data_5666 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C backbone assignment of the Green Fluorescent Protein (GFP) ; _BMRB_accession_number 5666 _BMRB_flat_file_name bmr5666.str _Entry_type original _Submission_date 2003-01-22 _Accession_date 2003-01-23 _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 Khan Farid . . 2 Stott Katherine . . 3 Jackson Sophie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 199 "13C chemical shifts" 588 "15N chemical shifts" 199 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-10 original BMRB . stop_ _Original_release_date 2003-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N and 13C backbone assignment of the Green Fluorescent Protein (GFP) ; _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 Khan Farid . . 2 Stott Katherine . . 3 Jackson Sophie . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 26 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 281 _Page_last 282 _Year 2003 _Details . loop_ _Keyword GFP NMR assignment chromophore stop_ save_ ################################## # Molecular system description # ################################## save_system_GFP _Saveframe_category molecular_system _Mol_system_name 'truncated GFPuv' _Abbreviation_common GFP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GFP monomer' $GFP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GFP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Green Fluorescent Protein' _Name_variant 'truncated GFPuv' _Abbreviation_common GFP _Molecular_mass . _Mol_thiol_state 'all free' _Details ; Residues 65S, 66Y and 67G are catalytically cyclised and then oxidised to form the chromophore. ; ############################## # Polymer residue sequence # ############################## _Residue_count 229 _Mol_residue_sequence ; GSKGEELFTGVVPILVELDG DVNGHKFSVSGEGEGDATYG KLTLKFICTTGKLPVPWPTL VTTFSYGVQCFSRYPDHMKR HDFFKSAMPEGYVQERTISF KDDGNYKTRAEVKFEGDTLV NRIELKGIDFKEDGNILGHK LEYNYNSHNVYITADKQKNG IKANFKIRHNIEDGSVQLAD HYQQNTPIGDGPVLLPDNHY LSTQSALSKDPNEKRDHMVL LEFVTAAGI ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 LYS 4 GLY 5 GLU 6 GLU 7 LEU 8 PHE 9 THR 10 GLY 11 VAL 12 VAL 13 PRO 14 ILE 15 LEU 16 VAL 17 GLU 18 LEU 19 ASP 20 GLY 21 ASP 22 VAL 23 ASN 24 GLY 25 HIS 26 LYS 27 PHE 28 SER 29 VAL 30 SER 31 GLY 32 GLU 33 GLY 34 GLU 35 GLY 36 ASP 37 ALA 38 THR 39 TYR 40 GLY 41 LYS 42 LEU 43 THR 44 LEU 45 LYS 46 PHE 47 ILE 48 CYS 49 THR 50 THR 51 GLY 52 LYS 53 LEU 54 PRO 55 VAL 56 PRO 57 TRP 58 PRO 59 THR 60 LEU 61 VAL 62 THR 63 THR 64 PHE 65 SER 66 TYR 67 GLY 68 VAL 69 GLN 70 CYS 71 PHE 72 SER 73 ARG 74 TYR 75 PRO 76 ASP 77 HIS 78 MET 79 LYS 80 ARG 81 HIS 82 ASP 83 PHE 84 PHE 85 LYS 86 SER 87 ALA 88 MET 89 PRO 90 GLU 91 GLY 92 TYR 93 VAL 94 GLN 95 GLU 96 ARG 97 THR 98 ILE 99 SER 100 PHE 101 LYS 102 ASP 103 ASP 104 GLY 105 ASN 106 TYR 107 LYS 108 THR 109 ARG 110 ALA 111 GLU 112 VAL 113 LYS 114 PHE 115 GLU 116 GLY 117 ASP 118 THR 119 LEU 120 VAL 121 ASN 122 ARG 123 ILE 124 GLU 125 LEU 126 LYS 127 GLY 128 ILE 129 ASP 130 PHE 131 LYS 132 GLU 133 ASP 134 GLY 135 ASN 136 ILE 137 LEU 138 GLY 139 HIS 140 LYS 141 LEU 142 GLU 143 TYR 144 ASN 145 TYR 146 ASN 147 SER 148 HIS 149 ASN 150 VAL 151 TYR 152 ILE 153 THR 154 ALA 155 ASP 156 LYS 157 GLN 158 LYS 159 ASN 160 GLY 161 ILE 162 LYS 163 ALA 164 ASN 165 PHE 166 LYS 167 ILE 168 ARG 169 HIS 170 ASN 171 ILE 172 GLU 173 ASP 174 GLY 175 SER 176 VAL 177 GLN 178 LEU 179 ALA 180 ASP 181 HIS 182 TYR 183 GLN 184 GLN 185 ASN 186 THR 187 PRO 188 ILE 189 GLY 190 ASP 191 GLY 192 PRO 193 VAL 194 LEU 195 LEU 196 PRO 197 ASP 198 ASN 199 HIS 200 TYR 201 LEU 202 SER 203 THR 204 GLN 205 SER 206 ALA 207 LEU 208 SER 209 LYS 210 ASP 211 PRO 212 ASN 213 GLU 214 LYS 215 ARG 216 ASP 217 HIS 218 MET 219 VAL 220 LEU 221 LEU 222 GLU 223 PHE 224 VAL 225 THR 226 ALA 227 ALA 228 GLY 229 ILE 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 5514 'green fluorescent protein uv' 99.13 239 100.00 100.00 2.47e-131 PDB 1GFL 'Structure Of Green Fluorescent Protein' 100.00 238 98.25 98.25 5.24e-130 PDB 1QY3 'Crystal Structure Of Precyclized Intermediate For The Green Fluorescent Protein R96a Variant (B)' 99.56 229 98.25 99.12 7.38e-130 PDB 1QYO 'Anaerobic Precylization Intermediate Crystal Structure For S65g Y66g Gfp Variant' 99.56 238 98.25 98.68 4.19e-129 DBJ BAA93576 'GFPuv4 [Cloning vector pGFPTA]' 99.56 262 98.68 99.12 1.32e-130 DBJ BAE45350 'cyan fluorescent protein fusion protein [Cloning vector p3216PCbeta]' 99.56 275 98.25 98.68 1.27e-129 DBJ BAG30881 'green fluorescent protein UV5 [synthetic construct]' 99.56 238 98.25 98.68 1.04e-129 EMBL CAA10279 'green flourescent