data_15192 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment ; _BMRB_accession_number 15192 _BMRB_flat_file_name bmr15192.str _Entry_type original _Submission_date 2007-03-20 _Accession_date 2007-03-20 _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 Burton Robert A. . 2 Tsurupa Galina . . 3 Roy Hantgan . . 4 Nico Tjandra . . 5 Leonid Medved . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 175 "13C chemical shifts" 148 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-26 update BMRB 'update entity name' 2008-07-17 update BMRB 'complete entry citation' 2007-09-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17590019 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burton Robert A. . 2 Tsurupa Galina . . 3 Hantgan Roy R. . 4 Tjandra Nico . . 5 Medved Leonid . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 46 _Journal_issue 29 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8550 _Page_last 8560 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'alphaC-Domain Fragment' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $entity_1 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'subunit 1' _Molecular_mass 8975.755 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; MIDNEKVTSGHTTTTRRSCS KVITKTVTNADGRTETTKEV VKSEDGSDCGDADFDWHHTF PSRGNLDDFFHRDKDDFFT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 405 MET 2 406 ILE 3 407 ASP 4 408 ASN 5 409 GLU 6 410 LYS 7 411 VAL 8 412 THR 9 413 SER 10 414 GLY 11 415 HIS 12 416 THR 13 417 THR 14 418 THR 15 419 THR 16 420 ARG 17 421 ARG 18 422 SER 19 423 CYS 20 424 SER 21 425 LYS 22 426 VAL 23 427 ILE 24 428 THR 25 429 LYS 26 430 THR 27 431 VAL 28 432 THR 29 433 ASN 30 434 ALA 31 435 ASP 32 436 GLY 33 437 ARG 34 438 THR 35 439 GLU 36 440 THR 37 441 THR 38 442 LYS 39 443 GLU 40 444 VAL 41 445 VAL 42 446 LYS 43 447 SER 44 448 GLU 45 449 ASP 46 450 GLY 47 451 SER 48 452 ASP 49 453 CYS 50 454 GLY 51 455 ASP 52 456 ALA 53 457 ASP 54 458 PHE 55 459 ASP 56 460 TRP 57 461 HIS 58 462 HIS 59 463 THR 60 464 PHE 61 465 PRO 62 466 SER 63 467 ARG 64 468 GLY 65 469 ASN 66 470 LEU 67 471 ASP 68 472 ASP 69 473 PHE 70 474 PHE 71 475 HIS 72 476 ARG 73 477 ASP 74 478 LYS 75 479 ASP 76 480 ASP 77 481 PHE 78 482 PHE 79 483 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-06 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 2BAF "Bovine Fibrinogen Alpha-C Domain" 100.00 166 98.73 100.00 4.76e-48 PDB 2JOR "Nmr Solution Structure, Stability, And Interaction Of The Recombinant Bovine Fibrinogen Alphac-Domain