data_4819
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
High precision NMR structure of YhhP, a novel Esherichia coli protein implicated
in the cell division
;
_BMRB_accession_number 4819
_BMRB_flat_file_name bmr4819.str
_Entry_type original
_Submission_date 2000-09-05
_Accession_date 2000-09-05
_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 Katoh Etsuko . .
2 Hatta Tomohisa . .
3 Shindo Heisaburo . .
4 Yamada H. . .
5 Mizuno T. . .
6 Yamazaki Toshimasa . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 471
"13C chemical shifts" 379
"15N chemical shifts" 72
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2012-12-07 update BMRB 'delete outlier: 68 THR N 11.74'
2000-12-21 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
High precision NMR structure of YhhP, a novel escherichia coli protein
implicated in cell division
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 20534887
_PubMed_ID 11080457
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Katoh Etsuko . .
2 Hatta Tomohisa . .
3 Shindo Heisaburo . .
4 Yamada H. . .
5 Mizuno T. . .
6 Yamazaki Toshimasa . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 304
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 219
_Page_last 229
_Year 2000
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_Yhh
_Saveframe_category molecular_system
_Mol_system_name 'Yhh monomer'
_Abbreviation_common Yhh
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Yhh monomer' $Yhh_monomer
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not reported'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Yhh_monomer
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Yhh
_Abbreviation_common Yhh
_Molecular_mass .
_Mol_thiol_state 'not reported'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 81
_Mol_residue_sequence
;
MTDLFSSPDHTLDALGLRCP
EPVMMVRKTVRNMQPGETLL
IIADDPATTRDIPGFCTFME
HELVAKETDGLPYRYLIRKG
G
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 THR 3 ASP 4 LEU 5 PHE
6 SER 7 SER 8 PRO 9 ASP 10 HIS
11 THR 12 LEU 13 ASP 14 ALA 15 LEU
16 GLY 17 LEU 18 ARG 19 CYS 20 PRO
21 GLU 22 PRO 23 VAL 24 MET 25 MET
26 VAL 27 ARG 28 LYS 29 THR 30 VAL
31 ARG 32 ASN 33 MET 34 GLN 35 PRO
36 GLY 37 GLU 38 THR 39 LEU 40 LEU
41 ILE 42 ILE 43 ALA 44 ASP 45 ASP
46 PRO 47 ALA 48 THR 49 THR 50 ARG
51 ASP 52 ILE 53 PRO 54 GLY 55 PHE
56 CYS 57 THR 58 PHE 59 MET 60 GLU
61 HIS 62 GLU 63 LEU 64 VAL 65 ALA
66 LYS 67 GLU 68 THR 69 ASP 70 GLY
71 LEU 72 PRO 73 TYR 74 ARG 75 TYR
76 LEU 77 ILE 78 ARG 79 LYS 80 GLY
81 GLY
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-29
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 1DCJ "Solution Structure Of Yhhp, A Novel Escherichia Coli Protein Implicated In The Cell Division" 100.00 81 100.00 100.00 1.41e-51
PDB 3LVJ "Crystal Structure Of E.Coli Iscs-Tusa Complex (Form 1)" 98.77 82 100.00 100.00 6.84e-51
PDB 3LVK "Crystal Structure Of E.Coli Iscs-Tusa Complex (Form 2)" 98.77 82 100.00 100.00 6.84e-51
DBJ BAB37742 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 100.00 81 100.00 100.00 1.41e-51
DBJ BAE77823 "conserved hypothetical protein required for cell growth [Escherichia coli str. K-12 substr. W3110]" 100.00 81 100.00 100.00 1.41e-51
DBJ BAG79262 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 81 100.00 100.00 1.41e-51
DBJ BAI27727 "conserved hypothetical protein [Escherichia coli O26:H11 str. 11368]" 100.00 81 100.00 100.00 1.41e-51
DBJ BAI32898 "conserved hypothetical protein [Escherichia coli O103:H2 str. 12009]" 100.00 81 100.00 100.00 1.41e-51
EMBL CAP77921 "Sulfurtransferase tusA [Escherichia coli LF82]" 100.00 81 100.00 100.00 1.41e-51
EMBL CAQ33789 "sulfur transfer protein [Escherichia coli BL21(DE3)]" 100.00 81 100.00 100.00 1.41e-51
EMBL CAQ90921 "sulfurtransferase [Escherichia fergusonii ATCC 35469]" 98.77 81 100.00 100.00 1.12e-50
EMBL CAR00415 "sulfurtransferase [Escherichia coli IAI1]" 100.00 81 100.00 100.00 1.41e-51
EMBL CAR05085 "sulfurtransferase [Escherichia coli S88]" 100.00 81 100.00 100.00 1.41e-51
GB AAB18445 "unnamed protein product [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51
GB AAC76495 "mnm(5)-s(2)U34-tRNA 2-thiolation sulfurtransferase [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51
GB AAG58579 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 100.00 81 100.00 100.00 1.41e-51
GB AAN44947 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 100.00 81 100.00 100.00 1.41e-51
GB AAN82699 "SirA protein [Escherichia coli CFT073]" 100.00 81 100.00 100.00 1.41e-51
REF NP_290018 "sulfur transfer protein SirA [Escherichia coli O157:H7 str. EDL933]" 100.00 81 100.00 100.00 1.41e-51
REF NP_312346 "sulfur transfer protein SirA [Escherichia coli O157:H7 str. Sakai]" 100.00 81 100.00 100.00 1.41e-51
REF NP_417927 "mnm(5)-s(2)U34-tRNA 2-thiolation sulfurtransferase [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51
REF NP_709240 "sulfur transfer protein SirA [Shigella flexneri 2a str. 301]" 100.00 81 100.00 100.00 1.41e-51
REF NP_756125 "sulfur transfer protein SirA [Escherichia coli CFT073]" 100.00 81 100.00 100.00 1.41e-51
SP A7ZT06 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli E24377A]" 100.00 81 100.00 100.00 1.41e-51
SP A8A5S8 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli HS]" 100.00 81 100.00 100.00 1.41e-51
SP B1J0G0 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli ATCC 8739]" 100.00 81 100.00 100.00 1.41e-51
SP B1LID3 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli SMS-3-5]" 100.00 81 98.77 98.77 6.36e-51
SP B1X7S8 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli str. K-12 subst" 100.00 81 100.00 100.00 1.41e-51
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Yhh_monomer E.coli 562 Eubacteria . 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
$Yhh_monomer 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Yhh_monomer . 1.0 .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_list
_Saveframe_category NMR_spectrometer
_Manufacturer .
_Model .
_Field_strength .
