data_27795 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FLNa4-6 ; _BMRB_accession_number 27795 _BMRB_flat_file_name bmr27795.str _Entry_type original _Submission_date 2019-02-21 _Accession_date 2019-02-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of filamin domains 4-6.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Haataja Tatu TH . 2 Permi Perttu PP . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 265 "13C chemical shifts" 556 "15N chemical shifts" 245 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-02-28 original BMRB . stop_ _Original_release_date 2019-02-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31542223 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Haataja Tatu . . 2 Capoulade Romain . . 3 Lecointe Simon . . 4 Hellman Maarit . . 5 Merot Jean . . 6 Permi Perttu . . 7 Pentikainen Ulla . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_name_full 'Biophysical journal' _Journal_volume 117 _Journal_issue 8 _Journal_ISSN 1542-0086 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1467 _Page_last 1475 _Year 2019 _Details . loop_ _Keyword 'Cardiovascular disease' FLNA-MVD Filamin 'Mitral valve prolapse' 'NMR spectroscopy' SAXS 'protein tyrosine phosphatase 12' 'protein-protein interaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FLNa4-6 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FLNa4-6 $FLNa4-6 stop_ _System_molecular_weight 31520.41 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 FLNa4-6 stop_ loop_ _Biological_function ; Cytoskeletal protein that connects ECM to actin cytoskeleton.Multiple functions in cells, such as signal transduction, force transmission and scaffolding. ; stop_ _Database_query_date . _Details 'one polypeptide chain' save_ ######################## # Monomeric polymers # ######################## save_FLNa4-6 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FLNa4-6 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function ; Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 298 _Mol_residue_sequence ; SMCGNQKVRAWGPGLEGGVV GKSADFVVEAIGDDVGTLGF SVEGPSQAKIECDDKGDGSC DVRYWPQEAGEYAVHVLCNS EDIRLSPFMADIRDAPQDFH PDRVKARGPGLEKTGVAVNK PAEFTVDAKHGGKAPLRVQV QDNEGCPVEALVKDNGNGTY SCSYVPRKPVKHTAMVSWGG VSIPNSPFRVNVGAGSHPNK VKVYGPGVAKTGLKAHEPTY FTVDCAEAGQGDVSIGIKCA PGVVGPAEADIDFDIIRNDN DTFTVKYTPRGAGSYTIMVL FADQATPTSPIRVKVEPS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 572 SER 2 573 MET 3 574 CYS 4 575 GLY 5 576 ASN 6 577 GLN 7 578 LYS 8 579 VAL 9 580 ARG 10 581 ALA 11 582 TRP 12 583 GLY 13 584 PRO 14 585 GLY 15 586 LEU 16 587 GLU 17 588 GLY 18 589 GLY 19 590 VAL 20 591 VAL 21 592 GLY 22 593 LYS 23 594 SER 24 595 ALA 25 596 ASP 26 597 PHE 27 598 VAL 28 599 VAL 29 600 GLU 30 601 ALA 31 602 ILE 32 603 GLY 33 604 ASP 34 605 ASP 35 606 VAL 36 607 GLY 37 608 THR 38 609 LEU 39 610 GLY 40 611 PHE 41 612 SER 42 613 VAL 43 614 GLU 44 615 GLY 45 616 PRO 46 617 SER 47 618 GLN 48 619 ALA 49 620 LYS 50 621 ILE 51 622 GLU 52 623 CYS 53 624 ASP 54 625 ASP 55 626 LYS 56 627 GLY 57 628 ASP 58 629 GLY 59 630 SER 60 631 CYS 61 632 ASP 62 633 VAL 63 634 ARG 64 635 TYR 65 636 TRP 66 637 PRO 67 638 GLN 68 639 GLU 69 640 ALA 70 641 GLY 71 642 GLU 72 643 TYR 73 644 ALA 74 645 VAL 75 646 HIS 76 647 VAL 77 648 LEU 78 649 CYS 79 650 ASN 80 651 SER 81 652 GLU 82 653 ASP 83 654 ILE 84 655 ARG 85 656 LEU 86 657 SER 87 658 PRO 88 659 PHE 89 660 MET 90 661 ALA 91 662 ASP 92 663 ILE 93 664 ARG 94 665 ASP 95 666 ALA 96 667 PRO 97 668 GLN 98 669 ASP 99 670 PHE 100 671 HIS 101 672 PRO 102 673 ASP 103 674 ARG 104 675 VAL 105 676 LYS 106 677 ALA 107 678 ARG 108 679 GLY 109 680 PRO 110 681 GLY 111 682 LEU 112 683 GLU 113 684 LYS 114 685 THR 115 686 GLY 116 687 VAL 117 688 ALA 118 689 VAL 119 690 ASN 120 691 LYS 121 692 PRO 122 693 ALA 123 694 GLU 124 695 PHE 125 696 THR 126 697 VAL 127 698 ASP 128 699 ALA 129 700 LYS 130 701 HIS 131 702 GLY 132 703 GLY 133 704 LYS 134 705 ALA 135 706 PRO 136 707 LEU 137 708 ARG 138 709 VAL 139 710 GLN 140 711 VAL 141 712 GLN 142 713 ASP 143 714 ASN 144 715 GLU 145 716 GLY 146 717 CYS 147 718 PRO 148 719 VAL 149 720 GLU 150 721 ALA 151 722 LEU 152 723 VAL 153 724 LYS 154 725 ASP 155 726 ASN 156 727 GLY 157 728 ASN 158 729 GLY 159 730 THR 160 731 TYR 161 732 SER 162 733 CYS 163 734 SER 164 735 TYR 165 736 VAL 166 737 PRO 167 738 ARG 168 739 LYS 169 740 PRO 170 741 VAL 171 742 LYS 172 743 HIS 173 744 THR 174 745 ALA 175 746 MET 176 747 VAL 177 748 SER 178 749 TRP 179 750 GLY 180 751 GLY 181 752 VAL 182 753 SER 183 754 ILE 184 755 PRO 185 756 ASN 186 757 SER 187 758 PRO 188 759 PHE 189 760 ARG 190 761 VAL 191 762 ASN 192 763 VAL 193 764 GLY 194 765 ALA 195 766 GLY 196 767 SER 197 768 HIS 198 769 PRO 199 770 ASN 200 771 LYS 201 772 VAL 202 773 LYS 203 774 VAL 204 775 TYR 205 776 GLY 206 777 PRO 207 778 GLY 208 779 VAL 209 780 ALA 210 781 LYS 211 782 THR 212 783 GLY 213 784 LEU 214 785 LYS 215 786 ALA 216 787 HIS 217 788 GLU 218 789 PRO 219 790 THR 220 791 TYR 221 792 PHE 222 793 THR 223 794 VAL 224 795 ASP 225 796 CYS 226 797 ALA 227 798 GLU 228 799 ALA 229 800 GLY 230 801 GLN 231 802 GLY 232 803 ASP 233 804 VAL 234 805 SER 235 806 ILE 236 807 GLY 237 808 ILE 238 809 LYS 239 810 CYS 240 811 ALA 241 812 PRO 242 813 GLY 243 814 VAL 244 815 VAL 245 816 GLY 246 817 PRO 247 818 ALA 248 819 GLU 249 820 ALA 250 821 ASP 251 822 ILE 252 823 ASP 253 824 PHE 254 825 ASP 255 826 ILE 256 827 ILE 257 828 ARG 258 829 ASN 259 830 ASP 260 831 ASN 261 832 ASP 262 833 THR 263 834 PHE 264 835 THR 265 836 VAL 266 837 LYS 267 838 TYR 268 839 THR 269 840 PRO 270 841 ARG 271 842 GLY 272 843 ALA 273 844 GLY 274 845 SER 275 846 TYR 276 847 THR 277 848 ILE 278 849 MET 279 850 VAL 280 851 LEU 281 852 PHE 282 853 ALA 283 854 ASP 284 855 GLN 285 856 ALA 286 857 THR 287 858 PRO 288 859 THR 289 860 SER 290 861 PRO 291 862 ILE 292 863 ARG 293 864 VAL 294 865 LYS 295 866 VAL 296 867 GLU 297 868 PRO 298 869 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P21333 FLNA_HUMAN . . . . . 