data_6302
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution structure of a diiron protein model: Due DF2-TURN_MUTANTturn mutant
;
_BMRB_accession_number 6302
_BMRB_flat_file_name bmr6302.str
_Entry_type original
_Submission_date 2004-08-26
_Accession_date 2004-08-26
_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 Maglio O. . .
2 Nastri F. . .
3 Calhoun J. R. .
4 Lahr S. . .
5 Pavone V. . .
6 DeGrado W. F. .
7 Lombardi A. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 348
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-05-19 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
6303 'DIIRON in DF2'
stop_
_Original_release_date 2005-05-19
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Artificial diiron proteins: From structure to function'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15700297
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Calhoun J. R. .
2 Nastri F. . .
3 Maglio O. . .
4 Pavone V. . .
5 Lombardi A. . .
6 DeGrado W. F. .
stop_
_Journal_abbreviation Biopolymers
_Journal_volume 80
_Journal_issue 2-3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 264
_Page_last 278
_Year 2005
_Details .
loop_
_Keyword
'Diiron proteins'
'four-helix bundle'
'inter-helical loops'
'protein design'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_DF2-TURN_MUTANT
_Saveframe_category molecular_system
_Mol_system_name 'Four-helix bundle model'
_Abbreviation_common 'Four-helix bundle model'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Four-helix bundle chain A' $DF2-TURN_MUTANT
'Four-helix bundle chain B' $DF2-TURN_MUTANT
'ZINC (II) ION 1' $ZN
'ZINC (II) ION 2' $ZN
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_DF2-TURN_MUTANT
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Four-helix bundle model'
_Abbreviation_common 'Four-helix bundle model'
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 53
_Mol_residue_sequence
;
MDYLRELYKLEQQAMKLYRE
ASEKARNPEKKSVLQKILED
EEKHIEWLETING
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ASP 3 TYR 4 LEU 5 ARG
6 GLU 7 LEU 8 TYR 9 LYS 10 LEU
11 GLU 12 GLN 13 GLN 14 ALA 15 MET
16 LYS 17 LEU 18 TYR 19 ARG 20 GLU
21 ALA 22 SER 23 GLU 24 LYS 25 ALA
26 ARG 27 ASN 28 PRO 29 GLU 30 LYS
31 LYS 32 SER 33 VAL 34 LEU 35 GLN
36 LYS 37 ILE 38 LEU 39 GLU 40 ASP
41 GLU 42 GLU 43 LYS 44 HIS 45 ILE
46 GLU 47 TRP 48 LEU 49 GLU 50 THR
51 ILE 52 ASN 53 GLY
stop_
_Sequence_homology_query_date .
_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 1MFT 'Crystal Structure Of Four-Helix Bundle Model' 100.00 53 100.00 100.00 1.04e-21
PDB 1U7M 'Solution Structure Of A Diiron Protein Model: Due Ferri(Ii) Turn Mutant' 100.00 53 100.00 100.00 1.04e-21
stop_
save_
#############
# Ligands #
#############
save_ZN
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "ZN (ZINC ION)"
_BMRB_code .
_PDB_code ZN
_Molecular_mass 65.409
_Mol_charge 2
_Mol_paramagnetic .
_Mol_aromatic no
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jun 15 12:20:01 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
ZN ZN ZN . 2 . ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$DF2-TURN_MUTANT 'E. coli' 562 Bacteria . Escherichia coli
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
$DF2-TURN_MUTANT 'recombinant technology' Bacteria Escherichia coli BL21(DE3) 'Plasmid PET28A'
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
$DF2-TURN_MUTANT 0.5 mM .
'phosphate buffer' 50 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.7
loop_
_Task
processing
stop_
_Details 'Delaglio et al.'
