data_5213
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ
;
_BMRB_accession_number 5213
_BMRB_flat_file_name bmr5213.str
_Entry_type original
_Submission_date 2001-11-20
_Accession_date 2001-11-20
_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 Banci L. . .
2 Bertini I. . .
3 'Del Conte' R. . .
4 Markey J. . .
5 Ruiz-Duenas J. F. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 373
"15N chemical shifts" 73
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2002-02-14 original BMRB .
stop_
_Original_release_date 2001-11-20
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21614397
_PubMed_ID 11747441
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Banci L. . .
2 Bertini I. . .
3 'Del Conte' R. . .
4 Markey J. . .
5 Ruiz-Duenas F. J. .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 40
_Journal_issue 51
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 15660
_Page_last 15668
_Year 2001
_Details .
loop_
_Keyword
beta-alpha-beta-beta-alpha-beta
stop_
save_
##################################
# Molecular system description #
##################################
save_system_CopZ
_Saveframe_category molecular_system
_Mol_system_name 'CopZ from Bacillus subtilis'
_Abbreviation_common CopZ
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'CopZ from Bacillus subtilis' $CopZ
'COPPER (I) ION' $entity_CU1
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state 'all other bound'
loop_
_Biological_function
'copper-transport in Bacillus subtilis'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_CopZ
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'CopZ from Bacillus subtilis'
_Abbreviation_common CopZ
_Molecular_mass 7826
_Mol_thiol_state 'all other bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 73
_Mol_residue_sequence
;
MEQKTLQVEGMSCQHCVKAV
ETSVGELDGVSAVHVNLEAG
KVDVSFDADKVSVKDIADAI
EDQGYDVAKIEGR
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLU 3 GLN 4 LYS 5 THR
6 LEU 7 GLN 8 VAL 9 GLU 10 GLY
11 MET 12 SER 13 CYS 14 GLN 15 HIS
16 CYS 17 VAL 18 LYS 19 ALA 20 VAL
21 GLU 22 THR 23 SER 24 VAL 25 GLY
26 GLU 27 LEU 28 ASP 29 GLY 30 VAL
31 SER 32 ALA 33 VAL 34 HIS 35 VAL
36 ASN 37 LEU 38 GLU 39 ALA 40 GLY
41 LYS 42 VAL 43 ASP 44 VAL 45 SER
46 PHE 47 ASP 48 ALA 49 ASP 50 LYS
51 VAL 52 SER 53 VAL 54 LYS 55 ASP
56 ILE 57 ALA 58 ASP 59 ALA 60 ILE
61 GLU 62 ASP 63 GLN 64 GLY 65 TYR
66 ASP 67 VAL 68 ALA 69 LYS 70 ILE
71 GLU 72 GLY 73 ARG
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
#############
# Ligands #
#############
save_CU1
_Saveframe_category ligand
_Mol_type "non-polymer (NON-POLYMER)"
_Name_common 'COPPER (I) ION'
_BMRB_code CU1
_PDB_code CU1
_Molecular_mass 63.546
_Mol_charge 1
_Mol_paramagnetic .
_Mol_aromatic no
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
CU CU CU . 1 . ?
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
$CopZ 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_type
_Vector_name
$CopZ 'recombinant technology' 'B. subtilis' Bacillus subtilis . plasmid pET21
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
$CopZ 2 mM '[U-99% 15N]'
$entity_CU1 2 mM .
'phosphate buffer' 100 mM .
DTT trace mM .
D2O 10 % .
H2O 90 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$CopZ 2 mM .
$entity_CU1 2 mM .
'phosphate buffer' 100 mM .
DTT trace mM .
D2O 10 % .