_Details .
save_
#############################
# NMR applied experiments #
#############################
save__1
_Saveframe_category NMR_applied_experiment
_Sample_label $sample
save_
#######################
# Sample conditions #
#######################
save_Ex-cond
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.2 0.1 n/a
temperature 298 1 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
TSP H 1 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 1
TSP C 13 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.25144581
'liquid ammonia' N 15 nitrogen ppm 24.93 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.10132944
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_na
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample
stop_
_Sample_conditions_label $Ex-cond
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Yhh monomer'
_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 4.03 . 1
2 . 1 MET HB2 H 2.15 . 2
3 . 1 MET HB3 H 2.11 . 2
4 . 1 MET HG2 H 2.62 . 1
5 . 1 MET HG3 H 2.62 . 1
6 . 1 MET CA C 55.55 . 1
7 . 1 MET CB C 34.06 . 1
8 . 1 MET CG C 31.47 . 1
9 . 2 THR HA H 4.35 . 1
10 . 2 THR HB H 4.15 . 1
11 . 2 THR HG2 H 1.19 . 1
12 . 2 THR C C 175.85 . 1
13 . 2 THR CA C 62.32 . 1
14 . 2 THR CB C 69.90 . 1
15 . 2 THR CG2 C 21.71 . 1
16 . 3 ASP H H 8.59 . 1
17 . 3 ASP HA H 4.77 . 1
18 . 3 ASP HB2 H 2.82 . 1
19 . 3 ASP HB3 H 2.82 . 1
20 . 3 ASP C C 177.12 . 1
21 . 3 ASP CA C 53.64 . 1
22 . 3 ASP CB C 41.47 . 1
23 . 3 ASP CG C 180.24 . 1
24 . 3 ASP N N 123.73 . 1
25 . 4 LEU H H 8.51 . 1
26 . 4 LEU HA H 4.00 . 1
27 . 4 LEU HB2 H 1.18 . 1
28 . 4 LEU HB3 H 1.02 . 1
29 . 4 LEU HG H 1.54 . 1
30 . 4 LEU HD1 H 0.80 . 2
31 . 4 LEU HD2 H 0.75 . 2
32 . 4 LEU C C 177.45 . 1
33 . 4 LEU CA C 56.76 . 1
34 . 4 LEU CB C 42.01 . 1
35 . 4 LEU CG C 26.98 . 1
36 . 4 LEU CD1 C 25.33 . 2
37 . 4 LEU CD2 C 23.06 . 2
38 . 4 LEU N N 123.07 . 1
39 . 5 PHE H H 8.14 . 1
40 . 5 PHE HA H 4.36 . 1
41 . 5 PHE HB2 H 2.99 . 1
42 . 5 PHE HB3 H 3.30 . 1
43 . 5 PHE HD1 H 7.15 . 1
44 . 5 PHE HD2 H 7.15 . 1
45 . 5 PHE HE1 H 7.04 . 1
46 . 5 PHE HE2 H 7.04 . 1
47 . 5 PHE HZ H 6.73 . 1
48 . 5 PHE C C 175.86 . 1
49 . 5 PHE CA C 58.27 . 1
50 . 5 PHE CB C 39.98 . 1
51 . 5 PHE CD1 C 131.39 . 1
52 . 5 PHE CD2 C 131.39 . 1
53 . 5 PHE CE1 C 131.09 . 1
54 . 5 PHE CE2 C 131.09 . 1
55 . 5 PHE CZ C 129.13 . 1
56 . 5 PHE N N 114.67 . 1
57 . 6 SER H H 7.38 . 1
58 . 6 SER HA H 4.30 . 1
59 . 6 SER HB2 H 3.97 . 1
60 . 6 SER HB3 H 3.97 . 1
61 . 6 SER C C 174.67 . 1
62 . 6 SER CA C 60.10 . 1
63 . 6 SER CB C 64.37 . 1
64 . 6 SER N N 112.76 . 1
65 . 7 SER H H 8.58 . 1
66 . 7 SER HA H 4.65 . 1
67 . 7 SER HB2 H 3.86 . 2
68 . 7 SER HB3 H 3.73 . 2
69 . 7 SER C C 171.86 . 1
70 . 7 SER CA C 56.46 . 1
71 . 7 SER CB C 63.27 . 1
72 . 7 SER N N 115.93 . 1
73 . 8 PRO HA H 4.60 . 1
74 . 8 PRO HB2 H 2.19 . 1
75 . 8 PRO HB3 H 1.87 . 1
76 . 8 PRO HG2 H 1.97 . 1
77 . 8 PRO HG3 H 1.86 . 1
78 . 8 PRO HD2 H 3.49 . 1
79 . 8 PRO HD3 H 3.66 . 1
80 . 8 PRO C C 177.49 . 1
81 . 8 PRO CA C 62.22 . 1
82 . 8 PRO CB C 31.91 . 1
83 . 8 PRO CG C 27.25 . 1
84 . 8 PRO CD C 49.60 . 1
85 . 9 ASP H H 8.29 . 1
86 . 9 ASP HA H 4.34 . 1
87 . 9 ASP HB2 H 3.51 . 1
88 . 9 ASP HB3 H 2.40 . 1
89 . 9 ASP C C 173.44 . 1
90 . 9 ASP CA C 58.31 . 1
91 . 9 ASP CB C 41.68 . 1
92 . 9 ASP CG C 179.92 . 1
93 . 9 ASP N N 121.75 . 1
94 . 10 HIS H H 8.08 . 1
95 . 10 HIS HA H 4.84 . 1
96 . 10 HIS HB2 H 2.92 . 1
97 . 10 HIS HB3 H 3.03 . 1
98 . 10 HIS HD2 H 6.88 . 1
99 . 10 HIS HE1 H 7.95 . 1
100 . 10 HIS C C 174.21 . 1
101 . 10 HIS CA C 54.79 . 1
102 . 10 HIS CB C 34.98 . 1
103 . 10 HIS CD2 C 118.82 . 1
104 . 10 HIS CE1 C 138.72 . 1
105 . 10 HIS N N 115.07 . 1
106 . 11 THR H H 8.90 . 1
107 . 11 THR HA H 5.29 . 1
108 . 11 THR HB H 3.99 . 1
109 . 11 THR HG2 H 1.16 . 1
110 . 11 THR C C 172.83 . 1