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 $FLNa4-6 Human 9606 Eukaryota Metazoa Homo sapiens FLNA 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 $FLNa4-6 'recombinant technology' . Escherichia coli . pGTvL1-SGC 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FLNa4-6 0.8 mM 0.5 1.1 '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 0.15 . M pH 7.0 . pH pressure 1 . atm temperature 273 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 FLNa4-6 _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 1 572 1 SER H H 7.378 0.000 . 2 572 1 SER CA C 54.193 0.000 . 3 572 1 SER CB C 64.065 0.000 . 4 572 1 SER N N 110.888 0.000 . 5 574 3 CYS CB C 27.467 0.000 . 6 575 4 GLY H H 7.274 0.005 . 7 575 4 GLY CA C 43.486 0.032 . 8 575 4 GLY N N 119.434 0.017 . 9 577 6 GLN CA C 55.723 0.000 . 10 577 6 GLN CG C 34.071 0.000 . 11 578 7 LYS H H 6.975 0.018 . 12 578 7 LYS N N 115.589 0.000 . 13 579 8 VAL CA C 61.710 0.099 . 14 579 8 VAL CB C 32.850 0.058 . 15 579 8 VAL CG1 C 21.179 0.000 . 16 579 8 VAL CG2 C 21.179 0.000 . 17 580 9 ARG H H 9.005 0.012 . 18 580 9 ARG CA C 50.874 8.376 . 19 580 9 ARG CB C 30.341 0.064 . 20 580 9 ARG N N 129.434 0.033 . 21 581 10 ALA H H 7.527 0.022 . 22 581 10 ALA CA C 50.858 0.087 . 23 581 10 ALA CB C 17.699 0.000 . 24 581 10 ALA N N 122.055 0.045 . 25 582 11 TRP CA C 54.389 0.060 . 26 582 11 TRP CB C 32.116 0.033 . 27 583 12 GLY H H 8.419 0.007 . 28 583 12 GLY CA C 45.298 0.029 . 29 583 12 GLY N N 112.082 0.026 . 30 584 13 PRO CA C 66.016 0.219 . 31 584 13 PRO CB C 31.304 0.000 . 32 585 14 GLY H H 9.454 0.008 . 33 585 14 GLY CA C 46.528 0.089 . 34 585 14 GLY N N 106.118 0.049 . 35 586 15 LEU H H 7.265 0.009 . 36 586 15 LEU CA C 54.509 0.033 . 37 586 15 LEU CB C 39.660 0.000 . 38 586 15 LEU N N 115.788 0.064 . 39 587 16 GLU H H 7.590 0.004 . 40 587 16 GLU CA C 55.946 0.101 . 41 587 16 GLU CB C 32.561 0.006 . 42 587 16 GLU N N 113.062 0.015 . 43 588 17 GLY H H 8.310 0.007 . 44 588 17 GLY CA C 47.204 0.029 . 45 588 17 GLY N N 109.332 0.074 . 46 589 18 GLY H H 7.371 0.005 . 47 589 18 GLY CA C 44.479 0.050 . 48 589 18 GLY N N 104.434 0.043 . 49 590 19 VAL H H 9.102 0.008 . 50 590 19 VAL CA C 59.270 0.062 . 51 590 19 VAL CB C 36.633 0.038 . 52 590 19 VAL N N 118.035 0.034 . 53 591 20 VAL H H 7.971 0.009 . 54 591 20 VAL CA C 64.998 0.050 . 55 591 20 VAL CB C 32.240 0.080 . 56 591 20 VAL N N 123.549 0.046 . 57 592 21 GLY H H 7.903 0.005 . 58 592 21 GLY CA C 45.647 0.093 . 59 592 21 GLY N N 113.177 0.039 . 60 593 22 LYS H H 7.980 0.005 . 61 593 22 LYS CA C 52.649 0.106 . 62 593 22 LYS CB C 33.730 0.060 . 63 593 22 LYS N N 118.933 0.043 . 64 594 23 SER H H 8.289 0.006 . 65 594 23 SER CA C 58.785 0.111 . 66 594 23 SER CB C 62.023 0.038 . 67 594 23 SER N N 118.591 0.041 . 68 595 24 ALA H H 8.195 0.006 . 69 595 24 ALA HB H 0.198 0.000 . 70 595 24 ALA CA C 50.311 0.088 . 71 595 24 ALA CB C 17.964 0.016 . 72 595 24 ALA N N 129.032 0.047 . 73 596 25 ASP H H 7.530 0.008 . 74 596 25 ASP CA C 53.786 0.143 . 75 596 25 ASP CB C 42.993 0.097 . 76 596 25 ASP N N 120.966 0.048 . 77 597 26 PHE H H 9.390 0.007 . 78 597 26 PHE CA C 56.850 0.108 . 79 597 26 PHE CB C 39.266 0.187 . 80 597 26 PHE N N 116.832 0.069 . 81 598 27 VAL H H 8.889 0.010 . 82 598 27 VAL CA C 61.196 0.567 . 83 598 27 VAL CB C 34.663 0.035 . 84 598 27 VAL N N 120.477 0.068 . 85 599 28 VAL H H 8.217 0.009 . 86 599 28 VAL CA C 61.411 1.704 . 87 599 28 VAL CB C 29.738 0.000 . 88 599 28 VAL N N 121.848 0.210 . 89 600 29 GLU H H 9.400 0.009 . 90 600 29 GLU CA C 55.490 0.038 . 91 600 29 GLU N N 121.126 0.018 . 92 601 30 ALA H H 9.349 0.010 . 93 601 30 ALA CA C 56.329 0.066 . 94 601 30 ALA N N 127.036 1.128 . 95 602 31 ILE H H 8.240 0.017 . 96 602 31 ILE CA C 61.462 0.054 . 97 602 31 ILE CB C 38.601 0.061 . 98 602 31 ILE CG2 C 16.204 0.000 . 99 602 31 ILE N N 116.009 0.020 . 100 603 32 GLY H H 8.144 0.008 . 101 603 32 GLY CA C 44.795 0.089 . 102 603 32 GLY N N 111.490 0.111 . 103 604 33 ASP H H 8.282 0.005 . 104 604 33 ASP CA C 54.822 0.075 . 105 604 33 ASP CB C 41.422 0.270 . 106 604 33 ASP N N 119.592 0.078 . 107 605 34 ASP H H 8.360 0.005 . 108 605 34 ASP CA C 52.206 4.308 . 109 605 34 ASP CB C 40.917 0.060 . 110 605 34 ASP N N 118.702 0.028 . 111 606 35 VAL H H 7.912 0.006 . 112 606 35 VAL CA C 63.734 0.086 . 113 606 35 VAL CB C 32.201 0.039 . 114 606 35 VAL N N 119.689 0.033 . 115 607 36 GLY H H 8.027 0.006 . 116 607 36 GLY CA C 44.993 0.036 . 117 607 36 GLY N N 108.519 0.023 . 118 608 37 THR H H 7.907 0.007 . 119 608 37 THR CA C 62.202 0.089 . 120 608 37 THR CB C 69.896 0.033 . 121 608 37 THR N N 114.216 0.017 . 122 609 38 LEU H H 8.437 0.006 . 123 609 38 LEU CA C 53.998 0.094 . 124 609 38 LEU CB C 43.326 0.192 . 125 609 38 LEU N N 128.815 0.070 . 126 610 39 GLY H H 8.325 0.009 . 127 610 39 GLY CA C 43.803 0.050 . 128 610 39 GLY N N 110.646 0.062 . 129 611 40 PHE H H 8.067 0.010 . 130 611 40 PHE CA C 55.877 0.072 . 131 611 40 PHE CB C 44.577 0.042 . 132 611 40 PHE N N 114.406 0.099 . 133 612 41 SER H H 8.467 0.006 . 134 612 41 SER CA C 58.146 0.133 . 135 612 41 SER CB C 64.982 0.076 . 