data_16804
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR assignments for Thermus thermophilus Rieske protein at pH 5.2 in oxidized state
;
_BMRB_accession_number 16804
_BMRB_flat_file_name bmr16804.str
_Entry_type original
_Submission_date 2010-03-30
_Accession_date 2010-03-30
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details 'same as title'
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Hsueh Kuang-Lung . .
2 Markley John . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 131
"13C chemical shifts" 336
"15N chemical shifts" 131
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2012-11-09 update author 'Correct the shifts of 16 TYR H and N; and update the ligand saveframe'
2010-08-12 update BMRB 'Complete entry citation'
2010-06-15 original author 'original release'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
16787 'reduced Rieske Protein'
stop_
save_
#############################
# Citation for this entry #
#############################
save_1
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'NMR investigations of the Rieske protein from Thermus thermophilus support a coupled proton and electron transfer mechanism.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 20496909
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Hsueh Kuang-Lung . .
2 Westler William M. .
3 Markley John L. .
stop_
_Journal_abbreviation 'J. Am. Chem. Soc.'
_Journal_name_full 'Journal of the American Chemical Society'
_Journal_volume 132
_Journal_issue 23
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 7908
_Page_last 7918
_Year 2010
_Details .
loop_
_Keyword
'iron sulfur cluster'
paramagnetic
'Rieske protein'
'thermus thermophilus'
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'Thermus thermophilus Rieske protein (cofactor bound)'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Rieske protein' $Rieske_protein
'[2Fe-2S] cofactor' $entity_FES
stop_
_System_molecular_weight 16508
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic yes
_System_thiol_state .
_Database_query_date .
_Details 'cluster bound to Cys151, Cys132, His134, His154. The molecular weight is apo-protein not for holoprotein.'
save_
########################
# Monomeric polymers #
########################
save_Rieske_protein
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Rieske_protein
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 157
_Mol_residue_sequence
;
MTPEKEPLKPGDILVYAQGG
GEPKPIRLEELKPGDPFVLA
YPMDPKTKVVKSGEAKNTLL
VARFDPEELAPEVAQHAAEG
VVAYSAVCTLPGPIVSQFVA
DEEAALCPCPGPVYDLRHGA
QVIAGPPPRPVPQLPVRVED
GVLVAAGEFLGPVGVQA
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 45 MET 2 46 THR 3 47 PRO 4 48 GLU 5 49 LYS
6 50 GLU 7 51 PRO 8 52 LEU 9 53 LYS 10 54 PRO
11 55 GLY 12 56 ASP 13 57 ILE 14 58 LEU 15 59 VAL
16 60 TYR 17 61 ALA 18 62 GLN 19 63 GLY 20 64 GLY
21 65 GLY 22 66 GLU 23 67 PRO 24 68 LYS 25 69 PRO
26 70 ILE 27 71 ARG 28 72 LEU 29 73 GLU 30 74 GLU
31 75 LEU 32 76 LYS 33 77 PRO 34 78 GLY 35 79 ASP
36 80 PRO 37 81 PHE 38 82 VAL 39 83 LEU 40 84 ALA
41 85 TYR 42 86 PRO 43 87 MET 44 88 ASP 45 89 PRO
46 90 LYS 47 91 THR 48 92 LYS 49 93 VAL 50 94 VAL
51 95 LYS 52 96 SER 53 97 GLY 54 98 GLU 55 99 ALA
56 100 LYS 57 101 ASN 58 102 THR 59 103 LEU 60 104 LEU
61 105 VAL 62 106 ALA 63 107 ARG 64 108 PHE 65 109 ASP
66 110 PRO 67 111 GLU 68 112 GLU 69 113 LEU 70 114 ALA
71 115 PRO 72 116 GLU 73 117 VAL 74 118 ALA 75 119 GLN
76 120 HIS 77 121 ALA 78 122 ALA 79 123 GLU 80 124 GLY
81 125 VAL 82 126 VAL 83 127 ALA 84 128 TYR 85 129 SER
86 130 ALA 87 131 VAL 88 132 CYS 89 133 THR 90 134 LEU
91 135 PRO 92 136 GLY 93 137 PRO 94 138 ILE 95 139 VAL
96 140 SER 97 141 GLN 98 142 PHE 99 143 VAL 100 144 ALA
101 145 ASP 102 146 GLU 103 147 GLU 104 148 ALA 105 149 ALA
106 150 LEU 107 151 CYS 108 152 PRO 109 153 CYS 110 154 PRO
111 155 GLY 112 156 PRO 113 157 VAL 114 158 TYR 115 159 ASP
116 160 LEU 117 161 ARG 118 162 HIS 119 163 GLY 120 164 ALA
121 165 GLN 122 166 VAL 123 167 ILE 124 168 ALA 125 169 GLY
126 170 PRO 127 171 PRO 128 172 PRO 129 173 ARG 130 174 PRO
131 175 VAL 132 176 PRO 133 177 GLN 134 178 LEU 135 179 PRO
136 180 VAL 137 181 ARG 138 182 VAL 139 183 GLU 140 184 ASP
141 185 GLY 142 186 VAL 143 187 LEU 144 188 VAL 145 189 ALA
146 190 ALA 147 191 GLY 148 192 GLU 149 193 PHE 150 194 LEU
151 195 GLY 152 196 PRO 153 197 VAL 154 198 GLY 155 199 VAL
156 200 GLN 157 201 ALA
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-02-05
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 16787 Rieske_protein 100.00 157 98.73 98.73 3.24e-101
stop_
save_
#############
# Ligands #
#############
save_FES
_Saveframe_category ligand
_Mol_type "non-polymer (NON-POLYMER)"
_Name_common 'FE2/S2 (INORGANIC) CLUSTER'
_BMRB_code FES
_PDB_code FES
_Molecular_mass 175.820
_Mol_charge 0
_Mol_paramagnetic .
