data_18024 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C and 15N chemical shift assignments of cAMP bound Cyclic Nucleotide-Binding Domain from a bacterial Cyclic Nucleotide-Gated channel ; _BMRB_accession_number 18024 _BMRB_flat_file_name bmr18024.str _Entry_type original _Submission_date 2011-10-26 _Accession_date 2011-10-26 _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 Cukkemane Abhishek . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 434 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-06 update BMRB 'update entry citation' 2012-02-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22302441 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cukkemane Abhishek . . 2 Nand Deepak . . 3 Gradmann Sabine . . 4 Weingarth Markus . . 5 Kaupp 'U. Benjamin' . . 6 Baldus Marc . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 225 _Page_last 229 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Cyclic nucleotide binding domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Cyclic nucleotide binding domain, subunit 1' $Cylic_Nucleotide_Binding_Domain 'cyclic adenosine monophosphate' $CMP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cylic_Nucleotide_Binding_Domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cyclic nucleotide binding domain, subunit 1' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; GSQEVRRGDFVRNWQLVAAV PLFQKLGPAVLVEIVRALRA RTVPAGAVICRIGEPGDRMF FVVEGSVSVATPNPVELGPG AFFGEMALISGEPRSATVSA ATTVSLLSLHSADFQMLCSS SPEIAEIFRKTALERRGAAA SA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 . GLN 4 . GLU 5 . VAL 6 . ARG 7 220 ARG 8 221 GLY 9 222 ASP 10 223 PHE 11 224 VAL 12 225 ARG 13 226 ASN 14 227 TRP 15 228 GLN 16 229 LEU 17 230 VAL 18 231 ALA 19 232 ALA 20 233 VAL 21 234 PRO 22 235 LEU 23 236 PHE 24 237 GLN 25 238 LYS 26 239 LEU 27 240 GLY 28 241 PRO 29 242 ALA 30 243 VAL 31 244 LEU 32 245 VAL 33 246 GLU 34 247 ILE 35 248 VAL 36 249 ARG 37 250 ALA 38 251 LEU 39 252 ARG 40 253 ALA 41 254 ARG 42 255 THR 43 256 VAL 44 257 PRO 45 258 ALA 46 259 GLY 47 260 ALA 48 261 VAL 49 262 ILE 50 263 CYS 51 264 ARG 52 265 ILE 53 266 GLY 54 267 GLU 55 268 PRO 56 269 GLY 57 270 ASP 58 271 ARG 59 272 MET 60 273 PHE 61 274 PHE 62 275 VAL 63 276 VAL 64 277 GLU 65 278 GLY 66 279 SER 67 280 VAL 68 281 SER 69 282 VAL 70 283 ALA 71 284 THR 72 285 PRO 73 286 ASN 74 287 PRO 75 288 VAL 76 289 GLU 77 290 LEU 78 291 GLY 79 292 PRO 80 293 GLY 81 294 ALA 82 295 PHE 83 296 PHE 84 297 GLY 85 298 GLU 86 299 MET 87 300 ALA 88 301 LEU 89 302 ILE 90 303 SER 91 304 GLY 92 305 GLU 93 306 PRO 94 307 ARG 95 308 SER 96 309 ALA 97 310 THR 98 311 VAL 99 312 SER 100 313 ALA 101 314 ALA 102 315 THR 103 316 THR 104 317 VAL 105 318 SER 106 319 LEU 107 320 LEU 108 321 SER 109 322 LEU 110 323 HIS 111 324 SER 112 325 ALA 113 326 ASP 114 327 PHE 115 328 GLN 116 329 MET 117 330 LEU 118 331 CYS 119 332 SER 120 333 SER 121 334 SER 122 335 PRO 123 336 GLU 124 337 ILE 125 338 ALA 126 339 GLU 127 340 ILE 128 341 PHE 129 342 ARG 130 343 LYS 131 344 THR 132 345 ALA 133 346 LEU 134 347 GLU 135 348 ARG 136 349 ARG 137 350 GLY 138 351 ALA 139 352 ALA 140 353 ALA 141 354 SER 142 355 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 15249 MlotiCNBDc 100.00 142 100.00 100.00 6.58e-94 BMRB 16628 MloK1_CNBD 100.00 142 100.00 100.00 6.58e-94 