data_5290
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Investigation of Penetratin Peptides. Part 1: The Environment Dependent
Conformational Properties of Penetratin and two of its Derivatives
;
_BMRB_accession_number 5290
_BMRB_flat_file_name bmr5290.str
_Entry_type original
_Submission_date 2002-02-15
_Accession_date 2002-02-15
_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 Czajlik Andras . .
2 Mesko Eszter . .
3 Penke Botond . .
4 Perczel Andras . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 143
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2002-03-29 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
5289 'Third helix of Antennapedia homeodomain'
5291 'penetratin 12'
stop_
_Original_release_date 2002-03-29
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Investigation of Penetratin Peptides. Part 1: The Environment Dependent
Conformational Properties of Penetratin and two of its Derivatives
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21986604
_PubMed_ID 11991205
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Czajlik Andras . .
2 Mesko Eszter . .
3 Penke Botond . .
4 Perczel Andras . .
stop_
_Journal_abbreviation 'J. Pept. Sci.'
_Journal_volume 8
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 151
_Page_last 171
_Year 2002
_Details .
loop_
_Keyword
'irregular helix'
NMR
'trifluoro-ethanol/water mixtures'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_penetratin_mutant
_Saveframe_category molecular_system
_Mol_system_name 'third helix[W6F,W14F] of Antennapedia homeodomain'
_Abbreviation_common 'penetratin double mutant[W6F,W14F]'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'third helix[W6F,W14F] of Antennapedia homeodomain' $penetratin_mutant
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Biological_function
'Translocation through biological membranes.'
;
Transportation of covalently linked oligonucleotides and oligopeptides through
biological membranes.
;
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_penetratin_mutant
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'third helix[W6F,W14F] of Antennapedia homeodomain'
_Abbreviation_common 'penetratin double mutant[W6F,W14F]'
_Molecular_mass 2168
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 16
_Mol_residue_sequence RQIKIFFQNRRMKFKK
loop_
_Residue_seq_code
_Residue_label
1 ARG 2 GLN 3 ILE 4 LYS 5 ILE
6 PHE 7 PHE 8 GLN 9 ASN 10 ARG
11 ARG 12 MET 13 LYS 14 PHE 15 LYS
16 LYS
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
BMRB 5543 Penetratin_W48F_W56F 100.00 16 100.00 100.00 3.83e+00
PDB 1KZ2 "Solution Structure Of The Third Helix Of Antennapedia Homeodomain Derivative [w6f,W14f]" 100.00 16 100.00 100.00 3.83e+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
_Details
$penetratin_mutant 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 'Engineered biopolymer.'
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
_Details
$penetratin_mutant 'chemical synthesis' . . . . . 'Solid phase peptide synthesis. Boc strategy.'
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
$penetratin_mutant 1.5 mM .
trifluoroethanol 90 % .
water 10 % .
stop_
save_
############################
# Computer software used #
############################
save_FELIX
_Saveframe_category software
_Name FELIX
_Version 97.2
loop_
_Task
'peak assignment'
'peak picking'
'raw spectral data processing'
stop_
_Details 'Accelrys Inc.'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-1H_DQF-COSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H DQF-COSY'
_Sample_label .
save_
save_2D_1H-1H_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H TOCSY'
_Sample_label .
save_
save_2D_1H-1H_NOESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H DQF-COSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_cond_set_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3 0.2 n/a
temperature 300 1 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 . . . 1.0
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_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details 'Aromatic amino acids can be only partly assigned.'