_Mol_aromatic no
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
FE1 FE1 FE . 0 . ?
FE2 FE2 FE . 0 . ?
S1 S1 S . 0 . ?
S2 S2 S . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING FE1 S1 ? ?
SING FE1 S2 ? ?
SING FE2 S1 ? ?
SING FE2 S2 ? ?
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
$Rieske_protein 'Thermus thermophilus' 274 Bacteria . Thermus thermophilus
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
$Rieske_protein 'recombinant technology' . Escherichia coli BL21(DE3)pLysS pET17b
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1_oxidized
_Saveframe_category sample
_Sample_type solution
_Details 'oxidized by ferricyanide'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Rieske_protein 5 mM '[U-98% 13C; U-98% 15N]'
TRIS 20 mM 'natural abundance'
'sodium phosphate' 20 mM 'natural abundance'
'boric acid' 20 mM 'natural abundance'
ferricyanide 30 mM 'natural abundance'
H2O 90 % 'natural abundance'
D2O 10 % 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_SPARKY
_Saveframe_category software
_Name SPARKY
_Version 3.114
loop_
_Vendor
_Address
_Electronic_address
Goddard . .
stop_
loop_
_Task
'chemical shift assignment'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $sample_1_oxidized
save_
save_3D_HNCACB_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label $sample_1_oxidized
save_
save_3D_CBCA(CO)NH_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_Sample_label $sample_1_oxidized
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0.4 0.1 M
pH 5.2 0.02 pH
pressure 1 . atm
temperature 298 0.2 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000
DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118
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_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Software_label
$SPARKY
stop_
loop_
_Experiment_label
'2D 1H-15N HSQC'
'3D HNCACB'
'3D CBCA(CO)NH'
stop_
loop_
_Sample_label
$sample_1_oxidized
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name 'Rieske 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 46 2 THR H H 8.213 . 1
2 46 2 THR N N 117.933 . 1
3 47 3 PRO CA C 65.887 . 1
4 47 3 PRO CB C 32.433 . 1
5 47 3 PRO CG C 27.828 . 1
6 48 4 GLU H H 9.384 . 1
7 48 4 GLU CA C 58.472 . 1
8 48 4 GLU CB C 28.481 . 1
9 48 4 GLU CG C 36.408 . 1
10 48 4 GLU N N 115.947 . 1
11 49 5 LYS H H 7.817 . 1
12 49 5 LYS CA C 55.594 . 1
13 49 5 LYS CB C 33.440 . 1
14 49 5 LYS CD C 29.476 . 1
15 49 5 LYS CG C 26.316 . 1
16 49 5 LYS N N 117.979 . 1
17 50 6 GLU H H 7.055 . 1
18 50 6 GLU CB C 29.635 . 1
19 50 6 GLU N N 120.546 . 1
20 51 7 PRO CA C 62.808 . 1
21 51 7 PRO CB C 32.765 . 1
22 51 7 PRO CG C 26.371 . 1
23 52 8 LEU H H 7.801 . 1
24 52 8 LEU CA C 57.281 . 1
25 52 8 LEU CB C 43.352 . 1
26 52 8 LEU CD1 C 27.601 . 2
27 52 8 LEU CG C 28.217 . 1
28 52 8 LEU N N 122.721 . 1
29 53 9 LYS H H 9.081 . 1
30 53 9 LYS CA C 52.702 . 1
31 53 9 LYS CB C 35.006 . 1
