data_7149 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of the Molten Globule of Human Serum Retinol-Binding Protein using NMR Spectroscopy ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greene Lesley H. . 2 Wijesinha-Bettoni Ramani . . 3 Redfield Christina . . stop_ _BMRB_accession_number 7149 _BMRB_flat_file_name bmr7149.str _Entry_type new _Submission_date 2006-06-06 _Accession_date 2006-06-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The entry contains the chemical shifts of backbone 15N and 1HN of RBP assigned in 8M urea at pH 2 and 20C. These assignments were obtained as part of the study of the unfolding of the pH 2 molten globule with urea. ; loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 174 "15N chemical shifts" 174 stop_ save_ ############################# # Citation for this entry # ############################# save_1 _Saveframe_category entry_citation _Citation_title ; Characterization of the molten globule of human serum retinol-binding protein using NMR spectroscopy. ; _Citation_status published _Citation_type journal _PubMed_ID 16878982 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greene Lesley H. . 2 Wijesinha-Bettoni Ramani . . 3 Redfield Christina . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 31 _Page_first 9475 _Page_last 9484 _Year 2006 loop_ _Keyword "retinol-binding protein" "molten globule" stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name RBP _Abbreviation_common RBP loop_ _Mol_system_component_name _Mol_label RBP $RBP stop_ _System_molecular_weight 21000 _System_physical_state unfolded _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all disulfide bound" loop_ _Biological_function "carrier of retinol" stop_ _Details "recombinant human serum retinol-binding protein" save_ ######################## # Monomeric polymers # ######################## save_RBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "human serum retinol-binding protein" _Name_variant RBP _Abbreviation_common RBP _Mol_thiol_state "all disulfide bound" loop_ _Biological_function "carrier of RBP" stop_ ############################## # Polymer residue sequence # ############################## _Residue_count 182 _Mol_residue_sequence ; ERDCRVSSFRVKENFDKARF SGTWYAMAKKDPEGLFLQDN IVAEFSVDETGQMSATAKGR VRLLNNWDVCADMVGTFTDT EDPAKFKMKYWGVASFLQKG NDDHWIVDTDYDTYAVQYSC RLLNLDGTCADSYSFVFSRD PNGLPPEAQKIVRQRQEELC LARQYRLIVHNGYCDGRSER NL ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ARG 3 ASP 4 CYS 5 ARG 6 VAL 7 SER 8 SER 9 PHE 10 ARG 11 VAL 12 LYS 13 GLU 14 ASN 15 PHE 16 ASP 17 LYS 18 ALA 19 ARG 20 PHE 21 SER 22 GLY 23 THR 24 TRP 25 TYR 26 ALA 27 MET 28 ALA 29 LYS 30 LYS 31 ASP 32 PRO 33 GLU 34 GLY 35 LEU 36 PHE 37 LEU 38 GLN 39 ASP 40 ASN 41 ILE 42 VAL 43 ALA 44 GLU 45 PHE 46 SER 47 VAL 48 