data_34508

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title
;
Solution NMR Structure of APP G38P mutant TM
;
   _BMRB_accession_number   34508
   _BMRB_flat_file_name     bmr34508.str
   _Entry_type              original
   _Submission_date         2020-03-30
   _Accession_date          2020-03-30
   _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 Silber     M. . .
      2 Muhle-Goll C. . .

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  159
      "13C chemical shifts" 103

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2020-12-04 original BMRB .

   stop_

   _Original_release_date   2020-07-14

save_


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

save_citation_1
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title
;
Altered hinge conformations in APP transmembrane helix mutants may affect complex formation with gamma-secretase
;
   _Citation_status             'in preparation'
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    ?

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Silber       M. . .
      2 Muhle-Goll   C. . .
      3 Hitzenberger M. . .
      4 Zacharias    M. . .

   stop_

   _Journal_abbreviation        'To be published'
   _Journal_volume               .
   _Journal_issue                .
   _Journal_CSD                  0353
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   .
   _Page_last                    .
   _Year                         .
   _Details                      .

save_


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

save_assembly
   _Saveframe_category         molecular_system

   _Mol_system_name           'Amyloid-beta precursor protein'
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      unit_1 $entity_1

   stop_

   _System_molecular_weight    .
   _System_oligomer_state      ?
   _System_paramagnetic        no
   _System_thiol_state         .
   _Database_query_date        .
   _Details                    .

save_


    ########################
    #  Monomeric polymers  #
    ########################

save_entity_1
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 entity_1
   _Molecular_mass                              3110.988
   _Mol_thiol_state                            'not present'
   _Details                                     .

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

      _Residue_count                               30
   _Mol_residue_sequence
;
SNKGAIIGLMVGPVVIATVI
VITLVMLKKK
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

       1 26 SER   2 27 ASN   3 28 LYS   4 29 GLY   5 30 ALA
       6 31 ILE   7 32 ILE   8 33 GLY   9 34 LEU  10 35 MET
      11 36 VAL  12 37 GLY  13 38 PRO  14 39 VAL  15 40 VAL
      16 41 ILE  17 42 ALA  18 43 THR  19 44 VAL  20 45 ILE
      21 46 VAL  22 47 ILE  23 48 THR  24 49 LEU  25 50 VAL
      26 51 MET  27 52 LEU  28 53 LYS  29 54 LYS  30 55 LYS

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   .

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $entity_1 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

      $entity_1 'chemical synthesis' . . . . .

   stop_

save_


#####################################
#  Sample contents and methodology  #
#####################################

    ########################
    #  Sample description  #
    ########################

save_sample_1
   _Saveframe_category   sample

   _Sample_type          solution
   _Details             '500 uM APP G38P, 80% TFE-d2, 20% H2O'

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $entity_1 500 uM 'natural abundance'

   stop_

save_


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

save_software_1
   _Saveframe_category   software

   _Name                 CNS
   _Version              1.2.1

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Brunger A. T. et.al.' . .

   stop_

   loop_
      _Task

      refinement

   stop_

   _Details              .

save_


save_software_2
   _Saveframe_category   software

   _Name                 ARIA
   _Version              2.3.2

   loop_
      _Vendor
      _Address
      _Electronic_address

      "Linge, O'Donoghue and Nilges" . .

   stop_

   loop_
      _Task

      'structure calculation'

   stop_

   _Details              .

save_


save_software_3
   _Saveframe_category   software

   _Name                'CcpNmr Analysis'
   _Version              2.4.2

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED.' . .

   stop_

   loop_
      _Task

      'chemical shift assignment'
      'peak picking'

   stop_

   _Details              .

