data_4522 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The restrained and minimized average NMR structure of MAP30. ; _BMRB_accession_number 4522 _BMRB_flat_file_name bmr4522.str _Entry_type original _Submission_date 1999-10-27 _Accession_date 1999-12-06 _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 Wang Y. X. . 2 Neamati N. . . 3 Jacob J. . . 4 Palmer I. . . 5 Stahl S. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count "residual dipolar couplings" 387 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-02 update BMRB 'residual coupling constant saveframe tags corrected' 2001-05-07 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of Anti-HIV-1 and Anti-Tumor Protein Map30: Structural Insights Into its Multiple Functions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20035963 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Y. X. . 2 Neamati N. . . 3 Jacob J. . . 4 Palmer I. . . 5 Stahl S. J. . stop_ _Journal_abbreviation Cell _Journal_volume 99 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 433 _Page_last 442 _Year 1999 _Details . loop_ _Keyword 'single chain' stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name MAP30 _Abbreviation_common MAP30 _Enzyme_commission_number 3.2.2.22 loop_ _Mol_system_component_name _Mol_label MAP30 $Protein_(MAP30) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Protein_(MAP30) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MAP30 _Abbreviation_common MAP30 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 263 _Mol_residue_sequence ; DVNFDLSTATAKTYTKFIED FRATLPFSHKVYDIPLLYST ISDSRRFILLNLTSYAYETI SVAIDVTNVYVVAYRTRDVS YFFKESPPEAYNILFKGTRK ITLPYTGNYENLQTAAHKIR ENIDLGLPALSSAITTLFYY NAQSAPSALLVLIQTTAEAA RFKYIERHVAKYVATNFKPN LAIISLENQWSALSKQIFLA QNQGGKFRNPVDLIKPTGER FQVTNVDSDVVKGNIKLLLN SRASTADENFITTMTLLGES VVN ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 VAL 3 ASN 4 PHE 5 ASP 6 LEU 7 SER 8 THR 9 ALA 10 THR 11 ALA 12 LYS 13 THR 14 TYR 15 THR 16 LYS 17 PHE 18 ILE 19 GLU 20 ASP 21 PHE 22 ARG 23 ALA 24 THR 25 LEU 26 PRO 27 PHE 28 SER 29 HIS 30 LYS 31 VAL 32 TYR 33 ASP 34 ILE 35 PRO 36 LEU 37 LEU 38 TYR 39 SER 40 THR 41 ILE 42 SER 43 ASP 44 SER 45 ARG 46 ARG 47 PHE 48 ILE 49 LEU 50 LEU 51 ASN 52 LEU 53 THR 54 SER 55 TYR 56 ALA 57 TYR 58 GLU 59 THR 60 ILE 61 SER 62 VAL 63 ALA 64 ILE 65 ASP 66 VAL 67 THR 68 ASN 69 VAL 70 TYR 71 VAL 72 VAL 73 ALA 74 TYR 75 ARG 76 THR 77 ARG 78 ASP 79 VAL 80 SER 81 TYR 82 PHE 83 PHE 84 LYS 85 GLU 86 SER 87 PRO 88 PRO 89 GLU 90 ALA 91 TYR 92 ASN 93 ILE 94 LEU 95 PHE 96 LYS 97 GLY 98 THR 99 ARG 100 LYS 101 ILE 102 THR 103 LEU 104 PRO 105 TYR 106 THR 107 GLY 108 ASN 109 TYR 110 GLU 111 ASN 112 LEU 113 GLN 114 THR 115 ALA 116 ALA 117 HIS 118 LYS 119 ILE 120 ARG 121 GLU 122 ASN 123 ILE 124 ASP 125 LEU 126 GLY 127 LEU 128 PRO 129 ALA 130 LEU 131 SER 132 SER 133 ALA 134 ILE 135 THR 136 THR 137 LEU 138 PHE 139 TYR 140 TYR 141 ASN 142 ALA 143 GLN 144 SER 145 ALA 146 PRO 147 SER 148 ALA 149 LEU 150 LEU 151 VAL 152 LEU 153 ILE 154 GLN 155 THR 156 THR 157 ALA 158 