data_6809 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H,13C, and 15N chemical shift assignments for rabbitpox encoded viral chemokine inhibitor (vCCI) ; _BMRB_accession_number 6809 _BMRB_flat_file_name bmr6809.str _Entry_type original _Submission_date 2005-09-06 _Accession_date 2005-09-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DeRider Michele L. . 2 Zhang Li . . 3 LiWang Patricia J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 195 "13C chemical shifts" 583 "15N chemical shifts" 195 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-02-08 update BMRB 'complete entry citation' 2006-04-27 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Resonance Assignments and Secondary Structure of vCCI, a 26 kDa CC Chemokine Inhibitor from Rabbitpox Virus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16534540 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DeRider Michele L. . 2 Zhang Li . . 3 LiWang Patricia J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 36 _Journal_issue 'Suppl. 5' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22 _Page_last 22 _Year 2006 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title ; The T1/35kDa family of poxvirus-secreted proteins bind chemokines and modulate leukocyte influx into virus-infected tissues ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9123853 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Graham Kathryn A. . 2 Lalani A.S. S. . 3 Macen J.L. L. . 4 Ness T.L. L. . 5 Barry M. . . 6 Liu L.Y. Y. . 7 Lucas A. . . 8 Clark-Lewis I. . . 9 Moyer Richard W. . 10 Mcfadden Grant . . stop_ _Journal_abbreviation Virology _Journal_name_full . _Journal_volume 229 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 12 _Page_last 24 _Year 1997 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'rabbitpox vCCI' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'viral chemokine inhibitor' $monomer stop_ _System_molecular_weight 26130 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common vCCI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 242 _Mol_residue_sequence ; MPASLQQSSSSSSSCTEEEN KHHMGIDVIIKVTKQDQTPT NDKICQSVTEITESESDPDP EVESEDDSTSVEDVDPPTTY YSIIGGGLRMNFGFTKCPQI KSISESADGNTVNARLSSVS PGQGKDSPAITHEEALAMIK DCEVSIDIRCSEEEKDSDIK THPVLGSNISHKKVSYEDII GSTIVDTKCVKNLEFSVRIG DMCKESSELEVKDGFKYVDG SASKGATDDTSLIDSTKLKA CV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 ALA 4 SER 5 LEU 6 GLN 7 GLN 8 SER 9 SER 10 SER 11 SER 12 SER 13 SER 14 SER 15 CYS 16 THR 17 GLU 18 GLU 19 GLU 20 ASN 21 LYS 22 HIS 23 HIS 24 MET 25 GLY 26 ILE 27 ASP 28 VAL 29 ILE 30 ILE 31 LYS 32 VAL 33 THR 34 LYS 35 GLN 36 ASP 37 GLN 38 THR 39 PRO 40 THR 41 ASN 42 ASP 43 LYS 44 ILE 45 CYS 46 GLN 47 SER 48 VAL 49 THR 50 GLU 51 ILE 52 THR 53 GLU 54 SER 55 GLU 56 SER 57 ASP 58 PRO 59 ASP 60 PRO 61 GLU 62 VAL 63 GLU 64 SER 65 GLU 66 ASP 67 ASP 68 SER 69 THR 70 SER 71 VAL 72 GLU 73 ASP 74 VAL 75 ASP 76 PRO 77 PRO 78 THR 79 THR 80 TYR 81 TYR 82 SER 83 ILE 84 ILE 85 GLY 86 GLY 87 GLY 88 LEU 89 ARG 90 MET 91 ASN 92 PHE 93 GLY 94 PHE 95 THR 96 LYS 97 CYS 98 PRO 99 GLN 100 ILE 101 LYS 102 SER 103 ILE 104 SER 105 GLU 106 SER 107 ALA 108 ASP 109 GLY 110 ASN 111 THR 112 VAL 113 ASN 114 ALA 115 ARG 116 LEU 117 SER 118 SER 119 VAL 120 SER 121 PRO 122 GLY 123 GLN 124 GLY 125 LYS 126 ASP 127 SER 128 PRO 129 ALA 130 ILE 131 THR 132 HIS 133 GLU 134 GLU 135 ALA 136 LEU 137 ALA 138 MET 139 ILE 140 LYS 141 ASP 142 CYS 143 GLU 144 VAL 145 SER 146 ILE 147 ASP 148 ILE 149 ARG 150 CYS 151 SER 152 GLU 153 GLU 154 GLU 155 LYS 156 ASP 157 SER 158 ASP 159 ILE 160 LYS 161 THR 162 HIS 163 PRO 164 VAL 165 LEU 166 GLY 167 SER 168 ASN 169 ILE 170 SER 171 HIS 172 LYS 173 LYS 174 VAL 175 SER 176 TYR 177 GLU 178 ASP 179 ILE 180 ILE 181 GLY 182 SER 183 THR 184 ILE 185 VAL 186 ASP 187 THR 188 LYS 189 CYS 190 VAL 191 LYS 192 ASN 193 LEU 194 GLU 195 PHE 196 SER 197 VAL 198 ARG 199 ILE 200 GLY 201 ASP 202 MET 203 CYS 204 LYS 205 GLU 206 SER 207 SER 208 GLU 209 LEU 210 GLU 211 VAL 212 LYS 213 ASP 214 GLY 215 PHE 216 LYS 217 TYR 218 VAL 219 ASP 220 GLY 221 SER 222 ALA 223 SER 224 LYS 225 GLY 226 ALA 227 THR 228 ASP 229 ASP 230 THR 231 SER 232 LEU 233 ILE 234 ASP 235 SER 236 THR 237 LYS 238 LEU 239 LYS 240 ALA 241 CYS 242 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 7024 rabbitpox_vCCI 100.00 242 100.00 100.00 1.23e-171 PDB 2FFK "Solution Structure Of The Complex Between Poxvirus-Encoded Cc Chemokine Inhibitor Vcci And Human Mip-1beta, Minimized Average S" 100.00 242 100.00 100.00 1.23e-171 PDB 2FIN "Solution Structure Of The Complex Between Poxvirus-Encoded Cc Chemokine Inhibitor Vcci And Human Mip-1beta, Ensemble Structure" 100.00 242 100.00 100.00 1.23e-171 DBJ BAA00487 "35K major secreted protein [Vaccinia virus]" 100.00 258 99.17 99.59 7.76e-170 EMBL CAA64086 "D1L protein [Cowpox virus]" 100.00 255 97.52 97.93 2.03e-165 EMBL CAD90757 "I5R protein [Cowpox virus]" 100.00 255 97.52 97.93 2.03e-165 EMBL CAM58165 "viral chemokine binding protein [Vaccinia virus Ankara]" 100.00 241 97.93 98.76 4.26e-166 EMBL CAM58393 "viral chemokine binding protein [Vaccinia virus Ankara]" 100.00 241 97.93 98.76 4.26e-166 GB AAA47970 "putative C23L [Vaccinia virus Copenhagen]" 100.00 244 98.76 99.59 7.88e-169 GB AAA48229 "putative B29R [Vaccinia virus Copenhagen]" 100.00 244 98.76 99.59 7.88e-169 GB AAB53969 "35kDa major secreted protein [Rabbitpox virus]" 100.00 258 100.00 100.00 1.14e-171 GB AAF33853 "TC20L [Vaccinia virus Tian Tan]" 100.00 244 99.17 100.00 5.90e-170 GB AAF34094 "TB23R [Vaccinia virus Tian Tan]" 100.00 244 99.17 100.00 5.90e-170 REF YP_232883 "chemokine-binding protein [Vaccinia virus]" 100.00 244 99.17 100.00 5.90e-170 REF YP_233100 "chemokine-binding protein [Vaccinia virus]" 100.00 244 99.17 100.00 5.90e-170 SP P19063 "RecName: Full=Chemokine-binding protein; Short=vCKBP; AltName: Full=35 kDa protein; Flags: Precursor [Vaccinia virus Lister]" 100.00 258 99.17 99.59 7.76e-170 SP P21090 "RecName: Full=Inactive chemokine-binding protein; Short=vCKBP [Vaccinia virus Copenhagen]" 100.00 244 98.76 99.59 7.88e-169 SP Q805H7 "RecName: Full=Inactive chemokine-binding protein; Short=vCKBP [Vaccinia virus WR]" 100.00 244 99.17 100.00 5.90e-170 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $monomer 'rabbitpox virus' 32606 Viruses 'Not applicable' Orthopoxvirus rabbitpox stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $monomer 'recombinant technology' yeast . . SMD1168 pPIC9K . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'unbound vCCI' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $monomer 2 mM '[U-2H; U-15N; U-13C]' NaCl 100 mM . 'Phosphate Buffer' 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address NIH . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample_1 save_ save_15N_HSQC-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 15N_HSQC-NOESY _Sample_label $sample_1 save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details ; 20 mM Phosphate Buffer pH 7.0 100 mM NaCl DSS Protease Inhibitor ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 120 5 mM pH 7.0 0.1 pH temperature 310 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ 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 'viral chemokine inhibitor' _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 2 PRO C C 178.2 0.2 . 2 2 2 PRO CA C 62.8 0.2 . 3 2 2 PRO CB C 30.88 0.2 . 4 3 3 ALA H H 8.364 0.05 . 5 3 3 ALA C C 174.8 0.2 . 6 3 3 ALA CA C 52.54 0.2 . 7 3 3 ALA CB C 18.09 0.2 . 8 3 3 ALA N N 123.67 0.2 . 9 4 4 SER H H 8.139 0.05 . 10 4 4 SER C C 174.2 0.2 . 11 4 4 SER CA C 58.16 0.2 . 12 4 4 SER CB C 63.06 0.2 . 13 4 4 SER N N 113.745 0.2 . 14 5 5 LEU H H 8.058 0.05 . 15 5 5 LEU CA C 55.01 0.2 . 16 5 5 LEU CB C 41.06 0.2 . 17 5 5 LEU N N 123.251 0.2 . 18 6 6 GLN H H 8.153 0.05 . 19 6 6 GLN CA C 55.567 0.2 . 20 6 6 GLN CB C 28.29 0.2 . 21 6 6 GLN N N 120.232 0.2 . 22 16 16 THR C C 176.5 0.2 . 23 16 16 THR CA C 61.76 0.2 . 24 16 16 THR CB C 68.49 0.2 . 25 17 17 GLU H H 8.482 0.05 . 26 17 17 GLU C C 176.4 0.2 . 27 17 17 GLU CA C 55.78 0.2 . 28 17 17 GLU CB C 29.13 0.2 . 29 17 17 GLU N N 123.697 0.2 . 30 18 18 GLU H H 8.273 0.05 . 31 18 18 GLU C C 176.5 0.2 . 32 18 18 GLU CA C 56.17 0.2 . 33 18 18 GLU CB C 29.67 0.2 . 34 18 18 GLU N N 121.933 0.2 . 35 19 19 GLU H H 8.477 0.05 . 36 19 19 GLU C C 173.9 0.2 . 37 19 19 GLU CA C 57.15 0.2 . 38 19 19 GLU CB C 28.94 0.2 . 39 19 19 GLU N N 122.531 0.2 . 40 20 20 ASN H H 8.654 0.05 . 41 20 20 ASN C C 175.3 0.2 . 42 20 20 ASN CA C 53.54 0.2 . 43 20 20 ASN CB C 37.55 0.2 . 44 20 20 ASN N N 116.126 0.2 . 45 21 21 LYS H H 7.157 0.05 . 46 21 21 LYS C C 175.2 0.2 . 47 21 21 LYS CA C 54.34 0.2 . 48 21 21 LYS CB C 34.54 0.2 . 49 21 21 LYS N N 116.318 0.2 . 50 22 22 HIS H H 9.243 0.05 . 51 22 22 HIS C C 174.5 0.2 . 52 22 22 HIS CA C 54.5 0.2 . 53 22 22 HIS CB C 31.86 0.2 . 54 22 22 HIS N N 116.744 0.2 . 55 23 23 HIS H H 9.935 0.05 . 56 23 23 HIS C C 176.6 0.2 . 57 23 23 HIS CA C 54.56 0.2 . 58 23 23 HIS CB C 26.15 0.2 . 59 23 23 HIS N N 127.945 0.2 . 60 24 24 MET H H 7.811 0.05 . 61 24 24 MET C C 169.8 0.2 . 62 24 24 MET CA C 52.7 0.2 . 63 24 24 MET CB C 29.02 0.2 . 64 24 24 MET N N 121.424 0.2 . 65 25 25 GLY H H 9.549 0.05 . 66 25 25 GLY C C 172.4 0.2 . 67 25 25 GLY CA C 42.67 0.2 . 68 25 25 GLY N N 109.442 0.2 . 69 26 26 ILE H H 8.241 0.05 . 70 26 26 ILE C C 173.7 0.2 . 71 26 26 ILE CA C 56.83 0.2 . 72 26 26 ILE CB C 42.15 0.2 . 73 26 26 ILE N N 115.232 0.2 . 74 27 27 ASP H H 8.872 0.05 . 75 27 27 ASP C C 174.4 0.2 . 76 27 27 ASP CA C 54.23 0.2 . 77 27 27 ASP CB C 44.94 0.2 . 78 27 27 ASP N N 127.124 0.2 . 79 28 28 VAL H H 9.402 0.05 . 