data_5251 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete backbone and partial side chain 1H, 15N and 13C assignments for human lymphotactin at 45 C ; _BMRB_accession_number 5251 _BMRB_flat_file_name bmr5251.str _Entry_type original _Submission_date 2002-01-08 _Accession_date 2002-01-09 _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 Kuloglu E. Sonay . 2 McCaslin Darrell R. . 3 Markley John L. . 4 Volkman Brian F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 253 "13C chemical shifts" 262 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-13 original BMRB . stop_ _Original_release_date 2002-01-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Rearrangement of Human Lymphotactin, a C Chemokine, under Physiological Solution Conditions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22001373 _PubMed_ID 11889129 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kuloglu E. Sonay . 2 McCaslin Darrell R. . 3 Markley John L. . 4 Volkman Brian F. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 277 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17863 _Page_last 17870 _Year 2002 _Details . loop_ _Keyword NMR chemokine 'conformational change' lymphotactin stop_ save_ ################################## # Molecular system description # ################################## save_system_ltn _Saveframe_category molecular_system _Mol_system_name lymphotactin _Abbreviation_common ltn _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'lymphotactin, chain A' $lymphotactin 'lymphotactin, chain B' $lymphotactin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'lymphotactin, chain A' 1 'lymphotactin, chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_lymphotactin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lymphotactin _Abbreviation_common ltn _Molecular_mass 10254 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; VGSEVSDKRTCVSLTTQRLP VSRIKTYTITEGSLRAVIFI TKRGLKVCADPQATWVRDVV RSMDRKSNTRNNMIQTKPTG TQQSTNTAVTLTG ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 GLY 3 SER 4 GLU 5 VAL 6 SER 7 ASP 8 LYS 9 ARG 10 THR 11 CYS 12 VAL 13 SER 14 LEU 15 THR 16 THR 17 GLN 18 ARG 19 LEU 20 PRO 21 VAL 22 SER 23 ARG 24 ILE 25 LYS 26 THR 27 TYR 28 THR 29 ILE 30 THR 31 GLU 32 GLY 33 SER 34 LEU 35 ARG 36 ALA 37 VAL 38 ILE 39 PHE 40 ILE 41 THR 42 LYS 43 ARG 44 GLY 45 LEU 46 LYS 47 VAL 48 CYS 49 ALA 50 ASP 51 PRO 52 GLN 53 ALA 54 THR 55 TRP 56 VAL 57 ARG 58 ASP 59 VAL 60 VAL 61 ARG 62 SER 63 MET 64 ASP 65 ARG 66 LYS 67 SER 68 ASN 69 THR 70 ARG 71 ASN 72 ASN 73 MET 74 ILE 75 GLN 76 THR 77 LYS 78 PRO 79 THR 80 GLY 81 THR 82 GLN 83 GLN 84 SER 85 THR 86 ASN 87 THR 88 ALA 89 VAL 90 THR 91 LEU 92 THR 93 GLY stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 15215 XCL1 100.00 93 100.00 100.00 5.51e-46 BMRB 5042 'human lymphotactin' 100.00 93 100.00 100.00 5.51e-46 PDB 1J8I 'Solution Structure Of Human Lymphotactin' 98.92 93 100.00 100.00 1.52e-45 PDB 1J9O 'Solution Structure Of Human Lymphotactin' 98.92 93 100.00 100.00 1.52e-45 PDB 2JP1 'Solution Structure Of The Alternative Conformation Of Xcl1LYMPHOTACTIN' 100.00 93 100.00 100.00 5.51e-46 PDB 2NYZ 'Viral Chemokine Binding Protein M3 From Murine Gammaherpesvirus68 In Complex With The C- Chemokine Xcl1' 100.00 93 100.00 100.00 5.51e-46 DBJ BAA07825 'cytokine [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 DBJ BAA09859 'SCM-1alpha precursor [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 EMBL CAA60198 'CD8+T cell specific protein [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 EMBL CAB46691 'chemokine (C motif) ligand 1 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 GenBank AAC50164 'lymphotactin precursor' 100.00 114 100.00 100.00 2.85e-46 GenBank AAH69817 'Chemokine (C motif) ligand 1 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 GenBank AAH70309 'Chemokine (C motif) ligand 1 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 GenBank EAW90827 'chemokine (C motif) ligand 2 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 GenBank EAW90828 'chemokine (C motif) ligand 1 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 REF NP_002986 'chemokine (C motif) ligand 1 [Homo sapiens]' 100.00 114 100.00 100.00 2.85e-46 REF XP_524955 'PREDICTED: similar to CD8+T cell specific protein [Pan troglodytes]' 100.00 114 100.00 100.00 3.85e-46 SWISS-PROT P47992 ; Lymphotactin precursor (C motif chemokine 1) (Cytokine SCM-1) (ATAC) (Lymphotaxin) (SCM-1-alpha) (Small-inducible cytokine C1) (XC chemokine ligand 1) ; 100.00 114 100.00 100.00 2.85e-46 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $lymphotactin 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 $lymphotactin 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $lymphotactin . mM 0.5 1.0 '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $lymphotactin . mM 0.5 1.0 [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY' _Sample_label . save_ save_15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY' _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C NOESY' _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 n/a temperature 318 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' '13C HSQC' '15N NOESY' '15N TOCSY' HNCA HN(CO)CA HNCO C(CO)NH '13C NOESY' HCCH-TOCSY stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'lymphotactin, chain A' _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 GLY CA C 45.4 . 