data_4593 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Rous sarcoma virus capsid protein: C-terminal domain ; _BMRB_accession_number 4593 _BMRB_flat_file_name bmr4593.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Kingston Richard L. . 2 Fitzon-Ostendorp Tanja . . 3 Eisenmesser Elan Z. . 4 Schatz Gisela W. . 5 Vogt Volker M. . 6 Post Carol B. . 7 Rossmann Michael G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 464 "13C chemical shifts" 252 "15N chemical shifts" 80 "coupling constants" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-02 original author . stop_ _Original_release_date 2001-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and Self-association of the Rous Sarcoma Virus Capsid Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20335023 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kingston Richard L. . 2 Fitzon-Ostendorp Tanja . . 3 Eisenmesser Elan Z. . 4 Schatz Gisela W. . 5 Vogt Volker M. . 6 Post Carol B. . 7 Rossmann Michael G. . stop_ _Journal_abbreviation 'Structure Fold Des.' _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 617 _Page_last 628 _Year 2000 _Details . loop_ _Keyword 'Virus/viral protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_RSV_CA _Saveframe_category molecular_system _Mol_system_name 'Rous sarcoma virus capsid protein: C-terminal domain' _Abbreviation_common 'CA RSV' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RSV CA' $RSV_CA 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_RSV_CA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RSV_CA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; MDIMQGPSESFVDFANRLIK AVEGSDLPPSARAPVIIDCF RQKSQPDIQQLIRTAPSTLT TPGEIIKYVLDRQKTAPLTD QGIAAAMSSAIQPLIM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 154 MET 2 155 ASP 3 156 ILE 4 157 MET 5 158 GLN 6 159 GLY 7 160 PRO 8 161 SER 9 162 GLU 10 163 SER 11 164 PHE 12 165 VAL 13 166 ASP 14 167 PHE 15 168 ALA 16 169 ASN 17 170 ARG 18 171 LEU 19 172 ILE 20 173 LYS 21 174 ALA 22 175 VAL 23 176 GLU 24 177 GLY 25 178 SER 26 179 ASP 27 180 LEU 28 181 PRO 29 182 PRO 30 183 SER 31 184 ALA 32 185 ARG 33 186 ALA 34 187 PRO 35 188 VAL 36 189 ILE 37 190 ILE 38 191 ASP 39 192 CYS 40 193 PHE 41 194 ARG 42 195 GLN 43 196 LYS 44 197 SER 45 198 GLN 46 199 PRO 47 200 ASP 48 201 ILE 49 202 GLN 50 203 GLN 51 204 LEU 52 205 ILE 53 206 ARG 54 207 THR 55 208 ALA 56 209 PRO 57 210 SER 58 211 THR 59 212 LEU 60 213 THR 61 214 THR 62 215 PRO 63 216 GLY 64 217 GLU 65 218 ILE 66 219 ILE 67 220 LYS 68 221 TYR 69 222 VAL 70 223 LEU 71 224 ASP 72 225 ARG 73 226 GLN 74 227 LYS 75 228 THR 76 229 ALA 77 230 PRO 78 231 LEU 79 232 THR 80 233 ASP 81 234 GLN 82 235 GLY 83 236 ILE 84 237 ALA 85 238 ALA 86 239 ALA 87 240 MET 88 241 SER 89 242 SER 90 243 ALA 91 244 ILE 92 245 GLN 93 246 PRO 94 247 LEU 95 248 ILE 96 249 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-25 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 1EOQ "Rous Sarcoma Virus Capsid Protein: C-Terminal Domain" 100.00 96 100.00 100.00 9.19e-61 PDB 2X8Q "Cryo-Em 3d Model Of The Icosahedral Particle Composed Of Rous Sarcoma Virus Capsid Protein Pentamers" 75.00 226 100.00 100.00 2.06e-42 PDB 3G0V "Crystal Structure Of The C-Terminal Domain From The Rous Sarcoma Virus Capsid Protein: Mutant D179a" 75.00 77 98.61 98.61 3.14e-42 PDB 3G1G "Crystal Structure Of The C-Terminal Domain From The Rous Sarcoma Virus Capsid Protein: High Ph" 86.46 87 100.00 100.00 2.29e-51 PDB 3G1I "Crystal Structure Of The C-Terminal Domain Of The Rous Sarcoma Virus Capsid Protein: Intermediate Ph" 75.00 77 100.00 100.00 3.03e-43 PDB 3G21 "Crystal Structure Of The C-Terminal Domain Of The Rous Sarcoma Virus Capsid Protein: Low Ph" 75.00 77 100.00 100.00 3.03e-43 PDB 3G26 "Crystal Structure Of The C-terminal Domain Of The Rous Sarcoma Virus Capsid Protein: Mutant A184c" 75.00 77 98.61 98.61 1.36e-42 PDB 3G28 "Crystal Structure Of The C-Terminal Domain Of The Rous Sarcoma Virus Capsid Protein: Mutant D179n, Low Ph" 75.00 77 98.61 100.00 9.81e-43 PDB 3G29 "Crystal Structure Of The C-Terminal Domain Of The Rous Sarcoma Virus Capsid Protein: D179n Mutant, Neutral Ph" 75.00 77 98.61 100.00 9.81e-43 PDB 3TIR "Pseudo-Atomic Model Of The Rous Sarcoma Virus Capsid Hexamer" 75.00 226 100.00 100.00 2.06e-42 PDB 5A9E "Cryo-electron Tomography And Subtomogram Averaging Of Rous- Sarcoma-virus Deltambd Virus-like Particles" 98.96 495 100.00 100.00 3.17e-56 EMBL CAA24512 "polyprotein gag [Rous sarcoma virus]" 98.96 701 100.00 100.00 3.34e-55 EMBL CAA36153 "unnamed protein product [Rous sarcoma virus]" 98.96 701 97.89 98.95 2.51e-54 EMBL CAA48534 "gag [Rous sarcoma virus]" 98.96 701 97.89 98.95 2.51e-54 GB AAA66157 "gag protein, partial [Avian carcinoma virus]" 53.13 68 98.04 98.04 6.19e-26 GB AAB59932 "gag-Pr76 polyprotein precursor [Rous sarcoma virus - Prague C]" 98.96 701 100.00 100.00 3.34e-55 GB AAB59933 "putative gag-pro-Pr180 polyprotein precursor [Rous sarcoma virus - Prague C]" 98.96 1472 100.00 100.00 4.06e-54 GB AAC82560 "Pr76 polyprotein precursor [Rous sarcoma virus]" 98.96 701 100.00 100.00 3.34e-55 GB AAC82561 "Pr180 polyprotein precursor [Rous sarcoma virus]" 98.96 1603 100.00 100.00 5.01e-54 REF NP_056886 "Pr180 polyprotein precursor [Rous sarcoma virus]" 98.96 1603 100.00 100.00 5.01e-54 REF NP_056887 "Pr76 polyprotein precursor [Rous sarcoma virus]" 98.96 701 100.00 100.00 3.34e-55 REF NP_955609 "p27 CA [Rous sarcoma virus]" 89.58 240 100.00 100.00 1.65e-52 SP P03322 "RecName: Full=Gag-Pro polyprotein; Contains: RecName: Full=p3; Contains: RecName: Full=Matrix protein p19; Contains: RecName: F" 98.96 701 100.00 100.00 3.34e-55 SP P03354 "RecName: Full=Gag-Pro-Pol polyprotein; Contains: RecName: Full=Matrix protein p19; Contains: RecName: Full=p2A; Contains: RecNa" 98.96 1603 100.00 100.00 5.01e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RSV_CA . . Virus . 'Avian type C retroviruses' 'Rous sarcoma virus - Prague C strain' 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 $RSV_CA 'recombinant technology' E.coil Escherichia coli . 'pET-3XC (NOVAGEN)' 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 $RSV_CA 1.5 mM [U-15N] 'Sodium phosphate' 50 mM . NaCl 50 mM . EDTA 1 mM . DTT 1 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RSV_CA 1.5 mM '[U-15N; U-13C]' 'Sodium phosphate' 50 mM . NaCl 50 mM . EDTA 1 mM . DTT 1 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.6 loop_ _Task 'data processing' stop_ _Details 'Delaglio, F.' save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'data analysis' stop_ _Details 'Kraulis, P.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details ; Brunger, Adams, Clore, Delano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warren. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.9 . n/a temperature 298 . K 'ionic strength' 0.1 . M pressure 1 . atm 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 H2O H 1 protons ppm 4.752 internal direct . . . . DSS C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 external 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RSV CA' _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 ASP H H 8.970 0.02 1 2 . 2 ASP HA H 4.816 0.02 1 3 . 2 ASP HB2 H 2.579 0.02 2 4 . 2 ASP HB3 H 2.718 0.02 2 5 . 2 ASP CA C 53.96 0.2 1 6 . 2 ASP CB C 40.79 0.2 1 7 . 2 ASP N N 126.61 0.1 1 8 . 3 ILE H H 7.638 0.02 1 9 . 3 ILE HA H 4.239 0.02 1 10 . 3 ILE HB H 1.811 0.02 1 11 . 3 ILE HG12 H 1.173 0.02 2 12 . 3 ILE HG13 H 1.520 0.02 2 13 . 3 ILE HG2 H 0.850 0.02 1 14 . 3 ILE HD1 H 0.772 0.02 1 15 . 3 ILE CA C 60.76 0.2 1 16 . 3 ILE CB C 39.13 0.2 1 17 . 3 ILE CG1 C 28.22 0.2 1 18 . 3 ILE CG2 C 17.24 0.2 1 19 . 3 ILE CD1 C 13.08 0.2 1 20 . 3 ILE N N 123.29 0.1 1 21 . 4 MET H H 8.250 0.02 1 22 . 4 MET HA H 4.867 0.02 1 23 . 4 MET HB2 H 2.023 0.02 1 24 . 4 MET HB3 H 2.023 0.02 1 25 . 4 MET HG2 H 2.464 0.02 2 26 . 4 MET HG3 H 2.522 0.02 2 27 . 4 MET CA C 54.50 0.2 1 28 . 4 MET CB C 36.00 0.2 1 29 . 4 MET CG C 31.56 0.2 1 30 . 4 MET N N 121.72 0.1 1 31 . 5 GLN H H 7.544 0.02 1 32 . 5 GLN HA H 3.737 0.02 1 33 . 5 GLN HB2 H 0.093 0.02 2 34 . 5 GLN HB3 H 1.533 0.02 2 35 . 5 GLN HG2 H 1.989 0.02 2 36 . 5 GLN HG3 H 2.922 0.02 2 37 . 5 GLN HE21 H 6.178 0.02 2 38 . 5 GLN HE22 H 7.465 0.02 2 39 . 5 GLN CA C 56.200 0.2 1 40 . 5 GLN CB C 27.900 0.2 1 41 . 5 GLN CG C 32.300 0.2 1 42 . 5 GLN N N 126.25 0.1 1 43 . 5 GLN NE2 N 105.35 0.1 1 44 . 6 GLY H H 9.732 0.02 1 45 . 6 GLY HA2 H 4.350 0.02 2 46 . 6 GLY HA3 H 3.922 0.02 2 47 . 6 GLY CA C 44.960 0.2 1 48 . 6 GLY N N 118.84 0.1 1 49 . 7 PRO HA H 4.196 0.02 1 50 . 7 PRO HB2 H 2.321 0.02 2 51 . 7 PRO HB3 H 2.029 0.02 2 52 . 7 PRO HG2 H 2.091 0.02 1 53 . 7 PRO HG3 H 2.091 0.02 1 54 . 7 PRO HD2 H 3.777 0.02 2 55 . 7 PRO HD3 H 3.707 0.02 2 56 . 7 PRO CA C 65.03 0.2 1 57 . 7 PRO CB C 31.74 0.2 1 58 . 7 PRO CG C 27.62 0.2 1 59 . 7 PRO CD C 49.96 0.2 1 60 . 8 SER H H 8.384 0.02 1 61 . 8 SER HA H 4.715 0.02 1 62 . 8 SER HB2 H 3.928 0.02 1 63 . 8 SER HB3 H 3.928 0.02 1 64 . 8 SER CA C 56.85 0.2 1 65 . 8 SER CB C 63.67 0.2 1 66 . 8 SER N N 112.57 0.1 1 67 . 9 GLU H H 7.299 0.02 1 68 . 9 GLU HA H 4.499 0.02 1 69 . 9 GLU HB2 H 2.365 0.02 2 70 . 9 GLU HB3 H 1.777 0.02 2 71 . 9 GLU HG2 H 2.388 0.02 2 72 . 9 GLU HG3 H 2.787 0.02 2 73 . 