ASP 49 GLU 50 THR 51 GLY 52 GLN 53 MET 54 SER 55 ALA 56 THR 57 ALA 58 LYS 59 GLY 60 ARG 61 VAL 62 ARG 63 LEU 64 LEU 65 ASN 66 ASN 67 TRP 68 ASP 69 VAL 70 CYS 71 ALA 72 ASP 73 MET 74 VAL 75 GLY 76 THR 77 PHE 78 THR 79 ASP 80 THR 81 GLU 82 ASP 83 PRO 84 ALA 85 LYS 86 PHE 87 LYS 88 MET 89 LYS 90 TYR 91 TRP 92 GLY 93 VAL 94 ALA 95 SER 96 PHE 97 LEU 98 GLN 99 LYS 100 GLY 101 ASN 102 ASP 103 ASP 104 HIS 105 TRP 106 ILE 107 VAL 108 ASP 109 THR 110 ASP 111 TYR 112 ASP 113 THR 114 TYR 115 ALA 116 VAL 117 GLN 118 TYR 119 SER 120 CYS 121 ARG 122 LEU 123 LEU 124 ASN 125 LEU 126 ASP 127 GLY 128 THR 129 CYS 130 ALA 131 ASP 132 SER 133 TYR 134 SER 135 PHE 136 VAL 137 PHE 138 SER 139 ARG 140 ASP 141 PRO 142 ASN 143 GLY 144 LEU 145 PRO 146 PRO 147 GLU 148 ALA 149 GLN 150 LYS 151 ILE 152 VAL 153 ARG 154 GLN 155 ARG 156 GLN 157 GLU 158 GLU 159 LEU 160 CYS 161 LEU 162 ALA 163 ARG 164 GLN 165 TYR 166 ARG 167 LEU 168 ILE 169 VAL 170 HIS 171 ASN 172 GLY 173 TYR 174 CYS 175 ASP 176 GLY 177 ARG 178 SER 179 GLU 180 ARG 181 ASN 182 LEU 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 1BRP "Crystal Structure Of The Trigonal Form Of Human Plasma Retinol-Binding Protein At 2.5 Angstroms Resolution" 100.00 182 100.00 100.00 7.32e-105 PDB 1BRQ "Crystal Structure Of The Trigonal Form Of Human Plasma Retinol-Binding Protein At 2.5 Angstroms Resolution" 100.00 182 100.00 100.00 7.32e-105 PDB 1JYD "Crystal Structure Of Recombinant Human Serum Retinol- Binding Protein At 1.7 A Resolution" 100.00 183 100.00 100.00 6.20e-105 PDB 1JYJ "Crystal Structure Of A Double Variant (W67lW91H) OF Recombinant Human Serum Retinol-Binding Protein At 2.0 A Resolution" 100.00 183 98.90 98.90 5.25e-103 PDB 1QAB "The Structure Of Human Retinol Binding Protein With Its Carrier Protein Transthyretin Reveals Interaction With The Carboxy Terminus Of Rbp" 98.35 180 98.32 98.32 3.35e-101 PDB 1RBP "Crystallographic Refinement Of Human Serum Retinol Binding Protein At 2 Angstroms Resolution" 100.00 182 100.00 100.00 7.32e-105 DBJ BAD16621 "retinol binding protein4 [Pan troglodytes]" 100.00 201 100.00 100.00 4.95e-105 EMBL CAA24959 "unnamed protein product [Homo sapiens]" 100.00 199 100.00 100.00 4.26e-105 EMBL CAA26553 "RBP [Homo sapiens]" 54.95 116 100.00 100.00 7.37e-53 EMBL CAH72328 "retinol binding protein 4, plasma [Homo sapiens]" 100.00 201 100.00 100.00 4.95e-105 EMBL CAH72329 "retinol binding protein 4, plasma [Homo sapiens]" 100.00 199 100.00 100.00 3.49e-105 GenBank AAF69622 "PRO2222 [Homo sapiens]" 85.71 157 100.00 100.00 6.83e-89 GenBank AAH20633 "Retinol binding protein 4, plasma [Homo sapiens]" 100.00 201 100.00 100.00 5.42e-105 GenBank ABC69164 "retinol-binding protein [Sus scrofa]" 54.95 118 98.00 98.00 1.03e-51 GenBank ABM82307 "retinol binding protein 4, plasma [synthetic construct]" 