protein [Cloning vector pOT1]' 99.56 238 100.00 100.00 4.82e-132 EMBL CAA65278 'green fluorescent protein [unidentified]' 99.13 238 98.68 98.68 2.37e-129 EMBL CAB61435 'green flourescent protein [Integration vector pSMUG+]' 99.56 274 98.25 98.25 1.25e-129 EMBL CAB70975 'green fluorescent protein [Synechocystis promoter probe vector pIGA]' 99.56 238 100.00 100.00 4.82e-132 EMBL CAC27829 'green fluorescent protein [Cloning vector pOT2]' 99.56 238 100.00 100.00 4.82e-132 GenBank AAA27721 'green-fluorescent protein' 99.56 238 98.25 98.68 1.91e-129 GenBank AAA69542 'green fluorescent protein' 99.13 242 98.24 98.24 5.99e-129 GenBank AAA69544 'green fluorescent protein' 99.13 242 98.24 98.24 5.99e-129 GenBank AAA69546 'green fluorescent protein' 99.13 264 98.68 98.68 1.64e-129 GenBank AAA69548 'green fluorescent protein' 99.13 242 98.24 98.24 5.99e-129 SWISS-PROT P42212 'Green fluorescent protein' 99.56 238 98.25 98.68 1.91e-129 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GFP jellyfish 6100 Eukaryota Metazoa Aequorea victoria 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 $GFP '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 _Isotopic_labeling $GFP 1.0 mM '[U-95% 13C; U-95% 15N]' 'sodium chloride' 137 mM . 'potassium chloride' 2.7 mM . 'sodium phosphate' 6.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GFP 1.0 mM '[U-95% 13C; U-95% 15N; U-75% 2H]' 'sodium chloride' 137 mM . 'potassium chloride' 2.7 mM . 'sodium phosphate' 6.0 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_Experimental_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 na temperature 310 0.5 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 . . . 1.000000000 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 HNCA HN(CO)CA HNCACB HN(CO)CACB HNCO stop_ _Sample_conditions_label $Experimental_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GFP monomer' _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 SER C C 174.37 0.1 1 2 . 3 LYS N N 121.91 0.05 1 3 . 3 LYS H H 8.547 0.01 1 4 . 3 LYS CA C 56.87 0.1 1 5 . 3 LYS C C 178.16 0.1 1 6 . 3 LYS CB C 33.71 0.2 1 7 . 4 GLY N N 109.37 0.05 1 8 . 4 GLY H H 8.230 0.01 1 9 . 4 GLY CA C 47.35 0.1 1 10 . 4 GLY C C 176.01 0.1 1 11 . 5 GLU N N 119.36 0.05 1 12 . 5 GLU H H 8.399 0.01 1 13 . 5 GLU CA C 59.58 0.1 1 14 . 5 GLU C C 179.03 0.1 1 15 . 5 GLU CB C 29.49 0.2 1 16 . 6 GLU N N 118.57 0.05 1 17 . 6 GLU H H 7.969 0.01 1 18 . 6 GLU CA C 58.41 0.1 1 19 . 6 GLU C C 177.88 0.1 1 20 . 6 GLU CB C 29.68 0.2 1 21 . 7 LEU N N 117.15 0.05 1 22 . 7 LEU H H 7.547 0.01 1 23 . 7 LEU CA C 55.99 0.1 1 24 . 7 LEU C C 177.24 0.1 1 25 . 7 LEU CB C 41.61 0.2 1 26 . 8 PHE N N 113.66 0.05 1 27 . 8 PHE H H 7.588 0.01 1 28 . 8 PHE CA C 58.23 0.1 1 29 . 8 PHE C C 176.47 0.1 1 30 . 8 PHE CB C 39.57 0.2 1 31 . 9 THR N N 113.16 0.05 1 32 . 9 THR H H 7.436 0.01 1 33 . 9 THR CA C 63.99 0.1 1 34 . 9 THR C C 174.28 0.1 1 35 . 9 THR CB C 69.03 0.2 1 36 . 10 GLY N N 111.30 0.05 1 37 . 10 GLY H H 8.149 0.01 1 38 . 10 GLY CA C 44.20 0.1 1 39 . 10 GLY C C 172.49 0.1 1 40 . 11 VAL N N 120.98 0.05 1 41 . 11 VAL H H 8.241 0.01 1 42 . 11 VAL CA C 63.38 0.1 1 43 . 11 VAL C C 176.97 0.1 1 44 . 11 VAL CB C 32.05 0.2 1 45 . 12 VAL N N 131.56 0.05 1 46 . 12 VAL H H 9.034 0.01 1 47 . 12 VAL CA C 59.25 0.1 1 48 . 12 VAL CB C 36.98 0.2 1 49 . 13 PRO CA C 62.82 0.1 1 50 . 13 PRO C C 175.17 0.1 1 51 . 13 PRO CB C 32.69 0.2 1 52 . 14 ILE N N 119.02 0.05 1 53 . 14 ILE H H 8.114 0.01 1 54 . 14 ILE CA C 59.51 0.1 1 55 . 14 ILE C C 176.24 0.1 1 56 . 14 ILE CB C 42.86 0.2 1 57 . 15 LEU N N 128.59 0.05 1 58 . 15 LEU H H 8.771 0.01 1 59 . 15 LEU CA C 54.19 0.1 1 60 . 15 LEU C C 174.80 0.1 1 61 . 15 LEU CB C 46.70 0.2 1 62 . 16 VAL N N 122.36 0.05 1 63 . 16 VAL H H 8.667 0.01 1 64 . 16 VAL CA C 60.13 0.1 1 65 . 16 VAL C C 174.98 0.1 1 66 . 16 VAL CB C 35.95 0.2 1 67 . 17 GLU N N 125.72 0.05 1 68 . 17 GLU H H 8.812 0.01 1 69 . 17 GLU CA C 55.61 0.1 1 70 . 17 GLU C C 174.12 0.1 1 71 . 17 GLU CB C 34.32 0.2 1 72 . 18 LEU N N 124.55 0.05 1 73 . 18 LEU H H 9.138 0.01 1 74 . 18 LEU CA C 54.50 0.1 1 75 . 18 LEU C C 174.09 0.1 1 76 . 18 LEU CB C 46.39 0.2 1 77 . 19 ASP N N 127.92 0.05 1 78 . 19 ASP H H 8.166 0.01 1 79 . 19 ASP CA C 54.30 0.1 1 80 . 19 ASP C C 174.74 0.1 1 81 . 19 ASP CB C 43.84 0.2 1 82 . 20 GLY N N 110.22 0.05 1 83 . 20 GLY H H 8.454 0.01 1 84 . 20 GLY CA C 44.00 0.1 1 85 . 20 GLY C C 172.32 0.1 1 86 . 21 ASP N N 120.13 0.05 1 87 . 21 ASP H H 7.076 0.01 1 88 . 21 ASP CA C 53.75 0.1 1 89 . 21 ASP C C 176.60 0.1 1 90 . 22 VAL N N 123.42 0.05 1 91 . 22 VAL H H 8.636 0.01 1 92 . 22 VAL CA C 60.99 0.1 1 93 . 