PDB 1U12 "M. Loti Cyclic Nucleotide Binding Domain Mutant" 97.18 138 99.28 99.28 1.18e-89 PDB 1VP6 "M.Loti Ion Channel Cylic Nucleotide Binding Domain" 97.18 138 100.00 100.00 1.07e-90 PDB 2K0G "Solution Structure Of A Bacterial Cyclic Nucleotide- Activated K+ Channel Binding Domain In Complex With Camp" 100.00 142 100.00 100.00 6.58e-94 PDB 2KXL "Solution Structure Of A Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain In The Unliganded State" 100.00 142 100.00 100.00 6.58e-94 PDB 2ZD9 "Structure Of A Bacterial Cyclic-Nucleotide Regulated Ion Channel" 98.59 355 100.00 100.00 2.58e-90 PDB 3BEH "Structure Of A Bacterial Cyclic Nucleotide Regulated Ion Channel" 98.59 355 100.00 100.00 2.58e-90 PDB 3CL1 "M. Loti Cyclic-Nucleotide Binding Domain, Cyclic-Gmp Bound" 98.59 140 100.00 100.00 1.84e-92 PDB 3CLP "M. Loti Cyclic-Nucleotide Binding Domain Mutant 2" 98.59 140 99.29 99.29 1.20e-91 PDB 3CO2 "Mlotik1 Ion Channel Cyclic-Nucleotide Binding Domain Mutant" 98.59 140 99.29 99.29 2.76e-91 PDB 4CHV "The Electron Crystallography Structure Of The Camp-bound Potassium Channel Mlok1" 98.59 361 100.00 100.00 2.87e-90 PDB 4CHW "The Electron Crystallography Structure Of The Camp-free Potassium Channel Mlok1" 98.59 361 100.00 100.00 2.87e-90 PDB 4MUV "M. Loti Cyclic-nucleotide Binding Domain Mutant Displaying Inverted Ligand Selectivity, Cyclic-gmp Bound" 100.00 142 97.89 98.59 1.07e-91 DBJ BAB50178 "mll3241 [Mesorhizobium loti MAFF303099]" 98.59 355 100.00 100.00 2.58e-90 REF WP_010911524 "Cyclic nucleotide-gated potassium channel mll3241 [Mesorhizobium loti]" 98.59 355 100.00 100.00 2.58e-90 REF WP_032931689 "cation tolerance protein CutA [Mesorhizobium loti]" 98.59 355 100.00 100.00 2.37e-90 SP Q98GN8 "RecName: Full=Cyclic nucleotide-gated potassium channel mll3241; AltName: Full=MlotiK1 channel" 98.59 355 100.00 100.00 2.58e-90 stop_ save_ ############# # Ligands # ############# save_CMP _Saveframe_category ligand _Mol_type non-polymer _Name_common "CMP (ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE)" _BMRB_code . _PDB_code CMP _Molecular_mass 329.206 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 26 15:38:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOP2 HOP2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB P O1P ? ? SING P O2P ? ? SING P O5' ? ? SING P O3' ? ? SING O2P HOP2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cylic_Nucleotide_Binding_Domain 'Mesorhizobium loti' 381 Bacteria . Mesorhizobium loti 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 $Cylic_Nucleotide_Binding_Domain 'recombinant technology' . Escherichia coli . pET-11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Cylic_Nucleotide_Binding_Domain 10 mg '[U-100% 13C; U-100% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' Tris 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . 'Cornilescu, Delaglio and Bax' . . Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_CC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC' _Sample_label $sample_1 save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_2D_NCACX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NCACX' _Sample_label $sample_1 save_ save_3D_CCC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 10 . mM pH 8 . pH pressure 1 . atm temperature 263 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 adamantane C 13 'methyl carbon' ppm 31.48 external indirect . . . 