data_4909 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectiin-3 ; _BMRB_accession_number 4909 _BMRB_flat_file_name bmr4909.str _Entry_type original _Submission_date 2000-12-05 _Accession_date 2000-12-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Umemoto Kimiko . . 2 Leffler Hakon . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 694 "13C chemical shifts" 275 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-17 original author . stop_ _Original_release_date 2001-05-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectin-3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Umemoto Kimiko . . 2 Leffler Hakon . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 20 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 91 _Page_last 92 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_galectin-3 _Saveframe_category molecular_system _Mol_system_name 'human galectin-3' _Abbreviation_common galectin-3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal fragment of galectin-3' $galectin-3C lactose $LAT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function lectin stop_ _Database_query_date . _Details ; Galectin-3C, the C-terminal fragment of galectin-3, starts from aa 108 to the terminal aa 250. ; save_ ######################## # Monomeric polymers # ######################## save_galectin-3C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common galectin-3 _Abbreviation_common galectin-3C _Molecular_mass . _Mol_thiol_state 'all free' _Details 'Galectin-3C contains the carbohydrate recignition domain of galectin-3.' ############################## # Polymer residue sequence # ############################## _Residue_count 143 _Mol_residue_sequence ; GAPAGPLIVPYNLPLPGGVV PRMLITILGTVKPNANRIAL DFQRGNDVAFHFNPRFNENN RRVIVCNTKLDNNWGREERQ SVFPFESGKPFKIQVLVEPD HFKVAVNDAHLLQYNHRVKK LNEISKLGISGDIDLTSASY TMI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 108 GLY 2 109 ALA 3 110 PRO 4 111 ALA 5 112 GLY 6 113 PRO 7 114 LEU 8 115 ILE 9 116 VAL 10 117 PRO 11 118 TYR 12 119 ASN 13 120 LEU 14 121 PRO 15 122 LEU 16 123 PRO 17 124 GLY 18 125 GLY 19 126 VAL 20 127 VAL 21 128 PRO 22 129 ARG 23 130 MET 24 131 LEU 25 132 ILE 26 133 THR 27 134 ILE 28 135 LEU 29 136 GLY 30 137 THR 31 138 VAL 32 139 LYS 33 140 PRO 34 141 ASN 35 142 ALA 36 143 ASN 37 144 ARG 38 145 ILE 39 146 ALA 40 147 LEU 41 148 ASP 42 149 PHE 43 150 GLN 44 151 ARG 45 152 GLY 46 153 ASN 47 154 ASP 48 155 VAL 49 156 ALA 50 157 PHE 51 158 HIS 52 159 PHE 53 160 ASN 54 161 PRO 55 162 ARG 56 163 PHE 57 164 ASN 58 165 GLU 59 166 ASN 60 167 ASN 61 168 ARG 62 169 ARG 63 170 VAL 64 171 ILE 65 172 VAL 66 173 CYS 67 174 ASN 68 175 THR 69 176 LYS 70 177 LEU 71 178 ASP 72 179 ASN 73 180 ASN 74 181 TRP 75 182 GLY 76 183 ARG 77 184 GLU 78 185 GLU 79 186 ARG 80 187 GLN 81 188 SER 82 189 VAL 83 190 PHE 84 191 PRO 85 192 PHE 86 193 GLU 87 194 SER 88 195 GLY 89 196 LYS 90 197 PRO 91 198 PHE 92 199 LYS 93 200 ILE 94 201 GLN 95 202 VAL 96 203 LEU 97 204 VAL 98 205 GLU 99 206 PRO 100 207 ASP 101 208 HIS 102 209 PHE 103 210 LYS 104 211 VAL 105 212 ALA 106 213 VAL 107 214 ASN 108 215 ASP 109 216 ALA 110 217 HIS 111 218 LEU 112 219 LEU 113 220 GLN 114 221 TYR 115 222 ASN 116 223 HIS 117 224 ARG 118 225 VAL 119 226 LYS 120 227 LYS 121 228 LEU 122 229 ASN 123 230 GLU 124 231 ILE 125 232 SER 126 233 LYS 127 234 LEU 128 235 GLY 129 236 ILE 130 237 SER 131 238 GLY 132 239 ASP 133 240 ILE 134 241 ASP 135 242 LEU 136 243 THR 137 244 SER 138 245 ALA 139 246 SER 140 247 TYR 141 248 THR 142 249 MET 143 250 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15705 Galectin-3-LBT 95.80 155 99.27 99.27 2.01e-93 BMRB 19491 Galectin-3 100.00 250 100.00 100.00 6.89e-99 BMRB 7422 Galectin-3-LBT 95.80 155 99.27 99.27 2.01e-93 PDB 1A3K "X-Ray Crystal Structure Of The Human Galectin-3 Carbohydrate Recognition Domain (Crd) At 2.1 Angstrom Resolution" 95.80 137 100.00 100.00 1.65e-94 PDB 1KJL "High Resolution X-Ray Structure Of Human Galectin-3 In Complex With Lacnac" 100.00 146 100.00 100.00 4.52e-99 PDB 1KJR "Crystal Structure Of The Human Galectin-3 Crd In Complex With A 3'- Derivative Of N-Acetyllactosamine" 100.00 146 100.00 100.00 4.52e-99 PDB 2NMN "Crystal Structure Of Human Galectin-3 Carbohydrate- Recognising Domain At 2.45 Angstrom Resolution" 96.50 138 100.00 100.00 2.55e-95 PDB 2NMO "Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain At 1.35 Angstrom Resolution" 96.50 138 100.00 100.00 2.55e-95 PDB 2NN8 "Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain With Lactose Bound, At 1.35 Angstrom Resolution" 96.50 138 100.00 100.00 2.55e-95 PDB 2XG3 "Human Galectin-3 In Complex With A Benzamido-N- Acetyllactoseamine Inhibitor" 95.80 138 100.00 100.00 1.28e-94 PDB 3AYA "Crystal Structure Of Galectin-3 Crd Domian Complexed With Thomsen- Friedenreich Antigen" 94.41 135 99.26 100.00 7.45e-93 PDB 3AYC "Crystal Structure Of Galectin-3 Crd Domian Complexed With Gm1 Pentasaccharide" 94.41 135 99.26 100.00 7.45e-93 PDB 3AYD "Crystal Structure Of Galectin-3 Crd Domian Complexed With Tfn" 94.41 135 99.26 100.00 7.45e-93 PDB 3AYE "Crystal Structure Of Galectin-3 Crd Domian Complexed With Lactose" 94.41 135 99.26 100.00 7.45e-93 PDB 3T1L "Crystal Structure Of Human Galectin-3 In Complex With Methyl 2-o- Acetyl-3-o-toluoyl-beta-d-talopyranoside" 100.00 143 100.00 100.00 2.37e-99 PDB 3T1M "Crystal Structure Of Human Galectin-3 Carbohydrate Recognition Domain In Complex With Methyl 3-deoxy-2-o-toluoyl-3-n-toluoyl-be" 100.00 143 100.00 100.00 2.37e-99 PDB 3ZSJ "Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose At 0.86 Angstrom Resolution" 96.50 138 