data_4486
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
METHANE MONOOXYGENASE COMPONENT B
;
_BMRB_accession_number 4486
_BMRB_flat_file_name bmr4486.str
_Entry_type original
_Submission_date 1999-03-11
_Accession_date 1999-12-06
_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 CHANG S. L. .
2 WAllAR B. J. .
3 LIPSCOMB J. D. .
4 MAYO K. H. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 536
"13C chemical shifts" 335
"15N chemical shifts" 121
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2013-07-30 update BMRB 'change shift from 92 GLY C to CA 47.91'
2000-06-17 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
SOLUTION STRUCTURE OF COMPONENT B FROM METHANE MONOOXYGENASE DERIVED THROUGH
HETERONUCLEAR NMR AND MOLECULAR MODELING"
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 992499790
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 CHANG S. L. .
2 WAllAR B. J. .
3 LIPSCOMB J. D. .
4 MAYO K. H. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 38
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 5799
_Page_last 5812
_Year 1999
_Details .
loop_
_Keyword
OXIDOREDUCTASE
MONOOXYGENASE
'METHANE OXIDATION'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_MMO_B
_Saveframe_category molecular_system
_Mol_system_name 'METHANE MONOOXYGENASE REGULATORY PROTEIN B'
_Abbreviation_common 'MMO B'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'MMO B' $MMO_B
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_MMO_B
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'METHANE MONOOXYGENASE REGULATORY PROTEIN B'
_Abbreviation_common 'MMO B'
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 138
_Mol_residue_sequence
;
MSSAHNAYNAGIMQKTGKAF
ADEFFAEENQVVHESNAVVL
VLMKSDEIDAIIEDIVLKGG
KAKNPSIVVEDKAGFWWIKA
DGAIEIDAAEAGELLGKPFS
VYDLLINVSSTVGRAYTLGT
KFTITSELMGLDRALTDI
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 SER 3 SER 4 ALA 5 HIS
6 ASN 7 ALA 8 TYR 9 ASN 10 ALA
11 GLY 12 ILE 13 MET 14 GLN 15 LYS
16 THR 17 GLY 18 LYS 19 ALA 20 PHE
21 ALA 22 ASP 23 GLU 24 PHE 25 PHE
26 ALA 27 GLU 28 GLU 29 ASN 30 GLN
31 VAL 32 VAL 33 HIS 34 GLU 35 SER
36 ASN 37 ALA 38 VAL 39 VAL 40 LEU
41 VAL 42 LEU 43 MET 44 LYS 45 SER
46 ASP 47 GLU 48 ILE 49 ASP 50 ALA
51 ILE 52 ILE 53 GLU 54 ASP 55 ILE
56 VAL 57 LEU 58 LYS 59 GLY 60 GLY
61 LYS 62 ALA 63 LYS 64 ASN 65 PRO
66 SER 67 ILE 68 VAL 69 VAL 70 GLU
71 ASP 72 LYS 73 ALA 74 GLY 75 PHE
76 TRP 77 TRP 78 ILE 79 LYS 80 ALA
81 ASP 82 GLY 83 ALA 84 ILE 85 GLU
86 ILE 87 ASP 88 ALA 89 ALA 90 GLU
91 ALA 92 GLY 93 GLU 94 LEU 95 LEU
96 GLY 97 LYS 98 PRO 99 PHE 100 SER
101 VAL 102 TYR 103 ASP 104 LEU 105 LEU
106 ILE 107 ASN 108 VAL 109 SER 110 SER
111 THR 112 VAL 113 GLY 114 ARG 115 ALA
116 TYR 117 THR 118 LEU 119 GLY 120 THR
121 LYS 122 PHE 123 THR 124 ILE 125 THR
126 SER 127 GLU 128 LEU 129 MET 130 GLY
131 LEU 132 ASP 133 ARG 134 ALA 135 LEU
136 THR 137 ASP 138 ILE
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-07-14
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 2MOB "Methane Monooxygenase Component B" 100.00 138 100.00 100.00 4.46e-93
EMBL CAA39070 "Protein B of soluble methane monooxygenase (sMMO) [Methylosinus trichosporium OB3b]" 100.00 138 100.00 100.00 4.46e-93
GB AAZ81970 "protein B of soluble methane monooxygenase [Methylosinus trichosporium]" 100.00 138 99.28 100.00 1.23e-92
GB AAZ81976 "protein B of soluble methane monooxygenase [Methylomonas sp. GYJ3]" 100.00 138 100.00 100.00 4.46e-93
GB ABD46894 "MmoB [Methylosinus sporium]" 100.00 138 97.10 99.28 4.19e-91
REF WP_003609343 "methane monooxygenase regulatory protein B [Methylosinus trichosporium]" 100.00 138 100.00 100.00 4.46e-93
SP P27356 "RecName: Full=Methane monooxygenase regulatory protein B" 100.00 138 100.00 100.00 4.46e-93
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$MMO_B . 426 Eubacteria . Methylosinus trichosporium
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
$MMO_B 'recombinant technology' 'Escherichia coli' Escherichia coli . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$MMO_B . mM .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityPlus
_Field_strength 800
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityPlus
_Field_strength 600
_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 6.8 . n/a
temperature 313 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_one
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
. H 1 . ppm . . . . . .
. C 13 . ppm . . . . . .
. N 15 . ppm . . . . . .