22 VAL C C 175.18 0.1 1 94 . 22 VAL CB C 34.50 0.2 1 95 . 23 ASN N N 127.18 0.05 1 96 . 23 ASN H H 9.077 0.01 1 97 . 23 ASN CA C 54.71 0.1 1 98 . 23 ASN C C 174.03 0.1 1 99 . 23 ASN CB C 37.14 0.2 1 100 . 24 GLY N N 104.15 0.05 1 101 . 24 GLY H H 8.176 0.01 1 102 . 24 GLY CA C 45.93 0.1 1 103 . 24 GLY C C 174.66 0.1 1 104 . 25 HIS N N 120.76 0.05 1 105 . 25 HIS H H 8.082 0.01 1 106 . 25 HIS CA C 55.40 0.1 1 107 . 25 HIS C C 175.02 0.1 1 108 . 25 HIS CB C 29.42 0.2 1 109 . 26 LYS N N 125.89 0.05 1 110 . 26 LYS H H 8.661 0.01 1 111 . 26 LYS CA C 55.93 0.1 1 112 . 26 LYS C C 177.27 0.1 1 113 . 26 LYS CB C 33.62 0.2 1 114 . 27 PHE N N 118.30 0.05 1 115 . 27 PHE H H 8.419 0.01 1 116 . 27 PHE CA C 56.13 0.1 1 117 . 27 PHE C C 172.65 0.1 1 118 . 27 PHE CB C 41.61 0.2 1 119 . 28 SER N N 114.26 0.05 1 120 . 28 SER H H 7.886 0.01 1 121 . 28 SER CA C 57.78 0.1 1 122 . 28 SER C C 173.30 0.1 1 123 . 28 SER CB C 66.18 0.2 1 124 . 29 VAL N N 122.32 0.05 1 125 . 29 VAL H H 9.057 0.01 1 126 . 29 VAL CA C 60.69 0.1 1 127 . 29 VAL C C 174.55 0.1 1 128 . 29 VAL CB C 37.87 0.2 1 129 . 30 SER N N 122.22 0.05 1 130 . 30 SER H H 8.778 0.01 1 131 . 30 SER CA C 57.25 0.1 1 132 . 30 SER C C 173.90 0.1 1 133 . 30 SER CB C 66.18 0.2 1 134 . 31 GLY N N 111.87 0.05 1 135 . 31 GLY H H 9.795 0.01 1 136 . 31 GLY CA C 45.49 0.1 1 137 . 31 GLY C C 171.80 0.1 1 138 . 32 GLU N N 116.97 0.05 1 139 . 32 GLU H H 8.133 0.01 1 140 . 32 GLU CA C 54.44 0.1 1 141 . 32 GLU C C 175.54 0.1 1 142 . 32 GLU CB C 34.05 0.2 1 143 . 33 GLY N N 109.32 0.05 1 144 . 33 GLY H H 8.091 0.01 1 145 . 33 GLY CA C 46.20 0.1 1 146 . 33 GLY C C 172.41 0.1 1 147 . 34 GLU N N 121.52 0.05 1 148 . 34 GLU H H 8.772 0.01 1 149 . 34 GLU CA C 55.23 0.1 1 150 . 34 GLU C C 174.18 0.1 1 151 . 34 GLU CB C 33.55 0.2 1 152 . 35 GLY N N 108.16 0.05 1 153 . 35 GLY H H 8.752 0.01 1 154 . 35 GLY CA C 44.17 0.1 1 155 . 35 GLY C C 171.74 0.1 1 156 . 36 ASP N N 121.96 0.05 1 157 . 36 ASP H H 8.918 0.01 1 158 . 36 ASP CA C 52.61 0.1 1 159 . 36 ASP C C 177.71 0.1 1 160 . 36 ASP CB C 43.09 0.2 1 161 . 37 ALA N N 129.93 0.05 1 162 . 37 ALA H H 10.714 0.01 1 163 . 37 ALA CA C 54.18 0.1 1 164 . 37 ALA C C 178.72 0.1 1 165 . 37 ALA CB C 20.76 0.2 1 166 . 38 THR N N 115.64 0.05 1 167 . 38 THR H H 9.027 0.01 1 168 . 38 THR CA C 66.48 0.1 1 169 . 38 THR C C 175.35 0.1 1 170 . 38 THR CB C 68.13 0.2 1 171 . 39 TYR N N 116.34 0.05 1 172 . 39 TYR H H 7.067 0.01 1 173 . 39 TYR CA C 58.58 0.1 1 174 . 39 TYR C C 176.71 0.1 1 175 . 39 TYR CB C 41.31 0.2 1 176 . 40 GLY N N 111.83 0.05 1 177 . 40 GLY H H 8.536 0.01 1 178 . 40 GLY CA C 46.93 0.1 1 179 . 40 GLY C C 173.68 0.1 1 180 . 41 LYS N N 117.82 0.05 1 181 . 41 LYS H H 7.829 0.01 1 182 . 41 LYS CA C 54.99 0.1 1 183 . 41 LYS CB C 37.79 0.2 1 184 . 42 LEU N N 124.99 0.05 1 185 . 42 LEU H H 8.865 0.01 1 186 . 42 LEU CA C 54.46 0.1 1 187 . 42 LEU C C 175.38 0.1 1 188 . 42 LEU CB C 46.23 0.2 1 189 . 43 THR N N 114.77 0.05 1 190 . 43 THR H H 7.995 0.01 1 191 . 43 THR CA C 60.58 0.1 1 192 . 43 THR C C 173.95 0.1 1 193 . 43 THR CB C 70.55 0.2 1 194 . 44 LEU N N 125.15 0.05 1 195 . 44 LEU H H 8.857 0.01 1 196 . 44 LEU CA C 54.16 0.1 1 197 . 44 LEU C C 173.61 0.1 1 198 . 44 LEU CB C 50.37 0.2 1 199 . 45 LYS N N 119.96 0.05 1 200 . 45 LYS H H 7.932 0.01 1 201 . 45 LYS CA C 55.06 0.1 1 202 . 45 LYS C C 174.43 0.1 1 203 . 45 LYS CB C 35.25 0.2 1 204 . 46 PHE N N 124.27 0.05 1 205 . 46 PHE H H 8.952 0.01 1 206 . 46 PHE CA C 56.30 0.1 1 207 . 46 PHE C C 174.52 0.1 1 208 . 46 PHE CB C 43.07 0.2 1 209 . 47 ILE N N 118.26 0.05 1 210 . 47 ILE H H 9.260 0.01 1 211 . 47 ILE CA C 59.41 0.1 1 212 . 47 ILE C C 176.10 0.1 1 213 . 47 ILE CB C 42.26 0.2 1 214 . 48 CYS N N 125.40 0.05 1 215 . 48 CYS H H 8.873 0.01 1 216 . 48 CYS CA C 59.22 0.1 1 217 . 48 CYS CB C 27.48 0.2 1 218 . 49 THR N N 121.79 0.05 1 219 . 49 THR H H 8.554 0.01 1 220 . 49 THR CA C 63.71 0.1 1 221 . 49 THR C C 176.14 0.1 1 222 . 49 THR CB C 68.18 0.2 1 223 . 50 THR N N 110.03 0.05 1 224 . 50 THR H H 8.017 0.01 1 225 . 50 THR CA C 61.62 0.1 1 226 . 50 THR C C 174.24 0.1 1 227 . 50 THR CB C 69.08 0.2 1 228 . 51 GLY N N 110.33 0.05 1 229 . 51 GLY H H 7.361 0.01 1 230 . 51 GLY CA C 45.66 0.1 1 231 . 51 GLY C C 172.37 0.1 1 232 . 52 LYS N N 125.48 0.05 1 233 . 52 LYS H H 8.426 0.01 1 234 . 52 LYS CA C 55.04 0.1 1 235 . 52 LYS C C 177.56 0.1 1 236 . 52 LYS CB C 33.45 0.2 1 237 . 53 LEU N N 132.53 0.05 1 238 . 53 LEU H H 9.471 0.01 1 239 . 53 LEU CA C 53.53 0.1 1 240 . 53 LEU CB C 42.11 0.2 1 241 . 56 PRO CA C 64.32 0.1 1 242 . 56 PRO C C 175.14 0.1 1 243 . 56 PRO CB C 31.53 0.2 1 244 . 57 TRP N N 106.84 0.05 1 245 . 