYR N N 114.853 0.1 . 470 248 248 THR H H 8.867 0.01 . 471 248 248 THR N N 114.775 0.1 . stop_ save_ save_assigned_chem_shift_list_1_3 _Saveframe_category assigned_chemical_shifts _Details ; Estimated error limits of chemical shifts are based upon the standard error in average chemical shift position of corresponding resonance lines across different NMR spectra. Typical standard errors of the average position of resonances taken over different spectra and sample preparations are 0.005 ppm for 1H, 0.06 ppm for 13C and 0.07 ppm for 15N. Number of equivalent peak positions per assigned resonance is considered as a Figure of Merit tohave an indicator of accurate shifts. Tbis number is given in column _Atom_chem_shift.Assign_fig_of_merit of the chemical shift table. No stereospecific assignments have been carried out for the protein and prochiral methylene and methyl groups are therefore listed as unambiguously assignments. Because of the highly repetative sequence parts PGAYP that are present in the first N-terminal region of the protein (1-109), the following residues must be considered interresidue ambiguous (index type 5) and the corresponding PGAYP resonances may well be interchangeable seen in terms of a five-amino stretch. P42 = P51 G43 = G52 A44 = A52 Y45 = Y53 P46 = P54 G47 = G55 Q48 = Q57 A49 = A58 P50 = P59 P67 = P98 G68 = G99 A69 = A100 Y70 = Y101 P71 = P102 ; loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D CC(CO)NH' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D HNHA' '3D HN(CO)CA' '3D HcCH DIPSI' '3D hCCH DIPSI' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D C_CON' '2D C_CACO' '2D C_CAN' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Galectin-3, cis form, 2 (c)' _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 5 5 PHE HA H 4.604 0.01 . 2 5 5 PHE HB2 H 3.178 0.01 . 3 5 5 PHE HB3 H 3.044 0.01 . 4 5 5 PHE C C 175.808 0.1 . 5 5 5 PHE CA C 58.006 0.1 . 6 5 5 PHE CB C 39.400 0.1 . 7 6 6 SER H H 8.083 0.01 . 8 6 6 SER N N 116.853 0.1 . 9 18 18 ASN HA H 4.788 0.01 . 10 18 18 ASN CA C 50.999 0.1 . 11 18 18 ASN CB C 40.299 0.1 . 12 19 19 PRO HA H 4.290 0.01 . 13 19 19 PRO HB2 H 2.193 0.01 . 14 19 19 PRO HB3 H 1.869 0.01 . 15 19 19 PRO C C 176.975 0.1 . 16 19 19 PRO CA C 63.791 0.1 . 17 19 19 PRO CB C 32.059 0.1 . 18 20 20 GLN H H 8.260 0.01 . 19 20 20 GLN HA H 4.251 0.01 . 20 20 20 GLN CA C 56.173 0.1 . 21 20 20 GLN CB C 29.208 0.1 . 22 20 20 GLN N N 118.645 0.1 . 23 21 21 GLY H H 8.256 0.01 . 24 21 21 GLY HA2 H 3.852 0.01 . 25 21 21 GLY HA3 H 3.852 0.01 . 26 21 21 GLY C C 172.893 0.1 . 27 21 21 GLY CA C 45.101 0.1 . 28 21 21 GLY N N 109.676 0.1 . 29 22 22 TRP H H 8.006 0.01 . 30 22 22 TRP HA H 4.945 0.01 . 31 22 22 TRP HB2 H 3.258 0.01 . 32 22 22 TRP HB3 H 3.144 0.01 . 33 22 22 TRP CA C 54.914 0.1 . 34 22 22 TRP CB C 29.263 0.1 . 35 22 22 TRP N N 121.991 0.1 . 36 28 28 ASN HA H 4.623 0.01 . 37 28 28 ASN HB2 H 2.745 0.01 . 38 28 28 ASN HB3 H 2.641 0.01 . 39 28 28 ASN C C 174.249 0.1 . 40 28 28 ASN CA C 53.106 0.1 . 41 28 28 ASN CB C 39.008 0.1 . 42 29 29 GLN H H 7.996 0.01 . 43 29 29 GLN HA H 4.425 0.01 . 44 29 29 GLN C C 174.236 0.1 . 45 29 29 GLN CA C 53.304 0.1 . 46 29 29 GLN CB C 29.758 0.1 . 47 29 29 GLN N N 119.045 0.1 . 