GLU 159 ALA 160 ALA 161 ARG 162 PHE 163 LYS 164 TYR 165 ILE 166 GLU 167 ARG 168 HIS 169 VAL 170 ALA 171 LYS 172 TYR 173 VAL 174 ALA 175 THR 176 ASN 177 PHE 178 LYS 179 PRO 180 ASN 181 LEU 182 ALA 183 ILE 184 ILE 185 SER 186 LEU 187 GLU 188 ASN 189 GLN 190 TRP 191 SER 192 ALA 193 LEU 194 SER 195 LYS 196 GLN 197 ILE 198 PHE 199 LEU 200 ALA 201 GLN 202 ASN 203 GLN 204 GLY 205 GLY 206 LYS 207 PHE 208 ARG 209 ASN 210 PRO 211 VAL 212 ASP 213 LEU 214 ILE 215 LYS 216 PRO 217 THR 218 GLY 219 GLU 220 ARG 221 PHE 222 GLN 223 VAL 224 THR 225 ASN 226 VAL 227 ASP 228 SER 229 ASP 230 VAL 231 VAL 232 LYS 233 GLY 234 ASN 235 ILE 236 LYS 237 LEU 238 LEU 239 LEU 240 ASN 241 SER 242 ARG 243 ALA 244 SER 245 THR 246 ALA 247 ASP 248 GLU 249 ASN 250 PHE 251 ILE 252 THR 253 THR 254 MET 255 THR 256 LEU 257 LEU 258 GLY 259 GLU 260 SER 261 VAL 262 VAL 263 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1CF5 "Beta-Momorcharin Structure At 2.55 A" 94.68 249 99.60 100.00 1.13e-178 PDB 1D8V "The Restrained And Minimized Average Nmr Structure Of Map30" 100.00 263 100.00 100.00 0.00e+00 EMBL CAA78166 "momordin II [Momordica balsamina]" 100.00 286 99.62 100.00 0.00e+00 EMBL CAC08217 "ribosome inactivating protein, RIP, type I [Momordica charantia]" 100.00 264 99.24 99.62 0.00e+00 EMBL CAH19208 "type I ribosome inactivating protein precursor [Momordica charantia]" 100.00 264 99.62 99.62 0.00e+00 EMBL CCD28523 "ribosome inactivating protein, partial [Momordica charantia]" 100.00 280 100.00 100.00 0.00e+00 EMBL CCD28524 "ribosome inactivating protein, partial [Momordica charantia]" 100.00 280 100.00 100.00 0.00e+00 GB AAB35194 "MAP30 [Momordica charantia]" 100.00 286 99.62 99.62 0.00e+00 GB AAG33028 "MAP30I [Momordica charantia]" 100.00 286 100.00 100.00 0.00e+00 GB AAS17014 "Rip [Momordica charantia]" 100.00 264 100.00 100.00 0.00e+00 GB AAV68558 "ribosomal inactivating protein [Momordica charantia]" 100.00 286 100.00 100.00 0.00e+00 GB ABG37691 "anti-HIV protein [Momordica charantia]" 100.00 286 100.00 100.00 0.00e+00 SP P24817 "RecName: Full=Ribosome-inactivating protein beta-momorcharin; Short=B-MMC; AltName: Full=MAP 30; AltName: Full=rRNA N-glycosida" 100.00 286 100.00 100.00 0.00e+00 SP P29339 "RecName: Full=Ribosome-inactivating protein momordin II; AltName: Full=rRNA N-glycosidase; Flags: Precursor" 100.00 286 99.62 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Protein_(MAP30) 'balsam pear' 3673 Eukaryota Viridiplantae Momordica charantia 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 $Protein_(MAP30) . . . . . . 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 $Protein_(MAP30) 0.7 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_MODIFIED_XPLOR _Saveframe_category software _Name 'MODIFIED XPLOR' _Version 3.5 loop_ _Task refinement 'structure solution' stop_ _Details BRUNGER save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-SEPARATED_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _Sample_label $sample_1 save_ save_4D_13C/15N-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C/15N-SEPARATED