57 TRP H H 6.082 0.01 1 246 . 57 TRP CA C 56.71 0.1 1 247 . 57 TRP CB C 32.44 0.2 1 248 . 57 TRP NE1 N 132.41 0.00 1 249 . 57 TRP HE1 H 10.553 0.000 1 250 . 58 PRO CA C 65.95 0.1 1 251 . 58 PRO C C 179.84 0.1 1 252 . 58 PRO CB C 32.52 0.2 1 253 . 59 THR N N 103.20 0.05 1 254 . 59 THR H H 7.666 0.01 1 255 . 59 THR CA C 64.68 0.1 1 256 . 59 THR C C 174.56 0.1 1 257 . 59 THR CB C 69.05 0.2 1 258 . 60 LEU N N 119.27 0.05 1 259 . 60 LEU H H 7.599 0.01 1 260 . 60 LEU CA C 54.62 0.1 1 261 . 60 LEU C C 175.98 0.1 1 262 . 60 LEU CB C 43.50 0.2 1 263 . 61 VAL N N 120.85 0.05 1 264 . 61 VAL H H 6.838 0.01 1 265 . 61 VAL CA C 68.85 0.1 1 266 . 61 VAL C C 175.92 0.1 1 267 . 61 VAL CB C 32.43 0.2 1 268 . 62 THR N N 105.05 0.05 1 269 . 62 THR H H 7.787 0.01 1 270 . 62 THR CA C 63.32 0.1 1 271 . 62 THR CB C 68.14 0.2 1 272 . 63 THR N N 120.81 0.05 1 273 . 63 THR H H 7.260 0.01 1 274 . 63 THR CA C 66.86 0.1 1 275 . 68 VAL CA C 58.68 0.1 1 276 . 68 VAL C C 175.44 0.1 1 277 . 68 VAL CB C 32.47 0.2 1 278 . 69 GLN N N 117.17 0.05 1 279 . 69 GLN H H 8.022 0.01 1 280 . 69 GLN CA C 58.06 0.1 1 281 . 69 GLN C C 175.91 0.1 1 282 . 69 GLN CB C 26.45 0.2 1 283 . 70 CYS N N 115.66 0.05 1 284 . 70 CYS H H 7.210 0.01 1 285 . 70 CYS CA C 57.56 0.1 1 286 . 70 CYS C C 172.60 0.1 1 287 . 70 CYS CB C 27.94 0.2 1 288 . 71 PHE N N 117.03 0.05 1 289 . 71 PHE H H 7.646 0.01 1 290 . 71 PHE CA C 61.04 0.1 1 291 . 71 PHE C C 172.42 0.1 1 292 . 71 PHE CB C 38.55 0.2 1 293 . 72 SER N N 110.03 0.05 1 294 . 72 SER H H 6.654 0.01 1 295 . 72 SER CA C 59.53 0.1 1 296 . 72 SER C C 173.79 0.1 1 297 . 72 SER CB C 64.24 0.2 1 298 . 73 ARG N N 125.41 0.05 1 299 . 73 ARG H H 8.263 0.01 1 300 . 73 ARG CA C 56.00 0.1 1 301 . 73 ARG C C 176.25 0.1 1 302 . 73 ARG CB C 30.29 0.2 1 303 . 74 TYR N N 132.63 0.05 1 304 . 74 TYR H H 9.139 0.01 1 305 . 74 TYR CA C 55.60 0.1 1 306 . 74 TYR CB C 39.20 0.2 1 307 . 77 HIS CA C 58.51 0.1 1 308 . 77 HIS C C 176.10 0.1 1 309 . 77 HIS CB C 29.74 0.2 1 310 . 78 MET N N 117.61 0.05 1 311 . 78 MET H H 8.089 0.01 1 312 . 78 MET CA C 55.24 0.1 1 313 . 78 MET CB C 34.34 0.2 1 314 . 79 LYS N N 120.88 0.05 1 315 . 79 LYS H H 7.256 0.01 1 316 . 79 LYS CA C 60.77 0.1 1 317 . 79 LYS C C 178.62 0.1 1 318 . 79 LYS CB C 32.58 0.2 1 319 . 80 ARG N N 115.67 0.05 1 320 . 80 ARG H H 8.154 0.01 1 321 . 80 ARG CA C 57.25 0.1 1 322 . 80 ARG C C 174.03 0.1 1 323 . 80 ARG CB C 28.43 0.2 1 324 . 81 HIS N N 115.92 0.05 1 325 . 81 HIS H H 7.617 0.01 1 326 . 81 HIS CA C 55.32 0.1 1 327 . 81 HIS C C 174.06 0.1 1 328 . 81 HIS CB C 31.39 0.2 1 329 . 82 ASP N N 118.35 0.05 1 330 . 82 ASP H H 6.530 0.01 1 331 . 82 ASP CA C 52.35 0.1 1 332 . 82 ASP C C 175.29 0.1 1 333 . 82 ASP CB C 38.34 0.2 1 334 . 83 PHE N N 125.94 0.05 1 335 . 83 PHE H H 8.231 0.01 1 336 . 83 PHE CA C 60.43 0.1 1 337 . 83 PHE C C 177.64 0.1 1 338 . 83 PHE CB C 39.32 0.2 1 339 . 84 PHE N N 112.93 0.05 1 340 . 84 PHE H H 6.847 0.01 1 341 . 84 PHE CA C 59.94 0.1 1 342 . 84 PHE C C 177.76 0.1 1 343 . 84 PHE CB C 38.12 0.2 1 344 . 85 LYS N N 111.93 0.05 1 345 . 85 LYS H H 7.307 0.01 1 346 . 85 LYS CA C 59.89 0.1 1 347 . 85 LYS C C 179.17 0.1 1 348 . 85 LYS CB C 32.82 0.2 1 349 . 86 SER N N 114.62 0.05 1 350 . 86 SER H H 6.915 0.01 1 351 . 86 SER CA C 60.97 0.1 1 352 . 86 SER C C 174.29 0.1 1 353 . 86 SER CB C 62.86 0.2 1 354 . 87 ALA N N 120.63 0.05 1 355 . 87 ALA H H 6.703 0.01 1 356 . 87 ALA CA C 52.17 0.1 1 357 . 87 ALA C C 176.85 0.1 1 358 . 87 ALA CB C 19.27 0.2 1 359 . 88 MET N N 116.29 0.05 1 360 . 88 MET H H 7.590 0.01 1 361 . 88 MET CA C 53.13 0.1 1 362 . 88 MET CB C 31.26 0.2 1 363 . 89 PRO CA C 64.43 0.1 1 364 . 89 PRO C C 176.73 0.1 1 365 . 89 PRO CB C 35.43 0.2 1 366 . 90 GLU N N 126.45 0.05 1 367 . 90 GLU H H 9.700 0.01 1 368 . 90 GLU CA C 61.91 0.1 1 369 . 90 GLU C C 177.45 0.1 1 370 . 90 GLU CB C 28.98 0.2 1 371 . 91 GLY N N 100.30 0.05 1 372 . 91 GLY H H 8.610 0.01 1 373 . 91 GLY CA C 45.40 0.1 1 374 . 91 GLY C C 174.72 0.1 1 375 . 92 TYR N N 111.51 0.05 1 376 . 92 TYR H H 8.752 0.01 1 377 . 92 TYR CA C 55.29 0.1 1 378 . 92 TYR C C 173.33 0.1 1 379 . 92 TYR CB C 41.61 0.2 1 380 . 93 VAL N N 120.68 0.05 1 381 . 93 VAL H H 9.554 0.01 1 382 . 93 VAL CA C 61.23 0.1 1 383 . 93 VAL C C 176.92 0.1 1 384 . 93 VAL CB C 33.62 0.2 1 385 . 94 GLN N N 128.66 0.05 1 386 . 94 GLN H H 9.695 0.01 1 387 . 94 GLN CA C 55.23 0.1 1 388 . 94 GLN C C 175.49 0.1 1 389 . 94 GLN CB C 33.58 0.2 1 390 . 95 GLU N N 132.19 0.05 1 391 . 95 GLU H H 9.703 0.01 1 392 . 95 GLU CA C 55.21 0.1 1 393 . 95 GLU C C 176.04 0.1 1 394 . 96 ARG N N 117.94 0.05 1 395 . 96 ARG H H 8.714 0.01 1 396 . 96 ARG CA C 56.13 0.1 1 397 . 