48 46 46 PRO HA H 3.707 0.01 . 49 46 46 PRO HB2 H 1.900 0.01 . 50 46 46 PRO HB3 H 1.612 0.01 . 51 46 46 PRO C C 176.465 0.1 . 52 46 46 PRO CA C 63.370 0.1 . 53 46 46 PRO CB C 33.887 0.1 . 54 46 46 PRO CG C 24.696 0.1 . 55 47 47 GLY H H 8.422 0.01 . 56 47 47 GLY HA2 H 3.884 0.01 . 57 47 47 GLY HA3 H 3.884 0.01 . 58 47 47 GLY C C 173.481 0.1 . 59 47 47 GLY CA C 45.486 0.1 . 60 47 47 GLY N N 111.050 0.1 . 61 62 62 ALA HA H 4.253 0.01 . 62 62 62 ALA HB H 1.207 0.01 . 63 62 62 ALA C C 176.980 0.1 . 64 62 62 ALA CA C 52.404 0.1 . 65 62 62 ALA CB C 19.469 0.1 . 66 63 63 TYR H H 8.063 0.01 . 67 63 63 TYR CA C 57.772 0.1 . 68 63 63 TYR CB C 38.781 0.1 . 69 63 63 TYR N N 119.207 0.1 . 70 65 65 GLY C C 172.881 0.1 . 71 65 65 GLY CA C 45.030 0.1 . 72 66 66 ALA H H 8.057 0.01 . 73 66 66 ALA C C 175.343 0.1 . 74 66 66 ALA CA C 50.504 0.1 . 75 66 66 ALA CB C 18.417 0.1 . 76 66 66 ALA N N 124.271 0.1 . 77 74 74 PRO C C 175.882 0.1 . 78 74 74 PRO CA C 62.993 0.1 . 79 74 74 PRO CB C 31.929 0.1 . 80 75 75 ALA H H 8.188 0.01 . 81 75 75 ALA HA H 4.364 0.01 . 82 75 75 ALA HB H 1.289 0.01 . 83 75 75 ALA C C 175.870 0.1 . 84 75 75 ALA CA C 50.513 0.1 . 85 75 75 ALA CB C 19.031 0.1 . 86 75 75 ALA N N 124.470 0.1 . 87 77 77 GLY HA2 H 3.844 0.01 . 88 77 77 GLY C C 173.213 0.1 . 89 77 77 GLY CA C 45.520 0.1 . 90 78 78 VAL H H 7.796 0.01 . 91 78 78 VAL HA H 4.110 0.01 . 92 78 78 VAL HB H 1.930 0.01 . 93 78 78 VAL C C 175.299 0.1 . 94 78 78 VAL CA C 61.703 0.1 . 95 78 78 VAL CB C 33.302 0.1 . 96 78 78 VAL N N 117.805 0.1 . 97 80 80 PRO HA H 4.403 0.01 . 98 80 80 PRO HB2 H 2.170 0.01 . 99 80 80 PRO HB3 H 1.923 0.01 . 100 80 80 PRO C C 176.608 0.1 . 101 80 80 PRO CA C 63.411 0.1 . 102 80 80 PRO CB C 32.030 0.1 . 103 81 81 GLY H H 7.631 0.01 . 104 81 81 GLY HA2 H 3.985 0.01 . 105 81 81 GLY HA3 H 3.985 0.01 . 106 81 81 GLY C C 171.401 0.1 . 107 81 81 GLY CA C 44.117 0.1 . 108 81 81 GLY N N 108.210 0.1 . 109 96 96 SER HA H 4.381 0.01 . 110 96 96 SER HB2 H 3.828 0.01 . 111 96 96 SER HB3 H 3.828 0.01 . 112 96 96 SER C C 173.382 0.1 . 113 96 96 SER CA C 58.197 0.1 . 114 96 96 SER CB C 64.109 0.1 . 115 97 97 ALA H H 8.137 0.01 . 116 97 97 ALA HA H 4.409 0.01 . 117 97 97 ALA HB H 1.289 0.01 . 118 97 97 ALA C C 175.796 0.1 . 119 97 97 ALA CA C 50.512 0.1 . 120 97 97 ALA CB C 19.184 0.1 . 121 97 97 ALA N N 125.567 0.1 . 122 103 103 ALA C C 177.760 0.1 . 123 103 103 ALA CA C 52.860 0.1 . 124 103 103 ALA CB C 19.273 0.1 . 125 104 104 THR H H 7.977 0.01 . 126 104 104 THR HA H 4.451 0.01 . 127 104 104 THR HB H 4.292 0.01 . 128 104 104 THR HG2 H 1.223 0.01 . 129 104 104 THR C C 175.089 0.1 . 130 104 104 THR CA C 61.437 0.1 . 131 104 104 THR CB C 70.016 0.1 . 132 104 104 THR CG2 C 21.490 0.1 . 133 104 104 THR N N 111.748 0.1 . 134 105 105 GLY H H 8.128 0.01 . 135 105 105 GLY N N 110.481 0.1 . 136 111 111 ALA HA H 4.417 0.01 . 137 111 111 ALA CA C 52.811 0.1 . 138 113 113 PRO HA H 4.586 0.01 . 139 113 113 PRO HB2 H 2.329 0.01 . 140 113 113 PRO HB3 H 2.238 0.01 . 141 113 113 PRO HG2 H 1.927 0.01 . 142 113 113 PRO HG3 H 1.837 0.01 . 143 113 113 PRO HD2 H 3.592 0.01 . 144 113 113 PRO HD3 H 3.518 0.01 . 145 113 113 PRO C C 176.801 0.1 . 146 113 113 PRO CA C 63.078 0.1 . 147 113 113 PRO CB C 34.503 0.1 . 148 113 113 PRO CG C 24.632 0.1 . 