NOESY' _Sample_label $sample_1 save_ save_3D_13C-SEPARATED_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _Sample_label $sample_1 save_ save_4D_13C-SEPARATED_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C-SEPARATED NOESY' _Sample_label $sample_1 save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HNCA-J_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA-J _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C/15N-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA-J _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 5.50 . n/a temperature 313.00 . K 'ionic strength' 0.01 . M pressure 1 . atm stop_ save_ save_residual_dipolar_couplings _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_1 stop_ _Details . _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 750 _Text_data_format . _Text_data . loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error 1DHC(i-1) 2 VAL H 1 ASP C -4.3500 ? ? . . . 1DHN 2 VAL H 2 VAL N 19.6100 ? ? . . . 1DNC(i-1) 2 VAL N 1 ASP C -0.5900 ? ? . . . 1DHC(i-1) 3 ASN H 2 VAL C -5.8700 ? ? . . . 1DHN 3 ASN H 3 ASN N 12.0100 ? ? . . . 1DNC(i-1) 3 ASN N 2 VAL C -1.6900 ? ? . . . 1DHN 4 PHE H 4 PHE N 3.1200 ? ? . . . 1DHC(i-1) 5 ASP H 4 PHE C -5.4200 ? ? . . . 1DHN 5 ASP H 5 ASP N 7.3000 ? ? . . . 1DNC(i-1) 5 ASP N 4 PHE C -1.4600 ? ? . . . 1DHC(i-1) 6 LEU H 5 ASP C -4.4000 ? ? . . . 1DHN 6 LEU H 6 LEU N 1.3700 ? ? . . . 1DNC(i-1) 6 LEU N 5 ASP C -2.0500 ? ? . . . 1DHN 7 SER H 7 SER N -12.1900 ? ? . . . 1DHC(i-1) 8 THR H 7 SER C -0.1000 ? ? . . . 1DHN 8 THR H 8 THR N 2.9700 ? ? . . . 1DNC(i-1) 8 THR N 7 SER C -1.0700 ? ? . . . 1DHC(i-1) 9 ALA H 8 THR C -5.8200 ? ? . . . 1DHN 9 ALA H 9 ALA N 2.8900 ? ? . . . 1DNC(i-1) 9 ALA N 8 THR C -2.4200 ? ? . . . 1DHC(i-1) 10 THR H 9 ALA C -0.5700 ? ? . . . 1DHN 10 THR H 10 THR N -4.2500 ? ? . . . 1DNC(i-1) 10 THR N 9 ALA C 1.8600 ? ? . . . 1DHC(i-1) 11 ALA H 10 THR C 2.9900 ? ? . . . 1DHN 11 ALA H 11 ALA N -0.3000 ? ? . . . 1DNC(i-1) 11 ALA N 10 THR C 2.4200 ? ? . . . 1DHC(i-1) 13 THR H 12 LYS C 3.9900 ? ? . . . 1DHN 13 THR H 13 THR N -0.9900 ? ? . . . 1DNC(i-1) 13 THR N 12 LYS C 1.8600 ? ? . . . 1DHC(i-1) 14 TYR H 13 THR C -2.7600 ? ? . . . 1DHN 14 TYR H 14 TYR N -3.1100 ? ? . . . 1DNC(i-1) 14 TYR N 13 THR C -1.6500 ? ? . . . 1DHN 15 THR H 15 THR N 4.6700 ? ? . . . 1DHC(i-1) 16 LYS H 15 THR C -2.0400 ? ? . . . 1DHN 16 LYS H 16 LYS N 4.1800 ? ? . . . 1DNC(i-1) 16 LYS N 15 THR C 0.0000 ? ? . . . 1DHN 18 ILE H 18 ILE N -2.1300 ? ? . . . 1DHN 19 GLU H 19 GLU N 3.1200 ? ? . . . 1DHC(i-1) 20 ASP H 19 GLU C -5.2200 ? ? . . . 1DHN 20 ASP H 20 ASP N 0.8400 ? ? . . . 1DNC(i-1) 20 ASP N 19 GLU C -1.6500 ? ? . . . 1DHN 21 PHE H 21 PHE N -4.7100 ? ? . . . 1DHN 22 ARG H 22 ARG N -0.3000 ? ? . . . 1DHC(i-1) 27 PHE H 26 PRO C -1.4500 ? ? . . . 1DNC(i-1) 27 PHE N 26 PRO C 1.7500 ? ? . . . 1DHN 28 SER H 28 SER N 5.2500 ? ? . . . 1DHN 29 HIS H 29 HIS N -11.8900 ? ? . . . 1DHN 30 LYS H 30 LYS N 5.5500 ? ? . . . 1DHC(i-1) 31 VAL H 30 LYS C -2.3400 ? ? . . . 