9 GLU CA C 54.75 0.2 1 74 . 9 GLU CB C 32.12 0.2 1 75 . 9 GLU CG C 36.21 0.2 1 76 . 9 GLU N N 125.82 0.1 1 77 . 10 SER H H 9.767 0.02 1 78 . 10 SER HA H 4.468 0.02 1 79 . 10 SER HB2 H 4.134 0.02 2 80 . 10 SER HB3 H 4.366 0.02 2 81 . 10 SER CA C 58.13 0.2 1 82 . 10 SER CB C 64.19 0.2 1 83 . 10 SER N N 127.28 0.1 1 84 . 11 PHE H H 9.430 0.02 1 85 . 11 PHE HA H 4.330 0.02 1 86 . 11 PHE HB2 H 2.943 0.02 2 87 . 11 PHE HB3 H 3.291 0.02 2 88 . 11 PHE HD1 H 7.127 0.02 1 89 . 11 PHE HD2 H 7.127 0.02 1 90 . 11 PHE HE1 H 7.040 0.02 1 91 . 11 PHE HE2 H 7.040 0.02 1 92 . 11 PHE HZ H 5.912 0.02 1 93 . 11 PHE CA C 62.93 0.2 1 94 . 11 PHE CB C 39.13 0.2 1 95 . 11 PHE N N 124.30 0.1 1 96 . 12 VAL H H 8.468 0.02 1 97 . 12 VAL HA H 3.480 0.02 1 98 . 12 VAL HB H 2.033 0.02 1 99 . 12 VAL HG1 H 1.084 0.02 2 100 . 12 VAL HG2 H 0.968 0.02 2 101 . 12 VAL CA C 66.36 0.2 1 102 . 12 VAL CB C 31.86 0.2 1 103 . 12 VAL CG1 C 23.13 0.2 2 104 . 12 VAL CG2 C 20.88 0.2 2 105 . 12 VAL N N 116.50 0.1 1 106 . 13 ASP H H 7.389 0.02 1 107 . 13 ASP HA H 4.508 0.02 1 108 . 13 ASP HB2 H 2.874 0.02 1 109 . 13 ASP HB3 H 2.874 0.02 1 110 . 13 ASP CA C 57.650 0.2 1 111 . 13 ASP CB C 39.750 0.2 1 112 . 13 ASP N N 121.55 0.1 1 113 . 14 PHE H H 8.249 0.02 1 114 . 14 PHE HA H 4.513 0.02 1 115 . 14 PHE HB2 H 3.004 0.02 2 116 . 14 PHE HB3 H 3.280 0.02 2 117 . 14 PHE HD1 H 7.119 0.02 1 118 . 14 PHE HD2 H 7.119 0.02 1 119 . 14 PHE HE1 H 7.141 0.02 1 120 . 14 PHE HE2 H 7.141 0.02 1 121 . 14 PHE HZ H 7.006 0.02 1 122 . 14 PHE CA C 59.52 0.2 1 123 . 14 PHE CB C 39.26 0.2 1 124 . 14 PHE N N 123.90 0.1 1 125 . 15 ALA H H 8.931 0.02 1 126 . 15 ALA HA H 3.366 0.02 1 127 . 15 ALA HB H 0.945 0.02 1 128 . 15 ALA CA C 55.29 0.2 1 129 . 15 ALA CB C 17.38 0.2 1 130 . 15 ALA N N 121.74 0.1 1 131 . 16 ASN H H 7.902 0.02 1 132 . 16 ASN HA H 4.381 0.02 1 133 . 16 ASN HB2 H 2.718 0.02 2 134 . 16 ASN HB3 H 2.873 0.02 2 135 . 16 ASN HD21 H 7.758 0.02 2 136 . 16 ASN HD22 H 6.843 0.02 2 137 . 16 ASN CA C 56.39 0.2 1 138 . 16 ASN CB C 38.50 0.2 1 139 . 16 ASN N N 114.02 0.1 1 140 . 16 ASN ND2 N 112.76 0.1 1 141 . 17 ARG H H 7.939 0.02 1 142 . 17 ARG HA H 4.038 0.02 1 143 . 17 ARG HB2 H 1.943 0.02 2 144 . 17 ARG HB3 H 2.002 0.02 2 145 . 17 ARG HG2 H 1.571 0.02 2 146 . 17 ARG HG3 H 1.693 0.02 2 147 . 17 ARG HD2 H 3.134 0.02 2 148 . 17 ARG HD3 H 3.435 0.02 2 149 . 17 ARG HE H 9.851 0.02 1 150 . 17 ARG CA C 59.920 0.2 1 151 . 17 ARG CB C 31.150 0.2 1 152 . 17 ARG CG C 28.550 0.2 1 153 . 17 ARG CD C 43.920 0.2 1 154 . 17 ARG N N 121.62 0.1 1 155 . 17 ARG NE N 84.831 0.1 1 156 . 18 LEU H H 8.604 0.02 1 157 . 18 LEU HA H 3.846 0.02 1 158 . 18 LEU HB2 H 0.860 0.02 2 159 . 18 LEU HB3 H 1.485 0.02 2 160 . 18 LEU HG H 0.688 0.02 1 161 . 18 LEU HD1 H 0.349 0.02 2 162 . 18 LEU HD2 H 1.120 0.02 2 163 . 18 LEU CA C 57.92 0.2 1 164 . 18 LEU CB C 41.63 0.2 1 165 . 18 LEU CG C 24.49 0.2 1 166 . 18 LEU CD1 C 27.11 0.2 2 167 . 18 LEU CD2 C 27.26 0.2 2 168 . 18 LEU N N 122.99 0.1 1 169 . 19 ILE H H 8.457 0.02 1 170 . 19 ILE HA H 3.307 0.02 1 171 . 19 ILE HB H 1.815 0.02 1 172 . 19 ILE HG12 H 0.962 0.02 2 173 . 19 ILE HG13 H 1.763 0.02 2 174 . 19 ILE HG2 H 0.842 0.02 1 175 . 19 ILE HD1 H 0.842 0.02 1 176 . 19 ILE CA C 66.50 0.2 1 177 . 19 ILE CB C 37.88 0.2 1 178 . 19 ILE CG1 C 30.80 0.2 1 179 . 19 ILE CG2 C 17.31 0.2 1 180 . 19 ILE CD1 C 13.77 0.2 1 181 . 19 ILE N N 119.22 0.1 1 182 . 20 LYS H H 7.668 0.02 1 183 . 20 LYS HA H 4.014 0.02 1 184 . 20 LYS HB2 H 1.838 0.02 1 185 . 20 LYS HB3 H 1.838 0.02 1 186 . 20 LYS HG2 H 1.431 0.02 2 187 . 20 LYS HG3 H 1.539 0.02 2 188 . 20 LYS HD2 H 1.658 0.02 1 189 . 20 LYS HD3 H 1.658 0.02 1 190 . 20 LYS HE2 H 2.962 0.02 1 191 . 20 LYS HE3 H 2.962 0.02 1 192 . 20 LYS CA C 59.42 0.2 1 193 . 20 LYS CB C 32.39 0.2 1 194 . 20 LYS CG C 25.30 0.2 1 195 . 20 LYS CD C 29.16 0.2 1 196 . 20 LYS CE C 42.25 0.2 1 197 . 20 LYS N N 118.14 0.1 1 198 . 21 ALA H H 7.900 0.02 1 199 . 21 ALA HA H 4.100 0.02 1 200 . 21 ALA HB H 1.489 0.02 1 201 . 21 ALA CA C 54.92 0.2 1 202 . 21 ALA CB C 18.34 0.2 1 203 . 21 ALA N N 122.23 0.1 1 204 . 22 VAL H H 8.446 0.02 1 205 . 22 VAL HA H 3.585 0.02 1 206 . 22 VAL HB H 1.989 0.02 1 207 . 22 VAL HG1 H 0.932 0.02 2 208 . 22 VAL HG2 H 0.912 0.02 2 209 . 22 VAL CA C 66.69 0.2 1 210 . 22 VAL CB C 31.81 0.2 1 211 . 22 VAL CG1 C 23.77 0.2 2 212 . 22 VAL CG2 C 21.55 0.2 2 213 . 22 VAL N N 118.75 0.1 1 214 . 23 GLU H H 8.895 0.02 1 215 . 23 GLU HA H 3.949 0.02 1 216 . 23 GLU HB2 H 2.045 0.02 2 217 . 23 GLU HB3 H 2.164 0.02 2 218 . 23 GLU HG2 H 2.527 0.02 2 219 . 23 GLU HG3 H 2.179 0.02 2 220 . 23 GLU CA C 59.540 0.2 1 221 . 23 GLU CB C 29.150 0.2 1 222 . 23 GLU CG C 36.830 0.2 1 223 . 