data_6893 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Bovine Fibrinogen alpha-C Domain ; _BMRB_accession_number 6893 _BMRB_flat_file_name bmr6893.str _Entry_type original _Submission_date 2005-11-10 _Accession_date 2005-11-29 _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 R. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 364 "13C chemical shifts" 328 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-20 original BMRB . stop_ _Original_release_date 2005-11-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification of an Ordered Compact Structure within the Recombinant Bovine Fibrinogen alphaC-Domain Fragment by NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16475814 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burton R. A. . 2 Tsurupa G. . . 3 Medved L. . . 4 Tjandra N. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2257 _Page_last 2266 _Year 2006 _Details . loop_ _Keyword Fibrinogen 'beta hairpin' stop_ save_ ################################## # Molecular system description # ################################## save_system_Fibrinogen_alpha _Saveframe_category molecular_system _Mol_system_name 'Fibrinogen alpha chain' _Abbreviation_common 'Fibrinogen alpha chain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Fibrinogen alpha chain' $Fibrinogen_alpha stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Fibrinogen_alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Fibrinogen alpha chain' _Abbreviation_common 'Fibrinogen alpha chain' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; MGTFREEGSVSSGTKQEFHT GKLVTTKGDKELLIDNEKVT SGHTTTTRRSCSKVITKTVT NADGRTETTKEVVKSEDGSD CGDADFDWHHTFPSRGNLDD FFHRDKDDFFTRSSHEFDGR TGLAPEFAALGESGSSSSKT STHSKQFVSSSTTVNRGGSA IESKHF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 373 MET 2 374 GLY 3 375 THR 4 376 PHE 5 377 ARG 6 378 GLU 7 379 GLU 8 380 GLY 9 381 SER 10 382 VAL 11 383 SER 12 384 SER 13 385 GLY 14 386 THR 15 387 LYS 16 388 GLN 17 389 GLU 18 390 PHE 19 391 HIS 20 392 THR 21 393 GLY 22 394 LYS 23 395 LEU 24 396 VAL 25 397 THR 26 398 THR 27 399 LYS 28 400 GLY 29 401 ASP 30 402 LYS 31 403 GLU 32 404 LEU 33 405 LEU 34 406 ILE 35 407 ASP 36 408 ASN 37 409 GLU 38 410 LYS 39 411 VAL 40 412 THR 41 413 SER 42 414 GLY 43 415 HIS 44 416 THR 45 417 THR 46 418 THR 47 419 THR 48 420 ARG 49 421 ARG 50 422 SER 51 423 CYS 52 424 SER 53 425 LYS 54 426 VAL 55 427 ILE 56 428 THR 57 429 LYS 58 430 THR 59 431 VAL 60 432 THR 61 433 ASN 62 434 ALA 63 435 ASP 64 436 GLY 65 437 ARG 66 438 THR 67 439 GLU 68 440 THR 69 441 THR 70 442 LYS 71 443 GLU 72 444 VAL 73 445 VAL 74 446 LYS 75 447 SER 76 448 GLU 77 449 ASP 78 450 GLY 79 451 SER 80 452 ASP 81 453 CYS 82 454 GLY 83 455 ASP 84 456 ALA 85 457 ASP 86 458 PHE 87 459 ASP 88 460 TRP 89 461 HIS 90 462 HIS 91 463 THR 92 464 PHE 93 465 PRO 94 466 SER 95 467 ARG 96 468 GLY 97 469 ASN 98 470 LEU 99 471 ASP 100 472 ASP 101 473 PHE 102 474 PHE 103 475 HIS 104 476 ARG 105 477 ASP 106 478 LYS 107 479 ASP 108 480 ASP 109 481 PHE 110 482 PHE 111 483 THR 112 484 ARG 113 485 SER 114 486 SER 115 487 HIS 116 488 GLU 117 489 PHE 118 490 ASP 119 491 GLY 120 492 ARG 121 493 THR 122 494 GLY 123 495 LEU 124 496 ALA 125 497 PRO 126 498 GLU 127 499 PHE 128 500 ALA 129 501 ALA 130 502 LEU 131 503 GLY 132 504 GLU 133 505 SER 134 506 GLY 135 507 SER 136 508 SER 137 509 SER 138 510 SER 139 511 LYS 140 512 THR 141 513 SER 142 514 THR 143 515 HIS 144 516 SER 145 517 LYS 146 518 GLN 147 519 PHE 148 520 VAL 149 521 SER 150 522 SER 151 523 SER 152 524 THR 153 525 THR 154 526 VAL 155 527 ASN 156 528 ARG 157 529 GLY 158 530 GLY 159 531 SER 160 532 ALA 161 533 ILE 162 534 GLU 163 535 SER 164 536 LYS 165 537 HIS 166 538 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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' 100.00 166 100.00 100.00 7.35e-89 GenBank AAC67562 'fibrinogen A-alpha chain [Bos taurus]' 100.00 391 99.40 99.40 7.47e-90 GenBank AAI02565 'Fibrinogen alpha chain [Bos taurus]' 100.00 615 99.40 99.40 7.66e-90 GenBank AAI42073 'Fibrinogen alpha chain [Bos taurus]' 100.00 615 99.40 99.40 1.08e-89 REF NP_001028798 'fibrinogen, alpha polypeptide [Bos taurus]' 100.00 615 99.40 99.40 7.66e-90 SWISS-PROT P02672 'Fibrinogen alpha chain precursor [Contains: Fibrinopeptide A]' 100.00 615 99.40 99.40 7.66e-90 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Fibrinogen_alpha Cow 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 $Fibrinogen_alpha 'recombinant technology' . . . . . 