data_4589
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin
Protein CIPC of Clostridum cellulolyticum
;
_BMRB_accession_number 4589
_BMRB_flat_file_name bmr4589.str
_Entry_type original
_Submission_date 2000-05-05
_Accession_date 2000-09-07
_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 Mosbah A. . .
2 Belaich A. . .
3 Bornet O. . .
4 Belaich J. P. .
5 Henrissat B. . .
6 Darbon H. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
coupling_constants 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 431
"15N chemical shifts" 86
"coupling constants" 77
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-03-08 original author .
stop_
_Original_release_date 2001-03-08
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin
Protein CIPC of Clostridum cellulolyticum
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 20534886
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Mosbah A. . .
2 Belaich A. . .
3 Bornet O. . .
4 Belaich J. P. .
5 Henrissat B. . .
6 Darbon H. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 304
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 201
_Page_last 217
_Year 2000
_Details .
loop_
_Keyword
'3.10 helix'
beta-beta-barrels
stop_
save_
##################################
# Molecular system description #
##################################
save_system_scaffoldin
_Saveframe_category molecular_system
_Mol_system_name 'scaffoldin protein'
_Abbreviation_common scaffoldin
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'scaffoldin protein' $scaffoldin
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_scaffoldin
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'scaffoldin protein'
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 94
_Mol_residue_sequence
;
MQDPTINPTSISAKAGSFAD
TKITLTPNGNTFNGISELQS
SQYTKGTNEVTLLASYLNTL
PENTTKTLTFDFGVGTKNPK
LTITVLPKDIPGLE
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLN 3 ASP 4 PRO 5 THR
6 ILE 7 ASN 8 PRO 9 THR 10 SER
11 ILE 12 SER 13 ALA 14 LYS 15 ALA
16 GLY 17 SER 18 PHE 19 ALA 20 ASP
21 THR 22 LYS 23 ILE 24 THR 25 LEU
26 THR 27 PRO 28 ASN 29 GLY 30 ASN
31 THR 32 PHE 33 ASN 34 GLY 35 ILE
36 SER 37 GLU 38 LEU 39 GLN 40 SER
41 SER 42 GLN 43 TYR 44 THR 45 LYS
46 GLY 47 THR 48 ASN 49 GLU 50 VAL
51 THR 52 LEU 53 LEU 54 ALA 55 SER
56 TYR 57 LEU 58 ASN 59 THR 60 LEU
61 PRO 62 GLU 63 ASN 64 THR 65 THR
66 LYS 67 THR 68 LEU 69 THR 70 PHE
71 ASP 72 PHE 73 GLY 74 VAL 75 GLY
76 THR 77 LYS 78 ASN 79 PRO 80 LYS
81 LEU 82 THR 83 ILE 84 THR 85 VAL
86 LEU 87 PRO 88 LYS 89 ASP 90 ILE
91 PRO 92 GLY 93 LEU 94 GLU
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
PDB 1EHX "Nmr Solution Structure Of The Last Unknown Module Of The Cellulosomal Scaffoldin Protein Cipc Of Clostridum Cellulolyticum" 100.00 94 100.00 100.00 1.16e-57
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$scaffoldin 'Clostridium cellulolyticum' 1521 Bacteria . Clostridium cellulolyticum
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
$scaffoldin . . . . . .
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
$scaffoldin 25 mM [U-15N]
'sodium acetate buffer' 20 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name xwinnmr
_Version 2.1
loop_
_Task
processing
stop_
_Details .
save_
save_Xeasy
_Saveframe_category software
_Name XEASY
_Version 1.2
loop_
_Task
'data analysis'
stop_
_Details .
save_
save_DIANA
_Saveframe_category software
_Name DIANA
_Version 2.8
loop_
_Task
'structure solution'
stop_
_Details .
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
refinement
stop_
_Details .
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_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label $sample_1
save_
save_3D_15N-separated_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N-separated_NOESY'
_Sample_label $sample_1
save_
save_DQF-COSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label $sample_1
save_
save_2D_15N_HSQC_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC'
_Sample_label $sample_1
save_
save_2D_15N_HSQC_NOESY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC_NOESY'
_Sample_label $sample_1
save_
save_2D_15N_HSQC_TOCSY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC_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 '3D 15N-separated_NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC_NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 15N HSQC_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 5.0 . n/a
pressure 1 . atm
temperature 300 . 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_citation_label
_Correction_value_citation_label
. H 1 . ppm . . . . . . $entry_citation $entry_citation
. N 15 . ppm . . . . . . $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 $chemical_shift_reference
_Mol_system_component_name 'scaffoldin protein'
_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 . 2 GLN N N 120.05 . .