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_chem_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_one
_Mol_system_component_name 'MMO B'
_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 . 2 SER H H 7.19 . 1
2 . 2 SER HA H 4.72 . 1
3 . 2 SER HB2 H 3.09 . 2
4 . 2 SER N N 122.66 . 1
5 . 3 SER H H 7.24 . 1
6 . 3 SER HA H 4.72 . 1
7 . 3 SER HB2 H 3.09 . 2
8 . 3 SER N N 122.32 . 1
9 . 4 ALA HA H 4.26 . 1
10 . 4 ALA HB H 0.98 . 1
11 . 4 ALA CA C 61.46 . 1
12 . 4 ALA CB C 17.46 . 1
13 . 5 HIS H H 8.33 . 1
14 . 5 HIS HB2 H 2.11 . 2
15 . 5 HIS CA C 55.82 . 1
16 . 5 HIS CB C 32.83 . 1
17 . 5 HIS N N 122.77 . 1
18 . 7 ALA HB H 1.36 . 1
19 . 7 ALA CA C 52.68 . 1
20 . 7 ALA CB C 19.33 . 1
21 . 8 TYR H H 8.07 . 1
22 . 8 TYR HA H 4.72 . 1
23 . 8 TYR HB2 H 3.18 . 2
24 . 8 TYR CA C 57.83 . 1
25 . 8 TYR CB C 39.67 . 1
26 . 8 TYR N N 118.28 . 1
27 . 10 ALA CA C 53.16 . 1
28 . 10 ALA CB C 19.08 . 1
29 . 11 GLY H H 8.30 . 1
30 . 11 GLY HA2 H 4.02 . 2
31 . 11 GLY CA C 45.63 . 1
32 . 11 GLY N N 106.72 . 1
33 . 12 ILE H H 7.84 . 1
34 . 12 ILE HA H 4.26 . 1
35 . 12 ILE HB H 2.00 . 1
36 . 12 ILE HG12 H 1.00 . 2
37 . 12 ILE CA C 61.46 . 1
38 . 12 ILE CB C 38.65 . 1
39 . 12 ILE N N 119.07 . 1
40 . 15 LYS HA H 4.45 . 1
41 . 15 LYS HB2 H 1.89 . 2
42 . 15 LYS CA C 56.70 . 1
43 . 15 LYS CB C 33.25 . 1
44 . 15 LYS CG C 24.82 . 1
45 . 16 THR H H 8.13 . 1
46 . 16 THR HA H 4.72 . 1
47 . 16 THR CA C 62.11 . 1
48 . 16 THR N N 113.68 . 1
49 . 17 GLY H H 8.35 . 1
50 . 17 GLY HA2 H 4.73 . 2
51 . 17 GLY HA3 H 3.91 . 2
52 . 17 GLY N N 110.92 . 1
53 . 19 ALA HB H 1.45 . 1
54 . 19 ALA CA C 52.79 . 1
55 . 19 ALA CB C 19.41 . 1
56 . 20 PHE H H 8.16 . 1
57 . 20 PHE HA H 4.65 . 1
58 . 20 PHE HB2 H 2.76 . 2
59 . 20 PHE CA C 54.88 . 1
60 . 20 PHE CB C 41.25 . 1
61 . 20 PHE N N 118.55 . 1
62 . 21 ALA H H 8.26 . 1
63 . 21 ALA HA H 4.28 . 1
64 . 21 ALA HB H 1.94 . 1
65 . 21 ALA CA C 54.90 . 1
66 . 21 ALA N N 119.87 . 1
67 . 23 GLU HA H 4.25 . 1
68 . 23 GLU HB2 H 2.14 . 2
69 . 23 GLU CA C 57.14 . 1
70 . 23 GLU CB C 30.27 . 1
71 . 23 GLU CG C 36.13 . 1
72 . 24 PHE H H 8.13 . 1
73 . 24 PHE HB2 H 2.99 . 2
74 . 24 PHE CA C 58.12 . 1
75 . 24 PHE CB C 39.78 . 1
76 . 24 PHE N N 119.85 . 1
77 . 25 PHE H H 8.01 . 1
78 . 25 PHE HB2 H 3.12 . 2
79 . 25 PHE CA C 57.70 . 1
80 . 25 PHE CB C 39.66 . 1
81 . 25 PHE N N 120.73 . 1
82 . 26 ALA H H 8.03 . 1
83 . 26 ALA HA H 4.35 . 1
84 . 26 ALA HB H 1.45 . 1
85 . 26 ALA CA C 52.63 . 1
86 . 26 ALA CB C 19.55 . 1
87 . 26 ALA N N 124.98 . 1
88 . 27 GLU H H 8.29 . 1
89 . 27 GLU HA H 4.28 . 1
90 . 27 GLU HB2 H 2.07 . 2
91 . 27 GLU HG2 H 2.36 . 2
92 . 27 GLU CA C 57.05 . 1
93 . 27 GLU CB C 30.53 . 1
94 . 27 GLU CG C 36.36 . 1
95 . 27 GLU N N 119.78 . 1
96 . 28 GLU H H 8.49 . 1
97 . 28 GLU HA H 4.32 . 1
98 . 28 GLU HB2 H 2.06 . 2
99 . 28 GLU CA C 57.10 . 1
100 . 28 GLU CB C 30.27 . 1
101 . 28 GLU CG C 36.17 . 1
102 . 28 GLU N N 120.69 . 1
103 . 29 ASN H H 8.36 . 1
104 . 29 ASN HA H 4.72 . 1
105 . 29 ASN HB2 H 3.22 . 2
106 . 29 ASN HB3 H 2.85 . 2
107 . 29 ASN CA C 53.46 . 1
108 . 29 ASN CB C 39.05 . 1
109 . 29 ASN N N 118.44 . 1
110 . 30 GLN HA H 4.41 . 1
111 . 30 GLN HG2 H 2.40 . 2
112 . 30 GLN CA C 56.12 . 1
113 . 30 GLN CB C 29.48 . 1
114 . 30 GLN CG C 33.77 . 1
115 . 31 VAL H H 8.08 . 1
116 . 31 VAL HA H 4.15 . 1
117 . 31 VAL HB H 2.10 . 1
118 . 31 VAL HG1 H 0.95 . 2
119 . 31 VAL CA C 62.42 . 1
120 . 31 VAL CB C 32.94 . 1
121 . 31 VAL CG1 C 20.87 . 2
122 . 31 VAL N N 120.80 . 1
123 . 32 VAL H H 8.14 . 1
124 . 32 VAL HA H 4.16 . 1
125 . 32 VAL HB H 2.12 . 1
126 . 32 VAL HG1 H 1.41 . 2
127 . 32 VAL HG2 H 0.98 . 2
128 . 32 VAL CA C 62.23 . 1
129 . 32 VAL CB C 32.82 . 1
130 . 32 VAL CG1 C 20.59 . 2
131 . 32 VAL N N 123.41 . 1
132 . 33 HIS H H 8.45 . 1
133 . 33 HIS HA H 4.73 . 1
134 . 33 HIS HB2 H 3.25 . 2
135 . 33 HIS HB3 H 3.15 . 2
136 . 33 HIS CA C 55.90 . 1
137 . 33 HIS CB C 30.63 . 1
138 . 33 HIS N N 123.12 . 1
139 . 34 GLU H H 8.56 . 1
140 . 34 GLU HA H 4.39 . 1
141 . 34 GLU HG2 H 2.33 . 2
142 . 34 GLU CA C 56.59 . 1