32 53 9 LYS N N 128.360 . 1
33 54 10 PRO CA C 63.633 . 1
34 54 10 PRO CB C 31.386 . 1
35 54 10 PRO CG C 28.042 . 1
36 55 11 GLY H H 9.256 . 1
37 55 11 GLY CA C 44.743 . 1
38 55 11 GLY N N 115.128 . 1
39 56 12 ASP H H 7.883 . 1
40 56 12 ASP CA C 58.454 . 1
41 56 12 ASP CB C 40.636 . 1
42 56 12 ASP N N 120.164 . 1
43 57 13 ILE H H 8.515 . 1
44 57 13 ILE CA C 60.464 . 1
45 57 13 ILE CB C 40.850 . 1
46 57 13 ILE CD1 C 13.222 . 1
47 57 13 ILE CG1 C 30.251 . 1
48 57 13 ILE CG2 C 21.018 . 1
49 57 13 ILE N N 122.602 . 1
50 58 14 LEU H H 8.618 . 1
51 58 14 LEU CA C 54.599 . 1
52 58 14 LEU CB C 40.930 . 1
53 58 14 LEU N N 126.465 . 1
54 59 15 VAL H H 9.041 . 1
55 59 15 VAL CA C 57.788 . 1
56 59 15 VAL CB C 34.425 . 1
57 59 15 VAL N N 114.848 . 1
58 60 16 TYR H H 7.89 . 1
59 60 16 TYR CA C 62.244 . 1
60 60 16 TYR CB C 33.095 . 1
61 60 16 TYR N N 118.4 . 1
62 61 17 ALA H H 8.695 . 1
63 61 17 ALA CA C 53.243 . 1
64 61 17 ALA CB C 18.953 . 1
65 61 17 ALA N N 123.123 . 1
66 62 18 GLN H H 8.465 . 1
67 62 18 GLN CA C 55.639 . 1
68 62 18 GLN CB C 30.227 . 1
69 62 18 GLN CG C 33.870 . 1
70 62 18 GLN N N 118.570 . 1
71 63 19 GLY H H 8.495 . 1
72 63 19 GLY CA C 46.172 . 1
73 63 19 GLY N N 110.525 . 1
74 64 20 GLY H H 7.799 . 1
75 64 20 GLY CA C 44.805 . 1
76 64 20 GLY N N 109.614 . 1
77 65 21 GLY H H 8.257 . 1
78 65 21 GLY CA C 44.299 . 1
79 65 21 GLY N N 107.322 . 1
80 66 22 GLU H H 8.225 . 1
81 66 22 GLU CB C 30.574 . 1
82 66 22 GLU N N 120.868 . 1
83 67 23 PRO CA C 61.342 . 1
84 67 23 PRO CB C 30.797 . 1
85 68 24 LYS H H 8.393 . 1
86 68 24 LYS N N 125.301 . 1
87 69 25 PRO CA C 62.984 . 1
88 69 25 PRO CB C 32.259 . 1
89 70 26 ILE H H 9.750 . 1
90 70 26 ILE CA C 62.672 . 1
91 70 26 ILE CB C 37.846 . 1
92 70 26 ILE CD1 C 14.677 . 1
93 70 26 ILE CG1 C 26.086 . 1
94 70 26 ILE CG2 C 17.453 . 1
95 70 26 ILE N N 126.946 . 1
96 71 27 ARG H H 7.633 . 1
97 71 27 ARG CA C 54.232 . 1
98 71 27 ARG CB C 31.527 . 1
99 71 27 ARG CD C 45.244 . 1
100 71 27 ARG N N 126.090 . 1
101 72 28 LEU H H 7.993 . 1
102 72 28 LEU CA C 58.881 . 1
103 72 28 LEU CB C 42.470 . 1
104 72 28 LEU CG C 29.134 . 1
105 72 28 LEU N N 123.780 . 1
106 73 29 GLU H H 8.725 . 1
107 73 29 GLU CA C 57.614 . 1
108 73 29 GLU CB C 28.815 . 1
109 73 29 GLU CG C 35.428 . 1
110 73 29 GLU N N 111.083 . 1
111 74 30 GLU H H 7.797 . 1
112 74 30 GLU CA C 56.720 . 1
113 74 30 GLU CB C 28.894 . 1
114 74 30 GLU N N 118.498 . 1
115 75 31 LEU H H 7.598 . 1
116 75 31 LEU CA C 53.255 . 1
117 75 31 LEU CB C 43.909 . 1
118 75 31 LEU N N 118.921 . 1
119 76 32 LYS H H 8.874 . 1
120 76 32 LYS N N 125.168 . 1
121 77 33 PRO CA C 62.147 . 1
122 78 34 GLY H H 8.076 . 1
123 78 34 GLY CA C 45.261 . 1
124 78 34 GLY N N 101.724 . 1
125 79 35 ASP H H 8.359 . 1
126 79 35 ASP N N 122.793 . 1
127 80 36 PRO CA C 63.129 . 1
128 80 36 PRO CB C 32.606 . 1
129 80 36 PRO CD C 55.286 . 1
130 80 36 PRO CG C 29.044 . 1
131 81 37 PHE H H 8.543 . 1
