data_28111

#######################
#  Entry information  #
#######################

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title
;
Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of ALIX-PRD
;
   _BMRB_accession_number   28111
   _BMRB_flat_file_name     bmr28111.str
   _Entry_type              original
   _Submission_date         2020-03-27
   _Accession_date          2020-03-27
   _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 Deshmukh Lalit .  .
      2 Elias    Ruben D. .

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"   73
      "13C chemical shifts" 292
      "15N chemical shifts" 106

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2020-11-30 update   BMRB   'update entry citation'
      2020-08-31 original author 'original release'

   stop_

   _Original_release_date   2020-03-27

save_


#############################
#  Citation for this entry  #
#############################

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title
;
Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    32917811

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Elias      Ruben   D. .
      2 Ma         Wen     .  .
      3 Ghirlando  Rodolfo .  .
      4 Schwieters Charles D. .
      5 Reddy      Vijay   .  .
      6 Deshmukh   Lalit   .  .

   stop_

   _Journal_abbreviation        'Proc. Natl. Acad. Sci. U. S. A.'
   _Journal_volume               117
   _Journal_issue                39
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   24274
   _Page_last                    24284
   _Year                         2020
   _Details                      .

   loop_
      _Keyword

       ALIX
      'CPMG relaxation dispersion'
       ESCRT
      'Intrinsically disordered protein'
      'Proline-rich domain'
      'carbon-detected NMR'

   stop_

save_


##################################
#  Molecular system description  #
##################################

save_assembly
   _Saveframe_category         molecular_system

   _Mol_system_name            ALIX
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      ALIX $ALIX

   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_ALIX
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 ALIX
   _Molecular_mass                              .
   _Mol_thiol_state                             unknown
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################

      _Residue_count                               107
   _Mol_residue_sequence
;
GDELLKDLQQSIAREPSAPS
IPTPAYQSSPAGGHAPTPPT
PAPRTMPPTKPQPPARPPPP
VLPANRAPSATAPSPVGAGT
AAPAPSQTPGSAPPPQAQGW
SHPQFEK
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

        1 702 GLY    2 703 ASP    3 704 GLU    4 705 LEU    5 706 LEU
        6 707 LYS    7 708 ASP    8 709 LEU    9 710 GLN   10 711 GLN
       11 712 SER   12 713 ILE   13 714 ALA   14 715 ARG   15 716 GLU
       16 717 PRO   17 718 SER   18 719 ALA   19 720 PRO   20 721 SER
       21 722 ILE   22 723 PRO   23 724 THR   24 725 PRO   25 726 ALA
       26 727 TYR   27 728 GLN   28 729 SER   29 730 SER   30 731 PRO
       31 732 ALA   32 733 GLY   33 734 GLY   34 735 HIS   35 736 ALA
       36 737 PRO   37 738 THR   38 739 PRO   39 740 PRO   40 741 THR
       41 742 PRO   42 743 ALA   43 744 PRO   44 745 ARG   45 746 THR
       46 747 MET   47 748 PRO   48 749 PRO   49 750 THR   50 751 LYS
       51 752 PRO   52 753 GLN   53 754 PRO   54 755 PRO   55 756 ALA
       56 757 ARG   57 758 PRO   58 759 PRO   59 760 PRO   60 761 PRO
       61 762 VAL   62 763 LEU   63 764 PRO   64 765 ALA   65 766 ASN
       66 767 ARG   67 768 ALA   68 769 PRO   69 770 SER   70 771 ALA
       71 772 THR   72 773 ALA   73 774 PRO   74 775 SER   75 776 PRO
       76 777 VAL   77 778 GLY   78 779 ALA   79 780 GLY   80 781 THR
       81 782 ALA   82 783 ALA   83 784 PRO   84 785 ALA   85 786 PRO
       86 787 SER   87 788 GLN   88 789 THR   89 790 PRO   90 791 GLY
       91 792 SER   92 793 ALA   93 794 PRO   94 795 PRO   95 796 PRO
       96 797 GLN   97 798 ALA   98 799 GLN   99 800 GLY  100 801 TRP
      101 802 SER  102 803 HIS  103 804 PRO  104 805 GLN  105 806 PHE
      106 807 GLU  107 808 LYS

   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

      UniProt Q8WUM4 'apoptosis-linked gene-2 interacting protein X' . . . . .