100.00 100.00 2.55e-95 PDB 3ZSK "Crystal Structure Of Human Galectin-3 Crd With Glycerol Bound At 0.90 Angstrom Resolution" 95.80 138 100.00 100.00 1.23e-94 PDB 3ZSL "Crystal Structure Of Apo Human Galectin-3 Crd At 1.08 Angstrom Resolution, At Cryogenic Temperature" 95.80 138 100.00 100.00 1.23e-94 PDB 3ZSM "Crystal Structure Of Apo Human Galectin-3 Crd At 1.25 Angstrom Resolution, At Room Temperature" 95.80 138 100.00 100.00 1.23e-94 PDB 4BLI "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 1" 95.80 138 100.00 100.00 1.23e-94 PDB 4BLJ "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 2" 95.80 138 100.00 100.00 1.23e-94 PDB 4BM8 "Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 3" 95.80 138 100.00 100.00 1.28e-94 PDB 4JC1 "Galectin-3 Carbohydrate Recognition Domain In Complex With Thiodigalactoside" 100.00 143 100.00 100.00 2.37e-99 PDB 4JCK "Galectin-3 Carbohydrate Recognition Domain In Complex With Thioditaloside" 100.00 143 100.00 100.00 2.37e-99 PDB 4LBJ "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnt" 95.80 138 99.27 99.27 1.42e-93 PDB 4LBK "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnnt" 95.80 138 99.27 99.27 1.42e-93 PDB 4LBL "Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With A-gm3" 95.80 138 99.27 99.27 1.42e-93 PDB 4LBM "Crystal Structure Of Human Galectin-3 Crd In Complex With Lnt" 97.20 139 100.00 100.00 3.72e-96 PDB 4LBN "Crystal Structure Of Human Galectin-3 Crd In Complex With Lnnt" 97.20 139 100.00 100.00 3.72e-96 PDB 4LBO "Crystal Structure Of Human Galectin-3 Crd In Complex With A-gm3" 96.50 138 100.00 100.00 2.55e-95 DBJ BAA22164 "galectin-3 [Homo sapiens]" 100.00 250 100.00 100.00 5.30e-99 DBJ BAD92628 "LGALS3 protein variant [Homo sapiens]" 100.00 258 100.00 100.00 1.31e-98 DBJ BAG37435 "unnamed protein product [Homo sapiens]" 100.00 250 100.00 100.00 6.89e-99 DBJ BAI46476 "lectin, galactoside-binding, soluble, 3 [synthetic construct]" 100.00 250 100.00 100.00 5.30e-99 EMBL CAD61918 "unnamed protein product [Homo sapiens]" 84.62 121 100.00 100.00 1.75e-82 EMBL CAG33178 "LGALS3 [Homo sapiens]" 100.00 250 100.00 100.00 5.30e-99 EMBL CAG46894 "LGALS3 [Homo sapiens]" 100.00 250 99.30 99.30 3.81e-98 GB AAA35607 "IgE-binding protein [Homo sapiens]" 100.00 250 100.00 100.00 6.89e-99 GB AAA36163 "laminin-binding protein [Homo sapiens]" 100.00 250 100.00 100.00 6.89e-99 GB AAA88086 "galactose-specific lectin [Homo sapiens]" 100.00 250 100.00 100.00 4.45e-99 GB AAB26229 "carbohydrate binding protein 35 [Homo sapiens]" 100.00 250 100.00 100.00 5.30e-99 GB AAB86584 "galectin 3 [Homo sapiens]" 100.00 250 100.00 100.00 5.30e-99 REF NP_002297 "galectin-3 isoform 1 [Homo sapiens]" 100.00 250 100.00 100.00 5.30e-99 REF XP_001148424 "PREDICTED: galectin-3 [Pan troglodytes]" 100.00 250 98.60 99.30 1.43e-97 REF XP_002824813 "PREDICTED: galectin-3 [Pongo abelii]" 100.00 250 100.00 100.00 4.55e-99 REF XP_003831735 "PREDICTED: galectin-3 [Pan paniscus]" 100.00 250 98.60 99.30 8.26e-98 REF XP_004055252 "PREDICTED: galectin-3 isoform 1 [Gorilla gorilla gorilla]" 100.00 250 99.30 99.30 4.84e-98 SP P17931 "RecName: Full=Galectin-3; Short=Gal-3; AltName: Full=35 kDa lectin; AltName: Full=Carbohydrate-binding protein 35; Short=CBP 35" 100.00 250 100.00 100.00 5.30e-99 stop_ save_ ############# # Ligands # ############# save_LAT _Saveframe_category ligand _Mol_type "non-polymer (saccharide)" _Name_common "LAT (BETA-LACTOSE)" _BMRB_code . _PDB_code LAT _Molecular_mass 342.296 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 16 10:39:17 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? C3' C3' C . 0 . ? C4' C4' C . 0 . ? C5' C5' C . 0 . ? C6' C6' C . 0 . ? O1' O1' O . 0 . ? O2' O2' O . 0 . ? O3' O3' O . 0 . ? O5' O5' O . 0 . ? O6' O6' O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HO2 HO2 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 0 . ? H1' H1' H . 0 . ? H2' H2' H . 0 . ? H3' H3' H . 0 . ? H4' H4' H . 0 . ? H5' H5' H . 0 . ? H6'1 H6'1 H . 0 . ? H6'2 H6'2 H . 0 . ? HO1' HO1' H . 0 . ? HO2' HO2' H . 0 . ? HO3' HO3' H . 0 . ? HO6' HO6' H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 O2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING O1 C4' ? ? SING O2 HO2 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? SING C1' C2' ? ? SING C1' O1' ? ? SING C1' O5' ? ? SING C1' H1' ? ? SING C2' C3' ? ? SING C2' O2' ? ? SING C2' H2' ? ? SING C3' C4' ? ? SING C3' O3' ? ? SING C3' H3' ? ? SING C4' C5' ? ? SING C4' H4' ? ? SING C5' C6' ? ? SING C5' O5' ? ? SING C5' H5' ? ? SING C6' O6' ? ? SING C6' H6'1 ? ? SING C6' H6'2 ? ? SING O1' HO1' ? ? SING O2' HO2' ? ? SING O3' HO3' ? ? SING O6' HO6' ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $galectin-3C human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $galectin-3C 'recombinant technology' 'E. coli' Escherichia coli K12-BL21-DE3 pET3C stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $galectin-3C 0.5 mM '[U-99% 13C; U-99% 15N]' $LAT 10 mM . 'potassium phosphate' 5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HCC-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCC-TOCSY _Sample_label $sample_1 save_ save_CN-NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name CN-NOESY-HSQC _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CN-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'C-terminal fragment of galectin-3' _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 ALA H H 8.01 0.02 1 2 . 2 ALA HA H 4.27 0.02 1 3 . 2 ALA HB H 0.19 0.02 1 4 . 2 ALA CA C 56.32 0.05 1 5 . 2 ALA CB C 18.00 0.05 1 6 . 2 ALA N N 119.51 0.05 1 7 . 3 PRO HA H 4.53 0.02 1 8 . 