data_5376

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
C-terminal peptide of alpha-subunit of transducin
;
   _BMRB_accession_number   5376
   _BMRB_flat_file_name     bmr5376.str
   _Entry_type              original
   _Submission_date         2002-05-15
   _Accession_date          2002-05-15
   _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 Koenig   Bernd  W. . 
      2 Kontaxis Georg  .  . 
      3 Mitchell Drake  C. . 
      4 Louis    John   M. . 
      5 Litman   Burton J. . 
      6 Bax      Ad     .  . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  69 
      "13C chemical shifts" 36 
      "15N chemical shifts" 10 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2003-01-06 original author . 

   stop_

   _Original_release_date   2003-01-06

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Structure and Orientation of a G Protein Fragment in the Receptor Bound State 
from Residual Dipolar Couplings
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              22206956
   _PubMed_ID                    12217702

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Koenig   Bernd  W. . 
      2 Kontaxis Georg  .  . 
      3 Mitchell Drake  C. . 
      4 Louis    John   M. . 
      5 Litman   Burton J. . 
      6 Bax      Ad     .  . 

   stop_

   _Journal_abbreviation        'J. Mol. Biol.'
   _Journal_volume               322
   _Journal_issue                2
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   441
   _Page_last                    461
   _Year                         2002
   _Details                      .

   loop_
      _Keyword

       NMR                            
      'membrane protein'              
       rhodopsin                      
       transducin                     
      'transferred dipolar couplings' 

   stop_

save_


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

save_Gt_alpha340-350
   _Saveframe_category         molecular_system

   _Mol_system_name           'complex of transducin peptide and rhodopsin'
   _Abbreviation_common        Gt-alpha(340-350)
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'S2 peptide' $S2        
       rhodopsin   $rhodopsin 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'not present'

   loop_
      _Biological_function

      'signal transduction in the visual system' 

   stop_

   _Database_query_date        .
   _Details                   'peptide analog of C-terminal binding region of alpha subunit of transducin'

save_


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

save_S2
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 Gt-alpha(340-350)
   _Name_variant                                Gt-alpha(340-350)K341R,C347S
   _Abbreviation_common                         S2
   _Molecular_mass                              .
   _Mol_thiol_state                            'not present'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               11
   _Mol_residue_sequence                        IRENLKDSGLF

   loop_
      _Residue_seq_code
      _Residue_label

       1 ILE   2 ARG   3 GLU   4 ASN   5 LEU 
       6 LYS   7 ASP   8 SER   9 GLY  10 LEU 
      11 PHE 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-01-28

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Sequence_query_to_submitted_percentage
      _Sequence_subject_length
      _Sequence_identity
      _Sequence_positive
      _Sequence_homology_expectation_value