100.00 201 100.00 100.00 5.42e-105 GenBank ABM85484 "retinol binding protein 4, plasma [synthetic construct]" 100.00 201 100.00 100.00 5.42e-105 PRF 1401251A "retinol binding protein" 100.00 182 100.00 100.00 7.32e-105 REF NP_001038960 "retinol-binding protein 4, plasma [Pan troglodytes]" 100.00 201 100.00 100.00 4.95e-105 REF NP_006735 "retinol-binding protein 4, plasma precursor [Homo sapiens]" 100.00 201 100.00 100.00 4.95e-105 SWISS-PROT P02753 "Plasma retinol-binding protein precursor (PRBP) (RBP) [Contains: Plasma retinol-binding protein(1-182); Plasma retinol-binding protein(1-181); Plasma retinol-binding protein(1-179); Plasma retinol-binding protein(1-176)]" 100.00 201 100.00 100.00 4.95e-105 SWISS-PROT P61641 "Plasma retinol-binding protein precursor (PRBP) (RBP)" 100.00 201 100.00 100.00 4.95e-105 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide RBP 4 CYS SG RBP 160 CYS SG single disulfide RBP 70 CYS SG RBP 174 CYS SG single disulfide RBP 120 CYS SG RBP 129 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RBP 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 $RBP "recombinant technology" E.coli ? ? ? ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 0.16mM 15N,2H-labeled RBP in 5mM sodium phosphate and 8M urea at pH 2 and 20C. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RBP 0.16 mM "[U-15N; U-2H]" "sodium phosphate" 5 mM ? urea 8 M ? stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name Felix _Version 2.3 loop_ _Vendor _Address _Electronic_address Accelrys "San Diego, CA" ? stop_ loop_ _Task processing stop_ _Details "used for processing of spectra" save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_750_MHz _Saveframe_category NMR_spectrometer _Manufacturer Home-built _Model ? _Field_strength 750 _Details ; home-built 750MHz spectrometer equipped with a triple-axis gradient probe uses Omega software ; save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H15N HSQC ; save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details "8M urea" loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2 0.05 pH temperature 293 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference 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 dioxane H 1 "methylene protons" ppm 3.743 direct internal ? ? ? 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 # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details ; 1HN and 15N backbone shifts are reported for RBP at pH 2 and 8M urea. ; loop_ _Experiment_label $1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name RBP loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 GLU H H 8.932 0.01 1 2 1 1 GLU N N 123.789 0.10 1 3 2 2 ARG H H 8.657 0.01 1 4 2 2 ARG N N 122.907 0.10 1 5 3 3 ASP H H 8.678 0.01 1 6 3 3 ASP N N 119.960 0.10 