1DHN 31 VAL H 31 VAL N -5.2400 ? ? . . . 1DNC(i-1) 31 VAL N 30 LYS C -1.2300 ? ? . . . 1DHN 32 TYR H 32 TYR N -2.4500 ? ? . . . 1DHC(i-1) 33 ASP H 32 TYR C -1.2100 ? ? . . . 1DHN 33 ASP H 33 ASP N -3.1100 ? ? . . . 1DNC(i-1) 33 ASP N 32 TYR C 0.4600 ? ? . . . 1DHN 34 ILE H 34 ILE N 12.7700 ? ? . . . 1DHN 37 LEU H 37 LEU N -4.2500 ? ? . . . 1DHN 38 TYR H 38 TYR N 3.3500 ? ? . . . 1DHN 39 SER H 39 SER N -1.6700 ? ? . . . 1DHC(i-1) 41 ILE H 40 THR C 4.3300 ? ? . . . 1DHN 41 ILE H 41 ILE N 8.6700 ? ? . . . 1DNC(i-1) 41 ILE N 40 THR C 2.2500 ? ? . . . 1DHC(i-1) 42 SER H 41 ILE C -12.2100 ? ? . . . 1DNC(i-1) 42 SER N 41 ILE C -3.6600 ? ? . . . 1DHN 43 ASP H 43 ASP N 3.7300 ? ? . . . 1DHC(i-1) 44 SER H 43 ASP C -2.3500 ? ? . . . 1DHN 44 SER H 44 SER N -5.1600 ? ? . . . 1DNC(i-1) 44 SER N 43 ASP C -8.3500 ? ? . . . 1DHN 45 ARG H 45 ARG N 20.4100 ? ? . . . 1DHC(i-1) 46 ARG H 45 ARG C -0.1600 ? ? . . . 1DHN 46 ARG H 46 ARG N -13.0700 ? ? . . . 1DNC(i-1) 46 ARG N 45 ARG C -1.7800 ? ? . . . 1DHC(i-1) 47 PHE H 46 ARG C 4.6600 ? ? . . . 1DHN 47 PHE H 47 PHE N -11.9300 ? ? . . . 1DNC(i-1) 47 PHE N 46 ARG C 1.9600 ? ? . . . 1DHN 48 ILE H 48 ILE N -2.9100 ? ? . . . 1DHC(i-1) 49 LEU H 48 ILE C -4.6200 ? ? . . . 1DHN 49 LEU H 49 LEU N 12.5400 ? ? . . . 1DNC(i-1) 49 LEU N 48 ILE C -0.5500 ? ? . . . 1DHN 50 LEU H 50 LEU N 21.2100 ? ? . . . 1DHN 51 ASN H 51 ASN N 8.2900 ? ? . . . 1DHN 52 LEU H 52 LEU N 23.9000 ? ? . . . 1DHN 53 THR H 53 THR N -2.5800 ? ? . . . 1DHC(i-1) 54 SER H 53 THR C -2.0300 ? ? . . . 1DHN 54 SER H 54 SER N -11.7000 ? ? . . . 1DNC(i-1) 54 SER N 53 THR C -6.0100 ? ? . . . 1DHC(i-1) 56 ALA H 55 TYR C 0.6900 ? ? . . . 1DHN 56 ALA H 56 ALA N 15.7300 ? ? . . . 1DNC(i-1) 56 ALA N 55 TYR C 1.1900 ? ? . . . 1DHN 58 GLU H 58 GLU N -13.2200 ? ? . . . 1DHC(i-1) 59 THR H 58 GLU C 5.0600 ? ? . . . 1DHN 59 THR H 59 THR N -18.3100 ? ? . . . 1DNC(i-1) 59 THR N 58 GLU C 1.2200 ? ? . . . 1DHN 60 ILE H 60 ILE N -6.0000 ? ? . . . 1DHC(i-1) 61 SER H 60 ILE C -2.6100 ? ? . . . 1DHN 61 SER H 61 SER N 4.4100 ? ? . . . 1DNC(i-1) 61 SER N 60 ILE C -1.6800 ? ? . . . 1DHN 62 VAL H 62 VAL N 16.6700 ? ? . . . 1DHN 63 ALA H 63 ALA N 13.8300 ? ? . . . 1DHN 64 ILE H 64 ILE N 11.6300 ? ? . . . 1DHN 65 ASP H 65 ASP N 23.3300 ? ? . . . 1DHN 66 VAL H 66 VAL N -18.2400 ? ? . . . 1DHN 67 THR H 67 THR N -8.8900 ? ? . . . 1DHN 68 ASN H 68 ASN N 27.0600 ? ? . . . 1DHN 69 VAL H 69 VAL N -4.4400 ? ? . . . 1DHN 70 TYR H 70 TYR N -1.1000 ? ? . . . 1DHN 72 VAL H 72 VAL N 19.7600 ? ? . . . 1DHC(i-1) 73 ALA H 72 VAL C -6.6400 ? ? . . . 1DNC(i-1) 73 ALA N 72 VAL C -2.1000 ? ? . . . 1DHN 74 TYR H 74 TYR N 12.1600 ? ? . . . 1DHN 75 ARG H 75 ARG N 7.3000 ? ? . . . 1DHC(i-1) 76 THR H 75 ARG C 2.8500 ? ? . . . 1DHN 76 THR H 76 THR N 6.3900 ? ? . . . 1DNC(i-1) 76 THR N 75 ARG C 1.4100 ? ? . . . 1DHC(i-1) 77 ARG H 76 THR C -7.2700 ? ? . . . 1DHN 77 ARG H 77 ARG N 7.9100 ? ? . . . 1DNC(i-1) 77 ARG N 76 THR C -2.7600 ? ? . . . 1DHC(i-1) 78 ASP H 77 ARG C 2.4000 ? ? . . . 1DHN 78 ASP H 78 ASP N -2.6600 ? ? . . . 1DNC(i-1) 78 ASP N 77 ARG C 2.7000 ? ? . . . 