3 PRO HB2 H 2.39 0.02 2 9 . 3 PRO HB3 H 2.05 0.02 2 10 . 3 PRO HG2 H 2.12 0.02 2 11 . 3 PRO HD2 H 3.91 0.02 2 12 . 3 PRO HD3 H 3.74 0.02 2 13 . 3 PRO CA C 62.98 0.05 1 14 . 3 PRO CB C 31.59 0.05 1 15 . 4 ALA H H 8.43 0.02 1 16 . 4 ALA HA H 4.45 0.02 1 17 . 4 ALA HB H 1.49 0.02 1 18 . 4 ALA CA C 52.04 0.05 1 19 . 4 ALA CB C 19.70 0.05 1 20 . 4 ALA N N 124.92 0.05 1 21 . 5 GLY H H 8.17 0.02 1 22 . 5 GLY HA2 H 4.22 0.02 2 23 . 5 GLY HA3 H 4.08 0.02 2 24 . 5 GLY CA C 44.43 0.05 1 25 . 5 GLY N N 108.82 0.05 1 26 . 6 PRO HA H 4.53 0.02 1 27 . 6 PRO HB2 H 2.33 0.02 2 28 . 6 PRO HB3 H 2.05 0.02 2 29 . 6 PRO HD2 H 3.70 0.02 2 30 . 6 PRO HD3 H 2.82 0.02 2 31 . 6 PRO CA C 62.50 0.05 1 32 . 6 PRO CB C 32.06 0.05 1 33 . 7 LEU H H 8.30 0.02 1 34 . 7 LEU HA H 4.47 0.02 1 35 . 7 LEU HB2 H 1.44 0.02 2 36 . 7 LEU HB3 H 1.10 0.02 2 37 . 7 LEU HG H 1.52 0.02 1 38 . 7 LEU HD1 H 0.67 0.02 2 39 . 7 LEU HD2 H 0.49 0.02 2 40 . 7 LEU CA C 53.94 0.05 1 41 . 7 LEU CB C 41.10 0.05 1 42 . 7 LEU N N 122.45 0.05 1 43 . 8 ILE H H 8.11 0.02 1 44 . 8 ILE HA H 4.23 0.02 1 45 . 8 ILE HB H 1.95 0.02 1 46 . 8 ILE HG12 H 1.62 0.02 2 47 . 8 ILE HG13 H 1.36 0.02 2 48 . 8 ILE HG2 H 1.01 0.02 4 49 . 8 ILE CA C 60.60 0.05 1 50 . 8 ILE CB C 38.72 0.05 1 51 . 8 ILE N N 123.51 0.05 1 52 . 9 VAL H H 7.92 0.02 1 53 . 9 VAL HA H 4.52 0.02 1 54 . 9 VAL HB H 2.25 0.02 1 55 . 9 VAL HG1 H 1.12 0.02 2 56 . 9 VAL CA C 58.70 0.05 1 57 . 9 VAL CB C 33.96 0.05 1 58 . 9 VAL N N 121.76 0.05 1 59 . 10 PRO HA H 5.04 0.02 1 60 . 10 PRO HB2 H 2.41 0.02 2 61 . 10 PRO HB3 H 2.13 0.02 2 62 . 10 PRO HG2 H 2.01 0.02 2 63 . 10 PRO CA C 62.98 0.05 1 64 . 10 PRO CB C 34.44 0.05 1 65 . 11 TYR H H 9.23 0.02 1 66 . 11 TYR HA H 4.88 0.02 1 67 . 11 TYR HB2 H 3.51 0.02 2 68 . 11 TYR HB3 H 2.62 0.02 2 69 . 11 TYR CA C 57.27 0.05 1 70 . 11 TYR CB C 42.52 0.05 1 71 . 11 TYR N N 126.51 0.05 1 72 . 12 ASN H H 7.89 0.02 1 73 . 12 ASN HA H 5.32 0.02 1 74 . 12 ASN HB2 H 2.47 0.02 2 75 . 12 ASN HB3 H 2.26 0.02 2 76 . 12 ASN HD21 H 7.37 0.02 2 77 . 12 ASN HD22 H 6.58 0.02 2 78 . 12 ASN CA C 51.56 0.05 1 79 . 12 ASN CB C 41.10 0.05 1 80 . 12 ASN N N 126.60 0.05 1 81 . 13 LEU H H 9.39 0.02 1 82 . 13 LEU HA H 4.97 0.02 1 83 . 13 LEU HB2 H 2.31 0.02 2 84 . 13 LEU HB3 H 1.28 0.02 2 85 . 13 LEU HG H 1.85 0.02 1 86 . 13 LEU HD1 H 0.91 0.02 2 87 . 13 LEU CA C 51.09 0.05 1 88 . 13 LEU CB C 44.43 0.05 1 89 . 13 LEU N N 128.38 0.05 1 90 . 14 PRO HA H 4.47 0.02 1 91 . 14 PRO HB2 H 2.49 0.02 2 92 . 14 PRO HB3 H 1.99 0.02 2 93 . 14 PRO HG2 H 2.27 0.02 2 94 . 14 PRO HD2 H 3.92 0.02 2 95 . 14 PRO HD3 H 4.30 0.02 2 96 . 14 PRO CA C 62.98 0.05 1 97 . 14 PRO CB C 32.54 0.05 1 98 . 15 LEU H H 7.86 0.02 1 99 . 15 LEU HA H 4.83 0.02 1 100 . 15 LEU HB2 H 1.66 0.02 2 101 . 15 LEU HB3 H 1.45 0.02 2 102 . 15 LEU HG H 0.95 0.02 1 103 . 15 LEU HD1 H 0.79 0.02 2 104 . 15 LEU HD2 H 0.59 0.02 2 105 . 15 LEU CA C 50.61 0.05 1 106 . 15 LEU CB C 40.62 0.05 1 107 . 15 LEU N N 122.79 0.05 1 108 . 16 PRO HA H 4.38 0.02 1 109 . 16 PRO HB2 H 2.35 0.02 2 110 . 16 PRO HB3 H 2.05 0.02 2 111 . 16 PRO HG2 H 2.22 0.02 2 112 . 16 PRO HG3 H 1.82 0.02 2 113 . 16 PRO HD2 H 3.56 0.02 2 114 . 16 PRO HD3 H 3.87 0.02 2 115 . 16 PRO CA C 64.40 0.05 1 116 . 16 PRO CB C 31.11 0.05 1 117 . 17 GLY H H 8.84 0.02 1 118 . 17 GLY HA2 H 3.98 0.02 2 119 . 17 GLY HA3 H 4.01 0.02 2 120 . 17 GLY CA C 44.90 0.05 1 121 . 17 GLY N N 113.30 0.05 1 122 . 18 GLY H H 8.27 0.02 1 123 . 18 GLY HA2 H 4.18 0.02 2 124 . 18 GLY HA3 H 4.10 0.02 2 125 . 18 GLY CA C 43.95 0.05 1 126 . 18 GLY N N 109.20 0.05 1 127 . 19 VAL H H 7.20 0.02 1 128 . 19 VAL HA H 4.39 0.02 1 129 . 19 VAL HB H 2.30 0.02 1 130 . 19 VAL HG1 H 1.07 0.02 2 131 . 19 VAL CA C 61.07 0.05 1 132 . 19 VAL CB C 32.54 0.05 1 133 . 19 VAL N N 113.89 0.05 1 134 . 20 VAL H H 6.58 0.02 1 135 . 20 VAL HA H 4.71 0.02 1 136 . 20 VAL HB H 2.06 0.02 1 137 . 20 VAL HG1 H 0.98 0.02 2 138 . 20 VAL HG2 H 0.89 0.02 2 139 . 20 VAL CA C 56.79 0.05 1 140 . 20 VAL CB C 34.91 0.05 1 141 . 20 VAL CG1 C 117.16 0.05 2 142 . 21 PRO HA H 4.01 0.02 1 143 . 21 PRO HB2 H 1.91 0.02 2 144 . 21 PRO HG2 H 1.58 0.02 2 145 . 21 PRO HG3 H 1.41 0.02 2 146 . 21 PRO HD2 H 2.70 0.02 2 147 . 21 PRO CA C 62.98 0.05 1 148 . 21 PRO CB C 31.11 0.05 1 149 . 22 ARG H H 8.81 0.02 1 150 . 22 ARG HA H 4.60 0.02 1 151 . 22 ARG HB2 H 1.78 0.02 2 152 . 22 ARG HB3 H 1.64 0.02 2 153 . 22 ARG HD3 H 3.22 0.02 2 154 . 22 ARG CA C 59.17 0.05 1 155 . 22 ARG CB C 26.83 0.05 1 156 . 22 ARG N N 112.97 0.05 1 157 . 23 MET H H 7.94 0.02 1 158 . 23 MET HA H 5.01 0.02 1 159 . 23 MET HB2 H 2.52 0.02 2 160 . 23 MET HB3 H 2.35 0.02 2 161 . 23 MET CA C 56.79 0.05 1 162 . 23 MET CB C 36.34 0.05 1 163 . 23 MET N N 119.54 0.05 1 164 . 24 LEU H H 9.23 0.02 1 165 . 24 LEU HA H 5.55 0.02 1 166 . 24 LEU HB2 H 1.98 0.02 2 167 . 24 LEU HB3 H 1.30 0.02 2 168 . 24 LEU HG H 0.88 0.02 1 169 . 24 LEU HD1 H 0.54 0.02 2 170 . 24 LEU CA C 52.99 0.05 1 171 . 24 LEU CB C 45.38 0.05 1 172 . 24 LEU N N 128.84 0.05 1 173 . 25 ILE H H 9.94 0.02 1 174 . 25 ILE HA H 5.03 0.02 1 175 . 25 ILE HB H 2.06 0.02 1 176 . 25 ILE HG12 H 1.83 0.02 2 177 . 25 ILE HG13 H 1.55 0.02 2 178 . 25 ILE HG2 H 1.01 0.02 4 179 . 25 ILE HD1 H 0.85 0.02 4 180 . 25 ILE CA C 60.60 0.05 1 181 . 25 ILE CB C 40.62 0.05 1 182 . 25 ILE N N 132.54 0.05 1 183 . 26 THR H H 9.14 0.02 1 184 . 26 THR HA H 5.28 0.02 1 185 . 26 THR HB H 3.88 0.02 1 186 . 26 THR HG2 H 1.16 0.02 1 187 . 26 THR CA C 62.50 0.05 1 188 . 26 THR CB C 69.63 0.05 1 189 . 26 THR N N 124.01 0.05 1 190 . 27 ILE H H 9.69 0.02 1 191 . 27 ILE HA H 4.94 0.02 1 192 . 27 ILE HB H 2.03 0.02 1 193 . 27 ILE HG12 H 1.06 0.02 2 194 . 27 ILE CA C 59.65 0.05 1 195 . 