H2O 90 % .
stop_
save_
############################
# Computer software used #
############################
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'solution structure calculation'
stop_
_Details 'Guenter et al. 1997'
save_
save_XWINNMR
_Saveframe_category software
_Name xwinnmr
_Version 2.6
loop_
_Task
'NMR experiments collection'
stop_
_Details .
save_
save_XEASY
_Saveframe_category software
_Name XEASY
_Version 1.3.13
loop_
_Task
'data analysis'
stop_
_Details 'Eccles et al. 1991'
save_
save_AMBER
_Saveframe_category software
_Name AMBER
_Version 5.0
loop_
_Task
'solution structure refinement'
stop_
_Details 'Pearlman et al. 1997'
save_
save_molmol
_Saveframe_category software
_Name Molmol
_Version 2.4
loop_
_Task
'data analysis'
stop_
_Details 'Koradi et al. 1996'
save_
save_CORMA
_Saveframe_category software
_Name CORMA
_Version .
loop_
_Task
'data analysis'
stop_
_Details 'Borgias et al. 1989'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 700
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D_TOSCY-HMQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D TOSCY-HMQC'
_Sample_label .
save_
save_3D_NOESY-HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D NOESY-HSQC'
_Sample_label .
save_
save_3D_HNHA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNHA'
_Sample_label .
save_
save_2D_TOSCY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOSCY'
_Sample_label .
save_
save_2D_NOESY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_2D_HSQC_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D HSQC'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details 'The samples were kept under reduction conditions with DTT in an inert atmophere.'
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.0 0.01 na
pressure 1 . atm
temperature 300 0.5 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
TMS H 1 'methyl protons' ppm 0.0 . direct . . . 1.000000000
TMS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'3D TOSCY-HMQC'
'3D NOESY-HSQC'
'3D HNHA'
'2D TOSCY'
'2D NOESY'
'2D HSQC'
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 'CopZ from Bacillus subtilis'
_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 MET HA H 4.047 0.05 1
2 . 1 MET HB2 H 1.901 0.05 1
3 . 1 MET HB3 H 1.910 0.05 1
4 . 1 MET HG2 H 2.401 0.05 1