1DHC(i-1) 79 VAL H 78 ASP C 3.5800 ? ? . . . 1DNC(i-1) 79 VAL N 78 ASP C 1.9700 ? ? . . . 1DHN 81 TYR H 81 TYR N 17.4800 ? ? . . . 1DHN 82 PHE H 82 PHE N -0.4600 ? ? . . . 1DHN 83 PHE H 83 PHE N 1.7100 ? ? . . . 1DHN 84 LYS H 84 LYS N -7.4400 ? ? . . . 1DHC(i-1) 85 GLU H 84 LYS C 3.2500 ? ? . . . 1DHN 85 GLU H 85 GLU N -10.1000 ? ? . . . 1DNC(i-1) 85 GLU N 84 LYS C 0.0300 ? ? . . . 1DHN 86 SER H 86 SER N -10.7100 ? ? . . . 1DHC(i-1) 89 GLU H 88 PRO C 5.9300 ? ? . . . 1DHN 89 GLU H 89 GLU N -9.8400 ? ? . . . 1DNC(i-1) 89 GLU N 88 PRO C 0.1900 ? ? . . . 1DHN 90 ALA H 90 ALA N 14.8500 ? ? . . . 1DHN 91 TYR H 91 TYR N 4.0800 ? ? . . . 1DHC(i-1) 93 ILE H 92 ASN C 8.9000 ? ? . . . 1DHN 93 ILE H 93 ILE N -5.7700 ? ? . . . 1DNC(i-1) 93 ILE N 92 ASN C 1.8100 ? ? . . . 1DHC(i-1) 94 LEU H 93 ILE C -4.5900 ? ? . . . 1DHN 94 LEU H 94 LEU N 17.5600 ? ? . . . 1DNC(i-1) 94 LEU N 93 ILE C -0.5500 ? ? . . . 1DHC(i-1) 96 LYS H 95 PHE C -0.7200 ? ? . . . 1DHN 96 LYS H 96 LYS N 8.8800 ? ? . . . 1DNC(i-1) 96 LYS N 95 PHE C 1.0500 ? ? . . . 1DHC(i-1) 98 THR H 97 GLY C 4.8600 ? ? . . . 1DHN 98 THR H 98 THR N -5.3900 ? ? . . . 1DNC(i-1) 98 THR N 97 GLY C 1.3600 ? ? . . . 1DHC(i-1) 99 ARG H 98 THR C -0.4000 ? ? . . . 1DNC(i-1) 99 ARG N 98 THR C -0.4800 ? ? . . . 1DHN 100 LYS H 100 LYS N -7.6000 ? ? . . . 1DHN 101 ILE H 101 ILE N 13.3800 ? ? . . . 1DHC(i-1) 102 THR H 101 ILE C -5.7400 ? ? . . . 1DHN 102 THR H 102 THR N 1.1400 ? ? . . . 1DNC(i-1) 102 THR N 101 ILE C -2.4200 ? ? . . . 1DHN 103 LEU H 103 LEU N 5.9300 ? ? . . . 1DHC(i-1) 105 TYR H 104 PRO C -5.7200 ? ? . . . 1DHN 105 TYR H 105 TYR N 10.1900 ? ? . . . 1DNC(i-1) 105 TYR N 104 PRO C -0.7500 ? ? . . . 1DHC(i-1) 106 THR H 105 TYR C 2.1600 ? ? . . . 1DHN 106 THR H 106 THR N 2.0000 ? ? . . . 1DNC(i-1) 106 THR N 105 TYR C 1.9800 ? ? . . . 1DHC(i-1) 107 GLY H 106 THR C -2.0600 ? ? . . . 1DHN 107 GLY H 107 GLY N -3.8200 ? ? . . . 1DNC(i-1) 107 GLY N 106 THR C -1.0300 ? ? . . . 1DHC(i-1) 109 TYR H 108 ASN C 2.8500 ? ? . . . 1DHN 109 TYR H 109 TYR N -3.0400 ? ? . . . 1DNC(i-1) 109 TYR N 108 ASN C 2.2100 ? ? . . . 1DHC(i-1) 110 GLU H 109 TYR C -9.9200 ? ? . . . 1DNC(i-1) 110 GLU N 109 TYR C -1.1000 ? ? . . . 1DHC(i-1) 111 ASN H 110 GLU C -2.5300 ? ? . . . 1DNC(i-1) 111 ASN N 110 GLU C 1.0300 ? ? . . . 1DHC(i-1) 112 LEU H 111 ASN C -3.6400 ? ? . . . 1DHN 112 LEU H 112 LEU N -4.0300 ? ? . . . 1DNC(i-1) 112 LEU N 111 ASN C -2.2900 ? ? . . . 1DHN 113 GLN H 113 GLN N -9.6000 ? ? . . . 1DHC(i-1) 114 THR H 113 GLN C 0.2500 ? ? . . . 1DHN 114 THR H 114 THR N -3.3400 ? ? . . . 1DNC(i-1) 114 THR N 113 GLN C -1.2500 ? ? . . . 1DHC(i-1) 115 ALA H 114 THR C 1.6400 ? ? . . . 1DHN 115 ALA H 115 ALA N 0.0800 ? ? . . . 1DNC(i-1) 115 ALA N 114 THR C -0.7600 ? ? . . . 1DHC(i-1) 116 ALA H 115 ALA C 2.2200 ? ? . . . 1DHN 116 ALA H 116 ALA N -6.8300 ? ? . . . 1DNC(i-1) 116 ALA N 115 ALA C 0.9500 ? ? . . . 1DHN 117 HIS H 117 HIS N -1.1400 ? ? . . . 1DHC(i-1) 118 LYS H 117 HIS C -2.3400 ? ? . . . 1DHN 118 LYS H 118 LYS N -5.4700 ? ? . . . 1DNC(i-1) 118 LYS N 117 HIS C -0.9500 ? ? . . . 