data_5073 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the monomeric variant of the chemokine MIP-1beta ; _BMRB_accession_number 5073 _BMRB_flat_file_name bmr5073.str _Entry_type original _Submission_date 2001-07-09 _Accession_date 2001-07-09 _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 Kim S. . . 2 Jao S. . . 3 Laurence J. S. . 4 LiWang P. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 318 "13C chemical shifts" 190 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-07 original BMRB . stop_ _Original_release_date 2001-07-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Comparison of Monomeric Variants of the Chemokine MIP-1beta having Differing Ability to bind the Receptor CCR5 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21426425 _PubMed_ID 11535053 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim S. . . 2 Jao S. . . 3 Laurence J. S. . 4 LiWang P. J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 36 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10782 _Page_last 10791 _Year 2001 _Details . loop_ _Keyword MIP-1beta chemokine 'macrophage inflammatory protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_MIP-1beta _Saveframe_category molecular_system _Mol_system_name 'macrophage inflammatory protein 1-beta (MIP-1beta)' _Abbreviation_common MIP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MIP-1-beta $MIP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MIP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MIP-1 beta' _Abbreviation_common MIP _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 69 _Mol_residue_sequence ; APMGSDPPTACCASYTARKL PRNFVVDYYETSSLCSQPAV VFQTKRSKQVCADPSESWVQ EYVYDLELN ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PRO 3 MET 4 GLY 5 SER 6 ASP 7 PRO 8 PRO 9 THR 10 ALA 11 CYS 12 CYS 13 ALA 14 SER 15 TYR 16 THR 17 ALA 18 ARG 19 LYS 20 LEU 21 PRO 22 ARG 23 ASN 24 PHE 25 VAL 26 VAL 27 ASP 28 TYR 29 TYR 30 GLU 31 THR 32 SER 33 SER 34 LEU 35 CYS 36 SER 37 GLN 38 PRO 39 ALA 40 VAL 41 VAL 42 PHE 43 GLN 44 THR 45 LYS 46 ARG 47 SER 48 LYS 49 GLN 50 VAL 51 CYS 52 ALA 53 ASP 54 PRO 55 SER 56 GLU 57 SER 58 TRP 59 VAL 60 GLN 61 GLU 62 TYR 63 VAL 64 TYR 65 ASP 66 LEU 67 GLU 68 LEU 69 ASN 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 PDB 1HUM 'Solution Structure Of The Chemokine Hmip-1beta(Slash)act-2 By Multi-Dimensional Nmr: A Novel Chemokine Dimer' 100.00 69 98.55 98.55 2.65e-32 PDB 1HUN 'Solution Structure Of The Chemokine Hmip-1beta(Slash)act-2 By Multi-Dimensional Nmr: A Novel Chemokine Dimer' 100.00 69 98.55 98.55 2.65e-32 PDB 1JE4 'Solution Structure Of The Monomeric