23 GLU N N 121.85 0.1 1 224 . 24 GLY H H 7.510 0.02 1 225 . 24 GLY HA2 H 3.707 0.02 2 226 . 24 GLY HA3 H 4.367 0.02 2 227 . 24 GLY CA C 45.17 0.2 1 228 . 24 GLY N N 104.10 0.1 1 229 . 25 SER H H 7.386 0.02 1 230 . 25 SER HA H 4.645 0.02 1 231 . 25 SER HB2 H 4.206 0.02 1 232 . 25 SER HB3 H 4.206 0.02 1 233 . 25 SER CA C 58.68 0.2 1 234 . 25 SER CB C 65.45 0.2 1 235 . 25 SER N N 117.06 0.1 1 236 . 26 ASP H H 8.391 0.02 1 237 . 26 ASP HA H 4.665 0.02 1 238 . 26 ASP HB2 H 2.786 0.02 1 239 . 26 ASP HB3 H 2.786 0.02 1 240 . 26 ASP CA C 53.78 0.2 1 241 . 26 ASP CB C 40.17 0.2 1 242 . 26 ASP N N 117.40 0.1 1 243 . 27 LEU H H 7.791 0.02 1 244 . 27 LEU HA H 4.425 0.02 1 245 . 27 LEU HB2 H 1.519 0.02 2 246 . 27 LEU HB3 H 1.244 0.02 2 247 . 27 LEU HG H 1.787 0.02 1 248 . 27 LEU HD1 H 0.912 0.02 1 249 . 27 LEU HD2 H 0.912 0.02 1 250 . 27 LEU CA C 53.77 0.2 1 251 . 27 LEU CB C 42.67 0.2 1 252 . 27 LEU CG C 27.11 0.2 1 253 . 27 LEU CD1 C 23.67 0.2 1 254 . 27 LEU CD2 C 23.67 0.2 1 255 . 27 LEU N N 122.15 0.1 1 256 . 28 PRO HA H 4.782 0.02 1 257 . 28 PRO HB2 H 1.920 0.02 2 258 . 28 PRO HB3 H 2.451 0.02 2 259 . 28 PRO HG2 H 2.095 0.02 1 260 . 28 PRO HG3 H 2.095 0.02 1 261 . 28 PRO HD2 H 3.516 0.02 2 262 . 28 PRO HD3 H 3.968 0.02 2 263 . 28 PRO CB C 31.01 0.2 1 264 . 28 PRO CG C 27.80 0.2 1 265 . 28 PRO CD C 50.58 0.2 1 266 . 29 PRO HA H 3.904 0.02 1 267 . 29 PRO HB2 H 2.040 0.02 2 268 . 29 PRO HB3 H 2.394 0.02 2 269 . 29 PRO HG2 H 2.273 0.02 1 270 . 29 PRO HG3 H 2.273 0.02 1 271 . 29 PRO HD2 H 3.950 0.02 2 272 . 29 PRO HD3 H 3.828 0.02 2 273 . 29 PRO CA C 66.50 0.2 1 274 . 29 PRO CB C 32.27 0.2 1 275 . 29 PRO CG C 28.00 0.2 1 276 . 29 PRO CD C 50.38 0.2 1 277 . 30 SER H H 8.409 0.02 1 278 . 30 SER HA H 4.222 0.02 1 279 . 30 SER HB2 H 3.947 0.02 2 280 . 30 SER HB3 H 4.011 0.02 2 281 . 30 SER CA C 60.50 0.2 1 282 . 30 SER CB C 62.74 0.2 1 283 . 30 SER N N 110.72 0.1 1 284 . 31 ALA H H 7.992 0.02 1 285 . 31 ALA HA H 4.523 0.02 1 286 . 31 ALA HB H 1.520 0.02 1 287 . 31 ALA CA C 52.04 0.2 1 288 . 31 ALA CB C 20.75 0.2 1 289 . 31 ALA N N 123.15 0.1 1 290 . 32 ARG H H 7.243 0.02 1 291 . 32 ARG HA H 3.685 0.02 1 292 . 32 ARG HB2 H 1.680 0.02 2 293 . 32 ARG HB3 H 1.856 0.02 2 294 . 32 ARG HG2 H 1.234 0.02 2 295 . 32 ARG HG3 H 2.013 0.02 2 296 . 32 ARG HD2 H 3.065 0.02 2 297 . 32 ARG HD3 H 3.256 0.02 2 298 . 32 ARG HE H 7.037 0.02 1 299 . 32 ARG CA C 60.880 0.2 1 300 . 32 ARG CB C 30.790 0.2 1 301 . 32 ARG CG C 28.510 0.2 1 302 . 32 ARG CD C 44.330 0.2 1 303 . 32 ARG N N 117.08 0.1 1 304 . 32 ARG NE N 83.09 0.1 1 305 . 33 ALA H H 8.781 0.02 1 306 . 33 ALA HA H 4.146 0.02 1 307 . 33 ALA HB H 1.538 0.02 1 308 . 33 ALA CA C 57.26 0.2 1 309 . 33 ALA CB C 15.74 0.2 1 310 . 33 ALA N N 119.75 0.1 1 311 . 34 PRO HA H 4.214 0.02 1 312 . 34 PRO HB2 H 1.896 0.02 2 313 . 34 PRO HB3 H 2.318 0.02 2 314 . 34 PRO HG2 H 2.025 0.02 2 315 . 34 PRO HG3 H 2.190 0.02 2 316 . 34 PRO HD2 H 3.587 0.02 2 317 . 34 PRO HD3 H 3.655 0.02 2 318 . 34 PRO CA C 66.16 0.2 1 319 . 34 PRO CB C 31.07 0.2 1 320 . 34 PRO CG C 28.15 0.2 1 321 . 34 PRO CD C 49.96 0.2 1 322 . 35 VAL H H 7.128 0.02 1 323 . 35 VAL HA H 3.810 0.02 1 324 . 35 VAL HB H 2.176 0.02 1 325 . 35 VAL HG1 H 1.118 0.02 2 326 . 35 VAL HG2 H 0.889 0.02 2 327 . 35 VAL CA C 66.39 0.2 1 328 . 35 VAL CB C 31.92 0.2 1 329 . 35 VAL CG1 C 23.50 0.2 2 330 . 35 VAL CG2 C 21.43 0.2 2 331 . 35 VAL N N 118.02 0.1 1 332 . 36 ILE H H 8.159 0.02 1 333 . 36 ILE HA H 3.145 0.02 1 334 . 36 ILE HB H 1.790 0.02 1 335 . 36 ILE HG12 H 0.495 0.02 2 336 . 36 ILE HG13 H 1.789 0.02 2 337 . 36 ILE HG2 H 0.269 0.02 1 338 . 36 ILE HD1 H 0.791 0.02 1 339 . 36 ILE CA C 66.06 0.2 1 340 . 36 ILE CB C 38.24 0.2 1 341 . 36 ILE CG1 C 30.66 0.2 1 342 . 36 ILE CG2 C 18.50 0.2 1 343 . 36 ILE CD1 C 14.59 0.2 1 344 . 36 ILE N N 121.93 0.1 1 345 . 37 ILE H H 8.348 0.02 1 346 . 37 ILE HA H 3.479 0.02 1 347 . 37 ILE HB H 1.849 0.02 1 348 . 37 ILE HG12 H 0.992 0.02 2 349 . 37 ILE HG13 H 1.641 0.02 2 350 . 37 ILE HG2 H 0.935 0.02 1 351 . 37 ILE HD1 H 0.650 0.02 1 352 . 37 ILE CA C 65.78 0.2 1 353 . 37 ILE CB C 37.45 0.2 1 354 . 37 ILE CG1 C 29.76 0.2 1 355 . 37 ILE CG2 C 17.38 0.2 1 356 . 37 ILE CD1 C 12.89 0.2 1 357 . 37 ILE N N 117.76 0.1 1 358 . 38 ASP H H 8.122 0.02 1 359 . 38 ASP HA H 4.491 0.02 1 360 . 38 ASP HB2 H 2.851 0.02 2 361 . 38 ASP HB3 H 2.718 0.02 2 362 . 38 ASP CA C 58.08 0.2 1 363 . 38 ASP CB C 41.42 0.2 1 364 . 38 ASP N N 119.84 0.1 1 365 . 39 CYS H H 8.149 0.02 1 366 . 39 CYS HA H 4.242 0.02 1 367 . 39 CYS HB2 H 2.577 0.02 2 368 . 39 CYS HB3 H 3.140 0.02 2 369 . 39 CYS CA C 64.18 0.2 1 370 . 39 CYS CB C 27.61 0.2 1 371 . 39 CYS N N 117.70 0.1 1 372 . 