data_15899 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone chemical shift assignments of the C-terminal CH domain of human alpha-parvin ; _BMRB_accession_number 15899 _BMRB_flat_file_name bmr15899.str _Entry_type original _Submission_date 2008-07-31 _Accession_date 2008-07-31 _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 Lorenz Sonja G. . 2 Vakonakis Ioannis . . 3 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 120 "13C chemical shifts" 231 "15N chemical shifts" 120 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-19 original author . stop_ _Original_release_date 2008-11-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Analysis of the Interactions between Paxillin LD motifs and alpha-Parvin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18940607 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lorenz Sonja . . 2 Vakonakis Ioannis . . 3 Lowe Edward D. . 4 Campbell Iain D. . 5 Noble Martin E.M. . 6 Hoellerer Maria K. . stop_ _Journal_abbreviation Structure _Journal_volume 16 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1521 _Page_last 1531 _Year 2008 _Details . loop_ _Keyword alpha-parvin 'calponin homology domain' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C-terminal CH domain of alpha-parvin monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal CH domain of alpha-parvin' $C-terminal_CH_domain_of_alpha-parvin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'C-terminal CH domain of alpha-parvin' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C-terminal_CH_domain_of_alpha-parvin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C-terminal_CH_domain_of_alpha-parvin _Molecular_mass 15460.8 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; GPLGSGRHERDAFDTLFDHA PDKLNVVKKTLITFVNKHLN KLNLEVTELETQFADGVYLV LLMGLLEGYFVPLHSFFLTP DSFEQKVLNVSFAFELMQDG GLEKPKPRPEDIVNCDLKST LRVLYNLFTKYRNVE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 GLY 2 -3 PRO 3 -2 LEU 4 -1 GLY 5 242 SER 6 243 GLY 7 244 ARG 8 245 HIS 9 246 GLU 10 247 ARG 11 248 ASP 12 249 ALA 13 250 PHE 14 251 ASP 15 252 THR 16 253 LEU 17 254 PHE 18 255 ASP 19 256 HIS 20 257 ALA 21 258 PRO 22 259 ASP 23 260 LYS 24 261 LEU 25 262 ASN 26 263 VAL 27 264 VAL 28 265 LYS 29 266 LYS 30 267 THR 31 268 LEU 32 269 ILE 33 270 THR 34 271 PHE 35 272 VAL 36 273 ASN 37 274 LYS 38 275 HIS 39 276 LEU 40 277 ASN 41 278 LYS 42 279 LEU 43 280 ASN 44 281 LEU 45 282 GLU 46 283 VAL 47 284 THR 48 285 GLU 49 286 LEU 50 287 GLU 51 288 THR 52 289 GLN 53 290 PHE 54 291 ALA 55 292 ASP 56 293 GLY 57 294 VAL 58 295 TYR 59 296 LEU 60 297 VAL 61 298 LEU 62 299 LEU 63 300 MET 64 301 GLY 65 302 LEU 66 303 LEU 67 304 GLU 68 305 GLY 69 306 TYR 70 307 PHE 71 308 VAL 72 309 PRO 73 310 LEU 74 311 HIS 75 312 SER 76 313 PHE 77 314 PHE 78 315 LEU 79 316 THR 80 317 PRO 81 318 ASP 82 319 SER 83 320 