Fragment" 100.00 79 100.00 100.00 6.08e-48 GB AAC67562 "fibrinogen A-alpha chain [Bos taurus]" 100.00 391 98.73 100.00 1.17e-46 GB AAI02565 "Fibrinogen alpha chain [Bos taurus]" 100.00 615 98.73 100.00 2.61e-45 GB AAI42073 "Fibrinogen alpha chain [Bos taurus]" 100.00 615 98.73 100.00 2.69e-45 REF NP_001028798 "fibrinogen alpha chain precursor [Bos taurus]" 100.00 615 98.73 100.00 2.61e-45 REF XP_005217494 "PREDICTED: fibrinogen alpha chain isoform X1 [Bos taurus]" 100.00 837 98.73 100.00 1.13e-44 SP P02672 "RecName: Full=Fibrinogen alpha chain; Contains: RecName: Full=Fibrinopeptide A; Contains: RecName: Full=Fibrinogen alpha chain;" 100.00 615 98.73 100.00 2.61e-45 TPG DAA20930 "TPA: fibrinogen, alpha polypeptide precursor [Bos taurus]" 100.00 615 98.73 100.00 2.69e-45 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 . 9913 Eukaryota Metazoa Bos taurus 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 $entity_1 'recombinant technology' . Escherichia coli . 'B834(DE3) pLysS' 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 $entity_1 150 uM '[U-99% 13C; U-99% 15N]' KPO4 10 mM 'natural abundance' NaCl 150 mM 'natural abundance' D20 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _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' 150 . mM pH 6.0 . pH pressure 1 . atm temperature 282 . 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 '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' 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 '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 1 405 1 MET HA H 4.945 0.003 1 2 405 1 MET CA C 55.881 0.000 1 3 405 1 MET CB C 33.352 0.000 1 4 406 2 ILE H H 8.234 0.009 1 5 406 2 ILE HA H 4.185 0.008 1 6 408 2 ILE HB H 1.763 0.000 1 7 406 2 ILE CA C 60.800 0.134 1 8 406 2 ILE CB C 38.511 0.115 1 9 406 2 ILE N N 120.860 0.021 1 10 407 3 ASP H H 8.581 0.006 1 11 407 3 ASP HA H 4.572 0.004 1 12 407 3 ASP HB2 H 2.561 0.021 2 13 407 3 ASP HB3 H 2.693 0.016 2 14 407 3 ASP CA C 54.026 0.076 1 15 407 3 ASP CB C 40.817 0.022 1 16 407 3 ASP N N 124.537 0.014 1 17 408 4 ASN HB2 H 2.756 0.008 2 18 408 4 ASN HB3 H 2.756 0.008 2 19 408 4 ASN H H 8.562 0.005 1 20 408 4 ASN HA H 4.611 0.021 1 21 408 4 ASN CA C 53.354 0.053 1 22 408 4 ASN CB C 38.534 0.004 1 23 408 4 ASN N N 119.475 0.021 1 24 409 5 GLU H H 8.461 0.005 1 25 409 5 GLU HA H 4.181 0.000 1 26 409 5 GLU HB2 H 1.986 0.011 2 27 409 5 GLU HB3 H 1.986 0.011 2 28 409 5 GLU CA C 56.668 0.000 1 29 409 5 GLU CB C 29.764 0.068 1 30 409 5 GLU N N 120.293 0.017 