27 ILE CB C 41.10 0.05 1 196 . 27 ILE N N 130.20 0.05 1 197 . 28 LEU H H 8.94 0.02 1 198 . 28 LEU HA H 5.10 0.02 1 199 . 28 LEU HB2 H 1.63 0.02 2 200 . 28 LEU HB3 H 1.50 0.02 2 201 . 28 LEU HD1 H 0.90 0.02 2 202 . 28 LEU HD2 H 0.98 0.02 2 203 . 28 LEU CA C 52.51 0.05 1 204 . 28 LEU CB C 44.43 0.05 1 205 . 28 LEU N N 127.40 0.05 1 206 . 29 GLY H H 7.00 0.02 1 207 . 29 GLY HA2 H 4.23 0.02 2 208 . 29 GLY HA3 H 4.02 0.02 2 209 . 29 GLY CA C 45.97 0.05 1 210 . 29 GLY N N 108.82 0.05 1 211 . 30 THR H H 8.93 0.02 1 212 . 30 THR HA H 4.81 0.02 1 213 . 30 THR HB H 3.87 0.02 1 214 . 30 THR HG2 H 1.04 0.02 1 215 . 30 THR CA C 61.55 0.05 1 216 . 30 THR CB C 71.06 0.05 1 217 . 30 THR N N 115.97 0.05 1 218 . 31 VAL H H 8.40 0.02 1 219 . 31 VAL HA H 4.13 0.02 1 220 . 31 VAL HB H 2.63 0.02 1 221 . 31 VAL HG1 H 1.34 0.02 2 222 . 31 VAL HG2 H 1.12 0.02 2 223 . 31 VAL CA C 63.45 0.05 1 224 . 31 VAL CB C 31.59 0.05 1 225 . 31 VAL N N 128.40 0.05 1 226 . 32 LYS H H 8.33 0.02 1 227 . 32 LYS HA H 4.42 0.02 1 228 . 32 LYS HB2 H 1.88 0.02 2 229 . 32 LYS HB3 H 1.29 0.02 2 230 . 32 LYS HG2 H 1.34 0.02 2 231 . 32 LYS HG3 H 1.18 0.02 2 232 . 32 LYS HD2 H 1.67 0.02 2 233 . 32 LYS HD3 H 1.50 0.02 2 234 . 32 LYS HE2 H 2.95 0.02 2 235 . 32 LYS CA C 55.84 0.05 1 236 . 32 LYS CB C 31.59 0.05 1 237 . 32 LYS N N 129.12 0.05 1 238 . 33 PRO HA H 4.18 0.02 1 239 . 33 PRO HB2 H 2.30 0.02 2 240 . 33 PRO HB3 H 1.80 0.02 2 241 . 33 PRO HG2 H 1.25 0.02 2 242 . 33 PRO CA C 63.45 0.05 1 243 . 33 PRO CB C 31.59 0.05 1 244 . 34 ASN H H 8.44 0.02 1 245 . 34 ASN HA H 4.44 0.02 1 246 . 34 ASN HB2 H 2.80 0.02 2 247 . 34 ASN HB3 H 2.74 0.02 2 248 . 34 ASN CA C 52.99 0.05 1 249 . 34 ASN CB C 36.82 0.05 1 250 . 34 ASN N N 116.07 0.05 1 251 . 35 ALA H H 6.93 0.02 1 252 . 35 ALA HA H 3.65 0.02 1 253 . 35 ALA HB H 0.62 0.02 1 254 . 35 ALA CA C 52.99 0.05 1 255 . 35 ALA CB C 20.17 0.05 1 256 . 35 ALA N N 119.85 0.05 1 257 . 36 ASN H H 9.64 0.02 1 258 . 36 ASN HA H 4.96 0.02 1 259 . 36 ASN HB2 H 2.84 0.02 2 260 . 36 ASN HB3 H 2.72 0.02 2 261 . 36 ASN HD21 H 7.78 0.02 2 262 . 36 ASN HD22 H 7.03 0.02 2 263 . 36 ASN CA C 54.89 0.05 1 264 . 36 ASN CB C 41.57 0.05 1 265 . 36 ASN N N 116.90 0.05 1 266 . 37 ARG H H 8.60 0.02 1 267 . 37 ARG HA H 5.57 0.02 1 268 . 37 ARG HB2 H 2.04 0.02 2 269 . 37 ARG HB3 H 1.62 0.02 2 270 . 37 ARG HG2 H 1.73 0.02 2 271 . 37 ARG HG3 H 1.38 0.02 2 272 . 37 ARG HD2 H 3.32 0.02 2 273 . 37 ARG HD3 H 3.16 0.02 2 274 . 37 ARG CA C 54.89 0.05 1 275 . 37 ARG CB C 33.49 0.05 1 276 . 37 ARG N N 118.00 0.05 1 277 . 38 ILE H H 8.22 0.02 1 278 . 38 ILE HA H 4.24 0.02 1 279 . 38 ILE HB H 1.92 0.02 1 280 . 38 ILE HG12 H 1.04 0.02 2 281 . 38 ILE HG2 H 0.79 0.02 4 282 . 38 ILE HD1 H 0.56 0.02 4 283 . 38 ILE CA C 60.60 0.05 1 284 . 38 ILE CB C 42.52 0.05 1 285 . 38 ILE N N 120.23 0.05 1 286 . 39 ALA H H 8.76 0.02 1 287 . 39 ALA HA H 5.24 0.02 1 288 . 39 ALA HB H 1.15 0.02 1 289 . 39 ALA CA C 52.04 0.05 1 290 . 39 ALA CB C 21.12 0.05 1 291 . 39 ALA N N 127.43 0.05 1 292 . 40 LEU H H 8.55 0.02 1 293 . 40 LEU HA H 5.12 0.02 1 294 . 40 LEU HB2 H 1.67 0.02 2 295 . 40 LEU HB3 H 1.56 0.02 2 296 . 40 LEU HG H 1.32 0.02 1 297 . 40 LEU HD1 H 0.82 0.02 2 298 . 40 LEU HD2 H 0.74 0.02 2 299 . 40 LEU CA C 52.99 0.05 1 300 . 40 LEU CB C 43.95 0.05 1 301 . 40 LEU N N 122.26 0.05 1 302 . 41 ASP H H 9.09 0.02 1 303 . 41 ASP HA H 5.52 0.02 1 304 . 41 ASP HB2 H 2.54 0.02 2 305 . 41 ASP HB3 H 2.38 0.02 2 306 . 41 ASP CA C 53.50 0.05 1 307 . 41 ASP CB C 43.50 0.05 1 308 . 41 ASP N N 121.50 0.05 1 309 . 42 PHE H H 9.36 0.02 1 310 . 42 PHE HA H 4.86 0.02 1 311 . 42 PHE HB2 H 3.40 0.02 2 312 . 42 PHE HB3 H 3.03 0.02 2 313 . 42 PHE CA C 58.22 0.05 1 314 . 42 PHE CB C 38.24 0.05 1 315 . 42 PHE N N 125.75 0.05 1 316 . 43 GLN H H 9.19 0.02 1 317 . 43 GLN HA H 4.76 0.02 1 318 . 43 GLN HB2 H 2.34 0.02 2 319 . 43 GLN HB3 H 2.06 0.02 2 320 . 43 GLN HE21 H 7.02 0.02 2 321 . 43 GLN HE22 H 6.43 0.02 2 322 . 43 GLN CA C 56.79 0.05 1 323 . 43 GLN CB C 31.59 0.05 1 324 . 43 GLN N N 127.58 0.05 1 325 . 44 ARG H H 8.23 0.02 1 326 . 44 ARG HA H 4.44 0.02 1 327 . 44 ARG HG2 H 1.48 0.02 2 328 . 44 ARG CA C 53.94 0.05 1 329 . 44 ARG CB C 31.59 0.05 1 330 . 44 ARG N N 125.82 0.05 1 331 . 45 GLY H H 8.16 0.02 1 332 . 45 GLY HA2 H 4.08 0.02 2 333 . 45 GLY HA3 H 3.70 0.02 2 334 . 45 GLY CA C 47.50 0.05 1 335 . 45 GLY N N 108.00 0.05 1 336 . 46 ASN HA H 4.73 0.02 1 337 . 46 ASN HB2 H 2.94 0.02 2 338 . 46 ASN HB3 H 2.67 0.02 2 339 . 46 ASN HD21 H 7.65 0.02 2 340 . 46 ASN HD22 H 6.95 0.02 2 341 . 46 ASN CA C 53.46 0.05 1 342 . 46 ASN CB C 38.72 0.05 1 343 . 47 ASP H H 8.51 0.02 1 344 . 47 ASP HA H 4.73 0.02 1 345 . 47 ASP HB2 H 3.16 0.02 2 346 . 47 ASP CA C 53.46 0.05 1 347 . 47 ASP CB C 42.05 0.05 1 348 . 47 ASP N N 120.34 0.05 1 349 . 48 VAL H H 9.26 0.02 1 350 . 48 VAL HA H 4.48 0.02 1 351 . 48 VAL HB H 1.90 0.02 1 352 . 48 VAL HG1 H 1.28 0.02 2 353 . 48 VAL HG2 H 0.86 0.02 2 354 . 48 VAL CA C 61.55 0.05 1 355 . 48 VAL CB C 32.54 0.05 1 356 . 48 VAL N N 121.48 0.05 1 357 . 49 ALA H H 8.93 0.02 1 358 . 49 ALA HA H 4.26 0.02 1 359 . 49 ALA HB H 1.60 0.02 1 360 . 49 ALA CA C 54.89 0.05 1 361 . 49 ALA CB C 19.72 0.05 1 362 . 49 ALA N N 127.97 0.05 1 363 . 50 PHE H H 7.70 0.02 1 364 . 50 PHE HA H 5.16 0.02 1 365 . 50 PHE HB2 H 3.21 0.02 2 366 . 50 PHE HB3 H 2.25 0.02 2 367 . 50 PHE CA C 55.84 0.05 1 368 . 50 PHE CB C 40.15 0.05 1 369 . 50 PHE N N 118.89 0.05 1 370 . 51 HIS H H 9.41 0.02 1 371 . 51 HIS HA H 5.50 0.02 1 372 . 51 HIS HB2 H 3.31 0.02 2 373 . 51 HIS HB3 H 3.13 0.02 2 374 . 51 HIS CA C 53.94 0.05 1 375 . 51 HIS CB C 31.59 0.05 1 376 . 51 HIS N N 133.91 0.05 1 377 . 52 PHE H H 8.45 0.02 1 378 . 