data_6177
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
N-terminal Domain of the Polypyrimidine Tract Binding Protein Contains a New RRM Variant That Contributes to High-Affinity RNA Binding
;
_BMRB_accession_number 6177
_BMRB_flat_file_name bmr6177.str
_Entry_type original
_Submission_date 2004-04-14
_Accession_date 2004-04-15
_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 Simpson P. J. .
2 Monie T. P. .
3 Szendroi A. . .
4 Davydova N. . .
5 Tyzack J. K. .
6 Conte M. R. .
7 Read C. M. .
8 Cary P. D. .
9 Svergun D. V. .
10 'V Konarev' P. . .
11 V. 'Petoukhov M.' . .
12 Curry S. . .
13 Matthews S. J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 642
"13C chemical shifts" 489
"15N chemical shifts" 115
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2004-11-08 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
6178 'Polypyrimidine tract-binding protein 1 domain 1'
stop_
_Original_release_date 2004-11-08
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Structure and RNA interactions of the N-terminal RRM domains of PTB'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15341728
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Simpson P. J. .
2 Monie T. P. .
3 Szendroi A. . .
4 Davydova N. . .
5 Tyzack J. K. .
6 Conte M. R. .
7 Read C. M. .
8 Cary P. D. .
9 Svergun D. I. .
10 Konarev P. V. .
11 Curry S. . .
12 Matthews S. J. .
stop_
_Journal_abbreviation 'Structure (Camb)'
_Journal_volume 12
_Journal_issue 9
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1631
_Page_last 1643
_Year 2004
_Details .
loop_
_Keyword
'extended BABBAB motif'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_PTB1-2
_Saveframe_category molecular_system
_Mol_system_name 'Polypyrimidine tract-binding protein 1 domain 2'
_Abbreviation_common PTB1-2
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'PTB1-2 monomer' $PTB1-2
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
'RNA binding protein'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_PTB1-2
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'polypyrimidine tract binding protein 1 domain 2'
_Abbreviation_common 'PTB1 RRM2'
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 164
_Mol_residue_sequence
;
MHHHHHHGSAQAALQAVNSV
QSGNLALAASAAAVDAGMAM
AGQSPVLRIIVENLFYPVTL
DVLHQIFSKFGTVLKIITFT
KNNQFQALLQYADPVSAQHA
KLSLDGQNIYNACCTLRIDF
SKLTSLNVKYNNDKSRDYTR
PDLPSGDSQPSLDQTMAAAF
GLSV
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 -35 MET 2 -34 HIS 3 -33 HIS 4 -32 HIS 5 -31 HIS
6 -30 HIS 7 -29 HIS 8 -28 GLY 9 -27 SER 10 -26 ALA
11 -25 GLN 12 -24 ALA 13 -23 ALA 14 -22 LEU 15 -21 GLN
16 -20 ALA 17 -19 VAL 18 -18 ASN 19 -17 SER 20 -16 VAL
21 -15 GLN 22 -14 SER 23 -13 GLY 24 -12 ASN 25 -11 LEU
26 -10 ALA 27 -9 LEU 28 -8 ALA 29 -7 ALA 30 -6 SER
31 -5 ALA 32 -4 ALA 33 -3 ALA 34 -2 VAL 35 -1 ASP
36 1 ALA 37 2 GLY 38 3 MET 39 4 ALA 40 5 MET
41 6 ALA 42 7 GLY 43 8 GLN 44 9 SER 45 10 PRO
46 11 VAL 47 12 LEU 48 13 ARG 49 14 ILE 50 15 ILE
51 16 VAL 52 17 GLU 53 18 ASN 54 19 LEU 55 20 PHE
56 21 TYR 57 22 PRO 58 23 VAL 59 24 THR 60 25 LEU
61 26 ASP 62 27 VAL 63 28 LEU 64 29 HIS 65 30 GLN
66 31 ILE 67 32 PHE 68 33 SER 69 34 LYS 70 35 PHE
71 36 GLY 72 37 THR 73 38 VAL 74 39 LEU 75 40 LYS
76 41 ILE 77 42 ILE 78 43 THR 79 44 PHE 80 45 THR
81 46 LYS 82 47 ASN 83 48 ASN 84 49 GLN 85 50 PHE
86 51 GLN 87 52 ALA 88 53 LEU 89 54 LEU 90 55 GLN
91 56 TYR 92 57 ALA 93 58 ASP 94 59 PRO 95 60 VAL
96 61 SER 97 62 ALA 98 63 GLN 99 64 HIS 100 65 ALA
101 66 LYS 102 67 LEU 103 68 SER 104 69 LEU 105 70 ASP
106 71 GLY 107 72 GLN 108 73 ASN 109 74 ILE 110 75 TYR
111 76 ASN 112 77 ALA 113 78 CYS 114 79 CYS 115 80 THR
116 81 LEU 117 82 ARG 118 83 ILE 119 84 ASP 120 85 PHE
121 86 SER 122 87 LYS 123 88 LEU 124 89 THR 125 90 SER
126 91 LEU 127 92 ASN 128 93 VAL 129 94 LYS 130 95 TYR
131 96 ASN 132 97 ASN 133 98 ASP 134 99 LYS 135 100 SER
136 101 ARG 137 102 ASP 138 103 TYR 139 104 THR 140 105 ARG
141 106 PRO 142 107 ASP 143 108 LEU 144 109 PRO 145 110 SER
146 111 GLY 147 112 ASP 148 113 SER 149 114 GLN 150 115 PRO
151 116 SER 152 117 LEU 153 118 ASP 154 119 GLN 155 120 THR
156 121 MET 157 122 ALA 158 123 ALA 159 124 ALA 160 125 PHE
161 126 GLY 162 127 LEU 163 128 SER 164 129 VAL
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 5409 PTB1-12 94.51 263 100.00 100.00 1.04e-105
PDB 1SJR "Nmr Structure Of Rrm2 From Human Polypyrimidine Tract Binding Protein Isoform 1 (Ptb1)" 100.00 164 100.00 100.00 2.31e-115
PDB 3ZZY "Crystal Structure Of A Raver1 Pri3 Peptide In Complex With Polypyrimidine Tract Binding Protein Rrm2" 79.27 130 100.00 100.00 6.81e-89
PDB 3ZZZ "Crystal Structure Of A Raver1 Pri4 Peptide In Complex With Polypyrimidine Tract Binding Protein Rrm2" 79.27 130 100.00 100.00 6.81e-89
DBJ BAB86943 "polypirimidine tract binding protein [Mus musculus]" 94.51 528 99.35 100.00 2.63e-102
DBJ BAC28230 "unnamed protein product [Mus musculus]" 92.68 555 100.00 100.00 3.09e-100
DBJ BAC29560 "unnamed protein product [Mus musculus]" 94.51 489 100.00 100.00 6.77e-103
DBJ BAC30837 "unnamed protein product [Mus musculus]" 92.68 555 100.00 100.00 3.09e-100
DBJ BAC31665 "unnamed protein product [Mus musculus]" 92.68 555 100.00 100.00 3.09e-100
EMBL CAA36321 "25kDa nuclear protein [Mus musculus]" 94.51 527 100.00 100.00 1.10e-102
EMBL CAA43056 "polypyrimidine tract-binding protein (pPTB) [Homo sapiens]" 94.51 531 100.00 100.00 2.98e-102
EMBL CAA43202 "pyrimidine binding protein 1 [Rattus norvegicus]" 94.51 530 100.00 100.00 1.52e-102
EMBL CAA43203 "pyrimidine binding protein 2 [Rattus norvegicus]" 66.46 367 100.00 100.00 1.48e-71
EMBL CAA43973 "polypirimidine tract binding protein [Homo sapiens]" 94.51 531 100.00 100.00 2.98e-102
GB AAC99798 "PTB_HUMAN [Homo sapiens]" 94.51 531 100.00 100.00 2.98e-102
GB AAH02397 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 92.68 557 100.00 100.00 5.52e-100
GB AAH04383 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 94.51 531 100.00 100.00 2.98e-102
GB AAH07472 "Polypyrimidine tract binding protein 1 [Mus musculus]" 92.68 555 100.00 100.00 3.09e-100
GB AAH13694 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 92.68 557 100.00 100.00 5.52e-100
REF NP_001070831 "polypyrimidine tract-binding protein 1 isoform 1 [Mus musculus]" 92.68 555 100.00 100.00 3.09e-100
REF NP_001257986 "polypyrimidine tract-binding protein 1 isoform a [Rattus norvegicus]" 92.68 556 100.00 100.00 3.08e-100
REF NP_001269942 "polypyrimidine tract-binding protein 1 isoform 3 [Mus musculus]" 94.51 489 100.00 100.00 6.77e-103
REF NP_001289713 "polypyrimidine tract-binding protein 1 isoform 1 [Bos taurus]" 92.68 557 100.00 100.00 5.65e-100
REF NP_002810 "polypyrimidine tract-binding protein 1 isoform a [Homo sapiens]" 92.68 557 100.00 100.00 5.52e-100
SP P17225 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=Heterogeneous nuclear ribonucleoprotein I; Short" 94.51 527 100.00 100.00 1.10e-102
SP P26599 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=57 kDa RNA-binding protein PPTB-1; AltName: Full" 94.51 531 100.00 100.00 2.98e-102
SP Q00438 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=Heterogeneous nuclear ribonucleoprotein I; Short" 92.68 555 100.00 100.00 2.60e-100
SP Q29099 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=Heterogeneous nuclear ribonucleoprotein I; Short" 92.68 557 99.34 100.00 1.49e-99
SP Q8WN55 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB [Bos taurus]" 94.51 531 100.00 100.00 3.32e-102
TPG DAA27468 "TPA: polypyrimidine tract-binding protein 1 [Bos taurus]" 94.51 531 100.00 100.00 3.32e-102
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$PTB1-2 Human 9606 Eukaryota Metazoa Homo sapiens
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
$PTB1-2 'recombinant technology' 'E. 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
$PTB1-2 0.25 mM '[U-13C; U-15N]'
'Na phosphate' 50 mM .
NaCl 100 mM .
DTT 10 mM .