5 . 1 MET HG3 H 2.410 0.05 1
6 . 2 GLU N N 124.775 0.05 1
7 . 2 GLU H H 8.774 0.05 1
8 . 2 GLU HA H 4.308 0.05 1
9 . 2 GLU HB2 H 1.910 0.05 1
10 . 2 GLU HB3 H 1.840 0.05 1
11 . 2 GLU HG2 H 1.140 0.05 1
12 . 2 GLU HG3 H 0.843 0.05 1
13 . 3 GLN N N 119.957 0.05 1
14 . 3 GLN H H 8.271 0.05 1
15 . 3 GLN HA H 5.462 0.05 1
16 . 3 GLN HB2 H 1.889 0.05 1
17 . 3 GLN HB3 H 1.785 0.05 1
18 . 3 GLN HG2 H 2.120 0.05 1
19 . 3 GLN HG3 H 2.208 0.05 1
20 . 4 LYS N N 122.366 0.05 1
21 . 4 LYS H H 8.845 0.05 1
22 . 4 LYS HA H 4.804 0.05 1
23 . 4 LYS HB2 H 1.726 0.05 1
24 . 4 LYS HB3 H 1.730 0.05 1
25 . 4 LYS HG2 H 1.255 0.05 2
26 . 4 LYS HG3 H 1.260 0.05 2
27 . 4 LYS HD2 H 1.450 0.05 1
28 . 5 THR N N 118.925 0.05 1
29 . 5 THR H H 8.716 0.05 1
30 . 5 THR HA H 5.187 0.05 1
31 . 5 THR HB H 3.640 0.05 1
32 . 5 THR HG2 H 1.070 0.05 1
33 . 6 LEU N N 126.496 0.05 1
34 . 6 LEU H H 9.696 0.05 1
35 . 6 LEU HA H 4.698 0.05 1
36 . 6 LEU HB2 H 2.915 0.05 1
37 . 6 LEU HB3 H 2.920 0.05 1
38 . 6 LEU HG H 2.513 0.05 1
39 . 7 GLN N N 125.808 0.05 1
40 . 7 GLN H H 9.159 0.05 1
41 . 7 GLN HA H 4.785 0.05 1
42 . 7 GLN HB2 H 1.926 0.05 1
43 . 7 GLN HB3 H 2.108 0.05 1
44 . 7 GLN HG2 H 2.257 0.05 1
45 . 7 GLN HG3 H 2.228 0.05 1
46 . 8 VAL N N 127.184 0.05 1
47 . 8 VAL H H 8.778 0.05 1
48 . 8 VAL HA H 4.966 0.05 1
49 . 8 VAL HB H 1.520 0.05 1
50 . 8 VAL HG1 H 0.810 0.05 1
51 . 8 VAL HG2 H 0.696 0.05 1
52 . 9 GLU N N 127.873 0.05 1
53 . 9 GLU H H 9.511 0.05 1
54 . 9 GLU HA H 4.688 0.05 1
55 . 9 GLU HB2 H 2.206 0.05 1
56 . 9 GLU HB3 H 2.112 0.05 1
57 . 9 GLU HG2 H 1.901 0.05 1
58 . 9 GLU HG3 H 1.910 0.05 1
59 . 10 GLY N N 108.257 0.05 1
60 . 10 GLY H H 8.499 0.05 1
61 . 10 GLY HA2 H 3.697 0.05 1
62 . 10 GLY HA3 H 3.700 0.05 1
63 . 11 MET N N 121.334 0.05 1
64 . 11 MET H H 8.926 0.05 1
65 . 11 MET HA H 4.716 0.05 1
66 . 11 MET HB2 H 2.209 0.05 1
67 . 11 MET HB3 H 2.156 0.05 1
68 . 11 MET HG2 H 1.789 0.05 1
69 . 11 MET HG3 H 1.205 0.05 1
70 . 11 MET HE H 3.163 0.05 1
71 . 12 SER N N 121.334 0.05 1
72 . 12 SER H H 8.040 0.05 1
73 . 12 SER HA H 5.133 0.05 1
74 . 12 SER HB2 H 3.410 0.05 1
75 . 12 SER HB3 H 3.391 0.05 1
76 . 12 SER HG H 4.201 0.05 1
77 . 13 CYS N N 118.925 0.05 1
78 . 13 CYS H H 10.196 0.05 1
79 . 13 CYS HA H 4.751 0.05 1
80 . 13 CYS HB2 H 3.410 0.05 1
81 . 13 CYS HB3 H 2.399 0.05 1