136 612 41 SER N N 115.640 0.043 . 137 613 42 VAL H H 8.842 0.007 . 138 613 42 VAL CA C 61.167 0.075 . 139 613 42 VAL N N 124.331 0.036 . 140 614 43 GLU H H 8.816 0.005 . 141 614 43 GLU CA C 56.635 0.105 . 142 614 43 GLU CB C 56.717 0.000 . 143 614 43 GLU N N 122.032 0.042 . 144 615 44 GLY H H 8.695 0.008 . 145 615 44 GLY CA C 44.461 0.018 . 146 615 44 GLY N N 107.194 0.023 . 147 616 45 PRO CA C 64.231 0.058 . 148 616 45 PRO CB C 32.060 0.017 . 149 617 46 SER H H 6.970 0.008 . 150 617 46 SER CA C 56.712 0.050 . 151 617 46 SER CB C 65.952 0.000 . 152 617 46 SER N N 107.633 0.081 . 153 618 47 GLN CA C 56.583 0.085 . 154 618 47 GLN CB C 28.895 0.049 . 155 619 48 ALA H H 8.740 0.005 . 156 619 48 ALA CA C 50.991 0.149 . 157 619 48 ALA CB C 21.180 0.079 . 158 619 48 ALA N N 129.068 0.047 . 159 620 49 LYS H H 8.831 0.005 . 160 620 49 LYS CA C 57.194 0.096 . 161 620 49 LYS CB C 33.436 0.081 . 162 620 49 LYS N N 125.184 0.036 . 163 621 50 ILE H H 8.407 0.007 . 164 621 50 ILE CA C 59.888 0.068 . 165 621 50 ILE CB C 41.640 0.040 . 166 621 50 ILE N N 123.654 0.043 . 167 622 51 GLU H H 9.285 0.005 . 168 622 51 GLU CA C 54.645 0.093 . 169 622 51 GLU CB C 34.172 0.084 . 170 622 51 GLU N N 126.170 0.070 . 171 623 52 CYS H H 8.476 0.008 . 172 623 52 CYS CA C 56.748 0.062 . 173 623 52 CYS CB C 29.061 0.032 . 174 623 52 CYS N N 120.175 0.078 . 175 624 53 ASP H H 9.318 0.007 . 176 624 53 ASP CA C 52.726 0.047 . 177 624 53 ASP CB C 43.105 0.038 . 178 624 53 ASP N N 129.033 0.045 . 179 625 54 ASP H H 8.684 0.009 . 180 625 54 ASP CA C 54.828 0.141 . 181 625 54 ASP CB C 41.120 0.000 . 182 625 54 ASP N N 125.618 0.043 . 183 626 55 LYS H H 8.539 0.006 . 184 626 55 LYS CA C 54.349 0.072 . 185 626 55 LYS CB C 30.091 0.055 . 186 626 55 LYS N N 125.684 0.085 . 187 627 56 GLY H H 9.034 0.008 . 188 627 56 GLY CA C 46.037 0.083 . 189 627 56 GLY N N 108.972 0.087 . 190 628 57 ASP H H 8.051 0.005 . 191 628 57 ASP CA C 52.679 0.085 . 192 628 57 ASP CB C 41.259 0.103 . 193 628 57 ASP N N 118.536 0.036 . 194 629 58 GLY H H 8.938 0.007 . 195 629 58 GLY CA C 45.527 0.084 . 196 629 58 GLY N N 110.297 0.070 . 197 630 59 SER H H 8.180 0.009 . 198 630 59 SER CA C 56.813 0.800 . 199 630 59 SER CB C 67.862 0.036 . 200 630 59 SER N N 116.169 0.123 . 201 631 60 CYS H H 8.965 0.006 . 202 631 60 CYS CB C 31.849 0.000 . 203 631 60 CYS N N 116.131 0.082 . 204 632 61 ASP CA C 53.943 0.000 . 205 632 61 ASP CB C 41.753 0.000 . 206 633 62 VAL H H 8.375 0.021 . 207 633 62 VAL CA C 60.570 0.000 . 208 633 62 VAL CB C 32.217 0.000 . 209 633 62 VAL N N 124.548 0.000 . 210 634 63 ARG H H 8.418 0.000 . 211 634 63 ARG CA C 53.685 0.167 . 212 634 63 ARG CB C 33.428 0.319 . 213 634 63 ARG N N 120.964 0.000 . 214 635 64 TYR H H 8.093 0.007 . 215 635 64 TYR CA C 55.863 1.845 . 216 635 64 TYR CB C 42.109 0.107 . 217 635 64 TYR N N 115.752 0.018 . 218 636 65 TRP H H 7.758 0.001 . 219 636 65 TRP CB C 29.531 0.000 . 220 636 65 TRP N N 118.521 0.014 . 221 638 67 GLN CA C 55.540 0.121 . 222 638 67 GLN CB C 30.417 0.207 . 223 639 68 GLU H H 6.983 0.006 . 224 639 68 GLU CA C 54.788 0.084 . 225 639 68 GLU CB C 33.915 0.080 . 226 639 68 GLU N N 115.688 0.118 . 227 640 69 ALA H H 9.393 0.007 . 228 640 69 ALA CA C 53.153 0.120 . 229 640 69 ALA CB C 18.878 0.116 . 230 640 69 ALA N N 130.833 0.066 . 231 641 70 GLY H H 8.866 0.006 . 232 641 70 GLY CA C 44.398 0.051 . 233 641 70 GLY N N 107.460 0.012 . 234 642 71 GLU H H 8.165 0.006 . 235 642 71 GLU CA C 56.382 0.579 . 236 642 71 GLU CB C 30.940 0.154 . 237 642 71 GLU N N 120.564 0.026 . 238 643 72 TYR H H 8.615 0.009 . 239 643 72 TYR CA C 56.411 0.117 . 240 643 72 TYR CB C 40.101 0.056 . 241 643 72 TYR N N 124.658 0.040 . 242 644 73 ALA H H 8.951 0.005 . 243 644 73 ALA CA C 50.288 0.085 . 244 644 73 ALA CB C 19.973 0.066 . 245 644 73 ALA N N 125.344 0.071 . 246 645 74 VAL H H 9.537 0.015 . 247 645 74 VAL CA C 62.142 0.067 . 248 645 74 VAL CB C 32.452 0.062 . 249 645 74 VAL N N 126.529 0.032 . 250 646 75 HIS H H 9.520 0.007 . 251 646 75 HIS CA C 54.672 0.035 . 252 646 75 HIS CB C 28.802 0.000 . 253 646 75 HIS N N 124.367 0.069 . 254 647 76 VAL CA C 61.447 0.081 . 255 647 76 VAL CB C 34.304 0.086 . 256 648 77 LEU H H 8.764 0.018 . 257 648 77 LEU CA C 53.107 0.527 . 258 648 77 LEU CB C 44.709 0.146 . 259 648 77 LEU N N 125.880 0.015 . 260 649 78 CYS H H 8.747 0.009 . 261 649 78 CYS CA C 57.418 0.084 . 262 649 78 CYS CB C 28.215 0.109 . 263 649 78 CYS N N 119.260 0.055 . 264 650 79 ASN H H 9.579 0.007 . 265 650 79 ASN CA C 54.851 0.081 . 266 650 79 ASN CB C 37.002 0.033 . 267 650 79 ASN N N 128.846 0.056 . 268 651 80 SER H H 9.024 0.005 . 269 651 80 SER CA C 60.241 0.784 . 270 651 80 SER CB C 61.865 0.050 . 271 651 80 SER N N 105.368 0.059 . 272 652 81 GLU H H 7.453 0.008 . 273 652 81 GLU CA C 54.309 0.010 . 274 652 81 GLU CB C 32.678 0.000 . 275 652 81 GLU N N 119.835 0.085 . 276 659 88 PHE CA C 56.263 0.095 . 277 659 88 PHE CB C 41.614 0.006 . 278 660 89 MET H H 8.996 0.008 . 279 660 89 MET CA C 52.847 0.085 . 280 660 89 MET CB C 29.434 0.098 . 281 660 89 MET N N 119.440 0.012 . 282 661 90 ALA H H 9.309 0.006 . 283 661 90 ALA CA C 50.768 0.036 . 284 661 90 ALA CB C 21.450 0.036 . 285 661 90 ALA N N 130.517 0.081 . 286 662 91 ASP H H 7.504 0.008 . 287 662 91 ASP CA C 53.409 0.116 . 288 662 91 ASP N N 122.930 0.038 . 289 664 93 ARG CA C 54.167 0.196 . 290 664 93 ARG CB C 33.434 0.030 . 291 665 94 ASP H H 8.430 0.005 . 292 665 94 ASP CA C 55.136 0.102 . 293 665 94 ASP CB C 41.676 0.093 . 294 665 94 ASP N N 119.435 0.044 . 