PHE 84 321 GLU 85 322 GLN 86 323 LYS 87 324 VAL 88 325 LEU 89 326 ASN 90 327 VAL 91 328 SER 92 329 PHE 93 330 ALA 94 331 PHE 95 332 GLU 96 333 LEU 97 334 MET 98 335 GLN 99 336 ASP 100 337 GLY 101 338 GLY 102 339 LEU 103 340 GLU 104 341 LYS 105 342 PRO 106 343 LYS 107 344 PRO 108 345 ARG 109 346 PRO 110 347 GLU 111 348 ASP 112 349 ILE 113 350 VAL 114 351 ASN 115 352 CYS 116 353 ASP 117 354 LEU 118 355 LYS 119 356 SER 120 357 THR 121 358 LEU 122 359 ARG 123 360 VAL 124 361 LEU 125 362 TYR 126 363 ASN 127 364 LEU 128 365 PHE 129 366 THR 130 367 LYS 131 368 TYR 132 369 ARG 133 370 ASN 134 371 VAL 135 372 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 15760 alpha-parvin 95.56 129 100.00 100.00 1.22e-86 PDB 2K2R "The Nmr Structure Of Alpha-Parvin Ch2PAXILLIN LD1 COMPLEX" 95.56 129 100.00 100.00 1.22e-86 PDB 2VZC "Crystal Structure Of The C-Terminal Calponin Homology Domain Of Alpha Parvin" 97.04 131 100.00 100.00 3.07e-88 PDB 2VZD "Crystal Structure Of The C-Terminal Calponin Homology Domain Of Alpha Parvin In Complex With Paxillin Ld1 Motif" 97.04 131 100.00 100.00 3.07e-88 PDB 2VZG "Crystal Structure Of The C-Terminal Calponin Homology Domain Of Alpha-Parvin In Complex With Paxillin Ld2 Motif" 97.04 131 100.00 100.00 3.07e-88 PDB 2VZI "Crystal Structure Of The C-Terminal Calponin Homology Domain Of Alpha-Parvin In Complex With Paxillin Ld4 Motif" 97.04 131 100.00 100.00 3.07e-88 PDB 3KMW "Crystal Structure Of The IlkALPHA-Parvin Core Complex (Mgatp)" 96.30 129 97.69 97.69 4.87e-83 PDB 3REP "Crystal Structure Of The IlkALPHA-Parvin Core Complex (Mnatp)" 96.30 129 97.69 97.69 4.87e-83 DBJ BAA91815 "unnamed protein product [Homo sapiens]" 97.04 372 100.00 100.00 2.68e-87 DBJ BAA97981 "unnamed protein product [Mus musculus]" 97.04 372 100.00 100.00 4.00e-87 DBJ BAC36771 "unnamed protein product [Mus musculus]" 97.04 372 100.00 100.00 4.41e-87 DBJ BAE28686 "unnamed protein product [Mus musculus]" 97.04 336 100.00 100.00 2.64e-87 DBJ BAG73514 "parvin, alpha [synthetic construct]" 97.04 372 100.00 100.00 2.68e-87 GB AAG09802 "actopaxin [Rattus norvegicus]" 97.04 372 100.00 100.00 3.87e-87 GB AAG09803 "actopaxin [Mus musculus]" 97.04 372 100.00 100.00 4.09e-87 GB AAG27173 "alpha-parvin [Homo sapiens]" 97.04 372 100.00 100.00 2.68e-87 GB AAG27175 "alpha-parvin [Mus musculus]" 97.04 372 100.00 100.00 4.09e-87 GB AAH14535 "Parvin, alpha [Homo sapiens]" 97.04 372 100.00 100.00 2.46e-87 REF NP_001092614 "alpha-parvin [Bos taurus]" 97.04 372 100.00 100.00 2.92e-87 REF NP_060692 "alpha-parvin [Homo sapiens]" 97.04 412 100.00 100.00 4.79e-87 REF NP_065631 "alpha-parvin [Mus musculus]" 97.04 372 100.00 100.00 4.09e-87 REF NP_065707 "alpha-parvin [Rattus norvegicus]" 97.04 372 100.00 100.00 3.87e-87 REF XP_001091788 "PREDICTED: alpha-parvin-like [Macaca mulatta]" 97.04 364 100.00 100.00 1.11e-86 