52 PHE HA H 4.70 0.02 1 379 . 52 PHE HB2 H 2.57 0.02 2 380 . 52 PHE HB3 H 2.19 0.02 2 381 . 52 PHE CA C 55.37 0.05 1 382 . 52 PHE CB C 40.62 0.05 1 383 . 52 PHE N N 127.33 0.05 1 384 . 53 ASN H H 8.40 0.02 1 385 . 53 ASN HA H 5.30 0.02 1 386 . 53 ASN HB2 H 2.75 0.02 2 387 . 53 ASN HB3 H 1.76 0.02 2 388 . 53 ASN HD21 H 7.52 0.02 2 389 . 53 ASN HD22 H 6.02 0.02 2 390 . 53 ASN CA C 49.66 0.05 1 391 . 53 ASN CB C 41.10 0.05 1 392 . 53 ASN N N 123.66 0.05 1 393 . 54 PRO HA H 4.32 0.02 1 394 . 54 PRO HB2 H 1.85 0.02 2 395 . 54 PRO HB3 H 1.41 0.02 2 396 . 54 PRO CA C 63.45 0.05 1 397 . 54 PRO CB C 31.11 0.05 1 398 . 55 ARG H H 9.36 0.02 1 399 . 55 ARG HA H 4.80 0.02 1 400 . 55 ARG HB2 H 1.78 0.02 2 401 . 55 ARG HB3 H 1.64 0.02 2 402 . 55 ARG HD2 H 3.22 0.02 2 403 . 55 ARG CA C 55.37 0.05 1 404 . 55 ARG CB C 31.11 0.05 1 405 . 55 ARG N N 126.60 0.05 1 406 . 56 PHE H H 8.17 0.02 1 407 . 56 PHE HA H 3.75 0.02 1 408 . 56 PHE HB2 H 3.05 0.02 2 409 . 56 PHE HB3 H 3.02 0.02 2 410 . 56 PHE CA C 59.65 0.05 1 411 . 56 PHE CB C 39.20 0.05 1 412 . 56 PHE N N 119.20 0.05 1 413 . 57 ASN H H 8.71 0.02 1 414 . 57 ASN HA H 4.52 0.02 1 415 . 57 ASN HB2 H 2.93 0.02 2 416 . 57 ASN HB3 H 2.70 0.02 2 417 . 57 ASN HD21 H 7.47 0.02 2 418 . 57 ASN HD22 H 6.72 0.02 2 419 . 57 ASN CA C 52.51 0.05 1 420 . 57 ASN CB C 38.24 0.05 1 421 . 57 ASN N N 117.89 0.05 1 422 . 58 GLU H H 8.98 0.02 1 423 . 58 GLU HA H 4.60 0.02 1 424 . 58 GLU HB2 H 2.12 0.02 2 425 . 58 GLU HB3 H 1.95 0.02 2 426 . 58 GLU CA C 54.41 0.05 1 427 . 58 GLU CB C 29.94 0.05 1 428 . 58 GLU N N 125.99 0.05 1 429 . 59 ASN HA H 4.35 0.02 1 430 . 59 ASN HB2 H 3.05 0.02 2 431 . 59 ASN HB3 H 2.73 0.02 2 432 . 59 ASN HD21 H 7.58 0.02 2 433 . 59 ASN HD22 H 6.84 0.02 2 434 . 59 ASN CA C 54.41 0.05 1 435 . 59 ASN CB C 37.29 0.05 1 436 . 60 ASN H H 8.09 0.02 1 437 . 60 ASN HA H 4.38 0.02 1 438 . 60 ASN HB2 H 3.10 0.02 2 439 . 60 ASN HB3 H 3.02 0.02 2 440 . 60 ASN HD21 H 7.49 0.02 2 441 . 60 ASN HD22 H 6.86 0.02 2 442 . 60 ASN CA C 54.80 0.05 1 443 . 60 ASN CB C 37.00 0.05 1 444 . 60 ASN N N 108.60 0.05 1 445 . 61 ARG H H 7.47 0.02 1 446 . 61 ARG HA H 4.60 0.02 1 447 . 61 ARG HB2 H 1.78 0.02 2 448 . 61 ARG HB3 H 1.75 0.02 2 449 . 61 ARG HG2 H 1.65 0.02 2 450 . 61 ARG HD2 H 3.22 0.02 2 451 . 61 ARG HD3 H 3.20 0.02 2 452 . 61 ARG CA C 53.94 0.05 1 453 . 61 ARG CB C 33.01 0.05 1 454 . 61 ARG N N 117.75 0.05 1 455 . 62 ARG H H 7.90 0.02 1 456 . 62 ARG HA H 4.50 0.02 1 457 . 62 ARG HB2 H 1.60 0.02 2 458 . 62 ARG HG2 H 0.93 0.02 2 459 . 62 ARG HG3 H -0.51 0.02 2 460 . 62 ARG HD2 H 2.92 0.02 2 461 . 62 ARG HD3 H 2.78 0.02 2 462 . 62 ARG CA C 53.94 0.05 1 463 . 62 ARG CB C 28.26 0.05 1 464 . 62 ARG N N 119.46 0.05 1 465 . 63 VAL H H 8.57 0.02 1 466 . 63 VAL HA H 4.66 0.02 1 467 . 63 VAL HB H 1.99 0.02 1 468 . 63 VAL HG1 H 0.90 0.02 2 469 . 63 VAL HG2 H 0.78 0.02 2 470 . 63 VAL CA C 60.12 0.05 1 471 . 63 VAL CB C 35.39 0.05 1 472 . 63 VAL N N 122.12 0.05 1 473 . 64 ILE H H 8.79 0.02 1 474 . 64 ILE HA H 4.29 0.02 1 475 . 64 ILE HB H 1.84 0.02 1 476 . 64 ILE HG2 H 0.20 0.02 4 477 . 64 ILE HD1 H 0.87 0.02 4 478 . 64 ILE CA C 60.60 0.05 1 479 . 64 ILE CB C 38.72 0.05 1 480 . 64 ILE N N 124.94 0.05 1 481 . 65 VAL H H 7.42 0.02 1 482 . 65 VAL HA H 4.35 0.02 1 483 . 65 VAL HB H 2.00 0.02 1 484 . 65 VAL HG1 H 0.87 0.02 2 485 . 65 VAL HG2 H 0.75 0.02 2 486 . 65 VAL CA C 62.02 0.05 1 487 . 65 VAL CB C 33.49 0.05 1 488 . 65 VAL N N 128.43 0.05 1 489 . 66 CYS H H 8.85 0.02 1 490 . 66 CYS HA H 6.15 0.02 1 491 . 66 CYS HB2 H 3.32 0.02 2 492 . 66 CYS HB3 H 3.11 0.02 2 493 . 66 CYS CA C 55.37 0.05 1 494 . 66 CYS CB C 32.06 0.05 1 495 . 66 CYS N N 124.01 0.05 1 496 . 67 ASN H H 9.02 0.02 1 497 . 67 ASN HA H 5.65 0.02 1 498 . 67 ASN HB2 H 3.01 0.02 2 499 . 67 ASN HD21 H 8.64 0.02 2 500 . 67 ASN HD22 H 7.72 0.02 2 501 . 67 ASN CA C 52.04 0.05 1 502 . 67 ASN CB C 42.52 0.05 1 503 . 67 ASN N N 119.52 0.05 1 504 . 68 THR H H 10.06 0.02 1 505 . 68 THR HA H 4.82 0.02 1 506 . 68 THR HB H 4.30 0.02 1 507 . 68 THR HG2 H 1.52 0.02 1 508 . 68 THR CA C 62.02 0.05 1 509 . 68 THR CB C 87.45 0.05 1 510 . 68 THR N N 118.73 0.05 1 511 . 69 LYS H H 9.14 0.02 1 512 . 69 LYS HA H 4.38 0.02 1 513 . 69 LYS HB2 H 2.33 0.02 2 514 . 69 LYS HG2 H 0.82 0.02 2 515 . 69 LYS HG3 H 0.55 0.02 2 516 . 69 LYS HE2 H 3.02 0.02 2 517 . 69 LYS HE3 H 3.11 0.02 2 518 . 69 LYS CA C 54.41 0.05 1 519 . 69 LYS CB C 33.01 0.05 1 520 . 69 LYS N N 130.81 0.05 1 521 . 70 LEU H H 7.96 0.02 1 522 . 70 LEU HA H 4.68 0.02 1 523 . 70 LEU HB2 H 1.59 0.02 2 524 . 70 LEU HB3 H 1.41 0.02 2 525 . 70 LEU HG H 1.47 0.02 1 526 . 70 LEU HD1 H 0.88 0.02 2 527 . 70 LEU HD2 H 0.80 0.02 2 528 . 70 LEU CA C 52.51 0.05 1 529 . 70 LEU CB C 44.43 0.05 1 530 . 70 LEU N N 126.63 0.05 1 531 . 71 ASP H H 9.05 0.02 1 532 . 71 ASP HA H 4.22 0.02 1 533 . 71 ASP HB2 H 2.92 0.02 2 534 . 71 ASP HB3 H 2.53 0.02 2 535 . 71 ASP CA C 55.37 0.05 1 536 . 71 ASP CB C 39.20 0.05 1 537 . 71 ASP N N 126.40 0.05 1 538 . 72 ASN H H 9.18 0.02 1 539 . 72 ASN HA H 3.80 0.02 1 540 . 72 ASN HB2 H 3.05 0.02 2 541 . 72 ASN HB3 H 2.90 0.02 2 542 . 72 ASN HD21 H 7.51 0.02 2 543 . 72 ASN HD22 H 6.85 0.02 2 544 . 72 ASN CA C 54.41 0.05 1 545 . 72 ASN CB C 38.24 0.05 1 546 . 72 ASN N N 109.00 0.05 1 547 . 73 ASN H H 7.83 0.02 1 548 . 73 ASN HA H 5.09 0.02 1 549 . 73 ASN HB2 H 2.75 0.02 2 550 . 73 ASN HB3 H 2.72 0.02 2 551 . 73 ASN HD21 H 7.44 0.02 2 552 . 73 ASN HD22 H 6.90 0.02 2 553 . 73 ASN CA C 52.04 0.05 1 554 . 73 ASN CB C 41.10 0.05 1 555 . 73 ASN N N 118.06 0.05 1 556 . 74 TRP H H 8.92 0.02 1 557 . 74 TRP HA H 4.87 0.02 1 558 . 74 TRP HB2 H 3.46 0.02 2 559 . 74 TRP HB3 H 3.14 0.02 2 560 . 