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model               'CP TCI'
   _Field_strength       600
   _Details              .

save_


    #############################
    #  NMR applied experiments  #
    #############################

save_1H-1H-NOESY_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      1H-1H-NOESY
   _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   . mM
       pH                7.0 . pH
       pressure          1   . atm
       temperature     298   . K

   stop_

save_


####################
#  NMR parameters  #
####################

    ##############################
    #  Assigned chemical shifts  #
    ##############################

	################################
	#  Chemical shift referencing  #
	################################

save_chem_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 0.000 internal indirect . . . 0.25144953
      DSS H  1 'methyl protons' ppm 0.000 internal direct   . . . 1.0
      DSS N 15 'methyl protons' ppm 0.000 internal indirect . . . 0.10132912

   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_chemical_shifts_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      1H-1H-NOESY

   stop_

   loop_
      _Sample_label

      $sample_1

   stop_

   _Sample_conditions_label         $sample_conditions_1
   _Chem_shift_reference_set_label  $chem_shift_reference_1
   _Mol_system_component_name        unit_1
   _Text_data_format                 .
   _Text_data                        .

   loop_
      _Atom_shift_assign_ID
      _Residue_author_seq_code
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1 26  1 SER HA   H  4.393 . .
        2 26  1 SER HB2  H  3.962 . .
        3 26  1 SER HB3  H  3.831 . .
        4 26  1 SER HG   H  7.766 . .
        5 26  1 SER CA   C 58.021 . .
        6 26  1 SER CB   C 63.143 . .
        7 27  2 ASN HA   H  4.792 . .
        8 27  2 ASN HB2  H  2.909 . .
        9 27  2 ASN HB3  H  2.909 . .
       10 27  2 ASN CA   C 52.409 . .
       11 27  2 ASN CB   C 37.119 . .
       12 28  3 LYS H    H  8.020 . .
       13 28  3 LYS HA   H  4.120 . .
       14 28  3 LYS HB2  H  1.894 . .
       15 28  3 LYS HB3  H  1.852 . .
       16 28  3 LYS HD2  H  1.714 . .
       17 28  3 LYS HD3  H  1.714 . .
       18 28  3 LYS CA   C 58.000 . .
       19 28  3 LYS CB   C 31.565 . .
       20 28  3 LYS CD   C 28.316 . .
       21 29  4 GLY H    H  8.209 . .
       22 29  4 GLY HA2  H  3.853 . .
       23 29  4 GLY HA3  H  3.855 . .
       24 29  4 GLY CA   C 45.739 . .
       25 30  5 ALA H    H  7.634 . .
       26 30  5 ALA HA   H  4.230 . .
       27 30  5 ALA HB   H  1.486 . .
       28 30  5 ALA CA   C 53.531 . .
       29 30  5 ALA CB   C 17.309 . .
       30 31  6 ILE H    H  7.484 . .
       31 31  6 ILE HA   H  3.945 . .
       32 31  6 ILE HB   H  2.019 . .
       33 31  6 ILE HG12 H  1.627 . .
       34 31  6 ILE HG13 H  1.296 . .
