data_5375
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Structure of BPTI_8A mutant
;
_BMRB_accession_number 5375
_BMRB_flat_file_name bmr5375.str
_Entry_type original
_Submission_date 2002-05-13
_Accession_date 2002-05-13
_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 Cierpicki T. . .
2 Otlewski J. . .
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" 322
"coupling constants" 39
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-01-06 original BMRB .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
5381 'BPTI A16V mutant.'
stop_
_Original_release_date 2002-05-13
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
NMR Structures of Two Variants of Bovine Pancreatic Trypsin Inhibitor (BPTI)
reveal Unexpected Influence of Mutations on Protein Structure and Stability
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22195730
_PubMed_ID 12206780
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Cierpicki T. . .
2 Otlewski J. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 321
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 647
_Page_last 658
_Year 2002
_Details .
loop_
_Keyword
BPTI
'Kunitz fold'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_anneal10_2
_Saveframe_category molecular_system
_Mol_system_name anneal10_2
_Abbreviation_common BPTI_8A
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'pancreatic trypsin inhibitor' $BPTI_8A
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_BPTI_8A
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'pancreatic trypsin inhibitor'
_Abbreviation_common BPTI_8A
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 58
_Mol_residue_sequence
;
RPDFCLEPPYAGACRAAAAR
YFYNAKAGLCQTFAYGACAA
KRNNFKSAEDCLRTCGGA
;
loop_
_Residue_seq_code
_Residue_label
1 ARG 2 PRO 3 ASP 4 PHE 5 CYS
6 LEU 7 GLU 8 PRO 9 PRO 10 TYR
11 ALA 12 GLY 13 ALA 14 CYS 15 ARG
16 ALA 17 ALA 18 ALA 19 ALA 20 ARG
21 TYR 22 PHE 23 TYR 24 ASN 25 ALA
26 LYS 27 ALA 28 GLY 29 LEU 30 CYS
31 GLN 32 THR 33 PHE 34 ALA 35 TYR
36 GLY 37 ALA 38 CYS 39 ALA 40 ALA
41 LYS 42 ARG 43 ASN 44 ASN 45 PHE
46 LYS 47 SER 48 ALA 49 GLU 50 ASP
51 CYS 52 LEU 53 ARG 54 THR 55 CYS
56 GLY 57 GLY 58 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
PDB 1LD6 'Structure Of Bpti_8a Mutant' 100.00 58 100.00 100.00 2.11e-24
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$BPTI_8A Cow 9913 Eukaryota Metazoa Bos taurus
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
$BPTI_8A 'recombinant technology' 'E. coli' Escherichia coli . .
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
$BPTI_8A 3 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.8
loop_
_Task
processing
stop_
_Details 'Delaglio, F.; Grzesiek, S.; Vuister, G.; Zhu, G.; Pfeifer, J.; Bax, A.'
save_
save_Sparky
_Saveframe_category software
_Name SPARKY
_Version 3.95
loop_
_Task
'data analysis'
stop_
_Details 'Goddard, T.D.; Kneller, D.G.'
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'structure solution'
stop_
_Details 'Guntert, P.; Mumenthaler, C.; Herrmann, T.'
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
refinement
stop_
_Details
;
Brunger, A.T.; Adams, P.D.; Clore, G.M.; DeLano, W.L., Gros,P.;
Grosse-Kunstleve, R.W.; Jiang, J.S.; Kuszewski, J.; Nilges, M.;
Pannu, N.S.; Read, R.J.; Rice, L.M.; Simonson, T.; Warren, G.L.
;
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_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label .
save_
save_2D_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_DQF-COSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-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
'ionic strength' 0 . M
pH 2.9 . n/a
pressure 1 . atm
temperature 298 . 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
. H 1 . ppm . . . . . .