132 81 37 PHE CA C 55.617 . 1
133 81 37 PHE CB C 40.266 . 1
134 81 37 PHE N N 122.040 . 1
135 82 38 VAL H H 9.416 . 1
136 82 38 VAL CA C 56.521 . 1
137 82 38 VAL CB C 33.195 . 1
138 82 38 VAL N N 116.923 . 1
139 83 39 LEU H H 8.493 . 1
140 83 39 LEU CA C 54.142 . 1
141 83 39 LEU CB C 43.660 . 1
142 83 39 LEU CD1 C 25.763 . 2
143 83 39 LEU N N 125.003 . 1
144 84 40 ALA H H 9.065 . 1
145 84 40 ALA CA C 50.645 . 1
146 84 40 ALA CB C 26.082 . 1
147 84 40 ALA N N 126.461 . 1
148 85 41 TYR H H 8.544 . 1
149 85 41 TYR N N 113.733 . 1
150 86 42 PRO CA C 61.747 . 1
151 86 42 PRO CB C 32.505 . 1
152 86 42 PRO CG C 26.842 . 1
153 87 43 MET H H 9.942 . 1
154 87 43 MET CA C 53.113 . 1
155 87 43 MET CB C 37.599 . 1
156 87 43 MET CG C 30.508 . 1
157 87 43 MET N N 123.561 . 1
158 88 44 ASP H H 8.219 . 1
159 88 44 ASP N N 127.859 . 1
160 89 45 PRO CA C 64.720 . 1
161 89 45 PRO CB C 32.445 . 1
162 89 45 PRO CD C 45.383 . 1
163 89 45 PRO CG C 27.688 . 1
164 90 46 LYS H H 8.633 . 1
165 90 46 LYS CA C 58.115 . 1
166 90 46 LYS CB C 33.324 . 1
167 90 46 LYS CD C 28.793 . 1
168 90 46 LYS CE C 42.203 . 1
169 90 46 LYS CG C 25.164 . 1
170 90 46 LYS N N 118.248 . 1
171 91 47 THR H H 8.493 . 1
172 91 47 THR CA C 62.245 . 1
173 91 47 THR CB C 70.346 . 1
174 91 47 THR N N 109.299 . 1
175 92 48 LYS H H 8.040 . 1
176 92 48 LYS CA C 57.284 . 1
177 92 48 LYS CB C 28.464 . 1
178 92 48 LYS CG C 25.010 . 1
179 92 48 LYS N N 114.681 . 1
180 93 49 VAL H H 7.360 . 1
181 93 49 VAL CA C 58.624 . 1
182 93 49 VAL CB C 32.121 . 1
183 93 49 VAL CG1 C 20.908 . 2
184 93 49 VAL CG2 C 21.988 . 2
185 93 49 VAL N N 118.032 . 1
186 94 50 VAL H H 8.666 . 1
187 94 50 VAL CA C 63.114 . 1
188 94 50 VAL CB C 31.774 . 1
189 94 50 VAL N N 130.078 . 1
190 95 51 LYS H H 8.936 . 1
191 95 51 LYS CA C 56.132 . 1
192 95 51 LYS CB C 30.261 . 1
193 95 51 LYS N N 132.803 . 1
194 96 52 SER H H 8.131 . 1
195 96 52 SER CA C 57.670 . 1
196 96 52 SER CB C 62.853 . 1
197 96 52 SER N N 110.880 . 1
198 97 53 GLY H H 8.675 . 1
199 97 53 GLY CA C 46.082 . 1
200 97 53 GLY N N 110.065 . 1
201 98 54 GLU H H 6.611 . 1
202 98 54 GLU CA C 52.928 . 1
203 98 54 GLU CB C 32.253 . 1
204 98 54 GLU N N 120.917 . 1
205 99 55 ALA H H 9.180 . 1
206 99 55 ALA CA C 55.059 . 1
207 99 55 ALA CB C 18.972 . 1
208 99 55 ALA N N 131.417 . 1
209 100 56 LYS H H 10.197 . 1
210 100 56 LYS CA C 59.436 . 1
211 100 56 LYS CB C 30.915 . 1
212 100 56 LYS CD C 27.186 . 1
213 100 56 LYS CE C 43.273 . 1
214 100 56 LYS N N 117.719 . 1
215 101 57 ASN H H 8.571 . 1
216 101 57 ASN CA C 52.636 . 1
217 101 57 ASN CB C 38.770 . 1
218 101 57 ASN N N 119.201 . 1
219 102 58 THR H H 7.742 . 1
220 102 58 THR CA C 65.722 . 1
221 102 58 THR CB C 68.724 . 1
222 102 58 THR N N 113.358 . 1
223 103 59 LEU H H 9.317 . 1
224 103 59 LEU CA C 53.765 . 1
225 103 59 LEU CB C 46.377 . 1
226 103 59 LEU N N 131.284 . 1
227 104 60 LEU H H 9.309 . 1
228 104 60 LEU CA C 53.846 . 1