2 . 2 GLN H H 8.04 . .
3 . 2 GLN HA H 4.39 . .
4 . 2 GLN HB2 H 1.59 . .
5 . 2 GLN HB3 H 1.53 . .
6 . 2 GLN HG2 H 1.65 . .
7 . 3 ASP N N 115.81 . .
8 . 3 ASP H H 7.19 . .
9 . 3 ASP HA H 4.69 . .
10 . 3 ASP HB2 H 3.76 . .
11 . 3 ASP HB3 H 3.57 . .
12 . 4 PRO HA H 4.57 . .
13 . 4 PRO HB2 H 1.93 . .
14 . 4 PRO HB3 H 1.81 . .
15 . 4 PRO HG2 H 1.58 . .
16 . 4 PRO HG3 H 0.86 . .
17 . 4 PRO HD2 H 3.98 . .
18 . 4 PRO HD3 H 3.81 . .
19 . 5 THR N N 110.17 . .
20 . 5 THR H H 8.05 . .
21 . 5 THR HA H 4.56 . .
22 . 5 THR HB H 4.22 . .
23 . 5 THR HG2 H 1.01 . .
24 . 6 ILE N N 112.11 . .
25 . 6 ILE H H 7.92 . .
26 . 6 ILE HA H 5.07 . .
27 . 6 ILE HB H 1.28 . .
28 . 6 ILE HG2 H 0.72 . .
29 . 6 ILE HD1 H 0.03 . .
30 . 7 ASN N N 117.64 . .
31 . 7 ASN H H 7.99 . .
32 . 7 ASN HA H 4.67 . .
33 . 7 ASN HB2 H 2.58 . .
34 . 7 ASN HD21 H 7.67 . .
35 . 7 ASN HD22 H 6.91 . .
36 . 8 PRO HA H 4.97 . .
37 . 8 PRO HB2 H 2.54 . .
38 . 8 PRO HB3 H 2.35 . .
39 . 8 PRO HG2 H 1.99 . .
40 . 8 PRO HG3 H 1.54 . .
41 . 8 PRO HD2 H 3.98 . .
42 . 8 PRO HD3 H 3.58 . .
43 . 9 THR N N 103.05 . .
44 . 9 THR H H 8.27 . .
45 . 9 THR HA H 4.96 . .
46 . 9 THR HB H 4.29 . .
47 . 9 THR HG2 H 1.28 . .
48 . 10 SER N N 118.11 . .
49 . 10 SER H H 7.52 . .
50 . 10 SER HA H 5.54 . .
51 . 10 SER HB2 H 3.85 . .
52 . 11 ILE N N 117.37 . .
53 . 11 ILE H H 8.63 . .
54 . 11 ILE HA H 4.85 . .
55 . 11 ILE HB H 2.15 . .
56 . 11 ILE HG2 H 0.97 . .
57 . 12 SER N N 117.14 . .
58 . 12 SER H H 8.50 . .
59 . 12 SER HA H 5.79 . .
60 . 12 SER HB2 H 3.77 . .
61 . 12 SER HB3 H 3.66 . .
62 . 13 ALA N N 122.98 . .
63 . 13 ALA H H 7.79 . .
64 . 13 ALA HA H 4.10 . .
65 . 13 ALA HB H 0.06 . .
66 . 14 LYS N N 132.72 . .
67 . 14 LYS H H 8.87 . .
68 . 14 LYS HA H 3.97 . .
69 . 14 LYS HB2 H 1.59 . .
70 . 14 LYS HB3 H 1.54 . .
71 . 14 LYS HG2 H 1.33 . .
72 . 14 LYS HD2 H 1.18 . .
73 . 14 LYS HE2 H 2.94 . .
74 . 15 ALA N N 125.49 . .
75 . 15 ALA H H 8.14 . .
76 . 15 ALA HA H 4.34 . .
77 . 15 ALA HB H 1.28 . .
78 . 16 GLY N N 111.31 . .
79 . 16 GLY H H 8.97 . .
80 . 16 GLY HA2 H 4.22 . .
81 . 16 GLY HA3 H 3.56 . .
82 . 17 SER N N 115.76 . .
83 . 17 SER H H 8.39 . .
84 . 17 SER HA H 4.72 . .
85 . 17 SER HB2 H 3.88 . .
86 . 17 SER HB3 H 3.80 . .
87 . 18 PHE N N 124.35 . .
88 . 18 PHE H H 9.62 . .
89 . 18 PHE HA H 4.16 . .
90 . 18 PHE HB2 H 2.89 . .
91 . 18 PHE HB3 H 2.71 . .
92 . 19 ALA N N 125.03 . .