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 TOCSY'
'2D NOESY'
DQF-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 'pancreatic trypsin inhibitor'
_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 4.38 . 1
2 . 1 ARG HB2 H 1.83 . 2
3 . 1 ARG HB3 H 1.90 . 2
4 . 1 ARG HG2 H 1.38 . 2
5 . 1 ARG HG3 H 1.51 . 2
6 . 1 ARG HD2 H 2.85 . 2
7 . 1 ARG HD3 H 3.07 . 2
8 . 1 ARG HE H 7.11 . 1
9 . 2 PRO HA H 4.32 . 1
10 . 2 PRO HB2 H 0.91 . 1
11 . 2 PRO HB3 H 2.02 . 1
12 . 2 PRO HG2 H 1.62 . 1
13 . 2 PRO HG3 H 1.89 . 1
14 . 2 PRO HD2 H 3.61 . 1
15 . 2 PRO HD3 H 3.73 . 1
16 . 3 ASP H H 8.95 . 1
17 . 3 ASP HA H 4.31 . 1
18 . 3 ASP HB2 H 2.96 . 1
19 . 3 ASP HB3 H 2.96 . 1
20 . 4 PHE H H 7.70 . 1
21 . 4 PHE HA H 4.60 . 1
22 . 4 PHE HB2 H 3.42 . 1
23 . 4 PHE HB3 H 3.06 . 1
24 . 4 PHE HD1 H 7.08 . 1
25 . 4 PHE HD2 H 7.08 . 1
26 . 4 PHE HE1 H 7.40 . 1
27 . 4 PHE HE2 H 7.40 . 1
28 . 4 PHE HZ H 7.36 . 1
29 . 5 CYS H H 7.37 . 1
30 . 5 CYS HA H 4.38 . 1
31 . 5 CYS HB2 H 2.78 . 2
32 . 5 CYS HB3 H 2.84 . 2
33 . 6 LEU H H 7.57 . 1
34 . 6 LEU HA H 4.32 . 1
35 . 6 LEU HB2 H 1.88 . 1
36 . 6 LEU HB3 H 1.88 . 1
37 . 6 LEU HG H 1.69 . 1
38 . 6 LEU HD1 H 0.97 . 1
39 . 6 LEU HD2 H 0.86 . 1
40 . 7 GLU H H 7.46 . 1
41 . 7 GLU HA H 4.84 . 1
42 . 7 GLU HB2 H 2.23 . 2
43 . 7 GLU HB3 H 2.38 . 2
44 . 7 GLU HG2 H 2.67 . 1
45 . 7 GLU HG3 H 2.67 . 1
46 . 8 PRO HA H 4.88 . 1
47 . 8 PRO HB2 H 2.37 . 1
48 . 8 PRO HB3 H 2.37 . 1
49 . 8 PRO HG2 H 2.09 . 2
50 . 8 PRO HG3 H 2.14 . 2
51 . 8 PRO HD2 H 3.88 . 2
52 . 8 PRO HD3 H 4.25 . 2
53 . 9 PRO HA H 4.72 . 1
54 . 9 PRO HB2 H 1.48 . 2
55 . 9 PRO HB3 H 1.84 . 2
56 . 9 PRO HG2 H 0.95 . 2
57 . 9 PRO HG3 H 1.08 . 2
58 . 9 PRO HD2 H 3.23 . 1
59 . 9 PRO HD3 H 3.23 . 1
60 . 10 TYR H H 8.25 . 1
61 . 10 TYR HA H 4.90 . 1
62 . 10 TYR HB2 H 2.90 . 2
63 . 10 TYR HB3 H 3.00 . 2
64 . 10 TYR HD1 H 6.95 . 1
65 . 10 TYR HD2 H 6.95 . 1
66 . 10 TYR HE1 H 6.67 . 1
67 . 10 TYR HE2 H 6.67 . 1
68 . 11 ALA H H 8.47 . 1
69 . 11 ALA HA H 4.47 . 1
70 . 11 ALA HB H 1.36 . 1
71 . 12 GLY H H 7.71 . 1
72 . 12 GLY HA2 H 3.83 . 2
73 . 12 GLY HA3 H 4.17 . 2
74 . 13 ALA H H 8.51 . 1
75 . 13 ALA HA H 4.41 . 1
76 . 13 ALA HB H 1.31 . 1
77 . 14 CYS H H 7.79 . 1
78 . 14 CYS HA H 4.44 . 1
79 . 14 CYS HB2 H 2.61 . 2
80 . 14 CYS HB3 H 3.30 . 2
