data_5401
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Conservation of chemical shift and secondary structure of the PNT/SAM domains
from the Ets family of transcription factors
;
_BMRB_accession_number 5401
_BMRB_flat_file_name bmr5401.str
_Entry_type original
_Submission_date 2002-06-17
_Accession_date 2002-06-18
_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 Mackereth Cameron D. .
2 Schaerpf Manuela . .
3 Gentile Lisa N. .
4 McIntosh Lawrence P. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 535
"13C chemical shifts" 412
"15N chemical shifts" 99
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2004-08-19 update author 'addition of relationship loop'
2003-02-20 original author 'original release'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
6287 'assignment and structure calculation for a different construct of the protein GABPa'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Chemical Shift and Secondary Structure Conservation of the PNT/SAM Domains from
the ets Family of Transcription Factors
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22333295
_PubMed_ID 12449421
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Mackereth Cameron D. .
2 Scharpf Manuela . .
3 Gentile Lisa N. .
4 McIntosh Lawrence P. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 24
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 71
_Page_last 72
_Year 2002
_Details .
loop_
_Keyword
'PNT/SAM domain'
'secondary chemical shift'
homology
stop_
save_
##################################
# Molecular system description #
##################################
save_GABPalpha
_Saveframe_category molecular_system
_Mol_system_name 'GABPalpha Pointed Domain'
_Abbreviation_common GABPalpha
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'GABPalpha Pointed domain' $GABPalpha_PNT
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
'PNT domain / SAM domain'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_GABPalpha_PNT
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'GABPalpha Pointed Domain'
_Abbreviation_common 'GABPalpha PNT'
_Molecular_mass 10339
_Mol_thiol_state 'all free'
_Details
;
This is a fragment of GABPalpha corresponding to the Pointed (PNT) or SAM
domain (residues 108-201)
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 87
_Mol_residue_sequence
;
AALEGYRKEQERLGIPYDPI
HWSTDQVLHWVVWVMKEFSM
TDIDLTTLNISGRELCSLNQ
EDFFQRVPRGEILWSHLELL
RKYVLAS
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 168 ALA 2 169 ALA 3 170 LEU 4 171 GLU 5 172 GLY
6 173 TYR 7 174 ARG 8 175 LYS 9 176 GLU 10 177 GLN
11 178 GLU 12 179 ARG 13 180 LEU 14 181 GLY 15 182 ILE
16 183 PRO 17 184 TYR 18 185 ASP 19 186 PRO 20 187 ILE
21 188 HIS 22 189 TRP 23 190 SER 24 191 THR 25 192 ASP
26 193 GLN 27 194 VAL 28 195 LEU 29 196 HIS 30 197 TRP
31 198 VAL 32 199 VAL 33 200 TRP 34 201 VAL 35 202 MET
36 203 LYS 37 204 GLU 38 205 PHE 39 206 SER 40 207 MET
41 208 THR 42 209 ASP 43 210 ILE 44 211 ASP 45 212 LEU
46 213 THR 47 214 THR 48 215 LEU 49 216 ASN 50 217 ILE
51 218 SER 52 219 GLY 53 220 ARG 54 221 GLU 55 222 LEU
56 223 CYS 57 224 SER 58 225 LEU 59 226 ASN 60 227 GLN
61 228 GLU 62 229 ASP 63 230 PHE 64 231 PHE 65 232 GLN
66 233 ARG 67 234 VAL 68 235 PRO 69 236 ARG 70 237 GLY
71 238 GLU 72 239 ILE 73 240 LEU 74 241 TRP 75 242 SER
76 243 HIS 77 244 LEU 78 245 GLU 79 246 LEU 80 247 LEU
81 248 ARG 82 249 LYS 83 250 TYR 84 251 VAL 85 252 LEU
86 253 ALA 87 254 SER
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-28
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
BMRB 6287 GABPalpha_PNT 100.00 91 100.00 100.00 7.81e-57
PDB 1SXD "Solution Structure Of The Pointed (Pnt) Domain From Mgabpa" 100.00 91 100.00 100.00 7.81e-57
DBJ BAA02575 "transcription factor E4TF1-60 [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54
DBJ BAD96884 "GA binding protein transcription factor, alpha subunit (60kD) variant [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54
DBJ BAE24181 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55
DBJ BAE26442 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55
DBJ BAE26687 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55
GB AAA53030 "GA binding protein [Mus musculus]" 100.00 454 98.85 98.85 9.34e-54
GB AAA65706 "nuclear respiratory factor-2 subunit alpha [Homo sapiens]" 100.00 454 98.85 98.85 6.95e-54
GB AAH13562 "Gabpa protein [Mus musculus]" 100.00 351 100.00 100.00 1.65e-55
GB AAH35031 "GA binding protein transcription factor, alpha subunit 60kDa [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54
GB AAH52448 "GA repeat binding protein, alpha [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55
REF NP_001068905 "GA-binding protein alpha chain [Bos taurus]" 100.00 454 97.70 98.85 3.49e-53
REF NP_001102311 "GA-binding protein alpha chain [Rattus norvegicus]" 100.00 454 98.85 98.85 6.19e-54
REF NP_001184226 "GA-binding protein alpha chain [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54
REF NP_001253514 "GA-binding protein alpha chain [Macaca mulatta]" 100.00 454 98.85 98.85 6.19e-54
REF NP_002031 "GA-binding protein alpha chain [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54
SP Q00422 "RecName: Full=GA-binding protein alpha chain; Short=GABP subunit alpha [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55
SP Q06546 "RecName: Full=GA-binding protein alpha chain; Short=GABP subunit alpha; AltName: Full=Nuclear respiratory factor 2 subunit alph" 100.00 454 98.85 98.85 5.57e-54
TPG DAA33658 "TPA: GA binding protein transcription factor, alpha subunit 60kDa [Bos taurus]" 100.00 454 97.70 98.85 3.49e-53
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$GABPalpha_PNT mouse 10090 Eukaryota Metazoa Mus musculus
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
_Details
$GABPalpha_PNT 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET22b
;
The corresponding cDNA was cloned into pET22b using PCR generated NdeI and
HindIII restriction enzyme sites
;
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_15N_GABPa_PNT
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$GABPalpha_PNT . mM 0.5 2.5 '[U-99% 15N]'
stop_
save_
save_13C-15N_GABPalpha_PNT
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$GABPalpha_PNT 1.5 mM '[U-99% 13C; U-99% 15N]'
stop_
save_
save_10_13C-15N_GABPalpha_PNT
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$GABPalpha_PNT 1.5 mM '[N-10% 13C; U-99% 15N]'
stop_
save_
############################
# Computer software used #
############################
save_FELIX
_Saveframe_category software
_Name FELIX
_Version 95.0
loop_
_Task
'processing spectra'
assignment
stop_
_Details 'Accelrys, Inc.'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UNITY
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC'
_Sample_label .
save_
save_1H-13C_HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C HSQC'
_Sample_label .
save_
save_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_HBCBCACONH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HBCBCACONH
_Sample_label .
save_
save_HNCO_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label .
save_
save_H(CCO)NH-TOCSY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CCO)NH-TOCSY
_Sample_label .
save_
save_C(CO)NH-TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name C(CO)NH-TOCSY
_Sample_label .