1DHN 119 ILE H 119 ILE N -5.3000 ? ? . . . 1DHC(i-1) 120 ARG H 119 ILE C -1.1800 ? ? . . . 1DHN 120 ARG H 120 ARG N 6.8700 ? ? . . . 1DNC(i-1) 120 ARG N 119 ILE C -0.7000 ? ? . . . 1DHC(i-1) 121 GLU H 120 ARG C -3.8900 ? ? . . . 1DHN 121 GLU H 121 GLU N 15.3500 ? ? . . . 1DNC(i-1) 121 GLU N 120 ARG C 1.8400 ? ? . . . 1DHC(i-1) 122 ASN H 121 GLU C -2.7400 ? ? . . . 1DHN 122 ASN H 122 ASN N -18.9200 ? ? . . . 1DNC(i-1) 122 ASN N 121 GLU C 1.9800 ? ? . . . 1DHC(i-1) 123 ILE H 122 ASN C -1.7500 ? ? . . . 1DHN 123 ILE H 123 ILE N -5.3200 ? ? . . . 1DNC(i-1) 123 ILE N 122 ASN C -1.3700 ? ? . . . 1DHC(i-1) 124 ASP H 123 ILE C 2.9600 ? ? . . . 1DHN 124 ASP H 124 ASP N -4.8600 ? ? . . . 1DNC(i-1) 124 ASP N 123 ILE C -0.2100 ? ? . . . 1DHC(i-1) 125 LEU H 124 ASP C 6.5800 ? ? . . . 1DHN 125 LEU H 125 LEU N -3.8700 ? ? . . . 1DNC(i-1) 125 LEU N 124 ASP C 0.0900 ? ? . . . 1DHN 126 GLY H 126 GLY N -10.5400 ? ? . . . 1DHC(i-1) 127 LEU H 126 GLY C -5.2200 ? ? . . . 1DHN 127 LEU H 127 LEU N -3.4700 ? ? . . . 1DNC(i-1) 127 LEU N 126 GLY C -2.6900 ? ? . . . 1DHC(i-1) 129 ALA H 128 PRO C 5.1600 ? ? . . . 1DHN 129 ALA H 129 ALA N 5.6200 ? ? . . . 1DNC(i-1) 129 ALA N 128 PRO C 0.1900 ? ? . . . 1DHN 131 SER H 131 SER N -8.8100 ? ? . . . 1DHC(i-1) 132 SER H 131 SER C 3.8400 ? ? . . . 1DHN 132 SER H 132 SER N -16.7900 ? ? . . . 1DNC(i-1) 132 SER N 131 SER C -1.5100 ? ? . . . 1DHN 133 ALA H 133 ALA N -7.4400 ? ? . . . 1DHN 135 THR H 135 THR N -7.9000 ? ? . . . 1DHC(i-1) 138 PHE H 137 LEU C 5.0600 ? ? . . . 1DHN 138 PHE H 138 PHE N -5.0100 ? ? . . . 1DNC(i-1) 138 PHE N 137 LEU C 1.0000 ? ? . . . 1DHC(i-1) 139 TYR H 138 PHE C 4.9800 ? ? . . . 1DNC(i-1) 139 TYR N 138 PHE C 1.1900 ? ? . . . 1DHC(i-1) 140 TYR H 139 TYR C 0.6100 ? ? . . . 1DHN 140 TYR H 140 TYR N -0.0700 ? ? . . . 1DNC(i-1) 140 TYR N 139 TYR C 0.0000 ? ? . . . 1DHC(i-1) 141 ASN H 140 TYR C 8.5000 ? ? . . . 1DHN 141 ASN H 141 ASN N -9.9500 ? ? . . . 1DNC(i-1) 141 ASN N 140 TYR C 0.6300 ? ? . . . 1DHC(i-1) 142 ALA H 141 ASN C 2.3800 ? ? . . . 1DHN 142 ALA H 142 ALA N -16.4900 ? ? . . . 1DNC(i-1) 142 ALA N 141 ASN C -1.5100 ? ? . . . 1DHC(i-1) 143 GLN H 142 ALA C 2.5100 ? ? . . . 1DHN 143 GLN H 143 GLN N -6.9900 ? ? . . . 1DNC(i-1) 143 GLN N 142 ALA C -0.4200 ? ? . . . 1DHN 144 SER H 144 SER N -2.5400 ? ? . . . 1DHC(i-1) 145 ALA H 144 SER C 3.2400 ? ? . . . 1DHN 145 ALA H 145 ALA N -7.4400 ? ? . . . 1DNC(i-1) 145 ALA N 144 SER C 0.4700 ? ? . . . 1DHC(i-1) 147 SER H 146 PRO C -1.8900 ? ? . . . 1DNC(i-1) 147 SER N 146 PRO C -0.9800 ? ? . . . 1DHN 148 ALA H 148 ALA N 0.0600 ? ? . . . 1DHN 149 LEU H 149 LEU N 10.2600 ? ? . . . 1DHN 150 LEU H 150 LEU N 3.8000 ? ? . . . 1DHC(i-1) 151 VAL H 150 LEU C 1.0600 ? ? . . . 1DHN 151 VAL H 151 VAL N -7.5200 ? ? . . . 1DNC(i-1) 151 VAL N 150 LEU C 1.8900 ? ? . . . 1DHN 152 LEU H 152 LEU N 2.5900 ? ? . . . 1DHN 153 ILE H 153 ILE N 11.4000 ? ? . . . 1DHN 154 GLN H 154 GLN N 1.8500 ? ? . . . 1DHN 155 THR H 155 THR N -4.2400 ? ? . . . 1DHC(i-1) 156 THR H 155 THR C 2.8300 ? ? . . . 