1 31 410 6 LYS H H 8.271 0.016 1 32 410 6 LYS HA H 4.279 0.007 1 33 410 6 LYS HB2 H 1.770 0.020 2 34 410 6 LYS HB3 H 1.770 0.020 2 35 410 6 LYS CA C 56.186 0.052 1 36 410 6 LYS CB C 32.505 0.061 1 37 410 6 LYS N N 121.478 0.041 1 38 411 7 VAL H H 8.236 0.005 1 39 411 7 VAL HA H 4.150 0.023 1 40 411 7 VAL HB H 2.092 0.091 1 41 411 7 VAL HG1 H 0.934 0.000 1 42 411 7 VAL HG2 H 0.934 0.000 1 43 411 7 VAL CA C 62.207 0.018 1 44 411 7 VAL CB C 32.447 0.029 1 45 411 7 VAL N N 121.345 0.021 1 46 412 8 THR H H 8.395 0.009 1 47 412 8 THR HA H 4.373 0.000 1 48 412 8 THR HB H 4.219 0.000 1 49 412 8 THR CA C 61.457 0.024 1 50 412 8 THR CB C 69.562 0.061 1 51 412 8 THR N N 117.638 0.020 1 52 413 9 SER H H 8.414 0.005 1 53 413 9 SER HA H 4.426 0.007 1 54 413 9 SER HB2 H 3.840 0.000 2 55 413 9 SER HB3 H 3.840 0.000 2 56 413 9 SER CA C 58.232 0.053 1 57 413 9 SER CB C 63.483 0.045 1 58 413 9 SER N N 117.795 0.020 1 59 414 10 GLY H H 8.502 0.005 1 60 414 10 GLY HA2 H 3.916 0.006 1 61 414 10 GLY HA3 H 3.916 0.006 1 62 414 10 GLY CA C 45.012 0.095 1 63 414 10 GLY N N 110.198 0.028 1 64 415 11 HIS H H 8.365 0.007 1 65 415 11 HIS HA H 4.748 0.000 1 66 415 11 HIS HB2 H 3.136 0.000 2 67 415 11 HIS HB3 H 3.136 0.000 2 68 415 11 HIS CA C 55.401 0.113 1 69 415 11 HIS CB C 29.609 0.110 1 70 415 11 HIS N N 118.264 0.008 1 71 416 12 THR H H 8.368 0.007 1 72 416 12 THR HA H 4.417 0.000 1 73 416 12 THR HB H 4.190 0.000 1 74 416 12 THR CA C 61.640 0.076 1 75 416 12 THR CB C 69.590 0.044 1 76 416 12 THR N N 115.786 0.011 1 77 417 13 THR H H 8.441 0.006 1 78 417 13 THR HA H 4.443 0.000 1 79 417 13 THR HB H 4.222 0.000 1 80 417 13 THR CA C 61.623 0.079 1 81 417 13 THR CB C 69.560 0.079 1 82 417 13 THR N N 116.596 0.012 1 83 418 14 THR H H 8.371 0.008 1 84 418 14 THR HA H 4.421 0.000 1 85 418 14 THR HB H 4.190 0.000 1 86 418 14 THR CA C 61.550 0.123 1 87 418 14 THR CB C 69.562 0.050 1 88 418 14 THR N N 116.644 0.016 1 89 419 15 THR H H 8.310 0.012 1 90 419 15 THR CA C 60.868 0.717 1 91 419 15 THR CB C 70.190 0.743 1 92 419 15 THR N N 117.203 0.014 1 93 420 16 ARG H H 8.471 0.016 1 94 420 16 ARG CA C 54.758 0.039 1 95 420 16 ARG CB C 34.511 0.024 1 96 420 16 ARG N N 121.510 0.041 1 97 421 17 ARG H H 8.774 0.012 1 98 421 17 ARG HA H 4.353 0.000 1 99 421 17 ARG CA C 55.271 0.443 1 100 421 17 ARG CB C 31.722 0.685 1 101 421 17 ARG N N 122.840 0.031 1 102 422 18 SER H H 8.470 0.005 1 103 422 18 SER CA C 57.608 0.172 1 104 422 18 SER CB C 63.890 0.006 1 105 422 18 SER N N 116.363 0.046 1 106 423 19 CYS H H 8.705 