40 PHE H H 8.691 0.02 1 373 . 40 PHE HA H 4.760 0.02 1 374 . 40 PHE HB2 H 3.256 0.02 2 375 . 40 PHE HB3 H 3.690 0.02 2 376 . 40 PHE HD1 H 7.137 0.02 1 377 . 40 PHE HD2 H 7.137 0.02 1 378 . 40 PHE HE1 H 6.941 0.02 1 379 . 40 PHE HE2 H 6.941 0.02 1 380 . 40 PHE HZ H 6.850 0.02 1 381 . 40 PHE CA C 59.95 0.2 1 382 . 40 PHE CB C 37.88 0.2 1 383 . 40 PHE N N 119.24 0.1 1 384 . 41 ARG H H 8.481 0.02 1 385 . 41 ARG HA H 4.065 0.02 1 386 . 41 ARG HB2 H 1.977 0.02 2 387 . 41 ARG HB3 H 2.124 0.02 2 388 . 41 ARG HG2 H 1.613 0.02 2 389 . 41 ARG HG3 H 1.985 0.02 2 390 . 41 ARG HD2 H 3.255 0.02 1 391 . 41 ARG HD3 H 3.255 0.02 1 392 . 41 ARG HE H 7.142 0.02 1 393 . 41 ARG CA C 60.160 0.2 1 394 . 41 ARG CB C 31.560 0.2 1 395 . 41 ARG CG C 29.270 0.2 1 396 . 41 ARG CD C 43.71 0.2 1 397 . 41 ARG N N 115.93 0.1 1 398 . 41 ARG NE N 84.03 0.1 1 399 . 42 GLN H H 8.237 0.02 1 400 . 42 GLN HA H 4.648 0.02 1 401 . 42 GLN HB2 H 2.112 0.02 2 402 . 42 GLN HB3 H 2.273 0.02 2 403 . 42 GLN HG2 H 2.387 0.02 2 404 . 42 GLN HG3 H 2.577 0.02 2 405 . 42 GLN HE21 H 6.786 0.02 2 406 . 42 GLN HE22 H 7.815 0.02 2 407 . 42 GLN CA C 57.090 0.2 1 408 . 42 GLN CB C 31.870 0.2 1 409 . 42 GLN CG C 34.120 0.2 1 410 . 42 GLN N N 111.63 0.1 1 411 . 42 GLN NE2 N 112.54 0.1 1 412 . 43 LYS H H 8.852 0.02 1 413 . 43 LYS HA H 4.881 0.02 1 414 . 43 LYS HB2 H 2.315 0.02 2 415 . 43 LYS HB3 H 2.597 0.02 2 416 . 43 LYS HG2 H 1.506 0.02 2 417 . 43 LYS HG3 H 1.670 0.02 2 418 . 43 LYS HD2 H 1.807 0.02 2 419 . 43 LYS HD3 H 1.863 0.02 2 420 . 43 LYS HE2 H 3.048 0.02 2 421 . 43 LYS HE3 H 3.117 0.02 2 422 . 43 LYS CA C 55.12 0.2 1 423 . 43 LYS CB C 33.06 0.2 1 424 . 43 LYS CG C 25.62 0.2 1 425 . 43 LYS CD C 28.74 0.2 1 426 . 43 LYS CE C 42.88 0.2 1 427 . 43 LYS N N 116.31 0.1 1 428 . 44 SER H H 7.016 0.02 1 429 . 44 SER HA H 4.500 0.02 1 430 . 44 SER HB2 H 4.222 0.02 2 431 . 44 SER HB3 H 4.124 0.02 2 432 . 44 SER CA C 57.74 0.2 1 433 . 44 SER CB C 65.16 0.2 1 434 . 44 SER N N 112.97 0.1 1 435 . 45 GLN H H 8.556 0.02 1 436 . 45 GLN HA H 4.248 0.02 1 437 . 45 GLN HB2 H 1.809 0.02 2 438 . 45 GLN HB3 H 2.451 0.02 2 439 . 45 GLN HG2 H 2.422 0.02 2 440 . 45 GLN HG3 H 1.901 0.02 2 441 . 45 GLN HE21 H 7.072 0.02 2 442 . 45 GLN HE22 H 7.378 0.02 2 443 . 45 GLN CA C 55.540 0.2 1 444 . 45 GLN CB C 28.290 0.2 1 445 . 45 GLN CG C 34.540 0.2 1 446 . 45 GLN N N 121.18 0.1 1 447 . 45 GLN NE2 N 114.43 0.1 1 448 . 46 PRO HA H 4.117 0.02 1 449 . 46 PRO HB2 H 2.031 0.02 2 450 . 46 PRO HB3 H 2.408 0.02 2 451 . 46 PRO HG2 H 2.212 0.02 1 452 . 46 PRO HG3 H 2.212 0.02 1 453 . 46 PRO HD2 H 3.794 0.02 1 454 . 46 PRO HD3 H 3.794 0.02 1 455 . 46 PRO CA C 66.85 0.2 1 456 . 46 PRO CB C 32.38 0.2 1 457 . 46 PRO CG C 28.01 0.2 1 458 . 46 PRO CD C 50.37 0.2 1 459 . 47 ASP H H 9.048 0.02 1 460 . 47 ASP HA H 4.331 0.02 1 461 . 47 ASP HB2 H 2.719 0.02 2 462 . 47 ASP HB3 H 2.579 0.02 2 463 . 47 ASP CA C 56.79 0.2 1 464 . 47 ASP CB C 38.92 0.2 1 465 . 47 ASP N N 115.78 0.1 1 466 . 48 ILE H H 7.430 0.02 1 467 . 48 ILE HA H 3.741 0.02 1 468 . 48 ILE HB H 2.422 0.02 1 469 . 48 ILE HG12 H 1.721 0.02 2 470 . 48 ILE HG13 H 1.560 0.02 2 471 . 48 ILE HG2 H 0.731 0.02 1 472 . 48 ILE HD1 H 0.652 0.02 1 473 . 48 ILE CA C 61.97 0.2 1 474 . 48 ILE CB C 35.38 0.2 1 475 . 48 ILE CG1 C 27.45 0.2 1 476 . 48 ILE CG2 C 18.15 0.2 1 477 . 48 ILE CD1 C 9.75 0.2 1 478 . 48 ILE N N 122.69 0.1 1 479 . 49 GLN H H 8.403 0.02 1 480 . 49 GLN HA H 3.755 0.02 1 481 . 49 GLN HB2 H 2.162 0.02 1 482 . 49 GLN HB3 H 2.162 0.02 1 483 . 49 GLN HG2 H 2.266 0.02 2 484 . 49 GLN HG3 H 2.422 0.02 2 485 . 49 GLN HE21 H 6.544 0.02 2 486 . 49 GLN HE22 H 7.658 0.02 2 487 . 49 GLN CA C 60.510 0.2 1 488 . 49 GLN CB C 29.000 0.2 1 489 . 49 GLN CG C 34.330 0.2 1 490 . 49 GLN N N 120.73 0.1 1 491 . 49 GLN NE2 N 110.81 0.1 1 492 . 50 GLN H H 7.788 0.02 1 493 . 50 GLN HA H 4.040 0.02 1 494 . 50 GLN HB2 H 2.141 0.02 1 495 . 50 GLN HB3 H 2.141 0.02 1 496 . 50 GLN HG2 H 2.467 0.02 1 497 . 50 GLN HG3 H 2.467 0.02 1 498 . 50 GLN HE21 H 6.860 0.02 2 499 . 50 GLN HE22 H 7.436 0.02 2 500 . 50 GLN CA C 58.88 0.2 1 501 . 50 GLN CB C 28.19 0.2 1 502 . 50 GLN CG C 33.42 0.2 1 503 . 50 GLN N N 116.27 0.1 1 504 . 50 GLN NE2 N 111.81 0.1 1 505 . 51 LEU H H 7.455 0.02 1 506 . 51 LEU HA H 4.180 0.02 1 507 . 51 LEU HB2 H 2.040 0.02 2 508 . 51 LEU HB3 H 1.537 0.02 2 509 . 51 LEU HG H 1.834 0.02 1 510 . 51 LEU HD1 H 0.855 0.02 2 511 . 51 LEU HD2 H 0.841 0.02 2 512 . 51 LEU CA C 57.72 0.2 1 513 . 51 LEU CB C 42.88 0.2 1 514 . 51 LEU CG C 26.88 0.2 1 515 . 51 LEU CD1 C 25.56 0.2 2 516 . 51 LEU CD2 C 24.79 0.2 2 517 . 51 LEU N N 120.30 0.1 1 518 . 52 ILE H H 8.584 0.02 1 519 . 