'sodium azide' 2 mM .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name XWINNMR
_Version 3.1
loop_
_Task
collection
stop_
_Details 'Data acquisition'
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1
loop_
_Task
processing
stop_
_Details .
save_
save_NMRView
_Saveframe_category software
_Name NMRView
_Version 4.1.3
loop_
_Task
'data analysis'
stop_
_Details .
save_
save_X-PLOR
_Saveframe_category software
_Name X-PLOR
_Version 3.851
loop_
_Task
'structure solution'
refinement
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 800
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details 'DRX500 had cryoprobe'
save_
#############################
# NMR applied experiments #
#############################
save_HNCO_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $sample_1
save_
save_HN(CA)CO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_Sample_label $sample_1
save_
save_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $sample_1
save_
save_CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label $sample_1
save_
save_HBHA_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA
_Sample_label $sample_1
save_
save_H(C)CH-TOCSY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(C)CH-TOCSY
_Sample_label $sample_1
save_
save_(H)CCH-TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name (H)CCH-TOCSY
_Sample_label $sample_1
save_
save_(HB)CB(CGCD)HD_8
_Saveframe_category NMR_applied_experiment
_Experiment_name (HB)CB(CGCD)HD
_Sample_label $sample_1
save_
save_15N-separated_NOESY_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-separated NOESY'
_Sample_label $sample_1
save_
save_13C-separated_NOESY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C-separated NOESY'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_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 CBCA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(C)CH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name (H)CCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name (HB)CB(CGCD)HD
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_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 6.5 0.2 n/a
temperature 310 2 K
'ionic strength' 0.3 0.02 M
pressure 1 . atm
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
_Indirect_shift_ratio_citation_label
_Correction_value_citation_label
TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel 1.0 $entry_citation $entry_citation
TSP N 15 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel 0.101329118 $entry_citation $entry_citation
TSP C 13 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel 0.251449530 $entry_citation $entry_citation
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PTB1-2 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 36 ALA CA C 53.500 0.75 1
2 1 36 ALA CB C 20.200 0.75 1
3 1 36 ALA C C 178.400 0.75 1
4 2 37 GLY N N 107.420 0.5 1
5 2 37 GLY H H 8.460 0.03 1
6 2 37 GLY CA C 46.150 0.75 1
7 2 37 GLY C C 174.500 0.75 1
8 6 41 ALA CA C 52.970 0.75 1
9 6 41 ALA HA H 4.080 0.03 1
10 6 41 ALA CB C 19.216 0.75 1
11 6 41 ALA HB H 1.350 0.03 1
12 6 41 ALA C C 178.080 0.75 1
13 7 42 GLY N N 108.401 0.5 1
14 7 42 GLY H H 8.174 0.03 1
15 7 42 GLY CA C 45.680 0.75 1
16 7 42 GLY HA3 H 3.760 0.03 1
17 7 42 GLY HA2 H 3.760 0.03 1
18 7 42 GLY C C 173.620 0.75 1
19 8 43 GLN N N 118.313 0.5 1
20 8 43 GLN H H 7.634 0.03 1
21 8 43 GLN CA C 55.780 0.75 1
22 8 43 GLN HA H 3.740 0.03 1
23 8 43 GLN CB C 30.040 0.75 1
24 8 43 GLN HB3 H 1.820 0.03 2
25 8 43 GLN HB2 H 1.740 0.03 2
26 8 43 GLN CG C 34.404 0.75 1
27 8 43 GLN HG3 H 2.040 0.03 1
28 8 43 GLN HG2 H 2.040 0.03 1
29 8 43 GLN NE2 N 111.540 0.5 1
30 8 43 GLN HE21 H 6.580 0.03 2
31 8 43 GLN HE22 H 7.280 0.03 2
32 8 43 GLN C C 174.920 0.75 1
33 9 44 SER N N 116.128 0.5 1
34 9 44 SER H H 7.581 0.03 1
35 9 44 SER CA C 54.800 0.75 1
36 9 44 SER HA H 4.900 0.03 1
37 9 44 SER CB C 66.200 0.75 1
38 9 44 SER HB3 H 4.070 0.03 2
39 9 44 SER HB2 H 4.020 0.03 2
40 9 44 SER C C 173.540 0.75 1
41 10 45 PRO CA C 64.030 0.75 1
42 10 45 PRO HA H 4.730 0.03 1
43 10 45 PRO CB C 32.000 0.75 1
44 10 45 PRO HB3 H 2.660 0.03 2
45 10 45 PRO HB2 H 1.640 0.03 2
46 10 45 PRO CG C 27.304 0.75 1
47 10 45 PRO HG3 H 2.290 0.03 2
48 10 45 PRO HG2 H 2.010 0.03 2
49 10 45 PRO CD C 50.200 0.75 1
50 10 45 PRO HD3 H 4.080 0.03 2
51 10 45 PRO HD2 H 3.890 0.03 2
52 10 45 PRO C C 174.150 0.75 1
53 11 46 VAL N N 120.940 0.5 1
54 11 46 VAL H H 8.442 0.03 1
55 11 46 VAL CA C 60.470 0.75 1
56 11 46 VAL HA H 5.110 0.03 1
57 11 46 VAL CB C 32.440 0.75 1
58 11 46 VAL HB H 2.140 0.03 1
59 11 46 VAL CG2 C 23.984 0.75 1
60 11 46 VAL HG2 H 0.760 0.03 2
61 11 46 VAL CG1 C 22.060 0.75 1
62 11 46 VAL HG1 H 0.500 0.03 2
63 11 46 VAL C C 175.290 0.75 1
64 12 47 LEU N N 125.077 0.5 1
65 12 47 LEU H H 9.151 0.03 1
66 12 47 LEU CA C 53.180 0.75 1
67 12 47 LEU HA H 4.920 0.03 1
68 12 47 LEU CB C 45.840 0.75 1
69 12 47 LEU HB3 H 1.600 0.03 2
70 12 47 LEU HB2 H 1.150 0.03 2
71 12 47 LEU CG C 27.704 0.75 1
72 12 47 LEU HG H 1.820 0.03 1
73 12 47 LEU CD1 C 23.470 0.75 1
74 12 47 LEU HD1 H 0.670 0.03 2
75 12 47 LEU CD2 C 27.700 0.75 1
76 12 47 LEU HD2 H 1.130 0.03 2
77 12 47 LEU C C 175.310 0.75 1
78 13 48 ARG N N 121.761 0.5 1
79 13 48 ARG H H 9.028 0.03 1
80 13 48 ARG CA C 55.970 0.75 1
81 13 48 ARG HA H 5.020 0.03 1
82 13 48 ARG CB C 32.190 0.75 1
83 13 48 ARG HB3 H 1.820 0.03 2
84 13 48 ARG HB2 H 1.490 0.03 2
85 13 48 ARG CG C 28.004 0.75 1
86 13 48 ARG HG3 H 1.690 0.03 2
87 13 48 ARG HG2 H 1.410 0.03 2
88 13 48 ARG CD C 44.624 0.75 1
89 13 48 ARG HD3 H 3.190 0.03 2
90 13 48 ARG HD2 H 3.150 0.03 2
91 13 48 ARG C C 174.780 0.75 1
92 14 49 ILE N N 128.906 0.5 1
93 14 49 ILE H H 9.458 0.03 1
94 14 49 ILE CA C 60.520 0.75 1
95 14 49 ILE HA H 4.780 0.03 1
96 14 49 ILE CB C 42.250 0.75 1
97 14 49 ILE HB H 1.580 0.03 1
98 14 49 ILE CG1 C 29.014 0.75 2
99 14 49 ILE HG13 H 1.290 0.03 1
100 14 49 ILE HG12 H 0.820 0.03 1
101 14 49 ILE CD1 C 17.000 0.75 1
102 14 49 ILE HD1 H 0.210 0.03 1
103 14 49 ILE CG2 C 19.800 0.75 1
104 14 49 ILE HG2 H 0.780 0.03 1
105 14 49 ILE C C 174.380 0.75 1
106 15 50 ILE N N 127.851 0.5 1
107 15 50 ILE H H 9.220 0.03 1
108 15 50 ILE CA C 60.840 0.75 1
109 15 50 ILE HA H 4.730 0.03 1
110 15 50 ILE CB C 41.770 0.75 1
111 15 50 ILE HB H 1.760 0.03 1
112 15 50 ILE CG1 C 29.400 0.75 2
113 15 50 ILE HG13 H 0.990 0.03 1
114 15 50 ILE HG12 H 1.530 0.03 1