295 666 95 ALA H H 8.664 0.008 . 296 666 95 ALA CA C 50.528 0.037 . 297 666 95 ALA CB C 18.801 0.000 . 298 666 95 ALA N N 124.344 0.043 . 299 667 96 PRO CA C 61.877 0.087 . 300 667 96 PRO CB C 32.252 0.034 . 301 668 97 GLN H H 8.443 0.007 . 302 668 97 GLN CA C 57.247 0.058 . 303 668 97 GLN CB C 29.119 0.029 . 304 668 97 GLN N N 118.520 0.060 . 305 669 98 ASP H H 8.548 0.005 . 306 669 98 ASP CA C 54.013 0.044 . 307 669 98 ASP CB C 39.723 0.035 . 308 669 98 ASP N N 118.116 0.059 . 309 670 99 PHE H H 7.323 0.007 . 310 670 99 PHE CA C 57.098 0.069 . 311 670 99 PHE CB C 40.931 0.055 . 312 670 99 PHE N N 119.900 0.048 . 313 671 100 HIS H H 7.846 0.008 . 314 671 100 HIS CA C 52.431 0.043 . 315 671 100 HIS CB C 29.773 0.000 . 316 671 100 HIS N N 122.319 0.049 . 317 672 101 PRO CA C 65.365 0.063 . 318 672 101 PRO CB C 30.548 0.029 . 319 673 102 ASP H H 8.633 0.007 . 320 673 102 ASP CA C 54.466 0.113 . 321 673 102 ASP CB C 39.632 0.384 . 322 673 102 ASP N N 111.202 0.035 . 323 674 103 ARG H H 7.479 0.008 . 324 674 103 ARG CA C 54.833 0.123 . 325 674 103 ARG CB C 30.186 0.099 . 326 674 103 ARG N N 117.075 0.084 . 327 675 104 VAL H H 7.108 0.007 . 328 675 104 VAL CA C 62.810 0.048 . 329 675 104 VAL CB C 30.988 0.033 . 330 675 104 VAL CG1 C 21.809 0.000 . 331 675 104 VAL CG2 C 19.724 0.000 . 332 675 104 VAL N N 124.186 0.063 . 333 676 105 LYS H H 8.071 0.010 . 334 676 105 LYS CA C 54.287 0.068 . 335 676 105 LYS CB C 36.191 0.075 . 336 676 105 LYS N N 124.738 0.152 . 337 677 106 ALA H H 8.676 0.009 . 338 677 106 ALA CA C 50.192 0.048 . 339 677 106 ALA CB C 22.496 0.052 . 340 677 106 ALA N N 126.428 0.057 . 341 678 107 ARG H H 8.613 0.007 . 342 678 107 ARG CA C 55.136 0.100 . 343 678 107 ARG CB C 33.713 0.109 . 344 678 107 ARG N N 117.996 0.056 . 345 679 108 GLY H H 8.617 0.007 . 346 679 108 GLY CA C 45.318 0.079 . 347 679 108 GLY N N 111.527 0.052 . 348 680 109 PRO CA C 65.191 0.117 . 349 680 109 PRO CB C 31.758 0.228 . 350 681 110 GLY H H 9.180 0.011 . 351 681 110 GLY CA C 46.246 0.104 . 352 681 110 GLY N N 101.899 0.047 . 353 682 111 LEU H H 7.408 0.011 . 354 682 111 LEU CA C 52.887 0.067 . 355 682 111 LEU CB C 41.185 0.108 . 356 682 111 LEU N N 115.261 0.046 . 357 683 112 GLU H H 7.109 0.008 . 358 683 112 GLU CA C 56.177 0.081 . 359 683 112 GLU CB C 30.748 0.033 . 360 683 112 GLU N N 121.670 0.056 . 361 684 113 LYS H H 8.587 0.006 . 362 684 113 LYS CA C 60.110 0.089 . 363 684 113 LYS CB C 33.237 0.093 . 364 684 113 LYS N N 119.262 0.046 . 365 685 114 THR H H 7.607 0.008 . 366 685 114 THR CA C 60.840 0.109 . 367 685 114 THR CB C 71.385 0.024 . 368 685 114 THR N N 106.801 0.076 . 369 686 115 GLY H H 8.415 0.006 . 370 686 115 GLY CA C 45.393 0.143 . 371 686 115 GLY N N 109.294 0.039 . 372 687 116 VAL H H 8.674 0.007 . 373 687 116 VAL CA C 64.166 0.090 . 374 687 116 VAL CB C 31.398 0.047 . 375 687 116 VAL N N 125.199 0.045 . 376 688 117 ALA H H 8.220 0.007 . 377 688 117 ALA CA C 50.485 0.111 . 378 688 117 ALA CB C 22.321 0.047 . 379 688 117 ALA N N 130.622 0.058 . 380 689 118 VAL H H 7.744 0.008 . 381 689 118 VAL CA C 62.566 0.183 . 382 689 118 VAL CB C 32.434 0.077 . 383 689 118 VAL N N 115.110 0.054 . 384 690 119 ASN H H 8.860 0.008 . 385 690 119 ASN CA C 55.243 0.100 . 386 690 119 ASN CB C 36.864 0.062 . 387 690 119 ASN N N 113.358 0.058 . 388 691 120 LYS H H 7.407 0.008 . 389 691 120 LYS CA C 52.817 0.037 . 390 691 120 LYS CB C 34.055 0.000 . 391 691 120 LYS N N 119.100 0.047 . 392 692 121 PRO CA C 63.888 0.022 . 393 692 121 PRO CB C 31.366 0.050 . 394 693 122 ALA H H 9.241 0.009 . 395 693 122 ALA CA C 50.680 0.158 . 396 693 122 ALA CB C 18.430 0.090 . 397 693 122 ALA N N 132.760 0.054 . 398 694 123 GLU H H 8.020 0.014 . 399 694 123 GLU CA C 55.487 0.098 . 400 694 123 GLU CB C 32.353 0.929 . 401 694 123 GLU N N 120.279 0.030 . 402 695 124 PHE H H 8.675 0.013 . 403 695 124 PHE CA C 57.159 0.085 . 404 695 124 PHE CB C 39.660 0.078 . 405 695 124 PHE N N 114.591 0.066 . 406 696 125 THR H H 9.170 0.008 . 407 696 125 THR CA C 60.764 0.167 . 408 696 125 THR CB C 72.026 0.078 . 409 696 125 THR N N 115.779 0.053 . 410 697 126 VAL H H 9.162 0.011 . 411 697 126 VAL CA C 61.603 0.125 . 412 697 126 VAL CB C 33.667 0.091 . 413 697 126 VAL N N 124.479 0.094 . 414 698 127 ASP H H 9.366 0.007 . 415 698 127 ASP CA C 53.282 0.117 . 416 698 127 ASP CB C 41.385 0.000 . 417 698 127 ASP N N 128.271 0.054 . 418 699 128 ALA H H 8.740 0.012 . 419 699 128 ALA CA C 50.194 0.156 . 420 699 128 ALA CB C 20.783 0.134 . 421 699 128 ALA N N 128.999 0.058 . 422 700 129 LYS H H 8.369 0.005 . 423 700 129 LYS CA C 60.684 0.055 . 424 700 129 LYS CB C 32.516 0.000 . 425 700 129 LYS N N 124.394 0.044 . 426 701 130 HIS CA C 54.869 0.099 . 427 701 130 HIS CB C 30.259 0.092 . 428 702 131 GLY H H 7.809 0.010 . 429 702 131 GLY CA C 46.316 0.041 . 430 702 131 GLY N N 104.688 0.054 . 431 703 132 GLY H H 9.072 0.006 . 432 703 132 GLY CA C 44.646 0.055 . 433 703 132 GLY N N 115.026 0.021 . 434 704 133 LYS H H 8.659 0.006 . 435 704 133 LYS CA C 55.887 0.065 . 436 704 133 LYS CB C 33.322 0.094 . 437 704 133 LYS N N 123.272 0.063 . 438 705 134 ALA H H 7.086 0.006 . 439 705 134 ALA CA C 50.007 0.081 . 440 705 134 ALA CB C 18.931 0.000 . 441 705 134 ALA N N 126.216 0.048 . 442 706 135 PRO CA C 61.813 0.143 . 443 706 135 PRO CB C 32.221 0.155 . 444 707 136 LEU H H 8.360 0.008 . 445 707 136 LEU CA C 53.786 0.082 . 446 707 136 LEU CB C 43.660 0.023 . 447 707 136 LEU N N 127.079 0.093 . 448 708 137 ARG H H 8.904 0.006 . 449 708 137 ARG CA C 55.549 0.064 . 450 708 137 ARG CB C 33.565 0.136 . 