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'structure solution'
stop_
_Details 'Guentert et al.'
save_
save_AMBER
_Saveframe_category software
_Name AMBER
_Version 7.0
loop_
_Task
refinement
stop_
_Details 'Case et al.'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label $sample_1
save_
save_2D_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 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_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 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_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.1 . pH
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
_Indirect_shift_ratio
_Indirect_shift_ratio_citation_label
_Correction_value_citation_label
TSP H 1 'methyl protons' ppm 0.0 internal . . . . 1.0 $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 'Four-helix bundle chain A'
_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 . 3 TYR H H 8.14 . 1
2 . 3 TYR HA H 3.97 . 1
3 . 3 TYR HB2 H 2.94 . 1
4 . 3 TYR HB3 H 2.94 . 1
5 . 3 TYR HD1 H 7.13 . 1
6 . 3 TYR HD2 H 7.13 . 1
7 . 3 TYR HE1 H 6.85 . 1
8 . 3 TYR HE2 H 6.85 . 1
9 . 4 LEU H H 8.22 . 1
10 . 4 LEU HA H 4.09 . 1
11 . 4 LEU HB2 H 1.97 . 1
12 . 4 LEU HB3 H 1.97 . 1
13 . 4 LEU HG H 1.62 . 1
14 . 4 LEU HD1 H 0.96 . 1
15 . 4 LEU HD2 H 0.96 . 1
16 . 5 ARG H H 7.69 . 1
17 . 5 ARG HA H 4.10 . 1
18 . 5 ARG HB2 H 1.77 . 1
19 . 5 ARG HB3 H 1.77 . 1
20 . 5 ARG HG2 H 2.01 . 1
21 . 5 ARG HG3 H 2.01 . 1
22 . 5 ARG HD2 H 3.22 . 1
23 . 5 ARG HD3 H 3.22 . 1
24 . 5 ARG HE H 7.28 . 1
25 . 6 GLU H H 7.96 . 1
26 . 6 GLU HA H 4.12 . 1
27 . 6 GLU HB2 H 2.03 . 2
28 . 6 GLU HB3 H 1.85 . 2
29 . 6 GLU HG2 H 2.37 . 1
30 . 6 GLU HG3 H 2.37 . 1
31 . 7 LEU H H 8.64 . 1
32 . 7 LEU HA H 3.92 . 1
33 . 7 LEU HB2 H 1.94 . 1
34 . 7 LEU HB3 H 1.94 . 1
35 . 7 LEU HG H 1.61 . 1
36 . 7 LEU HD1 H 0.50 . 2
37 . 7 LEU HD2 H -0.06 . 2
38 . 8 TYR H H 8.22 . 1
39 . 8 TYR HA H 3.94 . 1
40 . 8 TYR HB2 H 3.22 . 2
41 . 8 TYR HB3 H 3.18 . 2
42 . 8 TYR HD1 H 7.07 . 1
43 . 8 TYR HD2 H 7.07 . 1
44 . 8 TYR HE1 H 6.89 . 1
45 . 8 TYR HE2 H 6.89 . 1
46 . 9 LYS H H 7.77 . 1