1 Ala-Gly-Gly N 15 nitrogen ppm 38.9 external indirect . . . 1 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Cyclic nucleotide binding domain, subunit 1' _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 1 220 7 ARG CA C 57.595 0.164 1 2 220 7 ARG CB C 30.836 0.027 1 3 221 8 GLY C C 174.320 0.000 1 4 221 8 GLY CA C 45.302 0.135 1 5 221 8 GLY N N 108.764 0.131 1 6 222 9 ASP C C 180.227 0.160 1 7 222 9 ASP CA C 55.395 0.215 1 8 222 9 ASP CB C 40.666 0.198 1 9 222 9 ASP N N 121.233 0.372 1 10 223 10 PHE C C 176.300 0.000 1 11 223 10 PHE CA C 60.131 0.234 1 12 223 10 PHE CB C 39.753 0.227 1 13 223 10 PHE N N 118.832 0.000 1 14 224 11 VAL N N 119.456 0.000 1 15 225 12 ARG C C 177.900 0.000 1 16 225 12 ARG CA C 58.274 0.000 1 17 225 12 ARG CB C 29.458 0.000 1 18 226 13 ASN C C 175.700 0.000 1 19 226 13 ASN CA C 55.705 0.128 1 20 226 13 ASN CB C 37.704 0.052 1 21 226 13 ASN CG C 177.853 0.000 1 22 226 13 ASN N N 119.140 0.142 1 23 227 14 TRP C C 178.100 0.000 1 24 227 14 TRP CA C 59.544 0.000 1 25 227 14 TRP CB C 29.458 0.000 1 26 227 14 TRP N N 118.918 0.202 1 27 228 15 GLN N N 116.152 0.101 1 28 229 16 LEU CB C 42.615 0.039 1 29 229 16 LEU CD2 C 22.784 0.291 2 30 230 17 VAL C C 177.900 0.000 1 31 230 17 VAL CA C 65.253 0.000 1 32 230 17 VAL CB C 31.279 0.000 1 33 230 17 VAL CG2 C 22.465 0.000 2 34 230 17 VAL N N 116.110 0.142 1 35 231 18 ALA C C 177.642 0.000 1 36 231 18 ALA CA C 54.000 0.000 1 37 231 18 ALA CB C 18.636 0.000 1 38 231 18 ALA N N 119.705 0.070 1 39 232 19 ALA C C 176.500 0.000 1 40 232 19 ALA CA C 51.757 0.080 1 41 232 19 ALA N N 117.244 0.115 1 42 233 20 VAL N N 120.271 0.000 1 43 234 21 PRO C C 177.700 0.000 1 44 234 21 PRO CA C 65.909 0.116 1 45 234 21 PRO CB C 32.595 0.077 1 46 234 21 PRO CG C 27.012 0.000 1 47 234 21 PRO CD C 52.954 0.000 1 48 235 22 LEU CA C 58.266 0.098 1 49 235 22 LEU CB C 42.957 0.161 1 50 235 22 LEU N N 119.430 0.121 1 51 236 23 PHE CA C 57.320 0.092 1 52 236 23 PHE CB C 37.189 0.290 1 53 236 23 PHE N N 110.688 0.128 1 54 237 24 GLN C C 176.934 0.000 1 55 237 24 GLN CA C 57.703 0.000 1 56 237 24 GLN CG C 34.056 0.102 1 57 238 25 LYS C C 176.800 0.000 1 58 238 25 LYS CA C 55.900 0.000 1 59 238 25 LYS CB C 33.046 0.000 1 60 238 25 LYS CG C 25.394 0.000 1 61 238 25 LYS N N 114.585 0.105 1 62 239 26 LEU C C 176.875 0.000 1 63 239 26 LEU CA C 54.300 0.000 1 64 239 26 LEU N N 119.389 0.067 1 65 240 27 GLY CA C 44.690 0.034 1 66 240 27 GLY N N 108.906 0.016 1 67 241 28 PRO C C 178.358 0.050 1 68 241 28 PRO CA C 66.814 0.263 1 69 241 28 PRO CB C 31.127 0.000 1 70 241 28 PRO CD C 49.968 0.159 1 71 241 28 PRO N N 134.814 0.115 1 72 242 29 ALA C C 180.099 0.000 1 73 242 29 ALA N N 118.761 0.025 1 74 243 30 VAL C C 178.000 0.000 1 75 243 30 VAL CA C 65.338 0.000 1 76 243 30 VAL CB C 32.298 0.000 1 77 244 31 LEU C C 178.200 0.000 1 78 244 31 LEU CB C 41.853 0.000 1 79 244 31 LEU CG C 27.194 0.000 1 80 244 31 LEU N N 120.943 0.288 1 81 245 32 VAL C C 177.000 0.000 1 82 245 32 VAL CA C 67.114 0.338 1 83 245 32 VAL CB C 31.492 0.000 1 84 245 32 VAL N N 114.627 0.163 1 85 246 33 GLU C C 173.444 0.139 1 86 246 33 GLU CA C 58.731 0.306 1 87 246 33 GLU CB C 29.284 0.025 1 88 246 33 GLU CG C 