0.006 1 107 423 19 CYS CA C 55.119 0.000 1 108 423 19 CYS CB C 42.245 0.000 1 109 423 19 CYS N N 119.901 0.007 1 110 424 20 SER H H 8.555 0.010 1 111 424 20 SER CA C 57.674 0.000 1 112 424 20 SER CB C 64.823 0.029 1 113 424 20 SER N N 116.931 0.024 1 114 425 21 LYS H H 8.775 0.005 1 115 425 21 LYS HA H 4.111 0.000 1 116 425 21 LYS HB2 H 2.102 0.000 2 117 425 21 LYS HB3 H 2.102 0.000 2 118 425 21 LYS CA C 54.808 0.029 1 119 425 21 LYS CB C 33.841 0.924 1 120 425 21 LYS N N 121.844 0.028 1 121 426 22 VAL H H 8.638 0.023 1 122 426 22 VAL CA C 61.606 0.157 1 123 426 22 VAL CB C 32.582 0.259 1 124 426 22 VAL N N 123.384 0.072 1 125 427 23 ILE H H 9.126 0.005 1 126 427 23 ILE CA C 59.497 0.000 1 127 427 23 ILE CB C 39.575 0.255 1 128 427 23 ILE N N 126.709 0.023 1 129 428 24 THR H H 8.605 0.017 1 130 428 24 THR CA C 61.268 0.022 1 131 428 24 THR CB C 69.645 0.045 1 132 428 24 THR N N 120.178 0.038 1 133 429 25 LYS H H 8.885 0.010 1 134 429 25 LYS HA H 4.636 0.000 1 135 429 25 LYS HB2 H 1.674 0.000 2 136 429 25 LYS HB3 H 1.674 0.000 2 137 429 25 LYS CA C 54.901 0.078 1 138 429 25 LYS CB C 34.743 0.103 1 139 429 25 LYS N N 126.239 0.041 1 140 430 26 THR H H 8.656 0.008 1 141 430 26 THR HA H 4.929 0.000 1 142 430 26 THR CA C 61.518 0.094 1 143 430 26 THR CB C 70.030 0.038 1 144 430 26 THR N N 119.118 0.031 1 145 431 27 VAL H H 8.808 0.005 1 146 431 27 VAL HA H 4.442 0.000 1 147 431 27 VAL CA C 60.278 0.105 1 148 431 27 VAL CB C 34.702 0.002 1 149 431 27 VAL N N 123.821 0.033 1 150 432 28 THR H H 8.635 0.011 1 151 432 28 THR HA H 4.691 0.000 1 152 432 28 THR CA C 61.543 0.143 1 153 432 28 THR CB C 69.286 0.084 1 154 432 28 THR N N 120.131 0.016 1 155 433 29 ASN H H 8.804 0.010 1 156 433 29 ASN HA H 4.719 0.000 1 157 433 29 ASN CA C 51.913 0.084 1 158 433 29 ASN CB C 39.154 0.084 1 159 433 29 ASN N N 124.867 0.030 1 160 434 30 ALA H H 8.720 0.011 1 161 434 30 ALA HA H 4.107 0.000 1 162 434 30 ALA HB H 1.407 0.000 1 163 434 30 ALA CA C 54.294 0.034 1 164 434 30 ALA CB C 18.227 0.201 1 165 434 30 ALA N N 122.891 0.027 1 166 435 31 ASP H H 7.978 0.009 1 167 435 31 ASP HA H 4.551 0.000 1 168 435 31 ASP HB2 H 2.728 0.000 2 169 435 31 ASP HB3 H 2.728 0.000 2 170 435 31 ASP CA C 53.636 0.064 1 171 435 31 ASP CB C 40.394 0.017 1 172 435 31 ASP N N 115.257 0.034 1 173 436 32 GLY H H 8.236 0.004 1 174 436 32 GLY HA2 H 4.172 0.000 1 175 436 32 GLY HA3 H 3.559 0.000 1 176 436 32 GLY CA C 45.012 0.070 1 177 436 32 GLY N N 107.783 0.031 1 178 437 33 ARG H H 7.984 0.007 1 179 437 33 ARG HA H 4.463 