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 $Fibrinogen_alpha 0.2 mM '[U-15N; U-13C]' 'phosphate buffer' 10 mM . NaCl 150 mM . H20 90 % . D20 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_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 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis TSP C 13 . ppm . . . . . . TSP H 1 . ppm . . . . . . TSP N 15 . ppm . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Fibrinogen alpha chain' _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 . 1 MET HB2 H 2.078 0.000 2 2 . 2 GLY CA C 45.288 0.033 1 3 . 2 GLY H H 8.276 0.004 1 4 . 2 GLY N N 113.990 0.014 1 5 . 3 THR CA C 61.737 0.067 1 6 . 3 THR CB C 69.660 0.054 1 7 . 3 THR H H 8.041 0.002 1 8 . 3 THR N N 113.724 0.010 1 9 . 4 PHE CA C 57.765 0.007 1 10 . 4 PHE CB C 39.331 0.029 1 11 . 4 PHE HA H 4.636 0.000 1 12 . 4 PHE HB2 H 3.100 0.000 2 13 . 4 PHE H H 8.322 0.002 1 14 . 4 PHE N N 122.426 0.014 1 15 . 5 ARG CA C 55.666 0.058 1 16 . 5 ARG CB C 30.829 0.161 1 17 . 5 ARG H H 8.080 0.012 1 18 . 5 ARG N N 123.107 0.186 1 19 . 6 GLU CA C 56.028 0.191 1 20 . 6 GLU CB C 30.636 0.464 1 21 . 6 GLU CG C 35.996 0.000 1 22 . 6 GLU HA H 4.243 0.000 1 23 . 6 GLU HB2 H 2.274 0.000 2 24 . 6 GLU HG2 H 2.274 0.000 2 25 . 6 GLU H H 8.449 0.002 1 26 . 6 GLU N N 122.908 0.010 1 27 . 7 GLU CA C 56.754 0.065 1 28 . 7 GLU CB C 30.178 0.006 1 29 . 7 GLU CG C 36.013 0.000 1 30 . 7 GLU HA H 4.274 0.000 1 31 . 7 GLU HB2 H 2.289 0.000 2 32 . 7 GLU HG2 H 2.294 0.000 2 33 . 7 GLU H H 8.561 0.008 1 34 . 7 GLU N N 122.497 0.008 1 35 . 8 GLY CA C 45.236 0.032 1 36 . 8 GLY HA2 H 4.012 0.000 2 37 . 8 GLY H H 8.472 0.005 1 38 . 8 GLY N N 109.797 0.056 1 39 . 9 SER CA C 58.145 0.006 1 40 . 9 SER CB C 63.769 0.010 1 41 . 9 SER HA H 4.510 0.000 1 42 . 9 SER HB2 H 3.886 0.000 2 43 . 9 SER H H 8.214 0.006 1 44 . 9 SER N N 115.298 0.010 1 45 . 10 VAL CA C 62.143 0.017 1 46 . 10 VAL CB C 32.716 0.018 1 47 . 10 VAL CG1 C 20.564 0.000 2 48 . 10 VAL HA H 4.218 0.000 1 49 . 10 VAL HB H 2.138 0.000 1 50 . 10 VAL HG2 H 0.990 0.000 1 51 . 10 VAL H H 8.199 0.002 1 52 . 10 VAL N N 121.204 0.012 1 53 . 11 SER CA C 58.117 0.022 1 54 . 11 SER CB C 63.584 0.020 1 55 . 11 SER HA H 4.520 0.000 1 56 . 11 SER HB2 H 3.896 0.000 2 57 . 11 SER H H 8.409 0.006 1 58 . 11 SER N N 118.906 0.012 1 59 . 12 SER CA C 58.510 0.021 1 60 . 12 SER CB C 63.547 0.035 1 61 . 12 SER HA H 4.465 0.000 1 62 . 12 SER HB2 H 3.911 0.000 2 63 . 12 SER H H 8.428 0.002 1 64 . 12 SER N N 117.592 0.019 1 65 . 13 GLY CA C 45.725 0.143 1 66 . 13 GLY HA2 H 3.883 0.000 2 67 . 13 GLY H H 8.411 0.006 1 68 . 13 GLY N N 110.283 0.099 1 69 . 14 THR CA C 61.694 0.000 1 70 . 14 THR CB C 69.671 0.000 1 71 . 14 THR H H 7.969 0.006 1 72 . 14 THR N N 112.529 0.008 1 73 . 17 GLU CA C 56.922 0.000 1 74 . 17 GLU CB C 29.678 0.000 1 75 . 17 GLU CG C 35.963 0.000 1 76 . 17 GLU HA H 4.133 0.000 1 77 . 17 GLU HB2 H 2.022 0.000 2 78 . 17 GLU HG2 H 2.108 0.000 2 79 . 18 PHE CA C 58.645 0.000 1 80 . 18 PHE CB C 39.020 0.000 1 81 . 18 PHE H H 8.017 0.007 1 82 . 18 PHE N N 119.550 0.073 1 83 . 19 HIS CA C 55.444 0.000 1 84 . 19 HIS CB C 30.001 0.000 1 85 . 19 HIS HA H 4.546 0.000 1 86 . 19 HIS HB2 H 3.151 0.000 2 87 . 20 THR CA C 61.932 0.050 1 88 . 20 THR CB C 69.519 0.030 1 89 . 20 THR CG2 C 21.593 0.000 2 90 . 20 THR HA H 4.339 0.000 1 91 . 20 THR HG2 H 1.212 0.000 1 92 . 20 THR H H 8.182 0.005 1 93 . 20 THR N N 114.909 0.021 1 94 . 21 GLY CA C 45.120 0.028 1 95 . 