Variant Of The Chemokine Mip-1beta' 100.00 69 100.00 100.00 4.71e-33 EMBL CAA34291 'cytokine 21 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 EMBL CAA37723 'LAG-1 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 EMBL CAG46916 'CCL4 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 GenBank AAA51576 'act-2 protein precursor' 100.00 92 98.55 98.55 9.49e-33 GenBank AAA57256 lymphokine 100.00 92 98.55 98.55 6.15e-33 GenBank AAI07434 'Chemokine (C-C motif) ligand 4 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 GenBank AAX07292 'CC chemokine ligand 4 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 GenBank AAX07305 'CC chemokine ligand 4 [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 REF NP_002975 'chemokine C-C motif ligand 4 isoform 1 precursor [Homo sapiens]' 100.00 92 98.55 98.55 9.49e-33 SWISS-PROT P13236 ; C-C motif chemokine 4 precursor (Small-inducible cytokine A4) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (MIP-1-beta(1-69)) (T-cell activation protein 2) (ACT-2) (PAT 744) (Protein H400) (SIS-gamma) (Lymphocyte activation gene 1 protein) (LAG-1) (HC21) (G-26 T-lymphocyte-secreted protein) [Contains: MIP-1-beta(3-69)] ; 100.00 92 98.55 98.55 9.49e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MIP 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 $MIP 'recombinant technology' 'E. coli' . . . . 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 $MIP . mM 1 2 '[U-15N; U-13C]' 'sodium phosphate' 20 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details Delaglio save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure solution' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 2.5 . n/a pressure 1 . atm temperature 298 . 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 . C 13 . ppm . . . . . . . H 1 . ppm . . . . . . . N 15 . ppm . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 13C-separated NOESY' '3D 15N-separated NOESY' HNHA stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MIP-1-beta _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 PRO HA H 4.537 . . 2 . 2 PRO HB3 H 1.892 . . 3 . 2 PRO HB2 H 2.270 . . 4 . 2 PRO HG2 H 1.983 . . 5 . 2 PRO HG3 H 2.015 . . 6 . 2 PRO HD2 H 3.727 . . 7 . 2 PRO HD3 H 3.638 . . 8 . 2 PRO CA C 63.148 . . 9 . 2 PRO CB C 32.081 . . 10 . 2 PRO CG C 27.245 . . 11 . 2 PRO CD C 50.466 . . 12 . 3 MET H H 8.606 . . 13 . 3 MET N N 121.718 . . 14 . 3 MET HA H 4.478 . . 15 . 3 MET HB2 H 2.086 . . 16 . 3 MET HB3 H 2.057 . . 17 . 3 MET HG2 H 2.621 . . 18 . 3 MET HG3 H 2.587 . . 19 . 3 MET CA C 55.900 . . 20 . 3 MET CB C 32.800 . . 21 . 3 MET CG C 32.081 . . 