93 . 19 ALA H H 8.52 . .
94 . 19 ALA HA H 4.67 . .
95 . 19 ALA HB H 1.44 . .
96 . 20 ASP N N 122.76 . .
97 . 20 ASP H H 8.61 . .
98 . 20 ASP HA H 4.90 . .
99 . 20 ASP HB2 H 2.60 . .
100 . 20 ASP HB3 H 2.35 . .
101 . 21 THR N N 123.00 . .
102 . 21 THR H H 9.05 . .
103 . 21 THR HA H 4.58 . .
104 . 21 THR HB H 3.86 . .
105 . 21 THR HG2 H 1.24 . .
106 . 22 LYS N N 131.16 . .
107 . 22 LYS H H 8.94 . .
108 . 22 LYS HA H 4.95 . .
109 . 22 LYS HB2 H 1.78 . .
110 . 22 LYS HB3 H 1.63 . .
111 . 22 LYS HG2 H 1.38 . .
112 . 22 LYS HD2 H 1.31 . .
113 . 22 LYS HE2 H 2.85 . .
114 . 23 ILE N N 128.30 . .
115 . 23 ILE H H 9.48 . .
116 . 23 ILE HA H 4.56 . .
117 . 23 ILE HB H 2.05 . .
118 . 23 ILE HG2 H 0.71 . .
119 . 23 ILE HD1 H 0.57 . .
120 . 24 THR N N 124.43 . .
121 . 24 THR H H 9.16 . .
122 . 24 THR HA H 4.38 . .
123 . 24 THR HB H 4.16 . .
124 . 24 THR HG2 H 1.29 . .
125 . 25 LEU N N 127.40 . .
126 . 25 LEU H H 8.37 . .
127 . 25 LEU HA H 4.66 . .
128 . 25 LEU HB2 H 1.33 . .
129 . 25 LEU HB3 H 1.29 . .
130 . 25 LEU HG H 1.47 . .
131 . 25 LEU HD1 H 0.38 . .
132 . 25 LEU HD2 H 0.34 . .
133 . 26 THR N N 120.65 . .
134 . 26 THR H H 8.73 . .
135 . 26 THR HA H 3.98 . .
136 . 26 THR HB H 4.23 . .
137 . 26 THR HG2 H 1.08 . .
138 . 27 PRO HA H 4.58 . .
139 . 27 PRO HB2 H 2.73 . .
140 . 27 PRO HB3 H 2.43 . .
141 . 27 PRO HG2 H 2.30 . .
142 . 27 PRO HG3 H 2.06 . .
143 . 27 PRO HD2 H 3.90 . .
144 . 27 PRO HD3 H 3.57 . .
145 . 28 ASN N N 116.44 . .
146 . 28 ASN H H 8.86 . .
147 . 28 ASN HA H 4.30 . .
148 . 28 ASN HB2 H 2.78 . .
149 . 28 ASN HB3 H 2.19 . .
150 . 29 GLY N N 102.66 . .
151 . 29 GLY H H 8.20 . .
152 . 29 GLY HA2 H 4.23 . .
153 . 29 GLY HA3 H 3.64 . .
154 . 30 ASN N N 119.28 . .
155 . 30 ASN H H 7.40 . .
156 . 30 ASN HA H 4.95 . .
157 . 30 ASN HB2 H 3.25 . .
158 . 30 ASN HB3 H 2.77 . .
159 . 31 THR N N 121.05 . .
160 . 31 THR H H 9.11 . .
161 . 31 THR HA H 4.27 . .
162 . 31 THR HB H 4.02 . .
163 . 31 THR HG2 H 1.13 . .
164 . 32 PHE N N 127.09 . .
165 . 32 PHE H H 8.88 . .
166 . 32 PHE HA H 4.03 . .
167 . 32 PHE HB2 H 2.77 . .
168 . 33 ASN N N 127.72 . .
169 . 33 ASN H H 8.92 . .
170 . 33 ASN HA H 4.49 . .
171 . 33 ASN HB2 H 2.48 . .
172 . 33 ASN HB3 H 2.25 . .
173 . 34 GLY N N 104.26 . .
174 . 34 GLY H H 5.37 . .
175 . 34 GLY HA2 H 4.01 . .
176 . 35 ILE N N 118.61 . .
177 . 35 ILE H H 6.73 . .
178 . 35 ILE HA H 4.54 . .
179 . 35 ILE HB H 0.61 . .
180 . 35 ILE HG2 H 0.45 . .
181 . 35 ILE HD1 H 0.85 . .
182 . 36 SER N N 123.77 . .
183 . 36 SER H H 8.25 . .
184 . 36 SER HA H 3.97 . .