1 7 4 4 CYS H H 8.474 0.01 1 8 4 4 CYS N N 119.095 0.10 1 9 5 5 ARG H H 8.590 0.01 1 10 5 5 ARG N N 122.608 0.10 1 11 6 6 VAL H H 8.365 0.01 1 12 6 6 VAL N N 121.895 0.10 1 13 7 7 SER H H 8.501 0.01 1 14 7 7 SER N N 119.410 0.10 1 15 8 8 SER H H 8.403 0.01 1 16 8 8 SER N N 117.887 0.10 1 17 9 9 PHE H H 8.278 0.01 1 18 9 9 PHE N N 122.057 0.10 1 19 10 10 ARG H H 8.305 0.01 1 20 10 10 ARG N N 123.241 0.10 1 21 11 11 VAL H H 8.219 0.01 1 22 11 11 VAL N N 121.804 0.10 1 23 12 12 LYS H H 8.490 0.01 1 24 12 12 LYS N N 125.351 0.10 1 25 13 13 GLU H H 8.434 0.01 1 26 13 13 GLU N N 121.893 0.10 1 27 14 14 ASN H H 8.514 0.01 1 28 14 14 ASN N N 120.183 0.10 1 29 15 15 PHE H H 8.334 0.01 1 30 15 15 PHE N N 120.895 0.10 1 31 16 16 ASP H H 8.534 0.01 1 32 16 16 ASP N N 120.166 0.10 1 33 17 17 LYS H H 8.241 0.01 1 34 17 17 LYS N N 121.961 0.10 1 35 18 18 ALA H H 8.234 0.01 1 36 18 18 ALA N N 124.293 0.10 1 37 19 19 ARG H H 8.215 0.01 1 38 19 19 ARG N N 120.042 0.10 1 39 20 20 PHE H H 8.334 0.01 1 40 20 20 PHE N N 120.895 0.10 1 41 21 21 SER H H 8.377 0.01 1 42 21 21 SER N N 117.853 0.10 1 43 22 22 GLY H H 7.882 0.01 1 44 22 22 GLY N N 109.845 0.10 1 45 23 23 THR H H 8.093 0.01 1 46 23 23 THR N N 113.729 0.10 1 47 24 24 TRP H H 8.252 0.01 1 48 24 24 TRP N N 123.686 0.10 1 49 25 25 TYR H H 7.830 0.01 1 50 25 25 TYR N N 121.362 0.10 1 51 26 26 ALA H H 8.046 0.01 1 52 26 26 ALA N N 124.476 0.10 1 53 27 27 MET H H 8.153 0.01 1 54 27 27 MET N N 119.083 0.10 1 55 28 28 ALA H H 8.268 0.01 1 56 28 28 ALA N N 124.887 0.10 1 57 29 29 LYS H H 8.317 0.01 1 58 29 29 LYS N N 120.672 0.10 1 59 30 30 LYS H H 8.385 0.01 1 60 30 30 LYS N N 122.106 0.10 1 61 31 31 ASP H H 8.698 0.01 1 62 31 31 ASP N N 120.652 0.10 1 63 33 33 GLU H H 8.328 0.01 1 64 33 33 GLU N N 118.888 0.10 1 65 34 34 GLY H H 8.285 0.01 1 66 34 34 GLY N N 108.930 0.10 1 67 35 35 LEU H H 7.988 0.01 1 68 35 35 LEU N N 121.168 0.10 1 69 36 36 PHE H H 8.377 0.01 1 70 36 36 PHE N N 120.935 0.10 1 71 37 37 LEU H H 8.248 0.01 1 72 37 37 LEU N N 123.764 0.10 1 73 38 38 GLN H H 8.406 0.01 1 74 38 38 GLN N N 120.539 0.10 1 75 39 39 ASP H H 8.540 0.01 1 76 39 39 ASP N N 119.534 0.10 1 77 40 40 ASN H H 8.474 0.01 1 78 40 40 ASN N N 119.095 0.10 1 79 41 41 ILE H H 8.058 0.01 1 80 41 41 ILE N N 120.854 0.10 1 81 42 42 VAL H H 8.199 0.01 1 82 42 42 VAL N N 123.957 0.10 1 83 43 43 ALA H H 8.303 0.01 1 84 43 43 ALA N N 127.165 0.10 1 85 44 44 GLU H H 8.232 0.01 1 86 44 44 GLU N N 119.366 0.10 1 87 45 45 PHE H H 8.232 0.01 1 88 45 45 PHE N N 119.955 0.10 1 89 46 46 SER H H 8.317 0.01 1 90 46 46 SER N N 117.147 0.10 1 91 47 47 VAL H H 8.207 0.01 1 92 47 47 VAL N N 120.966 0.10 1 93 48 48 ASP H H 8.529 0.01 1 94 48 48 ASP N N 121.334 0.10 1 95 49 49 GLU H H 8.377 0.01 1 96 49 49 GLU N N 120.935 0.10 1 97 50 50 THR H H 