save_
save_HCCH-TOCSY_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HBCBCACONH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CCO)NH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name C(CO)NH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_conditions
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.2 0.1 n/a
temperature 303 1 K
'ionic strength' 0.02 . M
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
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
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_shift1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$13C-15N_GABPalpha_PNT
stop_
_Sample_conditions_label $sample_conditions
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'GABPalpha Pointed domain'
_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 ALA CA C 52.73 0.05 1
2 . 1 ALA HA H 4.01 0.02 1
3 . 1 ALA CB C 17.58 0.05 1
4 . 1 ALA HB H 0.84 0.02 1
5 . 1 ALA C C 178.21 0.05 1
6 . 2 ALA N N 125.97 0.05 1
7 . 2 ALA H H 8.58 0.02 1
8 . 2 ALA CA C 53.37 0.05 1
9 . 2 ALA HA H 4.56 0.02 1
10 . 2 ALA CB C 19.46 0.05 1
11 . 2 ALA HB H 1.61 0.02 1
12 . 2 ALA C C 178.63 0.05 1
13 . 3 LEU N N 125.48 0.05 1
14 . 3 LEU H H 7.72 0.02 1
15 . 3 LEU CA C 56.75 0.05 1
16 . 3 LEU HA H 4.32 0.02 1
17 . 3 LEU CB C 41.8 0.05 1
18 . 3 LEU HB3 H 1.67 0.02 1
19 . 3 LEU HB2 H 1.59 0.02 1
20 . 3 LEU CG C 27.08 0.05 1
21 . 3 LEU HG H 0.82 0.02 1
22 . 3 LEU CD2 C 24.16 0.05 1
23 . 3 LEU HD2 H 0.72 0.02 1
24 . 3 LEU C C 177.21 0.05 1
25 . 4 GLU N N 119.41 0.05 1
26 . 4 GLU H H 8.59 0.02 1
27 . 4 GLU CA C 58.28 0.05 1
28 . 4 GLU HA H 4.22 0.02 1
29 . 4 GLU CB C 29.99 0.05 1
30 . 4 GLU HB2 H 2.1 0.02 1
31 . 4 GLU HB3 H 2.1 0.02 1
32 . 4 GLU CG C 36.5 0.05 1
33 . 4 GLU HG2 H 2.37 0.02 2
34 . 4 GLU HG3 H 2.29 0.02 2
35 . 4 GLU C C 178.35 0.05 1
36 . 5 GLY N N 107.27 0.05 1
37 . 5 GLY H H 8.69 0.02 1
38 . 5 GLY CA C 46.58 0.05 1
39 . 5 GLY HA2 H 3.82 0.02 2
40 . 5 GLY HA3 H 3.74 0.02 2
41 . 5 GLY C C 175.03 0.05 1
42 . 6 TYR N N 125.02 0.05 1
43 . 6 TYR H H 8.64 0.02 1
44 . 6 TYR CA C 61.32 0.05 1
45 . 6 TYR HA H 3.94 0.02 1
46 . 6 TYR CB C 38.28 0.05 1
47 . 6 TYR CE1 C 116.62 0.05 1
48 . 6 TYR CE2 C 116.62 0.05 1
49 . 6 TYR HE1 H 6.32 0.02 1
50 . 6 TYR HE2 H 6.32 0.02 1
51 . 6 TYR C C 176.82 0.05 1
52 . 7 ARG N N 118.21 0.05 1
53 . 7 ARG H H 8.11 0.02 1
54 . 7 ARG CA C 58.8 0.05 1
55 . 7 ARG HA H 4.48 0.02 1
56 . 7 ARG CB C 29.52 0.05 1
57 . 7 ARG HB2 H 1.86 0.02 2
58 . 7 ARG HB3 H 1.79 0.02 2
59 . 7 ARG CG C 27.98 0.05 1
60 . 7 ARG HG2 H 1.62 0.02 1
61 . 7 ARG HG3 H 1.62 0.02 1
62 . 7 ARG CD C 42.97 0.05 1
63 . 7 ARG HD2 H 2.88 0.02 2
64 . 7 ARG HD3 H 3.08 0.02 2
65 . 7 ARG C C 178.93 0.05 1
66 . 8 LYS N N 116.95 0.05 1
67 . 8 LYS H H 7.39 0.02 1
68 . 8 LYS CA C 58.81 0.05 1
69 . 8 LYS HA H 4.07 0.02 1
70 . 8 LYS CB C 31.99 0.05 1
71 . 8 LYS HB2 H 1.9 0.02 2
72 . 8 LYS HB3 H 1.52 0.02 2
73 . 8 LYS CG C 28.98 0.05 1
74 . 8 LYS HG2 H 1.74 0.02 1
75 . 8 LYS HG3 H 1.74 0.02 1
76 . 8 LYS CD C 25.04 0.05 1
77 . 8 LYS HD2 H 1.53 0.02 1
78 . 8 LYS HD3 H 1.53 0.02 1
79 . 8 LYS CE C 41.79 0.05 1
80 . 8 LYS HE2 H 3.03 0.02 1
81 . 8 LYS HE3 H 3.03 0.02 1
82 . 8 LYS C C 179.11 0.05 1
83 . 9 GLU N N 122.27 0.05 1
84 . 9 GLU H H 6.89 0.02 1
85 . 9 GLU CA C 58.24 0.05 1
86 . 9 GLU HA H 4.22 0.02 1
87 . 9 GLU CB C 28.5 0.05 1
88 . 9 GLU HB2 H 1.59 0.02 2
89 . 9 GLU HB3 H 1.41 0.02 2
90 . 9 GLU CG C 34.17 0.05 1
91 . 9 GLU HG2 H 2.03 0.02 2
92 . 9 GLU HG3 H 1.89 0.02 2
93 . 9 GLU C C 177.87 0.05 1
94 . 10 GLN N N 117 0.05 1
95 . 10 GLN H H 8.14 0.02 1
96 . 10 GLN CA C 59.95 0.05 1
97 . 10 GLN HA H 3.45 0.02 1
98 . 10 GLN CB C 28.84 0.05 1
99 . 10 GLN HB2 H 2.06 0.02 2
100 . 10 GLN HB3 H 2.23 0.02 2
101 . 10 GLN CG C 36.83 0.05 1
102 . 10 GLN HG2 H 1.91 0.02 2
103 . 10 GLN HG3 H 1.45 0.02 2
104 . 10 GLN NE2 N 111.69 0.05 1
105 . 10 GLN HE21 H 6.25 0.02 1
106 . 10 GLN HE22 H 6.64 0.02 1
107 . 10 GLN C C 178.64 0.05 1
108 . 11 GLU N N 120.23 0.05 1
109 . 11 GLU H H 8.37 0.02 1
110 . 11 GLU CA C 58.83 0.05 1
111 . 11 GLU HA H 3.91 0.02 1
112 . 11 GLU CB C 29.35 0.05 1
113 . 11 GLU HB2 H 2.04 0.02 1
114 . 11 GLU HB3 H 2.04 0.02 1
115 . 11 GLU CG C 36.5 0.05 1
116 . 11 GLU HG2 H 2.29 0.02 2
117 . 11 GLU HG3 H 2.47 0.02 2
118 . 11 GLU C C 179.18 0.05 1
119 . 12 ARG N N 119.89 0.05 1
120 . 12 ARG H H 7.89 0.02 1
121 . 12 ARG CA C 59.12 0.05 1
122 . 12 ARG HA H 4 0.02 1
123 . 12 ARG CB C 30.93 0.05 1
124 . 12 ARG HB2 H 1.94 0.02 1
125 . 12 ARG HB3 H 1.94 0.02 1
126 . 12 ARG CG C 27.95 0.05 1
127 . 12 ARG HG2 H 1.51 0.02 2
128 . 12 ARG HG3 H 1.63 0.02 2
129 . 12 ARG CD C 43.47 0.05 1
130 . 12 ARG HD2 H 3.1 0.02 2
131 . 12 ARG HD3 H 3.35 0.02 2
132 . 12 ARG C C 178.04 0.05 1
133 . 13 LEU N N 115.31 0.05 1
134 . 13 LEU H H 7.42 0.02 1