       35 31  6 ILE HG2  H  0.980 . .
       36 31  6 ILE HD1  H  0.896 . .
       37 31  6 ILE CA   C 62.951 . .
       38 31  6 ILE CB   C 37.407 . .
       39 31  6 ILE CG1  C 27.515 . .
       40 31  6 ILE CG2  C 16.218 . .
       41 31  6 ILE CD1  C 11.280 . .
       42 32  7 ILE H    H  7.804 . .
       43 32  7 ILE HA   H  3.859 . .
       44 32  7 ILE HB   H  1.930 . .
       45 32  7 ILE HG12 H  1.267 . .
       46 32  7 ILE HG13 H  1.674 . .
       47 32  7 ILE HG2  H  0.948 . .
       48 32  7 ILE HD1  H  0.883 . .
       49 32  7 ILE CA   C 63.793 . .
       50 32  7 ILE CB   C 37.103 . .
       51 32  7 ILE CG1  C 27.856 . .
       52 32  7 ILE CG2  C 15.969 . .
       53 32  7 ILE CD1  C 11.100 . .
       54 33  8 GLY H    H  7.935 . .
       55 33  8 GLY HA2  H  3.843 . .
       56 33  8 GLY HA3  H  3.841 . .
       57 33  8 GLY CA   C 46.211 . .
       58 34  9 LEU H    H  7.765 . .
       59 34  9 LEU HA   H  4.290 . .
       60 34  9 LEU HB2  H  1.971 . .
       61 34  9 LEU HB3  H  1.640 . .
       62 34  9 LEU HG   H  1.836 . .
       63 34  9 LEU HD1  H  0.944 . .
       64 34  9 LEU HD2  H  0.915 . .
       65 34  9 LEU CA   C 56.378 . .
       66 34  9 LEU CB   C 41.609 . .
       67 34  9 LEU CG   C 26.125 . .
       68 34  9 LEU CD1  C 23.541 . .
       69 34  9 LEU CD2  C 21.751 . .
       70 35 10 MET H    H  7.955 . .
       71 35 10 MET HA   H  4.436 . .
       72 35 10 MET HB2  H  2.296 . .
       73 35 10 MET HB3  H  2.158 . .
       74 35 10 MET HG2  H  2.737 . .
       75 35 10 MET HG3  H  2.588 . .
       76 35 10 MET CA   C 56.725 . .
       77 35 10 MET CB   C 32.454 . .
       78 35 10 MET CG   C 31.514 . .
       79 36 11 VAL H    H  8.112 . .
       80 36 11 VAL HA   H  4.252 . .
       81 36 11 VAL HB   H  2.266 . .
       82 36 11 VAL HG1  H  1.033 . .
       83 36 11 VAL HG2  H  1.134 . .
       84 36 11 VAL CA   C 62.614 . .
       85 36 11 VAL CB   C 32.041 . .
       86 36 11 VAL CG1  C 19.502 . .
       87 36 11 VAL CG2  C 21.818 . .
       88 37 12 GLY H    H  7.921 . .
       89 37 12 GLY HA2  H  4.188 . .
       90 37 12 GLY HA3  H  3.936 . .
       91 37 12 GLY CA   C 47.222 . .
       92 38 13 PRO HA   H  4.265 . .
       93 38 13 PRO HB2  H  2.404 . .
       94 38 13 PRO HG2  H  2.178 . .
       95 38 13 PRO HG3  H  1.956 . .
       96 38 13 PRO HD2  H  3.682 . .
       97 38 13 PRO HD3  H  3.607 . .
       98 38 13 PRO CA   C 65.049 . .
       99 38 13 PRO CB   C 31.226 . .
      100 38 13 PRO CG   C 27.160 . .
      101 38 13 PRO CD   C 50.118 . .
      102 39 14 VAL H    H  7.423 . .
      103 39 14 VAL HA   H  3.803 . .
      104 39 14 VAL HB   H  2.310 . .
      105 39 14 VAL HG1  H  1.060 . .
      106 39 14 VAL HG2  H  0.992 . .
      107 39 14 VAL CA   C 64.953 . .
      108 39 14 VAL CB   C 31.192 . .
      109 39 14 VAL CG1  C 21.114 . .
      110 39 14 VAL CG2  C 19.842 . .