      PDB 1F88         "Crystal Structure Of Bovine Rhodopsin"                                                                                           100.00 348 100.00 100.00 0.00e+00 
      PDB 1GZM         "Structure Of Bovine Rhodopsin In A Trigonal Crystal Form"                                                                        100.00 349 100.00 100.00 0.00e+00 
      PDB 1HZX         "Crystal Structure Of Bovine Rhodopsin"                                                                                           100.00 349 100.00 100.00 0.00e+00 
      PDB 1JFP         "Structure Of Bovine Rhodopsin (Dark Adapted)"                                                                                    100.00 348 100.00 100.00 0.00e+00 
      PDB 1L9H         "Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution"                                                               100.00 349 100.00 100.00 0.00e+00 
      PDB 1LN6         "Structure Of Bovine Rhodopsin (Metarhodopsin Ii)"                                                                                100.00 348 100.00 100.00 0.00e+00 
      PDB 1U19         "Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution"                                                               100.00 349 100.00 100.00 0.00e+00 
      PDB 2G87         "Crystallographic Model Of Bathorhodopsin"                                                                                        100.00 349 100.00 100.00 0.00e+00 
      PDB 2HPY         "Crystallographic Model Of Lumirhodopsin"                                                                                         100.00 349 100.00 100.00 0.00e+00 
      PDB 2I35         "Crystal Structure Of Rhombohedral Crystal Form Of Ground-State Rhodopsin"                                                        100.00 349 100.00 100.00 0.00e+00 
      PDB 2I36         "Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin"                                                            100.00 349 100.00 100.00 0.00e+00 
      PDB 2I37         "Crystal Structure Of A Photoactivated Rhodopsin"                                                                                 100.00 349 100.00 100.00 0.00e+00 
      PDB 2J4Y         "Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells"                                                100.00 349  99.43  99.43 0.00e+00 
      PDB 2PED         "Crystallographic Model Of 9-Cis-Rhodopsin"                                                                                       100.00 349 100.00 100.00 0.00e+00 
      PDB 2X72         "Crystal Structure Of The Constitutively Active E113q,N2c, D282c Rhodopsin Mutant With Bound Galphact Peptide"                    100.00 349  99.14  99.43 0.00e+00 
      PDB 3C9L         "Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form"                                                          100.00 348 100.00 100.00 0.00e+00 
      PDB 3C9M         "Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form"                                                                100.00 348  99.43  99.43 0.00e+00 
      PDB 3CAP         "Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State"                            100.00 348 100.00 100.00 0.00e+00 
      PDB 3DQB         "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With A C-terminal Peptide Derived From The Galpha S" 100.00 348 100.00 100.00 0.00e+00 
      PDB 3OAX         "Crystal Structure Of Bovine Rhodopsin With Beta-Ionone"                                                                          100.00 349 100.00 100.00 0.00e+00 
      PDB 3PQR         "Crystal Structure Of Metarhodopsin Ii In Complex With A C-Terminal Peptide Derived From The Galpha Subunit Of Transducin"        100.00 348 100.00 100.00 0.00e+00 
      PDB 3PXO         "Crystal Structure Of Metarhodopsin Ii"                                                                                           100.00 348 100.00 100.00 0.00e+00 
      PDB 4A4M         "Crystal Structure Of The Light-Activated Constitutively Active N2c,M257y,D282c Rhodopsin Mutant In Complex With A Peptide Resem" 100.00 349  99.14  99.14 0.00e+00 
      PDB 4BEY         "Night Blindness Causing G90d Rhodopsin In Complex With Gact2 Peptide"                                                            100.00 349  99.14  99.14 0.00e+00 
      PDB 4BEZ         "Night Blindness Causing G90d Rhodopsin In The Active Conformation"                                                               100.00 349  99.14  99.14 0.00e+00 
      PDB 4J4Q         "Crystal Structure Of Active Conformation Of Gpcr Opsin Stabilized By Octylglucoside"                                             100.00 348 100.00 100.00 0.00e+00 
      PDB 4PXF         "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With The Finger-loop Peptide Derived From The Full-" 100.00 348 100.00 100.00 0.00e+00 
      DBJ BAB83621     "rhodopsin [synthetic construct]"                                                                                                 100.00 348 100.00 100.00 0.00e+00 
      GB  AAA30674     "rhodopsin [Bos taurus]"                                                                                                          100.00 348 100.00 100.00 0.00e+00 
      GB  AAA30675     "rhodopsin, partial [Bos taurus]"                                                                                                  98.56 343  99.71  99.71 0.00e+00 
      GB  ELR51227     "Rhodopsin, partial [Bos mutus]"                                                                                                  100.00 351  99.43  99.71 0.00e+00 
      PRF 0811197A      rhodopsin                                                                                                                        100.00 347  99.71  99.71 0.00e+00 
      PRF 0901188A      rhodopsin                                                                                                                        100.00 348 100.00 100.00 0.00e+00 
      PRF 0901212A      rhodopsin                                                                                                                        100.00 348 100.00 100.00 0.00e+00 
      PRF 1001148A      rhodopsin                                                                                                                        100.00 348 100.00 100.00 0.00e+00 
      REF NP_001014890 "rhodopsin [Bos taurus]"                                                                                                          100.00 348 100.00 100.00 0.00e+00 
      REF XP_004018583 "PREDICTED: rhodopsin [Ovis aries]"                                                                                               100.00 348  97.41  98.56 0.00e+00 
      REF XP_005902896 "PREDICTED: rhodopsin [Bos mutus]"                                                                                                100.00 348  99.43  99.71 0.00e+00 
      REF XP_006078962 "PREDICTED: rhodopsin [Bubalus bubalis]"                                                                                          100.00 348  98.85  99.14 0.00e+00 
      REF XP_010860750 "PREDICTED: rhodopsin [Bison bison bison]"                                                                                        100.00 348  99.43 100.00 0.00e+00 
      SP  P02699       "RecName: Full=Rhodopsin [Bos taurus]"                                                                                            100.00 348 100.00 100.00 0.00e+00 
      TPG DAA16827     "TPA: rhodopsin [Bos taurus]"                                                                                                     100.00 348 100.00 100.00 0.00e+00 