74 TRP CA C 57.27 0.05 1 561 . 74 TRP CB C 29.68 0.05 1 562 . 74 TRP N N 127.34 0.05 1 563 . 75 GLY H H 8.25 0.02 1 564 . 75 GLY HA2 H 4.64 0.02 2 565 . 75 GLY HA3 H 3.96 0.02 2 566 . 75 GLY CA C 44.43 0.05 1 567 . 75 GLY N N 110.85 0.05 1 568 . 76 ARG H H 8.66 0.02 1 569 . 76 ARG HA H 4.46 0.02 1 570 . 76 ARG HB2 H 1.93 0.02 2 571 . 76 ARG HB3 H 1.76 0.02 2 572 . 76 ARG HG2 H 1.82 0.02 2 573 . 76 ARG HD2 H 3.36 0.02 2 574 . 76 ARG HD3 H 3.40 0.02 2 575 . 76 ARG CA C 55.84 0.05 1 576 . 76 ARG CB C 30.16 0.05 1 577 . 76 ARG N N 124.72 0.05 1 578 . 77 GLU H H 8.83 0.02 1 579 . 77 GLU HA H 4.41 0.02 1 580 . 77 GLU HB2 H 2.20 0.02 2 581 . 77 GLU CA C 57.27 0.05 1 582 . 77 GLU CB C 30.63 0.05 1 583 . 77 GLU N N 125.89 0.05 1 584 . 78 GLU H H 9.20 0.02 1 585 . 78 GLU HA H 4.83 0.02 1 586 . 78 GLU HB2 H 2.30 0.02 2 587 . 78 GLU HB3 H 2.05 0.02 2 588 . 78 GLU HG2 H 2.40 0.02 2 589 . 78 GLU CA C 55.37 0.05 1 590 . 78 GLU CB C 30.63 0.05 1 591 . 78 GLU N N 122.93 0.05 1 592 . 79 ARG H H 8.93 0.02 1 593 . 79 ARG HA H 4.58 0.02 1 594 . 79 ARG HB2 H 1.69 0.02 2 595 . 79 ARG HB3 H 1.65 0.02 2 596 . 79 ARG HG2 H 1.56 0.02 2 597 . 79 ARG HG3 H 0.51 0.02 2 598 . 79 ARG HD2 H 3.27 0.02 2 599 . 79 ARG HD3 H 3.12 0.02 2 600 . 79 ARG CA C 55.00 0.05 1 601 . 79 ARG CB C 33.49 0.05 1 602 . 79 ARG N N 124.87 0.05 1 603 . 80 GLN H H 8.88 0.02 1 604 . 80 GLN HA H 5.48 0.02 1 605 . 80 GLN HB2 H 2.17 0.02 2 606 . 80 GLN HB3 H 2.06 0.02 2 607 . 80 GLN HG2 H 2.82 0.02 2 608 . 80 GLN HG3 H 2.63 0.02 2 609 . 80 GLN HE21 H 7.43 0.02 2 610 . 80 GLN HE22 H 7.11 0.02 2 611 . 80 GLN CA C 53.94 0.05 1 612 . 80 GLN CB C 32.54 0.05 1 613 . 80 GLN N N 121.84 0.05 1 614 . 81 SER HA H 4.70 0.02 1 615 . 81 SER HB2 H 4.06 0.02 2 616 . 81 SER HB3 H 4.04 0.02 2 617 . 81 SER CA C 59.17 0.05 1 618 . 81 SER CB C 63.93 0.05 1 619 . 82 VAL H H 7.86 0.02 1 620 . 82 VAL HA H 3.86 0.02 1 621 . 82 VAL HB H 1.92 0.02 1 622 . 82 VAL HG1 H 1.07 0.02 2 623 . 82 VAL HG2 H 0.89 0.02 2 624 . 82 VAL CA C 64.40 0.05 1 625 . 82 VAL CB C 31.11 0.05 1 626 . 82 VAL N N 125.65 0.05 1 627 . 83 PHE H H 8.37 0.02 1 628 . 83 PHE HA H 4.89 0.02 1 629 . 83 PHE HB2 H 3.42 0.02 2 630 . 83 PHE HB3 H 2.42 0.02 2 631 . 83 PHE CA C 55.84 0.05 1 632 . 83 PHE CB C 41.10 0.05 1 633 . 83 PHE N N 125.89 0.05 1 634 . 84 PRO HA H 4.64 0.02 1 635 . 84 PRO HB2 H 2.03 0.02 2 636 . 84 PRO HB3 H 1.63 0.02 2 637 . 84 PRO HG2 H 0.79 0.02 2 638 . 84 PRO HD2 H 3.45 0.02 2 639 . 84 PRO HD3 H 2.90 0.02 2 640 . 84 PRO CA C 62.50 0.05 1 641 . 84 PRO CB C 31.11 0.05 1 642 . 85 PHE H H 5.87 0.02 1 643 . 85 PHE HA H 4.46 0.02 1 644 . 85 PHE HB2 H 2.96 0.02 2 645 . 85 PHE HB3 H 2.32 0.02 2 646 . 85 PHE CA C 57.27 0.05 1 647 . 85 PHE CB C 41.57 0.05 1 648 . 85 PHE N N 114.20 0.05 1 649 . 86 GLU H H 9.20 0.02 1 650 . 86 GLU HA H 4.93 0.02 1 651 . 86 GLU HB2 H 2.61 0.02 2 652 . 86 GLU HB3 H 2.43 0.02 2 653 . 86 GLU CA C 54.89 0.05 1 654 . 86 GLU CB C 33.49 0.05 1 655 . 86 GLU N N 120.45 0.05 1 656 . 87 SER H H 9.10 0.02 1 657 . 87 SER HA H 3.95 0.02 1 658 . 87 SER HB2 H 3.97 0.02 2 659 . 87 SER CA C 60.60 0.05 1 660 . 87 SER CB C 62.98 0.05 1 661 . 87 SER N N 120.85 0.05 1 662 . 88 GLY H H 7.19 0.02 1 663 . 88 GLY HA2 H 4.26 0.02 2 664 . 88 GLY HA3 H 3.77 0.02 2 665 . 88 GLY CA C 45.38 0.05 1 666 . 88 GLY N N 112.89 0.05 1 667 . 89 LYS H H 7.80 0.02 1 668 . 89 LYS HA H 5.15 0.02 1 669 . 89 LYS HB2 H 2.12 0.02 2 670 . 89 LYS HB3 H 2.02 0.02 2 671 . 89 LYS HG2 H 1.42 0.02 2 672 . 89 LYS HD2 H 1.71 0.02 2 673 . 89 LYS HD3 H 1.80 0.02 2 674 . 89 LYS HE2 H 3.10 0.02 2 675 . 89 LYS CA C 52.99 0.05 1 676 . 89 LYS CB C 33.01 0.05 1 677 . 89 LYS N N 118.50 0.05 1 678 . 90 PRO HA H 5.26 0.02 1 679 . 90 PRO HB2 H 2.40 0.02 2 680 . 90 PRO HB3 H 1.99 0.02 2 681 . 90 PRO HG2 H 2.11 0.02 2 682 . 90 PRO HG3 H 3.81 0.02 2 683 . 90 PRO HD2 H 3.81 0.02 2 684 . 90 PRO HD3 H 4.06 0.02 2 685 . 90 PRO CA C 62.50 0.05 1 686 . 90 PRO CB C 33.01 0.05 1 687 . 91 PHE H H 8.79 0.02 1 688 . 91 PHE HA H 5.56 0.02 1 689 . 91 PHE HB2 H 3.37 0.02 2 690 . 91 PHE HB3 H 2.98 0.02 2 691 . 91 PHE CA C 55.84 0.05 1 692 . 91 PHE CB C 43.00 0.05 1 693 . 91 PHE N N 116.65 0.05 1 694 . 92 LYS H H 8.16 0.02 1 695 . 92 LYS HA H 5.25 0.02 1 696 . 92 LYS HB2 H 1.78 0.02 2 697 . 92 LYS HG2 H 1.33 0.02 2 698 . 92 LYS HG3 H 1.20 0.02 2 699 . 92 LYS HD2 H 1.70 0.02 2 700 . 92 LYS HD3 H 1.62 0.02 2 701 . 92 LYS CA C 54.89 0.05 1 702 . 92 LYS CB C 36.34 0.05 1 703 . 92 LYS N N 122.03 0.05 1 704 . 93 ILE H H 9.88 0.02 1 705 . 93 ILE HA H 4.96 0.02 1 706 . 93 ILE HB H 1.86 0.02 1 707 . 93 ILE HG2 H 0.71 0.02 4 708 . 93 ILE CA C 60.12 0.05 1 709 . 93 ILE CB C 41.57 0.05 1 710 . 93 ILE N N 127.72 0.05 1 711 . 94 GLN H H 9.36 0.02 1 712 . 94 GLN HA H 5.82 0.02 1 713 . 94 GLN HB2 H 2.61 0.02 2 714 . 94 GLN HB3 H 2.12 0.02 2 715 . 94 GLN HE21 H 7.83 0.02 2 716 . 94 GLN HE22 H 7.21 0.02 2 717 . 94 GLN CA C 53.94 0.05 1 718 . 94 GLN CB C 33.01 0.05 1 719 . 94 GLN N N 125.63 0.05 1 720 . 95 VAL H H 9.63 0.02 1 721 . 95 VAL HA H 5.09 0.02 1 722 . 95 VAL HB H 2.33 0.02 1 723 . 95 VAL HG1 H 1.13 0.02 2 724 . 95 VAL HG2 H 0.89 0.02 2 725 . 95 VAL CA C 60.60 0.05 1 726 . 95 VAL CB C 33.49 0.05 1 727 . 95 VAL N N 124.54 0.05 1 728 . 96 LEU H H 9.51 0.02 1 729 . 96 LEU HA H 5.47 0.02 1 730 . 96 LEU HB2 H 1.99 0.02 2 731 . 96 LEU HB3 H 1.48 0.02 2 732 . 96 LEU HD1 H 0.94 0.02 2 733 . 96 LEU HD2 H 0.47 0.02 2 734 . 96 LEU CA C 52.99 0.05 1 735 . 96 LEU CB C 44.90 0.05 1 736 . 96 LEU N N 130.91 0.05 1 737 . 97 VAL H H 9.08 0.02 1 738 . 97 VAL HA H 3.97 0.02 1 739 . 97 VAL HB H 2.54 0.02 1 740 . 97 VAL HG1 H 1.10 0.02 2 741 . 97 VAL HG2 H 0.49 0.02 2 742 . 97 VAL CA C 62.98 0.05 1 743 . 