      111 40 15 VAL H    H  8.016 . .
      112 40 15 VAL HA   H  3.611 . .
      113 40 15 VAL HB   H  2.298 . .
      114 40 15 VAL HG1  H  0.949 . .
      115 40 15 VAL HG2  H  1.051 . .
      116 40 15 VAL CA   C 66.573 . .
      117 40 15 VAL CB   C 30.904 . .
      118 40 15 VAL CG1  C 20.001 . .
      119 40 15 VAL CG2  C 21.114 . .
      120 41 16 ILE H    H  8.129 . .
      121 41 16 ILE HA   H  3.697 . .
      122 41 16 ILE HB   H  1.868 . .
      123 41 16 ILE HG12 H  1.235 . .
      124 41 16 ILE HG13 H  1.671 . .
      125 41 16 ILE HG2  H  0.943 . .
      126 41 16 ILE HD1  H  0.829 . .
      127 41 16 ILE CA   C 64.154 . .
      128 41 16 ILE CB   C 36.930 . .
      129 41 16 ILE CG1  C 27.900 . .
      130 41 16 ILE CG2  C 15.969 . .
      131 41 16 ILE CD1  C 10.631 . .
      132 42 17 ALA H    H  7.874 . .
      133 42 17 ALA HA   H  4.045 . .
      134 42 17 ALA HB   H  1.541 . .
      135 42 17 ALA CA   C 54.958 . .
      136 42 17 ALA CB   C 16.968 . .
      137 43 18 THR H    H  7.860 . .
      138 43 18 THR HA   H  3.890 . .
      139 43 18 THR HB   H  4.550 . .
      140 43 18 THR HG2  H  1.281 . .
      141 43 18 THR CA   C 66.779 . .
      142 43 18 THR CB   C 68.350 . .
      143 43 18 THR CG2  C 19.531 . .
      144 44 19 VAL H    H  8.252 . .
      145 44 19 VAL HA   H  3.634 . .
      146 44 19 VAL HB   H  2.338 . .
      147 44 19 VAL HG1  H  1.106 . .
      148 44 19 VAL HG2  H  0.944 . .
      149 44 19 VAL CA   C 67.376 . .
      150 44 19 VAL CB   C 30.880 . .
      151 44 19 VAL CG1  C 21.648 . .
      152 44 19 VAL CG2  C 20.001 . .
      153 45 20 ILE H    H  8.450 . .
      154 45 20 ILE HA   H  3.633 . .
      155 45 20 ILE HB   H  2.108 . .
      156 45 20 ILE HG12 H  1.095 . .
      157 45 20 ILE HG13 H  1.878 . .
      158 45 20 ILE HG2  H  0.923 . .
      159 45 20 ILE HD1  H  0.844 . .
      160 45 20 ILE CA   C 65.710 . .
      161 45 20 ILE CB   C 36.876 . .
      162 45 20 ILE CG1  C 28.201 . .
      163 45 20 ILE CG2  C 15.470 . .
      164 45 20 ILE CD1  C 11.616 . .
      165 46 21 VAL H    H  8.247 . .
      166 46 21 VAL HA   H  3.635 . .
      167 46 21 VAL HB   H  2.273 . .
      168 46 21 VAL HG1  H  1.135 . .
      169 46 21 VAL HG2  H  0.985 . .
      170 46 21 VAL CA   C 66.443 . .
      171 46 21 VAL CB   C 30.894 . .
      172 46 21 VAL CG1  C 21.818 . .
      173 46 21 VAL CG2  C 19.842 . .
      174 47 22 ILE H    H  8.559 . .
      175 47 22 ILE HA   H  3.698 . .
      176 47 22 ILE HB   H  1.976 . .
      177 47 22 ILE HG12 H  1.242 . .
      178 47 22 ILE HG13 H  1.850 . .
      179 47 22 ILE HG2  H  0.957 . .
      180 47 22 ILE HD1  H  0.829 . .
      181 47 22 ILE CA   C 64.791 . .
      182 47 22 ILE CB   C 36.988 . .
      183 47 22 ILE CG1  C 28.218 . .
      184 47 22 ILE CG2  C 16.094 . .
      185 47 22 ILE CD1  C 10.631 . .
      186 48 23 THR H    H  8.159 . .