21 GLY HA2 H 3.981 0.000 2 96 . 21 GLY H H 8.351 0.005 1 97 . 21 GLY N N 110.728 0.090 1 98 . 22 LYS CA C 55.983 0.009 1 99 . 22 LYS CB C 33.183 0.042 1 100 . 22 LYS H H 8.118 0.004 1 101 . 22 LYS N N 120.592 0.018 1 102 . 23 LEU CA C 55.023 0.016 1 103 . 23 LEU CB C 42.218 0.005 1 104 . 23 LEU CD1 C 24.198 0.000 1 105 . 23 LEU CG C 26.952 0.000 1 106 . 23 LEU HA H 4.400 0.000 1 107 . 23 LEU HB2 H 1.584 0.000 2 108 . 23 LEU HD2 H 0.908 0.000 2 109 . 23 LEU H H 8.291 0.002 1 110 . 23 LEU N N 123.651 0.026 1 111 . 24 VAL CA C 62.027 0.021 1 112 . 24 VAL CB C 32.787 0.004 1 113 . 24 VAL CG1 C 20.945 0.000 2 114 . 24 VAL HB H 2.073 0.000 1 115 . 24 VAL H H 8.219 0.006 1 116 . 24 VAL N N 122.088 0.014 1 117 . 24 VAL HA H 4.400 0.000 1 118 . 24 VAL HG1 H 1.217 0.000 2 119 . 25 THR CA C 61.410 0.007 1 120 . 25 THR CB C 69.696 0.002 1 121 . 25 THR CG2 C 21.493 0.000 1 122 . 25 THR HA H 4.490 0.000 1 123 . 25 THR HG2 H 1.196 0.000 1 124 . 25 THR H H 8.293 0.006 1 125 . 25 THR N N 118.002 0.020 1 126 . 26 THR CA C 61.445 0.033 1 127 . 26 THR CB C 69.684 0.019 1 128 . 26 THR CG2 C 21.526 0.000 1 129 . 26 THR HA H 4.394 0.000 1 130 . 26 THR HB H 4.384 0.000 1 131 . 26 THR HG2 H 1.201 0.000 1 132 . 26 THR H H 8.203 0.004 1 133 . 26 THR N N 116.406 0.009 1 134 . 27 LYS CA C 56.439 0.000 1 135 . 27 LYS CB C 33.087 0.028 1 136 . 27 LYS CD C 28.861 0.000 1 137 . 27 LYS CE C 42.136 0.000 1 138 . 27 LYS CG C 24.497 0.000 1 139 . 27 LYS HA H 4.475 0.000 1 140 . 27 LYS HB2 H 1.811 0.000 2 141 . 27 LYS HD2 H 1.453 0.000 2 142 . 27 LYS HE2 H 2.994 0.000 2 143 . 27 LYS HG2 H 1.695 0.000 2 144 . 27 LYS H H 8.394 0.004 1 145 . 27 LYS N N 123.435 0.045 1 146 . 28 GLY CA C 45.159 0.025 1 147 . 28 GLY HA2 H 3.931 0.000 2 148 . 28 GLY H H 8.437 0.004 1 149 . 28 GLY N N 110.000 0.041 1 150 . 29 ASP CA C 53.161 0.000 1 151 . 29 ASP CB C 38.854 0.000 1 152 . 29 ASP H H 8.336 0.005 1 153 . 29 ASP N N 118.415 0.013 1 154 . 32 LEU CA C 55.644 0.000 1 155 . 32 LEU CB C 41.065 0.000 1 156 . 32 LEU CD1 C 24.248 0.000 1 157 . 32 LEU CG C 26.604 0.000 1 158 . 32 LEU HA H 4.265 0.000 1 159 . 32 LEU HB2 H 2.274 0.000 2 160 . 32 LEU HD2 H 0.880 0.000 2 161 . 32 LEU HG H 1.607 0.002 1 162 . 33 LEU CA C 54.880 0.016 1 163 . 33 LEU CB C 41.928 0.074 1 164 . 33 LEU CD1 C 23.999 0.000 1 165 . 33 LEU CG C 26.836 0.000 1 166 . 33 LEU HA H 4.405 0.000 1 167 . 33 LEU HB2 H 1.599 0.000 2 168 . 33 LEU HD2 H 0.923 0.000 2 169 . 33 LEU H H 8.190 0.009 1 170 . 33 LEU N N 119.307 0.017 1 171 . 34 ILE CA C 60.788 0.029 1 172 . 34 ILE CB C 38.802 0.004 1 173 . 34 ILE CD1 C 18.423 0.000 1 174 . 34 ILE CG1 C 26.969 0.000 1 175 . 34 ILE CG2 C 21.443 0.000 1 176 . 34 ILE HA H 4.364 0.000 1 177 . 34 ILE HB H 1.855 0.000 1 178 . 34 ILE HD1 H 0.919 0.000 1 179 . 34 ILE HG2 H 1.196 0.000 1 180 . 34 ILE H H 8.035 0.005 1 181 . 34 ILE N N 121.516 0.041 1 182 . 35 ASP CA C 54.196 0.000 1 183 . 35 ASP CB C 41.015 0.000 1 184 . 35 ASP H H 8.368 0.004 1 185 . 35 ASP N N 124.015 0.027 1 186 . 37 GLU CA C 56.822 0.000 1 187 . 37 GLU CB C 29.872 0.000 1 188 . 37 GLU CG C 36.029 0.000 1 189 . 37 GLU HA H 4.248 0.000 1 190 . 37 GLU HB2 H 2.224 0.000 2 191 . 37 GLU HG2 H 2.304 0.000 2 192 . 38 LYS CA C 56.349 0.007 1 193 . 38 LYS CB C 32.746 0.020 1 194 . 38 LYS CD C 28.778 0.000 1 195 . 38 LYS CE C 42.169 0.000 1 196 . 38 LYS CG C 24.812 0.000 1 197 . 38 LYS HA H 3.976 0.000 1 198 . 38 LYS HB2 H 1.811 0.000 2 199 . 38 LYS HD2 H 1.690 0.000 2 200 . 38 LYS HE2 H 3.000 0.000 2 201 . 38 LYS HG2 H 1.393 0.000 2 202 . 38 LYS H H 8.140 0.009 1 203 . 38 LYS N N 121.012 0.017 1 204 . 39 VAL CA C 62.410 0.020 1 205 . 39 VAL CB C 32.718 0.008 1 206 . 39 VAL CG1 C 20.846 0.000 1 207 . 39 VAL HA H 4.435 0.000 1 208 . 39 VAL HB H 2.108 0.000 1 209 . 39 VAL HG2 H 0.989 0.000 2 210 . 39 VAL H H 8.074 0.006 1 211 . 39 VAL N N 120.633 0.086 1 212 . 40 THR CA C 61.625 0.000 1 213 . 40 THR CB C 69.550 0.059 1 214 . 40 THR CG2 C 20.896 0.000 2 215 . 