8.191 0.01 1 98 50 50 THR N N 113.772 0.10 1 99 51 51 GLY H H 8.392 0.01 1 100 51 51 GLY N N 110.294 0.10 1 101 52 52 GLN H H 8.291 0.01 1 102 52 52 GLN N N 119.586 0.10 1 103 53 53 MET H H 8.529 0.01 1 104 53 53 MET N N 121.334 0.10 1 105 54 54 SER H H 8.407 0.01 1 106 54 54 SER N N 116.802 0.10 1 107 55 55 ALA H H 8.498 0.01 1 108 55 55 ALA N N 125.808 0.10 1 109 56 56 THR H H 8.078 0.01 1 110 56 56 THR N N 111.702 0.10 1 111 57 57 ALA H H 8.215 0.01 1 112 57 57 ALA N N 125.861 0.10 1 113 58 58 LYS H H 8.318 0.01 1 114 58 58 LYS N N 120.318 0.10 1 115 59 59 GLY H H 8.367 0.01 1 116 59 59 GLY N N 109.256 0.10 1 117 60 60 ARG H H 8.242 0.01 1 118 60 60 ARG N N 120.541 0.10 1 119 61 61 VAL H H 8.519 0.01 1 120 61 61 VAL N N 125.417 0.10 1 121 62 62 ARG H H 8.290 0.01 1 122 62 62 ARG N N 121.317 0.10 1 123 63 63 LEU H H 8.399 0.01 1 124 63 63 LEU N N 123.306 0.10 1 125 64 64 LEU H H 8.429 0.01 1 126 64 64 LEU N N 124.610 0.10 1 127 65 65 ASN H H 8.474 0.01 1 128 65 65 ASN N N 119.095 0.10 1 129 66 66 ASN H H 8.397 0.01 1 130 66 66 ASN N N 118.942 0.10 1 131 67 67 TRP H H 8.096 0.01 1 132 67 67 TRP N N 120.356 0.10 1 133 68 68 ASP H H 8.304 0.01 1 134 68 68 ASP N N 119.832 0.10 1 135 69 69 VAL H H 7.929 0.01 1 136 69 69 VAL N N 119.377 0.10 1 137 70 70 CYS H H 8.354 0.01 1 138 70 70 CYS N N 120.346 0.10 1 139 71 71 ALA H H 8.268 0.01 1 140 71 71 ALA N N 124.526 0.10 1 141 72 72 ASP H H 8.371 0.01 1 142 72 72 ASP N N 117.254 0.10 1 143 73 73 MET H H 8.317 0.01 1 144 73 73 MET N N 120.672 0.10 1 145 74 74 VAL H H 8.156 0.01 1 146 74 74 VAL N N 120.644 0.10 1 147 75 75 GLY H H 8.429 0.01 1 148 75 75 GLY N N 111.790 0.10 1 149 76 76 THR H H 8.023 0.01 1 150 76 76 THR N N 113.326 0.10 1 151 77 77 PHE H H 8.405 0.01 1 152 77 77 PHE N N 122.204 0.10 1 153 78 78 THR H H 8.197 0.01 1 154 78 78 THR N N 115.536 0.10 1 155 79 79 ASP H H 8.508 0.01 1 156 79 79 ASP N N 121.095 0.10 1 157 80 80 THR H H 8.185 0.01 1 158 80 80 THR N N 114.032 0.10 1 159 81 81 GLU H H 8.290 0.01 1 160 81 81 GLU N N 121.317 0.10 1 161 82 82 ASP H H 8.523 0.01 1 162 82 82 ASP N N 119.950 0.10 1 163 84 84 ALA H H 8.180 0.01 1 164 84 84 ALA N N 122.854 0.10 1 165 85 85 LYS H H 8.125 0.01 1 166 85 85 LYS N N 119.577 0.10 1 167 86 86 PHE H H 8.125 0.01 1 168 86 86 PHE N N 120.175 0.10 1 169 87 87 LYS H H 8.324 0.01 1 170 87 87 LYS N N 123.106 0.10 1 171 88 88 MET H H 8.405 0.01 1 172 88 88 MET N N 122.204 0.10 1 173 89 89 LYS H H 8.423 0.01 1 174 89 89 LYS N N 122.965 0.10 1 175 90 90 TYR H H 8.247 0.01 1 176 90 90 TYR N N 121.114 0.10 1 177 91 91 TRP H H 8.248 0.01 1 178 91 91 TRP N N 123.401 0.10 1 179 92 92 GLY H H 7.851 0.01 1 180 92 92 GLY N N 109.577 0.10 1 181 93 93 VAL H H 7.993 0.01 1 182 93 93 VAL N N 118.729 0.10 1 183 94 94 ALA H H 8.399 0.01 1 184 94 94 ALA N N 126.967 