SP Q9EPC1 "RecName: Full=Alpha-parvin; AltName: Full=Actopaxin" 97.04 372 100.00 100.00 4.09e-87 SP Q9HB97 "RecName: Full=Alpha-parvin; AltName: Full=Actopaxin" 97.04 372 100.00 100.00 3.87e-87 SP Q9NVD7 "RecName: Full=Alpha-parvin; AltName: Full=Actopaxin; AltName: Full=CH-ILKBP; AltName: Full=Calponin-like integrin-linked kinase" 97.04 372 100.00 100.00 2.68e-87 TPG DAA22326 "TPA: parvin, alpha-like [Bos taurus]" 78.52 439 100.00 100.00 7.04e-67 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $C-terminal_CH_domain_of_alpha-parvin Human 9606 Eukaryota Metazoa Homo sapiens PARVA 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 $C-terminal_CH_domain_of_alpha-parvin 'recombinant technology' . Escherichia coli BL21 pGEX-6P1 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 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DSS 0.1 mM 'natural abundance' D2O 5 % 'natural abundance' CHAPS 1.5 mM 'natural abundance' $C-terminal_CH_domain_of_alpha-parvin 240 uM '[U-98% 13C; U-98% 15N]' DTT 2 mM 'natural abundance' H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.2.2_01 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer home-built _Model n.a. _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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' 325 . mM pH 6.9 0.05 pH pressure 1 . atm temperature 303 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '2D 1H-15N HSQC' 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 'C-terminal CH domain of alpha-parvin' _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 -3 2 PRO CA C 63.214 0.2 1 2 -3 2 PRO CB C 32.389 0.2 1 3 -2 3 LEU H H 8.482 0.01 1 4 -2 3 LEU CA C 55.415 0.2 1 5 -2 3 LEU CB C 42.306 0.2 1 6 -2 3 LEU N N 122.181 0.1 1 7 -1 4 GLY H H 8.379 0.01 1 8 -1 4 GLY CA C 45.417 0.2 1 9 -1 4 GLY N N 109.846 0.1 1 10 242 5 SER H H 8.293 0.01 1 11 242 5 SER CA C 58.620 0.2 1 12 242 5 SER CB C 64.059 0.2 1 13 242 5 SER N N 115.788 0.1 1 14 243 6 GLY H H 8.541 0.01 1 15 243 6 GLY CA C 45.497 0.2 1 16 243 6 GLY N N 110.966 0.1 1 17 244 7 ARG H H 8.142 0.01 1 18 244 7 ARG CA C 56.301 0.2 1 19 244 7 ARG CB C 30.730 0.2 1 20 244 7 ARG N N 120.500 0.1 1 21 245 8 HIS H H 8.369 0.01 1 22 245 8 HIS CA C 56.162 0.2 1 23 245 8 HIS CB C 30.693 0.2 1 24 245 8 HIS N N 120.372 0.1 1 25 246 9 GLU H H 8.359 0.01 1 26 246 9 GLU CA C 55.950 0.2 1 27 246 9 GLU CB C 30.429 0.2 1 28 246 9 GLU N N 122.500 0.1 1 29 247 10 ARG H H 8.369 0.01 1 30 247 10 ARG CA C 56.178 0.2 1 31 247 10 ARG CB C 31.488 0.2 1 32 247 10 ARG N N 122.457 0.1 1 33 248 11 ASP H H 8.869 0.01 1 34 248 11 ASP N N 123.127 0.1 1 35 249 12 ALA CA C 54.546 0.2 1 36 249 12 ALA CB C 18.908 0.2 1 37 250 13 PHE H H 8.352 0.01 1 38 250 13 PHE CA C 61.377 0.2 1 39 250 13 PHE CB C 38.938 0.2 1 40 250 13 PHE N N 118.733 0.1 1 41 251 14 ASP H H 8.172 0.01 1 42 251 14 ASP