22 . 4 GLY H H 8.498 . . 23 . 4 GLY N N 110.693 . . 24 . 4 GLY HA2 H 3.997 . . 25 . 4 GLY HA3 H 3.997 . . 26 . 4 GLY CA C 45.203 . . 27 . 5 SER H H 8.152 . . 28 . 5 SER N N 115.365 . . 29 . 5 SER HA H 4.479 . . 30 . 5 SER HB2 H 3.853 . . 31 . 5 SER CA C 58.324 . . 32 . 5 SER CB C 64.110 . . 33 . 6 ASP H H 8.424 . . 34 . 6 ASP N N 121.781 . . 35 . 6 ASP HA H 4.738 . . 36 . 6 ASP HB2 H 2.939 . . 37 . 6 ASP CA C 52.601 . . 38 . 6 ASP CB C 38.642 . . 39 . 8 PRO HA H 4.495 . . 40 . 8 PRO HB2 H 2.845 . . 41 . 8 PRO HB3 H 2.275 . . 42 . 8 PRO HG2 H 1.979 . . 43 . 8 PRO HG3 H 2.012 . . 44 . 8 PRO HD2 H 3.725 . . 45 . 8 PRO HD3 H 3.648 . . 46 . 8 PRO CA C 63.330 . . 47 . 8 PRO CB C 32.157 . . 48 . 8 PRO CG C 27.299 . . 49 . 8 PRO CD C 50.361 . . 50 . 9 THR H H 8.195 . . 51 . 9 THR N N 114.248 . . 52 . 9 THR HA H 4.303 . . 53 . 9 THR HB H 4.252 . . 54 . 9 THR HG2 H 1.146 . . 55 . 9 THR CA C 61.761 . . 56 . 9 THR CB C 70.100 . . 57 . 9 THR CG2 C 21.507 . . 58 . 10 ALA H H 8.103 . . 59 . 10 ALA N N 125.911 . . 60 . 10 ALA HA H 4.449 . . 61 . 10 ALA HB H 1.434 . . 62 . 10 ALA CA C 52.388 . . 63 . 10 ALA CB C 19.572 . . 64 . 11 CYS H H 8.297 . . 65 . 11 CYS N N 117.582 . . 66 . 11 CYS HA H 5.066 . . 67 . 11 CYS HB3 H 2.581 . . 68 . 11 CYS HB2 H 3.492 . . 69 . 11 CYS CA C 52.383 . . 70 . 11 CYS CB C 39.463 . . 71 . 12 CYS H H 9.345 . . 72 . 12 CYS N N 120.869 . . 73 . 12 CYS HA H 4.723 . . 74 . 12 CYS HB2 H 2.773 . . 75 . 12 CYS HB3 H 3.031 . . 76 . 12 CYS CA C 56.137 . . 77 . 12 CYS CB C 43.983 . . 78 . 13 ALA H H 9.064 . . 79 . 13 ALA N N 127.597 . . 80 . 13 ALA HA H 4.199 . . 81 . 13 ALA HB H 1.339 . . 82 . 13 ALA CA C 52.388 . . 83 . 13 ALA CB C 19.583 . . 84 . 14 SER H H 7.445 . . 85 . 14 SER N N 109.691 . . 86 . 14 SER HA H 4.186 . . 87 . 14 SER HB2 H 3.767 . . 88 . 14 SER CA C 56.450 . . 89 . 14 SER CB C 64.573 . . 90 . 15 TYR H H 8.461 . . 91 . 15 TYR N N 118.042 . . 92 . 15 TYR HA H 4.863 . . 93 . 15 TYR HB3 H 2.803 . . 94 . 15 TYR HB2 H 3.187 . . 95 . 15 TYR CA C 54.888 . . 96 . 15 TYR CB C 40.829 . . 97 . 16 THR H H 8.863 . . 98 . 16 THR N N 116.877 . . 99 . 16 THR HA H 4.462 . . 100 . 16 THR HB H 4.433 . . 101 . 16 THR HG2 H 1.541 . . 102 . 16 THR CA C 62.698 . . 103 . 16 THR CB C 69.541 . . 104 . 16 THR CG2 C 20.189 . . 105 . 17 ALA H H 8.792 . . 106 . 17 ALA N N 129.570 . . 107 . 17 ALA HA H 4.570 . . 108 . 17 ALA HB H 1.514 . . 109 . 17 ALA CA C 53.013 . . 110 . 17 ALA CB C 20.009 . . 111 . 18 ARG H H 7.899 . . 112 . 18 ARG N N 118.926 . . 113 . 18 ARG HA H 4.414 . . 114 . 18 ARG HB3 H 1.589 . . 115 . 18 ARG HB2 H 1.667 . . 116 . 18 ARG HG2 H 1.550 . . 117 . 