   stop_

save_


    ####################
    #  Natural source  #
    ####################

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $ALIX Human 9606 Eukaryota Metazoa Homo sapiens

   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

      $ALIX 'recombinant technology' . Escherichia coli . pet11a

   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

      $ALIX               1.5 mM '[U-100% 13C; U-100% 15N]'
       D2O                7   %  '[U-100% 2H]'
      'sodium phosphate' 20   mM 'natural abundance'
      'sodium chloride'  50   mM 'natural abundance'
       EDTA               2   mM 'natural abundance'
       TCEP               1   mM 'natural abundance'

   stop_

save_


############################
#  Computer software used  #
############################

save_CCPN
   _Saveframe_category   software

   _Name                 CCPN
   _Version              .

   loop_
      _Vendor
      _Address
      _Electronic_address

      CCPN . .

   stop_

   loop_
      _Task

      'data analysis'

   stop_

   _Details              .

save_


#########################
#  Experimental detail  #
#########################

    ##################################
    #  NMR Spectrometer definitions  #
    ##################################

save_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _Field_strength       800
   _Details              .

save_


save_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _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_HN(CA)CO_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HN(CA)CO'
   _Sample_label        $sample_1

save_


save_3D_(HACA)N(CA)CON_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D (HACA)N(CA)CON'
   _Sample_label        $sample_1

save_


save_2D_CON_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D CON'
   _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'  50   . mM
       pH                6.5 . 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

      water C 13 protons ppm 4.7 internal indirect . other . 0.251449530
      water H  1 protons ppm 4.7 internal direct   . other . 1.000000000
      water N 15 protons ppm 4.7 internal indirect . other . 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                         'TROSY offset'

   loop_
      _Software_label

      $CCPN

   stop_

   loop_
      _Experiment_label

      '2D 1H-15N HSQC'
      '3D HNCACB'
      '3D (HACA)N(CA)CON'
      '2D CON'

   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        ALIX
   _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