47 . 9 LYS HA H 4.09 . 1
48 . 9 LYS HB2 H 2.00 . 1
49 . 9 LYS HB3 H 2.00 . 1
50 . 9 LYS HG2 H 1.64 . 1
51 . 9 LYS HG3 H 1.64 . 1
52 . 9 LYS HD2 H 1.80 . 1
53 . 9 LYS HD3 H 1.80 . 1
54 . 9 LYS HE2 H 2.95 . 1
55 . 9 LYS HE3 H 2.95 . 1
56 . 10 LEU H H 7.93 . 1
57 . 10 LEU HA H 4.17 . 1
58 . 10 LEU HB2 H 2.04 . 1
59 . 10 LEU HB3 H 2.04 . 1
60 . 10 LEU HG H 1.75 . 1
61 . 10 LEU HD1 H 0.97 . 1
62 . 10 LEU HD2 H 0.97 . 1
63 . 11 GLU H H 8.58 . 1
64 . 11 GLU HA H 4.54 . 1
65 . 11 GLU HB2 H 2.15 . 2
66 . 11 GLU HB3 H 1.99 . 2
67 . 11 GLU HG2 H 2.86 . 2
68 . 11 GLU HG3 H 2.35 . 2
69 . 12 GLN H H 8.24 . 1
70 . 12 GLN HA H 3.95 . 1
71 . 12 GLN HB2 H 2.19 . 2
72 . 12 GLN HB3 H 2.39 . 2
73 . 12 GLN HG2 H 2.33 . 2
74 . 12 GLN HG3 H 1.99 . 2
75 . 12 GLN HE21 H 6.55 . 2
76 . 12 GLN HE22 H 6.98 . 2
77 . 13 GLN H H 8.05 . 1
78 . 13 GLN HA H 4.13 . 1
79 . 13 GLN HB2 H 2.26 . 1
80 . 13 GLN HB3 H 2.26 . 1
81 . 13 GLN HG2 H 2.52 . 2
82 . 13 GLN HG3 H 2.41 . 2
83 . 13 GLN HE21 H 7.18 . 2
84 . 13 GLN HE22 H 6.88 . 2
85 . 14 ALA H H 8.98 . 1
86 . 14 ALA HA H 3.97 . 1
87 . 14 ALA HB H 1.63 . 1
88 . 15 MET H H 8.92 . 1
89 . 15 MET HA H 3.96 . 1
90 . 15 MET HB2 H 2.24 . 1
91 . 15 MET HB3 H 2.24 . 1
92 . 15 MET HG2 H 2.66 . 1
93 . 15 MET HG3 H 2.66 . 1
94 . 15 MET HE H 1.99 . 1
95 . 16 LYS H H 7.68 . 1
96 . 16 LYS HA H 4.01 . 1
97 . 16 LYS HB2 H 1.90 . 1
98 . 16 LYS HB3 H 1.90 . 1
99 . 16 LYS HG2 H 1.45 . 1
100 . 16 LYS HG3 H 1.45 . 1
101 . 16 LYS HD2 H 1.72 . 1
102 . 16 LYS HD3 H 1.72 . 1
103 . 16 LYS HE2 H 2.95 . 1
104 . 16 LYS HE3 H 2.95 . 1
105 . 17 LEU H H 8.08 . 1
106 . 17 LEU HA H 4.27 . 1
107 . 17 LEU HB2 H 1.72 . 2
108 . 17 LEU HB3 H 1.49 . 2
109 . 17 LEU HG H 1.98 . 1
110 . 17 LEU HD1 H 0.94 . 1
111 . 17 LEU HD2 H 0.94 . 1
112 . 18 TYR H H 9.47 . 1
113 . 18 TYR HA H 4.12 . 1
114 . 18 TYR HB2 H 2.97 . 2
115 . 18 TYR HB3 H 2.88 . 2
116 . 18 TYR HD1 H 6.98 . 1
117 . 18 TYR HD2 H 6.98 . 1
118 . 18 TYR HE1 H 6.66 . 1
119 . 18 TYR HE2 H 6.66 . 1
120 . 18 TYR HH H 10.03 . 1
121 . 19 ARG H H 8.43 . 1
122 . 19 ARG HA H 3.91 . 1
123 . 19 ARG HB2 H 2.01 . 1