115 15 50 ILE CD1 C 14.300 0.75 1
116 15 50 ILE HD1 H 0.790 0.03 1
117 15 50 ILE CG2 C 18.304 0.75 1
118 15 50 ILE HG2 H 0.930 0.03 1
119 15 50 ILE C C 175.400 0.75 1
120 16 51 VAL N N 124.674 0.5 1
121 16 51 VAL H H 8.026 0.03 1
122 16 51 VAL CA C 61.100 0.75 1
123 16 51 VAL HA H 4.920 0.03 1
124 16 51 VAL CB C 32.570 0.75 1
125 16 51 VAL HB H 2.110 0.03 1
126 16 51 VAL CG2 C 21.590 0.75 1
127 16 51 VAL HG2 H 0.820 0.03 2
128 16 51 VAL CG1 C 23.100 0.75 1
129 16 51 VAL HG1 H 0.750 0.03 2
130 16 51 VAL C C 175.170 0.75 1
131 17 52 GLU N N 125.913 0.5 1
132 17 52 GLU H H 9.080 0.03 1
133 17 52 GLU CA C 55.650 0.75 1
134 17 52 GLU HA H 4.570 0.03 1
135 17 52 GLU CB C 32.990 0.75 1
136 17 52 GLU HB3 H 2.040 0.03 2
137 17 52 GLU HB2 H 1.910 0.03 2
138 17 52 GLU CG C 37.894 0.75 1
139 17 52 GLU HG3 H 2.260 0.03 2
140 17 52 GLU HG2 H 2.210 0.03 2
141 17 52 GLU C C 176.860 0.75 1
142 18 53 ASN N N 118.526 0.5 1
143 18 53 ASN H H 9.029 0.03 1
144 18 53 ASN CA C 53.900 0.75 1
145 18 53 ASN HA H 4.030 0.03 1
146 18 53 ASN CB C 36.820 0.75 1
147 18 53 ASN HB3 H 2.960 0.03 2
148 18 53 ASN HB2 H 2.560 0.03 2
149 18 53 ASN ND2 N 114.500 0.5 1
150 18 53 ASN HD21 H 6.970 0.03 2
151 18 53 ASN HD22 H 7.770 0.03 2
152 18 53 ASN C C 175.840 0.75 1
153 19 54 LEU N N 124.027 0.5 1
154 19 54 LEU H H 8.324 0.03 1
155 19 54 LEU CA C 55.400 0.75 1
156 19 54 LEU HA H 4.530 0.03 1
157 19 54 LEU CB C 41.690 0.75 1
158 19 54 LEU HB3 H 1.930 0.03 2
159 19 54 LEU HB2 H 1.220 0.03 2
160 19 54 LEU CG C 27.064 0.75 1
161 19 54 LEU HG H 1.480 0.03 1
162 19 54 LEU CD1 C 26.300 0.75 1
163 19 54 LEU HD1 H 0.820 0.03 1
164 19 54 LEU CD2 C 26.300 0.75 1
165 19 54 LEU HD2 H 0.820 0.03 1
166 19 54 LEU C C 176.280 0.75 1
167 20 55 PHE N N 125.752 0.5 1
168 20 55 PHE H H 7.858 0.03 1
169 20 55 PHE CA C 57.330 0.75 1
170 20 55 PHE HA H 4.660 0.03 1
171 20 55 PHE CB C 39.380 0.75 1
172 20 55 PHE HB3 H 3.210 0.03 2
173 20 55 PHE HB2 H 2.930 0.03 2
174 20 55 PHE CD1 C 131.600 0.75 1
175 20 55 PHE HD1 H 7.050 0.03 1
176 20 55 PHE CD2 C 131.600 0.75 1
177 20 55 PHE HD2 H 7.050 0.03 1
178 20 55 PHE C C 174.460 0.75 1
179 21 56 TYR N N 117.912 0.5 1
180 21 56 TYR H H 7.294 0.03 1
181 21 56 TYR CA C 55.570 0.75 1
182 21 56 TYR HA H 4.640 0.03 1
183 21 56 TYR CB C 40.776 0.75 1
184 21 56 TYR HB3 H 2.750 0.03 2
185 21 56 TYR HB2 H 2.310 0.03 2
186 21 56 TYR CD1 C 133.100 0.75 1
187 21 56 TYR HD1 H 6.920 0.03 1
188 21 56 TYR CD2 C 133.100 0.75 1
189 21 56 TYR HD2 H 6.920 0.03 1
190 21 56 TYR C C 172.130 0.75 1
191 22 57 PRO CA C 63.270 0.75 1
192 22 57 PRO HA H 4.170 0.03 1
193 22 57 PRO CB C 32.420 0.75 1
194 22 57 PRO HB3 H 2.160 0.03 2
195 22 57 PRO HB2 H 1.730 0.03 2
196 22 57 PRO CG C 28.200 0.75 1
197 22 57 PRO HG3 H 1.960 0.03 2
198 22 57 PRO HG2 H 1.880 0.03 2
199 22 57 PRO CD C 50.200 0.75 1
200 22 57 PRO HD3 H 3.620 0.03 2
201 22 57 PRO HD2 H 3.290 0.03 2
202 22 57 PRO C C 176.520 0.75 1
203 23 58 VAL N N 122.458 0.5 1
204 23 58 VAL H H 7.945 0.03 1
205 23 58 VAL CA C 62.800 0.75 1
206 23 58 VAL HA H 4.050 0.03 1
207 23 58 VAL CB C 33.550 0.75 1
208 23 58 VAL HB H 1.450 0.03 1
209 23 58 VAL CG2 C 23.000 0.75 1
210 23 58 VAL HG2 H 0.930 0.03 2
211 23 58 VAL CG1 C 22.100 0.75 1
212 23 58 VAL HG1 H 0.760 0.03 2
213 23 58 VAL C C 174.050 0.75 1
214 24 59 THR N N 113.113 0.5 1
215 24 59 THR H H 6.654 0.03 1
216 24 59 THR CA C 60.040 0.75 1
217 24 59 THR HA H 4.690 0.03 1
218 24 59 THR CB C 72.320 0.75 1
219 24 59 THR HB H 4.740 0.03 1
220 24 59 THR CG2 C 22.400 0.75 1
221 24 59 THR HG2 H 1.260 0.03 1
222 24 59 THR C C 175.230 0.75 1
223 25 60 LEU N N 121.014 0.5 1
224 25 60 LEU H H 8.925 0.03 1
225 25 60 LEU CA C 60.120 0.75 1
226 25 60 LEU HA H 3.910 0.03 1
227 25 60 LEU CB C 42.810 0.75 1
228 25 60 LEU HB3 H 1.820 0.03 2
229 25 60 LEU HB2 H 1.630 0.03 2
230 25 60 LEU CG C 27.554 0.75 1
231 25 60 LEU HG H 1.660 0.03 1
232 25 60 LEU CD1 C 25.800 0.75 1
233 25 60 LEU HD1 H 0.800 0.03 2
234 25 60 LEU CD2 C 27.700 0.75 1
235 25 60 LEU HD2 H 0.770 0.03 2
236 25 60 LEU C C 178.300 0.75 1
237 26 61 ASP N N 115.231 0.5 1
238 26 61 ASP H H 8.058 0.03 1
239 26 61 ASP CA C 57.960 0.75 1
240 26 61 ASP HA H 4.440 0.03 1
241 26 61 ASP CB C 41.290 0.75 1
242 26 61 ASP HB3 H 2.710 0.03 2
243 26 61 ASP HB2 H 2.610 0.03 2
244 26 61 ASP C C 178.870 0.75 1
245 27 62 VAL N N 121.231 0.5 1
246 27 62 VAL H H 7.525 0.03 1
247 27 62 VAL CA C 66.600 0.75 1
248 27 62 VAL HA H 3.820 0.03 1
249 27 62 VAL CB C 32.750 0.75 1
250 27 62 VAL HB H 2.220 0.03 1
251 27 62 VAL CG2 C 23.470 0.75 1
252 27 62 VAL HG2 H 1.190 0.03 2
253 27 62 VAL CG1 C 21.590 0.75 1
254 27 62 VAL HG1 H 1.060 0.03 2
255 27 62 VAL C C 178.000 0.75 1
256 28 63 LEU N N 117.853 0.5 1
257 28 63 LEU H H 7.746 0.03 1
258 28 63 LEU CA C 58.120 0.75 1
259 28 63 LEU HA H 4.160 0.03 1
260 28 63 LEU CB C 42.570 0.75 1
261 28 63 LEU HB3 H 2.160 0.03 2
262 28 63 LEU HB2 H 1.200 0.03 2
263 28 63 LEU CG C 26.824 0.75 1
264 28 63 LEU HG H 1.850 0.03 1
265 28 63 LEU CD1 C 23.000 0.75 1
266 28 63 LEU HD1 H 0.810 0.03 2
267 28 63 LEU CD2 C 26.800 0.75 1
268 28 63 LEU HD2 H 0.760 0.03 2
269 28 63 LEU C C 178.890 0.75 1
270 29 64 HIS N N 119.142 0.5 1
271 29 64 HIS H H 9.125 0.03 1
272 29 64 HIS CA C 62.900 0.75 1
273 29 64 HIS HA H 3.710 0.03 1
274 29 64 HIS CB C 31.080 0.75 1
275 29 64 HIS HB3 H 3.270 0.03 2
276 29 64 HIS HB2 H 3.210 0.03 2
277 29 64 HIS CD2 C 117.170 0.75 1
278 29 64 HIS HD2 H 5.690 0.03 3
279 29 64 HIS C C 178.700 0.75 1
280 30 65 GLN N N 120.933 0.5 1
281 30 65 GLN H H 8.359 0.03 1
282 30 65 GLN CA C 60.440 0.75 1
283 30 65 GLN HA H 3.920 0.03 1
284 30 65 GLN CB C 29.080 0.75 1
285 30 65 GLN HB3 H 2.280 0.03 2
286 30 65 GLN HB2 H 2.360 0.03 2
287 30 65 GLN CG C 34.484 0.75 1
288 30 65 GLN HG3 H 2.580 0.03 2
289 30 65 GLN HG2 H 2.430 0.03 2
290 30 65 GLN NE2 N 110.800 0.5 1
291 30 65 GLN HE21 H 6.780 0.03 2
292 30 65 GLN HE22 H 7.450 0.03 2
293 30 65 GLN C C 178.610 0.75 1
294 31 66 ILE N N 117.454 0.5 1
295 31 66 ILE H H 8.001 0.03 1
296 31 66 ILE CA C 64.800 0.75 1
297 31 66 ILE HA H 3.740 0.03 1
298 31 66 ILE CB C 39.640 0.75 1
299 31 66 ILE HB H 1.800 0.03 1
300 31 66 ILE CG1 C 29.004 0.75 2
301 31 66 ILE HG13 H 1.750 0.03 1
302 31 66 ILE HG12 H 1.200 0.03 1
303 31 66 ILE CD1 C 15.000 0.75 1
304 31 66 ILE HD1 H 0.790 0.03 1
305 31 66 ILE CG2 C 17.900 0.75 1
306 31 66 ILE HG2 H 0.510 0.03 1
307 31 66 ILE C C 178.640 0.75 1