        1 703   2 ASP C  C 176.494 0.000 .
        2 703   2 ASP CA C  54.586 0.000 .
        3 703   2 ASP CB C  40.996 0.000 .
        4 703   2 ASP N  N 121.838 0.000 .
        5 704   3 GLU H  H   8.711 0.000 .
        6 704   3 GLU C  C 176.822 0.000 .
        7 704   3 GLU CA C  57.503 0.000 .
        8 704   3 GLU CB C  29.329 0.000 .
        9 704   3 GLU N  N 122.401 0.051 .
       10 705   4 LEU H  H   8.154 0.000 .
       11 705   4 LEU C  C 177.620 0.000 .
       12 705   4 LEU CA C  55.448 0.000 .
       13 705   4 LEU CB C  41.924 0.000 .
       14 705   4 LEU N  N 122.918 0.012 .
       15 706   5 LEU H  H   7.950 0.000 .
       16 706   5 LEU C  C 177.629 0.000 .
       17 706   5 LEU CA C  55.382 0.000 .
       18 706   5 LEU CB C  41.858 0.000 .
       19 706   5 LEU N  N 122.743 0.028 .
       20 707   6 LYS H  H   7.983 0.000 .
       21 707   6 LYS C  C 176.598 0.000 .
       22 707   6 LYS CA C  56.840 0.000 .
       23 707   6 LYS CB C  32.842 0.000 .
       24 707   6 LYS N  N 121.980 0.014 .
       25 708   7 ASP H  H   8.123 0.000 .
       26 708   7 ASP C  C 176.687 0.000 .
       27 708   7 ASP CA C  54.586 0.000 .
       28 708   7 ASP CB C  40.863 0.000 .
       29 708   7 ASP N  N 121.077 0.022 .
       30 709   8 LEU H  H   8.007 0.000 .
       31 709   8 LEU C  C 177.976 0.000 .
       32 709   8 LEU CA C  55.686 0.000 .
       33 709   8 LEU CB C  42.016 0.000 .
       34 709   8 LEU N  N 122.992 0.010 .
       35 710   9 GLN H  H   8.205 0.000 .
       36 710   9 GLN C  C 176.457 0.000 .
       37 710   9 GLN CA C  56.310 0.000 .
       38 710   9 GLN CB C  28.798 0.000 .
       39 710   9 GLN N  N 120.569 0.043 .
       40 711  10 GLN H  H   8.135 0.000 .
       41 711  10 GLN C  C 176.252 0.000 .
       42 711  10 GLN CA C  56.243 0.000 .
       43 711  10 GLN CB C  29.130 0.000 .
       44 711  10 GLN N  N 120.937 0.013 .
       45 712  11 SER H  H   8.177 0.000 .
       46 712  11 SER C  C 174.616 0.000 .
       47 712  11 SER CA C  58.564 0.000 .
       48 712  11 SER CB C  63.668 0.000 .
       49 712  11 SER N  N 117.339 0.015 .
       50 713  12 ILE H  H   7.913 0.000 .
       51 713  12 ILE C  C 175.977 0.000 .
       52 713  12 ILE CA C  61.149 0.000 .
       53 713  12 ILE CB C  38.676 0.000 .
       54 713  12 ILE N  N 122.763 0.000 .
       55 714  13 ALA H  H   8.155 0.000 .
       56 714  13 ALA C  C 177.424 0.000 .
       57 714  13 ALA CA C  52.398 0.000 .
       58 714  13 ALA CB C  18.921 0.000 .
       59 714  13 ALA N  N 128.442 0.016 .
       60 715  14 ARG H  H   8.104 0.000 .
       61 715  14 ARG C  C 176.136 0.000 .
       62 715  14 ARG CA C  55.713 0.000 .
       63 715  14 ARG CB C  30.920 0.000 .
       64 715  14 ARG N  N 121.331 0.035 .
       65 716  15 GLU H  H   8.311 0.000 .
       66 716  15 GLU C  C 174.813 0.000 .
       67 716  15 GLU CA C  54.443 0.000 .
       68 716  15 GLU CB C  29.395 0.000 .
       69 716  15 GLU N  N 124.220 0.022 .
       70 717  16 PRO C  C 177.029 0.000 .
       71 717  16 PRO CA C  63.151 0.000 .
       72 717  16 PRO N  N 137.886 0.000 .
       73 718  17 SER H  H   8.220 0.000 .
       74 718  17 SER C  C 173.943 0.000 .
       75 718  17 SER CA C  58.100 0.000 .
       76 718  17 SER CB C  63.867 0.000 .
       77 718  17 SER N  N 116.363 0.017 .
       78 719  18 ALA H  H   8.130 0.000 .
       79 719  18 ALA C  C 175.494 0.000 .