143 . 34 GLU CB C 30.50 . 1
144 . 34 GLU N N 122.27 . 1
145 . 35 SER H H 8.47 . 1
146 . 35 SER HA H 4.52 . 1
147 . 35 SER HB2 H 4.00 . 2
148 . 35 SER CA C 58.86 . 1
149 . 35 SER CB C 63.88 . 1
150 . 35 SER N N 116.25 . 1
151 . 36 ASN H H 8.68 . 1
152 . 36 ASN HA H 5.03 . 1
153 . 36 ASN HB2 H 2.98 . 2
154 . 36 ASN HB3 H 2.81 . 2
155 . 36 ASN CA C 52.64 . 1
156 . 36 ASN CB C 39.25 . 1
157 . 36 ASN N N 120.73 . 1
158 . 37 ALA H H 7.77 . 1
159 . 37 ALA HA H 4.94 . 1
160 . 37 ALA HB H 1.46 . 1
161 . 37 ALA CA C 52.64 . 1
162 . 37 ALA CB C 20.34 . 1
163 . 37 ALA N N 123.05 . 1
164 . 38 VAL H H 8.81 . 1
165 . 38 VAL HA H 4.73 . 1
166 . 38 VAL HB H 2.12 . 1
167 . 38 VAL HG1 H 0.82 . 2
168 . 38 VAL HG2 H 0.67 . 2
169 . 38 VAL CA C 59.45 . 1
170 . 38 VAL CB C 34.95 . 1
171 . 38 VAL CG1 C 22.96 . 2
172 . 38 VAL CG2 C 18.80 . 2
173 . 38 VAL N N 114.46 . 1
174 . 39 VAL H H 8.47 . 1
175 . 39 VAL HA H 5.20 . 1
176 . 39 VAL HB H 1.77 . 1
177 . 39 VAL HG1 H 0.92 . 2
178 . 39 VAL HG2 H 0.82 . 2
179 . 39 VAL CA C 60.63 . 2
180 . 39 VAL CB C 36.46 . 2
181 . 39 VAL N N 119.56 . 1
182 . 40 LEU H H 9.36 . 1
183 . 40 LEU HA H 4.81 . 1
184 . 40 LEU HB2 H 1.87 . 2
185 . 40 LEU HB3 H 1.35 . 2
186 . 40 LEU HG H 1.55 . 1
187 . 40 LEU HD1 H 1.14 . 2
188 . 40 LEU HD2 H 0.92 . 2
189 . 40 LEU CA C 53.39 . 1
190 . 40 LEU CB C 46.39 . 1
191 . 40 LEU N N 127.57 . 1
192 . 41 VAL H H 8.37 . 1
193 . 41 VAL HA H 5.22 . 1
194 . 41 VAL HB H 1.69 . 1
195 . 41 VAL HG1 H 0.16 . 2
196 . 41 VAL HG2 H 0.00 . 2
197 . 41 VAL CA C 60.86 . 1
198 . 41 VAL CB C 32.11 . 1
199 . 41 VAL CG1 C 20.35 . 1
200 . 41 VAL CG2 C 20.35 . 1
201 . 41 VAL N N 126.28 . 1
202 . 42 LEU H H 9.39 . 1
203 . 42 LEU HA H 5.50 . 1
204 . 42 LEU HB2 H 1.84 . 2
205 . 42 LEU HG H 1.66 . 1
206 . 42 LEU HD1 H 0.87 . 2
207 . 42 LEU CA C 52.81 . 1
208 . 42 LEU CB C 47.14 . 1
209 . 42 LEU CG C 26.18 . 1
210 . 42 LEU N N 126.93 . 1
211 . 43 MET H H 9.09 . 1
212 . 43 MET HA H 4.36 . 1
213 . 43 MET HG2 H 2.76 . 2
214 . 43 MET HG3 H 2.25 . 2
215 . 43 MET CA C 56.79 . 1
216 . 43 MET CB C 34.07 . 1
217 . 43 MET CG C 32.81 . 1
218 . 43 MET N N 121.79 . 1
219 . 44 LYS H H 7.48 . 1
220 . 44 LYS HA H 4.26 . 1
221 . 44 LYS HB2 H 2.12 . 2
222 . 44 LYS HG2 H 0.63 . 2
223 . 44 LYS HD2 H 1.14 . 2
224 . 44 LYS HD3 H 1.05 . 2
225 . 44 LYS HE2 H 1.38 . 2
226 . 44 LYS CA C 58.41 . 1
227 . 44 LYS CB C 33.39 . 1
228 . 44 LYS CG C 24.79 . 1
229 . 44 LYS CD C 29.19 . 1
230 . 44 LYS N N 119.26 . 1
231 . 45 SER H H 7.86 . 1
232 . 45 SER HA H 4.69 . 1
233 . 45 SER HB2 H 4.35 . 2
234 . 45 SER CA C 57.55 . 1
235 . 45 SER CB C 65.88 . 1
236 . 45 SER N N 114.03 . 1
237 . 46 ASP H H 9.10 . 1
238 . 46 ASP HA H 4.43 . 1
239 . 46 ASP HB2 H 2.77 . 2
240 . 46 ASP HB3 H 2.69 . 2
241 . 46 ASP CA C 58.43 . 1
242 . 46 ASP CB C 40.00 . 1
243 . 46 ASP N N 120.67 . 1
244 . 47 GLU H H 8.70 . 1
245 . 47 GLU HA H 4.05 . 1
246 . 47 GLU HB2 H 2.17 . 2
247 . 47 GLU HB3 H 1.75 . 2
248 . 47 GLU HG2 H 2.59 . 2
249 . 47 GLU HG3 H 2.53 . 2
250 . 47 GLU CA C 60.25 . 1
251 . 47 GLU CB C 29.55 . 1
252 . 47 GLU CG C 37.53 . 1
253 . 47 GLU N N 117.40 . 1
254 . 48 ILE H H 7.79 . 1
255 . 48 ILE HA H 3.72 . 1
256 . 48 ILE HB H 2.50 . 1
257 . 48 ILE HG12 H 1.77 . 2
258 . 48 ILE HG13 H 1.72 . 2
259 . 48 ILE HG2 H 1.22 . 1
260 . 48 ILE HD1 H 0.96 . 1
261 . 48 ILE CA C 62.25 . 1
262 . 48 ILE CB C 36.00 . 1
263 . 48 ILE CG1 C 28.69 . 1
264 . 48 ILE CG2 C 19.45 . 1
265 . 48 ILE CD1 C 9.85 . 1
266 . 48 ILE N N 119.05 . 1
267 . 49 ASP H H 9.41 . 1
268 . 49 ASP HA H 4.34 . 1
269 . 49 ASP HB2 H 2.99 . 2
270 . 49 ASP CA C 57.87 . 1
271 . 49 ASP CB C 39.74 . 1
272 . 49 ASP N N 120.95 . 1
273 . 50 ALA H H 7.13 . 1
274 . 50 ALA HA H 4.26 . 1
275 . 50 ALA HB H 1.55 . 1
276 . 50 ALA CA C 54.92 . 1
277 . 50 ALA CB C 18.29 . 1
278 . 50 ALA N N 120.60 . 1
279 . 51 ILE H H 7.68 . 1
280 . 51 ILE HA H 3.44 . 1
281 . 51 ILE HB H 2.14 . 1
282 . 51 ILE HG12 H 0.64 . 2
283 . 51 ILE HG2 H 0.75 . 1
284 . 51 ILE HD1 H 0.41 . 1
285 . 51 ILE CA C 65.04 . 1
286 . 51 ILE CB C 38.28 . 1