135 . 13 LEU CA C 54.19 0.05 1
136 . 13 LEU HA H 4.33 0.02 1
137 . 13 LEU CB C 43.46 0.05 1
138 . 13 LEU HB2 H 1.4 0.02 1
139 . 13 LEU HB3 H 1.4 0.02 1
140 . 13 LEU CG C 27.34 0.05 1
141 . 13 LEU HG H 1.43 0.02 1
142 . 13 LEU CD1 C 25.89 0.05 1
143 . 13 LEU HD1 H 0.52 0.02 1
144 . 13 LEU CD2 C 22.17 0.05 1
145 . 13 LEU HD2 H 0.71 0.02 1
146 . 13 LEU C C 177.28 0.05 1
147 . 14 GLY N N 111.24 0.05 1
148 . 14 GLY H H 7.68 0.02 1
149 . 14 GLY CA C 46.71 0.05 1
150 . 14 GLY HA2 H 4.36 0.02 2
151 . 14 GLY HA3 H 4.1 0.02 2
152 . 14 GLY C C 176.1 0.05 1
153 . 15 ILE N N 123.12 0.05 1
154 . 15 ILE H H 8.22 0.02 1
155 . 15 ILE CA C 59.01 0.05 1
156 . 15 ILE HA H 4 0.02 1
157 . 15 ILE CB C 40.33 0.05 1
158 . 15 ILE CG1 C 23.35 0.05 1
159 . 15 ILE HG12 H 1.22 0.02 1
160 . 15 ILE HG13 H 1.22 0.02 1
161 . 15 ILE CD1 C 12.69 0.05 1
162 . 15 ILE HD1 H 0.39 0.02 1
163 . 15 ILE CG2 C 15.74 0.05 1
164 . 15 ILE HG2 H 0.65 0.02 1
165 . 15 ILE C C 174.02 0.05 1
166 . 16 PRO CA C 63.04 0.05 1
167 . 16 PRO HA H 4.17 0.02 1
168 . 16 PRO CB C 32.93 0.05 1
169 . 16 PRO HB2 H 2.55 0.02 1
170 . 16 PRO HB3 H 1.95 0.02 1
171 . 16 PRO CG C 27.66 0.05 1
172 . 16 PRO HG2 H 2.16 0.02 1
173 . 16 PRO HG3 H 2.16 0.02 1
174 . 16 PRO CD C 51.06 0.05 1
175 . 16 PRO HD2 H 3.57 0.02 2
176 . 16 PRO HD3 H 4.14 0.02 2
177 . 16 PRO C C 177.1 0.05 1
178 . 17 TYR N N 122.29 0.05 1
179 . 17 TYR H H 8.23 0.02 1
180 . 17 TYR CA C 60.29 0.05 1
181 . 17 TYR HA H 4.34 0.02 1
182 . 17 TYR CB C 37.97 0.05 1
183 . 17 TYR HB2 H 2.87 0.02 1
184 . 17 TYR HB3 H 3.06 0.02 1
185 . 17 TYR CD1 C 132.13 0.05 1
186 . 17 TYR CD2 C 132.13 0.05 1
187 . 17 TYR HD1 H 7.1 0.02 1
188 . 17 TYR HD2 H 7.1 0.02 1
189 . 17 TYR CE1 C 118.25 0.05 1
190 . 17 TYR CE2 C 118.25 0.05 1
191 . 17 TYR HE1 H 6.78 0.02 1
192 . 17 TYR HE2 H 6.78 0.02 1
193 . 17 TYR C C 177.11 0.05 1
194 . 18 ASP N N 119.05 0.05 1
195 . 18 ASP H H 8.42 0.02 1
196 . 18 ASP CA C 50.74 0.05 1
197 . 18 ASP HA H 4.57 0.02 1
198 . 18 ASP CB C 42.61 0.05 1
199 . 18 ASP HB2 H 2.93 0.02 2
200 . 18 ASP HB3 H 2.39 0.02 2
201 . 18 ASP C C 174.17 0.05 1
202 . 19 PRO CA C 61.7 0.05 1
203 . 19 PRO HA H 1.05 0.02 1
204 . 19 PRO CB C 30.46 0.05 1
205 . 19 PRO HB2 H -0.32 0.02 2
206 . 19 PRO HB3 H 0.39 0.02 2
207 . 19 PRO CG C 27.11 0.05 1
208 . 19 PRO HG2 H 0.74 0.02 2
209 . 19 PRO HG3 H 1.07 0.02 2
210 . 19 PRO CD C 50.12 0.05 1
211 . 19 PRO HD2 H 3.46 0.02 1
212 . 19 PRO HD3 H 3.68 0.02 1
213 . 19 PRO C C 176.21 0.05 1
214 . 20 ILE N N 117.24 0.05 1
215 . 20 ILE H H 7.54 0.02 1
216 . 20 ILE CA C 63.79 0.05 1
217 . 20 ILE HA H 3.32 0.02 1
218 . 20 ILE CB C 37.81 0.05 1
219 . 20 ILE HB H 1.33 0.02 1
220 . 20 ILE CG1 C 29.04 0.05 1
221 . 20 ILE HG12 H 0.92 0.02 1
222 . 20 ILE HG13 H 0.92 0.02 1
223 . 20 ILE CD1 C 14.14 0.05 1
224 . 20 ILE HD1 H 0.63 0.02 1
225 . 20 ILE CG2 C 15.95 0.05 1
226 . 20 ILE HG2 H 0.17 0.02 1
227 . 20 ILE C C 177.19 0.05 1
228 . 21 HIS N N 118.18 0.05 1
229 . 21 HIS H H 7.59 0.02 1
230 . 21 HIS CA C 55.53 0.05 1
231 . 21 HIS HA H 4.75 0.02 1
232 . 21 HIS CB C 31.84 0.05 1
233 . 21 HIS HB2 H 3.49 0.02 2
234 . 21 HIS HB3 H 2.9 0.02 2
235 . 21 HIS ND1 N 233.34 0.05 1
236 . 21 HIS CD2 C 118.7 0.05 1
237 . 21 HIS HD2 H 7.05 0.02 1
238 . 21 HIS CE1 C 138.7 0.05 1
239 . 21 HIS HE1 H 7.71 0.02 1
240 . 21 HIS NE2 N 173.2 0.05 1
241 . 21 HIS C C 176.73 0.05 1
242 . 22 TRP N N 120.23 0.05 1
243 . 22 TRP H H 7.84 0.02 1
244 . 22 TRP CA C 55.48 0.05 1
245 . 22 TRP HA H 5.33 0.02 1
246 . 22 TRP CB C 30.84 0.05 1
247 . 22 TRP HB2 H 3.47 0.02 2
248 . 22 TRP HB3 H 3.26 0.02 2
249 . 22 TRP CD1 C 124.25 0.05 1
250 . 22 TRP HD1 H 6.55 0.02 1
251 . 22 TRP NE1 N 128.07 0.05 1
252 . 22 TRP HE1 H 9.87 0.02 1
253 . 22 TRP CE3 C 120.75 0.05 1
254 . 22 TRP HE3 H 7.39 0.02 1
255 . 22 TRP CZ2 C 112.87 0.05 1
256 . 22 TRP HZ2 H 7.27 0.02 1
257 . 22 TRP CZ3 C 122.25 0.05 1
258 . 22 TRP HZ3 H 6.35 0.02 1
259 . 22 TRP CH2 C 125.87 0.05 1
260 . 22 TRP HH2 H 6.18 0.02 1
261 . 22 TRP C C 178.51 0.05 1
262 . 23 SER N N 122.27 0.05 1
263 . 23 SER H H 9.33 0.02 1
264 . 23 SER CA C 56.8 0.05 1
265 . 23 SER HA H 4.94 0.02 1
266 . 23 SER CB C 65.51 0.05 1
267 . 23 SER HB3 H 4.53 0.02 1
268 . 23 SER HB2 H 4.11 0.02 1
269 . 23 SER C C 175.81 0.05 1
270 . 24 THR N N 116.12 0.05 1
271 . 24 THR H H 8.97 0.02 1
272 . 24 THR CA C 67.92 0.05 1
273 . 24 THR HA H 4.44 0.02 1
274 . 24 THR CB C 65.73 0.05 1
275 . 24 THR HB H 4.43 0.02 1
276 . 24 THR CG2 C 21.88 0.05 1
277 . 24 THR HG2 H 1.15 0.02 1
278 . 24 THR C C 176.85 0.05 1
279 . 25 ASP N N 118.6 0.05 1
280 . 25 ASP H H 8.18 0.02 1
281 . 25 ASP CA C 57.32 0.05 1
282 . 25 ASP HA H 4.46 0.02 1
283 . 25 ASP CB C 40.64 0.05 1
284 . 25 ASP HB2 H 2.66 0.02 2
285 . 25 ASP HB3 H 2.55 0.02 2
286 . 25 ASP C C 179.28 0.05 1