18 ARG HD2 H 3.131 . . 118 . 18 ARG CA C 54.575 . . 119 . 18 ARG CB C 32.390 . . 120 . 18 ARG CG C 26.852 . . 121 . 18 ARG CD C 43.366 . . 122 . 19 LYS H H 7.915 . . 123 . 19 LYS N N 121.937 . . 124 . 19 LYS HA H 2.143 . . 125 . 19 LYS HB3 H 0.654 . . 126 . 19 LYS HB2 H 0.868 . . 127 . 19 LYS HG2 H 0.346 . . 128 . 19 LYS HG3 H 0.116 . . 129 . 19 LYS HD2 H 1.291 . . 130 . 19 LYS HD3 H 1.245 . . 131 . 19 LYS HE2 H 2.713 . . 132 . 19 LYS CA C 56.137 . . 133 . 19 LYS CB C 32.393 . . 134 . 19 LYS CG C 23.958 . . 135 . 19 LYS CD C 29.269 . . 136 . 19 LYS CE C 41.766 . . 137 . 20 LEU H H 5.206 . . 138 . 20 LEU N N 126.150 . . 139 . 21 PRO HA H 4.319 . . 140 . 21 PRO HB3 H 1.646 . . 141 . 21 PRO HB2 H 2.167 . . 142 . 21 PRO HG2 H 1.666 . . 143 . 21 PRO HG3 H 1.718 . . 144 . 21 PRO HD2 H 3.148 . . 145 . 21 PRO HD3 H 3.731 . . 146 . 21 PRO CA C 62.386 . . 147 . 21 PRO CB C 31.456 . . 148 . 21 PRO CG C 27.632 . . 149 . 21 PRO CD C 50.633 . . 150 . 22 ARG H H 8.584 . . 151 . 22 ARG N N 126.262 . . 152 . 22 ARG HA H 3.479 . . 153 . 22 ARG HB2 H 1.612 . . 154 . 22 ARG HG2 H 1.138 . . 155 . 22 ARG HG3 H 1.451 . . 156 . 22 ARG HD2 H 2.713 . . 157 . 22 ARG HD3 H 2.556 . . 158 . 22 ARG CA C 58.637 . . 159 . 22 ARG CB C 28.957 . . 160 . 22 ARG CG C 27.152 . . 161 . 22 ARG CD C 42.045 . . 162 . 23 ASN H H 8.580 . . 163 . 23 ASN N N 113.501 . . 164 . 23 ASN HA H 4.510 . . 165 . 23 ASN HB2 H 2.885 . . 166 . 23 ASN HB3 H 2.747 . . 167 . 23 ASN CA C 54.064 . . 168 . 23 ASN CB C 36.767 . . 169 . 24 PHE H H 7.854 . . 170 . 24 PHE N N 118.236 . . 171 . 24 PHE HA H 4.714 . . 172 . 24 PHE HB2 H 3.201 . . 173 . 24 PHE HD1 H 6.850 . . 174 . 24 PHE CA C 56.862 . . 175 . 24 PHE CB C 40.829 . . 176 . 25 VAL H H 7.475 . . 177 . 25 VAL N N 117.501 . . 178 . 25 VAL HA H 4.099 . . 179 . 25 VAL HB H 2.086 . . 180 . 25 VAL HG1 H 0.929 . . 181 . 25 VAL HG2 H 0.793 . . 182 . 25 VAL CA C 62.698 . . 183 . 25 VAL CB C 33.018 . . 184 . 25 VAL CG1 C 23.068 . . 185 . 25 VAL CG2 C 21.447 . . 186 . 26 VAL H H 8.936 . . 187 . 26 VAL N N 121.264 . . 188 . 26 VAL HA H 4.352 . . 189 . 26 VAL HB H 1.951 . . 190 . 26 VAL HG1 H 0.853 . . 191 . 26 VAL HG2 H 0.725 . . 192 . 26 VAL CA C 62.386 . . 193 . 26 VAL CB C 33.643 . . 194 . 26 VAL CG1 C 21.147 . . 195 . 26 VAL CG2 C 20.006 . . 196 . 27 ASP H H 8.030 . . 197 . 27 ASP N N 114.878 . . 198 . 27 ASP HA H 4.961 . . 199 . 27 ASP HB2 H 3.115 . . 200 . 27 ASP HB3 H 3.061 . . 201 . 27 ASP CA C 52.701 . . 202 . 27 ASP CB C 40.512 . . 203 . 28 TYR H H 8.566 . . 204 . 28 TYR N N 117.692 . . 205 . 28 TYR HA H 5.918 . . 206 . 28 TYR HB3 H 2.451 . . 207 . 28 TYR HB2 H 2.816 . . 