287 . 51 ILE CG1 C 29.19 . 1
288 . 51 ILE CG2 C 16.22 . 1
289 . 51 ILE CD1 C 14.85 . 1
290 . 51 ILE N N 118.47 . 1
291 . 52 ILE H H 8.66 . 1
292 . 52 ILE HA H 3.40 . 1
293 . 52 ILE HB H 1.55 . 1
294 . 52 ILE HG12 H 1.18 . 2
295 . 52 ILE HG13 H -0.30 . 2
296 . 52 ILE HG2 H -0.13 . 1
297 . 52 ILE HD1 H 0.26 . 1
298 . 52 ILE CA C 62.52 . 1
299 . 52 ILE CB C 34.82 . 1
300 . 52 ILE CG1 C 25.43 . 1
301 . 52 ILE CG2 C 16.37 . 1
302 . 52 ILE CD1 C 9.13 . 1
303 . 52 ILE N N 122.37 . 1
304 . 53 GLU H H 7.63 . 1
305 . 53 GLU HA H 3.92 . 1
306 . 53 GLU HB2 H 2.09 . 2
307 . 53 GLU HB3 H 1.99 . 2
308 . 53 GLU HG2 H 2.34 . 2
309 . 53 GLU HG3 H 2.31 . 2
310 . 53 GLU CA C 59.69 . 1
311 . 53 GLU CB C 29.98 . 1
312 . 53 GLU CG C 35.70 . 1
313 . 53 GLU N N 116.07 . 1
314 . 54 ASP H H 8.34 . 1
315 . 54 ASP HA H 4.99 . 1
316 . 54 ASP HB2 H 2.73 . 2
317 . 54 ASP CA C 55.44 . 1
318 . 54 ASP CB C 43.20 . 1
319 . 54 ASP N N 112.42 . 1
320 . 55 ILE H H 7.87 . 1
321 . 55 ILE HA H 4.47 . 1
322 . 55 ILE HB H 2.39 . 1
323 . 55 ILE HG12 H 1.52 . 2
324 . 55 ILE HG13 H 1.19 . 2
325 . 55 ILE HG2 H 1.00 . 1
326 . 55 ILE HD1 H 0.83 . 1
327 . 55 ILE CA C 63.87 . 1
328 . 55 ILE CB C 38.39 . 1
329 . 55 ILE CG1 C 27.80 . 1
330 . 55 ILE CG2 C 16.73 . 1
331 . 55 ILE CD1 C 13.09 . 1
332 . 55 ILE N N 117.74 . 1
333 . 56 VAL H H 8.45 . 1
334 . 56 VAL HA H 3.70 . 1
335 . 56 VAL HB H 2.50 . 1
336 . 56 VAL HG1 H 0.93 . 2
337 . 56 VAL HG2 H 0.88 . 2
338 . 56 VAL CA C 67.55 . 1
339 . 56 VAL CB C 30.96 . 1
340 . 56 VAL CG1 C 21.36 . 2
341 . 56 VAL N N 121.69 . 1
342 . 57 LEU H H 8.13 . 1
343 . 57 LEU HA H 4.23 . 1
344 . 57 LEU HB2 H 2.07 . 2
345 . 57 LEU HG H 1.69 . 1
346 . 57 LEU HD1 H 0.91 . 2
347 . 57 LEU CA C 55.98 . 1
348 . 57 LEU CB C 41.68 . 1
349 . 57 LEU CG C 25.64 . 1
350 . 57 LEU N N 113.05 . 1
351 . 58 LYS H H 6.85 . 1
352 . 58 LYS HA H 4.62 . 1
353 . 58 LYS HB2 H 1.81 . 2
354 . 58 LYS HG2 H 1.47 . 2
355 . 58 LYS CA C 56.51 . 1
356 . 58 LYS CB C 32.68 . 1
357 . 58 LYS CG C 25.15 . 1
358 . 58 LYS CD C 29.24 . 1
359 . 58 LYS N N 117.64 . 1
360 . 59 GLY H H 8.59 . 1
361 . 59 GLY HA2 H 4.73 . 2
362 . 59 GLY HA3 H 4.06 . 2
363 . 59 GLY CA C 47.21 . 1
364 . 59 GLY N N 111.49 . 1
365 . 60 GLY H H 8.79 . 1
366 . 60 GLY HA2 H 4.05 . 1
367 . 60 GLY CA C 47.83 . 1
368 . 60 GLY N N 110.10 . 1
369 . 61 LYS H H 7.51 . 1
370 . 61 LYS HA H 4.73 . 1
371 . 61 LYS HB2 H 1.80 . 2
372 . 61 LYS HE2 H 4.43 . 2
373 . 61 LYS CA C 56.88 . 1
374 . 61 LYS CB C 33.08 . 1
375 . 61 LYS CG C 25.65 . 1
376 . 61 LYS CD C 29.88 . 1
377 . 61 LYS N N 123.81 . 1
378 . 62 ALA H H 7.75 . 1
379 . 62 ALA HA H 4.26 . 1
380 . 62 ALA HB H 1.57 . 1
381 . 62 ALA CA C 54.41 . 1
382 . 62 ALA CB C 18.17 . 1
383 . 62 ALA N N 120.05 . 1
384 . 63 LYS H H 7.42 . 1
385 . 63 LYS HA H 4.73 . 1
386 . 63 LYS HB2 H 1.67 . 2
387 . 63 LYS HG2 H 2.01 . 2
388 . 63 LYS HE2 H 4.36 . 2
389 . 63 LYS CA C 57.68 . 1
390 . 63 LYS CB C 33.37 . 1
391 . 63 LYS CG C 25.37 . 1
392 . 63 LYS CD C 29.24 . 1
393 . 63 LYS N N 115.67 . 1
394 . 64 ASN H H 8.22 . 1
395 . 64 ASN HA H 5.26 . 1
396 . 64 ASN HB2 H 3.34 . 2
397 . 64 ASN HB3 H 2.87 . 2
398 . 64 ASN CA C 49.79 . 1
399 . 64 ASN CB C 38.26 . 1
400 . 64 ASN N N 114.75 . 1
401 . 65 PRO HA H 4.83 . 1
402 . 65 PRO HB2 H 2.58 . 2
403 . 65 PRO HG2 H 2.16 . 2
404 . 65 PRO HD2 H 3.97 . 2
405 . 65 PRO HD3 H 3.65 . 2
406 . 65 PRO CA C 63.90 . 1
407 . 65 PRO CB C 32.42 . 1
408 . 65 PRO CG C 26.80 . 1
409 . 66 SER H H 7.87 . 1
410 . 66 SER HA H 4.46 . 1
411 . 66 SER HB2 H 4.21 . 2
412 . 66 SER HB3 H 4.12 . 2
413 . 66 SER CA C 59.61 . 1
414 . 66 SER CB C 64.39 . 1
415 . 66 SER N N 113.44 . 1
416 . 67 ILE H H 7.44 . 1
417 . 67 ILE HA H 4.52 . 1
418 . 67 ILE HB H 1.66 . 1
419 . 67 ILE HG12 H 1.88 . 2
420 . 67 ILE HG13 H 0.97 . 2
421 . 67 ILE HG2 H 0.80 . 1
422 . 67 ILE HD1 H 0.97 . 1
423 . 67 ILE CA C 63.32 . 1
424 . 67 ILE CB C 39.59 . 1
425 . 67 ILE CG1 C 30.52 . 1
426 . 67 ILE CG2 C 17.11 . 1
427 . 67 ILE CD1 C 13.76 . 1
428 . 67 ILE N N 122.33 . 1
429 . 68 VAL H H 9.28 . 1