111 . 11 THR CA C 62.38 . 1
112 . 11 THR CB C 72.02 . 1
113 . 11 THR CG2 C 21.38 . 1
114 . 11 THR N N 116.94 . 1
115 . 12 LEU H H 9.67 . 1
116 . 12 LEU HA H 4.72 . 1
117 . 12 LEU HB2 H 1.45 . 1
118 . 12 LEU HB3 H 1.81 . 1
119 . 12 LEU HG H 1.50 . 1
120 . 12 LEU HD1 H 0.92 . 1
121 . 12 LEU HD2 H 0.82 . 1
122 . 12 LEU C C 173.29 . 1
123 . 12 LEU CA C 53.90 . 1
124 . 12 LEU CB C 45.94 . 1
125 . 12 LEU CG C 27.77 . 1
126 . 12 LEU CD1 C 23.80 . 1
127 . 12 LEU CD2 C 26.50 . 1
128 . 12 LEU N N 128.22 . 1
129 . 13 ASP H H 8.86 . 1
130 . 13 ASP HA H 4.74 . 1
131 . 13 ASP HB2 H 2.50 . 1
132 . 13 ASP HB3 H 3.02 . 1
133 . 13 ASP C C 175.30 . 1
134 . 13 ASP CA C 53.67 . 1
135 . 13 ASP CB C 40.51 . 1
136 . 13 ASP CG C 178.96 . 1
137 . 13 ASP N N 126.51 . 1
138 . 14 ALA H H 9.07 . 1
139 . 14 ALA HA H 4.79 . 1
140 . 14 ALA HB H 1.40 . 1
141 . 14 ALA C C 178.52 . 1
142 . 14 ALA CA C 49.64 . 1
143 . 14 ALA CB C 17.88 . 1
144 . 14 ALA N N 127.98 . 1
145 . 15 LEU H H 8.89 . 1
146 . 15 LEU HA H 4.01 . 1
147 . 15 LEU HB2 H 2.10 . 1
148 . 15 LEU HB3 H 1.28 . 1
149 . 15 LEU HG H 1.64 . 1
150 . 15 LEU HD1 H 0.90 . 1
151 . 15 LEU HD2 H 0.70 . 1
152 . 15 LEU C C 178.81 . 1
153 . 15 LEU CA C 57.79 . 1
154 . 15 LEU CB C 40.61 . 1
155 . 15 LEU CG C 26.98 . 1
156 . 15 LEU CD1 C 25.41 . 1
157 . 15 LEU CD2 C 23.29 . 1
158 . 15 LEU N N 125.09 . 1
159 . 16 GLY H H 10.26 . 1
160 . 16 GLY HA2 H 3.76 . 1
161 . 16 GLY HA3 H 4.32 . 1
162 . 16 GLY C C 174.48 . 1
163 . 16 GLY CA C 45.48 . 1
164 . 16 GLY N N 113.55 . 1
165 . 17 LEU H H 7.44 . 1
166 . 17 LEU HA H 4.70 . 1
167 . 17 LEU HB2 H 1.96 . 1
168 . 17 LEU HB3 H 1.26 . 1
169 . 17 LEU HG H 1.58 . 1
170 . 17 LEU HD1 H 0.87 . 1
171 . 17 LEU HD2 H 0.89 . 1
172 . 17 LEU C C 178.32 . 1
173 . 17 LEU CA C 54.15 . 1
174 . 17 LEU CB C 42.38 . 1
175 . 17 LEU CG C 27.08 . 1
176 . 17 LEU CD1 C 22.02 . 1
177 . 17 LEU CD2 C 25.82 . 1
178 . 17 LEU N N 118.12 . 1
179 . 18 ARG H H 9.50 . 1
180 . 18 ARG HA H 4.92 . 1
181 . 18 ARG HB2 H 1.91 . 1
182 . 18 ARG HB3 H 1.83 . 1
183 . 18 ARG HG2 H 1.83 . 2
184 . 18 ARG HG3 H 1.55 . 2
185 . 18 ARG HD2 H 3.30 . 1
186 . 18 ARG HD3 H 3.30 . 1
187 . 18 ARG C C 175.84 . 1
188 . 18 ARG CA C 53.88 . 1
189 . 18 ARG CB C 33.28 . 1
190 . 18 ARG CG C 26.95 . 1
191 . 18 ARG CD C 43.17 . 1
192 . 18 ARG N N 123.35 . 1
193 . 19 CYS H H 8.95 . 1
194 . 19 CYS HA H 4.58 . 1
195 . 19 CYS HB2 H 3.11 . 1
196 . 19 CYS HB3 H 2.96 . 1
197 . 19 CYS C C 174.75 . 1
198 . 19 CYS CA C 57.74 . 1
199 . 19 CYS CB C 27.36 . 1
200 . 19 CYS N N 124.56 . 1
201 . 20 PRO HA H 5.18 . 1
202 . 20 PRO HB2 H 2.43 . 1
203 . 20 PRO HB3 H 2.21 . 1
204 . 20 PRO HG2 H 1.79 . 1
205 . 20 PRO HG3 H 2.07 . 1
206 . 20 PRO HD2 H 3.65 . 1
207 . 20 PRO HD3 H 3.65 . 1
208 . 20 PRO C C 176.55 . 1
209 . 20 PRO CA C 65.27 . 1
210 . 20 PRO CB C 34.17 . 1
211 . 20 PRO CG C 24.63 . 1
212 . 20 PRO CD C 50.01 . 1
213 . 21 GLU H H 8.87 . 1
214 . 21 GLU HA H 4.28 . 1
215 . 21 GLU HB2 H 2.27 . 1
216 . 21 GLU HB3 H 2.09 . 1
217 . 21 GLU HG2 H 2.55 . 2
218 . 21 GLU HG3 H 2.35 . 2
219 . 21 GLU C C 175.56 . 1
220 . 21 GLU CA C 61.15 . 1
221 . 21 GLU CB C 28.93 . 1
222 . 21 GLU CG C 37.05 . 1
223 . 21 GLU CD C 182.57 . 1
224 . 21 GLU N N 123.89 . 1
225 . 22 PRO HA H 4.02 . 1
226 . 22 PRO HB2 H 1.74 . 1
227 . 22 PRO HB3 H 1.94 . 1
228 . 22 PRO HG2 H 2.40 . 1
229 . 22 PRO HG3 H 1.83 . 1
230 . 22 PRO HD2 H 3.79 . 1
231 . 22 PRO HD3 H 3.38 . 1
232 . 22 PRO C C 177.74 . 1
233 . 22 PRO CA C 67.72 . 1
234 . 22 PRO CB C 31.22 . 1
235 . 22 PRO CG C 28.80 . 1
236 . 22 PRO CD C 49.68 . 1
237 . 23 VAL H H 8.55 . 1
238 . 23 VAL HA H 3.14 . 1
239 . 23 VAL HB H 1.97 . 1
240 . 23 VAL HG1 H 0.75 . 1
241 . 23 VAL HG2 H 0.81 . 1
242 . 23 VAL C C 177.29 . 1
243 . 23 VAL CA C 67.07 . 1
244 . 23 VAL CB C 30.70 . 1
245 . 23 VAL CG1 C 21.83 . 1
246 . 23 VAL CG2 C 25.29 . 1