80 28 28 VAL C C 173.8 0.2 . 81 28 28 VAL CA C 59.94 0.2 . 82 28 28 VAL CB C 32.89 0.2 . 83 28 28 VAL N N 127.881 0.2 . 84 29 29 ILE H H 8.637 0.05 . 85 29 29 ILE C C 171.1 0.2 . 86 29 29 ILE CA C 58.93 0.2 . 87 29 29 ILE CB C 41.14 0.2 . 88 29 29 ILE N N 118.678 0.2 . 89 30 30 ILE H H 8.853 0.05 . 90 30 30 ILE C C 176.3 0.2 . 91 30 30 ILE CA C 58.77 0.2 . 92 30 30 ILE CB C 42.32 0.2 . 93 30 30 ILE N N 121.109 0.2 . 94 31 31 LYS H H 8.956 0.05 . 95 31 31 LYS C C 174.2 0.2 . 96 31 31 LYS CA C 54.83 0.2 . 97 31 31 LYS CB C 35.63 0.2 . 98 31 31 LYS N N 127.149 0.2 . 99 32 32 VAL H H 9.718 0.05 . 100 32 32 VAL C C 174.8 0.2 . 101 32 32 VAL CA C 61.14 0.2 . 102 32 32 VAL CB C 32.97 0.2 . 103 32 32 VAL N N 129.923 0.2 . 104 33 33 THR H H 9.087 0.05 . 105 33 33 THR C C 176.3 0.2 . 106 33 33 THR CA C 61.74 0.2 . 107 33 33 THR CB C 68.44 0.2 . 108 33 33 THR N N 123.977 0.2 . 109 34 34 LYS H H 9.124 0.05 . 110 34 34 LYS C C 176.6 0.2 . 111 34 34 LYS CA C 56.16 0.2 . 112 34 34 LYS CB C 32 0.2 . 113 34 34 LYS N N 128.151 0.2 . 114 35 35 GLN H H 7.395 0.05 . 115 35 35 GLN C C 175.5 0.2 . 116 35 35 GLN CA C 55.68 0.2 . 117 35 35 GLN CB C 26.91 0.2 . 118 35 35 GLN N N 116.253 0.2 . 119 36 36 ASP H H 8.748 0.05 . 120 36 36 ASP C C 174.2 0.2 . 121 36 36 ASP CA C 55.56 0.2 . 122 36 36 ASP CB C 39.77 0.2 . 123 36 36 ASP N N 122.606 0.2 . 124 37 37 GLN H H 7.773 0.05 . 125 37 37 GLN CA C 55.11 0.2 . 126 37 37 GLN CB C 31.02 0.2 . 127 37 37 GLN N N 121.995 0.2 . 128 38 38 THR H H 8.325 0.05 . 129 38 38 THR CA C 58.31 0.2 . 130 38 38 THR CB C 70.35 0.2 . 131 38 38 THR N N 117.429 0.2 . 132 39 39 PRO C C 173.8 0.2 . 133 39 39 PRO CA C 62.44 0.2 . 134 39 39 PRO CB C 33.51 0.2 . 135 40 40 THR H H 8.376 0.05 . 136 40 40 THR C C 173 0.2 . 137 40 40 THR CA C 62.26 0.2 . 138 40 40 THR CB C 68.73 0.2 . 139 40 40 THR N N 114.886 0.2 . 140 41 41 ASN H H 8.392 0.05 . 141 41 41 ASN CA C 53.65 0.2 . 142 41 41 ASN CB C 37.98 0.2 . 143 41 41 ASN N N 123.575 0.2 . 144 42 42 ASP H H 8.286 0.05 . 145 42 42 ASP C C 176.7 0.2 . 146 42 42 ASP CA C 51.8 0.2 . 147 42 42 ASP CB C 39.99 0.2 . 148 42 42 ASP N N 122.521 0.2 . 149 43 43 LYS H H 8.332 0.05 . 150 43 43 LYS C C 176.5 0.2 . 151 43 43 LYS CA C 55.95 0.2 . 152 43 43 LYS CB C 29.53 0.2 . 153 43 43 LYS N N 121.354 0.2 . 154 44 44 ILE H H 7.493 0.05 . 155 44 44 ILE C C 175.7 0.2 . 156 44 44 ILE CA C 60.15 0.2 . 157 44 44 ILE CB C 38.34 0.2 . 158 44 44 ILE N N 115.523 0.2 . 159 45 45 CYS H H 8.704 0.05 . 160 45 45 CYS C C 177.8 0.2 . 161 45 45 CYS CA C 52.5 0.2 . 162 45 45 CYS CB C 34.17 0.2 . 163 45 45 CYS N N 109.713 0.2 . 164 46 46 GLN H H 9.026 0.05 . 165 46 46 GLN C C 172.8 0.2 . 166 46 46 GLN CA C 59.7 0.2 . 167 46 46 GLN CB C 28.33 0.2 . 168 46 46 GLN N N 119.744 0.2 . 169 47 47 SER H H 7.695 0.05 . 170 47 47 SER C C 175.5 0.2 . 171 47 47 SER CA C 58.14 0.2 . 172 47 47 SER CB C 63.97 0.2 . 173 47 47 SER N N 108.69 0.2 . 174 48 48 VAL H H 8.494 0.05 . 175 48 48 VAL C C 172.2 0.2 . 176 48 48 VAL CA C 61.06 0.2 . 177 48 48 VAL CB C 33.7 0.2 . 178 48 48 VAL N N 124.911 0.2 . 179 49 49 THR H H 8.691 0.05 . 180 49 49 THR C C 175.2 0.2 . 181 49 49 THR CA C 60.51 0.2 . 182 49 49 THR CB C 70.9 0.2 . 183 49 49 THR N N 120.578 0.2 . 184 50 50 GLU H H 8.515 0.05 . 185 50 50 GLU C C 174.9 0.2 . 186 50 50 GLU CA C 54.22 0.2 . 187 50 50 GLU CB C 31.44 0.2 . 188 50 50 GLU N N 125.909 0.2 . 189 51 51 ILE H H 8.882 0.05 . 190 51 51 ILE C C 174.4 0.2 . 191 51 51 ILE CA C 60.08 0.2 . 192 51 51 ILE CB C 40.19 0.2 . 193 51 51 ILE N N 126.522 0.2 . 194 52 52 THR H H 8.473 0.05 . 195 52 52 THR C C 175.7 0.2 . 196 52 52 THR CA C 60.77 0.2 . 197 52 52 THR CB C 69.48 0.2 . 198 52 52 THR N N 119.512 0.2 . 199 53 53 GLU H H 8.561 0.05 . 200 53 53 GLU C C 174.4 0.2 . 201 53 53 GLU CA C 55.83 0.2 . 202 53 53 GLU CB C 30.36 0.2 . 203 53 53 GLU N N 124.239 0.2 . 204 54 54 SER H H 8.391 0.05 . 205 54 54 SER CA C 57.67 0.2 . 206 54 54 SER CB C 63.59 0.2 . 207 54 54 SER N N 117.086 0.2 . 208 55 55 GLU H H 8.546 0.05 . 209 55 55 GLU C C 173 0.2 . 210 55 55 GLU CA C 56.24 0.2 . 211 55 55 GLU CB C 29.35 0.2 . 212 55 55 GLU N N 122.991 0.2 . 213 56 56 SER H H 8.173 0.05 . 214 56 56 SER CA C 57.75 0.2 . 215 56 56 SER CB C 63.55 0.2 . 216 56 56 SER N N 116.8 0.2 . 217 57 57 ASP H H 8.349 0.05 . 218 57 57 ASP CA C 52.41 0.2 . 219 57 57 ASP CB C 40.13 0.2 . 220 57 57 ASP N N 123.634 0.2 . 221 58 58 PRO CA C 62.63 0.2 . 222 58 58 PRO CB C 31 0.2 . 223 59 59 ASP H H 8.366 0.05 . 224 59 59 ASP CA C 51.93 0.2 . 225 59 59 ASP CB C 40.43 0.2 . 226 59 59 ASP N N 121.845 0.2 . 227 60 60 PRO C C 176.7 0.2 . 228 60 60 PRO CA C 63.13 0.2 . 229 60 60 PRO CB C 31.17 0.2 . 230 61 61 GLU H H 8.441 0.05 . 231 61 61 GLU C C 176 0.2 . 232 61 61 GLU CA C 56.34 0.2 . 233 61 61 GLU CB C 28.92 0.2 . 234 61 61 GLU N N 119.426 0.2 . 