data_4509
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Automated 2D NOESY Assignment and Structure Calculation of crambin(S22/I25) with
Self-Correcting Distance Geometry Based NOAH/DIAMOND Programs
;
_BMRB_accession_number 4509
_BMRB_flat_file_name bmr4509.str
_Entry_type original
_Submission_date 1999-10-08
_Accession_date 1999-12-06
_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 Xu Y. . .
2 Wu J. . .
3 Gorenstein D. . .
4 Braun W. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 206
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2000-10-06 original author .
stop_
_Original_release_date 2000-10-06
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Automated 2D NOESY assignment and structure calculation of Crambin(S22/I25) with
the self-correcting distance geometry based NOAH/DIAMOD programs
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 99106048
_PubMed_ID 9887292
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Xu Y. . .
2 Wu J. . .
3 Gorenstein D. . .
4 Braun W. . .
stop_
_Journal_abbreviation 'J. Magn. Reson.'
_Journal_volume 136
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 76
_Page_last 85
_Year 1999
_Details .
loop_
_Keyword
crambin
'crambe abyssinica'
'plant seed protein'
stop_
save_
##################################
# Molecular system description #
##################################
save_system-crambin
_Saveframe_category molecular_system
_Mol_system_name crambin
_Abbreviation_common crambin
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
crambin $crambin
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not reported'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_crambin
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common crambin
_Abbreviation_common crambin
_Molecular_mass .
_Mol_thiol_state 'not reported'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 46
_Mol_residue_sequence
;
TTCCPSIVARSNFNVCRLPG
TSEAICATYTGCIIIPGATC
PGDYAN
;
loop_
_Residue_seq_code
_Residue_label
1 THR 2 THR 3 CYS 4 CYS 5 PRO
6 SER 7 ILE 8 VAL 9 ALA 10 ARG
11 SER 12 ASN 13 PHE 14 ASN 15 VAL
16 CYS 17 ARG 18 LEU 19 PRO 20 GLY
21 THR 22 SER 23 GLU 24 ALA 25 ILE
26 CYS 27 ALA 28 THR 29 TYR 30 THR
31 GLY 32 CYS 33 ILE 34 ILE 35 ILE
36 PRO 37 GLY 38 ALA 39 THR 40 CYS
41 PRO 42 GLY 43 ASP 44 TYR 45 ALA
46 ASN
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2014-10-26
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 1541 crambin 100.00 46 97.83 97.83 2.59e-22
BMRB 1542 thionin 100.00 46 97.83 97.83 2.59e-22
PDB 1AB1 "Si Form Crambin" 100.00 46 100.00 100.00 5.22e-23
PDB 1CRN "Water Structure Of A Hydrophobic Protein At Atomic Resolution. Pentagon Rings Of Water Molecules In Crystals Of Crambin" 100.00 46 97.83 97.83 4.08e-22
PDB 1CXR "Automated 2d Noesy Assignment And Structure Calculation Of Crambin(S22I25) WITH SELF-Correcting Distance Geometry Based NoahDIA" 97.83 46 100.00 100.00 2.04e-22
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$crambin 'Abyssinian crambe' 3271 Eukaryota Viridiplantae Crambe abyssinica
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
$crambin . . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details (SER/ILE)
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$crambin 2.5 mM .
acetone 75 % [U-2H]
H2O 20 % .
D2O 5 % .
stop_
save_
############################
# Computer software used #
############################
save_NOAH
_Saveframe_category software
_Name NOAH
_Version 1.0
loop_
_Task
'STRUCTURE SOLUTION'
stop_
_Details 'C.MUMENTHALER, Y.XU, W.BRAUN'
save_
save_DIAMOD
_Saveframe_category software
_Name DIAMOD
_Version 1.0
loop_
_Task
'STRUCTURE SOLUTION'
stop_
_Details 'P. GUNTERT, W. BRAUN, K. WUTHRICH'
save_
save_FANTOM
_Saveframe_category software
_Name FANTOM
_Version 4.0
loop_
_Task
REFINEMENT
stop_
_Details 'TH.SCHAUMANN, W.BRAUN, K.WUTHRICH, R.FRACZKIEWICZ'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model VXRS
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label $sample_1
save_
save_DQF-COSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label $sample_1
save_
save_2D_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 . n/a
temperature 298 . K
pressure 1 . atm
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_ref
_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_citation_label
_Correction_value_citation_label
. H 1 . . . . . . . . $entry_citation $entry_citation
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_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chem_shift_ref
_Mol_system_component_name crambin
_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 THR HA H 4.225 . .
2 . 1 THR HB H 4.115 . .
3 . 1 THR HG2 H 1.134 . .
4 . 2 THR H H 8.616 . .
5 . 2 THR HA H 5.225 . .
6 . 2 THR HB H 3.731 . .
7 . 2 THR HG2 H 0.869 . .
8 . 3 CYS H H 9.080 . .
9 . 3 CYS HA H 5.005 . .
10 . 3 CYS HB2 H 2.542 . .
11 . 3 CYS HB3 H 4.602 . .