124 . 19 ARG HB3 H 2.01 . 1
125 . 19 ARG HG2 H 1.71 . 2
126 . 19 ARG HG3 H 1.64 . 2
127 . 19 ARG HD2 H 3.23 . 1
128 . 19 ARG HD3 H 3.23 . 1
129 . 19 ARG HE H 7.34 . 1
130 . 20 GLU H H 7.74 . 1
131 . 20 GLU HA H 3.98 . 1
132 . 20 GLU HB2 H 2.17 . 2
133 . 20 GLU HB3 H 1.99 . 2
134 . 20 GLU HG2 H 2.48 . 1
135 . 20 GLU HG3 H 2.48 . 1
136 . 21 ALA H H 8.70 . 1
137 . 21 ALA HA H 3.25 . 1
138 . 21 ALA HB H 1.21 . 1
139 . 22 SER H H 8.49 . 1
140 . 22 SER HA H 4.01 . 1
141 . 22 SER HB2 H 4.02 . 1
142 . 22 SER HB3 H 4.02 . 1
143 . 23 GLU H H 7.63 . 1
144 . 23 GLU HA H 4.05 . 1
145 . 23 GLU HB2 H 2.17 . 2
146 . 23 GLU HB3 H 2.10 . 2
147 . 23 GLU HG2 H 2.48 . 1
148 . 23 GLU HG3 H 2.48 . 1
149 . 24 LYS H H 7.42 . 1
150 . 24 LYS HA H 4.24 . 1
151 . 24 LYS HB2 H 1.60 . 1
152 . 24 LYS HB3 H 1.60 . 1
153 . 24 LYS HG2 H 2.01 . 1
154 . 24 LYS HG3 H 2.01 . 1
155 . 24 LYS HD2 H 1.85 . 2
156 . 24 LYS HD3 H 1.39 . 2
157 . 24 LYS HE2 H 3.25 . 1
158 . 24 LYS HE3 H 3.25 . 1
159 . 25 ALA H H 7.36 . 1
160 . 25 ALA HA H 4.25 . 1
161 . 25 ALA HB H 1.37 . 1
162 . 26 ARG H H 8.59 . 1
163 . 26 ARG HA H 4.41 . 1
164 . 26 ARG HB2 H 1.82 . 1
165 . 26 ARG HB3 H 1.82 . 1
166 . 26 ARG HG2 H 2.04 . 1
167 . 26 ARG HG3 H 2.04 . 1
168 . 26 ARG HD2 H 2.85 . 2
169 . 26 ARG HD3 H 2.34 . 2
170 . 26 ARG HE H 6.98 . 1
171 . 27 ASN H H 7.99 . 1
172 . 27 ASN HA H 5.11 . 1
173 . 27 ASN HB2 H 2.96 . 2
174 . 27 ASN HB3 H 2.90 . 2
175 . 27 ASN HD21 H 8.04 . 2
176 . 27 ASN HD22 H 7.42 . 2
177 . 28 PRO HA H 4.18 . 1
178 . 28 PRO HB2 H 2.44 . 1
179 . 28 PRO HB3 H 2.44 . 1
180 . 28 PRO HG2 H 2.22 . 1
181 . 28 PRO HG3 H 2.22 . 1
182 . 28 PRO HD2 H 4.13 . 2
183 . 28 PRO HD3 H 3.95 . 2
184 . 29 GLU H H 8.36 . 1
185 . 29 GLU HA H 4.17 . 1
186 . 29 GLU HB2 H 2.20 . 2
187 . 29 GLU HB3 H 2.08 . 2
188 . 29 GLU HG2 H 2.34 . 1
189 . 29 GLU HG3 H 2.34 . 1
190 . 30 LYS H H 7.79 . 1
191 . 30 LYS HA H 4.09 . 1
192 . 30 LYS HB2 H 1.90 . 1
193 . 30 LYS HB3 H 1.90 . 1
194 . 30 LYS HG2 H 1.76 . 1
195 . 30 LYS HG3 H 1.76 . 1
196 . 30 LYS HE2 H 2.95 . 1
197 . 30 LYS HE3 H 2.95 . 1
198 . 31 LYS H H 8.34 . 1
199 . 31 LYS HA H 3.65 . 1