185 . 36 SER HB2 H 3.53 . .
186 . 36 SER HB3 H 3.53 . .
187 . 37 GLU N N 117.40 . .
188 . 37 GLU H H 9.26 . .
189 . 37 GLU HA H 4.09 . .
190 . 37 GLU HB2 H 2.11 . .
191 . 37 GLU HB3 H 1.89 . .
192 . 37 GLU HG2 H 2.68 . .
193 . 38 LEU N N 116.98 . .
194 . 38 LEU H H 7.03 . .
195 . 38 LEU HA H 4.67 . .
196 . 38 LEU HB2 H 1.57 . .
197 . 38 LEU HG H 1.16 . .
198 . 38 LEU HD1 H 0.22 . .
199 . 38 LEU HD2 H 0.28 . .
200 . 39 GLN N N 119.54 . .
201 . 39 GLN H H 8.32 . .
202 . 39 GLN HA H 4.59 . .
203 . 39 GLN HB2 H 1.66 . .
204 . 39 GLN HB3 H 1.58 . .
205 . 39 GLN HG2 H 2.35 . .
206 . 40 SER N N 117.78 . .
207 . 40 SER H H 8.87 . .
208 . 40 SER HA H 3.83 . .
209 . 40 SER HB2 H 3.14 . .
210 . 40 SER HB3 H 3.14 . .
211 . 41 SER N N 111.39 . .
212 . 41 SER H H 7.33 . .
213 . 41 SER HA H 4.28 . .
214 . 41 SER HB2 H 3.99 . .
215 . 41 SER HB3 H 3.78 . .
216 . 42 GLN N N 121.05 . .
217 . 42 GLN H H 7.96 . .
218 . 42 GLN HA H 4.36 . .
219 . 42 GLN HB2 H 2.23 . .
220 . 42 GLN HB3 H 2.16 . .
221 . 43 TYR N N 114.01 . .
222 . 43 TYR H H 7.43 . .
223 . 43 TYR HA H 5.29 . .
224 . 43 TYR HB2 H 2.89 . .
225 . 43 TYR HB3 H 2.76 . .
226 . 44 THR N N 113.39 . .
227 . 44 THR H H 9.03 . .
228 . 44 THR HA H 4.28 . .
229 . 44 THR HB H 4.13 . .
230 . 44 THR HG2 H 1.14 . .
231 . 45 LYS N N 124.59 . .
232 . 45 LYS H H 8.86 . .
233 . 45 LYS HA H 4.81 . .
234 . 45 LYS HB2 H 2.09 . .
235 . 45 LYS HB3 H 1.83 . .
236 . 45 LYS HG2 H 1.58 . .
237 . 46 GLY N N 115.41 . .
238 . 46 GLY H H 8.36 . .
239 . 46 GLY HA2 H 4.62 . .
240 . 46 GLY HA3 H 3.69 . .
241 . 47 THR N N 120.93 . .
242 . 47 THR H H 8.99 . .
243 . 47 THR HA H 4.27 . .
244 . 47 THR HB H 4.09 . .
245 . 47 THR HG2 H 1.23 . .
246 . 48 ASN N N 123.70 . .
247 . 48 ASN H H 9.16 . .
248 . 48 ASN HA H 4.35 . .
249 . 48 ASN HB2 H 3.48 . .
250 . 48 ASN HB3 H 3.01 . .
251 . 49 GLU N N 115.29 . .
252 . 49 GLU H H 7.24 . .
253 . 49 GLU HA H 5.26 . .
254 . 49 GLU HB2 H 1.99 . .
255 . 49 GLU HB3 H 1.85 . .
256 . 49 GLU HG2 H 2.08 . .
257 . 50 VAL N N 119.44 . .
258 . 50 VAL H H 8.92 . .
259 . 50 VAL HA H 5.11 . .
260 . 50 VAL HB H 2.14 . .
261 . 51 THR N N 120.76 . .
262 . 51 THR H H 8.86 . .
263 . 51 THR HA H 4.91 . .
264 . 51 THR HB H 4.12 . .
265 . 51 THR HG2 H 0.90 . .
266 . 52 LEU N N 128.71 . .
267 . 52 LEU H H 9.31 . .
268 . 52 LEU HA H 4.44 . .
269 . 52 LEU HB2 H 1.87 . .
270 . 52 LEU HB3 H 1.68 . .
271 . 52 LEU HG H 1.31 . .
272 . 52 LEU HD1 H 0.63 . .
273 . 52 LEU HD2 H 0.82 . .
274 . 53 LEU N N 124.64 . .
275 . 53 LEU H H 7.54 . .
276 . 53 LEU HA H 4.43 . .