430 . 68 VAL HA H 4.43 . 1
431 . 68 VAL HB H 2.12 . 1
432 . 68 VAL HG1 H 1.10 . 2
433 . 68 VAL CA C 61.39 . 1
434 . 68 VAL CB C 35.77 . 1
435 . 68 VAL CG1 C 21.27 . 2
436 . 68 VAL N N 128.23 . 1
437 . 69 VAL H H 8.51 . 1
438 . 69 VAL HA H 5.42 . 1
439 . 69 VAL HB H 2.07 . 1
440 . 69 VAL HG1 H 1.05 . 2
441 . 69 VAL HG2 H 0.94 . 2
442 . 69 VAL CA C 60.62 . 1
443 . 69 VAL CB C 34.85 . 1
444 . 69 VAL CG1 C 22.60 . 2
445 . 69 VAL N N 123.28 . 1
446 . 70 GLU H H 9.67 . 1
447 . 70 GLU HA H 4.97 . 1
448 . 70 GLU HB2 H 2.18 . 2
449 . 70 GLU HB3 H 2.11 . 2
450 . 70 GLU HG2 H 2.34 . 2
451 . 70 GLU HG3 H 2.29 . 2
452 . 70 GLU CA C 55.11 . 1
453 . 70 GLU CB C 34.20 . 1
454 . 70 GLU CG C 36.52 . 1
455 . 70 GLU N N 126.40 . 1
456 . 71 ASP H H 8.75 . 1
457 . 71 ASP HA H 4.96 . 1
458 . 71 ASP HB2 H 2.79 . 2
459 . 71 ASP HB3 H 2.41 . 2
460 . 71 ASP CA C 52.87 . 1
461 . 71 ASP CB C 41.20 . 1
462 . 71 ASP N N 124.67 . 1
463 . 72 LYS H H 8.85 . 1
464 . 72 LYS HA H 4.64 . 1
465 . 72 LYS HB2 H 1.71 . 2
466 . 72 LYS HB3 H 1.58 . 2
467 . 72 LYS HG2 H 1.53 . 2
468 . 72 LYS HG3 H 1.20 . 2
469 . 72 LYS CA C 55.65 . 1
470 . 72 LYS CB C 34.60 . 1
471 . 72 LYS CG C 24.31 . 1
472 . 72 LYS CD C 28.78 . 1
473 . 72 LYS N N 125.34 . 1
474 . 73 ALA H H 8.88 . 1
475 . 73 ALA HA H 4.13 . 1
476 . 73 ALA HB H 1.64 . 1
477 . 73 ALA CA C 53.49 . 1
478 . 73 ALA CB C 17.58 . 1
479 . 73 ALA N N 126.64 . 1
480 . 74 GLY H H 8.87 . 1
481 . 74 GLY HA2 H 4.03 . 2
482 . 74 GLY HA3 H 3.49 . 2
483 . 74 GLY CA C 45.26 . 1
484 . 74 GLY N N 105.75 . 1
485 . 75 PHE H H 7.81 . 1
486 . 75 PHE HA H 5.09 . 1
487 . 75 PHE HB2 H 2.98 . 2
488 . 75 PHE HB3 H 2.83 . 2
489 . 75 PHE CA C 56.49 . 1
490 . 75 PHE CB C 43.28 . 1
491 . 75 PHE N N 117.57 . 1
492 . 76 TRP H H 9.36 . 1
493 . 76 TRP HA H 5.59 . 1
494 . 76 TRP HB2 H 3.18 . 1
495 . 76 TRP HB3 H 3.11 . 1
496 . 76 TRP CA C 55.73 . 1
497 . 76 TRP CB C 32.36 . 1
498 . 76 TRP N N 118.83 . 1
499 . 77 TRP H H 9.87 . 1
500 . 77 TRP HA H 5.07 . 1
501 . 77 TRP HB2 H 3.35 . 2
502 . 77 TRP HB3 H 3.25 . 2
503 . 77 TRP CA C 56.87 . 1
504 . 77 TRP CB C 29.41 . 1
505 . 77 TRP N N 124.67 . 1
506 . 78 ILE H H 9.40 . 1
507 . 78 ILE HA H 5.15 . 1
508 . 78 ILE HB H 2.14 . 1
509 . 78 ILE HG12 H 1.81 . 2
510 . 78 ILE HG13 H 1.08 . 2
511 . 78 ILE HG2 H 0.88 . 1
512 . 78 ILE HD1 H 0.88 . 1
513 . 78 ILE CA C 60.55 . 1
514 . 78 ILE CB C 39.75 . 1
515 . 78 ILE CG1 C 27.43 . 1
516 . 78 ILE CG2 C 18.66 . 1
517 . 78 ILE CD1 C 15.03 . 1
518 . 78 ILE N N 125.67 . 1
519 . 79 LYS H H 9.08 . 1
520 . 79 LYS HA H 5.50 . 1
521 . 79 LYS HB2 H 1.89 . 2
522 . 79 LYS HB3 H 1.70 . 2
523 . 79 LYS HG2 H 1.59 . 1
524 . 79 LYS HD2 H 1.74 . 2
525 . 79 LYS HE2 H 2.96 . 2
526 . 79 LYS CA C 54.22 . 1
527 . 79 LYS CB C 35.97 . 1
528 . 79 LYS CG C 25.31 . 1
529 . 79 LYS CD C 29.64 . 1
530 . 79 LYS CE C 41.95 . 1
531 . 79 LYS N N 126.56 . 1
532 . 80 ALA H H 8.46 . 1
533 . 80 ALA HA H 4.53 . 1
534 . 80 ALA HB H 1.41 . 1
535 . 80 ALA CA C 50.94 . 1
536 . 80 ALA CB C 24.40 . 1
537 . 80 ALA N N 121.62 . 1
538 . 81 ASP H H 8.80 . 1
539 . 81 ASP HA H 5.07 . 1
540 . 81 ASP HB2 H 2.68 . 2
541 . 81 ASP CA C 53.76 . 1
542 . 81 ASP CB C 41.66 . 1
543 . 81 ASP N N 117.81 . 1
544 . 82 GLY H H 8.90 . 1
545 . 82 GLY HA2 H 4.37 . 2
546 . 82 GLY HA3 H 3.58 . 2
547 . 82 GLY CA C 47.80 . 1
548 . 82 GLY N N 113.60 . 1
549 . 83 ALA H H 7.81 . 1
550 . 83 ALA HA H 5.43 . 1
551 . 83 ALA HB H 1.36 . 1
552 . 83 ALA CA C 52.00 . 1
553 . 83 ALA CB C 22.39 . 1
554 . 83 ALA N N 122.94 . 1
555 . 84 ILE H H 8.67 . 1
556 . 84 ILE HA H 4.25 . 1
557 . 84 ILE HB H 1.47 . 1
558 . 84 ILE HG2 H 0.76 . 1
559 . 84 ILE HD1 H 0.67 . 1
560 . 84 ILE CA C 60.59 . 1
561 . 84 ILE CB C 42.20 . 1
562 . 84 ILE CG1 C 28.05 . 1
563 . 84 ILE CG2 C 16.98 . 1
564 . 84 ILE CD1 C 14.75 . 1
565 . 84 ILE N N 119.50 . 1
566 . 85 GLU H H 8.46 . 1
567 . 85 GLU HA H 5.47 . 1
568 . 85 GLU HB2 H 1.91 . 2
569 . 85 GLU HG2 H 2.14 . 2
570 . 85 GLU HG3 H 2.08 . 2
571 . 85 GLU CA C 54.37 . 1
572 . 85 GLU CB C 34.10 . 1
573 . 85 GLU CG C 36.47 . 1