451 708 137 ARG N N 127.441 0.060 . 452 709 138 VAL H H 8.895 0.008 . 453 709 138 VAL CA C 61.396 0.096 . 454 709 138 VAL CB C 33.940 0.106 . 455 709 138 VAL N N 125.950 0.065 . 456 710 139 GLN H H 8.974 0.007 . 457 710 139 GLN CA C 54.534 0.124 . 458 710 139 GLN CB C 32.925 0.109 . 459 710 139 GLN N N 127.506 0.039 . 460 711 140 VAL H H 9.253 0.008 . 461 711 140 VAL CA C 60.670 0.210 . 462 711 140 VAL CB C 32.693 0.088 . 463 711 140 VAL N N 126.564 0.060 . 464 712 141 GLN H H 8.481 0.010 . 465 712 141 GLN CA C 53.836 0.047 . 466 712 141 GLN CB C 33.083 0.403 . 467 712 141 GLN N N 123.142 0.073 . 468 713 142 ASP H H 7.982 0.007 . 469 713 142 ASP CA C 52.742 0.083 . 470 713 142 ASP CB C 40.624 0.190 . 471 713 142 ASP N N 120.242 0.067 . 472 714 143 ASN H H 6.899 0.006 . 473 714 143 ASN CA C 54.749 0.136 . 474 714 143 ASN CB C 37.943 0.000 . 475 714 143 ASN N N 115.888 0.034 . 476 715 144 GLU CA C 55.185 0.159 . 477 715 144 GLU CB C 30.458 0.048 . 478 716 145 GLY H H 7.749 0.005 . 479 716 145 GLY CA C 44.921 0.021 . 480 716 145 GLY N N 107.732 0.058 . 481 717 146 CYS H H 8.276 0.007 . 482 717 146 CYS CA C 56.660 0.076 . 483 717 146 CYS CB C 26.850 0.000 . 484 717 146 CYS N N 122.097 0.064 . 485 718 147 PRO CA C 62.687 0.082 . 486 718 147 PRO CB C 32.598 0.037 . 487 719 148 VAL H H 8.241 0.007 . 488 719 148 VAL CA C 61.179 0.061 . 489 719 148 VAL CB C 33.885 0.192 . 490 719 148 VAL N N 125.451 0.036 . 491 720 149 GLU H H 8.701 0.005 . 492 720 149 GLU CA C 58.217 0.059 . 493 720 149 GLU CB C 30.200 0.081 . 494 720 149 GLU N N 127.365 0.050 . 495 721 150 ALA H H 8.448 0.005 . 496 721 150 ALA CA C 49.830 0.089 . 497 721 150 ALA CB C 20.290 0.045 . 498 721 150 ALA N N 126.595 0.050 . 499 722 151 LEU H H 9.244 0.012 . 500 722 151 LEU CA C 54.389 0.058 . 501 722 151 LEU CB C 42.945 0.065 . 502 722 151 LEU N N 126.498 0.101 . 503 723 152 VAL H H 8.488 0.006 . 504 723 152 VAL CA C 61.922 0.079 . 505 723 152 VAL CB C 34.633 0.031 . 506 723 152 VAL N N 124.447 0.047 . 507 724 153 LYS H H 8.917 0.006 . 508 724 153 LYS CA C 54.674 0.073 . 509 724 153 LYS CB C 34.647 0.067 . 510 724 153 LYS N N 129.074 0.040 . 511 725 154 ASP H H 8.794 0.002 . 512 725 154 ASP CA C 56.238 0.068 . 513 725 154 ASP CB C 41.118 0.063 . 514 725 154 ASP N N 125.559 0.000 . 515 726 155 ASN H H 8.283 0.007 . 516 726 155 ASN CA C 54.484 0.104 . 517 726 155 ASN CB C 38.127 0.052 . 518 726 155 ASN N N 125.146 0.097 . 519 727 156 GLY H H 9.266 0.007 . 520 727 156 GLY CA C 46.000 0.056 . 521 727 156 GLY N N 109.828 0.054 . 522 728 157 ASN H H 7.467 0.009 . 523 728 157 ASN CA C 51.250 0.041 . 524 728 157 ASN CB C 38.466 0.050 . 525 728 157 ASN N N 116.530 0.075 . 526 729 158 GLY H H 8.962 0.007 . 527 729 158 GLY CA C 45.361 0.108 . 528 729 158 GLY N N 109.491 0.061 . 529 730 159 THR H H 7.349 0.040 . 530 730 159 THR CA C 59.359 0.092 . 531 730 159 THR CB C 73.079 0.096 . 532 730 159 THR N N 106.550 0.196 . 533 731 160 TYR H H 9.054 0.005 . 534 731 160 TYR CA C 56.456 0.101 . 535 731 160 TYR CB C 41.601 0.040 . 536 731 160 TYR N N 118.080 0.037 . 537 732 161 SER H H 9.237 0.008 . 538 732 161 SER CA C 58.522 0.219 . 539 732 161 SER CB C 64.444 0.341 . 540 732 161 SER N N 121.740 0.066 . 541 733 162 CYS H H 8.840 0.004 . 542 733 162 CYS CA C 56.922 0.075 . 543 733 162 CYS CB C 33.878 0.109 . 544 733 162 CYS N N 124.223 0.000 . 545 734 163 SER H H 7.460 0.009 . 546 734 163 SER CA C 60.906 0.013 . 547 734 163 SER CB C 66.508 0.651 . 548 734 163 SER N N 116.454 0.039 . 549 735 164 TYR H H 8.257 0.000 . 550 735 164 TYR N N 116.881 0.000 . 551 737 166 PRO CA C 62.340 0.059 . 552 738 167 ARG H H 10.233 0.011 . 553 738 167 ARG CA C 54.950 0.110 . 554 738 167 ARG CB C 32.752 0.198 . 555 738 167 ARG N N 120.820 0.049 . 556 739 168 LYS H H 7.979 0.004 . 557 739 168 LYS N N 120.146 0.042 . 558 740 169 PRO CA C 62.034 0.000 . 559 740 169 PRO CB C 27.460 0.000 . 560 740 169 PRO CG C 27.594 0.000 . 561 741 170 VAL H H 8.072 0.013 . 562 741 170 VAL CA C 61.977 0.080 . 563 741 170 VAL CB C 27.349 0.127 . 564 741 170 VAL N N 113.779 0.000 . 565 742 171 LYS H H 8.078 0.008 . 566 742 171 LYS CA C 58.062 0.058 . 567 742 171 LYS CB C 32.010 0.125 . 568 742 171 LYS N N 113.885 0.067 . 569 743 172 HIS H H 9.637 0.006 . 570 743 172 HIS CA C 54.859 0.097 . 571 743 172 HIS CB C 31.749 0.150 . 572 743 172 HIS N N 124.803 0.061 . 573 744 173 THR H H 8.783 0.007 . 574 744 173 THR CA C 61.854 0.118 . 575 744 173 THR CB C 70.275 0.005 . 576 744 173 THR N N 117.625 0.051 . 577 745 174 ALA H H 9.601 0.008 . 578 745 174 ALA CA C 49.707 0.130 . 579 745 174 ALA CB C 20.201 0.082 . 580 745 174 ALA N N 129.021 0.049 . 581 746 175 MET H H 9.660 0.010 . 582 746 175 MET CA C 53.993 0.112 . 583 746 175 MET CB C 33.941 0.000 . 584 746 175 MET N N 124.570 0.050 . 585 747 176 VAL H H 8.730 0.005 . 586 747 176 VAL CA C 61.246 0.121 . 587 747 176 VAL CB C 34.061 0.046 . 588 747 176 VAL N N 128.168 0.022 . 589 748 177 SER H H 9.382 0.009 . 590 748 177 SER CA C 56.039 0.119 . 591 748 177 SER CB C 66.852 0.019 . 592 748 177 SER N N 120.048 0.046 . 593 749 178 TRP H H 9.265 0.008 . 594 749 178 TRP CA C 54.408 0.067 . 595 749 178 TRP CB C 33.046 0.120 . 596 749 178 TRP N N 124.859 0.053 . 597 750 179 GLY H H 9.050 0.008 . 598 750 179 GLY CA C 47.782 0.050 . 599 750 179 GLY N N 114.681 0.040 . 600 751 180 GLY H H 8.783 0.006 . 601 751 180 GLY CA C 44.317 0.079 . 602 751 180 GLY N N 101.660 0.047 . 603 752 181 VAL H H 7.555 0.008 . 604 752 181 VAL CA C 60.845 0.084 . 605 752 181 VAL CB C 34.199 0.146 . 