12 . 4 CYS H H 9.041 . .
13 . 4 CYS HA H 5.432 . .
14 . 4 CYS HB2 H 2.897 . .
15 . 5 PRO HB2 H 2.023 . .
16 . 5 PRO HB3 H 1.930 . .
17 . 5 PRO HG2 H 2.887 . .
18 . 5 PRO HD2 H 3.997 . .
19 . 5 PRO HD3 H 3.794 . .
20 . 6 SER H H 7.000 . .
21 . 6 SER HA H 4.779 . .
22 . 6 SER HB2 H 4.032 . .
23 . 7 ILE H H 9.226 . .
24 . 7 ILE HA H 4.122 . .
25 . 7 ILE HB H 1.982 . .
26 . 7 ILE HG2 H 1.041 . .
27 . 7 ILE HG12 H 1.724 . .
28 . 7 ILE HG13 H 1.340 . .
29 . 7 ILE HD1 H 0.972 . .
30 . 8 VAL H H 7.680 . .
31 . 8 VAL HA H 3.769 . .
32 . 8 VAL HB H 2.039 . .
33 . 8 VAL HG1 H 1.076 . .
34 . 8 VAL HG2 H 0.987 . .
35 . 9 ALA H H 8.083 . .
36 . 9 ALA HA H 4.493 . .
37 . 9 ALA HB H 1.700 . .
38 . 10 ARG H H 7.794 . .
39 . 10 ARG HA H 4.609 . .
40 . 10 ARG HB2 H 2.034 . .
41 . 10 ARG HB3 H 1.714 . .
42 . 10 ARG HD2 H 3.430 . .
43 . 10 ARG HE H 9.690 . .
44 . 10 ARG HH11 H 6.640 . .
45 . 10 ARG HH12 H 6.640 . .
46 . 10 ARG HH21 H 7.061 . .
47 . 10 ARG HH22 H 7.061 . .
48 . 11 SER H H 8.411 . .
49 . 11 SER HA H 4.064 . .
50 . 11 SER HB2 H 4.093 . .
51 . 12 ASN H H 8.569 . .
52 . 12 ASN HA H 4.540 . .
53 . 12 ASN HB2 H 3.181 . .
54 . 12 ASN HB3 H 2.710 . .
55 . 12 ASN HD21 H 6.721 . .
56 . 12 ASN HD22 H 7.555 . .
57 . 13 PHE H H 9.305 . .
58 . 13 PHE HA H 3.960 . .
59 . 13 PHE HB2 H 3.831 . .
60 . 13 PHE HB3 H 3.557 . .
61 . 13 PHE HD1 H 7.220 . .
62 . 13 PHE HE1 H 7.461 . .
63 . 13 PHE HZ H 7.330 . .
64 . 14 ASN H H 8.748 . .
65 . 14 ASN HB2 H 2.774 . .
66 . 14 ASN HB3 H 3.314 . .
67 . 14 ASN HD21 H 7.064 . .
68 . 14 ASN HD22 H 7.817 . .
69 . 15 VAL H H 8.252 . .
70 . 15 VAL HA H 3.698 . .
71 . 15 VAL HB H 2.227 . .
72 . 15 VAL HG1 H 1.156 . .
73 . 15 VAL HG2 H 0.990 . .
74 . 16 CYS H H 9.302 . .
75 . 16 CYS HA H 3.823 . .
76 . 16 CYS HB2 H 2.600 . .
77 . 16 CYS HB3 H 2.465 . .
78 . 17 ARG H H 7.718 . .
79 . 17 ARG HA H 4.057 . .
80 . 17 ARG HB2 H 1.854 . .
81 . 17 ARG HB3 H 1.703 . .
82 . 17 ARG HG2 H 1.267 . .
83 . 17 ARG HG3 H 1.273 . .
84 . 17 ARG HD2 H 3.250 . .
85 . 17 ARG HD3 H 2.600 . .
86 . 17 ARG HE H 7.420 . .
87 . 18 LEU H H 7.639 . .
88 . 18 LEU HA H 4.211 . .
89 . 18 LEU HB2 H 2.078 . .
90 . 18 LEU HB3 H 1.635 . .
91 . 18 LEU HD1 H 1.010 . .
92 . 18 LEU HD2 H 0.930 . .
93 . 19 PRO HD2 H 4.070 . .
94 . 19 PRO HD3 H 3.963 . .
95 . 20 GLY H H 8.200 . .
96 . 20 GLY HA2 H 3.486 . .
97 . 20 GLY HA3 H 3.170 . .
98 . 21 THR H H 6.930 . .
99 . 21 THR HA H 4.030 . .
100 . 21 THR HB H 3.860 . .
101 . 21 THR HG2 H 1.338 . .
102 . 22 SER H H 8.202 . .
103 . 22 SER HA H 4.064 . .
104 . 22 SER HB2 H 3.539 . .
105 . 23 GLU H H 9.685 . .
106 . 23 GLU HA H 3.422 . .
107 . 23 GLU HB2 H 2.021 . .
108 . 23 GLU HB3 H 1.767 . .