40 THR HA H 4.525 0.000 1 216 . 40 THR HB H 4.389 0.000 1 217 . 40 THR HG2 H 0.978 0.000 1 218 . 40 THR H H 8.238 0.003 1 219 . 40 THR N N 117.098 0.007 1 220 . 41 SER CA C 58.532 0.007 1 221 . 41 SER CB C 63.573 0.077 1 222 . 41 SER HA H 4.480 0.000 1 223 . 41 SER HB2 H 3.886 0.000 2 224 . 41 SER H H 8.285 0.007 1 225 . 41 SER N N 117.602 0.005 1 226 . 42 GLY CA C 45.236 0.063 1 227 . 42 GLY HA2 H 3.956 0.000 2 228 . 42 GLY H H 8.400 0.010 1 229 . 42 GLY N N 110.152 0.113 1 230 . 43 HIS CA C 55.537 0.007 1 231 . 43 HIS CB C 29.835 0.027 1 232 . 43 HIS HA H 4.510 0.000 1 233 . 43 HIS HB2 H 3.135 0.000 2 234 . 43 HIS H H 8.263 0.004 1 235 . 43 HIS N N 118.372 0.057 1 236 . 44 THR CA C 61.708 0.009 1 237 . 44 THR CB C 69.715 0.050 1 238 . 44 THR CG2 C 21.526 0.000 1 239 . 44 THR HA H 4.465 0.000 1 240 . 44 THR HG2 H 1.191 0.000 1 241 . 44 THR H H 8.231 0.006 1 242 . 44 THR N N 115.681 0.048 1 243 . 45 THR CA C 61.681 0.015 1 244 . 45 THR CB C 69.615 0.050 1 245 . 45 THR CG2 C 21.493 0.000 1 246 . 45 THR HA H 4.470 0.000 1 247 . 45 THR HG2 H 1.207 0.000 1 248 . 45 THR H H 8.310 0.005 1 249 . 45 THR N N 116.484 0.031 1 250 . 46 THR CA C 61.642 0.009 1 251 . 46 THR CB C 69.531 0.017 1 252 . 46 THR CG2 C 21.443 0.000 1 253 . 46 THR HA H 4.455 0.000 1 254 . 46 THR H H 8.249 0.011 1 255 . 46 THR N N 116.495 0.014 1 256 . 47 THR CA C 61.957 0.000 1 257 . 47 THR CB C 69.516 0.000 1 258 . 47 THR HG2 H 1.222 0.000 1 259 . 47 THR H H 8.123 0.007 1 260 . 47 THR N N 116.505 0.008 1 261 . 48 ARG CA C 54.979 0.000 1 262 . 48 ARG CB C 34.336 0.000 1 263 . 49 ARG CA C 55.431 0.456 1 264 . 49 ARG CB C 31.875 0.698 1 265 . 49 ARG CD C 43.148 0.000 1 266 . 49 ARG HD2 H 3.135 0.000 2 267 . 49 ARG H H 8.691 0.003 1 268 . 49 ARG N N 122.785 0.017 1 269 . 50 SER CA C 57.988 0.000 1 270 . 50 SER CB C 63.895 0.000 1 271 . 50 SER H H 8.356 0.002 1 272 . 50 SER N N 116.391 0.023 1 273 . 53 LYS CA C 55.007 0.000 1 274 . 53 LYS CB C 32.561 0.000 1 275 . 53 LYS CE C 35.897 0.000 1 276 . 53 LYS HA H 4.581 0.000 1 277 . 53 LYS HB2 H 2.179 0.000 2 278 . 53 LYS HD2 H 2.118 0.000 2 279 . 53 LYS HE2 H 3.156 0.000 2 280 . 53 LYS HG2 H 1.821 0.000 2 281 . 54 VAL CA C 61.669 0.142 1 282 . 54 VAL CB C 32.851 0.008 1 283 . 54 VAL CG1 C 21.393 0.000 1 284 . 54 VAL HA H 4.606 0.000 1 285 . 54 VAL HB H 1.936 0.001 1 286 . 54 VAL HG2 H 0.913 0.005 2 287 . 54 VAL H H 8.475 0.006 1 288 . 54 VAL N N 123.210 0.018 1 289 . 55 ILE CA C 59.530 0.000 1 290 . 55 ILE CB C 39.975 0.000 1 291 . 55 ILE H H 8.969 0.010 1 292 . 55 ILE N N 126.270 0.089 1 293 . 56 THR CA C 61.295 0.000 1 294 . 56 THR CB C 69.924 0.000 1 295 . 56 THR CG2 C 21.526 0.000 1 296 . 56 THR HA H 4.881 0.000 1 297 . 56 THR HG2 H 1.135 0.000 1 298 . 57 LYS CA C 55.067 0.037 1 299 . 57 LYS CB C 34.865 0.064 1 300 . 57 LYS CD C 29.674 0.000 1 301 . 57 LYS CE C 42.153 0.000 1 302 . 57 LYS CG C 24.414 0.000 1 303 . 57 LYS HB2 H 1.614 0.000 2 304 . 57 LYS HD2 H 1.584 0.000 2 305 . 57 LYS HE2 H 2.858 0.000 2 306 . 57 LYS HG2 H 1.317 0.000 2 307 . 57 LYS H H 8.770 0.008 1 308 . 57 LYS N N 125.798 0.077 1 309 . 58 THR CA C 61.602 0.009 1 310 . 58 THR CB C 70.075 0.151 1 311 . 58 THR CG2 C 21.609 0.000 1 312 . 58 THR HA H 4.928 0.000 1 313 . 58 THR HG2 H 1.131 0.000 1 314 . 58 THR H H 8.507 0.007 1 315 . 58 THR N N 118.786 0.018 1 316 . 59 VAL CA C 60.471 0.003 1 317 . 59 VAL CB C 34.778 0.104 1 318 . 59 VAL CG1 C 20.514 0.000 1 319 . 59 VAL HB H 2.058 0.000 1 320 . 59 VAL HG2 H 0.918 0.000 2 321 . 59 VAL H H 8.723 0.004 1 322 . 59 VAL N N 123.671 0.044 1 323 . 60 THR CA C 61.605 0.039 1 324 . 60 THR CB C 69.392 0.117 1 325 . 60 THR CG2 C 21.145 0.000 1 326 . 60 THR HA H 4.717 0.000 1 327 . 60 THR HB H 4.661 0.000 1 328 . 60 THR HG2 H 1.186 0.000 1 329 . 60 THR H H 8.473 0.006 1 330 . 60 THR N N 119.785 0.016 1 331 . 61 ASN CA C 52.027 0.035 1 332 . 61 ASN CB C 39.401 0.004 1 333 . 61 ASN HA H 4.782 0.000 1 334 . 61 ASN HB2 H 2.279 0.000 2 335 . 61 ASN H H 8.700 0.005 1 336 . 