   stop_

save_


save_rhodopsin
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 rhodopsin
   _Name_variant                                rhodopsin
   _Molecular_mass                              .
   _Mol_thiol_state                            'not reported'
   _Details                                     .
   _Residue_count                               348
   _Mol_residue_sequence                       
;
MNGTEGPNFYVPFSNKTGVV
RSPFEAPQYYLAEPWQFSML
AAYMFLLIMLGFPINFLTLY
VTVQHKKLRTPLNYILLNLA
VADLFMVFGGFTTTLYTSLH
GYFVFGPTGCNLEGFFATLG
GEIALWSLVVLAIERYVVVC
KPMSNFRFGENHAIMGVAFT
WVMALACAAPPLVGWSRYIP
EGMQCSCGIDYYTPHEETNN
ESFVIYMFVVHFIIPLIVIF
FCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIMVIA
FLICWLPYAGVAFYIFTHQG
SDFGPIFMTIPAFFAKTSAV
YNPVIYIMMNKQFRNCMVTT
LCCGKNPLGDDEASTTVSKT
ETSQVAPA
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 ASN    3 GLY    4 THR    5 GLU 
        6 GLY    7 PRO    8 ASN    9 PHE   10 TYR 
       11 VAL   12 PRO   13 PHE   14 SER   15 ASN 
       16 LYS   17 THR   18 GLY   19 VAL   20 VAL 
       21 ARG   22 SER   23 PRO   24 PHE   25 GLU 
       26 ALA   27 PRO   28 GLN   29 TYR   30 TYR 
       31 LEU   32 ALA   33 GLU   34 PRO   35 TRP 
       36 GLN   37 PHE   38 SER   39 MET   40 LEU 
       41 ALA   42 ALA   43 TYR   44 MET   45 PHE 
       46 LEU   47 LEU   48 ILE   49 MET   50 LEU 
       51 GLY   52 PHE   53 PRO   54 ILE   55 ASN 
       56 PHE   57 LEU   58 THR   59 LEU   60 TYR 
       61 VAL   62 THR   63 VAL   64 GLN   65 HIS 
       66 LYS   67 LYS   68 LEU   69 ARG   70 THR 
       71 PRO   72 LEU   73 ASN   74 TYR   75 ILE 
       76 LEU   77 LEU   78 ASN   79 LEU   80 ALA 
       81 VAL   82 ALA   83 ASP   84 LEU   85 PHE 
       86 MET   87 VAL   88 PHE   89 GLY   90 GLY 
       91 PHE   92 THR   93 THR   94 THR   95 LEU 
       96 TYR   97 THR   98 SER   99 LEU  100 HIS 
      101 GLY  102 TYR  103 PHE  104 VAL  105 PHE 
      106 GLY  107 PRO  108 THR  109 GLY  110 CYS 
      111 ASN  112 LEU  113 GLU  114 GLY  115 PHE 
      116 PHE  117 ALA  118 THR  119 LEU  120 GLY 
      121 GLY  122 GLU  123 ILE  124 ALA  125 LEU 
      126 TRP  127 SER  128 LEU  129 VAL  130 VAL 
      131 LEU  132 ALA  133 ILE  134 GLU  135 ARG 
      136 TYR  137 VAL  138 VAL  139 VAL  140 CYS 
      141 LYS  142 PRO  143 MET  144 SER  145 ASN 
      146 PHE  147 ARG  148 PHE  149 GLY  150 GLU 
      151 ASN  152 HIS  153 ALA  154 ILE  155 MET 
      156 GLY  157 VAL  158 ALA  159 PHE  160 THR 
      161 TRP  162 VAL  163 MET  164 ALA  165 LEU 
      166 ALA  167 CYS  168 ALA  169 ALA  170 PRO 
      171 PRO  172 LEU  173 VAL  174 GLY  175 TRP 
      176 SER  177 ARG  178 TYR  179 ILE  180 PRO 
      181 GLU  182 GLY  183 MET  184 GLN  185 CYS 
      186 SER  187 CYS  188 GLY  189 ILE  190 ASP 
      191 TYR  192 TYR  193 THR  194 PRO  195 HIS 
      196 GLU  197 GLU  198 THR  199 ASN  200 ASN 
      201 GLU  202 SER  203 PHE  204 VAL  205 ILE 
      206 TYR  207 MET  208 PHE  209 VAL  210 VAL 
      211 HIS  212 PHE  213 ILE  214 ILE  215 PRO 
      216 LEU  217 ILE  218 VAL  219 ILE  220 PHE 
      221 PHE  222 CYS  223 TYR  224 GLY  225 GLN 
      226 LEU  227 VAL  228 PHE  229 THR  230 VAL 
      231 LYS  232 GLU  233 ALA  234 ALA  235 ALA 
      236 GLN  237 GLN  238 GLN  239 GLU  240 SER 
      241 ALA  242 THR  243 THR  244 GLN  245 LYS 
      246 ALA  247 GLU  248 LYS  249 GLU  250 VAL 
      251 THR  252 ARG  253 MET  254 VAL  255 ILE 
      256 ILE  257 MET  258 VAL  259 ILE  260 ALA 
      261 PHE  262 LEU  263 ILE  264 CYS  265 TRP 
      266 LEU  267 PRO  268 TYR  269 ALA  270 GLY 
      271 VAL  272 ALA  273 PHE  274 TYR  275 ILE 
      276 PHE  277 THR  278 HIS  279 GLN  280 GLY 
      281 SER  282 ASP  283 PHE  284 GLY  285 PRO 
      286 ILE  287 PHE  288 MET  289 THR  290 ILE 
      291 PRO  292 ALA  293 PHE  294 PHE  295 ALA 
      296 LYS  297 THR  298 SER  299 ALA  300 VAL 
      301 TYR  302 ASN  303 PRO  304 VAL  305 ILE 
      306 TYR  307 ILE  308 MET  309 MET  310 ASN 
      311 LYS  312 GLN  313 PHE  314 ARG  315 ASN 
      316 CYS  317 MET  318 VAL  319 THR  320 THR 
      321 LEU  322 CYS  323 CYS  324 GLY  325 LYS 
      326 ASN  327 PRO  328 LEU  329 GLY  330 ASP 
      331 ASP  332 GLU  333 ALA  334 SER  335 THR 
      336 THR  337 VAL  338 SER  339 LYS  340 THR 
      341 GLU  342 THR  343 SER  344 GLN  345 VAL 
      346 ALA  347 PRO  348 ALA 