1DHN 156 THR H 156 THR N 23.6400 ? ? . . . 1DNC(i-1) 156 THR N 155 THR C 2.6300 ? ? . . . 1DHN 157 ALA H 157 ALA N -7.0600 ? ? . . . 1DHN 159 ALA H 159 ALA N -13.9800 ? ? . . . 1DHN 160 ALA H 160 ALA N -4.2500 ? ? . . . 1DHN 161 ARG H 161 ARG N 0.0000 ? ? . . . 1DHN 162 PHE H 162 PHE N -7.7500 ? ? . . . 1DHC(i-1) 163 LYS H 162 PHE C 2.7700 ? ? . . . 1DHN 163 LYS H 163 LYS N -2.9500 ? ? . . . 1DNC(i-1) 163 LYS N 162 PHE C -0.8500 ? ? . . . 1DHC(i-1) 164 TYR H 163 LYS C -2.0500 ? ? . . . 1DHN 164 TYR H 164 TYR N 3.8800 ? ? . . . 1DNC(i-1) 164 TYR N 163 LYS C -0.9000 ? ? . . . 1DHN 167 ARG H 167 ARG N -0.9100 ? ? . . . 1DHN 168 HIS H 168 HIS N -18.3900 ? ? . . . 1DHN 169 VAL H 169 VAL N -0.2300 ? ? . . . 1DHC(i-1) 170 ALA H 169 VAL C 5.5800 ? ? . . . 1DNC(i-1) 170 ALA N 169 VAL C -0.5400 ? ? . . . 1DHN 172 TYR H 172 TYR N 0.7600 ? ? . . . 1DHC(i-1) 173 VAL H 172 TYR C -2.9400 ? ? . . . 1DHN 173 VAL H 173 VAL N -7.4400 ? ? . . . 1DNC(i-1) 173 VAL N 172 TYR C -2.2600 ? ? . . . 1DHC(i-1) 174 ALA H 173 VAL C -1.7000 ? ? . . . 1DHN 174 ALA H 174 ALA N -16.3400 ? ? . . . 1DNC(i-1) 174 ALA N 173 VAL C -1.5000 ? ? . . . 1DHC(i-1) 176 ASN H 175 THR C -5.9700 ? ? . . . 1DHN 176 ASN H 176 ASN N -2.8900 ? ? . . . 1DNC(i-1) 176 ASN N 175 THR C -2.8600 ? ? . . . 1DHC(i-1) 177 PHE H 176 ASN C -0.1400 ? ? . . . 1DHN 177 PHE H 177 PHE N -10.0300 ? ? . . . 1DNC(i-1) 177 PHE N 176 ASN C -0.7600 ? ? . . . 1DHC(i-1) 178 LYS H 177 PHE C 4.2100 ? ? . . . 1DHN 178 LYS H 178 LYS N -13.9000 ? ? . . . 1DNC(i-1) 178 LYS N 177 PHE C -0.0100 ? ? . . . 1DHN 180 ASN H 180 ASN N -7.9800 ? ? . . . 1DHC(i-1) 181 LEU H 180 ASN C 1.9000 ? ? . . . 1DHN 181 LEU H 181 LEU N -11.3900 ? ? . . . 1DNC(i-1) 181 LEU N 180 ASN C 0.6400 ? ? . . . 1DHC(i-1) 182 ALA H 181 LEU C -5.4300 ? ? . . . 1DHN 182 ALA H 182 ALA N 3.9500 ? ? . . . 1DNC(i-1) 182 ALA N 181 LEU C -2.2200 ? ? . . . 1DHC(i-1) 183 ILE H 182 ALA C 3.9800 ? ? . . . 1DHN 183 ILE H 183 ILE N -3.8700 ? ? . . . 1DNC(i-1) 183 ILE N 182 ALA C 1.9500 ? ? . . . 1DHC(i-1) 184 ILE H 183 ILE C -2.9300 ? ? . . . 1DNC(i-1) 184 ILE N 183 ILE C 2.0800 ? ? . . . 1DHN 186 LEU H 186 LEU N 0.9900 ? ? . . . 1DHC(i-1) 188 ASN H 187 GLU C -0.8100 ? ? . . . 1DHN 188 ASN H 188 ASN N -7.0600 ? ? . . . 1DNC(i-1) 188 ASN N 187 GLU C -0.6300 ? ? . . . 1DHC(i-1) 190 TRP H 189 GLN C -4.7600 ? ? . . . 1DHN 190 TRP H 190 TRP N -4.8600 ? ? . . . 1DNC(i-1) 190 TRP N 189 GLN C -2.5500 ? ? . . . 1DHC(i-1) 191 SER H 190 TRP C 0.1400 ? ? . . . 1DHN 191 SER H 191 SER N 1.1900 ? ? . . . 1DNC(i-1) 191 SER N 190 TRP C -0.2200 ? ? . . . 1DHC(i-1) 192 ALA H 191 SER C -0.8000 ? ? . . . 1DHN 192 ALA H 192 ALA N -0.9900 ? ? . . . 1DNC(i-1) 192 ALA N 191 SER C 0.1000 ? ? . . . 1DHN 193 LEU H 193 LEU N -6.6100 ? ? . . . 1DHN 194 SER H 194 SER N -4.6300 ? ? . . . 1DHN 195 LYS H 195 LYS N 0.5100 ? ? . . . 1DHN 197 ILE H 197 ILE N -0.5700 ? ? . . . 1DHC(i-1) 199 LEU H 198 PHE C -6.4800 ? ? . . . 1DHN 199 LEU H 199 LEU N -1.5900 ? ? . . . 1DNC(i-1) 199 LEU N 198 PHE C -2.7800 ? ? . . . 1DHN 201 GLN H 201 GLN N -9.7700 ? ? . . . 