277 . 53 LEU HB2 H 1.72 . .
278 . 53 LEU HB3 H 1.55 . .
279 . 53 LEU HG H 1.49 . .
280 . 53 LEU HD1 H 0.76 . .
281 . 53 LEU HD2 H 1.10 . .
282 . 54 ALA N N 130.99 . .
283 . 54 ALA H H 10.35 . .
284 . 54 ALA HA H 3.65 . .
285 . 54 ALA HB H 1.37 . .
286 . 55 SER N N 110.91 . .
287 . 55 SER H H 8.41 . .
288 . 55 SER HA H 4.01 . .
289 . 55 SER HB2 H 4.08 . .
290 . 56 TYR N N 121.98 . .
291 . 56 TYR H H 7.26 . .
292 . 56 TYR HA H 4.65 . .
293 . 56 TYR HB2 H 3.27 . .
294 . 56 TYR HB3 H 3.15 . .
295 . 57 LEU N N 123.75 . .
296 . 57 LEU H H 8.40 . .
297 . 57 LEU HA H 3.65 . .
298 . 57 LEU HB2 H 1.47 . .
299 . 57 LEU HB3 H 1.18 . .
300 . 57 LEU HG H 1.36 . .
301 . 57 LEU HD1 H 0.67 . .
302 . 57 LEU HD2 H 0.36 . .
303 . 58 ASN N N 113.97 . .
304 . 58 ASN H H 8.79 . .
305 . 58 ASN HA H 5.26 . .
306 . 58 ASN HB2 H 2.94 . .
307 . 58 ASN HB3 H 2.80 . .
308 . 59 THR N N 111.59 . .
309 . 59 THR H H 7.82 . .
310 . 59 THR HA H 4.42 . .
311 . 59 THR HB H 4.32 . .
312 . 59 THR HG2 H 1.36 . .
313 . 60 LEU N N 124.95 . .
314 . 60 LEU H H 7.01 . .
315 . 60 LEU HA H 3.98 . .
316 . 60 LEU HB2 H 1.75 . .
317 . 60 LEU HB3 H 1.75 . .
318 . 60 LEU HG H 1.1 . .
319 . 61 PRO HA H 4.85 . .
320 . 61 PRO HB2 H 2.31 . .
321 . 61 PRO HB3 H 1.96 . .
322 . 61 PRO HG2 H 2.06 . .
323 . 61 PRO HD2 H 4.09 . .
324 . 61 PRO HD3 H 3.68 . .
325 . 62 GLU N N 118.49 . .
326 . 62 GLU H H 8.49 . .
327 . 62 GLU HA H 3.69 . .
328 . 62 GLU HB2 H 1.95 . .
329 . 62 GLU HB3 H 2.06 . .
330 . 62 GLU HG2 H 2.33 . .
331 . 62 GLU HG3 H 2.24 . .
332 . 63 ASN N N 114.19 . .
333 . 63 ASN H H 7.59 . .
334 . 63 ASN HA H 4.53 . .
335 . 63 ASN HB2 H 3.14 . .
336 . 63 ASN HB3 H 2.91 . .
337 . 64 THR N N 115.46 . .
338 . 64 THR H H 7.52 . .
339 . 64 THR HA H 4.69 . .
340 . 64 THR HB H 4.07 . .
341 . 64 THR HG2 H 1.14 . .
342 . 65 THR N N 117.54 . .
343 . 65 THR H H 8.34 . .
344 . 65 THR HA H 5.45 . .
345 . 65 THR HB H 3.96 . .
346 . 65 THR HG2 H 1.14 . .
347 . 66 LYS N N 129.05 . .
348 . 66 LYS H H 9.42 . .
349 . 66 LYS HA H 4.79 . .
350 . 66 LYS HB2 H 1.80 . .
351 . 66 LYS HB3 H 1.67 . .
352 . 66 LYS HG2 H 1.72 . .
353 . 66 LYS HD2 H 1.41 . .
354 . 66 LYS HD3 H 1.25 . .
355 . 67 THR N N 122.22 . .
356 . 67 THR H H 8.52 . .
357 . 67 THR HA H 5.34 . .
358 . 67 THR HB H 3.88 . .
359 . 67 THR HG2 H 1.13 . .
360 . 68 LEU N N 125.80 . .
361 . 68 LEU H H 9.15 . .
362 . 68 LEU HA H 4.74 . .
363 . 68 LEU HB2 H 1.78 . .
364 . 68 LEU HB3 H 1.52 . .
365 . 68 LEU HG H 1.23 . .
366 . 68 LEU HD1 H 0.83 . .
367 . 68 LEU HD2 H 0.76 . .
368 . 69 THR N N 124.95 . .