287 . 26 GLN N N 120.89 0.05 1
288 . 26 GLN H H 7.71 0.02 1
289 . 26 GLN CA C 58.54 0.05 1
290 . 26 GLN HA H 3.96 0.02 1
291 . 26 GLN CB C 25.95 0.05 1
292 . 26 GLN HB3 H 1.37 0.02 1
293 . 26 GLN HB2 H 2.46 0.02 1
294 . 26 GLN CG C 34.98 0.05 1
295 . 26 GLN HG2 H 2.13 0.02 2
296 . 26 GLN HG3 H 2.47 0.02 2
297 . 26 GLN NE2 N 110.12 0.05 1
298 . 26 GLN HE21 H 7.54 0.02 1
299 . 26 GLN HE22 H 6.96 0.02 1
300 . 26 GLN C C 179.82 0.05 1
301 . 27 VAL N N 127.2 0.05 1
302 . 27 VAL H H 8.79 0.02 1
303 . 27 VAL CA C 68.07 0.05 1
304 . 27 VAL HA H 4.26 0.02 1
305 . 27 VAL CB C 32.12 0.05 1
306 . 27 VAL HB H 1.47 0.02 1
307 . 27 VAL CG2 C 24.04 0.05 1
308 . 27 VAL HG2 H 0.95 0.02 1
309 . 27 VAL C C 177.93 0.05 1
310 . 28 LEU N N 118.59 0.05 1
311 . 28 LEU H H 8.21 0.02 1
312 . 28 LEU CA C 58.28 0.05 1
313 . 28 LEU HA H 4.16 0.02 1
314 . 28 LEU CB C 41.54 0.05 1
315 . 28 LEU HB3 H 1.61 0.02 1
316 . 28 LEU HB2 H 1.96 0.02 1
317 . 28 LEU CG C 27.24 0.05 1
318 . 28 LEU HG H 2.05 0.02 1
319 . 28 LEU CD1 C 25.27 0.05 1
320 . 28 LEU HD1 H 0.93 0.02 1
321 . 28 LEU CD2 C 23.68 0.05 1
322 . 28 LEU HD2 H 1.46 0.02 1
323 . 28 LEU C C 178.64 0.05 1
324 . 29 HIS N N 118.2 0.05 1
325 . 29 HIS H H 8.1 0.02 1
326 . 29 HIS CA C 60.65 0.05 1
327 . 29 HIS HA H 3.97 0.02 1
328 . 29 HIS CB C 30.63 0.05 1
329 . 29 HIS HB2 H 3.23 0.02 2
330 . 29 HIS HB3 H 3.11 0.02 2
331 . 29 HIS ND1 N 215.99 0.05 1
332 . 29 HIS CD2 C 118.9 0.05 1
333 . 29 HIS HD2 H 7.34 0.02 1
334 . 29 HIS CE1 C 138.0 0.05 1
335 . 29 HIS HE1 H 7.99 0.02 1
336 . 29 HIS NE2 N 176.29 0.05 1
337 . 29 HIS C C 177.05 0.05 1
338 . 30 TRP N N 121.65 0.05 1
339 . 30 TRP H H 7.55 0.02 1
340 . 30 TRP CA C 60.62 0.05 1
341 . 30 TRP HA H 4.16 0.02 1
342 . 30 TRP CB C 27.63 0.05 1
343 . 30 TRP HB2 H 3.76 0.02 2
344 . 30 TRP HB3 H 2.91 0.02 2
345 . 30 TRP CD1 C 126.13 0.05 1
346 . 30 TRP HD1 H 5.71 0.02 1
347 . 30 TRP NE1 N 137.32 0.05 1
348 . 30 TRP HE1 H 12.51 0.02 1
349 . 30 TRP CE3 C 121.37 0.05 1
350 . 30 TRP HE3 H 8.19 0.02 1
351 . 30 TRP CZ2 C 114.49 0.05 1
352 . 30 TRP HZ2 H 7.87 0.02 1
353 . 30 TRP CZ3 C 120.37 0.05 1
354 . 30 TRP HZ3 H 7.03 0.02 1
355 . 30 TRP CH2 C 123.37 0.05 1
356 . 30 TRP HH2 H 7.03 0.02 1
357 . 30 TRP C C 176.18 0.05 1
358 . 31 VAL N N 118.31 0.05 1
359 . 31 VAL H H 8.4 0.02 1
360 . 31 VAL CA C 66.49 0.05 1
361 . 31 VAL HA H 2.6 0.02 1
362 . 31 VAL CB C 31.75 0.05 1
363 . 31 VAL HB H 2.11 0.02 1
364 . 31 VAL CG1 C 22.63 0.05 1
365 . 31 VAL HG1 H 0.76 0.02 1
366 . 31 VAL CG2 C 24.04 0.05 1
367 . 31 VAL HG2 H 1.19 0.02 1
368 . 31 VAL C C 178.05 0.05 1
369 . 32 VAL N N 117 0.05 1
370 . 32 VAL H H 8.07 0.02 1
371 . 32 VAL CA C 66.53 0.05 1
372 . 32 VAL HA H 3.49 0.02 1
373 . 32 VAL CB C 31.53 0.05 1
374 . 32 VAL HB H 2.01 0.02 1
375 . 32 VAL CG1 C 21.38 0.05 1
376 . 32 VAL HG1 H 0.84 0.02 1
377 . 32 VAL CG2 C 23.34 0.05 1
378 . 32 VAL HG2 H 1.04 0.02 1
379 . 32 VAL C C 177.85 0.05 1
380 . 33 TRP N N 122.7 0.05 1
381 . 33 TRP H H 8.16 0.02 1
382 . 33 TRP CA C 62.77 0.05 1
383 . 33 TRP HA H 3.88 0.02 1
384 . 33 TRP CB C 29.55 0.05 1
385 . 33 TRP HB2 H 3.14 0.02 2
386 . 33 TRP HB3 H 3.52 0.02 2
387 . 33 TRP CD1 C 127.13 0.05 1
388 . 33 TRP HD1 H 7.29 0.02 1
389 . 33 TRP NE1 N 129.4 0.05 1
390 . 33 TRP HE1 H 10.21 0.02 1
391 . 33 TRP CE3 C 121.62 0.05 1
392 . 33 TRP HE3 H 7.27 0.02 1
393 . 33 TRP CZ2 C 113.87 0.05 1
394 . 33 TRP HZ2 H 7.32 0.02 1
395 . 33 TRP CZ3 C 124.25 0.05 1
396 . 33 TRP HZ3 H 7.29 0.02 1
397 . 33 TRP CH2 C 120.37 0.05 1
398 . 33 TRP HH2 H 6.71 0.02 1
399 . 33 TRP C C 178.91 0.05 1
400 . 34 VAL N N 120.64 0.05 1
401 . 34 VAL H H 8.72 0.02 1
402 . 34 VAL CA C 67.01 0.05 1
403 . 34 VAL HA H 3.21 0.02 1
404 . 34 VAL CB C 31.41 0.05 1
405 . 34 VAL HB H 1.63 0.02 1
406 . 34 VAL CG1 C 22.74 0.05 1
407 . 34 VAL HG1 H 0.63 0.02 1
408 . 34 VAL CG2 C 24.06 0.05 1
409 . 34 VAL HG2 H 0.52 0.02 1
410 . 34 VAL C C 178.2 0.05 1
411 . 35 MET N N 117.77 0.05 1
412 . 35 MET H H 8.55 0.02 1
413 . 35 MET CA C 59.71 0.05 1
414 . 35 MET HA H 3.85 0.02 1
415 . 35 MET CB C 33.16 0.05 1
416 . 35 MET HB2 H 2.15 0.02 1
417 . 35 MET HB3 H 2.15 0.02 1
418 . 35 MET CG C 31.95 0.05 1
419 . 35 MET HG2 H 2.34 0.02 2
420 . 35 MET HG3 H 2.76 0.02 2
421 . 35 MET CE C 16.73 0.05 1
422 . 35 MET HE H 1.97 0.02 1
423 . 35 MET C C 178.7 0.05 1
424 . 36 LYS N N 118.18 0.05 1
425 . 36 LYS H H 7.82 0.02 1
426 . 36 LYS CA C 58.71 0.05 1
427 . 36 LYS HA H 3.98 0.02 1
428 . 36 LYS CB C 31.86 0.05 1
429 . 36 LYS HB2 H 1.73 0.02 1
430 . 36 LYS HB3 H 1.73 0.02 1
431 . 36 LYS HG2 H 1.41 0.02 2
432 . 36 LYS HG3 H 1.26 0.02 2
433 . 36 LYS CD C 29.11 0.05 1
434 . 36 LYS HD2 H 1.54 0.02 1
435 . 36 LYS HD3 H 1.54 0.02 1
436 . 36 LYS CE C 41.8 0.05 1
437 . 36 LYS HE2 H 2.83 0.02 1
438 . 36 LYS HE3 H 2.83 0.02 1