CA C 57.728 0.2 1 43 251 14 ASP CB C 40.949 0.2 1 44 251 14 ASP N N 118.456 0.1 1 45 252 15 THR H H 7.736 0.01 1 46 252 15 THR CA C 65.097 0.2 1 47 252 15 THR CB C 68.976 0.2 1 48 252 15 THR N N 112.620 0.1 1 49 253 16 LEU H H 7.578 0.01 1 50 253 16 LEU CA C 57.328 0.2 1 51 253 16 LEU CB C 42.143 0.2 1 52 253 16 LEU N N 122.105 0.1 1 53 254 17 PHE H H 7.737 0.01 1 54 254 17 PHE CA C 59.835 0.2 1 55 254 17 PHE CB C 39.175 0.2 1 56 254 17 PHE N N 115.525 0.1 1 57 255 18 ASP H H 7.813 0.01 1 58 255 18 ASP CA C 55.484 0.2 1 59 255 18 ASP CB C 41.139 0.2 1 60 255 18 ASP N N 117.701 0.1 1 61 256 19 HIS H H 7.898 0.01 1 62 256 19 HIS CA C 56.265 0.2 1 63 256 19 HIS CB C 31.080 0.2 1 64 256 19 HIS N N 115.935 0.1 1 65 257 20 ALA H H 8.062 0.01 1 66 257 20 ALA N N 123.674 0.1 1 67 258 21 PRO CA C 65.110 0.2 1 68 258 21 PRO CB C 31.459 0.2 1 69 259 22 ASP H H 8.580 0.01 1 70 259 22 ASP CA C 55.928 0.2 1 71 259 22 ASP CB C 39.723 0.2 1 72 259 22 ASP N N 116.864 0.1 1 73 260 23 LYS H H 7.767 0.01 1 74 260 23 LYS CA C 57.662 0.2 1 75 260 23 LYS CB C 32.225 0.2 1 76 260 23 LYS N N 119.850 0.1 1 77 261 24 LEU H H 8.035 0.01 1 78 261 24 LEU CA C 57.783 0.2 1 79 261 24 LEU CB C 41.014 0.2 1 80 261 24 LEU N N 120.507 0.1 1 81 262 25 ASN H H 8.133 0.01 1 82 262 25 ASN CA C 56.688 0.2 1 83 262 25 ASN CB C 37.834 0.2 1 84 262 25 ASN N N 116.885 0.1 1 85 263 26 VAL H H 7.563 0.01 1 86 263 26 VAL CA C 66.236 0.2 1 87 263 26 VAL CB C 31.704 0.2 1 88 263 26 VAL N N 120.120 0.1 1 89 264 27 VAL H H 7.935 0.01 1 90 264 27 VAL CA C 66.867 0.2 1 91 264 27 VAL CB C 31.411 0.2 1 92 264 27 VAL N N 123.012 0.1 1 93 265 28 LYS H H 8.593 0.01 1 94 265 28 LYS CA C 61.426 0.2 1 95 265 28 LYS CB C 32.435 0.2 1 96 265 28 LYS N N 118.881 0.1 1 97 266 29 LYS H H 7.792 0.01 1 98 266 29 LYS CA C 59.820 0.2 1 99 266 29 LYS CB C 32.176 0.2 1 100 266 29 LYS N N 117.693 0.1 1 101 267 30 THR H H 8.199 0.01 1 102 267 30 THR CA C 66.876 0.2 1 103 267 30 THR CB C 68.903 0.2 1 104 267 30 THR N N 118.152 0.1 1 105 268 31 LEU H H 8.308 0.01 1 106 268 31 LEU CA C 57.878 0.2 1 107 268 31 LEU CB C 41.730 0.2 1 108 268 31 LEU N N 120.870 0.1 1 109 269 32 ILE H H 8.699 0.01 1 110 269 32 ILE CA C 65.695 0.2 1 111 269 32 ILE CB C 37.741 0.2 1 112 269 32 ILE N N 121.411 0.1 1 113 270 33 THR H H 8.039 0.01 1 114 270 33 THR CA C 67.094 0.2 1 115 270 33 THR CB C 68.809 0.2 1 116 270 33 THR N N 117.523 0.1 1 117 271 34 PHE H H 7.803 0.01 1 118 271 34 PHE CA C 60.439 0.2 1 119 271 34 PHE CB C 39.584 0.2 1 120 271 34 PHE N N 122.098 0.1 1 121 272 35 VAL H H 8.709 0.01 1 122 272 35 VAL CA C 66.069 0.2 1 123 272 35 VAL CB C 31.277 0.2 1 124 272 35 VAL N N 113.634 0.1 1 125 273 36 ASN H H 8.244 0.01 1 126 273 36 ASN CA C 55.959 0.2 1 127 273 36 ASN CB C 37.920 0.2 1 128 273 36 ASN N N 118.986 0.1 1 129 274 37 LYS H H 7.758 0.01 1 130 274 37 LYS CA