606 752 181 VAL N N 120.058 0.036 . 607 753 182 SER H H 9.153 0.009 . 608 753 182 SER CA C 59.478 0.030 . 609 753 182 SER CB C 63.392 0.000 . 610 753 182 SER N N 122.837 0.115 . 611 754 183 ILE H H 7.735 0.006 . 612 754 183 ILE CA C 60.855 0.010 . 613 754 183 ILE CB C 35.432 0.000 . 614 754 183 ILE N N 120.980 0.020 . 615 755 184 PRO CA C 65.097 0.077 . 616 755 184 PRO CB C 31.408 0.030 . 617 756 185 ASN H H 8.383 0.008 . 618 756 185 ASN CA C 55.784 0.073 . 619 756 185 ASN CB C 37.591 0.095 . 620 756 185 ASN N N 113.811 0.045 . 621 757 186 SER H H 7.318 0.005 . 622 757 186 SER CA C 54.648 0.085 . 623 757 186 SER CB C 64.100 0.000 . 624 757 186 SER N N 112.074 0.051 . 625 758 187 PRO CA C 63.671 0.058 . 626 758 187 PRO CB C 32.289 0.000 . 627 759 188 PHE H H 7.859 0.005 . 628 759 188 PHE CA C 59.943 0.060 . 629 759 188 PHE CB C 41.239 0.119 . 630 759 188 PHE N N 119.279 0.027 . 631 760 189 ARG H H 8.750 0.006 . 632 760 189 ARG CA C 56.280 0.100 . 633 760 189 ARG CB C 30.749 0.120 . 634 760 189 ARG N N 127.774 0.021 . 635 761 190 VAL H H 9.242 0.008 . 636 761 190 VAL CA C 61.575 0.180 . 637 761 190 VAL CB C 36.109 0.202 . 638 761 190 VAL N N 126.681 0.038 . 639 762 191 ASN H H 8.410 0.009 . 640 762 191 ASN CA C 53.421 0.139 . 641 762 191 ASN CB C 38.303 0.092 . 642 762 191 ASN N N 125.136 0.096 . 643 763 192 VAL H H 7.105 0.008 . 644 763 192 VAL CA C 63.099 0.080 . 645 763 192 VAL CB C 31.685 0.087 . 646 763 192 VAL N N 127.033 0.051 . 647 764 193 GLY H H 8.637 0.008 . 648 764 193 GLY CA C 44.045 0.031 . 649 764 193 GLY N N 113.926 0.047 . 650 765 194 ALA H H 8.423 0.006 . 651 765 194 ALA CA C 52.797 0.036 . 652 765 194 ALA CB C 28.115 14.169 . 653 765 194 ALA N N 121.039 0.060 . 654 766 195 GLY H H 8.505 0.006 . 655 766 195 GLY CA C 44.858 0.079 . 656 766 195 GLY N N 106.856 0.031 . 657 767 196 SER H H 7.736 0.006 . 658 767 196 SER CA C 57.576 0.110 . 659 767 196 SER CB C 65.327 0.004 . 660 767 196 SER N N 114.702 0.020 . 661 768 197 HIS H H 9.120 0.006 . 662 768 197 HIS CA C 52.933 0.057 . 663 768 197 HIS CB C 30.297 0.000 . 664 768 197 HIS N N 120.910 0.026 . 665 769 198 PRO CA C 65.209 0.070 . 666 769 198 PRO CB C 31.567 0.024 . 667 770 199 ASN H H 8.525 0.011 . 668 770 199 ASN CA C 54.470 0.413 . 669 770 199 ASN CB C 36.508 0.123 . 670 770 199 ASN N N 109.944 0.069 . 671 771 200 LYS H H 7.886 0.026 . 672 771 200 LYS CA C 54.763 0.064 . 673 771 200 LYS CB C 32.671 0.035 . 674 771 200 LYS N N 117.638 0.042 . 675 772 201 VAL H H 7.129 0.018 . 676 772 201 VAL CA C 63.847 0.044 . 677 772 201 VAL CB C 32.231 0.188 . 678 772 201 VAL N N 122.939 0.033 . 679 773 202 LYS H H 8.403 0.006 . 680 773 202 LYS CA C 55.154 0.078 . 681 773 202 LYS CB C 35.598 0.025 . 682 773 202 LYS N N 128.107 0.028 . 683 774 203 VAL H H 8.433 0.006 . 684 774 203 VAL CA C 61.072 0.039 . 685 774 203 VAL CB C 33.948 0.046 . 686 774 203 VAL N N 123.301 0.053 . 687 775 204 TYR H H 8.564 0.004 . 688 775 204 TYR CA C 56.182 0.097 . 689 775 204 TYR CB C 39.394 0.130 . 690 775 204 TYR N N 123.257 0.095 . 691 776 205 GLY H H 8.600 0.009 . 692 776 205 GLY CA C 44.190 0.436 . 693 776 205 GLY N N 108.117 0.052 . 694 777 206 PRO CA C 65.637 0.077 . 695 777 206 PRO CB C 31.190 0.019 . 696 778 207 GLY H H 8.648 0.015 . 697 778 207 GLY CA C 47.075 0.034 . 698 778 207 GLY N N 101.215 0.040 . 699 779 208 VAL H H 6.893 0.021 . 700 779 208 VAL CA C 55.115 10.233 . 701 779 208 VAL CB C 30.155 0.060 . 702 779 208 VAL N N 106.738 0.025 . 703 780 209 ALA H H 7.116 0.021 . 704 780 209 ALA CA C 52.523 0.038 . 705 780 209 ALA CB C 19.962 0.000 . 706 780 209 ALA N N 125.812 0.019 . 707 781 210 LYS CA C 59.649 0.229 . 708 781 210 LYS CB C 33.127 0.073 . 709 782 211 THR H H 7.472 0.004 . 710 782 211 THR CA C 60.322 0.072 . 711 782 211 THR CB C 71.726 0.148 . 712 782 211 THR CG2 C 22.118 0.000 . 713 782 211 THR N N 106.915 0.078 . 714 783 212 GLY H H 8.676 0.009 . 715 783 212 GLY CA C 45.333 0.058 . 716 783 212 GLY N N 108.073 0.036 . 717 784 213 LEU H H 8.698 0.010 . 718 784 213 LEU CA C 55.864 0.063 . 719 784 213 LEU CB C 43.454 0.047 . 720 784 213 LEU N N 123.624 0.026 . 721 785 214 LYS H H 8.119 0.006 . 722 785 214 LYS CA C 54.265 0.065 . 723 785 214 LYS CB C 35.099 0.016 . 724 785 214 LYS N N 119.814 0.017 . 725 786 215 ALA H H 8.180 0.005 . 726 786 215 ALA CA C 53.170 0.081 . 727 786 215 ALA CB C 18.846 0.037 . 728 786 215 ALA N N 124.234 0.030 . 729 787 216 HIS H H 7.679 0.006 . 730 787 216 HIS CA C 58.098 0.011 . 731 787 216 HIS CB C 27.707 0.000 . 732 787 216 HIS N N 110.872 0.067 . 733 789 218 PRO CA C 63.462 0.041 . 734 789 218 PRO CB C 32.487 0.043 . 735 790 219 THR H H 8.752 0.016 . 736 790 219 THR HG2 H 0.453 0.000 . 737 790 219 THR CA C 60.456 0.064 . 738 790 219 THR CB C 69.502 0.066 . 739 790 219 THR CG2 C 17.874 0.000 . 740 790 219 THR N N 118.549 0.044 . 741 791 220 TYR H H 8.266 0.017 . 742 791 220 TYR CA C 55.815 0.036 . 743 791 220 TYR CB C 41.263 0.144 . 744 791 220 TYR N N 117.453 0.046 . 745 792 221 PHE H H 9.290 0.007 . 746 792 221 PHE CA C 56.568 0.085 . 747 792 221 PHE CB C 41.618 0.071 . 748 792 221 PHE N N 115.096 0.051 . 749 793 222 THR H H 9.472 0.006 . 750 793 222 THR CA C 62.107 0.111 . 751 793 222 THR CB C 70.875 0.048 . 752 793 222 THR CG2 C 22.243 0.000 . 753 793 222 THR N N 118.197 0.022 . 754 794 223 VAL H H 9.062 0.006 . 755 794 223 VAL CA C 61.582 0.126 . 756 794 223 VAL CB C 33.370 0.041 . 757 794 223 VAL CG1 C 21.555 0.000 . 758 794 223 VAL CG2 C 21.555 0.000 . 759 794 223 VAL N N 124.559 0.030 . 