235 62 62 VAL H H 7.763 0.05 . 236 62 62 VAL C C 176.4 0.2 . 237 62 62 VAL CA C 61.64 0.2 . 238 62 62 VAL CB C 31.94 0.2 . 239 62 62 VAL N N 119.486 0.2 . 240 63 63 GLU H H 8.39 0.05 . 241 63 63 GLU C C 174.6 0.2 . 242 63 63 GLU CA C 56.15 0.2 . 243 63 63 GLU CB C 29.29 0.2 . 244 63 63 GLU N N 124.407 0.2 . 245 64 64 SER H H 8.258 0.05 . 246 64 64 SER C C 176.3 0.2 . 247 64 64 SER CA C 57.7 0.2 . 248 64 64 SER CB C 63.57 0.2 . 249 64 64 SER N N 116.788 0.2 . 250 65 65 GLU H H 8.511 0.05 . 251 65 65 GLU C C 176 0.2 . 252 65 65 GLU CA C 56.3 0.2 . 253 65 65 GLU CB C 29.24 0.2 . 254 65 65 GLU N N 122.871 0.2 . 255 66 66 ASP H H 8.226 0.05 . 256 66 66 ASP C C 176.7 0.2 . 257 66 66 ASP CA C 54.04 0.2 . 258 66 66 ASP CB C 40.75 0.2 . 259 66 66 ASP N N 120.556 0.2 . 260 67 67 ASP H H 8.249 0.05 . 261 67 67 ASP C C 175.1 0.2 . 262 67 67 ASP CA C 54 0.2 . 263 67 67 ASP CB C 40.31 0.2 . 264 67 67 ASP N N 120.909 0.2 . 265 68 68 SER H H 8.312 0.05 . 266 68 68 SER C C 174.7 0.2 . 267 68 68 SER CA C 58.6 0.2 . 268 68 68 SER CB C 63.18 0.2 . 269 68 68 SER N N 116.15 0.2 . 270 69 69 THR H H 8.131 0.05 . 271 69 69 THR C C 174.6 0.2 . 272 69 69 THR CA C 61.8 0.2 . 273 69 69 THR CB C 68.93 0.2 . 274 69 69 THR N N 115.452 0.2 . 275 70 70 SER H H 8.252 0.05 . 276 70 70 SER C C 176.1 0.2 . 277 70 70 SER CA C 57.81 0.2 . 278 70 70 SER CB C 63.24 0.2 . 279 70 70 SER N N 118.407 0.2 . 280 71 71 VAL H H 8.12 0.05 . 281 71 71 VAL C C 176 0.2 . 282 71 71 VAL CA C 61.83 0.2 . 283 71 71 VAL CB C 31.6 0.2 . 284 71 71 VAL N N 121.416 0.2 . 285 72 72 GLU H H 8.313 0.05 . 286 72 72 GLU C C 175.8 0.2 . 287 72 72 GLU CA C 56.09 0.2 . 288 72 72 GLU CB C 29.5 0.2 . 289 72 72 GLU N N 123.335 0.2 . 290 73 73 ASP H H 8.239 0.05 . 291 73 73 ASP C C 175.8 0.2 . 292 73 73 ASP CA C 54.08 0.2 . 293 73 73 ASP CB C 40.46 0.2 . 294 73 73 ASP N N 121.357 0.2 . 295 74 74 VAL H H 7.899 0.05 . 296 74 74 VAL C C 176.9 0.2 . 297 74 74 VAL CA C 61.13 0.2 . 298 74 74 VAL CB C 32.2 0.2 . 299 74 74 VAL N N 119.061 0.2 . 300 75 75 ASP H H 8.346 0.05 . 301 75 75 ASP CA C 52.4 0.2 . 302 75 75 ASP CB C 39.75 0.2 . 303 75 75 ASP N N 125.157 0.2 . 304 77 77 PRO C C 173.5 0.2 . 305 77 77 PRO CA C 62.53 0.2 . 306 77 77 PRO CB C 31.1 0.2 . 307 78 78 THR H H 8.231 0.05 . 308 78 78 THR C C 172.6 0.2 . 309 78 78 THR CA C 62.35 0.2 . 310 78 78 THR CB C 70.28 0.2 . 311 78 78 THR N N 119.195 0.2 . 312 79 79 THR H H 8.637 0.05 . 313 79 79 THR C C 175.6 0.2 . 314 79 79 THR CA C 61.97 0.2 . 315 79 79 THR CB C 69.97 0.2 . 316 79 79 THR N N 122.914 0.2 . 317 80 80 TYR H H 9.144 0.05 . 318 80 80 TYR C C 175.6 0.2 . 319 80 80 TYR CA C 56.05 0.2 . 320 80 80 TYR CB C 40.1 0.2 . 321 80 80 TYR N N 125.245 0.2 . 322 81 81 TYR H H 9.348 0.05 . 323 81 81 TYR C C 175 0.2 . 324 81 81 TYR CA C 56.85 0.2 . 325 81 81 TYR CB C 41.83 0.2 . 326 81 81 TYR N N 118.775 0.2 . 327 82 82 SER H H 8.889 0.05 . 328 82 82 SER C C 176.6 0.2 . 329 82 82 SER CA C 56.29 0.2 . 330 82 82 SER CB C 63.87 0.2 . 331 82 82 SER N N 116.874 0.2 . 332 83 83 ILE H H 9.542 0.05 . 333 83 83 ILE C C 175.4 0.2 . 334 83 83 ILE CA C 60.18 0.2 . 335 83 83 ILE CB C 39.46 0.2 . 336 83 83 ILE N N 126.848 0.2 . 337 84 84 ILE H H 9.412 0.05 . 338 84 84 ILE C C 176 0.2 . 339 84 84 ILE CA C 60.38 0.2 . 340 84 84 ILE CB C 37.1 0.2 . 341 84 84 ILE N N 133.167 0.2 . 342 85 85 GLY H H 8.731 0.05 . 343 85 85 GLY C C 175.4 0.2 . 344 85 85 GLY CA C 45.74 0.2 . 345 85 85 GLY N N 116.138 0.2 . 346 86 86 GLY H H 8.264 0.05 . 347 86 86 GLY C C 174.5 0.2 . 348 86 86 GLY CA C 45.99 0.2 . 349 86 86 GLY N N 112.39 0.2 . 350 87 87 GLY H H 8.656 0.05 . 351 87 87 GLY C C 174.7 0.2 . 352 87 87 GLY CA C 44.51 0.2 . 353 87 87 GLY N N 106.942 0.2 . 354 88 88 LEU H H 7.584 0.05 . 355 88 88 LEU C C 174.6 0.2 . 356 88 88 LEU CA C 52.44 0.2 . 357 88 88 LEU CB C 45.34 0.2 . 358 88 88 LEU N N 119.34 0.2 . 359 89 89 ARG H H 8.807 0.05 . 360 89 89 ARG CA C 54.76 0.2 . 361 89 89 ARG CB C 30.93 0.2 . 362 89 89 ARG N N 121.938 0.2 . 363 90 90 MET H H 8.833 0.05 . 364 90 90 MET C C 174.2 0.2 . 365 90 90 MET CA C 55.23 0.2 . 366 90 90 MET CB C 34.37 0.2 . 367 90 90 MET N N 124.939 0.2 . 368 91 91 ASN H H 8.631 0.05 . 369 91 91 ASN C C 174.7 0.2 . 370 91 91 ASN CA C 51.39 0.2 . 371 91 91 ASN CB C 39.26 0.2 . 372 91 91 ASN N N 122.904 0.2 . 373 92 92 PHE H H 9.38 0.05 . 374 92 92 PHE C C 172.1 0.2 . 375 92 92 PHE CA C 55.74 0.2 . 376 92 92 PHE CB C 43.24 0.2 . 377 92 92 PHE N N 123.05 0.2 . 378 93 93 GLY H H 8.627 0.05 . 379 93 93 GLY C C 175.5 0.2 . 380 93 93 GLY CA C 44.45 0.2 . 381 93 93 GLY N N 110.528 0.2 . 382 94 94 PHE H H 8.987 0.05 . 383 94 94 PHE C C 171.6 0.2 . 384 94 94 PHE CA C 56.89 0.2 . 385 94 94 PHE CB C 41.88 0.2 . 386 94 94 PHE N N 121.804 0.2 . 387 95 95 THR H H 9.028 0.05 . 388 95 95 THR C C 174.5 0.2 . 389 95 95 THR CA C 61.7 0.2 . 390 95 95 THR CB C 69.58 0.2 . 