439 . 36 LYS C C 179.54 0.05 1
440 . 37 GLU N N 121.86 0.05 1
441 . 37 GLU H H 8.17 0.02 1
442 . 37 GLU CA C 58.26 0.05 1
443 . 37 GLU HA H 3.54 0.02 1
444 . 37 GLU CB C 28.73 0.05 1
445 . 37 GLU HB2 H 1.1 0.02 2
446 . 37 GLU HB3 H 0.87 0.02 2
447 . 37 GLU CG C 34.12 0.05 1
448 . 37 GLU HG2 H 1.36 0.02 2
449 . 37 GLU HG3 H 0.8 0.02 2
450 . 37 GLU C C 177.99 0.05 1
451 . 38 PHE N N 113.6 0.05 1
452 . 38 PHE H H 7.94 0.02 1
453 . 38 PHE CA C 57.67 0.05 1
454 . 38 PHE HA H 4.49 0.02 1
455 . 38 PHE CB C 38.72 0.05 1
456 . 38 PHE HB2 H 3.38 0.02 2
457 . 38 PHE HB3 H 2.61 0.02 2
458 . 38 PHE CD1 C 132.38 0.05 1
459 . 38 PHE CD2 C 132.38 0.05 1
460 . 38 PHE HD1 H 7.41 0.02 1
461 . 38 PHE HD2 H 7.41 0.02 1
462 . 38 PHE CE1 C 130.63 0.05 1
463 . 38 PHE CE2 C 130.63 0.05 1
464 . 38 PHE HE1 H 7.2 0.02 1
465 . 38 PHE HE2 H 7.2 0.02 1
466 . 38 PHE C C 174.21 0.05 1
467 . 39 SER N N 114.91 0.05 1
468 . 39 SER H H 7.5 0.02 1
469 . 39 SER CA C 58.68 0.05 1
470 . 39 SER HA H 4.03 0.02 1
471 . 39 SER CB C 61.13 0.05 1
472 . 39 SER HB2 H 4.46 0.02 1
473 . 39 SER HB3 H 4.46 0.02 1
474 . 39 SER C C 174.19 0.05 1
475 . 40 MET N N 119 0.05 1
476 . 40 MET H H 8.7 0.02 1
477 . 40 MET CA C 55.17 0.05 1
478 . 40 MET HA H 4.58 0.02 1
479 . 40 MET CB C 35.25 0.05 1
480 . 40 MET HB2 H 1.74 0.02 2
481 . 40 MET HB3 H 2.19 0.02 2
482 . 40 MET CG C 31.81 0.05 1
483 . 40 MET HG2 H 2.45 0.02 2
484 . 40 MET HG3 H 2.54 0.02 2
485 . 40 MET CE C 17.16 0.05 1
486 . 40 MET HE H 2.01 0.02 1
487 . 40 MET C C 176.04 0.05 1
488 . 41 THR N N 111.24 0.05 1
489 . 41 THR H H 8.18 0.02 1
490 . 41 THR CA C 61.06 0.05 1
491 . 41 THR HA H 4.42 0.02 1
492 . 41 THR CB C 70.54 0.05 1
493 . 41 THR HB H 4.25 0.02 1
494 . 41 THR CG2 C 21.26 0.05 1
495 . 41 THR HG2 H 1.1 0.02 1
496 . 41 THR C C 174.26 0.05 1
497 . 42 ASP N N 119 0.05 1
498 . 42 ASP H H 8.39 0.02 1
499 . 42 ASP CA C 54.89 0.05 1
500 . 42 ASP HA H 4.45 0.02 1
501 . 42 ASP CB C 39.95 0.05 1
502 . 42 ASP HB2 H 2.72 0.02 2
503 . 42 ASP HB3 H 2.63 0.02 2
504 . 42 ASP C C 174.83 0.05 1
505 . 43 ILE N N 118.59 0.05 1
506 . 43 ILE H H 7.19 0.02 1
507 . 43 ILE CA C 59.46 0.05 1
508 . 43 ILE HA H 4.1 0.02 1
509 . 43 ILE CB C 39.32 0.05 1
510 . 43 ILE HB H 1.74 0.02 1
511 . 43 ILE CG1 C 26.99 0.05 1
512 . 43 ILE HG12 H 1.23 0.02 1
513 . 43 ILE HG13 H 1.07 0.02 1
514 . 43 ILE CD1 C 12 0.05 1
515 . 43 ILE HD1 H 0.64 0.02 1
516 . 43 ILE CG2 C 16.93 0.05 1
517 . 43 ILE HG2 H 0.6 0.02 1
518 . 43 ILE C C 174.56 0.05 1
519 . 44 ASP N N 125.56 0.05 1
520 . 44 ASP H H 8.36 0.02 1
521 . 44 ASP CA C 52.7 0.05 1
522 . 44 ASP HA H 4.67 0.02 1
523 . 44 ASP CB C 40.62 0.05 1
524 . 44 ASP HB2 H 2.96 0.02 2
525 . 44 ASP HB3 H 2.61 0.02 2
526 . 44 ASP C C 176.66 0.05 1
527 . 45 LEU N N 126.78 0.05 1
528 . 45 LEU H H 8.65 0.02 1
529 . 45 LEU CA C 56.89 0.05 1
530 . 45 LEU HA H 3.97 0.02 1
531 . 45 LEU CB C 41.42 0.05 1
532 . 45 LEU HB2 H 1.59 0.02 2
533 . 45 LEU HB3 H 1.74 0.02 2
534 . 45 LEU CG C 27.15 0.05 1
535 . 45 LEU HG H 0.72 0.02 1
536 . 45 LEU CD1 C 25.2 0.05 1
537 . 45 LEU HD1 H 0.88 0.02 1
538 . 45 LEU CD2 C 23.55 0.05 1
539 . 45 LEU HD2 H 0.77 0.02 1
540 . 45 LEU C C 179.03 0.05 1
541 . 46 THR N N 111.35 0.05 1
542 . 46 THR H H 8.42 0.02 1
543 . 46 THR CA C 68.88 0.05 1
544 . 46 THR HA H 4.03 0.02 1
545 . 46 THR CB C 65.43 0.05 1
546 . 46 THR HB H 4.25 0.02 1
547 . 46 THR CG2 C 21.51 0.05 1
548 . 46 THR HG2 H 1.33 0.02 1
549 . 46 THR C C 176.95 0.05 1
550 . 47 THR N N 110.44 0.05 1
551 . 47 THR H H 7.43 0.02 1
552 . 47 THR CA C 68.93 0.05 1
553 . 47 THR HA H 4.32 0.02 1
554 . 47 THR CB C 62.52 0.05 1
555 . 47 THR HB H 4.06 0.02 1
556 . 47 THR CG2 C 22.09 0.05 1
557 . 47 THR HG2 H 1.25 0.02 1
558 . 47 THR C C 174.53 0.05 1
559 . 48 LEU N N 122.26 0.05 1
560 . 48 LEU H H 7.27 0.02 1
561 . 48 LEU CA C 53.97 0.05 1
562 . 48 LEU HA H 4.5 0.02 1
563 . 48 LEU CB C 42.41 0.05 1
564 . 48 LEU HB2 H 2.1 0.02 2
565 . 48 LEU HB3 H 1.4 0.02 2
566 . 48 LEU CG C 26.44 0.05 1
567 . 48 LEU HG H 0.84 0.02 1
568 . 48 LEU HD1 H 1.57 0.02 1
569 . 48 LEU CD2 C 23.02 0.05 1
570 . 48 LEU HD2 H 0.82 0.02 1
571 . 48 LEU C C 174.43 0.05 1
572 . 49 ASN N N 120.23 0.05 1
573 . 49 ASN H H 7.54 0.02 1
574 . 49 ASN CA C 52.09 0.05 1
575 . 49 ASN HA H 4.87 0.02 1
576 . 49 ASN CB C 37.12 0.05 1
577 . 49 ASN HB2 H 2.94 0.02 2
578 . 49 ASN HB3 H 2.61 0.02 2
579 . 49 ASN CG C 177.2 0.05 1
580 . 49 ASN ND2 N 109.59 0.05 1
581 . 49 ASN HD21 H 7.34 0.02 1
582 . 49 ASN HD22 H 6.65 0.02 1
583 . 49 ASN C C 174.66 0.05 1
584 . 50 ILE N N 116.54 0.05 1
585 . 50 ILE H H 8.12 0.02 1
586 . 50 ILE CA C 59.24 0.05 1
587 . 50 ILE HA H 4.68 0.02 1
588 . 50 ILE CB C 41.69 0.05 1
589 . 50 ILE HB H 1.65 0.02 1
590 . 50 ILE CG1 C 24.76 0.05 1
591 . 50 ILE HG12 H 2.01 0.02 2