574 . 85 GLU N N 124.59 . 1
575 . 86 ILE H H 9.26 . 1
576 . 86 ILE HA H 4.17 . 1
577 . 86 ILE HB H 1.78 . 1
578 . 86 ILE HG12 H 1.55 . 2
579 . 86 ILE HG13 H 0.92 . 2
580 . 86 ILE HG2 H 0.78 . 1
581 . 86 ILE HD1 H 0.69 . 1
582 . 86 ILE CA C 61.08 . 1
583 . 86 ILE CB C 42.21 . 1
584 . 86 ILE CG1 C 27.52 . 1
585 . 86 ILE CG2 C 17.01 . 1
586 . 86 ILE CD1 C 12.90 . 1
587 . 86 ILE N N 122.94 . 1
588 . 87 ASP H H 9.27 . 1
589 . 87 ASP HA H 5.18 . 1
590 . 87 ASP HB2 H 3.20 . 2
591 . 87 ASP HB3 H 2.52 . 2
592 . 87 ASP CA C 52.75 . 1
593 . 87 ASP CB C 42.31 . 1
594 . 87 ASP N N 127.26 . 1
595 . 88 ALA H H 9.68 . 1
596 . 88 ALA HA H 4.17 . 1
597 . 88 ALA HB H 1.68 . 1
598 . 88 ALA CA C 55.19 . 1
599 . 88 ALA CB C 18.44 . 1
600 . 88 ALA N N 129.82 . 1
601 . 89 ALA H H 8.80 . 1
602 . 89 ALA HA H 4.48 . 1
603 . 89 ALA HB H 1.63 . 1
604 . 89 ALA CA C 55.01 . 1
605 . 89 ALA CB C 18.36 . 1
606 . 89 ALA N N 120.00 . 1
607 . 90 GLU H H 7.23 . 1
608 . 90 GLU HA H 4.17 . 1
609 . 90 GLU HG2 H 2.32 . 2
610 . 90 GLU CA C 58.62 . 1
611 . 90 GLU CB C 30.08 . 1
612 . 90 GLU CG C 36.59 . 1
613 . 90 GLU N N 119.20 . 1
614 . 91 ALA H H 7.81 . 1
615 . 91 ALA HA H 3.89 . 1
616 . 91 ALA HB H 1.11 . 1
617 . 91 ALA CA C 55.11 . 1
618 . 91 ALA CB C 18.20 . 1
619 . 91 ALA N N 121.29 . 1
620 . 92 GLY H H 8.63 . 1
621 . 92 GLY HA2 H 4.22 . 2
622 . 92 GLY CA C 47.91 . 1
623 . 92 GLY N N 105.06 . 1
624 . 93 GLU H H 7.52 . 1
625 . 93 GLU HA H 4.16 . 1
626 . 93 GLU HB2 H 2.27 . 2
627 . 93 GLU HB3 H 2.18 . 2
628 . 93 GLU HG2 H 2.45 . 2
629 . 93 GLU HG3 H 2.35 . 2
630 . 93 GLU CA C 59.00 . 1
631 . 93 GLU CB C 29.50 . 1
632 . 93 GLU CG C 36.12 . 1
633 . 93 GLU N N 120.89 . 1
634 . 94 LEU H H 7.67 . 1
635 . 94 LEU HA H 4.20 . 1
636 . 94 LEU HB2 H 2.01 . 2
637 . 94 LEU HB3 H 1.72 . 2
638 . 94 LEU HG H 1.69 . 1
639 . 94 LEU HD1 H 0.90 . 2
640 . 94 LEU CA C 57.73 . 1
641 . 94 LEU CB C 42.63 . 1
642 . 94 LEU CG C 26.11 . 1
643 . 94 LEU CD1 C 23.84 . 1
644 . 94 LEU N N 120.32 . 1
645 . 95 LEU H H 8.37 . 1
646 . 95 LEU HA H 4.17 . 1
647 . 95 LEU HB2 H 1.81 . 2
648 . 95 LEU HB3 H 1.47 . 2
649 . 95 LEU HG H 1.76 . 1
650 . 95 LEU HD1 H 0.93 . 2
651 . 95 LEU HD2 H 0.41 . 2
652 . 95 LEU CA C 55.45 . 1
653 . 95 LEU CB C 43.25 . 1
654 . 95 LEU CG C 25.76 . 1
655 . 95 LEU CD1 C 22.26 . 1
656 . 95 LEU CD2 C 25.49 . 1
657 . 95 LEU N N 115.32 . 1
658 . 96 GLY H H 8.09 . 1
659 . 96 GLY HA2 H 4.04 . 2
660 . 96 GLY HA3 H 3.95 . 2
661 . 96 GLY CA C 46.33 . 1
662 . 96 GLY N N 107.83 . 1
663 . 97 LYS H H 7.94 . 1
664 . 97 LYS HA H 4.96 . 1
665 . 97 LYS HB2 H 1.95 . 2
666 . 97 LYS HB3 H 1.84 . 2
667 . 97 LYS HG2 H 1.34 . 2
668 . 97 LYS CA C 53.36 . 1
669 . 97 LYS CB C 32.91 . 1
670 . 97 LYS N N 116.34 . 1
671 . 98 PRO HA H 4.44 . 1
672 . 98 PRO HB2 H 2.33 . 2
673 . 98 PRO HB3 H 1.45 . 2
674 . 98 PRO HG2 H 2.19 . 2
675 . 98 PRO HG3 H 2.02 . 2
676 . 98 PRO HD2 H 3.85 . 2
677 . 98 PRO HD3 H 3.71 . 2
678 . 98 PRO CA C 63.51 . 1
679 . 98 PRO CB C 31.44 . 1
680 . 98 PRO CG C 27.88 . 1
681 . 98 PRO CD C 50.25 . 1
682 . 99 PHE H H 8.30 . 1
683 . 99 PHE HA H 4.71 . 1
684 . 99 PHE HB2 H 3.05 . 2
685 . 99 PHE HB3 H 2.90 . 2
686 . 99 PHE CA C 58.80 . 1
687 . 99 PHE CB C 42.24 . 1
688 . 99 PHE N N 126.10 . 1
689 . 100 SER H H 9.18 . 1
690 . 100 SER HA H 4.88 . 1
691 . 100 SER HB2 H 4.28 . 2
692 . 100 SER HB3 H 3.91 . 2
693 . 100 SER CA C 56.30 . 1
694 . 100 SER CB C 67.25 . 1
695 . 100 SER N N 124.65 . 1
696 . 101 VAL H H 9.08 . 1
697 . 101 VAL HA H 3.66 . 1
698 . 101 VAL HB H 2.02 . 1
699 . 101 VAL HG1 H 0.95 . 2
700 . 101 VAL HG2 H 0.86 . 2
701 . 101 VAL CA C 65.94 . 1
702 . 101 VAL CB C 31.70 . 1
703 . 101 VAL CG1 C 21.28 . 1
704 . 101 VAL N N 119.17 . 1
705 . 102 TYR H H 7.51 . 1
706 . 102 TYR HA H 4.06 . 1
707 . 102 TYR HB2 H 2.94 . 1
708 . 102 TYR CA C 61.35 . 1
709 . 102 TYR CB C 37.71 . 1
710 . 102 TYR N N 119.55 . 1
711 . 103 ASP H H 7.23 . 1
712 . 103 ASP HA H 4.14 . 1
713 . 103 ASP HB2 H 1.97 . 2
714 . 103 ASP HB3 H 1.76 . 2
715 . 103 ASP CA C 56.93 . 1
716 . 103 ASP CB C 40.28 . 1