369 . 69 THR H H 11.31 . .
370 . 69 THR HA H 4.42 . .
371 . 69 THR HB H 4.18 . .
372 . 69 THR HG2 H 1.10 . .
373 . 70 PHE N N 130.94 . .
374 . 70 PHE H H 9.12 . .
375 . 70 PHE HA H 4.27 . .
376 . 70 PHE HB2 H 3.42 . .
377 . 70 PHE HB3 H 2.66 . .
378 . 71 ASP N N 124.35 . .
379 . 71 ASP H H 8.42 . .
380 . 71 ASP HA H 4.43 . .
381 . 71 ASP HB2 H 2.83 . .
382 . 71 ASP HB3 H 2.32 . .
383 . 72 PHE N N 129.08 . .
384 . 72 PHE H H 8.44 . .
385 . 72 PHE HA H 5.41 . .
386 . 72 PHE HB2 H 3.63 . .
387 . 72 PHE HB3 H 2.69 . .
388 . 73 GLY N N 109.55 . .
389 . 73 GLY H H 9.51 . .
390 . 73 GLY HA2 H 4.22 . .
391 . 73 GLY HA3 H 4.03 . .
392 . 74 VAL N N 109.33 . .
393 . 74 VAL H H 7.68 . .
394 . 74 VAL HA H 4.73 . .
395 . 74 VAL HB H 2.49 . .
396 . 75 GLY N N 113.92 . .
397 . 75 GLY H H 8.31 . .
398 . 75 GLY HA2 H 3.95 . .
399 . 75 GLY HA3 H 3.64 . .
400 . 76 THR N N 121.74 . .
401 . 76 THR H H 8.86 . .
402 . 76 THR HA H 4.75 . .
403 . 76 THR HB H 4.13 . .
404 . 76 THR HG2 H 1.33 . .
405 . 77 LYS N N 120.24 . .
406 . 77 LYS H H 7.75 . .
407 . 77 LYS HA H 4.34 . .
408 . 77 LYS HB2 H 1.90 . .
409 . 77 LYS HB3 H 1.72 . .
410 . 77 LYS HG2 H 1.50 . .
411 . 77 LYS HD2 H 1.38 . .
412 . 78 ASN N N 123.80 . .
413 . 78 ASN H H 8.07 . .
414 . 78 ASN HA H 4.84 . .
415 . 78 ASN HB2 H 3.07 . .
416 . 78 ASN HB3 H 2.74 . .
417 . 79 PRO HA H 4.54 . .
418 . 79 PRO HB2 H 2.28 . .
419 . 79 PRO HB3 H 1.90 . .
420 . 79 PRO HD2 H 3.15 . .
421 . 79 PRO HD3 H 2.92 . .
422 . 80 LYS N N 119.24 . .
423 . 80 LYS H H 7.93 . .
424 . 80 LYS HA H 5.56 . .
425 . 80 LYS HB2 H 1.68 . .
426 . 80 LYS HB3 H 1.56 . .
427 . 80 LYS HG2 H 1.50 . .
428 . 80 LYS HD2 H 1.45 . .
429 . 80 LYS HE2 H 3.00 . .
430 . 81 LEU N N 126.24 . .
431 . 81 LEU H H 9.32 . .
432 . 81 LEU HA H 4.91 . .
433 . 81 LEU HB2 H 1.77 . .
434 . 81 LEU HB3 H 1.32 . .
435 . 81 LEU HG H 0.82 . .
436 . 81 LEU HD1 H 0.69 . .
437 . 82 THR N N 123.01 . .
438 . 82 THR H H 8.28 . .
439 . 82 THR HA H 4.82 . .
440 . 82 THR HB H 4.01 . .
441 . 82 THR HG2 H 1.13 . .
442 . 83 ILE N N 129.95 . .
443 . 83 ILE H H 9.42 . .
444 . 83 ILE HA H 4.71 . .
445 . 83 ILE HB H 1.81 . .
446 . 83 ILE HD1 H 0.62 . .
447 . 84 THR N N 125.62 . .
448 . 84 THR H H 8.84 . .
449 . 84 THR HA H 4.78 . .
450 . 84 THR HB H 3.97 . .
451 . 84 THR HG2 H 1.13 . .
452 . 85 VAL N N 128.17 . .
453 . 85 VAL H H 8.81 . .
454 . 85 VAL HA H 4.74 . .
455 . 85 VAL HB H 2.34 . .
456 . 86 LEU N N 110.94 . .
457 . 86 LEU H H 7.51 . .
458 . 86 LEU HA H 4.02 . .
459 . 86 LEU HB2 H 3.07 . .
460 . 86 LEU HB3 H 3.07 . .