1 2 . 2 GLY C C 174.0 . 1 3 . 3 SER N N 116.0 . 1 4 . 3 SER H H 8.29 . 1 5 . 3 SER CA C 58.5 . 1 6 . 3 SER CB C 63.9 . 1 7 . 3 SER C C 174.5 . 1 8 . 4 GLU N N 122.9 . 1 9 . 4 GLU H H 8.54 . 1 10 . 4 GLU CA C 56.9 . 1 11 . 4 GLU CB C 30.6 . 1 12 . 4 GLU CG C 36.3 . 1 13 . 4 GLU C C 176.6 . 1 14 . 5 VAL N N 120.3 . 1 15 . 5 VAL H H 8.04 . 1 16 . 5 VAL CA C 62.5 . 1 17 . 5 VAL HA H 4.15 . 1 18 . 5 VAL CB C 32.9 . 1 19 . 5 VAL HB H 2.09 . 1 20 . 5 VAL HG1 H 0.93 . 2 21 . 5 VAL CG1 C 21.0 . 1 22 . 5 VAL C C 176.2 . 1 23 . 6 SER N N 118.7 . 1 24 . 6 SER H H 8.21 . 1 25 . 6 SER CA C 58.5 . 1 26 . 6 SER CB C 64.0 . 1 27 . 6 SER HB2 H 3.83 . 1 28 . 6 SER HB3 H 3.83 . 1 29 . 6 SER C C 174.3 . 1 30 . 7 ASP N N 122.5 . 1 31 . 7 ASP H H 8.23 . 1 32 . 7 ASP CA C 54.5 . 1 33 . 7 ASP CB C 41.3 . 1 34 . 7 ASP HB2 H 2.68 . 1 35 . 7 ASP HB3 H 2.68 . 1 36 . 7 ASP C C 176.1 . 1 37 . 8 LYS N N 120.5 . 1 38 . 8 LYS H H 8.12 . 1 39 . 8 LYS CA C 56.2 . 1 40 . 8 LYS HA H 4.35 . 1 41 . 8 LYS CB C 30.7 . 1 42 . 8 LYS HB2 H 1.89 . 1 43 . 8 LYS HB3 H 1.89 . 1 44 . 8 LYS HG2 H 1.73 . 1 45 . 8 LYS HG3 H 1.73 . 1 46 . 8 LYS HD2 H 1.46 . 1 47 . 8 LYS HD3 H 1.46 . 1 48 . 8 LYS CE C 43.5 . 1 49 . 8 LYS C C 174.8 . 1 50 . 9 ARG N N 121.8 . 1 51 . 9 ARG H H 8.26 . 1 52 . 9 ARG CA C 56.8 . 1 53 . 9 ARG CB C 31.6 . 1 54 . 9 ARG CD C 43.8 . 1 55 . 9 ARG C C 176.2 . 1 56 . 10 THR N N 117.7 . 1 57 . 10 THR H H 8.36 . 1 58 . 10 THR CA C 62.0 . 1 59 . 10 THR HB H 4.25 . 1 60 . 10 THR HG2 H 1.27 . 1 61 . 10 THR C C 174.3 . 1 62 . 11 CYS N N 121.2 . 1 63 . 11 CYS H H 8.33 . 1 64 . 11 CYS CA C 55.5 . 1 65 . 11 CYS HA H 6.04 . 1 66 . 11 CYS HB2 H 2.66 . 2 67 . 11 CYS HB3 H 3.11 . 2 68 . 11 CYS C C 173.7 . 1 69 . 12 VAL N N 118.0 . 1 70 . 12 VAL H H 9.11 . 1 71 . 12 VAL CA C 60.4 . 1 72 . 12 VAL HA H 4.63 . 1 73 . 12 VAL HB H 2.03 . 1 74 . 12 VAL HG1 H 0.87 . 2 75 . 12 VAL C C 173.9 . 1 76 . 13 SER N N 118.3 . 1 77 . 13 SER H H 8.48 . 1 78 . 13 SER CA C 57.8 . 1 79 . 13 SER HA H 5.27 . 1 80 . 13 SER HB2 H 3.71 . 1 81 . 13 SER HB3 H 3.71 . 1 82 . 13 SER C C 172.6 . 1 83 . 14 LEU N N 125.7 . 1 84 . 14 LEU H H 8.88 . 1 85 . 14 LEU CA C 54.5 . 1 86 . 14 LEU HA H 4.66 . 1 87 . 14 LEU HB2 H 1.67 . 2 88 . 14 LEU HB3 H 1.35 . 2 89 . 14 LEU C C 175.8 . 1 90 . 15 THR N N 120.6 . 1 91 . 15 THR H H 8.29 . 1 92 . 15 THR CA C 62.3 . 1 93 . 15 THR HA H 4.18 . 1 94 . 15 THR HG2 H 0.91 . 1 95 . 15 THR C C 175.9 . 1 96 . 16 THR N N 116.3 . 1 97 . 16 THR H H 8.07 . 1 98 . 16 THR CA C 60.7 . 1 99 . 16 THR C C 174.6 . 1 100 . 17 GLN N N 119.3 . 1 101 . 17 GLN H H 8.10 . 1 102 . 17 GLN CA C 56.2 . 1 103 . 17 GLN CG C 33.7 . 1 104 . 17 GLN NE2 N 111.6 . 1 105 . 17 GLN HE21 H 7.44 . 2 106 . 