149 113 113 PRO CD C 50.361 0.1 . 150 114 114 LEU H H 8.315 0.01 . 151 114 114 LEU HA H 4.424 0.01 . 152 114 114 LEU N N 122.675 0.1 . 153 212 212 ALA HA H 5.008 0.01 . 154 212 212 ALA HB H 1.260 0.01 . 155 212 212 ALA CA C 50.961 0.1 . 156 212 212 ALA CB C 22.504 0.1 . stop_ save_ save_assigned_chem_shift_list_1_4 _Saveframe_category assigned_chemical_shifts _Details ; Estimated error limits of chemical shifts are based upon the standard error in average chemical shift position of corresponding resonance lines across different NMR spectra. Typical standard errors of the average position of resonances taken over different spectra and sample preparations are 0.005 ppm for 1H, 0.06 ppm for 13C and 0.07 ppm for 15N. Number of equivalent peak positions per assigned resonance is considered as a Figure of Merit tohave an indicator of accurate shifts. Tbis number is given in column _Atom_chem_shift.Assign_fig_of_merit of the chemical shift table. No stereospecific assignments have been carried out for the protein and prochiral methylene and methyl groups are therefore listed as unambiguously assignments. Because of the highly repetative sequence parts PGAYP that are present in the first N-terminal region of the protein (1-109), the following residues must be considered interresidue ambiguous (index type 5) and the corresponding PGAYP resonances may well be interchangeable seen in terms of a five-amino stretch. P42 = P51 G43 = G52 A44 = A52 Y45 = Y53 P46 = P54 G47 = G55 Q48 = Q57 A49 = A58 P50 = P59 P67 = P98 G68 = G99 A69 = A100 Y70 = Y101 P71 = P102 ; loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D CC(CO)NH' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D HNHA' '3D HN(CO)CA' '3D HcCH DIPSI' '3D hCCH DIPSI' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D C_CON' '2D C_CACO' '2D C_CAN' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Galectin-3, cis form, 3 (d)' _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 46 46 PRO HA H 3.712 0.01 . 2 46 46 PRO HB2 H 1.900 0.01 . 3 46 46 PRO HG2 H 1.681 0.01 . 4 46 46 PRO HG3 H 1.681 0.01 . 5 46 46 PRO HD2 H 3.470 0.01 . 6 46 46 PRO HD3 H 3.309 0.01 . 7 46 46 PRO C C 176.640 0.1 . 8 46 46 PRO CA C 63.360 0.1 . 9 46 46 PRO CB C 34.073 0.1 . 10 46 46 PRO CG C 24.648 0.1 . 11 46 46 PRO CD C 49.874 0.1 . 12 47 47 GLY H H 8.427 0.01 . 13 47 47 GLY C C 173.151 0.1 . 14 47 47 GLY CA C 45.458 0.1 . 15 47 47 GLY N N 111.066 0.1 . 16 74 74 PRO HA H 4.358 0.01 . 17 74 74 PRO C C 175.593 0.1 . 18 74 74 PRO CA C 62.759 0.1 . 19 74 74 PRO CB C 34.156 0.1 . 20 75 75 ALA H H 8.465 0.01 . 21 75 75 ALA HA H 4.555 0.01 . 22 75 75 ALA HB H 1.357 0.01 . 23 75 75 ALA C C 175.393 0.1 . 24 75 75 ALA CA C 50.802 0.1 . 25 75 75 ALA CB C 18.203 0.1 . 26 75 75 ALA N N 126.538 0.1 . 27 78 78 VAL HA H 4.047 0.01 . 28 78 78 VAL CA C 62.135 0.1 . 29 78 78 VAL CB C 32.946 0.1 . 30 79 79 TYR H H 8.326 0.01 . 31 79 79 TYR CA C 55.478 0.1 . 32 79 79 TYR CB C 38.734 0.1 . 33 79 79 TYR N N 124.957 0.1 . 34 80 80 PRO HA H 4.415 0.01 . 35 80 80 PRO HB2 H 2.176 0.01 . 36 80 80 PRO C C 176.554 0.1 . 37 80 80 PRO CA C 63.277 0.1 . 38 80 80 PRO CB C 32.067 0.1 . 39 81 81 GLY H H 7.700 0.01 . 40 81 81 GLY HA2 H 4.011 0.01 . 41 81 81 GLY HA3 H 4.011 0.01 . 