35.761 0.052 1 89 246 33 GLU CD C 184.058 0.049 1 90 246 33 GLU N N 117.105 0.192 1 91 247 34 ILE C C 178.000 0.000 1 92 247 34 ILE CA C 61.920 0.219 1 93 247 34 ILE CB C 35.919 0.277 1 94 247 34 ILE CG1 C 27.843 0.156 1 95 247 34 ILE CG2 C 17.722 0.174 1 96 247 34 ILE CD1 C 11.702 0.126 1 97 247 34 ILE N N 120.463 0.096 1 98 248 35 VAL CA C 67.500 0.148 1 99 248 35 VAL CB C 31.172 0.017 1 100 248 35 VAL CG1 C 24.054 0.005 2 101 248 35 VAL CG2 C 21.822 0.000 2 102 248 35 VAL N N 120.699 0.104 1 103 249 36 ARG C C 176.700 0.000 1 104 249 36 ARG CA C 58.642 0.000 1 105 249 36 ARG CB C 30.666 0.154 1 106 249 36 ARG CD C 43.770 0.000 1 107 249 36 ARG N N 115.652 0.093 1 108 250 37 ALA C C 178.900 0.000 1 109 250 37 ALA CA C 52.962 0.000 1 110 250 37 ALA CB C 19.768 0.000 1 111 250 37 ALA N N 120.271 0.048 1 112 251 38 LEU C C 177.600 0.000 1 113 251 38 LEU CA C 55.697 0.058 1 114 251 38 LEU CB C 43.922 0.208 1 115 251 38 LEU CD2 C 27.878 0.000 2 116 251 38 LEU N N 119.839 0.144 1 117 252 39 ARG C C 175.109 0.000 1 118 252 39 ARG CA C 54.300 0.000 1 119 252 39 ARG N N 119.076 0.140 1 120 253 40 ALA C C 177.400 0.000 1 121 253 40 ALA CA C 51.396 0.161 1 122 253 40 ALA CB C 19.979 0.000 1 123 253 40 ALA N N 128.014 0.203 1 124 254 41 ARG C C 174.600 0.000 1 125 254 41 ARG CA C 55.547 0.161 1 126 254 41 ARG CB C 34.653 0.295 1 127 254 41 ARG CG C 26.344 0.000 1 128 254 41 ARG CD C 43.628 0.000 1 129 254 41 ARG N N 120.696 0.167 1 130 255 42 THR C C 173.959 0.199 1 131 255 42 THR CA C 61.873 0.148 1 132 255 42 THR CB C 70.510 0.279 1 133 255 42 THR CG2 C 22.164 0.000 1 134 255 42 THR N N 121.758 0.192 1 135 256 43 VAL CA C 58.261 0.184 1 136 256 43 VAL CB C 34.155 0.138 1 137 256 43 VAL CG2 C 20.695 0.000 2 138 256 43 VAL N N 127.513 0.207 1 139 257 44 PRO C C 175.000 0.000 1 140 257 44 PRO CA C 62.115 0.000 1 141 257 44 PRO CB C 33.180 0.000 1 142 257 44 PRO CG C 27.424 0.000 1 143 258 45 ALA C C 178.900 0.000 1 144 258 45 ALA CA C 53.641 0.000 1 145 258 45 ALA CB C 18.871 0.000 1 146 258 45 ALA N N 120.415 0.136 1 147 259 46 GLY C C 174.300 0.000 1 148 259 46 GLY CA C 44.868 0.044 1 149 259 46 GLY N N 110.757 0.137 1 150 260 47 ALA C C 177.300 0.000 1 151 260 47 ALA CA C 52.356 0.050 1 152 260 47 ALA CB C 19.693 0.121 1 153 260 47 ALA N N 123.250 0.162 1 154 261 48 VAL C C 176.300 0.000 1 155 261 48 VAL CA C 63.688 0.000 1 156 261 48 VAL CB C 32.451 0.000 1 157 261 48 VAL CG1 C 22.730 0.000 2 158 261 48 VAL N N 121.614 0.000 1 159 262 49 ILE C C 176.500 0.000 1 160 262 49 ILE CA C 63.370 0.214 1 161 262 49 ILE CB C 40.112 0.109 1 162 262 49 ILE CG1 C 29.063 0.045 1 163 262 49 ILE CG2 C 17.814 0.029 1 164 262 49 ILE CD1 C 15.963 0.172 1 165 262 49 ILE N N 129.098 0.056 1 166 263 50 CYS C C 171.110 0.096 1 167 263 50 CYS CA C 55.918 0.121 1 168 263 50 CYS CB C 31.955 0.144 1 169 263 50 CYS N N 112.290 0.335 1 170 264 51 ARG C C 174.112 0.000 1 171 264 51 ARG CA C 54.480 0.063 1 172 264 51 ARG CB C 33.354 0.139 1 173 264 51 ARG N N 123.987 0.277 1 174 265 52 ILE C C 174.342 0.157 1 175 265 52 ILE CA C 62.500 0.141 1 176 265 52 ILE CB C 38.412 0.206 1 177 265 52 ILE CG1 C 29.020 0.304 1 178 265 52 ILE CG2 C 15.631 0.190 1 179 265 52 ILE CD1 C 14.457 0.090 1 180 265 52 ILE N N 123.912 0.184 1 181 266 53 GLY C C 173.704 0.000 1 182 266 53 GLY CA C 