308 32 67 PHE N N 114.635 0.5 1
309 32 67 PHE H H 8.565 0.03 1
310 32 67 PHE CA C 62.400 0.75 1
311 32 67 PHE HA H 4.230 0.03 1
312 32 67 PHE CB C 38.300 0.75 1
313 32 67 PHE HB3 H 3.060 0.03 2
314 32 67 PHE HB2 H 2.810 0.03 2
315 32 67 PHE CD1 C 131.800 0.75 1
316 32 67 PHE HD1 H 7.930 0.03 1
317 32 67 PHE CE1 C 129.800 0.75 1
318 32 67 PHE HE1 H 6.980 0.03 1
319 32 67 PHE CE2 C 129.800 0.75 1
320 32 67 PHE HE2 H 6.980 0.03 1
321 32 67 PHE CD2 C 131.800 0.75 1
322 32 67 PHE HD2 H 7.930 0.03 1
323 32 67 PHE C C 180.810 0.75 1
324 33 68 SER N N 120.692 0.5 1
325 33 68 SER H H 8.521 0.03 1
326 33 68 SER CA C 61.800 0.75 1
327 33 68 SER HA H 4.920 0.03 1
328 33 68 SER CB C 62.900 0.75 1
329 33 68 SER HB3 H 3.890 0.03 2
330 33 68 SER HB2 H 3.630 0.03 2
331 33 68 SER C C 173.950 0.75 1
332 34 69 LYS N N 118.688 0.5 1
333 34 69 LYS H H 6.810 0.03 1
334 34 69 LYS CA C 58.200 0.75 1
335 34 69 LYS HA H 3.920 0.03 1
336 34 69 LYS CB C 32.390 0.75 1
337 34 69 LYS HB3 H 1.430 0.03 2
338 34 69 LYS HB2 H 1.170 0.03 2
339 34 69 LYS CG C 25.300 0.75 1
340 34 69 LYS HG3 H 1.250 0.03 2
341 34 69 LYS HG2 H 1.000 0.03 2
342 34 69 LYS CD C 29.500 0.75 1
343 34 69 LYS HD3 H 1.470 0.03 1
344 34 69 LYS HD2 H 1.470 0.03 1
345 34 69 LYS CE C 43.084 0.75 1
346 34 69 LYS HE3 H 2.840 0.03 1
347 34 69 LYS HE2 H 2.840 0.03 1
348 34 69 LYS C C 176.840 0.75 1
349 35 70 PHE N N 112.363 0.5 1
350 35 70 PHE H H 7.105 0.03 1
351 35 70 PHE CA C 58.300 0.75 1
352 35 70 PHE HA H 4.460 0.03 1
353 35 70 PHE CB C 41.140 0.75 1
354 35 70 PHE HB3 H 3.410 0.03 2
355 35 70 PHE HB2 H 2.820 0.03 2
356 35 70 PHE CD1 C 130.700 0.75 1
357 35 70 PHE HD1 H 7.080 0.03 1
358 35 70 PHE CE1 C 131.000 0.75 1
359 35 70 PHE HE1 H 7.170 0.03 1
360 35 70 PHE CZ C 128.700 0.75 1
361 35 70 PHE HZ H 7.190 0.03 1
362 35 70 PHE CE2 C 131.000 0.75 1
363 35 70 PHE HE2 H 7.170 0.03 1
364 35 70 PHE CD2 C 130.700 0.75 1
365 35 70 PHE HD2 H 7.080 0.03 1
366 35 70 PHE C C 174.750 0.75 1
367 36 71 GLY N N 106.115 0.5 1
368 36 71 GLY H H 7.406 0.03 1
369 36 71 GLY CA C 45.550 0.75 1
370 36 71 GLY HA3 H 4.300 0.03 2
371 36 71 GLY HA2 H 4.070 0.03 2
372 36 71 GLY C C 171.070 0.75 1
373 37 72 THR N N 115.678 0.5 1
374 37 72 THR H H 8.701 0.03 1
375 37 72 THR CA C 63.400 0.75 1
376 37 72 THR HA H 4.320 0.03 1
377 37 72 THR CB C 69.990 0.75 1
378 37 72 THR HB H 4.050 0.03 1
379 37 72 THR CG2 C 22.530 0.75 1
380 37 72 THR HG2 H 1.180 0.03 1
381 37 72 THR C C 173.780 0.75 1
382 38 73 VAL N N 130.489 0.5 1
383 38 73 VAL H H 9.022 0.03 1
384 38 73 VAL CA C 63.450 0.75 1
385 38 73 VAL HA H 3.600 0.03 1
386 38 73 VAL CB C 32.470 0.75 1
387 38 73 VAL HB H 1.660 0.03 1
388 38 73 VAL CG2 C 22.000 0.75 1
389 38 73 VAL HG2 H 0.590 0.03 2
390 38 73 VAL CG1 C 22.500 0.75 1
391 38 73 VAL HG1 H 0.570 0.03 2
392 38 73 VAL C C 174.940 0.75 1
393 39 74 LEU N N 125.514 0.5 1
394 39 74 LEU H H 9.146 0.03 1
395 39 74 LEU CA C 56.800 0.75 1
396 39 74 LEU HA H 4.550 0.03 1
397 39 74 LEU CB C 44.290 0.75 1
398 39 74 LEU HB3 H 1.550 0.03 2
399 39 74 LEU HB2 H 1.480 0.03 2
400 39 74 LEU CG C 27.074 0.75 1
401 39 74 LEU HG H 1.590 0.03 1
402 39 74 LEU CD1 C 23.200 0.75 1
403 39 74 LEU HD1 H 0.820 0.03 2
404 39 74 LEU CD2 C 26.800 0.75 1
405 39 74 LEU HD2 H 0.940 0.03 2
406 39 74 LEU C C 176.980 0.75 1
407 40 75 LYS N N 113.043 0.5 1
408 40 75 LYS H H 7.226 0.03 1
409 40 75 LYS CA C 54.900 0.75 1
410 40 75 LYS HA H 5.630 0.03 1
411 40 75 LYS CB C 40.590 0.75 1
412 40 75 LYS HB3 H 1.840 0.03 2
413 40 75 LYS HB2 H 1.670 0.03 2
414 40 75 LYS CG C 27.184 0.75 1
415 40 75 LYS HG3 H 1.560 0.03 2
416 40 75 LYS HG2 H 1.280 0.03 2
417 40 75 LYS CD C 31.000 0.75 1
418 40 75 LYS HD3 H 1.670 0.03 2
419 40 75 LYS HD2 H 1.500 0.03 2
420 40 75 LYS CE C 44.114 0.75 1
421 40 75 LYS HE3 H 2.990 0.03 2
422 40 75 LYS HE2 H 2.870 0.03 2
423 40 75 LYS C C 174.770 0.75 1
424 41 76 ILE N N 118.976 0.5 1
425 41 76 ILE H H 8.825 0.03 1
426 41 76 ILE CA C 60.940 0.75 1
427 41 76 ILE HA H 5.000 0.03 1
428 41 76 ILE CB C 43.820 0.75 1
429 41 76 ILE HB H 1.670 0.03 1
430 41 76 ILE CG1 C 28.800 0.75 2
431 41 76 ILE HG13 H 1.670 0.03 1
432 41 76 ILE HG12 H 0.870 0.03 1
433 41 76 ILE CD1 C 14.300 0.75 1
434 41 76 ILE HD1 H 0.970 0.03 1
435 41 76 ILE CG2 C 18.800 0.75 1
436 41 76 ILE HG2 H 0.830 0.03 1
437 41 76 ILE C C 176.420 0.75 1
438 42 77 ILE N N 124.400 0.5 1
439 42 77 ILE H H 8.960 0.03 1
440 42 77 ILE CA C 62.020 0.75 1
441 42 77 ILE HA H 4.630 0.03 1
442 42 77 ILE CB C 43.820 0.75 1
443 42 77 ILE HB H 1.660 0.03 1
444 42 77 ILE CG1 C 28.524 0.75 2
445 42 77 ILE HG13 H 1.570 0.03 1
446 42 77 ILE HG12 H 1.040 0.03 1
447 42 77 ILE CD1 C 15.500 0.75 1
448 42 77 ILE HD1 H 0.920 0.03 1
449 42 77 ILE CG2 C 18.300 0.75 1
450 42 77 ILE HG2 H 1.000 0.03 1
451 42 77 ILE C C 174.750 0.75 1
452 43 78 THR N N 116.064 0.5 1
453 43 78 THR H H 8.573 0.03 1
454 43 78 THR CA C 59.600 0.75 1
455 43 78 THR HA H 5.250 0.03 1
456 43 78 THR CB C 71.900 0.75 1
457 43 78 THR HB H 4.020 0.03 1
458 43 78 THR CG2 C 23.000 0.75 1
459 43 78 THR HG2 H 1.080 0.03 1
460 43 78 THR C C 172.820 0.75 1
461 44 79 PHE N N 116.118 0.5 1
462 44 79 PHE H H 8.415 0.03 1
463 44 79 PHE CA C 56.700 0.75 1
464 44 79 PHE HA H 4.810 0.03 1
465 44 79 PHE CB C 39.960 0.75 1
466 44 79 PHE HB3 H 3.410 0.03 2
467 44 79 PHE HB2 H 2.910 0.03 2
468 44 79 PHE CD1 C 132.160 0.75 1
469 44 79 PHE HD1 H 6.830 0.03 1
470 44 79 PHE CE1 C 130.300 0.75 1
471 44 79 PHE HE1 H 7.000 0.03 1
472 44 79 PHE CE2 C 130.300 0.75 1
473 44 79 PHE HE2 H 7.000 0.03 1
474 44 79 PHE CD2 C 132.160 0.75 1
475 44 79 PHE HD2 H 6.830 0.03 1
476 44 79 PHE C C 173.020 0.75 1
477 45 80 THR N N 113.999 0.5 1
478 45 80 THR H H 8.395 0.03 1
479 45 80 THR CA C 61.000 0.75 1
480 45 80 THR HA H 5.190 0.03 1
481 45 80 THR CB C 70.500 0.75 1
482 45 80 THR HB H 4.070 0.03 1
483 45 80 THR CG2 C 21.700 0.75 1
484 45 80 THR HG2 H 1.160 0.03 1
485 45 80 THR C C 174.430 0.75 1
486 46 81 LYS N N 126.037 0.5 1
487 46 81 LYS H H 8.432 0.03 1
488 46 81 LYS CA C 56.350 0.75 1
489 46 81 LYS HA H 4.590 0.03 1
490 46 81 LYS CB C 36.090 0.75 1
491 46 81 LYS HB3 H 1.830 0.03 1
492 46 81 LYS HB2 H 1.830 0.03 1
493 46 81 LYS CG C 25.700 0.75 1
494 46 81 LYS HG3 H 1.450 0.03 2
495 46 81 LYS HG2 H 1.420 0.03 2
496 46 81 LYS CD C 30.000 0.75 1
497 46 81 LYS HD3 H 1.740 0.03 2
498 46 81 LYS HD2 H 1.690 0.03 2
499 46 81 LYS CE C 42.400 0.75 1
500 46 81 LYS HE3 H 2.950 0.03 1
