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
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