C 59.365 0.2 1 131 274 37 LYS CB C 31.540 0.2 1 132 274 37 LYS N N 122.851 0.1 1 133 275 38 HIS H H 6.377 0.01 1 134 275 38 HIS CA C 58.172 0.2 1 135 275 38 HIS CB C 31.970 0.2 1 136 275 38 HIS N N 113.944 0.1 1 137 276 39 LEU H H 9.104 0.01 1 138 276 39 LEU CA C 58.418 0.2 1 139 276 39 LEU CB C 39.967 0.2 1 140 276 39 LEU N N 118.376 0.1 1 141 277 40 ASN H H 8.962 0.01 1 142 277 40 ASN CA C 56.308 0.2 1 143 277 40 ASN CB C 38.905 0.2 1 144 277 40 ASN N N 116.985 0.1 1 145 278 41 LYS H H 7.923 0.01 1 146 278 41 LYS CA C 59.412 0.2 1 147 278 41 LYS CB C 32.427 0.2 1 148 278 41 LYS N N 120.861 0.1 1 149 279 42 LEU H H 7.530 0.01 1 150 279 42 LEU CA C 52.912 0.2 1 151 279 42 LEU CB C 42.073 0.2 1 152 279 42 LEU N N 115.713 0.1 1 153 280 43 ASN H H 7.948 0.01 1 154 280 43 ASN CA C 54.497 0.2 1 155 280 43 ASN CB C 37.164 0.2 1 156 280 43 ASN N N 113.656 0.1 1 157 281 44 LEU H H 7.304 0.01 1 158 281 44 LEU CA C 53.023 0.2 1 159 281 44 LEU CB C 45.482 0.2 1 160 281 44 LEU N N 117.422 0.1 1 161 282 45 GLU H H 7.984 0.01 1 162 282 45 GLU CA C 55.201 0.2 1 163 282 45 GLU CB C 32.910 0.2 1 164 282 45 GLU N N 117.914 0.1 1 165 283 46 VAL H H 9.846 0.01 1 166 283 46 VAL CA C 61.393 0.2 1 167 283 46 VAL CB C 33.346 0.2 1 168 283 46 VAL N N 125.484 0.1 1 169 284 47 THR H H 9.553 0.01 1 170 284 47 THR CA C 61.689 0.2 1 171 284 47 THR CB C 70.394 0.2 1 172 284 47 THR N N 116.724 0.1 1 173 285 48 GLU H H 8.107 0.01 1 174 285 48 GLU CA C 55.397 0.2 1 175 285 48 GLU CB C 31.249 0.2 1 176 285 48 GLU N N 123.538 0.1 1 177 286 49 LEU H H 9.091 0.01 1 178 286 49 LEU CA C 57.503 0.2 1 179 286 49 LEU CB C 42.857 0.2 1 180 286 49 LEU N N 125.009 0.1 1 181 287 50 GLU H H 9.800 0.01 1 182 287 50 GLU CA C 60.387 0.2 1 183 287 50 GLU CB C 29.933 0.2 1 184 287 50 GLU N N 115.521 0.1 1 185 288 51 THR H H 7.551 0.01 1 186 288 51 THR CA C 62.281 0.2 1 187 288 51 THR CB C 71.302 0.2 1 188 288 51 THR N N 102.535 0.1 1 189 289 52 GLN H H 7.443 0.01 1 190 289 52 GLN CA C 59.393 0.2 1 191 289 52 GLN CB C 29.097 0.2 1 192 289 52 GLN N N 117.666 0.1 1 193 290 53 PHE H H 9.692 0.01 1 194 290 53 PHE CA C 58.826 0.2 1 195 290 53 PHE CB C 38.923 0.2 1 196 290 53 PHE N N 116.529 0.1 1 197 291 54 ALA H H 7.019 0.01 1 198 291 54 ALA CA C 55.216 0.2 1 199 291 54 ALA CB C 20.983 0.2 1 200 291 54 ALA N N 123.994 0.1 1 201 292 55 ASP H H 7.437 0.01 1 202 292 55 ASP CA C 52.860 0.2 1 203 292 55 ASP CB C 40.401 0.2 1 204 292 55 ASP N N 107.956 0.1 1 205 293 56 GLY H H 7.619 0.01 1 206 293 56 GLY CA C 48.266 0.2 1 207 293 56 GLY N N 104.269 0.1 1 208 294 57 VAL H H 8.136 0.01 1 209 294 57 VAL CA C 68.042 0.2 1 210 294 57 VAL CB C 31.462 0.2 1 211 294 57 VAL N N 121.361 0.1 1 212 295 58 TYR H H 9.105 0.01 1 213 295 58 TYR CA C 58.384 0.2 1 214 295 58 TYR CB C 36.126 0.2 1 215 295 58 TYR N N 115.839 0.1 1 216 296 59 LEU H H 8.446 0.01 1 