45.460 0.181 1 183 266 53 GLY N N 111.061 0.078 1 184 267 54 GLU CG C 36.618 0.055 1 185 268 55 PRO C C 177.500 0.000 1 186 268 55 PRO CA C 63.036 0.000 1 187 268 55 PRO CB C 32.213 0.046 1 188 268 55 PRO CD C 50.564 0.000 1 189 269 56 GLY C C 171.800 0.000 1 190 269 56 GLY CA C 44.806 0.137 1 191 269 56 GLY N N 108.589 0.105 1 192 270 57 ASP C C 174.801 0.001 1 193 270 57 ASP CA C 53.051 0.091 1 194 270 57 ASP CB C 41.735 0.216 1 195 270 57 ASP CG C 180.702 0.017 1 196 270 57 ASP N N 121.763 0.000 1 197 271 58 ARG C C 173.536 0.114 1 198 271 58 ARG CA C 53.989 0.011 1 199 271 58 ARG CB C 32.334 0.109 1 200 271 58 ARG CG C 23.741 0.019 1 201 271 58 ARG N N 113.422 0.105 1 202 272 59 MET C C 172.352 0.248 1 203 272 59 MET CA C 54.053 0.000 1 204 272 59 MET CE C 17.734 0.000 1 205 272 59 MET N N 117.460 0.000 1 206 273 60 PHE C C 173.800 0.000 1 207 273 60 PHE CA C 56.528 0.055 1 208 273 60 PHE CB C 44.147 0.128 1 209 273 60 PHE N N 113.179 0.013 1 210 274 61 PHE C C 175.700 0.000 1 211 274 61 PHE CA C 56.551 0.000 1 212 274 61 PHE CB C 41.339 0.000 1 213 274 61 PHE N N 116.529 0.000 1 214 275 62 VAL C C 175.700 0.000 1 215 275 62 VAL CA C 63.747 0.042 1 216 275 62 VAL CB C 31.668 0.229 1 217 275 62 VAL CG1 C 21.975 0.000 2 218 275 62 VAL N N 123.579 0.323 1 219 276 63 VAL CA C 64.567 0.021 1 220 276 63 VAL CB C 34.036 0.000 1 221 276 63 VAL N N 127.965 0.249 1 222 277 64 GLU C C 174.400 0.000 1 223 277 64 GLU CA C 56.219 0.281 1 224 277 64 GLU CB C 34.046 0.124 1 225 277 64 GLU CG C 31.618 0.088 1 226 277 64 GLU CD C 175.647 0.000 1 227 277 64 GLU N N 116.547 0.000 1 228 278 65 GLY C C 170.412 0.212 1 229 278 65 GLY CA C 44.289 0.150 1 230 278 65 GLY N N 112.069 0.046 1 231 279 66 SER C C 174.641 0.000 1 232 279 66 SER CA C 56.481 0.169 1 233 279 66 SER CB C 66.574 0.202 1 234 279 66 SER N N 104.991 0.333 1 235 280 67 VAL C C 173.800 0.142 1 236 280 67 VAL CA C 58.648 0.292 1 237 280 67 VAL CB C 34.145 0.105 1 238 280 67 VAL CG1 C 22.764 0.072 2 239 280 67 VAL CG2 C 19.253 0.051 2 240 280 67 VAL N N 112.959 0.231 1 241 281 68 SER C C 173.527 0.114 1 242 281 68 SER CA C 56.403 0.128 1 243 281 68 SER CB C 64.142 0.063 1 244 281 68 SER N N 114.947 0.095 1 245 282 69 VAL C C 176.508 0.272 1 246 282 69 VAL CA C 61.210 0.182 1 247 282 69 VAL CB C 32.080 0.127 1 248 282 69 VAL CG1 C 19.539 0.065 2 249 282 69 VAL CG2 C 19.097 0.000 2 250 282 69 VAL N N 128.874 0.277 1 251 283 70 ALA C C 179.747 0.186 1 252 283 70 ALA CA C 52.086 0.117 1 253 283 70 ALA CB C 16.983 0.049 1 254 283 70 ALA N N 131.443 0.223 1 255 284 71 THR CA C 61.436 0.094 1 256 284 71 THR CB C 66.267 0.127 1 257 284 71 THR CG2 C 23.894 0.051 1 258 284 71 THR N N 114.433 0.456 1 259 285 72 PRO C C 177.732 0.000 1 260 285 72 PRO CA C 66.330 0.276 1 261 285 72 PRO CB C 32.029 0.000 1 262 285 72 PRO CG C 27.155 0.000 1 263 285 72 PRO CD C 51.083 0.350 1 264 286 73 ASN CA C 50.275 0.065 1 265 286 73 ASN CB C 38.889 0.105 1 266 286 73 ASN N N 113.370 0.204 1 267 287 74 PRO C C 176.200 0.000 1 268 287 74 PRO CA C 64.345 0.160 1 269 287 74 PRO CB C 33.045 0.018 1 270 287 74 PRO CG C 27.596 0.000 1 271 287 74 PRO CD C 51.711 0.178 1 272 287 74 PRO N N 138.216 0.000 1 273 288 75 VAL C C 173.900 0.000 1 274 288 75 VAL CA C 60.677 0.033 1 275 288 75 VAL CB C 36.445 0.163 1 276 288 75 VAL CG1 