717 . 103 ASP N N 118.12 . 1
718 . 104 LEU H H 6.97 . 1
719 . 104 LEU HA H 4.12 . 1
720 . 104 LEU HB2 H 1.78 . 2
721 . 104 LEU HG H 1.57 . 1
722 . 104 LEU HD1 H 0.86 . 2
723 . 104 LEU CA C 57.57 . 1
724 . 104 LEU CB C 42.25 . 1
725 . 104 LEU N N 117.97 . 1
726 . 105 LEU H H 8.01 . 1
727 . 105 LEU HA H 3.71 . 1
728 . 105 LEU HB2 H 1.74 . 2
729 . 105 LEU HB3 H 1.48 . 2
730 . 105 LEU HG H 1.62 . 1
731 . 105 LEU HD1 H 0.77 . 2
732 . 105 LEU HD2 H 0.54 . 2
733 . 105 LEU CA C 57.83 . 1
734 . 105 LEU CB C 42.10 . 1
735 . 105 LEU N N 117.17 . 1
736 . 106 ILE H H 7.54 . 1
737 . 106 ILE HA H 4.07 . 1
738 . 106 ILE HB H 1.94 . 1
739 . 106 ILE HG12 H 1.34 . 2
740 . 106 ILE HG2 H 0.91 . 1
741 . 106 ILE CA C 63.32 . 1
742 . 106 ILE CB C 38.31 . 1
743 . 106 ILE N N 115.23 . 1
744 . 107 ASN H H 7.71 . 1
745 . 107 ASN HA H 5.06 . 1
746 . 107 ASN HB2 H 3.26 . 2
747 . 107 ASN HB3 H 2.71 . 2
748 . 107 ASN HD21 H 7.27 . 2
749 . 107 ASN HD22 H 6.99 . 2
750 . 107 ASN CA C 53.93 . 1
751 . 107 ASN CB C 40.93 . 1
752 . 107 ASN N N 117.33 . 1
753 . 108 VAL H H 7.60 . 1
754 . 108 VAL HA H 4.15 . 1
755 . 108 VAL HB H 2.30 . 1
756 . 108 VAL HG1 H 0.90 . 2
757 . 108 VAL CA C 63.86 . 1
758 . 108 VAL CB C 39.77 . 1
759 . 108 VAL N N 122.26 . 1
760 . 109 SER H H 9.21 . 1
761 . 109 SER HA H 4.67 . 1
762 . 109 SER HB2 H 3.69 . 2
763 . 109 SER HB3 H 3.54 . 2
764 . 109 SER CA C 59.23 . 1
765 . 109 SER CB C 64.54 . 1
766 . 109 SER N N 123.69 . 1
767 . 110 SER H H 7.55 . 1
768 . 110 SER HA H 4.58 . 1
769 . 110 SER HB2 H 3.97 . 2
770 . 110 SER CA C 58.22 . 1
771 . 110 SER CB C 64.66 . 1
772 . 110 SER N N 111.31 . 1
773 . 111 THR H H 8.05 . 1
774 . 111 THR HA H 5.07 . 1
775 . 111 THR HB H 4.10 . 1
776 . 111 THR HG2 H 1.23 . 1
777 . 111 THR CA C 59.77 . 1
778 . 111 THR CB C 72.66 . 1
779 . 111 THR CG2 C 23.13 . 1
780 . 111 THR N N 110.91 . 1
781 . 112 VAL H H 9.06 . 1
782 . 112 VAL HA H 4.22 . 1
783 . 112 VAL HB H 1.98 . 1
784 . 112 VAL HG1 H 0.97 . 2
785 . 112 VAL CA C 63.82 . 1
786 . 112 VAL CB C 33.85 . 1
787 . 112 VAL CG1 C 20.51 . 2
788 . 112 VAL N N 123.76 . 1
789 . 113 GLY H H 8.14 . 1
790 . 113 GLY HA2 H 4.59 . 2
791 . 113 GLY HA3 H 3.84 . 2
792 . 113 GLY CA C 43.17 . 1
793 . 113 GLY N N 111.60 . 1
794 . 114 ARG H H 8.89 . 1
795 . 114 ARG HA H 4.57 . 1
796 . 114 ARG HB2 H 1.82 . 2
797 . 114 ARG HB3 H 1.75 . 2
798 . 114 ARG HG2 H 1.64 . 2
799 . 114 ARG HD2 H 3.28 . 2
800 . 114 ARG CA C 55.35 . 1
801 . 114 ARG CB C 31.11 . 1
802 . 114 ARG CG C 27.49 . 1
803 . 114 ARG N N 120.68 . 1
804 . 115 ALA H H 8.44 . 1
805 . 115 ALA HA H 5.42 . 1
806 . 115 ALA HB H 1.36 . 1
807 . 115 ALA CA C 50.25 . 1
808 . 115 ALA CB C 21.59 . 1
809 . 115 ALA N N 128.25 . 1
810 . 116 TYR H H 9.14 . 1
811 . 116 TYR HA H 4.98 . 1
812 . 116 TYR HB2 H 3.10 . 2
813 . 116 TYR HB3 H 2.93 . 2
814 . 116 TYR CA C 57.01 . 1
815 . 116 TYR CB C 41.00 . 1
816 . 116 TYR N N 119.85 . 1
817 . 117 THR H H 8.46 . 1
818 . 117 THR HA H 5.31 . 1
819 . 117 THR HB H 4.16 . 1
820 . 117 THR HG2 H 1.25 . 1
821 . 117 THR CA C 60.07 . 1
822 . 117 THR CB C 70.45 . 1
823 . 117 THR CG2 C 22.47 . 1
824 . 117 THR N N 112.74 . 1
825 . 118 LEU H H 8.66 . 1
826 . 118 LEU HA H 4.73 . 1
827 . 118 LEU HB2 H 1.80 . 2
828 . 118 LEU HB3 H 1.66 . 2
829 . 118 LEU HG H 1.04 . 1
830 . 118 LEU CA C 54.38 . 1
831 . 118 LEU CB C 43.59 . 1
832 . 118 LEU N N 126.57 . 1
833 . 119 GLY HA2 H 4.28 . 1
834 . 119 GLY HA3 H 3.81 . 1
835 . 119 GLY CA C 47.25 . 1
836 . 120 THR H H 8.67 . 1
837 . 120 THR HA H 4.51 . 1
838 . 120 THR HB H 4.86 . 1
839 . 120 THR HG2 H 1.38 . 1
840 . 120 THR CA C 62.23 . 1
841 . 120 THR CB C 68.18 . 1
842 . 120 THR CG2 C 21.68 . 1
843 . 120 THR N N 117.47 . 1
844 . 121 LYS H H 8.27 . 1
845 . 121 LYS HA H 4.95 . 1
846 . 121 LYS HB2 H 2.03 . 2
847 . 121 LYS HG2 H 1.46 . 2
848 . 121 LYS HG3 H 1.26 . 2
849 . 121 LYS HD2 H 1.74 . 2
850 . 121 LYS HE2 H 3.10 . 2
851 . 121 LYS CA C 56.49 . 1
852 . 121 LYS CB C 34.69 . 1
853 . 121 LYS CG C 25.92 . 1
854 . 121 LYS CD C 29.63 . 1
855 . 121 LYS N N 121.21 . 1