461 . 86 LEU HG H 2.91 . .
462 . 86 LEU HD1 H 0.82 . .
463 . 86 LEU HD2 H 0.73 . .
464 . 87 PRO HA H 4.58 . .
465 . 87 PRO HB2 H 2.33 . .
466 . 87 PRO HB3 H 1.89 . .
467 . 87 PRO HG2 H 2.06 . .
468 . 87 PRO HG3 H 1.96 . .
469 . 87 PRO HD2 H 3.96 . .
470 . 87 PRO HD3 H 3.78 . .
471 . 88 LYS N N 121.33 . .
472 . 88 LYS H H 8.65 . .
473 . 88 LYS HA H 4.08 . .
474 . 88 LYS HB2 H 1.78 . .
475 . 88 LYS HB3 H 1.74 . .
476 . 88 LYS HG2 H 1.65 . .
477 . 88 LYS HG3 H 1.52 . .
478 . 88 LYS HD2 H 1.47 . .
479 . 88 LYS HE2 H 2.93 . .
480 . 88 LYS HE3 H 3.62 . .
481 . 89 ASP N N 121.35 . .
482 . 89 ASP H H 8.35 . .
483 . 89 ASP HA H 4.57 . .
484 . 89 ASP HB2 H 2.58 . .
485 . 89 ASP HB3 H 2.44 . .
486 . 90 ILE N N 123.91 . .
487 . 90 ILE H H 8.19 . .
488 . 90 ILE HA H 3.98 . .
489 . 90 ILE HB H 1.82 . .
490 . 90 ILE HG12 H 1.50 . .
491 . 90 ILE HG2 H 1.15 . .
492 . 90 ILE HD1 H 0.91 . .
493 . 91 PRO HA H 4.38 . .
494 . 91 PRO HB2 H 2.28 . .
495 . 91 PRO HB3 H 1.91 . .
496 . 91 PRO HG2 H 2.04 . .
497 . 91 PRO HG3 H 1.97 . .
498 . 91 PRO HD2 H 3.10 . .
499 . 91 PRO HD3 H 3.84 . .
500 . 92 GLY N N 110.43 . .
501 . 92 GLY H H 8.49 . .
502 . 92 GLY HA2 H 4.75 . .
503 . 92 GLY HA3 H 3.93 . .
504 . 93 LEU N N 122.66 . .
505 . 93 LEU H H 7.98 . .
506 . 93 LEU HA H 4.25 . .
507 . 93 LEU HB2 H 1.55 . .
508 . 93 LEU HB3 H 1.55 . .
509 . 93 LEU HG H 0.87 . .
510 . 93 LEU HD1 H 0.81 . .
511 . 94 GLU N N 122.31 . .
512 . 94 GLU H H 8.47 . .
513 . 94 GLU HA H 4.14 . .
514 . 94 GLU HB2 H 1.85 . .
515 . 94 GLU HB3 H 1.85 . .
516 . 94 GLU HG2 H 2.19 . .
517 . 94 GLU HG3 H 2.10 . .
stop_
save_
########################
# Coupling constants #
########################
save_coupling_constants
_Saveframe_category coupling_constants
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Spectrometer_frequency_1H 500
_Mol_system_component_name 'scaffoldin protein'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 2 GLN H 2 GLN HA 8.00 . . .
2 3JHNHA 3 ASP H 3 ASP HA 7.98 . . .
3 3JHNHA 5 THR H 5 THR HA 8.98 . . .
4 3JHNHA 6 ILE H 6 ILE HA 9.14 . . .
5 3JHNHA 7 ASN H 7 ASN HA 5.25 . . .
6 3JHNHA 9 THR H 9 THR HA 8.19 . . .
7 3JHNHA 10 SER H 10 SER HA 8.04 . . .
8 3JHNHA 11 ILE H 11 ILE HA 9.16 . . .
9 3JHNHA 12 SER H 12 SER HA 9.05 . . .
10 3JHNHA 13 ALA H 13 ALA HA 7.93 . . .
11 3JHNHA 14 LYS H 14 LYS HA 5.25 . . .
12 3JHNHA 15 ALA H 15 ALA HA 5.80 . . .
13 3JHNHA 17 SER H 17 SER HA 9.93 . . .
14 3JHNHA 18 PHE H 18 PHE HA 5.24 . . .
15 3JHNHA 19 ALA H 19 ALA HA 9.20 . . .
16 3JHNHA 20 ASP H 20 ASP HA 4.74 . . .
17 3JHNHA 21 THR H 21 THR HA 10.13 . . .
18 3JHNHA 22 LYS H 22 LYS HA 8.47 . . .