0.000 1 180 437 33 ARG HB2 H 1.768 0.000 2 181 437 33 ARG HB3 H 1.768 0.000 2 182 437 33 ARG CA C 55.581 0.057 1 183 437 33 ARG CB C 30.763 0.052 1 184 437 33 ARG N N 120.973 0.024 1 185 438 34 THR H H 8.639 0.012 1 186 438 34 THR HA H 4.318 0.000 1 187 438 34 THR CA C 61.541 0.216 1 188 438 34 THR CB C 69.806 0.164 1 189 438 34 THR N N 117.617 0.025 1 190 439 35 GLU H H 8.562 0.152 1 191 439 35 GLU CA C 55.396 0.272 1 192 439 35 GLU CB C 31.587 0.929 1 193 439 35 GLU N N 124.134 0.038 1 194 440 36 THR H H 8.787 0.008 1 195 440 36 THR CA C 61.329 0.000 1 196 440 36 THR CB C 70.284 0.087 1 197 440 36 THR N N 119.267 0.023 1 198 441 37 THR H H 9.022 0.031 1 199 441 37 THR CA C 60.734 0.707 1 200 441 37 THR CB C 70.365 0.286 1 201 441 37 THR N N 118.907 0.025 1 202 442 38 LYS H H 8.965 0.006 1 203 442 38 LYS CA C 55.024 0.000 1 204 442 38 LYS CB C 32.426 0.000 1 205 442 38 LYS N N 124.587 0.021 1 206 443 39 GLU CA C 58.333 0.000 1 207 444 40 VAL H H 8.648 0.000 1 208 444 40 VAL CA C 61.786 0.000 1 209 444 40 VAL CB C 32.093 0.000 1 210 444 40 VAL N N 123.046 0.027 1 211 445 41 VAL H H 8.963 0.011 1 212 445 41 VAL HB H 1.958 0.000 1 213 445 41 VAL CA C 60.449 0.000 1 214 445 41 VAL CB C 34.168 0.000 1 215 445 41 VAL N N 125.687 0.046 1 216 446 42 LYS H H 8.639 0.013 1 217 446 42 LYS CA C 55.750 0.149 1 218 446 42 LYS CB C 33.255 0.036 1 219 446 42 LYS N N 124.860 0.049 1 220 447 43 SER H H 8.544 0.053 1 221 447 43 SER HA H 4.603 0.000 1 222 447 43 SER CA C 57.311 0.047 1 223 447 43 SER CB C 63.798 0.071 1 224 447 43 SER N N 118.006 0.029 1 225 448 44 GLU H H 8.957 0.008 1 226 448 44 GLU HA H 4.298 0.000 1 227 448 44 GLU CA C 56.966 0.017 1 228 448 44 GLU CB C 29.700 0.100 1 229 448 44 GLU N N 124.279 0.048 1 230 449 45 ASP H H 8.243 0.011 1 231 449 45 ASP HA H 4.613 0.000 1 232 449 45 ASP CA C 53.458 0.133 1 233 449 45 ASP CB C 40.900 0.042 1 234 449 45 ASP N N 118.407 0.041 1 235 450 46 GLY H H 8.352 0.006 1 236 450 46 GLY CA C 45.591 0.074 1 237 450 46 GLY N N 109.271 0.019 1 238 451 47 SER H H 8.280 0.009 1 239 451 47 SER CA C 58.926 0.143 1 240 451 47 SER CB C 63.475 0.120 1 241 451 47 SER N N 115.671 0.018 1 242 452 48 ASP H H 8.448 0.008 1 243 452 48 ASP HA H 4.528 0.000 1 244 452 48 ASP HB2 H 2.523 0.000 2 245 452 48 ASP HB3 H 2.523 0.000 2 246 452 48 ASP CA C 54.120 0.123 1 247 452 48 ASP CB C 40.701 0.193 1 248 452 48 ASP N N 120.893 0.017 1 249 453 49 CYS H H 7.991 0.007 1 250 453 49 CYS CA C 56.481 1.289 1 251 453 49 CYS CB C 40.332 0.867 1 252 453 49 CYS N N 