17 GLN HE22 H 6.76 . 2 107 . 17 GLN C C 174.9 . 1 108 . 18 ARG N N 119.7 . 1 109 . 18 ARG H H 8.10 . 1 110 . 18 ARG CA C 56.7 . 1 111 . 18 ARG HA H 4.35 . 1 112 . 18 ARG HB2 H 1.76 . 1 113 . 18 ARG HB3 H 1.76 . 1 114 . 18 ARG HG2 H 0.97 . 1 115 . 18 ARG HG3 H 0.97 . 1 116 . 18 ARG CD C 43.5 . 1 117 . 18 ARG C C 176.2 . 1 118 . 19 LEU N N 125.9 . 1 119 . 19 LEU H H 8.50 . 1 120 . 19 LEU CA C 52.0 . 1 121 . 19 LEU HA H 4.82 . 1 122 . 20 PRO CA C 62.8 . 1 123 . 20 PRO CB C 27.3 . 1 124 . 20 PRO CG C 24.2 . 1 125 . 20 PRO C C 175.7 . 1 126 . 21 VAL N N 119.2 . 1 127 . 21 VAL H H 7.72 . 1 128 . 21 VAL CA C 61.0 . 1 129 . 21 VAL HA H 4.28 . 1 130 . 21 VAL HB H 1.97 . 1 131 . 21 VAL HG1 H 0.72 . 2 132 . 22 SER CA C 59.1 . 1 133 . 22 SER C C 174.1 . 1 134 . 23 ARG N N 120.2 . 1 135 . 23 ARG H H 7.70 . 1 136 . 23 ARG CA C 55.0 . 1 137 . 23 ARG CB C 31.9 . 1 138 . 23 ARG CG C 26.6 . 1 139 . 23 ARG CD C 43.5 . 1 140 . 23 ARG C C 174.3 . 1 141 . 24 ILE N N 120.4 . 1 142 . 24 ILE H H 7.99 . 1 143 . 24 ILE CA C 62.1 . 1 144 . 24 ILE HA H 4.29 . 1 145 . 24 ILE CB C 39.2 . 1 146 . 24 ILE HB H 1.77 . 1 147 . 24 ILE HG2 H 1.13 . 1 148 . 24 ILE CG2 C 17.125 . 1 149 . 24 ILE HD1 H 0.93 . 1 150 . 24 ILE C C 175.9 . 1 151 . 25 LYS N N 127.1 . 1 152 . 25 LYS H H 8.36 . 1 153 . 25 LYS CA C 55.0 . 1 154 . 25 LYS HA H 4.63 . 1 155 . 25 LYS CB C 35.4 . 1 156 . 25 LYS HB2 H 1.68 . 1 157 . 25 LYS HB3 H 1.68 . 1 158 . 25 LYS HG2 H 1.40 . 1 159 . 25 LYS HG3 H 1.40 . 1 160 . 25 LYS C C 174.9 . 1 161 . 26 THR N N 115.3 . 1 162 . 26 THR H H 7.94 . 1 163 . 26 THR CA C 60.2 . 1 164 . 26 THR HA H 5.28 . 1 165 . 26 THR HB H 3.67 . 1 166 . 26 THR HG2 H 0.78 . 1 167 . 26 THR C C 173.5 . 1 168 . 27 TYR N N 123.5 . 1 169 . 27 TYR H H 8.84 . 1 170 . 27 TYR CA C 57.0 . 1 171 . 27 TYR HA H 4.71 . 1 172 . 27 TYR HB2 H 2.89 . 2 173 . 27 TYR HB3 H 2.56 . 2 174 . 27 TYR C C 174.4 . 1 175 . 28 THR N N 116.9 . 1 176 . 28 THR H H 8.41 . 1 177 . 28 THR CA C 61.6 . 1 178 . 28 THR C C 173.6 . 1 179 . 29 ILE N N 125.7 . 1 180 . 29 ILE H H 8.85 . 1 181 . 29 ILE CA C 60.0 . 1 182 . 29 ILE HA H 4.22 . 1 183 . 29 ILE HB H 1.43 . 1 184 . 29 ILE HG2 H 0.48 . 1 185 . 29 ILE C C 174.5 . 1 186 . 30 THR N N 120.2 . 1 187 . 30 THR H H 8.35 . 1 188 . 30 THR CA C 60.4 . 1 189 . 30 THR HA H 5.03 . 1 190 . 30 THR HB H 4.02 . 1 191 . 30 THR HG2 H 1.09 . 1 192 . 30 THR C C 173.9 . 1 193 . 31 GLU N N 126.5 . 1 194 . 31 GLU H H 8.47 . 1 195 . 31 GLU CA C 54.8 . 1 196 . 31 GLU HA H 4.54 . 1 197 . 31 GLU HB2 H 1.86 . 2 198 . 31 GLU HB3 H 2.13 . 2 199 . 31 GLU C C 175.6 . 1 200 . 32 GLY N N 116.2 . 1 201 . 32 GLY H H 8.88 . 1 202 . 32 GLY CA C 47.4 . 1 203 . 32 GLY C C 174.9 . 1 204 . 33 SER N N 121.4 . 1 205 . 