501 46 81 LYS HE2 H 2.950 0.03 1
502 46 81 LYS C C 176.130 0.75 1
503 47 82 ASN CA C 54.900 0.75 1
504 47 82 ASN HA H 4.380 0.03 1
505 47 82 ASN CB C 37.660 0.75 1
506 47 82 ASN HB3 H 3.060 0.03 2
507 47 82 ASN HB2 H 2.820 0.03 2
508 47 82 ASN C C 174.660 0.75 1
509 48 83 ASN N N 110.158 0.5 1
510 48 83 ASN H H 8.869 0.03 1
511 48 83 ASN CA C 54.900 0.75 1
512 48 83 ASN HA H 4.250 0.03 1
513 48 83 ASN CB C 38.540 0.75 1
514 48 83 ASN HB3 H 3.140 0.03 2
515 48 83 ASN HB2 H 2.960 0.03 2
516 48 83 ASN ND2 N 112.950 0.5 1
517 48 83 ASN HD21 H 6.900 0.03 2
518 48 83 ASN HD22 H 7.560 0.03 2
519 48 83 ASN C C 173.880 0.75 1
520 49 84 GLN N N 117.967 0.5 1
521 49 84 GLN H H 7.850 0.03 1
522 49 84 GLN CA C 55.250 0.75 1
523 49 84 GLN HA H 4.840 0.03 1
524 49 84 GLN CB C 32.550 0.75 1
525 49 84 GLN HB3 H 2.100 0.03 1
526 49 84 GLN HB2 H 2.100 0.03 1
527 49 84 GLN CG C 34.800 0.75 1
528 49 84 GLN HG3 H 2.440 0.03 2
529 49 84 GLN HG2 H 2.330 0.03 2
530 49 84 GLN NE2 N 111.200 0.5 1
531 49 84 GLN HE21 H 6.880 0.03 2
532 49 84 GLN HE22 H 7.620 0.03 2
533 49 84 GLN C C 174.440 0.75 1
534 50 85 PHE N N 127.481 0.5 1
535 50 85 PHE H H 8.988 0.03 1
536 50 85 PHE CA C 59.580 0.75 1
537 50 85 PHE HA H 4.650 0.03 1
538 50 85 PHE CB C 40.776 0.75 1
539 50 85 PHE HB3 H 3.080 0.03 2
540 50 85 PHE HB2 H 3.150 0.03 2
541 50 85 PHE CD1 C 131.500 0.75 1
542 50 85 PHE HD1 H 7.120 0.03 1
543 50 85 PHE HE1 H 7.130 0.03 1
544 50 85 PHE HE2 H 7.130 0.03 1
545 50 85 PHE CD2 C 131.500 0.75 1
546 50 85 PHE HD2 H 7.120 0.03 1
547 50 85 PHE C C 173.530 0.75 1
548 51 86 GLN N N 126.251 0.5 1
549 51 86 GLN H H 8.154 0.03 1
550 51 86 GLN CA C 53.500 0.75 1
551 51 86 GLN HA H 5.170 0.03 1
552 51 86 GLN CB C 33.570 0.75 1
553 51 86 GLN HB3 H 1.630 0.03 2
554 51 86 GLN HB2 H 1.000 0.03 2
555 51 86 GLN CG C 34.900 0.75 1
556 51 86 GLN HG3 H 2.010 0.03 2
557 51 86 GLN HG2 H 1.980 0.03 2
558 51 86 GLN NE2 N 109.329 0.5 1
559 51 86 GLN HE21 H 6.720 0.03 2
560 51 86 GLN HE22 H 6.890 0.03 2
561 51 86 GLN C C 172.580 0.75 1
562 52 87 ALA N N 118.784 0.5 1
563 52 87 ALA H H 9.067 0.03 1
564 52 87 ALA CA C 49.800 0.75 1
565 52 87 ALA HA H 5.130 0.03 1
566 52 87 ALA CB C 23.720 0.75 1
567 52 87 ALA HB H 0.960 0.03 1
568 52 87 ALA C C 175.790 0.75 1
569 53 88 LEU N N 120.943 0.5 1
570 53 88 LEU H H 9.069 0.03 1
571 53 88 LEU CA C 53.500 0.75 1
572 53 88 LEU HA H 5.450 0.03 1
573 53 88 LEU CB C 46.100 0.75 1
574 53 88 LEU HB3 H 1.610 0.03 2
575 53 88 LEU HB2 H 1.280 0.03 2
576 53 88 LEU CG C 28.000 0.75 1
577 53 88 LEU HG H 1.730 0.03 1
578 53 88 LEU CD1 C 24.400 0.75 1
579 53 88 LEU HD1 H 1.020 0.03 2
580 53 88 LEU CD2 C 26.800 0.75 1
581 53 88 LEU HD2 H 0.900 0.03 2
582 53 88 LEU C C 174.810 0.75 1
583 54 89 LEU N N 123.916 0.5 1
584 54 89 LEU H H 8.551 0.03 1
585 54 89 LEU CA C 54.500 0.75 1
586 54 89 LEU HA H 4.900 0.03 1
587 54 89 LEU CB C 47.440 0.75 1
588 54 89 LEU HB3 H 1.060 0.03 2
589 54 89 LEU HB2 H 0.980 0.03 2
590 54 89 LEU CG C 27.300 0.75 1
591 54 89 LEU HG H 1.210 0.03 1
592 54 89 LEU CD1 C 25.500 0.75 1
593 54 89 LEU HD1 H -0.070 0.03 2
594 54 89 LEU CD2 C 27.200 0.75 1
595 54 89 LEU HD2 H 0.080 0.03 2
596 54 89 LEU C C 173.220 0.75 1
597 55 90 GLN N N 126.539 0.5 1
598 55 90 GLN H H 8.880 0.03 1
599 55 90 GLN CA C 54.500 0.75 1
600 55 90 GLN HA H 5.050 0.03 1
601 55 90 GLN CB C 32.390 0.75 1
602 55 90 GLN HB3 H 1.840 0.03 2
603 55 90 GLN HB2 H 1.930 0.03 2
604 55 90 GLN CG C 33.500 0.75 1
605 55 90 GLN HG3 H 2.400 0.03 2
606 55 90 GLN HG2 H 2.150 0.03 2
607 55 90 GLN NE2 N 109.640 0.5 1
608 55 90 GLN HE21 H 6.970 0.03 2
609 55 90 GLN HE22 H 7.850 0.03 2
610 55 90 GLN C C 175.290 0.75 1
611 56 91 TYR N N 127.313 0.5 1
612 56 91 TYR H H 8.928 0.03 1
613 56 91 TYR CA C 59.100 0.75 1
614 56 91 TYR HA H 5.270 0.03 1
615 56 91 TYR CB C 42.870 0.75 1
616 56 91 TYR HB3 H 3.410 0.03 2
617 56 91 TYR HB2 H 2.910 0.03 2
618 56 91 TYR CD1 C 132.000 0.75 1
619 56 91 TYR HD1 H 6.940 0.03 1
620 56 91 TYR CE1 C 117.000 0.75 1
621 56 91 TYR HE1 H 6.590 0.03 1
622 56 91 TYR HH H 9.610 0.03 1
623 56 91 TYR CE2 C 117.000 0.75 1
624 56 91 TYR HE2 H 6.590 0.03 1
625 56 91 TYR CD2 C 132.000 0.75 1
626 56 91 TYR HD2 H 6.940 0.03 1
627 56 91 TYR C C 176.300 0.75 1
628 57 92 ALA N N 119.427 0.5 1
629 57 92 ALA H H 8.337 0.03 1
630 57 92 ALA CA C 54.400 0.75 1
631 57 92 ALA HA H 4.350 0.03 1
632 57 92 ALA CB C 19.196 0.75 1
633 57 92 ALA HB H 1.600 0.03 1
634 57 92 ALA C C 176.450 0.75 1
635 58 93 ASP N N 115.220 0.5 1
636 58 93 ASP H H 7.787 0.03 1
637 58 93 ASP CA C 50.600 0.75 1
638 58 93 ASP HA H 5.280 0.03 1
639 58 93 ASP CB C 44.840 0.75 1
640 58 93 ASP HB3 H 2.980 0.03 2
641 58 93 ASP HB2 H 2.730 0.03 2
642 59 94 PRO CA C 65.290 0.75 1
643 59 94 PRO HA H 4.210 0.03 1
644 59 94 PRO CB C 32.860 0.75 1
645 59 94 PRO HB3 H 2.040 0.03 2
646 59 94 PRO HB2 H 1.950 0.03 2
647 59 94 PRO CG C 28.200 0.75 1
648 59 94 PRO HG3 H 2.160 0.03 2
649 59 94 PRO HG2 H 1.960 0.03 2
650 59 94 PRO CD C 51.560 0.75 1
651 59 94 PRO HD3 H 3.910 0.03 2
652 59 94 PRO HD2 H 4.170 0.03 2
653 59 94 PRO C C 178.300 0.75 1
654 60 95 VAL N N 120.901 0.5 1
655 60 95 VAL H H 8.538 0.03 1
656 60 95 VAL CA C 66.100 0.75 1
657 60 95 VAL HA H 3.680 0.03 1
658 60 95 VAL CB C 31.520 0.75 1
659 60 95 VAL HB H 2.040 0.03 1
660 60 95 VAL CG2 C 23.500 0.75 1
661 60 95 VAL HG2 H 0.990 0.03 2
662 60 95 VAL CG1 C 22.000 0.75 1
663 60 95 VAL HG1 H 0.810 0.03 2
664 60 95 VAL C C 178.410 0.75 1
665 61 96 SER N N 117.098 0.5 1
666 61 96 SER H H 7.701 0.03 1
667 61 96 SER CA C 62.400 0.75 1
668 61 96 SER HA H 4.000 0.03 1
669 61 96 SER CB C 62.400 0.75 1
670 61 96 SER HB3 H 3.360 0.03 2
671 61 96 SER HB2 H 2.890 0.03 2
672 61 96 SER C C 174.580 0.75 1
673 62 97 ALA N N 120.318 0.5 1
674 62 97 ALA H H 6.518 0.03 1
675 62 97 ALA CA C 55.400 0.75 1
676 62 97 ALA HA H 3.970 0.03 1
677 62 97 ALA CB C 18.196 0.75 1
678 62 97 ALA HB H 1.760 0.03 1
679 62 97 ALA C C 178.480 0.75 1
680 63 98 GLN N N 117.042 0.5 1
681 63 98 GLN H H 7.713 0.03 1
682 63 98 GLN CA C 59.600 0.75 1
683 63 98 GLN HA H 4.230 0.03 1
684 63 98 GLN CB C 28.840 0.75 1
685 63 98 GLN HB3 H 2.290 0.03 1
686 63 98 GLN HB2 H 2.290 0.03 1
687 63 98 GLN CG C 34.124 0.75 1
688 63 98 GLN HG3 H 2.440 0.03 2
689 63 98 GLN HG2 H 2.490 0.03 2
690 63 98 GLN NE2 N 110.460 0.5 1
691 63 98 GLN HE21 H 6.750 0.03 2
692 63 98 GLN HE22 H 7.280 0.03 2
693 63 98 GLN C C 178.070 0.75 1
694 64 99 HIS N N 118.042 0.5 1