391 95 95 THR N N 123.731 0.2 . 392 96 96 LYS H H 9.116 0.05 . 393 96 96 LYS C C 174.1 0.2 . 394 96 96 LYS CA C 57.42 0.2 . 395 96 96 LYS CB C 27.45 0.2 . 396 96 96 LYS N N 120.258 0.2 . 397 97 97 CYS H H 8.002 0.05 . 398 97 97 CYS CA C 53.56 0.2 . 399 97 97 CYS CB C 43.35 0.2 . 400 97 97 CYS N N 113.366 0.2 . 401 98 98 PRO C C 176.4 0.2 . 402 98 98 PRO CA C 62.18 0.2 . 403 98 98 PRO CB C 30.89 0.2 . 404 99 99 GLN H H 8.23 0.05 . 405 99 99 GLN C C 181.2 0.2 . 406 99 99 GLN CA C 56.06 0.2 . 407 99 99 GLN CB C 28.58 0.2 . 408 99 99 GLN N N 117.156 0.2 . 409 100 100 ILE H H 8.267 0.05 . 410 100 100 ILE C C 174.4 0.2 . 411 100 100 ILE CA C 58.4 0.2 . 412 100 100 ILE CB C 35.31 0.2 . 413 100 100 ILE N N 124.872 0.2 . 414 101 101 LYS H H 7.997 0.05 . 415 101 101 LYS C C 173.7 0.2 . 416 101 101 LYS CA C 54.79 0.2 . 417 101 101 LYS CB C 35.68 0.2 . 418 101 101 LYS N N 122.661 0.2 . 419 102 102 SER H H 7.949 0.05 . 420 102 102 SER C C 174 0.2 . 421 102 102 SER CA C 56.12 0.2 . 422 102 102 SER CB C 63.07 0.2 . 423 102 102 SER N N 115.163 0.2 . 424 103 103 ILE H H 8.209 0.05 . 425 103 103 ILE C C 173.1 0.2 . 426 103 103 ILE CA C 61.36 0.2 . 427 103 103 ILE CB C 40.39 0.2 . 428 103 103 ILE N N 126.709 0.2 . 429 104 104 SER H H 9.101 0.05 . 430 104 104 SER C C 174.8 0.2 . 431 104 104 SER CA C 57.44 0.2 . 432 104 104 SER CB C 66.51 0.2 . 433 104 104 SER N N 123.631 0.2 . 434 105 105 GLU H H 8.636 0.05 . 435 105 105 GLU C C 171.8 0.2 . 436 105 105 GLU CA C 54.78 0.2 . 437 105 105 GLU CB C 35.13 0.2 . 438 105 105 GLU N N 116.114 0.2 . 439 106 106 SER H H 9.083 0.05 . 440 106 106 SER C C 176 0.2 . 441 106 106 SER CA C 57.7 0.2 . 442 106 106 SER CB C 66.33 0.2 . 443 106 106 SER N N 113.7 0.2 . 444 107 107 ALA H H 8.829 0.05 . 445 107 107 ALA CA C 51.41 0.2 . 446 107 107 ALA CB C 20.84 0.2 . 447 107 107 ALA N N 121.942 0.2 . 448 108 108 ASP H H 8.265 0.05 . 449 108 108 ASP CA C 53.39 0.2 . 450 108 108 ASP CB C 42.26 0.2 . 451 108 108 ASP N N 120.541 0.2 . 452 110 110 ASN C C 174.3 0.2 . 453 110 110 ASN CA C 51.85 0.2 . 454 110 110 ASN CB C 37.91 0.2 . 455 111 111 THR H H 8.267 0.05 . 456 111 111 THR C C 173.3 0.2 . 457 111 111 THR CA C 60.95 0.2 . 458 111 111 THR CB C 70.83 0.2 . 459 111 111 THR N N 114.48 0.2 . 460 112 112 VAL H H 9.24 0.05 . 461 112 112 VAL C C 174.5 0.2 . 462 112 112 VAL CA C 61.38 0.2 . 463 112 112 VAL CB C 33.91 0.2 . 464 112 112 VAL N N 125.843 0.2 . 465 113 113 ASN H H 9.188 0.05 . 466 113 113 ASN C C 174.5 0.2 . 467 113 113 ASN CA C 50.54 0.2 . 468 113 113 ASN CB C 41.16 0.2 . 469 113 113 ASN N N 124.921 0.2 . 470 114 114 ALA H H 9.073 0.05 . 471 114 114 ALA C C 175.1 0.2 . 472 114 114 ALA CA C 50.93 0.2 . 473 114 114 ALA CB C 22.06 0.2 . 474 114 114 ALA N N 119.83 0.2 . 475 115 115 ARG H H 8.348 0.05 . 476 115 115 ARG C C 175.2 0.2 . 477 115 115 ARG CA C 54.38 0.2 . 478 115 115 ARG CB C 33.89 0.2 . 479 115 115 ARG N N 118.494 0.2 . 480 116 116 LEU H H 9.095 0.05 . 481 116 116 LEU C C 176.1 0.2 . 482 116 116 LEU CA C 54.62 0.2 . 483 116 116 LEU CB C 42.76 0.2 . 484 116 116 LEU N N 129.319 0.2 . 485 117 117 SER H H 9.4 0.05 . 486 117 117 SER C C 171.3 0.2 . 487 117 117 SER CA C 57.4 0.2 . 488 117 117 SER CB C 69.65 0.2 . 489 117 117 SER N N 115.539 0.2 . 490 118 118 SER H H 8.889 0.05 . 491 118 118 SER C C 174.7 0.2 . 492 118 118 SER CA C 58.52 0.2 . 493 118 118 SER CB C 63.45 0.2 . 494 118 118 SER N N 118.064 0.2 . 495 119 119 VAL H H 8.087 0.05 . 496 119 119 VAL C C 176.6 0.2 . 497 119 119 VAL CA C 59.89 0.2 . 498 119 119 VAL CB C 33.34 0.2 . 499 119 119 VAL N N 119.304 0.2 . 500 120 120 SER H H 8.445 0.05 . 501 120 120 SER CA C 56.25 0.2 . 502 120 120 SER CB C 61.44 0.2 . 503 120 120 SER N N 123.23 0.2 . 504 121 121 PRO C C 175.5 0.2 . 505 121 121 PRO CA C 62.65 0.2 . 506 121 121 PRO CB C 31.47 0.2 . 507 122 122 GLY H H 8.779 0.05 . 508 122 122 GLY CA C 45.13 0.2 . 509 122 122 GLY N N 108.944 0.2 . 510 123 123 GLN H H 8.509 0.05 . 511 123 123 GLN C C 173.9 0.2 . 512 123 123 GLN CA C 54.51 0.2 . 513 123 123 GLN CB C 30.19 0.2 . 514 123 123 GLN N N 118.117 0.2 . 515 124 124 GLY H H 8.492 0.05 . 516 124 124 GLY CA C 44.98 0.2 . 517 124 124 GLY N N 107.569 0.2 . 518 125 125 LYS H H 7.408 0.05 . 519 125 125 LYS CA C 52.85 0.2 . 520 125 125 LYS CB C 32.63 0.2 . 521 125 125 LYS N N 117.839 0.2 . 522 126 126 ASP C C 176.6 0.2 . 523 126 126 ASP CA C 55.01 0.2 . 524 126 126 ASP CB C 40.74 0.2 . 525 127 127 SER H H 8.412 0.05 . 526 127 127 SER CA C 55.2 0.2 . 527 127 127 SER CB C 62.98 0.2 . 528 127 127 SER N N 116.401 0.2 . 529 128 128 PRO C C 177 0.2 . 530 128 128 PRO CA C 62.82 0.2 . 531 128 128 PRO CB C 31.51 0.2 . 532 129 129 ALA H H 8.479 0.05 . 533 129 129 ALA C C 176 0.2 . 534 129 129 ALA CA C 50.31 0.2 . 535 129 129 ALA CB C 17.99 0.2 . 536 129 129 ALA N N 125.335 0.2 . 537 130 130 ILE H H 8.52 0.05 . 