81 . 15 ARG H H 8.40 . 1
82 . 15 ARG HA H 4.23 . 1
83 . 15 ARG HB2 H 1.69 . 2
84 . 15 ARG HB3 H 1.80 . 2
85 . 15 ARG HG2 H 1.56 . 2
86 . 15 ARG HG3 H 1.60 . 2
87 . 15 ARG HD2 H 3.17 . 1
88 . 15 ARG HD3 H 3.17 . 1
89 . 15 ARG HE H 7.17 . 1
90 . 16 ALA H H 8.27 . 1
91 . 16 ALA HA H 4.21 . 1
92 . 16 ALA HB H 1.32 . 1
93 . 17 ALA H H 8.30 . 1
94 . 17 ALA HA H 4.36 . 1
95 . 17 ALA HB H 1.30 . 1
96 . 18 ALA H H 7.86 . 1
97 . 18 ALA HA H 4.31 . 1
98 . 18 ALA HB H 1.38 . 1
99 . 19 ALA H H 8.35 . 1
100 . 19 ALA HA H 4.35 . 1
101 . 19 ALA HB H 1.40 . 1
102 . 20 ARG H H 7.83 . 1
103 . 20 ARG HA H 4.88 . 1
104 . 20 ARG HB2 H 1.80 . 2
105 . 20 ARG HB3 H 2.29 . 2
106 . 20 ARG HG2 H 1.64 . 2
107 . 20 ARG HG3 H 1.68 . 2
108 . 20 ARG HD2 H 3.19 . 2
109 . 20 ARG HD3 H 3.30 . 2
110 . 20 ARG HE H 7.63 . 1
111 . 21 TYR H H 9.03 . 1
112 . 21 TYR HA H 5.29 . 1
113 . 21 TYR HB2 H 2.60 . 1
114 . 21 TYR HB3 H 2.60 . 1
115 . 21 TYR HD1 H 6.61 . 1
116 . 21 TYR HD2 H 6.61 . 1
117 . 21 TYR HE1 H 6.76 . 1
118 . 21 TYR HE2 H 6.76 . 1
119 . 22 PHE H H 9.21 . 1
120 . 22 PHE HA H 5.16 . 1
121 . 22 PHE HB2 H 2.84 . 1
122 . 22 PHE HB3 H 3.00 . 1
123 . 22 PHE HD1 H 6.45 . 1
124 . 22 PHE HD2 H 6.45 . 1
125 . 22 PHE HE1 H 6.96 . 1
126 . 22 PHE HE2 H 6.96 . 1
127 . 22 PHE HZ H 7.16 . 1
128 . 23 TYR H H 10.45 . 1
129 . 23 TYR HA H 4.36 . 1
130 . 23 TYR HB2 H 2.80 . 1
131 . 23 TYR HB3 H 3.49 . 1
132 . 23 TYR HD1 H 7.20 . 1
133 . 23 TYR HD2 H 7.20 . 1
134 . 23 TYR HE1 H 6.36 . 1
135 . 23 TYR HE2 H 6.36 . 1
136 . 24 ASN H H 8.22 . 1
137 . 24 ASN HA H 4.62 . 1
138 . 24 ASN HB2 H 2.24 . 1
139 . 24 ASN HB3 H 2.91 . 1
140 . 24 ASN HD21 H 7.16 . 1
141 . 24 ASN HD22 H 7.92 . 1
142 . 25 ALA H H 8.60 . 1
143 . 25 ALA HA H 3.81 . 1
144 . 25 ALA HB H 1.62 . 1
145 . 26 LYS H H 7.97 . 1
146 . 26 LYS HA H 4.09 . 1
147 . 26 LYS HB2 H 1.92 . 1
148 . 26 LYS HB3 H 1.92 . 1
149 . 26 LYS HG2 H 1.46 . 2
150 . 26 LYS HG3 H 1.54 . 2
151 . 26 LYS HD2 H 1.74 . 1
152 . 26 LYS HD3 H 1.74 . 1
153 . 26 LYS HE2 H 3.05 . 1
154 . 26 LYS HE3 H 3.05 . 1
155 . 27 ALA H H 6.84 . 1
156 . 27 ALA HA H 4.29 . 1
157 . 27 ALA HB H 1.17 . 1
158 . 28 GLY H H 8.12 . 1
159 . 28 GLY HA2 H 3.63 . 1
160 . 28 GLY HA3 H 3.90 . 1
161 . 29 LEU H H 6.77 . 1
162 . 29 LEU HA H 4.65 . 1
163 . 29 LEU HB2 H 1.36 . 2