247 . 23 VAL N N 115.71 . 1
248 . 24 MET H H 7.75 . 1
249 . 24 MET HA H 4.06 . 1
250 . 24 MET HB2 H 2.23 . 1
251 . 24 MET HB3 H 2.75 . 1
252 . 24 MET HG2 H 2.60 . 1
253 . 24 MET HG3 H 2.19 . 1
254 . 24 MET C C 179.53 . 1
255 . 24 MET CA C 59.50 . 1
256 . 24 MET CB C 32.21 . 1
257 . 24 MET CG C 32.21 . 1
258 . 24 MET N N 119.54 . 1
259 . 25 MET H H 8.22 . 1
260 . 25 MET HA H 4.37 . 1
261 . 25 MET HB2 H 2.18 . 1
262 . 25 MET HB3 H 2.02 . 1
263 . 25 MET HG2 H 2.66 . 1
264 . 25 MET HG3 H 2.66 . 1
265 . 25 MET C C 180.02 . 1
266 . 25 MET CA C 57.31 . 1
267 . 25 MET CB C 32.00 . 1
268 . 25 MET CG C 32.45 . 1
269 . 25 MET N N 117.51 . 1
270 . 26 VAL H H 8.52 . 1
271 . 26 VAL HA H 3.15 . 1
272 . 26 VAL HB H 1.76 . 1
273 . 26 VAL HG1 H 0.32 . 1
274 . 26 VAL HG2 H 0.78 . 1
275 . 26 VAL C C 176.84 . 1
276 . 26 VAL CA C 67.52 . 1
277 . 26 VAL CB C 31.32 . 1
278 . 26 VAL CG1 C 22.55 . 1
279 . 26 VAL CG2 C 24.33 . 1
280 . 26 VAL N N 124.20 . 1
281 . 27 ARG H H 8.68 . 1
282 . 27 ARG HA H 3.79 . 1
283 . 27 ARG HB2 H 1.98 . 2
284 . 27 ARG HB3 H 1.89 . 2
285 . 27 ARG HG2 H 1.85 . 2
286 . 27 ARG HG3 H 1.73 . 2
287 . 27 ARG HD2 H 3.32 . 1
288 . 27 ARG HD3 H 3.32 . 1
289 . 27 ARG C C 179.03 . 1
290 . 27 ARG CA C 60.51 . 1
291 . 27 ARG CB C 30.46 . 1
292 . 27 ARG CG C 28.27 . 1
293 . 27 ARG CD C 44.03 . 1
294 . 27 ARG N N 119.39 . 1
295 . 28 LYS H H 7.53 . 1
296 . 28 LYS HA H 4.00 . 1
297 . 28 LYS HB2 H 1.95 . 1
298 . 28 LYS HB3 H 1.95 . 1
299 . 28 LYS HG2 H 1.61 . 2
300 . 28 LYS HG3 H 1.48 . 2
301 . 28 LYS HD2 H 1.72 . 1
302 . 28 LYS HD3 H 1.72 . 1
303 . 28 LYS HE2 H 3.01 . 1
304 . 28 LYS HE3 H 3.01 . 1
305 . 28 LYS C C 178.14 . 1
306 . 28 LYS CA C 59.66 . 1
307 . 28 LYS CB C 32.88 . 1
308 . 28 LYS CG C 25.19 . 1
309 . 28 LYS CD C 29.89 . 1
310 . 28 LYS CE C 42.17 . 1
311 . 28 LYS N N 117.24 . 1
312 . 29 THR H H 7.80 . 1
313 . 29 THR HA H 3.93 . 1
314 . 29 THR HB H 4.07 . 1
315 . 29 THR HG2 H 1.14 . 1
316 . 29 THR C C 177.12 . 1
317 . 29 THR CA C 67.17 . 1
318 . 29 THR CB C 68.66 . 1
319 . 29 THR CG2 C 21.88 . 1
320 . 29 THR N N 116.22 . 1
321 . 30 VAL H H 8.89 . 1
322 . 30 VAL HA H 4.06 . 1
323 . 30 VAL HB H 2.06 . 1
324 . 30 VAL HG1 H 0.74 . 1
325 . 30 VAL HG2 H 0.89 . 1
326 . 30 VAL C C 178.83 . 1
327 . 30 VAL CA C 64.99 . 1
328 . 30 VAL CB C 31.70 . 1
329 . 30 VAL CG1 C 21.58 . 1
330 . 30 VAL CG2 C 23.70 . 1
331 . 30 VAL N N 120.41 . 1
332 . 31 ARG H H 7.47 . 1
333 . 31 ARG HA H 4.19 . 1
334 . 31 ARG HB2 H 2.01 . 1
335 . 31 ARG HB3 H 1.93 . 1
336 . 31 ARG HG2 H 1.73 . 2
337 . 31 ARG HG3 H 1.87 . 2
338 . 31 ARG HD2 H 3.29 . 1
339 . 31 ARG HD3 H 3.29 . 1
340 . 31 ARG C C 176.76 . 1
341 . 31 ARG CA C 59.41 . 1
342 . 31 ARG CB C 30.05 . 1
343 . 31 ARG CG C 27.37 . 1
344 . 31 ARG CD C 43.72 . 1
345 . 31 ARG N N 119.95 . 1
346 . 32 ASN H H 7.04 . 1
347 . 32 ASN HA H 4.86 . 1
348 . 32 ASN HB2 H 3.06 . 1
349 . 32 ASN HB3 H 2.74 . 1
350 . 32 ASN HD21 H 7.64 . 2
351 . 32 ASN HD22 H 6.92 . 2
352 . 32 ASN C C 175.35 . 1
353 . 32 ASN CA C 53.22 . 1
354 . 32 ASN CB C 39.66 . 1
355 . 32 ASN CG C 177.04 . 1
356 . 32 ASN N N 113.19 . 1
357 . 32 ASN ND2 N 112.76 . 1
358 . 33 MET H H 7.20 . 1
359 . 33 MET HA H 4.29 . 1
360 . 33 MET HB2 H 1.95 . 1
361 . 33 MET HB3 H 2.34 . 1
362 . 33 MET HG2 H 1.81 . 1
363 . 33 MET HG3 H 2.31 . 1
364 . 33 MET HE H 1.85 . 1
365 . 33 MET C C 175.84 . 1
366 . 33 MET CA C 55.78 . 1
367 . 33 MET CB C 36.04 . 1
368 . 33 MET CG C 29.29 . 1
369 . 33 MET CE C 15.50 . 1
370 . 33 MET N N 118.70 . 1
371 . 34 GLN H H 8.91 . 1
372 . 34 GLN HA H 4.81 . 1
373 . 34 GLN HB2 H 1.69 . 1
374 . 34 GLN HB3 H 2.26 . 1
375 . 34 GLN HG2 H 2.55 . 2
376 . 34 GLN HG3 H 2.45 . 2
377 . 34 GLN HE21 H 7.68 . 2
378 . 34 GLN HE22 H 6.89 . 2
379 . 34 GLN C C 174.38 . 1
380 . 34 GLN CA C 53.12 . 1
381 . 34 GLN CB C 28.21 . 1
382 . 34 GLN CG C 33.76 . 1