217 296 59 LEU CA C 58.453 0.2 1 218 296 59 LEU CB C 42.776 0.2 1 219 296 59 LEU N N 118.688 0.1 1 220 297 60 VAL H H 7.535 0.01 1 221 297 60 VAL CA C 67.797 0.2 1 222 297 60 VAL CB C 31.559 0.2 1 223 297 60 VAL N N 118.815 0.1 1 224 298 61 LEU H H 8.073 0.01 1 225 298 61 LEU CA C 57.760 0.2 1 226 298 61 LEU CB C 41.573 0.2 1 227 298 61 LEU N N 115.683 0.1 1 228 299 62 LEU H H 8.715 0.01 1 229 299 62 LEU CA C 57.965 0.2 1 230 299 62 LEU CB C 42.474 0.2 1 231 299 62 LEU N N 118.245 0.1 1 232 300 63 MET H H 7.529 0.01 1 233 300 63 MET CA C 55.675 0.2 1 234 300 63 MET CB C 28.536 0.2 1 235 300 63 MET N N 115.636 0.1 1 236 301 64 GLY H H 7.744 0.01 1 237 301 64 GLY CA C 47.936 0.2 1 238 301 64 GLY N N 105.514 0.1 1 239 302 65 LEU H H 7.933 0.01 1 240 302 65 LEU CA C 57.882 0.2 1 241 302 65 LEU CB C 42.567 0.2 1 242 302 65 LEU N N 121.567 0.1 1 243 303 66 LEU H H 8.319 0.01 1 244 303 66 LEU CA C 57.133 0.2 1 245 303 66 LEU CB C 40.592 0.2 1 246 303 66 LEU N N 119.269 0.1 1 247 304 67 GLU H H 7.458 0.01 1 248 304 67 GLU CA C 55.852 0.2 1 249 304 67 GLU CB C 30.970 0.2 1 250 304 67 GLU N N 114.223 0.1 1 251 305 68 GLY H H 7.649 0.01 1 252 305 68 GLY CA C 46.722 0.2 1 253 305 68 GLY N N 109.180 0.1 1 254 306 69 TYR H H 7.851 0.01 1 255 306 69 TYR N N 117.666 0.1 1 256 311 74 HIS CA C 56.319 0.2 1 257 311 74 HIS CB C 29.713 0.2 1 258 312 75 SER H H 7.536 0.01 1 259 312 75 SER CA C 59.312 0.2 1 260 312 75 SER CB C 64.419 0.2 1 261 312 75 SER N N 115.758 0.1 1 262 313 76 PHE H H 7.164 0.01 1 263 313 76 PHE CA C 54.918 0.2 1 264 313 76 PHE CB C 38.543 0.2 1 265 313 76 PHE N N 117.075 0.1 1 266 314 77 PHE H H 9.439 0.01 1 267 314 77 PHE CA C 55.417 0.2 1 268 314 77 PHE CB C 39.220 0.2 1 269 314 77 PHE N N 119.333 0.1 1 270 315 78 LEU H H 8.081 0.01 1 271 315 78 LEU CA C 57.295 0.2 1 272 315 78 LEU CB C 42.650 0.2 1 273 315 78 LEU N N 125.336 0.1 1 274 316 79 THR H H 8.121 0.01 1 275 316 79 THR N N 105.934 0.1 1 276 317 80 PRO CA C 62.305 0.2 1 277 317 80 PRO CB C 32.934 0.2 1 278 318 81 ASP H H 8.563 0.01 1 279 318 81 ASP CA C 53.736 0.2 1 280 318 81 ASP CB C 42.295 0.2 1 281 318 81 ASP N N 121.813 0.1 1 282 319 82 SER H H 7.348 0.01 1 283 319 82 SER N N 110.437 0.1 1 284 320 83 PHE CA C 62.199 0.2 1 285 320 83 PHE CB C 39.759 0.2 1 286 321 84 GLU H H 9.066 0.01 1 287 321 84 GLU CA C 60.739 0.2 1 288 321 84 GLU CB C 29.072 0.2 1 289 321 84 GLU N N 116.875 0.1 1 290 322 85 GLN H H 7.476 0.01 1 291 322 85 GLN CA C 59.145 0.2 1 292 322 85 GLN CB C 29.029 0.2 1 293 322 85 GLN N N 117.635 0.1 1 294 323 86 LYS H H 7.406 0.01 1 295 323 86 LYS N N 119.240 0.1 1 296 324 87 VAL CA C 66.859 0.2 1 297 324 87 VAL CB C 31.271 0.2 1 298 325 88 LEU H H 8.065 0.01 1 299 325 88 LEU CA C 58.677 0.2 1 300 325 88 LEU CB C 40.834 0.2 1 301 325 88 LEU N N 122.425 0.1 1 302 326 89 ASN H H 8.182 0.01 1 303 326 89 ASN