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_set_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'third helix[W6F,W14F] of Antennapedia homeodomain'
_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 ARG HA H 4.04 0.01 1
2 . 1 ARG HB2 H 2.16 0.01 2
3 . 1 ARG HB3 H 2.08 0.01 2
4 . 1 ARG HG2 H 1.83 0.01 1
5 . 1 ARG HG3 H 1.83 0.01 1
6 . 1 ARG HD2 H 3.23 0.01 1
7 . 1 ARG HD3 H 3.23 0.01 1
8 . 1 ARG HE H 7.20 0.01 1
9 . 1 ARG HH11 H 6.52 0.01 1
10 . 1 ARG HH12 H 6.52 0.01 1
11 . 1 ARG HH21 H 6.52 0.01 1
12 . 1 ARG HH22 H 6.52 0.01 1
13 . 2 GLN H H 9.08 0.01 1
14 . 2 GLN HA H 4.20 0.01 1
15 . 2 GLN HB2 H 2.19 0.01 2
16 . 2 GLN HB3 H 2.05 0.01 2
17 . 2 GLN HG2 H 2.54 0.01 2
18 . 2 GLN HG3 H 2.44 0.01 2
19 . 2 GLN HE21 H 6.91 0.01 2
20 . 2 GLN HE22 H 6.06 0.01 2
21 . 3 ILE H H 7.40 0.01 1
22 . 3 ILE HA H 4.02 0.01 1
23 . 3 ILE HB H 1.96 0.01 1
24 . 3 ILE HG12 H 1.55 0.01 2
25 . 3 ILE HG13 H 1.24 0.01 2
26 . 3 ILE HG2 H 0.94 0.01 1
27 . 3 ILE HD1 H 0.94 0.01 1
28 . 4 LYS H H 7.58 0.01 1
29 . 4 LYS HA H 4.16 0.01 1
30 . 4 LYS HB2 H 1.93 0.01 1
31 . 4 LYS HB3 H 1.93 0.01 1
32 . 4 LYS HG2 H 1.78 0.01 1
33 . 4 LYS HG3 H 1.78 0.01 1
34 . 4 LYS HD2 H 1.62 0.01 2
35 . 4 LYS HD3 H 1.55 0.01 2
36 . 4 LYS HE2 H 3.04 0.01 1
37 . 4 LYS HE3 H 3.04 0.01 1
38 . 5 ILE H H 7.39 0.01 1
39 . 5 ILE HA H 3.83 0.01 1
40 . 5 ILE HB H 1.96 0.01 1
41 . 5 ILE HG12 H 1.60 0.01 2
42 . 5 ILE HG13 H 1.23 0.01 2
43 . 5 ILE HG2 H 0.91 0.01 1
44 . 5 ILE HD1 H 0.94 0.01 1
45 . 6 PHE H H 7.77 0.01 1
46 . 6 PHE HA H 4.33 0.01 1
47 . 6 PHE HB2 H 3.21 0.01 1
48 . 6 PHE HB3 H 3.21 0.01 1
49 . 6 PHE HD1 H 7.04 0.01 1
50 . 6 PHE HD2 H 7.04 0.01 1
51 . 6 PHE HE1 H 7.22 0.01 1
52 . 6 PHE HE2 H 7.22 0.01 1
53 . 7 PHE H H 8.33 0.01 1
54 . 7 PHE HA H 4.28 0.01 1
55 . 7 PHE HB2 H 3.25 0.01 1
56 . 7 PHE HB3 H 3.25 0.01 1
57 . 7 PHE HD1 H 7.30 0.01 1
58 . 7 PHE HD2 H 7.30 0.01 1
59 . 8 GLN H H 8.59 0.01 1
60 . 8 GLN HA H 4.14 0.01 1
61 . 8 GLN HB2 H 2.34 0.01 2
62 . 8 GLN HB3 H 2.20 0.01 2
63 . 8 GLN HG2 H 2.52 0.01 1
64 . 8 GLN HG3 H 2.52 0.01 1
65 . 8 GLN HE21 H 6.79 0.01 2
66 . 8 GLN HE22 H 6.04 0.01 2
67 . 9 ASN H H 8.33 0.01 1
68 . 9 ASN HA H 4.42 0.01 1
69 . 9 ASN HB2 H 2.97 0.01 2
70 . 9 ASN HB3 H 2.71 0.01 2