19 3JHNHA 23 ILE H 23 ILE HA 8.40 . . .
20 3JHNHA 24 THR H 24 THR HA 11.17 . . .
21 3JHNHA 25 LEU H 25 LEU HA 9.90 . . .
22 3JHNHA 26 THR H 26 THR HA 9.85 . . .
23 3JHNHA 28 ASN H 28 ASN HA 6.45 . . .
24 3JHNHA 30 ASN H 30 ASN HA 9.66 . . .
25 3JHNHA 31 THR H 31 THR HA 9.23 . . .
26 3JHNHA 32 PHE H 32 PHE HA 11 . . .
27 3JHNHA 33 ASN H 33 ASN HA 10.33 . . .
28 3JHNHA 35 ILE H 35 ILE HA 8.64 . . .
29 3JHNHA 36 SER H 36 SER HA 6.74 . . .
30 3JHNHA 37 GLU H 37 GLU HA 4.65 . . .
31 3JHNHA 38 LEU H 38 LEU HA 8.83 . . .
32 3JHNHA 39 GLN H 39 GLN HA 4.97 . . .
33 3JHNHA 40 SER H 40 SER HA 6.7 . . .
34 3JHNHA 41 SER H 41 SER HA 4.97 . . .
35 3JHNHA 42 GLN H 42 GLN HA 4.24 . . .
36 3JHNHA 43 TYR H 43 TYR HA 5.83 . . .
37 3JHNHA 44 THR H 44 THR HA 9.70 . . .
38 3JHNHA 45 LYS H 45 LYS HA 7.50 . . .
39 3JHNHA 47 THR H 47 THR HA 6.95 . . .
40 3JHNHA 48 ASN H 48 ASN HA 7.71 . . .
41 3JHNHA 49 GLU H 49 GLU HA 7.24 . . .
42 3JHNHA 50 VAL H 50 VAL HA 8.20 . . .
43 3JHNHA 51 THR H 51 THR HA 8.91 . . .
44 3JHNHA 52 LEU H 52 LEU HA 7.63 . . .
45 3JHNHA 53 LEU H 53 LEU HA 10.71 . . .
46 3JHNHA 54 ALA H 54 ALA HA 7.69 . . .
47 3JHNHA 56 TYR H 56 TYR HA 7.95 . . .
48 3JHNHA 57 LEU H 57 LEU HA 4.07 . . .
49 3JHNHA 58 ASN H 58 ASN HA 6.43 . . .
50 3JHNHA 59 THR H 59 THR HA 9.18 . . .
51 3JHNHA 60 LEU H 60 LEU HA 5.52 . . .
52 3JHNHA 62 GLU H 62 GLU HA 4.39 . . .
53 3JHNHA 63 ASN H 63 ASN HA 5.39 . . .
54 3JHNHA 64 THR H 64 THR HA 8.31 . . .
55 3JHNHA 65 THR H 65 THR HA 8.77 . . .
56 3JHNHA 66 LYS H 66 LYS HA 5.79 . . .
57 3JHNHA 67 THR H 67 THR HA 9.00 . . .
58 3JHNHA 68 LEU H 68 LEU HA 8.27 . . .
59 3JHNHA 69 THR H 69 THR HA 11.11 . . .
60 3JHNHA 70 PHE H 70 PHE HA 9.04 . . .
61 3JHNHA 71 ASP H 71 ASP HA 8.00 . . .
62 3JHNHA 72 PHE H 72 PHE HA 12.00 . . .
63 3JHNHA 74 VAL H 74 VAL HA 10.00 . . .
64 3JHNHA 76 THR H 76 THR HA 5.39 . . .
65 3JHNHA 77 LYS H 77 LYS HA 8.14 . . .
66 3JHNHA 78 ASN H 78 ASN HA 3.86 . . .
67 3JHNHA 80 LYS H 80 LYS HA 9.98 . . .
68 3JHNHA 81 LEU H 81 LEU HA 9.91 . . .
69 3JHNHA 82 THR H 82 THR HA 9.20 . . .
70 3JHNHA 83 ILE H 83 ILE HA 9.61 . . .
71 3JHNHA 84 THR H 84 THR HA 9.32 . . .
72 3JHNHA 85 VAL H 85 VAL HA 8.98 . . .
73 3JHNHA 86 LEU H 86 LEU HA 7.12 . . .
74 3JHNHA 89 ASP H 89 ASP HA 7.57 . . .
75 3JHNHA 90 ILE H 90 ILE HA 7.62 . . .
76 3JHNHA 93 LEU H 93 LEU HA 6.63 . . .
77 3JHNHA 94 GLU H 94 GLU HA 5.72 . . .
stop_
save_