      187 48 23 THR HA   H  3.845 . .
      188 48 23 THR HB   H  4.545 . .
      189 48 23 THR HG1  H  5.683 . .
      190 48 23 THR HG2  H  1.244 . .
      191 48 23 THR CA   C 67.296 . .
      192 48 23 THR CB   C 68.040 . .
      193 48 23 THR CG2  C 19.366 . .
      194 49 24 LEU H    H  8.497 . .
      195 49 24 LEU HA   H  4.107 . .
      196 49 24 LEU HB2  H  1.522 . .
      197 49 24 LEU HB3  H  2.122 . .
      198 49 24 LEU HG   H  1.981 . .
      199 49 24 LEU HD1  H  0.897 . .
      200 49 24 LEU HD2  H  0.875 . .
      201 49 24 LEU CA   C 58.002 . .
      202 49 24 LEU CB   C 41.045 . .
      203 49 24 LEU CG   C 25.931 . .
      204 49 24 LEU CD1  C 23.906 . .
      205 49 24 LEU CD2  C 21.521 . .
      206 50 25 VAL H    H  8.627 . .
      207 50 25 VAL HA   H  3.610 . .
      208 50 25 VAL HB   H  2.334 . .
      209 50 25 VAL HG1  H  1.085 . .
      210 50 25 VAL HG2  H  0.952 . .
      211 50 25 VAL CA   C 66.573 . .
      212 50 25 VAL CB   C 30.880 . .
      213 50 25 VAL CG1  C 21.337 . .
      214 50 25 VAL CG2  C 19.498 . .
      215 51 26 MET H    H  8.557 . .
      216 51 26 MET HA   H  4.201 . .
      217 51 26 MET HB2  H  2.107 . .
      218 51 26 MET HB3  H  2.432 . .
      219 51 26 MET HG2  H  2.804 . .
      220 51 26 MET HG3  H  2.672 . .
      221 51 26 MET CA   C 58.059 . .
      222 51 26 MET CB   C 31.040 . .
      223 51 26 MET CG   C 31.949 . .
      224 52 27 LEU H    H  8.540 . .
      225 52 27 LEU HA   H  4.140 . .
      226 52 27 LEU HB2  H  2.019 . .
      227 52 27 LEU HB3  H  1.570 . .
      228 52 27 LEU HG   H  1.939 . .
      229 52 27 LEU HD1  H  0.905 . .
      230 52 27 LEU HD2  H  0.888 . .
      231 52 27 LEU CA   C 57.195 . .
      232 52 27 LEU CB   C 41.372 . .
      233 52 27 LEU CG   C 25.997 . .
      234 52 27 LEU CD1  C 23.906 . .
      235 52 27 LEU CD2  C 21.602 . .
      236 53 28 LYS H    H  8.205 . .
      237 53 28 LYS HA   H  4.123 . .
      238 53 28 LYS HB2  H  2.072 . .
      239 53 28 LYS HB3  H  1.989 . .
      240 53 28 LYS HD2  H  1.714 . .
      241 53 28 LYS HD3  H  1.714 . .
      242 53 28 LYS CA   C 57.707 . .
      243 53 28 LYS CB   C 31.342 . .
      244 53 28 LYS CD   C 28.316 . .
      245 54 29 LYS H    H  8.246 . .
      246 54 29 LYS HA   H  4.177 . .
      247 54 29 LYS HB2  H  1.953 . .
      248 54 29 LYS HB3  H  1.999 . .
      249 54 29 LYS HD2  H  1.710 . .
      250 54 29 LYS HD3  H  1.710 . .
      251 54 29 LYS CA   C 57.245 . .
      252 54 29 LYS CB   C 31.736 . .
      253 54 29 LYS CD   C 28.316 . .
      254 55 30 LYS H    H  8.000 . .
      255 55 30 LYS HA   H  4.222 . .
      256 55 30 LYS HB2  H  1.947 . .
      257 55 30 LYS HB3  H  1.947 . .
      258 55 30 LYS HD2  H  1.715 . .
      259 55 30 LYS HD3  H  1.715 . .
      260 55 30 LYS CA   C 56.207 . .
      261 55 30 LYS CB   C 32.030 . .
      262 55 30 LYS CD   C 28.316 . .

   stop_

save_