C 22.359 0.000 2 277 288 75 VAL CG2 C 22.320 0.000 2 278 288 75 VAL N N 119.615 0.239 1 279 289 76 GLU C C 175.977 0.023 1 280 289 76 GLU CA C 54.447 0.073 1 281 289 76 GLU CB C 32.056 0.048 1 282 289 76 GLU CG C 37.049 0.024 1 283 289 76 GLU N N 126.158 0.213 1 284 290 77 LEU C C 175.601 0.237 1 285 290 77 LEU CA C 53.505 0.095 1 286 290 77 LEU CB C 43.249 0.331 1 287 290 77 LEU CD1 C 26.207 0.000 2 288 290 77 LEU CD2 C 26.495 0.195 2 289 290 77 LEU N N 124.512 0.139 1 290 291 78 GLY CA C 43.248 0.000 1 291 291 78 GLY N N 110.397 0.166 1 292 292 79 PRO C C 178.100 0.000 1 293 292 79 PRO CA C 63.926 0.085 1 294 292 79 PRO CB C 31.875 0.000 1 295 292 79 PRO CG C 49.999 0.000 1 296 292 79 PRO CD C 50.281 0.023 1 297 292 79 PRO N N 137.792 0.000 1 298 293 80 GLY C C 173.437 0.000 1 299 293 80 GLY CA C 45.789 0.147 1 300 293 80 GLY N N 113.598 0.172 1 301 294 81 ALA C C 175.900 0.000 1 302 294 81 ALA CA C 51.515 0.076 1 303 294 81 ALA CB C 22.860 0.324 1 304 294 81 ALA N N 121.917 0.199 1 305 295 82 PHE C C 174.150 0.000 1 306 295 82 PHE CA C 54.159 0.030 1 307 295 82 PHE CB C 43.883 0.263 1 308 295 82 PHE N N 112.266 0.269 1 309 296 83 PHE C C 174.467 0.023 1 310 296 83 PHE CA C 56.220 0.167 1 311 296 83 PHE CB C 41.306 0.191 1 312 296 83 PHE N N 111.621 0.211 1 313 297 84 GLY C C 172.153 0.000 1 314 297 84 GLY CA C 44.810 0.228 1 315 297 84 GLY N N 107.063 0.252 1 316 298 85 GLU C C 177.700 0.000 1 317 298 85 GLU CA C 56.804 0.186 1 318 298 85 GLU CB C 28.327 0.000 1 319 298 85 GLU N N 118.886 0.000 1 320 299 86 MET C C 179.400 0.000 1 321 299 86 MET CA C 60.388 0.000 1 322 299 86 MET CB C 32.569 0.195 1 323 299 86 MET CE C 16.206 0.045 1 324 299 86 MET N N 119.392 0.232 1 325 300 87 ALA C C 181.000 0.000 1 326 300 87 ALA CA C 55.166 0.175 1 327 300 87 ALA CB C 20.320 0.137 1 328 300 87 ALA N N 122.976 0.096 1 329 301 88 LEU C C 178.943 0.081 1 330 301 88 LEU CA C 56.648 0.168 1 331 301 88 LEU CB C 40.333 0.194 1 332 301 88 LEU CG C 26.602 0.337 1 333 301 88 LEU CD1 C 22.272 0.101 2 334 301 88 LEU CD2 C 25.685 0.154 2 335 301 88 LEU N N 114.933 0.155 1 336 302 89 ILE C C 176.836 0.062 1 337 302 89 ILE CA C 63.381 0.000 1 338 302 89 ILE CB C 39.752 0.101 1 339 302 89 ILE CG2 C 17.142 0.325 1 340 302 89 ILE CD1 C 14.406 0.092 1 341 302 89 ILE N N 118.197 0.264 1 342 303 90 SER C C 176.593 0.000 1 343 303 90 SER CA C 59.498 0.133 1 344 303 90 SER CB C 66.356 0.157 1 345 303 90 SER N N 112.161 0.199 1 346 304 91 GLY C C 174.132 0.000 1 347 304 91 GLY CA C 46.208 0.118 1 348 304 91 GLY N N 112.394 0.340 1 349 305 92 GLU CA C 54.718 0.054 1 350 305 92 GLU CB C 29.249 0.000 1 351 305 92 GLU CG C 36.752 0.115 1 352 305 92 GLU N N 120.424 0.000 1 353 306 93 PRO C C 177.600 0.000 1 354 306 93 PRO CA C 61.869 0.243 1 355 306 93 PRO CB C 32.425 0.000 1 356 306 93 PRO CD C 50.565 0.115 1 357 306 93 PRO N N 135.155 0.226 1 358 307 94 ARG C C 178.800 0.000 1 359 307 94 ARG CA C 55.725 0.140 1 360 307 94 ARG CB C 30.944 0.171 1 361 307 94 ARG CG C 28.038 0.000 1 362 307 94 ARG N N 115.471 0.098 1 363 308 95 SER C C 173.882 0.018 1 364 308 95 SER CA C 60.004 0.098 1 365 308 95 SER CB C 65.778 0.108 1 366 308 95 SER N N 118.320 0.239 1 367 309 96 ALA C C 174.400 0.000 1 368 309 96 ALA CA C 51.381 0.106 1 369 309 96 ALA CB C 22.211 0.080 1 370 309 96 ALA