61 ASN N N 124.512 0.018 1 337 . 62 ALA CA C 54.245 0.034 1 338 . 62 ALA CB C 18.424 0.002 1 339 . 62 ALA HB H 1.442 0.000 1 340 . 62 ALA H H 8.578 0.005 1 341 . 62 ALA N N 122.880 0.030 1 342 . 63 ASP CA C 53.807 0.039 1 343 . 63 ASP CB C 40.656 0.007 1 344 . 63 ASP HA H 4.603 0.000 1 345 . 63 ASP H H 7.923 0.014 1 346 . 63 ASP N N 115.552 0.053 1 347 . 64 GLY CA C 45.132 0.018 1 348 . 64 GLY HA2 H 4.198 0.000 1 349 . 64 GLY HA3 H 3.634 0.000 1 350 . 64 GLY H H 8.178 0.013 1 351 . 64 GLY N N 107.839 0.023 1 352 . 65 ARG CA C 55.713 0.005 1 353 . 65 ARG CB C 31.050 0.048 1 354 . 65 ARG CD C 43.148 0.000 1 355 . 65 ARG CG C 30.188 0.000 1 356 . 65 ARG HA H 4.490 0.000 1 357 . 65 ARG HB2 H 1.846 0.000 2 358 . 65 ARG HD2 H 3.226 0.000 2 359 . 65 ARG HG2 H 1.660 0.000 2 360 . 65 ARG H H 7.923 0.014 1 361 . 65 ARG N N 120.894 0.009 1 362 . 66 THR CA C 61.591 0.003 1 363 . 66 THR CB C 69.771 0.083 1 364 . 66 THR HA H 4.430 0.000 1 365 . 66 THR HB H 4.163 0.000 1 366 . 66 THR HG2 H 0.933 0.000 1 367 . 66 THR H H 8.490 0.005 1 368 . 66 THR N N 117.417 0.082 1 369 . 67 GLU CA C 55.507 0.385 1 370 . 67 GLU CB C 32.484 0.026 1 371 . 67 GLU CG C 35.913 0.000 1 372 . 67 GLU HA H 4.682 0.000 1 373 . 67 GLU HB2 H 2.179 0.000 2 374 . 67 GLU HG2 H 2.179 0.000 2 375 . 67 GLU H H 8.378 0.006 1 376 . 67 GLU N N 123.722 0.033 1 377 . 68 THR CA C 61.343 0.023 1 378 . 68 THR CB C 70.163 0.082 1 379 . 68 THR HA H 5.069 0.000 1 380 . 68 THR HG2 H 1.150 0.000 1 381 . 68 THR H H 8.602 0.014 1 382 . 68 THR N N 118.605 0.014 1 383 . 69 THR CA C 61.191 0.450 1 384 . 69 THR CB C 70.406 0.201 1 385 . 69 THR HA H 4.908 0.000 1 386 . 69 THR HG2 H 1.151 0.000 1 387 . 69 THR H H 8.865 0.010 1 388 . 69 THR N N 118.799 0.015 1 389 . 70 LYS CA C 55.436 0.000 1 390 . 70 LYS CB C 32.553 0.000 1 391 . 70 LYS H H 8.868 0.006 1 392 . 70 LYS N N 124.509 0.019 1 393 . 71 GLU CA C 57.352 0.000 1 394 . 71 GLU CB C 30.074 0.000 1 395 . 71 GLU HA H 4.646 0.000 1 396 . 71 GLU HB2 H 2.299 0.000 2 397 . 71 GLU HG2 H 2.219 0.000 2 398 . 72 VAL CA C 61.806 0.175 1 399 . 72 VAL CB C 32.592 0.124 1 400 . 72 VAL HB H 1.952 0.000 1 401 . 72 VAL HG2 H 0.928 0.000 2 402 . 72 VAL H H 8.113 0.012 1 403 . 72 VAL N N 122.327 0.044 1 404 . 73 VAL CA C 60.606 0.050 1 405 . 73 VAL CB C 33.814 0.074 1 406 . 73 VAL HA H 4.394 0.000 1 407 . 73 VAL HB H 2.038 0.000 1 408 . 73 VAL HG2 H 0.928 0.000 2 409 . 73 VAL H H 8.822 0.008 1 410 . 73 VAL N N 125.384 0.027 1 411 . 74 LYS CA C 55.835 0.044 1 412 . 74 LYS CB C 33.433 0.007 1 413 . 74 LYS HA H 4.551 0.000 1 414 . 74 LYS HB2 H 1.771 0.000 2 415 . 74 LYS HD2 H 1.645 0.000 2 416 . 74 LYS HE2 H 2.954 0.000 2 417 . 74 LYS HG2 H 1.388 0.000 2 418 . 74 LYS H H 8.505 0.004 1 419 . 74 LYS N N 124.798 0.017 1 420 . 75 SER CA C 57.527 0.024 1 421 . 75 SER CB C 63.857 0.034 1 422 . 75 SER HA H 4.546 0.000 1 423 . 75 SER HB2 H 3.815 0.000 2 424 . 75 SER H H 8.462 0.008 1 425 . 75 SER N N 117.907 0.017 1 426 . 76 GLU CA C 56.895 0.007 1 427 . 76 GLU CB C 29.888 0.154 1 428 . 76 GLU HA H 4.359 0.000 1 429 . 76 GLU HB2 H 2.315 0.000 2 430 . 76 GLU HG2 H 2.249 0.000 2 431 . 76 GLU H H 8.827 0.004 1 432 . 76 GLU N N 124.147 0.041 1 433 . 77 ASP CA C 53.594 0.000 1 434 . 77 ASP CB C 41.354 0.137 1 435 . 77 ASP HA H 4.687 0.000 1 436 . 77 ASP H H 8.179 0.015 1 437 . 77 ASP N N 118.687 0.033 1 438 . 78 GLY CA C 45.239 0.000 1 439 . 78 GLY H H 8.570 0.002 1 440 . 78 GLY N N 109.963 0.027 1 441 . 79 SER CA C 58.050 0.000 1 442 . 79 SER CB C 63.742 0.000 1 443 . 79 SER H H 8.148 0.007 1 444 . 79 SER N N 115.197 0.004 1 445 . 80 ASP CA C 54.100 0.000 1 446 . 80 ASP CB C 40.957 0.000 1 447 . 80 ASP HA H 4.626 0.000 1 448 . 81 CYS CA C 54.000 0.000 1 449 . 81 CYS CB C 38.982 0.000 1 450 . 81 CYS HA H 4.656 0.000 1 451 . 81 CYS H H 8.380 0.002 1 452 . 81 CYS N N 119.411 0.041 1 453 . 82 GLY CA C 45.105 0.000 1 454 . 82 GLY HA2 H 3.976 0.000 2 455 . 82 GLY H H 8.262 0.003 1 456 . 82 GLY N N 109.221 0.022 1 457 . 