164 . 29 LEU HB3 H 1.61 . 2
165 . 29 LEU HG H 1.61 . 1
166 . 29 LEU HD1 H 0.74 . 2
167 . 29 LEU HD2 H 0.84 . 2
168 . 30 CYS H H 8.79 . 1
169 . 30 CYS HA H 5.42 . 1
170 . 30 CYS HB2 H 2.53 . 1
171 . 30 CYS HB3 H 3.45 . 1
172 . 31 GLN H H 8.80 . 1
173 . 31 GLN HA H 4.75 . 1
174 . 31 GLN HB2 H 1.51 . 2
175 . 31 GLN HG2 H 1.80 . 2
176 . 31 GLN HG3 H 1.91 . 2
177 . 31 GLN HE21 H 6.95 . 2
178 . 31 GLN HE22 H 7.43 . 2
179 . 32 THR H H 7.99 . 1
180 . 32 THR HA H 4.85 . 1
181 . 32 THR HB H 4.18 . 1
182 . 32 THR HG2 H 0.66 . 1
183 . 33 PHE H H 7.66 . 1
184 . 33 PHE HA H 4.47 . 1
185 . 33 PHE HB2 H 2.87 . 2
186 . 33 PHE HB3 H 3.09 . 2
187 . 33 PHE HD1 H 7.04 . 1
188 . 33 PHE HD2 H 7.04 . 1
189 . 33 PHE HE1 H 7.14 . 1
190 . 33 PHE HE2 H 7.14 . 1
191 . 33 PHE HZ H 7.54 . 1
192 . 34 ALA H H 8.75 . 1
193 . 34 ALA HA H 4.40 . 1
194 . 34 ALA HB H 1.41 . 1
195 . 35 TYR HA H 4.29 . 1
196 . 35 TYR HB2 H 2.96 . 2
197 . 35 TYR HB3 H 3.06 . 2
198 . 35 TYR HD1 H 7.13 . 1
199 . 35 TYR HD2 H 7.13 . 1
200 . 35 TYR HE1 H 6.83 . 1
201 . 35 TYR HE2 H 6.83 . 1
202 . 36 GLY H H 8.28 . 1
203 . 36 GLY HA2 H 3.65 . 2
204 . 36 GLY HA3 H 3.94 . 2
205 . 37 ALA H H 7.75 . 1
206 . 37 ALA HA H 4.40 . 1
207 . 37 ALA HB H 1.26 . 1
208 . 38 CYS H H 8.62 . 1
209 . 38 CYS HA H 4.33 . 1
210 . 38 CYS HB2 H 1.69 . 2
211 . 38 CYS HB3 H 2.63 . 2
212 . 39 ALA H H 7.83 . 1
213 . 39 ALA HA H 4.12 . 1
214 . 39 ALA HB H 1.10 . 1
215 . 40 ALA H H 8.50 . 1
216 . 40 ALA HA H 4.46 . 1
217 . 40 ALA HB H 1.50 . 1
218 . 41 LYS H H 8.32 . 1
219 . 41 LYS HA H 3.90 . 1
220 . 41 LYS HB2 H 1.78 . 2
221 . 41 LYS HB3 H 1.82 . 2
222 . 41 LYS HG2 H 1.40 . 2
223 . 41 LYS HG3 H 1.46 . 2
224 . 41 LYS HD2 H 1.68 . 1
225 . 41 LYS HD3 H 1.68 . 1
226 . 41 LYS HE2 H 2.99 . 1
227 . 41 LYS HE3 H 2.99 . 1
228 . 42 ARG H H 8.01 . 1
229 . 42 ARG HA H 3.81 . 1
230 . 42 ARG HB2 H 0.78 . 2
231 . 42 ARG HB3 H 1.21 . 2
232 . 42 ARG HG2 H 1.38 . 1
233 . 42 ARG HG3 H 1.38 . 1
234 . 42 ARG HD2 H 2.83 . 2
235 . 42 ARG HD3 H 2.89 . 2
236 . 42 ARG HE H 6.97 . 1
237 . 43 ASN H H 7.68 . 1
238 . 43 ASN HA H 5.02 . 1
239 . 43 ASN HB2 H 3.29 . 1
240 . 43 ASN HB3 H 3.36 . 1
241 . 43 ASN HD21 H 7.92 . 2
242 . 43 ASN HD22 H 8.24 . 2
243 . 44 ASN H H 6.24 . 1
244 . 44 ASN HA H 5.16 . 1
245 . 44 ASN HB2 H 2.53 . 2
246 . 44 ASN HB3 H 2.72 . 2