760 795 224 ASP H H 9.795 0.007 . 761 795 224 ASP CA C 53.755 0.041 . 762 795 224 ASP CB C 43.024 0.165 . 763 795 224 ASP N N 128.357 0.033 . 764 796 225 CYS H H 8.747 0.012 . 765 796 225 CYS CA C 57.798 0.069 . 766 796 225 CYS CB C 28.344 0.062 . 767 796 225 CYS N N 124.306 0.071 . 768 797 226 ALA H H 8.737 0.005 . 769 797 226 ALA CA C 55.621 2.090 . 770 797 226 ALA CB C 18.996 0.021 . 771 797 226 ALA N N 126.856 0.028 . 772 798 227 GLU H H 8.579 0.176 . 773 798 227 GLU CA C 55.356 0.060 . 774 798 227 GLU CB C 30.822 0.009 . 775 798 227 GLU N N 114.628 1.778 . 776 799 228 ALA H H 7.285 0.011 . 777 799 228 ALA CA C 52.614 0.076 . 778 799 228 ALA CB C 21.575 0.040 . 779 799 228 ALA N N 120.701 0.036 . 780 800 229 GLY H H 8.340 0.005 . 781 800 229 GLY CA C 45.019 0.108 . 782 800 229 GLY N N 107.156 0.020 . 783 801 230 GLN H H 8.372 0.011 . 784 801 230 GLN CA C 55.731 0.043 . 785 801 230 GLN CB C 30.307 0.025 . 786 801 230 GLN N N 121.835 0.102 . 787 802 231 GLY H H 8.158 0.005 . 788 802 231 GLY CA C 44.551 0.042 . 789 802 231 GLY N N 112.067 0.044 . 790 803 232 ASP H H 7.782 0.021 . 791 803 232 ASP CA C 52.481 0.066 . 792 803 232 ASP CB C 42.827 0.052 . 793 803 232 ASP N N 117.249 0.022 . 794 804 233 VAL H H 8.240 0.006 . 795 804 233 VAL CA C 60.779 0.059 . 796 804 233 VAL CB C 33.807 0.000 . 797 804 233 VAL N N 122.483 0.022 . 798 805 234 SER CA C 60.736 0.059 . 799 805 234 SER CB C 65.381 0.471 . 800 806 235 ILE H H 8.642 0.009 . 801 806 235 ILE CA C 57.093 0.125 . 802 806 235 ILE CB C 39.262 0.078 . 803 806 235 ILE N N 121.447 0.047 . 804 807 236 GLY H H 8.211 0.042 . 805 807 236 GLY CA C 45.362 0.011 . 806 807 236 GLY N N 112.188 0.235 . 807 810 239 CYS CA C 56.694 0.064 . 808 810 239 CYS CB C 43.835 0.051 . 809 811 240 ALA H H 8.465 0.005 . 810 811 240 ALA CA C 53.001 0.021 . 811 811 240 ALA CB C 16.694 0.000 . 812 811 240 ALA N N 129.546 0.026 . 813 812 241 PRO CA C 58.578 0.053 . 814 812 241 PRO CB C 28.154 0.078 . 815 813 242 GLY H H 8.447 0.010 . 816 813 242 GLY CA C 45.549 0.089 . 817 813 242 GLY N N 111.130 0.040 . 818 814 243 VAL H H 7.665 0.021 . 819 814 243 VAL CA C 66.311 0.044 . 820 814 243 VAL CB C 31.828 0.133 . 821 814 243 VAL N N 121.997 0.031 . 822 815 244 VAL H H 8.443 0.006 . 823 815 244 VAL CA C 60.934 0.050 . 824 815 244 VAL CB C 33.016 0.023 . 825 815 244 VAL N N 112.523 0.043 . 826 816 245 GLY H H 7.536 0.007 . 827 816 245 GLY CA C 44.832 0.060 . 828 816 245 GLY N N 110.538 0.016 . 829 817 246 PRO CA C 64.380 0.094 . 830 817 246 PRO CB C 32.166 0.109 . 831 818 247 ALA H H 7.764 0.013 . 832 818 247 ALA HB H 1.394 0.000 . 833 818 247 ALA CA C 50.091 0.054 . 834 818 247 ALA CB C 21.629 0.052 . 835 818 247 ALA N N 120.101 0.039 . 836 819 248 GLU H H 8.590 0.004 . 837 819 248 GLU CA C 57.105 0.121 . 838 819 248 GLU CB C 30.814 0.118 . 839 819 248 GLU CG C 36.949 0.000 . 840 819 248 GLU N N 121.301 0.031 . 841 820 249 ALA H H 7.744 0.016 . 842 820 249 ALA HB H 1.226 0.000 . 843 820 249 ALA CA C 50.940 0.065 . 844 820 249 ALA CB C 22.857 0.035 . 845 820 249 ALA N N 124.945 0.078 . 846 821 250 ASP H H 8.170 0.005 . 847 821 250 ASP CA C 54.462 0.058 . 848 821 250 ASP CB C 42.522 0.000 . 849 821 250 ASP N N 119.348 0.022 . 850 822 251 ILE CA C 60.691 0.143 . 851 823 252 ASP H H 8.704 0.005 . 852 823 252 ASP CA C 54.825 0.078 . 853 823 252 ASP CB C 41.794 0.142 . 854 823 252 ASP N N 114.837 0.040 . 855 824 253 PHE H H 7.516 0.006 . 856 824 253 PHE CA C 56.235 0.089 . 857 824 253 PHE CB C 41.641 0.000 . 858 824 253 PHE N N 114.440 0.049 . 859 825 254 ASP H H 8.364 0.007 . 860 825 254 ASP CA C 53.870 0.066 . 861 825 254 ASP CB C 42.110 0.050 . 862 825 254 ASP N N 123.054 0.035 . 863 826 255 ILE H H 8.363 0.006 . 864 826 255 ILE CA C 59.659 0.094 . 865 826 255 ILE CB C 40.918 0.238 . 866 826 255 ILE N N 124.527 0.032 . 867 827 256 ILE H H 9.344 0.007 . 868 827 256 ILE HD1 H 0.809 0.000 . 869 827 256 ILE CA C 60.113 0.058 . 870 827 256 ILE CB C 41.319 0.008 . 871 827 256 ILE CG1 C 28.028 0.000 . 872 827 256 ILE CG2 C 18.028 0.000 . 873 827 256 ILE CD1 C 13.809 0.004 . 874 827 256 ILE N N 129.774 0.020 . 875 828 257 ARG CA C 53.512 0.095 . 876 828 257 ARG CB C 30.780 0.013 . 877 829 258 ASN H H 8.284 0.005 . 878 829 258 ASN CA C 52.590 0.097 . 879 829 258 ASN CB C 40.054 0.134 . 880 829 258 ASN N N 125.151 0.095 . 881 830 259 ASP H H 8.422 0.005 . 882 830 259 ASP CA C 55.326 0.118 . 883 830 259 ASP CB C 40.281 0.059 . 884 830 259 ASP N N 118.452 0.037 . 885 831 260 ASN H H 7.844 0.012 . 886 831 260 ASN CA C 52.465 0.092 . 887 831 260 ASN CB C 37.289 0.065 . 888 831 260 ASN N N 117.113 0.053 . 889 832 261 ASP H H 8.169 0.005 . 890 832 261 ASP CA C 56.196 0.071 . 891 832 261 ASP CB C 39.200 0.048 . 892 832 261 ASP N N 112.435 0.032 . 893 833 262 THR H H 6.914 0.007 . 894 833 262 THR HG2 H 1.195 0.000 . 895 833 262 THR CA C 59.842 0.072 . 896 833 262 THR CB C 73.856 0.053 . 897 833 262 THR CG2 C 20.719 0.007 . 898 833 262 THR N N 103.369 0.040 . 899 834 263 PHE H H 9.180 0.006 . 900 834 263 PHE CA C 56.245 0.077 . 901 834 263 PHE CB C 41.975 0.026 . 902 834 263 PHE N N 118.382 0.024 . 903 835 264 THR H H 9.431 0.016 . 904 835 264 THR HG2 H 1.141 0.003 . 905 835 264 THR CA C 62.116 0.085 . 906 835 264 THR CB C 70.505 0.061 . 907 835 264 THR CG2 C 22.375 0.040 . 908 835 264 THR N N 120.804 0.034 . 909 836 265 VAL H H 9.121 0.014 . 910 836 265 VAL HG1 H 0.426 0.000 . 911 836 265 VAL CA C 60.577 0.082 . 912 836 265 VAL CB C 31.490 0.028 . 913 836 265 VAL CG1 C 22.170 0.000 . 914 836 265 VAL CG2 C 21.884 0.575 . 