data_5609
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR structure of [Ala1,15]kalata B1
;
_BMRB_accession_number 5609
_BMRB_flat_file_name bmr5609.str
_Entry_type original
_Submission_date 2002-12-02
_Accession_date 2002-12-02
_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 Daly N. L. .
2 Clark R. J. .
3 Craik D. J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 128
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-08-01 original BMRB .
stop_
_Original_release_date 2002-12-02
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Disulfide Folding Pathways of Cystine Knot Proteins: Tying the Knot within the
Circular Backbone of the Cyclotides
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22476988
_PubMed_ID 12482862
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Daly N. L. .
2 Clark R. J. .
3 Craik D. J. .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_volume 278
_Journal_issue 8
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 6314
_Page_last 6322
_Year 2003
_Details .
loop_
_Keyword
'cyclic peptide'
'cystine knot'
'triple stranded beta sheet'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_KALATA
_Saveframe_category molecular_system
_Mol_system_name 'kalata B1'
_Abbreviation_common 'kalata B1'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'kalata B1' $KALATA
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_KALATA
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common KALATA
_Abbreviation_common KALATA
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 29
_Mol_residue_sequence
;
AGETCVGGTCNTPGATCSWP
VCTRNGLPV
;
loop_
_Residue_seq_code
_Residue_label
1 ALA 2 GLY 3 GLU 4 THR 5 CYS
6 VAL 7 GLY 8 GLY 9 THR 10 CYS
11 ASN 12 THR 13 PRO 14 GLY 15 ALA
16 THR 17 CYS 18 SER 19 TRP 20 PRO
21 VAL 22 CYS 23 THR 24 ARG 25 ASN
26 GLY 27 LEU 28 PRO 29 VAL
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
PDB 1N1U 'Nmr Structure Of [ala1,15]kalata B1' 100.00 29 100.00 100.00 1.59e-07
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$KALATA . . . . . .
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
$KALATA 'chemical synthesis' . . . . .
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
$KALATA 1 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name xwinnmr
_Version 2.6
loop_
_Task
collection
stop_
_Details .
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
'structure solution'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_DQF-COSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label .
save_
save_E-COSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name E-COSY
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3.8 . n/a
pressure 1 . atm
temperature 290 . 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_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D NOESY'
DQF-COSY
E-COSY
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'kalata B1'
_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 ALA H H 8.578 0.003 1
2 . 1 ALA HA H 4.037 0.003 1
3 . 1 ALA HB H 1.338 0.003 1
4 . 2 GLY H H 8.737 0.003 1
5 . 2 GLY HA2 H 4.063 0.003 2
6 . 2 GLY HA3 H 3.737 0.003 2
7 . 3 GLU H H 7.729 0.003 1
8 . 3 GLU HA H 4.722 0.003 1
9 . 3 GLU HB2 H 2.055 0.003 2
10 . 3 GLU HB3 H 1.847 0.020 2
11 . 3 GLU HG2 H 2.443 0.003 2
12 . 3 GLU HG3 H 2.356 0.003 2
13 . 4 THR H H 8.547 0.003 1
14 . 4 THR HA H 4.714 0.003 1
15 . 4 THR HB H 4.294 0.016 1
16 . 4 THR HG2 H 1.106 0.001 1
17 . 5 CYS H H 8.286 0.003 1
18 . 5 CYS HA H 4.839 0.006 1