83 ASP CA C 54.437 0.025 1 458 . 83 ASP CB C 41.145 0.066 1 459 . 83 ASP HA H 4.616 0.000 1 460 . 83 ASP H H 8.229 0.008 1 461 . 83 ASP N N 120.197 0.005 1 462 . 84 ALA CA C 52.711 0.006 1 463 . 84 ALA CB C 19.257 0.022 1 464 . 84 ALA HA H 4.657 0.000 1 465 . 84 ALA HB H 1.348 0.000 1 466 . 84 ALA H H 8.261 0.004 1 467 . 84 ALA N N 123.423 0.059 1 468 . 85 ASP CA C 54.250 0.000 1 469 . 85 ASP CB C 41.115 0.000 1 470 . 85 ASP HA H 4.697 0.000 1 471 . 85 ASP H H 8.169 0.011 1 472 . 85 ASP N N 118.243 0.031 1 473 . 86 PHE H H 8.180 0.009 1 474 . 86 PHE N N 117.924 0.023 1 475 . 90 HIS CA C 55.878 0.000 1 476 . 90 HIS CB C 29.531 0.000 1 477 . 91 THR CA C 61.822 0.000 1 478 . 91 THR CB C 69.693 0.000 1 479 . 91 THR H H 7.931 0.001 1 480 . 91 THR N N 114.475 0.041 1 481 . 93 PRO CA C 62.711 0.000 1 482 . 93 PRO CB C 31.894 0.000 1 483 . 93 PRO CD C 50.334 0.000 1 484 . 93 PRO CG C 27.301 0.000 1 485 . 93 PRO HA H 4.440 0.000 1 486 . 93 PRO HB2 H 2.224 0.000 2 487 . 93 PRO HD2 H 3.569 0.080 2 488 . 93 PRO HG2 H 1.912 0.000 2 489 . 94 SER CA C 58.200 0.000 1 490 . 94 SER CB C 63.790 0.000 1 491 . 94 SER H H 8.334 0.004 1 492 . 94 SER N N 115.592 0.013 1 493 . 95 ARG CA C 56.039 0.000 1 494 . 95 ARG CB C 30.652 0.000 1 495 . 95 ARG HA H 4.374 0.000 1 496 . 96 GLY CA C 45.221 0.000 1 497 . 96 GLY H H 8.386 0.008 1 498 . 96 GLY N N 108.977 0.060 1 499 . 99 ASP HA H 4.591 0.000 1 500 . 100 ASP H H 8.124 0.000 1 501 . 100 ASP N N 120.100 0.000 1 502 . 101 PHE CA C 58.556 0.000 1 503 . 101 PHE CB C 39.312 0.000 1 504 . 101 PHE HA H 4.410 0.000 1 505 . 102 PHE CA C 58.540 0.000 1 506 . 102 PHE CB C 39.312 0.000 1 507 . 102 PHE H H 8.119 0.005 1 508 . 102 PHE N N 119.246 0.025 1 509 . 103 HIS HA H 4.520 0.000 1 510 . 104 ARG CA C 56.355 0.000 1 511 . 104 ARG CB C 28.891 0.000 1 512 . 104 ARG H H 8.073 0.004 1 513 . 104 ARG N N 117.909 0.007 1 514 . 105 ASP CA C 54.050 0.350 1 515 . 105 ASP CB C 40.072 1.119 1 516 . 105 ASP HA H 4.656 0.000 1 517 . 105 ASP H H 8.478 0.002 1 518 . 105 ASP N N 121.091 0.011 1 519 . 106 LYS CA C 56.940 0.000 1 520 . 106 LYS CB C 29.932 0.000 1 521 . 106 LYS H H 8.387 0.011 1 522 . 106 LYS N N 120.253 0.029 1 523 . 107 ASP CA C 54.914 0.000 1 524 . 107 ASP CB C 42.053 0.000 1 525 . 107 ASP HA H 4.354 0.000 1 526 . 108 ASP CA C 54.935 0.000 1 527 . 108 ASP CB C 42.075 0.000 1 528 . 108 ASP H H 8.123 0.005 1 529 . 108 ASP N N 122.898 0.011 1 530 . 109 PHE CA C 58.454 0.000 1 531 . 109 PHE CB C 39.352 0.000 1 532 . 109 PHE HA H 4.369 0.000 1 533 . 110 PHE CA C 58.184 0.069 1 534 . 110 PHE CB C 39.308 0.024 1 535 . 110 PHE HA H 4.515 0.000 1 536 . 110 PHE HB2 H 3.105 0.000 2 537 . 110 PHE H H 7.984 0.007 1 538 . 110 PHE N N 118.700 0.013 1 539 . 111 THR CA C 62.283 0.000 1 540 . 111 THR CB C 69.389 0.000 1 541 . 111 THR H H 8.005 0.005 1 542 . 111 THR N N 114.831 0.037 1 543 . 112 ARG CA C 56.375 0.000 1 544 . 112 ARG CB C 30.687 0.000 1 545 . 112 ARG CD C 43.148 0.000 1 546 . 112 ARG CG C 29.923 0.000 1 547 . 112 ARG HA H 4.470 0.000 1 548 . 112 ARG HD2 H 3.125 0.000 2 549 . 112 ARG HG2 H 1.201 0.000 2 550 . 113 SER CA C 58.288 0.012 1 551 . 113 SER CB C 63.544 0.050 1 552 . 113 SER HA H 4.530 0.000 1 553 . 113 SER HB2 H 3.916 0.000 1 554 . 113 SER H H 8.260 0.006 1 555 . 113 SER N N 116.098 0.020 1 556 . 114 SER CA C 58.315 0.000 1 557 . 114 SER CB C 63.493 0.000 1 558 . 114 SER H H 8.324 0.012 1 559 . 114 SER N N 117.205 0.013 1 560 . 118 ASP CA C 54.116 0.000 1 561 . 118 ASP CB C 40.979 0.000 1 562 . 118 ASP HA H 4.556 0.000 1 563 . 119 GLY CA C 45.585 0.003 1 564 . 119 GLY HA2 H 3.926 0.000 2 565 . 119 GLY H H 7.979 0.003 1 566 . 119 GLY N N 108.875 0.069 1 567 . 120 ARG CA C 56.370 0.009 1 568 . 120 ARG CB C 30.634 0.018 1 569 . 120 ARG CD C 43.231 0.000 1 570 . 120 ARG CG C 30.188 0.000 1 571 . 120 ARG HA H 4.389 0.000 1 572 . 120 ARG HB2 H 1.886 0.000 2 573 . 120 ARG HD2 H 3.171 0.000 2 574 . 120 ARG HG2 H 1.836 0.000 2 575 . 120 ARG H H 8.112 0.007 1 576 . 