52 ILE HA H 3.544 0.02 1 520 . 52 ILE HB H 1.900 0.02 1 521 . 52 ILE HG12 H 0.773 0.02 2 522 . 52 ILE HG13 H 1.687 0.02 2 523 . 52 ILE HG2 H 0.897 0.02 1 524 . 52 ILE HD1 H 0.639 0.02 1 525 . 52 ILE CA C 65.58 0.2 1 526 . 52 ILE CB C 37.87 0.2 1 527 . 52 ILE CG1 C 29.99 0.2 1 528 . 52 ILE CG2 C 17.82 0.2 1 529 . 52 ILE CD1 C 14.46 0.2 1 530 . 52 ILE N N 119.66 0.1 1 531 . 53 ARG H H 8.135 0.02 1 532 . 53 ARG HA H 4.166 0.02 1 533 . 53 ARG HB2 H 2.008 0.02 1 534 . 53 ARG HB3 H 2.008 0.02 1 535 . 53 ARG HG2 H 1.743 0.02 2 536 . 53 ARG HG3 H 1.883 0.02 2 537 . 53 ARG HD2 H 3.256 0.02 1 538 . 53 ARG HD3 H 3.256 0.02 1 539 . 53 ARG HE H 7.259 0.02 1 540 . 53 ARG CA C 59.290 0.2 1 541 . 53 ARG CB C 30.610 0.2 1 542 . 53 ARG CG C 28.420 0.2 1 543 . 53 ARG CD C 43.710 0.2 1 544 . 53 ARG N N 119.40 0.1 1 545 . 53 ARG NE N 84.34 0.1 1 546 . 54 THR H H 7.357 0.02 1 547 . 54 THR HA H 4.460 0.02 1 548 . 54 THR HB H 4.606 0.02 1 549 . 54 THR HG2 H 1.332 0.02 1 550 . 54 THR CA C 61.21 0.2 1 551 . 54 THR CB C 70.09 0.2 1 552 . 54 THR CG2 C 21.70 0.2 1 553 . 54 THR N N 106.14 0.1 1 554 . 55 ALA H H 7.276 0.02 1 555 . 55 ALA HA H 4.021 0.02 1 556 . 55 ALA HB H 0.907 0.02 1 557 . 55 ALA CA C 51.00 0.2 1 558 . 55 ALA CB C 17.22 0.2 1 559 . 55 ALA N N 126.72 0.1 1 560 . 56 PRO HA H 4.452 0.02 1 561 . 56 PRO HB2 H 1.905 0.02 2 562 . 56 PRO HB3 H 2.338 0.02 2 563 . 56 PRO HG2 H 2.040 0.02 2 564 . 56 PRO HG3 H 2.094 0.02 2 565 . 56 PRO HD2 H 3.134 0.02 2 566 . 56 PRO HD3 H 3.748 0.02 2 567 . 56 PRO CA C 63.23 0.2 1 568 . 56 PRO CB C 32.46 0.2 1 569 . 56 PRO CG C 27.41 0.2 1 570 . 56 PRO CD C 50.38 0.2 1 571 . 57 SER H H 8.533 0.02 1 572 . 57 SER HA H 4.281 0.02 1 573 . 57 SER HB2 H 3.920 0.02 1 574 . 57 SER HB3 H 3.920 0.02 1 575 . 57 SER CA C 59.55 0.2 1 576 . 57 SER CB C 63.47 0.2 1 577 . 57 SER N N 117.21 0.1 1 578 . 58 THR H H 7.268 0.02 1 579 . 58 THR HA H 4.048 0.02 1 580 . 58 THR HB H 4.314 0.02 1 581 . 58 THR HG2 H 1.200 0.02 1 582 . 58 THR CA C 62.24 0.2 1 583 . 58 THR CB C 68.57 0.2 1 584 . 58 THR CG2 C 22.67 0.2 1 585 . 58 THR N N 109.64 0.1 1 586 . 59 LEU H H 7.435 0.02 1 587 . 59 LEU HA H 4.556 0.02 1 588 . 59 LEU HB2 H 1.085 0.02 2 589 . 59 LEU HB3 H 1.848 0.02 2 590 . 59 LEU HG H 0.725 0.02 1 591 . 59 LEU HD1 H 0.679 0.02 2 592 . 59 LEU HD2 H 1.587 0.02 2 593 . 59 LEU CA C 54.38 0.2 1 594 . 59 LEU CB C 40.58 0.2 1 595 . 59 LEU CG C 22.73 0.2 1 596 . 59 LEU CD1 C 26.64 0.2 2 597 . 59 LEU CD2 C 26.52 0.2 2 598 . 59 LEU N N 123.62 0.1 1 599 . 60 THR H H 8.500 0.02 1 600 . 60 THR HA H 4.455 0.02 1 601 . 60 THR HB H 4.378 0.02 1 602 . 60 THR HG2 H 1.143 0.02 1 603 . 60 THR CA C 62.17 0.2 1 604 . 60 THR CB C 70.62 0.2 1 605 . 60 THR CG2 C 21.69 0.2 1 606 . 60 THR N N 112.25 0.1 1 607 . 61 THR H H 7.730 0.02 1 608 . 61 THR HA H 5.064 0.02 1 609 . 61 THR HB H 4.544 0.02 1 610 . 61 THR HG2 H 1.257 0.02 1 611 . 61 THR CA C 58.42 0.2 1 612 . 61 THR CB C 69.59 0.2 1 613 . 61 THR CG2 C 22.03 0.2 1 614 . 61 THR N N 111.72 0.1 1 615 . 62 PRO HA H 4.174 0.02 1 616 . 62 PRO HB2 H 2.218 0.02 2 617 . 62 PRO HB3 H 2.270 0.02 2 618 . 62 PRO HG2 H 2.374 0.02 2 619 . 62 PRO HG3 H 1.851 0.02 2 620 . 62 PRO HD2 H 4.075 0.02 2 621 . 62 PRO HD3 H 3.881 0.02 2 622 . 62 PRO CA C 66.12 0.2 1 623 . 62 PRO CB C 32.18 0.2 1 624 . 62 PRO CG C 28.52 0.2 1 625 . 62 PRO CD C 50.58 0.2 1 626 . 63 GLY H H 8.906 0.02 1 627 . 63 GLY HA2 H 3.977 0.02 2 628 . 63 GLY HA3 H 3.788 0.02 2 629 . 63 GLY CA C 47.31 0.2 1 630 . 63 GLY N N 103.49 0.1 1 631 . 64 GLU H H 7.766 0.02 1 632 . 64 GLU HA H 4.100 0.02 1 633 . 64 GLU HB2 H 2.103 0.02 2 634 . 64 GLU HB3 H 2.281 0.02 2 635 . 64 GLU HG2 H 2.387 0.02 1 636 . 64 GLU HG3 H 2.387 0.02 1 637 . 64 GLU CA C 58.99 0.2 1 638 . 64 GLU CB C 30.86 0.2 1 639 . 64 GLU CG C 37.25 0.2 1 640 . 64 GLU N N 120.59 0.1 1 641 . 65 ILE H H 7.750 0.02 1 642 . 65 ILE HA H 3.787 0.02 1 643 . 65 ILE HB H 2.147 0.02 1 644 . 65 ILE HG12 H 1.189 0.02 2 645 . 65 ILE HG13 H 1.643 0.02 2 646 . 65 ILE HG2 H 0.814 0.02 1 647 . 65 ILE HD1 H 0.790 0.02 1 648 . 65 ILE CA C 64.48 0.2 1 649 . 65 ILE CB C 37.25 0.2 1 650 . 65 ILE CG1 C 29.66 0.2 1 651 . 65 ILE CG2 C 18.09 0.2 1 652 . 65 ILE CD1 C 12.46 0.2 1 653 . 65 ILE N N 120.95 0.1 1 654 . 66 ILE H H 8.550 0.02 1 655 . 66 ILE HA H 3.580 0.02 1 656 . 66 ILE HB H 1.849 0.02 1 657 . 66 ILE HG12 H 1.921 0.02 2 658 . 66 ILE HG13 H 0.702 0.02 2 659 . 66 ILE HG2 H 0.950 0.02 1 660 . 66 ILE HD1 H 0.896 0.02 1 661 . 66 ILE CA C 66.70 0.2 1 662 . 66 ILE CB C 38.91 0.2 1 663 . 66 ILE CG1 C 30.29 0.2 1 664 . 66 ILE CG2 C 17.50 0.2 1 665 . 66 ILE CD1 C 14.41 0.2 1 666 . 66 ILE N N 119.72 0.1 1 667 . 67 LYS H H 7.616 0.02 1 668 . 