82 . 14 GLN N N 116.860 0.05 1
83 . 14 GLN H H 8.856 0.05 1
84 . 14 GLN HA H 3.934 0.05 1
85 . 14 GLN HB2 H 1.854 0.05 1
86 . 14 GLN HB3 H 1.861 0.05 1
87 . 14 GLN HG2 H 2.108 0.05 1
88 . 14 GLN HG3 H 2.120 0.05 1
89 . 15 HIS N N 123.399 0.05 1
90 . 15 HIS H H 9.444 0.05 1
91 . 15 HIS HA H 4.348 0.05 1
92 . 15 HIS HB2 H 3.175 0.05 1
93 . 15 HIS HB3 H 3.182 0.05 1
94 . 15 HIS HD2 H 7.730 0.05 1
95 . 15 HIS HE1 H 7.570 0.05 1
96 . 16 CYS N N 124.431 0.05 1
97 . 16 CYS H H 8.033 0.05 1
98 . 16 CYS HA H 4.197 0.05 1
99 . 16 CYS HB2 H 3.411 0.05 1
100 . 16 CYS HB3 H 2.715 0.05 1
101 . 17 VAL N N 116.516 0.05 1
102 . 17 VAL H H 7.040 0.05 1
103 . 17 VAL HA H 3.087 0.05 1
104 . 17 VAL HB H 2.117 0.05 1
105 . 17 VAL HG1 H 0.848 0.05 2
106 . 17 VAL HG2 H 0.716 0.05 2
107 . 18 LYS N N 116.860 0.05 1
108 . 18 LYS H H 7.583 0.05 1
109 . 18 LYS HA H 4.040 0.05 1
110 . 18 LYS HB2 H 1.799 0.05 1
111 . 18 LYS HB3 H 1.809 0.05 1
112 . 18 LYS HG2 H 1.395 0.05 1
113 . 18 LYS HG3 H 1.408 0.05 1
114 . 18 LYS HD2 H 1.600 0.05 1
115 . 18 LYS HD3 H 1.580 0.05 1
116 . 18 LYS HE2 H 4.130 0.05 1
117 . 18 LYS HE3 H 4.141 0.05 1
118 . 18 LYS NZ N 124.090 0.05 1
119 . 18 LYS HZ H 8.390 0.05 1
120 . 19 ALA N N 123.399 0.05 1
121 . 19 ALA H H 8.028 0.05 1
122 . 19 ALA HA H 4.016 0.05 1
123 . 19 ALA HB H 1.556 0.05 1
124 . 20 VAL N N 118.925 0.05 1
125 . 20 VAL H H 7.862 0.05 1
126 . 20 VAL HA H 3.335 0.05 1
127 . 20 VAL HB H 1.860 0.05 1
128 . 20 VAL HG1 H 0.743 0.05 2
129 . 20 VAL HG2 H 0.550 0.05 2
130 . 21 GLU N N 117.893 0.05 1
131 . 21 GLU H H 8.776 0.05 1
132 . 21 GLU HA H 3.488 0.05 1
133 . 21 GLU HB2 H 2.075 0.05 1
134 . 21 GLU HB3 H 2.080 0.05 1
135 . 21 GLU HG2 H 2.374 0.05 1
136 . 21 GLU HG3 H 2.381 0.05 1
137 . 22 THR N N 113.419 0.05 1
138 . 22 THR H H 8.395 0.05 1
139 . 22 THR HA H 3.819 0.05 1
140 . 22 THR HB H 4.097 0.05 1
141 . 22 THR HG2 H 1.109 0.05 1
142 . 23 SER N N 115.484 0.05 1
143 . 23 SER H H 7.565 0.05 1
144 . 23 SER HA H 4.041 0.05 1
145 . 23 SER HB2 H 3.739 0.05 1
146 . 23 SER HB3 H 3.749 0.05 1
147 . 24 VAL N N 118.925 0.05 1
148 . 24 VAL H H 8.074 0.05 1
149 . 24 VAL HA H 3.454 0.05 1
150 . 24 VAL HB H 1.829 0.05 1
151 . 24 VAL HG1 H 0.709 0.05 1
152 . 24 VAL HG2 H 0.678 0.05 1
153 . 25 GLY N N 103.439 0.05 1
154 . 25 GLY H H 7.471 0.05 1
155 . 25 GLY HA2 H 3.705 0.05 1