96 ARG C C 177.65 0.1 1 398 . 96 ARG CB C 35.10 0.2 1 399 . 97 THR N N 114.78 0.05 1 400 . 97 THR H H 8.176 0.01 1 401 . 97 THR CA C 63.60 0.1 1 402 . 97 THR C C 173.65 0.1 1 403 . 97 THR CB C 70.84 0.2 1 404 . 98 ILE N N 127.56 0.05 1 405 . 98 ILE H H 9.541 0.01 1 406 . 98 ILE CA C 59.95 0.1 1 407 . 98 ILE C C 174.86 0.1 1 408 . 98 ILE CB C 39.71 0.2 1 409 . 99 SER N N 121.80 0.05 1 410 . 99 SER H H 8.779 0.01 1 411 . 99 SER CA C 56.67 0.1 1 412 . 99 SER C C 174.97 0.1 1 413 . 99 SER CB C 63.60 0.2 1 414 . 100 PHE N N 128.26 0.05 1 415 . 100 PHE H H 8.607 0.01 1 416 . 100 PHE CA C 58.38 0.1 1 417 . 100 PHE C C 174.99 0.1 1 418 . 100 PHE CB C 38.23 0.2 1 419 . 101 LYS N N 127.06 0.05 1 420 . 101 LYS H H 7.715 0.01 1 421 . 101 LYS CA C 58.68 0.1 1 422 . 101 LYS C C 177.30 0.1 1 423 . 101 LYS CB C 32.82 0.2 1 424 . 102 ASP N N 121.71 0.05 1 425 . 102 ASP H H 9.167 0.01 1 426 . 102 ASP CA C 56.50 0.1 1 427 . 102 ASP C C 174.27 0.1 1 428 . 102 ASP CB C 39.93 0.2 1 429 . 103 ASP N N 122.77 0.05 1 430 . 103 ASP H H 8.581 0.01 1 431 . 103 ASP CA C 53.85 0.1 1 432 . 103 ASP C C 177.07 0.1 1 433 . 103 ASP CB C 44.20 0.2 1 434 . 104 GLY N N 107.92 0.05 1 435 . 104 GLY H H 7.718 0.01 1 436 . 104 GLY CA C 44.32 0.1 1 437 . 104 GLY C C 171.23 0.1 1 438 . 105 ASN N N 111.22 0.05 1 439 . 105 ASN H H 7.791 0.01 1 440 . 105 ASN CA C 51.74 0.1 1 441 . 105 ASN C C 175.67 0.1 1 442 . 105 ASN CB C 43.37 0.2 1 443 . 106 TYR N N 116.60 0.05 1 444 . 106 TYR H H 9.519 0.01 1 445 . 106 TYR CA C 53.12 0.1 1 446 . 106 TYR C C 175.60 0.1 1 447 . 106 TYR CB C 40.44 0.2 1 448 . 107 LYS N N 122.41 0.05 1 449 . 107 LYS H H 9.349 0.01 1 450 . 107 LYS CA C 55.92 0.1 1 451 . 107 LYS C C 177.15 0.1 1 452 . 107 LYS CB C 34.73 0.2 1 453 . 108 THR N N 114.55 0.05 1 454 . 108 THR H H 9.225 0.01 1 455 . 108 THR CA C 59.62 0.1 1 456 . 108 THR C C 173.92 0.1 1 457 . 108 THR CB C 70.90 0.2 1 458 . 109 ARG N N 123.57 0.05 1 459 . 109 ARG H H 8.688 0.01 1 460 . 109 ARG CA C 56.89 0.1 1 461 . 109 ARG C C 173.52 0.1 1 462 . 109 ARG CB C 32.65 0.2 1 463 . 110 ALA N N 131.07 0.05 1 464 . 110 ALA H H 9.071 0.01 1 465 . 110 ALA CA C 49.99 0.1 1 466 . 110 ALA C C 176.35 0.1 1 467 . 110 ALA CB C 25.30 0.2 1 468 . 111 GLU N N 119.14 0.05 1 469 . 111 GLU H H 8.548 0.01 1 470 . 111 GLU CA C 55.87 0.1 1 471 . 111 GLU C C 174.59 0.1 1 472 . 111 GLU CB C 32.86 0.2 1 473 . 112 VAL N N 125.53 0.05 1 474 . 112 VAL H H 8.656 0.01 1 475 . 112 VAL CA C 60.76 0.1 1 476 . 112 VAL C C 174.75 0.1 1 477 . 112 VAL CB C 32.25 0.2 1 478 . 113 LYS N N 119.58 0.05 1 479 . 113 LYS H H 8.584 0.01 1 480 . 113 LYS CA C 55.12 0.1 1 481 . 113 LYS C C 174.57 0.1 1 482 . 113 LYS CB C 35.47 0.2 1 483 . 114 PHE N N 117.76 0.05 1 484 . 114 PHE H H 7.626 0.01 1 485 . 114 PHE CA C 59.45 0.1 1 486 . 114 PHE C C 177.34 0.1 1 487 . 114 PHE CB C 39.92 0.2 1 488 . 115 GLU N N 124.30 0.05 1 489 . 115 GLU H H 9.186 0.01 1 490 . 115 GLU CA C 55.88 0.1 1 491 . 115 GLU C C 176.87 0.1 1 492 . 115 GLU CB C 29.91 0.2 1 493 . 116 GLY N N 115.46 0.05 1 494 . 116 GLY H H 8.808 0.01 1 495 . 116 GLY CA C 47.18 0.1 1 496 . 116 GLY C C 174.56 0.1 1 497 . 117 ASP N N 126.12 0.05 1 498 . 117 ASP H H 8.536 0.01 1 499 . 117 ASP CA C 54.56 0.1 1 500 . 117 ASP C C 175.32 0.1 1 501 . 117 ASP CB C 41.57 0.2 1 502 . 118 THR N N 114.96 0.05 1 503 . 118 THR H H 7.633 0.01 1 504 . 118 THR CA C 62.29 0.1 1 505 . 118 THR C C 171.48 0.1 1 506 . 118 THR CB C 71.40 0.2 1 507 . 119 LEU N N 130.43 0.05 1 508 . 119 LEU H H 8.549 0.01 1 509 . 119 LEU CA C 52.92 0.1 1 510 . 119 LEU C C 174.61 0.1 1 511 . 119 LEU CB C 41.48 0.2 1 512 . 120 VAL N N 125.05 0.05 1 513 . 120 VAL H H 8.931 0.01 1 514 . 120 VAL CA C 60.36 0.1 1 515 . 120 VAL C C 174.24 0.1 1 516 . 120 VAL CB C 34.44 0.2 1 517 . 121 ASN N N 122.26 0.05 1 518 . 121 ASN H H 8.550 0.01 1 519 . 121 ASN CA C 51.35 0.1 1 520 . 121 ASN C C 174.30 0.1 1 521 . 121 ASN CB C 40.82 0.2 1 522 . 122 ARG N N 124.72 0.05 1 523 . 122 ARG H H 8.599 0.01 1 524 . 122 ARG CA C 56.23 0.1 1 525 . 122 ARG C C 176.73 0.1 1 526 . 122 ARG CB C 31.86 0.2 1 527 . 123 ILE N N 123.69 0.05 1 528 . 123 ILE H H 9.314 0.01 1 529 . 123 ILE CA C 61.78 0.1 1 530 . 123 ILE C C 175.86 0.1 1 531 . 123 ILE CB C 43.86 0.2 1 532 . 124 GLU N N 127.16 0.05 1 533 . 124 GLU H H 8.993 0.01 1 534 . 124 GLU CA C 55.67 0.1 1 535 . 124 GLU C C 174.64 0.1 1 536 . 124 GLU CB C 32.94 0.2 1 537 . 125 LEU N N 126.54 0.05 1 538 . 125 LEU H H 8.553 0.01 1 539 . 125 LEU CA C 54.37 0.1 1 540 . 125 LEU C C 174.73 0.1 1 541 . 125 LEU CB C 46.22 0.2 1 542 . 126 LYS N N 128.65 0.05 1 543 . 126 LYS H H 9.064 0.01 1 544 . 126 LYS CA C 54.98 0.1 1 545 . 