695 64 99 HIS H H 8.180 0.03 1
696 64 99 HIS CA C 58.200 0.75 1
697 64 99 HIS HA H 4.400 0.03 1
698 64 99 HIS CB C 30.660 0.75 1
699 64 99 HIS HB3 H 3.330 0.03 1
700 64 99 HIS HB2 H 3.330 0.03 1
701 64 99 HIS CD2 C 119.200 0.75 1
702 64 99 HIS HD2 H 7.100 0.03 3
703 64 99 HIS C C 177.790 0.75 1
704 65 100 ALA N N 122.586 0.5 1
705 65 100 ALA H H 8.358 0.03 1
706 65 100 ALA CA C 55.200 0.75 1
707 65 100 ALA HA H 2.480 0.03 1
708 65 100 ALA CB C 19.696 0.75 1
709 65 100 ALA HB H 1.470 0.03 1
710 65 100 ALA C C 178.720 0.75 1
711 66 101 LYS N N 117.296 0.5 1
712 66 101 LYS H H 8.010 0.03 1
713 66 101 LYS CA C 60.600 0.75 1
714 66 101 LYS HA H 3.590 0.03 1
715 66 101 LYS CB C 33.260 0.75 1
716 66 101 LYS HB3 H 1.860 0.03 2
717 66 101 LYS HB2 H 1.520 0.03 2
718 66 101 LYS CG C 25.500 0.75 1
719 66 101 LYS HG3 H 1.160 0.03 2
720 66 101 LYS HG2 H 0.850 0.03 2
721 66 101 LYS CD C 30.500 0.75 1
722 66 101 LYS HD3 H 1.200 0.03 2
723 66 101 LYS HD2 H 0.990 0.03 2
724 66 101 LYS CE C 44.104 0.75 1
725 66 101 LYS HE3 H 2.970 0.03 1
726 66 101 LYS HE2 H 2.970 0.03 1
727 66 101 LYS C C 177.990 0.75 1
728 67 102 LEU N N 115.890 0.5 1
729 67 102 LEU H H 7.819 0.03 1
730 67 102 LEU CA C 57.700 0.75 1
731 67 102 LEU HA H 4.110 0.03 1
732 67 102 LEU CB C 42.790 0.75 1
733 67 102 LEU HB3 H 1.840 0.03 2
734 67 102 LEU HB2 H 1.640 0.03 2
735 67 102 LEU CG C 27.700 0.75 1
736 67 102 LEU HG H 1.850 0.03 1
737 67 102 LEU CD1 C 23.900 0.75 1
738 67 102 LEU HD1 H 0.950 0.03 2
739 67 102 LEU CD2 C 25.300 0.75 1
740 67 102 LEU HD2 H 0.970 0.03 2
741 67 102 LEU C C 179.860 0.75 1
742 68 103 SER N N 111.748 0.5 1
743 68 103 SER H H 7.637 0.03 1
744 68 103 SER CA C 61.500 0.75 1
745 68 103 SER HA H 4.330 0.03 1
746 68 103 SER CB C 64.700 0.75 1
747 68 103 SER HB3 H 3.690 0.03 2
748 68 103 SER HB2 H 3.470 0.03 2
749 68 103 SER C C 175.700 0.75 1
750 69 104 LEU N N 116.621 0.5 1
751 69 104 LEU H H 8.051 0.03 1
752 69 104 LEU CA C 54.800 0.75 1
753 69 104 LEU HA H 4.280 0.03 1
754 69 104 LEU CB C 44.290 0.75 1
755 69 104 LEU HB3 H 1.530 0.03 2
756 69 104 LEU HB2 H 1.190 0.03 2
757 69 104 LEU CG C 26.900 0.75 1
758 69 104 LEU HG H 1.100 0.03 1
759 69 104 LEU CD1 C 22.500 0.75 1
760 69 104 LEU HD1 H 0.590 0.03 2
761 69 104 LEU CD2 C 27.000 0.75 1
762 69 104 LEU HD2 H 0.005 0.03 2
763 69 104 LEU C C 177.040 0.75 1
764 70 105 ASP N N 118.520 0.5 1
765 70 105 ASP H H 7.508 0.03 1
766 70 105 ASP CA C 57.800 0.75 1
767 70 105 ASP HA H 4.220 0.03 1
768 70 105 ASP CB C 42.240 0.75 1
769 70 105 ASP HB3 H 3.030 0.03 2
770 70 105 ASP HB2 H 2.710 0.03 2
771 70 105 ASP C C 178.030 0.75 1
772 71 106 GLY N N 116.356 0.5 1
773 71 106 GLY H H 9.186 0.03 1
774 71 106 GLY CA C 46.000 0.75 1
775 71 106 GLY HA3 H 4.210 0.03 2
776 71 106 GLY HA2 H 3.570 0.03 2
777 71 106 GLY C C 174.130 0.75 1
778 72 107 GLN N N 118.839 0.5 1
779 72 107 GLN H H 8.119 0.03 1
780 72 107 GLN CA C 55.330 0.75 1
781 72 107 GLN HA H 4.350 0.03 1
782 72 107 GLN CB C 29.790 0.75 1
783 72 107 GLN HB3 H 2.080 0.03 2
784 72 107 GLN HB2 H 2.110 0.03 2
785 72 107 GLN CG C 34.734 0.75 1
786 72 107 GLN HG3 H 2.450 0.03 2
787 72 107 GLN HG2 H 2.140 0.03 2
788 72 107 GLN NE2 N 113.500 0.5 1
789 72 107 GLN HE21 H 6.800 0.03 2
790 72 107 GLN HE22 H 7.420 0.03 2
791 72 107 GLN C C 174.860 0.75 1
792 73 108 ASN N N 119.634 0.5 1
793 73 108 ASN H H 8.467 0.03 1
794 73 108 ASN CA C 52.600 0.75 1
795 73 108 ASN HA H 5.070 0.03 1
796 73 108 ASN CB C 39.800 0.75 1
797 73 108 ASN HB3 H 3.570 0.03 2
798 73 108 ASN HB2 H 2.610 0.03 2
799 73 108 ASN ND2 N 111.600 0.5 1
800 73 108 ASN HD21 H 6.810 0.03 2
801 73 108 ASN HD22 H 7.450 0.03 2
802 73 108 ASN C C 177.170 0.75 1
803 74 109 ILE N N 121.935 0.5 1
804 74 109 ILE H H 8.886 0.03 1
805 74 109 ILE CA C 64.300 0.75 1
806 74 109 ILE HA H 3.710 0.03 1
807 74 109 ILE CB C 39.720 0.75 1
808 74 109 ILE HB H 1.500 0.03 1
809 74 109 ILE CG1 C 28.800 0.75 2
810 74 109 ILE HG13 H 1.850 0.03 1
811 74 109 ILE HG12 H 0.910 0.03 1
812 74 109 ILE CD1 C 14.700 0.75 1
813 74 109 ILE HD1 H 0.770 0.03 1
814 74 109 ILE CG2 C 17.370 0.75 1
815 74 109 ILE HG2 H 0.290 0.03 1
816 74 109 ILE C C 175.700 0.75 1
817 75 110 TYR N N 115.557 0.5 1
818 75 110 TYR H H 7.190 0.03 1
819 75 110 TYR CA C 55.880 0.75 1
820 75 110 TYR HA H 4.830 0.03 1
821 75 110 TYR CB C 41.690 0.75 1
822 75 110 TYR HB3 H 3.070 0.03 2
823 75 110 TYR HB2 H 2.640 0.03 2
824 75 110 TYR CD1 C 132.900 0.75 1
825 75 110 TYR HD1 H 7.140 0.03 1
826 75 110 TYR CE1 C 117.620 0.75 1
827 75 110 TYR HE1 H 6.710 0.03 1
828 75 110 TYR CE2 C 117.620 0.75 1
829 75 110 TYR HE2 H 6.710 0.03 1
830 75 110 TYR CD2 C 132.900 0.75 1
831 75 110 TYR HD2 H 7.140 0.03 1
832 75 110 TYR C C 175.010 0.75 1
833 76 111 ASN N N 117.350 0.5 1
834 76 111 ASN H H 8.458 0.03 1
835 76 111 ASN CA C 56.350 0.75 1
836 76 111 ASN HA H 4.350 0.03 1
837 76 111 ASN CB C 38.770 0.75 1
838 76 111 ASN HB3 H 2.820 0.03 2
839 76 111 ASN HB2 H 2.770 0.03 2
840 76 111 ASN ND2 N 112.910 0.5 1
841 76 111 ASN HD21 H 6.950 0.03 2
842 76 111 ASN HD22 H 7.650 0.03 2
843 76 111 ASN C C 175.510 0.75 1
844 77 112 ALA N N 123.384 0.5 1
845 77 112 ALA H H 8.844 0.03 1
846 77 112 ALA CA C 53.100 0.75 1
847 77 112 ALA HA H 4.140 0.03 1
848 77 112 ALA CB C 18.746 0.75 1
849 77 112 ALA HB H 1.470 0.03 1
850 77 112 ALA C C 176.010 0.75 1
851 78 113 CYS N N 112.770 0.5 1
852 78 113 CYS H H 7.898 0.03 1
853 78 113 CYS CA C 57.800 0.75 1
854 78 113 CYS HA H 4.830 0.03 1
855 78 113 CYS CB C 30.340 0.75 1
856 78 113 CYS HB3 H 3.380 0.03 2
857 78 113 CYS HB2 H 3.230 0.03 2
858 78 113 CYS C C 171.470 0.75 1
859 79 114 CYS N N 112.217 0.5 1
860 79 114 CYS H H 8.491 0.03 1
861 79 114 CYS CA C 60.100 0.75 1
862 79 114 CYS HA H 3.980 0.03 1
863 79 114 CYS CB C 26.796 0.75 1
864 79 114 CYS HB3 H 3.570 0.03 2
865 79 114 CYS HB2 H 2.620 0.03 2
866 79 114 CYS C C 173.430 0.75 1
867 80 115 THR N N 119.929 0.5 1
868 80 115 THR H H 8.251 0.03 1
869 80 115 THR CA C 63.000 0.75 1
870 80 115 THR HA H 4.540 0.03 1
871 80 115 THR CB C 70.500 0.75 1
872 80 115 THR HB H 3.660 0.03 1
873 80 115 THR CG2 C 22.700 0.75 1
874 80 115 THR HG2 H 0.990 0.03 1
875 80 115 THR C C 174.600 0.75 1
876 81 116 LEU N N 127.117 0.5 1
877 81 116 LEU H H 8.913 0.03 1
878 81 116 LEU CA C 55.880 0.75 1
879 81 116 LEU HA H 4.600 0.03 1
880 81 116 LEU CB C 43.696 0.75 1
881 81 116 LEU HB3 H 2.430 0.03 2
882 81 116 LEU HB2 H 1.120 0.03 2