CA C 55.975 0.2 1 304 326 89 ASN CB C 38.625 0.2 1 305 326 89 ASN N N 120.620 0.1 1 306 327 90 VAL H H 8.223 0.01 1 307 327 90 VAL CA C 67.400 0.2 1 308 327 90 VAL CB C 31.304 0.2 1 309 327 90 VAL N N 119.359 0.1 1 310 328 91 SER H H 8.790 0.01 1 311 328 91 SER CA C 62.756 0.2 1 312 328 91 SER N N 114.469 0.1 1 313 329 92 PHE H H 8.531 0.01 1 314 329 92 PHE CA C 59.739 0.2 1 315 329 92 PHE CB C 38.715 0.2 1 316 329 92 PHE N N 124.027 0.1 1 317 330 93 ALA H H 8.518 0.01 1 318 330 93 ALA CA C 55.865 0.2 1 319 330 93 ALA CB C 17.413 0.2 1 320 330 93 ALA N N 121.686 0.1 1 321 331 94 PHE H H 8.886 0.01 1 322 331 94 PHE CA C 57.670 0.2 1 323 331 94 PHE CB C 36.609 0.2 1 324 331 94 PHE N N 117.374 0.1 1 325 332 95 GLU H H 8.241 0.01 1 326 332 95 GLU CA C 60.170 0.2 1 327 332 95 GLU CB C 29.041 0.2 1 328 332 95 GLU N N 124.349 0.1 1 329 333 96 LEU H H 8.269 0.01 1 330 333 96 LEU CA C 57.711 0.2 1 331 333 96 LEU CB C 41.001 0.2 1 332 333 96 LEU N N 119.889 0.1 1 333 334 97 MET H H 8.403 0.01 1 334 334 97 MET CA C 59.842 0.2 1 335 334 97 MET CB C 31.771 0.2 1 336 334 97 MET N N 118.448 0.1 1 337 335 98 GLN H H 7.776 0.01 1 338 335 98 GLN CA C 58.366 0.2 1 339 335 98 GLN CB C 29.943 0.2 1 340 335 98 GLN N N 120.033 0.1 1 341 336 99 ASP H H 8.707 0.01 1 342 336 99 ASP CA C 57.244 0.2 1 343 336 99 ASP CB C 40.324 0.2 1 344 336 99 ASP N N 123.963 0.1 1 345 337 100 GLY H H 7.676 0.01 1 346 337 100 GLY CA C 45.380 0.2 1 347 337 100 GLY N N 105.201 0.1 1 348 338 101 GLY H H 7.764 0.01 1 349 338 101 GLY CA C 44.825 0.2 1 350 338 101 GLY N N 106.027 0.1 1 351 339 102 LEU H H 7.713 0.01 1 352 339 102 LEU CA C 55.199 0.2 1 353 339 102 LEU CB C 41.991 0.2 1 354 339 102 LEU N N 122.482 0.1 1 355 340 103 GLU H H 8.101 0.01 1 356 340 103 GLU CA C 56.234 0.2 1 357 340 103 GLU CB C 30.117 0.2 1 358 340 103 GLU N N 120.471 0.1 1 359 341 104 LYS H H 8.292 0.01 1 360 341 104 LYS N N 123.692 0.1 1 361 342 105 PRO CA C 62.843 0.2 1 362 342 105 PRO CB C 32.363 0.2 1 363 343 106 LYS H H 8.763 0.01 1 364 343 106 LYS N N 122.647 0.1 1 365 344 107 PRO CA C 63.251 0.2 1 366 344 107 PRO CB C 31.495 0.2 1 367 345 108 ARG H H 8.527 0.01 1 368 345 108 ARG N N 120.130 0.1 1 369 346 109 PRO CA C 65.759 0.2 1 370 346 109 PRO CB C 32.158 0.2 1 371 347 110 GLU H H 10.211 0.01 1 372 347 110 GLU CA C 60.885 0.2 1 373 347 110 GLU CB C 29.094 0.2 1 374 347 110 GLU N N 115.845 0.1 1 375 348 111 ASP H H 7.785 0.01 1 376 348 111 ASP CA C 57.857 0.2 1 377 348 111 ASP CB C 40.702 0.2 1 378 348 111 ASP N N 118.359 0.1 1 379 349 112 ILE H H 7.125 0.01 1 380 349 112 ILE CA C 61.726 0.2 1 381 349 112 ILE CB C 35.884 0.2 1 382 349 112 ILE N N 117.638 0.1 1 383 350 113 VAL H H 7.471 0.01 1 384 350 113 VAL CA C 64.869 0.2 1 385 350 113 VAL CB C 31.312 0.2 1 386 350 113 VAL N N 123.789 0.1 1 387 351 114 ASN H H 8.196 0.01 1 388 351 114 ASN