538 130 130 ILE C C 175.6 0.2 . 539 130 130 ILE CA C 59.21 0.2 . 540 130 130 ILE CB C 39.22 0.2 . 541 130 130 ILE N N 115.415 0.2 . 542 131 131 THR H H 8.646 0.05 . 543 131 131 THR C C 176.3 0.2 . 544 131 131 THR CA C 61.56 0.2 . 545 131 131 THR CB C 70.65 0.2 . 546 131 131 THR N N 110.526 0.2 . 547 132 132 HIS H H 8.727 0.05 . 548 132 132 HIS CA C 60.88 0.2 . 549 132 132 HIS CB C 29.28 0.2 . 550 132 132 HIS N N 120.001 0.2 . 551 133 133 GLU H H 8.979 0.05 . 552 133 133 GLU C C 179.5 0.2 . 553 133 133 GLU CA C 60.03 0.2 . 554 133 133 GLU CB C 28.15 0.2 . 555 133 133 GLU N N 116.07 0.2 . 556 134 134 GLU H H 7.73 0.05 . 557 134 134 GLU C C 178.1 0.2 . 558 134 134 GLU CA C 58.55 0.2 . 559 134 134 GLU CB C 29.07 0.2 . 560 134 134 GLU N N 120.095 0.2 . 561 135 135 ALA H H 8.782 0.05 . 562 135 135 ALA C C 179.2 0.2 . 563 135 135 ALA CA C 55.28 0.2 . 564 135 135 ALA CB C 17.97 0.2 . 565 135 135 ALA N N 124.798 0.2 . 566 136 136 LEU H H 7.99 0.05 . 567 136 136 LEU C C 179.2 0.2 . 568 136 136 LEU CA C 56.92 0.2 . 569 136 136 LEU CB C 40.93 0.2 . 570 136 136 LEU N N 116.978 0.2 . 571 137 137 ALA H H 7.137 0.05 . 572 137 137 ALA C C 178 0.2 . 573 137 137 ALA CA C 53.97 0.2 . 574 137 137 ALA CB C 17.05 0.2 . 575 137 137 ALA N N 119.144 0.2 . 576 138 138 MET H H 7.869 0.05 . 577 138 138 MET C C 175.9 0.2 . 578 138 138 MET CA C 58.82 0.2 . 579 138 138 MET CB C 31.15 0.2 . 580 138 138 MET N N 118.918 0.2 . 581 139 139 ILE H H 7.813 0.05 . 582 139 139 ILE C C 178.1 0.2 . 583 139 139 ILE CA C 65.09 0.2 . 584 139 139 ILE CB C 36.35 0.2 . 585 139 139 ILE N N 113.393 0.2 . 586 140 140 LYS H H 6.709 0.05 . 587 140 140 LYS C C 176.6 0.2 . 588 140 140 LYS CA C 55.8 0.2 . 589 140 140 LYS CB C 31.47 0.2 . 590 140 140 LYS N N 114.734 0.2 . 591 141 141 ASP H H 7.851 0.05 . 592 141 141 ASP C C 173.8 0.2 . 593 141 141 ASP CA C 54.97 0.2 . 594 141 141 ASP CB C 41.88 0.2 . 595 141 141 ASP N N 119.178 0.2 . 596 142 142 CYS H H 7.919 0.05 . 597 142 142 CYS C C 175.1 0.2 . 598 142 142 CYS CA C 55.96 0.2 . 599 142 142 CYS CB C 37.2 0.2 . 600 142 142 CYS N N 118.569 0.2 . 601 143 143 GLU H H 8.882 0.05 . 602 143 143 GLU C C 174.6 0.2 . 603 143 143 GLU CA C 54.06 0.2 . 604 143 143 GLU CB C 33 0.2 . 605 143 143 GLU N N 129.484 0.2 . 606 144 144 VAL H H 7.986 0.05 . 607 144 144 VAL C C 176.7 0.2 . 608 144 144 VAL CA C 59.12 0.2 . 609 144 144 VAL CB C 34.27 0.2 . 610 144 144 VAL N N 124.652 0.2 . 611 145 145 SER H H 9.249 0.05 . 612 145 145 SER CA C 55.69 0.2 . 613 145 145 SER CB C 65.9 0.2 . 614 145 145 SER N N 122.614 0.2 . 615 150 150 CYS H H 8.049 0.05 . 616 150 150 CYS CA C 54.54 0.2 . 617 150 150 CYS CB C 40.15 0.2 . 618 150 150 CYS N N 124.927 0.2 . 619 151 151 SER H H 8.017 0.05 . 620 151 151 SER CA C 58.29 0.2 . 621 151 151 SER CB C 63.24 0.2 . 622 151 151 SER N N 114.755 0.2 . 623 152 152 GLU C C 176.9 0.2 . 624 152 152 GLU CA C 54.87 0.2 . 625 152 152 GLU CB C 28.32 0.2 . 626 153 153 GLU H H 7.751 0.05 . 627 153 153 GLU C C 176.7 0.2 . 628 153 153 GLU CA C 56.93 0.2 . 629 153 153 GLU CB C 29.45 0.2 . 630 153 153 GLU N N 122.029 0.2 . 631 154 154 GLU H H 8.442 0.05 . 632 154 154 GLU C C 174.6 0.2 . 633 154 154 GLU CA C 55.38 0.2 . 634 154 154 GLU CB C 30.21 0.2 . 635 154 154 GLU N N 126.284 0.2 . 636 155 155 LYS H H 8.599 0.05 . 637 155 155 LYS C C 176.9 0.2 . 638 155 155 LYS CA C 56.33 0.2 . 639 155 155 LYS CB C 30.6 0.2 . 640 155 155 LYS N N 121.711 0.2 . 641 156 156 ASP H H 8.16 0.05 . 642 156 156 ASP C C 173.1 0.2 . 643 156 156 ASP CA C 54.49 0.2 . 644 156 156 ASP CB C 40.64 0.2 . 645 156 156 ASP N N 117.447 0.2 . 646 157 157 SER H H 8.478 0.05 . 647 157 157 SER C C 174 0.2 . 648 157 157 SER CA C 60.73 0.2 . 649 157 157 SER CB C 64.46 0.2 . 650 157 157 SER N N 114.896 0.2 . 651 158 158 ASP H H 8.084 0.05 . 652 158 158 ASP C C 177.3 0.2 . 653 158 158 ASP CA C 52.37 0.2 . 654 158 158 ASP CB C 39.69 0.2 . 655 158 158 ASP N N 127.456 0.2 . 656 159 159 ILE H H 7.465 0.05 . 657 159 159 ILE CA C 60.17 0.2 . 658 159 159 ILE CB C 38.88 0.2 . 659 159 159 ILE N N 118.338 0.2 . 660 160 160 LYS H H 8.621 0.05 . 661 160 160 LYS C C 174.9 0.2 . 662 160 160 LYS CA C 52.69 0.2 . 663 160 160 LYS CB C 30.59 0.2 . 664 160 160 LYS N N 124.908 0.2 . 665 161 161 THR H H 8.378 0.05 . 666 161 161 THR CA C 61.1 0.2 . 667 161 161 THR CB C 67.5 0.2 . 668 161 161 THR N N 111.995 0.2 . 669 162 162 HIS H H 7.039 0.05 . 670 162 162 HIS CA C 52.43 0.2 . 671 162 162 HIS CB C 28.03 0.2 . 672 162 162 HIS N N 118.193 0.2 . 673 163 163 PRO C C 176.5 0.2 . 674 163 163 PRO CA C 62.09 0.2 . 675 163 163 PRO CB C 31.24 0.2 . 676 164 164 VAL H H 8.605 0.05 . 677 164 164 VAL C C 177.6 0.2 . 678 164 164 VAL CA C 62.97 0.2 . 679 164 164 VAL CB C 30.45 0.2 . 680 164 164 VAL N N 122.908 0.2 . 681 165 165 LEU H H 8.502 0.05 . 682 165 165 LEU C C 173.6 0.2 . 