67 LYS HA H 3.900 0.02 1 669 . 67 LYS HB2 H 1.881 0.02 2 670 . 67 LYS HB3 H 1.932 0.02 2 671 . 67 LYS HG2 H 1.453 0.02 2 672 . 67 LYS HG3 H 1.529 0.02 2 673 . 67 LYS HD2 H 1.742 0.02 1 674 . 67 LYS HD3 H 1.742 0.02 1 675 . 67 LYS HE2 H 3.027 0.02 1 676 . 67 LYS HE3 H 3.027 0.02 1 677 . 67 LYS CA C 59.76 0.2 1 678 . 67 LYS CB C 32.69 0.2 1 679 . 67 LYS CG C 25.31 0.2 1 680 . 67 LYS CD C 29.15 0.2 1 681 . 67 LYS CE C 42.65 0.2 1 682 . 67 LYS N N 117.24 0.1 1 683 . 68 TYR H H 7.751 0.02 1 684 . 68 TYR HA H 4.123 0.02 1 685 . 68 TYR HB2 H 3.165 0.02 1 686 . 68 TYR HB3 H 3.165 0.02 1 687 . 68 TYR HD1 H 6.937 0.02 1 688 . 68 TYR HD2 H 6.937 0.02 1 689 . 68 TYR HE1 H 6.709 0.02 1 690 . 68 TYR HE2 H 6.709 0.02 1 691 . 68 TYR CA C 61.70 0.2 1 692 . 68 TYR CB C 39.13 0.2 1 693 . 68 TYR N N 118.82 0.1 1 694 . 68 TYR CD1 C 133.08 0.2 1 695 . 68 TYR CD2 C 133.08 0.2 1 696 . 68 TYR CE1 C 117.67 0.2 1 697 . 68 TYR CE2 C 117.67 0.2 1 698 . 69 VAL H H 8.173 0.02 1 699 . 69 VAL HA H 3.110 0.02 1 700 . 69 VAL HB H 1.777 0.02 1 701 . 69 VAL HG1 H 0.599 0.02 2 702 . 69 VAL HG2 H 0.130 0.02 2 703 . 69 VAL CA C 66.90 0.2 1 704 . 69 VAL CB C 31.63 0.2 1 705 . 69 VAL CG1 C 22.94 0.2 2 706 . 69 VAL CG2 C 21.21 0.2 2 707 . 69 VAL N N 118.53 0.1 1 708 . 70 LEU H H 8.448 0.02 1 709 . 70 LEU HA H 4.004 0.02 1 710 . 70 LEU HB2 H 1.502 0.02 2 711 . 70 LEU HB3 H 1.919 0.02 2 712 . 70 LEU HG H 2.008 0.02 1 713 . 70 LEU HD1 H 0.915 0.02 2 714 . 70 LEU HD2 H 0.979 0.02 2 715 . 70 LEU CA C 58.17 0.2 1 716 . 70 LEU CB C 41.21 0.2 1 717 . 70 LEU CG C 27.23 0.2 1 718 . 70 LEU CD1 C 25.75 0.2 2 719 . 70 LEU CD2 C 23.34 0.2 2 720 . 70 LEU N N 118.79 0.1 1 721 . 71 ASP H H 8.366 0.02 1 722 . 71 ASP HA H 4.404 0.02 1 723 . 71 ASP HB2 H 2.734 0.02 2 724 . 71 ASP HB3 H 2.564 0.02 2 725 . 71 ASP CA C 56.88 0.2 1 726 . 71 ASP CB C 40.59 0.2 1 727 . 71 ASP N N 118.97 0.1 1 728 . 72 ARG H H 7.730 0.02 1 729 . 72 ARG HA H 4.109 0.02 1 730 . 72 ARG HB2 H 1.551 0.02 2 731 . 72 ARG HB3 H 1.784 0.02 2 732 . 72 ARG HG2 H 1.328 0.02 2 733 . 72 ARG HG3 H 1.211 0.02 2 734 . 72 ARG HD2 H 2.752 0.02 2 735 . 72 ARG HD3 H 2.909 0.02 2 736 . 72 ARG HE H 7.051 0.02 1 737 . 72 ARG CA C 56.65 0.2 1 738 . 72 ARG CB C 30.25 0.2 1 739 . 72 ARG CG C 26.68 0.2 1 740 . 72 ARG CD C 42.25 0.2 1 741 . 72 ARG N N 118.69 0.1 1 742 . 72 ARG NE N 84.34 0.1 1 743 . 73 GLN H H 7.994 0.02 1 744 . 73 GLN HA H 4.178 0.02 1 745 . 73 GLN HB2 H 2.064 0.02 1 746 . 73 GLN HB3 H 2.064 0.02 1 747 . 73 GLN HG2 H 2.230 0.02 2 748 . 73 GLN HG3 H 2.474 0.02 2 749 . 73 GLN HE21 H 6.634 0.02 2 750 . 73 GLN HE22 H 7.293 0.02 2 751 . 73 GLN CA C 57.29 0.2 1 752 . 73 GLN CB C 29.31 0.2 1 753 . 73 GLN CG C 34.54 0.2 1 754 . 73 GLN N N 118.47 0.1 1 755 . 73 GLN NE2 N 110.62 0.1 1 756 . 74 LYS H H 7.818 0.02 1 757 . 74 LYS HA H 4.308 0.02 1 758 . 74 LYS HB2 H 1.897 0.02 1 759 . 74 LYS HB3 H 1.897 0.02 1 760 . 74 LYS HG2 H 1.535 0.02 2 761 . 74 LYS HG3 H 1.472 0.02 2 762 . 74 LYS HD2 H 1.705 0.02 1 763 . 74 LYS HD3 H 1.705 0.02 1 764 . 74 LYS HE2 H 3.004 0.02 1 765 . 74 LYS HE3 H 3.004 0.02 1 766 . 74 LYS CA C 57.12 0.2 1 767 . 74 LYS CB C 32.86 0.2 1 768 . 74 LYS CG C 24.96 0.2 1 769 . 74 LYS CD C 29.32 0.2 1 770 . 74 LYS CE C 42.45 0.2 1 771 . 74 LYS N N 119.92 0.1 1 772 . 75 THR H H 7.885 0.02 1 773 . 75 THR HA H 4.325 0.02 1 774 . 75 THR HB H 4.223 0.02 1 775 . 75 THR HG2 H 1.218 0.02 1 776 . 75 THR CA C 61.81 0.2 1 777 . 75 THR CB C 69.98 0.2 1 778 . 75 THR CG2 C 21.82 0.2 1 779 . 75 THR N N 113.70 0.1 1 780 . 76 ALA H H 8.132 0.02 1 781 . 76 ALA HA H 4.610 0.02 1 782 . 76 ALA HB H 1.384 0.02 1 783 . 76 ALA CA C 51.00 0.2 1 784 . 76 ALA CB C 18.37 0.2 1 785 . 76 ALA N N 127.89 0.1 1 786 . 77 PRO HA H 4.435 0.02 1 787 . 77 PRO HB2 H 2.296 0.02 1 788 . 77 PRO HB3 H 2.296 0.02 1 789 . 77 PRO HG2 H 2.023 0.02 1 790 . 77 PRO HG3 H 2.023 0.02 1 791 . 77 PRO HD2 H 3.654 0.02 2 792 . 77 PRO HD3 H 3.794 0.02 2 793 . 77 PRO CA C 63.16 0.2 1 794 . 77 PRO CB C 32.17 0.2 1 795 . 77 PRO CG C 27.64 0.2 1 796 . 77 PRO CD C 50.58 0.2 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'RSV CA' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 ASP HN 2 ASP HA 8.70 . . . 2 3JHNHA 3 ILE HN 3 ILE HA 8.65 . . . 3 3JHNHA 4 MET HN 4 MET HA 8.00 . . . 4 3JHNHA 5 GLN HN 5 GLN HA 4.19 . . . 5 3JHNHA 6 GLY HN 6 GLY HA 6.58 . . . 6 3JHNHA 8 SER HN 8 SER HA 10.68 . . . 7 3JHNHA 9 GLU HN 9 GLU HA 8.48 . . . 8 3JHNHA 10 SER HN 10 SER HA 5.45 . . . 9 3JHNHA 11 PHE HN 11 PHE HA 3.42 . . . 10 3JHNHA 12 VAL HN 12 VAL HA 3.93 . . . 11 3JHNHA 13 ASP HN 13 ASP HA 6.13 . . . 12 3JHNHA 14 PHE HN 14 PHE HA 4.35 . . . 13 3JHNHA 15 ALA HN 15 ALA HA 2.55 . . . 