200 . 31 LYS HB2 H 2.07 . 2
201 . 31 LYS HB3 H 1.84 . 2
202 . 31 LYS HG2 H 1.67 . 1
203 . 31 LYS HG3 H 1.67 . 1
204 . 31 LYS HD2 H 1.76 . 1
205 . 31 LYS HD3 H 1.76 . 1
206 . 31 LYS HE2 H 2.99 . 1
207 . 31 LYS HE3 H 2.99 . 1
208 . 32 SER H H 7.95 . 1
209 . 32 SER HA H 3.96 . 1
210 . 32 SER HB2 H 4.13 . 1
211 . 32 SER HB3 H 4.13 . 1
212 . 33 VAL H H 7.31 . 1
213 . 33 VAL HA H 3.41 . 1
214 . 33 VAL HB H 2.05 . 1
215 . 33 VAL HG1 H 0.89 . 2
216 . 33 VAL HG2 H 0.72 . 2
217 . 34 LEU H H 7.88 . 1
218 . 34 LEU HA H 3.96 . 1
219 . 34 LEU HB2 H 1.99 . 1
220 . 34 LEU HB3 H 1.99 . 1
221 . 34 LEU HG H 1.41 . 1
222 . 34 LEU HD1 H 0.96 . 1
223 . 34 LEU HD2 H 0.96 . 1
224 . 35 GLN H H 8.39 . 1
225 . 35 GLN HA H 3.88 . 1
226 . 35 GLN HB2 H 2.25 . 2
227 . 35 GLN HB3 H 2.00 . 2
228 . 35 GLN HG2 H 2.49 . 1
229 . 35 GLN HG3 H 2.49 . 1
230 . 35 GLN HE21 H 7.67 . 2
231 . 35 GLN HE22 H 6.82 . 2
232 . 36 LYS H H 7.67 . 1
233 . 36 LYS HA H 4.01 . 1
234 . 36 LYS HB2 H 2.00 . 1
235 . 36 LYS HB3 H 2.00 . 1
236 . 36 LYS HG2 H 1.85 . 1
237 . 36 LYS HG3 H 1.85 . 1
238 . 36 LYS HD2 H 1.44 . 1
239 . 36 LYS HD3 H 1.44 . 1
240 . 36 LYS HE2 H 3.39 . 1
241 . 36 LYS HE3 H 3.39 . 1
242 . 37 ILE H H 8.06 . 1
243 . 37 ILE HA H 2.94 . 1
244 . 37 ILE HB H 1.04 . 1
245 . 37 ILE HG2 H -0.61 . 1
246 . 37 ILE HG12 H 0.95 . 1
247 . 37 ILE HG13 H 0.95 . 1
248 . 37 ILE HD1 H -0.61 . 1
249 . 38 LEU H H 7.96 . 1
250 . 38 LEU HA H 3.52 . 1
251 . 38 LEU HB2 H 2.04 . 1
252 . 38 LEU HB3 H 2.04 . 1
253 . 38 LEU HG H 1.48 . 1
254 . 38 LEU HD1 H 0.98 . 1
255 . 38 LEU HD2 H 0.98 . 1
256 . 39 GLU H H 7.59 . 1
257 . 39 GLU HA H 3.93 . 1
258 . 39 GLU HB2 H 2.26 . 2
259 . 39 GLU HB3 H 2.08 . 2
260 . 39 GLU HG2 H 2.54 . 1
261 . 39 GLU HG3 H 2.54 . 1
262 . 40 ASP H H 7.61 . 1
263 . 40 ASP HA H 4.15 . 1
264 . 40 ASP HB2 H 3.17 . 2
265 . 40 ASP HB3 H 2.12 . 2
266 . 41 GLU H H 8.29 . 1
267 . 41 GLU HA H 4.43 . 1
268 . 41 GLU HB2 H 1.73 . 1
269 . 41 GLU HB3 H 1.73 . 1
270 . 41 GLU HG2 H 2.73 . 1
271 . 41 GLU HG3 H 2.73 . 1
272 . 42 GLU H H 7.93 . 1
273 . 42 GLU HA H 3.92 . 1
274 . 42 GLU HB2 H 2.12 . 2
275 . 42 GLU HB3 H 1.99 . 2