683 165 165 LEU CA C 54.05 0.2 . 684 165 165 LEU CB C 41.76 0.2 . 685 165 165 LEU N N 130.336 0.2 . 686 166 166 GLY H H 8.749 0.05 . 687 166 166 GLY C C 174.5 0.2 . 688 166 166 GLY CA C 43.93 0.2 . 689 166 166 GLY N N 109.499 0.2 . 690 167 167 SER H H 8.563 0.05 . 691 167 167 SER C C 174.5 0.2 . 692 167 167 SER CA C 58.5 0.2 . 693 167 167 SER CB C 64.68 0.2 . 694 167 167 SER N N 114.73 0.2 . 695 168 168 ASN H H 8.227 0.05 . 696 168 168 ASN C C 175.4 0.2 . 697 168 168 ASN CA C 54.65 0.2 . 698 168 168 ASN CB C 38.19 0.2 . 699 168 168 ASN N N 115.214 0.2 . 700 169 169 ILE H H 8.073 0.05 . 701 169 169 ILE C C 173.6 0.2 . 702 169 169 ILE CA C 60.76 0.2 . 703 169 169 ILE CB C 37.56 0.2 . 704 169 169 ILE N N 120.203 0.2 . 705 170 170 SER H H 8.705 0.05 . 706 170 170 SER CA C 55.64 0.2 . 707 170 170 SER CB C 64.65 0.2 . 708 170 170 SER N N 120.618 0.2 . 709 171 171 HIS C C 173.6 0.2 . 710 171 171 HIS CA C 57.78 0.2 . 711 171 171 HIS CB C 28.16 0.2 . 712 172 172 LYS H H 6.889 0.05 . 713 172 172 LYS C C 176 0.2 . 714 172 172 LYS CA C 55.1 0.2 . 715 172 172 LYS CB C 31.49 0.2 . 716 172 172 LYS N N 118.113 0.2 . 717 173 173 LYS H H 8.033 0.05 . 718 173 173 LYS C C 174.7 0.2 . 719 173 173 LYS CA C 58.22 0.2 . 720 173 173 LYS CB C 31.06 0.2 . 721 173 173 LYS N N 118.001 0.2 . 722 174 174 VAL H H 6.593 0.05 . 723 174 174 VAL C C 176 0.2 . 724 174 174 VAL CA C 59.56 0.2 . 725 174 174 VAL CB C 31.96 0.2 . 726 174 174 VAL N N 118.605 0.2 . 727 175 175 SER H H 7.59 0.05 . 728 175 175 SER C C 175.7 0.2 . 729 175 175 SER CA C 59.81 0.2 . 730 175 175 SER CB C 63.14 0.2 . 731 175 175 SER N N 115.789 0.2 . 732 176 176 TYR H H 8.509 0.05 . 733 176 176 TYR C C 175.6 0.2 . 734 176 176 TYR CA C 58.94 0.2 . 735 176 176 TYR CB C 38.82 0.2 . 736 176 176 TYR N N 124.507 0.2 . 737 177 177 GLU H H 7.198 0.05 . 738 177 177 GLU C C 177.3 0.2 . 739 177 177 GLU CA C 53.94 0.2 . 740 177 177 GLU CB C 32.64 0.2 . 741 177 177 GLU N N 128.627 0.2 . 742 178 178 ASP H H 7.787 0.05 . 743 178 178 ASP CA C 53.25 0.2 . 744 178 178 ASP CB C 40.27 0.2 . 745 178 178 ASP N N 122.378 0.2 . 746 179 179 ILE C C 177.2 0.2 . 747 179 179 ILE CA C 61.88 0.2 . 748 179 179 ILE CB C 41.34 0.2 . 749 180 180 ILE H H 8.937 0.05 . 750 180 180 ILE CA C 61.44 0.2 . 751 180 180 ILE CB C 37.97 0.2 . 752 180 180 ILE N N 120.972 0.2 . 753 181 181 GLY H H 9.173 0.05 . 754 181 181 GLY CA C 44.23 0.2 . 755 181 181 GLY N N 118.284 0.2 . 756 190 190 VAL C C 174.5 0.2 . 757 191 191 LYS H H 8.973 0.05 . 758 191 191 LYS C C 173.7 0.2 . 759 191 191 LYS N N 128.509 0.2 . 760 192 192 ASN H H 7.859 0.05 . 761 192 192 ASN CA C 50.75 0.2 . 762 192 192 ASN CB C 42.14 0.2 . 763 192 192 ASN N N 110.211 0.2 . 764 193 193 LEU H H 9.633 0.05 . 765 193 193 LEU C C 173.7 0.2 . 766 193 193 LEU CA C 55.05 0.2 . 767 193 193 LEU CB C 45.47 0.2 . 768 193 193 LEU N N 121.711 0.2 . 769 194 194 GLU H H 9.104 0.05 . 770 194 194 GLU CA C 55.77 0.2 . 771 194 194 GLU CB C 34.17 0.2 . 772 194 194 GLU N N 124.21 0.2 . 773 195 195 PHE H H 9.431 0.05 . 774 195 195 PHE C C 172.8 0.2 . 775 195 195 PHE CA C 55.35 0.2 . 776 195 195 PHE CB C 43.08 0.2 . 777 195 195 PHE N N 123.696 0.2 . 778 196 196 SER H H 8.892 0.05 . 779 196 196 SER C C 172.8 0.2 . 780 196 196 SER CA C 56.91 0.2 . 781 196 196 SER CB C 61.65 0.2 . 782 196 196 SER N N 122.66 0.2 . 783 197 197 VAL H H 8.717 0.05 . 784 197 197 VAL C C 174.9 0.2 . 785 197 197 VAL CA C 59.75 0.2 . 786 197 197 VAL CB C 33.91 0.2 . 787 197 197 VAL N N 125.661 0.2 . 788 198 198 ARG H H 8.897 0.05 . 789 198 198 ARG C C 174.3 0.2 . 790 198 198 ARG CA C 52.42 0.2 . 791 198 198 ARG CB C 34.36 0.2 . 792 198 198 ARG N N 124.976 0.2 . 793 199 199 ILE H H 7.738 0.05 . 794 199 199 ILE C C 170.8 0.2 . 795 199 199 ILE CA C 59.76 0.2 . 796 199 199 ILE CB C 39.25 0.2 . 797 199 199 ILE N N 119.059 0.2 . 798 200 200 GLY H H 8.285 0.05 . 799 200 200 GLY C C 177.7 0.2 . 800 200 200 GLY CA C 45.55 0.2 . 801 200 200 GLY N N 111.191 0.2 . 802 201 201 ASP H H 9.493 0.05 . 803 201 201 ASP C C 176.4 0.2 . 804 201 201 ASP CA C 53.78 0.2 . 805 201 201 ASP CB C 42.38 0.2 . 806 201 201 ASP N N 122.13 0.2 . 807 202 202 MET H H 8.732 0.05 . 808 202 202 MET C C 174.5 0.2 . 809 202 202 MET CA C 58.26 0.2 . 810 202 202 MET CB C 34.38 0.2 . 811 202 202 MET N N 123.499 0.2 . 812 203 203 CYS H H 9.359 0.05 . 813 203 203 CYS C C 173.8 0.2 . 814 203 203 CYS CA C 57.17 0.2 . 815 203 203 CYS CB C 43.28 0.2 . 816 203 203 CYS N N 116.482 0.2 . 817 204 204 LYS H H 7.871 0.05 . 818 204 204 LYS C C 177.3 0.2 . 819 204 204 LYS CA C 55.55 0.2 . 820 204 204 LYS CB C 32.79 0.2 . 821 204 204 LYS N N 121.69 0.2 . 822 205 205 GLU H H 8.299 0.05 . 823 205 205 GLU C C 175.4 0.2 . 824 205 205 GLU CA C 57.21 0.2 . 825 205 205 GLU CB C 29.21 0.2 . 826 205 205 GLU N N 123.802 0.2 . 827 206 206 SER H H 8.96 0.05 . 828 206 206 SER CA C 57.03 0.2 . 