126 LYS C C 175.77 0.1 1 546 . 126 LYS CB C 35.76 0.2 1 547 . 127 GLY N N 114.97 0.05 1 548 . 127 GLY H H 10.290 0.01 1 549 . 127 GLY CA C 45.58 0.1 1 550 . 127 GLY C C 172.57 0.1 1 551 . 128 ILE N N 124.66 0.05 1 552 . 128 ILE H H 9.076 0.01 1 553 . 128 ILE CA C 60.12 0.1 1 554 . 128 ILE C C 173.14 0.1 1 555 . 128 ILE CB C 43.24 0.2 1 556 . 129 ASP N N 115.17 0.05 1 557 . 129 ASP H H 8.554 0.01 1 558 . 129 ASP CA C 55.93 0.1 1 559 . 129 ASP C C 175.59 0.1 1 560 . 129 ASP CB C 38.31 0.2 1 561 . 130 PHE N N 115.08 0.05 1 562 . 130 PHE H H 8.463 0.01 1 563 . 130 PHE CA C 59.60 0.1 1 564 . 130 PHE C C 177.86 0.1 1 565 . 130 PHE CB C 39.49 0.2 1 566 . 131 LYS N N 123.21 0.05 1 567 . 131 LYS H H 9.747 0.01 1 568 . 131 LYS CA C 55.84 0.1 1 569 . 131 LYS CB C 33.60 0.2 1 570 . 132 GLU N N 126.97 0.05 1 571 . 132 GLU H H 9.350 0.01 1 572 . 132 GLU CA C 59.93 0.1 1 573 . 132 GLU C C 175.69 0.1 1 574 . 132 GLU CB C 29.40 0.2 1 575 . 133 ASP N N 113.57 0.05 1 576 . 133 ASP H H 8.220 0.01 1 577 . 133 ASP CA C 52.56 0.1 1 578 . 133 ASP C C 176.83 0.1 1 579 . 133 ASP CB C 39.92 0.2 1 580 . 134 GLY N N 104.27 0.05 1 581 . 134 GLY H H 7.107 0.01 1 582 . 134 GLY CA C 44.39 0.1 1 583 . 134 GLY C C 174.60 0.1 1 584 . 135 ASN N N 114.08 0.05 1 585 . 135 ASN H H 9.133 0.01 1 586 . 135 ASN CA C 55.87 0.1 1 587 . 135 ASN C C 175.36 0.1 1 588 . 135 ASN CB C 38.55 0.2 1 589 . 136 ILE N N 115.84 0.05 1 590 . 136 ILE H H 7.093 0.01 1 591 . 136 ILE CA C 64.08 0.1 1 592 . 136 ILE C C 176.59 0.1 1 593 . 136 ILE CB C 36.23 0.2 1 594 . 137 LEU N N 117.57 0.05 1 595 . 137 LEU H H 8.937 0.01 1 596 . 137 LEU CA C 56.72 0.1 1 597 . 137 LEU C C 178.57 0.1 1 598 . 137 LEU CB C 39.80 0.2 1 599 . 138 GLY N N 103.06 0.05 1 600 . 138 GLY H H 7.098 0.01 1 601 . 138 GLY CA C 45.05 0.1 1 602 . 138 GLY C C 174.17 0.1 1 603 . 139 HIS N N 115.99 0.05 1 604 . 139 HIS H H 7.439 0.01 1 605 . 139 HIS CA C 58.19 0.1 1 606 . 139 HIS C C 175.49 0.1 1 607 . 139 HIS CB C 28.44 0.2 1 608 . 140 LYS N N 114.56 0.05 1 609 . 140 LYS H H 7.841 0.01 1 610 . 140 LYS CA C 55.21 0.1 1 611 . 140 LYS C C 175.90 0.1 1 612 . 140 LYS CB C 32.88 0.2 1 613 . 141 LEU N N 118.28 0.05 1 614 . 141 LEU H H 7.103 0.01 1 615 . 141 LEU CA C 55.83 0.1 1 616 . 141 LEU C C 178.37 0.1 1 617 . 141 LEU CB C 41.82 0.2 1 618 . 142 GLU N N 120.62 0.05 1 619 . 142 GLU H H 8.075 0.01 1 620 . 142 GLU CA C 56.92 0.1 1 621 . 142 GLU C C 176.75 0.1 1 622 . 142 GLU CB C 29.79 0.2 1 623 . 143 TYR N N 125.62 0.05 1 624 . 143 TYR H H 9.106 0.01 1 625 . 143 TYR CA C 57.51 0.1 1 626 . 148 HIS CA C 57.26 0.1 1 627 . 148 HIS C C 173.11 0.1 1 628 . 148 HIS CB C 33.54 0.2 1 629 . 149 ASN N N 119.18 0.05 1 630 . 149 ASN H H 8.528 0.01 1 631 . 149 ASN CA C 51.32 0.1 1 632 . 149 ASN CB C 40.59 0.2 1 633 . 150 VAL N N 121.68 0.05 1 634 . 150 VAL H H 8.558 0.01 1 635 . 150 VAL CA C 61.65 0.1 1 636 . 150 VAL C C 175.04 0.1 1 637 . 150 VAL CB C 33.25 0.2 1 638 . 151 TYR N N 126.55 0.05 1 639 . 151 TYR H H 7.521 0.01 1 640 . 151 TYR CA C 60.81 0.1 1 641 . 151 TYR C C 175.54 0.1 1 642 . 151 TYR CB C 38.20 0.2 1 643 . 152 ILE N N 126.44 0.05 1 644 . 152 ILE H H 8.832 0.01 1 645 . 152 ILE CA C 60.80 0.1 1 646 . 152 ILE C C 175.38 0.1 1 647 . 152 ILE CB C 40.56 0.2 1 648 . 153 THR N N 118.91 0.05 1 649 . 153 THR H H 8.744 0.01 1 650 . 153 THR CA C 59.91 0.1 1 651 . 153 THR C C 172.58 0.1 1 652 . 153 THR CB C 71.95 0.2 1 653 . 154 ALA N N 125.14 0.05 1 654 . 154 ALA H H 9.065 0.01 1 655 . 154 ALA CA C 53.07 0.1 1 656 . 154 ALA C C 176.97 0.1 1 657 . 154 ALA CB C 20.20 0.2 1 658 . 155 ASP N N 122.21 0.05 1 659 . 155 ASP H H 8.831 0.01 1 660 . 155 ASP CA C 52.56 0.1 1 661 . 155 ASP C C 176.62 0.1 1 662 . 155 ASP CB C 41.47 0.2 1 663 . 156 LYS N N 122.95 0.05 1 664 . 156 LYS H H 8.784 0.01 1 665 . 156 LYS CA C 59.71 0.1 1 666 . 156 LYS C C 178.92 0.1 1 667 . 156 LYS CB C 32.41 0.2 1 668 . 157 GLN N N 117.58 0.05 1 669 . 157 GLN H H 8.380 0.01 1 670 . 157 GLN CA C 58.53 0.1 1 671 . 157 GLN C C 177.41 0.1 1 672 . 157 GLN CB C 28.59 0.2 1 673 . 158 LYS N N 115.92 0.05 1 674 . 158 LYS H H 7.200 0.01 1 675 . 158 LYS CA C 55.16 0.1 1 676 . 158 LYS C C 175.72 0.1 1 677 . 158 LYS CB C 32.91 0.2 1 678 . 159 ASN N N 118.16 0.05 1 679 . 159 ASN H H 7.854 0.01 1 680 . 159 ASN CA C 54.37 0.1 1 681 . 159 ASN C C 172.30 0.1 1 682 . 159 ASN CB C 38.27 0.2 1 683 . 160 GLY N N 99.00 0.05 1 684 . 160 GLY H H 7.245 0.01 1 685 . 160 GLY CA C 44.99 0.1 1 686 . 160 GLY C C 173.23 0.1 1 687 . 161 ILE N N 110.14 0.05 1 688 . 161 ILE H H 7.576 0.01 1 689 . 161 ILE CA C 58.64 0.1 1 690 . 161 ILE C C 174.70 0.1 1 691 . 161 ILE CB C 43.11 0.2 1 692 . 162 LYS N N 120.19 0.05 1 693 . 