120.029 0.029 1 253 454 50 GLY H H 8.687 0.007 1 254 454 50 GLY HA2 H 4.203 0.000 1 255 454 50 GLY HA3 H 3.946 0.000 1 256 454 50 GLY CA C 45.156 0.017 1 257 454 50 GLY N N 109.960 0.021 1 258 455 51 ASP H H 8.363 0.008 1 259 455 51 ASP CA C 54.198 0.112 1 260 455 51 ASP CB C 41.038 0.041 1 261 455 51 ASP N N 120.210 0.037 1 262 456 52 ALA H H 8.407 0.011 1 263 456 52 ALA CA C 52.630 0.079 1 264 456 52 ALA CB C 18.977 0.028 1 265 456 52 ALA N N 123.461 0.012 1 266 457 53 ASP H H 8.265 0.007 1 267 457 53 ASP CA C 54.018 0.048 1 268 457 53 ASP CB C 40.778 0.061 1 269 457 53 ASP N N 118.078 0.019 1 270 458 54 PHE H H 8.253 0.009 1 271 458 54 PHE HA H 4.147 0.000 1 272 458 54 PHE CA C 57.648 3.163 1 273 458 54 PHE CB C 39.753 1.134 1 274 458 54 PHE N N 117.913 0.027 1 275 459 55 ASP H H 8.510 0.007 1 276 459 55 ASP CA C 53.849 0.131 1 277 459 55 ASP CB C 40.702 0.001 1 278 459 55 ASP N N 124.143 0.038 1 279 460 56 TRP H H 8.023 0.008 1 280 460 56 TRP HA H 4.524 0.000 1 281 460 56 TRP HB2 H 3.164 0.000 2 282 460 56 TRP HB3 H 3.164 0.000 2 283 460 56 TRP CA C 56.446 0.933 1 284 460 56 TRP CB C 28.544 0.435 1 285 460 56 TRP N N 121.854 0.040 1 286 461 57 HIS H H 8.272 0.010 1 287 461 57 HIS HA H 4.341 0.000 1 288 461 57 HIS CA C 55.680 0.080 1 289 461 57 HIS CB C 30.733 0.011 1 290 461 57 HIS N N 122.303 0.032 1 291 462 58 HIS H H 8.572 0.007 1 292 462 58 HIS HA H 4.487 0.000 1 293 462 58 HIS HB2 H 3.102 0.000 2 294 462 58 HIS HB3 H 3.102 0.000 2 295 462 58 HIS CA C 55.683 0.046 1 296 462 58 HIS CB C 30.053 0.734 1 297 462 58 HIS N N 123.102 0.039 1 298 463 59 THR H H 8.040 0.007 1 299 463 59 THR HA H 4.255 0.000 1 300 463 59 THR CA C 61.735 0.042 1 301 463 59 THR CB C 69.608 0.056 1 302 463 59 THR N N 114.699 0.019 1 303 464 60 PHE H H 8.385 0.007 1 304 464 60 PHE CA C 55.240 0.000 1 305 464 60 PHE CB C 38.845 0.000 1 306 464 60 PHE N N 122.533 0.031 1 307 465 61 PRO CA C 63.042 0.000 1 308 465 61 PRO CB C 31.754 0.000 1 309 466 62 SER H H 8.487 0.007 1 310 466 62 SER HA H 4.399 0.000 1 311 466 62 SER HB2 H 3.831 0.000 2 312 466 62 SER HB3 H 3.831 0.000 2 313 466 62 SER CA C 58.177 0.056 1 314 466 62 SER CB C 63.496 0.001 1 315 466 62 SER N N 115.652 0.021 1 316 467 63 ARG H H 8.528 0.007 1 317 467 63 ARG HA H 4.341 0.000 1 318 467 63 ARG HB2 H 1.734 0.000 2 319 467 63 ARG HB3 H 1.734 0.000 2 320 467 63 ARG CA C 56.063 0.026 1 321 467 63 ARG CB C 30.456 0.114 1 322 467 63 ARG N N 122.529 0.019 1 323 468 64 GLY H H 8.491 0.010 1 324 468 64 GLY HA2 H 3.886 0.000 1 325 468 64 GLY HA3 