383 . 34 GLN CD C 180.46 . 1
384 . 34 GLN N N 121.09 . 1
385 . 34 GLN NE2 N 113.10 . 1
386 . 35 PRO HA H 3.93 . 1
387 . 35 PRO HB2 H 1.91 . 1
388 . 35 PRO HB3 H 2.31 . 1
389 . 35 PRO HG2 H 2.29 . 1
390 . 35 PRO HG3 H 2.03 . 1
391 . 35 PRO HD2 H 3.71 . 1
392 . 35 PRO HD3 H 3.98 . 1
393 . 35 PRO C C 177.38 . 1
394 . 35 PRO CA C 64.47 . 1
395 . 35 PRO CB C 31.87 . 1
396 . 35 PRO CG C 28.53 . 1
397 . 35 PRO CD C 50.94 . 1
398 . 36 GLY H H 8.95 . 1
399 . 36 GLY HA2 H 4.46 . 2
400 . 36 GLY HA3 H 3.59 . 2
401 . 36 GLY C C 174.69 . 1
402 . 36 GLY CA C 45.59 . 1
403 . 36 GLY N N 112.59 . 1
404 . 37 GLU H H 7.92 . 1
405 . 37 GLU HA H 4.74 . 1
406 . 37 GLU HB2 H 2.60 . 1
407 . 37 GLU HB3 H 2.11 . 1
408 . 37 GLU HG2 H 2.49 . 2
409 . 37 GLU HG3 H 2.31 . 2
410 . 37 GLU C C 176.66 . 1
411 . 37 GLU CA C 56.56 . 1
412 . 37 GLU CB C 33.02 . 1
413 . 37 GLU CG C 38.84 . 1
414 . 37 GLU CD C 184.83 . 1
415 . 37 GLU N N 119.19 . 1
416 . 38 THR H H 9.92 . 1
417 . 38 THR HA H 5.62 . 1
418 . 38 THR HB H 4.18 . 1
419 . 38 THR HG2 H 1.22 . 1
420 . 38 THR C C 174.58 . 1
421 . 38 THR CA C 59.09 . 1
422 . 38 THR CB C 72.81 . 1
423 . 38 THR CG2 C 21.85 . 1
424 . 38 THR N N 109.40 . 1
425 . 39 LEU H H 9.17 . 1
426 . 39 LEU HA H 5.20 . 1
427 . 39 LEU HB2 H 1.48 . 1
428 . 39 LEU HB3 H 1.60 . 1
429 . 39 LEU HG H 1.38 . 1
430 . 39 LEU HD1 H 0.86 . 1
431 . 39 LEU HD2 H 0.75 . 1
432 . 39 LEU C C 174.52 . 1
433 . 39 LEU CA C 52.66 . 1
434 . 39 LEU CB C 45.92 . 1
435 . 39 LEU CG C 27.97 . 1
436 . 39 LEU CD1 C 24.50 . 1
437 . 39 LEU CD2 C 26.96 . 1
438 . 39 LEU N N 121.91 . 1
439 . 40 LEU H H 9.01 . 1
440 . 40 LEU HA H 5.51 . 1
441 . 40 LEU HB2 H 1.37 . 1
442 . 40 LEU HB3 H 2.20 . 1
443 . 40 LEU HG H 1.57 . 1
444 . 40 LEU HD1 H 1.08 . 1
445 . 40 LEU HD2 H 1.12 . 1
446 . 40 LEU C C 174.50 . 1
447 . 40 LEU CA C 53.55 . 1
448 . 40 LEU CB C 44.44 . 1
449 . 40 LEU CG C 28.23 . 1
450 . 40 LEU CD1 C 25.40 . 1
451 . 40 LEU CD2 C 26.84 . 1
452 . 40 LEU N N 129.08 . 1
453 . 41 ILE H H 9.78 . 1
454 . 41 ILE HA H 5.15 . 1
455 . 41 ILE HB H 1.93 . 1
456 . 41 ILE HG12 H 1.69 . 1
457 . 41 ILE HG13 H 1.03 . 1
458 . 41 ILE HG2 H 0.89 . 1
459 . 41 ILE HD1 H 0.87 . 1
460 . 41 ILE C C 174.45 . 1
461 . 41 ILE CA C 60.49 . 1
462 . 41 ILE CB C 41.55 . 1
463 . 41 ILE CG1 C 28.80 . 1
464 . 41 ILE CG2 C 18.51 . 1
465 . 41 ILE CD1 C 17.45 . 1
466 . 41 ILE N N 126.96 . 1
467 . 42 ILE H H 8.33 . 1
468 . 42 ILE HA H 5.11 . 1
469 . 42 ILE HB H 1.85 . 1
470 . 42 ILE HG12 H 1.57 . 1
471 . 42 ILE HG13 H 1.07 . 1
472 . 42 ILE HG2 H 0.95 . 1
473 . 42 ILE HD1 H 0.83 . 1
474 . 42 ILE C C 174.96 . 1
475 . 42 ILE CA C 60.15 . 1
476 . 42 ILE CB C 40.34 . 1
477 . 42 ILE CG1 C 27.93 . 1
478 . 42 ILE CG2 C 18.45 . 1
479 . 42 ILE CD1 C 13.97 . 1
480 . 42 ILE N N 126.36 . 1
481 . 43 ALA H H 9.30 . 1
482 . 43 ALA HA H 4.61 . 1
483 . 43 ALA HB H 1.73 . 1
484 . 43 ALA C C 174.01 . 1
485 . 43 ALA CA C 51.58 . 1
486 . 43 ALA CB C 24.64 . 1
487 . 43 ALA N N 126.30 . 1
488 . 44 ASP H H 8.64 . 1
489 . 44 ASP HA H 4.64 . 1
490 . 44 ASP HB2 H 3.07 . 1
491 . 44 ASP HB3 H 2.45 . 1
492 . 44 ASP C C 174.66 . 1
493 . 44 ASP CA C 52.84 . 1
494 . 44 ASP CB C 40.49 . 1
495 . 44 ASP CG C 181.17 . 1
496 . 44 ASP N N 114.86 . 1
497 . 45 ASP H H 7.44 . 1
498 . 45 ASP HA H 5.10 . 1
499 . 45 ASP HB2 H 3.69 . 1
500 . 45 ASP HB3 H 3.03 . 1
501 . 45 ASP C C 176.68 . 1
502 . 45 ASP CA C 51.46 . 1
503 . 45 ASP CB C 43.49 . 1
504 . 45 ASP CG C 178.58 . 1
505 . 45 ASP N N 119.81 . 1
506 . 46 PRO HA H 4.55 . 1
507 . 46 PRO HB2 H 2.18 . 1
508 . 46 PRO HB3 H 2.65 . 1
509 . 46 PRO HG2 H 2.32 . 2
510 . 46 PRO HG3 H 2.92 . 2
511 . 46 PRO HD2 H 4.36 . 1
512 . 46 PRO HD3 H 4.54 . 1
513 . 46 PRO C C 177.99 . 1
514 . 46 PRO CA C 65.51 . 1
515 . 46 PRO CB C 32.38 . 1
516 . 46 PRO CG C 27.57 . 1
517 . 46 PRO CD C 52.34 . 1