208 . 28 TYR HD1 H 6.775 . . 209 . 28 TYR CA C 56.137 . . 210 . 28 TYR CB C 42.703 . . 211 . 29 TYR H H 8.578 . . 212 . 29 TYR N N 115.295 . . 213 . 29 TYR HA H 4.405 . . 214 . 29 TYR HB2 H 2.968 . . 215 . 29 TYR HD1 H 6.810 . . 216 . 29 TYR CA C 56.762 . . 217 . 29 TYR CB C 40.204 . . 218 . 30 GLU H H 8.875 . . 219 . 30 GLU N N 119.744 . . 220 . 30 GLU HA H 5.102 . . 221 . 30 GLU HB3 H 2.019 . . 222 . 30 GLU HB2 H 2.270 . . 223 . 30 GLU HG2 H 2.538 . . 224 . 30 GLU HG3 H 2.622 . . 225 . 30 GLU CA C 54.575 . . 226 . 30 GLU CB C 29.581 . . 227 . 30 GLU CG C 33.097 . . 228 . 31 THR H H 8.217 . . 229 . 31 THR N N 112.539 . . 230 . 31 THR HA H 4.501 . . 231 . 31 THR HB H 4.969 . . 232 . 31 THR HG2 H 1.306 . . 233 . 31 THR CA C 62.073 . . 234 . 31 THR CB C 71.146 . . 235 . 31 THR CG2 C 22.948 . . 236 . 32 SER H H 8.883 . . 237 . 32 SER N N 115.186 . . 238 . 32 SER HA H 4.439 . . 239 . 32 SER HB3 H 3.952 . . 240 . 32 SER HB2 H 4.203 . . 241 . 32 SER CA C 58.637 . . 242 . 32 SER CB C 63.948 . . 243 . 33 SER H H 8.997 . . 244 . 33 SER N N 123.909 . . 245 . 33 SER HA H 4.342 . . 246 . 33 SER HB2 H 4.051 . . 247 . 33 SER HB3 H 4.012 . . 248 . 33 SER CA C 60.511 . . 249 . 33 SER CB C 62.386 . . 250 . 34 LEU H H 8.161 . . 251 . 34 LEU N N 120.151 . . 252 . 34 LEU HA H 4.281 . . 253 . 34 LEU HB2 H 1.581 . . 254 . 34 LEU HG H 1.589 . . 255 . 34 LEU HD1 H 0.827 . . 256 . 34 LEU HD2 H 0.784 . . 257 . 34 LEU CA C 55.750 . . 258 . 34 LEU CB C 42.078 . . 259 . 34 LEU CG C 27.132 . . 260 . 34 LEU CD1 C 25.000 . . 261 . 34 LEU CD2 C 22.828 . . 262 . 35 CYS H H 7.514 . . 263 . 35 CYS N N 118.485 . . 264 . 35 CYS HA H 4.670 . . 265 . 35 CYS HB3 H 2.733 . . 266 . 35 CYS HB2 H 3.597 . . 267 . 35 CYS CA C 54.263 . . 268 . 35 CYS CB C 38.642 . . 269 . 36 SER H H 8.741 . . 270 . 36 SER N N 118.146 . . 271 . 36 SER HA H 4.109 . . 272 . 36 SER HB2 H 3.922 . . 273 . 36 SER CA C 61.136 . . 274 . 36 SER CB C 62.698 . . 275 . 37 GLN H H 7.984 . . 276 . 37 GLN N N 118.329 . . 277 . 37 GLN HA H 4.902 . . 278 . 37 GLN HB2 H 1.898 . . 279 . 37 GLN HB3 H 1.945 . . 280 . 37 GLN HG2 H 2.217 . . 281 . 37 GLN HG3 H 2.083 . . 282 . 37 GLN CA C 52.388 . . 283 . 37 GLN CB C 29.269 . . 284 . 37 GLN CG C 32.393 . . 285 . 38 PRO HA H 4.465 . . 286 . 38 PRO HB3 H 1.806 . . 287 . 38 PRO HB2 H 2.204 . . 288 . 38 PRO HG2 H 1.988 . . 289 . 38 PRO HG3 H 2.001 . . 290 . 38 PRO HD2 H 3.737 . . 291 . 38 PRO HD3 H 3.643 . . 292 . 38 PRO CA C 62.522 . . 293 . 38 PRO CB C 32.706 . . 294 . 38 PRO CG C 27.092 . . 295 . 38 PRO CD C 50.573 . . 296 . 39 ALA H H 8.137 . . 297 . 39 ALA N N 120.856 . . 298 . 39 ALA HA H 4.855 . . 