829 206 206 SER CB C 63.96 0.2 . 830 206 206 SER N N 121.059 0.2 . 831 207 207 SER C C 175.9 0.2 . 832 207 207 SER CA C 61.22 0.2 . 833 207 207 SER CB C 62.7 0.2 . 834 208 208 GLU H H 8.965 0.05 . 835 208 208 GLU C C 173.4 0.2 . 836 208 208 GLU CA C 57.71 0.2 . 837 208 208 GLU CB C 28.79 0.2 . 838 208 208 GLU N N 120.112 0.2 . 839 209 209 LEU H H 7.99 0.05 . 840 209 209 LEU C C 177 0.2 . 841 209 209 LEU CA C 53.25 0.2 . 842 209 209 LEU CB C 41.55 0.2 . 843 209 209 LEU N N 117.609 0.2 . 844 210 210 GLU H H 6.763 0.05 . 845 210 210 GLU C C 177.4 0.2 . 846 210 210 GLU CA C 53.7 0.2 . 847 210 210 GLU CB C 28.41 0.2 . 848 210 210 GLU N N 112.162 0.2 . 849 211 211 VAL H H 8.445 0.05 . 850 211 211 VAL C C 173.4 0.2 . 851 211 211 VAL CA C 58.62 0.2 . 852 211 211 VAL CB C 36.42 0.2 . 853 211 211 VAL N N 113.5 0.2 . 854 212 212 LYS H H 8.664 0.05 . 855 212 212 LYS C C 175.5 0.2 . 856 212 212 LYS CA C 54.58 0.2 . 857 212 212 LYS CB C 37.29 0.2 . 858 212 212 LYS N N 124.212 0.2 . 859 213 213 ASP H H 9.085 0.05 . 860 213 213 ASP C C 170.8 0.2 . 861 213 213 ASP CA C 51.53 0.2 . 862 213 213 ASP CB C 44.93 0.2 . 863 213 213 ASP N N 124.619 0.2 . 864 214 214 GLY H H 9.839 0.05 . 865 214 214 GLY C C 173.4 0.2 . 866 214 214 GLY CA C 45.89 0.2 . 867 214 214 GLY N N 111.77 0.2 . 868 215 215 PHE H H 8.648 0.05 . 869 215 215 PHE CA C 56.43 0.2 . 870 215 215 PHE CB C 43.15 0.2 . 871 215 215 PHE N N 119.97 0.2 . 872 216 216 LYS H H 8.428 0.05 . 873 216 216 LYS C C 174.4 0.2 . 874 216 216 LYS CA C 54.83 0.2 . 875 216 216 LYS CB C 34.7 0.2 . 876 216 216 LYS N N 124.924 0.2 . 877 217 217 TYR H H 9.327 0.05 . 878 217 217 TYR N N 126.306 0.2 . 879 221 221 SER CA C 57.19 0.2 . 880 221 221 SER CB C 63.34 0.2 . 881 222 222 ALA H H 8.152 0.05 . 882 222 222 ALA C C 173.2 0.2 . 883 222 222 ALA CA C 52.46 0.2 . 884 222 222 ALA CB C 18.58 0.2 . 885 222 222 ALA N N 123.712 0.2 . 886 223 223 SER H H 8.541 0.05 . 887 223 223 SER C C 177 0.2 . 888 223 223 SER CA C 57.7 0.2 . 889 223 223 SER CB C 65.13 0.2 . 890 223 223 SER N N 114.777 0.2 . 891 224 224 LYS H H 8.555 0.05 . 892 224 224 LYS C C 172.2 0.2 . 893 224 224 LYS CA C 55.82 0.2 . 894 224 224 LYS CB C 33.91 0.2 . 895 224 224 LYS N N 121.24 0.2 . 896 225 225 GLY H H 7.929 0.05 . 897 225 225 GLY C C 175.7 0.2 . 898 225 225 GLY CA C 44.88 0.2 . 899 225 225 GLY N N 105.921 0.2 . 900 226 226 ALA H H 8.545 0.05 . 901 226 226 ALA C C 172.8 0.2 . 902 226 226 ALA CA C 50.94 0.2 . 903 226 226 ALA CB C 18.15 0.2 . 904 226 226 ALA N N 124.859 0.2 . 905 227 227 THR H H 8.427 0.05 . 906 227 227 THR CA C 59.35 0.2 . 907 227 227 THR CB C 70.44 0.2 . 908 227 227 THR N N 115.376 0.2 . 909 228 228 ASP H H 8.446 0.05 . 910 228 228 ASP C C 176.8 0.2 . 911 228 228 ASP CA C 53.8 0.2 . 912 228 228 ASP CB C 40.8 0.2 . 913 228 228 ASP N N 119.104 0.2 . 914 229 229 ASP H H 8.446 0.05 . 915 229 229 ASP C C 174.4 0.2 . 916 229 229 ASP CA C 53.98 0.2 . 917 229 229 ASP CB C 42.46 0.2 . 918 229 229 ASP N N 126.778 0.2 . 919 230 230 THR H H 8.427 0.05 . 920 230 230 THR CA C 65.77 0.2 . 921 230 230 THR CB C 68.79 0.2 . 922 230 230 THR N N 114.088 0.2 . 923 231 231 SER C C 177.2 0.2 . 924 231 231 SER CA C 56.8 0.2 . 925 231 231 SER CB C 62.72 0.2 . 926 232 232 LEU H H 7.16 0.05 . 927 232 232 LEU CA C 58.18 0.2 . 928 232 232 LEU CB C 41.68 0.2 . 929 232 232 LEU N N 123.454 0.2 . 930 233 233 ILE H H 7.673 0.05 . 931 233 233 ILE CA C 57.88 0.2 . 932 233 233 ILE CB C 40.96 0.2 . 933 233 233 ILE N N 106.389 0.2 . 934 234 234 ASP H H 8.218 0.05 . 935 234 234 ASP CA C 51.6 0.2 . 936 234 234 ASP CB C 39.01 0.2 . 937 234 234 ASP N N 120.061 0.2 . 938 235 235 SER C C 176.1 0.2 . 939 235 235 SER CA C 61.26 0.2 . 940 235 235 SER CB C 62.05 0.2 . 941 236 236 THR H H 8.349 0.05 . 942 236 236 THR C C 176.6 0.2 . 943 236 236 THR CA C 63.95 0.2 . 944 236 236 THR CB C 68.18 0.2 . 945 236 236 THR N N 112.692 0.2 . 946 237 237 LYS H H 6.907 0.05 . 947 237 237 LYS C C 176.4 0.2 . 948 237 237 LYS CA C 54.81 0.2 . 949 237 237 LYS CB C 32.05 0.2 . 950 237 237 LYS N N 117.724 0.2 . 951 238 238 LEU H H 6.77 0.05 . 952 238 238 LEU C C 175.1 0.2 . 953 238 238 LEU CA C 55.46 0.2 . 954 238 238 LEU CB C 41.39 0.2 . 955 238 238 LEU N N 116.92 0.2 . 956 239 239 LYS H H 8.637 0.05 . 957 239 239 LYS C C 176.8 0.2 . 958 239 239 LYS CA C 53.37 0.2 . 959 239 239 LYS CB C 33.66 0.2 . 960 239 239 LYS N N 119.987 0.2 . 961 240 240 ALA H H 8.655 0.05 . 962 240 240 ALA C C 175.3 0.2 . 963 240 240 ALA CA C 52.92 0.2 . 964 240 240 ALA CB C 18.15 0.2 . 965 240 240 ALA N N 123.45 0.2 . 966 241 241 CYS H H 9.184 0.05 . 967 241 241 CYS CA C 52.32 0.2 . 968 241 241 CYS CB C 35.19 0.2 . 969 241 241 CYS N N 116.929 0.2 . 970 242 242 VAL H H 7.625 0.05 . 971 242 242 VAL CA C 62.23 0.2 . 972 242 242 VAL CB C 33.89 0.2 . 973 242 242 VAL N N 118.701 0.2 . stop_ save_