247 . 44 ASN HD21 H 6.61 . 2
248 . 44 ASN HD22 H 7.23 . 2
249 . 45 PHE H H 10.17 . 1
250 . 45 PHE HA H 5.13 . 1
251 . 45 PHE HB2 H 2.77 . 1
252 . 45 PHE HB3 H 3.37 . 1
253 . 45 PHE HD1 H 7.35 . 1
254 . 45 PHE HD2 H 7.35 . 1
255 . 45 PHE HE1 H 7.89 . 1
256 . 45 PHE HE2 H 7.89 . 1
257 . 45 PHE HZ H 7.67 . 1
258 . 46 LYS H H 9.66 . 1
259 . 46 LYS HA H 4.44 . 1
260 . 46 LYS HB2 H 2.05 . 1
261 . 46 LYS HB3 H 2.05 . 1
262 . 46 LYS HG2 H 1.60 . 2
263 . 46 LYS HG3 H 1.63 . 2
264 . 46 LYS HD2 H 1.80 . 1
265 . 46 LYS HD3 H 1.80 . 1
266 . 46 LYS HE2 H 3.08 . 1
267 . 46 LYS HE3 H 3.08 . 1
268 . 46 LYS HZ H 7.62 . 3
269 . 47 SER H H 7.44 . 1
270 . 47 SER HA H 4.68 . 1
271 . 47 SER HB2 H 4.12 . 1
272 . 47 SER HB3 H 3.87 . 1
273 . 48 ALA H H 8.26 . 1
274 . 48 ALA HA H 3.03 . 1
275 . 48 ALA HB H 0.94 . 1
276 . 49 GLU H H 8.33 . 1
277 . 49 GLU HA H 3.91 . 1
278 . 49 GLU HB2 H 1.86 . 2
279 . 49 GLU HB3 H 2.05 . 2
280 . 49 GLU HG2 H 2.40 . 2
281 . 49 GLU HG3 H 2.47 . 2
282 . 50 ASP H H 7.89 . 1
283 . 50 ASP HA H 4.30 . 1
284 . 50 ASP HB2 H 2.84 . 2
285 . 50 ASP HB3 H 3.04 . 2
286 . 51 CYS H H 7.04 . 1
287 . 51 CYS HA H 1.80 . 1
288 . 51 CYS HB2 H 2.78 . 1
289 . 51 CYS HB3 H 3.16 . 1
290 . 52 LEU H H 8.56 . 1
291 . 52 LEU HA H 3.68 . 1
292 . 52 LEU HB2 H 1.48 . 2
293 . 52 LEU HB3 H 1.66 . 2
294 . 52 LEU HG H 1.66 . 1
295 . 52 LEU HD1 H 0.83 . 2
296 . 52 LEU HD2 H 0.87 . 2
297 . 53 ARG H H 8.33 . 1
298 . 53 ARG HA H 3.95 . 1
299 . 53 ARG HB2 H 1.84 . 2
300 . 53 ARG HB3 H 1.89 . 2
301 . 53 ARG HG2 H 1.63 . 2
302 . 53 ARG HG3 H 1.74 . 2
303 . 53 ARG HD2 H 3.19 . 1
304 . 53 ARG HD3 H 3.19 . 1
305 . 53 ARG HE H 7.17 . 1
306 . 54 THR H H 7.40 . 1
307 . 54 THR HA H 4.09 . 1
308 . 54 THR HB H 3.98 . 1
309 . 54 THR HG2 H 1.62 . 1
310 . 55 CYS H H 8.26 . 1
311 . 55 CYS HA H 4.67 . 1
312 . 55 CYS HB2 H 2.04 . 2
313 . 55 CYS HB3 H 2.21 . 2
314 . 56 GLY H H 7.93 . 1
315 . 56 GLY HA2 H 3.79 . 2
316 . 56 GLY HA3 H 3.88 . 2
317 . 57 GLY H H 8.22 . 1
318 . 57 GLY HA2 H 3.92 . 1
319 . 57 GLY HA3 H 3.92 . 1
320 . 58 ALA H H 8.14 . 1
321 . 58 ALA HA H 4.20 . 1
322 . 58 ALA HB H 1.36 . 1
stop_
save_
########################
# Coupling constants #
########################
save_coupling_constant_set_1
_Saveframe_category coupling_constants
_Details .