592 . 50 ILE HG13 H 1.55 0.02 2
593 . 50 ILE CD1 C 12.5 0.05 1
594 . 50 ILE HD1 H 1 0.02 1
595 . 50 ILE CG2 C 17.5 0.05 1
596 . 50 ILE HG2 H 0.84 0.02 1
597 . 50 ILE C C 172.67 0.05 1
598 . 51 SER N N 114.09 0.05 1
599 . 51 SER H H 8.45 0.02 1
600 . 51 SER CA C 57.74 0.05 1
601 . 51 SER HA H 4.21 0.02 1
602 . 51 SER CB C 65.67 0.05 1
603 . 51 SER HB2 H 4.39 0.02 1
604 . 51 SER HB3 H 4.39 0.02 1
605 . 51 SER C C 175.47 0.05 1
606 . 52 GLY N N 108.77 0.05 1
607 . 52 GLY H H 8.61 0.02 1
608 . 52 GLY CA C 47.93 0.05 1
609 . 52 GLY HA2 H 4.52 0.02 2
610 . 52 GLY HA3 H 3.57 0.02 2
611 . 52 GLY C C 175.89 0.05 1
612 . 53 ARG N N 121.87 0.05 1
613 . 53 ARG H H 8.19 0.02 1
614 . 53 ARG CA C 59.62 0.05 1
615 . 53 ARG HA H 3.85 0.02 1
616 . 53 ARG CB C 29.8 0.05 1
617 . 53 ARG HB2 H 1.92 0.02 2
618 . 53 ARG HB3 H 1.77 0.02 2
619 . 53 ARG CG C 26.96 0.05 1
620 . 53 ARG HG2 H 1.59 0.02 1
621 . 53 ARG HG3 H 1.59 0.02 1
622 . 53 ARG CD C 43.06 0.05 1
623 . 53 ARG HD2 H 3.52 0.02 2
624 . 53 ARG HD3 H 3.18 0.02 2
625 . 53 ARG C C 178.91 0.05 1
626 . 54 GLU N N 120.23 0.05 1
627 . 54 GLU H H 7.47 0.02 1
628 . 54 GLU CA C 59.28 0.05 1
629 . 54 GLU HA H 3.94 0.02 1
630 . 54 GLU CB C 29.97 0.05 1
631 . 54 GLU HB2 H 2.27 0.02 2
632 . 54 GLU HB3 H 2.04 0.02 2
633 . 54 GLU HG2 H 2.26 0.02 1
634 . 54 GLU HG3 H 2.26 0.02 1
635 . 54 GLU CG C 37.12 0.05 1
636 . 54 GLU C C 179.76 0.05 1
637 . 55 LEU N N 122.69 0.05 1
638 . 55 LEU H H 8.86 0.02 1
639 . 55 LEU CA C 58.54 0.05 1
640 . 55 LEU HA H 3.98 0.02 1
641 . 55 LEU CB C 42.94 0.05 1
642 . 55 LEU HB2 H 2.2 0.02 2
643 . 55 LEU HB3 H 1.58 0.02 2
644 . 55 LEU CG C 27.11 0.05 1
645 . 55 LEU HG H 1.01 0.02 1
646 . 55 LEU CD1 C 23.43 0.05 1
647 . 55 LEU HD1 H 1.22 0.02 1
648 . 55 LEU CD2 C 23 0.05 1
649 . 55 LEU HD2 H 0.85 0.02 1
650 . 55 LEU C C 178.61 0.05 1
651 . 56 CYS N N 112.37 0.05 1
652 . 56 CYS H H 8.12 0.02 1
653 . 56 CYS CA C 62.74 0.05 1
654 . 56 CYS HA H 4.04 0.02 1
655 . 56 CYS CB C 27.81 0.05 1
656 . 56 CYS HB2 H 2.68 0.02 2
657 . 56 CYS HB3 H 2.78 0.02 2
658 . 56 CYS C C 174.08 0.05 1
659 . 57 SER N N 114.49 0.05 1
660 . 57 SER H H 7.5 0.02 1
661 . 57 SER CA C 58.94 0.05 1
662 . 57 SER HA H 4.48 0.02 1
663 . 57 SER CB C 63.97 0.05 1
664 . 57 SER HB2 H 4 0.02 2
665 . 57 SER HB3 H 4.16 0.02 2
666 . 57 SER C C 174.07 0.05 1
667 . 58 LEU N N 121.87 0.05 1
668 . 58 LEU H H 7.08 0.02 1
669 . 58 LEU CA C 54.92 0.05 1
670 . 58 LEU HA H 4.56 0.02 1
671 . 58 LEU CB C 42.68 0.05 1
672 . 58 LEU HB2 H 2.21 0.02 2
673 . 58 LEU HB3 H 1.59 0.02 2
674 . 58 LEU CG C 26.52 0.05 1
675 . 58 LEU HG H 0.98 0.02 1
676 . 58 LEU CD2 C 22.85 0.05 1
677 . 58 LEU HD2 H 0.86 0.02 1
678 . 58 LEU C C 177.54 0.05 1
679 . 59 ASN N N 121.45 0.05 1
680 . 59 ASN H H 8.93 0.02 1
681 . 59 ASN CA C 51.42 0.05 1
682 . 59 ASN HA H 4.91 0.02 1
683 . 59 ASN CB C 38.56 0.05 1
684 . 59 ASN HB2 H 2.95 0.02 2
685 . 59 ASN HB3 H 3.17 0.02 2
686 . 59 ASN CG C 175.4 0.05 1
687 . 59 ASN ND2 N 110.97 0.05 1
688 . 59 ASN HD21 H 7.41 0.02 1
689 . 59 ASN HD22 H 6.82 0.02 1
690 . 59 ASN C C 174.86 0.05 1
691 . 60 GLN N N 119.82 0.05 1
692 . 60 GLN H H 8.46 0.02 1
693 . 60 GLN CA C 59.81 0.05 1
694 . 60 GLN HA H 2.25 0.02 1
695 . 60 GLN CB C 28.7 0.05 1
696 . 60 GLN HB2 H 1.51 0.02 2
697 . 60 GLN HB3 H 2.25 0.02 2
698 . 60 GLN CG C 33.49 0.05 1
699 . 60 GLN HG2 H 1.37 0.02 2
700 . 60 GLN HG3 H 0.74 0.02 2
701 . 60 GLN CD C 179.61 0.05 1
702 . 60 GLN NE2 N 110.41 0.05 1
703 . 60 GLN HE21 H 6.27 0.02 1
704 . 60 GLN HE22 H 6.73 0.02 1
705 . 60 GLN C C 176.85 0.05 1
706 . 61 GLU N N 117.36 0.05 1
707 . 61 GLU H H 8.19 0.02 1
708 . 61 GLU CA C 59.8 0.05 1
709 . 61 GLU HA H 3.84 0.02 1
710 . 61 GLU CB C 28.84 0.05 1
711 . 61 GLU HB2 H 1.95 0.02 2
712 . 61 GLU HB3 H 2.22 0.02 2
713 . 61 GLU CG C 36.61 0.05 1
714 . 61 GLU HG2 H 2.26 0.02 1
715 . 61 GLU HG3 H 2.26 0.02 1
716 . 61 GLU C C 179.45 0.05 1
717 . 62 ASP N N 120.23 0.05 1
718 . 62 ASP H H 8.31 0.02 1
719 . 62 ASP CA C 56.82 0.05 1
720 . 62 ASP HA H 4.38 0.02 1
721 . 62 ASP CB C 41.1 0.05 1
722 . 62 ASP HB2 H 2.67 0.02 2
723 . 62 ASP HB3 H 2.8 0.02 2
724 . 62 ASP C C 179.33 0.05 1
725 . 63 PHE N N 122.6 0.05 1
726 . 63 PHE H H 8.72 0.02 1
727 . 63 PHE CA C 62.78 0.05 1
728 . 63 PHE HA H 3.89 0.02 1
729 . 63 PHE CB C 39.58 0.05 1
730 . 63 PHE HB2 H 2.94 0.02 2
731 . 63 PHE HB3 H 2.84 0.02 2
732 . 63 PHE CD1 C 132.25 0.05 1
733 . 63 PHE CD2 C 132.25 0.05 1
734 . 63 PHE HD1 H 6.95 0.02 1
735 . 63 PHE HD2 H 6.95 0.02 1
736 . 63 PHE CE1 C 131.3 0.05 1
737 . 63 PHE CE2 C 131.3 0.05 1
738 . 63 PHE HE1 H 7.4 0.02 1
739 . 63 PHE HE2 H 7.4 0.02 1
740 . 63 PHE CZ C 128.38 0.05 1
741 . 63 PHE HZ H 7.32 0.02 1
742 . 63 PHE C C 177.16 0.05 1
743 . 64 PHE N N 116.54 0.05 1
744 . 64 PHE H H 8.35 0.02 1