162 LYS H H 9.100 0.01 1 694 . 162 LYS CA C 54.86 0.1 1 695 . 162 LYS C C 174.76 0.1 1 696 . 162 LYS CB C 37.01 0.2 1 697 . 163 ALA N N 119.37 0.05 1 698 . 163 ALA H H 8.716 0.01 1 699 . 163 ALA CA C 50.67 0.1 1 700 . 163 ALA C C 176.12 0.1 1 701 . 163 ALA CB C 23.13 0.2 1 702 . 164 ASN N N 116.75 0.05 1 703 . 164 ASN H H 8.569 0.01 1 704 . 164 ASN CA C 53.48 0.1 1 705 . 164 ASN C C 174.01 0.1 1 706 . 164 ASN CB C 43.21 0.2 1 707 . 165 PHE N N 115.72 0.05 1 708 . 165 PHE H H 8.087 0.01 1 709 . 165 PHE CA C 57.09 0.1 1 710 . 165 PHE C C 172.76 0.1 1 711 . 165 PHE CB C 39.97 0.2 1 712 . 166 LYS N N 120.00 0.05 1 713 . 166 LYS H H 8.559 0.01 1 714 . 166 LYS CA C 55.43 0.1 1 715 . 166 LYS C C 174.82 0.1 1 716 . 166 LYS CB C 35.21 0.2 1 717 . 167 ILE N N 123.63 0.05 1 718 . 167 ILE H H 7.984 0.01 1 719 . 167 ILE CA C 56.14 0.1 1 720 . 167 ILE C C 175.36 0.1 1 721 . 167 ILE CB C 37.42 0.2 1 722 . 168 ARG N N 127.20 0.05 1 723 . 168 ARG H H 10.221 0.01 1 724 . 168 ARG CA C 54.93 0.1 1 725 . 168 ARG C C 175.70 0.1 1 726 . 168 ARG CB C 30.66 0.2 1 727 . 169 HIS N N 124.15 0.05 1 728 . 169 HIS H H 8.779 0.01 1 729 . 169 HIS CA C 54.58 0.1 1 730 . 169 HIS C C 174.46 0.1 1 731 . 169 HIS CB C 30.02 0.2 1 732 . 170 ASN N N 126.22 0.05 1 733 . 170 ASN H H 9.531 0.01 1 734 . 170 ASN CA C 55.17 0.1 1 735 . 170 ASN C C 175.87 0.1 1 736 . 170 ASN CB C 37.88 0.2 1 737 . 171 ILE N N 125.24 0.05 1 738 . 171 ILE H H 8.554 0.01 1 739 . 171 ILE CA C 59.85 0.1 1 740 . 171 ILE C C 177.24 0.1 1 741 . 171 ILE CB C 37.50 0.2 1 742 . 172 GLU N N 124.22 0.05 1 743 . 172 GLU H H 8.476 0.01 1 744 . 172 GLU CA C 59.45 0.1 1 745 . 172 GLU C C 175.90 0.1 1 746 . 172 GLU CB C 29.96 0.2 1 747 . 173 ASP N N 117.47 0.05 1 748 . 173 ASP H H 7.327 0.01 1 749 . 173 ASP CA C 54.04 0.1 1 750 . 173 ASP C C 177.32 0.1 1 751 . 173 ASP CB C 40.43 0.2 1 752 . 174 GLY N N 108.76 0.05 1 753 . 174 GLY H H 8.279 0.01 1 754 . 174 GLY CA C 45.35 0.1 1 755 . 174 GLY C C 174.81 0.1 1 756 . 175 SER N N 117.57 0.05 1 757 . 175 SER H H 8.082 0.01 1 758 . 175 SER CA C 58.43 0.1 1 759 . 175 SER C C 172.79 0.1 1 760 . 175 SER CB C 64.31 0.2 1 761 . 176 VAL N N 115.63 0.05 1 762 . 176 VAL H H 8.108 0.01 1 763 . 176 VAL CA C 60.89 0.1 1 764 . 176 VAL C C 175.18 0.1 1 765 . 176 VAL CB C 36.11 0.2 1 766 . 177 GLN N N 126.77 0.05 1 767 . 177 GLN H H 9.389 0.01 1 768 . 177 GLN CA C 53.27 0.1 1 769 . 177 GLN C C 174.62 0.1 1 770 . 177 GLN CB C 31.85 0.2 1 771 . 178 LEU N N 130.21 0.05 1 772 . 178 LEU H H 8.983 0.01 1 773 . 178 LEU CA C 54.76 0.1 1 774 . 178 LEU C C 178.73 0.1 1 775 . 178 LEU CB C 44.06 0.2 1 776 . 179 ALA N N 125.82 0.05 1 777 . 179 ALA H H 9.208 0.01 1 778 . 179 ALA CA C 50.83 0.1 1 779 . 179 ALA C C 177.56 0.1 1 780 . 179 ALA CB C 21.54 0.2 1 781 . 180 ASP N N 131.58 0.05 1 782 . 180 ASP H H 8.820 0.01 1 783 . 180 ASP CA C 56.13 0.1 1 784 . 180 ASP C C 175.06 0.1 1 785 . 180 ASP CB C 42.38 0.2 1 786 . 181 HIS N N 122.80 0.05 1 787 . 181 HIS H H 9.158 0.01 1 788 . 181 HIS CA C 56.12 0.1 1 789 . 181 HIS C C 173.44 0.1 1 790 . 181 HIS CB C 30.02 0.2 1 791 . 182 TYR N N 123.04 0.05 1 792 . 182 TYR H H 8.427 0.01 1 793 . 182 TYR CA C 57.66 0.1 1 794 . 182 TYR C C 174.59 0.1 1 795 . 182 TYR CB C 40.00 0.2 1 796 . 183 GLN N N 126.86 0.05 1 797 . 183 GLN H H 8.600 0.01 1 798 . 183 GLN CA C 53.84 0.1 1 799 . 183 GLN C C 173.62 0.1 1 800 . 183 GLN CB C 34.03 0.2 1 801 . 184 GLN N N 123.75 0.05 1 802 . 184 GLN H H 9.131 0.01 1 803 . 184 GLN CA C 55.29 0.1 1 804 . 184 GLN C C 174.66 0.1 1 805 . 184 GLN CB C 33.24 0.2 1 806 . 185 ASN N N 121.49 0.05 1 807 . 185 ASN H H 8.842 0.01 1 808 . 185 ASN CA C 52.64 0.1 1 809 . 185 ASN C C 174.15 0.1 1 810 . 185 ASN CB C 41.42 0.2 1 811 . 186 THR N N 114.10 0.05 1 812 . 186 THR H H 8.720 0.01 1 813 . 186 THR CA C 58.78 0.1 1 814 . 186 THR CB C 71.36 0.2 1 815 . 187 PRO CA C 63.88 0.1 1 816 . 187 PRO C C 177.09 0.1 1 817 . 187 PRO CB C 32.53 0.2 1 818 . 188 ILE N N 123.94 0.05 1 819 . 188 ILE H H 8.756 0.01 1 820 . 188 ILE CA C 64.23 0.1 1 821 . 188 ILE C C 177.81 0.1 1 822 . 189 GLY N N 109.72 0.05 1 823 . 189 GLY H H 9.236 0.01 1 824 . 189 GLY CA C 44.27 0.1 1 825 . 189 GLY C C 173.73 0.1 1 826 . 190 ASP N N 116.91 0.05 1 827 . 190 ASP H H 8.271 0.01 1 828 . 190 ASP CA C 53.96 0.1 1 829 . 190 ASP C C 177.36 0.1 1 830 . 190 ASP CB C 41.93 0.2 1 831 . 191 GLY N N 109.50 0.05 1 832 . 191 GLY H H 8.336 0.01 1 833 . 191 GLY CA C 44.69 0.1 1 834 . 192 PRO CA C 63.04 0.1 1 835 . 192 PRO C C 176.73 0.1 1 836 . 192 PRO CB C 35.15 0.2 1 837 . 193 VAL N N 114.61 0.05 1 838 . 193 VAL H H 8.278 0.01 1 839 . 193 VAL CA C 59.65 0.1 1 840 . 