CA C 53.032 0.2 1 389 351 114 ASN CB C 37.949 0.2 1 390 351 114 ASN N N 113.945 0.1 1 391 352 115 CYS H H 8.132 0.01 1 392 352 115 CYS CA C 59.820 0.2 1 393 352 115 CYS CB C 24.762 0.2 1 394 352 115 CYS N N 113.472 0.1 1 395 353 116 ASP H H 8.183 0.01 1 396 353 116 ASP CA C 55.134 0.2 1 397 353 116 ASP CB C 42.158 0.2 1 398 353 116 ASP N N 118.137 0.1 1 399 354 117 LEU H H 9.117 0.01 1 400 354 117 LEU CA C 58.902 0.2 1 401 354 117 LEU CB C 41.764 0.2 1 402 354 117 LEU N N 135.411 0.1 1 403 355 118 LYS H H 8.746 0.01 1 404 355 118 LYS CA C 61.279 0.2 1 405 355 118 LYS CB C 31.528 0.2 1 406 355 118 LYS N N 119.152 0.1 1 407 356 119 SER H H 7.924 0.01 1 408 356 119 SER CB C 62.965 0.2 1 409 356 119 SER N N 114.326 0.1 1 410 357 120 THR H H 7.985 0.01 1 411 357 120 THR CA C 67.666 0.2 1 412 357 120 THR CB C 68.718 0.2 1 413 357 120 THR N N 119.118 0.1 1 414 358 121 LEU H H 8.820 0.01 1 415 358 121 LEU CA C 58.081 0.2 1 416 358 121 LEU CB C 41.478 0.2 1 417 358 121 LEU N N 118.777 0.1 1 418 359 122 ARG H H 8.062 0.01 1 419 359 122 ARG CA C 59.776 0.2 1 420 359 122 ARG CB C 30.351 0.2 1 421 359 122 ARG N N 119.224 0.1 1 422 360 123 VAL H H 7.489 0.01 1 423 360 123 VAL CA C 65.906 0.2 1 424 360 123 VAL CB C 31.780 0.2 1 425 360 123 VAL N N 116.378 0.1 1 426 361 124 LEU H H 7.952 0.01 1 427 361 124 LEU CA C 57.700 0.2 1 428 361 124 LEU CB C 43.247 0.2 1 429 361 124 LEU N N 118.354 0.1 1 430 362 125 TYR H H 9.322 0.01 1 431 362 125 TYR CA C 62.221 0.2 1 432 362 125 TYR CB C 38.920 0.2 1 433 362 125 TYR N N 121.716 0.1 1 434 363 126 ASN H H 8.057 0.01 1 435 363 126 ASN CA C 55.569 0.2 1 436 363 126 ASN CB C 37.524 0.2 1 437 363 126 ASN N N 118.124 0.1 1 438 364 127 LEU H H 7.452 0.01 1 439 364 127 LEU CA C 57.865 0.2 1 440 364 127 LEU CB C 42.188 0.2 1 441 364 127 LEU N N 118.672 0.1 1 442 365 128 PHE H H 8.370 0.01 1 443 365 128 PHE CA C 60.251 0.2 1 444 365 128 PHE CB C 39.218 0.2 1 445 365 128 PHE N N 121.957 0.1 1 446 366 129 THR H H 8.091 0.01 1 447 366 129 THR CA C 65.735 0.2 1 448 366 129 THR CB C 68.535 0.2 1 449 366 129 THR N N 109.615 0.1 1 450 367 130 LYS H H 6.910 0.01 1 451 367 130 LYS CA C 58.366 0.2 1 452 367 130 LYS CB C 33.210 0.2 1 453 367 130 LYS N N 119.705 0.1 1 454 368 131 TYR H H 8.281 0.01 1 455 368 131 TYR CA C 58.867 0.2 1 456 368 131 TYR CB C 38.628 0.2 1 457 368 131 TYR N N 114.640 0.1 1 458 369 132 ARG H H 7.416 0.01 1 459 369 132 ARG CA C 59.128 0.2 1 460 369 132 ARG CB C 29.469 0.2 1 461 369 132 ARG N N 121.066 0.1 1 462 370 133 ASN H H 8.500 0.01 1 463 370 133 ASN CA C 53.154 0.2 1 464 370 133 ASN CB C 38.862 0.2 1 465 370 133 ASN N N 115.321 0.1 1 466 371 134 VAL H H 7.736 0.01 1 467 371 134 VAL CA C 63.855 0.2 1 468 371 134 VAL CB C 32.273 0.2 1 469 371 134 VAL N N 121.535 0.1 1 470 372 135 GLU H H 8.383 0.01 1 471 372 135 GLU N N 132.640 0.1 1 stop_ save_