745 . 64 PHE CA C 59.11 0.05 1
746 . 64 PHE HA H 4.39 0.02 1
747 . 64 PHE CB C 37.8 0.05 1
748 . 64 PHE HB2 H 3.04 0.02 2
749 . 64 PHE HB3 H 3.21 0.02 2
750 . 64 PHE CD1 C 130.8 0.05 1
751 . 64 PHE CD2 C 130.8 0.05 1
752 . 64 PHE HD1 H 7.41 0.02 1
753 . 64 PHE HD2 H 7.41 0.02 1
754 . 64 PHE CE1 C 130.4 0.05 1
755 . 64 PHE CE2 C 130.4 0.05 1
756 . 64 PHE HE1 H 7.04 0.02 1
757 . 64 PHE HE2 H 7.04 0.02 1
758 . 64 PHE CZ C 128.75 0.05 1
759 . 64 PHE HZ H 7.17 0.02 1
760 . 64 PHE C C 177.86 0.05 1
761 . 65 GLN N N 117.77 0.05 1
762 . 65 GLN H H 7.63 0.02 1
763 . 65 GLN CA C 58.25 0.05 1
764 . 65 GLN HA H 4.11 0.02 1
765 . 65 GLN CB C 28.78 0.05 1
766 . 65 GLN HB2 H 2.22 0.02 1
767 . 65 GLN HB3 H 2.22 0.02 1
768 . 65 GLN CG C 34.07 0.05 1
769 . 65 GLN HG2 H 2.44 0.02 2
770 . 65 GLN HG3 H 2.56 0.02 2
771 . 65 GLN CD C 180.25 0.05 1
772 . 65 GLN NE2 N 111.66 0.05 1
773 . 65 GLN HE21 H 7.46 0.02 1
774 . 65 GLN HE22 H 6.78 0.02 1
775 . 65 GLN C C 177.61 0.05 1
776 . 66 ARG N N 117.77 0.05 1
777 . 66 ARG H H 7.34 0.02 1
778 . 66 ARG CA C 57.96 0.05 1
779 . 66 ARG HA H 4.14 0.02 1
780 . 66 ARG CB C 31.16 0.05 1
781 . 66 ARG HB2 H 2.15 0.02 2
782 . 66 ARG HB3 H 1.75 0.02 2
783 . 66 ARG CG C 28.03 0.05 1
784 . 66 ARG HG2 H 1.65 0.02 1
785 . 66 ARG HG3 H 1.65 0.02 1
786 . 66 ARG CD C 43.17 0.05 1
787 . 66 ARG HD2 H 3.08 0.02 1
788 . 66 ARG HD3 H 3.08 0.02 1
789 . 66 ARG C C 176.4 0.05 1
790 . 67 VAL N N 118.6 0.05 1
791 . 67 VAL H H 8.18 0.02 1
792 . 67 VAL CA C 65.71 0.05 1
793 . 67 VAL HA H 4.23 0.02 1
794 . 67 VAL CB C 31.3 0.05 1
795 . 67 VAL HB H 1.67 0.02 1
796 . 67 VAL CG1 C 19.74 0.05 1
797 . 67 VAL HG1 H 0.34 0.02 1
798 . 67 VAL CG2 C 22.33 0.05 1
799 . 67 VAL HG2 H 0.69 0.02 1
800 . 68 PRO CA C 64.52 0.05 1
801 . 68 PRO HA H 4.62 0.02 1
802 . 68 PRO CB C 31.97 0.05 1
803 . 68 PRO HB2 H 2.37 0.02 2
804 . 68 PRO HB3 H 1.84 0.02 2
805 . 68 PRO CG C 27.46 0.05 1
806 . 68 PRO HG2 H 2.02 0.02 1
807 . 68 PRO HG3 H 2.02 0.02 1
808 . 68 PRO CD C 49.97 0.05 1
809 . 68 PRO HD2 H 3.38 0.02 2
810 . 68 PRO HD3 H 3.58 0.02 2
811 . 68 PRO C C 178.22 0.05 1
812 . 69 ARG N N 115.31 0.05 1
813 . 69 ARG H H 8.47 0.02 1
814 . 69 ARG CA C 55.28 0.05 1
815 . 69 ARG HA H 4.58 0.02 1
816 . 69 ARG CB C 27.15 0.05 1
817 . 69 ARG HB3 H 1.8 0.02 1
818 . 69 ARG HB2 H 2.14 0.02 1
819 . 69 ARG CG C 27.1 0.05 1
820 . 69 ARG HG2 H 1.64 0.02 1
821 . 69 ARG HG3 H 1.64 0.02 1
822 . 69 ARG CD C 43.09 0.05 1
823 . 69 ARG HD2 H 3.26 0.02 2
824 . 69 ARG HD3 H 2 0.02 2
825 . 69 ARG C C 177.96 0.05 1
826 . 70 GLY N N 127.62 0.05 1
827 . 70 GLY H H 7.95 0.02 1
828 . 70 GLY CA C 47.17 0.05 1
829 . 70 GLY HA2 H 4.12 0.02 2
830 . 70 GLY HA3 H 3.66 0.02 2
831 . 70 GLY C C 174.85 0.05 1
832 . 71 GLU N N 124.7 0.05 1
833 . 71 GLU H H 9.49 0.02 1
834 . 71 GLU CA C 61.79 0.05 1
835 . 71 GLU HA H 4.22 0.02 1
836 . 71 GLU CB C 28.79 0.05 1
837 . 71 GLU HB3 H 2.1 0.02 1
838 . 71 GLU HB2 H 2.18 0.02 1
839 . 71 GLU CG C 36.36 0.05 1
840 . 71 GLU HG2 H 2.39 0.02 1
841 . 71 GLU HG3 H 2.39 0.02 1
842 . 71 GLU C C 178.72 0.05 1
843 . 72 ILE N N 119.41 0.05 1
844 . 72 ILE H H 8.88 0.02 1
845 . 72 ILE CA C 64.2 0.05 1
846 . 72 ILE HA H 3.8 0.02 1
847 . 72 ILE CB C 37.55 0.05 1
848 . 72 ILE HB H 1.66 0.02 1
849 . 72 ILE CG1 C 29.06 0.05 1
850 . 72 ILE HG12 H 1.48 0.02 2
851 . 72 ILE HG13 H 0.98 0.02 2
852 . 72 ILE CD1 C 17.2 0.05 1
853 . 72 ILE HD1 H 0.33 0.02 1
854 . 72 ILE CG2 C 12.9 0.05 1
855 . 72 ILE HG2 H 0.75 0.02 1
856 . 72 ILE C C 178.35 0.05 1
857 . 73 LEU N N 119.41 0.05 1
858 . 73 LEU H H 7.08 0.02 1
859 . 73 LEU CA C 58.33 0.05 1
860 . 73 LEU HA H 4.1 0.02 1
861 . 73 LEU CB C 42.31 0.05 1
862 . 73 LEU HB3 H 1.99 0.02 1
863 . 73 LEU HB2 H 2.17 0.02 1
864 . 73 LEU CG C 28.03 0.05 1
865 . 73 LEU HG H 1.5 0.02 1
866 . 73 LEU CD1 C 26.54 0.05 1
867 . 73 LEU HD1 H 0.79 0.02 1
868 . 73 LEU CD2 C 24.02 0.05 1
869 . 73 LEU HD2 H 0.38 0.02 1
870 . 73 LEU C C 177.81 0.05 1
871 . 74 TRP N N 119.4 0.05 1
872 . 74 TRP H H 8.46 0.02 1
873 . 74 TRP CA C 60.26 0.05 1
874 . 74 TRP HA H 3.77 0.02 1
875 . 74 TRP CB C 30 0.05 1
876 . 74 TRP HB2 H 3.11 0.02 2
877 . 74 TRP HB3 H 3.33 0.02 2
878 . 74 TRP CD1 C 126.88 0.05 1
879 . 74 TRP HD1 H 7.22 0.02 1
880 . 74 TRP NE1 N 128.88 0.05 1
881 . 74 TRP HE1 H 9.98 0.02 1
882 . 74 TRP CE3 C 119.75 0.05 1
883 . 74 TRP HE3 H 5.99 0.02 1
884 . 74 TRP CZ2 C 113.99 0.05 1
885 . 74 TRP HZ2 H 7.37 0.02 1
886 . 74 TRP CZ3 C 122 0.05 1
887 . 74 TRP HZ3 H 6.71 0.02 1
888 . 74 TRP CH2 C 124.37 0.05 1
889 . 74 TRP HH2 H 7.08 0.02 1
890 . 74 TRP C C 177.59 0.05 1
891 . 75 SER N N 112.04 0.05 1
892 . 75 SER H H 8.25 0.02 1
893 . 75 SER CA C 61.63 0.05 1
894 . 75 SER HA H 4.09 0.02 1
895 . 75 SER CB C 62.66 0.05 1
896 . 75 SER C C 176.68 0.05 1