518 . 47 ALA H H 8.41 . 1
519 . 47 ALA HA H 4.29 . 1
520 . 47 ALA HB H 1.71 . 1
521 . 47 ALA C C 180.76 . 1
522 . 47 ALA CA C 54.72 . 1
523 . 47 ALA CB C 17.90 . 1
524 . 47 ALA N N 119.72 . 1
525 . 48 THR H H 8.49 . 1
526 . 48 THR HA H 3.75 . 1
527 . 48 THR HB H 3.96 . 1
528 . 48 THR HG2 H 1.53 . 1
529 . 48 THR C C 175.60 . 1
530 . 48 THR CA C 66.15 . 1
531 . 48 THR CB C 70.24 . 1
532 . 48 THR CG2 C 23.16 . 1
533 . 48 THR N N 109.18 . 1
534 . 49 THR H H 7.39 . 1
535 . 49 THR HA H 4.20 . 1
536 . 49 THR HB H 4.26 . 1
537 . 49 THR HG2 H 0.95 . 1
538 . 49 THR C C 175.60 . 1
539 . 49 THR CA C 65.21 . 1
540 . 49 THR CB C 68.51 . 1
541 . 49 THR CG2 C 20.65 . 1
542 . 49 THR N N 111.61 . 1
543 . 50 ARG H H 6.99 . 1
544 . 50 ARG HA H 4.59 . 1
545 . 50 ARG HB2 H 1.89 . 1
546 . 50 ARG HB3 H 1.96 . 1
547 . 50 ARG HG2 H 1.75 . 2
548 . 50 ARG HG3 H 1.57 . 2
549 . 50 ARG HD2 H 3.27 . 1
550 . 50 ARG HD3 H 3.27 . 1
551 . 50 ARG C C 179.35 . 1
552 . 50 ARG CA C 57.06 . 1
553 . 50 ARG CB C 31.95 . 1
554 . 50 ARG CG C 27.21 . 1
555 . 50 ARG CD C 43.27 . 1
556 . 50 ARG N N 118.33 . 1
557 . 51 ASP H H 8.81 . 1
558 . 51 ASP HA H 4.48 . 1
559 . 51 ASP HB2 H 2.28 . 1
560 . 51 ASP HB3 H 2.63 . 1
561 . 51 ASP C C 179.22 . 1
562 . 51 ASP CA C 57.94 . 1
563 . 51 ASP CB C 41.06 . 1
564 . 51 ASP CG C 177.02 . 1
565 . 51 ASP N N 120.52 . 1
566 . 52 ILE H H 8.55 . 1
567 . 52 ILE HA H 4.11 . 1
568 . 52 ILE HB H 1.51 . 1
569 . 52 ILE HG12 H 0.85 . 1
570 . 52 ILE HG13 H 0.85 . 1
571 . 52 ILE HG2 H 0.46 . 1
572 . 52 ILE HD1 H 0.34 . 1
573 . 52 ILE C C 175.50 . 1
574 . 52 ILE CA C 65.38 . 1
575 . 52 ILE CB C 32.55 . 1
576 . 52 ILE CG1 C 28.96 . 1
577 . 52 ILE CG2 C 17.47 . 1
578 . 52 ILE CD1 C 10.25 . 1
579 . 52 ILE N N 117.02 . 1
580 . 53 PRO HA H 4.27 . 1
581 . 53 PRO HB2 H 1.89 . 1
582 . 53 PRO HB3 H 2.51 . 1
583 . 53 PRO HG2 H 2.47 . 1
584 . 53 PRO HG3 H 1.74 . 1
585 . 53 PRO HD2 H 3.30 . 1
586 . 53 PRO HD3 H 3.51 . 1
587 . 53 PRO C C 179.07 . 1
588 . 53 PRO CA C 66.74 . 1
589 . 53 PRO CB C 30.95 . 1
590 . 53 PRO CG C 28.79 . 1
591 . 53 PRO CD C 50.02 . 1
592 . 54 GLY H H 7.74 . 1
593 . 54 GLY HA2 H 3.82 . 1
594 . 54 GLY HA3 H 3.94 . 1
595 . 54 GLY C C 175.28 . 1
596 . 54 GLY CA C 47.50 . 1
597 . 54 GLY N N 102.91 . 1
598 . 55 PHE H H 8.02 . 1
599 . 55 PHE HA H 4.34 . 1
600 . 55 PHE HB2 H 3.30 . 1
601 . 55 PHE HB3 H 3.43 . 1
602 . 55 PHE HD1 H 7.27 . 1
603 . 55 PHE HD2 H 7.27 . 1
604 . 55 PHE HE1 H 7.18 . 1
605 . 55 PHE HE2 H 7.18 . 1
606 . 55 PHE HZ H 7.20 . 1
607 . 55 PHE C C 176.68 . 1
608 . 55 PHE CA C 61.33 . 1
609 . 55 PHE CB C 39.19 . 1
610 . 55 PHE CD1 C 131.87 . 1
611 . 55 PHE CD2 C 131.87 . 1
612 . 55 PHE CE1 C 131.49 . 1
613 . 55 PHE CE2 C 131.49 . 1
614 . 55 PHE CZ C 128.93 . 1
615 . 55 PHE N N 123.66 . 1
616 . 56 CYS H H 7.96 . 1
617 . 56 CYS HA H 3.76 . 1
618 . 56 CYS HB2 H 3.26 . 1
619 . 56 CYS HB3 H 3.07 . 1
620 . 56 CYS C C 176.61 . 1
621 . 56 CYS CA C 65.16 . 1
622 . 56 CYS CB C 26.17 . 1
623 . 56 CYS N N 116.45 . 1
624 . 57 THR H H 8.29 . 1
625 . 57 THR HA H 3.98 . 1
626 . 57 THR HB H 4.14 . 1
627 . 57 THR HG2 H 1.18 . 1
628 . 57 THR C C 176.83 . 1
629 . 57 THR CA C 66.16 . 1
630 . 57 THR CB C 68.95 . 1
631 . 57 THR CG2 C 21.95 . 1
632 . 57 THR N N 114.73 . 1
633 . 58 PHE H H 8.20 . 1
634 . 58 PHE HA H 4.37 . 1
635 . 58 PHE HB2 H 3.20 . 1
636 . 58 PHE HB3 H 3.04 . 1
637 . 58 PHE HD1 H 7.24 . 1
638 . 58 PHE HD2 H 7.24 . 1
639 . 58 PHE HE1 H 7.38 . 1
640 . 58 PHE HE2 H 7.38 . 1
641 . 58 PHE HZ H 7.33 . 1
642 . 58 PHE C C 176.97 . 1
643 . 58 PHE CA C 60.55 . 1
644 . 58 PHE CB C 39.56 . 1
645 . 58 PHE CD1 C 131.55 . 1
646 . 58 PHE CD2 C 131.55 . 1
647 . 58 PHE CE1 C 131.65 . 1
648 . 58 PHE CE2 C 131.65 . 1
649 . 58 PHE CZ C 129.98 . 1
650 . 58 PHE N N 120.36 . 1
651 . 59 MET H H 7.79 . 1
652 . 59 MET HA H 4.32 . 1
653 . 59 MET HB2 H 1.23 . 1