33 SER H H 8.50 . 1 206 . 33 SER CA C 59.0 . 1 207 . 33 SER CB C 62.3 . 1 208 . 33 SER C C 173.5 . 1 209 . 34 LEU N N 124.4 . 1 210 . 34 LEU H H 8.08 . 1 211 . 34 LEU CA C 54.9 . 1 212 . 34 LEU HA H 4.45 . 1 213 . 34 LEU HB2 H 2.05 . 1 214 . 34 LEU HB3 H 2.05 . 1 215 . 34 LEU HG H 1.43 . 1 216 . 34 LEU HD1 H 1.02 . 2 217 . 34 LEU HD2 H 0.88 . 2 218 . 34 LEU C C 174.8 . 1 219 . 35 ARG N N 126.7 . 1 220 . 35 ARG H H 8.19 . 1 221 . 35 ARG CA C 55.1 . 1 222 . 35 ARG HA H 5.04 . 1 223 . 35 ARG HB2 H 1.70 . 1 224 . 35 ARG HB3 H 1.70 . 1 225 . 35 ARG CD C 43.5 . 1 226 . 35 ARG C C 174.3 . 1 227 . 36 ALA N N 126.9 . 1 228 . 36 ALA H H 9.02 . 1 229 . 36 ALA CA C 50.1 . 1 230 . 36 ALA HA H 5.22 . 1 231 . 36 ALA HB H 1.06 . 1 232 . 36 ALA CB C 21.2 . 1 233 . 36 ALA C C 174.9 . 1 234 . 37 VAL N N 120.6 . 1 235 . 37 VAL H H 8.77 . 1 236 . 37 VAL CA C 60.8 . 1 237 . 37 VAL HA H 4.63 . 1 238 . 37 VAL HB H 1.58 . 1 239 . 37 VAL HG1 H 0.61 . 2 240 . 37 VAL HG2 H 0.33 . 2 241 . 37 VAL CG2 C 21.3 . 1 242 . 37 VAL C C 173.5 . 1 243 . 38 ILE N N 126.4 . 1 244 . 38 ILE H H 8.93 . 1 245 . 38 ILE CA C 59.9 . 1 246 . 38 ILE HA H 4.79 . 1 247 . 38 ILE HB H 1.76 . 1 248 . 38 ILE HG2 H 0.76 . 1 249 . 38 ILE C C 174.2 . 1 250 . 39 PHE N N 124.5 . 1 251 . 39 PHE H H 9.54 . 1 252 . 39 PHE CA C 56.2 . 1 253 . 39 PHE HA H 5.24 . 1 254 . 39 PHE CB C 41.3 . 1 255 . 39 PHE HB2 H 3.02 . 2 256 . 39 PHE HB3 H 2.78 . 2 257 . 39 PHE C C 175.4 . 1 258 . 40 ILE N N 124.4 . 1 259 . 40 ILE H H 9.23 . 1 260 . 40 ILE CA C 61.5 . 1 261 . 40 ILE HA H 4.56 . 1 262 . 40 ILE HB H 1.95 . 1 263 . 40 ILE HG2 H 0.87 . 1 264 . 40 ILE C C 175.0 . 1 265 . 41 THR N N 116.5 . 1 266 . 41 THR H H 8.40 . 1 267 . 41 THR CA C 59.4 . 1 268 . 41 THR HA H 4.91 . 1 269 . 41 THR C C 174.2 . 1 270 . 42 LYS N N 116.2 . 1 271 . 42 LYS H H 8.53 . 1 272 . 42 LYS CA C 59.1 . 1 273 . 42 LYS CB C 32.8 . 1 274 . 42 LYS CD C 25.314 . 1 275 . 42 LYS C C 176.9 . 1 276 . 43 ARG N N 114.0 . 1 277 . 43 ARG H H 7.66 . 1 278 . 43 ARG CA C 54.9 . 1 279 . 43 ARG CB C 31.0 . 1 280 . 43 ARG HB2 H 2.07 . 1 281 . 43 ARG HB3 H 2.07 . 1 282 . 43 ARG HG2 H 1.53 . 1 283 . 43 ARG HG3 H 1.53 . 1 284 . 43 ARG CD C 43.3 . 1 285 . 43 ARG HD2 H 3.17 . 1 286 . 43 ARG HD3 H 3.17 . 1 287 . 43 ARG C C 175.7 . 1 288 . 44 GLY N N 107.3 . 1 289 . 44 GLY H H 7.37 . 1 290 . 44 GLY CA C 45.7 . 1 291 . 44 GLY HA2 H 4.86 . 2 292 . 44 GLY HA3 H 3.81 . 2 293 . 44 GLY C C 172.2 . 1 294 . 45 LEU N N 120.5 . 1 295 . 45 LEU H H 8.28 . 1 296 . 45 LEU CA C 53.9 . 1 297 . 45 LEU HA H 5.40 . 1 298 . 45 LEU HB2 H 1.53 . 1 299 . 45 LEU HB3 H 1.53 . 1 300 . 45 LEU C C 175.5 . 1 301 . 46 LYS N N 125.5 . 1 302 . 46 LYS H H 9.11 . 1 303 . 46 LYS CA C 55.3 . 1 304 . 46 LYS HA H 5.22 . 