276 . 42 GLU HG2 H 2.38 . 1
277 . 42 GLU HG3 H 2.38 . 1
278 . 43 LYS H H 7.31 . 1
279 . 43 LYS HA H 3.75 . 1
280 . 43 LYS HB2 H 1.63 . 2
281 . 43 LYS HB3 H 1.38 . 2
282 . 43 LYS HG2 H 1.98 . 1
283 . 43 LYS HG3 H 1.98 . 1
284 . 43 LYS HD2 H 0.74 . 1
285 . 43 LYS HD3 H 0.74 . 1
286 . 44 HIS H H 8.19 . 1
287 . 44 HIS HA H 4.13 . 1
288 . 44 HIS HB2 H 3.56 . 2
289 . 44 HIS HB3 H 3.11 . 2
290 . 44 HIS HD2 H 6.26 . 1
291 . 44 HIS HE1 H 7.43 . 1
292 . 44 HIS HE2 H 15.00 . 1
293 . 45 ILE H H 7.94 . 1
294 . 45 ILE HA H 3.69 . 1
295 . 45 ILE HB H 1.75 . 1
296 . 45 ILE HG2 H 0.97 . 1
297 . 45 ILE HG12 H 0.67 . 1
298 . 45 ILE HG13 H 0.67 . 1
299 . 45 ILE HD1 H 0.97 . 1
300 . 46 GLU H H 7.47 . 1
301 . 46 GLU HA H 4.13 . 1
302 . 46 GLU HB2 H 2.26 . 2
303 . 46 GLU HB3 H 2.06 . 2
304 . 46 GLU HG2 H 2.22 . 1
305 . 46 GLU HG3 H 2.22 . 1
306 . 47 TRP H H 8.98 . 1
307 . 47 TRP HA H 4.74 . 1
308 . 47 TRP HB2 H 3.61 . 2
309 . 47 TRP HB3 H 3.16 . 2
310 . 47 TRP HD1 H 7.22 . 1
311 . 47 TRP HE3 H 7.43 . 1
312 . 47 TRP HE1 H 10.27 . 1
313 . 47 TRP HZ3 H 6.85 . 1
314 . 47 TRP HZ2 H 7.60 . 1
315 . 47 TRP HH2 H 7.29 . 1
316 . 48 LEU H H 9.07 . 1
317 . 48 LEU HA H 4.15 . 1
318 . 48 LEU HB2 H 2.40 . 2
319 . 48 LEU HB3 H 2.29 . 2
320 . 48 LEU HG H 1.51 . 1
321 . 48 LEU HD1 H 1.10 . 2
322 . 48 LEU HD2 H 0.98 . 2
323 . 49 GLU H H 8.25 . 1
324 . 49 GLU HA H 4.10 . 1
325 . 49 GLU HB2 H 2.44 . 2
326 . 49 GLU HB3 H 2.18 . 2
327 . 49 GLU HG2 H 2.87 . 1
328 . 49 GLU HG3 H 2.87 . 1
329 . 50 THR H H 7.90 . 1
330 . 50 THR HA H 4.37 . 1
331 . 50 THR HB H 4.50 . 1
332 . 50 THR HG2 H 1.44 . 1
333 . 51 ILE H H 7.58 . 1
334 . 51 ILE HA H 4.43 . 1
335 . 51 ILE HB H 2.12 . 1
336 . 51 ILE HG2 H 0.91 . 1
337 . 51 ILE HG12 H 1.60 . 1
338 . 51 ILE HG13 H 1.60 . 1
339 . 51 ILE HD1 H 0.91 . 1
340 . 52 ASN H H 7.89 . 1
341 . 52 ASN HA H 4.79 . 1
342 . 52 ASN HB2 H 2.87 . 2
343 . 52 ASN HB3 H 2.77 . 2
344 . 52 ASN HD21 H 7.58 . 2
345 . 52 ASN HD22 H 6.66 . 2
346 . 53 GLY H H 7.82 . 1
347 . 53 GLY HA2 H 3.79 . 1
348 . 53 GLY HA3 H 3.79 . 1
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