897 . 76 HIS N N 123.5 0.05 1
898 . 76 HIS H H 8.17 0.02 1
899 . 76 HIS CA C 61.77 0.05 1
900 . 76 HIS HA H 4.34 0.02 1
901 . 76 HIS CB C 32.17 0.05 1
902 . 76 HIS HB3 H 3.37 0.02 1
903 . 76 HIS HB2 H 3.54 0.02 1
904 . 76 HIS ND1 N 256.08 0.05 1
905 . 76 HIS CD2 C 116.8 0.05 1
906 . 76 HIS HD2 H 7.3 0.02 1
907 . 76 HIS CE1 C 135.8 0.05 1
908 . 76 HIS HE1 H 7.29 0.02 1
909 . 76 HIS NE2 N 165.88 0.05 1
910 . 76 HIS HE2 H 13.12 0.02 1
911 . 76 HIS C C 176.93 0.05 1
912 . 77 LEU N N 120.64 0.05 1
913 . 77 LEU H H 8.62 0.02 1
914 . 77 LEU CA C 57.78 0.05 1
915 . 77 LEU HA H 3.69 0.02 1
916 . 77 LEU CB C 40.76 0.05 1
917 . 77 LEU HB2 H 1.69 0.02 2
918 . 77 LEU HB3 H 1.58 0.02 2
919 . 77 LEU HG H 0.99 0.02 1
920 . 77 LEU CD1 C 21.52 0.05 1
921 . 77 LEU HD1 H 0.04 0.02 1
922 . 77 LEU CD2 C 25.72 0.05 1
923 . 77 LEU HD2 H 0.46 0.02 1
924 . 77 LEU C C 178.38 0.05 1
925 . 78 GLU N N 117.18 0.05 1
926 . 78 GLU H H 7.79 0.02 1
927 . 78 GLU CA C 59.17 0.05 1
928 . 78 GLU HA H 3.51 0.02 1
929 . 78 GLU CB C 29.75 0.05 1
930 . 78 GLU HB2 H 1.74 0.02 2
931 . 78 GLU HB3 H 1.96 0.02 2
932 . 78 GLU CG C 36.47 0.05 1
933 . 78 GLU HG2 H 1.5 0.02 2
934 . 78 GLU HG3 H 1.78 0.02 2
935 . 78 GLU C C 179.06 0.05 1
936 . 79 LEU N N 119.77 0.05 1
937 . 79 LEU H H 7.36 0.02 1
938 . 79 LEU CA C 57.89 0.05 1
939 . 79 LEU HA H 3.97 0.02 1
940 . 79 LEU CB C 41.97 0.05 1
941 . 79 LEU HB3 H 1.71 0.02 1
942 . 79 LEU HB2 H 1.89 0.02 1
943 . 79 LEU CG C 26.54 0.05 1
944 . 79 LEU HG H 0.99 0.02 1
945 . 79 LEU CD1 C 24.93 0.05 1
946 . 79 LEU CD2 C 24.23 0.05 1
947 . 79 LEU C C 179.3 0.05 1
948 . 80 LEU N N 118.99 0.05 1
949 . 80 LEU H H 8.13 0.02 1
950 . 80 LEU CA C 57.56 0.05 1
951 . 80 LEU HA H 3.94 0.02 1
952 . 80 LEU CB C 42.2 0.05 1
953 . 80 LEU HB3 H 1.2 0.02 1
954 . 80 LEU HB2 H 1.78 0.02 1
955 . 80 LEU CG C 27.94 0.05 1
956 . 80 LEU HG H 1.63 0.02 1
957 . 80 LEU CD1 C 27.05 0.05 1
958 . 80 LEU HD1 H 0.73 0.02 1
959 . 80 LEU CD2 C 22.9 0.05 1
960 . 80 LEU HD2 H 0.93 0.02 1
961 . 80 LEU C C 180.36 0.05 1
962 . 81 ARG N N 116.13 0.05 1
963 . 81 ARG H H 8.14 0.02 1
964 . 81 ARG CA C 57.64 0.05 1
965 . 81 ARG HA H 3.74 0.02 1
966 . 81 ARG CB C 30.23 0.05 1
967 . 81 ARG HB3 H 1.71 0.02 1
968 . 81 ARG HB2 H 1.63 0.02 1
969 . 81 ARG CG C 27.54 0.05 1
970 . 81 ARG HG2 H 1.11 0.02 2
971 . 81 ARG HG3 H 1.81 0.02 2
972 . 81 ARG CD C 43.62 0.05 1
973 . 81 ARG HD2 H 2.81 0.02 1
974 . 81 ARG HD3 H 2.81 0.02 1
975 . 81 ARG C C 178.13 0.05 1
976 . 82 LYS N N 119.8 0.05 1
977 . 82 LYS H H 7.84 0.02 1
978 . 82 LYS CA C 58.28 0.05 1
979 . 82 LYS HA H 4.02 0.02 1
980 . 82 LYS CB C 32.36 0.05 1
981 . 82 LYS HB2 H 1.77 0.02 1
982 . 82 LYS HB3 H 1.77 0.02 1
983 . 82 LYS CG C 29.33 0.05 1
984 . 82 LYS HG2 H 1.56 0.02 1
985 . 82 LYS HG3 H 1.56 0.02 1
986 . 82 LYS CD C 25.36 0.05 1
987 . 82 LYS HD2 H 1.23 0.02 2
988 . 82 LYS HD3 H 1.43 0.02 2
989 . 82 LYS HE2 H 2.87 0.02 1
990 . 82 LYS HE3 H 2.87 0.02 1
991 . 82 LYS C C 178.15 0.05 1
992 . 83 TYR N N 119 0.05 1
993 . 83 TYR H H 7.72 0.02 1
994 . 83 TYR CA C 59.41 0.05 1
995 . 83 TYR HA H 4.33 0.02 1
996 . 83 TYR CB C 38.3 0.05 1
997 . 83 TYR HB2 H 3.01 0.02 2
998 . 83 TYR HB3 H 3.09 0.02 2
999 . 83 TYR CD1 C 133 0.05 1
1000 . 83 TYR CD2 C 133 0.05 1
1001 . 83 TYR HD1 H 7.12 0.02 1
1002 . 83 TYR HD2 H 7.12 0.02 1
1003 . 83 TYR CE1 C 117.87 0.05 1
1004 . 83 TYR CE2 C 117.87 0.05 1
1005 . 83 TYR HE1 H 6.69 0.02 1
1006 . 83 TYR HE2 H 6.69 0.02 1
1007 . 83 TYR C C 176.88 0.05 1
1008 . 84 VAL N N 116.95 0.05 1
1009 . 84 VAL H H 7.32 0.02 1
1010 . 84 VAL CA C 63.23 0.05 1
1011 . 84 VAL HA H 3.94 0.02 1
1012 . 84 VAL CB C 32.16 0.05 1
1013 . 84 VAL HB H 2.15 0.02 1
1014 . 84 VAL CG1 C 21.27 0.05 1
1015 . 84 VAL HG1 H 0.92 0.02 1
1016 . 84 VAL HG2 H 0.88 0.02 1
1017 . 84 VAL C C 176.33 0.05 1
1018 . 85 LEU N N 122.69 0.05 1
1019 . 85 LEU H H 7.62 0.02 1
1020 . 85 LEU CA C 55.43 0.05 1
1021 . 85 LEU HA H 4.24 0.02 1
1022 . 85 LEU CB C 42.36 0.05 1
1023 . 85 LEU HB2 H 2.27 0.02 2
1024 . 85 LEU HB3 H 1.58 0.02 2
1025 . 85 LEU CG C 26.77 0.05 1
1026 . 85 LEU HG H 0.86 0.02 1
1027 . 85 LEU CD1 C 24.9 0.05 1
1028 . 85 LEU HD1 H 0.9 0.02 1
1029 . 85 LEU CD2 C 23.4 0.05 1
1030 . 85 LEU HD2 H 0.86 0.02 1
1031 . 85 LEU C C 176.87 0.05 1
1032 . 86 ALA N N 124.32 0.05 1
1033 . 86 ALA H H 7.87 0.02 1
1034 . 86 ALA CA C 52.31 0.05 1
1035 . 86 ALA HA H 4.35 0.02 1
1036 . 86 ALA CB C 19.28 0.05 1
1037 . 86 ALA HB H 1.36 0.02 1
1038 . 86 ALA C C 176.55 0.05 1
1039 . 87 SER N N 120.67 0.05 1
1040 . 87 SER H H 7.72 0.02 1
1041 . 87 SER CA C 59.88 0.05 1
1042 . 87 SER HA H 4.21 0.02 1
1043 . 87 SER CB C 64.82 0.05 1
1044 . 87 SER HB2 H 4.21 0.02 2
1045 . 87 SER HB3 H 3.74 0.02 2
1046 . 87 SER C C 178.63 0.05 1
stop_
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