   stop_

   _Sequence_homology_query_date                2008-08-19
   _Sequence_homology_query_revised_last_date   2008-08-19

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Sequence_query_to_submitted_percentage
      _Sequence_subject_length
      _Sequence_identity
      _Sequence_positive
      _Sequence_homology_expectation_value

      REF        NP_001014890 'rhodopsin [Bos taurus]'                                                                               100.00 348 100.00 100.00 0.00e+00 
      SWISS-PROT P02699        Rhodopsin                                                                                             100.00 348 100.00 100.00 0.00e+00 
      PRF        0901212A      rhodopsin                                                                                             100.00 348 100.00 100.00 0.00e+00 
      PRF        1001148A      rhodopsin                                                                                             100.00 348 100.00 100.00 0.00e+00 
      PRF        0811197A      rhodopsin                                                                                             100.00 347  99.71  99.71 0.00e+00 
      PRF        0901188A      rhodopsin                                                                                             100.00 348 100.00 100.00 0.00e+00 
      GenBank    AAA30674      rhodopsin                                                                                             100.00 348 100.00 100.00 0.00e+00 
      GenBank    AAA30675      rhodopsin                                                                                              98.56 343  99.71  99.71 0.00e+00 
      PDB        3CAP         'Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State' 100.00 348 100.00 100.00 0.00e+00 
      DBJ        BAB83621     'rhodopsin [synthetic construct]'                                                                      100.00 348 100.00 100.00 0.00e+00 
      PDB        3C9L         'Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form'                               100.00 348 100.00 100.00 0.00e+00 
      PDB        3C9M         'Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form'                                     100.00 348  99.43  99.43 0.00e+00 
      PDB        2J4Y         'Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells'                      99.43 348  99.42  99.42 0.00e+00 
      PDB        2PED         'Crystallographic Model Of 9-Cis-Rhodopsin'                                                            100.00 348 100.00 100.00 0.00e+00 
      PDB        2I36         'Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin'                                 100.00 348 100.00 100.00 0.00e+00 
      PDB        2I37         'Crystal Structure Of A Photoactivated Rhodopsin'                                                      100.00 348 100.00 100.00 0.00e+00 
      PDB        2HPY         'Crystallographic Model Of Lumirhodopsin'                                                              100.00 348 100.00 100.00 0.00e+00 
      PDB        2I35         'Crystal Structure Of Rhombohedral Crystal Form Of Ground- State Rhodopsin'                            100.00 348 100.00 100.00 0.00e+00 
      PDB        1U19         'Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution'                                    100.00 348 100.00 100.00 0.00e+00 
      PDB        2G87         'Crystallographic Model Of Bathorhodopsin'                                                             100.00 348 100.00 100.00 0.00e+00 
      PDB        1L9H         'Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution'                                    100.00 348 100.00 100.00 0.00e+00 
      PDB        1LN6         'Structure Of Bovine Rhodopsin (Metarhodopsin Ii)'                                                     100.00 348 100.00 100.00 0.00e+00 
      PDB        1HZX         'Crystal Structure Of Bovine Rhodopsin'                                                                100.00 348 100.00 100.00 0.00e+00 
      PDB        1JFP         'Structure Of Bovine Rhodopsin (Dark Adapted)'                                                         100.00 348 100.00 100.00 0.00e+00 
      PDB        1F88         'Crystal Structure Of Bovine Rhodopsin'                                                                 99.71 348 100.00 100.00 0.00e+00 
      PDB        1GZM         'Structure Of Bovine Rhodopsin In A Trigonal Crystal Form'                                             100.00 348 100.00 100.00 0.00e+00 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Organ
      _Tissue

      $S2 cow 9913 Eukaryota Metazoa Bos taurus eye retina 

   stop_

save_


    #########################
    #  Experimental source  #
    #########################

save_experimental_source
   _Saveframe_category   experimental_source


   loop_
      _Mol_label
      _Production_method
      _Host_organism_name_common
      _Genus
      _Species
      _Strain
      _Vector_type
      _Vector_name

      $S2 'recombinant technology' 'E. coli' Escherichia coli . plasmid GEV-S2 

   stop_

save_


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

save_sample_1
   _Saveframe_category   sample

   _Sample_type          emulsion
   _Details             
;
sample contains individual, intact rhodopsin rich 
disk membranes isolated from the rod outer segment
of bovine retina; S2 peptide is in fast exchange
between a free form in solution and a rhodopsin 
bound form
;

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $S2        2.6   mM '[U-15N; U-13C]' 
      $rhodopsin 0.063 mM  .               

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $S2 2.6 mM . 

   stop_

save_


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

save_NMRPipe
   _Saveframe_category   software

   _Name                 NMRPipe
   _Version              .

   loop_
      _Task

      'raw spectral data processing' 
      'peak picking'                 

   stop_

   _Details             'Delaglio, F. et al. (1995) J. Biomol. NMR 6(3), 277-293'

save_


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

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

save_NMR_spectrometer
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       750
   _Details              .

save_


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

save_2D_1H-1H_NOESY_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-1H NOESY'
   _Sample_label         .

save_


save_2D_1H-1H_TOCSY_(15N_separated)_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-1H TOCSY (15N separated)'
   _Sample_label         .

save_


save_2D_1H-15N_HSQC_(w/o_1H_decoupling)_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-15N HSQC (w/o 1H decoupling)'
   _Sample_label         .

save_


save_2D_1H-13C_CT-HSQC_(w/o_1H_decoupling)_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-13C CT-HSQC (w/o 1H decoupling)'
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '2D 1H-1H NOESY'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '2D 1H-1H TOCSY (15N separated)'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '2D 1H-15N HSQC (w/o 1H decoupling)'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '2D 1H-13C CT-HSQC (w/o 1H decoupling)'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