120 ARG N N 119.857 0.023 1 577 . 121 THR CA C 62.026 0.000 1 578 . 121 THR CB C 69.589 0.000 1 579 . 121 THR CG2 C 21.410 0.000 1 580 . 121 THR HA H 4.470 0.000 1 581 . 121 THR HB H 4.299 0.000 1 582 . 121 THR HG2 H 1.217 0.000 1 583 . 121 THR H H 8.180 0.007 1 584 . 121 THR N N 113.730 0.040 1 585 . 122 GLY CA C 45.113 0.000 1 586 . 122 GLY HA2 H 3.946 0.000 2 587 . 122 GLY H H 8.425 0.006 1 588 . 122 GLY N N 110.903 0.007 1 589 . 123 LEU CA C 54.483 0.014 1 590 . 123 LEU CB C 42.651 0.004 1 591 . 123 LEU CD1 C 24.165 0.000 1 592 . 123 LEU CG C 26.621 0.000 1 593 . 123 LEU HA H 4.374 0.000 1 594 . 123 LEU HB2 H 1.587 0.018 2 595 . 123 LEU HG H 0.903 0.000 1 596 . 123 LEU H H 7.986 0.005 1 597 . 123 LEU N N 120.980 0.022 1 598 . 124 ALA CA C 50.505 0.000 1 599 . 124 ALA CB C 18.383 0.000 1 600 . 124 ALA H H 8.294 0.004 1 601 . 124 ALA N N 125.895 0.012 1 602 . 125 PRO CA C 63.374 0.000 1 603 . 125 PRO CB C 31.879 0.000 1 604 . 125 PRO CD C 50.334 0.000 1 605 . 125 PRO CG C 27.334 0.000 1 606 . 125 PRO HA H 4.339 0.000 1 607 . 125 PRO HB2 H 2.239 0.000 2 608 . 125 PRO HB3 H 1.796 0.000 2 609 . 125 PRO HD2 H 3.710 0.000 2 610 . 125 PRO HG2 H 1.997 0.000 2 611 . 126 GLU CA C 56.966 0.056 1 612 . 126 GLU CB C 29.864 0.170 1 613 . 126 GLU CG C 35.946 0.000 1 614 . 126 GLU HA H 3.971 0.000 1 615 . 126 GLU HB2 H 2.017 0.000 2 616 . 126 GLU HG2 H 2.088 0.000 2 617 . 126 GLU H H 8.637 0.009 1 618 . 126 GLU N N 119.591 0.015 1 619 . 127 PHE CA C 57.590 0.003 1 620 . 127 PHE CB C 39.367 0.043 1 621 . 127 PHE HA H 4.611 0.000 1 622 . 127 PHE HB2 H 3.206 0.000 2 623 . 127 PHE HB3 H 2.994 0.000 2 624 . 127 PHE H H 8.246 0.003 1 625 . 127 PHE N N 119.789 0.021 1 626 . 128 ALA CA C 52.495 0.052 1 627 . 128 ALA CB C 19.121 0.071 1 628 . 128 ALA HA H 4.384 0.000 1 629 . 128 ALA HB H 1.358 0.000 1 630 . 128 ALA H H 8.042 0.006 1 631 . 128 ALA N N 124.689 0.012 1 632 . 129 ALA CA C 52.400 0.058 1 633 . 129 ALA CB C 18.977 0.049 1 634 . 129 ALA HA H 4.017 0.000 1 635 . 129 ALA HB H 1.343 0.000 1 636 . 129 ALA H H 8.094 0.004 1 637 . 129 ALA N N 122.320 0.014 1 638 . 130 LEU CA C 55.284 0.030 1 639 . 130 LEU CB C 42.186 0.018 1 640 . 130 LEU CD1 C 23.883 0.000 1 641 . 130 LEU CG C 26.637 0.000 1 642 . 130 LEU HA H 4.319 0.000 1 643 . 130 LEU HB2 H 1.695 0.000 2 644 . 130 LEU HD2 H 0.948 0.000 2 645 . 130 LEU HG H 1.620 0.000 1 646 . 130 LEU H H 8.080 0.011 1 647 . 130 LEU N N 120.510 0.009 1 648 . 131 GLY CA C 45.201 0.042 1 649 . 131 GLY HA2 H 3.981 0.000 2 650 . 131 GLY H H 8.258 0.004 1 651 . 131 GLY N N 108.720 0.025 1 652 . 132 GLU CA C 56.378 0.024 1 653 . 132 GLU CB C 30.236 0.002 1 654 . 132 GLU CG C 35.930 0.000 1 655 . 132 GLU HA H 4.354 0.000 1 656 . 132 GLU HB2 H 2.234 0.000 2 657 . 132 GLU HG2 H 2.299 0.000 2 658 . 132 GLU H H 8.244 0.006 1 659 . 132 GLU N N 120.350 0.064 1 660 . 133 SER CA C 58.562 0.022 1 661 . 133 SER CB C 63.552 0.038 1 662 . 133 SER H H 8.449 0.003 1 663 . 133 SER N N 116.514 0.015 1 664 . 134 GLY CA C 45.265 0.019 1 665 . 134 GLY HA2 H 4.007 0.000 2 666 . 134 GLY H H 8.407 0.009 1 667 . 134 GLY N N 110.284 0.053 1 668 . 135 SER CB C 63.579 0.003 1 669 . 135 SER HA H 4.525 0.000 1 670 . 135 SER HB2 H 3.906 0.000 2 671 . 135 SER H H 8.207 0.006 1 672 . 135 SER N N 115.180 0.012 1 673 . 135 SER CA C 57.983 0.000 1 674 . 136 SER CB C 63.599 0.008 1 675 . 136 SER HA H 4.435 0.000 1 676 . 136 SER HB2 H 3.810 0.000 2 677 . 136 SER H H 8.410 0.007 1 678 . 136 SER N N 117.665 0.329 1 679 . 136 SER CA C 58.331 0.000 1 680 . 137 SER CA C 58.264 0.050 1 681 . 137 SER CB C 63.591 0.017 1 682 . 137 SER HA H 4.530 0.000 1 683 . 137 SER HB2 H 3.906 0.000 2 684 . 137 SER H H 8.226 0.007 1 685 . 137 SER N N 117.120 0.054 1 686 . 138 SER CA C 58.215 0.000 1 687 . 138 SER CB C 63.575 0.000 1 688 . 138 SER H H 8.380 0.002 1 689 . 138 SER N N 117.279 0.053 1 690 . 139 LYS CA C 56.440 0.000 1 691 . 139 LYS CB C 32.828 0.000 1 692 . 139 LYS CD C 29.060 0.000 1 693 . 139 LYS CE C 42.169 0.000 1 694 . 