N N 120.334 0.279 1 371 310 97 THR C C 173.671 0.271 1 372 310 97 THR CA C 61.703 0.036 1 373 310 97 THR CB C 69.780 0.094 1 374 310 97 THR CG2 C 22.317 0.044 1 375 310 97 THR N N 118.723 0.213 1 376 311 98 VAL C C 174.700 0.000 1 377 311 98 VAL CA C 61.088 0.126 1 378 311 98 VAL CB C 33.571 0.252 1 379 311 98 VAL CG1 C 21.015 0.000 2 380 311 98 VAL CG2 C 20.900 0.000 2 381 311 98 VAL N N 127.259 0.348 1 382 312 99 SER C C 172.371 0.109 1 383 312 99 SER CA C 55.773 0.114 1 384 312 99 SER CB C 66.739 0.155 1 385 312 99 SER N N 121.397 0.255 1 386 313 100 ALA C C 177.938 0.063 1 387 313 100 ALA CA C 53.219 0.120 1 388 313 100 ALA CB C 19.315 0.149 1 389 313 100 ALA N N 124.773 0.232 1 390 314 101 ALA C C 177.984 0.000 1 391 314 101 ALA CA C 53.958 0.167 1 392 314 101 ALA CB C 19.081 0.102 1 393 314 101 ALA N N 132.234 0.127 1 394 315 102 THR C C 173.600 0.148 1 395 315 102 THR CA C 59.695 0.108 1 396 315 102 THR CB C 72.626 0.247 1 397 315 102 THR CG2 C 21.320 0.193 1 398 315 102 THR N N 108.934 0.350 1 399 316 103 THR C C 176.386 0.355 1 400 316 103 THR CA C 65.592 0.104 1 401 316 103 THR CB C 68.831 0.139 1 402 316 103 THR CG2 C 22.543 0.220 1 403 316 103 THR N N 116.415 0.339 1 404 317 104 VAL C C 173.626 0.159 1 405 317 104 VAL CA C 59.468 0.291 1 406 317 104 VAL CB C 36.623 0.239 1 407 317 104 VAL CG1 C 23.121 0.334 2 408 317 104 VAL N N 130.318 0.363 1 409 318 105 SER C C 173.445 0.078 1 410 318 105 SER CA C 56.559 0.085 1 411 318 105 SER CB C 64.296 0.135 1 412 318 105 SER N N 121.315 0.122 1 413 319 106 LEU C C 176.932 0.110 1 414 319 106 LEU CA C 53.290 0.149 1 415 319 106 LEU CB C 47.304 0.162 1 416 319 106 LEU CD1 C 26.467 0.306 1 417 319 106 LEU CD2 C 26.467 0.306 1 418 319 106 LEU N N 125.302 0.268 1 419 320 107 LEU C C 176.227 0.151 1 420 320 107 LEU CA C 53.470 0.148 1 421 320 107 LEU CB C 46.674 0.066 1 422 320 107 LEU CD1 C 23.267 0.102 1 423 320 107 LEU CD2 C 23.267 0.102 1 424 320 107 LEU N N 119.630 0.261 1 425 321 108 SER C C 172.887 0.013 1 426 321 108 SER CA C 56.505 0.335 1 427 321 108 SER CB C 66.351 0.128 1 428 321 108 SER N N 117.682 0.000 1 429 322 109 LEU C C 175.035 0.072 1 430 322 109 LEU CA C 52.527 0.108 1 431 322 109 LEU CB C 46.624 0.124 1 432 322 109 LEU CG C 27.155 0.000 1 433 322 109 LEU CD1 C 24.794 0.091 2 434 322 109 LEU CD2 C 24.851 0.034 2 435 322 109 LEU N N 124.629 0.265 1 436 323 110 HIS C C 176.500 0.000 1 437 323 110 HIS CA C 57.697 0.225 1 438 323 110 HIS CB C 32.912 0.000 1 439 323 110 HIS N N 127.220 0.419 1 440 324 111 SER C C 175.900 0.000 1 441 324 111 SER CA C 62.076 0.000 1 442 324 111 SER CB C 63.036 0.000 1 443 324 111 SER N N 119.168 0.336 1 444 325 112 ALA N N 124.828 0.240 1 445 326 113 ASP C C 177.700 0.000 1 446 326 113 ASP CA C 56.714 0.225 1 447 326 113 ASP CB C 42.920 0.115 1 448 327 114 PHE C C 176.900 0.000 1 449 327 114 PHE CA C 61.622 0.131 1 450 327 114 PHE CB C 39.250 0.044 1 451 327 114 PHE N N 122.914 0.073 1 452 328 115 GLN C C 178.700 0.000 1 453 328 115 GLN CA C 58.603 0.000 1 454 328 115 GLN CB C 27.980 0.000 1 455 328 115 GLN N N 119.810 0.000 1 456 329 116 MET C C 178.900 0.000 1 457 329 116 MET CA C 59.014 0.127 1 458 329 116 MET CB C 31.295 0.000 1 459 329 116 MET CE C 17.550 0.000 1 460 329 116 MET N N 120.367 0.048 1 461 330 117 LEU CA C 58.227 0.000 1 462 