loop_
_Experiment_label
'2D TOCSY'
'2D NOESY'
DQF-COSY
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Spectrometer_frequency_1H 500
_Mol_system_component_name 'pancreatic trypsin inhibitor'
_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 3 ASP H 3 ASP HA 2.8 . . 1.0
2 3JHNHA 5 CYS H 5 CYS HA 4.0 . . 1.0
3 3JHNHA 6 LEU H 6 LEU HA 7.8 . . 1.0
4 3JHNHA 7 GLU H 7 GLU HA 5.7 . . 1.0
5 3JHNHA 10 TYR H 10 TYR HA 7.5 . . 1.0
6 3JHNHA 13 ALA H 13 ALA HA 7.2 . . 1.0
7 3JHNHA 14 CYS H 14 CYS HA 6.2 . . 1.0
8 3JHNHA 15 ARG H 15 ARG HA 7.3 . . 1.0
9 3JHNHA 16 ALA H 16 ALA HA 6.1 . . 1.0
10 3JHNHA 17 ALA H 17 ALA HA 7.0 . . 1.0
11 3JHNHA 18 ALA H 18 ALA HA 5.5 . . 1.0
12 3JHNHA 19 ALA H 19 ALA HA 6.3 . . 1.0
13 3JHNHA 20 ARG H 20 ARG HA 9.0 . . 1.0
14 3JHNHA 21 TYR H 21 TYR HA 10.2 . . 1.0
15 3JHNHA 22 PHE H 22 PHE HA 8.7 . . 1.0
16 3JHNHA 23 TYR H 23 TYR HA 6.9 . . 1.0
17 3JHNHA 25 ALA H 25 ALA HA 3.8 . . 1.0
18 3JHNHA 27 ALA H 27 ALA HA 8.2 . . 1.0
19 3JHNHA 30 CYS H 30 CYS HA 9.0 . . 1.0
20 3JHNHA 31 GLN H 31 GLN HA 9.7 . . 1.0
21 3JHNHA 32 THR H 32 THR HA 5.8 . . 1.0
22 3JHNHA 34 ALA H 34 ALA HA 6.0 . . 1.0
23 3JHNHA 37 ALA H 37 ALA HA 4.7 . . 1.0
24 3JHNHA 38 CYS H 38 CYS HA 7.3 . . 1.0
25 3JHNHA 39 ALA H 39 ALA HA 5.4 . . 1.0
26 3JHNHA 41 LYS H 41 LYS HA 4.3 . . 1.0
27 3JHNHA 42 ARG H 42 ARG HA 7.6 . . 1.0
28 3JHNHA 43 ASN H 43 ASN HA 7.6 . . 1.0
29 3JHNHA 44 ASN H 44 ASN HA 7.7 . . 1.0
30 3JHNHA 45 PHE H 45 PHE HA 10.1 . . 1.0
31 3JHNHA 46 LYS H 46 LYS HA 4.4 . . 1.0
32 3JHNHA 48 ALA H 48 ALA HA 3.8 . . 1.0
33 3JHNHA 49 GLU H 49 GLU HA 4.3 . . 1.0
34 3JHNHA 50 ASP H 50 ASP HA 4.6 . . 1.0
35 3JHNHA 51 CYS H 51 CYS HA 4.8 . . 1.0
36 3JHNHA 52 LEU H 52 LEU HA 3.7 . . 1.0
37 3JHNHA 53 ARG H 53 ARG HA 4.5 . . 1.0
38 3JHNHA 54 THR H 54 THR HA 6.6 . . 1.0
39 3JHNHA 58 ALA H 58 ALA HA 6.3 . . 1.0
stop_
save_