139 LYS CG C 24.712 0.000 1 695 . 139 LYS HA H 4.420 0.000 1 696 . 139 LYS HB2 H 1.871 0.000 2 697 . 139 LYS HD2 H 1.690 0.000 2 698 . 139 LYS HE2 H 2.994 0.000 2 699 . 139 LYS HG2 H 1.463 0.000 2 700 . 140 THR CA C 61.705 0.000 1 701 . 140 THR CB C 69.553 0.000 1 702 . 140 THR H H 8.097 0.007 1 703 . 140 THR N N 114.095 0.012 1 704 . 141 SER CA C 58.115 0.000 1 705 . 141 SER CB C 63.508 0.000 1 706 . 141 SER HA H 4.546 0.000 1 707 . 141 SER HB2 H 3.992 0.000 2 708 . 142 THR CA C 61.886 0.000 1 709 . 142 THR CB C 69.446 0.000 1 710 . 142 THR H H 8.172 0.006 1 711 . 142 THR N N 115.393 0.026 1 712 . 147 PHE CA C 57.651 0.000 1 713 . 147 PHE CB C 39.523 0.000 1 714 . 148 VAL CA C 61.761 0.013 1 715 . 148 VAL CB C 32.948 0.088 1 716 . 148 VAL CG1 C 20.530 0.000 2 717 . 148 VAL HA H 4.112 0.000 1 718 . 148 VAL HB H 2.012 0.000 1 719 . 148 VAL HG2 H 0.953 0.000 2 720 . 148 VAL H H 8.013 0.002 1 721 . 148 VAL N N 122.580 0.006 1 722 . 149 SER CA C 57.983 0.000 1 723 . 149 SER CB C 63.658 0.050 1 724 . 149 SER HA H 4.525 0.000 1 725 . 149 SER HB2 H 3.906 0.000 2 726 . 149 SER H H 8.370 0.002 1 727 . 149 SER N N 119.493 0.017 1 728 . 150 SER CA C 58.057 0.025 1 729 . 150 SER CB C 63.608 0.033 1 730 . 150 SER HA H 4.525 0.000 1 731 . 150 SER H H 8.392 0.016 1 732 . 150 SER N N 117.802 0.006 1 733 . 151 SER CA C 58.032 0.000 1 734 . 151 SER CB C 63.625 0.000 1 735 . 151 SER H H 8.392 0.007 1 736 . 151 SER N N 117.882 0.037 1 737 . 152 THR CA C 61.484 0.000 1 738 . 152 THR CB C 69.565 0.000 1 739 . 152 THR HA H 4.465 0.000 1 740 . 152 THR HG2 H 1.207 0.000 1 741 . 153 THR CA C 61.896 0.000 1 742 . 153 THR CB C 69.548 0.000 1 743 . 153 THR H H 8.192 0.005 1 744 . 153 THR N N 116.909 0.015 1 745 . 154 VAL CA C 62.167 0.000 1 746 . 154 VAL CB C 32.868 0.000 1 747 . 154 VAL CG1 C 20.630 0.000 2 748 . 154 VAL HB H 2.062 0.000 1 749 . 154 VAL HG2 H 0.972 0.000 2 750 . 155 ASN CA C 52.977 0.021 1 751 . 155 ASN CB C 38.678 0.028 1 752 . 155 ASN HA H 4.737 0.000 1 753 . 155 ASN H H 8.511 0.004 1 754 . 155 ASN N N 122.383 0.038 1 755 . 156 ARG CA C 56.212 0.020 1 756 . 156 ARG CB C 30.511 0.059 1 757 . 156 ARG CD C 43.147 0.000 1 758 . 156 ARG CG C 30.088 0.000 1 759 . 156 ARG HA H 4.319 0.000 1 760 . 156 ARG HB2 H 1.898 0.000 2 761 . 156 ARG HD2 H 3.199 0.000 2 762 . 156 ARG HG2 H 1.761 0.000 2 763 . 156 ARG H H 8.440 0.004 1 764 . 156 ARG N N 122.195 0.012 1 765 . 157 GLY CA C 45.252 0.028 1 766 . 157 GLY HA2 H 3.999 0.000 2 767 . 157 GLY H H 8.435 0.006 1 768 . 157 GLY N N 109.512 0.033 1 769 . 158 GLY CA C 45.211 0.044 1 770 . 158 GLY HA2 H 4.002 0.000 2 771 . 158 GLY H H 8.266 0.006 1 772 . 158 GLY N N 108.589 0.065 1 773 . 159 SER CA C 58.063 0.031 1 774 . 159 SER CB C 63.817 0.036 1 775 . 159 SER HA H 4.484 0.000 1 776 . 159 SER HB2 H 3.888 0.000 2 777 . 159 SER H H 8.154 0.005 1 778 . 159 SER N N 115.277 0.022 1 779 . 160 ALA CA C 52.508 0.022 1 780 . 160 ALA CB C 19.117 0.018 1 781 . 160 ALA HA H 4.520 0.000 1 782 . 160 ALA HB H 1.399 0.000 1 783 . 160 ALA H H 8.373 0.004 1 784 . 160 ALA N N 125.725 0.017 1 785 . 161 ILE CA C 61.065 0.007 1 786 . 161 ILE CB C 38.559 0.083 1 787 . 161 ILE CG1 C 27.308 0.000 1 788 . 161 ILE HA H 4.147 0.000 1 789 . 161 ILE HB H 1.860 0.000 1 790 . 161 ILE HG2 H 0.937 0.000 1 791 . 161 ILE H H 8.044 0.002 1 792 . 161 ILE N N 119.354 0.075 1 793 . 162 GLU CA C 56.379 0.010 1 794 . 162 GLU CB C 30.291 0.036 1 795 . 162 GLU CG C 36.029 0.000 1 796 . 162 GLU HA H 4.510 0.000 1 797 . 162 GLU HB2 H 2.240 0.000 2 798 . 162 GLU HG2 H 2.294 0.000 2 799 . 162 GLU H H 8.397 0.004 1 800 . 162 GLU N N 124.547 0.102 1 801 . 163 SER H H 8.288 0.003 1 802 . 163 SER N N 117.222 0.047 1 803 . 165 HIS CA C 54.994 0.000 1 804 . 165 HIS CB C 29.642 0.000 1 805 . 165 HIS HA H 4.637 0.000 1 806 . 165 HIS HB2 H 3.120 0.000 2 807 . 166 PHE CA C 59.034 0.000 1 808 . 166 PHE CB C 40.004 0.000 1 809 . 166 PHE H H 7.863 0.004 1 810 . 166 PHE N N 126.247 0.035 1 stop_ save_