       80 719  18 ALA CA C  50.476 0.000 .
       81 719  18 ALA CB C  18.125 0.000 .
       82 719  18 ALA N  N 127.614 0.008 .
       83 720  19 PRO C  C 176.976 0.000 .
       84 720  19 PRO CA C  62.997 0.000 .
       85 720  19 PRO CB C  31.987 0.000 .
       86 720  19 PRO N  N 136.307 0.000 .
       87 721  20 SER H  H   8.275 0.000 .
       88 721  20 SER C  C 174.255 0.000 .
       89 721  20 SER CA C  58.100 0.000 .
       90 721  20 SER CB C  63.734 0.000 .
       91 721  20 SER N  N 116.989 0.033 .
       92 722  21 ILE H  H   8.006 0.000 .
       93 722  21 ILE C  C 174.607 0.000 .
       94 722  21 ILE CA C  58.497 0.000 .
       95 722  21 ILE CB C  38.742 0.000 .
       96 722  21 ILE N  N 124.519 0.040 .
       97 723  22 PRO C  C 176.797 0.000 .
       98 723  22 PRO CA C  63.138 0.000 .
       99 723  22 PRO CB C  31.914 0.000 .
      100 723  22 PRO N  N 140.346 0.000 .
      101 724  23 THR H  H   8.135 0.000 .
      102 724  23 THR C  C 173.103 0.000 .
      103 724  23 THR CA C  60.022 0.000 .
      104 724  23 THR CB C  69.833 0.000 .
      105 724  23 THR N  N 118.076 0.021 .
      106 725  24 PRO C  C 176.659 0.000 .
      107 725  24 PRO CA C  63.204 0.000 .
      108 725  24 PRO CB C  31.914 0.000 .
      109 725  24 PRO N  N 139.859 0.000 .
      110 726  25 ALA H  H   8.204 0.000 .
      111 726  25 ALA C  C 177.634 0.000 .
      112 726  25 ALA CA C  52.531 0.000 .
      113 726  25 ALA CB C  18.921 0.000 .
      114 726  25 ALA N  N 124.699 0.022 .
      115 727  26 TYR H  H   7.890 0.000 .
      116 727  26 TYR C  C 175.733 0.000 .
      117 727  26 TYR CA C  57.768 0.000 .
      118 727  26 TYR CB C  38.543 0.000 .
      119 727  26 TYR N  N 119.474 0.030 .
      120 728  27 GLN H  H   8.035 0.000 .
      121 728  27 GLN C  C 175.489 0.000 .
      122 728  27 GLN CA C  55.647 0.000 .
      123 728  27 GLN CB C  29.594 0.000 .
      124 728  27 GLN N  N 122.945 0.010 .
      125 729  28 SER C  C 174.262 0.000 .
      126 729  28 SER CA C  58.328 0.000 .
      127 729  28 SER CB C  63.760 0.000 .
      128 729  28 SER N  N 117.948 0.000 .
      129 730  29 SER H  H   8.189 0.000 .
      130 730  29 SER C  C 172.909 0.000 .
      131 730  29 SER CA C  56.352 0.000 .
      132 730  29 SER CB C  63.486 0.000 .
      133 730  29 SER N  N 119.155 0.018 .
      134 731  30 PRO C  C 177.020 0.000 .
      135 731  30 PRO CA C  63.469 0.000 .
      136 731  30 PRO N  N 138.939 0.000 .
      137 732  31 ALA H  H   8.259 0.000 .
      138 732  31 ALA C  C 178.466 0.000 .
      139 732  31 ALA CA C  52.660 0.000 .
      140 732  31 ALA CB C  18.854 0.000 .
      141 732  31 ALA N  N 124.802 0.006 .
      142 733  32 GLY H  H   8.209 0.000 .
      143 733  32 GLY C  C 174.809 0.000 .
      144 733  32 GLY CA C  45.242 0.000 .
      145 733  32 GLY N  N 108.794 0.000 .
      146 734  33 GLY H  H   8.064 0.000 .
      147 734  33 GLY C  C 173.895 0.000 .
      148 734  33 GLY CA C  45.106 0.000 .
      149 734  33 GLY N  N 108.912 0.003 .
      150 735  34 HIS C  C 174.507 0.000 .
      151 735  34 HIS CA C  55.504 0.000 .
      152 735  34 HIS CB C  30.232 0.000 .
      153 735  34 HIS N  N 119.275 0.000 .
      154 736  35 ALA H  H   8.239 0.000 .
      155 736  35 ALA C  C 175.426 0.000 .
      156 736  35 ALA CA C  50.511 0.000 .
      157 736  35 ALA CB C  17.964 0.000 .