883 81 116 LEU CG C 26.700 0.75 1
884 81 116 LEU HG H 1.950 0.03 1
885 81 116 LEU CD1 C 25.500 0.75 1
886 81 116 LEU HD1 H 0.910 0.03 1
887 81 116 LEU CD2 C 27.200 0.75 1
888 81 116 LEU HD2 H 0.910 0.03 1
889 81 116 LEU C C 176.620 0.75 1
890 82 117 ARG N N 122.969 0.5 1
891 82 117 ARG H H 9.043 0.03 1
892 82 117 ARG CA C 54.000 0.75 1
893 82 117 ARG HA H 5.040 0.03 1
894 82 117 ARG CB C 30.890 0.75 1
895 82 117 ARG HB3 H 1.980 0.03 2
896 82 117 ARG HB2 H 1.860 0.03 2
897 82 117 ARG CG C 26.500 0.75 1
898 82 117 ARG HG3 H 1.670 0.03 2
899 82 117 ARG HG2 H 1.510 0.03 2
900 82 117 ARG CD C 44.634 0.75 1
901 82 117 ARG HD3 H 3.290 0.03 2
902 82 117 ARG HD2 H 3.090 0.03 2
903 82 117 ARG NE N 85.700 0.5 1
904 82 117 ARG HE H 7.480 0.03 1
905 82 117 ARG C C 176.440 0.75 1
906 83 118 ILE N N 124.888 0.5 1
907 83 118 ILE H H 8.913 0.03 1
908 83 118 ILE CA C 60.600 0.75 1
909 83 118 ILE HA H 4.920 0.03 1
910 83 118 ILE CB C 42.720 0.75 1
911 83 118 ILE HB H 1.470 0.03 1
912 83 118 ILE CG1 C 28.600 0.75 2
913 83 118 ILE HG13 H 1.750 0.03 1
914 83 118 ILE HG12 H 1.010 0.03 1
915 83 118 ILE CD1 C 16.100 0.75 1
916 83 118 ILE HD1 H 0.960 0.03 1
917 83 118 ILE CG2 C 20.700 0.75 1
918 83 118 ILE HG2 H 0.760 0.03 1
919 83 118 ILE C C 173.400 0.75 1
920 84 119 ASP N N 125.846 0.5 1
921 84 119 ASP H H 8.930 0.03 1
922 84 119 ASP CA C 52.650 0.75 1
923 84 119 ASP HA H 4.640 0.03 1
924 84 119 ASP CB C 45.320 0.75 1
925 84 119 ASP HB3 H 2.690 0.03 2
926 84 119 ASP HB2 H 2.550 0.03 2
927 84 119 ASP C C 174.780 0.75 1
928 85 120 PHE N N 119.070 0.5 1
929 85 120 PHE H H 8.846 0.03 1
930 85 120 PHE CA C 59.200 0.75 1
931 85 120 PHE HA H 4.760 0.03 1
932 85 120 PHE CB C 40.510 0.75 1
933 85 120 PHE HB3 H 3.230 0.03 2
934 85 120 PHE HB2 H 2.860 0.03 2
935 85 120 PHE CD1 C 132.100 0.75 1
936 85 120 PHE HD1 H 7.450 0.03 1
937 85 120 PHE CE1 C 131.000 0.75 1
938 85 120 PHE HE1 H 7.340 0.03 1
939 85 120 PHE CZ C 128.900 0.75 1
940 85 120 PHE HZ H 7.270 0.03 1
941 85 120 PHE CE2 C 131.000 0.75 1
942 85 120 PHE HE2 H 7.340 0.03 1
943 85 120 PHE CD2 C 132.100 0.75 1
944 85 120 PHE HD2 H 7.450 0.03 1
945 85 120 PHE C C 176.410 0.75 1
946 86 121 SER N N 116.761 0.5 1
947 86 121 SER H H 8.626 0.03 1
948 86 121 SER CA C 57.690 0.75 1
949 86 121 SER HA H 4.540 0.03 1
950 86 121 SER CB C 64.700 0.75 1
951 86 121 SER HB3 H 3.620 0.03 1
952 86 121 SER HB2 H 3.620 0.03 1
953 86 121 SER C C 175.100 0.75 1
954 87 122 LYS N N 124.350 0.5 1
955 87 122 LYS H H 8.400 0.03 1
956 87 122 LYS CA C 58.030 0.75 1
957 87 122 LYS HA H 4.260 0.03 1
958 87 122 LYS CB C 32.790 0.75 1
959 87 122 LYS HB3 H 1.930 0.03 2
960 87 122 LYS HB2 H 1.810 0.03 2
961 87 122 LYS CG C 25.900 0.75 1
962 87 122 LYS HG3 H 1.540 0.03 1
963 87 122 LYS HG2 H 1.540 0.03 1
964 87 122 LYS CD C 29.600 0.75 1
965 87 122 LYS HD3 H 1.710 0.03 1
966 87 122 LYS HD2 H 1.710 0.03 1
967 87 122 LYS CE C 42.500 0.75 1
968 87 122 LYS HE3 H 3.030 0.03 1
969 87 122 LYS HE2 H 3.030 0.03 1
970 87 122 LYS C C 178.300 0.75 1
971 88 123 LEU N N 121.200 0.5 1
972 88 123 LEU H H 8.440 0.03 1
973 88 123 LEU CA C 55.500 0.75 1
974 88 123 LEU HA H 4.320 0.03 1
975 88 123 LEU CB C 42.790 0.75 1
976 88 123 LEU HB3 H 1.670 0.03 2
977 88 123 LEU HB2 H 1.460 0.03 2
978 88 123 LEU CG C 27.700 0.75 1
979 88 123 LEU HG H 1.650 0.03 1
980 88 123 LEU CD1 C 23.500 0.75 1
981 88 123 LEU HD1 H 0.880 0.03 1
982 88 123 LEU CD2 C 26.200 0.75 1
983 88 123 LEU HD2 H 0.880 0.03 1
984 88 123 LEU C C 177.000 0.75 1
985 89 124 THR N N 108.237 0.5 1
986 89 124 THR H H 8.353 0.03 1
987 89 124 THR CA C 62.000 0.75 1
988 89 124 THR HA H 4.430 0.03 1
989 89 124 THR CB C 69.830 0.75 1
990 89 124 THR HB H 4.430 0.03 1
991 89 124 THR CG2 C 22.444 0.75 1
992 89 124 THR HG2 H 1.270 0.03 1
993 89 124 THR C C 173.930 0.75 1
994 90 125 SER N N 112.230 0.5 1
995 90 125 SER H H 7.380 0.03 1
996 90 125 SER CA C 57.300 0.75 1
997 90 125 SER HA H 4.110 0.03 1
998 90 125 SER CB C 65.100 0.75 1
999 90 125 SER HB3 H 3.740 0.03 1
1000 90 125 SER HB2 H 3.740 0.03 1
1001 90 125 SER C C 172.230 0.75 1
1002 91 126 LEU N N 120.316 0.5 1
1003 91 126 LEU H H 8.064 0.03 1
1004 91 126 LEU CA C 53.510 0.75 1
1005 91 126 LEU HA H 4.680 0.03 1
1006 91 126 LEU CB C 44.530 0.75 1
1007 91 126 LEU HB3 H 1.640 0.03 2
1008 91 126 LEU HB2 H 1.180 0.03 2
1009 91 126 LEU CG C 27.200 0.75 1
1010 91 126 LEU HG H 1.540 0.03 1
1011 91 126 LEU CD1 C 23.900 0.75 1
1012 91 126 LEU HD1 H 0.810 0.03 2
1013 91 126 LEU CD2 C 26.300 0.75 1
1014 91 126 LEU HD2 H 0.660 0.03 2
1015 92 127 ASN CA C 52.100 0.75 1
1016 92 127 ASN HA H 4.870 0.03 1
1017 92 127 ASN CB C 40.000 0.75 1
1018 92 127 ASN HB3 H 2.710 0.03 2
1019 92 127 ASN HB2 H 2.590 0.03 2
1020 93 128 VAL N N 124.800 0.5 1
1021 93 128 VAL H H 8.130 0.03 1
1022 93 128 VAL CA C 62.500 0.75 1
1023 93 128 VAL HA H 3.960 0.03 1
1024 93 128 VAL CB C 34.160 0.75 1
1025 93 128 VAL HB H 1.760 0.03 1
1026 93 128 VAL CG2 C 23.204 0.75 1
1027 93 128 VAL HG2 H 0.780 0.03 1
1028 93 128 VAL CG1 C 23.204 0.75 1
1029 93 128 VAL HG1 H 0.780 0.03 1
1030 93 128 VAL C C 174.700 0.75 1
1031 94 129 LYS N N 126.879 0.5 1
1032 94 129 LYS H H 8.399 0.03 1
1033 94 129 LYS CA C 57.300 0.75 1
1034 94 129 LYS HA H 4.050 0.03 1
1035 94 129 LYS CB C 34.600 0.75 1
1036 94 129 LYS HB3 H 1.100 0.03 2
1037 94 129 LYS HB2 H 1.150 0.03 2
1038 94 129 LYS CG C 25.500 0.75 1
1039 94 129 LYS HG3 H 1.040 0.03 2
1040 94 129 LYS HG2 H 0.860 0.03 2
1041 94 129 LYS CD C 30.100 0.75 1
1042 94 129 LYS HD3 H 1.470 0.03 1
1043 94 129 LYS HD2 H 1.470 0.03 1
1044 94 129 LYS CE C 42.800 0.75 1
1045 94 129 LYS HE3 H 2.860 0.03 1
1046 94 129 LYS HE2 H 2.860 0.03 1
1047 94 129 LYS C C 174.470 0.75 1
1048 95 130 TYR N N 114.085 0.5 1
1049 95 130 TYR H H 7.142 0.03 1
1050 95 130 TYR CA C 55.000 0.75 1
1051 95 130 TYR HA H 5.140 0.03 1
1052 95 130 TYR CB C 43.190 0.75 1
1053 95 130 TYR HB3 H 2.900 0.03 2
1054 95 130 TYR HB2 H 2.310 0.03 2
1055 95 130 TYR CD1 C 132.600 0.75 1
1056 95 130 TYR HD1 H 6.970 0.03 1
1057 95 130 TYR CE1 C 116.900 0.75 1
1058 95 130 TYR HE1 H 6.710 0.03 1
1059 95 130 TYR CE2 C 116.900 0.75 1
1060 95 130 TYR HE2 H 6.710 0.03 1
1061 95 130 TYR CD2 C 132.600 0.75 1
1062 95 130 TYR HD2 H 6.970 0.03 1
1063 95 130 TYR C C 173.960 0.75 1
1064 96 131 ASN N N 119.706 0.5 1
1065 96 131 ASN H H 7.840 0.03 1
1066 96 131 ASN CA C 51.230 0.75 1
1067 96 131 ASN HA H 5.490 0.03 1
1068 96 131 ASN CB C 39.640 0.75 1