193 VAL C C 175.55 0.1 1 841 . 193 VAL CB C 35.09 0.2 1 842 . 194 LEU N N 122.01 0.05 1 843 . 194 LEU H H 8.022 0.01 1 844 . 194 LEU CA C 54.06 0.1 1 845 . 194 LEU C C 174.89 0.1 1 846 . 194 LEU CB C 41.20 0.2 1 847 . 195 LEU N N 120.79 0.05 1 848 . 195 LEU H H 7.955 0.01 1 849 . 195 LEU CA C 50.36 0.1 1 850 . 195 LEU CB C 41.32 0.2 1 851 . 196 PRO CA C 62.64 0.1 1 852 . 196 PRO C C 178.57 0.1 1 853 . 196 PRO CB C 33.68 0.2 1 854 . 197 ASP N N 120.85 0.05 1 855 . 197 ASP H H 9.548 0.01 1 856 . 197 ASP CA C 54.30 0.1 1 857 . 197 ASP C C 175.88 0.1 1 858 . 197 ASP CB C 41.60 0.2 1 859 . 198 ASN N N 120.67 0.05 1 860 . 198 ASN H H 8.890 0.01 1 861 . 198 ASN CA C 54.65 0.1 1 862 . 198 ASN C C 175.49 0.1 1 863 . 198 ASN CB C 37.33 0.2 1 864 . 199 HIS N N 116.84 0.05 1 865 . 199 HIS H H 8.250 0.01 1 866 . 199 HIS CA C 56.48 0.1 1 867 . 199 HIS C C 171.35 0.1 1 868 . 199 HIS CB C 27.69 0.2 1 869 . 200 TYR N N 114.30 0.05 1 870 . 200 TYR H H 8.418 0.01 1 871 . 200 TYR CA C 55.34 0.1 1 872 . 200 TYR C C 173.17 0.1 1 873 . 200 TYR CB C 42.50 0.2 1 874 . 201 LEU N N 115.21 0.05 1 875 . 201 LEU H H 8.559 0.01 1 876 . 201 LEU CA C 52.72 0.1 1 877 . 201 LEU C C 177.82 0.1 1 878 . 201 LEU CB C 42.35 0.2 1 879 . 202 SER N N 121.85 0.05 1 880 . 202 SER H H 9.252 0.01 1 881 . 202 SER CA C 57.61 0.1 1 882 . 202 SER CB C 62.97 0.2 1 883 . 206 ALA CA C 51.23 0.1 1 884 . 206 ALA C C 175.64 0.1 1 885 . 206 ALA CB C 22.29 0.2 1 886 . 207 LEU N N 122.56 0.05 1 887 . 207 LEU H H 8.977 0.01 1 888 . 207 LEU CA C 53.02 0.1 1 889 . 208 SER CA C 57.03 0.1 1 890 . 208 SER C C 175.52 0.1 1 891 . 208 SER CB C 65.11 0.2 1 892 . 209 LYS N N 123.75 0.05 1 893 . 209 LYS H H 8.693 0.01 1 894 . 209 LYS CA C 53.53 0.1 1 895 . 209 LYS C C 175.35 0.1 1 896 . 209 LYS CB C 36.21 0.2 1 897 . 210 ASP N N 128.01 0.05 1 898 . 210 ASP H H 12.612 0.01 1 899 . 210 ASP CA C 50.78 0.1 1 900 . 210 ASP CB C 42.22 0.2 1 901 . 211 PRO CA C 64.46 0.1 1 902 . 211 PRO C C 176.93 0.1 1 903 . 211 PRO CB C 32.71 0.2 1 904 . 212 ASN N N 113.63 0.05 1 905 . 212 ASN H H 8.199 0.01 1 906 . 212 ASN CA C 53.36 0.1 1 907 . 212 ASN C C 174.51 0.1 1 908 . 212 ASN CB C 39.64 0.2 1 909 . 213 GLU N N 122.32 0.05 1 910 . 213 GLU H H 7.501 0.01 1 911 . 213 GLU CA C 55.21 0.1 1 912 . 213 GLU C C 174.99 0.1 1 913 . 213 GLU CB C 31.17 0.2 1 914 . 214 LYS N N 126.05 0.05 1 915 . 214 LYS H H 8.379 0.01 1 916 . 214 LYS CA C 56.87 0.1 1 917 . 214 LYS C C 178.77 0.1 1 918 . 214 LYS CB C 33.24 0.2 1 919 . 215 ARG N N 120.50 0.05 1 920 . 215 ARG H H 9.025 0.01 1 921 . 215 ARG CA C 56.62 0.1 1 922 . 215 ARG C C 176.01 0.1 1 923 . 215 ARG CB C 31.17 0.2 1 924 . 216 ASP N N 124.97 0.05 1 925 . 216 ASP H H 9.207 0.01 1 926 . 216 ASP CA C 55.98 0.1 1 927 . 216 ASP C C 176.68 0.1 1 928 . 216 ASP CB C 41.84 0.2 1 929 . 217 HIS N N 124.32 0.05 1 930 . 217 HIS H H 8.300 0.01 1 931 . 217 HIS CA C 56.76 0.1 1 932 . 217 HIS C C 169.82 0.1 1 933 . 217 HIS CB C 33.23 0.2 1 934 . 218 MET N N 115.45 0.05 1 935 . 218 MET H H 7.666 0.01 1 936 . 218 MET CA C 54.94 0.1 1 937 . 218 MET C C 174.03 0.1 1 938 . 218 MET CB C 37.97 0.2 1 939 . 219 VAL N N 126.47 0.05 1 940 . 219 VAL H H 7.517 0.01 1 941 . 219 VAL CA C 62.35 0.1 1 942 . 219 VAL C C 173.24 0.1 1 943 . 219 VAL CB C 32.14 0.2 1 944 . 220 LEU N N 129.86 0.05 1 945 . 220 LEU H H 9.302 0.01 1 946 . 220 LEU CA C 53.79 0.1 1 947 . 220 LEU C C 173.04 0.1 1 948 . 220 LEU CB C 48.57 0.2 1 949 . 221 LEU N N 129.43 0.05 1 950 . 221 LEU H H 8.426 0.01 1 951 . 221 LEU CA C 53.83 0.1 1 952 . 221 LEU CB C 44.59 0.2 1 953 . 222 GLU C C 173.89 0.1 1 954 . 223 PHE N N 120.09 0.05 1 955 . 223 PHE H H 8.864 0.01 1 956 . 223 PHE CA C 56.35 0.1 1 957 . 223 PHE C C 176.43 0.1 1 958 . 223 PHE CB C 43.15 0.2 1 959 . 224 VAL N N 123.61 0.05 1 960 . 224 VAL H H 9.505 0.01 1 961 . 224 VAL CA C 60.90 0.1 1 962 . 224 VAL C C 175.18 0.1 1 963 . 224 VAL CB C 34.93 0.2 1 964 . 225 THR N N 120.67 0.05 1 965 . 225 THR H H 8.356 0.01 1 966 . 225 THR CA C 60.12 0.1 1 967 . 225 THR C C 172.30 0.1 1 968 . 225 THR CB C 71.96 0.2 1 969 . 226 ALA N N 128.21 0.05 1 970 . 226 ALA H H 8.208 0.01 1 971 . 226 ALA CA C 51.63 0.1 1 972 . 226 ALA C C 175.67 0.1 1 973 . 226 ALA CB C 19.22 0.2 1 974 . 227 ALA N N 121.40 0.05 1 975 . 227 ALA H H 8.750 0.01 1 976 . 227 ALA CA C 51.68 0.1 1 977 . 227 ALA C C 175.53 0.1 1 978 . 227 ALA CB C 22.36 0.2 1 979 . 228 GLY N N 103.70 0.05 1 980 . 228 GLY H H 8.173 0.01 1 981 . 228 GLY CA C 45.57 0.1 1 982 . 228 GLY C C 173.59 0.1 1 983 . 229 ILE N N 124.12 0.05 1 984 . 229 ILE H H 7.080 0.01 1 985 . 229 ILE CA C 63.32 0.1 1 986 . 229 ILE CB C 41.03 0.2 1 stop_ save_