      158 736  35 ALA N  N 127.599 0.016 .
      159 737  36 PRO C  C 176.873 0.000 .
      160 737  36 PRO CA C  62.873 0.000 .
      161 737  36 PRO CB C  31.781 0.000 .
      162 737  36 PRO N  N 136.268 0.000 .
      163 738  37 THR H  H   8.191 0.000 .
      164 738  37 THR C  C 172.620 0.000 .
      165 738  37 THR CA C  59.889 0.000 .
      166 738  37 THR CB C  69.833 0.000 .
      167 738  37 THR N  N 118.222 0.000 .
      168 739  38 PRO C  C 174.821 0.000 .
      169 739  38 PRO N  N 141.415 0.000 .
      170 740  39 PRO C  C 176.887 0.000 .
      171 740  39 PRO CA C  62.740 0.000 .
      172 740  39 PRO CB C  31.848 0.000 .
      173 740  39 PRO N  N 136.071 0.000 .
      174 741  40 THR H  H   8.137 0.000 .
      175 741  40 THR C  C 172.952 0.000 .
      176 741  40 THR CA C  59.823 0.000 .
      177 741  40 THR CB C  69.833 0.000 .
      178 741  40 THR N  N 117.875 0.037 .
      179 742  41 PRO C  C 176.349 0.000 .
      180 742  41 PRO CA C  62.939 0.000 .
      181 742  41 PRO CB C  31.980 0.000 .
      182 742  41 PRO N  N 139.913 0.000 .
      183 743  42 ALA H  H   8.257 0.000 .
      184 743  42 ALA C  C 175.721 0.000 .
      185 743  42 ALA CA C  50.410 0.000 .
      186 743  42 ALA CB C  17.727 0.000 .
      187 743  42 ALA N  N 126.642 0.006 .
      188 744  43 PRO C  C 176.982 0.000 .
      189 744  43 PRO CA C  63.005 0.000 .
      190 744  43 PRO CB C  31.914 0.000 .
      191 744  43 PRO N  N 136.415 0.000 .
      192 745  44 ARG H  H   8.342 0.000 .
      193 745  44 ARG C  C 176.559 0.000 .
      194 745  44 ARG CA C  56.111 0.000 .
      195 745  44 ARG CB C  30.654 0.000 .
      196 745  44 ARG N  N 121.945 0.023 .
      197 746  45 THR H  H   8.061 0.000 .
      198 746  45 THR C  C 174.256 0.000 .
      199 746  45 THR CA C  61.746 0.000 .
      200 746  45 THR CB C  69.966 0.000 .
      201 746  45 THR N  N 116.509 0.011 .
      202 747  46 MET H  H   8.314 0.000 .
      203 747  46 MET C  C 173.814 0.000 .
      204 747  46 MET CA C  53.061 0.000 .
      205 747  46 MET CB C  32.215 0.000 .
      206 747  46 MET N  N 125.131 0.002 .
      207 748  47 PRO C  C 174.789 0.000 .
      208 748  47 PRO N  N 139.098 0.000 .
      209 749  48 PRO C  C 177.179 0.000 .
      210 749  48 PRO CA C  62.873 0.000 .
      211 749  48 PRO CB C  31.781 0.000 .
      212 749  48 PRO N  N 135.800 0.000 .
      213 750  49 THR H  H   8.098 0.000 .
      214 750  49 THR C  C 174.412 0.000 .
      215 750  49 THR CA C  61.812 0.000 .
      216 750  49 THR CB C  69.966 0.000 .
      217 750  49 THR N  N 115.626 0.021 .
      218 751  50 LYS H  H   8.203 0.000 .
      219 751  50 LYS C  C 174.378 0.000 .
      220 751  50 LYS CA C  54.122 0.000 .
      221 751  50 LYS CB C  32.511 0.000 .
      222 751  50 LYS N  N 125.699 0.010 .
      223 752  51 PRO C  C 176.747 0.000 .
      224 752  51 PRO CA C  62.939 0.000 .
      225 752  51 PRO CB C  31.848 0.000 .
      226 752  51 PRO N  N 137.802 0.000 .
      227 753  52 GLN H  H   8.377 0.000 .
      228 753  52 GLN C  C 173.796 0.000 .
      229 753  52 GLN CA C  53.459 0.000 .
      230 753  52 GLN CB C  28.931 0.000 .
      231 753  52 GLN N  N 122.809 0.038 .
      232 754  53 PRO C  C 174.654 0.000 .
      233 754  53 PRO N  N 139.435 0.000 .
      234 755  54 PRO C  C 176.633 0.000 .
      235 755  54 PRO CA C  62.740 0.000 .
      236 755  54 PRO CB C  31.848 0.000 .