299 . 39 ALA HB H 1.600 . . 300 . 39 ALA CA C 52.701 . . 301 . 39 ALA CB C 24.554 . . 302 . 40 VAL H H 8.064 . . 303 . 40 VAL N N 121.123 . . 304 . 40 VAL HA H 4.140 . . 305 . 40 VAL HB H 1.134 . . 306 . 40 VAL HG2 H 0.560 . . 307 . 40 VAL HG1 H -0.114 . . 308 . 40 VAL CA C 61.761 . . 309 . 40 VAL CB C 33.955 . . 310 . 40 VAL CG2 C 21.729 . . 311 . 40 VAL CG1 C 21.100 . . 312 . 41 VAL H H 8.882 . . 313 . 41 VAL N N 126.885 . . 314 . 41 VAL HA H 4.536 . . 315 . 41 VAL HB H 0.576 . . 316 . 41 VAL HG1 H 0.555 . . 317 . 41 VAL HG2 H 0.570 . . 318 . 41 VAL CA C 60.199 . . 319 . 41 VAL CB C 31.996 . . 320 . 41 VAL CG1 C 22.047 . . 321 . 41 VAL CG2 C 22.370 . . 322 . 42 PHE H H 9.040 . . 323 . 42 PHE N N 123.337 . . 324 . 42 PHE HA H 5.248 . . 325 . 42 PHE HB3 H 2.809 . . 326 . 42 PHE HB2 H 3.031 . . 327 . 42 PHE HD1 H 7.260 . . 328 . 42 PHE CA C 57.074 . . 329 . 42 PHE CB C 41.453 . . 330 . 43 GLN H H 8.582 . . 331 . 43 GLN N N 121.044 . . 332 . 43 GLN HA H 5.133 . . 333 . 43 GLN HB2 H 2.055 . . 334 . 43 GLN HG2 H 2.393 . . 335 . 43 GLN HG3 H 2.357 . . 336 . 43 GLN CA C 54.888 . . 337 . 43 GLN CB C 30.209 . . 338 . 43 GLN CG C 34.178 . . 339 . 44 THR H H 8.922 . . 340 . 44 THR N N 115.843 . . 341 . 44 THR HA H 5.474 . . 342 . 44 THR HB H 4.167 . . 343 . 44 THR HG2 H 1.160 . . 344 . 44 THR CA C 59.574 . . 345 . 44 THR CB C 72.383 . . 346 . 44 THR CG2 C 21.567 . . 347 . 45 LYS H H 8.201 . . 348 . 45 LYS N N 118.804 . . 349 . 45 LYS HA H 4.064 . . 350 . 45 LYS HB3 H 1.639 . . 351 . 45 LYS HB2 H 1.846 . . 352 . 45 LYS HG2 H 1.426 . . 353 . 45 LYS HG3 H 1.351 . . 354 . 45 LYS HD2 H 1.680 . . 355 . 45 LYS HE2 H 2.863 . . 356 . 45 LYS CA C 58.324 . . 357 . 45 LYS CB C 32.706 . . 358 . 45 LYS CG C 26.145 . . 359 . 45 LYS CD C 29.074 . . 360 . 45 LYS CE C 42.105 . . 361 . 46 ARG H H 7.679 . . 362 . 46 ARG N N 115.776 . . 363 . 46 ARG HA H 4.511 . . 364 . 46 ARG HB2 H 1.628 . . 365 . 46 ARG HB3 H 2.069 . . 366 . 46 ARG HG2 H 1.562 . . 367 . 46 ARG HG3 H 1.665 . . 368 . 46 ARG HD2 H 3.193 . . 369 . 46 ARG CA C 55.618 . . 370 . 46 ARG CB C 30.206 . . 371 . 46 ARG CG C 27.452 . . 372 . 46 ARG CD C 43.066 . . 373 . 47 SER H H 7.888 . . 374 . 47 SER N N 112.539 . . 375 . 47 SER HA H 4.300 . . 376 . 47 SER HB2 H 3.949 . . 377 . 47 SER CA C 58.637 . . 378 . 47 SER CB C 62.323 . . 379 . 48 LYS H H 7.655 . . 380 . 48 LYS N N 119.885 . . 381 . 48 LYS HA H 4.520 . . 382 . 48 LYS HB2 H 1.767 . . 383 . 48 LYS HB3 H 1.841 . . 384 . 48 LYS HG2 H 1.448 . . 385 . 48 LYS HG3 H 1.346 . . 386 . 48 LYS HD2 H 1.661 . . 387 . 48 LYS HE2 H 2.981 . . 388 . 48 LYS CA C 55.200 . . 389 . 48 LYS CB C 33.490 . . 