1069 96 131 ASN HB3 H 2.640 0.03 2
1070 96 131 ASN HB2 H 2.500 0.03 2
1071 96 131 ASN ND2 N 111.800 0.5 1
1072 96 131 ASN HD21 H 6.840 0.03 2
1073 96 131 ASN HD22 H 7.240 0.03 2
1074 96 131 ASN C C 174.570 0.75 1
1075 97 132 ASN N N 123.108 0.5 1
1076 97 132 ASN H H 9.456 0.03 1
1077 97 132 ASN CA C 52.700 0.75 1
1078 97 132 ASN HA H 4.790 0.03 1
1079 97 132 ASN CB C 37.990 0.75 1
1080 97 132 ASN HB3 H 3.290 0.03 2
1081 97 132 ASN HB2 H 3.380 0.03 2
1082 97 132 ASN ND2 N 112.100 0.5 1
1083 97 132 ASN HD21 H 6.880 0.03 2
1084 97 132 ASN HD22 H 7.490 0.03 2
1085 97 132 ASN C C 174.320 0.75 1
1086 98 133 ASP N N 115.160 0.5 1
1087 98 133 ASP H H 8.735 0.03 1
1088 98 133 ASP CA C 56.510 0.75 1
1089 98 133 ASP HA H 4.550 0.03 1
1090 98 133 ASP CB C 40.820 0.75 1
1091 98 133 ASP HB3 H 2.780 0.03 1
1092 98 133 ASP HB2 H 2.780 0.03 1
1093 98 133 ASP C C 176.360 0.75 1
1094 99 134 LYS N N 117.525 0.5 1
1095 99 134 LYS H H 8.710 0.03 1
1096 99 134 LYS CA C 56.820 0.75 1
1097 99 134 LYS HA H 4.530 0.03 1
1098 99 134 LYS CB C 34.910 0.75 1
1099 99 134 LYS HB3 H 2.160 0.03 2
1100 99 134 LYS HB2 H 1.900 0.03 2
1101 99 134 LYS CG C 25.504 0.75 1
1102 99 134 LYS HG3 H 1.460 0.03 2
1103 99 134 LYS HG2 H 1.430 0.03 2
1104 99 134 LYS CD C 29.600 0.75 1
1105 99 134 LYS HD3 H 1.780 0.03 2
1106 99 134 LYS HD2 H 1.690 0.03 2
1107 99 134 LYS CE C 42.900 0.75 1
1108 99 134 LYS HE3 H 3.060 0.03 2
1109 99 134 LYS HE2 H 2.990 0.03 2
1110 99 134 LYS C C 176.130 0.75 1
1111 100 135 SER N N 114.269 0.5 1
1112 100 135 SER H H 7.957 0.03 1
1113 100 135 SER CA C 56.800 0.75 1
1114 100 135 SER HA H 5.280 0.03 1
1115 100 135 SER CB C 67.200 0.75 1
1116 100 135 SER HB3 H 4.040 0.03 2
1117 100 135 SER HB2 H 4.090 0.03 2
1118 100 135 SER C C 171.160 0.75 1
1119 101 136 ARG N N 120.112 0.5 1
1120 101 136 ARG H H 9.044 0.03 1
1121 101 136 ARG CA C 55.500 0.75 1
1122 101 136 ARG HA H 4.850 0.03 1
1123 101 136 ARG CB C 34.680 0.75 1
1124 101 136 ARG HB3 H 1.610 0.03 2
1125 101 136 ARG HB2 H 1.190 0.03 2
1126 101 136 ARG CG C 27.000 0.75 1
1127 101 136 ARG HG3 H 0.710 0.03 2
1128 101 136 ARG HG2 H 0.440 0.03 2
1129 101 136 ARG CD C 42.800 0.75 1
1130 101 136 ARG HD3 H 2.760 0.03 1
1131 101 136 ARG HD2 H 2.760 0.03 1
1132 101 136 ARG NE N 83.200 0.5 1
1133 101 136 ARG HE H 7.080 0.03 1
1134 101 136 ARG C C 173.610 0.75 1
1135 102 137 ASP N N 124.908 0.5 1
1136 102 137 ASP H H 8.971 0.03 1
1137 102 137 ASP CA C 52.600 0.75 1
1138 102 137 ASP HA H 4.990 0.03 1
1139 102 137 ASP CB C 42.320 0.75 1
1140 102 137 ASP HB3 H 3.110 0.03 2
1141 102 137 ASP HB2 H 2.020 0.03 2
1142 102 137 ASP C C 177.910 0.75 1
1143 103 138 TYR N N 124.187 0.5 1
1144 103 138 TYR H H 9.063 0.03 1
1145 103 138 TYR CA C 62.000 0.75 1
1146 103 138 TYR HA H 3.950 0.03 1
1147 103 138 TYR CB C 37.910 0.75 1
1148 103 138 TYR HB3 H 3.240 0.03 2
1149 103 138 TYR HB2 H 2.980 0.03 2
1150 103 138 TYR CD1 C 131.320 0.75 1
1151 103 138 TYR HD1 H 6.860 0.03 1
1152 103 138 TYR CE1 C 116.100 0.75 1
1153 103 138 TYR HE1 H 6.250 0.03 1
1154 103 138 TYR CE2 C 116.100 0.75 1
1155 103 138 TYR HE2 H 6.250 0.03 1
1156 103 138 TYR CD2 C 131.320 0.75 1
1157 103 138 TYR HD2 H 6.860 0.03 1
1158 103 138 TYR C C 176.690 0.75 1
1159 104 139 THR N N 111.215 0.5 1
1160 104 139 THR H H 9.294 0.03 1
1161 104 139 THR CA C 62.660 0.75 1
1162 104 139 THR HA H 4.610 0.03 1
1163 104 139 THR CB C 70.150 0.75 1
1164 104 139 THR HB H 4.400 0.03 1
1165 104 139 THR CG2 C 23.900 0.75 1
1166 104 139 THR HG2 H 1.360 0.03 1
1167 104 139 THR C C 174.440 0.75 1
1168 105 140 ARG N N 121.192 0.5 1
1169 105 140 ARG H H 6.928 0.03 1
1170 105 140 ARG CA C 53.200 0.75 1
1171 105 140 ARG HA H 4.930 0.03 1
1172 105 140 ARG CB C 32.070 0.75 1
1173 105 140 ARG HB3 H 1.800 0.03 2
1174 105 140 ARG HB2 H 1.510 0.03 2
1175 105 140 ARG CG C 26.700 0.75 1
1176 105 140 ARG HG3 H 1.720 0.03 2
1177 105 140 ARG HG2 H 1.520 0.03 2
1178 105 140 ARG CD C 43.500 0.75 1
1179 105 140 ARG HD3 H 3.190 0.03 1
1180 105 140 ARG HD2 H 3.190 0.03 1
1181 105 140 ARG C C 172.950 0.75 1
1182 106 141 PRO CA C 63.700 0.75 1
1183 106 141 PRO HA H 4.460 0.03 1
1184 106 141 PRO CB C 32.390 0.75 1
1185 106 141 PRO HB3 H 2.310 0.03 2
1186 106 141 PRO HB2 H 2.010 0.03 2
1187 106 141 PRO CG C 27.700 0.75 1
1188 106 141 PRO HG3 H 2.020 0.03 1
1189 106 141 PRO HG2 H 2.020 0.03 1
1190 106 141 PRO CD C 50.700 0.75 1
1191 106 141 PRO HD3 H 3.810 0.03 2
1192 106 141 PRO HD2 H 3.410 0.03 2
1193 106 141 PRO C C 176.700 0.75 1
1194 107 142 ASP N N 116.253 0.5 1
1195 107 142 ASP H H 8.760 0.03 1
1196 107 142 ASP CA C 54.070 0.75 1
1197 107 142 ASP HA H 4.600 0.03 1
1198 107 142 ASP CB C 40.900 0.75 1
1199 107 142 ASP HB3 H 2.740 0.03 2
1200 107 142 ASP HB2 H 2.650 0.03 2
1201 107 142 ASP C C 176.240 0.75 1
1202 108 143 LEU N N 120.438 0.5 1
1203 108 143 LEU H H 6.993 0.03 1
1204 108 143 LEU CA C 54.500 0.75 1
1205 108 143 LEU HA H 4.430 0.03 1
1206 108 143 LEU CB C 40.820 0.75 1
1207 108 143 LEU HB3 H 1.680 0.03 2
1208 108 143 LEU HB2 H 1.530 0.03 2
1209 108 143 LEU CG C 26.500 0.75 1
1210 108 143 LEU HG H 1.890 0.03 1
1211 108 143 LEU CD1 C 22.500 0.75 1
1212 108 143 LEU HD1 H 0.760 0.03 2
1213 108 143 LEU CD2 C 27.200 0.75 1
1214 108 143 LEU HD2 H 0.700 0.03 2
1215 108 143 LEU C C 175.080 0.75 1
1216 109 144 PRO CA C 62.900 0.75 1
1217 109 144 PRO HA H 4.760 0.03 1
1218 109 144 PRO CB C 33.260 0.75 1
1219 109 144 PRO HB3 H 2.560 0.03 2
1220 109 144 PRO HB2 H 2.290 0.03 2
1221 109 144 PRO CG C 27.800 0.75 1
1222 109 144 PRO HG3 H 2.210 0.03 2
1223 109 144 PRO HG2 H 2.180 0.03 2
1224 109 144 PRO CD C 50.300 0.75 1
1225 109 144 PRO HD3 H 3.910 0.03 2
1226 109 144 PRO HD2 H 3.840 0.03 2
1227 109 144 PRO C C 176.130 0.75 1
1228 110 145 SER N N 113.260 0.5 1
1229 110 145 SER H H 8.560 0.03 1
1230 110 145 SER CA C 59.200 0.75 1
1231 110 145 SER HA H 4.810 0.03 1
1232 110 145 SER CB C 65.100 0.75 1
1233 110 145 SER HB3 H 4.100 0.03 2
1234 110 145 SER HB2 H 4.020 0.03 2
1235 110 145 SER C C 175.770 0.75 1
1236 111 146 GLY N N 110.300 0.5 1
1237 111 146 GLY H H 7.720 0.03 1
1238 111 146 GLY CA C 45.240 0.75 1
1239 111 146 GLY HA3 H 3.450 0.03 2
1240 111 146 GLY HA2 H 3.040 0.03 2
1241 111 146 GLY C C 172.200 0.75 1
1242 112 147 ASP N N 125.100 0.5 1
1243 112 147 ASP H H 7.730 0.03 1
1244 112 147 ASP CA C 56.200 0.75 1
1245 112 147 ASP CB C 43.500 0.75 1
1246 112 147 ASP C C 181.000 0.75 1
stop_
save_