      237 755  54 PRO N  N 136.005 0.000 .
      238 756  55 ALA H  H   8.248 0.000 .
      239 756  55 ALA C  C 177.617 0.000 .
      240 756  55 ALA CA C  52.332 0.000 .
      241 756  55 ALA CB C  19.053 0.000 .
      242 756  55 ALA N  N 125.097 0.001 .
      243 757  56 ARG H  H   8.161 0.000 .
      244 757  56 ARG C  C 173.838 0.000 .
      245 757  56 ARG CA C  53.525 0.000 .
      246 757  56 ARG CB C  30.190 0.000 .
      247 757  56 ARG N  N 121.937 0.000 .
      248 758  57 PRO N  N 139.172 0.000 .
      249 759  58 PRO C  C 174.305 0.000 .
      250 759  58 PRO N  N 137.481 0.000 .
      251 760  59 PRO C  C 174.822 0.000 .
      252 760  59 PRO N  N 137.306 0.000 .
      253 761  60 PRO C  C 176.764 0.000 .
      254 761  60 PRO CA C  62.873 0.000 .
      255 761  60 PRO CB C  31.914 0.000 .
      256 761  60 PRO N  N 135.495 0.000 .
      257 762  61 VAL H  H   8.041 0.000 .
      258 762  61 VAL C  C 176.068 0.000 .
      259 762  61 VAL CA C  62.210 0.000 .
      260 762  61 VAL CB C  32.511 0.000 .
      261 762  61 VAL N  N 121.331 0.034 .
      262 763  62 LEU H  H   8.252 0.000 .
      263 763  62 LEU C  C 175.216 0.000 .
      264 763  62 LEU CA C  52.730 0.000 .
      265 763  62 LEU CB C  41.659 0.000 .
      266 763  62 LEU N  N 128.673 0.004 .
      267 764  63 PRO C  C 176.898 0.000 .
      268 764  63 PRO CA C  63.109 0.000 .
      269 764  63 PRO CB C  31.848 0.000 .
      270 764  63 PRO N  N 136.600 0.000 .
      271 765  64 ALA H  H   8.237 0.000 .
      272 765  64 ALA C  C 177.788 0.000 .
      273 765  64 ALA CA C  52.655 0.000 .
      274 765  64 ALA CB C  18.921 0.000 .
      275 765  64 ALA N  N 124.358 0.039 .
      276 766  65 ASN H  H   8.217 0.000 .
      277 766  65 ASN C  C 175.079 0.000 .
      278 766  65 ASN CA C  52.995 0.000 .
      279 766  65 ASN CB C  38.610 0.000 .
      280 766  65 ASN N  N 117.767 0.039 .
      281 767  66 ARG H  H   8.026 0.000 .
      282 767  66 ARG C  C 175.569 0.000 .
      283 767  66 ARG CA C  55.647 0.000 .
      284 767  66 ARG CB C  30.721 0.000 .
      285 767  66 ARG N  N 121.820 0.034 .
      286 768  67 ALA H  H   8.188 0.000 .
      287 768  67 ALA C  C 175.708 0.000 .
      288 768  67 ALA CA C  50.530 0.000 .
      289 768  67 ALA CB C  17.916 0.000 .
      290 768  67 ALA N  N 127.370 0.030 .
      291 769  68 PRO C  C 177.140 0.000 .
      292 769  68 PRO CA C  63.151 0.000 .
      293 769  68 PRO CB C  31.910 0.000 .
      294 769  68 PRO N  N 136.398 0.000 .
      295 770  69 SER H  H   8.199 0.000 .
      296 770  69 SER C  C 174.526 0.000 .
      297 770  69 SER CA C  58.214 0.000 .
      298 770  69 SER CB C  63.923 0.000 .
      299 770  69 SER N  N 116.236 0.044 .
      300 771  70 ALA H  H   8.273 0.000 .
      301 771  70 ALA C  C 177.894 0.000 .
      302 771  70 ALA CA C  52.597 0.000 .
      303 771  70 ALA CB C  19.186 0.000 .
      304 771  70 ALA N  N 126.768 0.003 .
      305 772  71 THR H  H   7.967 0.000 .
      306 772  71 THR C  C 174.050 0.000 .
      307 772  71 THR CA C  61.613 0.000 .
      308 772  71 THR CB C  69.900 0.000 .
      309 772  71 THR N  N 113.785 0.016 .
      310 773  72 ALA H  H   8.118 0.000 .
      311 773  72 ALA C  C 175.389 0.000 .
      312 773  72 ALA CA C  50.410 0.000 .
      313 773  72 ALA CB C  18.125 0.000 .
      314 773  72 ALA N  N 128.675 0.001 .