97 VAL CB C 30.68 0.05 1 744 . 97 VAL N N 127.87 0.05 1 745 . 98 GLU H H 8.41 0.02 1 746 . 98 GLU HA H 5.10 0.02 1 747 . 98 GLU HB2 H 2.05 0.02 2 748 . 98 GLU HB3 H 2.10 0.02 2 749 . 98 GLU CA C 53.94 0.05 1 750 . 98 GLU CB C 28.73 0.05 1 751 . 98 GLU N N 128.62 0.05 1 752 . 99 PRO HA H 4.72 0.02 1 753 . 99 PRO HB2 H 2.48 0.02 2 754 . 99 PRO HB3 H 2.20 0.02 2 755 . 99 PRO HG2 H 1.16 0.02 2 756 . 99 PRO HG3 H 2.02 0.02 2 757 . 99 PRO HD2 H 3.90 0.02 2 758 . 99 PRO CA C 65.83 0.05 1 759 . 99 PRO CB C 31.59 0.05 1 760 . 100 ASP H H 8.03 0.02 1 761 . 100 ASP HA H 5.00 0.02 1 762 . 100 ASP HB2 H 2.69 0.02 2 763 . 100 ASP HB3 H 2.65 0.02 2 764 . 100 ASP CA C 53.46 0.05 1 765 . 100 ASP CB C 41.57 0.05 1 766 . 100 ASP N N 107.50 0.05 1 767 . 101 HIS H H 6.56 0.02 1 768 . 101 HIS HA H 4.08 0.02 1 769 . 101 HIS HB2 H 3.35 0.02 2 770 . 101 HIS HB3 H 2.50 0.02 2 771 . 101 HIS CA C 54.41 0.05 1 772 . 101 HIS CB C 31.59 0.05 1 773 . 101 HIS N N 116.40 0.05 1 774 . 102 PHE H H 8.63 0.02 1 775 . 102 PHE HA H 5.02 0.02 1 776 . 102 PHE HB2 H 2.58 0.02 2 777 . 102 PHE HB3 H 2.41 0.02 2 778 . 102 PHE CA C 57.27 0.05 1 779 . 102 PHE CB C 41.10 0.05 1 780 . 102 PHE N N 115.17 0.05 1 781 . 103 LYS H H 9.77 0.02 1 782 . 103 LYS HA H 5.03 0.02 1 783 . 103 LYS HB2 H 2.23 0.02 2 784 . 103 LYS HB3 H 2.06 0.02 2 785 . 103 LYS HG2 H 1.22 0.02 4 786 . 103 LYS HG3 H 0.98 0.02 4 787 . 103 LYS HD2 H 1.83 0.02 4 788 . 103 LYS HD3 H 1.55 0.02 4 789 . 103 LYS CA C 56.32 0.05 1 790 . 103 LYS CB C 35.87 0.05 1 791 . 103 LYS N N 124.06 0.05 1 792 . 104 VAL H H 9.15 0.02 1 793 . 104 VAL HA H 5.05 0.02 1 794 . 104 VAL HB H 1.91 0.02 1 795 . 104 VAL HG1 H 0.85 0.02 2 796 . 104 VAL HG2 H 0.51 0.02 2 797 . 104 VAL CA C 61.07 0.05 1 798 . 104 VAL CB C 33.96 0.05 1 799 . 104 VAL N N 124.07 0.05 1 800 . 105 ALA H H 9.32 0.02 1 801 . 105 ALA HA H 5.06 0.02 1 802 . 105 ALA HB H 1.34 0.02 1 803 . 105 ALA CA C 50.61 0.05 1 804 . 105 ALA CB C 22.07 0.05 1 805 . 105 ALA N N 130.91 0.05 1 806 . 106 VAL H H 8.55 0.02 1 807 . 106 VAL HA H 5.16 0.02 1 808 . 106 VAL HB H 1.69 0.02 1 809 . 106 VAL HG1 H 0.80 0.02 2 810 . 106 VAL HG2 H 0.36 0.02 2 811 . 106 VAL CA C 60.12 0.05 1 812 . 106 VAL CB C 33.96 0.05 1 813 . 106 VAL N N 121.49 0.05 1 814 . 107 ASN H H 9.93 0.02 1 815 . 107 ASN HA H 4.38 0.02 1 816 . 107 ASN HB2 H 3.02 0.02 2 817 . 107 ASN HD21 H 7.67 0.02 2 818 . 107 ASN HD22 H 6.83 0.02 2 819 . 107 ASN CA C 54.41 0.05 1 820 . 107 ASN CB C 35.87 0.05 1 821 . 107 ASN N N 127.73 0.05 1 822 . 108 ASP H H 8.99 0.02 1 823 . 108 ASP HA H 4.14 0.02 1 824 . 108 ASP HB2 H 3.06 0.02 2 825 . 108 ASP HB3 H 2.93 0.02 2 826 . 108 ASP CA C 56.32 0.05 1 827 . 108 ASP CB C 38.72 0.05 1 828 . 108 ASP N N 108.27 0.05 1 829 . 109 ALA H H 7.74 0.02 1 830 . 109 ALA HA H 4.82 0.02 1 831 . 109 ALA HB H 1.40 0.02 1 832 . 109 ALA CA C 50.61 0.05 1 833 . 109 ALA CB C 21.12 0.05 1 834 . 109 ALA N N 122.06 0.05 1 835 . 110 HIS HA H 3.12 0.02 1 836 . 110 HIS HB2 H 2.96 0.02 2 837 . 110 HIS CA C 59.65 0.05 1 838 . 110 HIS CB C 30.63 0.05 1 839 . 111 LEU H H 8.93 0.02 1 840 . 111 LEU HA H 4.62 0.02 1 841 . 111 LEU HB2 H 1.66 0.02 2 842 . 111 LEU HB3 H 1.35 0.02 2 843 . 111 LEU HD1 H 0.93 0.02 2 844 . 111 LEU HD2 H 0.55 0.02 2 845 . 111 LEU CA C 55.37 0.05 1 846 . 111 LEU CB C 44.90 0.05 1 847 . 111 LEU N N 128.37 0.05 1 848 . 112 LEU H H 7.60 0.02 1 849 . 112 LEU HA H 4.73 0.02 1 850 . 112 LEU HB2 H 2.11 0.02 2 851 . 112 LEU HB3 H 1.83 0.02 2 852 . 112 LEU HG H 1.62 0.02 1 853 . 112 LEU HD1 H 1.04 0.02 2 854 . 112 LEU CA C 54.41 0.05 1 855 . 112 LEU CB C 43.00 0.05 1 856 . 112 LEU N N 110.52 0.05 1 857 . 113 GLN H H 8.78 0.02 1 858 . 113 GLN HA H 5.45 0.02 1 859 . 113 GLN HB2 H 2.20 0.02 2 860 . 113 GLN HB3 H 2.12 0.02 2 861 . 113 GLN HG2 H 2.93 0.02 2 862 . 113 GLN HG3 H 2.69 0.02 2 863 . 113 GLN HE21 H 6.88 0.02 2 864 . 113 GLN CA C 53.46 0.05 1 865 . 113 GLN CB C 32.54 0.05 1 866 . 113 GLN N N 119.52 0.05 1 867 . 114 TYR H H 8.99 0.02 1 868 . 114 TYR HA H 4.80 0.02 1 869 . 114 TYR HB2 H 2.24 0.02 2 870 . 114 TYR HB3 H 1.79 0.02 2 871 . 114 TYR CA C 56.79 0.05 1 872 . 114 TYR CB C 41.57 0.05 1 873 . 114 TYR N N 126.05 0.05 1 874 . 115 ASN H H 9.31 0.02 1 875 . 115 ASN HA H 4.56 0.02 1 876 . 115 ASN HB2 H 2.68 0.02 2 877 . 115 ASN HB3 H 2.65 0.02 2 878 . 115 ASN HD21 H 7.36 0.02 2 879 . 115 ASN HD22 H 6.80 0.02 2 880 . 115 ASN CA C 52.99 0.05 1 881 . 115 ASN CB C 37.29 0.05 1 882 . 115 ASN N N 130.12 0.05 1 883 . 116 HIS H H 7.18 0.02 1 884 . 116 HIS HA H 4.63 0.02 1 885 . 116 HIS HB2 H 2.71 0.02 2 886 . 116 HIS HB3 H 2.22 0.02 2 887 . 116 HIS CA C 57.27 0.05 1 888 . 116 HIS CB C 30.63 0.05 1 889 . 116 HIS N N 117.60 0.05 1 890 . 117 ARG H H 9.48 0.02 1 891 . 117 ARG HA H 4.56 0.02 1 892 . 117 ARG HB2 H 2.14 0.02 2 893 . 117 ARG HB3 H 1.70 0.02 2 894 . 117 ARG HD2 H 2.00 0.02 4 895 . 117 ARG HD3 H 3.41 0.02 2 896 . 117 ARG CA C 57.00 0.05 1 897 . 117 ARG CB C 31.00 0.05 1 898 . 117 ARG N N 125.62 0.05 1 899 . 118 VAL H H 8.38 0.02 1 900 . 118 VAL HA H 4.14 0.02 1 901 . 118 VAL HB H 2.12 0.02 1 902 . 118 VAL HG1 H 1.08 0.02 2 903 . 118 VAL HG2 H 0.92 0.02 2 904 . 118 VAL CA C 61.55 0.05 1 905 . 118 VAL CB C 32.54 0.05 1 906 . 118 VAL N N 120.77 0.05 1 907 . 119 LYS HA H 4.08 0.02 1 908 . 119 LYS HB2 H 2.00 0.02 2 909 . 119 LYS HB3 H 1.69 0.02 2 910 . 119 LYS HG2 H 1.66 0.02 2 911 . 119 LYS HG3 H 1.44 0.02 4 912 . 119 LYS HD2 H 1.35 0.02 4 913 . 119 LYS HE2 H 3.08 0.02 2 914 . 119 LYS CA C 56.32 0.05 1 915 . 119 LYS CB C 32.06 0.05 1 916 . 120 LYS H H 7.12 0.02 1 917 . 120 LYS HA H 4.53 0.02 1 918 . 120 LYS HB2 H 2.03 0.02 2 919 . 120 LYS HB3 H 1.80 0.02 2 920 . 