156 . 25 GLY HA3 H 3.536 0.05 1
157 . 26 GLU N N 115.484 0.05 1
158 . 26 GLU H H 7.044 0.05 1
159 . 26 GLU HA H 4.087 0.05 1
160 . 26 GLU HB2 H 1.992 0.05 1
161 . 26 GLU HB3 H 1.909 0.05 1
162 . 26 GLU HG2 H 2.386 0.05 2
163 . 26 GLU HG3 H 2.247 0.05 2
164 . 27 LEU N N 120.907 0.05 1
165 . 27 LEU H H 7.278 0.05 1
166 . 27 LEU HA H 4.069 0.05 1
167 . 27 LEU HB2 H 1.942 0.05 2
168 . 27 LEU HB3 H 1.822 0.05 2
169 . 27 LEU HG H 1.080 0.05 1
170 . 27 LEU HD1 H 0.710 0.05 1
171 . 27 LEU HD2 H 0.648 0.05 1
172 . 28 ASP N N 125.119 0.05 1
173 . 28 ASP H H 8.445 0.05 1
174 . 28 ASP HA H 4.259 0.05 1
175 . 28 ASP HB2 H 2.598 0.05 2
176 . 28 ASP HB3 H 2.515 0.05 2
177 . 29 GLY N N 109.978 0.05 1
178 . 29 GLY H H 8.357 0.05 1
179 . 29 GLY HA2 H 4.423 0.05 2
180 . 29 GLY HA3 H 3.555 0.05 2
181 . 30 VAL N N 123.055 0.05 1
182 . 30 VAL H H 7.815 0.05 1
183 . 30 VAL HA H 4.031 0.05 1
184 . 30 VAL HB H 2.226 0.05 1
185 . 30 VAL HG1 H 0.765 0.05 1
186 . 30 VAL HG2 H 0.780 0.05 1
187 . 31 SER N N 123.399 0.05 1
188 . 31 SER H H 9.021 0.05 1
189 . 31 SER HA H 4.575 0.05 1
190 . 31 SER HB2 H 3.737 0.05 2
191 . 31 SER HB3 H 3.602 0.05 2
192 . 32 ALA N N 122.022 0.05 1
193 . 32 ALA H H 7.674 0.05 1
194 . 32 ALA HA H 4.543 0.05 1
195 . 32 ALA HB H 1.273 0.05 1
196 . 33 VAL N N 118.581 0.05 1
197 . 33 VAL H H 8.207 0.05 1
198 . 33 VAL HA H 4.789 0.05 1
199 . 33 VAL HB H 1.830 0.05 1
200 . 33 VAL HG1 H 0.688 0.05 1
201 . 33 VAL HG2 H 0.690 0.05 1
202 . 34 HIS N N 124.775 0.05 1
203 . 34 HIS H H 8.974 0.05 1
204 . 34 HIS HA H 4.965 0.05 1
205 . 34 HIS HB2 H 2.996 0.05 1
206 . 34 HIS HB3 H 3.010 0.05 1
207 . 34 HIS HD2 H 6.990 0.05 1
208 . 35 VAL N N 127.528 0.05 1
209 . 35 VAL H H 9.333 0.05 1
210 . 35 VAL HA H 4.232 0.05 1
211 . 35 VAL HB H 1.947 0.05 1
212 . 35 VAL HG1 H 0.808 0.05 2
213 . 35 VAL HG2 H 0.663 0.05 2
214 . 36 ASN N N 125.808 0.05 1
215 . 36 ASN H H 8.816 0.05 1
216 . 36 ASN HA H 4.773 0.05 1
217 . 36 ASN HB2 H 2.840 0.05 1
218 . 36 ASN HB3 H 2.588 0.05 1
219 . 37 LEU N N 125.464 0.05 1
220 . 37 LEU H H 8.688 0.05 1
221 . 37 LEU HA H 3.615 0.05 1
222 . 37 LEU HB2 H 1.571 0.05 1
223 . 37 LEU HB3 H 1.534 0.05 1
224 . 37 LEU HG H 1.228 0.05 1
225 . 37 LEU HD1 H 0.484 0.05 1
226 . 37 LEU HD2 H 0.508 0.05 1
227 . 38 GLU N N 118.581 0.05 1
228 . 38 GLU H H 8.581 0.05 1