330 117 LEU CB C 41.301 0.072 1 463 330 117 LEU N N 123.206 0.310 1 464 331 118 CYS C C 176.300 0.000 1 465 331 118 CYS CA C 64.038 0.197 1 466 331 118 CYS CB C 27.263 0.176 1 467 331 118 CYS N N 113.660 0.000 1 468 332 119 SER C C 175.700 0.000 1 469 332 119 SER CA C 60.858 0.056 1 470 332 119 SER CB C 63.125 0.226 1 471 332 119 SER N N 113.653 0.053 1 472 333 120 SER CA C 60.846 0.002 1 473 333 120 SER CB C 64.418 0.090 1 474 333 120 SER N N 114.611 0.048 1 475 334 121 SER CA C 54.455 0.087 1 476 334 121 SER CB C 62.660 0.056 1 477 335 122 PRO C C 179.600 0.000 1 478 335 122 PRO CA C 64.782 0.000 1 479 335 122 PRO CB C 32.394 0.000 1 480 336 123 GLU CG C 36.723 0.000 1 481 336 123 GLU N N 117.307 0.212 1 482 337 124 ILE C C 177.300 0.000 1 483 337 124 ILE CA C 64.467 0.399 1 484 337 124 ILE CB C 37.096 0.185 1 485 337 124 ILE CG1 C 30.464 0.172 1 486 337 124 ILE CG2 C 18.328 0.178 1 487 337 124 ILE CD1 C 13.241 0.084 1 488 338 125 ALA C C 181.000 0.000 1 489 338 125 ALA CA C 56.186 0.000 1 490 338 125 ALA CB C 18.809 0.000 1 491 338 125 ALA N N 122.574 0.359 1 492 339 126 GLU C C 178.361 0.122 1 493 339 126 GLU CA C 58.469 0.000 1 494 339 126 GLU CB C 29.688 0.000 1 495 339 126 GLU CG C 35.434 0.320 1 496 339 126 GLU CD C 180.117 0.000 1 497 339 126 GLU N N 116.817 0.096 1 498 340 127 ILE C C 180.643 0.069 1 499 340 127 ILE CA C 65.599 0.093 1 500 340 127 ILE CB C 37.967 0.139 1 501 340 127 ILE CG1 C 28.830 0.415 1 502 340 127 ILE CG2 C 16.821 0.117 1 503 340 127 ILE CD1 C 14.376 0.000 1 504 340 127 ILE N N 120.169 0.228 1 505 341 128 PHE C C 177.700 0.000 1 506 341 128 PHE CA C 59.901 0.256 1 507 341 128 PHE CB C 37.939 0.043 1 508 341 128 PHE N N 119.748 0.100 1 509 342 129 ARG C C 179.500 0.000 1 510 342 129 ARG CA C 60.234 0.000 1 511 342 129 ARG CB C 31.338 0.000 1 512 342 129 ARG CG C 27.616 0.000 1 513 342 129 ARG N N 117.778 0.197 1 514 343 130 LYS C C 179.444 0.098 1 515 343 130 LYS CA C 59.845 0.124 1 516 343 130 LYS CB C 32.453 0.094 1 517 343 130 LYS CG C 25.895 0.068 1 518 343 130 LYS CD C 29.861 0.000 1 519 343 130 LYS CE C 41.999 0.010 1 520 343 130 LYS N N 119.440 0.181 1 521 344 131 THR C C 175.679 0.038 1 522 344 131 THR CA C 67.692 0.407 1 523 344 131 THR CB C 68.714 0.231 1 524 344 131 THR CG2 C 20.812 0.071 1 525 344 131 THR N N 117.436 0.201 1 526 345 132 ALA C C 179.800 0.000 1 527 345 132 ALA CA C 55.643 0.204 1 528 345 132 ALA CB C 19.481 0.128 1 529 345 132 ALA N N 123.559 0.337 1 530 346 133 LEU C C 180.455 0.114 1 531 346 133 LEU CA C 58.154 0.027 1 532 346 133 LEU CB C 42.116 0.211 1 533 346 133 LEU CD1 C 24.966 0.000 1 534 346 133 LEU CD2 C 24.966 0.000 1 535 346 133 LEU N N 116.673 0.144 1 536 347 134 GLU C C 180.500 0.000 1 537 347 134 GLU CA C 58.296 0.000 1 538 347 134 GLU CB C 29.707 0.000 1 539 347 134 GLU CG C 35.929 0.000 1 540 347 134 GLU N N 120.028 0.106 1 541 348 135 ARG C C 177.400 0.000 1 542 348 135 ARG CA C 58.968 0.000 1 543 348 135 ARG CB C 31.492 0.000 1 544 348 135 ARG N N 120.002 0.192 1 545 349 136 ARG C C 178.615 0.015 1 546 349 136 ARG CA C 58.392 0.000 1 547 349 136 ARG CB C 31.991 0.000 1 548 349 136 ARG N N 119.667 0.048 1 549 350 137 GLY C C 174.373 0.000 1 550 350 137 GLY CA C 45.683 0.130 1 551 350 137 GLY N N 106.110 0.279 1 552 351 138 ALA N N 123.567 0.000 1 stop_ save_