0.10 1 185 95 95 SER H H 8.215 0.01 1 186 95 95 SER N N 114.872 0.10 1 187 96 96 PHE H H 8.163 0.01 1 188 96 96 PHE N N 121.293 0.10 1 189 97 97 LEU H H 8.105 0.01 1 190 97 97 LEU N N 122.901 0.10 1 191 98 98 GLN H H 8.339 0.01 1 192 98 98 GLN N N 121.382 0.10 1 193 99 99 LYS H H 8.445 0.01 1 194 99 99 LYS N N 122.968 0.10 1 195 100 100 GLY H H 8.408 0.01 1 196 100 100 GLY N N 109.520 0.10 1 197 101 101 ASN H H 8.375 0.01 1 198 101 101 ASN N N 118.270 0.10 1 199 102 102 ASP H H 8.551 0.01 1 200 102 102 ASP N N 118.933 0.10 1 201 103 103 ASP H H 8.396 0.01 1 202 103 103 ASP N N 118.636 0.10 1 203 104 104 HIS H H 8.352 0.01 1 204 104 104 HIS N N 118.370 0.10 1 205 105 105 TRP H H 8.133 0.01 1 206 105 105 TRP N N 121.729 0.10 1 207 106 106 ILE H H 8.188 0.01 1 208 106 106 ILE N N 122.796 0.10 1 209 107 107 VAL H H 8.199 0.01 1 210 107 107 VAL N N 123.957 0.10 1 211 108 108 ASP H H 8.608 0.01 1 212 108 108 ASP N N 122.770 0.10 1 213 109 109 THR H H 8.186 0.01 1 214 109 109 THR N N 114.379 0.10 1 215 110 110 ASP H H 8.372 0.01 1 216 110 110 ASP N N 120.214 0.10 1 217 111 111 TYR H H 8.096 0.01 1 218 111 111 TYR N N 120.356 0.10 1 219 112 112 ASP H H 8.414 0.01 1 220 112 112 ASP N N 119.871 0.10 1 221 113 113 THR H H 8.063 0.01 1 222 113 113 THR N N 114.146 0.10 1 223 114 114 TYR H H 8.058 0.01 1 224 114 114 TYR N N 121.199 0.10 1 225 115 115 ALA H H 8.123 0.01 1 226 115 115 ALA N N 124.667 0.10 1 227 116 116 VAL H H 8.044 0.01 1 228 116 116 VAL N N 119.447 0.10 1 229 117 117 GLN H H 8.436 0.01 1 230 117 117 GLN N N 123.202 0.10 1 231 118 118 TYR H H 8.290 0.01 1 232 118 118 TYR N N 121.317 0.10 1 233 119 119 SER H H 8.377 0.01 1 234 119 119 SER N N 116.593 0.10 1 235 120 120 CYS H H 8.550 0.01 1 236 120 120 CYS N N 121.152 0.10 1 237 121 121 ARG H H 8.648 0.01 1 238 121 121 ARG N N 124.183 0.10 1 239 122 122 LEU H H 7.949 0.01 1 240 122 122 LEU N N 120.568 0.10 1 241 123 123 LEU H H 8.542 0.01 1 242 123 123 LEU N N 123.784 0.10 1 243 124 124 ASN H H 8.579 0.01 1 244 124 124 ASN N N 118.271 0.10 1 245 125 125 LEU H H 8.555 0.01 1 246 125 125 LEU N N 121.668 0.10 1 247 126 126 ASP H H 8.252 0.01 1 248 126 126 ASP N N 114.734 0.10 1 249 127 127 GLY H H 8.125 0.01 1 250 127 127 GLY N N 107.238 0.10 1 251 128 128 THR H H 7.730 0.01 1 252 128 128 THR N N 110.813 0.10 1 253 129 129 CYS H H 8.787 0.01 1 254 129 129 CYS N N 120.067 0.10 1 255 130 130 ALA H H 8.720 0.01 1 256 130 130 ALA N N 127.176 0.10 1 257 131 131 ASP H H 8.377 0.01 1 258 131 131 ASP N N 117.853 0.10 1 259 132 132 SER H H 8.312 0.01 1 260 132 132 SER N N 116.274 0.10 1 261 133 133 TYR H H 8.215 0.01 1 262 133 133 TYR N N 121.521 0.10 1 263 134 134 SER H H 8.190 0.01 1 264 134 134 SER N N 116.607 0.10 1 265 135 135 PHE H H 8.200 0.01 1 266 135 135 PHE N N 122.254 0.10 1 267 136 136 