#######################
#  Sample conditions  #
#######################

save_Ex-cond_1
   _Saveframe_category   sample_conditions

   _Details             
;
sample was studied in dark adapted state
and after photo activation of rhodopsin by
illuminating the sample for 60s with a
focussed microscope light, chemical shifts 
of S2 are identical in both states, TrNOEs
and TrDCs are difference values between the
dark and light-activated states
;

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.6 0.2 na 
      temperature 283   0.5 K  

   stop_

save_


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

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

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

save_chemical_shift_reference
   _Saveframe_category   chemical_shift_reference

   _Details              .

   loop_
      _Mol_common_name
      _Atom_type
      _Atom_isotope_number
      _Atom_group
      _Chem_shift_units
      _Chem_shift_value
      _Reference_method
      _Reference_type
      _External_reference_sample_geometry
      _External_reference_location
      _External_reference_axis
      _Indirect_shift_ratio

      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.000000000 
      DSS N 15 'methyl protons' ppm 0.0 .        indirect . . . 0.101329118 
      DSS C 13 'methyl protons' ppm 0.0 .        indirect . . . 0.251449530 

   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_S2_shift_set
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      '2D 1H-1H NOESY'                        
      '2D 1H-1H TOCSY (15N separated)'        
      '2D 1H-15N HSQC (w/o 1H decoupling)'    
      '2D 1H-13C CT-HSQC (w/o 1H decoupling)' 

   stop_

   _Sample_conditions_label         $Ex-cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'S2 peptide'
   _Text_data_format                 .
   _Text_data                        .