229 104 60 LEU CB C 45.168 . 1
230 104 60 LEU N N 118.563 . 1
231 105 61 VAL H H 8.917 . 1
232 105 61 VAL CA C 61.292 . 1
233 105 61 VAL CB C 34.415 . 1
234 105 61 VAL CG1 C 19.314 . 2
235 105 61 VAL CG2 C 21.847 . 2
236 105 61 VAL N N 122.543 . 1
237 106 62 ALA H H 9.073 . 1
238 106 62 ALA CA C 50.345 . 1
239 106 62 ALA CB C 24.499 . 1
240 106 62 ALA N N 128.521 . 1
241 107 63 ARG H H 8.744 . 1
242 107 63 ARG CA C 54.833 . 1
243 107 63 ARG CB C 34.690 . 1
244 107 63 ARG CD C 45.269 . 1
245 107 63 ARG CG C 31.433 . 1
246 107 63 ARG N N 119.712 . 1
247 108 64 PHE H H 8.758 . 1
248 108 64 PHE CA C 56.689 . 1
249 108 64 PHE CB C 43.234 . 1
250 108 64 PHE N N 125.157 . 1
251 109 65 ASP H H 9.331 . 1
252 109 65 ASP CA C 57.603 . 1
253 109 65 ASP N N 123.188 . 1
254 110 66 PRO CA C 65.786 . 1
255 110 66 PRO CB C 32.252 . 1
256 110 66 PRO CG C 27.752 . 1
257 111 67 GLU H H 8.797 . 1
258 111 67 GLU CA C 58.063 . 1
259 111 67 GLU CB C 28.936 . 1
260 111 67 GLU CG C 36.051 . 1
261 111 67 GLU N N 114.781 . 1
262 112 68 GLU H H 8.226 . 1
263 112 68 GLU CA C 56.269 . 1
264 112 68 GLU CB C 30.797 . 1
265 112 68 GLU CG C 36.697 . 1
266 112 68 GLU N N 116.429 . 1
267 113 69 LEU H H 7.085 . 1
268 113 69 LEU CA C 53.422 . 1
269 113 69 LEU CB C 43.644 . 1
270 113 69 LEU N N 116.985 . 1
271 114 70 ALA H H 8.024 . 1
272 114 70 ALA N N 125.483 . 1
273 115 71 PRO CA C 66.354 . 1
274 115 71 PRO CB C 31.985 . 1
275 115 71 PRO CG C 27.794 . 1
276 116 72 GLU H H 9.582 . 1
277 116 72 GLU CA C 59.401 . 1
278 116 72 GLU CB C 28.542 . 1
279 116 72 GLU CG C 36.153 . 1
280 116 72 GLU N N 116.507 . 1
281 117 73 VAL H H 7.235 . 1
282 117 73 VAL CA C 63.632 . 1
283 117 73 VAL CB C 32.740 . 1
284 117 73 VAL CG1 C 22.474 . 2
285 117 73 VAL N N 119.697 . 1
286 118 74 ALA H H 8.590 . 1
287 118 74 ALA CA C 54.559 . 1
288 118 74 ALA CB C 18.426 . 1
289 118 74 ALA N N 122.619 . 1
290 119 75 GLN H H 7.516 . 1
291 119 75 GLN CA C 57.881 . 1
292 119 75 GLN CB C 28.566 . 1
293 119 75 GLN CG C 33.234 . 1
294 119 75 GLN N N 114.479 . 1
295 120 76 HIS H H 7.276 . 1
296 120 76 HIS CA C 53.591 . 1
297 120 76 HIS CB C 28.992 . 1
298 120 76 HIS N N 113.119 . 1
299 121 77 ALA H H 7.572 . 1
300 121 77 ALA CA C 50.681 . 1
301 121 77 ALA CB C 22.997 . 1
302 121 77 ALA N N 125.774 . 1
303 122 78 ALA H H 8.348 . 1
304 122 78 ALA CA C 51.016 . 1
305 122 78 ALA CB C 20.878 . 1
306 122 78 ALA N N 122.345 . 1
307 123 79 GLU H H 9.128 . 1
308 123 79 GLU CA C 56.752 . 1
309 123 79 GLU CB C 27.030 . 1
310 123 79 GLU CG C 35.203 . 1
311 123 79 GLU N N 121.214 . 1
312 124 80 GLY H H 8.552 . 1
313 124 80 GLY CA C 44.445 . 1
314 124 80 GLY N N 103.599 . 1
315 125 81 VAL H H 8.324 . 1
316 125 81 VAL CA C 62.792 . 1
317 125 81 VAL CB C 30.834 . 1
318 125 81 VAL CG1 C 22.906 . 2
319 125 81 VAL N N 121.601 . 1
320 126 82 VAL H H 9.030 . 1
321 126 82 VAL CA C 58.133 . 1
322 126 82 VAL CB C 34.994 . 1