VAL H H 8.014 0.01 1 268 136 136 VAL N N 121.618 0.10 1 269 137 137 PHE H H 8.285 0.01 1 270 137 137 PHE N N 123.562 0.10 1 271 138 138 SER H H 8.305 0.01 1 272 138 138 SER N N 117.026 0.10 1 273 139 139 ARG H H 8.398 0.01 1 274 139 139 ARG N N 122.572 0.10 1 275 140 140 ASP H H 8.583 0.01 1 276 140 140 ASP N N 119.824 0.10 1 277 142 142 ASN H H 8.305 0.01 1 278 142 142 ASN N N 117.026 0.10 1 279 143 143 GLY H H 8.136 0.01 1 280 143 143 GLY N N 108.095 0.10 1 281 144 144 LEU H H 8.108 0.01 1 282 144 144 LEU N N 122.119 0.10 1 283 147 147 GLU H H 8.433 0.01 1 284 147 147 GLU N N 119.725 0.10 1 285 148 148 ALA H H 8.359 0.01 1 286 148 148 ALA N N 124.773 0.10 1 287 149 149 GLN H H 8.375 0.01 1 288 149 149 GLN N N 119.544 0.10 1 289 150 150 LYS H H 8.440 0.01 1 290 150 150 LYS N N 122.689 0.10 1 291 151 151 ILE H H 8.324 0.01 1 292 151 151 ILE N N 123.106 0.10 1 293 152 152 VAL H H 8.391 0.01 1 294 152 152 VAL N N 125.592 0.10 1 295 153 153 ARG H H 8.519 0.01 1 296 153 153 ARG N N 125.417 0.10 1 297 154 154 GLN H H 8.582 0.01 1 298 154 154 GLN N N 121.699 0.10 1 299 155 155 ARG H H 8.576 0.01 1 300 155 155 ARG N N 122.745 0.10 1 301 156 156 GLN H H 8.537 0.01 1 302 156 156 GLN N N 121.963 0.10 1 303 157 157 GLU H H 8.530 0.01 1 304 157 157 GLU N N 121.726 0.10 1 305 159 159 LEU H H 8.415 0.01 1 306 159 159 LEU N N 123.306 0.10 1 307 160 160 CYS H H 8.603 0.01 1 308 160 160 CYS N N 119.443 0.10 1 309 161 161 LEU H H 8.460 0.01 1 310 161 161 LEU N N 123.749 0.10 1 311 162 162 ALA H H 8.425 0.01 1 312 162 162 ALA N N 125.374 0.10 1 313 164 164 GLN H H 8.463 0.01 1 314 164 164 GLN N N 121.165 0.10 1 315 165 165 TYR H H 8.278 0.01 1 316 165 165 TYR N N 121.472 0.10 1 317 166 166 ARG H H 8.389 0.01 1 318 166 166 ARG N N 122.790 0.10 1 319 167 167 LEU H H 8.344 0.01 1 320 167 167 LEU N N 124.189 0.10 1 321 168 168 ILE H H 8.396 0.01 1 322 168 168 ILE N N 123.898 0.10 1 323 169 169 VAL H H 8.294 0.01 1 324 169 169 VAL N N 124.937 0.10 1 325 170 170 HIS H H 8.740 0.01 1 326 170 170 HIS N N 122.689 0.10 1 327 171 171 ASN H H 8.620 0.01 1 328 171 171 ASN N N 120.704 0.10 1 329 172 172 GLY H H 8.434 0.01 1 330 172 172 GLY N N 109.075 0.10 1 331 173 173 TYR H H 8.171 0.01 1 332 173 173 TYR N N 119.795 0.10 1 333 174 174 CYS H H 8.540 0.01 1 334 174 174 CYS N N 119.534 0.10 1 335 176 176 GLY H H 8.345 0.01 1 336 176 176 GLY N N 108.901 0.10 1 337 177 177 ARG H H 8.168 0.01 1 338 177 177 ARG N N 120.088 0.10 1 339 178 178 SER H H 8.459 0.01 1 340 178 178 SER N N 116.708 0.10 1 341 179 179 GLU H H 8.461 0.01 1 342 179 179 GLU N N 122.164 0.10 1 343 180 180 ARG H H 8.393 0.01 1 344 180 180 ARG N N 121.409 0.10 1 345 181 181 ASN H H 8.540 0.01 1 346 181 181 ASN N N 119.534 0.10 1 347 182 182 LEU H H 8.282 0.01 1 348 182 182 LEU N N 122.573 0.10 1 stop_ save_