   loop_
      _Atom_shift_assign_ID
      _Residue_author_seq_code
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1 .  1 ILE HA   H   3.86 . 1 
        2 .  1 ILE HB   H   1.95 . 1 
        3 .  1 ILE HG12 H   1.47 . 2 
        4 .  1 ILE HG13 H   1.21 . 2 
        5 .  1 ILE HG2  H   0.99 . 1 
        6 .  1 ILE HD1  H   0.92 . 1 
        7 .  1 ILE CA   C  60.5  . 1 
        8 .  1 ILE CB   C  39.3  . 1 
        9 .  1 ILE CG1  C  26.7  . 1 
       10 .  1 ILE CG2  C  16.9  . 1 
       11 .  1 ILE CD1  C  13.3  . 1 
       12 .  2 ARG HA   H   4.32 . 1 
       13 .  2 ARG HB2  H   1.86 . 2 
       14 .  2 ARG HB3  H   1.79 . 2 
       15 .  2 ARG HG2  H   1.63 . 1 
       16 .  2 ARG HG3  H   1.63 . 1 
       17 .  2 ARG HD2  H   3.20 . 1 
       18 .  2 ARG HD3  H   3.20 . 1 
       19 .  2 ARG CA   C  56.4  . 1 
       20 .  2 ARG CB   C  30.4  . 1 
       21 .  2 ARG CG   C  27.2  . 1 
       22 .  2 ARG CD   C  43.3  . 1 
       23 .  3 GLU H    H   8.76 . 1 
       24 .  3 GLU HA   H   4.23 . 1 
       25 .  3 GLU HB2  H   2.00 . 2 
       26 .  3 GLU HB3  H   1.92 . 2 
       27 .  3 GLU HG2  H   2.26 . 1 
       28 .  3 GLU HG3  H   2.26 . 1 
       29 .  3 GLU CA   C  56.9  . 1 
       30 .  3 GLU CB   C  30.4  . 1 
       31 .  3 GLU CG   C  36.3  . 1 
       32 .  3 GLU N    N 123.4  . 1 
       33 .  4 ASN H    H   8.65 . 1 
       34 .  4 ASN HA   H   4.67 . 1 
       35 .  4 ASN HB2  H   2.85 . 2 
       36 .  4 ASN HB3  H   2.75 . 2 
       37 .  4 ASN HD21 H   7.68 . 2 
       38 .  4 ASN HD22 H   6.97 . 2 
       39 .  4 ASN CA   C  53.1  . 1 
       40 .  4 ASN CB   C  38.6  . 1 
       41 .  4 ASN N    N 119.7  . 1 
       42 .  4 ASN ND2  N 113.2  . 1 
       43 .  5 LEU H    H   8.35 . 1 
       44 .  5 LEU HA   H   4.31 . 1 
       45 .  5 LEU HB2  H   1.65 . 2 
       46 .  5 LEU HB3  H   1.59 . 2 
       47 .  5 LEU HG   H   1.60 . 1 
       48 .  5 LEU HD1  H   0.92 . 1 
       49 .  5 LEU HD2  H   0.86 . 1 
       50 .  5 LEU CA   C  55.4  . 1 
       51 .  5 LEU CB   C  42.2  . 1 
       52 .  5 LEU CG   C  27.0  . 1 
       53 .  5 LEU CD1  C  25.0  . 1 
       54 .  5 LEU CD2  C  23.2  . 1 
       55 .  5 LEU N    N 122.9  . 1 
       56 .  6 LYS H    H   8.36 . 1 