323 126 82 VAL CG2 C 19.710 . 2
324 126 82 VAL N N 119.180 . 1
325 127 83 ALA H H 7.614 . 1
326 127 83 ALA CA C 49.281 . 1
327 127 83 ALA CB C 23.301 . 1
328 127 83 ALA N N 121.673 . 1
329 128 84 TYR H H 9.050 . 1
330 128 84 TYR CA C 55.775 . 1
331 128 84 TYR CB C 44.046 . 1
332 128 84 TYR N N 116.608 . 1
333 129 85 SER H H 8.479 . 1
334 129 85 SER CA C 58.885 . 1
335 129 85 SER CB C 63.535 . 1
336 129 85 SER N N 112.171 . 1
337 130 86 ALA H H 7.900 . 1
338 130 86 ALA CA C 52.707 . 1
339 130 86 ALA CB C 19.572 . 1
340 130 86 ALA N N 122.401 . 1
341 131 87 VAL H H 8.439 . 1
342 131 87 VAL CB C 33.095 . 1
343 131 87 VAL N N 119.717 . 1
344 132 88 CYS H H 8.513 . 1
345 132 88 CYS CA C 53.360 . 1
346 132 88 CYS CB C 39.187 . 1
347 132 88 CYS N N 109.320 . 1
348 133 89 THR H H 8.156 . 1
349 133 89 THR N N 123.702 . 1
350 134 90 LEU H H 8.673 . 1
351 134 90 LEU N N 128.349 . 1
352 135 91 PRO CA C 62.147 . 1
353 136 92 GLY H H 9.751 . 1
354 136 92 GLY N N 114.790 . 1
355 137 93 PRO CB C 29.987 . 1
356 137 93 PRO CD C 51.662 . 1
357 137 93 PRO CG C 27.819 . 1
358 138 94 ILE H H 8.682 . 1
359 138 94 ILE CA C 56.882 . 1
360 138 94 ILE CB C 39.207 . 1
361 138 94 ILE CD1 C 13.039 . 1
362 138 94 ILE CG1 C 27.169 . 1
363 138 94 ILE CG2 C 17.616 . 1
364 138 94 ILE N N 123.362 . 1
365 139 95 VAL H H 8.254 . 1
366 139 95 VAL CA C 62.512 . 1
367 139 95 VAL CB C 32.801 . 1
368 139 95 VAL CG1 C 19.204 . 2
369 139 95 VAL N N 120.820 . 1
370 140 96 SER H H 8.395 . 1
371 140 96 SER CA C 59.092 . 1
372 140 96 SER CB C 65.793 . 1
373 140 96 SER N N 124.925 . 1
374 141 97 GLN H H 8.783 . 1
375 141 97 GLN CA C 55.266 . 1
376 141 97 GLN CB C 31.903 . 1
377 141 97 GLN CG C 34.228 . 1
378 141 97 GLN N N 121.987 . 1
379 142 98 PHE H H 8.962 . 1
380 142 98 PHE CA C 55.910 . 1
381 142 98 PHE CB C 45.603 . 1
382 142 98 PHE N N 124.022 . 1
383 143 99 VAL H H 8.145 . 1
384 143 99 VAL CA C 60.847 . 1
385 143 99 VAL CB C 31.941 . 1
386 143 99 VAL CG1 C 21.789 . 2
387 143 99 VAL N N 120.735 . 1
388 144 100 ALA H H 8.646 . 1
389 144 100 ALA CA C 55.941 . 1
390 144 100 ALA CB C 18.826 . 1
391 144 100 ALA N N 130.575 . 1
392 145 101 ASP H H 8.856 . 1
393 145 101 ASP CA C 56.744 . 1
394 145 101 ASP CB C 39.709 . 1
395 145 101 ASP N N 115.565 . 1
396 146 102 GLU H H 6.908 . 1
397 146 102 GLU CA C 56.584 . 1
398 146 102 GLU CB C 29.970 . 1
399 146 102 GLU CG C 34.171 . 1
400 146 102 GLU N N 114.381 . 1
401 147 103 GLU H H 8.438 . 1
402 147 103 GLU CA C 57.210 . 1
403 147 103 GLU CB C 26.151 . 1
404 147 103 GLU N N 121.583 . 1
405 148 104 ALA H H 7.572 . 1
406 148 104 ALA CA C 50.349 . 1
407 148 104 ALA CB C 23.930 . 1
408 148 104 ALA N N 119.077 . 1
409 149 105 ALA H H 8.776 . 1
410 149 105 ALA CA C 50.439 . 1
411 149 105 ALA CB C 23.471 . 1
412 149 105 ALA N N 122.492 . 1
413 150 106 LEU H H 9.647 . 1
414 150 106 LEU CA C 52.991 . 1
415 150 106 LEU N N 127.612 . 1
416 151 107 CYS H H 7.383 . 1