1 305 . 46 LYS HB2 H 1.82 . 1 306 . 46 LYS HB3 H 1.82 . 1 307 . 46 LYS HG2 H 1.40 . 1 308 . 46 LYS HG3 H 1.40 . 1 309 . 46 LYS HD2 H 0.81 . 1 310 . 46 LYS HD3 H 0.81 . 1 311 . 46 LYS C C 174.2 . 1 312 . 47 VAL N N 125.2 . 1 313 . 47 VAL H H 9.10 . 1 314 . 47 VAL CA C 60.6 . 1 315 . 47 VAL HA H 5.21 . 1 316 . 47 VAL HB H 1.83 . 1 317 . 47 VAL HG1 H 0.81 . 2 318 . 47 VAL C C 174.9 . 1 319 . 48 CYS N N 123.2 . 1 320 . 48 CYS H H 9.30 . 1 321 . 48 CYS CA C 54.8 . 1 322 . 48 CYS HA H 5.84 . 1 323 . 48 CYS HB2 H 2.98 . 1 324 . 48 CYS HB3 H 2.98 . 1 325 . 48 CYS C C 173.3 . 1 326 . 49 ALA N N 124.4 . 1 327 . 49 ALA H H 8.89 . 1 328 . 49 ALA CA C 51.3 . 1 329 . 49 ALA HA H 4.93 . 1 330 . 49 ALA HB H 1.34 . 1 331 . 49 ALA CB C 21.5 . 1 332 . 49 ALA C C 175.6 . 1 333 . 50 ASP N N 121.5 . 1 334 . 50 ASP H H 8.44 . 1 335 . 50 ASP CA C 52.4 . 1 336 . 50 ASP HA H 5.06 . 1 337 . 50 ASP HB2 H 2.80 . 2 338 . 50 ASP HB3 H 2.57 . 2 339 . 51 PRO CA C 63.7 . 1 340 . 51 PRO C C 176.7 . 1 341 . 52 GLN N N 119.1 . 1 342 . 52 GLN H H 8.33 . 1 343 . 52 GLN CA C 55.9 . 1 344 . 52 GLN HA H 4.24 . 1 345 . 52 GLN HB2 H 1.97 . 1 346 . 52 GLN HB3 H 1.97 . 1 347 . 52 GLN HG2 H 2.30 . 1 348 . 52 GLN HG3 H 2.30 . 1 349 . 52 GLN NE2 N 111.8 . 1 350 . 52 GLN HE21 H 7.40 . 2 351 . 52 GLN HE22 H 6.69 . 2 352 . 52 GLN C C 175.8 . 1 353 . 53 ALA N N 124.5 . 1 354 . 53 ALA H H 8.06 . 1 355 . 53 ALA CA C 52.9 . 1 356 . 53 ALA HA H 4.08 . 1 357 . 53 ALA HB H 1.44 . 1 358 . 53 ALA CB C 19.2 . 1 359 . 53 ALA C C 177.7 . 1 360 . 54 THR N N 112.3 . 1 361 . 54 THR H H 7.97 . 1 362 . 54 THR CA C 62.4 . 1 363 . 54 THR C C 174.4 . 1 364 . 55 TRP N N 122.8 . 1 365 . 55 TRP H H 7.92 . 1 366 . 55 TRP CA C 57.4 . 1 367 . 55 TRP HA H 4.72 . 1 368 . 55 TRP HB2 H 3.22 . 1 369 . 55 TRP HB3 H 3.22 . 1 370 . 55 TRP NE1 N 129.276 . 1 371 . 55 TRP HD1 H 7.19 . 1 372 . 55 TRP HE1 H 10.02 . 1 373 . 57 ARG CA C 56.5 . 1 374 . 57 ARG CB C 32.4 . 1 375 . 57 ARG CG C 30.9 . 1 376 . 57 ARG CD C 43.5 . 1 377 . 57 ARG C C 176.2 . 1 378 . 58 ASP N N 121.5 . 1 379 . 58 ASP H H 8.18 . 1 380 . 58 ASP CA C 54.7 . 1 381 . 58 ASP CB C 41.5 . 1 382 . 58 ASP HB2 H 2.64 . 1 383 . 58 ASP HB3 H 2.64 . 1 384 . 58 ASP C C 176.3 . 1 385 . 59 VAL N N 119.9 . 1 386 . 59 VAL H H 7.95 . 1 387 . 59 VAL CA C 62.8 . 1 388 . 59 VAL HA H 4.08 . 1 389 . 59 VAL CB C 32.9 . 1 390 . 59 VAL HB H 2.06 . 1 391 . 59 VAL HG1 H 1.14 . 2 392 . 59 VAL HG2 H 0.88 . 2 393 . 59 VAL CG1 C 21.0 . 1 394 . 59 VAL C C 176.3 . 1 395 . 60 VAL N N 123.0 . 1 396 . 60 VAL H H 8.02 . 1 397 . 60 VAL CA C 63.0 . 1 398 . 60 VAL HA H 4.02 . 1 399 . 60 VAL CB C 32.6 . 1 400 . 60 VAL HB H 2.04 . 1 401 . 60 VAL HG1 H 0.93 . 2 402 . 60 VAL CG1 C 21.2 . 1 403 . 