915 836 265 VAL N N 128.780 0.022 . 916 837 266 LYS H H 8.973 0.006 . 917 837 266 LYS CA C 55.271 0.122 . 918 837 266 LYS CB C 35.330 0.144 . 919 837 266 LYS N N 125.263 0.024 . 920 838 267 TYR H H 8.284 0.005 . 921 838 267 TYR CA C 56.843 0.050 . 922 838 267 TYR CB C 41.728 0.087 . 923 838 267 TYR N N 120.065 0.068 . 924 839 268 THR H H 8.975 0.020 . 925 839 268 THR HG2 H 0.845 0.003 . 926 839 268 THR CA C 58.430 0.060 . 927 839 268 THR CB C 70.895 0.052 . 928 839 268 THR CG2 C 20.453 0.004 . 929 839 268 THR N N 117.285 0.032 . 930 840 269 PRO CA C 62.639 0.053 . 931 840 269 PRO CB C 32.192 0.043 . 932 841 270 ARG H H 7.515 0.005 . 933 841 270 ARG CA C 54.749 0.069 . 934 841 270 ARG CB C 29.070 0.029 . 935 841 270 ARG CG C 26.780 0.000 . 936 841 270 ARG CD C 43.739 0.000 . 937 841 270 ARG N N 123.829 0.026 . 938 842 271 GLY H H 6.924 0.017 . 939 842 271 GLY CA C 44.421 0.068 . 940 842 271 GLY N N 102.646 0.093 . 941 843 272 ALA H H 8.575 0.005 . 942 843 272 ALA HB H 1.283 0.000 . 943 843 272 ALA CA C 52.348 0.063 . 944 843 272 ALA CB C 19.563 0.157 . 945 843 272 ALA N N 122.830 0.061 . 946 844 273 GLY H H 8.619 0.039 . 947 844 273 GLY CA C 44.408 0.064 . 948 844 273 GLY N N 107.274 0.109 . 949 845 274 SER H H 8.246 0.010 . 950 845 274 SER CA C 59.156 0.094 . 951 845 274 SER CB C 63.839 0.013 . 952 845 274 SER N N 117.067 0.030 . 953 846 275 TYR H H 9.217 0.011 . 954 846 275 TYR CA C 56.575 0.100 . 955 846 275 TYR CB C 40.763 0.038 . 956 846 275 TYR N N 126.005 0.042 . 957 847 276 THR H H 9.156 0.015 . 958 847 276 THR HG2 H 0.977 0.000 . 959 847 276 THR CA C 61.602 0.096 . 960 847 276 THR CB C 71.067 0.133 . 961 847 276 THR CG2 C 22.443 0.120 . 962 847 276 THR N N 116.821 0.036 . 963 848 277 ILE H H 9.520 0.006 . 964 848 277 ILE HG2 H 0.448 0.000 . 965 848 277 ILE CA C 60.588 0.065 . 966 848 277 ILE CB C 40.433 0.029 . 967 848 277 ILE CG1 C 21.644 7.109 . 968 848 277 ILE CG2 C 17.576 0.000 . 969 848 277 ILE CD1 C 14.535 0.010 . 970 848 277 ILE N N 129.219 0.064 . 971 849 278 MET H H 9.282 0.006 . 972 849 278 MET CA C 53.423 0.095 . 973 849 278 MET CB C 34.229 0.078 . 974 849 278 MET N N 127.737 0.017 . 975 850 279 VAL H H 8.305 0.005 . 976 850 279 VAL HG1 H 0.690 0.004 . 977 850 279 VAL CA C 61.557 0.102 . 978 850 279 VAL CB C 32.507 0.006 . 979 850 279 VAL CG1 C 21.307 0.000 . 980 850 279 VAL CG2 C 20.120 0.082 . 981 850 279 VAL N N 123.377 0.046 . 982 851 280 LEU H H 9.113 0.005 . 983 851 280 LEU HD1 H 0.581 0.000 . 984 851 280 LEU CA C 53.130 0.070 . 985 851 280 LEU CB C 44.072 0.066 . 986 851 280 LEU CG C 27.876 0.000 . 987 851 280 LEU CD1 C 24.959 0.000 . 988 851 280 LEU CD2 C 23.540 0.011 . 989 851 280 LEU N N 128.491 0.038 . 990 852 281 PHE H H 9.184 0.009 . 991 852 281 PHE CA C 56.717 0.092 . 992 852 281 PHE CB C 43.873 0.020 . 993 852 281 PHE N N 120.286 0.028 . 994 853 282 ALA H H 8.463 0.012 . 995 853 282 ALA CA C 53.045 0.103 . 996 853 282 ALA CB C 16.766 0.025 . 997 853 282 ALA N N 129.357 0.004 . 998 854 283 ASP H H 8.882 0.005 . 999 854 283 ASP CA C 56.364 0.109 . 1000 854 283 ASP CB C 40.095 0.017 . 1001 854 283 ASP N N 109.443 0.018 . 1002 855 284 GLN H H 7.744 0.015 . 1003 855 284 GLN CA C 54.205 0.096 . 1004 855 284 GLN CB C 32.401 0.087 . 1005 855 284 GLN N N 118.596 0.040 . 1006 856 285 ALA H H 8.648 0.012 . 1007 856 285 ALA HB H 1.355 0.000 . 1008 856 285 ALA CA C 53.515 0.157 . 1009 856 285 ALA CB C 18.706 0.040 . 1010 856 285 ALA N N 125.267 0.021 . 1011 857 286 THR H H 7.682 0.006 . 1012 857 286 THR HG2 H 1.241 0.004 . 1013 857 286 THR CA C 61.088 0.044 . 1014 857 286 THR CB C 67.177 0.036 . 1015 857 286 THR CG2 C 22.412 0.018 . 1016 857 286 THR N N 112.481 0.077 . 1017 858 287 PRO CA C 66.791 0.103 . 1018 858 287 PRO CB C 32.923 0.056 . 1019 859 288 THR H H 8.225 0.014 . 1020 859 288 THR HG2 H 1.235 0.000 . 1021 859 288 THR CA C 60.751 0.079 . 1022 859 288 THR CB C 69.255 0.063 . 1023 859 288 THR CG2 C 22.148 0.024 . 1024 859 288 THR N N 105.625 0.070 . 1025 860 289 SER H H 7.473 0.009 . 1026 860 289 SER CA C 57.767 0.072 . 1027 860 289 SER CB C 64.397 0.000 . 1028 860 289 SER N N 116.897 0.077 . 1029 861 290 PRO CA C 62.287 0.041 . 1030 861 290 PRO CB C 34.530 0.002 . 1031 862 291 ILE H H 9.388 0.008 . 1032 862 291 ILE HD1 H 0.481 0.000 . 1033 862 291 ILE CA C 61.598 0.087 . 1034 862 291 ILE CB C 39.769 0.048 . 1035 862 291 ILE CG1 C 28.356 0.000 . 1036 862 291 ILE CG2 C 18.300 0.000 . 1037 862 291 ILE CD1 C 14.805 0.001 . 1038 862 291 ILE N N 126.042 0.025 . 1039 863 292 ARG H H 8.475 0.009 . 1040 863 292 ARG CA C 55.236 0.054 . 1041 863 292 ARG CB C 30.500 0.026 . 1042 863 292 ARG N N 128.044 0.036 . 1043 864 293 VAL H H 8.798 0.005 . 1044 864 293 VAL HG1 H 1.955 0.003 . 1045 864 293 VAL CA C 60.009 0.080 . 1046 864 293 VAL CB C 35.414 0.072 . 1047 864 293 VAL CG1 C 21.640 0.000 . 1048 864 293 VAL CG2 C 8.208 5.725 . 1049 864 293 VAL N N 121.338 0.019 . 1050 865 294 LYS H H 8.100 0.005 . 1051 865 294 LYS CA C 55.197 0.074 . 1052 865 294 LYS CB C 34.099 0.010 . 1053 865 294 LYS N N 124.613 0.022 . 1054 866 295 VAL H H 9.093 0.008 . 1055 866 295 VAL HG1 H 0.373 0.000 . 1056 866 295 VAL CA C 61.706 0.059 . 1057 866 295 VAL CB C 32.841 0.019 . 1058 866 295 VAL CG1 C 22.229 0.000 . 1059 866 295 VAL CG2 C 22.013 0.507 . 1060 866 295 VAL N N 129.506 0.071 . 1061 868 297 PRO CA C 61.279 0.123 . 1062 868 297 PRO CB C 29.615 0.000 . 1063 869 298 SER H H 8.708 0.011 . 1064 869 298 SER CA C 62.114 0.122 . 1065 869 298 SER CB C 71.344 0.000 . 1066 869 298 SER N N 123.709 0.030 . stop_ save_