42 81 81 GLY C C 171.183 0.1 . 43 81 81 GLY CA C 44.325 0.1 . 44 81 81 GLY N N 107.980 0.1 . 45 103 103 ALA CA C 52.811 0.1 . 46 103 103 ALA CB C 19.333 0.1 . 47 104 104 THR H H 7.967 0.01 . 48 104 104 THR HB H 4.295 0.01 . 49 104 104 THR HG2 H 1.236 0.01 . 50 104 104 THR C C 174.275 0.1 . 51 104 104 THR CA C 61.271 0.1 . 52 104 104 THR CB C 70.188 0.1 . 53 104 104 THR CG2 C 21.568 0.1 . 54 104 104 THR N N 111.194 0.1 . stop_ save_ save_assigned_chem_shift_list_1_5 _Saveframe_category assigned_chemical_shifts _Details ; Estimated error limits of chemical shifts are based upon the standard error in average chemical shift position of corresponding resonance lines across different NMR spectra. Typical standard errors of the average position of resonances taken over different spectra and sample preparations are 0.005 ppm for 1H, 0.06 ppm for 13C and 0.07 ppm for 15N. Number of equivalent peak positions per assigned resonance is considered as a Figure of Merit tohave an indicator of accurate shifts. Tbis number is given in column _Atom_chem_shift.Assign_fig_of_merit of the chemical shift table. No stereospecific assignments have been carried out for the protein and prochiral methylene and methyl groups are therefore listed as unambiguously assignments. Because of the highly repetative sequence parts PGAYP that are present in the first N-terminal region of the protein (1-109), the following residues must be considered interresidue ambiguous (index type 5) and the corresponding PGAYP resonances may well be interchangeable seen in terms of a five-amino stretch. P42 = P51 G43 = G52 A44 = A52 Y45 = Y53 P46 = P54 G47 = G55 Q48 = Q57 A49 = A58 P50 = P59 P67 = P98 G68 = G99 A69 = A100 Y70 = Y101 P71 = P102 ; loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D CC(CO)NH' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D HNHA' '3D HN(CO)CA' '3D HcCH DIPSI' '3D hCCH DIPSI' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D C_CON' '2D C_CACO' '2D C_CAN' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Galectin-3, cis form, 4 (e)' _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 46 46 PRO HA H 3.689 0.01 . 2 46 46 PRO HB2 H 1.890 0.01 . 3 46 46 PRO HB3 H 1.614 0.01 . 4 46 46 PRO C C 176.397 0.1 . 5 46 46 PRO CA C 63.347 0.1 . 6 46 46 PRO CB C 33.923 0.1 . 7 46 46 PRO CG C 24.669 0.1 . 8 46 46 PRO N N 137.542 0.1 . 9 47 47 GLY H H 8.367 0.01 . 10 47 47 GLY HA2 H 3.854 0.01 . 11 47 47 GLY HA3 H 3.854 0.01 . 12 47 47 GLY C C 172.905 0.1 . 13 47 47 GLY CA C 45.312 0.1 . 14 47 47 GLY N N 111.025 0.1 . 15 78 78 VAL HA H 4.043 0.01 . 16 78 78 VAL HB H 1.930 0.01 . 17 78 78 VAL C C 175.290 0.1 . 18 78 78 VAL CA C 62.123 0.1 . 19 78 78 VAL CB C 32.885 0.1 . 20 79 79 TYR H H 8.302 0.01 . 21 79 79 TYR HA H 4.797 0.01 . 22 79 79 TYR CA C 55.457 0.1 . 23 79 79 TYR CB C 38.671 0.1 . 24 79 79 TYR N N 124.888 0.1 . 25 80 80 PRO HA H 3.741 0.01 . 26 80 80 PRO HB2 H 1.920 0.01 . 27 80 80 PRO HB3 H 1.705 0.01 . 28 80 80 PRO C C 176.255 0.1 . 29 80 80 PRO CA C 63.335 0.1 . 30 80 80 PRO CB C 33.962 0.1 . 31 81 81 GLY H H 8.263 0.01 . 32 81 81 GLY HA2 H 3.992 0.01 . 33 81 81 GLY HA3 H 3.992 0.01 . 34 81 81 GLY C C 170.892 0.1 . 35 81 81 GLY CA C 44.582 0.1 . 36 81 81 GLY N N 110.263 0.1 . stop_ save_