390 . 48 LYS CG C 24.870 . . 391 . 48 LYS CD C 28.713 . . 392 . 48 LYS CE C 42.285 . . 393 . 49 GLN H H 8.452 . . 394 . 49 GLN N N 120.339 . . 395 . 49 GLN HA H 5.038 . . 396 . 49 GLN HB2 H 1.946 . . 397 . 49 GLN HG2 H 2.272 . . 398 . 49 GLN HG3 H 2.358 . . 399 . 49 GLN CA C 55.496 . . 400 . 49 GLN CB C 30.581 . . 401 . 49 GLN CG C 34.238 . . 402 . 50 VAL H H 9.086 . . 403 . 50 VAL N N 124.634 . . 404 . 50 VAL HA H 4.385 . . 405 . 50 VAL HB H 2.205 . . 406 . 50 VAL HG1 H 1.203 . . 407 . 50 VAL HG2 H 1.037 . . 408 . 50 VAL CA C 61.761 . . 409 . 50 VAL CB C 34.893 . . 410 . 50 VAL CG1 C 21.458 . . 411 . 50 VAL CG2 C 21.146 . . 412 . 51 CYS H H 8.939 . . 413 . 51 CYS N N 126.325 . . 414 . 51 CYS HA H 4.875 . . 415 . 51 CYS HB2 H 2.929 . . 416 . 51 CYS HB3 H 3.716 . . 417 . 51 CYS CA C 58.324 . . 418 . 51 CYS CB C 47.702 . . 419 . 52 ALA H H 9.957 . . 420 . 52 ALA N N 127.603 . . 421 . 52 ALA HA H 4.995 . . 422 . 52 ALA HB H 1.275 . . 423 . 52 ALA CA C 50.826 . . 424 . 52 ALA CB C 24.270 . . 425 . 53 ASP H H 8.299 . . 426 . 53 ASP N N 121.248 . . 427 . 53 ASP HA H 3.570 . . 428 . 53 ASP HB2 H 1.595 . . 429 . 53 ASP HB3 H 2.490 . . 430 . 53 ASP CA C 50.191 . . 431 . 53 ASP CB C 39.266 . . 432 . 54 PRO HA H 3.893 . . 433 . 54 PRO HB3 H 1.888 . . 434 . 54 PRO HB2 H 2.099 . . 435 . 54 PRO HG2 H 1.699 . . 436 . 54 PRO HG3 H 1.802 . . 437 . 54 PRO HD2 H 3.633 . . 438 . 54 PRO HD3 H 4.189 . . 439 . 54 PRO CA C 63.635 . . 440 . 54 PRO CB C 32.081 . . 441 . 54 PRO CG C 27.152 . . 442 . 54 PRO CD C 51.233 . . 443 . 55 SER H H 7.429 . . 444 . 55 SER N N 109.675 . . 445 . 55 SER HA H 4.188 . . 446 . 55 SER HB2 H 3.751 . . 447 . 55 SER CA C 58.949 . . 448 . 55 SER CB C 63.323 . . 449 . 56 GLU H H 7.327 . . 450 . 56 GLU N N 121.013 . . 451 . 56 GLU HA H 4.202 . . 452 . 56 GLU HB3 H 1.739 . . 453 . 56 GLU HB2 H 1.794 . . 454 . 56 GLU HG2 H 2.487 . . 455 . 56 GLU HG3 H 2.342 . . 456 . 56 GLU CA C 55.363 . . 457 . 56 GLU CB C 28.957 . . 458 . 56 GLU CG C 33.517 . . 459 . 57 SER H H 9.014 . . 460 . 57 SER N N 120.997 . . 461 . 57 SER HA H 4.019 . . 462 . 57 SER HB2 H 3.992 . . 463 . 57 SER CA C 62.257 . . 464 . 57 SER CB C 62.257 . . 465 . 58 TRP H H 8.031 . . 466 . 58 TRP N N 119.278 . . 467 . 58 TRP HA H 4.305 . . 468 . 58 TRP HB2 H 3.076 . . 469 . 58 TRP NE1 N 130.240 . . 470 . 58 TRP HE1 H 9.910 . . 471 . 58 TRP HD1 H 7.570 . . 472 . 58 TRP HZ2 H 7.280 . . 473 . 58 TRP CA C 58.949 . . 474 . 58 TRP CB C 27.082 . . 475 . 59 VAL H H 5.688 . . 476 . 59 VAL N N 122.723 . . 477 . 59 VAL HA H 2.747 . . 478 . 59 VAL HB H 1.733 . . 479 . 59 VAL HG2 H -0.708 . . 480 . 59 VAL HG1 H 0.369 . . 