120 LYS HG2 H 1.60 0.02 4 921 . 120 LYS HG3 H 1.41 0.02 4 922 . 120 LYS HE2 H 2.96 0.02 2 923 . 120 LYS HE3 H 3.08 0.02 2 924 . 120 LYS CA C 53.94 0.05 1 925 . 120 LYS CB C 29.68 0.05 1 926 . 120 LYS N N 121.30 0.05 1 927 . 121 LEU H H 7.69 0.02 1 928 . 121 LEU HA H 3.60 0.02 1 929 . 121 LEU HB2 H 1.60 0.02 2 930 . 121 LEU HB3 H 1.40 0.02 2 931 . 121 LEU HD1 H 0.36 0.02 2 932 . 121 LEU CA C 57.74 0.05 1 933 . 121 LEU CB C 40.15 0.05 1 934 . 121 LEU N N 123.14 0.05 1 935 . 122 ASN H H 8.45 0.02 1 936 . 122 ASN HA H 4.65 0.02 1 937 . 122 ASN HB2 H 2.94 0.02 2 938 . 122 ASN HB3 H 2.80 0.02 2 939 . 122 ASN HD21 H 7.56 0.02 2 940 . 122 ASN HD22 H 7.05 0.02 2 941 . 122 ASN CA C 54.89 0.05 1 942 . 122 ASN CB C 36.82 0.05 1 943 . 122 ASN N N 113.20 0.05 1 944 . 123 GLU H H 7.48 0.02 1 945 . 123 GLU HA H 4.30 0.02 1 946 . 123 GLU HB2 H 2.30 0.02 2 947 . 123 GLU HB3 H 1.92 0.02 2 948 . 123 GLU HG2 H 2.20 0.02 2 949 . 123 GLU CA C 55.84 0.05 1 950 . 123 GLU CB C 30.16 0.05 1 951 . 123 GLU N N 116.76 0.05 1 952 . 124 ILE H H 7.72 0.02 1 953 . 124 ILE HA H 4.50 0.02 1 954 . 124 ILE HB H 2.37 0.02 1 955 . 124 ILE HG12 H 1.17 0.02 2 956 . 124 ILE HG2 H 1.01 0.02 4 957 . 124 ILE CA C 61.07 0.05 1 958 . 124 ILE CB C 36.34 0.05 1 959 . 124 ILE N N 122.49 0.05 1 960 . 125 SER H H 7.78 0.02 1 961 . 125 SER HA H 4.99 0.02 1 962 . 125 SER HB2 H 4.24 0.02 2 963 . 125 SER HB3 H 3.74 0.02 2 964 . 125 SER CA C 58.22 0.05 1 965 . 125 SER CB C 64.88 0.05 1 966 . 125 SER N N 116.70 0.05 1 967 . 126 LYS H H 7.92 0.02 1 968 . 126 LYS HA H 4.89 0.02 1 969 . 126 LYS HB2 H 1.92 0.02 2 970 . 126 LYS HB3 H 1.71 0.02 2 971 . 126 LYS HG2 H 1.29 0.02 4 972 . 126 LYS HD2 H 1.56 0.02 4 973 . 126 LYS HE2 H 2.89 0.02 2 974 . 126 LYS CA C 55.84 0.05 1 975 . 126 LYS CB C 36.34 0.05 1 976 . 126 LYS N N 121.13 0.05 1 977 . 127 LEU H H 8.65 0.02 1 978 . 127 LEU HA H 4.93 0.02 1 979 . 127 LEU HB2 H 1.86 0.02 2 980 . 127 LEU HB3 H 1.16 0.02 2 981 . 127 LEU HD1 H 0.89 0.02 2 982 . 127 LEU HD2 H 0.65 0.02 2 983 . 127 LEU CA C 52.51 0.05 1 984 . 127 LEU CB C 43.48 0.05 1 985 . 127 LEU N N 125.04 0.05 1 986 . 128 GLY H H 9.35 0.02 1 987 . 128 GLY HA2 H 5.13 0.02 2 988 . 128 GLY HA3 H 3.56 0.02 2 989 . 128 GLY CA C 44.90 0.05 1 990 . 128 GLY N N 114.83 0.05 1 991 . 129 ILE H H 9.39 0.02 1 992 . 129 ILE HA H 4.85 0.02 1 993 . 129 ILE HB H 2.03 0.02 1 994 . 129 ILE HG12 H 1.70 0.02 2 995 . 129 ILE HG2 H 0.97 0.02 4 996 . 129 ILE HD1 H 0.88 0.02 4 997 . 129 ILE CA C 61.12 0.05 1 998 . 129 ILE CB C 40.15 0.05 1 999 . 129 ILE N N 127.66 0.05 1 1000 . 130 SER H H 9.41 0.02 1 1001 . 130 SER HA H 4.85 0.02 1 1002 . 130 SER HB2 H 4.00 0.02 2 1003 . 130 SER HB3 H 3.97 0.02 2 1004 . 130 SER CA C 57.27 0.05 1 1005 . 130 SER CB C 66.30 0.05 1 1006 . 130 SER N N 120.70 0.05 1 1007 . 131 GLY H H 8.84 0.02 1 1008 . 131 GLY HA2 H 4.61 0.02 2 1009 . 131 GLY HA3 H 3.74 0.02 2 1010 . 131 GLY CA C 43.00 0.05 1 1011 . 131 GLY N N 106.01 0.05 1 1012 . 132 ASP H H 8.63 0.02 1 1013 . 132 ASP HA H 4.80 0.02 1 1014 . 132 ASP HB2 H 2.70 0.02 2 1015 . 132 ASP HB3 H 2.52 0.02 2 1016 . 132 ASP CA C 53.94 0.05 1 1017 . 132 ASP CB C 40.62 0.05 1 1018 . 132 ASP N N 122.15 0.05 1 1019 . 133 ILE H H 7.92 0.02 1 1020 . 133 ILE HA H 5.17 0.02 1 1021 . 133 ILE HB H 1.93 0.02 1 1022 . 133 ILE HG12 H 1.15 0.02 2 1023 . 133 ILE HG2 H 0.81 0.02 4 1024 . 133 ILE HD1 H 0.72 0.02 4 1025 . 133 ILE CA C 58.22 0.05 1 1026 . 133 ILE CB C 42.05 0.05 1 1027 . 133 ILE N N 112.17 0.05 1 1028 . 134 ASP H H 8.93 0.02 1 1029 . 134 ASP HA H 5.00 0.02 1 1030 . 134 ASP HB2 H 2.62 0.02 2 1031 . 134 ASP HB3 H 2.46 0.02 2 1032 . 134 ASP CA C 53.46 0.05 1 1033 . 134 ASP CB C 42.05 0.05 1 1034 . 134 ASP N N 121.27 0.05 1 1035 . 135 LEU H H 9.15 0.02 1 1036 . 135 LEU HA H 4.56 0.02 1 1037 . 135 LEU HB2 H 1.68 0.02 2 1038 . 135 LEU HB3 H 1.12 0.02 2 1039 . 135 LEU HG H 1.80 0.02 1 1040 . 135 LEU HD1 H 0.85 0.02 2 1041 . 135 LEU CA C 53.94 0.05 1 1042 . 135 LEU CB C 44.90 0.05 1 1043 . 135 LEU N N 126.15 0.05 1 1044 . 136 THR H H 9.08 0.02 1 1045 . 136 THR HA H 4.40 0.02 1 1046 . 136 THR HB H 3.86 0.02 1 1047 . 136 THR HG2 H 1.13 0.02 1 1048 . 136 THR CA C 62.98 0.05 1 1049 . 136 THR CB C 68.68 0.05 1 1050 . 136 THR N N 120.26 0.05 1 1051 . 137 SER H H 7.79 0.02 1 1052 . 137 SER HA H 4.55 0.02 1 1053 . 137 SER HB2 H 3.80 0.02 2 1054 . 137 SER HB3 H 3.59 0.02 2 1055 . 137 SER CA C 57.74 0.05 1 1056 . 137 SER CB C 63.93 0.05 1 1057 . 137 SER N N 112.75 0.05 1 1058 . 138 ALA H H 8.42 0.05 1 1059 . 138 ALA HA H 5.29 0.05 1 1060 . 138 ALA HB H 1.30 0.05 1 1061 . 138 ALA CA C 51.53 0.05 1 1062 . 138 ALA CB C 21.44 0.05 1 1063 . 138 ALA N N 126.66 0.05 1 1064 . 139 SER H H 8.63 0.02 1 1065 . 139 SER HA H 4.89 0.02 1 1066 . 139 SER HB2 H 4.02 0.02 2 1067 . 139 SER HB3 H 4.00 0.02 2 1068 . 139 SER CA C 57.27 0.05 1 1069 . 139 SER CB C 65.35 0.05 1 1070 . 139 SER N N 115.63 0.05 1 1071 . 140 TYR H H 8.36 0.02 1 1072 . 140 TYR HA H 4.97 0.02 1 1073 . 140 TYR HB2 H 3.11 0.02 2 1074 . 140 TYR HB3 H 2.91 0.02 2 1075 . 140 TYR CA C 55.37 0.05 1 1076 . 140 TYR CB C 43.00 0.05 1 1077 . 140 TYR N N 115.46 0.05 1 1078 . 141 THR H H 8.92 0.02 1 1079 . 141 THR HA H 4.67 0.02 1 1080 . 141 THR HB H 4.20 0.02 1 1081 . 141 THR HG2 H 1.21 0.02 1 1082 . 141 THR CA C 59.17 0.05 1 1083 . 141 THR CB C 70.59 0.05 1 1084 . 141 THR N N 115.37 0.05 1 1085 . 142 MET H H 8.17 0.02 1 1086 . 142 MET HA H 5.55 0.02 1 1087 . 142 MET HB2 H 2.82 0.02 2 1088 . 142 MET HB3 H 2.65 0.02 2 1089 . 142 MET CA C 52.99 0.05 1 1090 . 142 MET CB C 32.06 0.05 1 1091 . 142 MET N N 121.22 0.05 1 1092 . 143 ILE H H 8.65 0.02 1 1093 . 143 ILE CA C 39.67 0.05 1 stop_ save_