       57 .  6 LYS HA   H   4.27 . 1 
       58 .  6 LYS HB2  H   1.82 . 2 
       59 .  6 LYS HB3  H   1.78 . 2 
       60 .  6 LYS HG2  H   1.43 . 2 
       61 .  6 LYS HG3  H   1.39 . 2 
       62 .  6 LYS HD2  H   1.66 . 1 
       63 .  6 LYS HD3  H   1.66 . 1 
       64 .  6 LYS HE2  H   2.97 . 1 
       65 .  6 LYS HE3  H   2.97 . 1 
       66 .  6 LYS CA   C  56.7  . 1 
       67 .  6 LYS CB   C  32.9  . 1 
       68 .  6 LYS CG   C  24.7  . 1 
       69 .  6 LYS CD   C  29.1  . 1 
       70 .  6 LYS CE   C  42.1  . 1 
       71 .  6 LYS N    N 121.8  . 1 
       72 .  7 ASP H    H   8.36 . 1 
       73 .  7 ASP HA   H   4.61 . 1 
       74 .  7 ASP HB2  H   2.75 . 2 
       75 .  7 ASP HB3  H   2.66 . 2 
       76 .  7 ASP CA   C  54.5  . 1 
       77 .  7 ASP CB   C  41.1  . 1 
       78 .  7 ASP N    N 121.4  . 1 
       79 .  8 SER H    H   8.31 . 1 
       80 .  8 SER HA   H   4.37 . 1 
       81 .  8 SER HB2  H   3.93 . 2 
       82 .  8 SER HB3  H   3.89 . 2 
       83 .  8 SER CA   C  58.9  . 1 
       84 .  8 SER CB   C  63.8  . 1 
       85 .  8 SER N    N 116.3  . 1 
       86 .  9 GLY H    H   8.53 . 1 
       87 .  9 GLY HA2  H   3.93 . 1 
       88 .  9 GLY HA3  H   3.93 . 1 
       89 .  9 GLY CA   C  45.4  . 1 
       90 .  9 GLY N    N 110.8  . 1 
       91 . 10 LEU H    H   7.94 . 1 
       92 . 10 LEU HA   H   4.30 . 1 
       93 . 10 LEU HB2  H   1.50 . 2 
       94 . 10 LEU HB3  H   1.44 . 2 
       95 . 10 LEU HG   H   1.50 . 1 
       96 . 10 LEU HD1  H   0.88 . 1 
       97 . 10 LEU HD2  H   0.81 . 1 
       98 . 10 LEU CA   C  55.0  . 1 
       99 . 10 LEU CB   C  42.4  . 1 
      100 . 10 LEU CG   C  26.8  . 1 
      101 . 10 LEU CD1  C  25.0  . 1 
      102 . 10 LEU CD2  C  23.1  . 1 
      103 . 10 LEU N    N 121.4  . 1 
      104 . 11 PHE H    H   7.71 . 1 
      105 . 11 PHE HA   H   4.43 . 1 
      106 . 11 PHE HB2  H   3.17 . 2 
      107 . 11 PHE HB3  H   2.94 . 2 
      108 . 11 PHE HD1  H   7.22 . 1 
      109 . 11 PHE HD2  H   7.22 . 1 
      110 . 11 PHE HE1  H   7.33 . 1 
      111 . 11 PHE HE2  H   7.33 . 1 
      112 . 11 PHE HZ   H   7.27 . 1 
      113 . 11 PHE CA   C  58.9  . 1 
      114 . 11 PHE CB   C  40.4  . 1 
      115 . 11 PHE N    N 124.9  . 1 

   stop_

save_