      315 774  73 PRO C  C 176.851 0.000 .
      316 774  73 PRO CB C  31.848 0.000 .
      317 774  73 PRO N  N 136.222 0.000 .
      318 775  74 SER H  H   8.278 0.000 .
      319 775  74 SER C  C 173.085 0.000 .
      320 775  74 SER CA C  56.376 0.000 .
      321 775  74 SER CB C  63.469 0.000 .
      322 775  74 SER N  N 118.189 0.015 .
      323 776  75 PRO C  C 177.088 0.000 .
      324 776  75 PRO CA C  63.303 0.000 .
      325 776  75 PRO CB C  31.887 0.000 .
      326 776  75 PRO N  N 138.739 0.000 .
      327 777  76 VAL H  H   8.053 0.000 .
      328 777  76 VAL C  C 176.960 0.000 .
      329 777  76 VAL CA C  62.543 0.000 .
      330 777  76 VAL CB C  32.472 0.000 .
      331 777  76 VAL N  N 120.728 0.039 .
      332 778  77 GLY H  H   8.315 0.000 .
      333 778  77 GLY C  C 174.039 0.000 .
      334 778  77 GLY CA C  45.173 0.000 .
      335 778  77 GLY N  N 113.220 0.032 .
      336 779  78 ALA H  H   8.110 0.000 .
      337 779  78 ALA C  C 178.463 0.000 .
      338 779  78 ALA CA C  52.597 0.000 .
      339 779  78 ALA CB C  19.186 0.000 .
      340 779  78 ALA N  N 124.640 0.027 .
      341 780  79 GLY H  H   8.335 0.000 .
      342 780  79 GLY C  C 174.510 0.000 .
      343 780  79 GLY CA C  45.239 0.000 .
      344 780  79 GLY N  N 108.849 0.013 .
      345 781  80 THR H  H   7.893 0.000 .
      346 781  80 THR C  C 174.315 0.000 .
      347 781  80 THR CA C  61.679 0.000 .
      348 781  80 THR CB C  69.966 0.000 .
      349 781  80 THR N  N 114.300 0.020 .
      350 782  81 ALA H  H   8.188 0.000 .
      351 782  81 ALA C  C 177.015 0.000 .
      352 782  81 ALA CA C  52.132 0.000 .
      353 782  81 ALA CB C  19.126 0.000 .
      354 782  81 ALA N  N 127.349 0.010 .
      355 783  82 ALA H  H   8.127 0.000 .
      356 783  82 ALA C  C 175.477 0.000 .
      357 783  82 ALA CA C  50.277 0.000 .
      358 783  82 ALA CB C  17.926 0.000 .
      359 783  82 ALA N  N 125.740 0.006 .
      360 784  83 PRO C  C 176.433 0.000 .
      361 784  83 PRO CA C  62.757 0.000 .
      362 784  83 PRO CB C  31.816 0.000 .
      363 784  83 PRO N  N 136.291 0.000 .
      364 785  84 ALA H  H   8.257 0.000 .
      365 785  84 ALA C  C 175.857 0.000 .
      366 785  84 ALA CA C  50.356 0.000 .
      367 785  84 ALA CB C  17.903 0.000 .
      368 785  84 ALA N  N 126.323 0.024 .
      369 786  85 PRO C  C 177.147 0.000 .
      370 786  85 PRO CA C  63.087 0.000 .
      371 786  85 PRO CB C  31.860 0.000 .
      372 786  85 PRO N  N 136.337 0.000 .
      373 787  86 SER H  H   8.238 0.000 .
      374 787  86 SER C  C 174.655 0.000 .
      375 787  86 SER CA C  58.418 0.000 .
      376 787  86 SER CB C  63.814 0.000 .
      377 787  86 SER N  N 116.299 0.000 .
      378 788  87 GLN H  H   8.293 0.000 .
      379 788  87 GLN C  C 175.930 0.000 .
      380 788  87 GLN CA C  55.647 0.000 .
      381 788  87 GLN CB C  29.461 0.000 .
      382 788  87 GLN N  N 122.707 0.071 .
      383 789  88 THR H  H   8.173 0.000 .
      384 789  88 THR C  C 173.086 0.000 .
      385 789  88 THR CA C  59.889 0.000 .
      386 789  88 THR CB C  69.634 0.000 .
      387 789  88 THR N  N 118.634 0.041 .
      388 790  89 PRO C  C 177.650 0.000 .
      389 790  89 PRO CA C  63.668 0.000 .
      390 790  89 PRO CB C  31.914 0.000 .
      391 790  89 PRO N  N 140.201 0.000 .
      392 791  90 GLY H  H   8.418 0.000 .
      393 791  90 GLY C  C 174.304 0.000 .