229 . 38 GLU HA H 3.811 0.05 1
230 . 38 GLU HB2 H 2.009 0.05 2
231 . 38 GLU HB3 H 1.923 0.05 2
232 . 38 GLU HG2 H 2.240 0.05 1
233 . 38 GLU HG3 H 2.178 0.05 1
234 . 39 ALA N N 116.860 0.05 1
235 . 39 ALA H H 7.391 0.05 1
236 . 39 ALA HA H 4.300 0.05 1
237 . 39 ALA HB H 1.176 0.05 1
238 . 40 GLY N N 108.945 0.05 1
239 . 40 GLY H H 7.794 0.05 1
240 . 40 GLY HA2 H 3.969 0.05 2
241 . 40 GLY HA3 H 3.429 0.05 2
242 . 41 LYS N N 114.795 0.05 1
243 . 41 LYS H H 7.398 0.05 1
244 . 41 LYS HA H 5.203 0.05 1
245 . 41 LYS HB2 H 1.591 0.05 1
246 . 41 LYS HB3 H 1.438 0.05 1
247 . 41 LYS HG2 H 1.074 0.05 1
248 . 41 LYS HG3 H 1.081 0.05 1
249 . 41 LYS HD2 H 1.303 0.05 1
250 . 41 LYS HD3 H 1.307 0.05 1
251 . 42 VAL N N 122.366 0.05 1
252 . 42 VAL H H 9.153 0.05 1
253 . 42 VAL HA H 4.575 0.05 1
254 . 42 VAL HB H 1.933 0.05 1
255 . 42 VAL HG1 H 0.730 0.05 1
256 . 42 VAL HG2 H 0.540 0.05 1
257 . 43 ASP N N 129.249 0.05 1
258 . 43 ASP H H 9.207 0.05 1
259 . 43 ASP HA H 5.482 0.05 1
260 . 43 ASP HB2 H 2.581 0.05 1
261 . 43 ASP HB3 H 2.593 0.05 1
262 . 44 VAL N N 123.399 0.05 1
263 . 44 VAL H H 9.211 0.05 1
264 . 44 VAL HA H 4.976 0.05 1
265 . 44 VAL HB H 2.094 0.05 1
266 . 44 VAL HG1 H 0.986 0.05 1
267 . 44 VAL HG2 H 0.834 0.05 1
268 . 45 SER N N 122.711 0.05 1
269 . 45 SER H H 8.779 0.05 1
270 . 45 SER HA H 5.784 0.05 1
271 . 45 SER HB2 H 3.728 0.05 1
272 . 45 SER HB3 H 3.761 0.05 1
273 . 46 PHE N N 122.022 0.05 1
274 . 46 PHE H H 9.148 0.05 1
275 . 46 PHE HA H 5.342 0.05 1
276 . 46 PHE HB2 H 2.818 0.05 1
277 . 46 PHE HB3 H 2.504 0.05 1
278 . 46 PHE HD1 H 6.782 0.05 1
279 . 46 PHE HE1 H 7.020 0.05 1
280 . 46 PHE HZ H 7.150 0.05 1
281 . 47 ASP N N 118.925 0.05 1
282 . 47 ASP H H 8.340 0.05 1
283 . 47 ASP HA H 4.658 0.05 1
284 . 47 ASP HB2 H 2.868 0.05 1
285 . 47 ASP HB3 H 2.542 0.05 1
286 . 48 ALA N N 129.593 0.05 1
287 . 48 ALA H H 8.626 0.05 1
288 . 48 ALA HA H 5.075 0.05 1
289 . 48 ALA HB H 1.417 0.05 1
290 . 49 ASP N N 115.828 0.05 1
291 . 49 ASP H H 8.486 0.05 1
292 . 49 ASP HA H 4.530 0.05 1
293 . 49 ASP HB2 H 2.712 0.05 1
294 . 49 ASP HB3 H 2.568 0.05 1
295 . 50 LYS N N 117.549 0.05 1
296 . 50 LYS H H 7.837 0.05 1
297 . 50 LYS HA H 4.318 0.05 1
298 . 50 LYS HB2 H 1.787 0.05 1
299 . 50 LYS HB3 H 1.698 0.05 1
300 . 50 LYS HG2 H 1.247 0.05 1
301 . 50 LYS HG3 H 1.256 0.05 1