481 . 59 VAL CA C 65.510 . . 482 . 59 VAL CB C 31.000 . . 483 . 59 VAL CG2 C 21.600 . . 484 . 59 VAL CG1 C 20.885 . . 485 . 60 GLN H H 7.172 . . 486 . 60 GLN N N 116.652 . . 487 . 60 GLN HA H 3.725 . . 488 . 60 GLN HB2 H 1.994 . . 489 . 60 GLN HG2 H 2.362 . . 490 . 60 GLN HG3 H 2.283 . . 491 . 60 GLN CA C 58.324 . . 492 . 60 GLN CB C 27.707 . . 493 . 60 GLN CG C 33.397 . . 494 . 61 GLU H H 8.169 . . 495 . 61 GLU N N 118.574 . . 496 . 61 GLU HA H 4.106 . . 497 . 61 GLU HB2 H 2.270 . . 498 . 61 GLU HG2 H 2.652 . . 499 . 61 GLU HG3 H 2.535 . . 500 . 61 GLU CA C 58.637 . . 501 . 61 GLU CB C 28.019 . . 502 . 61 GLU CG C 33.097 . . 503 . 62 TYR H H 8.409 . . 504 . 62 TYR N N 120.731 . . 505 . 62 TYR HA H 4.464 . . 506 . 62 TYR HB2 H 2.828 . . 507 . 62 TYR HB3 H 3.461 . . 508 . 62 TYR HD1 H 6.800 . . 509 . 62 TYR CA C 59.574 . . 510 . 62 TYR CB C 37.079 . . 511 . 63 VAL H H 8.187 . . 512 . 63 VAL N N 119.084 . . 513 . 63 VAL HA H 3.134 . . 514 . 63 VAL HB H 1.849 . . 515 . 63 VAL HG2 H 0.474 . . 516 . 63 VAL HG1 H 0.446 . . 517 . 63 VAL CA C 67.072 . . 518 . 63 VAL CB C 31.400 . . 519 . 63 VAL CG2 C 23.000 . . 520 . 63 VAL CG1 C 20.400 . . 521 . 64 TYR H H 7.836 . . 522 . 64 TYR N N 118.775 . . 523 . 64 TYR HA H 4.243 . . 524 . 64 TYR HB2 H 3.089 . . 525 . 64 TYR HB3 H 3.167 . . 526 . 64 TYR HD1 H 7.170 . . 527 . 64 TYR CA C 60.511 . . 528 . 64 TYR CB C 38.000 . . 529 . 65 ASP H H 8.341 . . 530 . 65 ASP N N 116.841 . . 531 . 65 ASP HA H 4.430 . . 532 . 65 ASP HB2 H 2.894 . . 533 . 65 ASP HB3 H 3.107 . . 534 . 65 ASP CA C 55.300 . . 535 . 65 ASP CB C 38.329 . . 536 . 66 LEU H H 8.220 . . 537 . 66 LEU N N 120.825 . . 538 . 66 LEU HA H 4.282 . . 539 . 66 LEU HB2 H 1.749 . . 540 . 66 LEU HB3 H 2.035 . . 541 . 66 LEU HG H 1.838 . . 542 . 66 LEU HD1 H 0.907 . . 543 . 66 LEU HD2 H 0.828 . . 544 . 66 LEU CA C 56.450 . . 545 . 66 LEU CB C 42.703 . . 546 . 66 LEU CG C 27.394 . . 547 . 66 LEU CD1 C 26.647 . . 548 . 66 LEU CD2 C 23.152 . . 549 . 67 GLU H H 8.110 . . 550 . 67 GLU N N 119.465 . . 551 . 67 GLU HA H 4.355 . . 552 . 67 GLU HB2 H 2.129 . . 553 . 67 GLU HB3 H 2.218 . . 554 . 67 GLU HG2 H 2.691 . . 555 . 67 GLU HG3 H 2.595 . . 556 . 67 GLU CA C 56.630 . . 557 . 67 GLU CB C 28.644 . . 558 . 67 GLU CG C 33.393 . . 559 . 68 LEU H H 7.718 . . 560 . 68 LEU N N 120.841 . . 561 . 68 LEU HA H 4.243 . . 562 . 68 LEU HB2 H 1.584 . . 563 . 68 LEU HG H 1.599 . . 564 . 68 LEU HD1 H 0.825 . . 565 . 68 LEU HD2 H 0.804 . . 566 . 68 LEU CA C 55.614 . . 567 . 68 LEU CB C 42.481 . . 568 . 68 LEU CG C 27.000 . . 569 . 68 LEU CD1 C 24.895 . . 570 . 68 LEU CD2 C 23.333 . . stop_ save_