654 . 59 MET HB3 H 1.67 . 1
655 . 59 MET HG2 H 2.24 . 2
656 . 59 MET HG3 H 2.12 . 2
657 . 59 MET C C 174.14 . 1
658 . 59 MET CA C 53.53 . 1
659 . 59 MET CB C 30.84 . 1
660 . 59 MET CG C 32.68 . 1
661 . 59 MET N N 112.87 . 1
662 . 60 GLU H H 7.36 . 1
663 . 60 GLU HA H 3.75 . 1
664 . 60 GLU HB2 H 2.02 . 2
665 . 60 GLU HB3 H 1.99 . 2
666 . 60 GLU HG2 H 2.02 . 2
667 . 60 GLU HG3 H 1.95 . 2
668 . 60 GLU C C 175.53 . 1
669 . 60 GLU CA C 57.59 . 1
670 . 60 GLU CB C 26.44 . 1
671 . 60 GLU CG C 36.94 . 1
672 . 60 GLU CD C 185.05 . 1
673 . 60 GLU N N 113.48 . 1
674 . 61 HIS H H 8.04 . 1
675 . 61 HIS HA H 5.16 . 1
676 . 61 HIS HB2 H 2.49 . 1
677 . 61 HIS HB3 H 3.27 . 1
678 . 61 HIS HD2 H 6.28 . 1
679 . 61 HIS HE1 H 7.73 . 1
680 . 61 HIS C C 174.81 . 1
681 . 61 HIS CA C 54.59 . 1
682 . 61 HIS CB C 33.35 . 1
683 . 61 HIS CD2 C 116.59 . 1
684 . 61 HIS CE1 C 139.57 . 1
685 . 61 HIS N N 117.17 . 1
686 . 62 GLU H H 8.36 . 1
687 . 62 GLU HA H 4.43 . 1
688 . 62 GLU HB2 H 1.95 . 1
689 . 62 GLU HB3 H 2.06 . 1
690 . 62 GLU HG2 H 2.26 . 2
691 . 62 GLU HG3 H 1.93 . 2
692 . 62 GLU C C 175.50 . 1
693 . 62 GLU CA C 55.74 . 1
694 . 62 GLU CB C 32.51 . 1
695 . 62 GLU CG C 35.96 . 1
696 . 62 GLU CD C 183.26 . 1
697 . 62 GLU N N 120.83 . 1
698 . 63 LEU H H 8.95 . 1
699 . 63 LEU HA H 4.79 . 1
700 . 63 LEU HB2 H 1.65 . 1
701 . 63 LEU HB3 H 2.16 . 1
702 . 63 LEU HG H 1.57 . 1
703 . 63 LEU HD1 H 1.10 . 1
704 . 63 LEU HD2 H 1.04 . 1
705 . 63 LEU C C 175.52 . 1
706 . 63 LEU CA C 54.22 . 1
707 . 63 LEU CB C 40.10 . 1
708 . 63 LEU CG C 27.65 . 1
709 . 63 LEU CD1 C 24.80 . 1
710 . 63 LEU CD2 C 27.42 . 1
711 . 63 LEU N N 128.94 . 1
712 . 64 VAL H H 9.00 . 1
713 . 64 VAL HA H 3.68 . 1
714 . 64 VAL HB H 1.77 . 1
715 . 64 VAL HG1 H 0.88 . 1
716 . 64 VAL HG2 H 0.90 . 1
717 . 64 VAL C C 176.42 . 1
718 . 64 VAL CA C 65.24 . 1
719 . 64 VAL CB C 32.72 . 1
720 . 64 VAL CG1 C 22.33 . 1
721 . 64 VAL CG2 C 21.68 . 1
722 . 64 VAL N N 130.31 . 1
723 . 65 ALA H H 7.84 . 1
724 . 65 ALA HA H 4.62 . 1
725 . 65 ALA HB H 1.12 . 1
726 . 65 ALA C C 174.58 . 1
727 . 65 ALA CA C 51.56 . 1
728 . 65 ALA CB C 23.26 . 1
729 . 65 ALA N N 116.44 . 1
730 . 66 LYS H H 8.85 . 1
731 . 66 LYS HA H 5.36 . 1
732 . 66 LYS HB2 H 2.04 . 1
733 . 66 LYS HB3 H 1.83 . 1
734 . 66 LYS HG2 H 1.59 . 1
735 . 66 LYS HG3 H 1.43 . 1
736 . 66 LYS HD2 H 1.73 . 1
737 . 66 LYS HD3 H 1.73 . 1
738 . 66 LYS HE2 H 3.11 . 1
739 . 66 LYS HE3 H 3.11 . 1
740 . 66 LYS C C 173.76 . 1
741 . 66 LYS CA C 55.07 . 1
742 . 66 LYS CB C 36.50 . 1
743 . 66 LYS CG C 23.51 . 1
744 . 66 LYS CD C 29.80 . 1
745 . 66 LYS CE C 42.39 . 1
746 . 66 LYS N N 116.19 . 1
747 . 67 GLU H H 9.12 . 1
748 . 67 GLU HA H 4.73 . 1
749 . 67 GLU HB2 H 1.88 . 1
750 . 67 GLU HB3 H 2.11 . 1
751 . 67 GLU HG2 H 2.32 . 2
752 . 67 GLU HG3 H 2.25 . 2
753 . 67 GLU C C 176.20 . 1
754 . 67 GLU CA C 56.18 . 1
755 . 67 GLU CB C 32.51 . 1
756 . 67 GLU CG C 36.67 . 1
757 . 67 GLU CD C 183.85 . 1
758 . 67 GLU N N 123.72 . 1
759 . 68 THR H H 8.80 . 1
760 . 68 THR HA H 4.87 . 1
761 . 68 THR HB H 4.48 . 1
762 . 68 THR HG2 H 0.94 . 1
763 . 68 THR C C 173.70 . 1
764 . 68 THR CA C 60.14 . 1
765 . 68 THR CB C 69.19 . 1
766 . 68 THR CG2 C 22.08 . 1
767 . 69 ASP H H 8.44 . 1
768 . 69 ASP HA H 4.79 . 1
769 . 69 ASP HB2 H 2.73 . 1
770 . 69 ASP HB3 H 2.83 . 1
771 . 69 ASP C C 175.55 . 1
772 . 69 ASP CA C 55.37 . 1
773 . 69 ASP CB C 41.12 . 1
774 . 69 ASP CG C 181.05 . 1
775 . 69 ASP N N 122.28 . 1
776 . 70 GLY H H 7.80 . 1
777 . 70 GLY HA2 H 4.08 . 1
778 . 70 GLY HA3 H 3.81 . 1
779 . 70 GLY C C 170.66 . 1
780 . 70 GLY CA C 44.18 . 1
781 . 70 GLY N N 108.46 . 1
782 . 71 LEU H H 7.84 . 1
783 . 71 LEU HA H 4.00 . 1
784 . 71 LEU HB2 H 1.18 . 1
785 . 71 LEU HB3 H 1.53 . 1
786 . 71 LEU HG H 1.40 . 1
787 . 71 LEU HD1 H 0.83 . 1
788 . 71 LEU HD2 H 0.34 . 1
789 . 71 LEU C C 175.50 . 1