417 151 107 CYS N N 121.348 . 1
418 154 110 PRO CA C 63.781 . 1
419 154 110 PRO CB C 31.995 . 1
420 154 110 PRO CD C 50.660 . 1
421 154 110 PRO CG C 27.528 . 1
422 155 111 GLY H H 7.503 . 1
423 155 111 GLY N N 101.971 . 1
424 156 112 PRO CA C 53.412 . 1
425 156 112 PRO CB C 32.104 . 1
426 156 112 PRO CD C 54.119 . 1
427 156 112 PRO CG C 24.856 . 1
428 157 113 VAL H H 8.643 . 1
429 157 113 VAL CA C 61.778 . 1
430 157 113 VAL CB C 34.336 . 1
431 157 113 VAL CG1 C 23.988 . 2
432 157 113 VAL N N 124.706 . 1
433 158 114 TYR H H 9.506 . 1
434 158 114 TYR CA C 56.152 . 1
435 158 114 TYR CB C 40.759 . 1
436 158 114 TYR N N 124.034 . 1
437 159 115 ASP H H 9.750 . 1
438 159 115 ASP CA C 53.702 . 1
439 159 115 ASP CB C 41.263 . 1
440 159 115 ASP N N 122.703 . 1
441 160 116 LEU H H 7.487 . 1
442 160 116 LEU CA C 58.450 . 1
443 160 116 LEU CB C 42.366 . 1
444 160 116 LEU N N 125.578 . 1
445 161 117 ARG H H 8.899 . 1
446 161 117 ARG CA C 58.752 . 1
447 161 117 ARG CB C 29.828 . 1
448 161 117 ARG N N 118.045 . 1
449 162 118 HIS H H 7.226 . 1
450 162 118 HIS CA C 53.819 . 1
451 162 118 HIS CB C 27.667 . 1
452 162 118 HIS N N 114.256 . 1
453 163 119 GLY H H 6.623 . 1
454 163 119 GLY CA C 48.032 . 1
455 163 119 GLY N N 105.869 . 1
456 164 120 ALA H H 8.160 . 1
457 164 120 ALA CA C 52.824 . 1
458 164 120 ALA CB C 17.386 . 1
459 164 120 ALA N N 118.590 . 1
460 165 121 GLN H H 6.790 . 1
461 165 121 GLN CA C 57.147 . 1
462 165 121 GLN CB C 29.546 . 1
463 165 121 GLN CG C 33.670 . 1
464 165 121 GLN N N 113.566 . 1
465 166 122 VAL H H 8.913 . 1
466 166 122 VAL CA C 63.575 . 1
467 166 122 VAL CB C 31.401 . 1
468 166 122 VAL CG1 C 24.694 . 2
469 166 122 VAL CG2 C 27.339 . 2
470 166 122 VAL N N 126.705 . 1
471 167 123 ILE H H 8.593 . 1
472 167 123 ILE CA C 61.228 . 1
473 167 123 ILE CB C 39.227 . 1
474 167 123 ILE CG1 C 26.830 . 1
475 167 123 ILE N N 119.546 . 1
476 168 124 ALA H H 7.637 . 1
477 168 124 ALA CA C 52.733 . 1
478 168 124 ALA CB C 22.109 . 1
479 168 124 ALA N N 121.995 . 1
480 169 125 GLY H H 8.454 . 1
481 169 125 GLY CA C 44.870 . 1
482 169 125 GLY N N 104.803 . 1
483 172 128 PRO CA C 63.394 . 1
484 172 128 PRO CB C 32.368 . 1
485 173 129 ARG H H 7.127 . 1
486 173 129 ARG N N 114.715 . 1
487 176 132 PRO CA C 54.999 . 1
488 176 132 PRO CB C 30.736 . 1
489 176 132 PRO CD C 50.525 . 1
490 176 132 PRO CG C 27.431 . 1
491 177 133 GLN H H 7.841 . 1
492 177 133 GLN CA C 55.512 . 1
493 177 133 GLN CB C 29.119 . 1
494 177 133 GLN CG C 32.912 . 1
495 177 133 GLN N N 117.804 . 1
496 178 134 LEU H H 8.681 . 1
497 178 134 LEU N N 128.403 . 1
498 179 135 PRO CA C 63.023 . 1
499 179 135 PRO CB C 32.746 . 1
500 179 135 PRO CD C 55.131 . 1
501 179 135 PRO CG C 31.525 . 1
502 180 136 VAL H H 7.630 . 1
503 180 136 VAL CA C 59.394 . 1
504 180 136 VAL CB C 36.865 . 1
505 180 136 VAL CG1 C 21.936 . 2
506 180 136 VAL CG2 C 27.433 . 2
507 180 136 VAL N N 116.305 . 1