19 . 5 CYS HB2 H 3.111 0.003 2
20 . 6 VAL H H 8.604 0.003 1
21 . 6 VAL HA H 4.022 0.003 1
22 . 6 VAL HB H 2.013 0.003 1
23 . 6 VAL HG1 H 0.956 0.014 2
24 . 7 GLY H H 8.972 0.003 1
25 . 7 GLY HA2 H 4.163 0.003 2
26 . 7 GLY HA3 H 3.865 0.003 2
27 . 8 GLY H H 8.324 0.003 1
28 . 8 GLY HA2 H 4.390 0.003 2
29 . 8 GLY HA3 H 3.955 0.003 2
30 . 9 THR H H 7.855 0.003 1
31 . 9 THR HA H 4.712 0.003 1
32 . 9 THR HB H 4.158 0.001 1
33 . 9 THR HG2 H 1.173 0.003 1
34 . 10 CYS H H 8.793 0.003 1
35 . 10 CYS HA H 4.817 0.003 1
36 . 10 CYS HB2 H 2.837 0.003 1
37 . 10 CYS HB3 H 3.242 0.003 1
38 . 11 ASN H H 8.775 0.003 1
39 . 11 ASN HA H 4.627 0.003 1
40 . 11 ASN HB2 H 2.767 0.002 2
41 . 12 THR H H 7.819 0.014 1
42 . 12 THR HA H 4.574 0.002 1
43 . 12 THR HB H 4.021 0.020 1
44 . 12 THR HG2 H 1.209 0.003 1
45 . 13 PRO HA H 4.342 0.003 1
46 . 13 PRO HB2 H 1.915 0.003 1
47 . 13 PRO HB3 H 2.334 0.003 1
48 . 13 PRO HG2 H 2.136 0.003 2
49 . 13 PRO HG3 H 2.008 0.003 2
50 . 13 PRO HD2 H 4.108 0.003 2
51 . 13 PRO HD3 H 3.703 0.003 2
52 . 14 GLY H H 8.891 0.003 1
53 . 14 GLY HA2 H 4.176 0.003 2
54 . 14 GLY HA3 H 3.717 0.006 2
55 . 15 ALA H H 7.768 0.003 1
56 . 15 ALA HA H 4.968 0.003 1
57 . 15 ALA HB H 1.269 0.022 1
58 . 16 THR H H 9.373 0.003 1
59 . 16 THR HA H 4.461 0.003 1
60 . 16 THR HB H 3.997 0.022 1
61 . 16 THR HG2 H 1.124 0.003 1
62 . 17 CYS H H 9.064 0.003 1
63 . 17 CYS HA H 4.691 0.003 1
64 . 17 CYS HB2 H 2.871 0.003 1
65 . 17 CYS HB3 H 3.143 0.003 1
66 . 18 SER H H 8.890 0.003 1
67 . 18 SER HA H 4.685 0.007 1
68 . 18 SER HB2 H 3.849 0.003 2
69 . 18 SER HB3 H 3.677 0.012 2
70 . 19 TRP H H 8.195 0.013 1
71 . 19 TRP HA H 4.155 0.016 1
72 . 19 TRP HB2 H 3.255 0.018 2
73 . 19 TRP HD1 H 7.306 0.022 1
74 . 19 TRP HE3 H 7.502 0.014 1
75 . 19 TRP HE1 H 10.367 0.001 1
76 . 19 TRP HZ2 H 7.562 0.023 1
77 . 20 PRO HA H 3.475 0.003 1
78 . 20 PRO HB2 H 1.703 0.003 1
79 . 20 PRO HB3 H 0.150 0.005 1
80 . 20 PRO HG2 H 1.499 0.022 2
81 . 20 PRO HG3 H 1.407 0.026 2
82 . 20 PRO HD2 H 3.342 0.019 2
83 . 20 PRO HD3 H 3.175 0.021 2
84 . 21 VAL H H 8.108 0.014 1
85 . 21 VAL HA H 4.326 0.020 1
86 . 21 VAL HB H 2.251 0.024 1
87 . 21 VAL HG1 H 0.808 0.007 2
88 . 22 CYS H H 7.928 0.003 1
89 . 22 CYS HA H 5.150 0.019 1
90 . 22 CYS HB2 H 2.916 0.003 1
91 . 22 CYS HB3 H 2.582 0.003 1
92 . 23 THR H H 9.384 0.003 1
93 . 23 THR HA H 5.078 0.003 1
94 . 23 THR HB H 3.643 0.018 1
95 . 23 THR HG2 H 0.913 0.017 1
96 . 24 ARG H H 9.010 0.003 1
97 . 24 ARG HA H 4.630 0.003 1
98 . 24 ARG HB2 H 1.714 0.008 2
99 . 24 ARG HB3 H 1.374 0.001 2
100 . 24 ARG HG2 H 1.497 0.026 2
101 . 24 ARG HG3 H 1.438 0.028 2
102 . 24 ARG HD2 H 3.145 0.002 2
103 . 24 ARG HD3 H 3.039 0.002 2
104 . 24 ARG HE H 7.222 0.002 1
105 . 25 ASN H H 9.637 0.003 1
106 . 25 ASN HA H 4.401 0.003 1
107 . 25 ASN HB2 H 3.075 0.003 2
108 . 25 ASN HB3 H 2.839 0.003 2
109 . 26 GLY H H 8.728 0.003 1
110 . 26 GLY HA2 H 4.202 0.003 2
111 . 26 GLY HA3 H 3.555 0.003 2
112 . 27 LEU H H 7.636 0.003 1
113 . 27 LEU HB2 H 1.751 0.026 2
114 . 27 LEU HB3 H 1.602 0.016 2
115 . 27 LEU HG H 1.608 0.056 1
116 . 27 LEU HD1 H 0.955 0.003 2
117 . 28 PRO HA H 4.504 0.003 1
118 . 28 PRO HB2 H 1.800 0.003 1
119 . 28 PRO HB3 H 2.195 0.003 1
120 . 28 PRO HG2 H 2.139 0.003 2
121 . 28 PRO HG3 H 1.950 0.003 2
122 . 28 PRO HD2 H 3.915 0.003 2
123 . 28 PRO HD3 H 3.666 0.017 2
124 . 29 VAL H H 8.615 0.001 1
125 . 29 VAL HA H 3.970 0.002 1
126 . 29 VAL HB H 1.811 0.020 1
127 . 29 VAL HG1 H 0.827 0.006 2
128 . 29 VAL HG2 H 0.764 0.021 2
stop_
save_