      394 791  90 GLY CA C  45.173 0.000 .
      395 791  90 GLY N  N 110.453 0.025 .
      396 792  91 SER H  H   7.968 0.000 .
      397 792  91 SER C  C 173.873 0.000 .
      398 792  91 SER CA C  58.100 0.000 .
      399 792  91 SER CB C  64.066 0.000 .
      400 792  91 SER N  N 116.057 0.030 .
      401 793  92 ALA H  H   8.166 0.000 .
      402 793  92 ALA C  C 175.020 0.000 .
      403 793  92 ALA CA C  50.457 0.000 .
      404 793  92 ALA CB C  18.094 0.000 .
      405 793  92 ALA N  N 127.612 0.010 .
      406 794  93 PRO C  C 174.346 0.000 .
      407 794  93 PRO N  N 137.816 0.000 .
      408 795  94 PRO C  C 174.944 0.000 .
      409 795  94 PRO N  N 137.194 0.000 .
      410 796  95 PRO C  C 177.170 0.000 .
      411 796  95 PRO CA C  63.138 0.000 .
      412 796  95 PRO CB C  31.848 0.000 .
      413 796  95 PRO N  N 135.727 0.000 .
      414 797  96 GLN H  H   8.253 0.000 .
      415 797  96 GLN C  C 175.949 0.000 .
      416 797  96 GLN CA C  55.779 0.000 .
      417 797  96 GLN CB C  29.262 0.000 .
      418 797  96 GLN N  N 120.561 0.058 .
      419 798  97 ALA H  H   8.176 0.000 .
      420 798  97 ALA C  C 177.723 0.000 .
      421 798  97 ALA CA C  52.521 0.000 .
      422 798  97 ALA CB C  18.976 0.000 .
      423 798  97 ALA N  N 125.870 0.006 .
      424 799  98 GLN H  H   8.197 0.000 .
      425 799  98 GLN C  C 176.605 0.000 .
      426 799  98 GLN CA C  56.045 0.000 .
      427 799  98 GLN CB C  29.130 0.000 .
      428 799  98 GLN N  N 120.043 0.022 .
      429 800  99 GLY H  H   8.235 0.000 .
      430 800  99 GLY C  C 173.898 0.000 .
      431 800  99 GLY CA C  45.305 0.000 .
      432 800  99 GLY N  N 110.544 0.013 .
      433 801 100 TRP H  H   7.821 0.000 .
      434 801 100 TRP C  C 176.236 0.000 .
      435 801 100 TRP CA C  57.238 0.000 .
      436 801 100 TRP CB C  29.527 0.000 .
      437 801 100 TRP N  N 121.211 0.024 .
      438 802 101 SER H  H   7.910 0.000 .
      439 802 101 SER C  C 173.472 0.000 .
      440 802 101 SER CA C  57.967 0.000 .
      441 802 101 SER CB C  63.867 0.000 .
      442 802 101 SER N  N 118.050 0.007 .
      443 803 102 HIS H  H   7.996 0.000 .
      444 803 102 HIS C  C 173.104 0.000 .
      445 803 102 HIS CA C  54.122 0.000 .
      446 803 102 HIS CB C  29.464 0.000 .
      447 803 102 HIS N  N 122.338 0.009 .
      448 804 103 PRO C  C 176.871 0.000 .
      449 804 103 PRO CA C  63.337 0.000 .
      450 804 103 PRO CB C  31.914 0.000 .
      451 804 103 PRO N  N 138.190 0.000 .
      452 805 104 GLN H  H   8.473 0.000 .
      453 805 104 GLN C  C 175.684 0.000 .
      454 805 104 GLN CA C  55.978 0.000 .
      455 805 104 GLN CB C  29.262 0.000 .
      456 805 104 GLN N  N 121.265 0.042 .
      457 806 105 PHE H  H   8.028 0.000 .
      458 806 105 PHE C  C 175.539 0.000 .
      459 806 105 PHE CA C  57.304 0.000 .
      460 806 105 PHE CB C  39.604 0.000 .
      461 806 105 PHE N  N 120.992 0.017 .
      462 807 106 GLU H  H   8.197 0.000 .
      463 807 106 GLU C  C 175.242 0.000 .
      464 807 106 GLU CA C  56.509 0.000 .
      465 807 106 GLU CB C  30.389 0.000 .
      466 807 106 GLU N  N 123.366 0.044 .
      467 808 107 LYS H  H   7.764 0.000 .
      468 808 107 LYS C  C 171.040 0.000 .
      469 808 107 LYS CA C  57.675 0.000 .
      470 808 107 LYS CB C  33.550 0.000 .
      471 808 107 LYS N  N 127.709 0.004 .

   stop_

save_