71 . 9 ASN HD21 H 7.21 0.01 2
72 . 9 ASN HD22 H 6.14 0.01 2
73 . 10 ARG H H 8.02 0.01 1
74 . 10 ARG HA H 3.96 0.01 1
75 . 10 ARG HB2 H 1.86 0.01 1
76 . 10 ARG HB3 H 1.86 0.01 1
77 . 10 ARG HG2 H 1.65 0.01 2
78 . 10 ARG HG3 H 1.57 0.01 2
79 . 10 ARG HD2 H 2.98 0.01 1
80 . 10 ARG HD3 H 2.98 0.01 1
81 . 10 ARG HE H 6.78 0.01 1
82 . 10 ARG HH11 H 6.24 0.01 1
83 . 10 ARG HH12 H 6.24 0.01 1
84 . 10 ARG HH21 H 6.24 0.01 1
85 . 10 ARG HH22 H 6.24 0.01 1
86 . 11 ARG H H 8.19 0.01 1
87 . 11 ARG HA H 4.03 0.01 1
88 . 11 ARG HB2 H 1.90 0.01 2
89 . 11 ARG HB3 H 1.78 0.01 2
90 . 11 ARG HG2 H 1.62 0.01 1
91 . 11 ARG HG3 H 1.62 0.01 1
92 . 11 ARG HD2 H 3.15 0.01 2
93 . 11 ARG HD3 H 3.09 0.01 2
94 . 11 ARG HE H 6.86 0.01 1
95 . 11 ARG HH11 H 6.41 0.01 1
96 . 11 ARG HH12 H 6.41 0.01 1
97 . 11 ARG HH21 H 6.41 0.01 1
98 . 11 ARG HH22 H 6.41 0.01 1
99 . 12 MET H H 8.10 0.01 1
100 . 12 MET HA H 4.25 0.01 1
101 . 12 MET HB2 H 2.22 0.01 2
102 . 12 MET HB3 H 2.17 0.01 2
103 . 12 MET HG2 H 2.77 0.01 2
104 . 12 MET HG3 H 2.59 0.01 2
105 . 12 MET HE H 2.08 0.01 1
106 . 13 LYS H H 7.92 0.01 1
107 . 13 LYS HA H 4.02 0.01 1
108 . 13 LYS HB2 H 1.81 0.01 2
109 . 13 LYS HB3 H 1.76 0.01 2
110 . 13 LYS HG2 H 1.44 0.01 2
111 . 13 LYS HG3 H 1.25 0.01 2
112 . 13 LYS HD2 H 1.60 0.01 1
113 . 13 LYS HD3 H 1.60 0.01 1
114 . 13 LYS HE2 H 2.94 0.01 1
115 . 13 LYS HE3 H 2.94 0.01 1
116 . 13 LYS HZ H 7.29 0.01 1
117 . 14 PHE H H 7.94 0.01 1
118 . 14 PHE HA H 4.48 0.01 1
119 . 14 PHE HB2 H 3.24 0.01 2
120 . 14 PHE HB3 H 3.10 0.01 2
121 . 14 PHE HD1 H 7.27 0.01 1
122 . 14 PHE HD2 H 7.27 0.01 1
123 . 15 LYS H H 7.85 0.01 1
124 . 15 LYS HA H 4.12 0.01 1
125 . 15 LYS HB2 H 1.95 0.01 1
126 . 15 LYS HB3 H 1.95 0.01 1
127 . 15 LYS HG2 H 1.48 0.01 1
128 . 15 LYS HG3 H 1.48 0.01 1
129 . 15 LYS HD2 H 1.73 0.01 1
130 . 15 LYS HD3 H 1.73 0.01 1
131 . 15 LYS HE2 H 3.06 0.01 1
132 . 15 LYS HE3 H 3.06 0.01 1
133 . 15 LYS HZ H 7.26 0.01 1
134 . 16 LYS H H 7.72 0.01 1
135 . 16 LYS HA H 4.35 0.01 1
136 . 16 LYS HB2 H 1.93 0.01 2
137 . 16 LYS HB3 H 1.82 0.01 2
138 . 16 LYS HG2 H 1.49 0.01 1
139 . 16 LYS HG3 H 1.49 0.01 1
140 . 16 LYS HD2 H 1.72 0.01 1
141 . 16 LYS HD3 H 1.72 0.01 1
142 . 16 LYS HE2 H 3.04 0.01 1
143 . 16 LYS HE3 H 3.04 0.01 1
stop_
save_