856 . 122 PHE H H 9.03 . 1
857 . 122 PHE HA H 5.09 . 1
858 . 122 PHE HB2 H 3.11 . 2
859 . 122 PHE HB3 H 2.89 . 2
860 . 122 PHE CA C 56.39 . 1
861 . 122 PHE CB C 41.61 . 1
862 . 122 PHE N N 127.41 . 1
863 . 123 THR H H 8.36 . 1
864 . 123 THR HA H 5.10 . 1
865 . 123 THR HB H 3.21 . 1
866 . 123 THR HG2 H 1.01 . 1
867 . 123 THR CA C 60.53 . 1
868 . 123 THR CB C 71.53 . 1
869 . 123 THR CG2 C 21.84 . 1
870 . 123 THR N N 123.47 . 1
871 . 124 ILE H H 8.55 . 1
872 . 124 ILE HA H 5.07 . 1
873 . 124 ILE HB H 1.58 . 1
874 . 124 ILE HG12 H 1.18 . 2
875 . 124 ILE HG13 H 0.98 . 2
876 . 124 ILE HG2 H 0.88 . 1
877 . 124 ILE HD1 H 0.75 . 1
878 . 124 ILE CA C 58.80 . 1
879 . 124 ILE CB C 40.23 . 1
880 . 124 ILE CG1 C 27.86 . 1
881 . 124 ILE CG2 C 18.06 . 1
882 . 124 ILE CD1 C 15.06 . 1
883 . 124 ILE N N 122.88 . 1
884 . 125 THR H H 8.96 . 1
885 . 125 THR HA H 5.41 . 1
886 . 125 THR HB H 4.28 . 1
887 . 125 THR HG2 H 1.40 . 1
888 . 125 THR CA C 58.96 . 1
889 . 125 THR CB C 71.28 . 1
890 . 125 THR CG2 C 21.53 . 1
891 . 125 THR N N 117.93 . 1
892 . 126 SER H H 8.36 . 1
893 . 126 SER HA H 4.53 . 1
894 . 126 SER HB2 H 4.27 . 2
895 . 126 SER HB3 H 3.90 . 2
896 . 126 SER CA C 58.09 . 1
897 . 126 SER CB C 64.24 . 1
898 . 126 SER N N 118.60 . 1
899 . 127 GLU H H 8.77 . 1
900 . 127 GLU HA H 4.34 . 1
901 . 127 GLU HB2 H 2.09 . 2
902 . 127 GLU HG2 H 2.36 . 2
903 . 127 GLU CA C 57.54 . 1
904 . 127 GLU CB C 30.45 . 1
905 . 127 GLU CG C 36.47 . 1
906 . 127 GLU N N 123.20 . 1
907 . 128 LEU H H 8.27 . 1
908 . 128 LEU HA H 4.35 . 1
909 . 128 LEU HB2 H 1.68 . 2
910 . 128 LEU HG H 0.95 . 1
911 . 128 LEU CA C 55.79 . 1
912 . 128 LEU CB C 42.17 . 1
913 . 128 LEU CG C 27.29 . 1
914 . 128 LEU CD1 C 24.66 . 1
915 . 128 LEU CD2 C 23.81 . 1
916 . 128 LEU N N 121.35 . 1
917 . 129 MET H H 8.06 . 1
918 . 129 MET HA H 4.49 . 1
919 . 129 MET HB2 H 2.06 . 2
920 . 129 MET HG2 H 2.60 . 2
921 . 129 MET HE H 1.43 . 1
922 . 129 MET CA C 55.89 . 1
923 . 129 MET CB C 33.10 . 1
924 . 129 MET N N 119.34 . 1
925 . 130 GLY H H 8.31 . 1
926 . 130 GLY HA2 H 4.01 . 2
927 . 130 GLY CA C 45.59 . 1
928 . 130 GLY N N 108.57 . 1
929 . 131 LEU H H 8.00 . 1
930 . 131 LEU HA H 4.37 . 1
931 . 131 LEU HB2 H 1.67 . 2
932 . 131 LEU HG H 0.91 . 1
933 . 131 LEU CA C 55.42 . 1
934 . 131 LEU CB C 42.49 . 1
935 . 131 LEU CG C 27.16 . 1
936 . 131 LEU CD1 C 24.87 . 1
937 . 131 LEU CD2 C 23.59 . 1
938 . 131 LEU N N 121.16 . 1
939 . 132 ASP H H 8.37 . 1
940 . 132 ASP HA H 4.61 . 1
941 . 132 ASP HB2 H 2.82 . 2
942 . 132 ASP HB3 H 2.70 . 2
943 . 132 ASP CA C 54.68 . 1
944 . 132 ASP CB C 41.06 . 1
945 . 132 ASP N N 120.04 . 1
946 . 133 ARG H H 8.07 . 1
947 . 133 ARG HA H 4.72 . 1
948 . 133 ARG HB2 H 1.77 . 2
949 . 133 ARG HD2 H 3.23 . 2
950 . 133 ARG CA C 56.10 . 1
951 . 133 ARG CB C 30.89 . 1
952 . 133 ARG CG C 29.21 . 1
953 . 133 ARG N N 120.77 . 1
954 . 134 ALA H H 8.33 . 1
955 . 134 ALA HA H 4.38 . 1
956 . 134 ALA HB H 1.47 . 1
957 . 134 ALA CA C 55.69 . 1
958 . 134 ALA CB C 19.28 . 1
959 . 134 ALA N N 123.93 . 1
960 . 135 LEU H H 8.16 . 1
961 . 135 LEU HA H 4.47 . 1
962 . 135 LEU HB2 H 1.77 . 2
963 . 135 LEU HB3 H 1.70 . 2
964 . 135 LEU HG H 0.98 . 1
965 . 135 LEU CA C 55.37 . 1
966 . 135 LEU CB C 42.27 . 1
967 . 135 LEU CG C 27.26 . 1
968 . 135 LEU CD1 C 25.03 . 1
969 . 135 LEU N N 120.12 . 1
970 . 136 THR H H 7.90 . 1
971 . 136 THR HA H 4.46 . 1
972 . 136 THR HB H 4.34 . 1
973 . 136 THR HG2 H 1.27 . 1
974 . 136 THR CA C 61.54 . 1
975 . 136 THR CB C 69.94 . 1
976 . 136 THR N N 111.88 . 1
977 . 137 ASP H H 8.28 . 1
978 . 137 ASP HA H 4.77 . 1
979 . 137 ASP HB2 H 2.82 . 2
980 . 137 ASP HB3 H 2.70 . 2
981 . 137 ASP CA C 54.60 . 1
982 . 137 ASP CB C 41.09 . 1
983 . 137 ASP N N 122.81 . 1
984 . 138 ILE H H 7.60 . 1
985 . 138 ILE HA H 4.17 . 1
986 . 138 ILE HB H 1.91 . 1
987 . 138 ILE HG12 H 1.49 . 2
988 . 138 ILE HG13 H 1.21 . 2
989 . 138 ILE HG2 H 0.96 . 1
990 . 138 ILE CA C 62.80 . 1
991 . 138 ILE CB C 39.90 . 1
992 . 138 ILE N N 124.00 . 1
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