H 3.886 0.000 1 326 468 64 GLY CA C 45.055 0.067 1 327 468 64 GLY N N 109.081 0.011 1 328 469 65 ASN H H 8.445 0.006 1 329 469 65 ASN HA H 4.667 0.000 1 330 469 65 ASN HB2 H 2.737 0.000 2 331 469 65 ASN HB3 H 2.737 0.000 2 332 469 65 ASN CA C 52.998 0.042 1 333 469 65 ASN CB C 38.575 0.040 1 334 469 65 ASN N N 118.439 0.013 1 335 470 66 LEU H H 8.393 0.011 1 336 470 66 LEU HA H 4.225 0.000 1 337 470 66 LEU HB2 H 1.571 0.000 2 338 470 66 LEU HB3 H 1.571 0.000 2 339 470 66 LEU CA C 55.534 0.063 1 340 470 66 LEU CB C 41.648 0.045 1 341 470 66 LEU N N 121.704 0.023 1 342 471 67 ASP H H 8.266 0.011 1 343 471 67 ASP CA C 54.613 0.000 1 344 471 67 ASP CB C 40.748 0.000 1 345 471 67 ASP N N 119.217 0.028 1 346 472 68 ASP HA H 4.495 0.000 1 347 472 68 ASP HB2 H 2.471 0.000 2 348 472 68 ASP HB3 H 2.471 0.000 2 349 472 68 ASP CA C 54.358 0.000 1 350 472 68 ASP CB C 40.742 0.000 1 351 473 69 PHE H H 8.119 0.025 1 352 473 69 PHE CA C 58.370 0.018 1 353 473 69 PHE CB C 39.127 0.093 1 354 473 69 PHE N N 119.575 0.045 1 355 474 70 PHE H H 8.094 0.014 1 356 474 70 PHE CA C 57.870 0.012 1 357 474 70 PHE CB C 39.264 0.267 1 358 474 70 PHE N N 118.882 0.026 1 359 475 71 HIS H H 8.245 0.007 1 360 475 71 HIS CA C 55.636 2.148 1 361 475 71 HIS CB C 30.734 1.827 1 362 475 71 HIS N N 121.853 0.054 1 363 476 72 ARG H H 8.153 0.008 1 364 476 72 ARG CA C 55.935 0.168 1 365 476 72 ARG CB C 29.662 1.179 1 366 476 72 ARG N N 117.822 0.022 1 367 477 73 ASP H H 8.624 0.010 1 368 477 73 ASP CA C 54.209 0.000 1 369 477 73 ASP CB C 41.020 0.000 1 370 477 73 ASP N N 121.561 0.010 1 371 478 74 LYS H H 8.313 0.019 1 372 478 74 LYS N N 120.514 0.039 1 373 479 75 ASP H H 8.373 0.007 1 374 479 75 ASP N N 120.476 0.020 1 375 480 76 ASP HA H 4.512 0.000 1 376 480 76 ASP HB2 H 2.546 0.000 2 377 480 76 ASP HB3 H 2.546 0.000 2 378 480 76 ASP CA C 54.105 0.000 1 379 480 76 ASP CB C 40.809 0.000 1 380 481 77 PHE H H 8.092 0.022 1 381 481 77 PHE HA H 4.316 0.000 1 382 481 77 PHE HB2 H 2.878 0.000 2 383 481 77 PHE HB3 H 2.878 0.000 2 384 481 77 PHE CA C 57.616 0.103 1 385 481 77 PHE CB C 39.275 0.125 1 386 481 77 PHE N N 119.544 0.037 1 387 482 78 PHE H H 8.188 0.046 1 388 482 78 PHE HA H 4.641 0.000 1 389 482 78 PHE HB2 H 3.152 0.000 2 390 482 78 PHE HB3 H 2.932 0.000 2 391 482 78 PHE CA C 57.441 0.019 1 392 482 78 PHE CB C 39.373 0.088 1 393 482 78 PHE N N 120.306 0.764 1 394 483 79 THR H H 7.724 0.005 1 395 483 79 THR CA C 63.016 0.000 1 396 483 79 THR CB C 70.404 0.000 1 397 483 79 THR N N 120.060 0.013 1 stop_ save_