508 181 137 ARG H H 9.000 . 1
509 181 137 ARG CA C 54.238 . 1
510 181 137 ARG CB C 33.386 . 1
511 181 137 ARG N N 118.650 . 1
512 182 138 VAL H H 8.587 . 1
513 182 138 VAL CA C 60.792 . 1
514 182 138 VAL CB C 32.985 . 1
515 182 138 VAL CG1 C 21.697 . 2
516 182 138 VAL N N 119.616 . 1
517 183 139 GLU H H 9.370 . 1
518 183 139 GLU CA C 55.118 . 1
519 183 139 GLU CB C 31.939 . 1
520 183 139 GLU CG C 35.583 . 1
521 183 139 GLU N N 128.318 . 1
522 184 140 ASP H H 9.526 . 1
523 184 140 ASP CA C 55.300 . 1
524 184 140 ASP CB C 39.717 . 1
525 184 140 ASP N N 128.508 . 1
526 185 141 GLY H H 8.125 . 1
527 185 141 GLY CA C 45.780 . 1
528 185 141 GLY N N 102.000 . 1
529 186 142 VAL H H 7.884 . 1
530 186 142 VAL CA C 61.022 . 1
531 186 142 VAL CB C 34.398 . 1
532 186 142 VAL CG1 C 22.844 . 2
533 186 142 VAL N N 120.939 . 1
534 187 143 LEU H H 8.275 . 1
535 187 143 LEU CA C 54.681 . 1
536 187 143 LEU CB C 43.247 . 1
537 187 143 LEU CD1 C 25.819 . 2
538 187 143 LEU CG C 32.256 . 1
539 187 143 LEU N N 124.843 . 1
540 188 144 VAL H H 8.776 . 1
541 188 144 VAL CA C 59.485 . 1
542 188 144 VAL CB C 36.334 . 1
543 188 144 VAL CG1 C 19.588 . 2
544 188 144 VAL CG2 C 21.360 . 2
545 188 144 VAL N N 119.362 . 1
546 189 145 ALA H H 9.137 . 1
547 189 145 ALA CA C 52.365 . 1
548 189 145 ALA CB C 19.044 . 1
549 189 145 ALA N N 124.998 . 1
550 190 146 ALA H H 9.133 . 1
551 190 146 ALA CA C 50.975 . 1
552 190 146 ALA CB C 19.489 . 1
553 190 146 ALA N N 128.743 . 1
554 191 147 GLY H H 7.350 . 1
555 191 147 GLY CA C 44.529 . 1
556 191 147 GLY N N 104.650 . 1
557 192 148 GLU H H 7.779 . 1
558 192 148 GLU CA C 55.242 . 1
559 192 148 GLU CB C 30.723 . 1
560 192 148 GLU CG C 35.762 . 1
561 192 148 GLU N N 115.249 . 1
562 193 149 PHE H H 7.845 . 1
563 193 149 PHE CA C 60.923 . 1
564 193 149 PHE CB C 40.887 . 1
565 193 149 PHE N N 115.293 . 1
566 194 150 LEU H H 8.720 . 1
567 194 150 LEU CA C 55.638 . 1
568 194 150 LEU CB C 40.570 . 1
569 194 150 LEU CD1 C 22.603 . 2
570 194 150 LEU N N 120.267 . 1
571 195 151 GLY H H 7.434 . 1
572 195 151 GLY N N 107.781 . 1
573 196 152 PRO CA C 63.260 . 1
574 196 152 PRO CB C 32.006 . 1
575 196 152 PRO CD C 50.678 . 1
576 196 152 PRO CG C 27.433 . 1
577 197 153 VAL H H 8.794 . 1
578 197 153 VAL CA C 63.063 . 1
579 197 153 VAL CB C 31.576 . 1
580 197 153 VAL CG1 C 23.834 . 2
581 197 153 VAL CG2 C 27.528 . 2
582 197 153 VAL N N 129.964 . 1
583 198 154 GLY H H 8.951 . 1
584 198 154 GLY CA C 44.023 . 1
585 198 154 GLY N N 113.936 . 1
586 199 155 VAL H H 8.346 . 1
587 199 155 VAL CA C 63.120 . 1
588 199 155 VAL CB C 31.904 . 1
589 199 155 VAL CG1 C 19.624 . 2
590 199 155 VAL CG2 C 20.415 . 2
591 199 155 VAL N N 120.719 . 1
592 200 156 GLN H H 8.807 . 1
593 200 156 GLN CA C 54.949 . 1
594 200 156 GLN CB C 30.045 . 1
595 200 156 GLN CG C 33.807 . 1
596 200 156 GLN N N 127.955 . 1
597 201 157 ALA H H 8.198 . 1
598 201 157 ALA N N 132.358 . 1
stop_
save_