302 . 50 LYS HD2 H 1.474 0.05 1
303 . 50 LYS HD3 H 1.464 0.05 1
304 . 51 VAL N N 120.302 0.05 1
305 . 51 VAL H H 8.142 0.05 1
306 . 51 VAL HA H 4.371 0.05 1
307 . 51 VAL HB H 2.292 0.05 1
308 . 51 VAL HG1 H 0.964 0.05 1
309 . 51 VAL HG2 H 0.720 0.05 1
310 . 52 SER N N 117.893 0.05 1
311 . 52 SER H H 8.291 0.05 1
312 . 52 SER HA H 5.112 0.05 1
313 . 52 SER HB2 H 4.177 0.05 1
314 . 52 SER HB3 H 3.833 0.05 1
315 . 53 VAL N N 116.860 0.05 1
316 . 53 VAL H H 8.597 0.05 1
317 . 53 VAL HA H 3.472 0.05 1
318 . 53 VAL HB H 2.091 0.05 1
319 . 53 VAL HG1 H 1.057 0.05 2
320 . 53 VAL HG2 H 1.001 0.05 2
321 . 54 LYS N N 119.613 0.05 1
322 . 54 LYS H H 7.714 0.05 1
323 . 54 LYS HA H 3.934 0.05 1
324 . 54 LYS HB2 H 1.640 0.05 1
325 . 54 LYS HB3 H 1.714 0.05 1
326 . 54 LYS HG2 H 1.327 0.05 1
327 . 54 LYS HG3 H 1.337 0.05 1
328 . 54 LYS HD2 H 1.470 0.05 1
329 . 54 LYS HD3 H 1.480 0.05 1
330 . 55 ASP N N 118.237 0.05 1
331 . 55 ASP H H 7.496 0.05 1
332 . 55 ASP HA H 4.080 0.05 1
333 . 55 ASP HB2 H 2.940 0.05 1
334 . 55 ASP HB3 H 2.441 0.05 1
335 . 56 ILE N N 119.613 0.05 1
336 . 56 ILE H H 7.321 0.05 1
337 . 56 ILE HA H 3.117 0.05 1
338 . 56 ILE HB H 1.396 0.05 1
339 . 56 ILE HG2 H -0.021 0.05 1
340 . 56 ILE HG12 H 0.205 0.05 1
341 . 56 ILE HG13 H 0.216 0.05 1
342 . 56 ILE HD1 H -0.238 0.05 1
343 . 57 ALA N N 120.990 0.05 1
344 . 57 ALA H H 8.229 0.05 1
345 . 57 ALA HA H 3.597 0.05 1
346 . 57 ALA HB H 1.446 0.05 1
347 . 58 ASP N N 116.860 0.05 1
348 . 58 ASP H H 8.753 0.05 1
349 . 58 ASP HA H 4.172 0.05 1
350 . 58 ASP HB2 H 2.692 0.05 1
351 . 58 ASP HB3 H 2.540 0.05 1
352 . 59 ALA N N 121.678 0.05 1
353 . 59 ALA H H 7.408 0.05 1
354 . 59 ALA HA H 4.070 0.05 1
355 . 59 ALA HB H 1.302 0.05 1
356 . 60 ILE N N 118.237 0.05 1
357 . 60 ILE H H 7.554 0.05 1
358 . 60 ILE HA H 3.330 0.05 1
359 . 60 ILE HB H 1.714 0.05 1
360 . 60 ILE HG12 H 0.701 0.05 1
361 . 60 ILE HG13 H 0.710 0.05 1
362 . 60 ILE HG2 H 0.352 0.05 1
363 . 60 ILE HD1 H 0.116 0.05 1
364 . 61 GLU N N 119.269 0.05 1
365 . 61 GLU H H 8.578 0.05 1
366 . 61 GLU HA H 4.607 0.05 1
367 . 61 GLU HB2 H 2.012 0.05 1
368 . 61 GLU HB3 H 2.021 0.05 1
369 . 61 GLU HG2 H 2.699 0.05 1
370 . 61 GLU HG3 H 2.508 0.05 1
371 . 62 ASP N N 121.334 0.05 1
372 . 62 ASP H H 8.596 0.05 1
373 . 62 ASP HA H 4.383 0.05 1
374 . 62 ASP HB2 H 2.766 0.05 2