1DHC(i-1) 202 ASN H 201 GLN C 4.4700 ? ? . . . 1DHN 202 ASN H 202 ASN N 2.8900 ? ? . . . 1DNC(i-1) 202 ASN N 201 GLN C -3.1200 ? ? . . . 1DHN 203 GLN H 203 GLN N 7.0100 ? ? . . . 1DHC(i-1) 204 GLY H 203 GLN C -5.2100 ? ? . . . 1DHN 204 GLY H 204 GLY N -10.5600 ? ? . . . 1DNC(i-1) 204 GLY N 203 GLN C -3.1900 ? ? . . . 1DHC(i-1) 205 GLY H 204 GLY C 5.2000 ? ? . . . 1DHN 205 GLY H 205 GLY N -7.1400 ? ? . . . 1DNC(i-1) 205 GLY N 204 GLY C 2.6900 ? ? . . . 1DHC(i-1) 206 LYS H 205 GLY C -0.7000 ? ? . . . 1DHN 206 LYS H 206 LYS N -3.1900 ? ? . . . 1DNC(i-1) 206 LYS N 205 GLY C -0.9100 ? ? . . . 1DHC(i-1) 208 ARG H 207 PHE C 4.2300 ? ? . . . 1DHN 208 ARG H 208 ARG N -9.3700 ? ? . . . 1DNC(i-1) 208 ARG N 207 PHE C 0.4500 ? ? . . . 1DHC(i-1) 209 ASN H 208 ARG C 3.8800 ? ? . . . 1DHN 209 ASN H 209 ASN N 2.6600 ? ? . . . 1DNC(i-1) 209 ASN N 208 ARG C 2.0200 ? ? . . . 1DHC(i-1) 211 VAL H 210 PRO C -6.2300 ? ? . . . 1DHN 211 VAL H 211 VAL N 10.6400 ? ? . . . 1DNC(i-1) 211 VAL N 210 PRO C -1.0200 ? ? . . . 1DHC(i-1) 212 ASP H 211 VAL C -1.9600 ? ? . . . 1DHN 212 ASP H 212 ASP N 4.4900 ? ? . . . 1DNC(i-1) 212 ASP N 211 VAL C -1.5700 ? ? . . . 1DHN 213 LEU H 213 LEU N -28.6400 ? ? . . . 1DHC(i-1) 214 ILE H 213 LEU C 1.3000 ? ? . . . 1DNC(i-1) 214 ILE N 213 LEU C 0.2800 ? ? . . . 1DHC(i-1) 217 THR H 216 PRO C 9.1800 ? ? . . . 1DHN 217 THR H 217 THR N -2.6200 ? ? . . . 1DNC(i-1) 217 THR N 216 PRO C 2.1800 ? ? . . . 1DHC(i-1) 218 GLY H 217 THR C -3.5400 ? ? . . . 1DHN 218 GLY H 218 GLY N 2.2800 ? ? . . . 1DNC(i-1) 218 GLY N 217 THR C -2.2700 ? ? . . . 1DHC(i-1) 220 ARG H 219 GLU C -4.9500 ? ? . . . 1DHN 220 ARG H 220 ARG N 1.5200 ? ? . . . 1DNC(i-1) 220 ARG N 219 GLU C -0.9100 ? ? . . . 1DHC(i-1) 221 PHE H 220 ARG C 2.0200 ? ? . . . 1DHN 221 PHE H 221 PHE N -17.6300 ? ? . . . 1DNC(i-1) 221 PHE N 220 ARG C 0.4100 ? ? . . . 1DHC(i-1) 222 GLN H 221 PHE C 5.0000 ? ? . . . 1DHN 222 GLN H 222 GLN N -16.3400 ? ? . . . 1DNC(i-1) 222 GLN N 221 PHE C 0.9500 ? ? . . . 1DHN 223 VAL H 223 VAL N 0.2700 ? ? . . . 1DHC(i-1) 224 THR H 223 VAL C -0.1300 ? ? . . . 1DHN 224 THR H 224 THR N 6.5400 ? ? . . . 1DNC(i-1) 224 THR N 223 VAL C 0.3200 ? ? . . . 1DHC(i-1) 225 ASN H 224 THR C -5.5400 ? ? . . . 1DHN 225 ASN H 225 ASN N -1.2900 ? ? . . . 1DNC(i-1) 225 ASN N 224 THR C -1.4900 ? ? . . . 1DHN 226 VAL H 226 VAL N -3.5900 ? ? . . . 1DHC(i-1) 227 ASP H 226 VAL C 4.8300 ? ? . . . 1DHN 227 ASP H 227 ASP N 4.9500 ? ? . . . 1DNC(i-1) 227 ASP N 226 VAL C 4.0300 ? ? . . . 1DHN 230 VAL H 230 VAL N 16.4300 ? ? . . . 1DHC(i-1) 232 LYS H 231 VAL C -3.0100 ? ? . . . 1DHN 232 LYS H 232 LYS N 16.2400 ? ? . . . 1DNC(i-1) 232 LYS N 231 VAL C -0.6600 ? ? . . . 1DHC(i-1) 234 ASN H 233 GLY C -4.2700 ? ? . . . 1DNC(i-1) 234 ASN N 233 GLY C -2.0900 ? ? . . . 1DHC(i-1) 235 ILE H 234 ASN C 2.4200 ? ? . . . 1DHN 235 ILE H 235 ILE N -14.1300 ? ? . . . 1DNC(i-1) 235 ILE N 234 ASN C -0.3500 ? ? . . . 1DHN 236 LYS H 236 LYS N 1.3700 ? ? . . . 1DHN 238 LEU H 238 LEU N -1.6700 ? ? . . . 1DHN 239 LEU H 239 LEU N -12.6100 ? ? . . . stop_ save_