60 VAL C C 176.4 . 1 404 . 61 ARG N N 124.0 . 1 405 . 61 ARG H H 8.23 . 1 406 . 61 ARG CA C 56.3 . 1 407 . 61 ARG CB C 30.9 . 1 408 . 61 ARG CD C 43.5 . 1 409 . 61 ARG C C 176.5 . 1 410 . 62 SER N N 116.5 . 1 411 . 62 SER H H 8.17 . 1 412 . 62 SER CA C 58.8 . 1 413 . 62 SER CB C 63.8 . 1 414 . 62 SER C C 174.8 . 1 415 . 63 MET N N 121.7 . 1 416 . 63 MET H H 8.27 . 1 417 . 63 MET CA C 55.9 . 1 418 . 63 MET CB C 32.3 . 1 419 . 63 MET C C 175.9 . 1 420 . 64 ASP N N 121.2 . 1 421 . 64 ASP H H 8.12 . 1 422 . 64 ASP CA C 54.6 . 1 423 . 64 ASP HA H 4.32 . 1 424 . 64 ASP CB C 41.8 . 1 425 . 64 ASP HB2 H 2.63 . 1 426 . 64 ASP HB3 H 2.63 . 1 427 . 64 ASP C C 175.9 . 1 428 . 65 ARG N N 121.4 . 1 429 . 65 ARG H H 8.14 . 1 430 . 65 ARG CA C 56.2 . 1 431 . 65 ARG CB C 31.0 . 1 432 . 65 ARG CD C 43.5 . 1 433 . 65 ARG C C 175.7 . 1 434 . 66 LYS N N 120.0 . 1 435 . 66 LYS H H 8.35 . 1 436 . 66 LYS CA C 53.4 . 1 437 . 66 LYS C C 177.2 . 1 438 . 67 SER N N 113.9 . 1 439 . 67 SER H H 8.01 . 1 440 . 67 SER CA C 62.1 . 1 441 . 69 THR CA C 62.8 . 1 442 . 69 THR CB C 62.8 . 1 443 . 69 THR CG2 C 21.0 . 1 444 . 69 THR C C 175.7 . 1 445 . 70 ARG N N 123.5 . 1 446 . 70 ARG H H 8.01 . 1 447 . 70 ARG CA C 56.5 . 1 448 . 70 ARG CB C 30.7 . 1 449 . 70 ARG CD C 43.4 . 1 450 . 70 ARG C C 176.0 . 1 451 . 71 ASN N N 119.3 . 1 452 . 71 ASN H H 8.29 . 1 453 . 71 ASN CA C 53.5 . 1 454 . 71 ASN CB C 39.0 . 1 455 . 71 ASN C C 175.0 . 1 456 . 72 ASN N N 118.9 . 1 457 . 72 ASN H H 8.28 . 1 458 . 72 ASN CA C 53.7 . 1 459 . 72 ASN CB C 39.1 . 1 460 . 72 ASN C C 175.1 . 1 461 . 73 MET N N 120.0 . 1 462 . 73 MET H H 8.14 . 1 463 . 73 MET CA C 55.9 . 1 464 . 73 MET CB C 32.3 . 1 465 . 73 MET C C 176.0 . 1 466 . 74 ILE N N 121.4 . 1 467 . 74 ILE H H 7.94 . 1 468 . 74 ILE CA C 61.2 . 1 469 . 74 ILE HA H 4.15 . 1 470 . 74 ILE CB C 38.8 . 1 471 . 74 ILE HB H 1.85 . 1 472 . 74 ILE HG2 H 1.14 . 1 473 . 74 ILE CG2 C 17.6 . 1 474 . 74 ILE CG1 C 27.4 . 1 475 . 74 ILE HD1 H 0.88 . 1 476 . 74 ILE CD1 C 12.7 . 1 477 . 74 ILE C C 176.0 . 1 478 . 75 GLN N N 124.3 . 1 479 . 75 GLN H H 8.32 . 1 480 . 75 GLN CA C 55.8 . 1 481 . 75 GLN CB C 33.9 . 1 482 . 75 GLN C C 175.9 . 1 483 . 76 THR N N 116.1 . 1 484 . 76 THR H H 8.09 . 1 485 . 76 THR CA C 62.0 . 1 486 . 76 THR CB C 69.8 . 1 487 . 76 THR CG2 C 21.4 . 1 488 . 76 THR C C 174.1 . 1 489 . 77 LYS N N 124.4 . 1 490 . 77 LYS H H 8.17 . 1 491 . 77 LYS CA C 54.3 . 1 492 . 77 LYS HA H 4.36 . 1 493 . 77 LYS HB2 H 1.74 . 1 494 . 77 LYS HB3 H 1.74 . 1 495 . 77 LYS HG2 H 1.47 . 1 496 . 77 LYS HG3 H 1.47 . 1 497 . 78 PRO CD C 50.8 . 1 498 . 78 PRO CA C 63.3 . 1 499 . 78 PRO CB C 32.2 . 1 500 . 78 PRO CG C 27.4 . 1 501 . 78 PRO C C 177.2 . 1 502 . 79 THR N N 113.9 . 