375 . 62 ASP HB3 H 2.530 0.05 2
376 . 63 GLN N N 114.107 0.05 1
377 . 63 GLN H H 7.308 0.05 1
378 . 63 GLN HA H 4.124 0.05 1
379 . 63 GLN HB2 H 2.194 0.05 1
380 . 63 GLN HB3 H 2.183 0.05 1
381 . 63 GLN HG2 H 2.680 0.05 1
382 . 63 GLN HG3 H 2.690 0.05 1
383 . 63 GLN HE21 H 6.690 0.05 1
384 . 63 GLN HE22 H 6.810 0.05 1
385 . 64 GLY N N 104.816 0.05 1
386 . 64 GLY H H 7.819 0.05 1
387 . 64 GLY HA2 H 3.785 0.05 1
388 . 64 GLY HA3 H 3.433 0.05 1
389 . 65 TYR N N 119.269 0.05 1
390 . 65 TYR H H 6.451 0.05 1
391 . 65 TYR HA H 4.744 0.05 1
392 . 65 TYR HB2 H 3.089 0.05 1
393 . 65 TYR HB3 H 2.088 0.05 1
394 . 65 TYR HE1 H 6.810 0.05 1
395 . 65 TYR HD1 H 6.680 0.05 1
396 . 66 ASP N N 118.237 0.05 1
397 . 66 ASP H H 7.972 0.05 1
398 . 66 ASP HA H 4.957 0.05 1
399 . 66 ASP HB2 H 2.516 0.05 1
400 . 66 ASP HB3 H 2.391 0.05 1
401 . 67 VAL N N 124.431 0.05 1
402 . 67 VAL H H 9.475 0.05 1
403 . 67 VAL HA H 4.334 0.05 1
404 . 67 VAL HB H 2.118 0.05 1
405 . 67 VAL HG1 H 0.998 0.05 1
406 . 67 VAL HG2 H 0.959 0.05 1
407 . 68 ALA N N 132.002 0.05 1
408 . 68 ALA H H 8.797 0.05 1
409 . 68 ALA HA H 4.259 0.05 1
410 . 68 ALA HB H 1.277 0.05 1
411 . 69 LYS N N 115.828 0.05 1
412 . 69 LYS H H 7.720 0.05 1
413 . 69 LYS HA H 4.280 0.05 1
414 . 69 LYS HB2 H 1.670 0.05 1
415 . 69 LYS HB3 H 1.680 0.05 1
416 . 69 LYS HG2 H 1.284 0.05 1
417 . 69 LYS HG3 H 1.289 0.05 1
418 . 69 LYS HD2 H 1.530 0.05 1
419 . 69 LYS HD3 H 1.540 0.05 1
420 . 70 ILE N N 123.399 0.05 1
421 . 70 ILE H H 8.276 0.05 1
422 . 70 ILE HA H 4.202 0.05 1
423 . 70 ILE HB H 1.466 0.05 1
424 . 70 ILE HG12 H 0.647 0.05 1
425 . 70 ILE HG13 H 0.656 0.05 1
426 . 70 ILE HG2 H 0.338 0.05 1
427 . 71 GLU N N 126.152 0.05 1
428 . 71 GLU H H 8.696 0.05 1
429 . 71 GLU HA H 4.359 0.05 1
430 . 71 GLU HB2 H 1.945 0.05 2
431 . 71 GLU HB3 H 1.848 0.05 2
432 . 71 GLU HG2 H 2.093 0.05 1
433 . 71 GLU HG3 H 2.085 0.05 1
434 . 72 GLY N N 109.978 0.05 1
435 . 72 GLY H H 8.469 0.05 1
436 . 72 GLY HA2 H 4.012 0.05 2
437 . 72 GLY HA3 H 3.942 0.05 2
438 . 73 ARG N N 125.808 0.05 1
439 . 73 ARG H H 7.885 0.05 1
440 . 73 ARG HA H 4.059 0.05 1
441 . 73 ARG HB2 H 1.748 0.05 1
442 . 73 ARG HB3 H 1.592 0.05 1
443 . 73 ARG HG2 H 1.476 0.05 1
444 . 73 ARG HG3 H 1.486 0.05 1
445 . 73 ARG HD2 H 3.068 0.05 1
446 . 73 ARG HD3 H 3.077 0.05 1
stop_
save_