790 . 71 LEU CA C 52.46 . 1
791 . 71 LEU CB C 43.54 . 1
792 . 71 LEU CG C 27.15 . 1
793 . 71 LEU CD1 C 25.46 . 1
794 . 71 LEU CD2 C 23.49 . 1
795 . 71 LEU N N 116.99 . 1
796 . 72 PRO HA H 4.05 . 1
797 . 72 PRO HB2 H 2.01 . 1
798 . 72 PRO HB3 H 2.22 . 1
799 . 72 PRO HG2 H 1.89 . 2
800 . 72 PRO HG3 H 1.69 . 2
801 . 72 PRO HD2 H 3.60 . 2
802 . 72 PRO HD3 H 3.30 . 2
803 . 72 PRO C C 175.18 . 1
804 . 72 PRO CA C 62.50 . 1
805 . 72 PRO CB C 34.06 . 1
806 . 72 PRO CG C 24.17 . 1
807 . 72 PRO CD C 50.01 . 1
808 . 73 TYR H H 8.32 . 1
809 . 73 TYR HA H 4.95 . 1
810 . 73 TYR HB2 H 2.62 . 1
811 . 73 TYR HB3 H 2.95 . 1
812 . 73 TYR HD1 H 6.80 . 1
813 . 73 TYR HD2 H 6.80 . 1
814 . 73 TYR HE1 H 6.43 . 1
815 . 73 TYR HE2 H 6.43 . 1
816 . 73 TYR C C 176.17 . 1
817 . 73 TYR CA C 55.97 . 1
818 . 73 TYR CB C 39.26 . 1
819 . 73 TYR CD1 C 132.09 . 1
820 . 73 TYR CD2 C 132.09 . 1
821 . 73 TYR CE1 C 118.37 . 1
822 . 73 TYR CE2 C 118.37 . 1
823 . 73 TYR N N 120.31 . 1
824 . 74 ARG H H 7.97 . 1
825 . 74 ARG HA H 5.59 . 1
826 . 74 ARG HB2 H 1.27 . 1
827 . 74 ARG HB3 H 1.05 . 1
828 . 74 ARG HG2 H 1.47 . 1
829 . 74 ARG HG3 H 1.59 . 1
830 . 74 ARG HD2 H 2.99 . 2
831 . 74 ARG HD3 H 2.63 . 2
832 . 74 ARG C C 174.59 . 1
833 . 74 ARG CA C 54.74 . 1
834 . 74 ARG CB C 35.33 . 1
835 . 74 ARG CG C 27.34 . 1
836 . 74 ARG CD C 43.90 . 1
837 . 74 ARG N N 117.27 . 1
838 . 75 TYR H H 8.84 . 1
839 . 75 TYR HA H 5.09 . 1
840 . 75 TYR HB2 H 2.91 . 1
841 . 75 TYR HB3 H 2.83 . 1
842 . 75 TYR HD1 H 6.89 . 1
843 . 75 TYR HD2 H 6.89 . 1
844 . 75 TYR HE1 H 6.44 . 1
845 . 75 TYR HE2 H 6.44 . 1
846 . 75 TYR C C 173.29 . 1
847 . 75 TYR CA C 56.25 . 1
848 . 75 TYR CB C 42.32 . 1
849 . 75 TYR CD1 C 133.30 . 1
850 . 75 TYR CD2 C 133.30 . 1
851 . 75 TYR CE1 C 117.08 . 1
852 . 75 TYR CE2 C 117.08 . 1
853 . 75 TYR N N 117.08 . 1
854 . 76 LEU H H 9.18 . 1
855 . 76 LEU HA H 5.75 . 1
856 . 76 LEU HB2 H 1.21 . 1
857 . 76 LEU HB3 H 1.94 . 1
858 . 76 LEU HG H 1.29 . 1
859 . 76 LEU HD1 H 0.98 . 1
860 . 76 LEU HD2 H 0.77 . 1
861 . 76 LEU C C 175.17 . 1
862 . 76 LEU CA C 53.42 . 1
863 . 76 LEU CB C 45.64 . 1
864 . 76 LEU CG C 27.98 . 1
865 . 76 LEU CD1 C 24.50 . 1
866 . 76 LEU CD2 C 26.49 . 1
867 . 76 LEU N N 125.85 . 1
868 . 77 ILE H H 9.37 . 1
869 . 77 ILE HA H 5.44 . 1
870 . 77 ILE HB H 1.81 . 1
871 . 77 ILE HG12 H 1.14 . 1
872 . 77 ILE HG13 H 1.50 . 1
873 . 77 ILE HG2 H 0.79 . 1
874 . 77 ILE HD1 H 0.69 . 1
875 . 77 ILE C C 174.04 . 1
876 . 77 ILE CA C 59.01 . 1
877 . 77 ILE CB C 41.72 . 1
878 . 77 ILE CG1 C 27.46 . 1
879 . 77 ILE CG2 C 17.46 . 1
880 . 77 ILE CD1 C 14.91 . 1
881 . 77 ILE N N 124.44 . 1
882 . 78 ARG H H 9.51 . 1
883 . 78 ARG HA H 5.16 . 1
884 . 78 ARG HB2 H 1.87 . 2
885 . 78 ARG HB3 H 1.35 . 2
886 . 78 ARG HG2 H 1.38 . 1
887 . 78 ARG HG3 H 1.38 . 1
888 . 78 ARG HD2 H 3.25 . 1
889 . 78 ARG HD3 H 3.25 . 1
890 . 78 ARG C C 175.85 . 1
891 . 78 ARG CA C 54.08 . 1
892 . 78 ARG CB C 33.80 . 1
893 . 78 ARG CG C 26.90 . 1
894 . 78 ARG CD C 43.41 . 1
895 . 78 ARG N N 125.21 . 1
896 . 79 LYS H H 8.53 . 1
897 . 79 LYS HA H 4.25 . 1
898 . 79 LYS HB2 H 2.12 . 2
899 . 79 LYS HB3 H 1.41 . 2
900 . 79 LYS HG2 H 1.82 . 2
901 . 79 LYS HG3 H 1.25 . 2
902 . 79 LYS HD2 H 1.70 . 2
903 . 79 LYS HD3 H 1.25 . 2
904 . 79 LYS HE2 H 3.02 . 2
905 . 79 LYS HE3 H 2.93 . 2
906 . 79 LYS C C 177.69 . 1
907 . 79 LYS CA C 57.30 . 1
908 . 79 LYS CB C 33.03 . 1
909 . 79 LYS CG C 26.50 . 1
910 . 79 LYS CD C 29.90 . 1
911 . 79 LYS CE C 42.71 . 1
912 . 79 LYS N N 127.64 . 1
913 . 80 GLY HA2 H 4.36 . 2
914 . 80 GLY HA3 H 4.14 . 2
915 . 80 GLY C C 173.13 . 1
916 . 80 GLY CA C 45.39 . 1
917 . 81 GLY H H 7.88 . 1
918 . 81 GLY HA2 H 3.96 . 2
919 . 81 GLY HA3 H 3.73 . 2
920 . 81 GLY C C 179.21 . 1
921 . 81 GLY CA C 45.98 . 1
922 . 81 GLY N N 113.09 . 1
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