14 3JHNHA 16 ASN HN 16 ASN HA 7.45 . . . 15 3JHNHA 17 ARG HN 17 ARG HA 6.05 . . . 16 3JHNHA 18 LEU HN 18 LEU HA 4.85 . . . 17 3JHNHA 19 ILE HN 19 ILE HA 2.37 . . . 18 3JHNHA 20 LYS HN 20 LYS HA 4.91 . . . 19 3JHNHA 21 ALA HN 21 ALA HA 4.79 . . . 20 3JHNHA 23 GLU HN 23 GLU HA 3.59 . . . 21 3JHNHA 24 GLY HN 24 GLY HA2 8.04 . . . 22 3JHNHA 24 GLY HN 24 GLY HA3 5.41 . . . 23 3JHNHA 25 SER HN 25 SER HA 8.24 . . . 24 3JHNHA 26 ASP HN 26 ASP HA 7.05 . . . 25 3JHNHA 27 LEU HN 27 LEU HA 5.04 . . . 26 3JHNHA 30 SER HN 30 SER HA 4.83 . . . 27 3JHNHA 31 ALA HN 31 ALA HA 8.41 . . . 28 3JHNHA 32 ARG HN 32 ARG HA 4.66 . . . 29 3JHNHA 33 ALA HN 33 ALA HA 3.97 . . . 30 3JHNHA 35 VAL HN 35 VAL HA 6.15 . . . 31 3JHNHA 36 ILE HN 36 ILE HA 4.00 . . . 32 3JHNHA 37 ILE HN 37 ILE HA 3.73 . . . 33 3JHNHA 38 ASP HN 38 ASP HA 3.83 . . . 34 3JHNHA 39 CYS HN 39 CYS HA 5.20 . . . 35 3JHNHA 40 PHE HN 40 PHE HA 3.95 . . . 36 3JHNHA 41 ARG HN 41 ARG HA 3.81 . . . 37 3JHNHA 42 GLN HN 42 GLN HA 9.76 . . . 38 3JHNHA 43 LYS HN 43 LYS HA 10.59 . . . 39 3JHNHA 44 SER HN 44 SER HA 6.69 . . . 40 3JHNHA 45 GLN HN 45 GLN HA 4.22 . . . 41 3JHNHA 47 ASP HN 47 ASP HA 5.34 . . . 42 3JHNHA 48 ILE HN 48 ILE HA 8.04 . . . 43 3JHNHA 49 GLN HN 49 GLN HA 2.98 . . . 44 3JHNHA 50 GLN HN 50 GLN HA 5.01 . . . 45 3JHNHA 51 LEU HN 51 LEU HA 5.55 . . . 46 3JHNHA 52 ILE HN 52 ILE HA 4.64 . . . 47 3JHNHA 53 ARG HN 53 ARG HA 3.46 . . . 48 3JHNHA 54 THR HN 54 THR HA 10.50 . . . 49 3JHNHA 55 ALA HN 55 ALA HA 3.71 . . . 50 3JHNHA 57 SER HN 57 SER HA 6.87 . . . 51 3JHNHA 58 THR HN 58 THR HA 5.34 . . . 52 3JHNHA 59 LEU HN 59 LEU HA 10.16 . . . 53 3JHNHA 60 THR HN 60 THR HA 10.78 . . . 54 3JHNHA 61 THR HN 61 THR HA 8.59 . . . 55 3JHNHA 63 GLY HN 63 GLY HA2 6.79 . . . 56 3JHNHA 63 GLY HN 63 GLY HA3 3.54 . . . 57 3JHNHA 66 ILE HN 66 ILE HA 4.64 . . . 58 3JHNHA 67 LYS HN 67 LYS HA 4.27 . . . 59 3JHNHA 69 VAL HN 69 VAL HA 5.02 . . . 60 3JHNHA 71 ASP HN 71 ASP HA 4.74 . . . 61 3JHNHA 73 GLN HN 73 GLN HA 6.30 . . . 62 3JHNHA 74 LYS HN 74 LYS HA 6.80 . . . 63 3JHNHA 75 THR HN 75 THR HA 7.49 . . . 64 3JHNHA 76 ALA HN 76 ALA HA 6.67 . . . 65 3JHNHB 9 GLU HN 9 GLU HB2 -1.54 . . . 66 3JHNHB 9 GLU HN 9 GLU HB3 -0.43 . . . 67 3JHNHB 10 SER HN 10 SER HB2 -3.70 . . . 68 3JHNHB 10 SER HN 10 SER HB3 -1.95 . . . 69 3JHNHB 11 PHE HN 11 PHE HB2 -0.58 . . . 70 3JHNHB 11 PHE HN 11 PHE HB3 -1.27 . . . 71 3JHNHB 14 PHE HN 14 PHE HB2 -0.52 . . . 72 3JHNHB 14 PHE HN 14 PHE HB3 -2.04 . . . 73 3JHNHB 16 ASN HN 16 ASN HB2 -3.65 . . . 74 3JHNHB 16 ASN HN 16 ASN HB3 -2.65 . . . 75 3JHNHB 18 LEU HN 18 LEU HB2 -1.69 . . . 76 3JHNHB 18 LEU HN 18 LEU HB3 -0.76 . . . 77 3JHNHB 27 LEU HN 27 LEU HB2 -4.21 . . . 78 3JHNHB 27 LEU HN 27 LEU HB3 -2.67 . . . 79 3JHNHB 32 ARG HN 32 ARG HB2 -4.63 . . . 80 3JHNHB 32 ARG HN 32 ARG HB3 -2.29 . . . 81 3JHNHB 38 ASP HN 38 ASP HB2 -2.76 . . . 82 3JHNHB 38 ASP HN 38 ASP HB3 -2.08 . . . 83 3JHNHB 39 CYS HN 39 CYS HB2 -3.21 . . . 84 3JHNHB 39 CYS HN 39 CYS HB3 -1.62 . . . 85 3JHNHB 40 PHE HN 40 PHE HB2 -4.64 . . . 86 3JHNHB 40 PHE HN 40 PHE HB3 -2.05 . . . 87 3JHNHB 41 ARG HN 41 ARG HB2 -3.10 . . . 88 3JHNHB 41 ARG HN 41 ARG HB3 -2.66 . . . 89 3JHNHB 42 GLN HN 42 GLN HB2 -3.75 . . . 90 3JHNHB 42 GLN HN 42 GLN HB3 -1.49 . . . 91 3JHNHB 43 LYS HN 43 LYS HB2 -3.53 . . . 92 3JHNHB 43 LYS HN 43 LYS HB3 -1.01 . . . 93 3JHNHB 44 SER HN 44 SER HB2 -2.42 . . . 94 3JHNHB 44 SER HN 44 SER HB3 -2.34 . . . 95 3JHNHB 45 GLN HN 45 GLN HB2 -4.19 . . . 96 3JHNHB 45 GLN HN 45 GLN HB3 -2.55 . . . 97 3JHNHB 47 ASP HN 47 ASP HB2 -3.72 . . . 98 3JHNHB 47 ASP HN 47 ASP HB3 -2.91 . . . 99 3JHNHB 51 LEU HN 51 LEU HB2 -3.56 . . . 100 3JHNHB 51 LEU HN 51 LEU HB3 -1.93 . . . 101 3JHNHB 59 LEU HN 59 LEU HB2 -4.52 . . . 102 3JHNHB 59 LEU HN 59 LEU HB3 -0.86 . . . 103 3JHNHB 64 GLU HN 64 GLU HB2 -4.44 . . . 104 3JHNHB 64 GLU HN 64 GLU HB3 -2.40 . . . 105 3JHNHB 71 ASP HN 71 ASP HB2 -3.72 . . . 106 3JHNHB 71 ASP HN 71 ASP HB3 -2.25 . . . 107 3JHNHB 3 ILE HN 3 ILE HB -1.62 . . . 108 3JHNHB 12 VAL HN 12 VAL HB -2.04 . . . 109 3JHNHB 19 ILE HN 19 ILE HB -2.04 . . . 110 3JHNHB 35 VAL HN 35 VAL HB -1.97 . . . 111 3JHNHB 36 ILE HN 36 ILE HB -1.74 . . . 112 3JHNHB 37 ILE HN 37 ILE HB -2.01 . . . 113 3JHNHB 48 ILE HN 48 ILE HB -1.47 . . . 114 3JHNHB 52 ILE HN 52 ILE HB -1.58 . . . 115 3JHNHB 54 THR HN 54 THR HB -3.12 . . . 116 3JHNHB 58 THR HN 58 THR HB -2.40 . . . 117 3JHNHB 60 THR HN 60 THR HB -2.84 . . . 118 3JHNHB 61 THR HN 61 THR HB -3.11 . . . 119 3JHNHB 65 ILE HN 65 ILE HB -2.11 . . . 120 3JHNHB 66 ILE HN 66 ILE HB -1.80 . . . 121 3JHNHB 69 VAL HN 69 VAL HB -1.17 . . . 122 3JHNHB 75 THR HN 75 THR HB -2.31 . . . stop_ save_