1 503 . 79 THR H H 8.13 . 1 504 . 79 THR CA C 62.0 . 1 505 . 79 THR HA H 4.32 . 1 506 . 79 THR CB C 70.0 . 1 507 . 79 THR CG2 C 21.4 . 1 508 . 79 THR C C 175.2 . 1 509 . 80 GLY N N 110.8 . 1 510 . 80 GLY H H 8.31 . 1 511 . 80 GLY CA C 45.5 . 1 512 . 80 GLY C C 174.4 . 1 513 . 81 THR N N 113.4 . 1 514 . 81 THR H H 7.99 . 1 515 . 81 THR CA C 62.0 . 1 516 . 81 THR CB C 69.8 . 1 517 . 81 THR CG2 C 21.4 . 1 518 . 81 THR C C 174.8 . 1 519 . 82 GLN N N 122.5 . 1 520 . 82 GLN H H 8.35 . 1 521 . 82 GLN CA C 56.2 . 1 522 . 82 GLN CB C 29.8 . 1 523 . 82 GLN CG C 34.0 . 1 524 . 82 GLN C C 175.9 . 1 525 . 83 GLN N N 121.5 . 1 526 . 83 GLN H H 8.34 . 1 527 . 83 GLN CA C 56.1 . 1 528 . 83 GLN CB C 29.7 . 1 529 . 83 GLN CG C 33.9 . 1 530 . 83 GLN C C 176.0 . 1 531 . 84 SER N N 116.9 . 1 532 . 84 SER H H 8.31 . 1 533 . 84 SER CA C 58.5 . 1 534 . 84 SER CB C 63.9 . 1 535 . 84 SER C C 174.8 . 1 536 . 85 THR N N 115.2 . 1 537 . 85 THR H H 8.10 . 1 538 . 85 THR CA C 62.0 . 1 539 . 85 THR CB C 69.7 . 1 540 . 85 THR CG2 C 21.4 . 1 541 . 85 THR C C 174.7 . 1 542 . 86 ASN N N 122.6 . 1 543 . 86 ASN H H 8.21 . 1 544 . 86 ASN CA C 56.3 . 1 545 . 86 ASN CB C 39.5 . 1 546 . 86 ASN C C 175.3 . 1 547 . 87 THR N N 114.4 . 1 548 . 87 THR H H 8.01 . 1 549 . 87 THR CA C 62.0 . 1 550 . 87 THR CB C 69.7 . 1 551 . 87 THR CG2 C 21.4 . 1 552 . 87 THR C C 174.2 . 1 553 . 88 ALA N N 126.2 . 1 554 . 88 ALA H H 8.13 . 1 555 . 88 ALA CA C 52.6 . 1 556 . 88 ALA HA H 4.38 . 1 557 . 88 ALA HB H 1.38 . 1 558 . 88 ALA CB C 19.3 . 1 559 . 88 ALA C C 177.5 . 1 560 . 89 VAL N N 119.1 . 1 561 . 89 VAL H H 7.93 . 1 562 . 89 VAL CA C 62.3 . 1 563 . 89 VAL HA H 4.17 . 1 564 . 89 VAL CB C 33.1 . 1 565 . 89 VAL HB H 2.07 . 1 566 . 89 VAL HG1 H 0.93 . 2 567 . 89 VAL CG1 C 20.8 . 1 568 . 89 VAL C C 176.1 . 1 569 . 90 THR N N 118.2 . 1 570 . 90 THR H H 8.10 . 1 571 . 90 THR CA C 61.7 . 1 572 . 90 THR HA H 4.35 . 1 573 . 90 THR CB C 69.9 . 1 574 . 90 THR HB H 4.15 . 1 575 . 90 THR HG2 H 1.19 . 1 576 . 90 THR CG2 C 21.4 . 1 577 . 90 THR C C 174.3 . 1 578 . 91 LEU N N 125.3 . 1 579 . 91 LEU H H 8.24 . 1 580 . 91 LEU CA C 55.4 . 1 581 . 91 LEU CB C 42.5 . 1 582 . 91 LEU HB2 H 1.65 . 1 583 . 91 LEU HB3 H 1.65 . 1 584 . 91 LEU CG C 27.0 . 1 585 . 91 LEU HD1 H 0.88 . 2 586 . 91 LEU CD1 C 24.9 . 1 587 . 91 LEU CD2 C 23.5 . 1 588 . 91 LEU C C 175.4 . 1 589 . 92 THR N N 113.8 . 1 590 . 92 THR H H 7.99 . 1 591 . 92 THR CA C 61.6 . 1 592 . 92 THR HA H 4.38 . 1 593 . 92 THR CB C 70.0 . 1 594 . 92 THR HG2 H 1.17 . 1 595 . 92 THR CG2 C 21.2 . 1 596 . 92 THR C C 174.1 . 1 597 . 93 GLY N N 117.1 . 1 598 . 93 GLY H H 7.83 . 1 599 . 93 GLY CA C 46.4 . 1 600 . 93 GLY HA2 H 3.78 . 1 601 . 93 GLY HA3 H 3.78 . 1 stop_ save_