109 . 23 GLU HG2 H 2.887 . .
110 . 23 GLU HG3 H 2.882 . .
111 . 24 ALA H H 8.597 . .
112 . 24 ALA HA H 4.104 . .
113 . 24 ALA HB H 1.470 . .
114 . 25 ILE H H 7.442 . .
115 . 25 ILE HA H 3.794 . .
116 . 25 ILE HB H 2.050 . .
117 . 25 ILE HG2 H 0.817 . .
118 . 25 ILE HG12 H 1.180 . .
119 . 25 ILE HG13 H 1.100 . .
120 . 26 CYS H H 8.327 . .
121 . 26 CYS HA H 4.674 . .
122 . 26 CYS HB2 H 2.766 . .
123 . 26 CYS HB3 H 2.492 . .
124 . 27 ALA H H 9.431 . .
125 . 27 ALA HA H 4.105 . .
126 . 27 ALA HB H 1.556 . .
127 . 28 THR H H 7.676 . .
128 . 28 THR HA H 3.989 . .
129 . 28 THR HG2 H 1.130 . .
130 . 29 TYR H H 7.921 . .
131 . 29 TYR HA H 4.435 . .
132 . 29 TYR HB2 H 3.238 . .
133 . 29 TYR HB3 H 3.050 . .
134 . 29 TYR HD1 H 7.252 . .
135 . 29 TYR HE1 H 6.764 . .
136 . 30 THR H H 7.592 . .
137 . 30 THR HA H 4.645 . .
138 . 30 THR HB H 4.744 . .
139 . 30 THR HG2 H 1.434 . .
140 . 31 GLY H H 8.038 . .
141 . 31 GLY HA2 H 3.960 . .
142 . 31 GLY HA3 H 3.563 . .
143 . 32 CYS H H 7.759 . .
144 . 32 CYS HA H 5.192 . .
145 . 32 CYS HB2 H 2.871 . .
146 . 32 CYS HB3 H 2.497 . .
147 . 33 ILE H H 9.047 . .
148 . 33 ILE HA H 4.770 . .
149 . 33 ILE HB H 1.616 . .
150 . 33 ILE HG2 H 0.606 . .
151 . 33 ILE HG12 H 1.095 . .
152 . 33 ILE HG13 H 0.817 . .
153 . 33 ILE HD1 H 0.160 . .
154 . 34 ILE H H 8.160 . .
155 . 34 ILE HA H 4.738 . .
156 . 34 ILE HB H 1.636 . .
157 . 34 ILE HG2 H 0.775 . .
158 . 34 ILE HG12 H 1.373 . .
159 . 34 ILE HG13 H 1.100 . .
160 . 35 ILE H H 8.490 . .
161 . 35 ILE HA H 4.998 . .
162 . 35 ILE HB H 2.040 . .
163 . 35 ILE HG2 H 0.816 . .
164 . 35 ILE HG12 H 1.467 . .
165 . 35 ILE HG13 H 0.965 . .
166 . 35 ILE HD1 H 0.773 . .
167 . 36 PRO HA H 4.603 . .
168 . 36 PRO HD2 H 3.795 . .
169 . 37 GLY H H 7.963 . .
170 . 37 GLY HA2 H 4.080 . .
171 . 38 ALA H H 8.472 . .
172 . 38 ALA HB H 1.446 . .
173 . 39 THR H H 7.716 . .
174 . 39 THR HA H 4.552 . .
175 . 39 THR HB H 3.959 . .
176 . 39 THR HG2 H 1.192 . .
177 . 40 CYS H H 8.762 . .
178 . 40 CYS HA H 4.880 . .
179 . 40 CYS HB2 H 2.634 . .
180 . 40 CYS HB3 H 3.446 . .
181 . 41 PRO HA H 4.612 . .
182 . 41 PRO HB2 H 2.420 . .
183 . 41 PRO HB3 H 2.226 . .
184 . 41 PRO HD2 H 3.813 . .
185 . 41 PRO HD3 H 3.676 . .
186 . 42 GLY H H 8.837 . .
187 . 42 GLY HA2 H 3.852 . .
188 . 43 ASP H H 8.389 . .
189 . 43 ASP HA H 4.683 . .
190 . 43 ASP HB2 H 3.039 . .
191 . 43 ASP HB3 H 2.846 . .
192 . 44 TYR H H 8.105 . .
193 . 44 TYR HA H 4.475 . .
194 . 44 TYR HB2 H 2.408 . .
195 . 44 TYR HB3 H 2.951 . .
196 . 44 TYR HD1 H 6.835 . .
197 . 44 TYR HE1 H 6.918 . .
198 . 45 ALA H H 7.668 . .
199 . 45 ALA HA H 4.486 . .
200 . 45 ALA HB H 1.370 . .
201 . 46 ASN H H 8.078 . .
202 . 46 ASN HA H 4.679 . .
203 . 46 ASN HB2 H 2.550 . .
204 . 46 ASN HB3 H 1.913 . .
205 . 46 ASN HD21 H 6.701 . .
206 . 46 ASN HD22 H 6.987 . .
stop_
save_